LOCUS       WP_175785489             324 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175785489
VERSION     WP_175785489.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12168323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..324
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34602
     Region          22..201
                     /region_name="AraC_binding_2"
                     /note="AraC-binding-like domain; pfam14525"
                     /db_xref="CDD:434015"
     Region          251..322
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdialsrhap nrlgtlhapd everavarrl gphrmaahgr dpfhaelyev plhhgallel
       61 cygretridf gddadhflfr ltlsgacelr agqrvaragp gelsvsspal asrlstspdc
      121 rnlvlrlerg alerklqdml hatltrplhf dlaaggngag aalvpptfey lcrlgaqpgv
      181 gtsattfgad ltawlmslll thlphsysaa largtpplpa hvrracdhvd anlgeplala
      241 alaavagvap rtlqhafraf lnttpaayvr errlaavhaa lqrgdarsvt dvliahgihg
      301 fghfakayar ryghapsvta rqap
//
LOCUS       WP_175785602             557 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Burkholderia ambifaria].
ACCESSION   WP_175785602
VERSION     WP_175785602.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60354
     Region          25..384
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          453..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mtpaslieqy gpresmeydv vivgggpagl saairlkqla aekgteigvc vlekgseiga
       61 hilsgavmdp raitelfpdw kergapldva vtedrflfls etgavttpnw alpanfqnhg
      121 nyvislgnvt rwlgaqaeal gveifpgfpa aeilynddgs vkgvatgnmg vgkdgepten
      181 fqlgmelhak ytlfaegcrg hlgrqliskf kldanadpqa ygigikelwe idpakhkpgl
      241 vihtagwplk sdtyggsfly hmdnnqvvvg fvvglgytnp ylspfeefqr ykthpsiraf
      301 leggkrvsyg araitaggll slpktvfpgg aligddagfl nasrikgsha aiktgmlaad
      361 aafdavqagr qsdelnaypd afkqswlyte lyrarnfkqw makglylgtl mvgleqkvmg
      421 gnvpwtlhhk hadhemlkpa sqctpieypk pdgkltfdrl ssvfisntnh eenqpahltl
      481 kdanvpvnvn lrtyagpear fcpaavyefv knddgsdrlv inaqncvhck tcdikdptqn
      541 ivwvtpeggg gpnypnm
//
LOCUS       WP_175785665             485 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia cenocepacia].
ACCESSION   WP_175785665
VERSION     WP_175785665.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..485
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51079
     Region          81..477
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mhgrvcvsar slkggacpwi fglmlvsiac haetrgipdg ladplltrps vldagkrlpg
       61 ddapvvcass thpaklltig davdlalchn priraawasi kiqaaavgea rsawlptvng
      121 aisqlttynr ypdapsmntr gvgrtsnatl nwrlldfggr aangaaaqql ltaalaghda
      181 amqkavvdvi gsyfdvqnaq aafaartesa tlaestlras hkrlamgvas radvlqaeta
      241 lakallaarr aggevarara elvfatglpa gtrveveeav vpvaldaerq lsdwlraaed
      301 shpeiraara rwkaaqakvt avrsdgmptl dlsgtlsrng ypnqglqsvr atqtsigltl
      361 tipffdgfsr tyrirgaqaq aelaqaqlld tqqqilrdvl kahadaeata dsldasarll
      421 aaaeaalasa rnryalgagd ilellsaqaa ladarqervr tlaeweaarl rlfasagiig
      481 rwafr
//
LOCUS       WP_175785688             321 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia cenocepacia].
ACCESSION   WP_175785688
VERSION     WP_175785688.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..321
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34761
     Region          11..224
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(52..53,55,69..71,77,79..80,121,223)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(52,54..55)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(77,80,83,90)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(113,117..120,122)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(118..119,142..144,196..197)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          237..321
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 msgatltvrv arkweeardi cgfelvsddg splprfdaga hidvhlpggl vrqyslcnhp
       61 eqrdryqiav lreaegrggs raihdevrqg dtvriglprn qfplapdaph hlllaggigv
      121 tpilamaerl fstgmpfdmh ycarsadrma fverintagf hdrvrfhvdd gdpaqrfdla
      181 avlagapdgt hlyvcgphgf mdavlnaare rdwsearlhy effggavvps gadrafqvqi
      241 assgkvidvp aectviaala angvdvltsc eqgvcgtclt rvlegepdhr dayltddeka
      301 agdqfmpccs rsrtdllvld l
//
LOCUS       WP_175785671             475 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia cepacia complex].
ACCESSION   WP_175785671
VERSION     WP_175785671.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..475
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51318
     Region          42..460
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(52..53,56..57,60,100,150..151,153..155,158,178,
                     181..182,185,296,299..300,303..305,308,335,339,388..389,
                     393,397,413,416..417,420..421,424)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mastqpdplt aagaarptai dpgsisarld rlpptrsvwk lvvllslgff felydllysg
       61 yvapglvksg ilsatthglf gttgvasfia alfsglfigt iacgfladrf grraiftwsl
      121 lwytaanvvm afqdtatgln fwrfvvglgl gvemvtigty iselvpkqir grafaceqav
      181 gfvavpvvaf layllvphap lgldgwrwvv ligahgalfv wwirrelpes prwlaqqgrv
      241 deadrimral eakveaeygr plpppapaep vpprgsfrdm wvppyrsrti mmtifnvfqt
      301 vgfygfanwv ptllikqgit itsslmyssv ialaapigpl iglviadrfe rksvivamaa
      361 aivvcgllfs qttvgafliv lgigltlasn imsysfhayq aelfptsira ravgfvysws
      421 rfsaifssfv iaavlrgfgt fgvfafiaga mvvvmaaigw mgprtkgial etisk
//
LOCUS       WP_175785690             248 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            cenocepacia].
ACCESSION   WP_175785690
VERSION     WP_175785690.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..248
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27122
     Region          27..184
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtaapadtmt atakadrads srapagrksq qraqdilrag revfaekgye hataaeiaqr
       61 vgvseatvfs yfrgkrelca rviadwydei iaafehgmpr dasvqqqfaf vvrthlrlml
      121 vngtglcalv lsegrakqha lsdeltalqr rytaplmdvl argqaagqvr adlplsllrs
      181 mvfgpmehvl wdailghrkl dtettatqli dmlwaavqpp apeqaalvrf rnevaeavrr
      241 legeasrg
//
LOCUS       WP_175785703             358 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia cenocepacia].
ACCESSION   WP_175785703
VERSION     WP_175785703.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..358
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=36480
     Region          211..358
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mnarsrfnar sdtsvkaglv rrhlpgfcig glllacgvlp ssaraacelg sggiylasls
       61 lpasvtvprd apvgavvast rfsyafnqsy pvgvycttgt tvdntsgsga sssngiiptn
      121 apglgfrlrl gaddyvpdtg sytvpvsvfn tpsrcgypas gkcyiylgtp ivlelvktge
      181 vspntsvsgg llftqrlggl taskvtlstp qvkvvpqsct vtsrsisvqf gqvgantfqk
      241 vgsvspsvpl gisidcrgvs srvavtftdv tspgnrsnvl sltsassatg lgiqilsgtq
      301 pisfgpdsat agnpnqvpir tvnntvyeap fsaryirtas titggtanga atftmsyq
//
LOCUS       WP_175785717             255 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cenocepacia].
ACCESSION   WP_175785717
VERSION     WP_175785717.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 255)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 255)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..255
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25899
     Region          55..239
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mttrgnvqfk qsslpayvar aaalalllvl llrpawlqgl fapfadngap viydraslld
       61 ltlahlgtva lssligtiva vaagiavtrp fgadflplar svvdigqtfp pvavlalavp
      121 avgfglkpvl ialvlygllp ifestiagle dvprdvvdaa rgmgmsgwqq lvsvelplaf
      181 pvivngirla vvinlgtati gstvaarglg dviiaglqts ntafvlqggv ivgllavlvs
      241 daigaiaraa sarra
//
LOCUS       WP_175785731             777 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia cenocepacia].
ACCESSION   WP_175785731
VERSION     WP_175785731.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 777)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 777)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..777
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..777
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=82170
     Region          61..740
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mirrpkaagw ygamrrgrra rcigttvgal alfglppgsv raqqqpdgga iappepsaiv
       61 lpavvvvgtt plpgigtpls kvpanvqsvr aaeldaqhra tltdffaanl psvtisdaqg
      121 npyqadvnyr gftaspllgt pqglsvfvdg vrvnepfgdv vnwdilptqa idrvqlipgs
      181 npvyglntlg galaittkng rsnpggeaev sggswgrkta sveqggtigs nldyyatanv
      241 andggwadhd asrvrqafgk lrytdadttl siaaggadnt lsgtqtiprs fldnrkqayt
      301 ypdrnrnsag yltlsgerff gehvelsgna yyrhlrntnt ssnnntdygs vdedgtidtv
      361 qgsnaqstiv tdsyggsvql tllgklggma nrlvagvsad vanssyvass qdasftdara
      421 aigigdfvpq tsaktrnanv gvylsdalsl tphwtltlsg rydwskaqig desgvqplld
      481 gshvfsrfnp avglnwnpvp gftayatyne gmrsptaiel acadpaapcs lpndfiadpa
      541 lkpvisktfe agmrgrvgaa ttwsaaayrt tltddiqfis spasaqgyfr nvgdtrrqgi
      601 elagrtrvgp lgvglsysyv datyrsswte hspansaada ngnvtvkpgd ripgipahtv
      661 klrldyaatp awdiganvtw rggvyargde nngdvngria gyvlvdldmr yritkrfevf
      721 asvtnlldkr yasfgalgqn ffngpnhtfd gahpvneqfv gpgaprgawv gvryawd
//
LOCUS       WP_175785733             677 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Burkholderia cenocepacia].
ACCESSION   WP_175785733
VERSION     WP_175785733.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 677)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 677)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..677
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=72840
     Region          2..663
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mrddveqaag sraahpagwp apsiqkaher setfglqvsa rpdydvlsna alvlkreqsr
       61 vlcvhampvm etlheqivnt qsmivltdae glilhsigdd dflrraekva lrpganwaen
      121 rqgtnaigta laelcpmvvh gdqhflaanr fltcssvpil dpygdaigvl dvtgdhrsyh
      181 qhtmalakms vqmienhlft ttfqetlqvs fhgrpeflgt lmegivafta dgrflsanrs
      241 aqfqlgmpla alrahtlssl fdvtsaqlid rmrastdrhl mlnlgngavv carvhfrrat
      301 laegsrptdv hdagapgarg navpapaagt saglsrlnyl dtgdaqvasv iakvrkvigk
      361 dipilitget gtgkellaqa ihndsprrda pfvavncasi petlieself gyeegaftga
      421 rrkgaigkll qanggtlfld eigdmpyplq vrllrvlqer lvnplgstkt iavdiaiica
      481 thrdlremia qnrfredlyy rlnglvvrlp plrdrtdlav vvqkmlqrea fagpgrppls
      541 vapdvmalfv rctwpgnfrq lgnllrtaaa mvdddgeirr ehlpddffdd lrrgdahvgq
      601 aapdssaaas agpcvadalp padarlqdva asaiaaalar hggnvsaaar algvsrntiy
      661 rkmpatdagr qpssded
//
LOCUS       WP_175785797             209 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Burkholderia cepacia
            complex].
ACCESSION   WP_175785797
VERSION     WP_175785797.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..209
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21990
     Region          1..207
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msiqtwmlfa aaylattlsp gpnvllvirn tvrygahgta atiagnlvaq gvvvllvalg
       61 vgavlaampp lfvamkviga ayliflgvrq lrgerkaaas sgaaeiavpd rrklfrealf
      121 vsgsnpktmi flsafmpqfi vhdrplalqf vvmyatiact vvvvhsvysa gvrrlhrgfg
      181 msgavralkr asgllfvglg iklltarqa
//
LOCUS       WP_175785810             301 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia
            cepacia complex].
ACCESSION   WP_175785810
VERSION     WP_175785810.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33129
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..291
                     /region_name="PBP2_CrgA_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08475"
                     /db_xref="CDD:176164"
     Site            order(103,107,146,161,163,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176164"
     Site            order(104..105,109..110,112..113,116,120,122..128,190,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176164"
ORIGIN      
        1 mtdrldgvtt fvqvvesgsf alaaerldmt rsavgkaiar lekrlgarll qrttrsqslt
       61 ddgqayydrc vralaeleaa eadldcgrne argklrlsvp lafghhcvtp ivldlartyp
      121 hlridvsitd rfvdlveegi dlavrigpla dstslavrrl gtqygslgaa psylarhgtp
      181 rslddlknhr tiaysrsgvv qpwylrapdg ssvhidmphq lsfddvqaia aagasgfgia
      241 wlpswlldhy vrrgemvvvl drcfvcegdi haiwpktryl prktrcvida lveavppmie
      301 r
//
LOCUS       WP_175785811             512 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia cepacia complex].
ACCESSION   WP_175785811
VERSION     WP_175785811.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..512
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52258
     Region          16..438
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,142,
                     145..146,149,273,276..277,280..282,285,313,317,371..372,
                     376,380,396,399..400,403..404,407)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtlsdsrrna valaavclts lmfgleissv pvilptlehv lhgdfngmqw imnaytiact
       61 tvlmaagtla drfgrkrvyv igtvlfgats llcglapnvp vlvagrllqg asggamlicq
      121 iavlshqfre grergrafgi wgivfgiglg fgpivggaii alaswpwvfl vhaplaaval
      181 vliggavqes rdphagaldv agivtlslav lglafyitqs aelgltsaag lgvlgatvla
      241 vigfviaera sarpmfdfsv friraftgai fgsmgmnfsf wpfmiylpiw fqvalgydsv
      301 taglallayt lptliappfg erlalrygpg vvipaglfti aagfvlmwlg saadhaswlt
      361 mlpgcviagi glgltntpvt ntttgavpsa ragmasgidm sarmislaln iatmgfvlva
      421 givaslkggp agaigdaalr rlaqeiaagr tdglqaiapa laqadpsgaa lhaalvhgfg
      481 wvmvygaagv avlatasava faparrgaav ce
//
LOCUS       WP_175785899             486 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175785899
VERSION     WP_175785899.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..486
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50444
     Region          31..475
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,156,
                     159..160,163,226,229..230,233,301..302,305,333,337,
                     390..391,395,399,415,418..419,422..423,426)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtnntlapca pacaaaaatp rshhgwalvv llvgailppl dyfivnlalp airdgigarq
       61 aelqlvvsay acanavvqit ggrlgdlygr krmfmigmag fvlastlcgl agngtvlvgg
      121 rvlqglfaai lapqvlatir svfspqeqvr vmgfygfafg laavigqlgg galislhpfg
      181 lgwraiflvn lpigilalig swrfipenra prgqridvpg tvlmslfllm lvyplthgre
      241 agwplwmiac gvgalpmlga llavearrla rghdplldvr llrnpvvalg lllaflfytl
      301 safflsygiy lqgclnwspl asgfailplg lgflaspllt trlvarfggy rvltlgfail
      361 aagvaiaaal ardgtpgpgf yagiaaigig qglvlpsvvr ivlaeveaar agvasgmvsa
      421 mlqigaavga atiggvffar lgvhpaaldy vqgfrtsmft ltivllgcia lsmalgplhr
      481 rlhada
//
LOCUS       WP_175785922             783 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175785922
VERSION     WP_175785922.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 783)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..783
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=86597
     Region          19..736
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mrtiqdvlkh pnsvvtqplh leiaaldapv svlsfvltee mntpfladit vtsqdkridg
       61 ativgqpavf tieehasvpa laavidpvrh aartvhgvvt qwtrvrtsrd eatyqvhlkp
      121 rfalleevhd savlldrsfr ellsdmivdr slfqsfdvef elegldgkle qtvmyeetva
      181 nfidrhcrra gvyyyfkqak kedgpqrdtl vfgntprgym ralevlllph sgltswheav
      241 ltlevtralv pqtvrewdhn yrvpddplqv esivahddrs vygsvnrsie hfhsveegqa
      301 ladarrdell arqvrltgts nvigmtpgmv vrisndevhe aphgmvitkl vttgsrsqsv
      361 vntfeaipah qtyrpeyvpe khwrwiagml igvvesgdde lyawmdeygr yrvrllftrh
      421 sgkrgtnsmp lrllrasasy qgglhipllp rsevrvvatq gncdrlliag alhdharrdl
      481 vhgkegwysr avfrspllgn klrfedlkdh egirlatvfg qsslnmghlv drdknkrgqg
      541 felttqhwgt lrapkglffs adaaagsetp hldmpaaiaq lktalqrvtd laaatkqtga
      601 dpadratqaa lldgldqlrd agllasapgg mafvtpkslq qsvgenvivt agrdmdvsiv
      661 rrlrmvagdl islcshklgi kifskgkiel haqgasmdlf sdeqlhvssa ganvlvsakt
      721 ramvacggas mtiengnvvf ncpgefrira asfvfegprh tsvnlpqlpv sdysprsrys
      781 htr
//
LOCUS       WP_175785936             128 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia cenocepacia].
ACCESSION   WP_175785936
VERSION     WP_175785936.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..128
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14650
     Region          7..122
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mhahlriarp vsnlarterm yrdaldlsvl arfedhdgfs gvmlgregld yhfefthcpd
       61 hpiapsptpe dlivfylpdr peweaacera tthgfmpvts fnpyweisgq tfedadgyri
      121 vlqngtwr
//
LOCUS       WP_175785946             466 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175785946
VERSION     WP_175785946.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..466
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49486
     Region          42..449
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(51..52,55..56,59,91,141..142,144..146,149,169,
                     172..173,176,284,287..288,291..293,296,324,328,379..380,
                     384,388,404,407..408,411..412,415)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mstfdnvvag raateaaast pgaiiarler lpanamqira rvligtatff dgfdvitiaa
       61 tlpllihkwg lsptqigmli asgaigqlig aflfpalaer hgrvkaiaws savigitsia
      121 cgfaptfeif vllrilqglg lggelpvaat yineitrahg rgrfvllyei vfpigllvsm
      181 algawlvprf gweimyfvgg lplilslvlt hlvpesprwl asrgrlaeag ravgvfegsv
      241 rgelppvtqv aafdemvrqh pkrrmsdlfs aayrkrtlav atlwatcgfi qyglstwlpt
      301 iyknfyhapl qlalnlavig svmgvlgsla sallvdklgr kpvivwsfvl calslalagi
      361 yhassvyvva vfcslslglm asgfitayvy tpeqyptsir asgcglgsaw lkiasfvapm
      421 vvphaiiggn lapafyligv vpliaavtvh fvgietkgkv lealea
//
LOCUS       WP_175785979             540 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia cenocepacia].
ACCESSION   WP_175785979
VERSION     WP_175785979.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..540
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58740
     Region          1..531
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mswdfiiiga gsagcvlanr lsadprhrvl lleaggsdnr faikipalam kamndpetdw
       61 mfptepdptr ndrtevvprg kvlggsssin atwyvrgnrg dydhwaalgn tgwsydellp
      121 yfrkvecnrd gvsetygktg aiviseirgv ppltrvflda meelgypknv dfnaeptegv
      181 ailhstqhhg lrwsaargyl dparrrpnlr vltgalvrrv lienrvavgv efdldgqrrv
      241 erchgevils asainspkil mhsgvgpadq lnlagipviv enravgrnlq ehpacqvkay
      301 vnvrtanqef nalgmlkygt rfllsrsgqa tfsysgvglv rtrpelaypd iqyhfgafss
      361 sytdqgirme peaainlqpn vnnsrsrgev klkssdplap psiqfnmlad aydretliag
      421 ariaraalrs rafapyvtge ckpgddvqtd dewqaylren aggsfhpcgt ckmgvdadav
      481 vapdlkvigv drlrvvdssi ipqipsgnln aislvigekg admilaahra ataveaaqht
//
LOCUS       WP_175786004             252 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia cenocepacia].
ACCESSION   WP_175786004
VERSION     WP_175786004.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..252
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26233
     Region          1..245
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 msvskkfaav tgagsgigra aaialarvgf tvallgrtea slnetqdair aaggdaqvfp
       61 vdvtdeasvd hafaqiaqrf grldvlfnna grnapvvsld eyeldvwnsv vatnltgvfl
      121 caraawrlmk tqtpqggrii nngsisahap rpdtiaytat khavtgitks laldgrryni
      181 acgqidigna ataltermtq gvpqadgsla pearmdvahv anaivqmanl pldtniltmt
      241 imatampfvg rg
//
LOCUS       WP_175786078             190 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            cenocepacia].
ACCESSION   WP_175786078
VERSION     WP_175786078.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..190
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=20121
     Region          1..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          82..179
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam13305"
                     /db_xref="CDD:463838"
ORIGIN      
        1 maragitldk lveagaqlad etgfeqltga alarhfdvkl aslyshipsf ddlksrialf
       61 alqeladrat dalagrtgkd alaalakvyr dyarahpgrf aaarhpvspe raaasaggql
      121 vrmtaavlhg ydlpdtehah airllggffm gyvtlesagg fshsapdsda swsrsldald
      181 vmlrhwpspa
//
LOCUS       WP_175786084             481 aa            linear   BCT 11-JAN-2025
DEFINITION  sialidase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175786084
VERSION     WP_175786084.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 481)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 481)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 481)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..481
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=50981
     Region          144..428
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Region          177..238
                     /region_name="Sialidase propeller 2"
                     /note="Sialidase propeller 2 [structural motif]"
                     /db_xref="CDD:271234"
     Region          243..296
                     /region_name="Sialidase propeller 3"
                     /note="Sialidase propeller 3 [structural motif]"
                     /db_xref="CDD:271234"
     Region          311..364
                     /region_name="Sialidase propeller 4"
                     /note="Sialidase propeller 4 [structural motif]"
                     /db_xref="CDD:271234"
     Region          375..428
                     /region_name="Sialidase propeller 5"
                     /note="Sialidase propeller 5 [structural motif]"
                     /db_xref="CDD:271234"
ORIGIN      
        1 mrrmivshpl vtrlsaamal aaaavahaep vvvsgpspfa actiggpgtn yvnaevepwl
       61 avnpanpnnm igvwqqdrws nggahglvag ytfdagatwa rtpqpfsaca pgglkyeras
      121 dpwvsfgpdg taysvsisfn qsnnanavga svstdggqtw sspavliand epttqffndk
      181 esvtanpvka gtayavwdrl elpngnpyan lhtkayrgpt lfsktidggk twsaakvivd
      241 vpsrqqtign qivvdpksgt lydffdliqp pfskaagkva fikstddgat wtkpqiiagl
      301 qtvgvtdpnt gepvrtgdii pepaidpasg qlyvvwqdsr fnggaydeia lstskdggat
      361 wstpqqvntp tgrpafnpsv rvdntgavmv thydfrdlqa gntttlptgf wrkishdgga
      421 tfaderrvgg pfdmklapna egffigdyqg ldvlpsssfh pffvqtnagn ltnrtdvffa
      481 p
//
LOCUS       WP_175786097             959 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia cenocepacia].
ACCESSION   WP_175786097
VERSION     WP_175786097.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 959)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..959
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=104117
     Region          42..958
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mknhglsrrg flkasvlagv avyvapigsr afaalfeekl ltpvkwdsvt gipqfridgi
       61 akvtgskvfa rdvraadmph wpqqqshali lrvtqadrty egfdlsllgd elkpdrvvta
      121 ddlardgvaf pafygddmll pagktpaylg havailiyhd farfrfakna lkfrddviry
      181 gavtgplerd pwgtfryvrv ggktaydddv ysslkdapif psmmrkhlpv wpdgkehgkl
      241 deqgmflagq iaseldhpsa dwlvfdreyn tqsvdtaale pdnancwyda atqslhlvvp
      301 tqsplevsen aaamvakcrf pvkklfvhpc ytvgygskdh fnvpfyglvc alyadgrpvr
      361 fandryeqfq tslkrhafkm hyriavdrnt gllqsfkgdf eangggrsnf spsvamvgat
      421 aaqsiyyfpk sdlaavaias raidagsarg ygtlqsmaat emavdeiaaq lnidpiefrl
      481 rnalrsgmkn tqgaipagal rvdevlerak qhplwtrraa rkaefeaahp gkrygvgfac
      541 vqkdfgtgae asfakvefda hgkvslqhta aeigtgmsts qavavakwlg rpatdvrvav
      601 tewpdlpvet sgdpylmlqa dqdrlsanpr wspgyaspss atnsayyfth streaaravf
      661 ryglwpaams iwtrglgggq aapytiried arwvdgklta dglepltfeq lakqahalgl
      721 ptgavvhvfn rwqwtdaefe vggaverlpi dglslrvgap ktgaddgpvp gtaapagata
      781 lrgtlpptan gyrvldrkrv fipptsrnna avtyytavgt lvelavheat gkvellthhs
      841 imecgnqisp qlvsgqlqgg lamgighalh eylplyedgp gngtwnfnry qlprasdvav
      901 wtqtgdvlpp lsetdppkgv aevvmipvvg aivngiahai ghrftdlpvt pqkiqevla
//
LOCUS       WP_175786144             413 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia cepacia complex].
ACCESSION   WP_175786144
VERSION     WP_175786144.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..413
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43829
     Region          17..395
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(27..28,31..32,35,69,124..125,127..129,132,152,
                     155..156,159,234,237..238,241..243,246,270,274,325..326,
                     330,334,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 msvpaagvfr slrsfnyrvw aigslvsnig twiqrtaqdw lvltqlthhd asavgtvmal
       61 qfgpqllllp wtgyaadrfd qrkllmatqa lmgalalvlg vltvtgavrl ehvyvfaflf
      121 gcasafdapv rqtfvaelvg drelanaval nstsfnaarm vgpaaagfli asvgtgwafl
      181 anglsffavl aslsrlrede lranvragrs rgslldgfry vwrrpdltai lvmlfligtf
      241 glnfqlfist maasvfhvda rgfgflssmm avgtisgall aarreqprfr hlwigaalfg
      301 lgcafaalap gywsfaaalv ltgvaaitfm nstnslmqls tepamrgrvm alrlavalgg
      361 tpigapvagw vanhlgprwa lglgaasgfa aalvathfvt rkraqprasd dga
//
LOCUS       WP_175786164             195 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Burkholderia cepacia
            complex].
ACCESSION   WP_175786164
VERSION     WP_175786164.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..195
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20237
     Region          1..193
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msmlvsmaaf alassitpgp vnivalsaga rhglgaslry aagatlgfva lflliglglh
       61 aalarwpvlt tatqwsgiaf llymalrlal ddgrlsadpd vagpsaaaga amqwlnpkaw
      121 lacvaamgay aadgdraqvw qfaalylvic fasiacwgya gaslrhrlan arrmrvfnrl
      181 malllagsal flldv
//
LOCUS       WP_175786155            1055 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cenocepacia].
ACCESSION   WP_175786155
VERSION     WP_175786155.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..1055
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112926
     Region          1..1038
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mwivnlalrr pytfivmaim ivlatplalm rtpvdvlpai nipvisviwn ysgfsatemt
       61 nritsvheri ltttvnniqh vestslpgia vvkvflqpga nvqtaiaqtv ssaqaivrqm
      121 pqgatpplvi tysassipvi qlglssktls eqsladialn flrpqlitvp gvqipfpygg
      181 rtrvvaidld pqalqakglt padivnavna qnlvlptgta kmgqteyrid tnasadtvad
      241 isnlpvqtin gattylreva avrdgfapqt nvvrqngqrg vlisilksgd astlkvvsdl
      301 kallpkvipt lpegltitpl fdqsvfvnaa vqgviheali aavltammil lflgnwrstl
      361 iiaisiplsi ftslialsal getinimtlg glalavgilv ddatvtieni erhlhlgtnl
      421 hdailegage iavpalvstl cicivfvpmf fltgvarflf vplaeavvfa mlasyvlsrt
      481 lvptlamllf rpqqantgad hstsrfarih hafnhaferl rawyivllsi llvrrrfyal
      541 cflgfcvlst glvfmlgrdf fpnadsgnlr lhvraptgyr ieetarladq verviretvp
      601 pdelgaivdn lglpvsginl sysnagtigt ldgellialk pghratghyv qtlrtllpqr
      661 fpgvefffqp sdiitqilnf gqpaaidvqv lgndlasnmt iasslmkkir qipgavdvhv
      721 lqrndeptll admdrtrmqq lnlsaqnvaq nmlislsgss qttpsfwinp rtgvqyplqi
      781 qtpqynlssv ddllgtpisa sgrtgtplql lgnlvqvrst vnpavithyn irpaidvyvs
      841 vegrdlgava geidrivada ratlprgtdl tmrgqietmr tsyiglgagv amaivlvyll
      901 ivvnfqswld pliiisampa alagiawmlf itgthlsvpa ltgaimtvgv atansilvvs
      961 farqrlaaga ppltaaleag atrirpvlmt alamiigmvp malglgegae qnaplgravi
     1021 ggllfatvst llfvplvfgg vhsrlarrra rqagh
//
LOCUS       WP_175786231             541 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia cenocepacia].
ACCESSION   WP_175786231
VERSION     WP_175786231.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..541
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57607
     Region          21..463
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpgqgnahps vplsrsahpg agpgkfkkql sltdltfigl gaifgsgwlf aashvstiag
       61 pagifswllg gfavlllgiv ycelgaalpr aggvvrypvf shgpllgylm gfitliafss
      121 liaievvaar qyaaawfpgl tvegssdptt vgwlvqaall cfffylnyss vktfakanni
      181 isvfkfivpl avigvlftff kpanltvhgf apfgmpgiem avsaggiifa ylgltpivsv
      241 asevrnpqrt ipialilsil lstliyvllq lafigsiptd mlaagwhdvs kafslpyrdi
      301 alalgvgwla vmvvadamis psgcgniymn atprvvygwa ktgtffkvfm rvdeasgipr
      361 aglwltfgla ifwtlpfpsw ealinivsaa lvlsyavapv svaalrrtap dlprpfrasa
      421 fgltgpasfv iaalivywsg wstvswllgl qivmfviyla crrwvptahl slaeqvrssa
      481 wliafyaami vlsylggfgg tgrlahpydt vvvaavalvi yywgantgvr adklqlddde
      541 d
//
LOCUS       WP_175786294             319 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175786294
VERSION     WP_175786294.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..319
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33922
     Region          6..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..302
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 medidlnlvt aldallseas vtgaarrlgv stsamsrtlt rlrtatgdql lvragrklvp
       61 tphaaalrdr vhavasdara vlrpatadvd latltatfti raaasfmeml sgpvvaalgd
      121 vaprvrirfv pkldrdpqal rdgtvdleig krgddapelh trmlfhdwhv avaraghplf
      181 asaritpary aacrhvmavq lgdfggladd stvnasdgpa vhvvvpgypd amrvaastdl
      241 ialvprsslg nacsqgltea lglrsfeipv rlpailvsal whprmhgdpv hrrlrdtvia
      301 vcqraypdar pprtaargk
//
LOCUS       WP_175786304             231 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: energy transducer TonB [Burkholderia cepacia
            complex].
ACCESSION   WP_175786304
VERSION     WP_175786304.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..231
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24763
     Region          161..230
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mttasqsrla aigrprrfgn kqthpvrrfg giviavalhl lliwalvsgl atrvvqivqq
       61 pietriivpv kppppppppk pvekvvskpr vapppppfvp ppevrvqapp qptithqdvp
      121 apsapvheap papapvpvak pvnreigvvc pnsdevrssi vypseaqdnn itgdvtveft
      181 vdpdgrvtnl rvaqpadpvl nraalnavkr frciaqgepv rvrvpfsfnl n
//
LOCUS       WP_175786318             780 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia cenocepacia].
ACCESSION   WP_175786318
VERSION     WP_175786318.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..780
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84813
     Region          71..750
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mkyrmlsasl gasallaasp alhaqqqpav taapiaasaa aaapaastnp aaapsgttra
       61 nsgapvaeaq lkdvivtaqr rrqsaqrvgt smsvlsgsdl ktlnvetvnd lqhatasvev
      121 epafgggqpq frirgvgfnd ytsnnastvg invddvayal piqtqgqlfd iarvevlrgp
      181 qgtlygrntt ggtvnfitnq ptrdfeagas veygthnllt tegyvsgpls drvrgrfaft
      241 tqdfgawqnn ratnqtlgnh dsaaaraqld wdvardfklh fgahggfdks dntglylftp
      301 ytsaktgevi padadhtktg wgvspafsrv tglstdakpg rnnvnggvdl tatwnlgpve
      361 lksitaynyl hrreysdwda tqyhdsdeyf ddtvnevtqe lrassrgdtr lrwvtglfys
      421 hddldekfys dfsdrlgfia ltryrqsvdt lgvygqatyd itkrlrgivg vrqehekrel
      481 rgfasgmltp sfvpfagfqg gdanqsltsn gtsgkvglef dlapatmlya tvsrgyksgg
      541 ftahntgnsn alapfkpesl tayevgfkad ltrslrwnas afhydyhdqq vlsatfdpns
      601 qsligtfvna pksridgfet dlkwqpvrgl eisqyvgyks gkytspfvty ntqasaasgh
      661 nvftdyngta lsfprlsygg qvayswlagg yrlraetnys yrdaysqlll lgpnytvdsy
      721 wlvnasltvt spdrhwdval warnlfnrqy dltknfflpg tnvaaagqpr tvgvrvtyty
//
LOCUS       WP_175786396             201 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            cenocepacia].
ACCESSION   WP_175786396
VERSION     WP_175786396.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..201
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21803
     Region          11..175
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvtkiaanvg rprefdmdda ldgfirvfre rgyhatsigd lsratgltag slykafadkn
       61 aifvaalnry idrrvselnv iladekngrd kvrallrfya dvshgdegrk gclvvagaiv
      121 lstldseiag ivhksmqrie rllrdlikqg qadgsvdaal naqatssclf amvqglrvvg
      181 klgqsrsdms mlvdeamrll d
//
LOCUS       WP_175786405             373 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cenocepacia].
ACCESSION   WP_175786405
VERSION     WP_175786405.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 373)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..373
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40682
     Region          4..373
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mksddvivsf rgvrktydge tlvvksldld iqrgefltll gpsgsgkttc lmmlagfefp
       61 tggeirldge llnsvpphkr nigmvfqnya lfphltveqn vgypltvrkl paaereerva
      121 halkmvqmer fakrypaqls ggqqqriala ralvfepklv lmdeplgald kqlrehmqye
      181 lkalheklgv tfvyvthdqg ealtmsdrva vfdkgivqql dtvdrlyesp cnefvanfig
      241 dsnrlrgtia rvdgefcefr lddgtklvgr higdaaegas avacirperm slaahgvnga
      301 ngtngtngta ancvsgears liyfgdhvrm rcalpgqdec fvkvplgtga ldafspgapv
      361 slafspehlr vfa
//
LOCUS       WP_175786432             289 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfurtransferase [Burkholderia cenocepacia].
ACCESSION   WP_175786432
VERSION     WP_175786432.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..289
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30393
     Region          15..284
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mphthyttli sasnlaerla aapgsvalfd crfdladpga geaayaaghl pgaqylhldr
       61 dlsgrktgtn grhplptrda latllasrgl kqgqqvvayd aqggayaarl wwllrwlghd
      121 svavldgglq aweaagqplt tdvpqpvagd frsatplest vdaaavlanv sspvrvvida
      181 rapdryrgen etidrvgghi pgarnrffkd nltadgrfkt ghelreafat vlagtepnrv
      241 ilqcgsgvta chnalaleva glhgaslypg swsewsadps rpiatgpnp
//
LOCUS       WP_175786448             235 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia cenocepacia].
ACCESSION   WP_175786448
VERSION     WP_175786448.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..235
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24572
     Region          51..149
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mslpasaakf dpsraheyae qsrialagyd achelaacml asaigatdar ilvagaggtg
       61 qeicvtaale pgwhftavdp sapmlalars nveaagfgah tafvedgvda ladapafdga
      121 tligvlhhvp gddakaallh aiarrlkpga plvlagnhrr yadhprllda wqqrwrmkga
      181 tpdavraqla kilqgadppa seeavfallr dagfdaplrf faslfwgawi avrra
//
LOCUS       WP_175786460             479 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175786460
VERSION     WP_175786460.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..479
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48557
     Region          21..418
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(28..29,32..33,36,68,118..119,121..123,126,148,
                     151..152,155,284,287..288,291..293,296,324,328,380..381,
                     385,389,405,408..409,412..413,416)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mdtttpppaf ppalarivat vsigfvvtql dvtivniala hlaadlhlpv aglqwvvday
       61 tlafavlmls agalgdrfgt rrlyvaglll fafaslacga avapamliaa ralqgvgaaa
      121 mlpnslalln dacrhdprlr aravggwtaa gsiaiaagpv vgglliaawg wrgiflvnlp
      181 lcaaglaatf awvparreqa aparstrsld prgqfiaiam ltaltgavie wrplgfthpv
      241 vaggfvlaal aalafvaves rtatpmlpls lfrhpafnaa vlfgicvnlt yygtvfvlal
      301 ylqrargesa lqaglaflpl tggfllsnla sgrvvarhgp rvpmvagalv aalgygslhf
      361 vdaatplgvl lvpfllipsg mgfavpamtt avlasvaper agiasavlnt arqaggaigv
      421 aafgalaggg gaaqvvsglr ietvvsvall vaaallatrv rtdanrgapr srqalsahd
//
LOCUS       WP_175786465             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175786465
VERSION     WP_175786465.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33521
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,223,240,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdfesirifl rvvergsfta asvqldlals rvsrkvkqle ddlgvqllyr ttrrvavtea
       61 grdyyerclr aeeilldadr qarslrtdpe gtlrvlvpys iglfelepal aefhrrysrv
      121 qlvliydnsp ldlvehgfdv alragtltds gyvarslgws haklaaspay ldragrpqtp
      181 qelaqhdily vgrdapgltl rltnaagdva dvpvrpvlis nesvtvlrqa asgggialis
      241 thytarrlek neleivlpdw hrtddielha lyprratlds kvrafveflt dvftgwrsap
//
LOCUS       WP_175786467             676 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia anthina].
ACCESSION   WP_175786467
VERSION     WP_175786467.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..676
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=70620
     Region          30..659
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mkfalpglpp faavrtalrd awpalppgal gfalrntaas llalyiafrm nlddpkwaas
       61 tvwivaqgsr gmglsksqyr ilgtaigaav alaltgafaq spelfllala awiglcagva
      121 tflrnfraya avlagytaai ismdaasapq hafdiatarf lyvavgilcg aafetvfapg
      181 splrdvrarl arylaravav gaealrreps gaavhrlfae aldldtaaey aaagappvrn
      241 aighlraavl gvlsahaagq aldahaarsg tvpdplvada arvldgvaas geagpdmaal
      301 rarvdgalra eaaepagsdt srlltldrld allagfdraf ankaqidlpv pppsrvryaf
      361 hrdavlavhn gmrafiavli asaiwivtaw psgagfvait avvgalfstr pnsaraalgf
      421 lkgaacaava gvvcnfvllp avsgfemlay iigvfmigtg lalrhprtaa lgsafsiffw
      481 nftspdntar igdaaflnga lstllgiafg vlvfalvfpg dpgtsrrrlh ravrrdladi
      541 arnprgwsas awlsrtadrl grelgfagsv pqtrierdmr ellaiwgigd sllslaelaa
      601 repavrraaa avrgrvarad farlertcda aarvlqrrva didsdggral lrgivllrri
      661 adataahghf lrghdd
//
LOCUS       WP_175786485             306 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA cytosine methyltransferase [Burkholderia anthina].
ACCESSION   WP_175786485
VERSION     WP_175786485.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..306
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=33532
     Region          1..305
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mraidlfaga ggfstgakma gldvvwaanh wpaaveihaa nhpgtqhvsq dlhqadwskv
       61 pahdillasp ccqghsparg kaannpqhda srstawavvs alefhrpqfg vvenvrefvg
      121 wqlypawrla vealgyqvap hvldaadhgv pqhrerlfli lsrserplml rlpqrehvpv
      181 aqiidfdags wspiqkpgrs vatlrrieng rrahgdrfva pyygsgsget grslarplgt
      241 ittrdrwavi dgdrmrmlsk eeardamsfp rnyilpkqhr lamhmlgnav apvvardvln
      301 aikaaa
//
LOCUS       WP_175786551             206 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            cenocepacia].
ACCESSION   WP_175786551
VERSION     WP_175786551.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22908
     Region          12..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtiptddpgr rarkriqmla hlaatgarlf dahgyeavtm eqiaaeadva krtlynhfpt
       61 keavlahwle gelardlahl qrdvarrktf asrmgcvlda saawceqhpv yllaylrhrf
      121 lgigtaeper agengsdial vwqqliaagq qsgelnaalr adqlatwfhh lylaamlrwl
      181 tvpglslkre fqsvaklfie gaeakr
//
LOCUS       WP_175786557             356 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia cenocepacia].
ACCESSION   WP_175786557
VERSION     WP_175786557.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..356
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38667
     Region          26..265
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mtaplptrlp plvrhtlrpl ldpyrryrha klihaarval avlvsialst glnvphgews
       61 titvlivvgg lqhhgnirkk aaeralgtsi galaglglil lysfldapfa iyllmavwcg
      121 vcayhaigka gyiallsait mvivaghgdn eivdglwrav nvlagiaial afsfalplya
      181 tyswryklad alracaavha rlagdrqvtd dahlkemaal stllvqlrsl mpsvskecet
      241 smtqleaiqr slrlcigyle ilssalpaad dvaareymrv emktlnrrir dtlvgasral
      301 kfgtpsrlap rrrpvdplhd apppqlsgyv sitaklaaev dqlrerlldt arswni
//
LOCUS       WP_175786146             382 aa            linear   BCT 11-JAN-2025
DEFINITION  epoxide hydrolase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175786146
VERSION     WP_175786146.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..382
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42180
     Region          4..108
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          73..>199
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mhaepfdiai pdqalddlrr rvrdtrppnl tpaepwqqgv dgawlrelaa ywadgfdwra
       61 aeralnrlpq fiadvggrrv hfvhrrgtgp kpyplvvthg wpgsafefha lidrlcdpaa
      121 fggdpddafd ivapslpgfl fspapaapgt salqvadcwa almaglgypr fgaqggdlga
      181 gvsvalgarh egvvdgihln ylpgsydppi daarpltdde qaflkqrgew aaleggyayv
      241 hmtkpqtlav alndsplgla awigekfraw sdcdgdvarr fshdtlltgi slywftgcig
      301 ssmqmywenr lqpmrfapgq rlavpvgfar fpkeisrppr swlervfdvv qwtdmpsggh
      361 faameepdll addirrffrr fr
//
LOCUS       WP_175786587             405 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Burkholderia
            anthina].
ACCESSION   WP_175786587
VERSION     WP_175786587.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..405
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43537
     Region          8..403
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(103..105,129,179,211,240,242..243,251)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(106,139,204,249..251,280,283)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            243
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mnapidtlnr flaaarpsat ykvmdrvaar rasgaevisl sagepdfdtp ehvreagiaa
       61 iragytrytq vaglralrea iadkfrreng ldvdwhdtlv csggkqvifn alaatlnegd
      121 evivpapywv sypeivqlcg grsvtiasga esgfkltpda lraaitprtr wlilnspsnp
      181 tgavysrael qaladvllah phvlvlsddi yehlifdgia fftiaqvepr lrervltmng
      241 vskayamtgw rigfgtgprw lidameklqg qqtsgastis qhaalaaltg pqdfiadsra
      301 aferrrdlvv gqlnrasglr cdvpqgafyv fascealisk ttragtrlds dedvvnalld
      361 eagvatvhgs afglgpyiri ayalddksll racaavqefc rtlag
//
LOCUS       WP_175786602             743 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cenocepacia].
ACCESSION   WP_175786602
VERSION     WP_175786602.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..743
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79855
     Region          24..743
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mtvnrttaar arrrrakvgl gvglgvtlfa aqaamaqgdt papgaeaagn atlpaitvsg
       61 ergqplrare asvaglddap lrdtpasvnv itraliddqq akrlsdvvrn dasvvndyap
      121 vgyfegfair gfpvdlasai ridgltvsge qnvpldnker veilkglagi dsgvvapggv
      181 infvtkrsan vasvtggvds rgstsaavdf grrfgpdhqf gfrinaaken mhsyidgtng
      241 rrtfgsiaad wdispraslq lnaefqqwiq rsapgyqllg gtvvpsvktt skalgtqpwa
      301 kpvttdalnl narfdyqfnd dwkayvaagr srtmiddnsa faygcsyaas caagatspff
      361 fgangdydvy dfrspgeyrr nddlravttg kfatgplrhe ltlgvsvqrr vvhmadavyd
      421 yvgseniygp dltfppspns pgpsyprlda wqygvfgldr isigehwqvl aggkevllrq
      481 rswssldget thtdrsvflp qvalvykpvn vlslyasysk alslgdqapv ratnayaflp
      541 pveshqievg akydwldrls ltaavfsisk pfqfadpdas gtsytfvqrg tqrhqgielg
      601 aagrvterlg ltasvaaira raydsgspay eghqiinvpa lraslyadya vpgvaglnvl
      661 ggveysatrn aneegtarvp swfvfnlgar yttkigghrt vlrvsvdnlf nkfywrdage
      721 qqgdaylfpg aprtarvslt ydf
//
LOCUS       WP_175786603             397 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Burkholderia anthina].
ACCESSION   WP_175786603
VERSION     WP_175786603.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..397
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44382
     Region          48..393
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mtspvpsdaa lrplpidrlt vpaaldgrag tnrstsahpq iaatndldav rawlarfvdt
       61 pttfqnyrke aerlllwavi gcgkplsslt hedlvvyrqf llapapadvw canggrkhpr
      121 gdprwrpfyg plsaasqrqa mvilnvmfsw lvqagylagn plalsrqrqr rpaprvtrhl
      181 gaplwqavkd aiaamprdea raafhadrar wvftllylgg lriteaadtt mghffarrda
      241 ngrdrwwldv tgkggrqrlv pataemmael aryrrahglp alpahgeptp lvlpvgrtrk
      301 pltraalhri vkqvfrfaad rlrahgeage eqarvleqas ahwlrhsags hmadgrvdlr
      361 lvrdnlghvs ltttsqylha dddwrhretd ekhridw
//
LOCUS       WP_175786606             391 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175786606
VERSION     WP_175786606.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..391
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42623
     Region          221..388
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mttappalpp slaqstltle qfdallaniy egpledvpwg daleqirvhl danyvtmilr
       61 wpasghaglm inasgrsapl pgvasynnyy yaldpfvnlp sdrvvtvdel lgvgvwrgsa
      121 myreflepfd vgylmgadlr tpdgiecrfr vcrshhghaf sttdkavcna llphlkravr
      181 lhakfgmves ertlyastid rmlvataild ergaimktnc vadeifaecd glrvragvle
      241 asypledrkl qklirqvlae ragglptvaq aiavprpsgk splgvlirtv plsewsednp
      301 rrpacaifir daerksqash divrklfdlt paettlalal vngstleeaa daldisknta
      361 rshlraifsk tgvtrqatlv rtllnsvlsl g
//
LOCUS       WP_175786550             168 aa            linear   BCT 11-JAN-2025
DEFINITION  KilA-N domain-containing protein [Burkholderia anthina].
ACCESSION   WP_175786550
VERSION     WP_175786550.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Iyer,L.M., Koonin,E.V. and Aravind,L.
  TITLE     Extensive domain shuffling in transcription regulators of DNA
            viruses and implications for the origin of fungal APSES
            transcription factors
  JOURNAL   Genome Biol 3 (3), RESEARCH0012 (2002)
   PUBMED   11897024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10516234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..168
                     /product="KilA-N domain-containing protein"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19771
     Region          14..102
                     /region_name="KilA-N"
                     /note="KilA-N domain; pfam04383"
                     /db_xref="CDD:367917"
     Region          <104..>126
                     /region_name="EngB"
                     /note="GTP-binding protein EngB required for normal cell
                     division [Cell cycle control, cell division, chromosome
                     partitioning]; COG0218"
                     /db_xref="CDD:439988"
ORIGIN      
        1 mqhivhatfe gmavrftddg wfdatapasr ygkdayewlr lpatrrylta lerkfgkipy
       61 fktkrgrggg twlhpklavp farwldddfa vwcddqidql irdgyarisd aerqhwrqml
      121 elekrdessk vrasfgshlm lqrkrekpti ekererlska lqpsfkfh
//
LOCUS       WP_175786636             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175786636
VERSION     WP_175786636.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32727
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdrlqtmqiy vqivergnft qaadalalhr pavtkavqql eqelgvrlln rstrrvsvta
       61 egeafharcv qllagiddaf asfpkqravp rgrlridial alaktivipa lpdfqqrypq
      121 ielvlgasdq padligegid cvvrvgtlkd ssmvartvgv vsmatcaspa yiarhglprt
      181 lddlrthrav nfftgrnrrv lewtfrphge tvavklassl ltdnsealls cglaglgivh
      241 alrpalqpsi dsgqliellp gvpavpkpvs vlypnrahlp dkvrafidwl telfarrypa
//
LOCUS       WP_175786649             326 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cenocepacia].
ACCESSION   WP_175786649
VERSION     WP_175786649.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 326)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..326
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34615
     Region          38..319
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mgqpsrplst dgapaglaas paaadamspr avggnaprar wradaplwlm capafalfaa
       61 lvlvplamtf vltfyrfdpa tgpiaafqfg nyaevlgssy fhtifartfg iaalttaicv
      121 aigtpeayvl skmrdpwrsl fllailapll vsvvvrafgw smllntsglv nqtlalvglg
      181 pykleyttfa ivialvhvml pfmvipvwta lqrldpqteh aalslgaspf ttlrrivvpq
      241 lmpgvlsgsl mvfglsasaf aipgllggrr lkvaatavyd eflgslnwpl gatiavllla
      301 anlvvmltyy rvlerryars lggasr
//
LOCUS       WP_175786677             374 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Burkholderia cenocepacia].
ACCESSION   WP_175786677
VERSION     WP_175786677.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..374
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37399
     Region          17..364
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mtgfidtftl ggpgptiaik dtidiaghpt raasralada ppaehhadvv rllldagwqi
       61 agkanmhela fgmtgindyt gtpvnpqdaa ripggsssgs aslvglgavd aalgtdtggs
      121 irgpaaccgv aglkptfgrv srrgvapadt tldcvgpfar eirtlvavma aiapgfdrar
      181 atasaagctv aqlaveadpa iaaaldaavr asglrshtvv ldempaafaa gltvinaets
      241 rafghlvatg klgadldarl raaattapaa lkeaeavrar ftaqvdaale hadvlvlptl
      301 palpitlqqa rdgvsviams slirpfnlsg hpalslplpl agsplkaglq ivgrkgadeq
      361 vcaiaahfea alaa
//
LOCUS       WP_175786705             603 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia cepacia
            complex].
ACCESSION   WP_175786705
VERSION     WP_175786705.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 603)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12379621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..603
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62777
     Region          1..284
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
     Region          329..603
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 maswldytln glivgniyal lavglalifg vshlinfahg svymvgafig wlcltrfglp
       61 lpvalaavvv gcgalgiaie riglrplrha ariapllati gisfildqla qlafgadpra
      121 vptplpdwhv riagatlgsl dlliagigia aaallygflr ftrlgwavra taqdrdaalq
      181 mgvdvdrvnq tvfaiacalg gvsgllvgmy ynsidpamgf qatlkgvval ligglgnvpg
      241 aiagslllgl vesygvalfg tsyrdlfafg llivflvwrp nglfsanral ppepmtgtfl
      301 aaakavrvpr pvlvalvaaa avlpwlgasp yvlqtltnaw lygllalslt lvagtvgqis
      361 lghaallvig ayasallssd lgwspavtip cagaitavlg tllvypafrl rghyvsiatl
      421 gigevvslvi lnwdgltrgp lgitgiaplp wattaraayw ftfavlvvfa lvqvrllrsh
      481 lgrtlravre ddvaarahgi apnrykaiaf avggvaagvs ggiaahlysy inhqtfdsqv
      541 silaltmvil gglgnvlggi vgaialiglp elfrwaadyr mliyglvlll lvrfrpqgll
      601 gtv
//
LOCUS       WP_175786709             337 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175786709
VERSION     WP_175786709.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..337
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35726
     Region          1..>172
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..287
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 melhqleafs avmsagsvtg agellgrsqp avtrqiqele adlgyalfdr hgprvtptrr
       61 afllyeever slvglraiea raralgdeta epvriaatps laatlvpaal aalpdgahap
      121 hyqlrsesae hvvhevlagt advgvvtlpm ahagldvhwi aqtpcvavlp addplaakpr
      181 islrdlarrr ivtvanrhrl rqridaafaa arvdarvfie tnaslnavma aragigigiv
      241 dpatgvalpv egvvaraldv dipfafgvat pagkartaav dalldalhrt trtllddvif
      301 hdaaahdall rgdrlrtdrt arpprptrar rarpeaa
//
LOCUS       WP_175786729             240 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD family hydrolase [Burkholderia cenocepacia].
ACCESSION   WP_175786729
VERSION     WP_175786729.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..240
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26192
     Region          6..233
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mrlakvsals fdlddtlwpf gpsvvraeat lrtwliehap ntasvlptqq alsalreeye
       61 qlrpdlasdy ramrigsirl aleranedvs ltesaydvfy aarnrvefye dalpalawls
      121 arfpliavtn gnadlrltgg geffrttlsa rafgfakpep eifhaaadtl dvrpaellhv
      181 gddfhldivg alnaglqaaw vvrepraage qaplraetph ltlrdlamlc halggpdtvs
//
LOCUS       WP_175786806             406 aa            linear   BCT 11-JAN-2025
DEFINITION  cation:proton antiporter [Burkholderia cenocepacia].
ACCESSION   WP_175786806
VERSION     WP_175786806.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..406
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42740
     Region          3..396
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mwliqvalvv lvcngcgaia erlgqckvig eiaggillgp lalgvvtpsl yhelftpdnt
       61 saisrigeig lallmfeigl dvrlpaqral lgpvliavpg mllpfggglt vgwlahdvla
      121 pqqpfwpfvl fcgvalsvsa vpvmarivtd lnltrhggaa salsaamvgd llgwgalsll
      181 vclshnaagw rtlgvnvvll vayvallvia akgvllrvvg rslaqgwsrd tvailvasvl
      241 vsgwitsqlg fhsafgalli gmllrdvpsv reqfdrllgg flhtilmpif facaglnlqf
      301 fdvtahaqwl wllvfivvgf agkylgvfag arltghtsgd atviatlmna rglmelvfls
      361 iglqlrilpq nvytmlvifa lfttaitapl lrhhlrpvag gatesv
//
LOCUS       WP_175786816              63 aa            linear   BCT 11-JAN-2025
DEFINITION  CsbD family protein [Burkholderia cenocepacia].
ACCESSION   WP_175786816
VERSION     WP_175786816.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..63
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..63
                     /product="CsbD family protein"
                     /calculated_mol_wt=6630
     Region          1..57
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 mdrnriegkl kqvkgsvkea lgkvtgdret eaegvaeqqa gklqekagea adavrnqtga
       61 drh
//
LOCUS       WP_175786888             430 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia cenocepacia].
ACCESSION   WP_175786888
VERSION     WP_175786888.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..430
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46148
     Region          108..419
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 msfvfrtlrm pragrrapvp waallvagav haqqspltld aalqsatdrs asmqaaqasv
       61 larseaavka gqlpdpmlka gidnlpingg qrftvgqdfm tmrrigieqe wvsgdkrrlr
      121 taladeqvgr eragylvqla avrrqtataw ldavyakqal alqqallghm nheldatqas
      181 yrgakasagd vvqaramlaq tqdqvlkaqq ayrtaliala rwtavpvtdv agtppapesf
      241 vsalppdelr lsqpalvaaa ddiavaeada avanserspn wtweiayqqr ggaysnmvsv
      301 gvsiplplnr knrqnrdvae kaalatkarl myedtlrqvq adirtqsdtl asgrerianl
      361 gaallpaadq rvqlataayr agtgsladtf aarraqleaq lqvldlrrdv sqtwaqleyq
      421 vvpsamaaaq
//
LOCUS       WP_175786936             147 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia cenocepacia].
ACCESSION   WP_175786936
VERSION     WP_175786936.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..147
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=15243
     Region          2..147
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mptckvrekt lnvplgdisa yqvlptvgst seakpfkivl dcgggeegsi tktymtltdv
       61 snnanrsstl tlapestakg lgvqvlngtq ilsygpdssv tgnpnqfytg ttqngvleip
      121 lsaryvptgm vlggtatara sftmsyq
//
LOCUS       WP_175786978             278 aa            linear   BCT 11-JAN-2025
DEFINITION  ion transporter [Burkholderia cenocepacia].
ACCESSION   WP_175786978
VERSION     WP_175786978.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11997982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..278
                     /product="ion transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0034702 - monoatomic ion channel complex
                     [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30219
     Region          29..234
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
ORIGIN      
        1 misliqssfd tardavthva rrpsflrkld iavlalivas vlvvmadsvq elhqqyghal
       61 ysaewaftll fsaeyllrlc takkpvayar sffgivdlvs vlptylafff pglhalidvr
      121 llrllrvfri lglsiyleeg qmliraltra rrkifvfigg mfvlvvilgt viflvegpeh
      181 gitsipvgvy waavtmsttg ygdltpvtpl grlitscail lgygiiafpt gimgaelvas
      241 alerkrpnad tdtrccpncg aavpppepvd aaaprrpe
//
LOCUS       WP_175786980             880 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Burkholderia anthina].
ACCESSION   WP_175786980
VERSION     WP_175786980.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 880)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 880)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 880)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 880)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 880)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 880)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 880)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18409402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..880
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..880
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=96952
     Region          2..>88
                     /region_name="SbcC"
                     /note="DNA repair exonuclease SbcCD ATPase subunit
                     [Replication, recombination and repair]; COG0419"
                     /db_xref="CDD:440188"
     Region          180..877
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
ORIGIN      
        1 mklsrlrieq lrkfrqpaqi gdladginlf vgpneagkst iaeairaaff erhrsssveh
       61 lrpwgdgaas psieidftvg grsarlhksf lqrkrcelei ngqrlegaqa edhladllgf
      121 gfagrgasgp ehwgipgllw ieqgaaqdid apvahaaehl qralgaalge vasssgdvvl
      181 drverarnel ltpatgqprg dyaearrrev tlatelaele gqvatyrgkv dqlatlrrdh
      241 aaddteqpwq alrakeraaq veldaveavk ksladvreka eqttqrqall vanldtfdqq
      301 esdlsardae reeaqaraqa veaahascka rneqaqialg tarkvaslar qeenrrsqst
      361 ranelriqia amatqltdae ieqqallvsr raaaatelsp ddltalrkqa tqlreleirr
      421 aaaasrlryd lepgrevqvg nevwngagev liteptmlvl pgigsleivp ggsdlaevar
      481 elrsvaerqa aalerlglps leaaearret hreyeadikt reaklkilap agidalrgel
      541 aalrarleec ekrlaelpvr pndadslpsv adaevteeka rrdlerldge lnqagltman
      601 aqsaleaaqr evkaaqakla apgraerlsk arndlleaka agagyaseik tldaqvraar
      661 pdmllqdikr wrssaealer ayderrgrie rleaelqalg aqgleekrad vareleqthr
      721 riaemqrran aldyllellr rkraavtqrl haplqrhlnh yvqllfpqat lelgedfvpr
      781 llnrpgteag dfhdmsfgar eqmgvisrla yadllkeagr ptlimlddal vhsdderlaq
      841 mkrvlfdaat rhqillfsch pekwrdlgvg arsveelrgg
//
LOCUS       WP_175786885            1068 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cenocepacia].
ACCESSION   WP_175786885
VERSION     WP_175786885.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..1068
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=114692
     Region          1..1046
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 miarlihwsv hhrflvllat vllaawgvhs lrqtpldalp dlsdtqvivk asypgkapqv
       61 vedqvtyplt ttllgvpgak tvrayssfgd afvyvlfddr tdpywarsrv leylsqvqsr
      121 lpagatvslg pdatgvgwvy eyalvdrtgr hdlgqlralh dwflkfelka vpdvsevasi
      181 ggmvrqyqvv ldpdklrayg itqaavakal gkanqasggs vvelaeseym vrssgylrtl
      241 ddfrhvvlrt ddtgtpvllg dvariqvgpa mrrgiaelng qgevtggvvv mrsgknaltt
      301 idavkaklad lkrslpagve ivttydrsql iaravdnltd klieefvivg vvcavflfhl
      361 rsalvailsl plgvlaafiv mryqgvnanl mslggiaiai gamidaaivm ienahkhlea
      421 ydhahpgepl taarrwelva asavevgpal ffslliitls fvpvfslegq egklfaplaf
      481 tktytiaaaa glsvtlvpvl mgyllrgrip hehanpinrv lirlyrplle atlrrpwaai
      541 gvavvalvlt avplsrlgge fmppldegdl lymptalpgi sadkasellq qtdrliktvp
      601 evdtvfgksg radtatdpap lemfettirf kprstwrpgm tpeklvdeld rtvrvpglsn
      661 vwvppirnrl dmlstgiktp vgvkisgpdl tgidaiatqv eaavkrvpgv tsalaerlng
      721 gryvdvdidr laaaryglsv adiqsvvssa iggedvgevi agrerfpini rypreirdsl
      781 enlrqlpvvt argaqirlgd varvaiadgp pmirsenarl sgyvyvdlrg vdlstavram
      841 qqavarqval ppgysiawsg qfeyleraaa tlrtvvpvtl vvifvllfvt fdsaadalll
      901 mstvpfalvg gfwlvwalgh avsvatsvgf ialagvaaef gvvmllylkg alqrrldage
      961 pltdalllda iregavlrvr pkamtvavvl aglvpimigh gagsevmqri aapmvggmvt
     1021 apllsmfvip aawlllqrrr arsagrtrhs davpsgtnvp slptgesr
//
LOCUS       WP_175787023             328 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175787023
VERSION     WP_175787023.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..328
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35070
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,146,160,162,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdliqsmqaf vtladagtft etgkrlgitt ahvsrlvasl ehrlgirlln rttrsmclte
       61 agerylarar ditlavdase reardarvhp hgrlrahcsa sianhfvipl igqfqarypd
      121 vavdltlaph lpklvrdsyd vaviampslp sseqvaidvg rirsvlcasp ayldahgmpd
      181 spgalvhhrc vqlvapayhe riwtlwngve aqtvdvdpsm tadvaaslai avregagigl
      241 lpdfvaaadl rsgtlvrvlp dyqaeeigvf lvyasrqhld aktrawvdfm kaalrdafaq
      301 argdacappa gtknhapgka gawagaaa
//
LOCUS       WP_175787070             452 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia cenocepacia].
ACCESSION   WP_175787070
VERSION     WP_175787070.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..452
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=48377
     Region          29..434
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mdnttptlat draprlprvv ivgggagglq latrlgdtvg rrgqadvvlv drypthfwkp
       61 llheaasghr dpashtieya aqakrhgfrf vqgalqqvdr aartatiatv qdadgtevlp
      121 qrtldyddlv lavgsvtnff nvpgaerhal plenldqaed frrkflaact kanhlaeqqp
      181 arrgapicin vigagatgve laaalrhaiq qlttyrfkal vsardvhirl ieggprilpa
      241 lderlsgkmh aqlralnvdv ltdtrvaevg adavttatge rlasditiwa agvagpamlr
      301 sigdialnrs nqvivtdtlq tpddphvyaf gdcaacpstg aggflppraq vahqqavylv
      361 nafarrvagk pvagftfrda gtvvslghag avyqadiggr srslivdgla aiglykflyr
      421 khlfsvvgmk ralfqslshw lqsrhqpsik lh
//
LOCUS       WP_175787122             360 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175787122
VERSION     WP_175787122.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..360
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37897
     Region          11..109
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(55,58,62..63,72,91,95,101,105,108..109)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mgtdtprlna saaaarlgvs ikalrlyerh glvtpertpa gyraygpadl araadiaalr
       61 klglglaqva svldgdarsl daalaaheaa ldrgiqdlvg kldsvramra glargrmpad
      121 geltrlvdsg aagvafnlpw pwggewfecr dirplnyiig slgsgktrla lrladalpga
      181 vfvgldrldd dcaaasdalr adpelksrvd rtaallvgng atpspaltal lvsleaegpr
      241 vrivdmieqd ldratqlali ahlracaaag mrplflltrs saildlaavg pdetillcpa
      301 nhspparvap ypgapgyeav atclaapevr eriarrpear aimllteqem ntsrparrrt
//
LOCUS       WP_175787157             211 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Burkholderia anthina].
ACCESSION   WP_175787157
VERSION     WP_175787157.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132949
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..211
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=23958
     Region          3..147
                     /region_name="SR_Res_par"
                     /note="Serine recombinase (SR) family, Partitioning
                     (par)-Resolvase subfamily, catalytic domain; Serine
                     recombinases catalyze site-specific recombination of DNA
                     molecules by a concerted, four-strand cleavage and
                     rejoining mechanism which involves a transient...;
                     cd03767"
                     /db_xref="CDD:239736"
     Site            order(8,10,71..72,75)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239736"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239736"
ORIGIN      
        1 mfvraylras tkeqdanrak ndliefsker glqiaafyve hesgaslhrp elfrllsdch
       61 egdillieqv drlsrlngdd wnklkgelqs rrvrvvaldl ptswmmttaa dditsrmmda
      121 lnsmmldmla aiarkdyedr rrrqrqgiek lkaeggyrgr kpddqrnagi ismlrrgdsw
      181 ntiiaatkcs rstlsrlsrq ikgeataeai s
//
LOCUS       WP_175787173             237 aa            linear   BCT 11-JAN-2025
DEFINITION  PadR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175787173
VERSION     WP_175787173.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 237)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..237
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25567
     Region          83..162
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mrhnpsrgha rcdghgahag pdwfagvlha igrhrrghdp fggggpfggr ggrggfgdfg
       61 ddgmprgrqf ssddlqllll alvaeqpshg yelikaldtr sngfyspspg mvypaltyle
      121 evgfvasqae gnrkryalid agrahldaqr ervdtlfarl thlarkmefm rrafagesag
      181 neaqdesqag wlpefvdarl alkrallhks atnadeqrri aailrratae ieggaga
//
LOCUS       WP_175787214             385 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cenocepacia].
ACCESSION   WP_175787214
VERSION     WP_175787214.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 385)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..385
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41378
     Region          1..373
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masismrrvq kaygehapvi rdvdleigah efcvflgpsg cgkstllrmi agledlsage
       61 lsidgrrvdd vpaaergvam vfqsyalfph mtvyenmafg lklarvpkve idrkvrdaar
      121 ilqldtller kpkalsggqr qrvaigraiv repgvflfde plsnldaalr gqtrieiarl
      181 hrqferasvv yvthdqteam tladkivllh agadtarhgs iaqvgapldl yhhpasrfva
      241 gfigsprmnf lpavvtacda rrttvtlvps getftlprdg salsagaavt lgirpehltl
      301 gatpdattla rdvalverlg eqtyvhldps gqpsatqlia kvpgdaqvrt gervhvhapa
      361 aachlftedg ravpacadlp vhhya
//
LOCUS       WP_175787216             451 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrolipoamide acetyltransferase family protein [Burkholderia
            anthina].
ACCESSION   WP_175787216
VERSION     WP_175787216.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..451
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48121
     Region          2..451
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mgihvikmpd igegiaevel vawhvqpgqt iaedqpladv mtdkaaveip spvagkvlel
       61 ggrigemmav gselirleve gdgnlkpgak grdagtdatp rpavteaada haksseasaa
      121 saasgapass dathhaanrt saeprraeha aspraalapg erplaspavr qrawdmgiel
      181 ryvrgtgeag rilhadlday artgggtvra sqahgydern detdvpvigl rraiarkmqe
      241 akrriphfsy veeidvtele slrtelnrry gdtrgrltpl plliramvva lrdfpqinar
      301 yddeagvvtr ygavhmgvat qtdggltvpv lrhaeardvw sisaeiarla davrtnraqr
      361 delggstiti sslgalggiv stpvinhpev givgvnrmve rpmirdgaiv arkmmnlsss
      421 fdhrvvdgad aaefiqavrr llerpallfv e
//
LOCUS       WP_175787223             213 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175787223
VERSION     WP_175787223.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..213
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23836
     Region          7..211
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 meakldstad tvaaslrdmi ingelagger lverdlaerf gisripmrea iqrleregll
       61 difrnrgavv rmlsasdvqe iydlrvlleg daiyrsvkrl ddetlarael vhrllgdatv
      121 arrqgelnre fhallysccg narqlksiae lrgqveryer lqatlladtp sfqvehddil
      181 qaclernarg aramtvahld sarrivlrlv egg
//
LOCUS       WP_175787221             353 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia cenocepacia].
ACCESSION   WP_175787221
VERSION     WP_175787221.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..353
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=36887
     Region          4..353
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkriivvsal acvaadavaq ssvtlfgyig agvrwtdgvk ggsqvgfdnn aisgnifgik
       61 gaedlgggmq aifmlqsgfl tgtgalaksp gllfsqmayv glsggygrvt fgrqlnaled
      121 igialdpnsa qgqslstipg vvwggnfftn dsrfnntiky vgtfggatvr gsyspggvag
      181 nqragsnvav gtsyrfqtll lgaayqttwn adasqwarti mggaswqvgp arlylsysdl
      241 avsaakagap errdripavg ivyqvtpflq lsgatyydfa qnlknaagad grkltsyaml
      301 qyflskrtsl yaefdrngfs gaykkdqtni gglslrpdgr tvtgvsvgmi tqf
//
LOCUS       WP_175787248             298 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175787248
VERSION     WP_175787248.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..298
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=31171
     Region          4..292
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 msiplkgiia ypvtpfstdg dvdltaldal idrliadgvh aiaplgstge sayladaewe
       61 avatasirav rrrvptvvgi sdlttagavr rarfaeqaga davmvlpvsy wklgndeiva
      121 hyraigdaig ipimlynnpa tsgvdmspel iaticrtvdn vtmvkestgd igrmhrlaql
      181 sdgtipfyng snpmalaala agaagwctaa pnlnaalpla lfdamrtgdl ararsafhaq
      241 lpllqfivng glpvtvkagl rlrgfdagep rrpllplgda rmrelerlla alpdgvaa
//
LOCUS       WP_175787271             470 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175787271
VERSION     WP_175787271.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..470
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47540
     Region          18..447
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(25..26,29..30,33,65,115..116,118..120,123,144,
                     147..148,151,274,277..278,281..283,286,314,318,370..371,
                     377,381,397,400..401,404..405,408)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtaavpdqaa arrvlaatcv symlvlldas ivnvaltdia htfgsrvggl qwivnaytla
       61 fasllltggt lgdrlgdrtv yvaglavfva asalcgiapt lpalavaral qgvgsamlvp
      121 cslalinraf pepaarasai svwmgcggia masgpliggl lidlsgwrsl ffvnlplgla
      181 giglgrtvap aavdrsrqfd wggqaaaiva igaligtlie gpslgwrsap ivggamasvv
      241 awiafiaiea rrrepmlpla ffrnrlfags tfvsmasafv fygllfvlsl fyrqvrgasp
      301 ldtglaflpm tamvalgglt sgrivarfga rgtmcaafgl yaagalgmtt igattpawla
      361 vapmlaigfa sgfispaata papalgtidr qragvaaavl naarqsgsal gvaifgacia
      421 tlqpfpvavr vvltlaagls vlaaatwwlt aqaapataet tappraaarr
//
LOCUS       WP_175787285             506 aa            linear   BCT 11-JAN-2025
DEFINITION  peptide MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175787285
VERSION     WP_175787285.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..506
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55269
     Region          7..462
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mmhapvsqtr sfttvfliem werfgyygma allvlfmvdr laftdshanl twgaftalvy
       61 aapsiggwig dkvlgarrtm iigasvlcag ylmlavpndh laymyaslgv ivvgnglfka
      121 naanlvrriy egddaridsa ftiyymavni gstvsmlatp wikdhwgwht afavccggml
      181 lailnfmlmh rtlahvgsqp ddepirwkrl gavaaggial alitlyvlqh kqlavasvwt
      241 aafailaifa ymiakserse ragliaalvl igqvilffif yvqmstsltl falrnvdprf
      301 mlfgttlftw saaqfqalnp iwimllspvl vwvynavakg grdlpvaaky algfgavaag
      361 ylvftisgry avdgrvsswf mvwgyglysl gellvsglgl amiaryvpar msgfmmgayf
      421 vatgvsqylg svvanfaqmp shelpatesl plylslfekl gwlaaigmll allllplmnr
      481 lsrqhqrcte erreealqaq aaaaaq
//
LOCUS       WP_175787320            1017 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Burkholderia cenocepacia].
ACCESSION   WP_175787320
VERSION     WP_175787320.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1017)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 1017)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 1017)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 1017)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 1017)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11534155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..1017
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=103658
     Region          11..77
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          109..171
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(115..117,120)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          194..256
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(200..202,205)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          272..1015
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mteplasaal qtielnvdgm hcggctgrvq ralaavpgvv daavdldaht atvtvqetve
       61 pdrlvdaihq agyraavrda ageavartha ahttadatps apaaattvel didgmtcasc
      121 vsrvekalvk vpgvtrasvn lateratvda sagvsatqla davkqagyga tptasdidvp
      181 arvptlptap anieldidgm tcascvsrve kalakvpgvt rasvnlater atvdasddvs
      241 aaqlvdavkq agygatptav aappatstsa dveldiggmt cascagrvek alaavpgvtr
      301 atvnlatdra svhgagalda atliaavtta gyraslpaas pasapagadl qpaspaqdpd
      361 arkrreaire rnlvigaavl saplvapmla apfgidlmlp gwlqlvlasi vqfgfgarfy
      421 raawhavkar tgnmdllval gtsaayglsl wmllrdpahp ghlyfeasav ivtlvrfgkw
      481 lesrakrqtt eairalnalr pdrarvvehg verdvplsqv rvgtrvgirp gervpvdgri
      541 vsgrshides litgeslpvp kddgdavtag singegalvv ettaigaett lariirlves
      601 aqaekapiqr lvdrvsevfv pailgiavlt lvgwliagag tetailnava vlviacpcal
      661 glatpaaima gtgvaarhgv likdaqalel aqrttviafd ktgtltegkp svtafdavgm
      721 praetlalaa avqrqsdhpl aravvaahda dvaaqggaaa svvatdarav agrgveahvg
      781 gqqlalgstr wrdelgiavp paldaraael eragntiswl mradapravl aliafgdtvk
      841 pgardaiaal sargvasalv tgdnrgsata vaaalgigev haqvlpddka rvvaelkrth
      901 ggvvamvgdg indapalaaa dvgiamatgt dvamhtagit lmrgdpalva daidisrrty
      961 rkiqqnlfwa fvynlvgvpl aalgllnpvi agaamafssv svvtnalllr rwkgrar
//
LOCUS       WP_175787326             558 aa            linear   BCT 11-JAN-2025
DEFINITION  alkaline phosphatase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175787326
VERSION     WP_175787326.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 558)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..558
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=58300
     Region          48..536
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 misrfvkqrn mavmvagala lasagvyaaq qdgnaqgesn grpsrvvkhv lllsidglhe
       61 qdlarcigan tcpnlavlak sgvtyanayt pglsdsfpgl aalvtggspk taglfydvsy
      121 drnlyapsdt tcsgkqgwnv vfdettgida qnggalvhld gggafnpqai phakvngqcv
      181 pvyphdyvkt ntvfeavkag vphartawad khawgydwln gpsgtgvddl mrteinsidp
      241 atntaytdvy shtarfdnlh vqalirqigg rdstgtktap vptlfganfq tlsvaqkapv
      301 akgggyldad ftpngqvana ityvddaigh vvaalkqanl ysstavivts khgqspsdht
      361 klvkngdtlt klleandfid pngnfgqnnt ttgnlndgsg lvgtgfvqtd dvgliwlrdr
      421 gqrtavvqal kanlgcnapg icadgpqayv lygaaladrf gdpangrtpd ivvqpnpgvi
      481 ytsstkkdee hggnapddsh lgllvsypgi hrartvndlv gtkqvaptil allgadprll
      541 qavvaentrv lpglgigr
//
LOCUS       WP_175787353             289 aa            linear   BCT 11-JAN-2025
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175787353
VERSION     WP_175787353.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..289
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31998
     Region          1..125
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mnanelvlyf dgrcplcvae irclgehdvr hrlafvdiae pgfdpaplgv dlpalnrelh
       61 arlpdgrmlt gidsilaaht llgrrglvrl lrvpamravf aslyrrlagn rqavsrwlgy
      121 raeacceggt csigrnaesa aanrppqdip rrivvrwmya aaivhllvgv vlpwiagasw
      181 ldayhrgier hfwsaaapga araqqvwwms llgatvqcas vwmlalvhlg nrlrkrevwg
      241 wllaglliwa pqdmllswqa qvwghvvidv valvamvppl vwlsrrdta
//
LOCUS       WP_175787363             712 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia cenocepacia].
ACCESSION   WP_175787363
VERSION     WP_175787363.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..712
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=76806
     Region          40..642
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mtdptanpsp ppappstppr rrriwrtlag allgltlaca gigawtidri wtqlpsvehl
       61 avyrpalplr ifsrdgdlla eygverrefv pleripplmr hallaaedak fyehgpvdvg
      121 glaratfanv vtgqpgqggs titmqvarnf yltrdkvlsr klaeilmaak lereyskdkl
      181 lelymneiyl geraygfaaa ahvyfgkpld alsageaavl aglpkapsaf npvvnparat
      241 arrnyvlgrm halgqlddat yraavdapia lattpppgiv aapyvaerar rmmverfhdd
      301 aytlgldvtt tismrdqraa eaaldrtlsr qsrakrdmrn glegalvsld aatgdmlalv
      361 ggadfdrnvf dhalqayrqp gssfkpfvys aalekgyfpg vlvddtqrtl thaetgarpw
      421 rprnfgnrye gfipvrrglv rsknlvavsl mqatdaryvq qhavhfgfda qrnpaslpla
      481 lgagavtple lasaysvfan ggtrmeprli lsvkqrhgga myeatvpage rvvsarnafv
      541 mdsmlrdvvr agtargalal rrddaagktg tsngskdvwf agyssgivav awlgydtprp
      601 mgratgatla lpvwldymkt avdgrtpvaa tppqdvalvd gdfvyaeytr gtctadvpay
      661 irsrfacgga aasdapgald vpaghdkrde pmpaavdaae rervldlfrt dd
//
LOCUS       WP_175787390             316 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Burkholderia anthina].
ACCESSION   WP_175787390
VERSION     WP_175787390.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..316
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36417
     Region          113..275
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mwihdkvvqf fgvsglmals sahqlnwhal ltlngleaai apifpfaivl emaflvwlnr
       61 rstasiyaay kipvlmyvfn aaiagvvnln vflwtqshfa afapftaplr irwfiyayvv
      121 wefshfvyhw tchkvrllwc lhsphhapeh mnisviftaf flqgayativ rtaicsflgv
      181 piellflvmv idscwgtlih vseevwpsgk frgvlgrlil npahhrvhha snpeyldmny
      241 cntlpiwdki fgtlqheiqg ikpvygitrd vknlsftdmy fgeiwllwkd irnadswkdr
      301 vlhivmppgw qprskr
//
LOCUS       WP_175787524             400 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175787524
VERSION     WP_175787524.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..400
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42130
     Region          7..384
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(15..16,19..20,23,55,109..110,112..114,117,137,
                     140..141,144,223,226..227,230..232,235,259,263,314..315,
                     319,323,339,342..343,346..347,350)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mrvdrpaflg slflsrladq mllflvplvv fqvtqkatws glaffietlp rfiafpicga
       61 lsdrvspirv lrmsqasrav acligivgyv awsgigwlia lsavcgvlts qglvarevll
      121 pqifplqrfe kvlahtqlad qsgvvlgpiv aaallgwrtw ewgvacaall fvaadllafv
      181 wqrtstaria rpehavgpwy apfgvalthv ltlpglsrlv llaaaenlvi gttlatsaam
      241 vtgtfrqsgg fyaglqvaga vatvvillfv arievsrvrl givafvaiaa gglvmglsgs
      301 iamyvagflm vvgfdkmfnv yirsarqaii pprdygkttg vivllnnatq plagllvglf
      361 sgrgrvalvv tltsigmail ggaivavgta rtrstarvsd
//
LOCUS       WP_175787550             479 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175787550
VERSION     WP_175787550.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..479
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51652
     Region          45..464
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(54..55,58..59,62,102,152..153,155..157,160,180,
                     183..184,187,300,303..304,307..309,312,339,343,392..393,
                     397,401,417,420..421,424..425,428)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mqqtvtaggp plaassvhvg nqpgaavsar mdrlpvtrhl wmlellislg gffeiydlif
       61 tgyiapgmar sgllatttha ffgftgiagf iaatfaglfv gtfcfgwlpd rfgrrsvfti
      121 sllwysvgsa imafqttpea vvfwrfvtgi gvgveivtid syvteivpqh mrgramafnq
      181 mvmfaaapva ailsywlvpt tvfgidgwrv vvlagsvgav lvwfirrsvp esprwlashg
      241 rpeqadaivs riegivsrqa raplspplpi vdqplhrras faellhppyr srfvmlvvfn
      301 lcqaigyygf anwvptllig qgitvtksll ysfviafalp vgpmlailya drvqrkwliv
      361 ggavmvivcg iafafarsaa llialgvlis lagqtisvcy htyqaelfpt aircranglv
      421 ysasrvgamm sgfiiaallr dfgvvgvfag itacmlvvvl sigifgpntn gkrleelcr
//
LOCUS       WP_175787552             348 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175787552
VERSION     WP_175787552.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..348
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37133
     Region          17..197
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          230..312
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mlysaiylrd stmmsddpfs dilrltnaes latggfsagg awavrfpapd kikffavvkg
       61 tcwvsidgee tpirfgsgdv glltakrsfv lasdpcvpav damalfsgtg rstaklgngg
      121 efaqigghvl ldpvtgslls dvlppwihvp aaspqavkvr wlleqlveer aadlpgaqlv
      181 saqlsqllfi qilrahlkts asltgwlraf gnpriapalr lmhgdparsw hldelaaaca
      241 msrttfashf rasagvaplt ylgewrmrla errlrdedip vallaqslgy ssesafshaf
      301 krmsghspta yrhivrtaae gadsgrggvr aaveatgatp qpfplepr
//
LOCUS       WP_175787589             343 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia anthina].
ACCESSION   WP_175787589
VERSION     WP_175787589.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..343
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37691
     Region          43..307
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mskkldnala asfstrrdpe klardmestp faqlaarmpd psmvpigqiv rspfqsrvdm
       61 prdeapided yiadlaasie hdsllnpiiv relapgtpip pervlpyygk aspgepasng
      121 lpyygqlnld apiyeliage nrvfahmylg rdvvsakvlr igdieaaral tvdnlvrkgm
      181 tdwelylhmv mlrrvgaant qrelapllgc srgkvamlec ygrlpvrvqe mlgkkptlig
      241 anqvqmlatk gflennpeav teavekvaed kisqtgmvgf ierrlrtase sdrreyaltl
      301 grakvrivsa ggetritgdv daetllnllq qnlerlikpa dae
//
LOCUS       WP_175787637             403 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175787637
VERSION     WP_175787637.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..403
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41463
     Region          8..390
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(18..19,22..23,26,61,108..109,111..113,116,139,
                     142..143,146,221,224..225,228..230,233,263,267,316..317,
                     321,325,341,344..345,348..349,352)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mpdsryrwvi vaaggllsci gigamfslpv flravardtg wsmtgisaam tlgfiamafa
       61 siawgslsdr igtravvatg avllaaslal asrapsllaf qlifglgvgs aaaavfapmm
      121 acvtgwfdth rslavslmsa gmgmapmtms plaawlvsrh dwrasmltia vlaaavmipa
      181 slfvrrppal drppaepvaa gapvplsvgn alrspqfivl lltnffccat hsgpifhtvs
      241 yavtcgipli aavsiysveg lagmggriaf gllgdrfgak rmlaagllaq algalgyyfv
      301 rtldgfyava mlfgfiyagv mplysvlare nfplrmigtv iggsamagsl gmaagpvagg
      361 livdalgsyg wlyigsfvig iaafavalmf rpfpkapsqt vav
//
LOCUS       WP_175787686             325 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia anthina].
ACCESSION   WP_175787686
VERSION     WP_175787686.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 325)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 325)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 325)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..325
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34557
     Region          39..318
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mrppprplpt dgapgslaqp aaadaapara agrrapnatw rahaplwlmc apafalfaal
       61 vlvplamtfa ltfyrfdpat gpiaalqfgn yaevlgssyf htifartfgi aalttaicva
      121 igtpeayvls kmrdpwrslf llailapllv svvvrafgws mllntgglvn qalglvglgp
      181 ykleyttfai vialvhvmlp fmvipvwtal qrldpqteha alslgaspft tlrrivvpql
      241 mpgvlsgslm vfglsasafa ipgllggrrl kvaatavyde flgslnwplg atiavlllva
      301 nlivmltyyr vlerryarsl ggasr
//
LOCUS       WP_175787842             613 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp70 family protein [Burkholderia anthina].
ACCESSION   WP_175787842
VERSION     WP_175787842.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Fernandez-Fernandez,M.R. and Valpuesta,J.M.
  TITLE     Hsp70 chaperone: a master player in protein homeostasis
  JOURNAL   F1000Res 7 (2018)
   PUBMED   30338057
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 613)
  AUTHORS   Mayer,M.P. and Bukau,B.
  TITLE     Hsp70 chaperones: cellular functions and molecular mechanism
  JOURNAL   Cell Mol Life Sci 62 (6), 670-684 (2005)
   PUBMED   15770419
REFERENCE   3  (residues 1 to 613)
  AUTHORS   Bukau,B. and Horwich,A.L.
  TITLE     The Hsp70 and Hsp60 chaperone machines
  JOURNAL   Cell 92 (3), 351-366 (1998)
   PUBMED   9476895
REFERENCE   4  (residues 1 to 613)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   5  (residues 1 to 613)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   6  (residues 1 to 613)
  AUTHORS   Rensing,S.A. and Maier,U.G.
  TITLE     Phylogenetic analysis of the stress-70 protein family
  JOURNAL   J Mol Evol 39 (1), 80-86 (1994)
   PUBMED   7545947
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..613
                     /product="Hsp70 family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0051082 - unfolded protein binding
                     [Evidence IEA]"
                     /GO_function="GO:0140662 - ATP-dependent protein folding
                     chaperone [Evidence IEA]"
                     /calculated_mol_wt=65721
     Region          7..608
                     /region_name="DnaK"
                     /note="Molecular chaperone DnaK (HSP70) [Posttranslational
                     modification, protein turnover, chaperones]; COG0443"
                     /db_xref="CDD:440212"
ORIGIN      
        1 msdprysigi dlgtthcals yvdsaasdge kitqqvlpia qltapgales rdllpsflyl
       61 pheseltqgd ltlpwtasrg favgemartr gagtpirlvs sakswlchpg vdrraailps
      121 dappevsrvs plessirylt hlreawdhth pdapfadqdv tvtipasfdp aareltaeaa
      181 raagysrmtl leepqaalys wiqkseggwr kqvrvgdlil cvdvgggttd lsliavverd
      241 gnlelhrvav gehillggdn mdlalahvva rklaqqgtqa dpwqlralty acrsaketll
      301 sdptidavpl vvpsrgskli ggsirteltr aeltqtileg ffpqvdaaar pvsrarvglt
      361 qlglpyaqda gitrhlaafl grqvaaldal egvqrtlpqg atflhptavl fnggvfkstl
      421 ltqrvldtln gwlaaegapp arllegadld lavargaayy gfvkrgrgvr irggtarayy
      481 vaiesampav pgleppvqal cvapfgmeeg tdaalppqef glvvgepvqf rffgssvrrq
      541 dqvgtlldyw speelqelee iqatlpaegr tvgeivpvkl harvteagtl eleaipsgtd
      601 erwkvefdvr gta
//
LOCUS       WP_175787866             381 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein, partial [Burkholderia
            anthina].
ACCESSION   WP_175787866
VERSION     WP_175787866.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         <1..>381
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
     Region          1..>381
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 yeivlesrla llrnapkcrf fldktfpeii eqvlrehefn qifarfefql hrtyrkrsfv
       61 mqwgeddlaf itrlcrrsgi wfvceegerc ervrfgddya yyrrdperlt vayrphsgle
      121 tggvesvsal emrartlpsa yavrtfntea aisepieavs pirddrttyg eayswgapnr
      181 seeeakeeaq lrreaalagq veyrgecdml dltpgsvlkl snrelpdakh gllvvrticg
      241 asrkksyhvt fdaipsdrqy rmplkeeawp ridgvitgti assggwrdpy ldgqgeyivd
      301 lhldrdtrap glqscpmrla kpfagpnqtg fhfglvegtv vgvsflwgcv dlpfishvlh
      361 taqhtdpiva gvpwgtrnti r
//
LOCUS       WP_175787988             267 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cenocepacia].
ACCESSION   WP_175787988
VERSION     WP_175787988.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..267
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28423
     Region          7..261
                     /region_name="FetB"
                     /note="ABC-type iron transport system FetAB, permease
                     component [Inorganic ion transport and metabolism];
                     COG0390"
                     /db_xref="CDD:440159"
ORIGIN      
        1 mtpalqdlsl vdvgiaaalv avngaisaal slglgrklal aaartvvqll aigyvlgwvf
       61 ghphwyvvlp ltalmtliag fagagrgkrt yrgqridsia siwfsswfva avglfvviri
      121 hpwfapqyai pilgmilgnt ltgvslgver mmeeltarrd rvetalalga trweaaqdaa
      181 rqavragmlp tlnqmavvgv vslpgmmtgq vlagqsplqa vryqivimfl iaaasalgtv
      241 gavlmtyrrl fsadhrflas rleertq
//
LOCUS       WP_175787993             332 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175787993
VERSION     WP_175787993.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..332
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=36802
     Region          14..287
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mnslavtfde irgaydlgrg gpptqvserv whlpadsgag vavklyaleh haravketav
       61 lahlethgdt rfhvqtlkrt rsgaslwsgq nshamltrwe vgqfktydtf sptewdalga
      121 slaalhlsle rmplpspdti rarltaidad avrsslldal dradanvtgt anlrryvdla
      181 lrmldryypg sidafpvddp qhpihndynq fnylftgtlp plildweasi gapreyelvr
      241 clnhlpleap hlaqafvhay qrvrpvnpay iawavdaacl qhalklwivq gwlddpsrfa
      301 shlngavtma samvnardrl vdffsrcmet gs
//
LOCUS       WP_175788123             159 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF2280 domain-containing protein [Burkholderia cenocepacia].
ACCESSION   WP_175788123
VERSION     WP_175788123.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009432
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..159
                     /product="DUF2280 domain-containing protein"
                     /calculated_mol_wt=17548
     Region          1..149
                     /region_name="COG5556"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:444299"
ORIGIN      
        1 maalpdaikv yivqslacfd tisrvakavr eefgvevspq qcerydptkr agsslskkyr
       61 eifertreef lkdtsqigva hravrlrkld havgiaeqrg niplmaqlle qaakeagdaf
      121 tnrhrlehtg keggpitais tvtndpqeaa kiyaklmnp
//
LOCUS       WP_175788161             164 aa            linear   BCT 11-JAN-2025
DEFINITION  TadE/TadG family type IV pilus assembly protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175788161
VERSION     WP_175788161.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..164
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=17069
     Region          6..>65
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mtavlpasgm rrrqrgatai efamvlpvff lilyaiityg mifaaqqnlt laategaraa
       61 lnyqqvgaag svqaaqqaal aaraqaacta atnlttwlkg stcsptqqgs csydptmlcv
      121 qitltypysq splippfpll gsllpvpstl tgtamvqisp vnii
//
LOCUS       WP_175788169             137 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175788169
VERSION     WP_175788169.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..137
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15416
     Region          19..106
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(20..22,36,53..55)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mtttvekvvl ppipakryft igevselcgv kphvlryweq eftqlrpvkr rgnrryyqhh
       61 evllirrire llyeqgftin garnrldspg seraaaepve sdaqavdarg avksganvdv
      121 ialrqalldv idglkhd
//
LOCUS       WP_175788021             233 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Burkholderia cenocepacia].
ACCESSION   WP_175788021
VERSION     WP_175788021.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..233
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24868
     Region          162..232
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mkveehlvas nsglatlgrp refgkkqqnp vrrfggivvv lllhavliya llnglatkvv
       61 qviqhpietr iiepvkpppp ppmpvvklpp pkfapppppf vpppevpvqa ppqqatithq
      121 sapvpsapav qapvvappap akpvshevgv vcpnsdsmra smqypkeaqe nnitgdvtie
      181 fvvdaegnit nervaqsadp vldraayntv krfkcvaqgq avrvqvpfsf nln
//
LOCUS       WP_175788181             506 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CoA-acylating methylmalonate-semialdehyde
            dehydrogenase [Burkholderia cepacia complex].
ACCESSION   WP_175788181
VERSION     WP_175788181.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..506
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53868
     Region          13..490
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(70,72,76,79,83,116,119..120,129..136,141,144,147,
                     240,244,247,250,252,426,428..429,431..432,435,438..439,
                     441,443..446,455,459,461,475,482..487,489..490)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(156..159,167,182,185,215,232..235,238,256..258,290,
                     391,393,419)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(159,256,287,290)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mttvpaytsd advghyldga pvagrsgrfq dvfnpalgra vrrvalagnd everavasah
       61 aafpawadtp pirrarvlhr flqlmnehrd tlaaiitaeh gkvfsdaqge vargidiief
      121 acgvpqllkg dftdqvstgi dnwtmrqplg vvagitpfnf pcmvpcwmfp valatgntfv
      181 lkpserdpsa alfiadlltq aglpagvfnv vqgdkgavda lldhpdvqav sfvgstpiaa
      241 yvqqravqsg krvqalggak nhlvvmpdan ldqavdalig aaygsagerc maisiavlvg
      301 dvadrivpav aerarklvig dgmspevemg pivtgealkr iegyieqgvn egaqlvvdgr
      361 glrvpgreag fftggtlfdh vspdmriyke eifgpvlgcv rvkdfgeavd linahefgng
      421 vscftsdggi arefarriqv gmvginvpip vpmawhgfgg wkkslfgdmh aygeegvrfy
      481 trqksvmqrw sssigkgaef amptak
//
LOCUS       WP_175788202             130 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Burkholderia cenocepacia].
ACCESSION   WP_175788202
VERSION     WP_175788202.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..130
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=13760
     Region          14..129
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mselsveasi gpvdylvhft dgvhqwrade paslgggdaa ptpvalllss lgactaitlk
       61 myaqrkgwpl devhvklahe sgsagstivr rislegdltd eqrerllqia nacpvhkilt
      121 hpitidtaia
//
LOCUS       WP_175788203             293 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia cenocepacia].
ACCESSION   WP_175788203
VERSION     WP_175788203.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..293
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31256
     Region          12..270
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 msasiktllt presdignlv vrrvlparaa rlvgpfiffd emgptvlpag rgidvlphph
       61 iglatvtylf dgslmhhdsl gfrqkivpgd vnwmtagrgi vhserspded rpreqpvhgi
      121 qtwvalpveh edtapafvhh aadtlpsftr dgvtvrviag tafglvspva vfsptlyava
      181 efaaggtlal daeheergvy lvdgdlsvdg tplapatmav lepgasvala stngarvmll
      241 ggahlpgerf iewnfvsser akidaaraaw adqtfgkvpg eenewtrqpa rka
//
LOCUS       WP_175788216             194 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175788216
VERSION     WP_175788216.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..194
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21106
     Region          7..161
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mdshiapval nkayrllnhg ptvlvsarhd gidnvmaaaw acaldflppk ltvvldksak
       61 trelversgt fviqvptaaq lqlthavgsh slaqrpdklr eagvtlfdvd ghdlpfvagc
      121 sgwlacrlip ephnqqtydl figevvaaws dtrvfrdghw yfesadpalr slhyiaggnf
      181 yaigeslhvd pdaq
//
LOCUS       WP_175788232             774 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia cenocepacia].
ACCESSION   WP_175788232
VERSION     WP_175788232.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..774
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81706
     Region          <68..>194
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          203..764
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msapelsvhn esrralllgf asgglllafg vpslaqaaap vqppvsanpq yggagmphgl
       61 rddpnlfvai apdgtvtvtc irsemgqgvr tsvalvvade lgadwarvkv aqavgdepry
      121 gnqntdgsrs lrqsfaalrr agaaartmle qaaaatwgvd vrqvkatvhe vvdtktgrkl
      181 gfgelaakaa alpvpdtksv vlkapaefry igkgktalid grdivggraq ygidtrldgm
      241 lyavvarppv ygdtvasfdt saagklpgvv kvvqlastpl psgfqplggv aviahdtwta
      301 iqaraqlkid wkhgpnagyd saeyrkalea aaaqpgdvir ndgdaaaala gaakrvraty
      361 yiphlahatm eppaavarva dgrcevwtct qapqttrdei akalglpter vtvnvtllgg
      421 gfgrkskpdy vveaallska vgapvkltft reddiahdyf havsleafdg gidasgkvva
      481 wqhrtvapsi qstfrpgvvh eqpgelaqgi adlpfaipnv rienpaaqah trigwfrsvy
      541 niphafgiqs fvselahaag rdpkdflldl igparrfeph itvknvnyge dpalypvdtg
      601 rlrrvvetva reagwgrklp kghglgiaah rsfvsytaav cevqvdadgk isvprvdiai
      661 dcgpqvnper vrsqlegavv mglgialhge itfkdgrpeq snfngfqvlr mneapreirv
      721 hlvapddyat plggvgepgl ppvapaltna ifaatgtrir slpvadqlak rqag
//
LOCUS       WP_175788278             436 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrolipoamide acetyltransferase family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175788278
VERSION     WP_175788278.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..436
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46815
     Region          2..436
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mgihvikmpd igegiaevel vawhvevgqt ikedqpladv mtdkaaveip spvtgkviel
       61 ggrigemmav gselirleve gdgnlkaaap vretkvatap veaappskpa adtsveppaq
      121 pvaprapakp rrdepaappr aalapgerpl aspavrqraw dmgielryvr gtgeagrilh
      181 adldayartg gaahasqprg yderhdetev pviglrraia rkmqeakrri phfsyveeid
      241 vteleslrte lnrrhgdtrg kltplpllir amvialrdfp qinarfddea gvvtrygavh
      301 mgvatqtdgg ltvpvlrhae ardvwsisae iarladavra nraqrdelsg stitisslga
      361 lggivstpvi nhpevgivgv nriverpmir dgavvarkmm nlsssfdhrv vdgadaaefi
      421 qavravlerp allfve
//
LOCUS       WP_175788307             146 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia cenocepacia].
ACCESSION   WP_175788307
VERSION     WP_175788307.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..146
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=15477
     Region          1..146
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mrftlngqpf dfdgdpdtpl lwvirdsarl tgtkygcgig acgactvhld geaartcvlp
       61 aasvagravt tieglshdrs hpvqrawiek dvpqcgycqs gmvmataall ahhrkptdaq
      121 idaavtnlcr catyqrirea ihvaag
//
LOCUS       WP_175788341             331 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175788341
VERSION     WP_175788341.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 331)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 331)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..331
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35177
     Region          19..148
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          <192..331
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msstrlpdsa rywrtplvpd adlltatyrd hafaphwhda ytipvilega erftyrgtgy
       61 vaetgtvpvi npgevhtgsr aadegwcyrv sympvefihe lastiagrpq dapwfapdvi
      121 rdadlaarlt lahrmleags eralssqada pgqptgdpaa gdpaagdsaa gdsaagdsaa
      181 gdsaagdsat gapriydpla aetamldals tlivrhadvr pqpaplaade prvdamrerl
      241 aadlmctvtl ddvaqvvgls pfhaarlftr ttgmpphawr nqlrlqrala plragvpvad
      301 vaaasgfvdq shftrhfkrm fgvppgrwqa s
//
LOCUS       WP_175788350             264 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Burkholderia cenocepacia].
ACCESSION   WP_175788350
VERSION     WP_175788350.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..264
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28147
     Region          3..264
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mqrrfmlkft aalgaavlfa gaqahaetik vgvtggphaq imevvkkvaa kdgleirive
       61 fsdyvqpnaa lasgdldans yqhdpylqaq vkdrgyklik vadtvtfpmg iyskrvksla
      121 elkpgarvav pndptnggra llllqkqgll klradaglka tpldivdnpr klkiveldaa
      181 qiprslgdvd aaaintnyam eaglkpkqda iaiegpsgpy anilairdad rnkpwvakli
      241 aayhsadvkq fiegkfggav iaaw
//
LOCUS       WP_175788417             243 aa            linear   BCT 11-JAN-2025
DEFINITION  DsbA family oxidoreductase [Burkholderia cenocepacia].
ACCESSION   WP_175788417
VERSION     WP_175788417.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..243
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26074
     Region          15..214
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(23,26)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 mttaptptdr ptltveiwsd licpwcwigk rrfdealaaf ahtdrvdval rayrlmpgqp
       61 vepveamlag kyrmspaqvd qmlrqvtdaa asvglrydlp gtlvgdtldg hrlvklaeat
      121 grahalterl yrayfcehgs lfdhaaltef aveagleraa veavlrsday rdeveadiar
      181 aaqiggrgvp lfvfggryav sgaqpadafa qaldqawrdg ivaldgsdaa acgpdgcelp
      241 ars
//
LOCUS       WP_175788485             215 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Burkholderia cepacia complex].
ACCESSION   WP_175788485
VERSION     WP_175788485.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..215
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22704
     Region          14..129
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          80..209
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mkdkpaqgpr gldkdaivaa alalledvge aafsvrklaq svgcdpmsvl yhfkskegls
       61 raianalsrs lvpvepslpw rerlrdlarq yrtlalrypa afallqrhms tgpadlahie
      121 avhraltdag iphaalpsvc vgwyasvigl aaaeaggltr aandvelaem halsdaahpl
      181 vksaaplyaq ldpavvhdtm ldvlldgiaq rarta
//
LOCUS       WP_175788514             424 aa            linear   BCT 11-JAN-2025
DEFINITION  GspE/PulE family protein [Burkholderia cenocepacia].
ACCESSION   WP_175788514
VERSION     WP_175788514.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..424
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=44707
     Region          <35..414
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mhfpspgapl htqsppahsd apagaphald aaqlddapav rlltdtlhaa rardasdihv
       61 epfeagwrir lridgvlheh arpplhlrda lvtrikvlsr mdiaerrlpq dgrlriaidg
      121 gtrgdyrvss lptlfgeklv lrrletlppd ltlanlgfda rqaaameaai raphglvlvt
      181 gptgsgktls lycalqmldr dahnvctved paeiqldgin qvgvadkagl tfatalrall
      241 rqdpdvimvg eirdaetadv aikaaqtghl vlstlhtnda paavarlldi gvapynlaaa
      301 lhlvtaqrlv rrlcvacrvh sdasahalre agcdpaalaa gwrpfvargc sachgigyrg
      361 riglhqtmpv spglaeriva rasvgelaqc vaaegvrtlr daafarvldg ttsiaeavaa
      421 tpaa
//
LOCUS       WP_175788519             468 aa            linear   BCT 11-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Burkholderia cenocepacia].
ACCESSION   WP_175788519
VERSION     WP_175788519.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..468
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=48118
     Region          2..458
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mtmlslgeaa rlipgatvhg dagvtfdrvs tdsrtvgpgd lfvalkgerf dahdflgdva
       61 argaaaalva hapagiampm ieggetraal galahgwrmr fplplvavtg sngkttvkem
      121 iasifaaavg adarlatagn lnndvglplt llrlsaahrl avieigmnhp getevlarlt
      181 aptvalvnna qrehqefmat veavalehaa vihalppdgv avfpaddaya siwrvaatgn
      241 rildfalhda erqndaqvvg rmrggelaid tpagavtvrl ralgehnarn alaataaalg
      301 agvalsairq gleafepvkg rlqvkqasvg slagatvvdd tynanpdsmr aaidvlaahp
      361 aprvlvigdm gevgdegpaf hreigayare rgidalfalg dasrdactay gdtarhfddv
      421 galvsallaa gygaqatvlv kgsrymkmer vvdaltnqpa agtvpaah
//
LOCUS       WP_175788569             293 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia cenocepacia].
ACCESSION   WP_175788569
VERSION     WP_175788569.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..293
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31319
     Region          13..270
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mtdsikallk phvrdignlq vrrtlpalaa rlvgpfiffd hmgpatlpag tgldvrphph
       61 iglatvtylf dgailhrdsl gslqeivpgd vnwmtagrgi vhsertpdaq rasghtvhgi
      121 qtwvalpqah ettepsfehh aadtlpkrde ngvaltviag dafglrspvt tfsrtlyvaa
      181 efaaggrlel dasheeravy vvdgalaidg tpvpaeqmav lapgatvtlt sasgaramll
      241 ggdrmdgerf iewnfvassr eaieqakaaw trqemgkvpg etewiplpea kpr
//
LOCUS       WP_175788529             177 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Burkholderia orbicola].
ACCESSION   WP_175788529
VERSION     WP_175788529.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia orbicola
  ORGANISM  Burkholderia orbicola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Burkholderia orbicola"
                     /db_xref="taxon:2978683"
     Protein         1..177
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19430
     Region          4..171
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrprvsvfla lsldgfiage nddlswlepf ssdspddtgy talmndidvi vmgrntydtv
       61 infdpwpyag krmvvmtrre lasrhgeepf dgalatlldr laaqghrhvy ldggltareg
      121 ikagvvdrit lswvpivlgk giplfgaelp qtllrlddtk rlpsglmqat yvpvmqd
//
LOCUS       WP_175788593             304 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175788593
VERSION     WP_175788593.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..304
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35185
     Region          85..242
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mrfdvellll alapvfllci aweawhlart raqdriyawr dtlcnaalal mhqgadklaw
       61 lfvipvyayc yrhyrvytwh dgwlsfavlf vaqdflyyvf hrashrvrwl waahvvhhss
      121 ermnfstafr qslmypvagm wlfwlplafa gfppqqvvgi vlinlafqff vhtqaigklg
      181 wleyvlntps ihrahharna ryidrnyagv lviwdrlfgs yveetpddpp qygiverlgs
      241 nnplvatfhe wvsmasdalr vdgwrnklra ifgppewasa yhaqiaeaan qdprteplaa
      301 ardr
//
LOCUS       WP_175788595             895 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175788595
VERSION     WP_175788595.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 895)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 895)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..895
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..895
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=98026
     Region          15..827
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnsqalrsal lagpvqherl ikldtplgpd vllpqrvtgr srlgrhfeft vdtvsvsddl
       61 elkkliaqpv tlwiqqadqs yaphhgyvha arrlgsdsgv thhqivfasf lhflkfrrdq
      121 riwqdrsadd iiadvlnqhp qakgrftfkl yqplpsrsfc mqyeddwnfv hrlmesegly
      181 gfweqdsdgk shrlvivdri dalpalsprt vrfhhagtgd eadtlvqftg trtlrsvart
      241 trtfdykqpp tasnpkatht ptianqgdlp qqlevyeytg aytypeqsrg dhlskiwmee
      301 qeshakrfhg iggvrrmdag rvfefaehpe hdkddagqre favietawvi vnnlpvadep
      361 avfphslqae igsimqatdt drsrvrhpdg segffqirie aqrttvpfrs pfehakppmh
      421 lqsaivvapq geevhtdeln rvkvrfhwdr lndgdekasc wlratasdsg ngygavhphr
      481 sgeevlvdfl ggdcdrpiiv gkvyngatsp qwhsngilsg yrskeyagag ynqlvlddat
      541 aqnrvhlyss qanthlhlgy lidhtgnnrg sylgsgfdlr sdaygavran rglyvtthpk
      601 qaasqpldvd etreqlvraq glidamsqvs aqhqgesldp ghtalkqfsd atqnsvsgst
      661 sggrtagggt gnanafkepv mlfgspagig mstqqsaqfs adqhinlvsg qsthvaagks
      721 liasvldris lfaqnagmkl fagkgkvevq aqadnielta qkalkliavt qsiegaaake
      781 illtsggayi riadgnievh apgkidikga qhafsgpthl sqtmptlpns ngnydqafia
      841 hwagtdipvt ntryqmfsng kllsegvtna agetgltqsh vphdvvvkfl gksng
//
LOCUS       WP_175788603             486 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [Burkholderia cepacia
            complex].
ACCESSION   WP_175788603
VERSION     WP_175788603.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..486
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52224
     Region          1..388
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfeslglae plvkavnelg ytsptpiqqq aipavlgggd llagaqtgtg ktagftlpil
       61 qrlhtfyaeh rgakravral iltptrelaa qveesvrays kylklrstvm fggvsinpqi
      121 dalkrgvdiv vatpgrlldh mqqktidlsd ldilvldead rmldmgfihd ikrvlaklpp
      181 qrqnllfsat fsdeikalad slldspalie varrnttaes vaqkihpvdr drkrellthl
      241 irehnwfqvl vftrtkhgan rlaeqltkdg isamaihgnk sqsartrala efknstlqvl
      301 vatdiaargi didqlphvvn fdlpnvpedy vhrigrtgra gatgeavslv cvdekqllrd
      361 ierlikreip qeviagfepd pnakpepiqq rrgqqqprgg gggggnrqpr aggsgqpaak
      421 rdgnaqpkag qpkaapqqka akprtqggaa gnggrpaggg ngarpasgna ahpnrnrssr
      481 sgqrgh
//
LOCUS       WP_175788630             320 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cenocepacia].
ACCESSION   WP_175788630
VERSION     WP_175788630.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..320
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34834
     Region          81..282
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mswqskfacw llrwqfrpet trevldpara rrftdlrmfv prrppsgyrl rqcygaadap
       61 lrgewlertd aaaghgpgrt llyfhgggyy fcstkthrpl vfgltkragv rsfsldyrla
      121 penrfpaald dalaayrqll algtppesiv fggdsagggl alatlvalrd rgeplpagai
      181 lfspwtdlag tggtmrgndg vdpmfaaaal pkaaklylgd apathpyasp fyadftglpp
      241 lyiqvgstev llddsrrvae kakaagvqve ievwpdmphv wqlyapmvpe ardaldraag
      301 flrrvavera vqrageasia
//
LOCUS       WP_175788673             381 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175788673
VERSION     WP_175788673.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..381
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40494
     Region          1..376
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfqhtedrr mladtlnrfi aeqyafpvrd riaqsaegfd ramwqrfael gtvgalfaea
       61 dggfggagfd iavvfeclgr glvvepflga llagralala ggaahrdrla alidgsasaa
      121 fahdepgshy elttvrtrae rsgdgwvltg akgvvdqaaq aaffvvsarv sgndddaagi
      181 glfvvpadap gvslrdyrki dggraaevrf ervalpadaa lgapdaldge agaellervl
      241 gygllalsae algamdvaka ytldylrtrk qfgipigsfq alqhrmadll leveqarsav
      301 inaaaqldap ravreralaa akysigrigt lvaeesiqlh ggigmtwelp lshyakrlvm
      361 idhqlgdedh hlaryialsk q
//
LOCUS       WP_175788685             408 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175788685
VERSION     WP_175788685.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..408
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43865
     Region          1..291
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mrlalvlmgg garaayqvgv lkalaeiare adpqrhtlpf tvvcgssaga inatsvasha
       61 ddfshgvrrl lefweplrad yvyrtdwlgi aaagarwlat mtfgwaarrs prglldntpl
      121 ahllqrelsf hrieqmlear llhalaital syssgrhltf yqaaepiqaw rraqrtarlv
      181 dlsashllas saipfvfpav plvldgqiey fgdgsirqia plspaihfga drivvvgaad
      241 prpeipaang agrargypsl aqigqqvlas vfldsigsdi eriehinrmi ehlphqveid
      301 sgwrhvdvla iapserieli aakhlkqmpa tmrgllgaig gsqpagasfa syllfeeaft
      361 relielgyrd graqrdtlag wiaqadgssa paagtppegg laageirv
//
LOCUS       WP_175788718             261 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia cenocepacia].
ACCESSION   WP_175788718
VERSION     WP_175788718.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..261
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=27181
     Region          9..242
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 merkplvgit adltqigaha shtvgdkyva aivdgahala mvlpalgerq ssadvldavd
       61 gllftgsysn vephryggep sapgtkhdpa rdattlpllr aaivagvpvl avcrgfqeln
      121 vvcggtlhqr vhevpgfadh redddapmdt qygpahvvrl tpggklhala ggrdevhvns
      181 lhkqgiaqlg sglaieavap dglieavsvv dapafalavq whpewrhaqd plssaifraf
      241 gdacrarraa rtramaaaal a
//
LOCUS       WP_175788814             357 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia cenocepacia].
ACCESSION   WP_175788814
VERSION     WP_175788814.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..357
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=37288
     Region          43..357
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkktrqvvvr vaarrgvgtv gvtaifsagl vlnsvgayad sgsqvqlygl lgtyvgsikr
       61 sdtpqsavqm gsgglttsfw gfrgkedlgg gvgaifvles ffqpangalg rsaadpfwsr
      121 nayvgfqgdf gqvtfgrqrn paytaeslvn pfgsstvfsp lvlqtfvtny ggtiigdtvw
      181 nntvkyttpd fkgfaatviy glggvagspg vgnlgvhlny qghgltavls gqrvrytaag
      241 pvgaqyayla gaaydfklvt lygawamtsd astptgshty eaglsiplsp adfllaewar
      301 tkrsgatpaa gslrntasvg ynhllskrtd lyavyaydkl sahptgnsfa vgirhtf
//
LOCUS       WP_175788840             214 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia cenocepacia].
ACCESSION   WP_175788840
VERSION     WP_175788840.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..214
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22897
     Region          1..203
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mkllhldssi ldgnsitrtl saavvadlra rhplaevtyr dlvsdeiahl tgpiaagfrd
       61 vatdafddda irehrvsvtl vteflasdvi vigapmynfs vpsqlkawld riaqagrtfr
      121 ytehgpvgla sgkcvviasa rggfyaegpl agmdfqenyl nrffgflgvt dvwfvraega
      181 skgqrvrdeg ialaraaiad vlagvpapda rpvk
//
LOCUS       WP_175788842             556 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia cenocepacia].
ACCESSION   WP_175788842
VERSION     WP_175788842.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..556
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=60081
     Region          6..537
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mthrdtksvd yivvgggstg cviagrlsed erssvallee gprdrspyih ipgayyktaq
       61 gpllkripwh ptqgharpam ptmvqasvlg ggssvnamiy irgvpsdydq wrdsgatgwg
      121 fddvlpyfkr sednerfcnd vhgtggplrv sdiphthplt kawlkacqqs glpynedfns
      181 ghpagcglyq itardgrrss aavayihpal nrpnltvrtg vrvtriliek gravgvefrr
      241 ngrieqmran revivsagal stpkllmlsg igpsaalqrh giaveqdlpg vgrnlqdhie
      301 islvyqlngp ysydkykkph wkalaglnyl lfrngpaasn lieggafwwg dkealtpdiq
      361 yflvvgagie egvdsvpggn gctinlgqir prsrgfvels gpdpmdaprv fpeyfsdpyd
      421 leavvdgcek aidimgqpai dkyiaqrivp gkqaasrdel rkfvrqdaha alhpcgtcrm
      481 gtdgdsvvdp slrvhgidgl rvadasimpn iisgnlnavc imigekaadl ilgkapltri
      541 ghasvpidse asrvts
//
LOCUS       WP_175788846             566 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia cenocepacia].
ACCESSION   WP_175788846
VERSION     WP_175788846.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..566
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=64532
     Region          23..388
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mtqqslangh dsnhfdviil gsgmsgtqmg ailakqrfrv liieesshpr ftigessipe
       61 tslmnriiad rygipeldhi tsfyatqryv asstgikrnf gfvfhkpgee hdpkeftqcv
      121 ipelpwgpes hyyrqdvday llqaaikygc tvrqktsvte yhadedgvav ataqgerftg
      181 rymidcggpr aplatkfglr eepcrfkths rslythmlgv kpfddifkvk gqrwrwhegt
      241 lhhmfeggwl wvipfnnhpr stnnlvsvgl qldprvhpkp dispqqefda flarfpsiaa
      301 qfrdavpvrd wvrtdrlqfs sracvgdryc lmlhangfid plfsrglent avtihalaar
      361 likalrdddf sperfeyier lqqklldhnd dfvsccytaf sdfrlwdafh rlwavgtilg
      421 qfrlvqahar frasrderal dhlddnppyl gylcadmegy yqlfndakae veavsarrkp
      481 ageaaariha liderefakp mfgfgycitg akpqlnnsky sllpamkllh wtqtsapaev
      541 kryfdynpmf allrayvttr iglalk
//
LOCUS       WP_175788854             245 aa            linear   BCT 11-JAN-2025
DEFINITION  YoaK family protein [Burkholderia cenocepacia].
ACCESSION   WP_175788854
VERSION     WP_175788854.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..245
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=25104
     Region          22..233
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mqpaqvtaag aaapdrvrge dvflasiagy vdtlgfialf glftahvtgn filigsglag
       61 vgqglmikwl afpafiagiv aarvldhrmr vrghgvrars lyalqtillv gfmlagvaas
      121 pigsadapat ivcgllgaaa mgvqnahgrl tartvvantv mtgnvtqavi dafdwlvpia
      181 apaereaara rlrrtlppvv gfalgagaga sayvyagfwt lvlplaalgf ltwrsgrtge
      241 psvsr
//
LOCUS       WP_175788879             216 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cenocepacia].
ACCESSION   WP_175788879
VERSION     WP_175788879.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..216
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22233
     Region          7..193
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtlhypllfa ylaaivllia tpgpvvmlvt gtvarrgfrq gvltavgana aslvliagam
       61 lmvfgvvmvs arllvglhva gclfiavlai rtllgewrag rgrsgdgtaa gepasqprgl
      121 pgvvrgflvg ianpkdllff vaffpqfvgi tpdsrvslai laalwiavdf timigymaai
      181 nhpaihrkqr wivassalal laialaglgg tiagva
//
LOCUS       WP_175788926             401 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia cenocepacia].
ACCESSION   WP_175788926
VERSION     WP_175788926.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..401
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43139
     Region          5..361
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mstawsrarr ilcvrldsig dvlmttpalr alkesgadrq ltlltsrtga alakhlpmvd
       61 dvwsydapwv khpdvrgdpv adldmidrll agrfdaavif tvysqnplpa ammcwlagip
      121 lrlahcrenp yelltdrvpe tepeshvrhe varqlalvra vgaktsdwrm afepgdaarr
      181 avharlqaal qriggargle atrarwlvvh pgataasrrw paerfgeaaa avaplfdgia
      241 vtgsaderal vdavceragp ravplagvlp lgelgaliet adlllsnnsg pvhlaaalgt
      301 pvvdlyaltn pqhtpwrvph rvlnvdvpcr ncyrsvcnqp ghpclrgvsv ddvaaavhal
      361 lrgrarhaqr aaeraaahde gepvaahasn vipfahvitr n
//
LOCUS       WP_175788996             159 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia cenocepacia].
ACCESSION   WP_175788996
VERSION     WP_175788996.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..159
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=16831
     Region          82..144
                     /region_name="BON"
                     /note="BON domain; pfam04972"
                     /db_xref="CDD:428229"
ORIGIN      
        1 mnsrtpsnpl lnlavavacg aaamyfldpa sgrrrraylr dkavagrhdv adyantqvkr
       61 aadhargaia glradwlagd asdvqvaerv raalgrlvar prdievsver gnvcltgqve
      121 eaerqalidg vaalhgvhhv edamgarsey kaspdghsq
//
LOCUS       WP_175789050             295 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            cenocepacia].
ACCESSION   WP_175789050
VERSION     WP_175789050.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..295
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30453
     Region          2..294
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mssfvihllt vgclyatmal glnlqagyag lvnfgfiafs glgayaagia sqlgwplpsa
       61 lalalaaaga laivvarlgr qlsadywgia tlaiaeilrt ialneswltg gaqgiggiap
      121 lfpglrapwa dlaflaitag claltyatyr rltasrfgra lkvmreepal avcfgydpla
      181 lktraciaga lpaalagala awyigyvgpd amiasetfal wtvvmvgglg shmgvlvgtl
      241 ivqavyalap flkdwlavgs dltgavrlgl vglmllacvl wrphglvper levrp
//
LOCUS       WP_175789012             255 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cenocepacia].
ACCESSION   WP_175789012
VERSION     WP_175789012.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..255
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=27695
     Region          3..235
                     /region_name="ArtM"
                     /note="ABC-type arginine/histidine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4160"
                     /db_xref="CDD:443325"
ORIGIN      
        1 mifslpflld tvmpkllaav pttlaltlvs gaasvllgvp lalaagarht plrwsargwl
       61 mlirgtpllv qlyllyygfg qivprewmrd swaspllrda fwyaivalsv nesayvatil
      121 rgaiagvpag eieaghaygm trvqvlrriv gprawrlalp altgeailll kstvlastvt
      181 vfdvmgtant lrfetlrvye plagaaivyv vlvalltipa arleqrinry ltrqpdervp
      241 arrrrassga waapn
//
LOCUS       WP_175789053             465 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175789053
VERSION     WP_175789053.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..465
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46804
     Region          27..455
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,153,
                     156..157,160,283,286..287,290..292,295,323,327,378..379,
                     383,387,403,406..407,410..411,414)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msggsatpaa gayasaaarp vlvmvalacg fvmamldvti vnvalkamet slsmsltalv
       61 wvvdaytlsf aallllggal anrygskavy vaglalfvga svlcaaaqss galvaarlaq
      121 gvgaalfmps slslltlafp pgptrtrmig iwgalvsaam algpcvggvl vdaigwrgif
      181 wvnlpvgaag lwltyrhiar aprhpgplna lghlfgalal aalsftlieg psagwrspsi
      241 lagvaatlaa taafvlrery ahsrilspal lanrrfvags tlglainfgi laeifllsly
      301 lqnvrgasal vagfelfplm amfgignlas akvsarlgar rtlliglala algsvalvgv
      361 aampypalav aiglanfgag qaipamnlvv mqsadaadtn laaaslnasr qigslvgiai
      421 asvilhaidd pdratavgfv viaalyalgf aivfraihag paeqs
//
LOCUS       WP_175788729             319 aa            linear   BCT 11-JAN-2025
DEFINITION  complex I NDUFA9 subunit family protein [Burkholderia cenocepacia].
ACCESSION   WP_175788729
VERSION     WP_175788729.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Parey,K., Wirth,C., Vonck,J. and Zickermann,V.
  TITLE     Respiratory complex I - structure, mechanism and evolution
  JOURNAL   Curr Opin Struct Biol 63, 1-9 (2020)
   PUBMED   32058886
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Babot,M., Birch,A., Labarbuta,P. and Galkin,A.
  TITLE     Characterisation of the active/de-active transition of
            mitochondrial complex I
  JOURNAL   Biochim Biophys Acta 1837 (7), 1083-1092 (2014)
   PUBMED   24569053
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..319
                     /product="complex I NDUFA9 subunit family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0010257 - NADH dehydrogenase complex
                     assembly [Evidence IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=33881
     Region          5..278
                     /region_name="NDUFA9_like_SDR_a"
                     /note="NADH dehydrogenase (ubiquinone) 1 alpha subcomplex,
                     subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs;
                     cd05271"
                     /db_xref="CDD:187579"
     Site            order(10,12..15,34..36,74..76,93,116..118,129,133,
                     156..159)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187579"
     Site            order(129,133)
                     /site_type="active"
                     /db_xref="CDD:187579"
ORIGIN      
        1 mdrqtvallg gtgfigsrlv nalidagkhv rigtrrrdha rhlqmlpvdi veldaldtrt
       61 larfvagaha ainligvlhg grgtpygpgf erahvalpaa latacsevgv rrllhmsalg
      121 adshgasmyq rskgdgeaal havaatdsla ltifrpsvvf gpgdaflntf anlqrtvpvl
      181 plampdarfq pvfvgdvvrv fvntldltga hgktyelggp svytleqlvr ycgtlvgrqa
      241 rivrlpdala rlqasvfecl pgepvltrdn latmsvpnvl sgplapelgl spaslesiap
      301 aylgeatgrs rfdwfrsrr
//
LOCUS       WP_175789137             127 aa            linear   BCT 11-JAN-2025
DEFINITION  GtrA family protein [Burkholderia cenocepacia].
ACCESSION   WP_175789137
VERSION     WP_175789137.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..127
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=13635
     Region          5..127
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mstllqaert rlvrfgvsgl cstaihvlva talfarldaa pvtanaiafl cattfsylan
       61 tlwsfsstvr trnamrfltv tlvgfvetml iaraaealga sramgvvaia llippttfvl
      121 hrlwtyr
//
LOCUS       WP_175789141             480 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175789141
VERSION     WP_175789141.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..480
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48765
     Region          37..470
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(43..44,47..48,51,83,133..134,136..138,141,163,
                     166..167,170,294,297..298,301..303,306,334,337,390..391,
                     395,399,415,418..419,422..423,426)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msdraptldr vdrvptptad ssrtslraif ptvaaaslgf aivqldvtvv nvaipslgha
       61 fgssvhglqw ivdaytlsfa allltsgtla drfgsrrlfa yglalfllas lgcalapsla
      121 alvaarvaqg vgaamilpts lalithacan daaarvrava wwsatggais aagptlggll
      181 idslgwraif finlpicalg lwltlrrvrd saaartrlfd pagqfvavlv lglltggiir
      241 agahglgdpy aagaliasvv fgalfvaier rvsapmlqla lfrlprvpgv laigsitnaa
      301 fyglifslsv yfqnargfta tesglalapl tiimlanias arlavrygfr atviiglavs
      361 lagylwlwqt laahtpyvll apglaamaig ggiaipalts tmlgsveagr sgtasailnt
      421 arqvgaaigv aalgalvagq gaaivagatr afaiaavlva icvvlavrwp rdasgtgtrp
//
LOCUS       WP_175789148             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175789148
VERSION     WP_175789148.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33922
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..294
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,223..228,
                     234..235,237..238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdllkamavf vrivetgslt aaaqasdlsp tmvgnylqtl etrlgavlvh rttrkqkvsa
       61 fghayyercv eilglvddte qlalahlkqp rgrlrvtapv vftneclipa ladyyrrype
      121 ikldivatds ladlfdegfe aairigtlan pdvvarplap yrlvlcaspa yvrehgapat
      181 phalsehhcl tyayppraew haaqtqwtle gpdgpmslsv dgrlkidnad alrraalrgl
      241 giamlpsili rddirekrli eimpdfagpe rtmnllylqe rqqspklrsf tefvvdrfga
      301 etacrt
//
LOCUS       WP_175789149             209 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            cenocepacia].
ACCESSION   WP_175789149
VERSION     WP_175789149.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..209
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22390
     Region          17..154
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maiaidrssg twyfsrmtrk tdararaiat aerlfriqgy tatgltqile esgapkgsfy
       61 fhfprgkaql aeeaidnyit hriavlqnis adttghaldf vrqifstfaa emvatdfqyg
      121 clmqnlanel paldaeltqr vargfadste viaahfrgcg faaarassaa aalvaalega
      181 rtvarlersp avfdaladvs sqgwgdseg
//
LOCUS       WP_175789157             442 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175789157
VERSION     WP_175789157.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..442
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48251
     Region          33..421
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(46..47,50..51,54,86,136..137,139..141,144,164,
                     167..168,171,266,269..270,273..275,278,306,310,361..362,
                     366,370,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 meidaacnpg dlaapasahd laqedrifrr lalqilpilm fayvtsyidr vnvsfaklqm
       61 sqhlgfsdav fgfgagiffl gyvifevpsn mllvrvgprr witrivvswg vvsgltafvs
      121 tpmqfyvmrf llgvaeagfi paivlymars fpgrrraril smfyaalala gligspltgf
      181 ilqyfdgamq ipgwkwifil eslpafvaal yvwkgldddv trserfsqae ravltrvlae
      241 drattesvnh rglfsnwlvw afcviyfldv faiygytfwa ptmikqmgig sdfvigllaa
      301 lpnavavvvm vlfgrsadrr grqrlhvaal llmgatglgl svvwhdqlwl gmfalciana
      361 glisfpplfw smptaalgta svsmgiavis sfgnlggffg pyavgylkqa sgslaaplfv
      421 mvgclllglv ltmllparlv dr
//
LOCUS       WP_175789183             188 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: carboxymuconolactone decarboxylase family protein
            [Burkholderia cepacia complex].
ACCESSION   WP_175789183
VERSION     WP_175789183.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..188
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19618
     Region          40..178
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msrlplptie tapaasqpfl eksqrangfl pnlvrslana pvaletyltv aeingraglt
       61 faereavqit aaavhgcafc vaghtaaalk kahvdradvd alrdgepvae prleavaaft
      121 raviatrgav tddalaafla agfteanale vvlgvslatl cnfannlsrn elnpelaayr
      181 weprtqaa
//
LOCUS       WP_175789202             343 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ParB/RepB/Spo0J family partition protein
            [Burkholderia cepacia complex].
ACCESSION   WP_175789202
VERSION     WP_175789202.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..343
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37390
     Region          70..299
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 makdtskdkk ptgnlhlaag llrglaqena aletrlpepa aapaavvdaa pasgpaatap
       61 agtpelgapq kvlvkdcipn pfnprvfyse sslhelaltl kregqiepik vtrlpefpgk
      121 lvvidgqrrl ratsingdet inatfrtdht peqlytiayr anhdherqti fddaiawkrl
      181 ldekvfsdqn tlaekigkdk asisktlsln alpntllerm asandvvglq aayflklife
      241 rlgeatadrl ltavidrkks vrdlenflra qsdgtkkagr trysvrhdfa lesraigqlk
      301 typdgrldlq lkgvdashqe aladklktvi dayveelata psk
//
LOCUS       WP_175789237             374 aa            linear   BCT 11-JAN-2025
DEFINITION  Fic family protein [Burkholderia cenocepacia].
ACCESSION   WP_175789237
VERSION     WP_175789237.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..374
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40826
     Region          23..367
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mmsgdytfiw eaadwpawrf dlpalatpla dvsraqgmla grladvglal rdeaslaalt
       61 ddvvktsaie genlnvasvr ssiarrlgvd igalapvdrh vegvvdmvld atthsaapvt
      121 earlfgwhaa lfptgysgls ritvggwrtd asgpmqvvsg pigrqrvhfe aplaarvpde
      181 igrflawlna ppaepllira glahlwfvtl hpfddgngri aralgdlvla radrspqrfy
      241 slsaqiqrer nayydvlert qrgsldvtew lawflntlgr aidhahttld avlikarfwq
      301 rcagvamner qvkvmnrlld gfegkltttk waalakcsqd talrditelv eqgmlrrsas
      361 ggrstsyelv pfdg
//
LOCUS       WP_175789240             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175789240
VERSION     WP_175789240.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46230
     Region          22..420
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,150,
                     153..154,157,245,248..249,252..254,257,285,289,347..348,
                     352,356,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mndnppvpha pprirrgqri alallmasgi vnyldrgtla vassairgdl glslaqmgll
       61 lsafswsyal cqfpvgglvd rigprrllgi glivwsfaqv sgglvstfgw fivarivlgi
      121 geapqfpsaa rvvsnwfplr argtptgifn aasplgtala plllsvlvas fhwrwafivt
      181 galglvvavv wfafyrdpvr aqlsaaerny ldadaqsvaa apkltfaewr slfshgttwg
      241 mligffgsvy lnwvyltwlp gyltmerhms lirtgfaasv pflcgfvgsl vagwlsdlvt
      301 rrsrspvvsr rnavvaamlg mvaftipaal vqsntvalac isvviflana asacswalat
      361 aaappsrias lgaiqnfggf iggalapilt giiaqkwsfv palltaaaia fagamaylll
      421 vrkpipeqaa naapgplpa
//
LOCUS       WP_175789286             281 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia cenocepacia].
ACCESSION   WP_175789286
VERSION     WP_175789286.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..281
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29988
     Region          10..257
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(24,105,107,109..110,138,189,210,213,226,228,257)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 msnvtfpgqr vgdftitais dgyltasldf lsnidatdaa gmqraagqqa psavhincyv
       61 vrgagrtvli dagaggikqw ggrlmdnlrl agvepaaidt vllthahpdh vgglvhadgh
      121 vafpnaelvt hrrevafwrd dgnlsraser argnfriarq vfdaysdalr tfeegevlpg
      181 iaaiplpght dghtgyllas gdqgllvwgd ivhfphiqik rpdvsiafdq dasqaattrs
      241 rlldrvsseg lliagmhlge pgfarirras geyglfyetd a
//
LOCUS       WP_175789343             320 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175789343
VERSION     WP_175789343.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..320
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35285
     Region          7..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..291
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(111..112,114..115,118,122,124..130,221..226,
                     232..233,235..236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 matklsfevl evldaidrtg tfaeaaellh rvpstltylv qklesdmdve lfdrsgrrtr
       61 lteagravve dgrrlldaar hleakakgir dsweselrlc vdailpirsl wpyvhafydl
      121 emntqlslst evlggvwdal vtrradlaig afgepphaan iaarpigtlr hvfvvapdhp
      181 laripeples etiagyrgvv isdtsrelqp qsvatrdgqp lvivptlaak lqalcegiav
      241 gmlpdfvake pihegrlvar rivgvreftn gylawredkv gnalnwwiaq ldstdllerl
      301 ltprqeskgq pgtatcavry
//
LOCUS       WP_175789356             196 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: flavodoxin family protein [Burkholderia cepacia
            complex].
ACCESSION   WP_175789356
VERSION     WP_175789356.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..196
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=20704
     Region          <47..189
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mdqlnppvkt avvyhsgygh tqrmaaavad gagaalvaid adgnladdaw ntladadail
       61 fgsptymggp swqfkkfada sskvwfksgw qnkifggftn sasingdkln tleyffllag
      121 qhggiwvsmd ikpanlkast rddlnrmgay iapmaqtpad aspeemspgd letarrygar
      181 vaaiagqlra gqsrsn
//
LOCUS       WP_175789383             127 aa            linear   BCT 11-JAN-2025
DEFINITION  sirohydrochlorin chelatase [Burkholderia cenocepacia].
ACCESSION   WP_175789383
VERSION     WP_175789383.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..127
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=13073
     Region          1..>127
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 msshgivlfg hgardprwae pferlaarlr gagssaahvs laflelmtps lgeavaaqva
       61 agcaritvvp vffgqgghvr rdlpqlvdac raahpgveir catavgeddg vldavaryci
      121 dqlggda
//
LOCUS       WP_175789408             207 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            cenocepacia].
ACCESSION   WP_175789408
VERSION     WP_175789408.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22152
     Region          6..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maergrprsf dkeaaldram evfwrlgyeg asmtdltaam giaspslyaa fgskealfrq
       61 alehyrateg qeiwggvera asaydavqny lmdtarvftr rskpagcliv lsalhpaers
      121 dmvrqtligm regtvdalre rlaqgvatge iaahanldai aryyvtvqqg msiqardgas
      181 rrdleavaqa alaawpalvg tgsaagv
//
LOCUS       WP_175789468             392 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 9 protein [Burkholderia
            cepacia complex].
ACCESSION   WP_175789468
VERSION     WP_175789468.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..392
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43019
     Region          8..369
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 malfssarpp rtilvaaprr igdvllttpl vrslkarwpd aqidmlvfrg tegvlehnpd
       61 vrrvivvaqr aglgerlrda lsmwrrydla caalssdrpr fyswfagrkr vglvdpnrvt
      121 wltrmmlngi ainhhesaht vvstlalapv igiepvsevv apgigddpar rarfdawlae
      181 spairagkpl vvlhpypmfr ykqwrldgwv emigwlreqg faialsggpa drereyaeqv
      241 ateaggdvln lvgrltfges aelvrrarlf igpdtgathv aaatgtdtia lfgpsdpvrw
      301 gpwpqhwpat enpwalrgsg rhanvwllqg dgdcvpcrhe gcerhvdsrs dclvhldaqr
      361 vkaaaaemlg lnppgpadvi vdtsrlrrag ad
//
LOCUS       WP_175789477             871 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cenocepacia].
ACCESSION   WP_175789477
VERSION     WP_175789477.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 871)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 871)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 871)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 871)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 871)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 871)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 871)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..871
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..871
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=91816
     Region          35..871
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mkgpqhaaqp pagqsghdgr ahagrfglrd lihqaarmta rdwrageltl lvlalvlava
       61 altsvgflad rlrqglerda rqmlgadfvv radrpvdpsf drqaralglr tattaifpsm
      121 iaaaaggqpa daapsrlaav kavspgyplr gaveilpaga tvaqkaaaip apgtvwadpa
      181 lldalhlkag dtvrvglrtf tvaaaitrel drgfsfvnfs prlmmradel aatgltgygs
      241 rvtyrllvag daptiarfet yahqrvdggk lrgvgleslq egqpqvrqtl drarhfltlv
      301 alltallaav aiamaaqrym rrhldgcatm rclgvsrrtl galfalefvg vgivsgaaga
      361 vlgygghwal laalgslidv vlppptlwpa ligmgaalvl llgfalpplv pltrvppvrv
      421 lrrewgdasr tawaayaigv vlfaglliva agnlklgliv aggfagtlvg faliarlvlf
      481 aaaravrnar vaagvgwrya laslhrrgta salqitalal glmcllliai trndlvagwr
      541 qstppdapnq flidiqpdqr advaaylaah gvrdavpapm vrgrlvaing kpvnpdayps
      601 eearrlvdre fnlsyttelp sdnrivegdw fgtaatpqis ieaglaktln vkpgdtlrfd
      661 vtgltvdapi tsvrkldwgs frvnffvlmp ppvlkdfpav yltsfhllas naalldplia
      721 rypnltaidv apilaqlqrm mlqvvgavqf lfaftlaagv lvlytalags rdervreaal
      781 lralgasraq vnavqraefv mvgalagvla sagaiavgwv lasrvfdfql avdpwlvpag
      841 iaagvvcaga agwlslhnvl rrpalqslrd a
//
LOCUS       WP_175789499             421 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175789499
VERSION     WP_175789499.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..421
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=43597
     Region          205..412
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(212,252,290,393,396)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(212,393,396)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(212,252,290)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 msfrssfaaa vlgaavlvap lavsaapagw vaawatalqp ipdlaapppl yrapdvagrt
       61 vrqivyptvs graarirvsn aygraplvve aaslaragdg aalaggaavp vrfggkasvt
      121 lapgaelesd pvtigvtaaq pyaislqmgp dqrmtvwhrv snqfnyvsaq gdhvsdpgaa
      181 dfrtrftqya wvtelaveag sahasvaaig dsitdglrss vnrnrrwpda larrltasgv
      241 dsigvvnlgi sgnrllsdsa cygtslasrf erdalsrsgv kaaivligin dinfaamppr
      301 agldcdhpht qvtaaslidg yrrlieaahr qgvkvfgatl tpaalpagre airlevnrwi
      361 rggggfdgvv dfdavlrdpa rpsvlqrryd sgdgihpsda gytamagavp verlqaavgg
      421 k
//
LOCUS       WP_175789543             222 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            cenocepacia].
ACCESSION   WP_175789543
VERSION     WP_175789543.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..222
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23716
     Region          29..187
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpprhvqvpa ppgspaaqpa palrrrprqs raqassdalq qafvqlller gyakatirei
       61 aavagvsigt fyeyfgdkqs laalcihrrv laladrlrdt vqrlrgapra elavalvdlq
      121 vdaiaadaal wgalfalerq vsplaayrrh ydayvalwrd alaqaadppp aarldglarm
      181 ahticyggls qalltlgpal dfaaqrrelr avllaylaaa ga
//
LOCUS       WP_175789613             532 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia cenocepacia].
ACCESSION   WP_175789613
VERSION     WP_175789613.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..532
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58033
     Region          1..449
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mkssiqrnig pfalmltglg siigsgwlfg awkaakiagp aaicawiiga vvilaialty
       61 aelgamfpes ggmvryarys hgslvgfisa wanwiaivsv ipieaeasiq ymstwpypwa
      121 halfvngelq tlglllsavl vvvyfmlnyw gvkafarant aitifkflip gltilglmlt
      181 sfhsenlgva snasfapygw savltavats givfafngfq spvnlagear npsrsvpfav
      241 itsillalvi yvllqmayig svnpadvakg wahfnfsspf aelaialnln wlaillyvda
      301 fispsgtgtt ymatttrmiy amernntmpk mfgnvhpiyg vprqamwfnl lvsfvflfff
      361 rgwsslaavi svatvisylt gpislmalrr satdierpls iplmkliapf afvcaslily
      421 wakwpltgei illmivalpv yfyfqaksgw tgwgadlkaa wwlvaylptm avlsligske
      481 fggygylpyg wdmlivaais lvfyfwgvnt gyrtqylder eshdeilegi ga
//
LOCUS       WP_175789637             402 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein, partial [Burkholderia
            ambifaria].
ACCESSION   WP_175789637
VERSION     WP_175789637.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..>402
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
     Region          26..>391
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 malrptdsgs lrysdifdai nrglmqhgrl ltlrtplgdn vltpvrakgw skigrdyrwt
       61 vdavstrddi ellalmhqqv slliqqpaas fsnveyrpvh gfvhqirrlg adgalslyqi
      121 efasalfflg egrddyywld snavqsistv fdkypqlrgy yrfnlstqps trtytrqses
      181 dlnfvqrlle degwyfyweh apvkdneppk tmlvivdsvs alpeahdvty srsnagdeid
      241 gltqwvmqqt aqptefksts fdqdrpgssf aagslmeatt ytvqhyrdke tlsvpgvpat
      301 vyepttlgyp dadsgarraq irtqaweama rrfigvggvr wldagsrfvl ndhprhdapg
      361 skdreflave mhwfilnnvp farqseafpf slqpefdrvq ae
//
LOCUS       WP_175789651             266 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia ambifaria].
ACCESSION   WP_175789651
VERSION     WP_175789651.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..266
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28735
     Region          14..261
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mvsaavleps vvtaprgari dirrvshafd gpggplpvld dvtlsvaage fvallgpsgc
       61 gkstllrlva gldaarqgti aqdgapierp dpsrivvfqd ptlypwrrvr anvalglear
      121 gvartaqhrv ddalarvglq efsnvfphql sggmaqrval aralvndprl lildeplgkl
      181 dsltrltmqa eltalwqrdg fsallvthdv eealflaqrv ivfgprpari vaelrvdlpy
      241 prhrgdprla elrhealrhl gldasw
//
LOCUS       WP_175789719             541 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia ambifaria].
ACCESSION   WP_175789719
VERSION     WP_175789719.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..541
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57750
     Region          19..463
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpgqgnthps vplsrsvpad gghgkfkkql sltdltfigl gaifgsgwlf aashvstiag
       61 pagifswllg gfsvlllgiv ycelgaalpr aggvvrypvf shgpllgylm gfitliafss
      121 liaievvaar qyaaawfpgl tkagssdptt lgwlvqagll cfffylnyss vktfakannv
      181 isifkfivpl sviavlftff kpanltlhgf apfgmpgiem avsaggiifa ylgltpivsv
      241 asevrnpqrt ipialilsiv lstliyvllq lafigsiptd mlaagwhdvs kafslpyrdi
      301 alalgvgwla vmvvadamis psgcgniymn atprvvygwa ktgtffkvft rvdeasgipr
      361 aglwltfgls ifwtmpfpsw ealinivsaa lvlsyavapv svaalrrtap dlprpfrava
      421 fgitgpasfv iaalivywsg wstvswllgl qivmfviyla crrwvptahl siaeqvrssa
      481 wliafyaami vlsyfggfgg tgklahpydt vvvaavalvi fywgantgir sdklqledde
      541 d
//
LOCUS       WP_175789722             295 aa            linear   BCT 11-JAN-2025
DEFINITION  SH3 domain-containing protein [Burkholderia ambifaria].
ACCESSION   WP_175789722
VERSION     WP_175789722.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..295
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30471
     Region          7..96
                     /region_name="YraI"
                     /note="Uncharacterized conserved protein YraI [Function
                     unknown]; COG4991"
                     /db_xref="CDD:444015"
ORIGIN      
        1 msntiirslc vvlfgiaavp gvadaqssay tnsgaelfag papdypvvaq lppgtavdvf
       61 gclsdyswcd valpgvrgwi daqqldypyq gnyvplleyg aiigvpvtgf aigaywdryy
      121 rhrpwfqdrd rwehraeprv gpggmppayy grpqpgwpaq reprgappvq hdarpsatrg
      181 gwngpnrapa pqvapapara papmpapapm papapmpapa pmpapapmpg aagvrqpapp
      241 paqpaqpaps ggavqmmppa hqggggyggr pqgggdgggn hgggggrgrs defrr
//
LOCUS       WP_175789728             240 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia ambifaria].
ACCESSION   WP_175789728
VERSION     WP_175789728.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..240
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26626
     Region          6..210
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mtmptltlis hplcpfvqra aivllekqvp fqrinvdlsd kpawfleisp tgkvpvlqvq
       61 eaggsnevlf esvaiceylq ethsgpslyp ddplerakhr awiefgsatl aeawgylnan
      121 dhvtanvkat llkdklaqle kvlglgpyfd getfgmvdav fapvfryfdv lqtdsgpspf
      181 pdfpkvdawr erlrvrasvi aavsadypal frahlrrqka llmeeiygas qpypatshkl
//
LOCUS       WP_175789766             508 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Burkholderia ambifaria].
ACCESSION   WP_175789766
VERSION     WP_175789766.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..508
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53669
     Region          16..491
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(72,74,78,81,85,118,121..122,131..138,143,146,149,
                     242,246,249,252,254,427,429..430,432..433,436,439..440,
                     442,444..447,456,460,462,476,483..488,490..491)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(158..161,169,184,187,217,234..237,240,258..260,292,
                     392,394,420)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(161,258,289,292)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnaavpqttl alptakllid gafvdsqsae wgdivnpatq evigrvpyat ldevdaaias
       61 aqrafqtwkt tpigarlrim lkfqdlvrrn leriahtlta eqgktlpdaq gdifrglevv
      121 ehacsigtlq qgefaenvag gvdtytlrqp igvcagitpf nfpamiplwm fpmaivcgnt
      181 fvlkpseqdp lstmqlvela ieagvpqgvl nvvhggktvv drlcthpdik aisfvgstrv
      241 gthvynlgsq hgkrvqsmmg aknhavvlpd ahreqainal vgagfgaagq rcmatsvvvl
      301 vgrardwlpd lvekanalkv nagaeagtdv gpvvskaaka rvlslidagv kegatllldg
      361 rdvkvpgyeq gnfvgptifs gvttdmsiyq eeifgpvvvv leadtlddai alvnanpmgn
      421 gvglftqsga aarkfqseid vgqvginipi pvpvpyfsft gsrgsklgdl gpygkqvvqf
      481 ytqtktvtar wfdddatagg vnttialr
//
LOCUS       WP_175789777             472 aa            linear   BCT 11-JAN-2025
DEFINITION  CpaF family protein [Burkholderia ambifaria].
ACCESSION   WP_175789777
VERSION     WP_175789777.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..472
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51127
     Region          81..461
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mtfgtrkrsa pepapavspa aprddppapa papiashaps plrgaaaadt qealirsgkf
       61 dairtavfss mnmsaalmkt rdevragieq vaahtverer lkitageqvl ivdailndmf
      121 gvgpieplla ddtvsdilvn gpdqvyvera grleltslkf rdnahvtsva qriaaavgrr
      181 vdesspmvda rladgsrvnv vlppiamrga sisirkfakr ditlarmahq gnishgmlqv
      241 lkiacacrln ivisggtgsg kttllnalsq hieeherivt iedaaelqll qphvvsletr
      301 penteglggi sqrdlvrnal rmrpdriilg eirgaeafdv lqamntghdg smttihantp
      361 rdaisrlesm vmmananlql lsirrqiasa vhlfvqierm rdgvrrvtri teivgmegev
      421 vitqdlftfr qesdttrdvv kgvfeasslr pafapraayy gmedalsevf rq
//
LOCUS       WP_175789790             140 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia ambifaria].
ACCESSION   WP_175789790
VERSION     WP_175789790.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 140)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..140
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15540
     Region          20..136
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04667"
                     /db_xref="CDD:467552"
ORIGIN      
        1 mpqaplstkp peasavpike rativcyrde qvllvarats rwalpggtik rgetpleaah
       61 relqeetgit gqhlvysmqf tglakvhhvf faevgpdqtp qasneiqkck wfridsvdgv
      121 rasiptkriv elvyrhellk
//
LOCUS       WP_175789853             119 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia ambifaria].
ACCESSION   WP_175789853
VERSION     WP_175789853.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..119
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=12494
     Region          33..>117
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mhvrvmvcra avataltvla asaaaqerqa epalssmpaa aptkaqkaad rqlrkrvara
       61 lgrakrldas rllifvrgdv vtlsgdvads eqsalaiata qrvpgvgdvr nqlrirtrn
//
LOCUS       WP_175789955             261 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Burkholderia ambifaria].
ACCESSION   WP_175789955
VERSION     WP_175789955.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..261
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=29233
     Region          2..220
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mnvlivyahp eprslngalr dfavehleaa ghavqvtdly amnwksafaa ddvtdrapda
       61 rfdpaldskr afetgtqrdd iareqdklkw adavilqfpl wwfsmpaimk gwvervyayg
      121 faygvgehsd qhwgdrygeg slagkramvi vttggweshy sargingpid dvlfpiqhgi
      181 lyypgfdvlp pfviyrtgrm ndvrfdetra algkrldelw tarpipfrrq nagdyeipal
      241 tlkagiapek vgfaahlahe q
//
LOCUS       WP_175789949             779 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175789949
VERSION     WP_175789949.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 779)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 779)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..779
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..779
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=86184
     Region          1..755
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msmilpsqay elklaphpap tsvlrftgrd avselyrydi eftspvvgip mdqvigrpak
       61 fivapvdpnm dylrrmfgen teqfskmppt ytihgvitef deldtsadqt hyrvrlepkl
      121 adlnrgvtsr lfqkqsieei vtdtlrhygy ragvdfqfql rgqykrceyv tqyhettfsf
      181 iqricaeegl wfrweqqkdy avlvfgddld ayarkqrtvs hrrdsgless gmdaiktlek
      241 rtrrvpeavr lhdynhreag vsllveenaa rddkttsgid yqwgehyetp eegksvarrr
      301 heeyltnqit fsgtgntfwl eagevmrlap hpvdakhgif itavesqggr dqsywvtfeg
      361 ipsdrvwrtp vasieqpvid gilparitsp gdykyaylte qgwyviklpf dldewspggt
      421 srpvrfakpy sgdnyghhfp lidgaevavv ftqgdpdrpv iigamhdslh pdlvtsqnht
      481 rnlirtaaqn elrmedkegv ehvhlttpfe aselnlghmv dgdrkdrgrg velrtdgpaa
      541 vrgskgvlvt aegqpgaagq qldmqdadtt leqaeqilna lndsanaaka lqadidqqrv
      601 liqqklkqlq kpvivatapd gvgivsgqqm qlaarkqmfv tagdgldigv mkriavaage
      661 aislfaaklg irifakkgkv qvqaqsdame lmsmqdmavs ssdgeviitg rkgvtlgdgs
      721 gayiklsggk iilgspagei eakgnltidd pdggsfkfpt waaapvsdvq tatnfgfse
//
LOCUS       WP_175789876             665 aa            linear   BCT 11-JAN-2025
DEFINITION  AI-2E family transporter [Burkholderia ambifaria].
ACCESSION   WP_175789876
VERSION     WP_175789876.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 665)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..665
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=70761
     Region          27..378
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mfdfkesrpa rpsarikppe tpgveglitl avgvtvvaal yfareilipv tlaillsflv
       61 aplanllgri rlghvvsvll avtmslsviv vigaviaaqi tdlavdipry qasidkkida
      121 vhgltvekln rlasaagqal qratvdppka iresasssag sqppmalpve vrepaqtpfq
      181 larrilspvv spletafivf ivtivillqr ddlrdrtirl fgsrdlhrtt tamdeaarrl
      241 sryfvsqlgv nagvgivigi glsiigvpgp vlwgilaall rlvpyvgiwi sailatalaa
      301 avspewsmai wslvlflive llvgqvvepl lyghstglsp fsvvvaaifw swiwgpigli
      361 lstpltlcll vlgrhvtrle fldvllgdqp altpvenfyq ralagdpdda ieqarillrd
      421 rplssyydei vlkglqlaad dvsrggvspa qlariettvn diieglegfa dtdpgtnaaa
      481 gnrgalapaa ggqkvscepa phavspsieg ppvpragkqi lciagrgpld elasamlvql
      541 lgkhdldcrv vshdaasrvr iggldvtevt vvcifylgid gipshlryll rrvrqrlpda
      601 livvglwpag dtdqwskdlq saigadhyat sirdmvkacl vstgtasalg pepqldgrcs
      661 vrgmq
//
LOCUS       WP_175789856             415 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175789856
VERSION     WP_175789856.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454559
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..415
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44578
     Region          53..381
                     /region_name="MelB"
                     /note="Na+/melibiose symporter or related transporter
                     [Carbohydrate transport and metabolism]; COG2211"
                     /db_xref="CDD:441813"
ORIGIN      
        1 mdelvlaapg rrsrghlgit ltlafigvwl alipypmmil pmlaeriapl dkanvlaqai
       61 gvgaivgsia qpifgllsdh trarwgmrkp wifggavagm gamailatag spaqlalgwa
      121 lmalsfnatl sglnailpdq vpparlgffs sivgftppig illgvwivrq lapdlvfvam
      181 lqgaiaftai tcfvvfandr rleeghfkrl qwkrlaacfw tnpvkhpdfa iawlsralvl
      241 fgvsclqhyl mfylrdrigl sqqetphamf mcllvataam tvsallfgrl sdrlqrrkvf
      301 vfvagvgmaf gllallactt laqllgvivw iglaqgayla vdlalvtevl pdpdtaakdm
      361 gvfhlanvlp qfvlslfvtw ltlpggairy dtlfvtasca talgalviif ikavr
//
LOCUS       WP_175789979             206 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            ambifaria].
ACCESSION   WP_175789979
VERSION     WP_175789979.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22666
     Region          12..169
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpmttddpgr rarkriqmla hlaatgarlf dahgydavtm eqiaaqadva krtlynhfpt
       61 keavlahwle gelardlahl erdvarrksf asriacvlda saawceqhpv yllaylrhrf
      121 lsigavsaeg gmengsdial vwqqliaagq qagelnpala adqlatwfhh lylaamlrwl
      181 tvpglslkre fqsvaklfve gaqakp
//
LOCUS       WP_175790004             743 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia ambifaria].
ACCESSION   WP_175790004
VERSION     WP_175790004.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..743
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79813
     Region          50..743
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mtvnrttaap arrrrakvgv gvglgitlfa ahaaaaqgda papeadaavs atlpaievsg
       61 erggafrare asvaglddap lrdtpasvsv vtraqlddqq akrlsdvvrn dasvvndyap
      121 vgyfegfair gfpvdlasai ridgltvsge qnvplenker veilkglagi dsgvvapggv
      181 infvtkrsan vasvttgvds rgstsaavdl grrfgpdrqf gfrinaaken mhsyidgtng
      241 rrtfgsiaad wdistraslq fnaefqqwiq rsapgyqllg gtvvpsvntt skalgtqpwa
      301 kpvttdalnl narfdyrfnd dwnayiaagr srtmiddnsa faygcyyaps caagatspff
      361 fgangdydvy dfrspgeyrr nddlravttg kfatgplrhe ltlgvsvqrr vvhmasavyd
      421 yvgseniygp dvafapssnt agpsypqlds wqygvfgldr isigehwqvl aggkevllrq
      481 rswssldgda thtdrsvflp qvalvykpvn vlslyasysk alslgdqapl ratnayaflp
      541 pveshqfelg akydwldrls ltaavfsisk pfqfadpdas gtsytfvqrg tqrhqgielg
      601 aagrvterls ltasvaaira raydsgspay eghqiinvpa lraslyadya vpgvaglnml
      661 ggveysggrn aneegtarvp swfvfnlgar yttkigghrt vlrvsvdnlf nkfywrdage
      721 qqgdaylfpg aprtarvslt ydf
//
LOCUS       WP_175790016             190 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Burkholderia ambifaria].
ACCESSION   WP_175790016
VERSION     WP_175790016.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..190
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19814
     Region          15..169
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 msteprtdse rridivalcg slraqsynaa lldaaarvap hgmritrfdr lgefplfnpd
       61 aehpspaavr dlierlnaad gvliaspeya hgvtgvmkna ldwvvgceav vdkpvavlna
      121 sprathadaa lretlsvmsa civerasial pilgsqldaa giaahppfas altdalhalr
      181 aaidaqapgr
//
LOCUS       WP_175790051             517 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Burkholderia ambifaria].
ACCESSION   WP_175790051
VERSION     WP_175790051.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 517)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 517)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 517)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..517
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=56631
     Region          <55..>204
                     /region_name="PRK13560"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:106506"
     Region          148..513
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mraahagaml dirprdaarl hpnpimsfpd eddfhrllda lttcvllhda qtraivwanr
       61 aacialgfsv eellplkaqd mtrpepkyrr eiavsawdra lvdgpqvyew cyrsrtgvdm
      121 lseatatyvp lrgrdvvmvq frdisaeeav rqqlrryear lrefmqdlde giavvtphgr
      181 vqfisesgrr vlglapdeal gevldycsaa drdrlvaqlr dapsacpsep qryrivrrdg
      241 stcwlrilcr qveiegdldg llvqfrdvsd evaiedarra earmleyagr ynamgemasv
      301 iahelsqpla avrnfiegav rrlnargavd daiwglrsad rqaehaalii ksvrefivkr
      361 epavaladlr eiladvayfi elrakeagvt vaivqadapl pircervlig qvvlnlafna
      421 ieafagcert prtltlgtan vdgqaelrai dngpgvaega hdrlfdgfss skaggngigl
      481 slcksivtrh gghigaspae gggldcrvtl pladaqa
//
LOCUS       WP_175790054             210 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator transcription factor [Burkholderia ambifaria].
ACCESSION   WP_175790054
VERSION     WP_175790054.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..210
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22879
     Region          7..199
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mtspapivyi vdddsgmrts lawllesvgi asegfanaad flarfdvnlp aclvldvrmp
       61 eksgfdvqae lnargatlpv ifvsghgdip msvralqnga idfvekpyns qqmlervqra
      121 lrlaqqrhav drhhrelrqr ldaltareke vlrgvvdgkg skqiasdlsi svktvdvhra
      181 sikeklgats iaalvrdvmv vwggnnetpr
//
LOCUS       WP_175790064             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175790064
VERSION     WP_175790064.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47142
     Region          23..422
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,154,
                     157..158,161,256,259..260,263..265,268,295,299,349..350,
                     354,358,374,377..378,381..382,385)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnatetldpa sadeqrvmsk iarrllpilv vmfliafidr qnvgfaklqm vhslgmteaa
       61 fglasslffi gyllfevpst lalhrygarv wlarimltwg litvlmgftt smpafcslrf
      121 llgiaeagfy pgviyyltlw fpqsyrakvl giftlgsala nmlgslvggv llslngvwgl
      181 agwqwvfvat gipavivaiv vfrvlpasfr easflderek qivaaalere kpaqaehgqp
      241 wkalldprvm vfaatymlms tslygvtywl ptlvksfgvs sstngflsml pwalavvllv
      301 wlpsklrrvk silrtiaiva algalgflls lvlpstplrf ialvlggaci pllypcfwsm
      361 ppryftgara aasvaainsi gnlggffsqn lmpfagkvtg tafgpmivpi vclallgiga
      421 lvawtrserg mvavra
//
LOCUS       WP_175790137             922 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175790137
VERSION     WP_175790137.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 922)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 922)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..922
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=99159
     Region          37..818
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msiaktlrnf asglidgnpr pvdlhfgraq ravghllalh hadiheglms giegqltcvs
       61 thdhlspalf lglpvsvrvt tdrggvrain aivrevrtgq sdgeltvyql qvcdalslme
      121 grtnarvfrs rsvteilvtl mnewkqrsya larafdfdls glqadrypvr eltrqvnesd
      181 arfirrllrr egitvfakae pvgrvhgmad eppvhtlvfc ddphclketp agalrlhprd
      241 agaaqrdtvt lfahrqrlss gkvrrpswdy ktariddsta vaslhqgesg ndlahlltdv
      301 aidiphvgds wndhdritrd rilahqfeae rydgisnvrd lpvghwftlt gdpeldmrpv
      361 ehrrfvvtsv rhdirnnlpt qlasraqglf aasrnltqta ppttadpseq tdtryenrft
      421 cvrrgvplkp aydpkidvpp vhlltgtivg mqgeevfcds agrvrvrihg ydpadhahaq
      481 gagtngragd sapirvganl aggnfgtlfl prvgmevllg clagdpdrlv iigvlsngan
      541 ppatfshtga lpgnrflsgi ktkeingrry nqlrlddtps qisaqlaseh ahtelnlgyl
      601 thprenghge argegaelrt daaaalraar gillstyart ratgdqldrd elirlldqct
      661 elfkslgdya gqhggqaadt sgqdnvasaf rnwtpggapa gaaddasall afgaqsgalh
      721 vtpkthviha genidqvaqq hvqvtsgeri nlhagrgvam fahgdgvsai anqgkvtiqs
      781 qnddtrvdsa kniqltaagg klvgtasdev vlitsggayl rlrggdielg cpgtftvksa
      841 ghawdgpasm nadmptfaqd tlgrvpklvr atdghaaagf egeiqkpsgp vsnvssdvag
      901 qlpavdadqf erlavrfikk ni
//
LOCUS       WP_175790151             325 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175790151
VERSION     WP_175790151.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..325
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34187
     Region          6..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..302
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 medidlnlvt aldmlltegs vtgaarrlgl stsamsrtlt rlrtatgdpl lvragrklvp
       61 tphaaalrdr vhavavdara vlrpatadid mttlsstfti raaasfmdml agpvvaaigd
      121 iapgvrvrfv akpdrdpapl rdgtvdleig krgddapelh trelfhdghv avaraghplf
      181 aaaritpary aacrhviaaq lgdfggptnd aadtsavaht vqvvvpgypd amrvaagtdl
      241 ialvprsslg naftpglvda lglrsfaipv rlpeilisal whprmhgdpv hrrlrdavid
      301 vcrraypaar aprapahgtk prgvg
//
LOCUS       WP_175790165             587 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia ambifaria].
ACCESSION   WP_175790165
VERSION     WP_175790165.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..587
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62366
     Region          470..572
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(473..474,507..508,511,515..516,519,562,566)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mlptaatrad snaaraalsg lgypvrtvvt lsaalalavv gwvvpvergv mwgwvalvva
       61 lsalivwlhs rgltrareqn vqviaqlgaa tadlpvtlrt rmplalvtgd glsalfdrdt
      121 amsrfvhvgd gaiwlradrp qdlprlavav rqwrdghapd cvvlavapav handdtlsqs
      181 lrvirqavad asrmlgtslp gyvalyqrls nanaaatlpa vesaarwygm stgsaiadth
      241 rfdtaieaae sdalhaggsp avaaraagva smigwtrrvv fdtltdrrqp aspwplfgag
      301 widhgpasap gkpwerevrs ltgiapatlp asptpwplpq plidamprrt wrspritaaa
      361 hviaivacaa iaaicgaakn nevlmtrigk hlqhynripa thdtakrdal rvlasdrdql
      421 dryarvgvpl rlsfgtyrga pllpvlndai asyepppppp avvtldsmsl fdsgkatlrt
      481 gttramveal elikahpgkr vlvagyaddq grpdrnlkls idrasavrdw lveasgippt
      541 rfaiqgygdt rpvadnatpe graknrrvei tlvpdtpvpa vptgaar
//
LOCUS       WP_175790168             240 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD family hydrolase [Burkholderia ambifaria].
ACCESSION   WP_175790168
VERSION     WP_175790168.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..240
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26170
     Region          6..233
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mhltnvsais fdlddtlwpf gpsveraeas lhawllahap dtarvlptsq alnqlrdeye
       61 rlrpdlvgdy ralrigsirl aleranedvt ltdraydvfy aarnrveffd dalpalawls
      121 arfpliavtn gnadlrltgg geffrdtlsa rafgfakpep eifhaaaatl gvpagellhv
      181 gddyhldvvg alnaglqaaw vvrdthpdge hvrqrapsah ltlrdlsmlc ralggpgevl
//
LOCUS       WP_175790178             236 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia ambifaria].
ACCESSION   WP_175790178
VERSION     WP_175790178.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..236
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=24384
     Region          60..224
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mttaqtaasa asagaaaaaa aataasapna asaapasasa asaaapaave rplvrfqqkp
       61 lsvningksv gpmqvpeglm mieflheyag ltgsrlgcgq gvchacvviv dqpdgtseem
      121 rtcitgahff hgrsirtieg hakrndagev velspiqqkf lehfsfqcgy ctpgfvnaat
      181 vlierlkrep iakadverti tdalnahlcr ctgyvryyaa vkdvilttpg lvkdaa
//
LOCUS       WP_175790192             676 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia ambifaria].
ACCESSION   WP_175790192
VERSION     WP_175790192.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 676)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..676
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=72514
     Region          26..665
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mlfaavaqaq aadtpasptp tqttplapif vtanplgdsq liaptaqlsg daltrrqads
       61 lgetlnglpg vstttygpmv grpiirgmdg drirllqngv aaydasslsy dhavpedpls
      121 ierveivrgp aallyggnav ggvvntidnr ipreaiegvt galdarygga nsvragaaqv
      181 eggngrfafh vdafdreask lripgyarsg aqraidgpdt pqpygnvpns dgrvhggaag
      241 asytwadgfa glsysgyesn ygsvaeddvr lrmrqerlaf asevrnlsgp ftklkfdfay
      301 tdyrhkevdn getattfrnr gyeariearh rrigpfegai gvqfgrntfs algdellvps
      361 trtnsvalfg leewqvdpal kvslggrfeh vkvdpdpagv ekfagaqprd fnagsvsaga
      421 lfsltpvwsv aanvaytera ptfyelysng phdatgqfli gnpnaskeka vstdlslrya
      481 sgpnrgsvgv fynrfsnylt eyntgrvvdd dgeavapgad gslneaiyrg vraefygvel
      541 dgkwrafsrr ghtvdlelta dytharnvdt gqplpriapl ratlaadygy gpfgaraqvt
      601 hawsqhrvpd ndfstdgyts lgvmltykfr vgathwltyl rgdnltnqei ryatsvvrgf
      661 apqggrsvma glrttf
//
LOCUS       WP_175790241             288 aa            linear   BCT 11-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Burkholderia
            ambifaria].
ACCESSION   WP_175790241
VERSION     WP_175790241.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..288
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=30117
     Region          182..279
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mslsllpcat iclalfaaaa fawlrplhga siavaalgya galavgklsp ivlaplallv
       61 aaawgvapsr plavriaahv vfaalaials lhlipgfhnp rvieptrftp davpftmyln
      121 fdkplvglwl lwvlpwvmpd vplaralrtg viaciptaav clvgalafgm vgwapkwpas
      181 gwmwlvnnvl lvtlaeealf rgyvqggltr vlgrfgwgpw valaigallf gaahaaagwh
      241 wivlgtvagi gyglawrrgg llasalahag lnvihfglft ypmlaaar
//
LOCUS       WP_175790274             676 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia ambifaria].
ACCESSION   WP_175790274
VERSION     WP_175790274.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..676
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=70917
     Region          30..671
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mkfafpslpp favvrtalrd awpilppgal gfalrntaas llalyiafrm nlddpkwaas
       61 tvwivaqgtr gmglsksqyr ilgtaigaav alaltgafaq tpelfltala awiglcagva
      121 tflrnfraya avlagytaai vamdaasapl hafdiatarf lyvmvgilca aafetvfapg
      181 splrdvrtrl arylgravav gaaalrrepn aaavhrlfae aldldtaaey aaagappvrn
      241 aighlraaal gvlsahaaaq aieahaarsg dapdplvaea arvldgvaas geagpemavl
      301 rarvdqalha eaaeptgsdd srlltldrls tllagfddaf ankarvdlpa pppsrvryaf
      361 hrdavlachn girafiavla asaiwivtaw psgagfvait avvgalfstr pnsaraaigf
      421 lkgtacaava givcnfillp avsgfetlay iigvfmigtg lamrhprtaa lgsafaiffw
      481 nftspdntar igdaaflnsa lstllgiafg vlvfalvfpg dpgtsrrrlh ravrrdlaai
      541 arnprgwsas awlsrtadrl grelgfagrl pqtlierdmr dllaiwgigd sllslaelaa
      601 qepaarravg vvrgraalad farlerscdm aarllrrrva dvdsdgaral lrgivllrri
      661 adavaghghf lrgrrd
//
LOCUS       WP_175790284             183 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia ambifaria].
ACCESSION   WP_175790284
VERSION     WP_175790284.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..183
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=18441
     Region          9..183
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mriikrsaip fllvaagaaf ssaahaadgs vtfrgniias tcsvdggsdl tvplppvstt
       61 aladvgsvag rsafslaltg ctvgddnpvk vgvvfengtn vdqssgrlti dsgaksaegv
      121 qinvldsqqn hipvgaqtga ntemvaidad gkakvnyfae yyaagavkag dvssrveysl
      181 iyq
//
LOCUS       WP_175790297             252 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia ambifaria].
ACCESSION   WP_175790297
VERSION     WP_175790297.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..252
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26310
     Region          1..245
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 msaskkfaai tgagsgigra aaialanagf tvaligrnea slletketia aghgdayall
       61 advtdeasve hafsriaref grldvlfnna grnapavpld eyeldvwndv vatnltgvfl
      121 caraawrlmk tqtpqggrii nngsisaytp rpntiaytat khavagitks laldgrayni
      181 acsqidigna atsltdrmtd gvlqadgrma pearmdvthv anavvqmasl pldtnilnmt
      241 imattmpfvg rg
//
LOCUS       WP_175790326             292 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia ambifaria].
ACCESSION   WP_175790326
VERSION     WP_175790326.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..292
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31785
     Region          35..275
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 mtglqqdhqd hrdapdstaa rvalwralhv eldapphvla devglrllap apgwqqrgdm
       61 dpqftrpfra sivararfie dlvidqaaqg vsqyvilgag ldsfvqrrpe masrltvfev
      121 dppapqawkr rrltelgfgv pdwlrfvpvd feaqqswrda lvgagfdagk pavvvstgvs
      181 myltreanaa slrevaslap gstfamtfll plehadpdvr pglemaakga rasgtpfisf
      241 fmpaeirala tqagfaraeh vsaaeltrry fadrpdglrp pnnaeellva tv
//
LOCUS       WP_175790300             327 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH:quinone reductase [Burkholderia ambifaria].
ACCESSION   WP_175790300
VERSION     WP_175790300.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169595
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..327
                     /product="NADPH:quinone reductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34276
     Region          1..325
                     /region_name="zeta_crystallin"
                     /note="Zeta-crystallin with NADP-dependent quinone
                     reductase activity (QOR); cd08253"
                     /db_xref="CDD:176215"
     Site            order(42,46,128,132,151..157,176..177,196..197,220..221,
                     225,242,245,250,268..270,314,318..319)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176215"
ORIGIN      
        1 mkaafyerqg aardvlivge lpmpepapde vrvrihvsgl nptdvkartg fsapmpyprv
       61 iphqdgagvi davgmnvspd rlgervwiye aqhgratgta aefvvipssh avhlpdnvsf
      121 dvgaalgipa ltahrclfsd gslkgqrvlv hggagvvgta aillakwaga wvsatvmnae
      181 qatvakanga dlvidrkadn vadhvleata glgidrvvdv dlrsnlnvnl allsqggvis
      241 ayamasasde lavpllkamm hgcvlrfvyi yrvpieakqa aigdinacle agaysprigl
      301 kvpldqiaya hetlesgqvi gkvlvhn
//
LOCUS       WP_175790334             466 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175790334
VERSION     WP_175790334.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..466
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49493
     Region          42..449
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(51..52,55..56,59,91,141..142,144..146,149,169,
                     172..173,176,284,287..288,291..293,296,324,328,379..380,
                     384,388,404,407..408,411..412,415)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mstfdnvvag ratmeaaast pgaiiarler lpanamqira rvligtatff dgfdvitiaa
       61 tlpllihkwg lsptqigmli asgaigqlig aflfpalaek hgrvkaiaws savigitsia
      121 cgfaptfeif vllrilqglg lggelpvaat yineitrahg rgrfvllyei vfpigllvsm
      181 algawlvprf gweimyfvgg lplilalvlt rlvpesprwl asrgrlaeag ravgvfeasv
      241 rgelppatqa aafdemvrqh pkrrmsdlfs aayrkrtlav atlwatcgfi qyglstwlpt
      301 iyknfyhapl qlalnlavig svmgvlgsla sallvdklgr kpvivwsfvl calslalagv
      361 yhassvyvva ifcslslglm asgfitayvy tpeqyptsir asgcglgsaw lkiasfaapm
      421 ivphaiiggn lapafyligi vpliaaltvh fvgietkgkv lealea
//
LOCUS       WP_175790350            1057 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia ambifaria].
ACCESSION   WP_175790350
VERSION     WP_175790350.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..1057
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113329
     Region          1..1038
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mdfsrffidr pifavvlsiv ifaiglisip mlpageypev vppsvvvrat ypganpkeia
       61 esvaepleea ingvegimym ksvagsdgsl qvvvtflqgv dpdtaavrvq nrvsqalsrl
      121 pdevrqygvt tqkqsptplm yvslyspdns rdslylrnyl tlhvkdelsr ltgigdvgvy
      181 gsgdyamrlw ldpnrlasrg laasdviaav reqnvqvsag qlgaepspnk ndflmsinvr
      241 grlrtvqefg divlrngddg qvvklsdvar ielgagdytl rsyfndkhsa vvgiflspga
      301 nalevakavy akldelskrf ppgiayrpvw dptvfvresi ravqhtliea vvlvvlvvil
      361 flqtwrasii plvavpvsvv gtfawlyllg ysintltlfg lvlaigivvd daivvvenve
      421 rniarglspr daahqamrev sgpivaialv lcavfvpmaf msgvtgqfyk qfavtiaist
      481 visainsltl spalaakllr phgapkdalt raldrafgwl fhpfnrffer ssdryhgvvg
      541 rtlkrrgmvf avyaallaat allfnavpgg fipvqdklyl fagaklpega slartsavte
      601 qmtkialgtd gvemvpafag lnalqgvntp nvtnsyvilk pfdqrhrsaa qinadlnarf
      661 aairggitya lmpppiqglg ngsgyslyle drgglgygal qnalsafqaa vaktpgmsyp
      721 vsayqanipq levkvdrlka kaqgvaltdl fntlqvylgs myvndfnafg rvyrvmaqad
      781 sghrqtaadi anlrtrnakg emvpigsmvt vapaygpdpv vryngypaad ligdadpkvm
      841 sssqaiaklq qiakdvlppg itlewtdlsy qqvtqsnaai vvfplavmlv flvlaslyes
      901 wtlplavili vpvcmcaalf gvwlsggdnn vfvqvglvvl mglacknail ivefarelei
      961 qgkgvieaal eacklrlrpi vmtsvafiag svplligsga gsevraatgv tvfagmlgvt
     1021 lfglfltpvf yvairklagg tpavwseqha tlegenr
//
LOCUS       WP_175790383             486 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175790383
VERSION     WP_175790383.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..486
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49957
     Region          31..475
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,156,
                     159..160,163,293,296..297,300..302,305,333,337,390..391,
                     395,399,415,418..419,422..423,426)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msentlapct pagaaaaasp rshhgwalvv llvgailppl dyfivnlalp airdglgarp
       61 aelqlvvsay acanavvqit ggrlgdlygr krmfmvgmag fvvasalcgl agsgavlvgg
      121 rvlqglfaai lapqvlatir svfspqeqvr vmgfygfvfg laavigqlgg galislhpfg
      181 lgwraiflvn vpigilallg swrfipesrp prgqridvpg tvllslfllm lvyplthgre
      241 agwplwmvac ivgalpmlga llavearrla ggrdalldvr llrnpvvalg ltlaflfyml
      301 safflsygiy lqgclnwspl asglailplg igflaspllm prlvarfggy rvltlgfall
      361 tagvataaal agehapgagf yagiaaigvg qglvlpsvvr ivlaevdaah agvasgmvta
      421 mlqigaavga atlgglffar lgaqpgaldy vhgfrtamwa ltvvllgcva lsaalgpmhr
      481 rahagv
//
LOCUS       WP_175790400             337 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia ambifaria].
ACCESSION   WP_175790400
VERSION     WP_175790400.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..337
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34419
     Region          23..337
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mnlpessstp sttlaaaagn gdapppramw tqlrrstlfy plvglivvci ammiaspsfl
       61 saanlenvlr qvsinaiiav gmtcviltgg idlsvgsvma lsgtraaglm vagvnavaal
      121 aigiavgfgf gflngvfvaf agmppiivtl atmgiargla liytggypid glpdwvaffg
      181 sgkvlgiqap vlimlivyai awllldrmpf gryvyaiggn eqatrltgvr varvklivyt
      241 lagltsalaa ivltgrlmsg qpnagvgfel daiaavvmgg tsisggrgai lgtlvgalll
      301 gvlnnglnmi gvnpyvqnvi kggiillaiy isrersr
//
LOCUS       WP_175790451             567 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia ambifaria].
ACCESSION   WP_175790451
VERSION     WP_175790451.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..567
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=62281
     Region          17..552
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 msageinear atrsvgefdy ivvgagtagc avanrlsedd dvsvllieag gkdnyhwihi
       61 pvgylycign prtdwryktr deaglngral syprgrvlgg cssingmiym rgqredydew
      121 arvtgdsswq wdsvletfkk sedyhggasd vhgaggpwrv ekqrlkwdil etfaqaaeqt
      181 gipatddfnr gdntgvgyfd vnqkhgirwn askgylrpvs trgnltiltn aqtrrllfen
      241 rrcagiefrl gdepriakak revilcagav nspqllelsg igsaehlakl gievvqdlcg
      301 vgenlqdhlq lrmafkvegv rtlntlsahw wgklmigley glfrsgpmam apsqlgvfak
      361 sdpndktltr pdvqyhvqpl slerfgeplh pfdaftasvc qlrpssrgsv hitsndplma
      421 psiapnylst eedrhvaana lrltrrivaa palerfrpqe ilpgiqfqte eelqyaagnv
      481 gttifhpvgt crmgraddpg svvdsrlrvr gvsglrvvda svmptitsgn tnsptlmiae
      541 rasemiradr kregrlaeti rggvlst
//
LOCUS       WP_175790492             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175790492
VERSION     WP_175790492.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33441
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,219..224,
                     230..231,233..234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mklsfevlea ldaidragtf aeaavlihrv psalsylvqk aesdlgvilf drsgrraqlt
       61 eagrllvedg rrllqagrel enkvrgvhag weaelrlcld eilplpslwp hvrafydmem
      121 ttrlrlstev lggvwdalvt gradiaigaa gepphapnia arpigllrhv fvvaphhpla
      181 aveqpldsdt isshrgvvis dtsraleprs vaihdgqsvi ivptlaakld llcegmavgm
      241 lpapvveepi rqgklverrv igvrdhttcy lgwredktgr askwwinrld qidlistlfs
      301 trgvat
//
LOCUS       WP_175790510             209 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia ambifaria].
ACCESSION   WP_175790510
VERSION     WP_175790510.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..209
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22237
     Region          1..207
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msiqtwilfa taylattlsp gpnvllvirn tvrygthgta atiagnlvaq gvvvllvalg
       61 vgavlaampp lflamkvvga aylmflgvrq lrgdrqaaas sgtaqiavpe rrklfrealf
      121 vsgsnpktmi flsafmpqfi ahdrplalqf vvmyatiast vvivhsvysf gvrrlhrgfg
      181 vspwvrtakr asgllfvglg iklltarqa
//
LOCUS       WP_175790514             441 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175790514
VERSION     WP_175790514.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47433
     Region          33..435
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(46..47,50..51,54,86,136..137,139..141,144,164,
                     167..168,171,267,270..271,274..276,279,307,311,361..362,
                     366,370,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mrakypaspv qgemlkrdda rtfeaatyak varrlipflm lcylgayldr vnvgfaklqm
       61 lndlrfsetv ygmgagiffl gyflfevpsn lilhrvgarr wlarimltwa visasfvfvk
      121 spgafyalrf llgvaeagfa pgvilyltyw fpsarrakal smffmaipla giiggplsga
      181 imhslhgams magwkwlfll ealpslvlgf aillylddgi agakwltdae kalltrnvsa
      241 daehttahls irafvadrrl wlmaaiyfcv vlgqygltfw lptiirkagv adplwvglft
      301 avpyacaiva lpligisadr rrerrfhlav pmliaaagfa tlpllgsvga sivclsiasa
      361 gilasssqfw slptallggm saaagiaavn cfanlagffs paivgwlndl tgkstagllf
      421 isaaitvgal lvflvprsvn r
//
LOCUS       WP_175790516             433 aa            linear   BCT 11-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Burkholderia ambifaria].
ACCESSION   WP_175790516
VERSION     WP_175790516.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..433
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46513
     Region          14..431
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 mslnddatfw hnarqhliry ggtfepmiie raqgsfvyda dgraildfts gqmsavlghc
       61 hpeivsvise yagkldhlfs gmlsrpvvdl atrladitpp gldralllst gaesneaair
      121 maklvtgkye ivgfaqswhg mtgaaasaty sagrrgvgpa avgsfaipap ftyrprferg
      181 gtydylaeld yafdlidrqs sgnlaafiae pilssggiie lpegymaalk rkceargmll
      241 ildeaqtgvg rtgtmfacqr dgvtpdiltl sktlgaglpl aavvtstqie erahelgylf
      301 ytthvsdplp aavglrvldv vqrdglvqra nvmgdrlrrg lldlmerfdc igdvrgrgll
      361 lgveivkdrr tkepadglga kitrecmklg lsmnivqlpg mggvfriapp ltvsdeeidl
      421 glslleqaia ral
//
LOCUS       WP_175790548             551 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia ambifaria].
ACCESSION   WP_175790548
VERSION     WP_175790548.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Gournas,C., Athanasopoulos,A. and Sophianopoulou,V.
  TITLE     On the Evolution of Specificity in Members of the Yeast Amino Acid
            Transporter Family as Parts of Specific Metabolic Pathways
  JOURNAL   Int J Mol Sci 19 (5), 1398 (2018)
   PUBMED   29738448
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Vangelatos,I., Vlachakis,D., Sophianopoulou,V. and Diallinas,G.
  TITLE     Modelling and mutational evidence identify the substrate binding
            site and functional elements in APC amino acid transporters
  JOURNAL   Mol Membr Biol 26 (5), 356-370 (2009)
   PUBMED   19670073
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146941
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..551
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59556
     Region          31..470
                     /region_name="AA_permease_2"
                     /note="Amino acid permease; pfam13520"
                     /db_xref="CDD:404414"
ORIGIN      
        1 msqaglranr tsdveatish dstghtlhrg ltwkdafwvt sgvpagvlft iggvcatigq
       61 pawaiwiaai tmgliqsaty aeisglfphk sggasvygai gwvrysklia pvsvwcnwla
      121 wspmlalgcg laasyaltsl fpadaavlhw qlriadlgfi kpglslrina tfiiatilll
      181 itfklqhsga skaartqril giasltplli vgivpfvtgd vpmsnllpll plghdangnl
      241 ttatfgswng qgvtmalgam fmagwasygf etavcytref rdprrdtaka ifwsgalclv
      301 vmtlvpmafq galgtqamld paigdgtgva aamarivggg awvanavvvm lmlsillivm
      361 tsmmgssrtl yqasvdgwlp kylshvnehg sptramwtdl gfnlvllmms dymtvlsisn
      421 vcymlfvfln lqsgwihrmd rgnwdrpfrc ptwllvagsi cgyanlvyvg aganlqgegt
      481 lrngliamll ivpvflfrhy wqdrgrfpaq mqqdmelevp kralwlslmp yaaligaglt
      541 iwlsyylawv k
//
LOCUS       WP_175790568             299 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175790568
VERSION     WP_175790568.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..299
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32924
     Region          6..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mprdnfadll afiavarers ftraaarlgv sqsalshtir aletrlgvrl ltrttrsvap
       61 teagerllqn laprfdeied elsalaelrd kpagtvrina tdyvirtllw prlspilrdy
      121 rdlkvefvtd yglsdivaqr fdigvrlgdq vakdmiavri spdlkmaivg apayfaerep
      181 patpqdlvah dcinlrlpth galyawelar gddtlqvrvd gqvtfngtye mldaalagyg
      241 layvpaelag phvaagrlvs vlddwcptfp ghhlyyasrr qssrafaliv dalrhpghs
//
LOCUS       WP_175790598             216 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Burkholderia ambifaria].
ACCESSION   WP_175790598
VERSION     WP_175790598.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..216
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22850
     Region          12..176
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mtafdqhrrp fvvgiggttr aassterals falrgaqaag artrlfdgpf lhtlphyape
       61 hktltdaqre lidtvreada iviatpgyhg gvsglvknal dtleelrade rpyldgravg
      121 livtaygwqa agtvltslrs ivhalrgwpt pfgatvntle trfdsadscs dpkvvaqlet
      181 vgtqaaefal afashraash aasvdvlapv lkianh
//
LOCUS       WP_175790607             666 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Burkholderia ambifaria].
ACCESSION   WP_175790607
VERSION     WP_175790607.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..666
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70769
     Region          1..458
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          598..662
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(620,629..631,638)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            630
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mfdkilianr geiacrvaat ckrlgiasva vysdadanak hvaacdeavh iggaaaadsy
       61 lrglriieaa ratgaqaihp gygflsened fahaceaagi vfigppvdai aamgskaaak
      121 almhaaavpl vpgyhgddqd tanldreade igypvllkas aggggkgmrv versedfraa
      181 lascqreaas sfgnarvlie kyltrprhve vqvfgdthgn tvylfdrdcs vqrrhqkvle
      241 eapapglpdd lrramgeaav aaaravhyvg agtvefimta dafyfmemnt rlqvehpvte
      301 mvtgldlvew qlrvaagepl pltqdqlrvq ghaiearlya enpargflps tgtlkhlrlp
      361 egvefaigap vrvdsgvreg daitpfydpm iaklivhgad raealgrmlr alracevvgl
      421 htnaaflqri vasepfatan ldtgliernh dalfapqpsp ratlalacaa llvrergaaa
      481 qqrvspwqal pdwrlnggyr rtlewhapdr eadvtvtydd ngghaslatg daaaqpfawt
      541 rgatpldfdv tldgvrssgr vyadgdsfhv ftqgvaetfe wrnvlahagd aehgggrlta
      601 pmpgkviavl veagqkveag tplivmeamk mehtigapgt gvvaevlygv gdqvadgaql
      661 lvmaed
//
LOCUS       WP_175790580             441 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175790580
VERSION     WP_175790580.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48446
     Region          30..433
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(43..44,47..48,51,83,133..134,136..138,141,161,
                     164..165,168,265,268..269,272..274,277,305,309,360..361,
                     365,369,385,388..389,392..393,396)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtaldaaasr spavpaqsae ldrtykkvfw rivpflmlcy vvayldrvnv gfaklqmsqd
       61 lafsetvfgl gagifflgyf lfelpsnllm hrlgariwia rimitwglls avfafvrtpt
      121 qfyvlrfllg laeagfypgv ilyltywfps hrrakiiavf msaipvsgif gnplsgwime
      181 rfhggsgfhg wqwmfmieav pavlvgiati lyldnsirga kwlderekql ledeiaaqpq
      241 eqhkhghslk avfadprmww msliyfafvt gqygltfwmp tlvkstgitd tlqigllsai
      301 pfivaivvmn lfghsadkhr errwhlivpa lmgavgfava asyshntavs ivflslaagg
      361 vltcaplfws lptaflagsa aaagiaiins vgnlagfasp yvigylkdlt hstssgmyvl
      421 asmlvigaia vwltpaklvn r
//
LOCUS       WP_175790612             725 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia ambifaria].
ACCESSION   WP_175790612
VERSION     WP_175790612.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 725)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..725
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77982
     Region          56..725
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mpsrrtprra rtlrpwrasl palitlcvas gahaeaepaq aasasapasv spperelpti
       61 svnasavadp tvgyqprtss iaggdarpik eipqavavvs ssvmqdqqar slddvlgnis
      121 gitqtntlgg trdafikrgf gsnndgsvlv dgvrtpvlhs ylatidrvev lkgpasllyg
      181 mqdpggvinl itrkpedtfg gsisasrtsh ggssaqfdlt gplgkpgqva ggtlafrltg
      241 eydtsrywrs fgrernalia palswhdant sidvsyqyvd ytmpfdrgtv lvngrpddal
      301 ryrrydepwa qsngiqetlr arvehrfsda wrvratygwg rdrydqyiar gtafnsatga
      361 mtrtadanlg rndsdqiatl gllgnltlag mnhalyigge yerqrsfrgd tirgkaikgf
      421 dlydpvygll apggtpnakq sdsrslvhty smivqdsvki tdrltavggl rwedwqqesg
      481 mgrpfafadr shgkvwlpqf glayaltpsl tayanvsrsf kanvasnvts plapefgrvl
      541 eaglkfdlkp gitgtlaayq idkrnvavtv gditstigta rsrgieldva gqitrhlsli
      601 gsyaytnand rdsntslvnv arhtgslfav ydtaiaslpg rwrfgggarl vgarpgdtan
      661 sftlpgyvtv dafaayetti gkfptriqln vknlldktyy pssnsnliva vgeprlvtlt
      721 ttvsf
//
LOCUS       WP_175790657             834 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175790657
VERSION     WP_175790657.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..834
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=91638
     Region          16..797
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mvsdllnkal rtqyaqhgri vrldtplged wlvplyvrgr aclgrdfeft idatstrlet
       61 iqakalirqs vtlwirqtdg sempihghvt afsrlggdga ntyyqlrfns flallrlgsd
      121 rrdwietpaq qtvsdvlgky pqaagnftwq lrqalrsysq rmqwesdwny vhrtfeelgl
      181 fprfdiaqdg kshkvvimdd lfsvpelkyk tilfsrsvqn eefdglsewi dsqeiqsael
      241 dtgtfdykrp dlskhvtmpa fdlddvpglg eqyeytgsht wsdrdmgeaq anvvteewrs
      301 raqrfygvga lrcawpgryg mltghpvhda qpdqdremai lsvnwliqnn vpglenlmrf
      361 rrslraeveq arasgagssv rhddggvgff hveieaqrrr vafrspfehk kpimqlqtgi
      421 vggpeaeeiy tdamlrakvr ltsnrlndgd qnvsawiraa mpdaghkrgg mfplrkndev
      481 ligfingdcd rpvilsrmhg gesmpewhth gltsgllsre yggegynqlm mddasgqnrv
      541 hlystsyssh lhlgyliqhs gntrgafigq gfdlkslgyg avraeqglyv stqpattqpl
      601 sttaateqlt raeamlatts kasqsnraqs qqdghdalkt ftdatqhpva gtskggrtag
      661 ggtgnangfa kpimllsspe giaastqgsa hitankqtnl vageninlaa grallasvle
      721 qislfaeklg vkiyaasgpi dlqaqndsms laasqdvkit agkkmylsad eiwigangsy
      781 ikltanmien atsgqivekc adwekagaas galqnplhss pvsteggrft vfsg
//
LOCUS       WP_175790689             212 aa            linear   BCT 11-JAN-2025
DEFINITION  carbonic anhydrase [Burkholderia ambifaria].
ACCESSION   WP_175790689
VERSION     WP_175790689.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Lindskog,S.
  TITLE     Structure and mechanism of carbonic anhydrase
  JOURNAL   Pharmacol Ther 74 (1), 1-20 (1997)
   PUBMED   9336012
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10096752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..212
                     /product="carbonic anhydrase"
                     /EC_number="4.2.1.1"
                     /GO_function="GO:0004089 - carbonate dehydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22862
     Region          11..190
                     /region_name="beta_CA_cladeA"
                     /note="Carbonic anhydrases (CA) are zinc-containing
                     enzymes that catalyze the reversible hydration of carbon
                     dioxide in a two-step mechanism in which the nucleophilic
                     attack of a zinc-bound hydroxide ion on carbon dioxide is
                     followed by the regeneration of an...; cd00883"
                     /db_xref="CDD:238448"
     Site            order(33,35,42,44..46,58,61,83,88,98,101,180)
                     /site_type="active"
                     /note="active site clefts [active]"
                     /db_xref="CDD:238448"
     Site            order(42,44,98,101)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238448"
     Site            order(43..46,48,50..51,53,58..60,62,64,78..79,82..83,121,
                     180,182..183,185,187)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238448"
ORIGIN      
        1 mnrpksmlva niawaretrd htpgffdala rgqnprvlwi gcadsrvpae tithsvpgel
       61 fvhrnianlf hpdddnsasv leyavrvlev dhvivcghyg cggvrasllp ppadlphvar
      121 riaplcalar rhrdaldgld dtaaadrlae lnvleqvrll raspivqgrk rpplvhgwif
      181 sladgllkel dsgyaappve aepehaataa aa
//
LOCUS       WP_175790694             243 aa            linear   BCT 11-JAN-2025
DEFINITION  alanyl-tRNA editing protein [Burkholderia ambifaria].
ACCESSION   WP_175790694
VERSION     WP_175790694.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V.
  TITLE     Evolution of aminoacyl-tRNA synthetases--analysis of unique domain
            architectures and phylogenetic trees reveals a complex history of
            horizontal gene transfer events
  JOURNAL   Genome Res 9 (8), 689-710 (1999)
   PUBMED   10447505
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Cusack,S., Hartlein,M. and Leberman,R.
  TITLE     Sequence, structural and evolutionary relationships between class 2
            aminoacyl-tRNA synthetases
  JOURNAL   Nucleic Acids Res 19 (13), 3489-3498 (1991)
   PUBMED   1852601
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Schimmel,P.
  TITLE     Classes of aminoacyl-tRNA synthetases and the establishment of the
            genetic code
  JOURNAL   Trends Biochem Sci 16 (1), 1-3 (1991)
   PUBMED   2053131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..243
                     /product="alanyl-tRNA editing protein"
                     /GO_function="GO:0002161 - aminoacyl-tRNA editing activity
                     [Evidence IEA]"
                     /GO_function="GO:0002196 - Ser-tRNA(Ala) hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004813 - alanine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006419 - alanyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=26102
     Region          1..243
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
ORIGIN      
        1 mttlalfred ayltqcdavv aavgddgirl drtvfyplgg gqagdtgmlt lpdggtiaia
       61 dtrkakfdga tpddavhvpa pgqearvaal apgarvvagi dwqrryrhmr lhtaahlmca
      121 vlpypvdgcs vtadyvrldf atsdaidrad verrlaelvs gahavttewi tdaemterpe
      181 lvrtmsvkpp mglgrvrllr iagvdlqpcg gthvrntsei gdlrvaklek ksartrrvvl
      241 efa
//
LOCUS       WP_175790711             151 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia ambifaria].
ACCESSION   WP_175790711
VERSION     WP_175790711.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..151
                     /product="VOC family protein"
                     /calculated_mol_wt=16541
     Region          3..135
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(3..8,24,62..63,66,83..88,90,94,123,133)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 mqvqpyltfy graeealqfy ekalgaktmf kmhfkdappn pdypmtpema dkvmhasfti
       61 gdsmimcsdg dcsqpgggth agyslslnpa tveegqklfn aladggevtm pfgktfwalg
      121 fgmakdrfgv hwmvnvedls rredlakraq g
//
LOCUS       WP_175790731             232 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia ambifaria].
ACCESSION   WP_175790731
VERSION     WP_175790731.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..232
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24758
     Region          10..232
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mfqirraadr chtrqgwles sssfplagha gathppfgal rllsedriap trgfgmqprr
       61 dleivtyvld galahrdslg ngaivraggv qrmsagtglm hsetnawcdr plhllqiwlq
      121 paerggrpgy aqrrfaddek rgrlrlvasp dgddgalsvr adarifagli dgddetafgv
      181 pagrstyvhv argdvevngh alaegdgari agvdtvafar graaevllfd va
//
LOCUS       WP_175790733             308 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175790733
VERSION     WP_175790733.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34174
     Region          16..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          101..300
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(116..117,119..120,123,127,129..135,229..234,
                     240..241,243..244)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mmhpdlrrld lnlllafdal yrhrsvaaaa helamspsal shalarlrda igdalfvrlg
       61 nemqptvrad diatwagdal dtmskglara rrfdpaqsdr tfvfaasdyt afavlpalla
      121 riervaprlr irvvhserki sidelaagri dfalgyhees tadspgiedf dwfsddyvvi
      181 asaahpdirr rltldqylaa rhvvvtpwne srgvvdyvld rlglvrqvav qlpsvlaapf
      241 aiaestllmt vpnraaqalr haapirifpa pfeiprytvk vyshakhart dahrwiraql
      301 ldarpaqg
//
LOCUS       WP_175790787             309 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175790787
VERSION     WP_175790787.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33719
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..294
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdkldqvrif lqvaemgsfi kaahaldvpr atvsaavqql eaalgtrllh rttrqvqlta
       61 dgalllergr rllaeadeld rlfrgrdrdv vgrlnvdaps riarrviapa lpslfrrhpk
      121 lqlslgstdr tidlvqegvd cairvgrlad sslvvrplgq ftlincaspd ylrecgvpeh
      181 pdalahghwa igyaspttgr elgweycadg aqhtlalpsr vivnnaetyi asciagmgli
      241 qiprfdvahl ldsgalvevm pghraapmdv savyphrrhr srrlnafiew fgelmadaln
      301 dtgvaargd
//
LOCUS       WP_175790806             293 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia ambifaria].
ACCESSION   WP_175790806
VERSION     WP_175790806.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..293
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31364
     Region          17..270
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mtepikallk phirdignlq vrrtlpalaa rlvgpfiffd hmgpaalpag tgldvrphph
       61 iglatvtylf dgailhrdsl gsrqeivpgd vnwmtagrgi vhsertpdaq rasghtvhgi
      121 qtwvalpvah ettepsfehh aadtlptrhe ngvtltviag dafglrspvt tfsrtlyvaa
      181 efaagsrlel dasheeravy vvdgdlting tpvpaeqmav ltpgatvtla sgngaramll
      241 ggdkidgerf iewnfvassr eaierakaaw tnqemgkvpg etewiplpaa kpr
//
LOCUS       WP_175790803             520 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175790803
VERSION     WP_175790803.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..520
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54571
     Region          24..520
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mssparssap pdiaallaal pariadvpar waahapahpa liedarrlsy gelaqaveaa
       61 aarlarlgvr ggdrvmivae nsvaqivllf avarvdawal vsnarlsase ldaiaaharp
      121 kliafateas pdarahaarh datpadalpv digawshrvd psapsepvaa dgaaqcaali
      181 yttgttgtpk gvmlshrnll fiaamsstlr rvspddvvyt vlpvshvygl asvclgslya
      241 gatlrlaprf speavrvala degvtifqgv pamhaklleh lhthahawra prlrfaysgg
      301 spldadlkar vervygvplh ngygmtessp titqtpldap rtdcsvgvpi pgvemrivap
      361 dgtdvpqgev geirvrgpnv mlgyyrdada traavspdgw lgtgdlarqe adgsvtiagr
      421 skeliirsgf nvypveveqv lnahpdvvqa avvgravegn eevlafvelv pgasateaal
      481 nawcaqrlap ykrparirvl dalpaastgk vlkhklrela
//
LOCUS       WP_175790809             169 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia ambifaria].
ACCESSION   WP_175790809
VERSION     WP_175790809.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..169
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17892
     Region          10..165
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mnhanppdfd saafrqalgq fatgvtvitt qapsgqligi tassfnsvsl npplvlwsla
       61 hksastpvfr snshyvvnvl aasqidlckr fstykgdrfe giahvagnsg mpvldgalaw
      121 fechnrsryd egdhvifvge vercgvravs daapplvfhg ggfhgltpl
//
LOCUS       WP_175790812             314 aa            linear   BCT 11-JAN-2025
DEFINITION  ketopantoate reductase family protein [Burkholderia ambifaria].
ACCESSION   WP_175790812
VERSION     WP_175790812.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..314
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32660
     Region          1..312
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mriailgaga mgslfgarla ehgeavtlid vndahldair rdglridddr gerrirtlqa
       61 vrpeaanaaa gdapdapfdl livftkslht caalegvhal ltprtsvltl qnglgnveal
      121 nafvpleril vgvttwpadf agaghvrshg agtirmmtad gaprpfaaav adalsragla
      181 csldadvwaa iwekvafnaa lntlcaatgc tvdqlgrdpe gprlalaiaa etaavarakg
      241 iavdseriar nvehaigehr ghrpsmlqdv lagrrteiga ingqvvaaar etgvavphve
      301 tllalvrlid aqld
//
LOCUS       WP_175790819             369 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia ambifaria].
ACCESSION   WP_175790819
VERSION     WP_175790819.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..369
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39542
     Region          1..355
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masvllrnia kryddtevlr nvnldiadge fvvfvgpsgc gkstlmrmia gledissgel
       61 lidgakvndv psakrgiamv fqsyalyphm tlydnmafgl klagakkpei dqavkqaaki
      121 lhidhllerk pkqlsggqrq rvaigraitr kpkvflfdep lsnldaalrv kmrlefarlh
      181 delkttmiyv thdqveamtl adkivvlsgg avqqvgtpnt lyhapanqfv agfigspkmn
      241 flkgtaesad atgvlvrfds getqrvavda aglqpgaavt vgvrpehllv gaagtgvaar
      301 tmaveslgda aylyaesava pdgliaripp letyrtgeal hvhaqpehch lfdeqgqafr
      361 rlsahakaa
//
LOCUS       WP_175790856             552 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175790856
VERSION     WP_175790856.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..552
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58950
     Region          18..538
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(31..32,35..36,39,77,135..136,138..140,143,163,
                     166..167,170,256,259..260,263..265,268,296,300,464..465,
                     469,473,489,492..493,496..497,500)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 matlggqish spmtaeekkv ifasslgtvf ewydfylags laayisksff sgvnptaafi
       61 ftllgfaagf avrpfgaivf grlgdlvgrk htflvtivim gistfvvgfl pgyttigiaa
      121 pvifiamrll qglalggeyg gaatyvaeha panrrgfyta wiqttatlgl flsllvilgv
      181 rtligeesfg swgwrvpfva silllavsvw irlqlnespv flrikaegkt skaplteafg
      241 qwknlkivil alvgltagqa vvwytgqfya lffltqtlkv dgasanilia ialligtpff
      301 lffgslsdri grkpiilagc liaaltyfpl fkalthyanp qlelatqkap isviadpatc
      361 sfqfnpvgts kftsscdivk salakaglny envaapagst aqikvgdtvi paydgkapda
      421 kvqgaafdkt lastlkgagy pakadpaqln wpmtivilti lviyvtmvyg piaamlvemf
      481 ptrirytsms lpyhigngwf ggflpatafa ivaakgniys glwypivial gtfvigllfv
      541 ketkdsniya qd
//
LOCUS       WP_175790908             266 aa            linear   BCT 11-JAN-2025
DEFINITION  (Fe-S)-binding protein [Burkholderia ambifaria].
ACCESSION   WP_175790908
VERSION     WP_175790908.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..266
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28332
     Region          <7..256
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mnerhyptaa pahvylfatc lvdlfvpeag ldtvrllere gltvhyprgq sccgqpayss
       61 gnpdearrva aaqldlfaep wpvivpsgsc agmirhhwpa lfaddpvhgp karaiaerty
      121 elaeflvhvl hvrldavtan agpdervvlh tscaarremg trvhgvalvd alpgvtrieh
      181 ereseccgfg gtfslkhpdi sgamvtdkva sacatgcerl vsadcgclln ighaaekaga
      241 alpvehlasf lwrrtagags lrgdsq
//
LOCUS       WP_175790932             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175790932
VERSION     WP_175790932.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33714
     Region          7..>178
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          95..293
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(105,109,148,162,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(106..107,111..112,114..115,118,122,124..130,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mqhlpdleaw aifarvaetg sfakaaellg isqptvskai arlekrlgam llyrtsrkls
       61 ltptgellrd rairlladae lieseasaqa lephglvrvn apmsfglrhl spllpafler
      121 yprvdidlvl tdnivdivsg gfdiairiae lsdsslrsrr lcavrrplva spaylerrgr
      181 pthprdleqh vcltytnlpt pehwrfrnpa sgedvgvsvq grirtnnadv iapallaghg
      241 lalqpeflaw dalqsgelee vmpewkiadv nvnlvtppgm lraarvtvll efladhfaha
      301 pwalpva
//
LOCUS       WP_175790923             834 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia ambifaria].
ACCESSION   WP_175790923
VERSION     WP_175790923.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 834)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 834)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 834)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 834)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 834)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..834
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87854
     Region          1..834
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mtardwrage ltllvlalvl avaaltsvgf ladrlrqgle rdarqmlgad fvvradhpvd
       61 psfdrearal glrtattaif psmiasaagg hasgaaparl aavkavspgy plrgaveivp
      121 agasaahkat tipapgtvwa dpalldalhl kagdtvrvgl rtftvaasis reldrgfsfv
      181 nfsprlmmra delaatgltg ygsrvtyrll iagdtpavar feayahgrvd ggklrgvgle
      241 slqegqpqvr qtldrarhfl tlvalltall aavaiamaaq rymrrhldgc atmrclgvsr
      301 rtlgalfale fagigivagi agallgyggh wallaalggl ievalppptl wpalvgvgaa
      361 lvlllgfalp plapltrvpp vrvlrrdwgd asriawaaya igvvlfagll ivaagnlklg
      421 livaggfaga lvgfsliarl vlymaaravr narvaagigw ryalaslhrr gtasalqita
      481 lalglmclll iaitrndlva gwrqstppda pnqflidiqp dqrddvaawl aahgvrdavp
      541 apmvrgrlva ingkpvnpda ypsddarrlv drefnlsytt elpsdnriva ghwfghsarp
      601 eisiedglak ilnvkpgdtl rfdvtgltvd apitsvrkld wgsfrvnffv lmpppvlkdf
      661 pavyltsfhl paeqaalldp liarypnlta idvapilaql qrmmlqvvga vqflfgftla
      721 agvlvlytal agsrdervhe aallralgas raqvnavqra efivvgalag alasagaiav
      781 gwvlasrvfd fqlavdpwlv pagiaagvac agaagwlslh nvlrrpalqs lrda
//
LOCUS       WP_175790934             294 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia ambifaria].
ACCESSION   WP_175790934
VERSION     WP_175790934.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..294
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31374
     Region          12..270
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 msasiktvlt presdignlv vrrvlparaa rlvgpfiffd emgpavlpag sgidvlphph
       61 iglatvtylf dgtlmhhdsl gfrqkivpgd vnwmtagrgi vhserspded rpleqpvhgi
      121 qtwvalpveh edtapafahh aadtlpsftr dgasvrviag tafgltspva vfsptlyaya
      181 efaadgqlal daehdergvy lvdgdltidg aplapatmav lepgasvala sangarvmll
      241 ggahlpgerf iewnfvsser akieaarnaw aeqtfgkvpg eenewtrqpa rkpq
//
LOCUS       WP_175790973             539 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA synthetase [Burkholderia ambifaria].
ACCESSION   WP_175790973
VERSION     WP_175790973.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..539
                     /product="acyl-CoA synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016405 - CoA-ligase activity [Evidence
                     IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57846
     Region          48..538
                     /region_name="MACS_like_3"
                     /note="Uncharacterized subfamily of medium-chain acyl-CoA
                     synthetase (MACS); cd05971"
                     /db_xref="CDD:341275"
     Site            order(111,241..243,267,287,289,293,314..317,336..341,
                     344..345,361,421,433,436,442,444..447,476,505,510..511,
                     513,515)
                     /site_type="active"
                     /db_xref="CDD:341275"
     Site            order(192,195..200,202..203)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341275"
     Site            order(237,289..290,293,314,444..446,505,511)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341275"
     Site            order(314..317,336..341,361,421,433,436,442,447)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341275"
ORIGIN      
        1 mlpaaerydd llsrfqwevp aryniavdvc dkwadgsgrl alihetsqgd vsritfddlr
       61 nasnrlansf araglqrgdr iaiflaqgpe taiahlaayk lgaiavplft lfgtdaleyr
      121 lanseaaalv tdaagyakia plraqlptlr tcycigddvp dapgvlryda alaaespdfv
      181 padtaaddpa viiytsgttg kpkgalhahr vllghlpgve msqqcfprda rlfwtpadwa
      241 wigglldvll pswhhgvpvl arrfekfdae aafalmarhg vthaflppta lklmravpap
      301 rerytlalks vasggeslgt eltawgrdal gvtinefygq tecnmvlssc aalfdaqpga
      361 igkavpghtv aivdehgtpl ppgvegriav rrpdpvmfle ywrnpaatrd kfagdylltg
      421 dtgtidadgf vrfvgrdddv itsagyrigp gpiedcllth pavrmaavvg vpdptrteiv
      481 kafvvlnpgh vgddalvqal qahvrtrlaa heypraiafv dslpmtatgk ivrralrda
//
LOCUS       WP_175790993             146 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Burkholderia ambifaria].
ACCESSION   WP_175790993
VERSION     WP_175790993.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..146
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=15883
     Region          44..146
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 msgihygydl fdefarvqrq vaslfgehpt giravrpsaf palnvgatdd sieivafapg
       61 maaadfdvsi dkdlltisge rkpvphdagd dlrtyaqerf hgafrrvvel pqnadadnvs
      121 aryengclli rvgrreaakp raitvq
//
LOCUS       WP_175791008             343 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia ambifaria].
ACCESSION   WP_175791008
VERSION     WP_175791008.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..343
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36769
     Region          8..343
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkldstpitl thcaktfrgt rvlepldlsi gagetlvllg psgcgktttl rliagldtpd
       61 aggtiafggd dvtqlpierr qvgmvfqnya lfpnltvrgn vgyglkirkt epralrervd
      121 ellammrlda hadkpvdqls ggqrqrvala ralavrprvl lldepltald aklrdvlrre
      181 mnallrelgv ttvyvthdqa eamelgdriv vmgagrieqi gtprdiyyrp anrtvaqfig
      241 tlnrlagqwr dgalvttgga ivtphaadew ffrpedaqla dpahaplrga igacaflger
      301 trltieqaap dalvidvpgr ielargtavg iaiaaeglia laa
//
LOCUS       WP_175791059             257 aa            linear   BCT 11-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Burkholderia ambifaria].
ACCESSION   WP_175791059
VERSION     WP_175791059.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 257)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 257)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..257
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27106
     Region          23..>203
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mekrplnpps tpsppprrpf newldgardt ipmmigaapf gvifgtlvag gplaawhgal
       61 mslavfagsa qfialgliag sasfvvvlat tlivnlrhll ysatlapyva hlplrwratl
      121 galltdevfa vayshyrhfp pgaigphyff gsglamylnw qvwtlagigf gaafpglqsl
      181 gldfamaatf iaivvpqlgk lryfaaaata gtlayfwqgw pyklgllgav avgvavgval
      241 tlrhersrtg srteaas
//
LOCUS       WP_175791155             244 aa            linear   BCT 11-JAN-2025
DEFINITION  DsbA family oxidoreductase [Burkholderia ambifaria].
ACCESSION   WP_175791155
VERSION     WP_175791155.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..244
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26140
     Region          15..214
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(23,26)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 mtttaaptar ptltveiwsd licpwcwigk rrfdealaaf ahaehvdvvl rayrlmpgqp
       61 vepveamlag kyqmspaqvd qmlrqvtdaa asvglrydlp gtsvgdtlda hrlvklaeat
      121 grahalterl yrayfsehgs lfdhaalidf aveaglersa veavlrsday rdeveadiar
      181 aaqiggrgvp lfvfggryav sgaqpadvfa qaleqawrdg aivefagdda aacgpdgcel
      241 pprg
//
LOCUS       WP_175791234             241 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            ambifaria].
ACCESSION   WP_175791234
VERSION     WP_175791234.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..241
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25943
     Region          25..181
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdqtsepprp igaavatehr vprgarrkqa trmrllraaf mlmaekgmdn vaiseiteaa
       61 dvgfgsfynh faskdglfaa liewvfddfa drlervtggl sdpaevvsvc vrhtlmqahr
      121 ewmwgrflmr egvsvraldr glgqrlrrds argiaarrfi vgdpfvsvla stgtilaaia
      181 aqlhiagtve ggarrraagv gdfpertaav vlqtlgiara eahaianrpl ppgdftvtag
      241 d
//
LOCUS       WP_175791248             360 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia ambifaria].
ACCESSION   WP_175791248
VERSION     WP_175791248.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..360
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38269
     Region          3..340
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,225,294,314,316..318)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,173,176,178,225,232,294,314,
                     316..317)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,173,176,178,317)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            178
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mptlfdpirl gaieapnril mapmtrargt rehvptamma dyysqrasag liiseaigis
       61 rqglgwpyat glwtpaqvag wrkvtdavhe aggrivaqlw hmgrvvhpsf ldgaqpvsss
      121 ittapghaht yegkqsytpa ralatheipa vieqfaaaar halqagfdgv qlhasngyli
      181 dqflrdsanf rddayggsis nrlrllievt eavadvvgad rtsvrlspng etlgvrdsdp
      241 vplfiaaaea lstvgiafle lrepplngsf gvgyldplaa rirpafkgpl vlnsdfdaar
      301 aqaeldagig davafgrpfi snpdyprrla nsiplasddp ttwftqgadg yvdypgatsa
//
LOCUS       WP_175791259             334 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Burkholderia ambifaria].
ACCESSION   WP_175791259
VERSION     WP_175791259.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..334
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36036
     Region          7..303
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(12..14,44,49,75,138..139,179..180,201,230..236,272,
                     289..292,297,300..301)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(44,49,75,138)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 mritlpsrlg fgtaplgnmy rdiphdeala tvdaawrggi ryfdaaplyg aglaelrlge
       61 alagrprdey slgtkvgrlv ldehedasqr dlgekgglfr hglpnrivyd ytadgtlrsi
      121 easlarlrtd rldtvwihdp avdfhgdawr dvfdvamsga akaltqlrde kvikgwglgv
      181 nrvepcelal ersdpdgfll agrytlldha galerlmpes aarglgiivg gpynsgvlag
      241 gthfeyqpat qamlervari rrlcerfgvd vravalqfsl ahpavaaaip gasrperide
      301 nlrlaaapip aalwaalkae rliaehaptp tgad
//
LOCUS       WP_175791275             203 aa            linear   BCT 11-JAN-2025
DEFINITION  trimeric intracellular cation channel family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175791275
VERSION     WP_175791275.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..203
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=20988
     Region          1..196
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mhtlyliaiv aeamsgalmg mrrgmdrfgl alvgavtalg ggtvrdvllg hyplgwiarp
       61 eylvitlaaa tvaswaarhv armkalfvtv daiglaafti igcdvgastg tapiivvlag
      121 aitgvcggml rdllcnempl ilreelyasv alatgalyvg mqylgidagf atmvalaagf
      181 smrmlavrlg wkmrtfgaad vgh
//
LOCUS       WP_175791298             219 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Burkholderia].
ACCESSION   WP_175791298
VERSION     WP_175791298.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..219
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24987
     Region          4..207
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mtptlyahpf ssycqkvlta lyengtpfdy rvlahddpkp mqelaalwpl krfpvlvdag
       61 rpvieatiii eyldlyhpgp vrlvpddrra alevrtmdrf fdnyvstpqq kvvhdalrpe
      121 herdargvad aramldtsya wldrtmadre waagdrfsla dcgaapflfy adwthridps
      181 fanviayrkr llarpsfara vdearpyraf fplgapdrd
//
LOCUS       WP_175791284             417 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia ambifaria].
ACCESSION   WP_175791284
VERSION     WP_175791284.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10396284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..417
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=43936
     Region          1..261
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Site            order(7,9..10,12,66..68,104..106,116,120,139..142)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187579"
     Site            order(82,106,116,120)
                     /site_type="active"
                     /db_xref="CDD:187579"
     Region          308..407
                     /region_name="DoxX_3"
                     /note="DoxX-like family; pfam13781"
                     /db_xref="CDD:463982"
ORIGIN      
        1 mnilvcgang figralcarl eagghrvlrg vrhavgphdv aidfatdvdp gawlarldgv
       61 dvvinavgil tdrrdatldt vhraapcalf tacsrarvrr viqisalgve rgdtpyfask
      121 yaadtflqtl pldyrivrpa lvygtagtsa rffrmlaslp vhalpagghq rlrpvhvddl
      181 aelvarlvvs paaghsvida vgadeveyre mlsgyraaqg fppaaritlp gplvgaaaal
      241 lgtlpgamlt rdtwtmlrgg ntgdpaalaa vlgrpprglr sfigadalal rrdalamwrr
      301 plllgalaiv wiwtaivsaf vhpqgdslam larahltglp alialyaaca ldfafgvati
      361 aapsrrlwaa qgvlivaysa viavtmpgll aepfgpvikn vpilaillil fseeerp
//
LOCUS       WP_175791340             249 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase, partial [Burkholderia cenocepacia].
ACCESSION   WP_175791340
VERSION     WP_175791340.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..>249
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          1..>243
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 msatdtqpdl ilhngrittl dranpvatav aikdgrfvav ggnaeivpla gratkvvdld
       61 grtvlpglid nhthvirggl nynlelrwdg vrslavamem lkrqvaitpa pqwvrvvggf
      121 tehqfaekrl ptiaelnava pdtpvfilhl ydrallnaaa lrvvgytkdt peppggtilr
      181 ddagnptgll lanpnatily atlakgpklp feyqynstrh fmrelnrlgv tgvidagggs
      241 qnypddyev
//
LOCUS       WP_175791341             234 aa            linear   BCT 11-JAN-2025
DEFINITION  MOSC domain-containing protein [Burkholderia ambifaria].
ACCESSION   WP_175791341
VERSION     WP_175791341.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12233312
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..234
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25812
     Region          31..183
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
     Region          180..219
                     /region_name="3-alpha"
                     /note="3-alpha domain; pfam03475"
                     /db_xref="CDD:460938"
ORIGIN      
        1 msgdarpaia vaiaavrvgt srplagtphl saidkqpvda rlwlgtlgfa gdgqadarhh
       61 ggpdkavhhy aydhypwwse qigardvlgr pgafgenlst hgvtehdvcl gdvftlggav
      121 lqvsqsrqpc wklnarfdhp rmaalvqqsg rtgwyyrvld egwvapgdvl alherrypqw
      181 plsavldvly rrtldmtald alcgvpvlpp gwrkmldkrr terqvedwtk rleg
//
LOCUS       WP_175791377             158 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Burkholderia ambifaria].
ACCESSION   WP_175791377
VERSION     WP_175791377.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..158
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=17339
     Region          5..153
                     /region_name="OsmC"
                     /note="Organic hydroperoxide reductase OsmC/OhrA [Defense
                     mechanisms]; COG1764"
                     /db_xref="CDD:441370"
ORIGIN      
        1 mahgehkyrv avewtgnrgt gtsgyreygr dhvisagtkp dipgssdaaf rgdaarwnpe
       61 dlllasasac hklwylhlcs eagirvlayv ddaegtmlds peqgrfteiv lhprvtirag
      121 ddrelaerlh ydahakcyia nsvnfpirce pviefaaa
//
LOCUS       WP_175791378             213 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175791378
VERSION     WP_175791378.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..213
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24144
     Region          7..213
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mearldstad avaaslremi ingeleager lverdlaerf gisripmrea iqrleregll
       61 difrnrgavv rmlsasdvqe iydmrvlleg daiyrsvkrl ddetlarael vhrllgessv
      121 arrqgelnre fhvllysccg narqlkaiae lrsqveryer lqatlladtp sfqveheeil
      181 qacrernarg aramtvahld sarrivmrlv egd
//
LOCUS       WP_175791382             663 aa            linear   BCT 11-JAN-2025
DEFINITION  beta-galactosidase [Burkholderia ambifaria].
ACCESSION   WP_175791382
VERSION     WP_175791382.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 663)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 663)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 663)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448998
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..663
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73917
     Region          1..622
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
ORIGIN      
        1 mrlgvcyype hwpesmwadd arrmkvlgia qvriaefaws riepspgeyd wgwldravdv
       61 lgaagleivm ctptatppkw lvdrhpdila igadgrprgf gsrrhydfss ptyleasrqi
      121 ctavaerygr hpavrywqtd nelgchqtvv syspaalvrf rewlkarygt idalnrawgt
      181 vfwsmeyrhf devdapigtv teahpshrld yrrfasdeva ryhrmqvdvi rahspgrpva
      241 hnfmqlftef dhyevardld iatwdsyplg aleeqwfape lkarwlrtgh pdfasfnhdl
      301 yrgmsklpfw vmeqqpgpvn waqwnpaplp gmvrlwswea fahgagcvsy frwrqapfaq
      361 eqmhaglhtp ddqldeggre aqrvareiaa vldagadada ngavrapval vfdyeakwlf
      421 evqpqgadfh yprcafeyys alrslgldvd visahapldg yglvvvpplp ivpddfaarl
      481 aasgahavfg prtgsktadl qipptlppgp lasilplrvw rveslrpnvt epidgtlrdg
      541 saftgdarrw rdlvelrdda psvvrarfad ghpacvshga lhywaalfdd attarlfadv
      601 aaeagltpsp lgdgvrvsrr ggltyvfnyg stphtldgvp psafvvgaaq vepqgvavyr
      661 srs
//
LOCUS       WP_175791399             337 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Burkholderia ambifaria].
ACCESSION   WP_175791399
VERSION     WP_175791399.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..337
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=37662
     Region          31..304
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mslptpsdtp arpeekdlfd rgasdwivsp etafdawlam qdyrrssadv yraqwgaflt
       61 wlrahqknla tvdtasianf vgelpirktq rmrylrlier vldhirrtel astnparfia
      121 qdgeanwrqa rdneptgflt paerakllay lfspigvsgs aywkerrdra lvaaflgagv
      181 ktgearalti scintsgtsl qipsthpdfa rethlasfai alleawlver krqeipgelv
      241 fpashagrpm hkatmlraid aivesaglts srtaraspqt lrntyaaelf ehdvppervg
      301 kwlgfmrpis snrlhrawkn wrdglangda hvpdeth
//
LOCUS       WP_175791402             273 aa            linear   BCT 11-JAN-2025
DEFINITION  siderophore-interacting protein [Burkholderia ambifaria].
ACCESSION   WP_175791402
VERSION     WP_175791402.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..273
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=29825
     Region          5..266
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mqntsertvt rvrhtlkfrl lqvvrvhavt phllrvtlgg pdladfesss fddhvkvffp
       61 ppgaerpamp tlgangpefp egepkpiard ftprrfdraa celdlefvln hpgpasqwaa
      121 qarvgqwlgi ggprgsfvvp idfdwhllig ddtalpaiar rleqlpagar aavvlevadr
      181 taqiafdtra dvheiwrfra eadaadgdal ltavrelplp ssgdgyvwaa geaqsmravr
      241 lhltgergid ksriraaayw krgaaavhet led
//
LOCUS       WP_175791410             532 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia ambifaria].
ACCESSION   WP_175791410
VERSION     WP_175791410.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..532
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=57671
     Region          2..532
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 msdrtfdyiv igagsagcti athlverglg tvllleaggh dkdlfihmpg glakaipryt
       61 wpyaaepsdd vkgrsiavpq grvlggsssv ngmlyvrghr ndydrwetef gckgwgaddm
      121 lryfakaenn esltapyhgn kgqlqvteir yrhplsqafv ragqqmgldy lvdyngerqq
      181 gvgfyqatif ngergstaat ylsairnrpe lslevdalve rveieggrat gvtyrqgnrr
      241 vtararaeii vsagaigspk ilqlsgigpq kvledagvqv rhvlpvgenf hdhmhmsvna
      301 tirtpvslyg qdkgwralkh giqwkwfrsg iltspvlegf afvdtcgqgq pdvqfhflpt
      361 idsfddpigv tagrthgiti ktghlqpysr grvtirssnp qelpridgry ladrrdvdgq
      421 iraaklalki lrqpalaehv deifspdcpp dddaaiedwv rgaaktvyhp vgtcrmgtda
      481 assvvdpqlr vhgiaglsva dsstmpsips gntnaptial aekasdlian aa
//
LOCUS       WP_175791414             433 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175791414
VERSION     WP_175791414.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..433
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45398
     Region          7..406
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mtshrsskpa wtyenrllli lfmtfgfvff drlalsflfp fmsaelhlsn tqlgmvssal
       61 altwalsgaa tgawsdargt rkplliaavl gfsvcsalsg lvggfaslia fralmgiaeg
      121 pvlplsqslm iesstpsrrg lnmgllqgsa agllgamigp pvvigiatay gwreafyasc
      181 ipgfliafci wrwvrevppg gvrhaqavga gapaasgaai nrwallkern illcvliscf
      241 fltwfvviis fapvflvesr hlspadmgvv mtclgaawvf wgftvpaisd rigrkptmia
      301 falvaavcpi vmihvgsvwa lgalvfvtyt glgcftlfma tipaetvppr aiasalglim
      361 gageliggfi aptvagftad tyglqfamwt saagailacv lsfglvetap avlrkralag
      421 atarldtqnl ggh
//
LOCUS       WP_175791470             456 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia ambifaria].
ACCESSION   WP_175791470
VERSION     WP_175791470.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..456
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47704
     Region          <36..452
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          222..411
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mrldlclrla reqgrpahcg airfpirral vrgvvaaasl agmqgavawa ssdampfspm
       61 taqaadlvdv pffnsartiw ggllastdvp rvalephats trtdaasvtf tmrtgacapy
      121 vvlcdaarda ierdyaarfa ygfasplpai gaapaldarp vdlasaepfv laeqengtra
      181 gaitgslras laradlpadv aaqvtrmlag ridstqrgam gdtfrvafep ddsaavpgrm
      241 rvtaldirfr gqrvaavwfa pqagspgayy dldgmplaga qfampvnatr issqfgarvh
      301 pvtgarhvhs gvdlaaptgr avhasergvv tfigsepggy gkyvvirhdg gyasyyahls
      361 afeptlrtga rvvrgqrvga vgstgtatgp hlhfevrrha rlvnpielvq aaraaklkge
      421 qrvafnrvah aartqlaaat lapslamsqh gapsdg
//
LOCUS       WP_175791505             290 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia ambifaria].
ACCESSION   WP_175791505
VERSION     WP_175791505.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..290
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31666
     Region          15..280
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mttarsldrt ypalrttegg gfvvhrpfpt rllmdfdpfl lldemgpvdy apgeakgapd
       61 hphrgfetvt yvldgrfrhr dsaghagtlg pgdvqwmtag agvvhsempd pefaqaggrs
      121 hgfqlwvnlp rrdkliapry qeipadripi atspdgraqv rviageafgv raaietrtpi
      181 lyqhftlqpg amvtqpvppg yrvfaysldg agrygpdrqp vdarqmvvyg ddgdavtfea
      241 gdtpldllli ggvplnepiv rygpfvmnte eeirqavvdy qtgrmgriea
//
LOCUS       WP_175791528             353 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia ambifaria].
ACCESSION   WP_175791528
VERSION     WP_175791528.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..353
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=36946
     Region          10..353
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mirfavptma gllaasgama qgsvtlygiv dqsiryttha nasndasvql tngaitnsrw
       61 glkgsealgg glkaifqles gfepqngqld galfgryayv glasdwgtvk lgrqateafn
      121 lfgdldpltv gnytanmwpy fltqgrasnt vsydgtfggl dvgasygfgg vagslganay
      181 wgthvsytlg glmvgatyqq vrdlnsraqq awgagaryaf gaatlyagyl ggidrtgmld
      241 rqllnapgrd vsygsfadnp rrdaifytgv svkvtpavsv tgvgyyddir nvngvagngg
      301 krytgvleae yalskatqvy atldynrvtg gaftempgrg nqtgiaaglr hlf
//
LOCUS       WP_175791539             695 aa            linear   BCT 11-JAN-2025
DEFINITION  M3 family metallopeptidase [Burkholderia ambifaria].
ACCESSION   WP_175791539
VERSION     WP_175791539.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..695
                     /product="M3 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=76911
     Region          4..693
                     /region_name="Dcp"
                     /note="Zn-dependent oligopeptidase, M3 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0339"
                     /db_xref="CDD:440108"
ORIGIN      
        1 msasantnpl ldfsglsrfg eirpehvtpa ldtlldtanr avdtasapat patwativet
       61 veqateplgr awgvvghlna vadtpelraa ygenlprvte fwssvgqnla lyekykaiaa
      121 saeyatlsae rkkildnalr dfrlsgaelp edqkprfael qeqqaalska fsdhvldatn
      181 ayayfaqdea elaglpgdai eaareaaqke gkegwkftlh fpsyfpvlqy aenramretl
      241 yrayatrase lgpqygggka ewdntaivad elklrreeaq mlgyrnfaev slapkmaesp
      301 qqvvafledl atrarphadk dwdelrafaa kelgltelap wdvafaaerl rqqryafsen
      361 evkqyfpepa vlkglftvte tlfgvrikpd dapvwhrdvr ffrvenrdgs lvaqfyldly
      421 aregkrggaw mddararakr ggtvqtpvay ltcnfsapvg gkpacfthde vitlfhefgh
      481 glhhmltrvd elgvsgingv ewdavelpsq fmenfcwewd vlssmsshid tgaslprelf
      541 dkmiaaknfq sglgtlrqiv fsmfdmllhv dfdpagatgv nafareiner yhvipqaafs
      601 rwpntfshif aggyaagyys ykwaevlsad ayaafeeaaa aggsvldaat gtryrreile
      661 vggsrpamds fkafrgrepe idallrhngm tsaah
//
LOCUS       WP_175791546             470 aa            linear   BCT 11-JAN-2025
DEFINITION  lactate utilization protein B [Burkholderia ambifaria].
ACCESSION   WP_175791546
VERSION     WP_175791546.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..470
                     /product="lactate utilization protein B"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=51930
     Region          2..462
                     /region_name="LutB"
                     /note="L-lactate utilization protein LutB, contains a
                     ferredoxin-type domain [Energy production and conversion];
                     COG1139"
                     /db_xref="CDD:440754"
ORIGIN      
        1 mqvqsmhfka ragqkladqr lqqnlkklst kfvsaradam taidfpatra alkarrnral
       61 enldvwleaf ereatrrgtt vlfaetteda arlvadiarr hdvkkviktk smvseemrln
      121 avlaemgvqs ietdlgeyil qindneppsh iiapvvhkdk deiadlfart hhrerlteip
      181 dmtrearevl rphflsadmg vtggnfviae tgsvaivtne gnegmctvmp rvhvavtgie
      241 kvlptledla tamrllprsa tgqktsnyfs lltgprgpgd edgpehnyvv lvdggrtgli
      301 ggefqemlrc ircgacmnhc pvyqkvggha ygwvypgpmg svltpsyvgl draldlpqaa
      361 tlcgecdsvc pvgiplshll rtlrekqver hlrpwrerag lavwgffarr pllyalttkl
      421 avrvlerlgg sggmlrrlpm mggwmdtrdm ptptgrtfre lyaasqshlg
//
LOCUS       WP_175791574             540 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia ambifaria].
ACCESSION   WP_175791574
VERSION     WP_175791574.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 540)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..540
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58982
     Region          9..537
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msdtvvsksg epllslehlh vrfgdtvavd dvtlaigrge rvalvgesgs gksvtalail
       61 rllrdadvsg tirlagqdla gkseremrgl rgsdiamifq epmtalnply tigaqigeti
      121 vlhdgvtaae arkraialla rtgiaeperr vdsyphqlsg gqrqramiam alacrprlll
      181 adepttaldv tiraqivdll lelqreeaek rgmaillith dlnlvrhfad rvavmergkl
      241 vesgpverif aepehpytqr llnsrpqrav vpvmpiapvv ldarhvsvqf arkrpgfagw
      301 fgtvpvtava dvsvsvrqge tlgivgesgs gkstlamall glqktahgei efqgralsty
      361 rgreqtalrs nmqvvfqdpf sslsprhtie rivgeglelh rpeltpdarr akslavlrev
      421 gldrtvlhry phefsggqrq riaiaralvl eprilildep tsaldvsiqq qvlkllanlq
      481 qkynlgyvfi shdlevigam ahrvavmqeg vvvesgevae ifarpshpyt qkllkavwka
//
LOCUS       WP_175791602             405 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175791602
VERSION     WP_175791602.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..405
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41433
     Region          8..392
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(18..19,22..23,26,61,108..109,111..113,116,139,
                     142..143,146,223,226..227,230..232,235,265,269,318..319,
                     323,327,343,346..347,350..351,354)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mpdsryrwvi vaagglmgci aigamfslpv flraiardtg wsmtgisgam tlgfiamafa
       61 sigwgslsdr igtravvvtg avllsaslal asrapsllaf qlifglavgs ataavfapmm
      121 acvtgwfdth rslavslvsa gmgmapmtma plaawlvsgh gwrtsmlaia alaavvmipa
      181 sllvrrapal dgppagptpa gepataplsv ggalrspqfv vllltnffcc athsgpifht
      241 vsyavtcgip liaavsiysv eglagmggri afgllgdrlg akrmlvagll aqalgalgyy
      301 fvrtldgfyv vatlfgfiya gvmplyavla renfplrmmg tviggcamag slgmaagpva
      361 gglivdalgs yswlylgsfa igigaflvam mfrpfpkers qpvva
//
LOCUS       WP_175791703             297 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175791703
VERSION     WP_175791703.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33273
     Region          6..>51
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mprenlndll vflavardrs ftraaarlgv sqsalsqtvr dletrlgvrl ltrttrsvst
       61 teageelfqa vaprideiem klaavadfrd kpagvvrita tehpidtiiw pklrrvlpey
      121 pdirvelsvd yglaniveer ydigvrygdq vakdmiavri spdirmtmva spayldgrkp
      181 prtpqdlldh dcvtlrlata kgiyawelkk grneiqarvs gritcntqph mvqaaldgfg
      241 iafvtedivl dhvrsgqlri vmpdwcpvfp gyhayypsrr qasrafsivi dalrhra
//
LOCUS       WP_175791645             351 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia ambifaria].
ACCESSION   WP_175791645
VERSION     WP_175791645.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..351
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37560
     Region          34..334
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 msfplspalr rttrlarral aatlsaalsf aaagtpqaah aegririaeq fgvvylmlnv
       61 ardqqlieke grkagidikv dwvrlsggaa vndallsgav diagagvgpl ltvwdrtrgr
      121 qnvkgvaslg nfpyylvssn pnvktiadlg akdriavpav gvsvqsrvlq yaaakqwgdk
      181 qfdkldpltq aiphpdataa ilansnvitg hfgnppfqeq elagnpnahi vlnsydvlgg
      241 pssatvlyat gkfrddnpkt yrafvaalad aarqiaadpe raadtyirvn gskidralll
      301 kilrnpqvqf ktapqntlkl aqfmyrtgai rnepkswrdy ffddpatagg s
//
LOCUS       WP_175791712             235 aa            linear   BCT 11-JAN-2025
DEFINITION  PIG-L deacetylase family protein [Burkholderia ambifaria].
ACCESSION   WP_175791712
VERSION     WP_175791712.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..235
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25734
     Region          6..>163
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mtdptrwlvi sphlddavfs cgqvlaqapg svsvtvfagi pargsdappw drragfrtad
       61 eavrsrrded rralamlgaq pvwldflddq ygtraastai aarladtida hpgfgvlapa
      121 glfhrdhiqv qqavltllrd nsragdaarv wrfyedvpyr ridglmakrv idwrehgwig
      181 hpvgppagnr tdgaaakaaa vdayasqial fephmradlr epetywrlec dkvsa
//
LOCUS       WP_175791718             403 aa            linear   BCT 11-JAN-2025
DEFINITION  zinc-dependent alcohol dehydrogenase [Burkholderia ambifaria].
ACCESSION   WP_175791718
VERSION     WP_175791718.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 403)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..403
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42207
     Region          1..403
                     /region_name="FDH_like_1"
                     /note="Glutathione-dependent formaldehyde dehydrogenase
                     related proteins, child 1; cd08283"
                     /db_xref="CDD:176243"
     Site            order(38..40,43,86,162,166,185..186,188..190,211..213,217,
                     231,255..257,305,322..324,347..349,389)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176243"
     Site            order(38,40,60,162)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
     Site            order(90..91,93,96,104)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
ORIGIN      
        1 mkavvfhgig diridtvpdp evsqptdavv rltasaicgt dlhmvrgtlg gmkpgtilgh
       61 egvgivetvg rdvrnlkrgd rvlipstiac gscaycragy taqcdvanpg gpragtaffg
      121 gpadtgpfdg lqaeyartpl anaslirlpd aidddrailm sdifptgyfg aqlaevkpgd
      181 tvavfgagpv gqfaiasasa kllgagrvia idriasrldm acaqgaetid fseedpvdtv
      241 lrltggigvd rvidavgvda mrathgpaaa drdaarafda evdavaprrk pdgrywtpgd
      301 gpsqvlqwav ravakagtva vigvyppqar vfpigeamnr nltikmgncn hrtitphlie
      361 lvrsgafdpv svltrceplt naidayrafd vrepgwmkvk ltp
//
LOCUS       WP_175791723             950 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Burkholderia
            ambifaria].
ACCESSION   WP_175791723
VERSION     WP_175791723.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 950)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 950)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 950)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..950
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..950
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103947
     Region          82..875
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mpalcdicha rpavaratvm qdgerktisi cdyhfrqlmr hqsmlnpfds llggggsslf
       61 gesgdaspla aeipresvdp tdafseqtle llqhaaekah elrrseldte hllyaladtd
      121 vcaallkelk lspqdlkayi dehahtgtaa adasldklsi sprvkkavqy afqasrdlgh
      181 syigpehlli glaavpdsia gtllkkygvt pealrqkvvk vvgkgaedgr vdaptgtpnl
      241 dkfgrdltai arqgkldpvl graqeiesti evlarrkknn pvligepgvg ktaiveglaq
      301 rivngdvpev lrgkrlvevn insmvagaky rgefeerakq lidevtakhd elilfidelh
      361 tivgagqggg eggldianvl kpalargels ligattlney qkhiekdaal errfqpvfvp
      421 epsveqtivi lrglrdslea hhqvtfadda fvaaaefadr yitarflpdk aidlidqaaa
      481 rvrigatsrp adiqedeaqi vqlkreqdya tsrkrfdqak qfdeqinakq ksldekmeaw
      541 qrktgsetle vtvesvaevv srltgipvse ltqeerqkll kmeeqlrerv igqndavvav
      601 sdavrlsrag lgqthrpiat flflgptgvg ktelakalae tvfgdeqsii ridmseymer
      661 havarligap pgyvgydegg qltervrrrp ysvilldeie kahpdvynvl lqvfddgrlt
      721 dgkgrvvdfs ntiiiatsnl gaaiimdnlt qpeaarktdk aireqlmqvl kghfrpefln
      781 ridevivfha lskenirsiv qiqldrvvrt aaaqditlvm gdalvehlte agyqpefgar
      841 elkrqvrqii etklakeila dklqsgdhve vdydktsdav tfnklappda kdvkdaarna
      901 dgkarpngka akkesdakdd eaknetrapa pvpaakpsgk kssgakkdaq
//
LOCUS       WP_175791725             149 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Burkholderia ambifaria].
ACCESSION   WP_175791725
VERSION     WP_175791725.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..149
                     /product="RidA family protein"
                     /calculated_mol_wt=16558
     Region          28..137
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 msqpthtrir mfntkdtypn qtldndlcqa vragntvyvr gqvgtdfdgn lvglgdpraq
       61 aeqamknvkq lleeagsdit hivktttyli dpryrepvyq evgkwlkgvy pistglvvsa
      121 lgqpqwlmei dviavipdnw qpnraqeat
//
LOCUS       WP_175791729             306 aa            linear   BCT 11-JAN-2025
DEFINITION  bestrophin family protein [Burkholderia ambifaria].
ACCESSION   WP_175791729
VERSION     WP_175791729.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..306
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33908
     Region          1..299
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 mivrprqnwl rmlfvwngsv lqsiipqlvf maivstlavf tngrifgeki plntapftlf
       61 glalaiflaf rnnasferfk earllwgnll iaartvtsql hrylpdsvgd aernrladll
      121 iaftyalkhq lrhtdatqdl qrilgaeraa afahkcyqpv aildelrggi vralgrapgs
      181 datcwmfdaq lvelgravgg cerilttpip fsysvllhrt vyaycvllpf glvdstefft
      241 plicvfisyt lialeaiane vaepfglapn alaldamart iersvlelgd rampeefvpa
      301 styqit
//
LOCUS       WP_175791731             466 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Burkholderia ambifaria].
ACCESSION   WP_175791731
VERSION     WP_175791731.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..466
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51743
     Region          4..440
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 meifdafhla rlqfaftvsf hivfpaisig masflavlew rylvtgdaay ksmfqfwski
       61 faigfgmgvv sgvvmayefg tnwagfsrva gnitgpllty evltafflea gflgvmlfgw
      121 qrvsprahff atlmvavgtl istfwilasn sfmqtpqgyk ienglvvpvd wfkiifnpsf
      181 pyrlvhmtia afivagfiva acgawhllkg rrdepvkrsf smalwmllll apiqivvgda
      241 hglntreyqp akiaaieglw etekggtaln lvglpdmqae ttryaiqvph lgslilthsw
      301 dgeirglkef apqdrpyspi ifwtfrimag lgmlmlltal lglllrkggr lyetrwfqwf
      361 vvcmgpsgiv allagwitte vgrqpwtvyg vlrtvdsvsp ltaqqvgvsl lvfvvvyflv
      421 fgtgiyymmk lmkrgpaaqa gyielhrhpg lrksalstpl nvteae
//
LOCUS       WP_175791754             281 aa            linear   BCT 11-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Burkholderia
            ambifaria].
ACCESSION   WP_175791754
VERSION     WP_175791754.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..281
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=30161
     Region          176..273
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mtaltwcaif laaltaisrl prgltlslla vgyaiafasr qlqpialvpi allvgtgvll
       61 qrnlpfagkv vcnvvfcvia vglfqhwlpg fdnlrvihaa rltpdaapyt mylnfdkpli
      121 afwlvlaypw vlpekplstr viaavvacaa tsavcfsiaw wagliawapk wphfawlwml
      181 dnlllvafae eaffrgyiqa gatrlmraqp nagwlalvag avlfglahyq ggallvllag
      241 lsgigyglay ragglqsavl ahfgvnlvqf glltypfiar a
//
LOCUS       WP_175791771             295 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175791771
VERSION     WP_175791771.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..295
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=31578
     Region          3..290
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 msfegvhtpl vtpfdtdgei dhallgrhaa dlagrvsglg iggttgeyya lsfdervrtf
       61 dtvaaaaggk tfltaginat ttkevlrlgr eakraglnal lvaapyyaqp tqqellahll
      121 avddaldmpi mlynfpartg teigddilat llerknfvam kestgdiahl hhlsthfggr
      181 lvlscgmddq aleffawgar swvggasnfl peahtdlfda cvkrgdlatg rklmaqllpv
      241 lellersgkf iqyvrygcel aglpvgvara plgalsgaer dafvklvkpl lrdar
//
LOCUS       WP_175791864             341 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175791864
VERSION     WP_175791864.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12168325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37994
     Region          31..203
                     /region_name="AraC_binding_2"
                     /note="AraC-binding-like domain; pfam14525"
                     /db_xref="CDD:434015"
     Region          247..334
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mgqfagtgwl gdaacfnhdt lvlqsndlde vrarvadvfk phrltltgds calhsrmhha
       61 rwgnlslnll dyggevsiep gplehfyllq iplrgdaeie cgttrfvssp dtasllsptl
      121 plrmrwgeac pqvilriere vmerhaqrhf gddrrvpvef epefrlsspq gaclaqmlpm
      181 ladaiatdgh plrhplafeq lestllnlll ygqpnsarng arvapaplap fyvrrveeyi
      241 rthvdeplti erlaelagvs pstlfagfrn rhgitpmafv rqlrlqhvrd ellddatpgl
      301 asvtdvalkw gfahlgrfai dykrafgesp satlrmrrvr g
//
LOCUS       WP_175791871             909 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia ambifaria].
ACCESSION   WP_175791871
VERSION     WP_175791871.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 909)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..909
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..909
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=97830
     Region          53..909
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 maihvpvtrr tflklagsga vvavsvthlp avvlaagdtq adangpnwap vpgkarwrid
       61 gmpkvtgqki yardfkardf vgwpqrenwl yalrcdrvda vyqgydlsvl ppelrpiaiv
      121 dsallsarri plapepdpia nqdiywlarp ghpadcygqp aallifenfd vyrrakklld
      181 fnrsviryga stgagpaapv vpylpvtvyv rdderrfnyv dnyqtdsngk psakyleere
      241 aavanidati arqaaagawi gvratgddgf qtpaidpmfm epesglawyd tsaakmslvl
      301 gtqsanddat gacalfdgsd iavkeahvia cypgggfggr dksyfplyla laapfakgal
      361 rwqqsryeqf qvglkrcetq fseslwfdrr gkleaitcdf llngggkknl spyvaqlaal
      421 samscyeipr araqaastyt revfggsqrg fggpqafmai etlmdeaarr lglspfeirr
      481 anllgkapgp gkaraitgap ilfdlqldal ldrlerhplw lerehtraer narnlrygvg
      541 lamaneaygt sgdgmfgmvq ilpdgnlrvi tpytdmgnga attlglapae flgqnaqtia
      601 mseiapfnal gltpkgpssa pnwvryyygs ssaclgafhq fhavkgaaqa lflqsvlpaa
      661 rarwgvnvra advrwvdrtl vangltpipw pvllgtigkl glqtvaavha syagyfwkgt
      721 ypfasgsaqi dydyvavgld pyrlaplqrv lqpppvntsl ygrttyapsa tlvavavdpa
      781 tgrvkvehvv tavsvgrqls pelvegqsqg avamgignvl tetcplgpdg pgggrwnldr
      841 yevtrlpdip vqelialppp agdpanargi aeavmcpiap allnalamat grrfrvtpvt
      901 pekirealq
//
LOCUS       WP_175791873             325 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia ambifaria].
ACCESSION   WP_175791873
VERSION     WP_175791873.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..325
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=36223
     Region          110..316
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mdsiyygfvi ltfvavvlai egvyqwwnar hgaaarries rlramsaggs vqqerlsilk
       61 krmldeskpf drllmrvpri qaldlvlqqs glnwtvaklv visavlpvta alvlavsplp
      121 livvlpiall tacmpamyvm rhrnrrmlkl erqlpeicdm iaralrsghs fssalgmvge
      181 efpdpmggef ritfdeinyg vslhdalvnl atrvpahdlr yfviavliqr etggnlaell
      241 dsiaslvrer fklfdkvrvl saegrlsawi lgllpfgtaa mmamvnrefl svlwqdpagi
      301 kmvgvmlgsm afgllwirri irirv
//
LOCUS       WP_175791897             462 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175791897
VERSION     WP_175791897.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..462
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48793
     Region          24..430
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,152,
                     155..156,159,265,268..269,272..274,277,304,308,358..359,
                     363,367,383,386..387,390..391,394)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mantvnaagr ldrlpvsrfh wkilgliagg afldafdiyl angsvasmvk dgftdlrhga
       61 mfvsstfvgm migafvagyv gdrlgrrysy qlnlavfgla siaacfapdi ewlivlrfim
      121 giglgaelvv aagtlaefvp petrgkwvsl laiitnsglf aalaagywii phlgwrymfa
      181 lagigalvvw fmrkrmpesp rwlesvgrld eaeatlaaie qevskqvgal ppvrrtidlh
      241 vgkvplgvlf skgmrgrmav aaltaigvnv glygfiawlp tffvtqglsv vkslgfvflm
      301 sigspvggli gyliadrigr argiviasil sialgwlyvs lrdttaiilv gfclvsaiyt
      361 ittlglfgyi pelfptevrl rgtgvagmcg rmssigtpal alalyqafgv sgviamvsat
      421 lgvlcvaigl lrvetgrqal eevapgtsda dgaavaprvp qv
//
LOCUS       WP_175791915             310 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Burkholderia ambifaria].
ACCESSION   WP_175791915
VERSION     WP_175791915.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..310
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31439
     Region          2..310
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtilviaehd nasikaatln tvaaaakigg dihvlvaghn aqgaadaaak iagvskvlla
       61 dapqleagla enveatalni akdyshilap ataygkniap riaakldvaq isditavdsa
      121 dtferpiyag naiatvqssd pikvitvrat gfdpvaaegg sasvekieaa adagksqfvs
      181 revtkldrpe ltsakiivsg grglgsgeny tkvlepladk lsaalgasra avdagyvpnd
      241 yqvgqtgkiv apqlyiavgi sgaiqhlagm kdskvivain kdpeapifsv adyglvgdlf
      301 elvpevvdav
//
LOCUS       WP_175791957             310 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175791957
VERSION     WP_175791957.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33972
     Region          14..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,232,249,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,195,
                     226..230,237..238,241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mrssseklsg sisvfaavvd mgtfaaasev igmtppgvsr aiarlekkln irlfnrttrs
       61 vslteegrrf yeqvmphlag leeaaaaaag sasavrgklr vnldpvvyrt ilgpqldafm
      121 dahpeleiel iardslgdlv mdgfdiavrf geprastlia rklldtgivt vaspayiarr
      181 grpakpedle srshrciefr npetgkpfaw efhrrrkriv vdtrgrltvn dpgallnacl
      241 agsgiaqmll lgaepliang qlinlfpewa derfplyayy psrhhlpakt rafldfvvel
      301 mgnherggar
//
LOCUS       WP_175791970             395 aa            linear   BCT 11-JAN-2025
DEFINITION  YncE family protein [Burkholderia ambifaria].
ACCESSION   WP_175791970
VERSION     WP_175791970.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..395
                     /product="YncE family protein"
                     /calculated_mol_wt=41361
     Region          48..268
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mhsnsfrlrr arllaaltla ttavaahaad wivsgndgky qrvegrdtfl asppadtltl
       61 ldasvfppkv alqvdvengi qgppqavait pdaklalvga ptrydpgakq lvydtflqvv
      121 tldaspaait ridlgthpqg iaidrsgrva lvanvdgsvs ilridgtqvt ldgnlkigkk
      181 rlagisfthd gkhalvslrd eqgvavlnvd dgkvtdsgar lstgvapyti dvssdnhwav
      241 vsnvglaglp gytgtlagda dsvalidvsr tpfrtvqyln vpslpegvai spngkwiavq
      301 amdgsnltad npgrhklgkv vlfeirngra vqtsevpgge aaqgivftad srhvivqfnv
      361 erqlalyave ggqlrdtgmr ialsggpssl rtlpr
//
LOCUS       WP_175791959             319 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175791959
VERSION     WP_175791959.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..319
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34973
     Region          1..316
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mritlialdg vfdtgytaml dalrmansfa aregrqlpfe isvvgvrkkv rtnggllipv
       61 qpitpalmpd wvilpalats tpellipale radvkqavme lrrwheqgak latscigafv
      121 laetgllddr eatttwwlap lfrqrfpkvq leesrmlvpt digvtagaam ghldlalwli
      181 rkaspelavv vsrylladlr ssqaqyiipn hlaqadplvl rferwardhl kdgfslqdaa
      241 savgtstrsl qrrcqailgk splsyfqdlr vehaqallhg gmdleaaaaq vgyidgatlg
      301 allrqrtgrg vrdlradlr
//
LOCUS       WP_175792020             596 aa            linear   BCT 11-JAN-2025
DEFINITION  polysaccharide biosynthesis/export family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175792020
VERSION     WP_175792020.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12809731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..596
                     /product="polysaccharide biosynthesis/export family
                     protein"
                     /GO_function="GO:0015159 - polysaccharide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0015774 - polysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=63428
     Region          127..291
                     /region_name="Wza"
                     /note="Periplasmic protein Wza involved in polysaccharide
                     export, contains SLBB domain of the beta-grasp fold [Cell
                     wall/membrane/envelope biogenesis]; COG1596"
                     /db_xref="CDD:441204"
     Region          <496..>546
                     /region_name="Wza"
                     /note="Periplasmic protein Wza involved in polysaccharide
                     export, contains SLBB domain of the beta-grasp fold [Cell
                     wall/membrane/envelope biogenesis]; COG1596"
                     /db_xref="CDD:441204"
ORIGIN      
        1 minlstgrka lialmlgaas tagwaglsdt lfglsgtdsd sgstssraaa dggqrgaast
       61 gfgynpddva agammlqggk vshqqggpgg mapspvnvsv apqapnsmfg sqlfggtfhn
      121 srgtgfnpay qvgigdtvtl rmwgafvfdg qltvdpqgni fvpnvgpvtv agvrnadlng
      181 rvlnevrkvy kanvnvytsl dvaqpvkvfv tgyvkqpgmy ggiasesils yldkaggvdv
      241 drgsyvdvmv krggavrkrf nlydfllnge idqlqladgd vivvgprehv fsvrgevyna
      301 ydfefatpvi tlqqalavar pkpgathvsi vrrqgtertt eyypisnasn vrlndgdqla
      361 vtsdryagti qvrvegahsg ehalvlpygs tmaqvlsqvr knplsrvdea qlfrksvadr
      421 qkemlgvelq klqeaalsap satseeanlr skeaenitkf aalasktefk gqvvlneqtm
      481 gnviledgdv inipertsvv mvhgevlfpn avewqsgmtt sdyvahvggy tqkadnskii
      541 vihqngkael adsgtkveag delmvlpkvr sksieitrgi tqilyqmava aklifw
//
LOCUS       WP_175792075             401 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia ambifaria].
ACCESSION   WP_175792075
VERSION     WP_175792075.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..401
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=42097
     Region          8..401
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 mhapphetrf awrgrrrdgt pcrgniiafd taaaraalar dgvavlsldi rgtarppaag
       61 trevtrftrq lasllqaglp lapslemlar trtrdglpri aaglareivg gqrfaaalar
      121 ypsqfgtlyr qlievgeasg algvvltrva ehreradaqw rklcaalayp vavivfalai
      181 saalmvwvvp tfrqifdgfg aalpaptral lalssatsaw ggmfvagtav aglgarhalr
      241 rspslrytaa rhvlnaplvg saltrfaaar wcrslatllg agvpladafa tlertaghpv
      301 feqataqiaa rvlrgarlad amhaagcfpd dvvqpiavae etgaldtmla diaalcerql
      361 derldalaal geplivivlg alvgglviam ylpilqlgnv v
//
LOCUS       WP_175792093             310 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175792093
VERSION     WP_175792093.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34214
     Region          13..>176
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          98..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(108,112,151,165,167,232,249,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(109..110,114..115,117..118,121,125,127..133,194,
                     225..226,228..230,237..238,241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mqrkfddlll gsielfclaa elgsftlaat aasvtpaavs rsvarleerl gvrlfvrttr
       61 qirltdsgrr yfeqcrdals qlvdaereat gqqatpagvl rismptpygh yrvlpllpaf
      121 rdrypdvrve thlsnrnidf aeegfdlair grapadsslv arkledaelv vvatpgylkr
      181 agvpravddl haheciqfel pssgrpipwl fndgaaeiei attggygtsg dvlagvtlar
      241 sgaglfqtyr fiverdlrdg tlvevlsgqg grsrpfmlly pharylssrv rvfvdflveh
      301 leqapdkrkr
//
LOCUS       WP_175792097             241 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia ambifaria].
ACCESSION   WP_175792097
VERSION     WP_175792097.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..241
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26008
     Region          152..236
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mreataghee ggshpldnav whalageqhr falgdvrarr fpsalapfag madrspaafd
       61 alrglidayg paalfspdei ptpaglsvvr ratlhqmiwq gtlddmdpse hvplteadvp
      121 emlaliaate pgpfgprtie fggyigvrrq grlvamtgqr lrasghaeis avcvdpafrg
      181 qglaaglirs liatiraree tpflhvltsn hvaieryral gfvtrrdmhl lvleraqtrt
      241 d
//
LOCUS       WP_175792101             485 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175792101
VERSION     WP_175792101.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..485
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51754
     Region          56..465
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(66..67,70..71,74,108,158..159,161..163,166,186,
                     189..190,193,305,308..309,312..314,317,344,348,397..398,
                     402,406,422,425..426,429..430,433)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mnsqsldlgg taggpasavp paaragtdat alparaitlg efmddlpvga lhrfvvwvig
       61 iglffdmyei flvstigsal qneyglsrqs adfklllasa figmfvgamc lgsladrigr
      121 rkaflmtlvw ysafsligaf svnadmlvac rfltgigvga iypvadsfls eilpkekrgr
      181 laawayttsy vavplvcfla lwlnplhvag vagwriilai gslgavyvll iqhrlpespr
      241 wllaqgrtae ahaaarrfae sagvrapeqf aasvepqrpl slgeriallr rrpygarylm
      301 lavfhllqgf gyygfgtlag tvvksrgfdv tdstlfials figypigsll sipllnwier
      361 rtlvivsils iaafglcfay sgntalivcf gflttcasnv fsnayhvyqa eifparvrst
      421 aigstyalsr ivsgalpfvl lpvlvahgag amfgvisval givavtlrvl gplttrrsqd
      481 dinpv
//
LOCUS       WP_175792110             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia ambifaria].
ACCESSION   WP_175792110
VERSION     WP_175792110.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..359
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39413
     Region          8..355
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkhsferlrl dgvcrsftna egaqvaaldg ldldirrgef iallgpsgcg kstalnciag
       61 lqpltrggiw lddtridvlp perrgfgmvf qnyalfphms vldnvgfglk mrgvpkqetr
      121 rraqqalelv qlvghegklp gqlsggqqqr vaiaraivie pplvlmdepl snldtklrie
      181 mraeirriht qleratiyvt hdqdealsma drivvmkegv vqqvaspkdv ytrphnlhva
      241 rfmgyrnvlp ftlegmaddy vnvaaagvri tgvpmagfdg kdvvialrpd dieraepgad
      301 nafdatvetv eyggrdslir aitpfgaiwa rvagefvege rlrlrvppar tlvyagdar
//
LOCUS       WP_175792156             339 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia ambifaria].
ACCESSION   WP_175792156
VERSION     WP_175792156.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..339
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34800
     Region          36..338
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtqppvspsd agaqqdvtgr rartlsgtrl glsnylglag alaamialfs alsshfltyd
       61 tfstianqip dlvvmsvgmt fvliiagidl svgsvlalaa smvsvaalkw qwgplpaali
      121 giavatatgs ltgaitvgwr ipsfivslgv leaargvayq ltnsrtayig dafdflsnpi
      181 algispafli avavmiaaqf vltrtvfgry lvgigtneea vrlagvnprp ykilvfalmg
      241 alaglaslfq isrleaadpn agaglelqvi aavviggtsl mggrgsvist ffgvliisvl
      301 aaglaqigan eptkriitga vivvavvldt yrsrrvrar
//
LOCUS       WP_175792224             200 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: YbhB/YbcL family Raf kinase inhibitor-like protein
            [Burkholderia].
ACCESSION   WP_175792224
VERSION     WP_175792224.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..200
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=20989
     Region          43..199
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mrvdrritsp acpgrpspfi vavlcaaaci afaaprarae gpftvssdal tpggrvpaan
       61 vfdrgdckge nrspqlswhn pppgtrsyai tifdpdapgh gwwhwavtgi pasvtsvpad
      121 asasgflrri gasearndfg idgyggpcpp pgkphryvit vhalkgtdlr vaqgrpapmf
      181 eheigtltig tarltvnygq
//
LOCUS       WP_175792242             265 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia ambifaria].
ACCESSION   WP_175792242
VERSION     WP_175792242.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..265
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=27253
     Region          47..197
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mnqsrvkqtl vrttllaalt aglamslqgc vlgvlgaaag ggaliatdrr tlgaqtedre
       61 iqvksltqin nglpeqshvn vtvfnrrvll tgevpndask qraeeivrgi nnvsaivnel
      121 svepasslss randsylegr vkseliatkg lsanyykvvs ergniyllgl vtvdegnrga
      181 aaasqvpgve kvvkvfqyik pqdaqalqaa spsnasdaqa aaapadaatv gavpdasvqs
      241 aplqppapis nsssvhpgnp katpq
//
LOCUS       WP_175792241             119 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia ambifaria].
ACCESSION   WP_175792241
VERSION     WP_175792241.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 119)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 119)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..119
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12309
     Region          30..117
                     /region_name="CytC552"
                     /note="Cytochrome c551/c552 [Energy production and
                     conversion]; COG4654"
                     /db_xref="CDD:443692"
ORIGIN      
        1 mksmqirirq wfvqgaaagv laagafgtah advgdglkva rsnacmgcha vdrklvgpsf
       61 kdiaaryksd pqavaklskk vkdggsgvwg aipmpahprl sdadlrsvve wvlagapsk
//
LOCUS       WP_175792245             404 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175792245
VERSION     WP_175792245.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..404
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40734
     Region          31..398
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(41..42,45..46,49,81,131..132,134..136,139,158,
                     161..162,165,233,236..237,240..242,245,273,277,326..327,
                     331,335,351,354..355,358..359,362)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 msesssrsss dfaappdahr tlalpvrqra rtatmalffv agmmyaswgv hvptvrdkfa
       61 lspgllsial favaggsiaa mltiarwiar vgsrtaclvg glvmsacaal ilvvpdywml
      121 lvvlavfgfs matldvamna easaveialg kpimsslhgm fsiggmsgaa aggallsagm
      181 apavhlalaa ainaavllaa ipavlphvph hehahgggnr wrsaalwmlg giallaliae
      241 gamydwatvy mrdvvaaspa lasaayaafs ggmaiarfag davrarfgap qlvfasasla
      301 cagmigalll pnpiavltgf tlmglglanm mpvlfaaaar vkgihaaegl ahvaglayfg
      361 llfgpvviga vaqtanltvg lavvalcaal vaviapkvla hlki
//
LOCUS       WP_175792248             492 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Burkholderia ambifaria].
ACCESSION   WP_175792248
VERSION     WP_175792248.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..492
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52221
     Region          3..487
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mhsdylahda iglaalvrer kasprellda aigqaeavng avnaivlqdy eaarkrtesa
       61 vdagtdapfa gvpylvkdlg aavaglplsm gsrhyryfvp addspliars raaglnvfgk
      121 tntseigqmp ytepelfgac rnpwnldhtp ggssggaaaa vaagivplah asdgggsiri
      181 pasccglfgl kpsrnpvlvd lpsngelvvq havsrsvrds allldvttgq tlppgapgtf
      241 lgeldtppgp lriglvtdpm lapaldddtr aalddaaalv eslghhvepa tlhidyaraa
      301 etfltlwati aeemvlgart itgrtpkrae fepatwamav igrriararl qdvlewqrql
      361 tvqvaglvsr ydvvlcatla gppvrigalq ptpfeaaqmk llgalpvkpl lremlaktse
      421 kafawagcte lfnltgqpam svplywnarg lpigvqfvar htddalllkl arqleqarpw
      481 fdrrpplmqa qr
//
LOCUS       WP_175792263             201 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA-3-methyladenine glycosylase I [Burkholderia ambifaria].
ACCESSION   WP_175792263
VERSION     WP_175792263.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..201
                     /product="DNA-3-methyladenine glycosylase I"
                     /EC_number="3.2.2.20"
                     /GO_function="GO:0008725 - DNA-3-methyladenine glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=22221
     Region          3..187
                     /region_name="Tag"
                     /note="3-methyladenine DNA glycosylase Tag [Replication,
                     recombination and repair]; COG2818"
                     /db_xref="CDD:442066"
ORIGIN      
        1 msqrcnwvrt eadahyhdte wgvpshddrh lfemlilega qaglswstil nkragyreaf
       61 adfdvdavar ftpkhiekll enpgivrnra kvqsavtnal avqrirdehg slahflwsfv
      121 dhmpvqnawq syrdapasta qsdalskalk aygckfvgst icyalmqatg mvndheagcp
      181 chakcaalgg kqqparrrkt g
//
LOCUS       WP_175792286             370 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia ambifaria].
ACCESSION   WP_175792286
VERSION     WP_175792286.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..370
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39211
     Region          85..311
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mtmgmhaapa slalshddal vlpgtllapd gtlvapydie hgsdraegcv paaaalgllh
       61 avhrpfrrdy grasdvhvin gmgvalgdsv igltalaalr amhpgvrftl yrparapryv
      121 ealyalaadv vapsralpya adalpahapc idlgnhlywp afarqpmidf fldalgvdpa
      181 tvpaaakrnr wlarlrlpal paewqrpyvl fcptastavr svppalraaf verlaqrygl
      241 pvvgfgpvah payvdvsrha pdtahfiawv kgasvlfapd taalhvadgf dvptlacftt
      301 igpalrvrdy phcvpveldv paelrglhrs erpedltave aayraidwda lpwpapreaa
      361 aaaaagaaae
//
LOCUS       WP_175792298             222 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia ambifaria].
ACCESSION   WP_175792298
VERSION     WP_175792298.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..222
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24489
     Region          1..206
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mstllhiess prksrsasld vahayldawr dahpehrvdv ldlwathlpe ldgdaldaky
       61 adlsgtplse gqqqvwagfr qlaqrmhdad tllfsvplwn fsipyklkhf idavshrgil
      121 fsyderglag llngkkavvi yargldysrq sstpaesfdf qrpfleawlr figitdiesi
      181 vvektlfgpe idhagreaar eramtlahaa ssssaasasv dg
//
LOCUS       WP_175792307             351 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            ambifaria].
ACCESSION   WP_175792307
VERSION     WP_175792307.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..351
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=36964
     Region          3..339
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mdfsiaaila qdgittgaiy allslalvlv fsvtrvifip qgefvaygal tlaalqaqkf
       61 patcwllfvm giacfmlevg glvrhrerrh qlgrtlatla sryvllplav faltrsfaaq
      121 plpmlaqial tlaivvpmgp fiyrlvyqpi aegttlllli vsvavhfamv glglvmfgae
      181 gsrtngfada slsvgsmtvs vqsilvvvta lvligalyvy fgrtiagkal ratsvnrlga
      241 rlvgigttea grlaftlaag lgvlsgilvg plttiyydsg fliglkgfvg aiigglvsyp
      301 laaagsllvg vlesyssfwa saykevivft liipvllwrs fatphaeeee e
//
LOCUS       WP_175792311             165 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175792311
VERSION     WP_175792311.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..165
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18153
     Region          6..146
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mrsmlmeldh fdlalldvlq rfgrathqql geevplspsq igrrlqrlea agviegyrvm
       61 lrpeklglgv taftslklkh hgdsiieqfq qqidvlpqvl echavvgdad yllrivapdl
      121 nalsqfvmkk lmrvpgvdsv rsnivlttfk rngalplahl apgaa
//
LOCUS       WP_175792352             140 aa            linear   BCT 11-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Burkholderia ambifaria].
ACCESSION   WP_175792352
VERSION     WP_175792352.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..140
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=14472
     Region          35..135
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mtfftdytnl aliaillvsg gllawpalrr grgglsaaea tqlinrrnav vidlraatdf
       61 aaghlpsarq vaageigaki aqvaknkstp vllvcqngqq sqkaarevqa agyaevhvle
      121 ggvaawqqag mpvvkqgvsk
//
LOCUS       WP_175792372             303 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia ambifaria].
ACCESSION   WP_175792372
VERSION     WP_175792372.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..303
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32327
     Region          29..269
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 mnasndpaag aasahtavag tppaaapgdd fvievrnltk rygrniihqk ldfdvrrgei
       61 vaivggsgsg kttlvrqilg lerptsgtik vfgedtakid dasarmmrtr sgmlfqqgal
      121 fssmtvfdnv aqplrelgrv ppdllhdivm lklemvglpc khaskmpaal sggmvkrvgi
      181 araialepel lfldeptagl dpqasdefve liatlhrtlg ltvvmvthdl dtmvalstrv
      241 avladrkvlv aapveeaanv dhpfiheyfl glrgrralqa lpperraklp kaalepalss
      301 vel
//
LOCUS       WP_175792406             163 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175792406
VERSION     WP_175792406.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..163
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17730
     Region          13..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mskrlsppav asldatdrai laalaedari atselarrig lsapatadrv rrleaqgvia
       61 gftveldpra lgytlqaivr vkplpgqlhl veevlrripe fvecdkvtge dcficrlylr
      121 tighlddils kvteraetst aivkstpvpr rlpplvedda arr
//
LOCUS       WP_175792448             404 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent rRNA methyltransferase [Burkholderia
            ambifaria].
ACCESSION   WP_175792448
VERSION     WP_175792448.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..404
                     /product="class I SAM-dependent rRNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=43588
     Region          3..403
                     /region_name="RlmK"
                     /note="23S rRNA G2069 N7-methylase RlmK or C1962
                     C5-methylase RlmI [Translation, ribosomal structure and
                     biogenesis]; COG1092"
                     /db_xref="CDD:440709"
ORIGIN      
        1 mqtvtlkpsk eksllrrhpw iyanaidrvd gkpapgatvi vrahdgrfla rgayspqsqi
       61 rvrvwsfden epidhaffkr rvqravahrt tmvsgtgavr lvfgeadglp glivdyyvad
      121 taeagatprg qlvcqfmaag veawkeaiva altgatgcpn vyersdvsir dkegleqttg
      181 vlagdappat lianengvry hvdvpnghkt gfyvdqrdnr alvaqyaaer dvlncfcytg
      241 gfslaalkgg akrvvsidss gdalalaqqn vvangfdaer atwldadafk tlrrlvdege
      301 rfdlivldpp kfaptrdsvd raaraykdin lsgfkllrpg gllftyscsg aidmdlfqki
      361 vagaaadakv darilkrlga gvdhpllaaf pegeylkgll lqiv
//
LOCUS       WP_175792454             870 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia
            ambifaria].
ACCESSION   WP_175792454
VERSION     WP_175792454.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 870)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 870)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 870)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 870)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..870
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..870
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=92582
     Region          44..861
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mranhlilnp eaparfalkp gylfvmaalg swaagacade tpgasaegfq vaqvqfndtl
       61 mmkprgqrld ldrfakgnpv pagdylvdly vnetwtgrst vrfnaaagav natpcfdral
      121 vgrlglddqa ltdsaraelv rvqagectdi dklvadatvv fdmsdlrlnv sipqasllrn
      181 prgyvspelw dggvpsatlk ynanvfrnts sgyestqgyl glnagvnvgt whlrhngtys
      241 aqtrgdsryq slntyvqhdl pawrsqlkig etytdgtlfd svgmrgatle tddrmlpdsm
      301 rgyapmirgv atsnahvsvs qngavlyetn vapgpfeidd lyatgyggnl lvtvteadgr
      361 khsftvpyaa vvqslrpgis rfgialgqlr epqlnrhpnf aqatyqrgis nlmtgyvgai
      421 vaenylaglv gaafntplga lavdvthasa ripgvsatsg qsvrvsysks vdatgtniav
      481 aayryssrgy wgmrdamyar emsaagmdpn nvyrqrnqvq ltlnqslgek rgslfavgss
      541 vnywnrqgtt tqfqlgynnn lrllgvnlsy nlsvsrqrdg ysgrlnnqvf anltvplgrr
      601 syaptlstgi ahdsqggtte qmaltgtvgk saalsygvnv nsssgatsgg gnvqyrspwa
      661 tfsgsasggs gyssvsagvs galvghaggv tlanelgdtv aiveakdavg asitngtdvr
      721 idrrgfavip yltpyqmnti eldpkgipid vemqstsqqv apransvvkv kfgtttgrav
      781 lltirqpdgt pvpfgstvad adgnaigwsg qggtlftrdl kdsgvltakw gnrtadactf
      841 syslpiersk haayeriesk cdyslnksrp
//
LOCUS       WP_175792456             180 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia ambifaria].
ACCESSION   WP_175792456
VERSION     WP_175792456.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..180
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=17776
     Region          21..180
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mkfalssiaa ltvvaaatlp avshaadgti tingnigtqt ctidgngtgg kdftvalpkv
       61 sttalatgga tagrtpfkig lkncspasgn vythfepgtt vnattgqlln atgtaknvev
      121 gllngdstni gvgkadensk svalsngaae lpyyaqyvat ggpagqgtvn tsvmysimyq
//
LOCUS       WP_175792539             795 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia ambifaria].
ACCESSION   WP_175792539
VERSION     WP_175792539.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 795)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..795
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=86988
     Region          23..743
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mqstsptspp pppepkkrpw wqkaligvaa mcvalvvagg lvlgyalvva wpnmpsldal
       61 tdyrpkvplr iytsdhvlig efgeerrdiv hfkevpdslk kailaiedar fydhggvdlt
      121 giaraglval tnghasqgas titmqvarnf flssektytr kiyemllayr ieraltkdqi
      181 levymnqiyl gqraygfasa arvyfgkdlk ditlgeaaml aglpkapsay npvvnpkrak
      241 vrqeyilqrm lelnfitreq ydeaaaqplv vkgagrefsv haeyvaemvr qmmyaqyree
      301 tytrgfnvvt tidsadqqva ytalrkgimd yerrhgyrgp egfielpaga ddreqaidda
      361 llehpdngel iaavvtaatp rqitvafidg statiegdnl rfasgalsan aqpnrrirpg
      421 aivrvvknda gkwsitqlpq vegafisivp qdgairslvg gfdynknkfn hvtqawrqpg
      481 ssfkpfiysa sldkglgpat vindgplyfs aaetggqpwe pknygggfeg pmsmrtalqr
      541 srnlvsiril nqigtkyaqq yitrfgfdad rhpaylpmal gagqvtplqm agaysvfang
      601 gfrvnpylia evtdpngaiv araqpliaeq napraidarn ayvtnsllqs vaqrgtgart
      661 nvlkrtdlag ktgttndshd awfagyqhtl aaiawigydn prslgdretg gglslpvwie
      721 ymgaalkgvp efkptmpddv qsiggelyft eftpghgfvs tvgvpqapav qdteepvphv
      781 deqekqdimn lfrgh
//
LOCUS       WP_175792566             739 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia ambifaria].
ACCESSION   WP_175792566
VERSION     WP_175792566.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..739
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=78278
     Region          70..>204
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          212..732
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msrglieagr agagvsrrsf lkagmslgaa aggglllgfs mpaagddarr sviggdaden
       61 aragvfapna fvqidrsgkv tlvmpkvemg qgvytalpml iaeelevpls nvtldhappn
      121 eklfldpllg gqltggstsv ryaweplrra gatartllva aaakqwnvdp ascraengev
      181 qhapsgrras ygqladaask lpvpkdvalk qpadfkligk pvkrldspek vdgtaqfgld
      241 vrlpgmlyav ivnspvfggt vasvdetaar kipgvrqvvr vdnavavvgd htwaakrgas
      301 alvvkwnega dakvstkdiv adlaqaaang kgavarkegd vgrafanakt rvdavyeqpf
      361 lahatmepvn ctvqvradgc eiwvgtqvpt rardtvqqlt glapekivvh nhllgggfgr
      421 rletdmigqa vkvakqvnap vkvvwtreed iqhdmyrpyy ydrisaglda ngkpvawqhr
      481 ivgssiiarf appafkngvd pdavevaael pydlpnqlvd yvrqeprhip tafwrgvgpt
      541 rgtfvvesfi delaaqtktd pvqyrralld ktprarnvld vatkaagwgt slpkgqgrgv
      601 svmhafgsff sividvavee gevqvkrvvc avdcgmavnp stieaqvqgg iifgitgaly
      661 geitiedgrv vqsnftdyrm mrinetppie vhlvksaeap ggigepgtaa taaalsnaif
      721 aatgkrlrkl pvgsqlkta
//
LOCUS       WP_175792572             167 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia ambifaria].
ACCESSION   WP_175792572
VERSION     WP_175792572.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..167
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17289
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mysnilvald gsdtssrald aaltlawdth arltpvyivd flvpaydaag ydpsilidaf
       61 rdeglrvtad aatrmkargv agtpqianva pagedvaqri vgfageidad livlgthgrr
      121 gfrrvvlgsv aervlrhatc pvlmiparca agasagtaaa stekeps
//
LOCUS       WP_175792573             156 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia ambifaria].
ACCESSION   WP_175792573
VERSION     WP_175792573.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..156
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15905
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 myqrilvald gshsarlald eaislarhsg grviatcvvs dalrpasvdn gdvdqrdstg
       61 ldaknaatai sdaeaafrrs gvrgiartid acgagisdvl ahaaaecdad livmgthgrr
      121 glrralvgsv aeslvriadr pvlvvregpg pgadls
//
LOCUS       WP_175792597             472 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia ambifaria].
ACCESSION   WP_175792597
VERSION     WP_175792597.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..472
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=50748
     Region          83..470
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mtarpafpsp dasgaaaprs parvlcraaf algaavlgyg afaiafpart paaigdvvad
       61 wtganphpvv lqrpaaqpls avaqlgralf adpslsasgk qscaschspd haygppngld
      121 vqpgglamtq qgyrpppslm ylyrqpnfsi gpdagendaa psvaqqaaaa agvvktqkva
      181 gtsaapqlvp qggmfwdgra dtlqqqafgp llnpvemana svddvarkla qsshraqfeq
      241 lfgarvfssp qllvseamfa iaryqvedps fhpynskydr wlegrarltr aelrglrlfn
      301 dpdkancagc hlsrpgkdgl ppmftdyqye algaprnral aqnrnpafhd lgvcgpfred
      361 lkdqtqycgm fltptlrnaa trqvffhngv fhtldqvmaf ynersispqk fyargadgkv
      421 deyddippqy ranvdvtdap fdrkpgdkpa mteqdikdiv aflgtltdep ar
//
LOCUS       WP_175792613             217 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia ambifaria].
ACCESSION   WP_175792613
VERSION     WP_175792613.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..217
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23185
     Region          1..214
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msfrlylsfl aasavliyap gpvnlltmnq alrtgwrral pcvwggtlav llqlaltalc
       61 lnslvhldeh altvlrwaga aylvwlgckq wlsrapatas aapaasaetg iaapdtdtgr
      121 alfwrgvats glnpktllff psffpqfivp nadwslnaqf lllaatfall faggvasmal
      181 fshrlsralr rparmramnr vtggllvgmg aimvgwn
//
LOCUS       WP_175792621             356 aa            linear   BCT 11-JAN-2025
DEFINITION  AI-2E family transporter [Burkholderia ambifaria].
ACCESSION   WP_175792621
VERSION     WP_175792621.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..356
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37774
     Region          35..355
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mrvhvsqsqd saarpraqqi aravlyaall llalwvirdf lpaiawacvi aialwpllkr
       61 lesgrwfrnr ptliatvitv gvsllvilpv alalgqaiaq ehdlrmwlqs vqdngiplpd
      121 viarlpygaa qvtewwqanl ghplhagaam hgasgekfia fgrqfgtkla halfefgfml
      181 vtlfvilrag hklsgallhg arrafgpggg eliermvaav ygtvtglvvv glgegailgv
      241 ayalagvpha allglvtava amlpfcapiv fcgaalwlfv qgatvwavvv lvvgfvvvfv
      301 aehfvrpvli gsstrlpfll vlfgilggae tfgliglfvg palmtvltml waewva
//
LOCUS       WP_175792646             216 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia ambifaria].
ACCESSION   WP_175792646
VERSION     WP_175792646.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..216
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=23519
     Region          3..144
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
     Region          132..>215
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mktdkqlkqd vqdeldfdps idstrigvev tdcivtlsgh ppsyaeklai eraanrvagv
       61 kalvvdmtvh lpdddvrtde diakamrsvl hwtvglhdda vkvqvergwi tlsgkvdway
      121 qshlavrsis qmrsvtgvtd hiavqgtiga ddigsnikra imrhaerear hiaidvhdgt
      181 vrlsgkvgsf serkavrgaa wsargvravv ddlvve
//
LOCUS       WP_175792693             370 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia ambifaria].
ACCESSION   WP_175792693
VERSION     WP_175792693.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..370
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39408
     Region          4..344
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,233,300,320,322..324)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,181,184,186,233,240,300,320,
                     322..323)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,181,184,186,323)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            186
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mssllstydl rglplpnrvv mgpmtrsrap srglptalma eyyaqrasag livteatnvs
       61 htsaafeltp glvtdeqasg wkqvtdavha nggrifaqlw hggrvssltl lggdaplsps
      121 ginddleqlq vwarlqngyy tkihatpsra mttaevaatv ddfgraaara maagfdgvei
      181 haangylphq flsstlnrrd dryggsvanr arfleeivda vgdvmplsrv gvrispyaqy
      241 nnvrdadpda tyayvgrmld eagvaylhaa dtngwsgepd lpriiehtrk tfsgtlivng
      301 gitpdaanal idagdadlva farayianpd lveriathap lavpksigwy ggeragyvdy
      361 arhdtaapia
//
LOCUS       WP_175792654             465 aa            linear   BCT 11-JAN-2025
DEFINITION  SLC13 family permease [Burkholderia ambifaria].
ACCESSION   WP_175792654
VERSION     WP_175792654.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..465
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48838
     Region          102..461
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 msggalggpg rgagmltggr vtaallaagl asvaalgarg tlsagdariv aivftcivlw
       61 atgavaslwv sllffflaat ctavptaeif sgfgssafwl vfsgaaigfa lkesglseri
      121 gialarrigg sylkallafa ilsfllslvm pstfgriail vpiaigycdv vklgahangr
      181 rgilllvivg syelaaavlp anlpnvimag ileqshgmhl rfseylllff pagvivrgav
      241 lvlaswwlfa dtvgeveipa arvalgrrew haimllaitl afwftdavhr iapgwvglgf
      301 alvyfgtspp aqlerftatl kmdllwfiaa iigltalvnh ldvrvpdtla ldalrdspml
      361 vyfaltalsi vvcfavtsna epalyvpivs rllaqglhlk agllaqvmgy attvlpyqsp
      421 pivfgnalaq ldrgavlryc iatallgvvf vipvnalwwr ligll
//
LOCUS       WP_175792663             594 aa            linear   BCT 11-JAN-2025
DEFINITION  GspE/PulE family protein [Burkholderia ambifaria].
ACCESSION   WP_175792663
VERSION     WP_175792663.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..594
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=63242
     Region          106..576
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 msssptppgk tptsvtplil sravkpietd psvtqgqpaa pagpalapva rprepvlsav
       61 aaaaaasvqp aqtasqsqpp gqalplaava rplsdsgefa aseeerkflc llddgtllva
      121 eghemnpfvl sycarlerln chyttrlvtl dairrsyqgp rrdgsaerid htrmqvlakn
      181 liaracdera sdihirvnrf steilfrihn elvriseqtr eygerllatl yaamssvsdn
      241 tykpnerqda aigdrdklpd rlfgvriata ptsvgsvmvl rllyndagea taltelgftv
      301 aqanafella qqphgmniis gptgsgkstt lqrvltkqlr emagsihvit vedpveypie
      361 gavqtpvvna pteearslaf aaaianamrl dpdtimigev rdrasaqsal raamtghqvw
      421 ttvhangala ivdrlvdlgl piamvtdesl vtglisqrla kllcphcsrp laeamaqldm
      481 glvarvkrav garfdavrva gpgcphckng tvgrtvvaev vrtdatfcel lragrkpdaq
      541 aywlselagq tvaqhalekv aaglidprma ervvgpfmpg sggrpqplgs gygt
//
LOCUS       WP_175792732             278 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia
            ambifaria].
ACCESSION   WP_175792732
VERSION     WP_175792732.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..278
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30689
     Region          114..273
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mlpdvnsshr dtdrfnvsfk algelietvg tphfvprlaq llndvvpldv ahiersrvdg
       61 amptgyrcew igssgigaet dtaeisdvmt lyyerffdsd plfaglrgkt gtmlvvrdia
      121 aippgefrqr lfddvrighe cvlargtrya qhsialergr drppftlaem srfrsisdvl
      181 fpllelhast taarriahpt pdvhplaqfd ariasdgvkl skreyetckh lisgktvpet
      241 aeilgvrvas aesyvkrafa klgvrtkrel aawgafvg
//
LOCUS       WP_175792776             230 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator transcription factor [Burkholderia ambifaria].
ACCESSION   WP_175792776
VERSION     WP_175792776.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..230
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24886
     Region          13..208
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mnealhstpd asvvalvddd eavrdglall lhsvglatrc yadaqaflvd addaalgcvl
       61 ldirmpgmsg ldaldelrar rdlpaivmtg hgnidtcrra fkrgaldflr kpvdddelid
      121 avqqairrha aqreqgahgg adtaraaria tlsarerevl dgivrgwsnk eiarelglsp
      181 rtvetyranv fdklqaaslv elvreyaafa gaaslwrvhd asvalrrrnp
//
LOCUS       WP_175792781             240 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia ambifaria].
ACCESSION   WP_175792781
VERSION     WP_175792781.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..240
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25373
     Region          136..237
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(139..140,173..174,177,181..182,185,227,231)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mkistlllra asigaiamal gacttqsglt ydiravsipg kpdnvfrvsc dgllgsanac
       61 araaeefcqg kgftplemid rvysrapvkd preitficgk pqpvpvaapv aqpqpqpala
      121 pqpvpqrqvl lqgdanfald saalspqarn qldrfieinr gvefrhvtvt gftdstggkt
      181 hnlalsasra rnvmsylssn glkaqsfqse gmgaadpvat nataegraqn rrveiridar
//
LOCUS       WP_175792822             260 aa            linear   BCT 11-JAN-2025
DEFINITION  TatD family hydrolase [Burkholderia ambifaria].
ACCESSION   WP_175792822
VERSION     WP_175792822.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..260
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28953
     Region          2..257
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mfvdshchin fkgladrlpa vlenmrehdv thalcvsvdf etlpdvlaia qahdnvyasv
       61 gvhpdhedar eptlaeliel aahpkvvaig etgldyyrle grsiadmewq rerfrthira
      121 atatmkplii htrassedtl rimaeeradv pggvmhcfte pwpvaerala qnfhislsgi
      181 vtfknatdvq dvarrvpler llietdspyl apvpyrgkpn epayvshvgr fiasergiav
      241 ealadattqn ffrlfkiars
//
LOCUS       WP_175792805             643 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Burkholderia ambifaria].
ACCESSION   WP_175792805
VERSION     WP_175792805.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..643
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=69672
     Region          6..636
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mpyavpqaqh adrvlgalag rlpapadsar lvsswqrsle ryaldpassi gprvltaael
       61 revrdkeeaf lrasgqcltr lhemirvady cvmltdahgv tidyridrer rndfrhaglh
      121 igscwsesee gtcgvasvlt dlapitvhkt dhfraafttl tcsaapifsp ggeligvlda
      181 savqspdgrd sqrlvyqlvr qsaaliedgy fvhstaqhwi lfghpnrhyv eaqpewliaf
      241 decgnivaan rqardalpal reprhideif datemplrda arldaivalr lratgaplya
      301 rlraplrrag retgtaraas asrrpgttqr hvgaltpflh ssdtrvaqqa elalrvaskr
      361 lpilvlgetg agkevfarai hdagarrarp fvavncgalp ealieselfg yaagaftgar
      421 khgargkial adggtlflde igdmpltlqt rllrvladge vvplgsdtpv rvdldvicat
      481 hrdlarmvad gtfredlyyr lsgatfelpp lreradvgdv iatvfaeeaq atghvltldp
      541 tlaaqlaayp wpgnvrqlrn vlryacavcd aacvtrrdlp adlaaqlgag pagalpdder
      601 grivaaltah rwrpdaaaka lgisratlyr riakhrivap hri
//
LOCUS       WP_175792821             391 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Burkholderia ambifaria].
ACCESSION   WP_175792821
VERSION     WP_175792821.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 391)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..391
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41774
     Region          4..386
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 mtalntlaia nyrslreliv plaalnvvtg pngsgkssvy ralrlladta qgrvipslar
       61 egglpstlwa gperfsraml agdepvtgtv rtgpvslrlg facddfgyai dlglpvpsrs
      121 qfaldpvvkr eciwggalpr pstllvdrqg aqirtrtasg dwrtipqpva sfdsmmtefa
      181 dptgapemia vrerirswrf ydhfrtdaqa parqshigth tpvladdgad laaalqtire
      241 igdgaaldaa iddafpgasv eidnpggrgr fdvlmrqpgl lrplaaaels dgtlryllla
      301 aalltprppa lmvlnepets lhpdllpalg rliaqaarrs qvlvvshaar liatlereag
      361 ceslvldkql gatalvdadt rnlpawkwps r
//
LOCUS       WP_175792840             255 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia ambifaria].
ACCESSION   WP_175792840
VERSION     WP_175792840.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..255
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=27459
     Region          3..235
                     /region_name="ArtM"
                     /note="ABC-type arginine/histidine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4160"
                     /db_xref="CDD:443325"
ORIGIN      
        1 mnfsltflld tvmpkllaav pttlalllls giasvvigip lalaagsrha pyrwpargwi
       61 mlirgtpllv qlyllyygfg qivprewmrd slaspllrda ywyavvalsv negayvatil
      121 rgaiagvpvg eieagyaygm tragvlrriv gpralrlalp altgeailll kstvlastvt
      181 vfdvmgtant lrfetlrvye plagaaivyv vlvalltipa ahlekhlnry ltrvpddrip
      241 arrrgtssga waapn
//
LOCUS       WP_175792841             244 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia ambifaria].
ACCESSION   WP_175792841
VERSION     WP_175792841.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..244
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=25511
     Region          6..244
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 maaddsllal lafgdggygr ifasafaltl gvaaasfgag tllgiagalg klsrhaslaw
       61 lariyttlvr alpellclll afyavapale avlhrigvvp dgfafdpfiv aalslgfiqg
      121 ayltdifraa lvnvpvgqie aahaygmspw qtltrvrlpi aarlalsgvg nvwlnatkda
      181 sfisvlgsft dllkasqlaa gatrhyvffy lvtaalflvm sitstglfal leryanrgtr
      241 rasa
//
LOCUS       WP_175792873            1052 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia ambifaria].
ACCESSION   WP_175792873
VERSION     WP_175792873.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..1052
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114827
     Region          11..1032
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msgpreegrf nlsawalrhq alvvyliala tlagilaytr laqsedppft frvmvirtfw
       61 pgasarqvqe qvtdrigrkl qetpaidflr sysrpgesli fftmkdaapv kdvpetwyqi
      121 rkkvgdigyt lppgvqgpff ndefgdvytn iwtlegdgft paqlhdyadq lrtvllrvpg
      181 vgkvdyfgdp dqrifieadn tqltrlgisp qqlgqainaq ndissagvlt taddrvfvrp
      241 sgqfdnvtai adtliringr tfrlgdlatv krgyddpvvt qmrtagpgan ghavlgigvt
      301 mqpggdvirl gkaldaeskd lqaqlpaglk ltlvssmpha vahsvddfle avaeavaivl
      361 vvslvslglr tgmvvvisip vvlavtalfm ylfdiglhkv slgtlvlalg llvddaiiav
      421 emmavkleqg ysraraaafa ytstafpmlt gtlvtvsgfl pialaksstg eytrsifevs
      481 aialiaswfa avvlipllgy hllperkkha heahlpddhe hdiydtrfyq rlrgwvdwci
      541 errfvvllit galfvvalmg fslvpqqffp ssdrpellvd vrlpegasfa atlreterle
      601 kildkrpeid hsvnfvgsga prfylpldqq lqlpnfaqfv vtaksvkdre klatwlettl
      661 rdqfpavrwr lsrlengppv gypvqfrvsg ddiatvrsia ekvaatmrgd artvnvqfdw
      721 depaersvrf eldqkkarel nvtsqdvssf lamtlsgttv tqyrerdkli avdlraprad
      781 rvdpaklagl alptpngpvp lgslgrftpa leygvvwerd rqptitvqsd vragaqgidv
      841 thaidgklnp lraqlpvgyq iniggsvees akaqssinaq mplmaiavft llmiqlqsfs
      901 rvlmvvltap lgligvvgtl llfgqpfgfv amlgviamfg iimrnsvilv dqieqdiaag
      961 hgrldaivga tvrrfrpitl taaaavlali pllrsnffgp matalmggit satvltlfyl
     1021 palyaawfrv krderdphep phdgppaaps ga
//
LOCUS       WP_175792916             557 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Burkholderia ambifaria].
ACCESSION   WP_175792916
VERSION     WP_175792916.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60340
     Region          25..384
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          453..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mtpaslieqy gpresmeydv vivgggpagl saairlkqla aekgteigvc vlekgseiga
       61 hilsgavmdp raitelfpdw kergapldva vtedrflfls ensavttpnw alpanfqnhg
      121 nyvislgnvt rwlgaqaeal gveifpgfpa aeilynddgs vkgvatgnmg vgkdgepten
      181 fqlgmelhak ytlfaegcrg hlgrqliskf kldanadpqa ygigikelwe idpakhkpgl
      241 vihtagwplk sdtyggsfly hmdnnqvvvg fvvglgytnp ylspfeefqr ykthpsiraf
      301 leggkrvsyg araitaggll slpktvfpgg aligddagfl nasrikgsha aiktgmlaad
      361 aafdavqagr qsdelnaypd afkqswlyte lyrarnfkqw makglylgtl mvgleqkvmg
      421 gnvpwtlhhk hadhemlkpa sqctpieypk pdgkltfdrl ssvfisntnh eenqpahltl
      481 kdasvpvnvn lrtyagpear fcpaavyefv knddggdrlv inaqncvhck tcdikdptqn
      541 ivwvtpeggg gpnypnm
//
LOCUS       WP_175792917             315 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175792917
VERSION     WP_175792917.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..315
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=34439
     Region          11..301
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mqhhqqssat iqgivpvmlt pfddagaidy aglerliewy lahgadalfa vaqssemqfl
       61 slaeraelar fvvervagrv pvvasghisd dldaqvaelr aaaesgaqgv vlvtnrldpq
      121 rkgsaafldh lhkllarlps dlplglyecp apyrrllsdd elracidtgr fvmlkdvscd
      181 letvkrrval aagsplkiln anaaiawdam kagsagfngv ftnfhpdlyr wlrtrgdsdp
      241 aladelstfl vvsavsealg ypalakiyhq rigtfasirc raidydvrer fwaldavldk
      301 ivsgtehfrr riaar
//
LOCUS       WP_175792918             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175792918
VERSION     WP_175792918.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46173
     Region          22..420
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,150,
                     153..154,157,245,248..249,252..254,257,285,289,347..348,
                     352,356,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnenhavpta pprirrgqri alallmvsgi vnyldrgtla vassairndl glslsemgll
       61 lsafswsyal cqfpvgglvd rigprrllgv glivwslaqa sggivatfgw fivarivlgi
      121 geapqfpsaa rvvsnwfplr argtptgifn aasplgtala plllavlvas fnwrwafiat
      181 galglvvavi wfalyrdpar aqltvaerty ldadaqtava mpkltfadwr slfshgttwg
      241 mligffgsvy lnwvyltwlp gyltmerhms lirtgfaasv pflcgfvgsl vagwlsdvvt
      301 rrsrspvvsr rnavvvamlg mvaftipaal vqsntvalac isvviflana asacswalat
      361 aaappsrias lgaiqnfggf iggalapilt gviaqkwsfv palltaaaia fagamaylll
      421 vrkpipeqaa stasgalpa
//
LOCUS       WP_175792943             449 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia ambifaria].
ACCESSION   WP_175792943
VERSION     WP_175792943.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..449
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=48232
     Region          76..440
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mhtllkpaas arslisaaat ltlvagfaal agcdarpaan apavavvpaa qaapaapava
       61 pasqpqtraq vfegvkqmta lgkqlffdps lsgsgklaca schsaehafg ppnalsvqlg
      121 gddmhrtgfr avpslkylrg ippfsehfhd spdegdesid agptggltwd grvdtrdaqa
      181 ripltspfem sssparvaka vraapyadaf rhafgdrvla ddqatfgavl raldafqqqp
      241 alfdpytsky daylaghaql tpaelhglql fndekkgnca schvsqrtle ggppqfsdfg
      301 liaiavprnr alpvnrdprf hdlgacgper tdlkgrdefc glfrtpslrn valrktffhn
      361 gvyhsledvm rfyverdihp ekfypvvhgk vqvyddlpkr ywpninrepp fdrkrgdapa
      421 lnaaeikdvi aflntltdgy qpaaasaar
//
LOCUS       WP_175792948             473 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia ambifaria].
ACCESSION   WP_175792948
VERSION     WP_175792948.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..473
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50311
     Region          4..473
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 misseafvsa crdaigaagv ltdphdtepf ltdwrrrykg sacavlkpad taevaalvrl
       61 anvhgvalvp qggntglagg atpdasgaqa vlslarlnrv raldphnnti tveagvilad
      121 vqarareggr lfalslaaeg sctiggnlst naggtavlry gnarelclgl evvtpqgeiw
      181 dglrglrkdn tgydlrdlfi gaegtlgiit aavmklhplp aaqvtalaal esphaaldfl
      241 alaqraagpl ltgfelmsdf cmklvgkhyp qlrypfdrph aqtvllelsd neseaharal
      301 feklmeeafe aglvvdavva enlaqsrafw glrehiplaq adeglnikhd iavpissiar
      361 fidetdaaiq qaapgarmvt fghlgdgnlh ynvqtpeggd pkaflaqfqk pinrivydnv
      421 hrhhgtisae hgigqlkidd aqrykspvet almrtlktal dprglmnpgk vlr
//
LOCUS       WP_175793001             187 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Burkholderia ambifaria].
ACCESSION   WP_175793001
VERSION     WP_175793001.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..187
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=20955
     Region          84..186
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mntdpkkwnp fkflrgaark sdaegaents aseqwraswp disrlfsres wgamedffhd
       61 pfagrgaler wfgdfsssrf qpridvvdeg pvlrvtaelp gmerddlkvs vedgaivlrg
      121 ekrqdvhsee ngcyrlerah gsftrtipmp enadpehtla kfdngvltlt vpksepakfa
      181 srtidig
//
LOCUS       WP_175793055             107 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA transferase subunit A, partial [Burkholderia ambifaria].
ACCESSION   WP_175793055
VERSION     WP_175793055.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004510
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         <1..107
                     /product="CoA transferase subunit A"
                     /GO_function="GO:0008410 - CoA-transferase activity
                     [Evidence IEA]"
     Region          <1..97
                     /region_name="AtoD"
                     /note="Acyl CoA:acetate/3-ketoacid CoA transferase, alpha
                     subunit [Lipid transport and metabolism]; COG1788"
                     /db_xref="CDD:441394"
ORIGIN      
        1 iaegketrqf gdrhyvleps ltadvalvka wkadksgnli yrrtarnfnp mcamagkitv
       61 veveeiveng tldpdqvhtp gifvqrivln atpekrieqr vvrakgd
//
LOCUS       WP_175793084             466 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Burkholderia cenocepacia].
ACCESSION   WP_175793084
VERSION     WP_175793084.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..466
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51782
     Region          4..440
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 meifdafhla rlqfaftvsf hivfpaisig masflavlew rylvtgdaay ksmfqfwski
       61 faigfgmgvv sgvvmayefg tnwagfsrva gnitgpllty evltafflea gflgvmlfgw
      121 qrvsprahff atlmvavgtl istfwilasn sfmqtrqgyk ienglvvpvd wfkvvfnpsf
      181 pyrlvhmtia afivagfiva acgawhllkg rrdepvkrsf smalwmllvl apiqivvgda
      241 hglntreyqp akiaaieglw etekggtaln lvglpdmqae ttryaiqvph lgslilthsw
      301 dgeirglkef ppqdrpyspi ifwtfrimag lgmlmlltal lglllrkggr lyetrwfqwf
      361 vvamgpsgiv allagwitte vgrqpwtvyg vlrtidsvsp ldaqqvgvsl lvfvvvyflv
      421 fgtgiyymmk lmkrgpaaqa gyielhrhpg lrksalstpl nvteae
//
LOCUS       WP_175793163             435 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia cenocepacia].
ACCESSION   WP_175793163
VERSION     WP_175793163.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..435
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45294
     Region          51..431
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mlkpylavai vfamaataha qpslspgpap aaaaapigap psdalpassl tlsdalavaa
       61 rnnpalrgar advdasagal mqagarpnpe vsflqegfsr aertstalin qtielggkrr
      121 arldvasygr eaasasldeq gaavradvia afygllaaqr qlqvteesaa iaarsadlag
      181 rraqagkvsp veatkaqvaa agvqievvta rgrvevarek lnavmgearn drlavlgdle
      241 tvppveplsa ltaqlddapl arvaraemlr snaaislera rripdvtvsa gvkrvttggv
      301 pnnqavvgvs ipiplfntnk galleathka eranadldre rtrlrleltq ayanfeaaeq
      361 eaqrlksdil paarlaldam wrgyelgkfs fldvldaqrt lfqgqsqyvr alagahaara
      421 digrlvgtpl aavaq
//
LOCUS       WP_175793193             141 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Burkholderia
            cenocepacia].
ACCESSION   WP_175793193
VERSION     WP_175793193.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         <1..>141
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
     Region          <69..140
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 khkpglviht agwplksdty ggsflyhmdn nqvvvgfvvg lgytnpylsp feefqrykth
       61 psiraflegg krvsygarai taggllslpk tvfpggalig ddagflnasr ikgshaaikt
      121 gmlaadaafd avqagrqsde l
//
LOCUS       WP_175793186             195 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: recombinase family protein [Pseudomonadota].
ACCESSION   WP_175793186
VERSION     WP_175793186.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonadota (proteobacteria)
  ORGANISM  Pseudomonadota
            Bacteria; Pseudomonadati.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Pseudomonadota"
                     /db_xref="taxon:1224"
     Protein         1..195
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=21460
     Region          4..128
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(9,11,66..67,70)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            11
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(65,109..110,112..113,117)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(71,76..77,105,108..109,112..113,116,119)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(94..96,105..106,109..110,113,117,120,124)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(94,110,113,117,120,124)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(118,124..125)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          140..181
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
     Site            order(141..143,176..177,179..181)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 mnqrigyarv stddqnldlq rdalrqagcs tiyeeaasgk saarpeleqc rkalrpgdtl
       61 vvwrldrlgr slpdlvqiva dleqrgvhfe sltekietgs aagklqfhvf aalaefergl
      121 irertragld aarargrsgg rkpkldakqi rhikallrdp ntcvaelard ygvsrttiyk
      181 hcgvvlprta degai
//
LOCUS       WP_175793210             958 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia ambifaria].
ACCESSION   WP_175793210
VERSION     WP_175793210.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 958)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..958
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..958
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=104100
     Region          42..957
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mqnhglsrrg flkasvlagv avyvapigsr afaalfeekl ltpvkwdsvt gipqfridgi
       61 akvtgskvfa rdvraadmph wpqqqshali lrvtqadrly egfnlsllgd elkpdrvvta
      121 ddlardgvaf ptfygddmll pagktpaylg havailiyhd farfrfakna lkfrddviry
      181 gavtgplerd pwgtfryvrv ggktaydddv ysslkdapif psmmrkhlpv wpdgkehgrl
      241 deqgmflagq iaaeldhpsa dwlvfereyn tqsvdtaale pdnancwyda atqsmhlvvp
      301 tqsplevaen aaamvakcrf pvkklfvhpc ytvgygskdh cnvpfyglvc alyadgrpvr
      361 fandryeqfq tslkrhafkm hyriavdrnt gllqsfkgdf eangggrsnf spsvamvgat
      421 aaqsiyyfpk sdlaavaias raidagsarg ygtlqsmaat emavdeiaaq lnldpidfrl
      481 rnalrsgmkn tqgaipagal rveevlerak qhplwtrrat rkaefeaanp gkrygvgfac
      541 vqkdfgtgae asfakvefde ngkvslhhta aeigtgmsts qavavakwlg rpatdvrval
      601 tewpdlpvet sgdpylmsqa dqdrlstdpr wspsyaspss atnsayyfth streaaravf
      661 ryglwpaams iwtrglgggq aapytiried arwvdgklta dglepltfeq lakqahalgl
      721 ptgavvhvfn rwqwtdaefe vggmvdrlpv dglslrvgap ktgddgplpg taapagatam
      781 rgtlaptang yrvldrkrvf ipptsrnnaa vtyytavgtl velavheatg kvellthhsi
      841 mecgnqispq lvsgqlqggl amgighalhe alplyedgpg ngtwnfnryp lpratdvavw
      901 sqtgdilppl setdppkgva evvmipvvga ivngiahaig hrftdlpvtp qkiqevla
//
LOCUS       WP_175793228             766 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Burkholderia ambifaria].
ACCESSION   WP_175793228
VERSION     WP_175793228.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..766
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=83989
     Region          178..765
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 msyvvavram ceftarrgdl dlrftpapta legiaghgav tskrgaryet eialtgtwgt
       61 ltvrgradgy dpvanrieei ktyrgsldam panhralhwa qakvyahlmc darglaeidv
      121 alvyfdivse retvltetls adelaaffae qcacfvgwae retahraard aalralafph
      181 gqfrsgqrel avsvyraard erclmaqapt gigktlgtvf pllkacgege ldhvffltak
      241 tpgralalea attlgagtpa lplrvlelva rdkacehpdr achgescpla qgfydrlpaa
      301 rdaaigagll dratvrdaal ahdvcpyyls qelarwsdmv igdynyyydg samlhtlaqq
      361 nqwrvgvlvd eahnlldrar rmysasldpf afaaardaap aalrkafdrl srawgtvnra
      421 qaeryaaype ipgpivsavq nlvaaigehl tdaprandda llrfhfeaiq fgvladafds
      481 asifdaslhg eplprqsgld gvapagrqrr iqstlcvrnv ipaaflapry eaaratvlfs
      541 gtlspfhfyr dtlglpadtg wldvdgpfra eqltvrvash vstrwrdrdr slepiadlia
      601 aqyatrpgny lgflssfdyl grvvalmqtr hpdvpvwaqa pgmaeserda flarfdaggr
      661 gvgfavlgga fsegvdlvge rligafiatl glpqvndvne qmrramdarf gngydymyly
      721 pglqkvvqaa grvirterde gvvhliddry rrrevrdllp rwwrig
//
LOCUS       WP_175793234             157 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia ambifaria].
ACCESSION   WP_175793234
VERSION     WP_175793234.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..157
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16274
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mykrifvgld ggpsarlaln eairialasg gevtcayvve hrpqlvdvda gfaaerdrda
       61 aataaatpvl ddaravlaqq hvpgtvrald aygedvaavl mrtaaevgad livmgtsgrh
      121 glrrlllgsv aesllrsadr pvllvrhdep gavatar
//
LOCUS       WP_175793237             853 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia ambifaria].
ACCESSION   WP_175793237
VERSION     WP_175793237.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 853)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 853)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..853
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..853
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=91900
     Region          45..697
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mssvrdlcak wvaraqpvaa aaavpvkrvl atawrrlrhp trrgvllaaa avpvlfllyv
       61 lalipftpgi gdirkarvdq paqvlsadgk llaefkpsnr ewvplkqisp hmvdaliate
      121 dhrfyehhgl dwkrtasaal htfsgnrqgg stitqqlarn lypdeigrap tltrkvkeai
      181 talkieaiys kpqiletyln tvpflynayg vemaartyfd ksadqldvld satlvgmlkg
      241 nsyynpvlnp eralqrrntv lgqmvkygkl saaqfaqlqr rplrvdferq keppgpaphf
      301 aqqlrkwlig wadrndyniy sdglivrtti darlqqmatq altqqanqlq giannawsgr
      361 dgcgtdnevf rtfmrespey kaaqdagkdd aaamkqlaad rgfmralcka ktdvqagfva
      421 idprdgqira wvgsrdftne pfdhvsqarr qpgstfkpfv ygvafangmk pddtfvdqai
      481 eiplkggeiw rpnddappsg kpmtlrdava lsrnritaqv mekvgpaava rlardmgvre
      541 splervpsla lgtspvtlke mvasyatian gglyvepqmv trietrqgdv laeyapappe
      601 raldaetdkt lldvmrdvvt rgtggsirtr fgirgdvagk tgttqdnadg wfilmqpglv
      661 agawvgfddg rvtlrsdywg qgahsalpiv gdffqraqra rivdtklkfd tepspgwfas
      721 arervtdlfa gwfgpeskqa papvrtqrie rqpdedadea saasaasapa pasggiveew
      781 ipasevaasa aalsagasqp qavqppaagg saaspgntgg aglgsapada psavpapspa
      841 papaspdaas gse
//
LOCUS       WP_175793250             319 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia ambifaria].
ACCESSION   WP_175793250
VERSION     WP_175793250.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..319
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35071
     Region          24..225
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd16282"
                     /db_xref="CDD:293840"
     Site            order(79,81,83..84,166..167,185,222)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293840"
     Site            order(79,81,83,166,185,222)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:293840"
ORIGIN      
        1 makafasqad levkkitwtq lsenayayta egdpnsgvii gddsvlivdt tatpamaqdl
       61 iakirsvtdk pikhvvlshy havrvlgasa yfaegaqhvi asrgtyemiv ergeadmkse
      121 ierfprlfag vetvpgltwp tlvfereitl flgklevkim hvgsghtkgd tivwlpsqkv
      181 lfsgdlveyd aacycgdaql eqwpatleal rafgaeklvp grgpallnpa dvnkgldytk
      241 dfvttllaqg rkaverkldl kasmaltrea mdpkfgnvfi yehclpfdvs rafdeasgit
      301 hpriwtaqrd keiwdalqd
//
LOCUS       WP_175793260             232 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            ambifaria].
ACCESSION   WP_175793260
VERSION     WP_175793260.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..232
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25953
     Region          21..179
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnakstvarp rgrrpsvedf dlrdhmldva iqlfaehgia attvaqiaaa agvtsamvhy
       61 yftnreqlld aiveerlaqv iafvwrptap riendpfalv aelvdrffdv thrmpwlpsi
      121 wlreivhegg llrermvrri plehvgrfae riraaqqagt lnpslepafl fhsiialvml
      181 plataklwqs arglppidrd vlhrhvrall gsgmqppvta pdahsrsprr ps
//
LOCUS       WP_175793318             319 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease signature motif containing protein [Burkholderia
            ambifaria].
ACCESSION   WP_175793318
VERSION     WP_175793318.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10052677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..319
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36137
     Region          216..308
                     /region_name="COG3183"
                     /note="Predicted restriction endonuclease, HNH family
                     [Defense mechanisms]"
                     /db_xref="CDD:442416"
ORIGIN      
        1 mptervfrkp esfeaerlsr dairpflesr gfavlsderi vrgvsqaqvv tarsetgeti
       61 kmrvrlcwrh rgpddlrfsa aqlradlidn dwdktldqlv drdvkvgish aliiqrvget
      121 vpyaalvpid qlgliwrrqa evseelikag rlgrttknha kngssptvyl mdsrhedahf
      181 vpdvlwqwpg vqdlvkmgdv kqrvpiddtw ddlyapdpsg ygsdgasdrt vtrsevkrdp
      241 rvradvvkra dgkcerstcg aiarykgfld vhhilgvrns drvwncvalc pschrdahfa
      301 perdeindtl ldfasrfrk
//
LOCUS       WP_175793346             390 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175793346
VERSION     WP_175793346.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..390
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=43131
     Region          27..84
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          116..318
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(131..132,134..135,138,142,144..150,244..249,
                     255..256,258..259)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrdapepngl pldasdatga ldvldarlmr illvlltert vsraavrlnm sqpatsaalk
       61 rlrtllgdpl lvrsrygmvp tefgsrlidp lrnalrvidf iriqqptfda rtsvrtyrig
      121 cpdylnvlfv pklialfrer apnaqlvfhp lgdgyddera ladgeldvvi dnrparssrf
      181 rqddlfddrv vclmrathpl arrgamtaae faqaaqlcpt pswleasgai dlqlervglq
      241 rrivvtlphf elaahalvrs dliltttyrl arhyakllpl gavalpaepp divyrmtwne
      301 sgpcvdgvrw lrtliaeatr swldaeaalp dvtavaanad anartaasva ddppetvrrp
      361 rrrhathcgt sqrprparaa rlhriatksh
//
LOCUS       WP_175793391             249 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia ambifaria].
ACCESSION   WP_175793391
VERSION     WP_175793391.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..249
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26230
     Region          11..244
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mnathdparq slagrtalvt gggrglgeai ceelaqhgah vivadldgdr aaavaqrler
       61 hggqvvgrpl dvrdeasvlq vvhdarealg dldvivnnaa idvtapiddv svaawqqvlm
      121 tnlfgpylmc haavpmmkar gsghivnias taskrawpna sayhatkwgl lglshalhae
      181 lrpagvsvsa ivaggmrtpf lldrfpdide dtlqppehva aavrfvltqp pgtvvpelmv
      241 lpmketswp
//
LOCUS       WP_175793392             400 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia ambifaria].
ACCESSION   WP_175793392
VERSION     WP_175793392.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..400
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42867
     Region          5..362
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 msaawdrarr ilcvrldslg dvlmttpalr alnesgqgrr ltlltsrtga alskhlpmvd
       61 dvwtydapwv khpgargdpv vdldmigrll aghfdaavif tvysqsplpa ammcwlagip
      121 lrlahcrenp yelltdrvpe pepesyvrhe varqlalvrs igaktsdwrm afepgdaarh
      181 alharlraal eriggprrpg aararwlvvh pgasaasrrw paerfgaaaa rlaplfdgia
      241 vtgsaderpl veavceragp ravplagalp lgelgaliet adlllsnnsg pvhlaaalgt
      301 pvvdlyaltn pqhtpwrvph ralnvdvpcr ncyrsvcnqp ghpcllgvsv ddvvaathal
      361 lrgserhaqr aagraavrgv epvaanasnv ipfahvitrs
//
LOCUS       WP_175793408             231 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia ambifaria].
ACCESSION   WP_175793408
VERSION     WP_175793408.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..231
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24487
     Region          129..230
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(132..133,166..167,170,174..175,178,220,224)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 msaksllvig vtvllaacas qgptwnayrv smpngqqayr vdchglfegq eacyseavei
       61 cgkkqvqple avaplsdeqn prdvriltfq catpaqpapp aavkpapvpa pvaaapvtak
      121 hitldsdanf dtdkstlkad ardkldalie aahgtpfktv tisgytdstg tadhnqqlsq
      181 rraqsvaqyl hehglaaqkf dvrgygennp vasnatpagr aknrrvdiml e
//
LOCUS       WP_175793461             348 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA-binding protein [Burkholderia ambifaria].
ACCESSION   WP_175793461
VERSION     WP_175793461.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13774834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..348
                     /product="DNA-binding protein"
                     /calculated_mol_wt=38550
     Region          10..124
                     /region_name="KfrA_N"
                     /note="Plasmid replication region DNA-binding N-term;
                     pfam11740"
                     /db_xref="CDD:432038"
     Region          <76..>329
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
ORIGIN      
        1 mgrsgltimd vkhardalva qrqhpsidav rialgntgsk stihrylkel eeqeeqdgvk
       61 ladaeslsap iqtlvaqlsa qlhaeaqavv haqveaaaid rqaaqvetgk llrelndlra
      121 qladtttale qeqaahvear dllqkrtlen erlaqqvrdq naraaeqegf rqsleeklvh
      181 ardalehfrs aarelreqei rrhehqiqql qadlrqlnqs aivkqneitq lnkdnarlva
      241 eagaagkqlr eqqglnerqq aalaqaaada argeaerdsl rtslqrqaae laslreslpq
      301 latarteaaq areesaqlrg qievmreqqt hllrtietrf seggkdas
//
LOCUS       WP_175793482             300 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia ambifaria].
ACCESSION   WP_175793482
VERSION     WP_175793482.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15202679
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..300
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32173
     Region          18..134
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          166..278
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 mndehvmnas gaatalhyrr ftaadvpaah alsmalrwpf raedwqfstd tsiafaaeen
       61 gvvigtamcw kygadraaig hvivssehqg rgigralmei lldelgsriv flhatpagqp
      121 lyeklgfnvc gsldqfqgnv sqpaavalpd garlragtsa dlsrfvelda hasglerdal
      181 msallkrges vvleqdgeia gfsvlrrfgr gyvigpvvar rssddaqaka lishwlsare
      241 nefvridvpt gtslpdwlda qglkrvdtcs kmvrnapada hpgatdpayv qyglisqaml
//
LOCUS       WP_175793487             244 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia ambifaria].
ACCESSION   WP_175793487
VERSION     WP_175793487.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..244
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25427
     Region          127..235
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 mtavfvlhra dgapsstafr kqafgasdpf ashreiaweg pdamaagrig fvgeldiasf
       61 phietlvvve geltleagga aplvvgpgqg avigggtalr iaaqspvrlm fcaaacaqpt
      121 krgvfalhad adfkpsatla aevllgpapq crsdnvftdd gagycagtwd stpyhrivrp
      181 hranefmfll dggvrfaapd gsvqslgtgd alfvprgasi gwesservak fyvmqnvkps
      241 perd
//
LOCUS       WP_175793497             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175793497
VERSION     WP_175793497.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32436
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..295
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(103,107,146,160,164,230,247,274)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(104..105,109..110,112..113,116,120,122..128,191,
                     221..224,228,235..236,239)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mqvdlgdlna fvavarakgf reaarladas asglseavrr leaqlgvrll hrttrsvspt
       61 eagarllarl tpalseveaa ldvvntfrek pvgtlklnvp msaarlvlps ivprfldayp
      121 eirlevvade sfvdilaagc dagirygerl eqdmiavpig prsqrlataa apayldrrgr
      181 pahprdlldh aclrgrfasg ampaweyerd gevvrvepsg plvvqiggav dlivdaacag
      241 lgvvhlyedw lrpyfasgal epvldgwwrp fsgpylyypg rrfvpaplra fvdfltsspa
//
LOCUS       WP_175793542             486 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175793542
VERSION     WP_175793542.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..486
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50138
     Region          31..475
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,156,
                     159..160,163,293,296..297,300..302,305,333,337,390..391,
                     395,399,415,418..419,422..423,426)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msdntlapct pagaaaaaap rshhgwalvv llvgailppl dyfivnlalp airdgigarp
       61 aelqlvvsay acanavvqit ggrlgdlygr krmfmvgmag fvvasalcgl agsgamlvgg
      121 rvlqglfaai lapqvlatir svfspqeqvr vmgfygfvfg laavigqlgg galislhpfg
      181 lgwraiflvn vpigilallg swrfipesrp prgqridvpg tvllslfllm lvyplthgre
      241 agwplwmvac vvgalpmlga llavearrla ggrdalldvr llrnpvvalg ltlaflfyml
      301 safflsfgiy lqgclnwspl asglailplg igflaspllm prlvarfggy rvltlgfaml
      361 aagvataaal agdhapgagf hagiaaigvg qglvlpsvvr ivlaevdaar agvasgmvta
      421 mlqigaavga atlgglffar lgaqpetldy vqgfrtamwa ltvvllvcva lsatlgpmhr
      481 rvrada
//
LOCUS       WP_175793535             500 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia ambifaria].
ACCESSION   WP_175793535
VERSION     WP_175793535.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..500
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52165
     Region          31..474
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msgwsgvtga agetpagapa eagggtvlta gavgfptala savglimasp viltatsgfg
       61 mggwafavam iiafvmmqaq attfseaaam lptagsvydy lscglgrfwa itgtisayfl
      121 vhvfagtaet ilsgimalvn feslnaalek hnsswlvgvg lvvtfaitni igikvfskle
      181 ivltagmwls lmifgilgla aapavhldgw fggsavgtsg pavlslvgma mfmfvgcefv
      241 tplapemkap grtipramal glvgvaicmf lygaairrqv anvpvspdgl thlldtpgai
      301 pafalqvlgp fgrvwfgiaf lcagaatint lmaglprily gmaidgalpr cfaylhprfk
      361 tpvvgivaaa ivpiahawli hgnldsilhl vlaatcawgt ayllvtasvv mlrirrpdlp
      421 rpyrsplfpl pqivssvgiv laiwyitppg mnardiyvpf gvmlgltaly alfwtvvvqr
      481 rhpfkpvpie evlrrehvas
//
LOCUS       WP_175793546             264 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175793546
VERSION     WP_175793546.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..264
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28017
     Region          12..140
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          179..260
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mhrithyrrt degieaisle sdrafprhah defgvgvivs gahrswsgrg qvdalagdai
       61 mvnpgemhdg mpidtgtgrr wrmlylapal vasvateegl eavelthpav rdarlaaafg
      121 rlharivage tlplardeal vtlvagllar hsnralpaag vapairmare rldaapaapv
      181 slaelaglsg vsrfqllrgf arelgitpha yllqsrtrla rallasgrpi adaaaeagfa
      241 dqshltrafa rqfgitpgrf tqsg
//
LOCUS       WP_175793553             515 aa            linear   BCT 11-JAN-2025
DEFINITION  FGGY-family carbohydrate kinase [Burkholderia ambifaria].
ACCESSION   WP_175793553
VERSION     WP_175793553.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..515
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=55209
     Region          3..448
                     /region_name="ASKHA_NBD_FGGY_RrXK-like"
                     /note="nucleotide-binding domain (NBD) of Rhodospirillum
                     rubrum xylulose kinase (RrXK) and similar proteins;
                     cd07804"
                     /db_xref="CDD:466806"
ORIGIN      
        1 meyvigvdig tqstkallvd rrgtivarrs agyqpdtprp lwaeqwpqvw fdavldciag
       61 cvsdarahgv padairavcv sslyggsgvp vdsdmrplhp cliwmdrrat aevdwvnanv
      121 nverlrvitg ngvdsyygft kmlwlreqrp dvwanvryfl ppnayviyll tgevavdhss
      181 agniggvydv arrewsddal dmlgipatmm perlvqstdi vggllsqwte qlglpagtpv
      241 vaggvdaava tfaagatrgg qhvatigtsm cwgyvnqhvd arhglvsmph vfngqrdlyv
      301 fggaitagas vawfrdqfch aeidaarllp hgdphvllee aaesvppgad gvlflpylmg
      361 erspvwdaqa sgafvglsla htrahlyrav legvafalrh nieagrrgtv alddrlivvg
      421 gaahsalwmq iiadvtgfpv wtieqdveaa mgaallagvg vglvshddaq ggwvtlvera
      481 rpdaaranay aarfalytal ypalkptmha lrtss
//
LOCUS       WP_175793586             286 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Burkholderia
            ambifaria].
ACCESSION   WP_175793586
VERSION     WP_175793586.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..286
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30574
     Region          4..283
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 maanfdelas riraqfsels pqfqagaafl ldhpdevats smrkvaqraq vqpaslvrla
       61 qqfgfpgwne lrdlcvarvr trpepltqra rslvrpdaka slahdllaaq qhnlaataaq
      121 nehaladaak lirkashvhv agfrscypva fgfvygyrlf rptvsllngv agslemelrt
      181 iakqsvtviv sfapysaeat rvaqaakarg skivaitdsa vspialhada qlifthdsps
      241 ffpslvaaha mtealvaqll alegsdavaa lerteaelha kgayvv
//
LOCUS       WP_175793592             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175793592
VERSION     WP_175793592.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33485
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,219..224,
                     230..231,233..234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mklsfevlea ldaidragtf aeaaalihrv psaltylvqk aesdlgvtlf drsgrraqlt
       61 eagrllvedg rrllqtgrel eskvrgvhag wevelrlcld eilplpslwp hvrafydmem
      121 ttrlrlstev lggvwdalvt gradiaigaa gepphapnia arpigllrhv fvvaphhpla
      181 aveqpldsdt isshrgaiis dtsraleprs vaihdgqpvi ivptlaakld llcegmavgm
      241 lpapvveesv rqgklverrv igvrehtncy lgwredktgr alkwwinrld qidlistlfs
      301 trgiat
//
LOCUS       WP_175793623             551 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia ambifaria].
ACCESSION   WP_175793623
VERSION     WP_175793623.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Gournas,C., Athanasopoulos,A. and Sophianopoulou,V.
  TITLE     On the Evolution of Specificity in Members of the Yeast Amino Acid
            Transporter Family as Parts of Specific Metabolic Pathways
  JOURNAL   Int J Mol Sci 19 (5), 1398 (2018)
   PUBMED   29738448
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Vangelatos,I., Vlachakis,D., Sophianopoulou,V. and Diallinas,G.
  TITLE     Modelling and mutational evidence identify the substrate binding
            site and functional elements in APC amino acid transporters
  JOURNAL   Mol Membr Biol 26 (5), 356-370 (2009)
   PUBMED   19670073
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146941
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..551
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59714
     Region          31..470
                     /region_name="AA_permease_2"
                     /note="Amino acid permease; pfam13520"
                     /db_xref="CDD:404414"
ORIGIN      
        1 msqaglranr tsdveatish dstghtlhrg ltwkdafwvt sgvpagvlft iggvcatigq
       61 pawaiwiaai tmgliqsaty aeisglfphk sggasvygai gwvrysklia pvsvwcnwla
      121 wspmlalgcg laasyaltsl fpadaavlhw qlriadlgfi kpglslrina tfiiatilll
      181 itfklqhsga skaartqril giasltplli vgivpfvtgd vpmsnllpll plghdahgnl
      241 ttatfgswng qgvtmalgam fmagwasygf etavcytref rdprrdtaka ifwsgalclv
      301 vmtlvpmafq galgtqamld paigdgtgva aamarivggg awvanavvvm lmlsillivm
      361 tsmmgssrtl yqasvdgwlp kylshvnehg sptramwtdl gfnlvllmms dymtvlsisn
      421 vcymlfvfln lqsgwihrmd rgnwdrpfrc ptwllvagsi cgyanlvyvg aganlqgegt
      481 lrngliamll ivpvflfrhy wqdrgrfpaq mqrdmelevp rramwlnlmp yaaligaglt
      541 iwlsyyfawv k
//
LOCUS       WP_175793634             392 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia ambifaria].
ACCESSION   WP_175793634
VERSION     WP_175793634.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 392)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..392
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39908
     Region          168..370
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mtgravasar ritldkvgil igvltiiavv gmpfmvlrpn riaagtglsv faalpsaqga
       61 alaalwivga lwamtasrpa wrlaagctwl atlayavgaa aahvvapddm larvspaagv
      121 wlllfawavl vadalarlaf gpwrrlvala vaiaaisvpl asgwwdglsv mreyavrtdd
      181 fwreairhvs laggsvaaal vagvplgiac ariapvrtvv mpvlnivqti psiamyglmm
      241 aplgllathv plaaalgirg igvapavlal flysllpias svvvgleqvp phvteaaram
      301 gmtrvqrllg vdlvlalpvi lsgvrivlvq nigltavaal iggggfgtfi fqgigqsaad
      361 lvllgaipti alalaaavvf eaattlakgr ta
//
LOCUS       WP_175793652             475 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175793652
VERSION     WP_175793652.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..475
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51206
     Region          42..460
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(52..53,56..57,60,100,150..151,153..155,158,178,
                     181..182,185,296,299..300,303..305,308,335,339,388..389,
                     393,397,413,416..417,420..421,424)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mastvpdpas vadtirtapi dagsisarld rlpptrsvwk lvvllslgff felydllysg
       61 yiapglvkgg ilsatthglf gttgvasfia alfsglfigt iacgfladrf grraiftwsl
      121 lwytaanvvm afqdtaggln fwrfvvglgl gvemvtigty iselvpkqir grafaceqav
      181 gfvavpvvaf layllvphap fgldgwrwvv ligahgalfv wwirralpes prwlaqqgrv
      241 eeadrimral eakveaeygr plpppapaep vpprgsfrdm wvppyrsrti mmtifnvfqt
      301 vgfygfanwv ptllikqgit itsslmyssv ialaaplgpl iglviadrfe rksvivamaa
      361 aivvcgllfs qttvgafliv lgigltlasn imsysfhayq aelfptsira ravgfvysws
      421 rfsaifssfv iaavlrgfgt fgvfafiaga mvivmaaigl mgprtkgial eaisk
//
LOCUS       WP_175793680            1284 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175793680
VERSION     WP_175793680.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1284)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 1284)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1284
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..1284
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=139893
     Region          1..785
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 maifsqdrtl siagaslptw gmdalpvfap vrlqgtetig cldacrylvt lrtddayafs
       61 pshaadvdld kivgtevtvs iqlegrgrli pelvgaaghd ntgagtreis glveaarvag
      121 qdrdailyel elrpwlyraa ltqdcrlfqd mtvvdvtdav lakypypvdk rlgafrgayp
      181 trdvqrqafe sdwaflqrlw eewgiwwwfe hdggrhrlvl cdsmgghrph raayatlryr
      241 ppgaqridee hihtlsvtsr ltpggvsvtd ydytrpradl aatvedprps asadgeiygw
      301 gdysqplaga sgltgqpndt erearhfarv qleaqrckgl rangqgnlrg lavghtftlt
      361 gypqqaanre ylvvsctldi eavaqrtsde qacrvdaqfe llptnepfrl arsvrkpils
      421 gpeqatvvgp agqevwtdry grvkvqfawd rqgphdehsg iwlrvlspwq gmdvgatfvp
      481 righevavsh yhgdpdlpvi igsavnafrq paldlphnha isvirgrefh gtasghlaid
      541 dtqeqiqtqi asdagasvls lgnlrritrk ngradargkg fdlrtddwgv vralkgllvs
      601 tdgqpggpgh akaakeavsr ltqardlqks ltdlaqrhda qppgadqsdv prainarnea
      661 irgtpsggad hfpelaepdi vltgsagism aaersthias gedvavtsgr hvgiavgrsl
      721 iasvsnafsl fvhkagmalv aaagkvrida qtdgvdvtar kairltstad tihlhaakei
      781 vlhagrtevr isdrgyvvrt agehtihags hqtdhaqvrp mhvpvtpehp gryaaqfvll
      841 ehgsgfalpn qpyritldng rvvdgvsnel getdvvtshd iafvtvella asatdkviav
      901 nqaaivrena apytvrapna dkrtatirgr evstpergat sgsqrpafta cdplnfglrf
      961 hhfiggakqg dtpldmpvrr dveypvtkay taaikkalkg igwgrfntss geisdeakes
     1021 ialavgnvln talaagpygl prgssgdqmr snggfpkfdi vnekggqsry nmrsdvsasf
     1081 stlrwtivvq eaeirkimaa rkndaaldgt lktladtlyh earhcqqtfw mmallqqhss
     1141 dyamfssamh vyktncpkei feaaaktkip edariatglh rmlifhyywm isymqnqprg
     1201 ayvkpdvpia qaevckllrv spetaakmls fddgyrsqlh eedayacaev vqaywdrpdr
     1261 afvrnpgtct geydaalhai geri
//
LOCUS       WP_175793716             936 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Burkholderia ambifaria].
ACCESSION   WP_175793716
VERSION     WP_175793716.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 936)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 936)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 936)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 936)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 936)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11534155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..936
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..936
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=95538
     Region          11..79
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          114..174
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(120..122,125)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          187..934
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mteplasagl qtieltvdgm hcggctarvq ralaavpgvv eaavdldaqv atvtaqdtve
       61 paqlvdavga agyratvrea afeavaaaqa qhasraealp atpaalpata atieleidgm
      121 tcascvsrve kalakvpgvt rasvnlater atidaapdvs asrlaeavqq agygatavaa
      181 tppaasrdle fdiggmtcas cagrvekala avpgvarasv nlaterasvh gagaldaavl
      241 iaavttagyr aslaaapdaa tggaaevpag dptqapeark rreairernl vigsavlsap
      301 livpmlvapf gidamlpgwl qlvlasivqf gfgarfyraa whamkartgn mdllvalgts
      361 aafglslwml vrdpadpghl yfeasavivt lvrfgkwlea rakrqtseai ralnalrpdr
      421 arvvehgver dvplalvrvg ttvsirpger vpvdgrivsg rshvdeslit geslpvpkdd
      481 gdpvtagsin gegalvvatt aigaettlar iirlvesaqa ekapiqrlvd rvsevfvpai
      541 lgiavltlig wliagagtet ailnavavlv iacpcalgla tpaaimagtg vaarhgvlik
      601 daqalelaqr ttviafdktg tltegkpsvt afdavgipre qalalaaavq rqsdhplara
      661 vvaaheadvv arggdagspd ivaadarava grgvqahvdg qllalgstrw rdelgivvpp
      721 eldaraaele ragntiswlm radappalla liafgdtvkp gardaiaals argvasvlvt
      781 gdnhgsaaav aaalgigevh aqvlpddkar vvaelkrthg gvvamvgdgi ndapalaaad
      841 vgiamatgtd vamhtagitl mrgdpalvad aidiskrtyr kiqqnlfwaf vynligvpla
      901 algwlnpvia gaamafssvs vvtnalllrr wkgrar
//
LOCUS       WP_175793737             334 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Burkholderia ambifaria].
ACCESSION   WP_175793737
VERSION     WP_175793737.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..334
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35995
     Region          7..303
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(12..14,44,49,75,138..139,179..180,201,230..236,272,
                     289..292,297,300..301)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(44,49,75,138)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 mritlpsrlg fgtaplgnmy rdipheeala tvdaawrggi ryfdaaplyg aglaelrlge
       61 alagrprdey algtkvgrlv ldehedasqr dlgekgglfr hglpnrivyd ytadgtlrsi
      121 easlarlrtd rldtvwihdp avdfhgdawr dvfdvamsga akaltrlrde kvikgwglgv
      181 nrvepcelal ersdpdgfll agrytlldha galerlmpes aarglgiivg gpynsgvlag
      241 gthfeyqpat qailervari rrlcerfgvd vravalqfsl ahpavaaaip gasrperide
      301 nlrlaaapip aalwaalkae hliaehaptp agad
//
LOCUS       WP_175793745             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175793745
VERSION     WP_175793745.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32957
     Region          9..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..295
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,230,247,274)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,193,
                     224..228,235..236,239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 meqisldrlt gliafsraas lgsysaaara lgvtpsavsk siqrleqhfe lklfnrttrs
       61 ltltqegrel hertlrllae meaieqaavs arsepagtlk vtaplpigih liapalpafr
      121 krfpklsidl rlgdhfvdlv gegvdvairv gdltgsrlis rqlsphhiga yaspdylarr
      181 gvpkhpddlv dhdcvnfrfq ssgqvfrwnf vtgdgsldli pdagivvdts davaavmvag
      241 ggvgitpayv aasyvkrgel vplltefvep rstitalwpe srrsspnvka fvahltkvfa
      301 syaadk
//
LOCUS       WP_175793807             428 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175793807
VERSION     WP_175793807.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..428
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45842
     Region          22..421
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(35..36,39..40,43,75,125..126,128..130,133,153,
                     156..157,160,253,256..257,260..262,265,293,297,348..349,
                     353,357,373,376..377,380..381,384)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mlaipsesav gdtsnlyski nwrllpflls cylfayldrv nigfaklqmq sdlgfsdaay
       61 gvgagiffig yvlfeipsnl mlprigarkt fsrilvlwgi tsacmlfvrn vpmfyamrfv
      121 lgifeagfap gmiyylscwy gpqrmaraia vvflagplgg ivggpvsawl italsgaggl
      181 agwqwmflve glpcillgvl alffvpnrpa daawltegek rllaneigsa aghnhsflav
      241 ardvrvyvla fayfciiaai yaisfwlptl ikaqgvsdtv qlgwysalpy iaaafgmyym
      301 grrsdrager rfhsavpati gglllaastl vdgnlaaslv lltlgtcalw mtytvfwamp
      361 seyikgpgaa ggialintig lsggfwgpai igwaktatgn lhlgmlilat lpiiaaliil
      421 anklpakp
//
LOCUS       WP_175793852             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175793852
VERSION     WP_175793852.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33873
     Region          7..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..293
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(105,109,148,162,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(106..107,111..112,114..115,118,122,124..130,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mqhlpdleaw aifarvaetg sfakaaellg isqptvskai arlekrlgam llyrtsrkls
       61 ltptgellrd rairlladae lieseasaqa lephglvrvn apmsfglrhl spllpafler
      121 yprvdidlvl tdhivdivsg gfdvairiae lsdsslrsrr lcavrrplva spaylerrgr
      181 pthprdieqh vcltytnlpt pehwrfrnpa sgedvgvsvh grirtnnadv iapallaghg
      241 lalqpeflvw dalqrgelee vmpewkiadi nvnlvtppgm lraarvtvll dfladhfaha
      301 pwalpvd
//
LOCUS       WP_175793873             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175793873
VERSION     WP_175793873.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46143
     Region          13..417
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(25..26,29..30,33,72,130..131,133..135,138,158,
                     161..162,165,247,250..251,254..256,259,287,291,343..344,
                     348,352,368,371..372,375..376,379)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mtqslpssrq paraataafv gtmiewydfy iyataaalvf gelyfpshdr fvstmasfat
       61 favgffarpl ggivfghlgd rigrkkalmt tlmmmgvatv cvgllpdysq vgmlapvlli
      121 vlrvvqgiav ggewggavlm agehapqgrr tffasfaqlg spaglilslv afravtsmdk
      181 adflawgwrl pflassvllv vgilirlgvn espefarvke anrtvklpva evlrsasglv
      241 llcigantig iagvyftntf miayttqyvg vsrslildsl favaiiqfia qplaawiaer
      301 iggarflkia allamlspyp mfmlvqggts gslvagiala vvcmagfysv iagfvsdvfp
      361 ahvrysaisl ayqvcgaiag gltplvgtwl ahrfagqwwp lavfytclag isllcivald
      421 arraarptaa ealgsh
//
LOCUS       WP_175793892             835 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175793892
VERSION     WP_175793892.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..835
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=91177
     Region          16..763
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msgevllkvl rggyaqfdri vkldtplgdd wltplyvkin arlgrnfevt vdassvmgdk
       61 iklsalmlqp vtlwirqtdg gylpihgyvq rarrlgndgt vsyfqlqfss wlsflklssd
      121 rrdwqeasgw qiladvfdkh pqasgnygqe lraamrsysh rvqwetdwnf vhrsleevgv
      181 fprfdfakdg kshkvvmmdd lyfgpslpns emkfshagtd edfdgltqls eqqdaqsatl
      241 tlgtadykrp dldkqvsmpa anledlpgqg edylytgsqt waesdigqqq arirteewas
      301 rakryfaigs pryalpgywf kvsghpvlda lpeeerelsi iasdwliqnn lpgldaltrf
      361 prslrseieh vqaagtgatv shrdggvgff hveieaqrrk tpfrspfehe kpemhlqtai
      421 vvtdsdeeia tddgnrvrvr tsnsrndrnt kstswiraam pdagakrggy fplrkddqvl
      481 lgfvngdcdr pviisrlhgg atmpvwhthg llsgfrsrey ggdgfnqlvl ddasgqnrvq
      541 lsttsyashl hlgylieqsd ntrgsfvgsg fdlkseahga iravqglsis thpaavqpmn
      601 vsaatdqlaa seavfetvsq asetnraesl qdgsdalkaf temtqhsvpg atkggrtagg
      661 gtgnasgfak pallvsspag iglssqqsih asanqqvnlv agknvnlaaa ksllasvmdk
      721 islyaqnlgi kifatkgpie iqaqndaltm laqqdvkies asgrmilrae kelilnvggs
      781 yikitpdmie ngtsgqilek caswdkpgas tmtlrdplng tpvskhggya ddfsg
//
LOCUS       WP_175793896             453 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175793896
VERSION     WP_175793896.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..453
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49050
     Region          21..410
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,152,
                     155..156,159,257,260..261,264..266,269,297,301,350..351,
                     355,359,375,378..379,382..383,386)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtspalpgrd plasavskvk whvlplvlim fianyidrvn vgfvdrhlea sigigaaayg
       61 lgaglffvgy alfevpsnll mqrygariwl arimatwgvv aaamafvwnd tsfyalrfll
      121 gaaeagffpg vvlylsqwlp pqergkamai flggsafasv lsgpvtgall sihgfglqgw
      181 qwmfliegmf svalcgaswl llkshirdat wltaderaal qnaldderat rdvrskvhvs
      241 attllrdpqi mlfcflyfai qltiyaatfw lptiirkmgg ltdfqvglyn tipwmiaiga
      301 mygfavlsak wkhpqrwlsf alvlaacglf astshdpvws fasicfaalg fkaasalfwp
      361 ipqgyldtrv aaavialins ignlggfvap tafgylkqht gsitgglyal aiaslvaava
      421 alfarthrrs dpprglpade sftntamlrh aeh
//
LOCUS       WP_175793902             475 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175793902
VERSION     WP_175793902.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..475
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50105
     Region          16..419
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(28..29,32..33,36,76,134..135,137..139,142,162,
                     165..166,169,251,254..255,258..259,262,290,294,346..347,
                     351,355,371,374..375,378..379,382)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msrpqspsav pprpgraala afvgttiewy dfyiygtaaa lvfgkvffss tmdpgvatll
       61 afvtfwagfa arpfggivfg hlgdrvgrkt alvitlimmg lattgigllp gyasigvwap
      121 aglvvlrvlq giavggewgg avliasenap khrsilyaaf aqqgsptgnl latvaffals
      181 alptpsflmw gwripfllsa vlviigmvir lrleesidmq rvlarkrtvk lplrdvvrdh
      241 wlvvllaagt lpvinvtyfr stfalswatk elgyaqgtfl gilsislvvq flmqpigawf
      301 vskidmrram cwilipeivl mpvmfhalat rsywvavvgm cistipsamf ygavggvlar
      361 vfpanirytg lslayqlsal vvgggtpvla qailnatgsi vgvaiasgly alvslacmla
      421 llnrtgyrad elssaersda aewgtasasa daaagesaqp aergtlkpag qagat
//
LOCUS       WP_175793966             277 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia
            ambifaria].
ACCESSION   WP_175793966
VERSION     WP_175793966.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..277
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30590
     Region          114..273
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mlldvnsshr dtdrfnvsfk algelietvg tphfvprltq llndvvpldv ahversrvdg
       61 ampigyrcew igssgigagt dtaeisdvmt lyyerfldsd plfaglrgkt gtmlvvrdia
      121 aippgefrqr lfddvrighe cvlargtrya qysialergr drppftlaem srfrsisdvl
      181 fpllelhast taarriahpt pdvhplarfd ariaadgvkl skreyetckh lisgktvpet
      241 aeilgvrvas aesyvkrafa klgvrtkrel aawgaid
//
LOCUS       WP_175793999             545 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia ambifaria].
ACCESSION   WP_175793999
VERSION     WP_175793999.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..545
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=58373
     Region          1..545
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mcvtlicggv aclfepvhaq vpdagramrd ietprpdlpp etapdltvap seeaagsape
       61 sgprvlvraf aldgntvfgn delqplvadl agstlgfadl qraaaritay yrrhgyvlar
      121 aylprqdidd gvvrieiaeg rygaitiqnh srvlgaalrq plsalhpgdv vrgsglersl
      181 lllddlagva argtlrpgda pgttdlvvda dkgplasgsl efdnfgdvsl gryrvggsvd
      241 vnsplrlgdr lslrglvsnq rqryyraayq vpvgpastri gvaysslryr lggafsdlds
      301 sgrasvqtay vtqplvrarn lsvtaqaqye nknlrddygv fdirrdknvg lwtfgvsgns
      361 qdgwlgggrn gfsvmfgvgr lrsndpfead vlkksigsft klnvsalrvq algrrfelya
      421 qfsaqlasrn ldesekfslg gpygvrayal gagsgdqgwq asaelrylva pgwqvstfvd
      481 agrvqadkfp wtrernmqhm qaggvgaswf gakrqvalta awplgaafgs ptrapsvwvq
      541 aaqyf
//
LOCUS       WP_175794000             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia ambifaria].
ACCESSION   WP_175794000
VERSION     WP_175794000.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22001
     Region          2..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 midfstlalf sgaglaltat pgpdmllias rsvsqgrrag fatlagiqag tychalaval
       61 glsqlflavp iaydivrfag aayllylawk tfrsdatals pvasqrrhst atifrqgltt
      121 nllnpkmalf vlalfpqfvr pghgsiavqi lvlatvlnli glvvngavil sasrlsqrig
      181 arrrpsklpq yllgtvfagl aarlavagrn
//
LOCUS       WP_175794002             295 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175794002
VERSION     WP_175794002.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..295
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31349
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..286
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mlldnlalfl rivekgglaa agrevglspa tvserlaale shygaalltr ttraisltde
       61 grtlvagarr llaeadeles rvrlgaqtls gpvrlsapad lgqarvvpvv daflaehpgv
      121 tvdlhlgdgy vdlvgqgldf airrgtlads alrsrslgrs rrvvcaapay laahgtprhp
      181 delaahdciv mrfgqelyae wpfriddelk rvmvrgqrva ndgalvrawc vaghgialks
      241 lldveqdlas galveilrdf spgevdlqiv ypgaaaqprr vralieqlaq alaag
//
LOCUS       WP_175794008             451 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia ambifaria].
ACCESSION   WP_175794008
VERSION     WP_175794008.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..451
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47314
     Region          207..406
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mrldlcsrla reqgrparcg airfpirral vrgvvaaawl agmqgavawa ssdampfspv
       61 aaqaadlvdv pffssartiw gglvastavp rvaleprats tsvpfalrtg acapyvvlcd
      121 aardaierdy aarfaygfas plpaigvrag fdarpvdlas aepfvlaeqq sgtragaitg
      181 slraslarad lpagvaaqim rmlagridst qrgalgdtfr vaferddsat qparvrvtal
      241 dirfrgqrva avwfapqags pgayydldgm plagarfamp vnatrissrf garvhpvtgv
      301 rhvhsgvdla aptgravhas ergvvtfigt epggygkyvv irhdggyasy yahlsafept
      361 lrtgarvvrg qrvgavgstg tatgphlhfe vrrharlvdp ielveaaraa klkgeqrvaf
      421 nrvadaartq laaatlappl amsqsgapnd g
//
LOCUS       WP_175794014             452 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia ambifaria].
ACCESSION   WP_175794014
VERSION     WP_175794014.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..452
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=48381
     Region          17..434
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mdnitptfat draprvpriv ivgggagglq latrlgdtlg rrgqadvvlv drypthfwkp
       61 llheaasghr dpashtieya aqakrhgfrf vqgalhrvdr aartatiaav qdadgteilp
      121 qrelgyddlv lavgsvtnff nvpgaarhal plenldqaed frrkflaact kanhlaeqqp
      181 arpaapicin vigagatgve laaalrhaiq qlttyrfkal vsardvhirl ieggprilpa
      241 ldarlsarmh aqlrtlnvdv ltdtrvaevg adavttaage rlasditiwa agvagpailr
      301 elgdialnrs nqvivtdtlq tpddphvyaf gdcaacpsad asgflppraq vahqqavylg
      361 ealarrlagk plagftfrda gtvvslgqag avyqgdlgvr shslivdgla aiglykflyr
      421 khlfsvyglk ralfqslshw lqsrnqpsik lh
//
LOCUS       WP_175793886             419 aa            linear   BCT 11-JAN-2025
DEFINITION  M48 family metallopeptidase [Burkholderia ambifaria].
ACCESSION   WP_175793886
VERSION     WP_175793886.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Bode,W., Grams,F., Reinemer,P., Gomis-Ruth,F.X., Baumann,U.,
            McKay,D.B. and Stocker,W.
  TITLE     The metzincin-superfamily of zinc-peptidases
  JOURNAL   Adv Exp Med Biol 389, 1-11 (1996)
   PUBMED   8860988
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Stocker,W. and Bode,W.
  TITLE     Structural features of a superfamily of zinc-endopeptidases: the
            metzincins
  JOURNAL   Curr Opin Struct Biol 5 (3), 383-390 (1995)
   PUBMED   7583637
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..419
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46704
     Region          8..417
                     /region_name="M48A_Zmpste24p_like"
                     /note="Peptidase M48 subfamily A, a type 1 CaaX
                     endopeptidase; cd07343"
                     /db_xref="CDD:320702"
     Site            order(279..280,283,361,365,405)
                     /site_type="active"
                     /db_xref="CDD:320702"
     Site            order(279,283,361,405)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320702"
ORIGIN      
        1 mspfsftllf aiavlamvvt klwlasrqir fvaahrngvp aqfsatiplt ahqraadytv
       61 ertrlamfei vvsaavlvgl tllggvgald tlltgwfgrg ygqqvalvaa vlvittvidv
      121 pfeyyrqfgi eqrfgfnrmt krlfftdmlk ntllgavlgl pllfvvlwlm nqagglwwlw
      181 twivwvafqm lvlliyptfi apifnkfepl kdealrarie slmkrcgfaa kglfvmdgsr
      241 rsahgnayft gfgaskrivf fdtllarlsg eeveavlahe lghfkrrhvm krmlvsfvls
      301 lvllallgwl aqrtwfytgl gvtpsldtsn agaalvlffl aipvflffat pfssltsrkh
      361 efeadafaas qtdaqdlvsa lvklyednas tltpdpvyta fyyshppasq ridrlmqha
//
LOCUS       WP_175794040             302 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175794040
VERSION     WP_175794040.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32902
     Region          8..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..295
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(106,110,149,163,165,230,247,274)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(107..108,112..113,115..116,119,123,125..131,192,
                     223..224,226..228,235..236,239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 marrfdhlgd veafvtviek gsmtagaval gstpsvlsra itrletrlgv qllrrstrrl
       61 slteqgrlyl eqsraaflli ddaeraiqgh ggtltghvrl svpttyghyr lppllrqftq
      121 qhpevrveln ianrnvdlva egfdlairlg elpdsglvar kledaalclv aspeyvarag
      181 mpenvaelar hlclpfmlps sgriapwvfr dggqdidwlp psnvavsddv lgvvsmaqsg
      241 agicqtydfi vqdrvragsl vemlphlrgr srpfsviyap hrrlsaasra lidmivastg
      301 dh
//
LOCUS       WP_175794084             396 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia ambifaria].
ACCESSION   WP_175794084
VERSION     WP_175794084.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..396
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=41946
     Region          18..381
                     /region_name="MidA"
                     /note="SAM-dependent methyltransferase, MidA family
                     [General function prediction only]; COG1565"
                     /db_xref="CDD:441173"
ORIGIN      
        1 mnpkahesas lpapgpdala qsetlaaqlr deiaaaggwl pfdrfmeral yapglgyysg
       61 garkfgrrad dgsdfvtape lsplfaqtla npvadalaas gtrrvmefga gtgklaagll
      121 aalaaldvel deylivdlsg elrerqrdti aatapalagk vrwldalper fdgvvvgnev
      181 ldampvrlfa ksggawlerg valdarhafv fddrpvgaag lppvlatldv ddgyvtethe
      241 aalaftrtvc tmlargaill vdygfpahey yhpqrgggtl mchyrhhahd daflypglqd
      301 itahveftgi ydagvgtgad llgytsqarf llnagitdal aaidpsdihq flpaanavqk
      361 liseaemgel fkviafsrgi dgtldafarg drshal
//
LOCUS       WP_175794053             403 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia ambifaria].
ACCESSION   WP_175794053
VERSION     WP_175794053.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..403
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41690
     Region          2..397
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mkqplaivgs glagvraaqt lrangygdri ilvgeeaqhp yerpalskea lcggappvlc
       61 stedlntlel dwrrgaravs idggvlaldd gtsvatdgil latgararkv dlpgvslpgv
      121 htlralddaf alrdalaaqs eivvigggli gcevastark aghavtvves geelmeralg
      181 rmmglwarvq lqqlgvvihr satvasiegh trargvrlsn gaylpadvvv lsvgaqpcde
      241 laqtagaacm rgvvvdaagr stipgifaag dvaswplveg grrslesfln sqaqaavaac
      301 amigrvneqp qtalswteia grkiqlagdl tgsgemvirg detgasfsvf rvsngrvagv
      361 atvdapreya takrlvesri avqtnllads stelrsllsy kvn
//
LOCUS       WP_175794103             257 aa            linear   BCT 11-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Burkholderia ambifaria].
ACCESSION   WP_175794103
VERSION     WP_175794103.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..257
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28574
     Region          13..253
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mssslqsesi rgqvaelrer gfvvarglvg eaqcaalkri aerqlqeaae piefeadlry
       61 pgapeskhap gghtvrrlld aygrdpafae raiapeigaw mreyfgeqpv lsrthhncmm
      121 tkhpaygslt gwhrdfryws feradmvsvw lalgpetnen galwlvpgsh taefgpeafd
      181 dakffrgdlp enrkmidaat cpplqtgdvv ffhcntlhsa gqnrsdqvkf slvytyhgvs
      241 nrpvpgtrsa tkpevqf
//
LOCUS       WP_175794161             895 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175794161
VERSION     WP_175794161.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 895)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 895)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..895
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..895
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=97996
     Region          15..797
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnsqtlrsal lagpvqherl vkldtplgpn vllpyrvigr srlgrhfeft vdtvsvsdnl
       61 elkkliaqpv tlwilqanqs yaphhgyvhc arrlgsdsgv thyqivfasf lhflkfrrdq
      121 riwqdqsadd iiadvlnqhp qakgrftfkl hqplplrsfc mqyeddwnfv hrlmesegly
      181 gfweqdqdgk shrlvvvdrv dalpalsprt vrfhhagtgd eadtfvqfsg trtlrsvart
      241 trtfdykqpp saanpkatht ptianqgdlp pqlevyeytg aytyleqsrg dhlskiwmee
      301 qesrakrfhg vggvrrmdag rtfeladhpe hdkddagqre favietawvi vnnlpvadeq
      361 avfphslrae vgsivqatdt aqsrvrhpdg segffqirve aqrttvpfrs pfehakppmh
      421 lqsaivvapk geeihtdaln rvkvrfhwdr lndgdekasc wlratasdsg kgygavhphr
      481 ngeevlvdfl ggdcdrpiiv gkvyngatsp qwhsngilsg yrskeyagag ynqlvlddat
      541 sqnrvhlyss qtnahlhlgy lidhtgnnrg sylgsgfdlr sdaygavran rglyvtthpk
      601 qpasqpldvq etqqqlvrae glmeamsevg aqhqadpldh ghaalkqftd atqnsvsggt
      661 sggrtagggt gtanafkepv mlfgspsgig mstqqsvqla adqhvnlvsg qsthvaagks
      721 liasvldris lfaqnsgikl fagkgkvevq ahadnielta qkalklmavt esiegaaake
      781 illtsggayi riangnievh apgkidikga qhafsgpthl sqtmptlpns tgnydqafia
      841 hwagtdipva ntryqmfsng kllkegvtna agetgltqsh vphdvvvkfl gksng
//
LOCUS       WP_175794110             929 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia
            ambifaria].
ACCESSION   WP_175794110
VERSION     WP_175794110.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 929)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 929)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 929)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 929)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..929
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..929
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=98390
     Region          102..923
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mvqaarnial ggshdvdlsv frrgrvalav glafgigfpg ddagaaeasg sdvgpqagge
       61 pvmivaartm sdpvmqvaar attepvmqva arapaepaav afnprlfagg gvdlsrfakg
      121 npvepgnyav dvtvngkgrg rhdvpflavp gsdvaapcft lamleqfgvd gdklasrrrr
      181 skqdddgapa ahesapdacl tlratipdat ytfdsadlkl dltipqtams ktahgyvdps
      241 rwdeginvgl lqynvngyts esnffghnfs slytglqsgv nigpwrfrhr stlnwasrss
      301 gvswrsletf vqrditalrs qivlgdsfts gevfdsfgvr gvqlssddrm lpnslqayap
      361 tvrgiadtna rvvvrqggnt vyeetvspgp fefndlpatg yggdldvtvt esdgrvrrfs
      421 vpfaavpqll rpgrhrfnvt vgqyrdnaid tkpwvaqlvy qrgitnlvta yagvlssagy
      481 gsgllgmaln tsagalafdv tsahtsvpgr rtyhglssrv tyskmlvptg tnfsvaayry
      541 stsnffslqd avnarkdwng sigqynyrar trlqlnvnqr lgdrsaiyvt gssqdywgge
      601 rgrdlqyqvg fnstfrqvsy avyaqrarng dnrtvtqvgi nltiplgkqt ytksslfnsl
      661 ttsasrdssg nsaiqmdmsg skgsvapfsy gitasriagg danalssfgg ygtyrsavgt
      721 ysanaslsnr mrqasigang amivhrggvt lspplgqaaa lieakgatgg qivngqgasi
      781 drfgyavips ltpyrvntve idpsklpddv elgntseevv prynsvvfvk mgtvrgrpvf
      841 atmerhdgsp lpmgtqlfda sgksvggvgq ggmaflrgle gtgeltakwg igaadrcslp
      901 yavpaatada gkvkmatrvr lrcdtaamq
//
LOCUS       WP_175794290             247 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175794290
VERSION     WP_175794290.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..247
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26838
     Region          3..240
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mdvklvartl dlfelfaaer rplpltelar llnvpasscl amartlvsrg ylyevrkrgg
       61 yyptrrlqai aaaidatdpv vdivhphlva lrdasretav lgkiqgvsvt yldvveseqa
      121 irytrqpgel rplhansigk aifaelasea qqalgaqlsf erftdasvad lpalvaqtar
      181 frelgwaenf gesapelsai avaltldgdw yglsvvgpte rirqhrdtha allvdakarl
      241 laeqgrg
//
LOCUS       WP_175794278             425 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia ambifaria].
ACCESSION   WP_175794278
VERSION     WP_175794278.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..425
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45166
     Region          <225..357
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mwtplvkpaa ipdafapgra qrlvralvpa avlgalaafg laaalpavsq lpgavdsgta
       61 alpqrvlsdt pfptaqhfvt selartlger nelneqgdrs pqpglfapls ahrndmlgya
      121 slfqfaapet qhgtragdie ltlsdtlnrl dvppevriql gdlvtgkvam rasaqrgdyy
      181 riaydtnngt phltalelrv agrtfgaiwf rapgadhgay ytldgaplea aaftmpvkwt
      241 rissffgerv hplsqamafh tgvdlaapsg tpvnaaadgv vsfvgtdpdg ygryvivdha
      301 dgystyyahl sayarglktg etvkqgqrig svgmtgaatg phlhfevrva ndpvdplvtl
      361 anaqtglsdm qltafrqeva qwrfrlasik tspfafaqnd gslwgdfatd sstlravfnt
      421 hysas
//
LOCUS       WP_175794329             304 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia ambifaria].
ACCESSION   WP_175794329
VERSION     WP_175794329.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..304
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31996
     Region          5..298
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mqnhhevivi ggsfaglsaa mqlararrrv lvidagrprn rfaehahgff gqdgkppari
       61 vadaaaqlaa yptvqriage artaerdasg rfhvtladgt rasadrlila tglhdalpal
      121 pglaqrwgvs vlhcpychgy evsdrqlgvl athplsvhqa ilipdwgptt wftqrvvepn
      181 eeeaallgar gvrierspvv eilgdaphid alrladgqvv pidalfigar temasdlaqq
      241 lgcafdegpl gvairvdtwk qtsipgvfaa gdasslmtna tfasasgvaa gvgahrslif
      301 glda
//
LOCUS       WP_175794225             270 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175794225
VERSION     WP_175794225.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..270
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29069
     Region          4..256
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mpnletaqqf lmtrgldlgl nllaaivlwf igrwairigt rllgkvvrrs gkvdptlady
       61 ltsvvgvllt illilailqi fgvqttsfaa llaglglaig tawggllahf aagvfmqvlr
      121 pfkigdvisa ggvtgtvkel glfgttiita dnivtivgnn kifsdniany satphrrvdl
      181 takiangvda vdainrlktq iqvipnvlkv papdvgvlqf tpegpllfvr pstqpenywq
      241 vycdtnrvil etfrdaqypt petplshrnt
//
LOCUS       WP_175794361             163 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175794361
VERSION     WP_175794361.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..163
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17827
     Region          4..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 magitlddld lrilailqdd asvsnlqlae ralsspptcm rrvqrlteag virrqvavld
       61 pvaigtavta lieisldrqt aedydafeay vcaepavtqc yrvspgpdfv vvadladvae
      121 ydefarrlft gasnvrnvrt ffsthrakfe anarvahamr kra
//
LOCUS       WP_175794378             306 aa            linear   BCT 11-JAN-2025
DEFINITION  bestrophin family protein [Burkholderia ambifaria].
ACCESSION   WP_175794378
VERSION     WP_175794378.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..306
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33429
     Region          1..299
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 mivrprehwl rmllvwngsv lptilpqlvl tlaislvavw gggrvlgekv plnptpftli
       61 gltlaifagf rnnasyeryr egrqlwggvl tatrtlvsqa lcygaidadd aarqafvrkv
      121 iafvhalkhq lrgtdpaadl rallddgtha rivaaryapi aivhelreaf aarvdaghlt
      181 dtrlwmldar lddlvsmvsg ceriastpip fsydvllhrt iyaycvllpf glvdsigaat
      241 pfvtvfvayt lialdaiaha iaepfgdgpn hlaldamtrm iertllelnh eplpaevtpg
      301 payrlt
//
LOCUS       WP_175794405             783 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175794405
VERSION     WP_175794405.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 783)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..783
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=86363
     Region          1..736
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mptiqdvlkh pgsvvtqplh leiatldapi svvsfvlteq mntpfladit vtstdkridg
       61 asivgrpaif tieehatvps magmidpvrh aartvhgvvt qwtrvktsrd eatyqlhlkp
      121 rlslldevhd savfldrslr elltdtivdr nlfqsfdvef elegldgkfe qtvmyeetva
      181 nfidrhcrra gvyyyfkqar kedgpqrdtl vfgntprgym ralevpllph sglvnwheai
      241 ltleatrvlv pqkvrewdhd yrvpddplqv eavvanddrs vygsvnrsie hfhsveegqa
      301 ladarrdell trqlrlagts nvigmtpgmv vrivndvvpe aphgmvitkl vttgdrsqsv
      361 intfeaipah qtyrpeyvpe khwrwvagml igvvesgdde pyawmdeygr yrvrllfsrh
      421 sgkrgtnsmp lrllrtsasy qgglhipllp rsevrvvatq gncdrlliag alhdharrdl
      481 vhgkegwysr avfrspllgn klrfedlkdh egirlatvfg qsslnmgnlv draknkrgeg
      541 felttqhwgs vrapkglfvs adagggsetp hldmpaavaq lkaalervte laattsqmka
      601 apadratqaa lldglnqlrd agllasapgg mafvtpksaq hsagenvivt agrdmdvsvv
      661 rrlrmvagdl islcahklgi kifskgkiel qaqrapmdlf sdeqlhvssa nanvlvnakt
      721 ramvtsggas mtiedgnvvf ecpgefrira asfkfegpgn tsislpqlpv seyqpsakys
      781 htq
//
LOCUS       WP_175794452             325 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia ambifaria].
ACCESSION   WP_175794452
VERSION     WP_175794452.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..325
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=36238
     Region          110..316
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mdsiyygfvi ltfvavvlai egvyqwwnar hgaaarries rlramsaggs vqqerlsilk
       61 krmldeskpf drllmrvpri qaldlvlqqs gldwtvaklv visavlpvta alvltvsplp
      121 litvlpiall taclpamyvm rhrnrrmlkl erqlpdicdm iaralrsghs fssalgmvge
      181 efpepmggef ritfdeinyg vslhdalvnl atrvpahdlr yfviavliqr etggnlaell
      241 dsiaslvrer fklfdkvrvl saegrlsawi lgllpfgtaa mmamvnrefl svlwqdpagi
      301 kmvgvmlgsm afgllwirri irirv
//
LOCUS       WP_175794532             292 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia multivorans].
ACCESSION   WP_175794532
VERSION     WP_175794532.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 292)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..292
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31467
     Region          18..258
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 msasnepasp savadahddr vievrnltkr ygrnivhqkl dfdvrrgeiv sivggsgsgk
       61 ttlvrqilgl erptsgtikv fgqdtstida asarlmrtrs gmlfqhgalf ssmtvfdnva
      121 qplrelgrvp pdllhdivml klemvglpck haskmpaals ggmvkrvgia raialepell
      181 fldeptagld pqasdefvel iatlhrtlgl tvvmvthdld tmvalstrva vlanrkvlva
      241 apveeaanvd hpfiheyflg lrgrralqal pperraklpk aalepalssv el
//
LOCUS       WP_175794586             393 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase [Burkholderia multivorans].
ACCESSION   WP_175794586
VERSION     WP_175794586.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 393)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..393
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40332
     Region          1..393
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mtdvvivsaa rtavgkfggs lakvaapelg atviravler agvkpdqvse vimgqvltag
       61 sgqnparqsl ikaglpsavp gmtinkvcgs glkavmlaan aiiagdaeiv vaggqenmsa
      121 aphvlpgsrd gfrmgdaklv dtmivdglwd vynqyhmgit aenvakeygi treeqdafaa
      181 lsqnkaeaaq kagrfndeiv pvsipqrkge plqfatdefv rhgvtaesla glkpafakdg
      241 tvtaanasgi ndgaaavlvm saqkaqalgl tplarikaya nagvdpsvmg mgpvpasrrc
      301 leragwtpgd ldlmeineaf aaqalavhkq mgwdtskvnv nggaiaighp igasgcrilv
      361 tllhemvkrd akrglaslci gggmgvalav erp
//
LOCUS       WP_175794595             215 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia ambifaria].
ACCESSION   WP_175794595
VERSION     WP_175794595.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..215
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22445
     Region          6..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mhtsgslygf lviggmlavt pgpnmvyvms rsiaqgraag lislagvmig ylfymfgaaf
       61 gittlfmsvp yagtvlgvvg aayllylawq avrpggrspf evrtlpneqp lrllamgatt
      121 svlnpklaml fvsllpqfid yrqgsvfgqs lflgslliaa fasanglvav csssiakylh
      181 arpalllaqr wamglilgsl gvqmvvdask magva
//
LOCUS       WP_175794598            1051 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia multivorans].
ACCESSION   WP_175794598
VERSION     WP_175794598.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..1051
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114805
     Region          11..1033
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msaareegrf nlsawalrhq alvvylivla tvagilaytr laqsedppft frvmvirtfw
       61 pgatarqvqe qvtdrigrkl qetpaidflr sysrpgesli fftmkdsapv kdvpetwyqi
      121 rkkvgdigyt lppgvqgpff ndefgdvytn iwtlegdgfs paqlhdyadq lrtvllrvpg
      181 vakvdyfgdp aqrifievdn akltrlgisp qqlgqainaq ndvssagvlt ttddrvfvrp
      241 sgqfdnvaai adtliringr tfrlgdlatv rrgyddpavt qmrtaasgtg agkpvlgigv
      301 tmqpggdvir lgkaldaqsk alqaqlpagl kltevssmph avshsvddfl eavaeavaiv
      361 livslvslgl rtgmvvvisi pvvlavtalf mylfdiglhk vslgtlvlal gllvddaiia
      421 vemmavkleq gynraraaaf aytstafpml tgtlvtvsgf lpialaksst geytrsifev
      481 saialiaswf aavvlipllg yhllperkkh ahdahlpddh eheiydtrfy rrlrgwidwc
      541 ierrfvvlai tvalfvvsll gfslvpqqff pssdrpellv dlrlpegasf aatlreterv
      601 eqaiakrpei dhwvnfvgsg aprfylpldq qlqlpnfaqf vitaksvedr eklaswlett
      661 lrdrfpavrw rlsrlengpp vgypvqfrvs gddiatvrsi adkvaatmrg dartvnvqfd
      721 wdepaersvr feldqkkare lnvtsqdvss flamtlsgtt vtqyrerdkl iavdlraaqp
      781 drvdpaklag lamptpngav plgslgrftp tleygviwer drqptitvqs dvragaqgid
      841 vthaidgkln alrtqlpvgy rveiggsvee sakaqasina qmplmaiavf tllmiqlqsf
      901 srvlmvvlta plgligvvgt lllfgqpfgf vamlgviamf giimrnsvil vdqieqdiaa
      961 ghgrfdaivg atvrrfrpit ltaaaavlal ipllrsnffg pmatalmggi tsatvltlfy
     1021 lpalyatwfr vkrderdphd gdtppaapsg a
//
LOCUS       WP_175794606             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia multivorans].
ACCESSION   WP_175794606
VERSION     WP_175794606.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..359
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39039
     Region          8..355
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkhsferlrl dgvcrsftna egaqvaalng ldldirrgef iallgpsgcg kstalnciag
       61 lqpltrggiw lddtridvlp perrgfgmvf qnyalfphmt vldnvgfglk mrgvpnqear
      121 rraqqalelv qlvghegklp gqlsggqqqr vaiaraivie pplvlmdepl snldtklrie
      181 mraeirriht qleratiyvt hdqdealsma drivvmkegv vqqvaspkev ytrphnlhva
      241 rfmgyrnvlp ftlegmagdy vtvaaagvrl agvpmagfdg kavavalrpd dieradaaad
      301 ntfeatvetv eyggrdslir alapfgaiwa rvagefapge rltlrvapsr tlvypgdap
//
LOCUS       WP_175794614             338 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia multivorans].
ACCESSION   WP_175794614
VERSION     WP_175794614.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..338
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36898
     Region          180..317
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mlaevrpdgy tvpdtcrltf andlcaardg aeirvshgdg igaqllraql tddgalrlva
       61 ynhravpaeq rravlaalaa afavdvarps vrldaaawpa valdalrasg vlgdggqclr
      121 egwaqqadlw lvearppcat lptltdgrrh prrppaprae vyardvpalg vrftlrgwqp
      181 addpariarw feaprvrdgw pgaqpgtaad fephvtplvg cfdgepfayf eavwlkedal
      241 aphvaardyd ralrmlvges rwrgahciaa wlpsvvhylf lddprteaig cavpaghari
      301 adllarhgfa rrrrlaladg qplwmctrrd tffsgrhv
//
LOCUS       WP_175794641             818 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia
            multivorans].
ACCESSION   WP_175794641
VERSION     WP_175794641.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 818)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 818)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 818)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 818)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..818
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..818
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=87225
     Region          1..802
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mlvvgsqsha tefnssflsi dgttdvdlsq fsqadftlpg eymlevqvnd lfyglqpief
       61 valdasgagk pclraelvaq fglkpslakd lprfhggrcv dlaaiegvtv rylkgdgrlr
      121 itipqaalef tdgtylpper wsdgiagaml dyrviantnr sfgsggrqtn avqaygtiga
      181 nwgawrvrgd yqaqsnvgnt vyadrtfrfs rlyafralps iqstvtfgdd ylssdifdtf
      241 altgasirsd drmlppslrg yaplisgvar tnatvtvsqq grvlyvtrvs pgafalqnin
      301 tsvqgtldva veeedgsvqr fqmttaavpf lartgqfryk aavgkprrfg gagitpffgf
      361 geaayglpfd vtvyggfiaa sgytsialgv grdfgtfgav sadvtharar lwwngatrhg
      421 nsyrinyskh fdgldadvrf fgyrfserdy tnfaqfsgdp tayglanskq rysatmskrf
      481 gdtsayfsyd qttywerase qrvgvtltra fsvgalrnln vsvsafrtqs agasgnqvsv
      541 tatlpiggrh tvtsnlttgn gstsvnagyl yddpagrtyq isagttdgra sanasfrqrt
      601 sayqltaqas tvangyaaas levdgslvat qygiaahang nagdtrllvs tdgvrdvpls
      661 gtlthtdsrg yavldgispy nvydaavnve klplevqvsn piqrmvltdg aigfvqfsaa
      721 rgsnlyltlt daagkplpfg asvqdaangk elgivgegga ayltqvqpks slvvragert
      781 lctidtlpnr lqlegtpipv acdmtvapha aaqpetih
//
LOCUS       WP_175794661             959 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia multivorans].
ACCESSION   WP_175794661
VERSION     WP_175794661.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 959)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..959
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=104298
     Region          42..958
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mknhglsrrg flkasvlagv avyvaplgsr afaalfeekl ltpvkwdsvt giprfridgm
       61 akvtgskvfa rdvraadmph wpqqqshali lrvtqadriy egfdlsllgd elkpdrvvta
      121 ddlardgvaf pafygedmll pagktpaylg havailiyhd farfrfakna lkfrddviry
      181 gavtgplerd pwgtfryvrv ggktaydddv ysslkdapif psqmrkhqpv wpdgkehgkl
      241 deqgmfhagq iaaelehpsa dwlvfdreys tqsvdtaale pdnancwyda atqslhlvva
      301 sqsplevaen aaamvakcrf pvkklfvhpc ytvgygskdh cnvpfyglvc alyadgrpvr
      361 fandryeqfq tslkrhafrm hyriavdrnt gllqsfkgdf eangggrsnf spsvamvgat
      421 aaqsiyyfpk sdlaavaias raidagsarg ygtlqsmaat emaideiaaq lnidpidfrl
      481 rnalrsgmkn tqgaipagal rvdevlerak qhplwtrraa rkaefeaanp gkrygvgfac
      541 vqkdfgtgae asfakvefde ngkvtlhhta aeigtgmsts qavavakwlg rpatdvrvav
      601 tewpdlpvet sgdpytmsqa dqdrlsanpr wspsyaspss atnsafyfth streaaravf
      661 ryglwpaams iwsrglgggq aapytvried arwvdgklta dgleplsfeq lakqahalgl
      721 ptgavvhvfn rwqwtdaefe iggtverlpi dglslrigap ktgdehgpvp gtavpagata
      781 vrgtlpptan gyrvldrkrv fippmsrnna avtyytavgt lvelavheat gkvellthhs
      841 imecgnqisp qlvsgqlqgg lamgighalh eylplyedgp gngtwnfnry hlpratdvav
      901 wtqtgdvlpp lsetdppkgv aevvmipvvg aivngiahai ghrftdlpvt pqkiqevla
//
LOCUS       WP_175794645             240 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia ambifaria].
ACCESSION   WP_175794645
VERSION     WP_175794645.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Upton,C. and Buckley,J.T.
  TITLE     A new family of lipolytic enzymes?
  JOURNAL   Trends Biochem Sci 20 (5), 178-179 (1995)
   PUBMED   7610479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..240
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=25238
     Region          43..214
                     /region_name="FeeA_FeeB_like"
                     /note="SGNH_hydrolase subfamily, FeeA, FeeB and similar
                     esterases/lipases. FeeA and FeeB are part of a
                     biosynthetic gene cluster and may participate in the
                     biosynthesis of long-chain N-acyltyrosines by providing
                     saturated and unsaturated fatty acids, which it...;
                     cd01836"
                     /db_xref="CDD:238874"
     Site            order(53,90,118,209,212)
                     /site_type="active"
                     /db_xref="CDD:238874"
     Site            order(53,209,212)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238874"
     Site            order(53,74,118)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238874"
ORIGIN      
        1 mgypfataal gpllflqgrh vrrvtprlpe aagprdgvag dgpplrvlvv gdsaaagvgv
       61 asqhdalsgq lahtlaathr vgwkllartg lttrelvdwl atepaepfdv avtslgvndv
      121 tggvpparwq aqqaelvrll aarfqvghvi lsavppmerf palpqplawy lglrakrlna
      181 aladwaatqp nctflrvalp lerhlmaadg fhpgaaacaa waaqvadalp rqrapdlatr
//
LOCUS       WP_175794727             661 aa            linear   BCT 11-JAN-2025
DEFINITION  beta-galactosidase [Burkholderia multivorans].
ACCESSION   WP_175794727
VERSION     WP_175794727.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 661)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 661)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 661)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 661)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 661)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448998
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..661
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..661
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=74019
     Region          1..620
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
ORIGIN      
        1 mrvgvcyype hwpesmwadd arrmkalgia qvriaefaws riepspgeyd wgwldravdv
       61 laaagldivm ctptatppkw lidrhpeila igadgrpraf gsrrhydfss pvyydasrqi
      121 ctavaerygr hpavrfwqtd nemgchqtvv syspaalarf rewlkarygt idalnrawgt
      181 vfwsmeyrnf deidapvgtv teahpthrld yrrfasdevv ryhrmqvdvi rahspgrpva
      241 hnfmqlftdf dhyavardld vatwdsyplg aleehwfapd vkarwlrtgh pdfasfnhdl
      301 yrgmsklpfw vmeqqpgpvn wahwnpaplp gmvrlwswea fahgagcvsy frwrqapfaq
      361 eqmhaglhtp ddrldeggre aervvheiav vqgadahada avharvalvf dyeakwlldv
      421 qpqgadfqya riafeyysal ralgldvdvi saqapldgyr lvvvpplpiv pddfaarlaa
      481 sgahavfgpr tgsktvdlqi pptlppgala silplrvwrv eslrpnvter vdgalvdgtp
      541 fagharhwrd lvelrdaqrt vvrarfaddh pawlshgtlh ywaalfddat taqlfasvaa
      601 daglaptpla dgvrisrrgg ltyvfnygdt vhtidavppa afvvgsadve prgvavyrsp
      661 v
//
LOCUS       WP_175794878             370 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia ambifaria].
ACCESSION   WP_175794878
VERSION     WP_175794878.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..370
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39326
     Region          4..344
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,233,300,320,322..324)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,181,184,186,233,240,300,320,
                     322..323)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,181,184,186,323)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            186
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mssllstydl rglplpnrvv mgpmtrsrap srgqptalma eyyaqrasag livteatnvs
       61 htsaafeltp glvtdeqaag wkqvtdavha nggrifaqlw hggrvssltl lggdaplsps
      121 gvnddleqlq vwarlqngyy tkihatpsra mttdevaatv ddfgraaara maagfdgvei
      181 haangylphq flsstlnrrd dryggsvanr arfleeivda vggvmplsrv gvrispyaqy
      241 nnvrdadpda tyayvgrmld eagvaylhaa dtngwsgepd lpriiertrk tfggtlivng
      301 gitpdaanal idagdadlva farayianpd lveriathap lavpksigwy ggeragyvdy
      361 arhdaaapta
//
LOCUS       WP_175794830             270 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia ambifaria].
ACCESSION   WP_175794830
VERSION     WP_175794830.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 270)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..270
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29000
     Region          15..264
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mthavphtag dmtcaavglt lkagdrtlld gftqafrpge iwcvagpnga gkttllatla
       61 glrqptgghv eidrvplaaw ppeqlarrra lmpqqlhdaf satvfdtvll nrfpylggwg
      121 werdgdraaa rdalatfgls alasrdvlsl sggerqrval aatlcqdapl mlldeplahl
      181 dlhhqidglt alctwldagp rtvlfschdl nlarrfatha llldgrghaw agpvhdvltp
      241 arasdafgyp lvlirengrd allpawperr
//
LOCUS       WP_175794882             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175794882
VERSION     WP_175794882.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32243
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdkfsalraf vevaeaggfs sagrrldlaa ssvvravdal easlgtvlln rttrqvtlsd
       61 agavyyartk qllealaead alvadrgdep sgplrvsvpv aygmhriaph vgaflarypr
      121 ldldlqltda rvdlvtgrid vairlgeaap saevvarqlg tfrryvvasp dyldahgtps
      181 tpgelvdhgc lrfhfggdqq awsfvdahga tkvlvtgrlk snhsevlraa aldgggiall
      241 pdwlidadvr agrlrrlfeq ydvvpdaars ivtalylpnq rgskrvtafi dfveaqartp
      301 c
//
LOCUS       WP_175794940             323 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia ambifaria].
ACCESSION   WP_175794940
VERSION     WP_175794940.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..323
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34024
     Region          13..224
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(54..55,57,71..73,79,81..82,123,223)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(54,56..57)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(79,82,85,92)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(115,119..122,124)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(120..121,144..146,197..198)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          239..323
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 miendllaar viarervacd vislrlvsda pglalpafea gahidlhlrd gltrkyslcn
       61 dpvergvyei aikrepassg gsahvhdair vgdvlrigap lnyfplapdd spavllaagi
      121 gvtpllamah slvragrpla fhyfvrsada aaygatlasr ladvatvhtg ltpdatrdai
      181 ttivgamdsr shlyfcgpap fmaavdaiar palgdarlhq eyfsapaaep adgeadafri
      241 elarsqrall vppgqsitdv lyehgiavat sceagvcgac rttvlegtpd hrdaflsaae
      301 karndcmmpc vsrcrgerlv ldl
//
LOCUS       WP_175794959             355 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia ambifaria].
ACCESSION   WP_175794959
VERSION     WP_175794959.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..355
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38387
     Region          1..340
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfvfdedqe aladsvkrll mtemtpelir elwatptgrs dalwslfasq gltavsvpea
       61 ygglglteve wallaqtygy fgspeplldt alvaagvlar lpasgwrdal lrdiaegrar
      121 valvhpvnpy aadvhvaqtl lcehrgelhr vepaqcawra idsvdpsrrl ftldwepsaa
      181 tciasadeaa pllnraldhg afavaaqllg ltqrvldvai dysaqrkqfg kaigsyqalk
      241 hlladvairy efarpvlara aqaiaddhpq ravlvshakl aataaaqlaa rhtmqvhgai
      301 gytweldlqi fmkriwalsg swgdsafhka rvadallgda lpigpaqtfd fegth
//
LOCUS       WP_175794990             368 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia multivorans].
ACCESSION   WP_175794990
VERSION     WP_175794990.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..368
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40466
     Region          4..368
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkaddvivsf rgvrktydge tlvvksldld irrgefltll gpsgsgkttc lmmlagfefp
       61 tggeirldge llnhvpphkr nigmvfqnya lfphltveqn vaypltvrkl paaeraervt
      121 halkmvqmer fakrypaqls ggqqqriala ralvfepklv lmdeplgald kqlrehmqye
      181 lkalheklgv tfvyvthdqg ealtmsdrva vfdkgivqql dtvdrlyesp cnefvanfig
      241 dsnrlrgtia rvdgefcelr lgdgtrligr nvanaapgaa aiacirperm rlcrepeppa
      301 ahgdaanrva gealgliyfg dhvrmrcavp gqgecfvkvp lgtealdnff pgapvslsfa
      361 pahlrvfa
//
LOCUS       WP_175795001             557 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Burkholderia multivorans].
ACCESSION   WP_175795001
VERSION     WP_175795001.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60603
     Region          25..384
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          453..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mtpaslieqy gpresmeydv vivgggpagl saairlkqla aekgteigvc vlekgseiga
       61 hilsgavmdp raltelfpdw kergaplnve vtedrflfls eksavqapnw alpdnfknhg
      121 nyvislgnvt rwlgqqaeal gveifpgfpa aeilynddgs vkgvatgnmg vgkdgepten
      181 fqlgmelhak ytlfaegcrg hlgrqliakf kldanadpqa ygigikelwe idpakhkpgl
      241 vihtagwplk pdtyggsfly hmdnnqvvvg fvvglgytnp ylspfeefqr ykthpsiraf
      301 leggkrvsyg araitagglm slpktvfpgg aligddagfl nasrikgsha aiktgmlaad
      361 aafdavqagr qsdelnaypd afrqswlyte lyrarnfkqw makglylgtl mvgieqklmg
      421 gnvpwtlhhk hadhemlkpa sqcepivypk pdgkltfdrl ssvfisntnh eenqpahltl
      481 kdpsvpvnvn lrtyagpegr fcpaavyefv knddgsdrlv inaqncvhck tcdikdptqn
      541 ivwvtpeggg gpnypnm
//
LOCUS       WP_175795002             390 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia multivorans].
ACCESSION   WP_175795002
VERSION     WP_175795002.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..390
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42941
     Region          12..282
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 midgqillgh sipwamvggg lgsqigyshr saalrdgsfr lvagafdldp ergrqfgvkl
       61 gvdaercypd yqtmfdaeak redgiravsi atpnnthfei craalnaglh vvcekplcft
      121 tqeaealqrl aveknrivgv aygysghqmi eqaremiarg dlgeirivqm qfahgfhseg
      181 veaesaaarw rvdpkfagps yvlgdigthp lyiaevmvpw lkirrlmcsr qsfvksrapl
      241 ednaftimey dtgaigyvws savnagsmhg qkvrvigska svewwdehpn qlryevqgqp
      301 aqvldrgmpy lhpnalredr igaghpeglf dawsnlyarf alamdaadrg dadalqgirf
      361 pdvhagvegv hwvencvrsa daggvwvdyr
//
LOCUS       WP_175795031             153 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175795031
VERSION     WP_175795031.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..153
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16741
     Region          14..126
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(15..17,31,48..50)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(62,65,69..70,79,97,101,107,111,114..115)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 msktvskpsa agsltigqva eltgvsthtl ryyeqagllr aisrtaaghr lyapadldwl
       61 afvmrlkatg mpiaqmqqfa alraqgestf gerrrllaah rdavrahiae lqasldaigd
      121 kivyyetqer eterrakpth slseqdghhg ttr
//
LOCUS       WP_175795103             343 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175795103
VERSION     WP_175795103.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10859374
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..343
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38740
     Region          3..99
                     /region_name="HTH_NolA-AlbR"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators NolA and AlbR; cd04788"
                     /db_xref="CDD:133415"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133415"
     Site            order(51,54,58..59,68,81,85,91,95,98..99)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133415"
     Region          <260..>306
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 mrlkvgelak rsgltvrtlh hyhaiglltp saradngyrl ydrddiarlh qiqalrrfgl
       61 slteigdhln qpgttplvel varqialldr qlaqtaqlre rlvslhaqla agtepeladw
      121 lttlelmtvy dkyfseeela rmpmyqksqa gdaewislig kvralhdasv ppedervral
      181 aarwmallvr dtnndprlla klnlmherep amqskigist alrdyvlrat aeskmrifek
      241 ylapdeirfm rahygerame wpqlmadvrd aidagatpds sqgralaqrw ldlfcsyagh
      301 dpathakfrh almnepaltk dswtddtllg fvrdamaqlv par
//
LOCUS       WP_175795129             315 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175795129
VERSION     WP_175795129.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..315
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=34449
     Region          11..301
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mqhhqqssat iegivpvmlt pfddagaidy aglerliewy lahgsdalfa vaqssemqfl
       61 slaeraelar fvvervagrv pvvasghise dldaqvaelr avaesgaqgv vlvtnrldpq
      121 rkgsavllah lhkllarlps dlplglyecp apyrrllsdd elracidtgr fvmlkdvscd
      181 letvkrrval aagsplkiln anaaiawdam kagsagfngv ftnfhpdlyr wlrtrgdsdp
      241 aladelstfl vvsavsealg ypalakiyhq rigtfasirc raidydvrer fwaldavldk
      301 ivsgtehfrr riaar
//
LOCUS       WP_175795131             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175795131
VERSION     WP_175795131.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46146
     Region          22..420
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,150,
                     153..154,157,245,248..249,252..254,257,285,289,347..348,
                     352,356,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnenhavpta pprirraqri alallmvsgi vnyldrgtla vassairndl glslsemgll
       61 lsafswsyal cqfpvgglvd rigprrllgv glivwslaqa sggivstfgw fivarivlgi
      121 gdapqfpsaa rvvsnwfplr argtptgifn aasplgtala plllavlvas fnwrwafvat
      181 galglvvavi wfalyrdpar aqltmaeray ldadaqtava tpkltfadwr slfshgttwg
      241 mligffgsvy lnwvyltwlp gyltmerhms lirtgfaasv pflcgfvgsl vagwlsdvvt
      301 rrsrspvvsr rnavvvamlg mvaftipaal vqsntvalac isvviflana asacswalat
      361 aaappsrias lgaiqnfggf iggalapilt gviaqkwsfv palltaaaia fagamaylll
      421 vrkpipeqaa stasgalpa
//
LOCUS       WP_175795144             473 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia ambifaria].
ACCESSION   WP_175795144
VERSION     WP_175795144.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..473
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50361
     Region          4..473
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 misseafvsa crdaigaagv ltephdtepf ltdwrrrykg sacavlkpad taevaalvrl
       61 anthgvalvp qggntglagg atpdasggqa vlslarlnrv raldphnnti tveagvilad
      121 vqarareggr lfalslaaeg sctiggnlst naggtavlry gnarelclgl evvtpqgeiw
      181 dglrglrkdn tgydlrdlfi gaegtlgiit aavmklhplp aaqvtalaal esphaaldfl
      241 alaqraagpl ltgfelmsdf cmqlvgkhyp qlrypfdrph aqtvllelsd nesetharal
      301 feklmeeafe aglvvdavva enlaqsrafw glrehiplaq adeglnikhd iavpissiar
      361 fidetdaaiq qaapgarmvt fghlgdgnlh ynvqtpeggd pkaflaefqk pinrmvydnv
      421 hrhhgtisae hgigqlkidd aqrykspvet almrtlktal dprglmnpgk vlr
//
LOCUS       WP_175795169             207 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD family hydrolase [Burkholderia multivorans].
ACCESSION   WP_175795169
VERSION     WP_175795169.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..207
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23114
     Region          3..191
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mtikavvfdf ggvlidwspe ylyrkliadd aerrwflthv camewvvrqd ggqtieegtn
       61 elvaqfpehe alirafyarw hemiggvlae gvalverlea rgmplfgltn wsaqtfpyaw
      121 ehfpvlrrfk divvsghvkl vkpdpaiyra mharvdphlp giaphelvfi ddnaknaaaa
      181 talgwhgihh tsaaatearl relgala
//
LOCUS       WP_175795183             301 aa            linear   BCT 11-JAN-2025
DEFINITION  ketopantoate reductase family protein [Burkholderia ambifaria].
ACCESSION   WP_175795183
VERSION     WP_175795183.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..301
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31648
     Region          1..298
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mrfavlgaga vgcyfggmla lhghevmfig rplhvdaird hglriqtrtf dtrvfahast
       61 diaaagsadv vlvcvkagdt aeaarglrhv lapdaivisl qngvdnaall raeiaqpvic
      121 aavyvasema gpghllhhgr gdlaieasps serlaqvlra adiptriadd vravlwrkfm
      181 lncaynaisa ivhlplgemp hrdalretmc aivaeciava aaegvhvdde padivahiea
      241 tippgqysst aqdlargkpg eidhlngavv rrglaarigt pvnrtlhllv kmleakaaar
      301 s
//
LOCUS       WP_175795199             230 aa            linear   BCT 11-JAN-2025
DEFINITION  YoaK family protein [Burkholderia ambifaria].
ACCESSION   WP_175795199
VERSION     WP_175795199.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..230
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=23190
     Region          6..203
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mksedtllsa vagfvdtlsf vslfglftah vtgnfvliga gvagfgqglv lklsvfpafi
       61 cgviaaslia rslsarpawq garalyavqa vmllgfcaag vwatpvtqsd slpvlvagiv
      121 gtfamgvqna hprviarasv pntvmtgnvt qaildvvdll sagtadsarm aararfgkml
      181 paivafalga magalgfryi gfwallapag alaalalmsg ahdtapavrs
//
LOCUS       WP_175795283             290 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia ambifaria].
ACCESSION   WP_175795283
VERSION     WP_175795283.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..290
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31583
     Region          15..280
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mttarsldrt ypalrttegg gfvvhrpfpt rllmdfdpfl lldemgpvdy apgeakgapd
       61 hphrgfetvt yvldgrfrhr dsaghagtlg pgdvqwmtag agvvhsempd pefaqaggrs
      121 hgfqlwvnlp rrdkliapry qeisadrips atspdgraqv rviageafgv raaietrtpi
      181 lyqhftlqpg atvtqpvpag yrvfaypldg agrygpdrqs vdarhmvvyg ddgdavtfea
      241 gdtpldllli ggvplnepiv rygpfvmnte eeirqavvdy qtgrmgriea
//
LOCUS       WP_175795250             198 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Burkholderia
            multivorans].
ACCESSION   WP_175795250
VERSION     WP_175795250.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..198
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20963
     Region          44..>185
                     /region_name="COG3576"
                     /note="Predicted flavin-nucleotide-binding protein,
                     pyridoxine 5'-phosphate oxidase superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442796"
ORIGIN      
        1 mryatvskln taaaqhgrav fgifttracv paaiawhaac vciahrpspa aapirsmhap
       61 apltddaiaf ireqafliva tsddagnsdc syrgrqprad gtpaplvasv dartlvlpdf
      121 agnnlfntig nllvnpaial lfvdfvrqtt clvqgratid edagrfaalw pdarryvivd
      181 vecaqprtda tlpplvla
//
LOCUS       WP_175795318             374 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase, partial [Burkholderia ambifaria].
ACCESSION   WP_175795318
VERSION     WP_175795318.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 374)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..>374
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
     Region          1..374
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mtdvvivsaa rtavgkfggs lakiaapelg atviravler sgvkpeqvse vimgqvlaag
       61 sgqnparqsl ikaglpsavp gmtinkvcgs glkavmlaan aiaagdaeiv iaggqenmsa
      121 aphvlpgsrd gfrmgdaklv dtmivdglwd vynqyhmgit aenvakeygi trdeqdafaa
      181 lsqnkaeaaq kagrfndeiv pvsipqrkge plqfatdefv rhgvtaesla glkpafakeg
      241 tvtaanasgl ndgaaavlvm saqkaaalgl tplarikaya nagvdpsvmg mgpvpasrrc
      301 leragwtpgd ldlmeineaf aaqalavhkq mgwdtskvnv nggaiaighp igasgcrilv
      361 tllhemvkrd akrg
//
LOCUS       WP_175795335             189 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Burkholderia
            ambifaria].
ACCESSION   WP_175795335
VERSION     WP_175795335.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         <1..>189
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
     Region          1..>184
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 aairlkqlaa ekgteigvcv lekgseigah ilsgavmdpr aitelfpdwk ergapldvav
       61 tedrflflse tgavttpnwa lpanfqnhgn yvislgnvtr wlgaqaealg veifpgfpaa
      121 eilynddgsv kgvatgnmgv gkdgeptenf qlgmelhaky tlfaegcrgh lgrqliskfk
      181 ldanadpqa
//
LOCUS       WP_175795388             633 aa            linear   BCT 11-JAN-2025
DEFINITION  acyltransferase family protein [Burkholderia multivorans].
ACCESSION   WP_175795388
VERSION     WP_175795388.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Bera,A., Biswas,R., Herbert,S. and Gotz,F.
  TITLE     The presence of peptidoglycan O-acetyltransferase in various
            staphylococcal species correlates with lysozyme resistance and
            pathogenicity
  JOURNAL   Infect Immun 74 (8), 4598-4604 (2006)
   PUBMED   16861647
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Slauch,J.M., Lee,A.A., Mahan,M.J. and Mekalanos,J.J.
  TITLE     Molecular characterization of the oafA locus responsible for
            acetylation of Salmonella typhimurium O-antigen: oafA is a member
            of a family of integral membrane trans-acylases
  JOURNAL   J Bacteriol 178 (20), 5904-5909 (1996)
   PUBMED   8830685
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15196437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..633
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=69323
     Region          2..348
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
     Region          399..622
                     /region_name="SGNH"
                     /note="SGNH domain (fused to AT3 domains); pfam19040"
                     /db_xref="CDD:436916"
ORIGIN      
        1 mshpgvsyra didglravav slvvlfhafp sllpggfvgv diffvisgyl igsillrefa
       61 agsftyrafy arrirrifpa lllvltacya fgwfellade fkqlgaqiag gagfvsnivl
      121 wkgagyfatq aekqpllhlw slgveeqfyi vlpiafwiaf kfrrgpliai allwiasfvv
      181 nivsvqqhpv aafflpsgrf welmtgcala wlqnvkrvev grwvnaisvi gagmiavavv
      241 linekrifpg wwallpvlga tlliaagpra tvnrallsrq vlvqvglvsy plylwhwpll
      301 vfgrildaat psvvfrlgav aasivlaflt tylvekpirv sirkprwavt mlcvvmlcvg
      361 lagantyrrd gmafrltama grftstdfdv ktawrekvcf rdgddkpqfp dvcqgagtgp
      421 lvllwgdsfa aslypgiesl qrqyafrlaq ytasgcppll padarsprca aiheqsveai
      481 rqlkpelvvl qanwsqddle kmpntiaalr avgvgkivmv gavphwhdkl pnvywaywrk
      541 nghqtlpsrs sfdldesfat idaavaavaa aqhvgfvdsy ralcdargck trigegkgei
      601 vafddahltp sgakylvaqv vdqigipvia arr
//
LOCUS       WP_175795434             485 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia multivorans].
ACCESSION   WP_175795434
VERSION     WP_175795434.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..485
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52733
     Region          30..451
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(40..41,44..45,48,80,130..131,133..135,138,158,
                     161..162,165,285,288..289,292..294,297,324,328,377..378,
                     382,386,402,405,407,410..411,414)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mnqtfevgra hqlterlstl rqgrktfvlf vaigvacmve gldivsmsvv lphikvlfhl
       61 spqdvgllaa astfgitlga lptglladrf grrktllagf lvcscftfls gvaadywmlv
      121 vcrfasglgm aaifampygl vsevvpsarr gmyvsivetf lglgyllapv fglvcfgfir
      181 qdyawrvdli lsglpalfff firrnviesp kwliskdrld eaeaiisrle ewgstttprs
      241 slvekvlpaa prtaflenrl siskalrtvf sapliwqwia lgggvfgvfa vfyvaiaflp
      301 svflarglsy thslwyalva tafqvpgkic msilgdrigr kaafgicivl aalflglfcy
      361 ftdpistmff staflffiag sgplcklwya elfptacrat gqnivegffg rllggvvwvs
      421 vfpvlthhfg qnqvlayvaa mlvilsipal lftpetrkhs apiesdvare spesgdglrs
      481 gvsgg
//
LOCUS       WP_175795657             245 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Burkholderia multivorans].
ACCESSION   WP_175795657
VERSION     WP_175795657.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..245
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25305
     Region          165..243
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mqpshsasag vlpavprmnl rvvavavgvl aahaimltaa wlhrsapppk svevqsitaq
       61 liappapvaq qvaaesipqp tppkpvphvk pkvepkpvpk vakpapqpva pspepsptpa
      121 paaaepspaa paapapapap apgparetmq vsapknvptl qcsfvkpdyp amsrrrgetg
      181 tayvhfvvgv tgkiesielq kssgyprlde aaldamratt crpyiengqa iraartqpyn
      241 fgltd
//
LOCUS       WP_175795669             264 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia multivorans].
ACCESSION   WP_175795669
VERSION     WP_175795669.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..264
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29330
     Region          4..264
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mlgmlralwa yrgfilgsvk refqskyrns llgaawtvln plamivvytv ifsqvmrarl
       61 pgvdssfays ihlcagvlpw gmfveivsra qnafidnanl ikklsfprlc lpvivvanal
      121 vnfaivfglf vaflvmtgnf pgvafaavip llvlltlfai glgitlgvln vffrdvgqff
      181 givlnfwfwl tpivysidil pkpvqgwmqf npmasliqaf qvvmmegkwp ewsrlwlvia
      241 lgvglcligf slfrkhagem vdel
//
LOCUS       WP_175795682             303 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia multivorans].
ACCESSION   WP_175795682
VERSION     WP_175795682.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33832
     Region          6..>146
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          95..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(105,109,148,162,164,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(106..107,111..112,114..115,118,122,124..130,191,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mtaladlndi avfvrvaqfe sfsraaralg mpvstvsrkv saleerlgat llqrttrkls
       61 ltaqgrayfd qcseplshly daervitqtq kkpegvlris gpvmleqepf yaflsaflkd
      121 ypqiqvdlyf tnafidliae nvdiairfge lqdsslvaqr vgrsvrqlvv sadyarthtl
      181 psrpeelsqh pcvlinarnn etewqlvsrr kavkvhvsgp vaardfhivh afalrghgia
      241 llpssycdph iasgelvhvl pdwsspeifv havyptrrfm psklkaflda lkawegplwl
      301 plc
//
LOCUS       WP_175795683             861 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Burkholderia multivorans].
ACCESSION   WP_175795683
VERSION     WP_175795683.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 861)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 861)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 861)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 861)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 861)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 861)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 861)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..861
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..861
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=94938
     Region          74..679
                     /region_name="RloC"
                     /note="Wobble nucleotide-excising tRNase [Translation,
                     ribosomal structure and biogenesis]; COG4694"
                     /db_xref="CDD:443729"
ORIGIN      
        1 mskdsfeewl aehprwlqta aarllgsqrp pddkdinala dlclaevskd qaavfekvpi
       61 gaftaaiaal nirlskiekv ngvnairqga tldfdnkdfa ivygpngagk sgfarlvkna
      121 cgartrtdll snvfeakpia psaefvvmhn gkseavgwta atgpagklrh ihvfdsavaa
      181 syvndknvas yeprrmrfis tlieiservv aeltrrknal ptklpqippd htdtkaglfw
      241 aaikptttrd avetaciwtd adaderlkie nslkqqdisg rlkelerqkk llaqlesevk
      301 slrdalsddk llavlnarrd aaekrkaasd daervfanap ldgvgkqswr lmwdqarqys
      361 eelaypkrsf pavdenedkc vlcqqpldea artrlsdfea yvkggletsa kaaeklrdtl
      421 ikalpvlpsa ekwrldvglv kieatdadgl lgsiharraa aetaaveadl psinwaqldd
      481 giatvaaslg kegalltelq kdgkkaehek tlkelrarew maqqkaalea eiqrrgvvrn
      541 vedairlagt haltrkkndl adeelakgyq erflaeisal ggkrllvspe plqegkgris
      601 ftltlrdtkq naaahavlse gesrivalaa fladitgsgq ptpfvfddpi ssldqefeer
      661 vadrlvelsr trqvivfthr lsllalleda ldkasknaaa tggafpsraf vslrrlgslv
      721 gvvdtldvrr erpdkgftkl rdhrlpvlrk lldagdvsyd nemkavcgdf rilversvek
      781 vmlnglierf rrsvqtqqir slakitqddc vlvdqmmtky srfehsqsde idanlpgvde
      841 laddlkhmid wigefekrav a
//
LOCUS       WP_175795747             366 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia anthina].
ACCESSION   WP_175795747
VERSION     WP_175795747.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Saurin,W. and Dassa,E.
  TITLE     Sequence relationships between integral inner membrane proteins of
            binding protein-dependent transport systems: evolution by recurrent
            gene duplications
  JOURNAL   Protein Sci 3 (2), 325-344 (1994)
   PUBMED   8003968
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004772
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..366
                     /product="ABC transporter substrate-binding protein"
                     /calculated_mol_wt=39949
     Region          62..364
                     /region_name="AfuA"
                     /note="ABC-type Fe3+ transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG1840"
                     /db_xref="CDD:441445"
ORIGIN      
        1 mpfapkhlaa alaivlgtva ggaaaqvpag ypgnyqgmvd aakkegrliv ysttdtglvr
       61 plikdfesly gvkveyndmn stelynryis enaasstsad vlwssamdlq vklvndglma
      121 sydspespnv pqwaqyqkqa ygttfeplai vynkrlipen evpktradli kllttqadkf
      181 kgkvttydie ksgvgfnylt qdahvnekvt welvkaigat gpklqsstga mmerissgen
      241 ligyniigsy ayakakkdks igyvfpkdyt qvvsrlatis kkaknpnaak lwvdyllskr
      301 gqtlianqan lyairadvng etsaasltke lgdslkpiqm gtgllvyldq skrlaflkqw
      361 qqaikr
//
LOCUS       WP_175795748            1055 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia anthina].
ACCESSION   WP_175795748
VERSION     WP_175795748.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..1055
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112954
     Region          1..1038
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mwivnlalrr pytfivmaim ivlatplalm rtpvdvlpav nipvisviws yngfsaqdmt
       61 nritavheri ltttvnniqh iestslpgia vvkvflqpga nvqtaiaqtv ssaqaivrqm
      121 pqgatpplvi tysassipvi qlglssktls eqsladialn flrpqlitvr gaqipfpygg
      181 rtrvvaidld pqallakglt padivnaina qnlvlptgta kmgqteyrid tnasadtiad
      241 innlpiqtvn gattylreva avrdgfapqt nvvrqngqrg vlisilksgd astlkvvsdl
      301 kallpkvipt lpegltitpl fdqsvfvnaa vqgviheali aavltammil lflgnwrstl
      361 iiaisiplsi ftslialsal getinimtlg glalavgilv ddatvtieni erhlhlgtnl
      421 hdailegage iavpafvstl cicivfvpmf fltgvarflf vplaeavvfa mlasyvlsrt
      481 lvptlamllf rpqqastgpd hstsrfarih hafnnaferl rawyivllsi llvrrrfyam
      541 cflgfcvlst glvftlgrdf fpnadsgnir lhmraptgyr ieetarladq verviretvp
      601 pdelgaivdn lglpvsginl sysnagtigs ldgellialk pghratehyv rtlrallpqr
      661 fpgvefffqp sdiitqilnf gqpaaidvqv lgndlasnma iasslmkkir qipgavdvhv
      721 lqrndgptll admdrtrmqq lnlsaqnvaq nmlislsgss qttpsfwinp rtgvqyplqi
      781 qtpqyniasv ddllgtpvsa sgragtplql lgnlvqirta qtpavithyn irpaidlyvs
      841 vegrdlgsva geidrvmsda ratlprgtdl svrgqvetmr tsyiglgagv amaivlvyll
      901 ivvnfqswld pliiisampa alagiawmlf itgthlsvpa ltgaimtvgv atansilvvs
      961 farqrlaaga ppltaaleag atrirpvmmt alamiigmvp malglgegae qnaplgravi
     1021 ggllfatvst llfvplvfgg vhsrlarrra rqagh
//
LOCUS       WP_175795759              88 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein, partial [Burkholderia ambifaria].
ACCESSION   WP_175795759
VERSION     WP_175795759.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..>88
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
     Region          19..>88
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mttltgrcsp rwirallsqa wvgslvrlal vsafliggvn kamhfgdava eqahfglhpp
       61 alwaalaiav eiggslcvvf rrftwlga
//
LOCUS       WP_175795804             206 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175795804
VERSION     WP_175795804.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23463
     Region          9..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mqiarqaqqe rseqtradil dialeqfstr gfdavslrdi adaagvnham iryyfgnken
       61 lwraavtqlf drfmagvelp spssdtfsin aikqyirnyv rycaahpeha rlmmqeanrd
      121 serlkwmaet fvrprhdrtv pliryvseqi dglagidpvr llymitaiaq vpylltaemr
      181 yahgidalde qaidahcdav ialvfr
//
LOCUS       WP_175795811             211 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175795811
VERSION     WP_175795811.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..211
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23069
     Region          22..179
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtdrtstttt kddapagktp rtkpaevrle elmaaaetlf laqgvdatti seivehaqva
       61 kgtfyhyfes ksdmlaalaq rytasflerl rqavdacaeg dwlgrlrawi rtnietyaat
      121 yrihdivyan hhhhdrtnad rnaiveqlra ileggaqaga wrlahptvta lliyagvhga
      181 tdhiiaapdt nratfveavv adclrmlgid a
//
LOCUS       WP_175795847             341 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia anthina].
ACCESSION   WP_175795847
VERSION     WP_175795847.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..341
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37244
     Region          180..320
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mlaevrpdgi tmpdtcglvf addlfaardd aeirvahgdg igaqllraql addgtlrlva
       61 ynhraapadq rrallaalaa afsddvrraa irldpaawpa valdelrasg vladgglcmr
      121 egwaqqadlw rvgahlpcat lpmltdgrrh prrppaprgd vyardlpalg vrftlrgwqp
      181 gedaarvarw fdeprvrdgw pgtqpgadgt apdadphvtp lvgcfdgepf ayfeafwlke
      241 dplaphvgar dydrglrmlv gesrwrgphc vagwlpsvvh ylflddprte algcavpagh
      301 arvvdilarh gfarqrrlal adaqplwmha lretffsgrh v
//
LOCUS       WP_175795856             528 aa            linear   BCT 11-JAN-2025
DEFINITION  MDR family MFS transporter [Burkholderia anthina].
ACCESSION   WP_175795856
VERSION     WP_175795856.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..528
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56406
     Region          37..516
                     /region_name="MFS_LmrB_MDR_like"
                     /note="Bacillus subtilis lincomycin resistance protein
                     (LmrB) and similar multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17503"
                     /db_xref="CDD:341046"
     Site            order(39..40,43,75,125..126,128..130,133,153,156..157,160,
                     287,290..291,294..296,299,327,331,383..384,388,392,408,
                     411..412,415..416,419)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341046"
ORIGIN      
        1 madtaaippa pphegrasvt dwiavaagal galmatldis itnsalpqiq geigatgteg
       61 twistgylms eivmiplaaw ltrvfglrnf lltnaalfia fsmmcgwshs lammiagrig
      121 qgftggalip taqtiirtrl plsqlpvgmt lfglivllgp lfgpvlggwl aenvswswcf
      181 flnlpvclll mallvfglps dkpqwntffn adwlgiagla iglssltvvl eegqrerwfe
      241 sqtivtlsyv slagmilial sqrfakrpim rlslmrnpry asvivivsav gaglygvsyl
      301 lpqflaivag ynaeqagsim llsglpaflv mpilprllgk vdfrilvisg lllfclscml
      361 disltaqsvg hdfvwsqlir gvaqmlammp lnqasmaava redsgdaagl ynmarnlggs
      421 iglaiigtvi drrttfhaaa lresvtansl igqerlsnya anwfahtgdl aysnmralgq
      481 laqqiqvqai vmtysetfyl lglallacvp lalllktprg pqpmssgh
//
LOCUS       WP_175795855             476 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175795855
VERSION     WP_175795855.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..476
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48344
     Region          23..450
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,277,280..281,284..286,289,317,321,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msefassaga repavnwram savllavala tldtaianta lpaiaadlha spaasvwiin
       61 ayqlamvatl lpfaslgdiv ghkrvyiagl avftlaslgc svastlpqlt aarivqgfga
      121 saimsvnval irnlfpahrl grgvgfnalv vgvsfavgpt iaslilsvaa wpwlfavnvp
      181 lgvvalavai pslprtargk hafdplaalf nvitfaslif algefaqrgp lsvvfaaaav
      241 alafgwllir rqaghpapml pvdlfrrpvf tlsaltavca faaqglafvs lpfyfetvlh
      301 rsavetgflm tpwsaivala apiagrlsdr yppgllgaig lallsagmvs laalpaapgv
      361 vdigwrmmlc gagfgffqsp nlkalmssap persggasgi iatarligqa tgaalvalsf
      421 giagrhgptl almlgagfag aasvasglrl fapshragap vasapvkeha terdsa
//
LOCUS       WP_175795883             110 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF190 domain-containing protein [Burkholderia anthina].
ACCESSION   WP_175795883
VERSION     WP_175795883.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..110
                     /product="DUF190 domain-containing protein"
                     /calculated_mol_wt=12151
     Region          5..100
                     /region_name="COG1993"
                     /note="PII-like signaling protein [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:441596"
ORIGIN      
        1 mkgsqltvya anlshrkdhm tvvdwileet kradihgatv ievtqgvdsr ghyhaarffe
       61 lvdqpvavtv aaeddkidal larlreskvr lfytrcpiey eaiggegdap
//
LOCUS       WP_175795871             288 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia anthina].
ACCESSION   WP_175795871
VERSION     WP_175795871.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..288
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31152
     Region          6..>261
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtqknvltvs glsiavgdee gdrslvrdvn fslaegrtig ivgesgsgkt ltslalmgll
       61 shplkvtsgs iklageelvt aseqrmrelr gnriamvfqe pmtslnpvlt igyqlsealm
      121 vhsgcsrkta lekavkller vkipnaqvrv ksyphelsgg mrqrvmiama mmcdpkviva
      181 depttaldvt vqaevlmllk dlqrefqtav vfishdlgvi gdvcddvmvm yrgdvvetgt
      241 vtdvlknpkh aytaallaar pafhrgdqah llnqkkrlad lnslmeas
//
LOCUS       WP_175795885             122 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF190 domain-containing protein [Burkholderia anthina].
ACCESSION   WP_175795885
VERSION     WP_175795885.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..122
                     /product="DUF190 domain-containing protein"
                     /calculated_mol_wt=13484
     Region          4..103
                     /region_name="COG1993"
                     /note="PII-like signaling protein [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:441596"
ORIGIN      
        1 mngyqltfyt eqnrrhghqt vcnwllhvvh elgirgatvi sasegighag ahhaahmlnl
       61 adqpvqiila ltegeaekil nvvraegvhv fytrfpiefg vlgedlpakq skhfslfrrs
      121 ah
//
LOCUS       WP_175795891             352 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Burkholderia anthina].
ACCESSION   WP_175795891
VERSION     WP_175795891.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..352
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=38060
     Region          34..329
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mnqqglnagn rtsgdgcgks vrapsraewq sdpekafkgw vvevatskdd lpysersqrq
       61 yaamfhrfat flktcgssvl sagpdvieay laslegrnpy epgcagsapp asstpatrst
      121 lkrhsdlidd vmnhlvvegy rtenpvfagt rrlpghdtgp qlvclpdqvd arlqdyllnv
      181 mdtsswagrr nralllllsg sgitsgqasn arlsqfifdd avpsfecvpq nnvdhyrapl
      241 aqssvaaire wveerqlggg psgadpevaf pgkgggalst trvylevrkv lqaiefhgnd
      301 mgprvlrnty arrqllngas vdvvarllgi enprnilrll ritpaqtgyv pv
//
LOCUS       WP_175795902             632 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent helicase [Burkholderia anthina].
ACCESSION   WP_175795902
VERSION     WP_175795902.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..632
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69921
     Region          8..613
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mndtiarila plndeqmava ncnghclvia gpgsgktnti srkiaaalqd pneriaavtf
       61 treaalelra rtislagraa aprllvgtfh svmnlmsfpn lavdgrdvvf grdiiagrpw
      121 pfgktkwkiv keglrrsfih ralseleied lkledasrii ehvksgrpat elrheqltqi
      181 ytdimarqkv idfqdillkt nagldsgavp pldvtrlfid eyqdtdkpqf dmaaahfran
      241 viltgvgddd qsiygfrnal gyegmllfer sfdaerlmlg nnyrshaeiv gaatkvinhn
      301 ldrvdktlva ikgaggktaw ktfktreeea haaavyagqa ltastsrqpc aifarnnrrl
      361 devearlqtl gipyrrppge silnsvevmi fsaavqavvk pekkvidqll swckvdeqsi
      421 vkleklfrga fvigqaedfd rakvedsvke kwrafvrtft gwqsslaaga dtllvygice
      481 wltsyapdkr senvlqiard mfmprradpe qgilaqtvqd rlkaikmaqs kpeakkeege
      541 dapkvvelmt ahgskglefd fvwivgaede vfpakdgtle eerrlmfvam trarkdlmls
      601 tgggkppsgf lkesgieriv dpvdadpdla ae
//
LOCUS       WP_175796148             385 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia anthina].
ACCESSION   WP_175796148
VERSION     WP_175796148.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..385
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42609
     Region          4..383
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnptdayqdi reavrdlcgq fsaeyfrkid eergypeafv daltqagwla alipqeyggs
       61 glglteasvi meeinraggn sgachgqmyn mgtllrhgsa eqkqrylpki asgelrlqsm
      121 gvtepttgtd ttkikttavr kgdryvingq kvwisrvqhs dlmillartt plsdvkkkse
      181 gmsifivdlh haigngmtvr pipnmvnhet nelffdnlei paenligeeg qgfkyildgl
      241 naertliaae cigdgywfvd kvsqyvkdrv vfgrpigqnq gvqfpiarlf inveaaslmr
      301 feaarrfdah epcgaqanma kllaadaswe aanaclqfhg gfgfaceydv erkfretrly
      361 qvapistnli lsyvaehilg lprsf
//
LOCUS       WP_175796110             441 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175796110
VERSION     WP_175796110.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47452
     Region          33..435
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(46..47,50..51,54,86,136..137,139..141,144,164,
                     167..168,171,267,270..271,274..276,279,307,311,361..362,
                     366,370,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mrakypappv qgemlqrdda stfeaatyak varrlipflm lcylgayldr vnvgfaklqm
       61 lndlrfsetv ygvgagiffl gyflfevpsn lilhrvgarr wlarimltwa visasfvfvk
      121 sptafyvlrf llgvaeagfa pgvilyltyw fpsarrakal slffmaipla givggplsga
      181 imhslhgams magwkwlfll ealpscvlgf aillylddgi drakwltdae kgllarnvsa
      241 daahttahls irafvadrrl wlmaaiyfcv vlgqygltfw lptiirkagv adplwvglft
      301 aipyacaiva lpligmsadr rrerrfhlav pmliaaagfa tlpilgsvga sivclsiasa
      361 gilaassqfw slptallggm saaagiaavn cvanlagffs paivgwlndl tgkstaglif
      421 isvaitvgal lvfrvprsvn r
//
LOCUS       WP_175796023             688 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA cytosine methyltransferase [Burkholderia anthina].
ACCESSION   WP_175796023
VERSION     WP_175796023.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..688
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=74721
     Region          8..>232
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
     Region          <603..675
                     /region_name="AdoMet_MTases"
                     /note="S-adenosylmethionine-dependent methyltransferases
                     (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes
                     that use S-adenosyl-L-methionine (SAM or AdoMet) as a
                     substrate for methyltransfer, creating the product
                     S-adenosyl-L-homocysteine (AdoHcy); cl17173"
                     /db_xref="CDD:473071"
ORIGIN      
        1 mkhdlltral dlgselivdn faggggtstg leaafgrpvd iainhdpeal amhalnhpyt
       61 khlcesvwdv dpikvtgnrp vglvwlspdc khfskakggt pvakhirgla wvglrwvalt
      121 kprvlmlenv eefqqwgpli impdgtsrpd pkrkgktfes fvrqlrqhgy tvdwrelrac
      181 dngaptirkr lflvarrdgl pivfpepthg eptsrevlag mlapyrtaae cidfsvqsns
      241 ifgrkkplvt nterrvakgm wkhvlanasp fivpteqgnd gdlssmatpf vtehanasnq
      301 rtmradeplr ticaevkggh fsvvaptlvq lrgtseahlg arsveqpvst vtasgthhal
      361 asahlitvgy geregqeprt qsieqplgta vaggvkqaiv aahitkfrtg ssgaamnepm
      421 ptvtansfqk rpggaaplgm vaahlmhvth hgdrpgttpa mplptitgan rgeqalsaaf
      481 feqanggfwe dndgrsadap lstiaskgan qrlvtaylvk yyssggqwqd lgepmhtlpt
      541 kgrmglvqat qvsadclspe hrenarlcae llrahlpdef pepaemimmf hsgswwvlvd
      601 itlrmlrape lfraqsfpkd yiiheipdpk llfkdgvqvp gdprllprvp ltataqirmc
      661 gnsvspvqae aliranfahe kqlayaaa
//
LOCUS       WP_175796206             304 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175796206
VERSION     WP_175796206.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33019
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..295
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,224..229,
                     235..236,238..239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mtfdlrqlra fttivacgsl graadalhvt qpalsrilkr ledqvgaplf erhskgvqlt
       61 afgdallpha tllqheaeha reeldamrgf akgtikvgav gsiaslvlpv avgrvldrwp
      121 nlrveilegv wdrlaeglhk heidlalsah gpdtdeivai pecrwedrsh ivaaphhplr
      181 algraptlad tlharwaipp rgtapfdhmr atfdahglal pdiavetrsv ttlkslvaha
      241 gflswmaepm ygaeqragti dtlpvsevva vrmltafrrr hgilpgpagk lldelvaltr
      301 dear
//
LOCUS       WP_175796189             455 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175796189
VERSION     WP_175796189.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..455
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47132
     Region          19..447
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(26..27,30..31,34,66,116..117,119..121,124,144,
                     147..148,151,273,276..277,280..282,285,313,317,369..370,
                     374,378,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mnadiglplp qrywaivcva lgitlavldg aianvalpti ardlhasdaa siwivnayql
       61 avtitllpla slgerigyrr iyiaglalft aaslgcalag slpmlavmrv iqgfgaagim
      121 svnaalvrmi ypsamlgrgl sinamvvals saigptvasa ilsfaswpwl favnvpigia
      181 avfgslralp tnprhnapyd fpsalmnacv fgllimavdg fghgesrayv vielavafgi
      241 gyffvkrqls qpapllpvdl mripmfalsi ctsvasftsq mlafvalpfw lqnslgfsqv
      301 etglymtpwp lvivfaapla gvlsdrysag llggiglalf algllslati gphpgtvdiv
      361 wrmalcgagf glfqspnnra mlssaprers ggaggmlsta rltgqtlgaa lvalifglap
      421 drgptialyl atafaaiaav vsmlriaspk pdaat
//
LOCUS       WP_175796248             310 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175796248
VERSION     WP_175796248.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34293
     Region          6..>51
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mlkenlsdlq afvviarers ftraaaqlgl srsalshaml glearlgirl ltrttrsvtt
       61 teagtrllna vapqfdeiel eldsvsamrd kpagmvrita hdhaivtslw prllplmrdy
      121 pdiqiefsvd ygftdiaanr fdagvrlgaq vdkdmiavri apdlrmavvg spaylatqpr
      181 pgtphdltkh rcinlrlpth gglytwefek dgqeinvrvd gqtilnntfl mlqaaldgmg
      241 layvpldiaq lhidagqlvp vledwwprfp gyhlyyasrr qlppalalvi dtlrwregrp
      301 ggakvpgsar
//
LOCUS       WP_175796243             292 aa            linear   BCT 11-JAN-2025
DEFINITION  toll/interleukin-1 receptor domain-containing protein [Burkholderia
            anthina].
ACCESSION   WP_175796243
VERSION     WP_175796243.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Nimma,S., Gu,W., Maruta,N., Li,Y., Pan,M., Saikot,F.K., Lim,B.Y.J.,
            McGuinness,H.Y., Zaoti,Z.F., Li,S., Desa,S., Manik,M.K.,
            Nanson,J.D. and Kobe,B.
  TITLE     Structural Evolution of TIR-Domain Signalosomes
  JOURNAL   Front Immunol 12, 784484 (2021)
   PUBMED   34868065
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Essuman,K., Summers,D.W., Sasaki,Y., Mao,X., Yim,A.K.Y.,
            DiAntonio,A. and Milbrandt,J.
  TITLE     TIR Domain Proteins Are an Ancient Family of NAD+-Consuming Enzymes
  JOURNAL   Curr Biol 28 (3), 421-430 (2018)
   PUBMED   29395922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10615567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..292
                     /product="toll/interleukin-1 receptor domain-containing
                     protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=33083
     Region          157..>224
                     /region_name="TIR_2"
                     /note="TIR domain; pfam13676"
                     /db_xref="CDD:463954"
ORIGIN      
        1 meagnrkpyy nllmsgsada wagpswamey drvfehthge vkkqfetldd aalqalmelp
       61 tlfayekyig aparvgrlte imrqqrefsf tftfdsaiap iphdafmgll haldidpkwe
      121 inrthwavkn vdlgrvlhas glaatslvas lrrppkvfis yswdspehrv wvaqlatslr
      181 rdgieaildq wyvklgedla afmainvrec drvlvictee yvrkarerkg grrlranagh
      241 wpndarcwnh evhpcrptve qsvyaarrvg gtalrgslrw pwparcvsal gp
//
LOCUS       WP_175796250             337 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia anthina].
ACCESSION   WP_175796250
VERSION     WP_175796250.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..337
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36713
     Region          29..336
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mnaqnetgdv gaqpsvqski qldekwdktf aksdkldhkk vsfknrygit laadlyqpkn
       61 atgkiaaiav ggpfgavkeq ssglyaqtia ehgfvtlafd psytgesgge prnvaspdin
      121 tedfsaavdy lglypavdre rigivgicgw ggmalnaaav dkrikavvas tmydmtrvms
      181 kgyndsvnle qrtqaleqlg qqrwqdaerg tpaygpvsle lkggepqfvv eyadyyktsr
      241 gfhprainsn gswtvttpls fmnmpilnyi aeisprplll vhgenahsry fsetayaaaa
      301 epkelviipg anhtdlydrp daipfdkias ffqtnlk
//
LOCUS       WP_175796265             269 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175796265
VERSION     WP_175796265.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..269
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28337
     Region          1..240
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mtqlvpgqvv vvtggatgig falaeafash glrialadid seglqsater lanrgvtvig
       61 vhtdvadrds vrslrrqvls qfgtvdiicn nagiyqvlds iwnidpvqwr rlfdinywgv
      121 vhgiqefvpl flargsghvv ntasmsglst vpgsadygss khavialset lradldlaga
      181 taigvtvlcp sivgttmger altfltqsag drsaigsgpn lvnvitseav ataavqgier
      241 nllhvtptpg srdrflkriq pilenwqit
//
LOCUS       WP_175796274             333 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            anthina].
ACCESSION   WP_175796274
VERSION     WP_175796274.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..333
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=34768
     Region          32..314
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 msinmrrrgf tldlcgvlll lpllllpfvt tdplmnsltn qsavgvtaam giyimlrlgl
       61 lsfsvpsfma lggyaaaiva nsgttnllll mavsaivpai vavplgavvl rlkgvyfifi
      121 tfvfneilql vifetptltg gangiagvpp atlfmlnmns ttasvvvtvv vcivatlgtl
      181 avthilrpef asieenetla eslgiapwkf rttgfiasaa vsglagfelv nmlstahpss
      241 ftswsvnnyi ayvfiggrgn llgvvvgsll ligmttvfss yanlasgmfg vllvivmmia
      301 pggivgtmlk lfgrfggrra dvsrphvqdg gra
//
LOCUS       WP_175796269             302 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175796269
VERSION     WP_175796269.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..302
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=31894
     Region          9..290
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mnsqsrentv gfvglgmmgg pmaenilkkg hklvvydidk qkvdrlvalg aqpadgpadv
       61 srqarivism vdttaqaeev iigsggfiaa gqagdvvism stidpmalrk mqgvlagkgv
      121 diidspvtgm ekgakegtlk ayvggeteal ekarpvleam tsqilhlgdv gngiamklvn
      181 nmlfqvnrvl iaealalgak vgldpqqmve visnttgnsv afqysapril arefegirmd
      241 itykdielqt slakalkmpm fmantaqqvy qmaraagmgn edgvavvkiy eqftgvpvsp
      301 ha
//
LOCUS       WP_175796284             408 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia anthina].
ACCESSION   WP_175796284
VERSION     WP_175796284.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..408
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44570
     Region          1..381
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdqsmseeie avrdlvnrfm qnevvpvmdg fekrgefpre lvrkageagl ygavfpesvg
       61 gsnmgylaaa viqeemcrid vrfascnnqq gstcpsciyf ggtpeqikky vpnlvagkti
      121 gmmsltesgg gsdaagnmqt farrdgdvyr itgqkmfasi anetdvgvlf akterdggtk
      181 gvtafivqpk kypgwtaqpi dmmglsnsfr tnvvylddfv vpvedrlgee gegfkiimrt
      241 lqpgrvgvaa kalgvaracy edalryaner tlrgqpigrf qmiqsdlaem avaieasral
      301 vykaaqmmde slpsnriaai akyhasqtak fcadkavqif ggyglakeyr vswyrayadm
      361 fftgegsanv qkiliaedal gykladrhhg ktglrdirkd dvlknsgq
//
LOCUS       WP_175796291             256 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Burkholderia
            anthina].
ACCESSION   WP_175796291
VERSION     WP_175796291.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..256
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=27228
     Region          7..250
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mpiqtcvegs iayitlnrpe alnalsfevl qelsdafdsv aasdaralvi tgqgekafca
       61 gadirelmgr nliaerngal fgqatfakld rlpipsiavi hgyafgggle lamactfria
      121 tkkakvglpe iklglipgyg gtqrlprlvg qaraldivms grtvaaeeae riglvncive
      181 dgdpralgae yanryigfsk cassfareav rraadvdlse glsieadlst layrtqdave
      241 gmqaflekrq pnfkda
//
LOCUS       WP_175796302             298 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175796302
VERSION     WP_175796302.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32927
     Region          6..>51
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 marenlndll aflavarers ftrgaarlgv sqsalshtir sletrlgvrl ltrttrsvst
       61 teagerifqa vaprieeids elaalaefrd kptgtvrita tdhsaetvlw pklssflpay
      121 pdikieitvd ygladivser hdigvrlgdq vakdmiavri gpdlrmmvva speyfakfpp
      181 pktpddllqh ncislrlatl gniyswelkk gehdlqvrve gqlivnnapq llnaalggfg
      241 iaylpedvvm phmragrlrs alnewsptvt gyhayypsrr qsslalslvi dalryspr
//
LOCUS       WP_175796379             361 aa            linear   BCT 11-JAN-2025
DEFINITION  C40 family peptidase [Burkholderia anthina].
ACCESSION   WP_175796379
VERSION     WP_175796379.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..361
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37011
     Region          <6..176
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mlricapvvv vsllaacssv pqqsasrsas gmrittpraf papanfpkfv dhsvgqeeis
       61 iqamslvgvp yrwggntpts gfdcsglvry vigraadvnl prttadmssr gvsidpdqva
      121 pgdliffntt grphshvgiy vgklrfvnap stggtvrldy ltnpywakrf dgirrvappr
      181 saptpfdapt yearhdaprt apvaaaapvp vvtaaaprqp ayaapqasat pspapmmpaa
      241 pvmaaamtap aaaaadpyep ppprmqaaqs qatatnddmn vmtanaapan paeigspipt
      301 taltaaqaaa fdaeppsaav apsprgaepv qvlrastqsa pagartgtad dpiarfangs
      361 y
//
LOCUS       WP_175796389             368 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia anthina].
ACCESSION   WP_175796389
VERSION     WP_175796389.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..368
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39350
     Region          4..336
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(24,26,57,99,228,290,310,312..314)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(24,26,57,99,101,108,176,179,181,228,235,290,310,
                     312..313)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(26,101,176,179,181,313)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            181
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mtlpllepar igafampnri vmapmtrsra dehdapgdlh iayyaqraga glivaegtyp
       61 hadgkgycrt pgiatqrqid awrrvsdavh rengrivlql mhvgrvasrl nkapgadtva
      121 psalrangti hadghgqvsl dmpraltrae ipdvidcfrq aavnartagf dgvelhassg
      181 ylpmqfllac snhrtddygg tperrarfti ealeamagai gaqrvglric pgnpyndmhd
      241 ddpastygal ldavsplela ylhvsrspdr qldafalahr hfhgpliand gfdahsatsv
      301 laaghadavs farhfianpd lvvrlrdgap laafdratly tpgergftdy pplrvadagg
      361 psiqrsap
//
LOCUS       WP_175796461             379 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia anthina].
ACCESSION   WP_175796461
VERSION     WP_175796461.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..379
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=41084
     Region          9..312
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mtanhsappk lpgqvvlvlq gggalgayql gvyealdaag iqpdwiigts igainaalia
       61 gnapghraqr maefwrrvte rpalnvpgfp tswdkigael gvigagipgf frpnpaawlg
      121 plahvgveha syyvvdplra tlvslvdfdr lnagrprvtv gavdactsam hyfdsrdrpl
      181 giehvmssga lppafpavri dgapywdggi ysntpvevvl ddaprrssii fsvqmwnpvg
      241 pepksiwqvs erqkdiqyas rtdshiarqq qihrlrhviq elvtrlpeae rasadvqala
      301 awgcqttmrv iklaaprldg ddqwkdidft pagiaarrqa gfeatmqtia arpweipmdp
      361 teglsvwspe enrigeqhs
//
LOCUS       WP_175796470            1057 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia anthina].
ACCESSION   WP_175796470
VERSION     WP_175796470.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..1057
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113196
     Region          1..1038
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mdfsrffidr pifavvlsiv ifaiglisip mlpageypev vppsvvvrat ypganpkeia
       61 esvaepleea ingvegimym ksvagsdgsl qvvvtflpgv dpdtaavrvq nrvsqalsrl
      121 pdevrqygvt tqkqsptplm yvslyspdns rdslylrnyl tlhvkdelsr ltgigdvgvy
      181 gsgdyamrlw ldpnrlasrg ltasdviaav reqnvqvsag qlgaepspkk sdflvsinvr
      241 grlrtvqefg divlrngddg qvvklsdvar ielgagdytl rsyfddkhsa vvgiflspga
      301 naldvakavy akldalskrf ppgvayrpvw dptvfvresi ravqhtliea vvlvvlvvil
      361 flqtwrasii plvavpvsvv gtfawlyllg ysintltlfg lvlaigivvd daivvvenve
      421 rniaqglspr daahqamrev sgpivaialv lcavfvpmaf msgvtgqfyk qfavtiaist
      481 visainsltl spalaakllr phgapkdalt rgldrafgwl fhpfnrffer sseryhgvva
      541 rtlkrrgavf vvyaallaat allfnavpgg fipvqdklyl fagaklpega slartsavte
      601 qmtkialgtd gvemvpafag lnalqgvntp nitnsyvilk pfdqrhrsaa qinadlnarf
      661 aaigggitya lmpppiqglg ngsgyslyle drgglgygel qnaltafqaa vaktpgmsyp
      721 vssyqanipq levkvdrlka kaqgvaltdl fntlqvylgs myvndfnafg rvyrvmaqad
      781 aghrqtaadi anlrtrnakg emvpigsmvt vapaygpdpv vryngypaad ligdadpkam
      841 sssqtiaklq qiakdvlppg itlewtdlsy qqvtqsnaai vvfplavmlv flvlaslyes
      901 wtlplavili vpvcmcaalf gvwlsggdnn vfvqvglvvl mglacknail ivefarelei
      961 qgkgaieaal eacrlrlrpi vmtsvafiag svplligsga gsevraatgv tvfagmlgvt
     1021 lfglfltpvf yvairklagg tpavwreqhg tlegenr
//
LOCUS       WP_175796485             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175796485
VERSION     WP_175796485.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33940
     Region          7..>158
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          95..293
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(105,109,148,162,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(106..107,111..112,114..115,118,122,124..130,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mqtlpdleaw aifarvaetg sfakaaellg isqptvskai arlekrlgam llyrtsrkls
       61 ltptgellrd rairlladae lieseataqa lephglvrvn apmsfglrhl spllpafler
      121 yprvdidlvl tdhivdivsg gfdvairiae lsdsslrsrr lcavrrplva spaylnrhgr
      181 pthprdieqh vcltytnlpt pehwrfrlpa sgedfgvnvh grirtnnadv ivpalvaghg
      241 lalqpeflvw damqrgelee vmrdwkiadi nvnlvtppgm lraarvtvll dflaehfaha
      301 pwalpat
//
LOCUS       WP_175796534             192 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Burkholderia anthina].
ACCESSION   WP_175796534
VERSION     WP_175796534.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..192
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=21255
     Region          <1..173
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mrisevasgq mghffrrlge dghdqwwlei lgkgekdriv pvsadlvsel rryrvanglc
       61 plpsrsdesp llipfrganr clhrsavhda ikgvfrgaaa wlrsrgpefg dradeldras
      121 ahwlrhtags hmvdggvdlr tvrdnlghas ltttslylha gddvrhretv arhtmkwdeq
      181 gtavapndpt vp
//
LOCUS       WP_175796551             194 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Burkholderia anthina].
ACCESSION   WP_175796551
VERSION     WP_175796551.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 194)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 194)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..194
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=20974
     Region          3..133
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,70..71,74)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(69,114..115,117..118,122)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(75,80..81,110,113..114,117..118,121,124)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(98..99,101,110..111,114..115,118,122,125,129)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(98,115,118,122,125,129)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(123,129..130)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          145..182
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
ORIGIN      
        1 maifgygrvs tgqqitenqr lelegagfai dywfadhgvs gktcaserpe fgrllekird
       61 getlvvakld rlgrdavdvl qtiralekrs ikvivmqlgq tdltspagkl lltmlasvae
      121 merdlliert qaglarakle gkklgrpskt tpeqrrqihv glqqgasvsa larayavsra
      181 tiisirgsal saet
//
LOCUS       WP_175796569             468 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Burkholderia anthina].
ACCESSION   WP_175796569
VERSION     WP_175796569.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..468
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50038
     Region          7..465
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 msslprdlhn leihdlslqi rsgklspvev ttamlarvda ldanlhsfar vtpelalkqa
       61 gqaeqeirag nvrsplhgip lavkdlfdtk givtaggmpi hsqrvptena tvvqrlqdag
      121 svmlgklqmt egafaihhpt ipdpvnpwga ahwcgasssg cgvataarlc ygtvgsdtgg
      181 svrfpsaann ltglktthgt isskgamela asldhigpma rsardvllll aiigghdtqr
      241 lldtideqrf gnflkgfrgl rigmdeawis agvdsviqra iqqvkvilaq vggeiksikv
      301 pdtratssnw ehhcgvqtav ahwatypgka aeygpalarl idqgrqikav dyeriireat
      361 qfardmdavf tevdvvlapv qpyaaptyek ladlasdpet nrrliqftap fnasghpals
      421 ipvgfteqgl pvggqligrk yqddllcmvg mvlqshsdwh rqvppgla
//
LOCUS       WP_175796573             199 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Burkholderia anthina].
ACCESSION   WP_175796573
VERSION     WP_175796573.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 199)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..199
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=21557
     Region          4..139
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(9,11,76..77,80)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            11
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(75,120..121,123..124,128)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(81,86..87,116,119..120,123..124,127,130)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(105..107,116..117,120..121,124,128,131,135)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(105,121,124,128,131,135)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(129,135..136)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          151..192
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
     Site            order(152..154,186..187,189..191)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 msrtfiyarv stadqttenq lreiqaagfa idddkrkqri veetisgsva amerpgfakl
       61 vdrlesgdvl ivtkldrlgr namdvratve hlaaigvrvh clalggvdlt saagrmtmtv
      121 lsavaeferd lliertqagl srakaegkkl grkpalsgsq qaevlqklte gmtisqiard
      181 fkttrqtimr vrngagseq
//
LOCUS       WP_175796596            1181 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia anthina].
ACCESSION   WP_175796596
VERSION     WP_175796596.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1181)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 1181)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1181
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..1181
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=130466
     Region          35..735
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 maefdrvtsy ltgrqsaylk lmrrkskrdp etgepppmpt vsvvswvvre aicepysvka
       61 vvaapiaipr ktvlgqlakf svqpedgrak refagfvtqf dsvsesrdgy tyrivmrqhl
      121 avmdgpsnca tyqgmaswei ikeilarydl rfwiqvefnl rrehprhpfr fqynmgdwdy
      181 iklemeqagl ycytktgehg dvlviaddvd gymrpavpvl drptaglatf eesifsfkvr
      241 srvvpesylv adynpeqawe rfraedravs ddetmigkpy vwgthhddae gakreaqlrh
      301 eaacasqiry svestvlair pgsivqsdra ledagaamfv ttvvhrgarn asyvnsftai
      361 padrpyrrei derrwpkipg tlggtitspd kykfayltdk geyvarfhcd fgnwpkgges
      421 vplrlakpfa grnhtgmhmp aldgdealig fregnpnkpf iaafihnser pdlinssrrr
      481 msrneirtqs gnkfwmddwd nqegielgte hsgrsqlhlg hmvdralnqr gagaelrtsg
      541 havarggagv mvtaydrpgg agkqldmaet iaqlkemlal aeslaksvea skaspadtqa
      601 qkaisdglde lkrpgavvta pgpvgvvsgd gvqlaadgsi igtakkgihf salkritaaa
      661 ggllslfark gmsliasage vvvqaqrgrm qlaaqedmtv etvngvlhvk spkeillnvg
      721 gsyirlnpeg iemgsrgrvh frtsglkktg paqldlsgaa fapafvpfkt ecevwrtnpn
      781 fvqppasape pngsqwesqg ntgavarala paadggklsd fspfdgkpsn vdsnvpkakv
      841 elngpddqtq ryvapdpikl anavpcdwki tdlkvdvrqh ieakpywgml dnrtpwkdsn
      901 gnqirgggsr dsnfefayne qdktitctvr vmlipmdlfp vdvtgnrdlt vspqtvpyea
      961 tthwrmmpgs tvdgvkmgyr gtvgdkydid alrnrieavl nqrtyklild gcskgaacgc
     1021 rvkvdfrvdl risvrgapia gfkphvtnhl ypavlradas swgegqkwqd dqgevhdser
     1081 anveahecgh yfnfpdeyfd rggwlhesyi kgeqidfslv dakagtmvwq arsptnlmgy
     1141 gansswqigk vtatikpyyl eyvrrqfsla tnklwrvgyd s
//
LOCUS       WP_175796676             220 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Burkholderia].
ACCESSION   WP_175796676
VERSION     WP_175796676.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..220
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23773
     Region          7..192
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mqqdrhltly hsprsrsaga rmlleelgad yavhafdlst gkhrepdyla vnplgkvpal
       61 rhgdvivteq aavylyaael ypeaglspap gdalrgpylr wmtfygscfe palvdrsmnr
      121 ppaaystspy gdfdavvnai atqlangpyl lgerftaadv lwasalnwtt mlklvpetpl
      181 irayidrvla rpaiqraqaa daalaaeqdk areaaatags
//
LOCUS       WP_175796709             221 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein,
            partial [Burkholderia anthina].
ACCESSION   WP_175796709
VERSION     WP_175796709.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         <1..221
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
     Region          1..220
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 anvkmsmnpf deiaveeavr lkeagvatev iavsvgvaqa qetlrtalai gadrailves
       61 tdsveplava kilkalvdke qpqlvilgkq aidddsnqtg qmlaalaglp qatfaskvti
      121 adgkatvare vdggaetlsl qlpavvttdl rlnepryvtl pnimkakkkp letvkpeelg
      181 vdvaprlktl kvveppkraa gvkvpdvktl veklkteakv l
//
LOCUS       WP_175796736             166 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase, partial [Burkholderia anthina].
ACCESSION   WP_175796736
VERSION     WP_175796736.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         <1..166
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          <1..95
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 vdlaaprgtr vnaaadgvva fvgvdphgyg ryvvidhpdh ystlyahlsa yapglkvgmt
       61 ltegqrvgav gmtgaatgph lhfevriadt pvdpivalad asntlspmql dafrrdlvdv
      121 rtqfaaaagp nvgiamldaa pagaglstld ptlrtllqtp qvssas
//
LOCUS       WP_175796810             288 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein, partial [Burkholderia
            cenocepacia].
ACCESSION   WP_175796810
VERSION     WP_175796810.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..>288
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
     Region          23..276
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mhnpnavnap vqtsqpprlg eeilrvdhvc rgfnktqgel lvlddanlsl regeivgllg
       61 rsgsgkstll riiagliept ggevtylgkp lrgpaegvam vfqtfalfpw ltvlqnveag
      121 lealgvgare rreralaaid ligldgfena yprelsggmr qrvgfaralv vdptillmde
      181 pfsaldvlta etlrtdlldl wtqgrmpiks vlivthniee avfmcdrilv lssnpgrvia
      241 eikvpfkhpr nrldpafrkl vddiyakmta rqtgeatkkg lelgswlp
//
LOCUS       WP_175796816             168 aa            linear   BCT 11-JAN-2025
DEFINITION  cation diffusion facilitator family transporter, partial
            [Burkholderia cenocepacia].
ACCESSION   WP_175796816
VERSION     WP_175796816.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         <1..168
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          <1..156
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mlavatrvks smlvanawha rsdaasslvv acgivgnlfg yplldpvaal ivggmivkmg
       61 atfgwdalhd lmdraadaee vqairatlva trgvldvhdl rtrktgdlil vdvhldidad
      121 ltvaqghdia vdararvmkh hrvlnvmthv dprsreslpa vasgmrvr
//
LOCUS       WP_175796821             400 aa            linear   BCT 11-JAN-2025
DEFINITION  benzoate/H(+) symporter BenE family transporter [Burkholderia
            cenocepacia].
ACCESSION   WP_175796821
VERSION     WP_175796821.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..400
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41373
     Region          11..399
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mqpntppgai rtlgndwsvs aitagflavl isyagplaif fqasqaahas neivtswvwa
       61 isigagvsgl faswklkvpv vtawsapgta llvglfpqlt lnqavgayit aaliilaigv
      121 sgyfdrlvrh iprgiacgmm agillpfgmh afsaasaqpa lafgmiaayv ifrrllprys
      181 ivlvlltgaa latllgmahl gnvspslarp ifiapewtlg ttlslalplv vvsltgqflp
      241 gmailrvsgy htparpiita tsvmsllvac fggitivvaa itaalctgkd ahedqdrryv
      301 aglvngviyl igglfagtiv tlffalpkaf vailaglali gaisanvhgi fenenhreas
      361 vitflatasg mtwlglgsaf wgivigsvay gvlngvrrpa
//
LOCUS       WP_175796848             304 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175796848
VERSION     WP_175796848.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33403
     Region          10..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..295
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(105,109,148,162,165,229,246,274)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(106..107,111..112,114..115,118,122,124..130,192,
                     223..227,234..235,238)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 msrrdpmagl hvfmtvatag nftraaaalg ltpaavslsi gqlegelnvk lfnrstrgvs
       61 lteagqrywr qtepayrqvm qardalkdar sepsgllrvt alplarllvi apvlapfrer
      121 ypkvrleiry enelvdiake gfdagirlad rlqpgmigvr iapaltcalv aspgylarhg
      181 apasiaqler hacirfrfte sgrshkwllh dgrrdvdldp dgvfvtndad avidaaragv
      241 giafafmrer ieqdlrdgtl vevlpgtcrt lppmwlyyvn rkhvpaklra fidvlrerag
      301 adaa
//
LOCUS       WP_175796886             245 aa            linear   BCT 11-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175796886
VERSION     WP_175796886.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..245
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=26176
     Region          5..221
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mqsygiahvw aqgdfvtrai aitllvmsvl swivivikgw nvirlnrltk naeqafwhsd
       61 nfddgikkll glaastpndn pflalalsgk eaadhhhqtq phlhdrmdvs dwvtrclkdt
      121 mdegisrmqs glailasvgs tapfvglfgt vwgiyhalla igatgqtsid qvagpvgesl
      181 imtafglfva ipavlgynal trankgvvsk lrrfahglha yfvtgaslas sstrdglrla
      241 sraas
//
LOCUS       WP_175796914             739 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia ambifaria].
ACCESSION   WP_175796914
VERSION     WP_175796914.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..739
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=78302
     Region          70..>204
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          212..732
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msrglieagr agagvsrrsf lkvgmslgaa aggglllgfs mpaagddarr sviggdaden
       61 aragvfapna fvqidrggkv tlvmpkvemg qgvytalpml iaeelevpls nvtldhappn
      121 eklfldpllg gqltggstsv ryaweplrra gatartllva aaakqwnvdp atcraengev
      181 qhppsgrras ygqladaask lpvpkdvalk qpadfkligk pvkrldspek vdgtaqfgld
      241 vrlpgmlyav ivnspvfggt vasvddtaar kipgvrqvvr vdnavavvgd htwaakrgas
      301 alvvkwnega dakvstkdiv adlaqaaang kgavarkegd vgrafanakt rvdavyeqpf
      361 lahatmepvn ctvqvradgc eiwvgtqvpt rardtvqqlt glapekivvh nhllgggfgr
      421 rletdmigqa vkvakqvnap vkvvwtreed iqhdmyrpyy ydrisaglda ngkpvawqhr
      481 ivgssiiarf appafkngvd pdavevaael pydlpnqlvd yvrqeprhip tafwrgvgpt
      541 rgtfvvesfi delaaqtktd pvqyrralld ktprarnvld vatkaagwgt slpkgqgrgv
      601 svmhafgsff sividvavee gevqvkrvvc avdcgmavnp stieaqvqgg iifgitgaly
      661 geitiedgrv vqsnftdyrm mrinetppie vhlvksaeap ggigepgtaa taaalsnaif
      721 aatgkrlrkl pvgsqlkta
//
LOCUS       WP_175796925             766 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Burkholderia ambifaria].
ACCESSION   WP_175796925
VERSION     WP_175796925.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..766
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=84029
     Region          178..765
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 msyvvavram ceftarrgdl dlrftpapta legiaghgav tskrgaryet eialtgtwgt
       61 ltvrgradgy dpvanrieei ktyrgsldam panhralhwa qakvyahlmc darglaeidv
      121 alvyfdivse retvltetls adelaaffae qcacfvgwae retahraard aalralafph
      181 gqfrsgqrel avsvyraard erclmaqapt gigktlgtvf pllkacgege ldhvffltak
      241 tpgralalea attlgagtpa lplrvlelva rdkacehpdr achgescpla qgfydrlpaa
      301 rdaaigagll dratvreaal ahdvcpyyla qelarwsdmv igdynyyydg samlhtlaqq
      361 nqwrvgvlvd eahnlldrar rmysasldpf afaaareaap aalrkafdrl arawgtvnra
      421 qaeryaaype ipgpivsavq nlvaaigehl tdaprandda llrfhfeaiq fgvladafds
      481 asifdatlhg eplprqsgld gvapagrqrr iqstlcvrnv ipaaflapry etaratvlfs
      541 gtlspfhfyr dtlglpadtg wldvdgpfra eqltvrvash vstrwrdrdr slepiadlia
      601 aqyatrpgny lgflssfdyl grvvalmqtr hpdvpvwaqa pgmaeserda flarfdaggr
      661 gvgfavlgga fsegvdlvge rligafiatl glpqvndvne qmrramdarf gngydymyly
      721 pglqkvvqaa grvirterde gvvhliddry rrrevrdllp rwwrig
//
LOCUS       WP_175796939             442 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175796939
VERSION     WP_175796939.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..442
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46436
     Region          28..429
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(39..40,43..44,47,79,129..130,132..134,137,157,
                     160..161,164,262,265..266,269..271,274,302,306,355..356,
                     360,364,380,383..384,387..388,391)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mstqhaqilp satgdasasl nrllfrklmp lliaayvisf ldrtniafak hsmgvdlgis
       61 saayglgagl ffltyalfei psnlimhrvg arfwitrimi twgalsvama fvggptsfyv
      121 mrlllgaaea glfpgvmlyl tywfgreera ratgyfllgv cianivggpl agalieldgt
      181 lgfhgwqwlf vvegipaill afvvwtrlpd rpsrapwlap etgraleral aaeqdagvaa
      241 hgghafgaal rdpqiwlaif vyfchqltiy tvifflpgii gasghfspfa vglltalpwl
      301 aaalgaatvp rfareshhsr rilcgglivm aagmvgaana spvaglacvc iaasmffvvq
      361 sivftfpasr lagsalaggl glvntcgllg gfvgptvvga ieqatgnakn gltlltaalv
      421 vaafaslalr hgherpaars qr
//
LOCUS       WP_175796948             163 aa            linear   BCT 11-JAN-2025
DEFINITION  2,4'-dihydroxyacetophenone dioxygenase family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175796948
VERSION     WP_175796948.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14449000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..163
                     /product="2,4'-dihydroxyacetophenone dioxygenase family
                     protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17625
     Region          24..143
                     /region_name="cupin_DAD"
                     /note="2,4'-Dihydroxyacetophenone dioxygenase (DAD), cupin
                     domain; cd20302"
                     /db_xref="CDD:380436"
     Site            order(40..41,44,50,52,69,71,73,75,88,91..95,97..99,117,
                     123,125,133,136,139)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:380436"
     Site            order(64,66,81,102,118)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380436"
ORIGIN      
        1 mtqpsaplpt dlppisclpg dalpwlpmsa dlpglaikyl hinaaedtlt allkmpaggt
       61 lprhrhdgev fvhtlqgawr yreydwiaqa gstvlepags vhtpetlgap gddvitlnvm
      121 rgdlvllddd gretarencr vallrqrkhs rvaphdataf vtr
//
LOCUS       WP_175796949             319 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175796949
VERSION     WP_175796949.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..319
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34971
     Region          2..313
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhrigflisd gfqimalaaq svfeyanmga gepfyamdny svdggdvrss lglpvatral
       61 rgrldvdtwi vagvndpvas papagvvafl rrpnararri agictgafvl aeagllaqrr
      121 atthwaygrd mqkhfpevrv eedriyivdg piwtsagmta gldlalamve kdlgadaars
      181 vahklvmhqr raggqsqhse mldlapksdr iqnalnyarq hlgraltvee ladaahlspr
      241 qfsrvftlet gqspakaier lrleaarlmi eqsrhsldvi akengfrdrr hlrdafvrgf
      301 gvppqavrrd aradereta
//
LOCUS       WP_175796958             356 aa            linear   BCT 11-JAN-2025
DEFINITION  AI-2E family transporter [Burkholderia ambifaria].
ACCESSION   WP_175796958
VERSION     WP_175796958.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..356
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37881
     Region          35..355
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mrvhvspsqd starprvqqi aravlyaall llalwvirdf ipaiawacvi aialwpllkr
       61 feserwfrnr ptliatvita gvsllvilpv alalgqaisq ehdlrmwlqs iqdngiplpd
      121 viarlpygaa qvtewwqanl ghplhagaam hgasgekfia fgrqfgtkla halfefgfml
      181 vtlfvilrag hklsgallhg arrafgpggg eliermvaav ygtvtglvvv glgegailgv
      241 ayalagvpha allglvtava amlpfcapiv fcgaalwlfv qgatawavvv lvvgfvvvfv
      301 aehfvrpvli gsstrlpfll vlfgilggae tfgliglfvg palmtvltml waewva
//
LOCUS       WP_175797030             497 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia ambifaria].
ACCESSION   WP_175797030
VERSION     WP_175797030.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..497
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52668
     Region          27..480
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mkhvserpad taggadprha drdamfashe agyakqlkpr hvqmiamgga igtglflgag
       61 grlqsagpal avvylvcgvf aflimralge lvmhrptsga fvsyarefmg erasfvagwm
      121 yylnwattgi vditavaiym kywaafsdvp qwvfalgalg ivsvmnmigv kvfgemefwf
      181 sivkvgtlal flgvgavfla sghpvagqmp glhliadhgg ifphgilpav livqgvvfay
      241 asielvgvaa getadarkvl pkainsvmwr ialfyvgsvv lltmllpwta ysahespfvt
      301 ffgklgvpyv gtvmnvvvlt aalsslnsgl ystgrvlrsl amggsaprfv srmnargvpy
      361 ggilvtvavn aigvplnyiv paqafeivln maslgiittw gfivmcqilf rravnrgels
      421 pvsfrmpgap ftswltlgfl vsvlvlmafd ypggtwtvgm iplvvlalvi gwklakrgta
      481 rqqagaapai adpasnm
//
LOCUS       WP_175797034             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175797034
VERSION     WP_175797034.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46775
     Region          28..433
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(39..40,43..44,47,86,144..145,147..149,152,172,
                     175..176,179,261,264..265,268..270,273,301,305,358..359,
                     363,367,383,386..387,390..391,394)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mqtrstldeh asvatpapar ttrhyllagw asmagttiew ydfflygtaa alvfnriffp
       61 sldpvvgtla afgtfavgfi grpmggivfg hfgdrigrks mlmitlllmg vpsmiiglip
      121 sydsigywaa alliamrflq gmavggewgg avlmavehap kgrkglfgsl pqtgvglgli
      181 lssvamaava alpdadmlsw gwrvpflasi alvglgwfir akvpespdfe kiqrqgkaek
      241 spvtaalrrh prevltivga raaentwfym vvtfalayat qqlhlpkaem lhaitagaal
      301 slvtmplcgh lsdrigqrrm faiglvlmca faapffmmlg tqqtstawwa ivlglgvvfp
      361 ilyapeallf aqqfpaeiry sgislsvqla gvigggfapm iatsllkagg gqphyviayl
      421 igfgvfalac talmrpara
//
LOCUS       WP_175797041             470 aa            linear   BCT 11-JAN-2025
DEFINITION  CpaF family protein [Burkholderia ambifaria].
ACCESSION   WP_175797041
VERSION     WP_175797041.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..470
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50965
     Region          <1..>74
                     /region_name="PRK14959"
                     /note="DNA polymerase III subunits gamma and tau;
                     Provisional"
                     /db_xref="CDD:184923"
     Region          79..459
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mtfgtrkrst pepapavspa vprddapapa piashapppl rgaaaadtqe alirsgkfda
       61 irtavfssmn msaalmktrd evragieqva ahtvererlk itageqvliv dailndmfgv
      121 gpieplladd tvsdilvngp dqvyveragr leltplkfrd nahvtsvaqr iaaavgrrvd
      181 esspmvdarl adgsrvnvvl ppiamrgasi sirkfakrdi tlarmahqgn ishgmlqvlk
      241 iacacrlniv isggtgsgkt tllnalsqhi eeherivtie daaelqllqp hvvsletrpe
      301 nteglggisq rdlvrnalrm rpdriilgei rgaeafdvlq amntghdgsm ttihantprd
      361 aisrlesmvm mananlqlls irrqiasavh lfvqvermrd gvrrvtrite ivgmegevvi
      421 tqdlfafrqe sdttrdvvkg vfeasslrpa fapraayygv edtlsevfrq
//
LOCUS       WP_175797095             490 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54 dependent transcriptional regulator [Burkholderia
            ambifaria].
ACCESSION   WP_175797095
VERSION     WP_175797095.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..490
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=52741
     Region          21..139
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <157..465
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mvarspdang taapemplvs vtapeagrkl fvimrspdep llaqlrglgw disvaktaga
       61 aqnmtsgvnv aaglvdfsgf tsrdypalka clsqaaigwi svaqagvtis pavremirsy
      121 cfdyvtlplp hewishvlgh argmaaldrv dgaayaasig ehgmigncea mqqlfstirk
      181 vaktdasvfi sgesgtgkel talaihersa rgkgpfvain cgaiphhllq selfgyerga
      241 ftganqrrag riesanggtl fldeigdmpv esqasllrfl qegkierlgg qesisvdvri
      301 isathvdldg aveaarfrad lyhrlcvlri hepplrargk didilahyvl qkykadsgrk
      361 isgftsaald amrryewpgn vrelinrvrr aivmaesrll tpndlgletp getepvtleq
      421 arslaertai enallrndhr inkaaaelgi srvtlyrmmi ehglndhdns gdnggkdgsp
      481 pgdadhqrvg
//
LOCUS       WP_175797104             138 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia ambifaria].
ACCESSION   WP_175797104
VERSION     WP_175797104.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..138
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14794
     Region          1..126
                     /region_name="COG3607"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]"
                     /db_xref="CDD:442825"
ORIGIN      
        1 mhktifinlp vadlpraraf yvalgfevvp aytteqgaci risdaifvml lvrpffqtft
       61 gktivepath vqvlpclscd sraevdavva karaaggavp repqaypgmy thdfadpdgh
      121 ewglvyaeqd aasqgpas
//
LOCUS       WP_175797134             206 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            ambifaria].
ACCESSION   WP_175797134
VERSION     WP_175797134.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22707
     Region          12..169
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpmttddqgr rarkrsqmla hlaatgarlf dahgydavtm eqiaaqadva krtlynhfpt
       61 keavlahwle gelardlahl krdvarrksf asriacvlda saawceqhpv yllaylrhrf
      121 lsigavqaeg atenvgdial vwqqliaagq qagelnpala adqlatwfhh lylaamlrwl
      181 tvpglslkre fqsvaklfve gaqakp
//
LOCUS       WP_175797142             743 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia ambifaria].
ACCESSION   WP_175797142
VERSION     WP_175797142.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..743
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79793
     Region          52..743
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mtvnrttasp arrwrakvgv gvglgitlfa aqaaaaqgda papdadaaas atlpaiavsg
       61 erggafrare asvaglddgp lrdtpasvsv vtraqlddqq akrlsdvvrn dasvvndyap
      121 vgyfegfair gfpvdlasai ridgltvsge qnvplenker veilkglagi dsgvvapggv
      181 infvtkrsan vasvttgvds rgstsaavdl grrfgpdhqf gfrinaaken mhsyidgtng
      241 rrtfgsiaad wdispraslq fnaefqqwvq rsapgyqllg gtvvpsvntt skalgtqpwa
      301 kpvttdalnl narfdyrfdd dwnayiaagr srtmiddnsa faygcyyaps caagatspff
      361 fgangdydvy dfrspgeyrr nddlravttg rfatgplrhe ltlgvsvqrr vvhmanavyd
      421 yvgseniygp dvafapspnt agpsypqlds wqygvfgldr isigehwqvl aggkevllrq
      481 rswdsldgda thtdrsvflp qvalvykpvn vlslyasysk alslgdqapv ratnayaflp
      541 pveshqfelg akydwldrls ltaavfsisk pfqfadpdas gtsytfvqrg tqrhqgielg
      601 aagrlterls ltasvaaira raydsgspay eghqiinvpa lraslyadya vpgvaglnml
      661 ggveysggrn aneegtarvp swfvfnlgar yttkigghrt vlrvsvdnlf nkfywrdage
      721 qqgdaylfpg aprtarvslt ydf
//
LOCUS       WP_175797189             392 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia ambifaria].
ACCESSION   WP_175797189
VERSION     WP_175797189.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 392)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..392
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39850
     Region          168..370
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mtgravasar ritldkvgil igvltiiavv gmpfmvlrpn riaagtglsv faalpsaqga
       61 alaalwivga lwamtasrpa wrlaagctwl atlayavgaa aahvvapddm larvspaagv
      121 wlllfawavl vadalarlaf gpwrrlvala vaiaaisvpl asgwwdglsv mreyaartdd
      181 fwreairhvs laggsvaaal vagvplgiac ariapvrtvv mpvlnivqti psiamyglmm
      241 aplgllaahv plaaalgirg igvapavlal flysllpias svvvgleqvp phvteaaram
      301 gmtrvqrllg vdlvlalpvi lsgvrivlvq nigltavaal iggggfgtfi fqgigqsaad
      361 lvllgaipti alalaaavvf eaattlakgr ta
//
LOCUS       WP_175797192             299 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175797192
VERSION     WP_175797192.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..299
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32925
     Region          8..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mprdnfvdll afiavarers ftraaaglgv sqsalshtir sletrlgvrl ltrttrsvap
       61 teagerllqn laprfdeied elsalaelrd kpagtvrina tdyvirtllw prlspilrdy
      121 relkvefvtd yglsdivaqr fdigvrlgdq vakdmiavri spdlkmaivg apayfaerep
      181 patpqdlvah dcinlrlpth galyawelar gddtlqvrvd gqvtfngtye mldaalagyg
      241 layvpaelav phvaagrlvs vlddwcptfp ghhlyyasrr qssrafaliv dalrhpghs
//
LOCUS       WP_175797225             318 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia ambifaria].
ACCESSION   WP_175797225
VERSION     WP_175797225.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..318
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33482
     Region          80..293
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mlepeiaafv savdaaypag aaacspdeqr rlydrfaaaw tpaelppgiv rhdavwhape
       61 ghaialrrya lahgeprgtv lffhgggfvv gsldshalit aqlaadtgla viavdyrlap
      121 ehrapaalad clavtraard acwsfgscar pltlagdsag gnlaaavata lrdageggid
      181 gialvypmlg iepqsparet qahapmltld dvhryralyw ggdahfapgd ddpllrasvp
      241 laasrfdrlp pvlaigaehd plrddarvyv erihaaggaa rywmgkglvh gcwralgtsp
      301 qaarmhrmvg efllapha
//
LOCUS       WP_175797237             286 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175797237
VERSION     WP_175797237.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13673967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..286
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31398
     Region          24..159
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          <159..279
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mttaannpdt rdhwlvarrd aetgieslha hfnghaydah dhddmlvgft eqgvqrfqch
       61 rslhtsvpgr ailiepgamh dghapeaggf tygmlylpqa wveraarrld lpglgsveaa
      121 fghtlvddrg lvdairhafv aihgnegrla rdqtldrllm rlggelrgvp lalessvvpp
      181 aiarvrdllh ahmdgnlgld elagaagidr frltrlfqra ygtsphaylv rlrlraarrl
      241 laagrtpaqa asdvgfadqs hlgrwfrray ritpaayrql ctnvpd
//
LOCUS       WP_175797241             287 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia ambifaria].
ACCESSION   WP_175797241
VERSION     WP_175797241.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..287
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30519
     Region          15..261
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(28,109,111,113..114,142,193,214,217,230,232,261)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mstpiprlsf prrevgdfsv taisdgtlta gldllsnidv ddatgimhra gvhapsdvni
       61 ncyvirgngr tvlvdtgagg irnwggrlra slahagidar didtilltha hpdhigglld
      121 adgqpafaqa avllherera fwldddayer aserarvnfq iarrtfdayr aqlrtieagd
      181 vqpgivavpl pghtpghtgy rvesrgerll iwgdlvhfap iqvarpdvsi afdqdpsqas
      241 atraatlaev asdnvliagm hladtgfari arangatdgt yaligad
//
LOCUS       WP_175797284             515 aa            linear   BCT 11-JAN-2025
DEFINITION  FGGY-family carbohydrate kinase [Burkholderia ambifaria].
ACCESSION   WP_175797284
VERSION     WP_175797284.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..515
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=55248
     Region          3..448
                     /region_name="ASKHA_NBD_FGGY_RrXK-like"
                     /note="nucleotide-binding domain (NBD) of Rhodospirillum
                     rubrum xylulose kinase (RrXK) and similar proteins;
                     cd07804"
                     /db_xref="CDD:466806"
ORIGIN      
        1 meyvigvdig tqstkallvd rrgtivarrs agyqpdtprp lwaeqwpqvw fdavldciag
       61 cvsdarahgv padairavcv sslyggsgvp vdsdmrplhp cliwmdrrat aevdwvnanv
      121 nverlrvitg ngvdsyygft kmlwlreqrp dvwanvryfl ppnayviyll tgevavdhss
      181 agniggvydv arrewsddal dmlgipatmm perlvqstdi vggllsqwte qlglpagtpv
      241 vaggvdaava tfaagatrgg qhvamigtsm cwgyvnqhvd arhglvsmph vfngqrdlyv
      301 fggaitagas vawfrdqfch aeidaarllp hgdphvllee aaesvppgad gvlflpylmg
      361 erspvwdaqa sgafvglsla htrahlyrav legvafalrh nieagrrgtv alddrlivvg
      421 gaahsalwmq iiadvtgfpv wtieqdveaa mgaallagvg vglvshddah ggwvtlvera
      481 rpdaaranay aarfalytal ypalkptmha lrtss
//
LOCUS       WP_175797290             264 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175797290
VERSION     WP_175797290.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..264
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28001
     Region          12..140
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          179..260
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mhrithyrrt degieaisle sdrafprhah defgvgvivs gahrswsgrg qvdalagdai
       61 mvnpgemhdg mpidtgtgrr wrmlylapal vasvateegl eavelthpav rdarlaaafg
      121 rlharivage tlplardeal vtlvagllar hsnralpaag vapairmare rldaapaapv
      181 slaelaglsg vsrfqllrgf arelgitpha yllqsrtrla rallasgrpi adaaaeagfa
      241 dqshltrafa rqfgitpgrf tqag
//
LOCUS       WP_175797325             286 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia ambifaria].
ACCESSION   WP_175797325
VERSION     WP_175797325.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..286
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30962
     Region          29..269
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 mtglhpdapd staarvalwr alhveldapp hvlvdevglr llapapgwqq rgdmdprftr
       61 pfrasivara rfiedlvveq aaqgvsqyvi lgagldsfvq rrpemasrlt vfevdppapq
      121 awkrrrltel gfgvpdwlrf vpvdfeakqs wrdalvgagf dagkpavvvs tgvsmyltre
      181 anaaalreva slapgstfam tfllplehad pdvrpglema akgaaasgtp fisffmpaei
      241 ralatragfa raehvsgael trryfaertd glrppnnaee llvatv
//
LOCUS       WP_175797345             246 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia ambifaria].
ACCESSION   WP_175797345
VERSION     WP_175797345.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..246
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25295
     Region          10..239
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; pfam01925"
                     /db_xref="CDD:460386"
ORIGIN      
        1 mhihtltiia lvfllagavk gmiglglpti amglltlamp psaaaslllv psfitnvwql
       61 wlgpsfgpll rrlwpllagl tvgtltgglp alaagstwth aalgvvlvay gcwglaaarl
      121 papgrhekwl savvgyltgv vtaatgvfvv pavpylqalr lskddliqal glsftastiv
      181 lglqlrvtga lqtvdlgvsa lalvpalagm aggqyarrvm sekmfkrcff vglialgaym
      241 agsgws
//
LOCUS       WP_175797357             555 aa            linear   BCT 11-JAN-2025
DEFINITION  S8 family peptidase [Burkholderia ambifaria].
ACCESSION   WP_175797357
VERSION     WP_175797357.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..555
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55373
     Region          243..522
                     /region_name="Peptidases_S8_13"
                     /note="Peptidase S8 family domain, uncharacterized
                     subfamily 13; cd07496"
                     /db_xref="CDD:173820"
     Site            order(250,318,322,389..391,417,419..420,490)
                     /site_type="active"
                     /db_xref="CDD:173820"
     Site            order(250,318,490)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173820"
ORIGIN      
        1 mratrfnial arstharmla gmlsaaallp lagcgggggd gsnpsssnaa papapspapt
       61 ptpapptapp atsggnactt qqaasqmaar ttapaeppvd hlivklktlt atramaaldt
      121 gtrldaviqr sitrwsaptt tgaarayaav ttsqaslnvq vertlsdgaa vlsigqrias
      181 gdaaalaqaf aadgdvdyae pdhpmrirdt psdpaysqqw ylsdasvgin tppawtrtkg
      241 sptvvtavld tgyrphpdlv gnllpgynfi snantsnngq trsadatdpg dwvtqqeldd
      301 vngpyyhcas epstsswhgt rvmgvigana nngigvagvs wlgrilpvrv lgkcggktsd
      361 iadamrwaag ipvagvatnp npakvinlsl ggvgacsatf qqaiddvnak gvtvvvaagn
      421 dglstafdqp ancrgvisvg atdaaglras fsnfgsdval sapgvsilst anggtttpga
      481 dtygtasgts latpqvsgiv glmlsmngnl tpaqiqqklq ggaraamlpa stsctalpag
      541 agiadagaav maaiq
//
LOCUS       WP_175797369             322 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175797369
VERSION     WP_175797369.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..322
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35684
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,220,
                     222..225,232..233,236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdmlenmrlf vrvveagsft avakeidatt aqvsravsnl eahvqtrllh rttrhlglte
       61 sgeryferak silaeidyan aearnallrp sgkmrihamt glgqshvvss ivryqednpd
      121 vsveltlaqr mpnlveegyd vsivtasqlp dsgyvaqtcg tscsvlvasr dylarhgtpk
      181 tpddlpnhvc lrldtpaspa sewrlergdd eetvyelqpa pfqvnvpdal cvavragrgi
      241 acvalytvld dlregrlirv lpeyrlqtvs vyavyatrry ldakirtfld hlrttltpal
      301 endlreldrl tvghapgsrq ra
//
LOCUS       WP_175797420             153 aa            linear   BCT 11-JAN-2025
DEFINITION  Fur family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175797420
VERSION     WP_175797420.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..153
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16649
     Region          9..147
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 matsspidar lsradafaae hglawtplrr qvyervlvaq rpigaydlla elepqrgrvp
       61 pttvyraldf lvehgfihri esknaffacc eigvphegqf licdscgetv eipgsdlakq
      121 lsasapahgf evhhqvveln glcghckgkp ahr
//
LOCUS       WP_175797450             238 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Burkholderia ambifaria].
ACCESSION   WP_175797450
VERSION     WP_175797450.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..238
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=25633
     Region          6..223
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mdlesilytq gfgsrrqcrg lietgrvsva gasatdpdas fdtdglvftv ddtawpfhah
       61 aylalnkpag yecsrdpqhh asvfsllptp lvargvqcvg rldqdttgll llsddgqfvh
      121 aytspkrkvp ktyvatvrhp lddtqlnalr agvqlhgepk piavvaahar dthalaltvl
      181 egkyhqvkrm vaaasnrvea lhresigglt lpddlapgaw rwlgegelsa lrdsvktl
//
LOCUS       WP_175797466             269 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia
            ambifaria].
ACCESSION   WP_175797466
VERSION     WP_175797466.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..269
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29481
     Region          19..98
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(44,69)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(51..52,63,66,70..71)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          117..267
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mnqpssaptp pldatparal gefirahrer lspqavglpp gprrrtpglr reevaqlcgv
       61 sptwytwieq grpvsasada lariavalql skaeraylfe laaqrdpaep dvaagdlppt
      121 laatvaaiat payvldrqwn alawnapaaa lftgwldgeh drnllrftfm apaartlivd
      181 wetrarrlaa efradsirhl adaptralid almagsdafa qywasqdvfe regglrefdh
      241 padgrivyqq itlkpahred lklvvlvrd
//
LOCUS       WP_175797474             232 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia ambifaria].
ACCESSION   WP_175797474
VERSION     WP_175797474.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..232
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24832
     Region          10..232
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mfqirraadr chtrqgwles sssfplagha gathppfgal rllsedriap trgfgmqprr
       61 dleivtyvld galahrdslg ngaivraggi qrmsagtglm hsetnawcdr plhllqiwlq
      121 paerggrpgy aqrrfaddek rgrlrlvasp dgddgalsvr adarifagli dgdeetafgv
      181 pagrstyvhv argdvevngh altegdgari agvdtvafsr graaevllfd va
//
LOCUS       WP_175797478             455 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175797478
VERSION     WP_175797478.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..455
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47013
     Region          19..446
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(26..27,30..31,34,66,116..117,119..121,124,144,
                     147..148,151,273,276..277,280..282,285,313,317,369..370,
                     374,378,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mnadtglplp qrywaivcva lgitlavldg aianvalpti ardlhasdaa siwivnayql
       61 avtitllpla slgervgyrr iyiaglalft aaslgcalag slpmlavmrv iqgfgaagim
      121 svnaalvrmi ypssmlgrgl sinamvvals saigptvasa ilsfaswpwl favnvpigia
      181 avlgsvralp anplhdapyd fpsalmnacv fgllitavdg lghgerhayv aaelavafvv
      241 gyffvkrqls qpapllpvdl mripmfalsi ytsmasftsq mlafvalpfw lqnslgfsqv
      301 etglymtpwp lvivfaapla gvlsdrysag ilggiglalf aagllslati gahpgtvdiv
      361 wrmalcgagf glfqspnnra mlssaprers ggaggmlsta rltgqtlgaa lvalifglap
      421 dhgptialyv atgfaaiaam vsmlritspr pdaat
//
LOCUS       WP_175797635             507 aa            linear   BCT 11-JAN-2025
DEFINITION  HDOD domain-containing protein [Burkholderia ambifaria].
ACCESSION   WP_175797635
VERSION     WP_175797635.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..507
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=55540
     Region          18..216
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 msitahlprt alldklwarm nergdfplls eslratmaam knddldftal vrvvlsdfal
       61 tqkvlrlans amymafggni ttvtralmvl gmdtvghlvv glklvdhfhh stprridakl
      121 elnrallsgc varkltehae lrggeeavvc tlmrqvgkll vvcyldsewd rirrraaeln
      181 gddaaacvdv lgvgfdeigl eaaaswrlpd viragmtdgd graahaahrd egeeddeder
      241 ddcrrpaara degadrvrwl rsvsrcstdi agalampagp qrdahiavla qrygqeleid
      301 adalveiadr lareeasdtv mreivelran adaiaraqpe peacleagla dlralpsehv
      361 ltpvlalase sllaglaftr tvmfvrrddg mfaarlgfgp dvdaaldrlc fderfepdvf
      421 hlaitnsvgi fieqaqepkm vkrlpawyld alpdtrafvl lpvrvgtttv gllygdwaga
      481 qparkitqle msvlnelare lgrffpa
//
LOCUS       WP_175797552             386 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175797552
VERSION     WP_175797552.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..386
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39892
     Region          12..359
                     /region_name="MFS_YcaD_like"
                     /note="YcaD and similar transporters of the Major
                     Facilitator Superfamily; cd17477"
                     /db_xref="CDD:341030"
     Site            order(19..20,23..24,27,59,109..110,112..114,117,137,
                     140..141,144,214,217..218,221..223,226,250,254,304..305,
                     309,313,329,332..333,336..337,340)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341030"
ORIGIN      
        1 mkailnrdfl alilsvavvg lgtgatlplt alaltqaghg tnvvgmltaa qalgglaivp
       61 fvtalarrig arraivvsvv llaaatvlmq ftsnlilwgv lrvlcgaalm llftigeawv
      121 nqladdstrg rvvaiyatnf tlfqmagpvl vsqiagatsi rfalcgalfl lalptlatir
      181 raplagddah heahdswlav lprmpaliig tgffalfdtl alsllplyam dhgvasatav
      241 llasimlfgd tamqfpigwl adklgrervh lgagwivlag lpllpfvian pwlcwpllfv
      301 lgaaagsiyt lslvacgerf rgaalvtass lvsaswsaas fggplvagal meqlgsnalv
      361 gvlvacvaaf vaaalwerra alprav
//
LOCUS       WP_175797609             264 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Burkholderia ambifaria].
ACCESSION   WP_175797609
VERSION     WP_175797609.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..264
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28166
     Region          25..264
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mqrrfmlkfa aalgaaalfa sahaqaetik vgvtggphaq imdvvkrvaa ksgldirvve
       61 fsdyvqpnaa lasgdldans yqhdpylqaq vkdrgyklik vaetvtfpmg iyskrvksla
      121 elkpgariav pndptnggra llllqkqgil klradaglka tpldivdnpr klkiveldaa
      181 qiprslgdvd aaaintnyam eaglkpkqda iaiegtngpy anvlairdad rskpwvaklv
      241 aayhsaevkq fieqkfggav iaaw
//
LOCUS       WP_175797652             454 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrolipoamide acetyltransferase family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175797652
VERSION     WP_175797652.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..454
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48473
     Region          2..454
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mgihvikmpd igegiaevel vawhvdvgqt ikedqpladv mtdkaaveip spvagkvlal
       61 ggrigemmav gselirveve gdgnlkpgak ahdagadats rpaavdapar ssnvteaaea
      121 aeaaeaaeah daskaarhta erapaeprrt ehaappraar apgerplasp avrqrawdmg
      181 ielryvrgtg eagrilhadl dayartggaa ahgsqarghd erndetevpv iglrraiark
      241 mqeakrriph fsyveeidvt eleslrseln rrhgdtrgrl tplplliram vialrdfpqi
      301 narhddeagv vtrygavhmg vatqtesglt vpvlrhaear dvwsisaeia rladavranr
      361 aqrdeltgst itisslgalg gimstpvinh pevgivgvnr iverpmirdg aivarklmnl
      421 sssfdhrvvd gadaaefiqa vrgllerpal lfve
//
LOCUS       WP_175797680             774 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia ambifaria].
ACCESSION   WP_175797680
VERSION     WP_175797680.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..774
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81695
     Region          <68..>194
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          203..764
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mnapelsvhn esrralllgf asgglllafg vpslaraatp aqppvspnpq yggagmphgl
       61 rddphlfvai apdgavtvtc irsemgqgvr tsvalvvade lgadwarvkv aqavgdepry
      121 gnqntdgsrs lrqsfaalrr agaaartmle qaaaaiwgvd vrqvkatvhe vvdtktgrkl
      181 gfgelaakaa alpvpdtqsv alkapaefry igkgetalid grdivggrah ygidtrldgm
      241 lyavvarppa ygdtvasfda saaeqlpgvv kvvqlasapl psgfqplggv aviardtwta
      301 iqararlkid wkrgphagyd saayrktlea aaaqpgdvir ddgdtaaala gaakrvraty
      361 yiphlahatm eppaavarva dgrcevwtct qapqttrdei akalalpser vtvnvtllgg
      421 gfgrkskpdy vveaallska vgapvkltft reddiahdyf havsleafdg gldaagkvva
      481 wqhrtvapsi qstfragvvh eqpgelaqgi adlpfavpnv rienpaaqah trigwfrsvy
      541 niphafgiqs fvselahaag rdpkdflldl igparrfeph itvknvnyge dpalypidtg
      601 rlrrvietva reagwgrklp kghglgiaah rsfvsytaav cevqvaadga isvprvdiai
      661 dcgpqvnper vrsqlegavv mglgialhge itfkdgqpeq snfngfqvlr mneapreirv
      721 hlvapddyat plggvgepgl ppvapaltna ifaatgtrir slpvadqlak qkvg
//
LOCUS       WP_175797712             151 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175797712
VERSION     WP_175797712.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..151
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16548
     Region          11..147
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mskrldynqi apagvkalgg vygyvlqsgl spvlvdlvyl rvsqinncay cldmhtrdll
       61 kkgvkvekla lvqawreagn lfdereraal awaesvtlva atgvpdeayd aaravfdere
      121 ivdltiavgl mntynrmais frntpqavle q
//
LOCUS       WP_175797812             133 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia ambifaria].
ACCESSION   WP_175797812
VERSION     WP_175797812.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..133
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=13834
     Region          60..>132
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mkvfplqara prfhrrpatr lgmavaiaaa vactavapnv faagddgass smssthtstg
       61 akirdatitt kakaelvgts glsagdihvk trrgivmltg svpdeqqrtq avsvvrqieg
      121 vqdvrdqlti rpk
//
LOCUS       WP_175797820             400 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia ambifaria].
ACCESSION   WP_175797820
VERSION     WP_175797820.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..400
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42956
     Region          5..362
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 msaawdrarr ilcvrldslg dvlmttpalr alkesgqgrr ltlltsrtga alskhlpmvd
       61 dvwtydapwv khpdargdpv vdldmigrll aghfdaavif tvysqsplpa ammcwlagip
      121 lrlahcrenp yelltdrvpe pepesyvrhe varqlalvrs igaktsdwrm afepgdaarh
      181 alharlraal eriggprrpg sararwlvvh pgasaasrrw paerfgaaaa rlaplfdgia
      241 vtgsaderpl veavceragp ravplagalp lgelgaliet adlllsnnsg pvhlaaalgt
      301 pvvdlyaltn pqhtpwrvph ralnvdvpcr ncyrsvcnqp ghpcllgvsv ddvvaathal
      361 lrgserhaqr aagraavrgv epvaanasnv ipfahvitrs
//
LOCUS       WP_175797821             283 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia ambifaria].
ACCESSION   WP_175797821
VERSION     WP_175797821.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..283
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=32473
     Region          160..>240
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mqrrypgrqa ersgppdwqe rgerayrgge rdfrgdetrr hdadyesayr rfasedvgpe
       61 dwgsewsers artsaerrpg dvgadwrdap ggsrdpewea ergygsrgrr meggegregr
      121 yggdqpgfre hyrmggygge raydprdphd prrtdaqrea mrqrrgpkgy trsderired
      181 vcerlahald idvsdvtvqv rdgrveldgt vpsrwmkhdi ediadgcmcv rdvenrvrvr
      241 rdddeqqpgt vlhpsqrtvt ptqpavrdpe pgrgtgrdre shh
//
LOCUS       WP_175797884             146 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia ambifaria].
ACCESSION   WP_175797884
VERSION     WP_175797884.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..146
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15754
     Region          17..144
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mtddwvetgd wtvlggdaar irdavfvreq rippeweldd edplslhavv yrvdaatgtr
       61 ravgtgrllr sgmigrvavl adargqgags avlhalldaa rhrgepvvrl yaqdaavafy
      121 vrhgfttigd rfvevgvphv emarap
//
LOCUS       WP_175797907             405 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175797907
VERSION     WP_175797907.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..405
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41453
     Region          8..392
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(18..19,22..23,26,61,108..109,111..113,116,139,
                     142..143,146,223,226..227,230..232,235,265,269,318..319,
                     323,327,343,346..347,350..351,354)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mpdsryrwvi vaagglmgcv aigamfslpv flraiardtg wsmtgisaam tlgfiamafa
       61 sigwgslsdr vgtravvvtg avllsaslal asrapsllaf qlifglavgs ataavfapmm
      121 acvtgwfdth rslavslvsa gmgmapmtms plaawlvsgh dwrtsmlaia alaavvmipa
      181 sllvrrapal dgpldgptpa ggpvtpplsv ggalrspqfl vllltnffcc athsgpifht
      241 vsyavtcgip liaavsiysv eglagmggri afgllgdrlg akrmlvagll aqalgalgyy
      301 fvrtldgfya vatlfgfiya gvmplyavla renfplrmmg tviggcamag slgmaagpva
      361 gglivdalgs ygwlylgsfa igiggflvam mfrpfpkers qtvaa
//
LOCUS       WP_175797916             273 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Burkholderia ambifaria].
ACCESSION   WP_175797916
VERSION     WP_175797916.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..273
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28151
     Region          2..272
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mlktrvitav vmlavllpvt lfapltafga ligvvlvfaa wewarllklg aagsvvyaia
       61 aaaalaatap lgvgaassrp lfmaagvfwl lvgpfslrrk pelaggvwra fllaaglvvf
      121 aacwhalvaa raegvpfvls lllvvwladi gayfagkafg krklaitisp gkswegaigg
      181 wlavmvvagv amaahwlept lfsafaaryg mpgawaaltl lvaysvigdl fesllkrqag
      241 vkdssgllpg hggvldrvda llpvlplaml llg
//
LOCUS       WP_175797935             695 aa            linear   BCT 11-JAN-2025
DEFINITION  M3 family metallopeptidase [Burkholderia ambifaria].
ACCESSION   WP_175797935
VERSION     WP_175797935.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..695
                     /product="M3 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=76919
     Region          4..693
                     /region_name="Dcp"
                     /note="Zn-dependent oligopeptidase, M3 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0339"
                     /db_xref="CDD:440108"
ORIGIN      
        1 msasantnpl ldfsglprfg eirpehvtpa ldtlldtanr avdtasapat patwativet
       61 veqateplgr awgvvghlna vadtpelraa ygenlprvte fwssvgqnla lyekykaiaa
      121 saeyatlsae rkkildnalr dfrlsgaelp edqkprfael qeqqaalska fsdhvldatn
      181 ayayfaqdea elaglpgdai eaareaaqke gkegwkftlh fpsyfpvlqy aenramretl
      241 yrayatrase lgpqygggka ewdntaivad elklrreeaq mlgyrnfaev slapkmaesp
      301 qqviafledl atrarphadk dwdelrafaa kelgltelap wdvafaaerl rqqryafsen
      361 evkqyfpepa vlkglftvte tlfgvrikpd dapvwhrdvr ffrvenrdgs lvaqfyldly
      421 aregkrggaw mddararakr ggtvqtpvay ltcnfsapvg gkpacfthde vitlfhefgh
      481 glhhmltrvd elgvsgingv ewdavelpsq fmenfcwewd vlssmsshid tgaalprelf
      541 dkmiaaknfq sglgtlrqiv fsmfdmllhv dfdpagatgv nafareiner yhvipqaafs
      601 rwpntfshif aggyaagyys ykwaevlsad ayaafeeaaa aggsvldaat gtryrreile
      661 vggsrpamds fkafrgrepe idallrhngm tsaah
//
LOCUS       WP_175797944             353 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia ambifaria].
ACCESSION   WP_175797944
VERSION     WP_175797944.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..353
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=37124
     Region          10..353
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mirfavptma sllaasgama qgsvtlygiv dqsiryttha nasndasvqm tngaitnsrw
       61 glkgsealgg glkaifqles gfepqngqld galfgryayv glasdwgtvk lgrqateafn
      121 lfgdldpltv gnytanmwpy fltqgrasna vsydgtfggl dvgasygfgg vagslganay
      181 wgthvsytlg glmvgatyqq vrdlhsraqq awgagaryaf gaatlyagyl ggidrtgmld
      241 rqmlnapgrd vsygsfvdnp rrdaifytgv svkvtpavsv tgvayyddmr nvngvagngg
      301 krytgvleae yalskatqvy atldynrvtg gaftempgrd nqtgiaaglr hlf
//
LOCUS       WP_175797961             396 aa            linear   BCT 11-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Burkholderia
            ambifaria].
ACCESSION   WP_175797961
VERSION     WP_175797961.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 396)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 396)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 396)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..396
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41523
     Region          41..394
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mtqlfdtlgf ietsavrara aardahgapp eaamradvaa vslvhvgkvf atprghaaal
       61 rdvtldvrrg evfgiigrsg agkstllrlv nglerpssgs vrvqgvdvga ldedglvalr
      121 rrtgmvfqhf nllsaktvfe nvalplkiag vpkaertrkv dalldlvgla akrdaypasl
      181 sggqkqrvgi aralvhdpev llcdeatsal dpettqsila lladinrrlg ltivlithem
      241 eviravcdtv avieqgevve tgpvwrvfgd prhgatrall stlvhdlpae laarvqplpe
      301 qaalpdgaqv vldvrytges ggepdvgala aalggsvrfl hggieriqgh aqgrlviaas
      361 pradevgqsl ahggavaall erarrhanha evlgyv
//
LOCUS       WP_175797971             241 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            ambifaria].
ACCESSION   WP_175797971
VERSION     WP_175797971.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..241
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25984
     Region          25..181
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 meqtsepprp igaavatehr lprgarrkqa trmrllraaf mlmaekgmdn vaiseiteaa
       61 dvgfgsfynh faskdglfaa liewvfddfa drlervtggl sdpaevvsvc vrhtlmqahq
      121 ewmwgrflml eglsvraldr glgqrlrrds argiaarrfv vgdpfvsvla stgtilaaia
      181 aqlhiartvk ggarrraagv gdfpertaav vlqtlgiara eahaianrpl ppgdftvtgg
      241 d
//
LOCUS       WP_175797977             257 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            ambifaria].
ACCESSION   WP_175797977
VERSION     WP_175797977.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..257
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27800
     Region          39..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpntpnrrtp krsapeagna pepaksevav aeereprgar rkretrarll daalrlmaqk
       61 gmegvainei teaadvgfgs fynhfeskea iyatlvesvf eefadsldrv asglsdpaei
      121 vsvsvrhtli rarrepvwgh fliregfsar vltlglgqrl lrdiergiae krfvvadpfi
      181 gflsvggtvl taiaaelnfv apgapaadvl kelgfsgehf pertaatllh tlglkraeae
      241 kiasrplpvv eaaetpq
//
LOCUS       WP_175797988             334 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Burkholderia ambifaria].
ACCESSION   WP_175797988
VERSION     WP_175797988.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..334
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35936
     Region          7..303
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(12..14,44,49,75,138..139,179..180,201,230..236,272,
                     289..292,297,300..301)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(44,49,75,138)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 mritlpsrlg fgtaplgnmy rdipheeala tvdaawrggi ryfdaaplyg aglaelrlge
       61 alagrprdey algtkvgrlv ldehedasqr dlgekgglfr hglpnrivyd ytadgtlrsi
      121 easlarlrtd rldtvwihdp avdfhgdawr hvfdvamsga akaltrlrde kvikgwglgv
      181 nrvepcelal ersdpdgfll agrytlldha galerlmpes aarglgiivg gpynsgvlag
      241 gthfeyqpat qamlervari rglcerfgvd vravalqfsl ahpavaaaip gasrperide
      301 nlrlaaapip aalwaalkae hliaehaptp agad
//
LOCUS       WP_175797997             417 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia ambifaria].
ACCESSION   WP_175797997
VERSION     WP_175797997.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10396284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..417
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=43873
     Region          1..261
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Site            order(7,9..10,12,66..68,104..106,116,120,139..142)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187535"
     Site            order(82,106,116,120)
                     /site_type="active"
                     /db_xref="CDD:187535"
     Region          308..407
                     /region_name="DoxX_3"
                     /note="DoxX-like family; pfam13781"
                     /db_xref="CDD:463982"
ORIGIN      
        1 mnilvcgang figqalcarl eaaghrvlrg vrhavgphdv aidfatdldp dawlarldgv
       61 dvvinavgil adrrdatldt vhraapcalf tacsrarvrr viqisalgve rgdtpyfask
      121 yaadtflqtl pldyrivrpa lvygatgtsa rffrmlaslp vhalpagghq rlrpvhvddl
      181 aelvarlvvs paagnsviaa vgadeveyre mlsgyraalg fppaarialp gslvgaaaal
      241 fgtlpgamlt rdtwtmlrgg ntgdpaalaa vlgrpprglr sfigadalal rrdalamwrr
      301 plllgalaiv wiwtaivsaf vhpqsdslam lsrahltglp alialyaaca ldfalgvatv
      361 aapsrrlwva qgvlivaysa viavtmpgll aepfgpvlkn vpilaillil fseeeqp
//
LOCUS       WP_175798006             558 aa            linear   BCT 11-JAN-2025
DEFINITION  alkaline phosphatase family protein [Burkholderia ambifaria].
ACCESSION   WP_175798006
VERSION     WP_175798006.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 558)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..558
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=58140
     Region          48..536
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 misrfakqrn mavmvagala lasagayaaq qdgnsqgeng gharrvvkhv llisvdglhe
       61 qdlarcvgan tcpniavlaq sgvtytnayt pglsdsfpgl aalvtggspk taglfydvsy
      121 drnlyapgdt tcsgkqgwnv vfdettgida fnggalvhld gggafnpqai pnakvdgkcv
      181 pvyphnyvkt ntvfeavkag vpnaytawad khawgydwvn gpsgkgvddl mrteinsidp
      241 atqtaytdvy shtaqfdnlh vqalinqing rdstgtkssp vptlfgadfq tlsvaqkapv
      301 tkgggyldan ftpngqvana ityvdnsigh vvaalkqanl ysstavivta khgqsptdht
      361 klvkngdtlt klleannyld pngnfgqnnt ttgnpndgsg lvgtglvqtd dvgliwlrdr
      421 gqrtavvqtl kanlgcnapg icadgaqati lygaaladrf gdpangrtpd iivqpnpgvi
      481 ytsstkkdee hggnapddsh lgllvsypgl hrartvsdlv gtkqvaptil gllgaeprll
      541 navvaenthv lpglgigr
//
LOCUS       WP_175798026             234 aa            linear   BCT 11-JAN-2025
DEFINITION  MOSC domain-containing protein [Burkholderia ambifaria].
ACCESSION   WP_175798026
VERSION     WP_175798026.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12233312
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..234
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25646
     Region          31..183
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
     Region          180..219
                     /region_name="3-alpha"
                     /note="3-alpha domain; pfam03475"
                     /db_xref="CDD:460938"
ORIGIN      
        1 msgdtrpaia vaiaavrvgt srplagtphl saidkqpvda rlwlgargfa gdgqadarhh
       61 ggpdkavhhy aydhyawwsa qigardvlgr pgafgenlst hgvteddvcl gdvftlggav
      121 lqvsqsrqpc wklnarfdhp rmaalvqqsg rtgwyyrvld egwvapgdvl alherrypqw
      181 plsavldvly rrtldmaald alggvpvlpp gwrkmldtrr terqvedwtk rleg
//
LOCUS       WP_175798008             936 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Burkholderia ambifaria].
ACCESSION   WP_175798008
VERSION     WP_175798008.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 936)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 936)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 936)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 936)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 936)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11534155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..936
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..936
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=95538
     Region          11..79
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          114..174
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(120..122,125)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          187..934
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mteplasagl qtieltvdgm hcggctarvq ralaavpgvv eaavdldaqv atvtaqdtve
       61 paqlvdavga agyratvrea afeavaaaqa qhasraealp atpaalpata atieleidgm
      121 tcascvsrve kalakvpgvt rasvnlater atidaapdvs asrlaeavqq agygatavaa
      181 tppaasrdle fdiggmtcas cagrvekala avpgvarasv nlaterasvh gagaldaavl
      241 iaavttagyr aslaaapdaa tggaaevpag dptqapeark rreairernl vigsavlsap
      301 livpmlvapf gidamlpgwl qlvlasivqf gfgarfyraa whavkartgn mdllvalgts
      361 aafglslwml vrdpadpghl yfeasavivt lvrfgkwlea rakrqtseai ralnalrpdr
      421 arvvehgver dvplalvrvg ttvsirpger vpvdgrivsg rshvdeslit geslpvpkdd
      481 gdpvtagsin gegalvvatt aigaettlar iirlvesaqa ekapiqrlvd rvsevfvpai
      541 lgiavltlig wliagagtet ailnavavlv iacpcalgla tpaaimagtg vaarhgvlik
      601 daqalelaqr ttviafdktg tltegkpsvt afdavgipre qalalaaavq rqsdhplara
      661 vvaaheadvv arggdagspd ivaadarava grgvqahvdg qllalgstrw rdelgivvpp
      721 eldaraaele ragntiswlm radapralla liafgdtvkp gardaiaals argvasvlvt
      781 gdnhgsaaav aaalgigevh aqvlpddkar vvaelkrthg gvvamvgdgi ndapalaaad
      841 vgiamatgtd vamhtagitl mrgdpalvad aidiskrtyr kiqqnlfwaf vynligvpla
      901 algwlspvia gaamafssvs vvtnalllrr wkgrar
//
LOCUS       WP_175798021             507 aa            linear   BCT 11-JAN-2025
DEFINITION  peptide MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175798021
VERSION     WP_175798021.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 507)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..507
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55513
     Region          7..462
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mmhapvsqtr sfttvfliem werfgyygma allvlfmvdr lgftdshanl twgaftalvy
       61 aspsiggwig dkvlgarrtm iigaavlcag ylmlavpnda laymyaslgv ivvgnglfka
      121 naanlvrriy egddaridsa ftiyymavni gstvsmlatp wikdhwgwht afavccggml
      181 lailnfmlmh rtlahigsqp ddepirwkrl ggvaaggval alitlyvlqh kqlavasvwt
      241 aafailaifa ymiakserse ragliaalvl igqvilffif yvqmstsltl falrnvdprf
      301 ilfgttlftw saaqfqalnp iwimmlspll vwiynafsks grdlpvaaky afgfgavaag
      361 ylvftisgry avdgrvsswf mvwgyglysl gellvsglgl amiaryvpar msgfmmgayf
      421 vatgvsqylg svvanfaqmp shdlpatesl plylslfekl gwlaaigmll allllpmmnr
      481 lsrqhqrcad erreeeavqt qamasaq
//
LOCUS       WP_175798062             580 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia ambifaria].
ACCESSION   WP_175798062
VERSION     WP_175798062.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..580
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=62772
     Region          38..564
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mhasvfaqta ptpavrpiqd paqliieqqr eqarqrqldq ppasitvapt tgtsldippg
       61 tpvesiietg ptfavkriel qtpdgkpfdp prgistkqld vivksfvdhe lgshrinvll
      121 kritdvfier gyvttrallg pqnlatgtlk itiqlgviea ftvtgkpihr lkagessagg
      181 gwftdagyen afptssgdpl rlsdidqgva qinrlrrnqa tvqilpgqnp gesvvdignk
      241 pgdrlyytlg vdnygssatg vtryragvea dnllglqesl slnfldslds naivgsfavp
      301 fgrhtfsyti sdseyqqlig ttaleygrtl shifgwnylv srsvsditsv datvswrrtd
      361 revngidldp qrvavfrlgg swlhkfvmnd aqgnftlngg vsqglpwfga nhdphgitrd
      421 eahsqftkvd ataaftlplp kigrallayr gvlggqytnm alfgseqlyl ggmdtirgfr
      481 sgeiagdrgf ysrnelawvn apawkdgrie pyvfvdagka slvaipgfpt lagagtglrv
      541 qwqwhkqsls gellvgralv qpaalgskat lvlgtlnwfy
//
LOCUS       WP_175798140             468 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia anthina].
ACCESSION   WP_175798140
VERSION     WP_175798140.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..468
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48837
     Region          17..467
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mammsestgt lqatptteda pralsqtlsv rdavmitvsg vtpassifvi apfaiqqags
       61 gavlsfvlgg vlalafalcy aelsaahrsa ggeyvmakrv fgtlpgyltf itvlsvsvfi
      121 pavlasgaap ylnnalgthf snqsvaltiv llsyvlgmln iktnawitga flvveigvlm
      181 liaglgfgsp hrgadvlvap vvvsgtalvp atlaaivpai gtaifcyngf gsaaylaedl
      241 rggnrnvaka viysllvilv velvpltaiv lgapsltelt ksadpigyvv rslsnpvvsr
      301 ivsggiflsv fnaiiaivit mgrllyssgr helwsracnr afstihprle spwlatlala
      361 vpsaglvfvs sldeltaftv dlllliylvv glaalasryv rrdvehhyrm plwpvtplva
      421 vagaaytlyt tlatatkstd lliiggllva alvmygvwar hsdafrsl
//
LOCUS       WP_175798143             462 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175798143
VERSION     WP_175798143.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..462
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48817
     Region          24..430
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,152,
                     155..156,159,265,268..269,272..274,277,304,308,358..359,
                     363,367,383,386..387,390..391,394)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mantvnaagr ldrlpvsrfh wkilgliagg afldafdiyl angsvasmvk dgftdlrhga
       61 mfvsstfvgm migafvagyv gdrlgrrysy qlnlavfgla siaacfapdi awlivlrfim
      121 giglgaelvv aagtlaefvp petrgkwvsl laiitnsglf aalaagywii phlgwrymfa
      181 lagigalvvw fmrkrmlesp rwlesvgrld eaeatlaaie qevsqqvgtl ppvrrtidlh
      241 vgkvplgvlf skgmrgrmav aaltaigvnv glygfiawlp tffvtqglsv vkslgfvflm
      301 sigspvggli gyliadrigr argiviasll smalgwlyvs lrdttaiilv gfclvsaiyt
      361 ittlglfgyi pelfptevrl rgtgvagmcg rmssigtpal alalyqafgv sgviamvsat
      421 lgvlcvaigl lrietgrqal eevapgtsda dgaavaprvt qv
//
LOCUS       WP_175798184             218 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator transcription factor [Burkholderia ambifaria].
ACCESSION   WP_175798184
VERSION     WP_175798184.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..218
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23686
     Region          12..206
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mtdlngdtte pvvfviddds avreavetll dsvglhvvsf dsahaflaas lpdrpscvvl
       61 dvrlkghsgl avqehivrnm rlpvilmtah gdipmsvqam kagavdflpk pfrgqdmida
      121 vtralesdrk rrtsdrsmai lrasydtltp rertimtmva ngllnkqiat elglseitvk
      181 lhrgqamkkm kspsiadfvl kaealglisr derlaaqa
//
LOCUS       WP_175798189             282 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175798189
VERSION     WP_175798189.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 282)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15747380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..282
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30755
     Region          23..158
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          197..278
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msrsantiav pspfwrdaal pfieartvdd grticyakht hdtfslgaiv ggtstylnga
       61 tkehvgrgvl viidpeqvha cnpygpdawa yrmvyvdvpw ltrlqhslgr dpngdfrgfs
      121 pkltqrcdlf aqfggfyrtl vspgvdplgk esaavefftr lhgaldrdlp adaargvdna
      181 klaraadyia ahcrqavtld aicaaadlsp sylirafnar ygmtphafli drrvqygrae
      241 lrrgrpiadv aldagfadqa hfqrafrria aatpgqyrsa as
//
LOCUS       WP_175798214             437 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia anthina].
ACCESSION   WP_175798214
VERSION     WP_175798214.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..437
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46568
     Region          25..396
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msaslaassp lpqqsslrhl paddarvaal lerlapelaa daarndterl fphenfarlh
       61 ragliaqvvp rehggagatl aqasrivaav aradpatalv ltmtylqhra lgradnrwpa
      121 hlraavfnsa vdegalinal rvepalgsps rgglpetiar rdgdgwrlsg hklystgipa
      181 lrwlavwart depeprvgvf lvprergadd arirvieswd hlglrasgsh evvfddvplp
      241 adhavdvrap dawavsaash advdaqtdqq awmvallgsl ydavarasrd wlldfattra
      301 psglgaslat lprvqeavge iegwlhanrv llddhiartd agvapsvtts glvkrtvteh
      361 airvvehalk lsgnhglsrr nplerhyrdv lcsrvhtpqd daiavaagra aldaaarrag
      421 vadessrnap aagrnda
//
LOCUS       WP_175798209             455 aa            linear   BCT 11-JAN-2025
DEFINITION  CpaF family protein [Burkholderia ambifaria].
ACCESSION   WP_175798209
VERSION     WP_175798209.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..455
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50687
     Region          54..438
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mslreqmsly rtqpqaagte pagaahssvr dayqklrrei hltvlervel erlsrlpqeq
       61 vrqeisslis rildeerlla ndierrqlai dvydemfgfg plesllrdpg isdilvntyr
      121 qvyversgql eltdvtfydd ahlmkvieki vsrvgrride stpmvdarlp dgsrvnaiip
      181 psaidgplms irrfavnplk mddlvsyqsl tppmaellda lahakvnvlv sggtgsgktt
      241 llnilsgfip rserivtied aaelqlqqph vlrletrppn iegkgeitqr tlvrnalrmr
      301 pdriilgevr gaealdmlna mntghegsla tihantprda ltrlenmisv ggltlppktm
      361 rqqiasaisv vvqatrltdg krkivsiqel tgmegdiinm qeiftfkrtg mdrdgtvrgh
      421 fcatgvrpkf aerlqafgin lpdslydpaq ryetk
//
LOCUS       WP_175798218             271 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia anthina].
ACCESSION   WP_175798218
VERSION     WP_175798218.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..271
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29058
     Region          19..266
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mvsaavless vsaspdaaap rgaridihhv shafdgpggp lpvlddvtls vaagefvall
       61 gpsgcgkstl lrlvagldaa rqgtiaqdga pieqpdpsri vvfqdptlyp wrrvranval
      121 gleargvart aqhrvddala rvglqefsnv fphqlsggma qrvalaralv ndprllilde
      181 plgkldsltr ltmqaeltal wqrdgfsall vthdveealf laqrvivfgp rparivaelr
      241 vdlpyprhrg dprlaelrhe alrhlgldas w
//
LOCUS       WP_175798284             328 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia ambifaria].
ACCESSION   WP_175798284
VERSION     WP_175798284.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..328
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34543
     Region          6..324
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mndldnrpvr fgivgagsia rrfaqslahv pgaalagvwa rradaaaafc dscggtpaas
       61 ldallasdid aiyiatlhds haqyaqaala agkavlcekp atlnaaqlda vldaaraagr
      121 lfmeamkppf fplyrqlrah lrddpigeir lvragcasss vpddhsvyrl draggalldi
      181 giyeaflavd wlgaaldvqt lgrigatgvd vfaslnsrha nggiaqlfcg ldvmgrgdal
      241 iaaagghvti hekwwnpara tiryadgrtv eldapfdggg lnyetahfcd llrvgeresp
      301 imthdhsrqm iamtdaaraa lgvrysge
//
LOCUS       WP_175798398             463 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175798398
VERSION     WP_175798398.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..463
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=48433
     Region          8..463
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 msdlssnddv vaalrdalga dcvsagdaig arhftnygea agirprallr prsvddvsra
       61 laictahrqt vvpqggmtgl aagaepgahd vvlslermtg vveidadaat vtawagtple
      121 alqqavddag falgidlgar gscqiggnva tnaggnrvir ygttreqvlg levvladgtv
      181 lstlnkmlkn nagydlrqif vgsegtlgvv trvvlrlhpr laapstalca vrdtaaalal
      241 lraartacsd llsfeamwpa fygyvcehtp glraplpadd gvkvliecas gdaaqtaerf
      301 eavladwler gliddaalaq qaadaqafwt vreglaidal pglvnfdvgi ppretaafie
      361 acdralktrw pgayvfffgh lgdsnlhvcv sapyaagesa hdvdavlypl vrdaggsvsa
      421 ehgigrykrd wlgcsrsdae iaamrrlkha fdplgllnpg kvi
//
LOCUS       WP_175798402             229 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia anthina].
ACCESSION   WP_175798402
VERSION     WP_175798402.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..229
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24199
     Region          23..227
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mtdvlplttd sesglqyrlr paagrpagrl lllhgvggne tnllnlagti dprieiafvr
       61 gpltfgpnqh awfpvrfgpn gpeidaarad asrvqlitll ralnardaeh dtpalptvia
      121 gfsqggimsa svgltspadv aafavlcgri lpeidpliap rdalsrlhal vmhghaddkl
      181 pvawahaadt kltalgvahd trlydaghel taqmardfgr wvdaragln
//
LOCUS       WP_175798404             496 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia anthina].
ACCESSION   WP_175798404
VERSION     WP_175798404.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..496
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52540
     Region          27..474
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mkhaserpae taggadprha drdamfashe agyakqlkpr hvqmiamgga igtglflgag
       61 grlqsagpal avvylvcgvf aflimralge lvmhrptsga fvsyarefmg erasfvagwm
      121 yylnwattgi vditavaiym kywavftdvp qwvfalgalg ivsvmnmigv kvfgemefwf
      181 sivkvgtlal flavgaifla sghpvaghap glhlvaehgg ifphgilpav livqgvvfay
      241 asielvgvaa getadarkvl pkainsvmwr ialfyvgsvv lltmllpwta ysshespfvt
      301 ffsklgvpyv gtvmnivvlt aalsslnsgl ystgrvlrsl amggsaprfv srmnargvpy
      361 ggilvtvain aigvplnyiv paqafeivln maslgiistw gfivmcqilf rravnrgels
      421 pvsfrmpgap ftswltlgfl asvlvlmafd ypggtwtiat ipvvalalvi gwklakrgaa
      481 reaaaapaig dparnv
//
LOCUS       WP_175798456             431 aa            linear   BCT 11-JAN-2025
DEFINITION  multicopper oxidase family protein [Burkholderia ambifaria].
ACCESSION   WP_175798456
VERSION     WP_175798456.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..431
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=47256
     Region          64..327
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mvsrrqflsg sgaallgaam vskagaaslp eaptmakagt qpplvppngr pytpvatlng
       61 wtlpwrmkng wkefhltaep vvremapgmn anlwgyngqs pgptieaveg dkvrifvtnr
      121 lpehttihwh glrlpngmdg vggltqphip pgktfvyefq leahgtfmyh phademvqma
      181 mgmmgmfivh pkdratmpvd rdfvfllaay didpgsytpr vnemtdfnmw tfnsrvfpgi
      241 dplpvragdr vrirfgnltm tnhpihlhgy sfevagtdgg wippaarwpe vtadvavgqm
      301 raieftadrp gdwafhchks hhtmnamghq vpnligvpqk dlakrigklv pdymamgstg
      361 gamggmempl pdntlpmmtg tgpfgplemg gmftvlkvrq glgrydyrdp gwfrhpkgtv
      421 ayeytgelpd g
//
LOCUS       WP_175798468            1068 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia ambifaria].
ACCESSION   WP_175798468
VERSION     WP_175798468.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..1068
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=114867
     Region          1..1035
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 miahvirwsv rnrflvllat vllvawgvhs lrqtpldalp dlsdtqvivk asypgkapqi
       61 vedqvtyplt ttllgvpgak tvrayssfgd afvyvlfddh tdpywarsrv leylsqvqsr
      121 lpagatvslg pdatgvgwvy eyalvdrsgr hdpgqlraln dwflkfelka vpdvsevasi
      181 ggmvrqyqiv ldpdklrayg itqaavadal gkanqasggs vvelaeseym vrssgylrtl
      241 ddfrhvvlrt deagtpvllg dvarmqvgpa mrrgiaelng qgevtggvvv mrsgknaltt
      301 idavkaklaa lkrslppgve ivttydrsql ieravdnlrd klieefviva ivcavflfhl
      361 rsalvailal plgvltafiv mryqgvnanl mslggiaiai gamidaaivm ienahkhlea
      421 ygdahpgepi ttarrwelvt asaaevgpal ffslliitls fipvfslegq egklfaplaf
      481 tktytiaaaa glsvtlvpvl mgylvrgrip pehanpinrv lirvyrplle atlrrpwfai
      541 gvavvalllt alpvsrlgge fmppldegdl lymptalpgi sadkasellq qtdrliktvp
      601 evdtvfgksg radtatdpap lemfettirf kprsawrpgm tpeklvdald rtvkvpglsn
      661 vwvppirnrl dmlstgiktp vgvkisgpdl pgidaiatqv eavvkhvpgv tsalaerlng
      721 gryidvdidr laaaryglsv adiqsvvssa iggedvgevi agrerfpini rypreirdsl
      781 enlrqlpvvt argaqlrlgd varvviadgp pmirsenarl sgyvyvdirg tdlrtavram
      841 qqavaqqval ppgysiawsg qfeyleraaa tlrtvvpvtl avifvllflt fgsaadalll
      901 mstvpfalvg gfwlvwalgh avsvatsvgf ialagvaaef gvvmllylkg alrrrldage
      961 pltdavllda iregavlrvr pkamtvavvl aglvpimigh gagsevmqri aapmvggmvt
     1021 apllsmfvip aawllrqrrr argasrrrhs davphgmnvp snptgesr
//
LOCUS       WP_175798555             430 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175798555
VERSION     WP_175798555.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..430
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45798
     Region          22..424
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(36..37,40..41,44,77,127..128,130..132,135,155,
                     158..159,162,256,259..260,263..265,268,296,300,351..352,
                     356,360,376,379..380,383..384,387)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnllnpatpa yeageaiprr rwlrvippll lacivsymdr vniafampgg mnadlgmdat
       61 maglaggiff fgylflqipg grraalgsgk tfiawslvsw avlsaltglv thtwqlltlr
      121 fllgvaeggm lpvvltmvsh wfpdrergra namvimfvpl agmitaplsg lilaaydwrh
      181 lffsagalsl lclvawmlfa ddgpetarwv sprekayild alrdeqarkq aagapaaasf
      241 gailrnptiw lliainfcyq vgiygytmwl ptllknlthg gmgkvgllam lpyvamvigm
      301 fatsylsdrt gkrrlfvllp lvgfaaclal svlmhasmvv sfafligcgf flqaaagvfw
      361 aippklcsve tagsarglin algnlggfcg pyavgvltqh vsaaagvysl avtlavagll
      421 altlpkrceg
//
LOCUS       WP_175798566             317 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175798566
VERSION     WP_175798566.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..317
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34080
     Region          2..182
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          214..297
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdplsevlsl lttrdayftg lraggewavd lpppegikfn avvegscwlt vdgagppvrl
       61 rtgdcfllas praftlasdp svapltvadv yrnvergiah ygepadcfli ggrfsyhegm
      121 plllgslppv vivsgesdqa avlrwalqql arefgtsspg aalmvrhlgh mmlvqilrhy
      181 vdsganrdvg wlagfadarv saalaaihaa parrwtvdel aacchvsrst falhfkrrlg
      241 fgpleyvlrw riqlamrelr rsnasisava qmlgydsdsa fghafkrivg cspsayrhek
      301 agaqngqprd avdngag
//
LOCUS       WP_175798576             351 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia anthina].
ACCESSION   WP_175798576
VERSION     WP_175798576.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..351
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37634
     Region          31..334
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 msfplspafr rttlsarral aatltaalaf agvglpqaah aegririaeq fgvvylmlnv
       61 ardqqlieke grkagidikv dwvrlsggaa vndallsgav dvagagvgpl ltvwdrtrgr
      121 qnvkgvaslg nfpyylvsnn pnvktiadls akdriavpav gvsvqsrvlq yaaatqwgdk
      181 qfdkldaltq aiphpdataa ilansnvitg hfgnppfqeq elagnpgahi vlssydvlgr
      241 pssatvlyat qkfrddnpkt yhafvaalad aarqiaadpe raadtyirvn gskidralll
      301 kilrnpqvqf ktapqntlrl aqfmyrtgai rnepkswrdy ffddpatagg s
//
LOCUS       WP_175798577             302 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175798577
VERSION     WP_175798577.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32812
     Region          8..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..295
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(106,110,149,163,165,230,247,274)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(107..108,112..113,115..116,119,123,125..131,192,
                     223..224,226..228,235..236,239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 marrfdhlgd veafvtviek gsmtagaval gstpsvlsra itrletrlgv qllrrstrrl
       61 slteqgrlyl eqsraaflli ddaeraiqgh ggtltghvrl svpttyghyr lppllrqftq
      121 qhpevrveln ianrnvdlva egfdlairlg elpdsglvar kledaalclv aapeyvarag
      181 mpenvadlah hlclpfmlps sgriapwvfr dggqdidwlp psnvavsddv lgvvsmaqsg
      241 agicqtydfi vqdrvragsl vevlphlrgr srpfsviyap hrrlsaasra lidmivastg
      301 dq
//
LOCUS       WP_175798620             427 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia ambifaria].
ACCESSION   WP_175798620
VERSION     WP_175798620.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..427
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46746
     Region          22..419
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mlrlktelnl pdvcltgfet plseeeravq etlhrfarev lrpmgtaldk mtaeqavapg
       61 spfysvftef aklgvdpalf aslpaetalr mesmiaeelg wgdsglalsl gianfpmqla
      121 vtagkqelve lcagrigcwi gtqpdrgsdf qvfdierdwp qgtpgnqgnl wakvgddeiv
      181 ingqssawvs ngavaqvaia ymgadygdgr ldknglphgv gviipldlpg vsrgkpleki
      241 glralpqgei yfdnvrvpkr favalkdeyy gnfasvwsya gahtspifvg varaafemal
      301 qycherkqgg rllidhqltr yrlgdmlrri elaratarrs lafarlsert hpyvtaankv
      361 tvteeamkvv healqlfgav gttreypiek lfrdarpsli gdgesytvtm hlgllcqqly
      421 aegwsnp
//
LOCUS       WP_175798627             293 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein,
            partial [Burkholderia anthina].
ACCESSION   WP_175798627
VERSION     WP_175798627.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         <1..293
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
     Region          1..293
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 tlntvaaaak iggdihvlva ghnaqgaada aakiagvgkv lladapqlas glaenveatv
       61 ltiaanyshi fvpataygkn iapriaakld vaqiseitav vsadtferpi yagnaiatvq
      121 ssdpikvitv ratgfdpvaa eggsasveki eaaadagksh fvsrevtkld rpeltsakii
      181 vsggrglgsg enytkvlepl adklsaalga sraavdagyv pndyqvgqtg kivapqlyia
      241 vgisgaiqhl agmkdskviv ainkdeeapi fsvadyglvg dlfvelpgiv aal
//
LOCUS       WP_175798674             247 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175798674
VERSION     WP_175798674.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..247
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25716
     Region          8..237
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mtqqsdadrp valvtgasrg igravargla adgytvalva rtpvaletva adiaaagaap
       61 piahaldvgd eaavadavra vhartgridv lfngagivrr gtaalsdada rvlldtnllg
      121 alnviravap fmrrsrsghi vnvasrsall pkagnggyaa skaalraygd alyqelardg
      181 vkvttlcpsy vhteqsarqt wlsdddkipa ddvyrtvryl lslsraasvr eltiectyvv
      241 ahgeqyv
//
LOCUS       WP_175798717             833 aa            linear   BCT 11-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Burkholderia ambifaria].
ACCESSION   WP_175798717
VERSION     WP_175798717.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18415115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..833
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=89090
     Region          4..32
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          31..274
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          38..66
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          71..99
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(72,75..76,79..80,82,106,109..110,113..114,116..117,
                     140,143..144,147..148,151)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          104..134
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          139..167
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          173..826
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          173..201
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          207..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          274..302
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(275,278..279,282..283,285,309,312..313,316..317,
                     319..320,343,346..347,350..351,354)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          307..337
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          342..370
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          376..404
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mesielqlra alahheagrl geakalydei lhaqpgqpda mhflgllacq lkqydaglal
       61 merslaarpd asyfnnlgnm lrecgrldda iahyrraval rpdypeahnn lgnalrdard
      121 paeamqscsr aielrpgyae aynnlgnvlq dlgelnaaaa sygkaiafhp ayaeahsnlg
      181 nvlraqdrha daivhyrrai elspalpaac hglglslwal gelseavsvl gaaaagsgda
      241 slhnnyagvl rdvgdldaaa ahyaraiald aslavahanl sgvrrrqary aqalvhaqda
      301 iriapelada hnqagnahhg lgdlvaaqac yrtalelnpa dsgachnlsv vllkrerhae
      361 alaycrqala ggrptvsmyv nlgdilraqg nvdaavpayr dalalvrdda sddaaevlgr
      421 llfaaaasat vspadylnda rrygrhlaar strythdvre raadalhrpl ragfvsgdlr
      481 qhpvgifles vfahldctri apyvyttsde adaitarlkp haavwrsiag cdpqaaarti
      541 hddgidvlvd laghtqasgl aafgwkpapv qaswlgffas tgsdaidyfi gdartlpade
      601 ahhfveqpwr lpdsylcftp psddvavgpl pmaanghvtf gcfgklvklg ddvvrvwsrv
      661 ldalpgarll lkareleqaa vrdataarfa rhgidasrll fdgaspraey faaynridva
      721 lspfpypggt ttaealwmgv pvlgmkggrf vthicesllh aagmpdwiag deddyvakav
      781 aaaqdgarla alrttlrert lasplcdaar farnledafv gmwtryteta qta
//
LOCUS       WP_175798722             146 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Burkholderia anthina].
ACCESSION   WP_175798722
VERSION     WP_175798722.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..146
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=15869
     Region          44..146
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 msgihhghdl fdefarvqrq maslfgeppt giravrpgaf palnvgttdd aieivafapg
       61 msaadfdvsi dkdlltisge rkpaprdagd dvrsyaqerf hgtfrrvvel pqhadadnvs
      121 aryengclli rigrreaskp raitvq
//
LOCUS       WP_175798724             137 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Burkholderia anthina].
ACCESSION   WP_175798724
VERSION     WP_175798724.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..137
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=14984
     Region          33..135
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mntsqtlser qsgathaaaa tdaarrpait pavdivedkq rvtlradlpg vprenldvkv
       61 hdntltiead tridtpaelr vrhaevrapr yartfvlspd ldtsridanl rdgvltltia
      121 rreetrprri dvtagna
//
LOCUS       WP_175798748             385 aa            linear   BCT 11-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Burkholderia
            ambifaria].
ACCESSION   WP_175798748
VERSION     WP_175798748.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..385
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40881
     Region          17..298
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mstfsgdaqs adkhtvarks tlvsivlnvv latfqiavgv vahsqaliad gvhsisdlis
       61 dfvvlvanrh sgaspdadhn yghsryetva slflgailia vgigmlwrag nrlvnlenip
      121 avhfsaliva ltvlvskeal frymlrearr vrsamlvana wharsdaass lvvaigivgs
      181 lagvrlldpi aaaivgfmva rmgwtfgyda lqdlsdrald tsasaeiral lvatpgvrdv
      241 hdlrtrkmgd aalvdahilv dpmisvsegh yiaetararv lrdprvldal ihvdpendva
      301 rrpalalppr aeiatrleaa laqrglhpaa inlhylstgl eidvtldaga gdtdaalagr
      361 ldvdtlkrqf garrigftrg lpaqp
//
LOCUS       WP_175798750             265 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia ambifaria].
ACCESSION   WP_175798750
VERSION     WP_175798750.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..265
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=27225
     Region          47..197
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mnqsrvkqtl vrttllaalt aglamslqgc vlgvlgaaag ggaliatdrr tlgaqtedre
       61 iqvksltqin nglpdqshvn vtvfnrrvll tgevpndask qraeeivrgi nnvsaivnel
      121 svepasslss randsylegr vkseliatkg lsanyykvvs ergniyllgl vtvdegnrga
      181 daasqvpgve kvvkvfqyik pqdaqalqaa spsnasgaqa aaapadaatv gavpdasvqs
      241 aplqppapis nsssvhpgnp katpq
//
LOCUS       WP_175798767             232 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia ambifaria].
ACCESSION   WP_175798767
VERSION     WP_175798767.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 232)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..232
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25029
     Region          6..228
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mndaspplve ishvaksyrr gnqvvpvltd itldigegdf valmgpsgsg kstllnlvag
       61 idrpdsgelr vggldisrle eaqlaewraa nigfifqfyn lmpvltafen velplmltdl
      121 srrerrerve lvldmvnlgd rtshypsels ggqqqrvaia ralitdpvli vadeptgdld
      181 rasasdvltm lqrmnaelgk tiimvthdah aagaaqslvh lekgelidgh av
//
LOCUS       WP_175798823             288 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia anthina].
ACCESSION   WP_175798823
VERSION     WP_175798823.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..288
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30848
     Region          12..278
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mkkiqgvysa prghwvgdgf pvrsmfsyqs hgahlspfll ldyagpanfe pasaprgvgq
       61 hphrgfetvt ivydgevahr dstgaggtig pgdvqwmtag sgilheefhs eaftkrggpl
      121 emvqlwvnlp aadkmnapgy qtildadipv velpdgagra riiagefdgr rgparthtpi
      181 dvwdvrlaag grvrfpiaeg rtlavvvlsg tllvngetva reaqfvqlsr dgrdvelean
      241 gdvkllilsg epidepvvgy gpfvmnsqee irtaiddfns grfgqmpa
//
LOCUS       WP_175798851             241 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Burkholderia
            ambifaria].
ACCESSION   WP_175798851
VERSION     WP_175798851.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..241
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26467
     Region          1..239
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 misiknvskw ygqfqvltdc ttevnkgevv vvcgpsgsgk stliktvngl epfqqgailv
       61 ngqsvgdrkt nlsklrskvg mvfqhfelfp hlsitenltl aqikvlgrgk deandkgmkl
      121 ldrvglkaha hkfpgqlsgg qqqrvaiara lsmdpiamlf deptsaldpe minevldvmv
      181 elaqegmtmm vvthemgfak kvahrvifmd kgaiveddrk ddffsnprsd rakdflakil
      241 h
//
LOCUS       WP_175798877             255 aa            linear   BCT 11-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Burkholderia anthina].
ACCESSION   WP_175798877
VERSION     WP_175798877.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 255)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 255)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..255
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26747
     Region          21..247
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mekrplnpvp sapprrplne wldgardtip mmigaapfgv ifgtlvgggp laawhgalms
       61 lavfagsaqf ialgliagsa sfvvvlattl ivnlrhllys atlapyvahl plrwratlga
      121 lmtdevfava yahyrhfppg aigpyyffgs glamylnwqv wtlagigfga afpglqslgl
      181 dfamaatfia ivvpqlgtlr yfaaaatagt layfwqgwpy klgllgavaa gvtvgvaltl
      241 lharsrtgsr teaas
//
LOCUS       WP_175798875             300 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175798875
VERSION     WP_175798875.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 300)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 300)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..300
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32383
     Region          12..84
                     /region_name="QdoI"
                     /note="Cupin domain protein related to quercetin
                     dioxygenase [General function prediction only]; COG1917"
                     /db_xref="CDD:441521"
     Region          52..300
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msatrlpdsa rywrtpllpd adlltatyrd htfaphwhda ytipvilega erytcrgsgh
       61 vaetgtvpvi npgevhtgsr atdegwcyrv syvpidyira lasaiagrpq dapwfpsgvi
      121 rdpdlaarlv lahrmmeags epmppsglhg paaadapapg tprvydplaa etamldalst
      181 liarhadarl qpavlaadep rvdamrerla adltcavtld dvaqaaglss fhaarlftrt
      241 tgmpphawrn qlrlqralap lragvpvadv aaasgfvdqs hftrhfkrmf gvppgrwqar
//
LOCUS       WP_175798928             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia anthina].
ACCESSION   WP_175798928
VERSION     WP_175798928.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22166
     Region          4..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mpalptliaf glvslgmvlt pgpnmiylis rsicqgrrag lvslggvalg fvfymfcaaf
       61 gitalvltvp yaydalrfcg alyllylawn alkpggrsaf qvrqlphdsg aklfamgfvt
      121 nlanpkiavm ylsllpqfis pghgsvltqs valgcvqiav sicvnaliac magaiaefla
      181 grpvwaraqr wlmgtvlagl avrialesrr
//
LOCUS       WP_175798945             397 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Burkholderia anthina].
ACCESSION   WP_175798945
VERSION     WP_175798945.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..397
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44306
     Region          48..393
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mtspvpsdaa lrplpidtlt vpaaldgrtg tnrstsahpq iaathdldav rawlarfvdt
       61 pttfqnyrke aerlllwavi acgkplsslt hedlvvyrqf llapapadvw canggrkhpr
      121 gdprwrpfyg plsaasqrqa mvilnvmfsw lvqagylagn plalsrqrqr rpaprvtrhl
      181 gaplwqavkd aiaamprdda rasfhadrar wvftllylgg lriteaadat mghffarrda
      241 ngrerwwldv tgkggrqrlv pataemmael aryrrahglp aqpadgeltp lvlpvghtrk
      301 pltraalhri vkqvfrfaad rlraqgeage eqarvleqas ahwlrhsags hmadgrvdlr
      361 lvrdnlghvs ltttsqylha dddwrhsete ekhridw
//
LOCUS       WP_175799008             249 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Burkholderia anthina].
ACCESSION   WP_175799008
VERSION     WP_175799008.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26143
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkalvavkrv vdanvkvgvk sdrtgvdian vkmsmnpfde iaveeavrlk eagvvtevva
       61 vsvgvaqaqe tlrtalaiga drailveand gveplgvakv lkalvdkeqp qlvilgkqai
      121 dddsnqtgqm laalaglpqa tfaskvtiad gkatvarevd ggaetlsltl pavvttdlrl
      181 nepryvtlpn imkakkkple ivkpdalgvd vtprlkvlev neppkraagv kvpdvktlve
      241 klkteakvl
//
LOCUS       WP_175799045             297 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia ambifaria].
ACCESSION   WP_175799045
VERSION     WP_175799045.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..297
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32128
     Region          3..293
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mndviiiggs faglaaalql grarrkvtvl dtgrprnrfa ghshgllghd hkppldilve
       61 arqqlarypm irlvdaraes msgaiddfcv vtddneslra rrlilsygva dqmpdvpgfa
      121 eswgtsivpc pycdgfevag qhwglvwsgp qshqsvrlfr dwtdkltvfa dghdiapdiq
      181 adlarrnipv vdgriveiah hqgrittvnl dtrrnvavdv lfahprnkps anlheslgla
      241 tvdtpvgial kvderrqtsm pgiyaagdla tpllpsvtqa ssqgamagif aqqsmlv
//
LOCUS       WP_175799046             215 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            ambifaria].
ACCESSION   WP_175799046
VERSION     WP_175799046.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..215
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23354
     Region          11..172
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtensqgrrg rpanealrqt ivdaacelfv elgfqattmd kvaqrakisk lsiyrhfenk
       61 ealfsaamaa hchqfapqal fegvdgsaed qlmavgssll rtllspdvrs veamvladkt
      121 nqkslsklhy eagpahviaq ieavlrqlha kailnvpdal rsarlfaalf kgsdllliar
      181 fdaararddn eiesycrsav amfiaahgrs dhahg
//
LOCUS       WP_175799122             376 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia ambifaria].
ACCESSION   WP_175799122
VERSION     WP_175799122.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..376
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=38723
     Region          17..376
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mnhpngradr lavpratlia alltcaslpa laqssvtlyg ridtaieyan agpnhvtrmg
       61 sgnlwasqwg lkgvedlggg yaaifkledg fnaasgalsn ssalfgreaw vgitgpfggv
      121 qfgelytilh ttlvtyslpg lgaglawgna tnnfvgpafl rvrnsmryts pryagfllra
      181 maargtngaa gqpatlgdty gaglnyargg lsvdvdymqq kfspvaasal gatspaangn
      241 ytlgaisydf nvvkiaalyl rhrggpdvaa aidsqsayph sdtmelsatv pigrasllls
      301 ighyrkvads dgnadsygir fdyplskrtv lytgaamvrn gaharfivng aagggvavak
      361 pgatassiva giltsf
//
LOCUS       WP_175799128             368 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD/NADP-dependent octopine/nopaline dehydrogenase family protein
            [Burkholderia ambifaria].
ACCESSION   WP_175799128
VERSION     WP_175799128.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13367875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..368
                     /product="NAD/NADP-dependent octopine/nopaline
                     dehydrogenase family protein"
                     /calculated_mol_wt=39346
     Region          1..>107
                     /region_name="GpsA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0240"
                     /db_xref="CDD:440010"
     Region          187..334
                     /region_name="Octopine_DH"
                     /note="NAD/NADP octopine/nopaline dehydrogenase,
                     alpha-helical domain; pfam02317"
                     /db_xref="CDD:426715"
ORIGIN      
        1 mkvcvlgggh gchaaaidlf ekghdvtwwr rdrepharlr elgalhvtdy rgeravplgd
       61 tpgairltdd laaalrgarl vvvplpavsh dalaaqvapl ledgqvvflp pgtfgsfvfa
      121 raaadagnra rvayaetgtl pylvrkhgdn avvisayatr lptgvfpana agwafdvlra
      181 gypsvepved alsgalmnag pvihpplilm nagplehfda wdihnegtqp sirrvtnald
      241 aeriavreal gyraphfpla dhyatdgdew mygrgahgkl tdsgdwreki dlrthrymle
      301 dtrlglsfiv scgrwanvpt pvaqgllsva savtgrdlya qgrtldglgl aalsrdalra
      361 lldagyaa
//
LOCUS       WP_175799135             326 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia ambifaria].
ACCESSION   WP_175799135
VERSION     WP_175799135.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 326)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..326
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34681
     Region          38..316
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mgqptrplpa dgataglapp vatgdavtpr aaggrvprat wrahaplwlm capafalfaa
       61 lvlvplamtf altfyrfdpa tgpiaafqfg hyaevlgssy fhtifartfg iaalttaici
      121 aigtpeayvl skmrdpwrsl fllvilapll vsvvvrafgw smllntsglv nqalglaglg
      181 pykleyttfa ivialvhvml pfmvipvwta lqrldpqteh aalslgaspf ttlrrivvpq
      241 lmpgvlsgsl mvfglsasaf aipgllggrr lkvaatavyd eflgslnwpl gatiavlllv
      301 anlvvmltyy rvlerrytrs lggasr
//
LOCUS       WP_175799140             285 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia
            ambifaria].
ACCESSION   WP_175799140
VERSION     WP_175799140.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..285
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31378
     Region          9..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          105..270
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 madasdnllg aylrdrrekl dpaalglpva rrrtpglrre evaqrahvsa awytwleqgr
       61 ggapsadvle rlarallltd aerehlflig lghppevryh asrdvtprlq hvldsldasp
      121 ailrtatwdv vawndaaaat ltdyamlppp arnilrlifi daavryaqpn wervarfavg
      181 afradiarsg atqavqafvd emrttsaefd amwrshdihs hdegtkeirh pqagrialey
      241 safsvtgrpd lslvvftpat padrariral vaareqardp hapaa
//
LOCUS       WP_175799159             240 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD family hydrolase [Burkholderia ambifaria].
ACCESSION   WP_175799159
VERSION     WP_175799159.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..240
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25948
     Region          6..233
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mhltnvsais fdlddtlwpf gpsveraeas lhawllahap etarvlptsq alnqlrdeye
       61 rlrpdlvgay ralrigsirl aleranedvt ltehaydvfy sarnqveffd dalpalawls
      121 arfpliavtn gnadlrltgg geffrdtlsa rafgfakpep eifhaaaatl gvpagellhv
      181 gddyhldvvg alnaglqaaw vvrdegaeta haahrappph ltirdlsmlc ralgapvgls
//
LOCUS       WP_175799161             506 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Burkholderia anthina].
ACCESSION   WP_175799161
VERSION     WP_175799161.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..506
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53751
     Region          13..490
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(70,72,76,79,83,116,119..120,129..136,141,144,147,
                     240,244,247,250,252,426,428..429,431..432,435,438..439,
                     441,443..446,455,459,461,475,482..487,489..490)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(156..159,167,182,185,215,232..235,238,256..258,290,
                     391,393,419)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(159,256,287,290)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mttvpaftss ddvghyinga rvsgasggfq dvfnpaagkp arrvaladdn evaqavaaaq
       61 aafpawsetp pirrarvmhr flqlmnehrd tlaaiitaeh gkvfsdaqge vargidiief
      121 aagvpqllkg dftdqvstgi dnwtmrqplg vvagitpfnf pcmvpcwmfp valatgntfv
      181 lkpserdpsa alfiadllte aglpkgvfnv vqggknavda lidhpdvqav sfvgstpiah
      241 yvhqrasqng kraqalggak nhmvvmpdan idqavdglig aaygsagerc maisvavlvg
      301 digdrivakl aeraqtlvig dgmspevemg pivtgealkr iegyidigvq egaklvvdgr
      361 glkvpgheqg fftggtlfdn vttdmriyke eifgpvlacv rvkdfaeavn linahefgng
      421 vacytsdggi arefarriqv gmvginvpip vpmawhgfgg wkkslfgdmh aygeegvrfy
      481 tkqksimqrw sssigkgaef amptak
//
LOCUS       WP_175799167             266 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Burkholderia
            anthina].
ACCESSION   WP_175799167
VERSION     WP_175799167.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..266
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28614
     Region          27..260
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mtdthdseri hhagttpils yhgkdraelt lnrpafhnrl epgdlatlre hiamlnddra
       61 vrvvmltgag trtfssgyhl gafdaartdd dtafeqvana iegmravtia rvngavygga
      121 sdlalacdfr vgthdtrmsv paarlglhfy gsgirrwvsr vgvnatkraf laaqtfssqe
      181 lvacgfltqa veateldaec talidrlcal aplavqgmkr iinaaahaey deraareqcl
      241 dsmrskdfae glaalaakrp pvftge
//
LOCUS       WP_175799245             311 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia anthina].
ACCESSION   WP_175799245
VERSION     WP_175799245.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..311
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=32866
     Region          12..155
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          168..307
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mqstqsvppl arialavdpt peslsaaryv stllrpgmrv rivcaidnpr lvlpdiprid
       61 alltsaredm vreaqtvlar taalfagtgv eleqaiidts vtggtvanal andtstwqad
      121 vlvvganphh gllrlvegam sdtlatrarc allivpadya rpsdgplqrl mfavdgseps
      181 lhavhvglgf aapttllyaa yvvdravrlt divpvraled ayraegedal arigpvlhat
      241 gnptkrgive trppsddvah almrdavhwh aellvvgthg rrgiaawlig svarrvahla
      301 qvpvllvrga a
//
LOCUS       WP_175799270             472 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia anthina].
ACCESSION   WP_175799270
VERSION     WP_175799270.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..472
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=50766
     Region          83..470
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mtarpaypsp dasgaaaprs psralrraal algaavlgyg afaiafpart paaigdvvad
       61 wtganphpvv lqrpaaqpls avaqlgralf vdpslsasgk qscaschspd haygppngld
      121 vqpgglamtq qgyrpppslm ylyrqpnfsi gpdagendaa psvaqqasaa agvvkaqkva
      181 gtsaapqlvp qggmfwdgra dtlqqqafgp llnpvemana siddvahkla qsshraqfeq
      241 lfgprvfdsp qlavseamfa iaryqvedps fhpynskydr wlegrarltq aelhglrlfn
      301 dpdkancagc hlskpgkdgl ppmftdyqye algaprnrql aqnrnpafyd lgvcgpfred
      361 lkdqtqycam fltptlrnaa trhvffhngv fhtldqvmaf ynersispqk fysrgadgkv
      421 deyddipaky ranvdvtdap fdrkpgdkpa mtaqdikdie aflgtltdep ah
//
LOCUS       WP_175799249             291 aa            linear   BCT 11-JAN-2025
DEFINITION  PilZ domain-containing protein [Burkholderia anthina].
ACCESSION   WP_175799249
VERSION     WP_175799249.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..291
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30424
     Region          173..278
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mrlitdhvtl arddfsagvp lgfdlydasg aallpagttl rdpaqhaflf dhfrpvrkrd
       61 gtehgpctpd tapaatrmgl sagaaigirr rvgttrvlqr crligvgasg vlfvepqsat
      121 vldfaqgddv eavaigrsav srfgatvesv qlsgaapfmv lsrpgfvdrl rtraeprvpv
      181 riaaccsggp agmesigivr dlslsglsia vdrpiaatge plhvqlpcrv adrvelltla
      241 gtvravhadp aapawtlhha afdetaetdr irlkallfdl stglgdadpa s
//
LOCUS       WP_175799284             445 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia ambifaria].
ACCESSION   WP_175799284
VERSION     WP_175799284.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..445
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45523
     Region          1..416
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdlaltdeqa mirdaaadvl aarsasadvr rameqsagrd dalwaalage lgwnalalpe
       61 aaggmglgav eqtllmeqlg rrvacvpyfs taclaatala gcdtplatgw lakiaegacs
      121 atlalpfdwp fgepsgawgg rpyggpdana cgasfgdsfd epvsarplpf iaeetaagfa
      181 lsgvaahvld garadlllvp arianegrsv glfaidmtvg aagaavtpld tldatrplar
      241 vtlddirvsr dallagrdaa qvlertawfa alalaaeqlg gaqqcldltv dytsqrvqfg
      301 raiasfqavk hrcaqmmvli esarsavlga ahawdaedgi apgaalradi aaakaaanda
      361 aafcaqeaiq lhggvgftwe ydphlyfkra qasgaqfgtt pqllewiarh aidggaahrd
      421 dapaaavapv aaaarpsaar agalq
//
LOCUS       WP_175799341             232 aa            linear   BCT 11-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Burkholderia
            anthina].
ACCESSION   WP_175799341
VERSION     WP_175799341.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..232
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24730
     Region          23..228
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 msayvidape rpsveveqss arfpvrrvfc vgrnyadhar emgadpdrep pffftkpada
       61 ivpasgtvpy ppltsdlhhe ielvvaigkd grsidpadal shvwgygvgv dltrrdlqae
      121 akklsrpwdw akgfdasgpv talrpatatg hpasgriwld vngetrqqgd ladmiwavpd
      181 viayvsrsve lkagdliftg tpagvgalqp gdrvtggvdg vasfefvvda kp
//
LOCUS       WP_175799369             357 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia ambifaria].
ACCESSION   WP_175799369
VERSION     WP_175799369.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..357
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=37358
     Region          29..357
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mtlrtprarf ragflmagaa gaigiaplah aqssvtlygv adafvgsvkq pggrttlvqs
       61 gggmttsfwg lggsedlgng nkaffvlesy fqpqsgaygr yagdslfsrn ayaglqtrfg
      121 qlrlgrittp lylatiqfnp lfnsytfspm ifhtfkgvga egvvgdsawn nalaytsptf
      181 ggfnagllya lgntagrnga kkwsvnanya rgafaaavvf qyvnfsatpg dldgalaaap
      241 glssqrtvqv galydwrvvk lfaqymnvan raqrgnfhgd tlqagvsvpi gvgsllasya
      301 ythssgalad gahrstgalg ydyllskrtd lysaikvdhv gglstgityg aglrtrf
//
LOCUS       WP_175799415             248 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia ambifaria].
ACCESSION   WP_175799415
VERSION     WP_175799415.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..248
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=26746
     Region          3..231
                     /region_name="ArtM"
                     /note="ABC-type arginine/histidine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4160"
                     /db_xref="CDD:443325"
ORIGIN      
        1 msfdfdfllg tlgqllaavp ttlglffasl vlggllslvi vtmrvsphwl pnrfartyil
       61 vfrgsplliq mflvyyglgq fgviresfvw pllrepyvca vlslalctag ytaeilrggl
      121 mavpvgqiea gysiglsgfa llrrvigpia lrqclpayst eavllvksta laslvtvwev
      181 tgvaqqiiqq tyrttevfvc aaliylglnf ivvrllgale wrlsghlrap kpsgasaaaa
      241 rnprrvas
//
LOCUS       WP_175799512             415 aa            linear   BCT 11-JAN-2025
DEFINITION  lactonase family protein [Burkholderia anthina].
ACCESSION   WP_175799512
VERSION     WP_175799512.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..415
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44267
     Region          52..411
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 mpnrlrerda rastrgfplr lahwmkgfai vlslsathaf aqqspapadg vynllvgtyt
       61 ghgsdgiyvy rfdtqtgsva pvssaktvnp syllpsrdgr tvyavnelpg dngpanergg
      121 vsafsfdakt galtfidrvs segndpcyla lspdgkylvt anysvaadpg gsfavfpird
      181 ggavgqavlt vhhegsgpvk grqdgahvhs tvfspdghyl fvqdlgtdki ygyrytvdgs
      241 rglisptdtr ytpvkagtgp rhmvfsadgr fayvtselsa svevfgyhdg kltpveilpm
      301 tvpgfkgkvg ggaihlspdg rflyvsnrgd vndiviyavn kadgrlktvg rqsslgktpr
      361 eflidptgkw livgnqdsdt fyvfrrdvet gqlgpnpqkv algspvdfkl vpvaq
//
LOCUS       WP_175799546             436 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Burkholderia anthina].
ACCESSION   WP_175799546
VERSION     WP_175799546.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 436)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 436)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 436)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 436)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..436
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48628
     Region          4..312
                     /region_name="COG3950"
                     /note="Predicted ATP-binding protein involved in virulence
                     [General function prediction only]"
                     /db_xref="CDD:443150"
ORIGIN      
        1 malylsklqf snirgfknfe lsfenprkyr qwtifigdng hgkttilrai avglgdeats
       61 sellallpgq firinkkgiy spssqiivtl rdseskkhid iitelkldeh ggvsvnktvs
      121 daafqwndvf vcgygsnrgt ggrmhsqyal rnslltlfnd ragllepesv lrdfalmaaq
      181 kkkgtddplk emknclwklw dlnpnhaldi saeqvvihgp wggmpfhalg dgyrgtgswl
      241 ldlmgncvks grwitpqkla givlldemde hlhprwqkal vptlrrllpn vqfiatthsp
      301 laivntlpge lfatrlhnsv aelipdalps pdgrganell lgewfglast ldttseillk
      361 ryrnafqknd kallkqlepk lrqriksflp sqldnkaqad lderrrgavd iltpaqeekl
      421 vasaarkrla tlkekk
//
LOCUS       WP_175799579            1082 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia anthina].
ACCESSION   WP_175799579
VERSION     WP_175799579.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..1082
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115726
     Region          3..1060
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mlkivrlalt rpytfivlal lilligplaa lrtptdifpd iripvisviw nysglqpddm
       61 sgrivtyyer tlgttvndiq hiesqsfrgy givkiffqpt vdirtataqv tsisqtvlkq
      121 mppgvtppqi lnynastvpv lqialtsdtl deqkledyae nfirpqllsv pgvaiptpyg
      181 gktrevqidl dpqalqarkl saqdvanala qqnqiipagt qkigrfeyni klnnsptaid
      241 alnalpiksv dgtliymrdv ahvrdgyppq pnivrvdghr avlmsilkng sastlaiisg
      301 vksklplieq tlppglklvt mgdqstfvtg avsgvaregi iaaaltsami llflgswrst
      361 liiaasipla vlaaiaglaa lgetlnvmtl gglalavgil vddatvtien inwhleqgke
      421 vrhaimdgaa qivmpafvsl lcicivfvpm lqldgiarfl fvpmaeavif amiasfilsr
      481 tfvpmmaqyl lkphasggha sgelaavmat thgahahqpp shnplvrlqr gferrferir
      541 aryrivlgla lthrkrfiag flvavaasfl lvpwlgrnff pdidagqiti hvrtpvgtri
      601 edtadefdhi enavrgvipp kqlanivdni glphsginlt ynnsgtigpe dgdimvslga
      661 dhaptasyvr rlrevlpraf pgttfsflpa divsqilnfg spapidiqia gpdqaanhry
      721 atellrqvrl vagvadariq qattypqfti nvdrsradel gitehdvtns vvaslsgtgq
      781 vsptfwlnpn ngvsypivaq tpqyrmtsls dlknlpvtga ngnsqvlgai atiqrgvgda
      841 ivshynikpl fdiyattqgq dlgavasrid aivhatahdv pkgsvvtvrg qvqtmnsafs
      901 elllgllgav aliyllivvn fhswsdafvi vtalpaalag ivwmlfttht plsvpaltga
      961 ilcmgvatan silvvsfard rlaatgdalv aameagftrf rpvlmtalam iigmapmalg
     1021 lgdggeqnap lgraviggll catfatllfv pvvfslvhrr dalrppaard lsssesgvth
     1081 vn
//
LOCUS       WP_175799590             379 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia anthina].
ACCESSION   WP_175799590
VERSION     WP_175799590.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..379
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40997
     Region          15..312
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mtanqpapak lpgqvvlvlq gggalgayql gvyealdaag iqpdwvigts igainaalia
       61 gnapghrarr maefwrrvte rpafnvpgfp tswdkigael gvigaglpgf frpnpaawlg
      121 plahvgveha syyvvdplra mlaslvdfdr lnagqprvtv gavnactgam ryfdsrdrpl
      181 giehvmssga lppafpavri dgapywdggl ysntpvevvl ddaprrssii fsvqmwnpvg
      241 peptsiwqvs erqkdiqyas rtdttiarqq qihrlrhvik elvmhvpeae rtsadveala
      301 aygcqttmrv iklaaprldg ddqwkdidft pdgiaarrqa gfdatmqtia arpwdlpmdp
      361 teglsvwspe enrvgeqhg
//
LOCUS       WP_175799619             449 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia ambifaria].
ACCESSION   WP_175799619
VERSION     WP_175799619.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..449
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=48370
     Region          76..440
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mhtllkpvas arslisaaat ltliagfaal agcdarpaan apavpvvpaa qaapaapava
       61 pasqpqtraq vfegvkqmta lgkqlffdps lsgsgklaca schsaehafg ppnalsvqlg
      121 gddmhrtgfr avpslkylrg ippfsehfhd spdegdesid agptggltwd grvdtrdaqa
      181 ripltspfem sssparvaka vraapyadaf rhtfgdrvla ddqatfgavl raldafqqqp
      241 alfdpytsky daylaghaql tpaelhglql fndekkgnca schvsqrtle ggppqfsdfg
      301 liaiavprnr alpvnrdprf hdlgacgper tdlkgrdefc glfrtpslrn valrktffhn
      361 gvyhsledvm rfyverdihp ekfypvvhgk vqiyddlpkr ywpninrepp fdrkrgdppa
      421 lnaaeikdvi aflntltdgy qpaaasaar
//
LOCUS       WP_175799629             408 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            ambifaria].
ACCESSION   WP_175799629
VERSION     WP_175799629.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 408)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..408
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41438
     Region          32..313
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mgsrvpagal rwvlfaacva lpawlwphga mlgylaqtaa lvvlalsynl qlgttgllsf
       61 ghaafaglga faaahwfnrv ggplpllplv ggvagagfgf iagllatrra gtvfamitlg
      121 laecvaaaaw svpawfgglg gvpidrasgt pwggwhfgap aqayaviaaw civsalamra
      181 ltrtplarla navrdnparv aalgteprrv rlamvtsasf fagiagtltl idveiatpds
      241 lsmarsatvl iaaviggtgt ffgpaagavv ltalsvvvag vsrawalylg vlfvavvvaa
      301 pggiagvaqt lahalrrdap aaerwrvlcg vgacmfwgva ivcaaelgya wrfaqddgag
      361 talgawaida dapagwvvac saagigmllw gwrarlmhpg hgkredgr
//
LOCUS       WP_175799645             506 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Burkholderia ambifaria].
ACCESSION   WP_175799645
VERSION     WP_175799645.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..506
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53927
     Region          13..490
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(70,72,76,79,83,116,119..120,129..136,141,144,147,
                     240,244,247,250,252,426,428..429,431..432,435,438..439,
                     441,443..446,455,459,461,475,482..487,489..490)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(156..159,167,182,185,215,232..235,238,256..258,290,
                     391,393,419)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(159,256,287,290)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnpvpaytsd advghyldga pvagrsgrfq dvlnpalgra vrrvaladgd evqravasah
       61 aafpawaetp pirrarvlhr flqlmnehrd tlaaiitaeh gkvfsdaqge vargidiief
      121 acgvpqllkg dftdqvstgi dnwtmrqplg vvagitpfnf pcmvpcwmfp valatgntfv
      181 lkpserdpsa alfiadlltq aglpagvfnv vqgdkgavda lldhpdvqav sfvgstpiaa
      241 yvqqravqsg krvqalggak nhlvvmpdan ieqavdalig aaygsagerc maisiavlvg
      301 dvadrivpav aerarklvvg dgmqpevemg pivtgealkr iegyieqgvs egaqlvvdgr
      361 glrvpgreeg fftggtlfdh vtpdmriyke eifgpvlgcv rvkdfgeavd linahefgng
      421 vacftsdggi arefarriqv gmvginvpip vpmawhgfgg wkkslfgdmh aygeegvrfy
      481 trqksvmqrw sssigkgaef amptak
//
LOCUS       WP_175799664             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175799664
VERSION     WP_175799664.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34261
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdtlqnmrvf vrvvdagsft aaaqqmnstt ayasravsdl eahlrtrlln rttrrialte
       61 agerylqrce qilayvdqae aeagdaharp sgklkvhcft slgqhylvpa iaryrqrypd
      121 vhveltlaqr mpdlldegyd vaivvgrdlp dsglvsqrlg esysvvcasp gyvdahgaph
      181 tpadleqhic lgmvapgfhf dewalsgphg devipitapp frvnvaeala vavregmgig
      241 glplysaigg lrsgnivrvm seyrshvmni yalypsrqyl dakirtwvdf lrdelpatle
      301 adeaalaqfr aat
//
LOCUS       WP_175799718             548 aa            linear   BCT 11-JAN-2025
DEFINITION  NRAMP family divalent metal transporter [Burkholderia anthina].
ACCESSION   WP_175799718
VERSION     WP_175799718.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..548
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=59015
     Region          48..452
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 mstpsnvspp iaaersavld eahlgdirga lgtiahhdta argtwwarlr tllaiigpgl
       61 ivmvgdndag afgtytqagq nygttllwtl lllvpvlyvn qemvlrlgav tgvgharlif
      121 erfgkfwgaf svidlfllna ltivtefigi tfvldffglp kvagvcvaaa ltmaavstgd
      181 frrferfaiv lclmslllvp vlvtihppva qmsrdffvpn wpahaklsdv mllvigivgt
      241 tvapwqlffq qsyvidkrit prfmkyekad lwigiafvlv gavamiafsa qlfaghpefg
      301 nftdaggiia glekyaghts atlfaialld aciigaaavs lstayaigdv fkirhslhrg
      361 vsdakgfylv yfgivaaaaa lvlipgsplg llteavqtla gvllpsatvf llllcndkqv
      421 lgpwinstrl niftgaviwv lvmlsiilta svmypdisge aildvlvggs vfaivgylvt
      481 vlirrhkrvv epgvdralrd twrmppldtl epqkmtlstr vwmtvlrgyl viavglvivk
      541 vvqmmllk
//
LOCUS       WP_175799724             656 aa            linear   BCT 11-JAN-2025
DEFINITION  beta-galactosidase [Burkholderia ambifaria].
ACCESSION   WP_175799724
VERSION     WP_175799724.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 656)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..656
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73173
     Region          1..615
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
     Region          607..654
                     /region_name="Glyco_hydro_42C"
                     /note="Beta-galactosidase C-terminal domain; pfam08533"
                     /db_xref="CDD:400716"
ORIGIN      
        1 mhlgvcyype hwpreqward arrmaelglt rvriaefaws rmepepgryd wawldeaidt
       61 lasrqlkvvl gtptasppkw lvdrhpeilp vgadgavwqf gsrrhydias pvyrehcvri
      121 adamarryga hpaviawqtd nelgchntlp sytraaldgf rawlavrygd igalnrawgn
      181 vfwsmeyrgf deielprhtp tdanpahlld frryqsdeva rfhavqvdai rphapgrdvl
      241 hnfmgffaef dhyafarggl diaawdsypv prtevlplde adkrrwartg hpdvsafshd
      301 lyrgvgngrm wvmeqqagpv nwgpynpvph agavrlwtwe afahgaelvs yfrwrqypha
      361 qeqlhsglna pddqlspggr evarvarela aldpalvaga reparvallf dytadwmiri
      421 qphgagfdyq qhvfdwyral relgldvdiv aadaevsrya lvvaptlpvv pdrvveqaar
      481 gnahwlfgpr tgsrtadfai vpglapgklr dvlpvriaqv eslrpslapr vafdgvdgha
      541 lkwrdhidld astpvdvlaa cddgvpalvr hghvtmatac fdpallraiv grcardaglp
      601 vralpdgvrl crrgrvvfaf nygdtpctlp apdgarfvlg grelgavdva awvepd
//
LOCUS       WP_175799750             395 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia
            ambifaria].
ACCESSION   WP_175799750
VERSION     WP_175799750.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..395
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43092
     Region          224..390
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mrialapddt aaddgfddaa wtarelsawl glvyqgpset tpwadfleam rvrldasftt
       61 lvlrnpggsr rgliinasah gpllpgepsy seqfyalcpf ldqppgqvft adalfgaarw
      121 cahdfyrqyl qpldlrfilg anlrgdggve caffvsrahh grdfdaaera qvatllphlq
      181 ravelhaald lldaeralya gavdrldvgt aildedgrvi khnriaerli eqqdglclrq
      241 arlhascpld errlqkalqa tlehfragal grieattlsr pggamplnvl lrplapyhga
      301 qdrqhrpava vfvrdpassp htsrdmlhrl frltpmetei alllvdgltl deaaaatgit
      361 kntarahlrg ifaktgatrq avlvktllns vvsma
//
LOCUS       WP_175799756             835 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175799756
VERSION     WP_175799756.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..835
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=90718
     Region          16..789
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msgevllkvl rggyaqfdri vkldtplgdd wltplyvkin arlgrnfevt vdassvmgdk
       61 iklsalmlqp vtlwirqtdg gylpihgyvq rarrlgndgt vsyfqlqfss wlsflklssd
      121 rrdwqeasgw qiladvfdkh pqasgnygqe lraamrsysh rvqwetdwnf vhrsleevgv
      181 fprfdfakdg kshkvvmmdd lyfgpslpns emkfshagtd edfdgltqls eqqdaqsatl
      241 tlgtadykrp dldkqvsmpa adledlpgqg edylytgsqt waesdigqqq arirteewas
      301 rakryfaigs pryalpgywf kvsghpvlda lpeeerelsi iasdwliqnn lpgldaltrf
      361 prslrseieh vqaagtgatv shrdggvgff hveieaqrrk tpfrspfehe kpemhlqtai
      421 vvtdsdeeia tddgnrvrvr tsnsrndrnt kstswiraam pdagakrggy fplrkddqvl
      481 lgfvngdcdr pviisrlhgg atmpvwhthg llsgfrsrey ggdgfnqlvm ddssgqnrvh
      541 lysssysshl hlgylieqsd ntrgsflgng fdlksgayga vraeqglyvs tqpataqpln
      601 vtaateplag aeavletask asetnraesl qdgqaalksf tdatqrtvag stsggrtagg
      661 gtgnangfsk pvmllsspeg iaastqqsvh vtanqhtnmv agknvnlaag ksllasvldk
      721 islfaqnlgi kifaakgpvd iqaqsgpasl vglqdvkies adgrliltaa kevwigaggs
      781 yisikgglie nvttgqilek caswdkpsga sgtirdplqa tpvstdggrg slfsg
//
LOCUS       WP_175799793             396 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175799793
VERSION     WP_175799793.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..396
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41310
     Region          11..376
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mstsetsgsr rdpvvivgtg lagyttarew rklddetplv misrddgsfy skpalsnala
       61 qrktpdqlam sdartmagql ratilthsav rqiraathei vlddarvqry ralvlatgad
      121 arrvhcegdg aadilsindl gdytrfrdgl rdcrsvallg agligcefan dlvaaglsvt
      181 vidpadapls rllppeagdv fgralrdagi qlrlgagvqs iarlargyrl altsgehvea
      241 dlvvsaiglv prialareag ldvadgivtd awcrtsvpdi falgdcaaie grvrpyvlpi
      301 mhaaralaqc lrgtptpvaf pvmpivvktp aipavvvaad gggrwttdvg vgnapratra
      361 lyadagsgri tgfalldaat sekaallktm agdaas
//
LOCUS       WP_175799892             345 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia anthina].
ACCESSION   WP_175799892
VERSION     WP_175799892.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..345
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35788
     Region          16..345
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msndthpvpp latgdtpaaa pglrarffnp aarqkllafa slvllivffs iassnfldvd
       61 nlvsilqata vngvlavact yviitsgidl svgtlmtfca vmagvvltnw gmplplgila
      121 alffgalsgs vsgfviakmk vppfiatlgm mmllkglslv isgtrpiyfn dtpgftsiaq
      181 dslignlips lpipnavlil flvaigasiv lnrtifgryt falgsneeal rlsgvnvdaw
      241 kiavytfsga vcgiagllia srlnsaqpal gqgyeldaia avviggtsls ggagsivgti
      301 igafimsvlt nglrimsvaq ewqtvvtgvi iilavyvdil rrrrr
//
LOCUS       WP_175799927             205 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175799927
VERSION     WP_175799927.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22503
     Region          15..179
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnsnptssgs rdrgrprefd tdevieaaar vfweqgyyat sidtlcdatg vfrgslyrtf
       61 gdkhgllvaa fdryaegaia rlkerlaadl pprealreal mhytrvgarl serrgcfitn
      121 aaiellpgdd alrphiestl lriamqlsla vargqqsghf drhldpegvg rfllcliqgm
      181 rvlgkssate aelvsivdia mrali
//
LOCUS       WP_175799947              98 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia anthina].
ACCESSION   WP_175799947
VERSION     WP_175799947.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 98)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002085
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..98
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10323
     Region          1..98
                     /region_name="ManC"
                     /note="Mannose-6-phosphate isomerase, cupin superfamily
                     [Carbohydrate transport and metabolism]; COG0662"
                     /db_xref="CDD:440426"
ORIGIN      
        1 mslvdfksva aaqavawkst ivgevgpari kvlrmdaqpy eaevhdyneg llvldgrlml
       61 evdaqtivve agqmylalag thhavlpgsh gtlaiidv
//
LOCUS       WP_175799969             392 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia anthina].
ACCESSION   WP_175799969
VERSION     WP_175799969.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 392)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..392
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39995
     Region          168..370
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mtdraavsar rvtldkvgil igvltivavf glpfmvlrpn riaagtglsv faalpamqgt
       61 alaalwvvga lwamtasrpe wrlaagcawl atlayalgag athvvapddm larvspaagv
      121 wlllfawavl vadalarlaf gpwrrlaalv vaiaaisvpl asggwdglsv mreyavrsdd
      181 fwreairhvs laggsvaaal vaglplgiac arvapvrtvv mpvlnivqti psiamyglmm
      241 aplgllaarv plaaalgirg igvapaalal flysllpias svvvglaqvp ehvseaaram
      301 gmtrmqrllr vdlvlalpvi lsgvrivlvq nigltavaal iggggfgtfi fqgigqsaad
      361 lvllgaipti alalaaavvf eaattlakgr ta
//
LOCUS       WP_175799974             146 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydroneopterin aldolase [Burkholderia anthina].
ACCESSION   WP_175799974
VERSION     WP_175799974.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Illarionova,V., Eisenreich,W., Fischer,M., Haussmann,C.,
            Romisch,W., Richter,G. and Bacher,A.
  TITLE     Biosynthesis of tetrahydrofolate. Stereochemistry of
            dihydroneopterin aldolase
  JOURNAL   J Biol Chem 277 (32), 28841-28847 (2002)
   PUBMED   12039964
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..146
                     /product="dihydroneopterin aldolase"
                     /EC_number="4.1.2.25"
                     /GO_function="GO:0004150 - dihydroneopterin aldolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0046656 - folic acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16469
     Region          23..133
                     /region_name="FolB"
                     /note="Dihydroneopterin aldolase [Coenzyme transport and
                     metabolism]; COG1539"
                     /db_xref="CDD:441148"
ORIGIN      
        1 mkpfdepfva iesprlrgrg wsvfvdelkv parigihahe heapqpivid arlgyrceps
       61 eqgewidydg ycarlasfls hkphtrllet lvadiavlsf rewpaleslt lsvykpkirp
      121 gtkrvgvsld wtrgdylrwt gaagqm
//
LOCUS       WP_175799970             255 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia anthina].
ACCESSION   WP_175799970
VERSION     WP_175799970.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 255)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 255)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..255
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25862
     Region          55..253
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mtahaarpsl prrlpayvar aaavalllvl llrpawlqgv fapfadngap viydraslld
       61 ltlahlgtva lssligtlla vaagiavtrp sgadflpvar svvdigqtfp pvavlalavp
      121 avgfglkpvl ialvlygllp ifestiagle dvprdvvdaa rgmgmsgwqq lvsvelplaf
      181 pvivngirla vvinlgtati gstvaarglg dviiaglqts ntafvlqggv ivgllavlvs
      241 daigalarma sarht
//
LOCUS       WP_175799993             325 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175799993
VERSION     WP_175799993.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..325
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36024
     Region          6..316
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mkplfnfcfl lmpnfnmiaf tnalevlraa nqlretdeya wslasidggr idasngiald
       61 ttavrelarp divfvcggnd vhdattrdhl aalrqfdrqg vvlggictga yvlakaglmt
      121 gypcaihweh lfahretfrd iefsrrlfvi drnrvtcagg laplhmmlel isdqvgparv
      181 aeiadffive nlrdtdslqt iplvarlgsa nrvifdvidi meeniedpls gddlalrsgi
      241 svrqiqrlfr dalgttiahy yvtlrlkrar elllqtgmqi cdiatvcgfk sisnfgrnyr
      301 etfgcapgie rkrraaliea eargg
//
LOCUS       WP_175800016             732 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia anthina].
ACCESSION   WP_175800016
VERSION     WP_175800016.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 732)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..732
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78456
     Region          55..732
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mpsrrlprra rtlrpwrtsl palialcvas gahaaaddra paapaaaass ptpmpavppi
       61 erelpaisvs asatadptvg yqprtssvag gddraikdip qsvavvsssv mqdqqarsld
      121 dvlgnisgvt qtntlggtrd afikrgfgsn ndgsvlvdgv rtpvlhsyla tidrvevlkg
      181 pasllygmqd pggvinlvtr kpedtfggsi sasrtshggs saqfdltgpl gkpgqvaggt
      241 lafrltgeyd tsrywrsfgr erdaliapal swhdantsid vsyqyvdytt pfdrgtalvn
      301 grpddalryr ryeeawaqss giqetlrari ehrfsdawrv ratygwgrdr yaqnitrata
      361 fnsttgamtr sadanlgrnd sdqiatlgll gnltlagmnh alyvggeyer qrsfrgdtir
      421 gtatkgfdly dpvygllapg gtvsakqsds lskvhtysmi vqdsvkltdr ltavaglrwe
      481 dwqqesgmgr pfvfadrshg nvwlpqfgla yaltpsltay anvsrsfkpn vasnvtspla
      541 pefgrvleag lkfslkpgit gtlaayqidk rnvavtvgdi tstigtarsr gieldvagqi
      601 trhlsligsy aytnandrds ntslvnvarh tgslfavydt aianlpgrwr fgggarlvga
      661 rpgdtansft lpgymtvdaf aayettigkf ptriqlnvkn lldktyypss nsnlivavge
      721 prlvtltttv sf
//
LOCUS       WP_175800033             732 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia anthina].
ACCESSION   WP_175800033
VERSION     WP_175800033.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 732)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..732
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=80715
     Region          37..704
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mnrfvpflrn lwlrcrdgar algagawhrl rhptrrgval tlaaipvlgl lvllafvpft
       61 psigdirkar idrparvlsa dgqliaefrp vnrewvplkq isphmvdali atedhrfyah
      121 hgidwrrtla aglhtfsgsr qggstitqql arnlypdevg raptltrkvk elitafkiet
      181 vyskdeilet ylntvpflyn aygvemaart yfgksadqld ivesatlvgm lkgnsyynpv
      241 lnperavqrr nivlgrmaam gmlspqqlaq lqrrplrvdf epqtaqpgpa phfavqlrkw
      301 liawadrnny dlysdglvvr ttldaqlqem atqaltrqte rlqaiadsaw rgpsgcglrn
      361 dlfrgfirqt pdyraahdag ltdaaalkql ganrafmral cerktqvqag fvaidprnga
      421 irawvgspdf gsepfdhvvq srrqpgstfk pfvygaafad gmrpgdtfvd rpvaipvdah
      481 tvwrptdaep ptdapmtlrd alalsrnrit aqvmqregaa rvaqlaramg vrdspldavp
      541 slalgtspvt lkemvsaygt ianrgvyvap qmitriedrn gkvlaafgsa pperalpvat
      601 aqtlvdvmrg vvdygtgadi rsrygirvdv agktgttqdn tdgwfilmhp qlvagawvgf
      661 ddgsvtlrsd ywgagahsal pivgsfyeta lraraidphv qfspdfrprs apapapkrrp
      721 hvglfdwlri fr
//
LOCUS       WP_175800083             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175800083
VERSION     WP_175800083.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34091
     Region          7..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..293
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(105,109,148,162,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(106..107,111..112,114..115,118,122,124..130,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mqhlpdldaw aifarvaetg sfaksaelig tsqstvskai arlenrlgtm llyrtsrrls
       61 ltptgellrd rairlladae lieneasaqa lephglvrvn apmsfslryl apvlpafler
      121 ypnvdvdlml sdhlidvvpg gfdiairiae lndstlrfrr lcavrrplva spayldrygr
      181 pahprdlerh vcftyanlpt sgfwrfrhat sgdkfsvsvn grirtnnadv ilpalvagyg
      241 lalqpeflvv dalrdgelve vmhdwkiadi nvnlvtppgm lrtarvavll dyladqftta
      301 pweplvr
//
LOCUS       WP_175800097             477 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia anthina].
ACCESSION   WP_175800097
VERSION     WP_175800097.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..477
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51046
     Region          1..434
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfaslglie pllrnlqnln yqtptpvqak aipavlsgnd vmaaaqtgtg ktagfalpll
       61 qrlvqhgpav ssnrarvlvl vptrelaeqv lqsfveygqg ldlrflaayg gvsinpqmmk
      121 lrkgvdvlva tpgrlldlnr qnavqfdqve tlvldeadrm ldlgfareln avfaalpaqr
      181 qtllfsatft ddiramaasi lrspvnisvs ppnataskik qwvvpvdkrn kpelfmhlva
      241 ennwehalvf vktrngvdyl aamldeagya vdtihgdkpq parlralerf karevqmlva
      301 tdvaargldi ddlplvinvd lpivaqdyvh rigrtgraga sgvavslvca deapqlaaie
      361 alirqtlrre eepgfeaehr vpetsatgqi ikkpkkpkkp kvpqatpsam pasgkkprpq
      421 ggegkrkpat tagkgksvis gspfsvqkpr akpagkpaag grkpaakpag gagkrrp
//
LOCUS       WP_175800110             180 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia anthina].
ACCESSION   WP_175800110
VERSION     WP_175800110.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..180
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=19871
     Region          29..169
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 mrhdhdiveh awhhhreipq apgdfrralg cfatgvtvvt tvdgdgrrig ltansfssvs
       61 idpplilwsl arrspnlraf ehcrffavnv laasqqaict rfatpiddrf sgvdtvdgqg
      121 gvplisgala qfeceneivh aggdhaifig rvnrfrwreq vplvfcmgal reldtnrqes
//
LOCUS       WP_175800117             316 aa            linear   BCT 11-JAN-2025
DEFINITION  ketopantoate reductase family protein [Burkholderia anthina].
ACCESSION   WP_175800117
VERSION     WP_175800117.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..316
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33003
     Region          1..305
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkiaflgaga lgcaigsalt egghetwlvd rfaahvdams rdglqvdder gtrrvavrat
       61 thpaevgpvd lvvvlvksfh tdsamrgard lvgpetvvls lqnglghedv lseivgrerv
      121 lagktyvggv llapghiqsg vtgkltiige ldgritrraq aiadafnsag ltttvsdniv
      181 gtmwdkllin vatgaitgit rltygqlyde pvlkaaslaa ideamtvaqa agialsikna
      241 eeawnmaaeg lspafktsml qslekssvte idfingavvr wgervgvptp vnatlvacik
      301 gieramtdrl rdgvpa
//
LOCUS       WP_175800129             115 aa            linear   BCT 11-JAN-2025
DEFINITION  SMI1/KNR4 family protein [Burkholderia anthina].
ACCESSION   WP_175800129
VERSION     WP_175800129.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10558574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..115
                     /product="SMI1/KNR4 family protein"
                     /GO_process="GO:0042546 - cell wall biogenesis [Evidence
                     IEA]"
                     /calculated_mol_wt=12564
     Region          14..>112
                     /region_name="SMI1_KNR4"
                     /note="SMI1 / KNR4 family (SUKH-1); pfam09346"
                     /db_xref="CDD:430545"
ORIGIN      
        1 mpvlygtkpa qrllakfese lgfnfsadyv dflrrwggif idgadyldld fngvdngvis
       61 faslfgvgsn ngsfdlieqn ecvrdemdfl sdflvigddp ggnyyalalr tgavr
//
LOCUS       WP_175800118             130 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia anthina].
ACCESSION   WP_175800118
VERSION     WP_175800118.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..130
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14325
     Region          8..115
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 msapkayleh vaiwvkdihw hirffeqvlg mtmrevdgtr eaprqywtlg glqfisaprh
       61 egaegrlahl gvmcedleaa iaaaqafsvt elpqgrnwlr lpdglvveli qarpatcvaq
      121 alainpraea
//
LOCUS       WP_175800133             385 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia anthina].
ACCESSION   WP_175800133
VERSION     WP_175800133.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..385
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42512
     Region          4..383
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnptdayqdi reavrdlcgq fsaeyfrkid eargypeafv daltqagwla alipqeyggs
       61 glglteasvi meeinraggn sgachgqmyn mgtllrhgsa eqkqrylpki asgelrlqsm
      121 gvtepttgtd ttkikttavr kgdhyvingq kvwisrvqhs dlmillartt plsdvkkkse
      181 gmsifivdlh haighgmtvr pipnmvnhet nelffdnlei paenligeeg qgfkyildgl
      241 naertliaae cigdgywfvd kvsqyvkdrv vfgrpigqnq gvqfpiaraf inveaaslmr
      301 feaarrfdah epcgaqanma kllaadaswe aanaclqfhg gfgfaceydv erkfretrly
      361 qvapistnli lsyvaehilg lprsf
//
LOCUS       WP_175800143             442 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175800143
VERSION     WP_175800143.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..442
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48218
     Region          35..421
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(46..47,50..51,54,86,136..137,139..141,144,164,
                     167..168,171,266,269..270,273..275,278,306,310,361..362,
                     366,370,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 meidatcspg giatpasthn pahedrlfrr lalhilpilm fayvtsyidr vnvsfaklqm
       61 sqhlgfsdav fgfgagiffl gyvifevpsn mllvrvgprr witrivvswg ivsgltafvs
      121 tpmqfyvmrf llgvaeagfi paivlymtha fprhrraril slfyaalala gligspltgf
      181 ilqyfdgamq ipgwkwifiv eslpafvaal yvwkgldddv trserfsqad railtrvlae
      241 dreitatash qglfsswlvw afcviyfldv faiygytfwa ptmikqmgig sdfvigllaa
      301 lpnavavvvm vlfgrsadrr ggrrlhvaal llmgaaglgl sviwrdqlwl gmfalciana
      361 glisfpplfw smptaalgta svsmgiavis sfgnlggffg pyavgylkqv sggltaplfl
      421 mvgclllglv ltmllparli dr
//
LOCUS       WP_175800185             130 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia anthina].
ACCESSION   WP_175800185
VERSION     WP_175800185.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..130
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14229
     Region          7..125
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 miefkwdhlq lcsadaeata awfarclnae ivrrpgrvdl rigtinlfit anpdahspda
       61 hdgaprqgid hfgvlvenld aayahlveng aeivqpvtri ragvrgcfvr apgeilvevl
      121 errsaemtfn
//
LOCUS       WP_175800160             341 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175800160
VERSION     WP_175800160.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12168325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38031
     Region          31..203
                     /region_name="AraC_binding_2"
                     /note="AraC-binding-like domain; pfam14525"
                     /db_xref="CDD:434015"
     Region          247..334
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mgqfsgtgwl geatcfnhdt lllqsndlde vrarvadvfk phrltltgds ralhscmhha
       61 rwgnlslnll dyggevsiep gplehfyllq mplrgdaeie cgatrfvssp dtasllsptl
      121 slrmrwgeac pqailriere vmerhaqrhf gddrrgpvef epefglsspq gaclaqmlpm
      181 ladaiatdgh plrhplafeq lestllnlll yghpntarng trpapaplap fyvrrveeyv
      241 rahldeplti erlaelagvs pstlfagfrn rhgitpmafv rqlrlqrvrd elrddatpgl
      301 asvtdvalkw gfahlgrfai eykrafgesp satlrmrrvr n
//
LOCUS       WP_175800218             358 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            anthina].
ACCESSION   WP_175800218
VERSION     WP_175800218.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..358
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38692
     Region          22..325
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mkhlpsylal avfasvplwl rdqyflhili ttgifiigam slnlllgytg qlnlghiaff
       61 gigayasalt algfdvpifg whivhepwpp lagiaigtvv aglcgylvgk lsfrirgayf
      121 vivtisfaqv arlialnwvd ltqgplalnn ippvgldlpg lgeitlwqkv pnyylvlalg
      181 tvayilirri vcsrmgrami alreneslan svgidvtryl vfaavisaai agaagglyah
      241 yiriidpdif lfiytvtmvi mvvtggkgtl agpivggllf gilpvglrda appqvqwiiy
      301 gvlmiliiff lprgivpavs dwwhrrfgak arhvrmqanq ldalagqglt pnkilsrk
//
LOCUS       WP_175800250             837 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia anthina].
ACCESSION   WP_175800250
VERSION     WP_175800250.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 837)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..837
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=90784
     Region          56..775
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mpiikrpsss sdrkephysl rrspsgayyp dddngdndrr tprsggggrr sfgsrvmlwf
       61 vglfatlavv galivgyalv vmapqlpsld altnyqpkvp lrvftadhvl igefgeerrs
      121 lvrfqdipdv mkkavlaied yrfyehggvd fvgilragva dllhggarqg astitmqvar
      181 nfflssekty trkiyemlla ykieraltkd qilelymnqi ylgqrsygfa aaarvyfgkd
      241 lkditlaeaa mlaglpkaps aynpvvnpkr akvrqeyilk rmleigyitq pqydeavkee
      301 ihvrtpgnqy avhgeyvaem vrqmmyqqyk detytrgltv tttinsadqe aayqavrrgi
      361 ldyerrhgyr gpegsinlpa agddrdeaid daladhpdng dlqsavvlsa spnavdvqfv
      421 ggatttigsa glrfvsaals pranatlrik pgsivrvmkd gktgwqvvql pqvegalvai
      481 apqdgairsl vggfdfnksk fnhvtqawrq pgssfkpfiy sasldkgmgp atiindaply
      541 fppsvpggta wepkdddqpd gpmtmrtglq rsknlvsiri lasigtqyaq qyvtqrfgfd
      601 paktppylpm algaglvtpl qlatgyavfa nggykvdpyl iaevddargq plqksqpvva
      661 ggtaprtieg rnayvmnsll htvatagtga gtnvlgrsdl qgktgttnda kdgwfagyqq
      721 slvavawmgf dqpkslgsre fgaqlalpiw vnymrtalng vpeqqmpmpd glttidgely
      781 yadrtpgngf vasvdinpaa naisandalg sagaaglapp pvtpqekqqi mdmfesk
//
LOCUS       WP_175800274             440 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175800274
VERSION     WP_175800274.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..440
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47407
     Region          27..429
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(40..41,44..45,48,80,130..131,133..135,138,158,
                     161..162,165,262,265..266,269..271,274,301,305,355..356,
                     360,364,380,383..384,387..388,391)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mkaasstsln spatgdenlp vfrkiafril pllvlcylsa fmdrvnvgfa avsmredial
       61 satafgigsg vfflsyflle vpsnlaltkf garrwiarim iswgilsglt afvwngpsfi
      121 alrfllgaae agfypgvlly ltqwfpekkr aqilgyfila nplatiigap lsgwllsmgh
      181 fgslkgwqlm flveavpail lgivtffclp drvadarwls ddekrevasq lqkealqtvk
      241 raridlrhvf thprvlglsf ifltismtna tvnfwlpqmi kssgfstyvt gwisaipyva
      301 avgsllfwgr hsdrtgerry hilvpmvaaa vciavsglsd apvvrilgft iasaglfaal
      361 piywslpgrf lvgnaaaggi afinsvgnlg gfigpsamgy vkdmtgsfsg gllldsialv
      421 lgavvvmrvt srtsaanrea
//
LOCUS       WP_175800307             380 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175800307
VERSION     WP_175800307.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..380
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42171
     Region          193..359
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <308..359
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mrittdirqd ldalrdvpaa ivldesawpp lpsrradfdg vtrgdasqre lglmlldlya
       61 vaaqsgigef ecrffsllqa lipfdaawtg vathvptgpv mhnsflyrlp haffsdwkrv
      121 rdcdplarrt llgahghavr lsvvepgvda rfrdwcvkyg laqlmcvctl drrfglttfm
      181 siyrqglnrp fsdedanrfe emiphlaaal tinraaqltr ergdavapav ralcdnfgvl
      241 hhadhgfddv lrtewpawtg srvpeplvth vrrqsgqpfi gdalriqcvp vaglfqiear
      301 prslldrlsp relaairyyg agrshkevaq qmaispttvr hylrcayrkl gmhdksqiag
      361 vlgatgptdd epaeagspvr
//
LOCUS       WP_175800331             367 aa            linear   BCT 11-JAN-2025
DEFINITION  C40 family peptidase [Burkholderia anthina].
ACCESSION   WP_175800331
VERSION     WP_175800331.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..367
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37346
     Region          <6..175
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mlricvpvav vsllaacssv ppqsasrtsg mkittprafp apanfpkfvd hsvgqeeisi
       61 qamslvgvpy rwggntptsg fdcsglvryv lgraadvnlp rttadmssrg msidpdqvap
      121 gdliffnttg rphshvgiyv gklrfvnaps tggtvrldyl tnpywakrfd girrvappra
      181 tpapfdapty earrdapvat papapvvtaa aprqpayaap qagatptpap impaapvvaa
      241 apvvaaapvv aaavaapaaa aadpyepppr mqaaqqqata tngdmnamta daapaspaet
      301 gsqipttalt aaqaaafdve ppsaaaapsp rstepvqvlr aatqsapasa rtgtaddpia
      361 rfangsy
//
LOCUS       WP_175800370             393 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase [Burkholderia anthina].
ACCESSION   WP_175800370
VERSION     WP_175800370.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 393)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..393
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40325
     Region          1..393
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mtdvvivsaa rtavgkfggs lakvaapelg atviravler sgvkpdqvse vimgqvltag
       61 sgqnparqsl ikaglpsavp gmtinkvcgs glkavmlaan aimagdaeiv iaggqenmsa
      121 sphvlpgsrd gfrmgdaklv dtmivdglwd vynqyhmgit aenvakeygi treeqdafaa
      181 lsqnkaeaaq kagrfndeiv pvsipqrkge plqfatdefv rhgvtaesls glkpafskdg
      241 svtaanasgl ndgaaavlvm saqkaaalgl tplarikaya nagvdpsvmg mgpvpasrra
      301 leragwtpgd ldlmeineaf aaqalavhkq mgwdtskvnv nggaiaighp igasgcrilv
      361 tllhemvkrd akrglaslci gggmgvalav erp
//
LOCUS       WP_175800421             268 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Burkholderia anthina].
ACCESSION   WP_175800421
VERSION     WP_175800421.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..268
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29030
     Region          12..193
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(15,17,98)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(42,97..98)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            96..98
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mskqhassth lvlipsynpg akvdttvrna raqwspvwvv vdgstdgsae rlqamaardp
       61 glrvivlpen rgkgaavlag ldaaaasgft hvltmdsdgq hpaqlipdfm aasqaapdam
      121 vlglpkfdas apqlrvqgrr lsnawadlet lwagigdsly gfrvypvapl aaimhrqpwm
      181 rgfdfdpeaa vrlcwagvpp irieapvryf geheggvshf hygrdnalla wmhlrlfagf
      241 varlpmlvar rltrrsrspl srspgrgd
//
LOCUS       WP_175800425             266 aa            linear   BCT 11-JAN-2025
DEFINITION  (Fe-S)-binding protein [Burkholderia anthina].
ACCESSION   WP_175800425
VERSION     WP_175800425.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..266
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28364
     Region          <14..256
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mnerhypata pthvylfatc lvdlfvpeag ldavrllere gltvhyprgq sccgqpayss
       61 gnpdearrva aaqldlfgep wpvivpsgsc agmirhhwpa lfaddpvhgp karaiaerty
      121 elaeflvhvl dvrldalpah tgpaervvlh tscaarremg trvhgvalvd alpgvtrieh
      181 ereseccgfg gtfslkhpdi sgamvhdkva sacatgcdrl vsadcgclln ighaatkaga
      241 alpvehlasf lwrrtagaas lrgdqq
//
LOCUS       WP_175800440             786 aa            linear   BCT 11-JAN-2025
DEFINITION  LPS-assembly protein LptD [Burkholderia anthina].
ACCESSION   WP_175800440
VERSION     WP_175800440.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..786
                     /product="LPS-assembly protein LptD"
                     /GO_process="GO:0015920 - lipopolysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87029
     Region          67..757
                     /region_name="LptD"
                     /note="LPS assembly outer membrane protein LptD (organic
                     solvent tolerance protein OstA) [Cell
                     wall/membrane/envelope biogenesis]; COG1452"
                     /db_xref="CDD:441061"
ORIGIN      
        1 mppkplfpnv fpgdgaprkr rlalallavp glvpavsyaq lsgaaaqpqp ldspwdlrla
       61 pqledhplkd gtkpaafvia dhtsgtaeqd laakgsaelr rgdavvkada ihydqdtdma
      121 daygqvrvin sgtsfagpea hlkieanqgf mtapkyhfnm tggsgsaerv dlldsersvf
      181 vngtytacqc stnpawyikg srfdfdtgad egtvrnsvlf fqgvpifasp wmtfplsgdr
      241 rsgllpptfs mnsnngfelt lpyyfniapn rdltltprii srrgvqteat frylsptysg
      301 tftanylpdd rlahrdryai ywqhqqnfgg gfggyvyfnk vsdntypedl gsmnqfingt
      361 qtlyqqeagl tynkgpwsvl aryqhwqtlp psiapysrep qlnvkytkyn vggfdygaea
      421 dysrfritta dstegdrvvf npylsygvyg pgyfvvpkvq yhfasydlny lssstpnspk
      481 rftesiptvs fdsglifdrs vrlfgqdfiq tleprlyyvy tpyrdqsnap lfdtaesdfg
      541 laeiyqpntf vgndriadan ritagltsrf idprtgdera rfviaqqyyf adqrvtlnsg
      601 qtaaqarhsd livgaalklg sgfmsetafq ynqnnnqlvk ssvgfgyspg errvinvgyr
      661 ytranttldg qpinqflvsa qwpltrrlya igrfnydlag drvvdgllgl qydadcwalg
      721 vgvqrfangv ntsgqqnsst rfmmqltlkg lstvdnglvs afragvpgyt plpsapppms
      781 rfsnye
//
LOCUS       WP_175800467             251 aa            linear   BCT 11-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Burkholderia anthina].
ACCESSION   WP_175800467
VERSION     WP_175800467.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 251)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 251)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..251
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27036
     Region          16..208
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mlarlsatdr falihgardy sptlmailsw glvtgiamsk svmtlgqasa msifvyagss
       61 qlavlpllva klpiwtvllt aamvnmrfvi fsaglaphfs ylplwrrlai gyfngdviyl
      121 lfqkqgfayg rvpgkeayfw gmalaswasw qvsslagill asffpaswgl elagtlalip
      181 imvsavanrs tlaavavagi vsliafdlpy rlalplavla alaagctadf fveradwrri
      241 rtetvhekev e
//
LOCUS       WP_175800485             466 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175800485
VERSION     WP_175800485.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..466
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50649
     Region          10..419
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(23..24,27..28,31,70,128..129,131..133,136,156,
                     159..160,163,245,248..249,252..254,257,288,292,345..346,
                     350,354,370,373..374,377..378,381)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mderarkqar karasgwigs aleyydffiy aqaaalvfpq iffpkgdpki aivaslatyg
       61 vgyvarpiga fvlghwgdth grktvllicm flmgfstmav gvlptyhsvg mlapallvil
      121 rlvqgfavag eisgassmil eqapfgrrgy fasftlqgvq agqilaaavf lplayymped
      181 afaawgwrip fllsavvlia gfiirrevde taafakedas gqvarapile afkfswpdml
      241 rvlfmafmnv ipvvttifga ayavqpsygi nfhpsvylwi pvvgnivavl vipyvgnlsd
      301 rigrrplmif galssgllsy aylyaisvhn lpvafamsil mwgvvyqgyn avfpgyypel
      361 fptrfrvsam aiaqnigtti tallpalfaa vappgshnvp lmigsitlaa tivsalaaws
      421 aretyrvrld dlgkqdavpi pkeqydrlre eslsetrlak asmqth
//
LOCUS       WP_175800490             351 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175800490
VERSION     WP_175800490.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..351
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37340
     Region          15..329
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mtsseklpis nplrtdvliv gagpvglfaa feagviglsc rivdgierpg gqcielypdk
       61 piydipaips ctardlvdrl leqcrpfdpp mhlgerietl epleggrwla rtdkgqsfda
      121 aailiaagng afvpqrlald eaaplegrcv hysvtdihgf agrnvvvagg gdaaldwala
      181 lrsaarhvtl vhrrngfsam dssvnrlhqa isageidfvv gtiaalnape galesievrq
      241 iggsvhldad qllvlfglva nlgpianwgi dvqagrivvd tsyyessrpg ifaagdiagy
      301 ankqrlilsg fheaslalrk aytyafpdkk rvhvhssyda klaervaaih p
//
LOCUS       WP_175800509             310 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175800509
VERSION     WP_175800509.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33807
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrlkaltvf vrvavagsis agarelgmtp qaaskqvaal eallsvrlfq rstrrivlta
       61 egerllsqcr gavgelesal rmldddraqa vgtirvaapy slarrflapl lgefcdrqlg
      121 itaellvsdd madvveqrid iavrtgnlpd sglvarrvad lqlvvcaapa ylrrhgepqt
      181 idalsehrct aflyprtgkp fpweflvdgg vhtrqvnpfi atndidaeld tvlsgaaigq
      241 ffgysvhahv regrlvpllt rhvtcrygly lcmpqrthlp rrnrllmdfl adrlgahpdl
      301 aplaladapa
//
LOCUS       WP_175800525             490 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54 dependent transcriptional regulator [Burkholderia
            anthina].
ACCESSION   WP_175800525
VERSION     WP_175800525.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..490
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=52987
     Region          21..139
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <157..465
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mvarspdang taapempfvs vtapeagrkl fvimrspdes llaqlrelgw eiavaktaga
       61 aqnmtasvsv aaglidftgf tsrdypalka clsqpaigwi svaqagnmig tavrelirsy
      121 cfdyvtlplp hewishvlgh argmaaldrv dgaayaasig ehgmigncea mqqlfstirk
      181 vaktdasvfi sgesgtgkel talaihersg rgkgpfvain cgaiphhllq selfgyerga
      241 ftganqrrag riesanggtl fldeigdmpv esqasllrfl qegkierlgg qesipvdvri
      301 isathvdlds aveagrfrad lyhrlcvlri hepplrargk didilahyvl qkyksdsgrk
      361 isgftsaald amrryewpgn vrelinrvrr aivmaesrll tphdlgldtp getepvtleq
      421 aralaertai enallrndhr inkaaaelgi srvtlyrmmi ehglndhdnn gdnggkdsap
      481 sgdedhqrvg
//
LOCUS       WP_175800636             343 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175800636
VERSION     WP_175800636.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..343
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=37691
     Region          33..92
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          123..323
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(138..139,141..142,145,149,151..157,249..254,
                     260..261,263..264)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 mthaatgrpp arsdapspda dapdglrvqd ldlnllktfr avyeerhvgr aalrlgvtqp
       61 svsyalgrlr lmfrdalfvr tgtgveptpr aqrlagsvdk alailqdvld egsrfapdst
      121 qrvfrlhmsd faasaflptl laefdrrapg avietlhvde cqlnvalesg ridfalghfa
      181 dasshfqrta llhercvllm prrtaqrval pddfvldgda pdtlrlvavt shpqsmqlle
      241 rhglmprvra alpdfmvvpa llehgdyali lpetvaitfa arqpcalyei agasewpvna
      301 ywhrrfdadp ghrwlralll elfdiggqap fdawlaphpp aca
//
LOCUS       WP_175800612             317 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175800612
VERSION     WP_175800612.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..317
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33409
     Region          9..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..294
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,229,246,273)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,193,
                     223..227,234..235,238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 madlrdvnln rlaifvavvd agsltaaaer lglaktvvst hmqrlesevg anllvrttrr
       61 lsvtdagraf ydacrdivra tesaldavss dagplrgtlr vsvpidygal vvapavvalr
      121 dahpgldvel iandrvvdlv adnldvairi grladsnhra vqlgeyekwl vaspafvarh
      181 glprepdala alpfvmlstl prphtieldh adgghasvrc vapvvsntat acraitlagg
      241 gfglltdfsi addlaagrlv rllpawrsap agihavypst rlpspkvraf idamktrvge
      301 trpgapagra qskrtar
//
LOCUS       WP_175800652              99 aa            linear   BCT 11-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Burkholderia
            anthina].
ACCESSION   WP_175800652
VERSION     WP_175800652.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..99
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=11528
     Region          3..94
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 msyqvrypra aredlvrlyr yllehdvdaa araaqaiecg vamlrlfpft crkidernpf
       61 lrelivsfst sgyvllfeie saehvtilav rhqrdedyy
//
LOCUS       WP_175800670             295 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            anthina].
ACCESSION   WP_175800670
VERSION     WP_175800670.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..295
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30875
     Region          3..292
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mysfvlhvat lsciyallal glnlqagfag llnfgfvafa gvgayasaim stlgypvpvg
       61 lvlgvaaama vgfvmaslgr nlasdywaia tlaiaelirt valnenwltg gaqgisgvrp
      121 miatrsgaen dlvffmlalv ltviaylacr rlsrgrfgra irlmreepal atslgyrlvp
      181 lkvkatmtsa avasiggsll ahymsfvgpd ymlasetfvv wtmvmigglg nnlgvvlgaf
      241 vveviysavp fvkdyldins diagavrlgt igcvllacll lrpggivper irspq
//
LOCUS       WP_175800690             197 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175800690
VERSION     WP_175800690.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..197
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21989
     Region          11..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkkgtntngs apdtrerilq taselfyreg travgvdliv aqagvaktsl yrhfatkddl
       61 ieafllreda dfwahwdava aqyrrtpree ldaqlqwige riarpgyrgc pqiniaaeya
      121 dgnhparkva vahkqelrrr laeladamri depetyalrl atvidgalss gqalhahgpv
      181 rflqefaqll mpkkgrk
//
LOCUS       WP_175800704             649 aa            linear   BCT 11-JAN-2025
DEFINITION  arylsulfatase [Burkholderia anthina].
ACCESSION   WP_175800704
VERSION     WP_175800704.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..649
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=69263
     Region          47..615
                     /region_name="PAS_like"
                     /note="Bacterial Arylsulfatase of Pseudomonas aeruginosa
                     and related proteins; cd16025"
                     /db_xref="CDD:293749"
     Site            order(57..58,95,156,158,263,406..407,466)
                     /site_type="active"
                     /db_xref="CDD:293749"
     Site            order(57..58,95,156,158,263,407,466)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293749"
ORIGIN      
        1 mtksasplla frfrvvcaav agalslascg gvdsdpppqa satpeakrpn ilyimaddlg
       61 ysdihafgge intpnldalv asgrilsnhh tgtvcaitra mlisgtdhhl vgegtmgvpt
      121 derrglpgye gylndralsf aqllkdagyh tyiagkwhig sgivgsttgg gqtpdqwgfe
      181 hsyvllggaa tnhfahepag ssnytedgry vqpgqpgqpg gaggspavfy stdfytqkli
      241 syidsnkqdg kpffayaayt sphwplqvpd pwlhkyagvy dagydairna riarqkalgl
      301 ipadfkpfdg lpettaaspa tandgsasak yisavhsaad gysdygagkv dklwsslspa
      361 erkaqaryme iyagmvenld yniglliqhl kdigeydntf imfqsdngae gwpidsgadp
      421 tatdtangqe pvystlgtdn gkqnaqrlqy glrwaevsat pfrltkgysa eggvstptiv
      481 rlpgqtqplp tlrafthvtd ntatflavag vtppsqpapp lvntltgvdq nkgkvvynnr
      541 yvypvtgqsl lpvltgsasg evhttpfgde aygraylrsa dgrwkalwte pplgpldghw
      601 qlydlaadrg ettdvsaqnp svvstlvdqw ktymsnvggv eplrprgyy
//
LOCUS       WP_175800727             202 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175800727
VERSION     WP_175800727.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22224
     Region          2..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mamtrqfded avlervleif wikgwkatsm adlaeaanvq rgslyhaygg keqlfqlafd
       61 ryatrvldet raalnapsah talqqffess iasmtahvpp rgclttksai eadasadniq
      121 dsvrsllknl enaivealsr deiraslaqs peataqmiit ftrglavmer inhdpeqlre
      181 mcdhlvnlly sdnsqalaav np
//
LOCUS       WP_175800777             875 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia anthina].
ACCESSION   WP_175800777
VERSION     WP_175800777.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..875
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..875
                     /product="DEAD/DEAH box helicase"
                     /calculated_mol_wt=95907
     Region          145..>536
                     /region_name="BRR2"
                     /note="Replicative superfamily II helicase [Replication,
                     recombination and repair]; COG1204"
                     /db_xref="CDD:440817"
ORIGIN      
        1 mstfatevai eirqepgfws dlaelravgi rstvlqenqq vrvegpvlae kalarllnta
       61 svfasatdee skelaqqiav fasltsgddi vreasirils dlgnfpglrk lerehpvdlg
      121 fethmrsgll relntvdmag arvplteyql dlwrsldssa atavsaptss gksfvvlehl
      181 seraiaaerf gaiyiaptra llteihgkle krlssisdsi rittipvpdp esrpkqiyvl
      241 tqeraqflls tvavaglidl visdeaqslg ddsrgmilqd aleklresnp aarflflapg
      301 asglqligds iglpdinvke ttlspvvqnr isvgfsdlde hvvrldlvtp krlepigtyh
      361 fqrgfalgdd tklaavalel gasgrslvya tgaknaedlt allalnrqpe tskglsdlak
      421 fieqhihkqy slatyvrqgv afhygnmpsl lregieaafk rgeldylcct ttlfqgvnlp
      481 arnvfidtpt rgkgaaldea slwnfagrag rlgeevvgnv flvnyenwet kplterkpfa
      541 mqaafkqtve adfdavvell qaavdkapil erdrasgdri taaaglilfr ssqktldgll
      601 grrglsltte qkdtltelae qalaslelpa svlttswmld pvalagllqr irelvrhrdf
      661 sklmpsnpsg dsytvynsii rrlykylggm nlsgeegrrq rgyvshvtvt alkwmrgepl
      721 tqlvaeavky kkkvaqqtnk rsltqaaidg airdmftlie qtirfklvqw akayvdllky
      781 alaqegldem vtqvydfsla lelgvstrtg rslvefglsr itaaamasli tdsslssdqv
      841 rgwflqqpas liqqlsplvv aelrerglva ieysa
//
LOCUS       WP_175800870             404 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid aminotransferase [Burkholderia anthina].
ACCESSION   WP_175800870
VERSION     WP_175800870.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Alexander,F.W., Sandmeier,E., Mehta,P.K. and Christen,P.
  TITLE     Evolutionary relationships among pyridoxal-5'-phosphate-dependent
            enzymes. Regio-specific alpha, beta and gamma families
  JOURNAL   Eur J Biochem 219 (3), 953-960 (1994)
   PUBMED   8112347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..404
                     /product="amino acid aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43585
     Region          1..396
                     /region_name="PRK09257"
                     /note="aromatic amino acid transaminase"
                     /db_xref="CDD:181731"
     Site            order(102..104,130,183,214,243,245..246,254)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(105,140,207,252..254,290,293)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            246
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 myehipaypg dpilslfqaf qqdahphkvn lsiglyydda gripvlestr vaaerlreag
       61 aphtylpmeg laayrqgvqr lvfgadcaal aqgriatlqt lggsgalrlg aefvkryfpd
      121 saiwisdptw dnhrvifsaa gldvhtypyy dearnglrvd amlaaldalp arsivllqpc
      181 chnptgldls ldawravidv lvrrglipfl dmayqgfgdg ldddawavra ivdaglpaiv
      241 snsfsknfsl ygervgglsi vcastgeaat vlsqlqagvr rtysspplfg aqlvstvlnd
      301 dalrarwede vaqvrarikr mrgalkarld aclpapafda lvtqrgmfsy tgisaadvdr
      361 lrmshgvyll rsgrmciagl ndanvehvan aiadvlggat rqta
//
LOCUS       WP_175800932             240 aa            linear   BCT 11-JAN-2025
DEFINITION  (Fe-S)-binding protein [Burkholderia anthina].
ACCESSION   WP_175800932
VERSION     WP_175800932.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..240
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25911
     Region          <2..237
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mrvglfvtcl vdlmrpeigf salklirdag yevfvppaqt ccgqpaynsg dralardlae
       61 ktlrefeqfd yvvapsgscg gmirahygdl frddpelmgr yarfqqkvye ltdflvsvak
      121 vtlvpgeftg pvtyhdscsg lrelgvkaqp rallaqrgva vtemkdcehc cgfggtfsvk
      181 ygdisaaiad ekcanvrasg tgavvlgdlg cmlniegrlr rtgdrdtrvl hvaqvlagdv
//
LOCUS       WP_175800871             128 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Burkholderia anthina].
ACCESSION   WP_175800871
VERSION     WP_175800871.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..128
                     /product="RidA family protein"
                     /calculated_mol_wt=13546
     Region          15..124
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 madripvdlp qlaqpfswat ragglmftgh gpvdasgaiv gdtmteqari tlgnlakaaa
       61 aagatmddva qvlvylsdvk ampefdaeyr rhfrepypnr tcvgvqgfah pdmrvelvay
      121 valpaasd
//
LOCUS       WP_175800965             297 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175800965
VERSION     WP_175800965.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32107
     Region          11..>51
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 maiedftgvl afiavaqeqs ftraaaklgi tqsslsqtvr glearlgvrl ltrttrsvst
       61 teagarllet agprlaevqa emsavselrd kpsgmlrita tehaadtvlw prlaeflkty
      121 pdvkvevsid ygmadiaaer ydmgirlggt vadgmiavrv gpdqrfavvg spaymsthpa
      181 pstpgdlvgh ncisfrlpth gslyawefkk gkkavrvrae gqlvlngmyq tvtaaltgvg
      241 lafvpedvar pyinqgrlie ampdwcpifp gfhlyyasrr gtskamsllv ealryra
//
LOCUS       WP_175800968             613 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175800968
VERSION     WP_175800968.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..613
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=62825
     Region          1..270
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
     Region          320..602
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mktigyiglg smgsalarrl ldeyqlivwd lnpaaasafe algavvassa ielarrcdli
       61 llclprtsdv dalifgdggl agglragtli idqtsgipvq tralavrlve lgvalidapv
      121 sggviganag tisimvsgpa adcetalpvl raispnvfrc gdrvgdgqam klvnnllsag
      181 crlstlevva mgrkmgvsla altdavnrgs grnrttrttl selaagklmp shfamalmlk
      241 dmnqaiqlam dngvptpltn ivrgllqigv stlgetaqle qaidlvesma gtritdaepg
      301 apavsgsvpr avagaqgtpp rigyvglgtm ggalarrlll shpvrvfdvk adarlaleaa
      361 gakvaedlps lardcdvifi cvptsaavra lifgegglae glsagkivvd qttgdpsttv
      421 aigaelgqlg vslidapvag gargavagti aimcggrdda fdavypilas ispnvvhcgp
      481 lgnghitklv nnaistcncl ltyeaasiav kvglkldtva tvinrstgws vaserilpsl
      541 segrptadfq lqwmvkdlql agrmalacga pmlvartvcc lyeagahmlg ktenidaiar
      601 ffetmtdvrf iga
//
LOCUS       WP_175800973             330 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            anthina].
ACCESSION   WP_175800973
VERSION     WP_175800973.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..330
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=34894
     Region          31..313
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mnpnrhrdfk ldiwgvvlll plavvplvta dtflnslayq caigvsaala vyitlrlgll
       61 sftvpafmav ggyaaamlak agmtdllvlm gvsfiipalv aiplgaivlr lkgvyfiiit
      121 flfneilqlv ifetptltgg adgipdvpsa tlfghhlgss smlilvtvai cviatlitlf
      181 vtqwfraeft sidenetlae slgvavwkyr tigfvasagv sglagfalvn mlatahpssf
      241 aswsinnyia yafvggrgsm lgivvgslll ivmtnifsgy asfsaglfgl llvvvmmaap
      301 gglvgtcmkl csrrkahvda qrksvhwrka
//
LOCUS       WP_175800986             259 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175800986
VERSION     WP_175800986.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143283
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..259
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=27026
     Region          7..254
                     /region_name="TER_DECR_SDR_a"
                     /note="Trans-2-enoyl-CoA reductase (TER) and
                     2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR;
                     cd05369"
                     /db_xref="CDD:187627"
     Site            order(16,19..21,40..42,66..68,93..95,116,144..146,163,
                     189..192,194)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187627"
     Site            order(41,68,95..98,106,108..109,112,146,148,159,191)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187627"
     Site            order(70,101..103,105..107,110..111,114,118..119,122..123,
                     126,130,133,138,148,152..155,157,160..161,164..165,
                     168..169,171..178,180,191,216,217,219..221,225,228..229,
                     232,237,239..244,246..254)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:187627"
     Site            order(97,148,159,163)
                     /site_type="active"
                     /db_xref="CDD:187627"
     Site            order(101..103,105,110..111,114,119,122..123,152..155,157,
                     160..161,164..165,168..169,172,175..176)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187627"
ORIGIN      
        1 mfanetlkgr valitgggsg igleiattya klgasvmlvg rneervqiaa qaikemggia
       61 aarktdvrny devkatveat veqfgsldil vnnaagnfvc ataelsprgw qtvididlng
      121 tfhgchaayp ylkqsthggs iisiitmlgv tgwpqaahaa aakggilsls rtlavewggd
      181 girvntispg pigdtegvqr myieggrgel emkktalgrf gkkedianaa vylasdlgay
      241 vtgenlivdg grwlkyvaa
//
LOCUS       WP_175800992             155 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia
            anthina].
ACCESSION   WP_175800992
VERSION     WP_175800992.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..155
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16792
     Region          1..126
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mseammngps pltqgereli layaagvagc afvyvahsev ayargipegl ierllidpda
       61 vtlpaklksl lafvrklsvt pgdieqadad avfaqgwdeh alhdaiaita raafmqrlvq
      121 gfgfvpmsre havkrakqri ehgyvnlysa frepk
//
LOCUS       WP_175800994             540 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175800994
VERSION     WP_175800994.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..540
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58624
     Region          1..531
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mesydyvvig agsagcvvar rlsddptlrv llleagppad dfwvrtpagm gklfkhddyn
       61 wkyftepvpt lrnrriywpr gkalggssai ngmvyvrgnr adfdhwaslg npgwgwddvl
      121 pyfkraesnq rigaplwgtd gplaisdpav khptayafia aarengipti deisgveqhg
      181 agflqatiag gvrqtaysay itpvagrpnl vvranthvrr ivvenreata ievidadgir
      241 tiaarreviv cagalnspqv lmlsgigdgr llkqhdipiv ahlpgvgknl qdhfvvrvqa
      301 ratressynh vlsgwrkywe glryitthqg ylalgssmaa afvkshpdvp yadleisfrp
      361 mtfryletgs vevdsypgvs asvynmrpas tgeislrsad plqapvfnpn ylgnaadigv
      421 mlaglrqirr ifateplasr icseiapgad vttdeqlidy meregqcafh pagsckmggd
      481 emavvderlc vrgierlrvv dasimptvts gntnapsimi gekgadlilr hpvdargvta
//
LOCUS       WP_175800996             297 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175800996
VERSION     WP_175800996.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33415
     Region          9..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 msrdnfssll afiavarars ftraaarlrv sqpalsytir aletklgarl lmrnarnvep
       61 teagqrlldr lapefdriea eiealselrd qptgtirita idyairsvlw pklaaflpky
      121 pdikvelvne yesvdivarg ydagvrfgqe laqdmisvri gpditnrvvg spaylarrkp
      181 prtpddlteh vcinlrtsty gglyewefvk gkrawnvavd gqlvfnnayd ifeaakagfg
      241 laylpedmvr pyiergqlvs lleawcptws glhlyfpnrh qpsramallv ealrhhs
//
LOCUS       WP_175801004             669 aa            linear   BCT 11-JAN-2025
DEFINITION  acyltransferase family protein [Burkholderia anthina].
ACCESSION   WP_175801004
VERSION     WP_175801004.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Bera,A., Biswas,R., Herbert,S. and Gotz,F.
  TITLE     The presence of peptidoglycan O-acetyltransferase in various
            staphylococcal species correlates with lysozyme resistance and
            pathogenicity
  JOURNAL   Infect Immun 74 (8), 4598-4604 (2006)
   PUBMED   16861647
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 669)
  AUTHORS   Slauch,J.M., Lee,A.A., Mahan,M.J. and Mekalanos,J.J.
  TITLE     Molecular characterization of the oafA locus responsible for
            acetylation of Salmonella typhimurium O-antigen: oafA is a member
            of a family of integral membrane trans-acylases
  JOURNAL   J Bacteriol 178 (20), 5904-5909 (1996)
   PUBMED   8830685
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15196437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..669
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=73278
     Region          18..360
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
     Region          411..665
                     /region_name="SGNH"
                     /note="SGNH domain (fused to AT3 domains); pfam19040"
                     /db_xref="CDD:436916"
ORIGIN      
        1 mtktlsapat aaagtlvyrp didglravav lavvifhafp svlpggfvgv diffvisgyl
       61 itgillsdle tgrfsfrhfy arrtrrispa lvvvllatyg mgwfslygde yrelgkhiva
      121 gagfvsnwas wteagyfdqe aqakpllhlw slgveeqfyi vwplllwaah karrvdwacg
      181 viglasfaan ialvgrhpsa afywpvtrmw ellagaalai aaarfrsgdg kwanllpvgg
      241 gvlciasftl lsarvafpga walmpvvgav aliaagregw inrrvlaqpv piwfgkisya
      301 lylwhwplls fafviagrvp ssavrtglvv iavalawltt aiierpirfg aakrwklvap
      361 cllmigvvyl ggmtymrggl gfrkgyspda dvttarlggg hefinpmcgv spdeqrlfpf
      421 catdkrvrsh favwgdskad alywglvres apgegwtlia rpscapmagv wrtssnagdd
      481 palcrdanit alrmlldtpe lktvvlvmtd rdvigqtfad rdqttpresa aldgldqavt
      541 aleragprva lvldnprlrd prqcmdrrpl awpflrralg vtdmsaaqrc aisyrehvar
      601 tkqftalvda lkrrhpallv ydpanalcds grdvcpmtrd rhylysygdh lsdygnglva
      661 rqflpllrq
//
LOCUS       WP_175801020             540 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia anthina].
ACCESSION   WP_175801020
VERSION     WP_175801020.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 540)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..540
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59007
     Region          9..537
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msdtavskpg epllslehlh vrfgdtvavd dvtfaigrge rvalvgesgs gksvtalsil
       61 rllrdadvsg tirfagqdla gkserqmrgl rgsdiamifq epmtalnply tigaqigeti
      121 vlhdgvtare arkraialla rtgitepekr vdsyphqlsg gqrqramiam alacrprlll
      181 adepttaldv tiraqivdll lelqreeaek rgmaillith dlnlvrhfae rvavmehgkl
      241 vesgpverif aepehpytrr llnsrpqrav apvmpiapvv ldarhvsvqf arkrpgfagw
      301 fgtmpvtavs dvsvsvrqge tlgivgesgs gkstlamall glqktahgei efqgralssy
      361 rgreqtalrs nmqvvfqdpf sslsprhtie rivgeglalh rpeltpdarr akslavlrev
      421 gldrtvlhry phefsggqrq riaiaralvl eprilildep tsaldvsiqq qvlkllanlq
      481 qkynlgyvfi shdlevigam ahrvavmqgg avvesgdvvd iftkpshpyt qkllkavwka
//
LOCUS       WP_175801043             256 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF899 domain-containing protein [Burkholderia anthina].
ACCESSION   WP_175801043
VERSION     WP_175801043.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 256)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..256
                     /product="DUF899 domain-containing protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28595
     Region          1..254
                     /region_name="COG4312"
                     /note="Predicted dithiol-disulfide oxidoreductase, DUF899
                     family [General function prediction only]"
                     /db_xref="CDD:443453"
ORIGIN      
        1 mtnhltgtra ewlaarrall daekaltrqs delarqrqal pwvrvdktyr fdtedgqatl
       61 adlfggrsql lvyhfmygpd ykagcpscsa ladgfdgfai hlanhdvtla avsraplakl
      121 layrqrmgwt fpwassvgnd fnfdfnvsft etqqrtgdve ynyaragham dmapppaavv
      181 qfaatcgtda atysldrpgm safvredgvv yhtystyarg ldglwgmyqw ldraplgrne
      241 tgpwwrrhde yargra
//
LOCUS       WP_175801055             403 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175801055
VERSION     WP_175801055.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..403
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41628
     Region          8..388
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(18..19,22..23,26,61,108..109,111..113,116,139,
                     142..143,146,221,224..225,228..230,233,263,267,316..317,
                     321,325,341,344..345,348..349,352)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mpdsryrwvi vaaggllsci aigamfslpv flraiardtg wsmtgisaam tlgfiamafa
       61 siawgslsdr igtravvvtg avllgaslal asrapsllaf qlvfglgvgs aaaavfapmm
      121 acvtgwfdth rslavslvsa gmgmapmtms plaawlvsrh dwrasmlmia alaavvmipa
      181 sllvrrppal drthaepmaa gapaplsvgd alrspqfvvl lltnffccat hsgpifhtvs
      241 yavtcgipli aavsiysveg lagmggriaf gllgdrfgak rmlvagllaq algalgyyfv
      301 rtldgfyava mlfgfiyagv mplysvlare nfqlrmmgtv iggsamagsl gmaagpvagg
      361 livdalgsyg wlyigsfvig laafavamlf rpfpkeqsqt vaa
//
LOCUS       WP_175801061             297 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175801061
VERSION     WP_175801061.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..297
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=29950
     Region          1..287
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mevgfcgpgl mgapmirhll aaghrvsvwn rtrekaeala kdgaqvvdtp relaervetv
       61 fvcvldarav gdvafgengl fagdaaarrv rrivdhssip paatrdyaar aaalgagwid
      121 apvsggvpga lagtlavmag ggaadldavr plidtyasri thmgeagagq taklcnqaiv
      181 tatvtaiaea vglaqasgid aarlaealag gwadsvllqt fvprmtsggh apigalatfq
      241 kdvdaiadaa retgavmpvs atvqqvlrlg aaqglasadf aafidivrpg ngrtgar
//
LOCUS       WP_175801082             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175801082
VERSION     WP_175801082.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33064
     Region          6..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 msgenfrdil aflavarers ftraaaqlgv sqsalshtir sletrlglrl ltrttrsvap
       61 teagerliqt vgprfdvisa eleaftalrd kpagtvrita sdfathtvlw prlsrlqpdy
      121 pdlkieiamd agltdivaer ydagvrfgdq igkdmtsvpi spdirmaivg apsyldkrst
      181 palpndlidh dcinmrfspr ggiyswelkk gkdrvnvrvn gawtfnsitl avdaavagcg
      241 laympedlam phiaagrlrp vmqawcptfp glhiyyasrs cpspalsliv dtlryrhkrr
      301 a
//
LOCUS       WP_175801158             238 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Burkholderia anthina].
ACCESSION   WP_175801158
VERSION     WP_175801158.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..238
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=25513
     Region          6..223
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mdlesilytq gfgsrrqcrg liesgrvtva gasatapdas fdtdgfvftv ddtawpfhah
       61 aylalnkpag yecsrdpqhh asvfsllpap lvargvqcvg rldqdttgll llsddgqfvh
      121 aytspkrkvp ktyvatvrhp lddaqlaalr agvqlhgepk piaavaadar dthalaltvl
      181 egkyhqvkrm vaaasnrvea lhresiggft lpddlapgaw rwlgeadlsa lrnpvktl
//
LOCUS       WP_175801178             270 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia anthina].
ACCESSION   WP_175801178
VERSION     WP_175801178.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 270)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..270
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28632
     Region          15..264
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtltatgtag dltctaagvt lkagdrtlld gftqtfgpge iwcvagpnga gkttllatla
       61 glqppaggqv eidgrplaaw ppeqlaqrra lmpqqlhdaf satvfdtvll nrfpylggwg
      121 werdgdraaa rdalatfgla alasrdvlsl sggerqrval aatlcqdapl mlldeplahl
      181 dlhhqidcls altawldagp rtvlfschdl nlarrfatha llldgrghaw agpvhdvltp
      241 araskafgyp lvlirengrd allpawperr
//
LOCUS       WP_175801209             442 aa            linear   BCT 11-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Burkholderia anthina].
ACCESSION   WP_175801209
VERSION     WP_175801209.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..442
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=46904
     Region          3..408
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mnkrmsaavw illamaagil igyliytqfp nkqsaaeiag yislvsdvfl rlikmvigpl
       61 vfstlvvgia hmgdassvgr vfvkalgwfv taslislllg llmanllrpg enlglplpdi
      121 gasahlatsk ftlkdfvghm vpksfaeama nneilqivvf smffgvalsa lgergkilva
      181 aidqlahvml kitgyvmkla plavlaamas tvainglsil lkfavfmgdf yvslfllwst
      241 lvaagllflg rrvfkllgli keafmlsfat asseaaypki ldaldrfgvr rkissfvmpm
      301 gysfnldgsm myctfaslfi aqaydihlsl gtqitmllil mltskgmagv praslvviaa
      361 tlhqfdipea glllilgvdt fldmgrsatn avgnsiasav vakwegalms eseaaayaah
      421 ldaelerqtg gaapdagras lv
//
LOCUS       WP_175801233             382 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175801233
VERSION     WP_175801233.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..382
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=41897
     Region          210..374
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mpahnadspg tgellyriha ardedawrga maqlrerfda asavlaqrhl argqgevlyg
       61 apddpafarv faeyaprnpw flstdacqpl hvssgdeilg grelvgtdyy kallhpqrlr
      121 hrlcgvvard ddalcyvely rsegqrrfga keksefrgll ahialamenr whrrhaadle
      181 qalmhvvdgh anatflvepd griaysnrna qalceqdsgl yrdgpylaav tpadqralre
      241 tladlarqag eggpraglpp tqvlsvsspg arlpttltlq pagaslrgga eharvllvvs
      301 arrqraehah hdcsfarqfk lsdaqarvsa lifdghsiat laqtlhvsen tvrshlkqvf
      361 qktnthgqme lvrlhaqhcp na
//
LOCUS       WP_175801247             235 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175801247
VERSION     WP_175801247.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..235
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25319
     Region          18..228
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mpsslapylp qieahpwfaa lppdlraqll eraalrrlpa ghalfrrgdp pcglyavlag
       61 sltigavdah gkealltvae pvtwfgeial fdgqprthda ialddtlllh vpqaallgil
      121 dttpqywrqf allmaqklrl sfltveamsv mpaaqrlaar llmiangygg isagrtrirl
      181 sqeklasmls ltrqttnqll kalqadgivr lhvgeielvd vdalrrasgl pdgma
//
LOCUS       WP_175801265             309 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia anthina].
ACCESSION   WP_175801265
VERSION     WP_175801265.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..309
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33465
     Region          2..256
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msdvislgvi gigkiardqh lpaiaaepgf altacasrha evagvrnypd lrallaaepe
       61 ldavslcapp qvryaqarta leagkhvmle kppgatlgev aaldaftrer gltlfatwhs
      121 rcasavepar awlatrsira vqvhwkedvr rwhpgqqwiw epgglgvfdp ginalsivtr
      181 ilprelvlre atlyvpsdaq mpiaaeldca dtdgvpvrae fdwrhgpveq weiavdtsdg
      241 vlaisrggaq lsidgepvei gpereypaly ahfraliarg esdvdvrplr lvadaflfgr
      301 rvgtdafgr
//
LOCUS       WP_175801277             158 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175801277
VERSION     WP_175801277.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..158
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18032
     Region          4..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mptpldafdr kllmevqrda htpqnelgar vnlstaavnr rlrrlaedgv ierytaivap
       61 ekvdhpltiv vnveveseqi dqldamkrtf ercpqiqqcy yvtgewdfvl ilavrnmdqy
      121 naltrelffs nnnvkrfktl vsmsrvkvgl evpvdpge
//
LOCUS       WP_175801283             664 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 28 protein [Burkholderia anthina].
ACCESSION   WP_175801283
VERSION     WP_175801283.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 664)
  AUTHORS   Abbott,D.W. and Boraston,A.B.
  TITLE     The structural basis for exopolygalacturonase activity in a family
            28 glycoside hydrolase
  JOURNAL   J Mol Biol 368 (5), 1215-1222 (2007)
   PUBMED   17397864
REFERENCE   5  (residues 1 to 664)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 664)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..664
                     /product="glycoside hydrolase family 28 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=69230
     Region          82..620
                     /region_name="Pgu1"
                     /note="Polygalacturonase [Carbohydrate transport and
                     metabolism]; COG5434"
                     /db_xref="CDD:444185"
ORIGIN      
        1 maapsrrsss svrsfsskrv srrafigwtg alagsavlsg slaatrafaa gsppnaavdl
       61 iwgehgaaar iaaslahvsr lafrgrdfdv thygaracat vtqtspypva kspvspgsel
      121 ttapgafdsr paflaaidac mragggrvvv ppgnwycagp ivlqsnvnfh lsanctiyfs
      181 pnpadyakdg pvdcgangrl yysrwqandc lnygapvyar natnialtge gstsvlngqa
      241 mtpfsgsgsn svcwwtykgs sgaygasatv psqayanpnn vdlrivapai pdalyallts
      301 pvtpwqqdqn ylpalseagv pvekrifglg hylrpcmvef igctnvlmen yqtqntpfwq
      361 hhptasrnvv irgvttnsig pnndgfdpda ctdvlcedct fntgddciai ksgkdrdtey
      421 gpakrhlirn ctmnsghggi tlgsemgggv eqiyatnlsm lnanwqtnpl niairvktnm
      481 nrggyvkdfh vkgvtlpngv tqkgggygsa llagspinas vplgvvtpaa gnpsaaqggi
      541 vtfdcdyqpa ndavrtrppv vqnvtisdvt asnvtlngvs ascfqaivaq gpvafdyngt
      601 pptpavqpis gvtisncdfg tpvasgtatv tspgpiyafn vnamtltnvt iagqvvntti
      661 tdkr
//
LOCUS       WP_175801334             558 aa            linear   BCT 11-JAN-2025
DEFINITION  alkaline phosphatase family protein [Burkholderia anthina].
ACCESSION   WP_175801334
VERSION     WP_175801334.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 558)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..558
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=58296
     Region          48..536
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 misrfakqrk mavmvagala lastgvsaaq qdgnaqgnda ahgrrvvkhv lllsidglhe
       61 qdlarcigan tcpniavlaq sgvtytnayt pglsdsfpgl aalvtggspk taglfydvsy
      121 drnlyapsdt tcsgkqgwnv vfdettgida enggalvhln gggafnpqai pnakvngkcv
      181 pvyphnyvkt ntvfeavkag ipnaytawad khawgydwln gpsgtgvddl arteinsidp
      241 atgtnytdvy shtarfdnlh vqalinqiag rdstgtksap vptlfgadfq tlsvaqkatv
      301 atgggyldas ftpngqvana ityvdnsigh ivaalkqanl ysstavivts khgqsptdht
      361 klvkngdtlt klleannyld pngnfgqnnt ttgnlndgsg lvgtgfvqtd dvgliwlrdr
      421 nqrtavvqtl kanlscnapg icadgsqayi lygaaladrf gdpangrtpd iivqpnpgvi
      481 ytssktkdee hggnapddsh lgllvsypgl hrartvtdvv gtkqvaptil gllgaeprll
      541 navvaentrv lpglgier
//
LOCUS       WP_175801336             473 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Burkholderia anthina].
ACCESSION   WP_175801336
VERSION     WP_175801336.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..473
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52345
     Region          5..446
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mdtafsaldl arlqfaftvs fhivfpalsi glasfiavle yrwlktgkqy yktlclfwsk
       61 ifavafgmgv vsgvvmsyqf gtnwsgfssf agsvtgpllm yevmtaffle agflgimlfg
      121 wnrvsprahf gatlmvaigt listfwilas nswmqtpqgf eivdgrvvpt dwfaiifnps
      181 fpyrlfhmai aafivaalvv aatgawhllk grrdkgvkkm fsmalwlllv laplqavigd
      241 qhgintlkhq pakiaaiegl wdtekggtal nlfgipdmka ettryavkvp hlgslilths
      301 wdgeirglkd fppqdrpnst ivfwsfrimv glgfamigla alawllrrrg nlyeskwfqr
      361 falvmgptgf vsllagwvtt eagrqpwvvy gvmrtaqavs plsvqqvsls mmtfvivyfl
      421 vfgtgvyyml klmkagpalp daphdpkhdl pdtrpdhtar rplsavdeli etv
//
LOCUS       WP_175801341             212 aa            linear   BCT 11-JAN-2025
DEFINITION  2-hydroxychromene-2-carboxylate isomerase [Burkholderia anthina].
ACCESSION   WP_175801341
VERSION     WP_175801341.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Thompson,L.C., Ladner,J.E., Codreanu,S.G., Harp,J., Gilliland,G.L.
            and Armstrong,R.N.
  TITLE     2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class
            glutathione transferase from Pseudomonas putida
  JOURNAL   Biochemistry 46 (23), 6710-6722 (2007)
   PUBMED   17508726
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122490
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..212
                     /product="2-hydroxychromene-2-carboxylate isomerase"
                     /EC_number="5.99.1.4"
                     /GO_function="GO:0018845 - 2-hydroxychromene-2-carboxylate
                     isomerase activity [Evidence IEA]"
                     /GO_function="GO:0043295 - glutathione binding [Evidence
                     IEA]"
                     /GO_process="GO:1901170 - naphthalene catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23384
     Region          8..188
                     /region_name="DsbA_HCCA_Iso"
                     /note="DsbA family, 2-hydroxychromene-2-carboxylate (HCCA)
                     isomerase subfamily; HCCA isomerase is a glutathione (GSH)
                     dependent enzyme involved in the naphthalene catabolic
                     pathway. It converts HCCA, a hemiketal formed
                     spontaneously after ring cleavage of 1; cd03022"
                     /db_xref="CDD:239320"
     Site            15
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239320"
ORIGIN      
        1 mnaartatwy fdfvspfayl qqerfeqlpp avafepkpiv lgallahwgq kapaeiaakr
       61 tftyrhaqyr adklgiafrm ppahpfnpir plrlaiamgs tpdairrifr hiwrdshdvs
      121 tpdgfaalcd avgfpegvta vetqvvkdal rantdqaiad gvfgvptfal dgdlfwgdda
      181 tdmfvdcats rawldspevr risalpegir rg
//
LOCUS       WP_175801349             415 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175801349
VERSION     WP_175801349.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10396284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..415
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=43507
     Region          1..261
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Site            order(7,9..10,12,31..33,66..68,104..106,116,120,139..142)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187535"
     Site            order(82,106,116,120)
                     /site_type="active"
                     /db_xref="CDD:187535"
     Region          308..407
                     /region_name="DoxX_3"
                     /note="DoxX-like family; pfam13781"
                     /db_xref="CDD:463982"
ORIGIN      
        1 mnilvcgang figralgarl eagghrvlrg vrraadprdl eidfakdgda dawlprlegv
       61 dvvinavgil agrrgatlda vhraapcalf taccragvrr viqisalgve rgdtpyfask
      121 yaadrflqtl plesrivrpa lvygasgtsa rffrmlaslp vhvlpagghq rlrpvhvddl
      181 aelvarlvda paagerviea vgadeveyrd mlggyraalg fppaarialp gllvgaaatl
      241 sgaipgamlt rdtwtmlrgg ntgdpaaita vlgraprglr tfigadaavl rhdalamwrr
      301 plllgalaiv wiwtaivsaf vhprsdslam lahahltglp alialyaaca ldcafgvatv
      361 vapsrrlwaa qgalivaysa viavtmpall aepfgpvlkn vpilaillil fadee
//
LOCUS       WP_175801350             284 aa            linear   BCT 11-JAN-2025
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Burkholderia
            anthina].
ACCESSION   WP_175801350
VERSION     WP_175801350.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..284
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31518
     Region          1..137
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mssselvlyf dgrcplcaae irrlgaqdtr hrlafvdiae pgfdpaplgv dlsalnrelh
       61 arlpdgrmlt gmdsivaayt lvgrhglvwl lrapavrdvf aplyrrlarn ryvvsrwlgh
      121 haeahcdara cgigtaadrp arddvrrivv ngmyaaaivh llagaalpwv agaswfdayh
      181 rrielhfwaa tapdaaraqq iwwlslfgat lqcasvwmla lvhlgnrlrr revwgwllag
      241 lliwapqdml lswhaqvash vvadvaalva mvpplvwlwr rdta
//
LOCUS       WP_175801353             139 aa            linear   BCT 11-JAN-2025
DEFINITION  HIT family protein [Burkholderia anthina].
ACCESSION   WP_175801353
VERSION     WP_175801353.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..139
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=14810
     Region          5..136
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 msydnnnpfa kilrgelpcv kvaeddetia imdlmpqsdg hvlvipkepa aqifelsgea
       61 aaagirmtqr iaaavraalg pdgvfigqfn gaaagqtvph vhfhviprwe gvelrmhard
      121 iadaaalesv aqrirahlv
//
LOCUS       WP_175801367             221 aa            linear   BCT 11-JAN-2025
DEFINITION  O-methyltransferase [Burkholderia anthina].
ACCESSION   WP_175801367
VERSION     WP_175801367.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..221
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23736
     Region          65..219
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mttlihdpla sllarlfdea dasspashpd fadlthdeha rlmrsktgya dfyaslkdyp
       61 lavsretgtl lymlargsga raivefgtsf gistlhlaaa lrdngggrli tsefeaskva
      121 raqanlaaag lddlveireg dalrtlavdl pdtvdlllld gakalypeil arveprlrpg
      181 afvvadnaey spdylayvra prngylsvpf ggdvelsmri r
//
LOCUS       WP_175801403             323 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175801403
VERSION     WP_175801403.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..323
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35529
     Region          7..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..291
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(110..111,113..114,117,121,123..129,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176117"
ORIGIN      
        1 mrelnqrrlr yfhevlthgs irgaadsint apsvitrqir lleeevgvvl ferqargvrp
       61 teaaahlley wrgcrsqqel feerlqalrr lqsgqvrivt segyvdvlmd evltdfcmry
      121 pkldvivdvl pvnnvlqeva esrahiglay nppahaeiqy latssqpvva lvhaghplal
      181 rggavrahel geyplalmpp afglgqvaqm laytenlpir ptlttnslav lrhfvkrhdg
      241 itligafaay relesgelva lpiahplfds akarllvkag rplgvaadtl lncllhdmkm
      301 fagtgtrrap sgkgpraaar rar
//
LOCUS       WP_175801445             196 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia anthina].
ACCESSION   WP_175801445
VERSION     WP_175801445.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..196
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20102
     Region          4..190
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msdflfglmi alsvgpvalm ianygmragt asgvraavgv asadgcyava aftigamlas
       61 tlashlplfr cvgacvllam garmmwqalr drrrtldgaa pspgtrpfts mffvtlanpl
      121 tillfygyat aaagahrhwl agaacvfags lvgqlvfafg ggmigrivks prwlaashvv
      181 aalvvfgygv agivrv
//
LOCUS       WP_175801477             349 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia anthina].
ACCESSION   WP_175801477
VERSION     WP_175801477.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..349
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=38881
     Region          13..331
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mattharrrn dvprkpiala lqgggmhgaf twgvldrlle dgrltiegvs atsagamnaa
       61 vlayglekgg edgarqalhd fwqavarsae rynplrwvpw lkgthsfgld hsplyaftdm
      121 mlrvfspyqf npnnlnplre vlesqvdfda lrkhcpirly lcatnvetgk irlftgedvs
      181 adavlasacv ptlfqavtid geyywdggym gnpaiypliy ncvtrdvviv hinslvrrgl
      241 pitaaeilnr iseisfnssl mremraiafv tdliqqgkiq rgdmkemlih siraddalsa
      301 lsvsskynad wgflselrdh grreadawla hhygnigqrs sidvrrefl
//
LOCUS       WP_175801503             395 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175801503
VERSION     WP_175801503.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..395
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41127
     Region          22..389
                     /region_name="MFS_YajR_like"
                     /note="Escherichia coli inner membrane transport protein
                     YajR and similar multidrug-efflux transporters of the
                     Major Facilitator Superfamily; cd17472"
                     /db_xref="CDD:341025"
     Site            order(29..30,33..34,37,71,121..122,124..126,129,151,
                     154..155,158,221,224..225,228..230,233,260,264,308..309,
                     313,317,340,343..344,347..348,351)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341025"
ORIGIN      
        1 msnpsatssr msapelrata slaaifalrm lglfmimpvf svyaktipgg dnvllvglal
       61 gaygvtqsll yifygwasdk fgrkpviatg llifalgsfv aafahditwi ivgrviqgmg
      121 avssavlafi adltseqnrt kamamvggsi gmsfaiaivg apivfhwvgm sglfaivgvl
      181 silaigvvvw ivpnaakpvh vpapfaevlh nvellrlnfg vlvlhatqta lflvvprllv
      241 dgglpvashw kvylpvmgla fvmmvpaiiv aekrgkmkpv llggilaili gqlllgsaph
      301 tilmvaailf vyflgfnile asqpslvskl apgsrkgaat gvynttqsig lalggiaggw
      361 llkhggadtv flvcaglvav wlaiavgmkp pprrt
//
LOCUS       WP_175801523             140 aa            linear   BCT 11-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Burkholderia anthina].
ACCESSION   WP_175801523
VERSION     WP_175801523.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..140
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=14442
     Region          35..135
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mtfftnytnl aliailvvsg gllawpvlrr grgglsaaea tqlinrrnav vidvraasdf
       61 aaghlpsarq vaageigaki aqvaknkstp vllvcqngqq sqkaarevea agyaevhvle
      121 ggvaawqqag mpvvkqgvak
//
LOCUS       WP_175801542             408 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia anthina].
ACCESSION   WP_175801542
VERSION     WP_175801542.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..408
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43879
     Region          1..291
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mrlalvlmgg garaayqvgv lkalaeiare adphrhtlpf avvcgssaga inatsiasha
       61 ddfshgvrrl lefweplrad yvyrtdwlgi alagarwlaa mtfgwaarrs prglldnapl
      121 ahllqrelsf hrieqmlesr llhalsital syssgrhltf yqaaepiqaw rraqrtarlv
      181 dlsashllas saipfvfpav plvldgqiey fgdgsirqva plspaihfga drivvigaad
      241 prpeipagng sglvrgyptl aqigqqvlas vfldsigsdi eriehinrmi ehlphqvevd
      301 sgwrhvdvla iapserieli aakhlkqmpa tmrgllgaig gsqpagasfa syllfeeaft
      361 relielgyrd graqretlag wiaqadggsa aaagmspegg haagemrv
//
LOCUS       WP_175801571             163 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175801571
VERSION     WP_175801571.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..163
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17662
     Region          13..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mpkrlsppav asldatdrai laalaedari atselarqig lsapataerv rrleaqgvia
       61 gftveldpra lgytlqaivr vkplpgqlhl veevlrripe fvecdkvtgd dcficrlylr
      121 tiahlddila kvteraetst aivkstpvpr rlpplaedda ahr
//
LOCUS       WP_175801582             261 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia anthina].
ACCESSION   WP_175801582
VERSION     WP_175801582.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..261
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=27075
     Region          9..247
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 merkplvgit adltqigaha shtvgdkyva aivdgaqala mvlpalgdrq svddvletvd
       61 gllftgsysn vephlyggep stpgtkhdpa rdattlpllr aaiaagvpvl avcrgfqeln
      121 vvcggtlhqr vhdvpgladh redddapmdt qygpahavrl tpggvlhtla ggrddvhvns
      181 lhkqgiaqlg sglaveavap dglieavsvv dalafalavq whpewrhaqd plssaifraf
      241 gdacrarrda rtsataaaal a
//
LOCUS       WP_175801630             401 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175801630
VERSION     WP_175801630.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..401
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=42583
     Region          2..375
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mtkrilviga gfagmwsals aarlldeqgr idveitvvap dahlhvrprl yeegpanfra
       61 plgeifdavg vkfvqgtver idvtrrtvdv lgtnghastl dydrlvlaag srlfrpaipg
      121 laehafsvdq tdeaveleth iralarqpas marntvvvag ggftgietaa emptrlraal
      181 geetdvrvvi versdaigpd lgagprpvie ealrtlgvtw rlgsgvasvd aggvttadge
      241 riesstviwt aglrastlte qvpgrrdaag rlhvdrnlav dgvpgvyatg dvayaatddd
      301 gnhtmmscqh amnlgrsagh naaadllgle qipysqpkyv tcldlgpwga vytegwdrev
      361 klagaeakkl khqinsewiy ppradraeal aaadplrivv a
//
LOCUS       WP_175801622             295 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175801622
VERSION     WP_175801622.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..295
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31510
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mlldnlvlfl rivekgglaa agrevglspa tvserlaale syygaalltr ttraisltde
       61 grtlvagarr llaeadeles rvrlgaqtls gpvrlsapad lgqarvvpvv daflaehpgv
      121 tvalhlgdgy vdlvgqgldf airrgtlads alrsrslgrs rrvvcaapay laahgtprhp
      181 delaahdciv mrfgqelyae wpfridadlk rvmvrgrrva ndgalvrawc vaghgialkl
      241 lldveqdlas galveilrdf spgevdlqiv ypgagvqprr vralierlth altta
//
LOCUS       WP_175801633             456 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia anthina].
ACCESSION   WP_175801633
VERSION     WP_175801633.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..456
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47569
     Region          212..411
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mrfdlclrla rergrcaprg airlpnrral lrgivaaawl agaqgavaqa ssgaapftpa
       61 vaqaadlfdv pffnsartvw ggllasttvp rivhapdaag artddrpraf vvragacapy
      121 ivlcdaarda ierdyagrfd ygfasslpai gvpfafasrd aglasaepfm laepaggarv
      181 gaiagslras laranlpagv saqvtrmlad rldlkqqgav gdtfrvafep addaslsgdp
      241 rvtaldirfr gqrvaavwfa adarspgayy dldgvplagt rfaqpvgatr tssrfgtrvh
      301 pvtgarhvhs gvdlaaptgr tvrasergvv sfigtepggy gkyvvvrhdg gyasyyahls
      361 afeptlrtgm riargqrvga vgstgtatgp hlhfevrrhn rpvdpvalvq aakadvlkgp
      421 qrvafervak gartqlasaa wsqpmaaaqr gaspag
//
LOCUS       WP_175801657             948 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia anthina].
ACCESSION   WP_175801657
VERSION     WP_175801657.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 948)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 948)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..948
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=103108
     Region          14..825
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mdahsmigti tgglaqrerl lkldtplgsn vliphrvlgq srigrdylfm idcvstsndv
       61 qlkalisqpi tlwiqqtdkt ylphhgyvht arklgvdggl acyqlsfssw lhflkfrrdq
      121 rhwqdksvda ivtdvfndhp qargmyrfel sqplpsrsyc rqdetdwnfv hrllesegly
      181 giwqqaqdgk shtlvitdhl qtleplapat vdfsrasaqg evdaftqwag trtlqsvlls
      241 trtfdyknps tpanpkatsv ptmanqgdlp sqtevyeytg gytypeqerg dhlgkirmee
      301 wesrakrydg vggvrridag rrftltghpe hdqdaadhre favievewii vnnvplsghe
      361 anyphslyqa vkqadaddte ksfavphidg stgfyriaie aqrtsapyhs plehgkpeak
      421 lesaivagpk gqqaytddln rikvlfiwdr hnegderasc wvrvaqsdtg dgyggvhmpr
      481 ageellighi gndidrpial hrvyngtskp rwhsnallsg yrsqefsgsg ynqmvmddst
      541 gqnrvhlyss stnaalhlgy lvdqtdnarg sylgrgfdls seaygalrag rgllvtthpv
      601 asqpldasla arqlngsanv ldglsqaset skaeslkdgh dafkafaeat qhnesgaasg
      661 ggvtagggtg nagaftrpvi lvaapagigl stqqsthvaa dqhvnivsgq sthvatgksl
      721 vasiteklsl fvqnagmklf aakgkievqt hadnvevtaq kslllasvte kvqasaqqei
      781 lltsggayir lkggdieiha pgkidikgaq hafsgpaqmd vtnpafkdlp trrlmlntma
      841 spsatsvvpv gmpyklyadg alvkqgvfdk tgqlpidhqv ttqkytlema ngvkheipvp
      901 geyrdaangk lanqgfqfhe gspdngdapd ravhrqlysd llnsasda
//
LOCUS       WP_175801661             327 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Burkholderia anthina].
ACCESSION   WP_175801661
VERSION     WP_175801661.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..327
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38330
     Region          99..255
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mpaewmtwlq afmghdvdwk qvlligmtpv fliafmiefa iatrrgrreq frwkeivanl
       61 slgagyqvae tvmgilftga ifawvyrhrl fdvpvngwti vpifvvvefc yywfhrtshr
      121 vrwfwaahvp hhsgevmnft tamrqsllna fvgvfvfylp pvwlgippav vlfllavdla
      181 yqyfvhteai grlprwfeyv fdtpsnhrah hgrnpryidr nyggvliifd rmfgtyveet
      241 epvdygitqq irsynflvln lhefvdmwrd vfapgpfaqr irhlwmppew erpghrpiht
      301 wsverkgdge ddtvevgdva dvvehra
//
LOCUS       WP_175801672             235 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175801672
VERSION     WP_175801672.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..235
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26192
     Region          20..>175
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mskeaveteg ggrrhggryv yeelrkqilt lklkpgvqld eislaaqfgl srspvrdaia
       61 rlsseglvtv lpnrttlvtp feieefpkyi saldliqrav trlaatqrsd adlakirkad
      121 dvymeavasg dfqamsetnk alhmaiahaa nnpyfigyye rllgegqrll hlhfdftvss
      181 ptaaklgrdh delidaiarr dadaaeraah ehtmlfqkrf ldymkqnmte smavl
//
LOCUS       WP_175801713             521 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175801713
VERSION     WP_175801713.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..521
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=55454
     Region          1..521
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 metydhivvg ggsagctvah rlvkagkrvl lledgpkdds lfiripatfi rvlgtqrtvt
       61 fesepqagaa grktyvpqgr tlgggssvna mlyvrgtrad ydewaalgca gwgwndvlpv
      121 fkraeshlrl sepfhgtdgp lkvgdtrfrh plslafvkaa qeagiayndd fngaaqhgag
      181 fyhttifdgq rgstaatyla dvlghanlrv ltgcrvtrvr fdgrratgve wraesgatgs
      241 aaaradvvla agalstpkll mlsgigpgah lhahgidvlh dspevganyq dhlevsiygy
      301 shapislfge drglkalrhg aqwmlcrtgl ltsnvvesga fvdttgegrp diqfhvlptl
      361 vgdvdreplp ghglsinpcl lrprsrgsvq lrgndpaapi rfdsgalsdp advdglvrgv
      421 alarqilrap slarvvreae tltddalady vrhraktvyh pagtcrmgsd enavvtprla
      481 vqgidglric dasvmprivs gntnaptimi aercaefmla d
//
LOCUS       WP_175801681             424 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175801681
VERSION     WP_175801681.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..424
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46301
     Region          9..403
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(21..22,25..26,29,61,111..112,114..116,119,139,
                     142..143,146,228,231..232,235..237,240,268,272,330..331,
                     335,339,354,357..358,361..362,365)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mklfratsiv lvmlcvmyfi tyldrvnvst aaagfsrefg lnrteiglvf safaypylvf
       61 qiiggwvsdr fgarrtllac gllwavatll tgmagglmsl laarlllglg egatfpaats
      121 amsrwvprek rgfaqgitha fsrvgnavap aavvaviavy gwresfyicg visivwvaiw
      181 alvytehpkd hpritqaeld alpppkqkpa tvpwgplfrr mmpvtivyfc ygwtlwlfls
      241 wipqyflhsy dldlkksaif asavffagvi gdtlgglvtd riltrtgslk rarswmvsic
      301 mlltllallp llfthhlyvs maclaagfff aemtigpmwa vpmdiapehs gtasgmmnsg
      361 salaailspv isgyvidrfg swelpfigsm vlmgvgvlla frmqpdsrft essteqpaak
      421 rspa
//
LOCUS       WP_175801727             401 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Burkholderia
            anthina].
ACCESSION   WP_175801727
VERSION     WP_175801727.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..401
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43288
     Region          1..400
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(99..101,125,175,207,236,238..239,247)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(102,135,200,245..247,276,279)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            239
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mniiadrigq iapaetmama araaelrrag lnvislsqge pdfptpeniq eaairamrsg
       61 ktryteaagi pelreaiaak landngliyp vagisvssga kqaifaaffa slnvgdeviv
      121 ptpcwvsype ivkmsggtpv cvpcpetagf kltaaqleaa mtprtkwlml nspsnptgav
      181 ysrdelasla dvlrrhphvw vlsddiyekl iyadtpfsni lnvapdlyer tllvngvskv
      241 yamtgwrigy aagptqlika mnlvqgqivt satsiaqyas vealtgnqaf vetsrrafnq
      301 rrkqvvealr ripglqcrep egafyafvgc qeligrhtls garigndqdf vrylldeakv
      361 avvsgtgfll spyfrlsyaa sveqleealq rieaacakll a
//
LOCUS       WP_175801756             213 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175801756
VERSION     WP_175801756.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..213
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23343
     Region          24..181
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtdrtstrtt ttqddapagk tprtkpaevr leelmaaaet lflaqgvdat tiseivehaq
       61 vakgtfyhyf esksdmlaal aqrytasfle rlqqavdaca egdwlgrlrv wirtnietya
      121 atyrthdivy anhhhhdrtn adrnaiveql raileggaqa gawrlahptv talliyagvh
      181 gatdhiiaap dtdratfiea ivadclrmlg ida
//
LOCUS       WP_175801804             515 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia anthina].
ACCESSION   WP_175801804
VERSION     WP_175801804.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..515
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52158
     Region          91..494
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrvpeppaas laaaalatav altgcatssi dlapeapdrp wqpqtsaagd ivpappqasa
       61 sraphdytlp aspalasvpp paaldaahpy tlpelidlae ttnpltriaw ndarnaalav
      121 giakaaylpn lsatamgayq tshgststil gdassnstvh gtisalslqw llfdfggraa
      181 rveaaeqasv asnvaftavh qqvihdvtva yyryeaarsr aasaqqglvn adailaasra
      241 rlkhgvgtvv elaqatqnra qanlalvqan gaqsdsylal vaalgispls kptiaalpkr
      301 plppalassv daivsdaiar rpdlqgayal eqanrakika aeaafmpkif lsastsyasg
      361 gtaisalpai gdqaptvnln gsrygggvfl gvtiplydgg lrsavlmqar ndaqsasarl
      421 trtkeeavrq vvaaqnavqt slashdaaka lvdaaqtsyd aaltayrngv gsvtdatiaq
      481 sqllaarnae vdsyagalsa aaalalatgt igssq
//
LOCUS       WP_175801820             144 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia anthina].
ACCESSION   WP_175801820
VERSION     WP_175801820.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..144
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15882
     Region          1..143
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mlkllvpvgh sprslqavrh atflyrerca seivlinvqa pleatrleaf hplsrlrsie
       61 ekfacddlav aeqilreagv rysvvkkvgp vvdtiatvaa etgcdeivvv aprhdpfhtl
      121 lsmfrrsmma rlvrisnvpv tavq
//
LOCUS       WP_175801830             277 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175801830
VERSION     WP_175801830.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..277
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30229
     Region          19..239
                     /region_name="HTH_MerR-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     transcription regulators from the MerR superfamily;
                     cd04778"
                     /db_xref="CDD:133405"
     Site            order(21..23,37,53..55)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133405"
     Site            order(67,70,74..75,84,105,109,115,119,122..123)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133405"
ORIGIN      
        1 mskqtpthtd eaaadsrney tvdelarvsd ttvrnvrayq drgllappek rgrvgiyddt
       61 hvarlklinh llargytlsn iqdlimaide ghdlrsilgl enaiggrwsh elpktyslaa
      121 laqmfgpqta sqlsrvtelg llerrglsfv akspalleaa aamtkegipp relldvisla
      181 rphfdaiarl lvdlvvkrld rydegtlppv ndvpalvdai wrlrplaavf vegetnrale
      241 taasaylggr vatildkkls deaarqsgtp apkdder
//
LOCUS       WP_175801871             676 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia anthina].
ACCESSION   WP_175801871
VERSION     WP_175801871.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..676
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=70801
     Region          30..560
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mkfalpslpp fatvrtalrd awptlppgal gfalrntaas llalyiafrm nlddpkwaas
       61 tvwivaqgsr gmglsksqyr ilgtaigaav alaltgafaq tpelflpala vwiglcagva
      121 tflrnfraya avlagytaai ismdavsapq hafdiatarf lyvvvgilcg aafetvfapg
      181 splrdvrarl arylaravtv gaealrrepn gaavhrlfad avdldtaaey aaagappvrn
      241 aighlraavl gvlsahaagq ainahaarsg dvpdplvaaa arvldgvaas geagpdlaal
      301 rarvddalra eaaepagsda srlltldrld allagfdray askaqidlpv pppsrvryaf
      361 hrdavlafhn gmrafiavlv asaiwivtaw psgagfvait avvgalfstr pnsaraamgf
      421 lkgaacaava gvvcnfvllp avsgfemlay iigvfmigtg valrhprtaa lgsafsiffw
      481 nftspdntar igdaaflnsa lstllgiafg vlvfalvfpg dpgtsrrrlh ravrrdltei
      541 arnpggwsas awlsrtadrl rcelgfaggl phtlierdmr dllaiwgigd sllslaelaa
      601 repaarraaa vvrgrvarad farlerscda aarllrrhva didsdggral lrgivllrri
      661 adaaaehggf lrgrrd
//
LOCUS       WP_175801857             246 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Burkholderia].
ACCESSION   WP_175801857
VERSION     WP_175801857.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..246
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25345
     Region          10..239
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; pfam01925"
                     /db_xref="CDD:460386"
ORIGIN      
        1 mhlhtltiiv lvfllagavk gmiglglpti amglltlamp psaaaslllv psfitnvwql
       61 wlgpsfgpll rrlwpllvgl tigtltgglp alaagnawth aalgvvliay gcwglaaarl
      121 papgrhekwl savvgyltgv vtaatgvfvv pavpylqalr lskddliqal glsftastia
      181 lglqlrvtga lqtvdlgvsa lalvpalagm iggqyarrvm sekafkrcff vgmvalgaym
      241 aasglr
//
LOCUS       WP_175801884             554 aa            linear   BCT 11-JAN-2025
DEFINITION  S8 family peptidase [Burkholderia anthina].
ACCESSION   WP_175801884
VERSION     WP_175801884.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..554
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55462
     Region          242..521
                     /region_name="Peptidases_S8_13"
                     /note="Peptidase S8 family domain, uncharacterized
                     subfamily 13; cd07496"
                     /db_xref="CDD:173820"
     Site            order(249,317,321,388..390,416,418..419,489)
                     /site_type="active"
                     /db_xref="CDD:173820"
     Site            order(249,317,489)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173820"
ORIGIN      
        1 mrakrfnsar vrsthtrvla gllsaavlvp lascgggggd gsnpsssnaa paptptpapt
       61 pspspttppa tsgsnacatq qaavqmaaqt aapaeppvdh livklktlta aramaavdtg
      121 trldaviqrs mtrwnaptas gaarayaaat tsqapldvqv ertlsngaav lsigqriaag
      181 daaalaqafa adsdvdyaep dhpmqirdtp sdpdysqqwn lfdpaagidv ppawtrtkgs
      241 ptvvtavldt gyrphpdlvg nllpgynfis nintsnngqt rsgdatdpgd wvtqqeldda
      301 sgpyyrcase pstsswhgtr vmgvigatan ngigiagvsw lgrilpvrvl gkcggvtsdi
      361 adamrwaagi pvngvptnpt pakiinlslg gvgacsatfq qaiddvnakg vtvvvaagnd
      421 glstgldqpa ncrgvisvga tdaagrrasf snfgtdvals apgvnilsta nngtttpgad
      481 tygtasgtsf atpqvagvaa lmlavngnlt paqiqqklqg garaallpts tsctalpags
      541 gildagaavt assq
//
LOCUS       WP_175801930             500 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia anthina].
ACCESSION   WP_175801930
VERSION     WP_175801930.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..500
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=54222
     Region          12..500
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mpapaeeppp atadgpripv safaiegnaa ipatrldpll adlvgrdlsf gdlqqaasrv
       61 ttyyrehgyv laraylprqd iehgvvriav vegrygqiel hnrsrvldra lrqplaslqp
      121 geiahgnrle rslmllneip gvdakgtlrp gaepgttdlv idaersrfat gsieldnfgd
      181 pltgryratg svdvnaplrv gdrfslrglt sntnqryfrt syqlpvgpas trvgvaysdm
      241 nyriggslkd lrfhggadvr safvtqpllr srrtnldaqv vyenkhlrdv ygafdvvtdk
      301 tvdlwsfgvs gnhqdtfggg grsgfsatlg ighlsgndpl dmdyyvhtqg qfaklnvsal
      361 rlqalgsrfq lytqfsaqls srnldasekf slggpygvra falgagsgdq gwqataelry
      421 laapslqlsv fadtgriqls kqrwsrernt vqlsslgiga swfgarhqin ltaalpvgya
      481 dpvasptrsp svwlqaaqyf
//
LOCUS       WP_175801942             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175801942
VERSION     WP_175801942.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33528
     Region          6..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mlrtglgelt tfitiaeqrs fsgaarilgv spsalshair hlearlgvrl fnrttrsval
       61 teageqlllr vrpavadled amndaatarn rpsgqirisa sesaaqplir hvlpgfvary
      121 pdihvefivd srlidivehg fdagirvred vprdmiavry gdavrfvava spdylsrhpa
      181 patpqdlphh rcirfrfesg aryrwdltrd gkrvsvdvdg pmtlgnlslm veaalagigi
      241 awvtqsrvae hlaagrlvrv lpeweqafds lclyypanrh pptalrlfve avrewaagag
      301 dalhd
//
LOCUS       WP_175801944             196 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia anthina].
ACCESSION   WP_175801944
VERSION     WP_175801944.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008163
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..196
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=20981
     Region          2..191
                     /region_name="COG3963"
                     /note="Phosphatidylethanolamine N-methyltransferase [Lipid
                     transport and metabolism]"
                     /db_xref="CDD:443163"
ORIGIN      
        1 mtwpnalrvs alfvrewvgr pasvgalcps srqlaremae avpdgdglvv elgggtgavt
       61 aallergiap qrlvvversp afvrhlrtrf pgitivsgda rqlerllppa arvdaivscl
      121 plrtlprdav taiveqcrrv lsddgamiqf tydlrppdrh plgnsglaaa dsrivwanip
      181 parivtmrra evgqta
//
LOCUS       WP_175801985             517 aa            linear   BCT 11-JAN-2025
DEFINITION  S41 family peptidase [Burkholderia anthina].
ACCESSION   WP_175801985
VERSION     WP_175801985.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..517
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55228
     Region          69..433
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mmpatrvvrr ivawstgaaa aaafvacasa araqsasaat ttlppasppa aasqpspcpp
       61 dwepqlcelk aavevlkkqh ltdvdigall datvhdgikt lpyarffnak erqqqldder
      121 rardgtpgig ivfetrpdgl hiidvipdap aeqagvrpdd lvvamngqsv vgidssdvvk
      181 lakgdagmpl kltvrrgpda amltftpvra ivrphpatak rldgdilytr lssfpepavg
      241 syidavqaar rtgppvkgvi ldlringgga lnaaigital fagrdrtamv tlerdgtkrr
      301 rfttnwpdye lpvmhgqdpl aplqaddwwh tvplvvlvdg qsasaaeata aalkdlgrar
      361 llgmptygkg laqtgvdlid gtrlnftfar nlrpngcpmd gygvvpdwlv pprrdsdvdg
      421 vllwyrevdl arapyadrla pdpfaqvrta rqklrdarar akvdtsksaa lpqrafgtaa
      481 dwqlrqalda lagrpvqtid ppaqlmparp vcergdg
//
LOCUS       WP_175802146             137 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175802146
VERSION     WP_175802146.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..137
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15348
     Region          19..>94
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(20..22,36,53..55)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mtttvekvvl ppipakryft igevselcgv kphvlryweq eftqlrpvkr rgnrryyqhh
       61 evllirrire llyeqgftin garnrldspg servaaapad peapaadvra pgkpgttvdv
      121 valrqalldv ldglkhd
//
LOCUS       WP_175802231             330 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia anthina].
ACCESSION   WP_175802231
VERSION     WP_175802231.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..330
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=36043
     Region          116..328
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 myspmiwala iamlcvasal mlwrhaetrr vrtdakrfid srlepgvraa aqvarpvatg
       61 gartaplpgg aqsvtsrafw vhwyavtsey lgnlvsragi egargkaiaa iivlvaivsi
      121 agsrggllag faalacgsti fgvwltsriq rrrlkivrqi psfldgivrl vtlgnsvpaa
      181 fqsallttee plrgcldhvs rmlrtgveid ramlhiakiy raeefellgs vlrlsvkygg
      241 radvmlerma vfmrdleqae reltamsaet rlsafvlvml piaigsfvvm tnpsylagmw
      301 ndssgrlllm faflmqlags vwlyrmarlr
//
LOCUS       WP_175802150             557 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Burkholderia anthina].
ACCESSION   WP_175802150
VERSION     WP_175802150.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60362
     Region          25..356
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          453..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mtpaslieqy gpresmeydv vivgggpagl saairlkqla aekgaeigvc vlekgseiga
       61 hilsgavmdp raitelfpdw kergapltvd vtedrflfls eksavqtpnw alpanfqnhg
      121 nyvislgnvt rwlgaqaeal gveifpgfpa aeilynddgs vkgvatgnmg vgkdgepten
      181 fqlgmelhak ytlfaegcrg nlgrqliskf kldanadpqa ygigikelwe idpakhkpgl
      241 vihtagwplk sdtyggsfly hmdnnqvvvg fvvglgytnp ylspfeefqr ykthpsiraf
      301 leggkrvsyg araitaggll slpktvfpgg aligddagfl nasrikgsha aiktgmlaad
      361 aafdalqagr qsdelnaypd afkqswlhte lyrarnfkqw makglylgtl mvgleqkvmg
      421 gnvpwtlhhk hadhemlkpa sqctpieypk pdgkltfdrl ssvfisntnh eenqpahltl
      481 kdasvpvnvn lrtyagpegr fcpaavyefv knddgsdrlv inaqncvhck tcdikdptqn
      541 ivwvtpeggg gpnypnm
//
LOCUS       WP_175802235             747 aa            linear   BCT 11-JAN-2025
DEFINITION  LPS-assembly protein LptD [Burkholderia anthina].
ACCESSION   WP_175802235
VERSION     WP_175802235.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..747
                     /product="LPS-assembly protein LptD"
                     /GO_process="GO:0015920 - lipopolysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=82087
     Region          37..719
                     /region_name="LptD"
                     /note="LPS assembly outer membrane protein LptD (organic
                     solvent tolerance protein OstA) [Cell
                     wall/membrane/envelope biogenesis]; COG1452"
                     /db_xref="CDD:441061"
ORIGIN      
        1 mpwcaahaqr dladdwalrp ateltdhata pehrpattai gdsatsttdt dlslkghael
       61 rrdrsivkgd avhyafdtdt adayghvvla ddgrlffgpe ahfridarqg yivtpkyrft
      121 lnggrgsaqr idvadearti vehgtyttca cgdrpawymk asrfdidsgs dtgvahdgvl
      181 ffqgvpifas pwlsfplsga rrtgllpptl sfdstnglva tqpvyvnlap nydltltpry
      241 mqrrgtmlga dyrylgaays gelaaaylpg drltgtnrys lhvkhdwnlg ngfgfylygd
      301 rvsdsaaaae lassgtaass tlyrqeaglt yakapwsvlf rvqhwqsfss stvyasepql
      361 nvryarynvg gfdfgmetda trfrstvsga tqgnrfvldp yvaysverpg wfftpklkwh
      421 fasydltsig sdapsgqpkr fdvnvptlsv dtglrfergv slfghaylqt leprlyyvyt
      481 pyrnqndapl fdttvtdfgi gelftdntfv ghdrvadanr vtaaltsrli epstgderar
      541 vvlaqqydfr aprvtllesd aastvartgl vlgasyrigd giqanqavqy deihdylrra
      601 sigfgwspge rrvlnlsyry nraidyssss edvepirqav lsaqwplarn lsgvarlnyd
      661 ldthrlltgl vgieydadcw slgvaaekyl yatssttyha gsrimlqlql kglgtadsgl
      721 srefaaavpg ytaaaqkapg drftdyp
//
LOCUS       WP_175802245             200 aa            linear   BCT 11-JAN-2025
DEFINITION  YbhB/YbcL family Raf kinase inhibitor-like protein [Burkholderia
            anthina].
ACCESSION   WP_175802245
VERSION     WP_175802245.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..200
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=20976
     Region          43..199
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mrvdrritsp apsgrppafi aallcvavcg afvirparae gpftvssddl tpggrvglan
       61 vfdrgdckgd nhspqltwrn ppagtrgyav tifdpdapgh gwwhwavagi pstvtslpad
      121 asasgflrri gasearndfg tdgyggpcpp pgkphryvit vyalkgtdlr vaqgrpapmf
      181 eheigtltig taqltvtygq
//
LOCUS       WP_175802039             379 aa            linear   BCT 11-JAN-2025
DEFINITION  YncE family protein [Burkholderia anthina].
ACCESSION   WP_175802039
VERSION     WP_175802039.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..379
                     /product="YncE family protein"
                     /calculated_mol_wt=39126
     Region          <35..225
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          50..84
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          92..133
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          131..351
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mrvdfksrvl hravlavala mlaadvvaqa apekadapaa iavgngpagi afgpdgkrly
       61 vtsngdnsva vidvaagqrv rdfgappaka pndgcpdnfc rgtgatgiai aaderhayvs
      121 smradslarl dldsghvdgv akvqrfpqav avspdgtray vlnvvansvs ivdldtfrtl
      181 gkpialgggn agnqpfgrpa alvlsrdgqr lfvtngmass idafdtqtra qvgtipdada
      241 ydlavepgsg dlvalfrdgi aaydantlrp rqaaqycrgl tsynfalspd gravafslpq
      301 entvlvvdra tgmlraayrs gewplalafs pdgsrlavln asqsgsvslf dareagtlsd
      361 yvaasgelfc rpaaedasq
//
LOCUS       WP_175802292             226 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175802292
VERSION     WP_175802292.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..226
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24171
     Region          29..187
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpprhvqvpa ppgqsavqpa palrrrprqs raqatsdalq qafvqlller gyakatirei
       61 aavagvsigt fyeyfgdkqs laalcihrrv laladrlrda ahglrgapra elaaalvdlq
      121 ldaigadaal wsalfalerq vsplvayrrh ydayvalwrd alaqaadppp aerldrlarm
      181 ahtvcyggvs qalltlgpal dfgvlrgelh tllraylaag dspssa
//
LOCUS       WP_175802294             502 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Burkholderia
            anthina].
ACCESSION   WP_175802294
VERSION     WP_175802294.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..502
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=53792
     Region          3..498
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mnlvaaldra aratpdkpfl ihddttitya aarershraa avlsalgvaa gdrvaamcln
       61 tpafvdlmfg awrlgaafvp vnhklqapev dyllehsgsk vilfdaalap vlsrvihpar
      121 rlvtegsadg vpdfdamraa mdgiagiepa dgdvaqvlyt sgttgrpkgc vhshrtvtfa
      181 amaaalatgi grnertlmam piwhssplnn wfggtlyagg tvvllreyhp lrflqaiere
      241 rvtlyfgapv sytlpldtid rfaafdlssv rawlygggpi gaaqaerlar ayrsnaffqv
      301 ygmtetgpag ttlypdeqia kagsigrqgg pgvdlrvvrs ngadalpgdt geiwlkadsm
      361 mlgyldddta traafapggw yrtgdiarid qdgylfivdr lkdmivtgge nvyskevedv
      421 lgahpgiaea avvgvphpdw getvvahvvl ragtapdada lrafcgerla aykiprefvf
      481 aetlprtptg klqkfllrvr re
//
LOCUS       WP_175802283             540 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175802283
VERSION     WP_175802283.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 540)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..540
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54093
     Region          23..449
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,279,282..283,286..288,291,319,323,375..376,
                     380,384,400,403..404,407..408,411)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mdqpfsaast qsarrrawvl aavcmaaval plsfsggava tpaigrdlhg gpvamnwitn
       61 afmlafgscl maagaladqf grkrvfaigv ggftlmsval afapsmlavd llraaqglaa
      121 aaalaggtaa laqefdgaar trafsllgtt fgiglafgpv lagcliahyg wraifvtgav
      181 agalslgvgl prmhesrdph atgldwpgta afttaltlft fgvieaparg wadplvaall
      241 agaalgaaaf vaietrvarp mldlslfria rfvgvqvlpv stcccyivll vvlplrfigi
      301 dgfseidagw lmlaisapml vvplvaatlt rwlspgvisg iglliaaagl vwlgialrgg
      361 agpaaiapml aigvgagmpw glmdglsvsv vpkeragmat gifsttrvag egialaivga
      421 vlaalahadl sqaaagtsga adttlraaar latgdlagaa vvlpgvghaa llasythafd
      481 rlliglavvt vlcagvvfaf lgaraveada daqedagahp hvdasvrcrt dadcaetsgr
//
LOCUS       WP_175802370             294 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175802370
VERSION     WP_175802370.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..294
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32730
     Region          27..178
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <173..286
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mrrendslae lqalirrhav sgesgtafpg lilsaytlpt qpelhwaepa faliaqgakd
       61 vvlgdevyry atgqylvysv dlplssrvvs asqkepvlgl gfrlnadkva allleaglqp
      121 kdrgrqrsia vsnvddalld pvvrllrlld hpkdlfmlad aiereilwrl ingeqgalvr
      181 qlgfadgrtm qisraikwir vnyarvlriq eladvacmsv tsfhrhfaav tslspiqfqr
      241 qvrlqvartl llssaktvad iglevgydsp sqfsreyrrq fgrpprvdgd flkr
//
LOCUS       WP_175802387             304 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia
            cepacia complex].
ACCESSION   WP_175802387
VERSION     WP_175802387.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33211
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdrfdsmraf arvvelgsft raanslnlqk ttvsaqisal erglgvrlln rttrsvtatp
       61 eggiyyervv sllsdldeae aavttskvep kgrlridmpp aighrivipa lgsfierypg
      121 ivlevgctdr pvdlvgegid cvirgnlihd eglvaralgv fdiatcaspa ylekygtpat
      181 pmemenhlvc rlfspknrrf fefnftkngv rtnvkgrhva ayndiesslt galsglgivq
      241 lplyileehl atgrltrilt dytsegvpvn llypenrmls akvkafasws rdlfastkhv
      301 nvaa
//
LOCUS       WP_175802397             426 aa            linear   BCT 11-JAN-2025
DEFINITION  TniQ family protein [Burkholderia anthina].
ACCESSION   WP_175802397
VERSION     WP_175802397.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Li,Z., Zhang,H., Xiao,R. and Chang,L.
  TITLE     Cryo-EM structure of a type I-F CRISPR RNA guided surveillance
            complex bound to transposition protein TniQ
  JOURNAL   Cell Res 30 (2), 179-181 (2020)
   PUBMED   31900425
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Kholodii,G.Y., Mindlin,S.Z., Bass,I.A., Yurieva,O.V.,
            Minakhina,S.V. and Nikiforov,V.G.
  TITLE     Four genes, two ends, and a res region are involved in
            transposition of Tn5053: a paradigm for a novel family of
            transposons carrying either a mer operon or an integron
  JOURNAL   Mol Microbiol 17 (6), 1189-1200 (1995)
   PUBMED   8594337
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10534787
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..426
                     /product="TniQ family protein"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=47756
     Region          17..152
                     /region_name="TniQ"
                     /note="pfam06527"
                     /db_xref="CDD:461938"
ORIGIN      
        1 mynppitars vlnpvtplgv gtreveslis yfcrlalshc ittgdlarki aciedwnlnp
       61 kwnsisvsls gmgdsaekws raisemtaie crntltllpw seviakpsli stsprlcptc
      121 faddhargkt pytrlawdig ivvacarhrt kliqacpdcg htgtrhrsay vvpgwctkcg
      181 aflgnttdqr patpeetwia sqvgdmlarq atlniipsre vlldcirnli ahlddgnyas
      241 farrigssks tvhywvqkev vpplptllri afqtgldlhk lltgdlsdws lacaenrift
      301 lslllrkara sqvadrnefi lsylkiikes pepvsvleva rqlktdsrrl yrianedtra
      361 igerwkqlcr eraeqhrnia rraiegvyfe ilaegkcvnl relrrripnn ilarisnvfs
      421 llndvk
//
LOCUS       WP_175802498             319 aa            linear   BCT 11-JAN-2025
DEFINITION  complex I NDUFA9 subunit family protein [Burkholderia anthina].
ACCESSION   WP_175802498
VERSION     WP_175802498.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Parey,K., Wirth,C., Vonck,J. and Zickermann,V.
  TITLE     Respiratory complex I - structure, mechanism and evolution
  JOURNAL   Curr Opin Struct Biol 63, 1-9 (2020)
   PUBMED   32058886
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Babot,M., Birch,A., Labarbuta,P. and Galkin,A.
  TITLE     Characterisation of the active/de-active transition of
            mitochondrial complex I
  JOURNAL   Biochim Biophys Acta 1837 (7), 1083-1092 (2014)
   PUBMED   24569053
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..319
                     /product="complex I NDUFA9 subunit family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0010257 - NADH dehydrogenase complex
                     assembly [Evidence IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=33788
     Region          5..278
                     /region_name="NDUFA9_like_SDR_a"
                     /note="NADH dehydrogenase (ubiquinone) 1 alpha subcomplex,
                     subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs;
                     cd05271"
                     /db_xref="CDD:187579"
     Site            order(10,12..15,34..36,74..76,93,116..118,129,133,
                     156..159)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187579"
     Site            order(129,133)
                     /site_type="active"
                     /db_xref="CDD:187579"
ORIGIN      
        1 mdgqtvallg gtgfigsrlv nalidagkqv rigtrrreha rhlqmlpvei veldaldtrt
       61 larfvagaha ainlvgvlhg grgapygpgf erahvalpaa laaacievgv rrvlhmsalg
      121 adshgasmyq rskgdgeaal havaatdsla ltifrpsvvf gpgdaflntf aklqrtvpvl
      181 plampdarfq pvfvgdvvra fvntldlaaa hgktyelggp tvytleqlvr ycgtlvgrqa
      241 rivrlpdala rlqarvfesl pgepvltrdn lasmsvpnvl sgplapelgl spaslesiap
      301 aylgnaaqrs rfdwfrsrr
//
LOCUS       WP_175802449             465 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia anthina].
ACCESSION   WP_175802449
VERSION     WP_175802449.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..465
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49967
     Region          2..451
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mpiqtehdpr lkralktrhi smlalggvig aglfvgssav iastgpaafi tygitgvivg
       61 limrmlgema aahpmkgsfv dyarmaygdl agfstgwlyw yfwvivvgfe avvggqiing
      121 wlpqlpvwai slglmivmts vnqlsvnsfg eaeywfagik vaaivvflvi agayvfrlwp
      181 gstarfsnlt ahggflphgt ltlfsgvvsv ifsmtgveva tiaaaesdhp arnirravnt
      241 vmarilvffv lstffivvaq pwtdivpgks pfvatlekig ipgaatmlta vilvavlsvl
      301 naglytssrl lfvlstnhea pkwlsktssr gvprlgvlas tlvgygcvvi aalwpdtvfq
      361 fllnssgavf lfvylmicls qlklrkrwer egtlkfrmwl hpwlplavtc sivavlasma
      421 ldpatrlslv qcliaiaviv vtygvlklvr agrpqpaaht rpvge
//
LOCUS       WP_175802435             279 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175802435
VERSION     WP_175802435.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..279
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30241
     Region          16..271
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mnpdtpdttg tlsdddtylv palerglril elfnardpml tpnliaqrlg lprttalrlv
       61 qtlqtlgyle ranrdrdvrl garvmklgfd ylsslaltdi gtpvierlrd atgfashlvv
      121 rdgrdvvfva kawthdsvms aikvnigtri pahasvhghv llgdldqtel dalfpepmlp
      181 tytphtprta aevharaqky aadgyalses sfepgisvis apvrdssgli vaavtltvar
      241 pfleksmidq glvgqvrhaa ddlsarlnyh aaehdaghd
//
LOCUS       WP_175802520             257 aa            linear   BCT 11-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Burkholderia anthina].
ACCESSION   WP_175802520
VERSION     WP_175802520.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..257
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28516
     Region          12..253
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mssplqsesi raqvaelrer gfvvarglvg eaqcaalkri aeqqlqeaae piefeadlry
       61 pgapeskhap gghtvrrlln aytrdpafae raiapeigaw mreyfgeqpv lscahhncmm
      121 tkhpaygslt gwhrdfryws feradmvsvw lalgpetnen galwlvpgsh taecgpeafd
      181 dakffrsdlp enrkmidaat cpplqtgdvv ffhcntlhsa gqnrsdqvkf slvytyhgvs
      241 nrplpgtrsa skpevqf
//
LOCUS       WP_175802530             279 aa            linear   BCT 11-JAN-2025
DEFINITION  polyphosphate kinase 2 family protein [Burkholderia anthina].
ACCESSION   WP_175802530
VERSION     WP_175802530.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Motomura,K., Hirota,R., Okada,M., Ikeda,T., Ishida,T. and Kuroda,A.
  TITLE     A new subfamily of polyphosphate kinase 2 (class III PPK2)
            catalyzes both nucleoside monophosphate phosphorylation and
            nucleoside diphosphate phosphorylation
  JOURNAL   Appl Environ Microbiol 80 (8), 2602-2608 (2014)
   PUBMED   24532069
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Sureka,K., Sanyal,S., Basu,J. and Kundu,M.
  TITLE     Polyphosphate kinase 2: a modulator of nucleoside diphosphate
            kinase activity in mycobacteria
  JOURNAL   Mol Microbiol 74 (5), 1187-1197 (2009)
   PUBMED   19843229
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Nocek,B., Kochinyan,S., Proudfoot,M., Brown,G., Evdokimova,E.,
            Osipiuk,J., Edwards,A.M., Savchenko,A., Joachimiak,A. and
            Yakunin,A.F.
  TITLE     Polyphosphate-dependent synthesis of ATP and ADP by the family-2
            polyphosphate kinases in bacteria
  JOURNAL   Proc Natl Acad Sci U S A 105 (46), 17730-17735 (2008)
   PUBMED   19001261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..279
                     /product="polyphosphate kinase 2 family protein"
                     /EC_number="2.7.4.-"
                     /GO_function="GO:0008976 - polyphosphate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016776 - phosphotransferase activity,
                     phosphate group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006797 - polyphosphate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31735
     Region          7..277
                     /region_name="PPK2_rel_1"
                     /note="polyphosphate:nucleotide phosphotransferase, PPK2
                     family; TIGR03709"
                     /db_xref="CDD:274737"
ORIGIN      
        1 makqpslddf rvpystreke aaafkldgfd pgakpfssgs kdadrerlta vstaldvqqe
       61 rlhtqqkkrv llvlqgmdts gkdgtvravf rdvdplglri vpfkaptpie aahdflwrvh
      121 aqvpaagela ifnrshyedv lvprvldlid dkececryrq irdfetmlae ngttivkcfl
      181 hiskdeqrer lqariddptk hwkfdisdld arkhwdayqs ayrdalaats aehapwyvip
      241 anskthrnvm iaelllrtmt dmklefpppk peldgvkir
//
LOCUS       WP_175802537             349 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175802537
VERSION     WP_175802537.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..349
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38217
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdhlqsmrvf vkvadlgsfa raasamdisn avatrhvadl egrlgtrlln rttrslslte
       61 sgqvylerar qildeledve qmvvarnhep vgtlrivvpv vfglhnlapv lqsytesfpk
      121 vvpdltlvdr qvdlveegfd vgivvtrqmr sasivtrrlt tgcmtvcatp sylekhgvpt
      181 hpeqlaehpa lslpteywgd ervftgpdge vrvrptnviv anntamlrqc allgmgvail
      241 psyliggdia rgalvrllpd frlpqveini aypsrrhlpa kvrtfidhlv ehfshstdam
      301 mgeqwasqga apapigvemr aepaestdpn lqprlvrasr praavpspl
//
LOCUS       WP_175802561            1056 aa            linear   BCT 11-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Burkholderia anthina].
ACCESSION   WP_175802561
VERSION     WP_175802561.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1056)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1056)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1056)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1056)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..1056
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=118301
     Region          1..1047
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mlneqqleeq clswfqetgw rfahgpdiap dssapertdy rqvvlrerll aalarinphi
       61 ptsgleqavh alqtvsepqm vmrnrsvhrl llngvlvefv vgnekktdlv hfidfaqpsn
      121 ndflvvnqft itgtkqprrp dvitfvngmp lavvelknpv neqadvwdaf dqlqtykdei
      181 sdlfncnval vvsdgwtarv gsltanterm lpwrtidned drprlqmele tvvrgffkpe
      241 lfldyvrhfv lfeqdgdtii kkiagyhqfh avreavratv iaaqdvekgm levheerasy
      301 gkevkpgsrk agvvwhtqgs gksitmacya gklvqqpemk nptlvvvtdr ndldgqlfst
      361 fsaasdllkt tptqaedrdq lrdmlasrea ggiifttvqk falledeeah pllsdrtniv
      421 visdeahrsq ygtkgrldtk tgkyvfgyak hlrdalknat figftgtpia ledkdtravf
      481 gdyvsiydiq davddgatvp ifyesrlakl dvnqaeidal neqvdevved eediasrekt
      541 ksewatlekl vgskprlqqv ardliqhfea rvsvvdgkam ivcmsrdicv qlynvicvgd
      601 ennppmrpew hstdpeqgai kimmtgsaad kallqphlys kqvkkrlear fkdvkdplkl
      661 vivrdmwltg fdapcchtmy idkpmkghnl mqaiarvnrv fknkpgglvv dyigianelk
      721 aalktytdak gkgdpthnaa eavsvmlekm divrgmmhgf dysafetqai qllvpaanhi
      781 lglkdgktrf ldtmvavaka fslcgtldea gtirkeiaff saikaaiakf ttvdkkrsda
      841 eknsalkqil dnaiisdgva dvfalaglgk pnigllsdef lediremesr nlavellekl
      901 lrdeikarar nnvvqekkyg drlletlrky hnraietaqv ieeliqmake fqatlereaa
      961 lglgpdeiaf ydalannesa arelgdevlk riaieitekl rasttvdwqv resvraklri
     1021 lvrrtlkkwk yppvgedaai elvlkqaesl snawst
//
LOCUS       WP_175802570             528 aa            linear   BCT 11-JAN-2025
DEFINITION  MDR family MFS transporter [Burkholderia anthina].
ACCESSION   WP_175802570
VERSION     WP_175802570.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..528
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56491
     Region          37..516
                     /region_name="MFS_LmrB_MDR_like"
                     /note="Bacillus subtilis lincomycin resistance protein
                     (LmrB) and similar multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17503"
                     /db_xref="CDD:341046"
     Site            order(39..40,43,75,125..126,128..130,133,153,156..157,160,
                     287,290..291,294..296,299,327,331,383..384,388,392,408,
                     411..412,415..416,419)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341046"
ORIGIN      
        1 madaattppa pphedrasvt dwiavaagal galmatldis itnsalpqiq geigatgteg
       61 twistgylms eivmiplaaw ltrvfglrnf lltnaalfia fsmmcgwshs lammiagrig
      121 qgftggalip taqtiirtrl plsqlpvgmt lfglivllgp lfgpvlggwl aenvswswcf
      181 flnlpvclll mallvfglps dkpqwhtffn adwlgiagla iglssltvvl eegqrerwfe
      241 sqmivtlsyv slagmilial sqrfakrpim rlslmrnpry asvivivsav gaglygvsyl
      301 lpqflaivag ynaeqagsim llsglpaflv mpilprllgk vdfrilvisg lllfclscml
      361 disltaqsvg hdfvwsqlir gvaqmlammp lnqasmaava redsgdaagl ynmarnlggs
      421 iglaiigtvi drrttfhaaa lresvtansl igqqrlsdya anwfahtgdl aysnmralgq
      481 laqqiqvqav vmtysetfyl lglallacvp lalllktprg pqpmssgh
//
LOCUS       WP_175802573             825 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia anthina].
ACCESSION   WP_175802573
VERSION     WP_175802573.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 825)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..825
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87890
     Region          497..783
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mrlfllgwll aavvstahaa tpapaaasaa sgatpaltpq qaqqalsvlq nprereqvet
       61 tlraiaavgv lstpavpass ataasaassa aapatlttng lasmvvrqgs hwaaeigaal
      121 neslhslldv gsvgswwher lvraderadl mhailiilav lvpafavewf akrllrrala
      181 altarraeas rrseaespep dddiapepap pdsagqpgtq dathsssqgr gharrhttll
      241 rrmpralvgl alrvvpllvf vgvasltmsv ldntatpver aleslidiyv icrlvtivsr
      301 lffqpdarql rllhisdawa afaqrsiari aivvgactaa veiaanfgls daghvallka
      361 valvghlmvs alilqcrrpv aariraaced rptfamigna ladawapvsv fvvmalwfvw
      421 aldvhngyrv litlggrsia vtigmrivsi ivfgalarlf qqrdddrtlv hlhayryypl
      481 lrqivsavia vvtvvlllqi wgvpifhafg sgtighrlas almtiaiaav valivweaan
      541 isierrlqqw tregnlvraa rlrtllpmlr sllfimialv vvltglseig vnigpllaga
      601 sifgvalgfg sqklvqdfit gifllmenam qvgdwvtlag vsgtveylsi rtvrlragdg
      661 slytipfssv ttvnntnrgl gnaavkvsia ygqdidraia tlkeigaalr edpnyqngil
      721 sdfsywgidq vdgatialag qvqckdsarw gvqrefnrri avmfaergir ianpqrslva
      781 ydqgsrpvgp gnddthenge rttgtpaaep pppaapapap arkpd
//
LOCUS       WP_175802604             488 aa            linear   BCT 11-JAN-2025
DEFINITION  flippase [Burkholderia anthina].
ACCESSION   WP_175802604
VERSION     WP_175802604.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..488
                     /product="flippase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52309
     Region          5..414
                     /region_name="MATE_Wzx_like"
                     /note="Wzx, a subfamily of the multidrug and toxic
                     compound extrusion (MATE)-like proteins; cd13128"
                     /db_xref="CDD:240533"
ORIGIN      
        1 mdkgilknvs infiglilpt fvslvtvpay ihalgveryg vvslvwtlig yfgvldlgms
       61 maaqnhiska lasgnadesa rvfwsafwln lgtgiaggll iyfgafvyta yftkvsaamq
      121 hevylalpwl alaiplanvs wvfagainga erfgvfntnq tigtflfqll plgaawwiap
      181 nlqtvlaaav varliaavml ghasikvlgi rridppqwgt akglfnfggw mliastasmi
      241 adtldrvmlg agmgakfvty ytvpqnlvtr lnmlpnalvr tlfprlsavg rdhadtlarq
      301 sleflngvft pvgivaifal apfltlwvgp dlaahsapvg rvlvisvwlv gqasvtrili
      361 qsqvnparaa faglvempff vgglwfgihh fgligaavvv atralvdygv llylsairmr
      421 aivldmlahl afllaslfla qawsglgesi gmcavvlvln vawsltmtpg lralvrdlfv
      481 rlnarkti
//
LOCUS       WP_175802641             508 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Burkholderia anthina].
ACCESSION   WP_175802641
VERSION     WP_175802641.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..508
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53764
     Region          16..491
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(72,74,78,81,85,118,121..122,131..138,143,146,149,
                     242,246,249,252,254,427,429..430,432..433,436,439..440,
                     442,444..447,456,460,462,476,483..488,490..491)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(158..161,169,184,187,217,234..237,240,258..260,292,
                     392,394,420)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(161,258,289,292)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnaavpqttl alptakllid gafvesqsae wgdivnpatq evigrvpyat ldevdaaias
       61 aqrafqtwkt tpigarlrim lkfqdlvrrn leriaktlta eqgktlpdaq gdifrglevv
      121 ehacsigtlq qgefaenvag gvdtytlrqp igvcagitpf nfpgmiplwm fpmaivcgnt
      181 fvlkpseqdp lstmqlvela ieagvpqgvl nvvhggktvv drlcthpdik aisfvgstrv
      241 gthvynlgsq hgkrvqsmmg aknhavvlpd ahreqsinal vgagfgaagq rcmatsvvvl
      301 vgqardwlpd lvekakalkv nagaeagtdv gpvvskaakt rilslidagv kegatllldg
      361 rdvkvpgyeq gnfvgptifs gvttdmsiyq eeifgpvvvv leadtldeai alvnanpmgn
      421 gvglftqsga aarkfqseid igqvginipi pvpvpyfsft gsrgsklgdl gpygkqvvqf
      481 ytqtktvtar wfdddttagg vnttialr
//
LOCUS       WP_175802642             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175802642
VERSION     WP_175802642.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46763
     Region          28..433
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(39..40,43..44,47,86,144..145,147..149,152,172,
                     175..176,179,261,264..265,268..270,273,301,305,358..359,
                     363,367,383,386..387,390..391,394)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mqtrstldeh ataaapapar takhyllagw asmagttiew ydfflygtaa alvfnriffp
       61 sldpvvgtla afgtfavgfi grpmggivfg hfgdrigrks mlmitlllmg vpsmviglip
      121 sydsigywaa alliamrflq gmavggewgg avlmavehap kgrkglfgsl pqtgvglgli
      181 lssvamaava alpdadmlsw gwrvpflasi alvglgwfir akvpespdfe kvrkqgkaek
      241 spvtaalrrh prevltivga raaentwfym vvtfalayat qqlhlpkaem lhaitagaal
      301 slvtmplcgh lsdrigqrrm faiglvlmca faapffmmlg tqqtsyawwa ivlglgvvfp
      361 ilyapesllf aqqfpaeiry sgislsvqla gvigggfapm iatsllkagg gqphyviayl
      421 vgfgvfalvc talmrppra
//
LOCUS       WP_175802650             421 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia anthina].
ACCESSION   WP_175802650
VERSION     WP_175802650.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 421)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 421)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 421)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..421
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45371
     Region          <198..415
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mtiapsspst aalkrelkaa earkrtmall liaplaifll lifvvpigtl ltravqnpei
       61 atalpntiaa lsgwdrkapp sdaayvalaa dmtkvadsea mgalarrlnt eipgyrslva
      121 ktaramplkd dndaaaaalt paqtraklid ldsrwgdvay wqsiakngsq lspfyllasl
      181 dhkqdgfghv vqadpdqsiy laifgrtfvi gvavtlfall lgyplaywis tlserranlv
      241 milvlipfwt svlvrvaawi vllqseglin kaligsglis hpltllfnrv gvyismthil
      301 lpfmilplys vmksipptyq raavslgshp faafwrvyvp qtypgigaga llvfilaigy
      361 yitpallggp ndqmvsyyva yftnvtinwg macalgglll aatlvlyavy grftrtnvsl
      421 g
//
LOCUS       WP_175802669             226 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175802669
VERSION     WP_175802669.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..226
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24988
     Region          10..225
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mntltdalrd rpaasavsla drayaliqrd iitmrlkpga alneadlvar tgigrtpvhq
       61 avhrlvlegl lsvmprkgll vqplslddiv svidvrrine aycvelaarh atpddlarma
      121 allgdgqacv dmhdvegmme ldrafhqaia aaarntvlae vlralhersl rfwfvtlsep
      181 hhlsdvqreh relferlstr davgaraave rhidsfratl vqhlrp
//
LOCUS       WP_175802655             306 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia anthina].
ACCESSION   WP_175802655
VERSION     WP_175802655.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..306
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32198
     Region          49..287
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
ORIGIN      
        1 mtvittpaaa sataapgsaa asaprmgrlr tadglelasy rwpagdgtap pratialvhg
       61 laehagryaa laarlnaagi evlaidlrgh gqspgkrawv erfdgylnda dalvaqaard
      121 dtplflmghs mggavaalya iervpargya ltglvlsspa lapgrdvprw mlamsriisr
      181 iwptfpairi daallsrdpa ivaanradpl vhhgavpart gaeildamar iergrgalht
      241 pvlvyhgtdd kltepdgsra fgarvgstdr tltlyeggfh etmndlerdr vidaliawih
      301 arapar
//
LOCUS       WP_175802693             769 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA translocase FtsK [Burkholderia anthina].
ACCESSION   WP_175802693
VERSION     WP_175802693.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12144184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..769
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=83485
     Region          18..198
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          148..769
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 makapysaqa qalphrmskl lteirwilqv alcaflvmal lsysrrdpsw thaaqvdhis
       61 nwagrvgawt adiilllfgl saywlivplg rriavnyrri trheavadep erpigwltei
      121 lsfvlvvlac dgieamrmws lkvqlprapg gvigeavaga mshafgftgg tllllillav
      181 glslyfrfsw lsvservgga ilsavtvakl rreaerdrkl geaaavrreg kveeervrie
      241 dhepvtivpp vvtpakserv ererqvplft dlpgdstlpp vslldpapkt qeaisadtle
      301 ftsrliekkl kdfgveasvv aaypgpvvtr yeiepatgvk gsqivnlakd larslslvsi
      361 rvvetipgkn ymalelpnqr rqtvhlseii gsevyaaass altlslgkdi ggkpvcadla
      421 kmphllvagt tgsgksvgin amilsllyka taeqvrlili dpkmlemsvy egiphllcpv
      481 vtdmrqagha lnwtvaemer ryklmsklgv rnlagynnki ddaakreeki pnpfsltpdd
      541 peplgrlpni vvvideladl mmvvgkkvee liariaqkar aagihlilat qrpsvdvitg
      601 likanvptri afqvsskids rtildqmgae sllgmgdmly lapgtglpvr vhgafvadde
      661 vhrvvdklke qgepnyvegl leggttdgde gsagagtgeg gdesdplydq aveiviknrr
      721 asislvqrhl rigynraarl leqmeqsglv samsssgnre ilvpardae
//
LOCUS       WP_175802743             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia anthina].
ACCESSION   WP_175802743
VERSION     WP_175802743.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..359
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39185
     Region          8..355
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkhsferlrl dgvcrsftna egaqvaalsg ldldirrgef iallgpsgcg kstalnciag
       61 lqpltsggiw lddtridvlp perrgfgmvf qnyalfphms vlenvgfglk mrgvakqetr
      121 rraqqalelv qlvghegklp gqlsggqqqr vaiaraivie pplvlmdepl snldtklrie
      181 mraeirriht qleratiyvt hdqdealsma drivvmkegv vqqvaspkdv ytrphnlhva
      241 rfmgyrnvlp ftlegmagdh vnvtaagvli tgvpmagfdg kdvlvalrpd dieravegad
      301 nafdatidtl eyggrdslir attpfgpiwa rvageftege rlrlrvapar tlvyagdaq
//
LOCUS       WP_175802771             247 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175802771
VERSION     WP_175802771.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..247
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26832
     Region          3..240
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mdvklvartl dlfelfaaek rplpltelar llnvpasscl amartlvsrg ylyevrkrgg
       61 yyptrrlqti aaaidatdpv vdfvhphlva lrdasretav lgkiqgasvt yldvveseqa
      121 irytrqpgel rplhansigk aifaeladda qqalgaqlsf erftdasvad lpslvaqaar
      181 frelgwaenf gesapelsai avavtldgdw yglsvvgpte rirqhrdtha allvdakarl
      241 laeqgrg
//
LOCUS       WP_175802893             232 aa            linear   BCT 11-JAN-2025
DEFINITION  YoaK family protein [Burkholderia anthina].
ACCESSION   WP_175802893
VERSION     WP_175802893.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..232
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=23292
     Region          6..211
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mkhedtilaa vagfvdtlsf valfglftah vtgnfvliga gvagfgqgvv lklsvfpafv
       61 cgviasslia rsmsvrpawq gtralhavqa vlllgfcvag vwatpvtqpd slpalvagiv
      121 gafamgvqna hprvipragg vpntvmtgnv tqaildvvdm lsagtadsar atararfgkm
      181 lpaivafalg amggalgfrh vgflalllpv galallavca aqaagsvkqe ha
//
LOCUS       WP_175802903             413 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            anthina].
ACCESSION   WP_175802903
VERSION     WP_175802903.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 413)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..413
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=42085
     Region          32..313
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mdsralagvl rwltfaacvm lpawlwphga mlgylaqtaa lvvlalsynl qlgttgllsf
       61 ghaafaglga faaahwfnrf ggplpllplv ggvagagfgf vagllatrra gtvfamitlg
      121 lgecvaaaaw svpawfgglg gvpidrasgt pwgswnfgap lqaytvigaw ciasaiamea
      181 ltrtplarla navrdnparv aalgteprrv rlamvtcasf fagiagtltl idveiatqds
      241 vsmarsatvl iaaviggtga ffgpaagaav ltalsivvag vsrawalylg vlfvavvvaa
      301 prgiaglaqd vahalrrdap averwrmlcg vgacvfwgia ivcaaelgya wrfaqddgaa
      361 gvafgawgid adapagwava csaagigtll wgwrarlang gagarrgkre arr
//
LOCUS       WP_175802922             732 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia anthina].
ACCESSION   WP_175802922
VERSION     WP_175802922.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..732
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80047
     Region          32..715
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 msassptsph agglaawyaa fddwartdga awlylfkall aafisigvsm rldlpapkta
       61 mttvfivmqp qsgavlaksf yrvagtifgl iatltfvglf pqqpqlflla valwvalcta
      121 gaarnrnfrs ygfllagytt aliglpasqh pdgafmsamt rvaeimvgiv sagvvsalvf
      181 pqytgeqmrt tvrkrfgsfv dyvaaalsgk ldrahiesih trfvadvvgf eaarsmavfe
      241 dpdtrmrsgr larlnsefms vssrfhalhq lmnrlravga qaaidaiepy freiaplltr
      301 hgepvrtsad atlaaeqlla wrdalprrir atratletqp dfplldfdta aellyrfitd
      361 lheyaatyas lstatherer wieryeprtn vtamviaair tatvilvlgw fwietawpsg
      421 vtltltaaat calasstprp tamsaqmgmg talavctgfl ltfgiyphid gfpllcvala
      481 pllaigifmt lkpklagygm gyliffcfla gpdsithydp tsfmndalal vlsmlvsaia
      541 favlfpptap wlkkrlfadl rhqvvaachv rlaglrtrfe sgardlmyqa htlsadqpdv
      601 qrdalrwmfa vletgnaald lrhelatlps dpryapatpw rraietlrta lsalfskpsa
      661 erfdatlaav naaidatrqt ldaftparee rhrlqrilsn lhfvrtalld pespleplnr
      721 nrpvrpqpga ss
//
LOCUS       WP_175802925             473 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175802925
VERSION     WP_175802925.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..473
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50565
     Region          4..473
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mnsseafvsa crdaigtayv ltdphdtepf ltdwrrrykg aacavlkpad taevaalvkl
       61 anthgvalvp qggntglagg atpdasgsqa vlnlsrlnrv raldphnnti tveagvilad
      121 vqarareggr lfalslaaeg sctiggnlst naggtavlry gnarelclgl evvtpqgeiw
      181 dglrglrkdn tgydlrdlfi gaegtlgiit aavmklhplp aaqvtalaal esphaaldfl
      241 slaqraagpl ltgfelmsdf cmqlvgkhyl qlrypfdrth aqtvllelsd nesetharal
      301 feklmeeafe aglvvdavva enlaqsrafw dlrehiplaq adeglnikhd iavpissiar
      361 fidetdaaiq qaapgarmvt fghlgdgnlh ynvqtpeggd pkaflaeyqa pinrvvydnv
      421 hrhhgtisae hgigqlkidd aqrykspvet tlmrtlktal dprglmnpgk vlr
//
LOCUS       WP_175802968             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175802968
VERSION     WP_175802968.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33497
     Region          8..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(104,108,151,165,167,226,243,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(105..106,110..111,113..114,117,121,123..129,194,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mddflsphla lfvdvvdqqs fsaaarrqgv aassvtrrid rleaqlgirl lhrtthalrp
       61 teaglllygr atrmlaelrg lqedlhsqhd epsgllrvdc papfgrrhlm aalaafmqrh
      121 palqvdlllt dsmvdpqgtr lgsdvdlavr igpledtrfv atvlapqrrv lcaspdyvar
      181 rgepeapdal aghdclawhg vpppgawrfd grrhvpsqpr frsnhseall eaaidglgia
      241 hlptwlagda lrdgrlrall pryaaasepa tihvlrqqar gsaraarlva flvtwfaqpa
      301 wdaawt
//
LOCUS       WP_175802975             427 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175802975
VERSION     WP_175802975.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..427
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45389
     Region          15..415
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(26..27,30..31,34,69,116..117,119..121,124,148,
                     151..152,155,243,246..247,250..252,255,286,290,341..342,
                     346,350,366,369..370,373..374,377)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mnwavtrirg rfhygwlaaa vvflillaaa gtratpsvlm vplerelgws ratislaisv
       61 nialygltgp faaaamqrfg lrptilaalv tmsagvalss lmtqswqmvl iwglmvgcst
      121 gvvaltlsat fvtrwfharr glvmgiltas tatgqlvflp mlaaiaqrhg wrpvvlvvav
      181 aaaiviplva fllperpadv qlrpygepad appapdatke nplavafral ltasrsrdfw
      241 llffsfficg astngyvgth liamcsdygm tevqgaslla amgvfdlfgt tlsgwlsdry
      301 dnrvllfwyy glrglsliyl phafgidffg lplfamfygl dwiatvpptv rlatdvfgka
      361 aapvvfgwiv aghqlgaafa algagllras lgtytiasmi sgglcivgal ivlrinrgps
      421 raaaqaa
//
LOCUS       WP_175803035             344 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia anthina].
ACCESSION   WP_175803035
VERSION     WP_175803035.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..344
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37722
     Region          68..271
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 makdtskdkk ptgnlhlaag llrglaqena aletrlpepv apasdiavet tttaapsapa
       61 padasdlgap qrvavkdcip npfnprvfys esslhelalt lkregqiepi kvtrlpqfpg
      121 klvvidgqrr lratsingde tinatfrtdh tpeqlytiay ranhdherqt ifddavawkr
      181 lldekvfpdq ntlaekigkd kasisktlsl nalpntller masandvvgl qaayflklif
      241 erlgepaadr lltsvidrkk svrdlenflr aqsdgnkktg rtrysvrhdf alesraigql
      301 ktypdgrldl qlkgvdashq ealadrlktv idayvaelas atqk
//
LOCUS       WP_175803062             215 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia anthina].
ACCESSION   WP_175803062
VERSION     WP_175803062.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..215
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22409
     Region          6..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mhtsgslygf lviggmlavt pgpnmvyvms rsiaqgrtag lislagvmvg ylfymfgaaf
       61 gittlflsmp yagtvlgvvg aayllylawq avrpggrspf evkalpseqp lrllamgatt
      121 svlnpklaml fvsllpqfid yrqgsvfgqs lflgslliaa fasangmvai cssgiakflh
      181 grptlllaqr wamgmvlggl gvemlvdasr magva
//
LOCUS       WP_175803100             460 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpP1/FadL family transporter [Burkholderia anthina].
ACCESSION   WP_175803100
VERSION     WP_175803100.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Black,P.N. and Zhang,Q.
  TITLE     Evidence that His110 of the protein FadL in the outer membrane of
            Escherichia coli is involved in the binding and uptake of
            long-chain fatty acids: possible role of this residue in
            carboxylate binding
  JOURNAL   Biochem J 310 (Pt 2) (Pt 2), 389-394 (1995)
   PUBMED   7654173
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Munson,R. Jr. and Grass,S.
  TITLE     Purification, cloning, and sequence of outer membrane protein P1 of
            Haemophilus influenzae type b
  JOURNAL   Infect Immun 56 (9), 2235-2242 (1988)
   PUBMED   2842261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..460
                     /product="OmpP1/FadL family transporter"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47366
     Region          6..460
                     /region_name="FadL"
                     /note="Long-chain fatty acid transport protein [Lipid
                     transport and metabolism]; COG2067"
                     /db_xref="CDD:441670"
ORIGIN      
        1 mtgaraalaa gcliaqcssg tawaqdafni safgasslam ggvaaasnvg lpgmmvnpat
       61 lglmnegsyg elgagvitas vkakneatge iadshtrgrn ngpyyapela ylwryrryal
      121 gigvfassgv gteygtgsfl srtttngvdt gldnfsrlma lkipfsmayq vtdkltvgga
      181 veavliaanm gllfdasqlg vlgaqgrlsg gllsslmsvp glsgaqlqfs ngkiaggaad
      241 gwgvsgklgl tyqatprtrl glayqfkthv sdltgsaqvt avsasagnip iggtvriadf
      301 qlpasftvgi sqdlsdrltv aadyqrvfwr dvmsslqvgf tqdgsgkgis lslplnyrdt
      361 nvfsigaqyr ynanwtfrgg fhyaqeaapg sgllaiipst pttsitagga ytfnrggtid
      421 falgyslpkr vassgntgss vpisvtdsmf hvacsytqrf
//
LOCUS       WP_175803070             348 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175803070
VERSION     WP_175803070.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..348
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38762
     Region          25..338
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mytdnedygd gsqeadeapp grpdlrvgfi llnqftlvpv aglvdslrfa adksfrsrqi
       61 ycqwdwmtcn depisascgm pilptkrleq lesydyvvva ggllaetrnp pdwlldalrn
      121 vhaagipiig lcsasfvlgk aglldgrrca ihftirdefs erfplatali dksyvddegi
      181 itcpggtaid laanmirrhc geiraqkglk ylladtaldt apeherdsep hvyqneivrk
      241 aiafmranlg asatlkevad hagtsarqlh raflnntnda panywrklrl eharkqladt
      301 slnvttiaie cgfsdashfi lwfrkqyget psvyrkrrhe verllaar
//
LOCUS       WP_175803107             180 aa            linear   BCT 11-JAN-2025
DEFINITION  aromatic-ring-hydroxylating dioxygenase subunit beta [Burkholderia
            anthina].
ACCESSION   WP_175803107
VERSION     WP_175803107.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10791045
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..180
                     /product="aromatic-ring-hydroxylating dioxygenase subunit
                     beta"
                     /EC_number="1.14.-.-"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0009056 - catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=20690
     Region          24..166
                     /region_name="HcaF"
                     /note="3-phenylpropionate/cinnamic acid dioxygenase, small
                     subunit [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG5517"
                     /db_xref="CDD:444268"
ORIGIN      
        1 mnaitiekep vripssrdfa eyvtrveved llfheaelld twqlhdwlsl ftddgtyyvp
       61 stdlprtasa ddslfyiadd pvrlrervir lmkktahsey prsrtrhlvg nvrildagpd
      121 eikvatafvt yrikfgsnda yvgsahyrlr rvdgqlriae krcfldleal rphgrvsiil
//
LOCUS       WP_175802879             467 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatase PAP2/dual specificity phosphatase family protein
            [Burkholderia anthina].
ACCESSION   WP_175802879
VERSION     WP_175802879.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Pulido,R. and Lang,R.
  TITLE     Dual Specificity Phosphatases: From Molecular Mechanisms to
            Biological Function
  JOURNAL   Int J Mol Sci 20 (18), 4372 (2019)
   PUBMED   31489884
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Patterson,K.I., Brummer,T., O'Brien,P.M. and Daly,R.J.
  TITLE     Dual-specificity phosphatases: critical regulators with diverse
            cellular targets
  JOURNAL   Biochem J 418 (3), 475-489 (2009)
   PUBMED   19228121
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12932297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..467
                     /product="phosphatase PAP2/dual specificity phosphatase
                     family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=49848
     Region          42..216
                     /region_name="PAP2_Aur1_like"
                     /note="PAP2_like proteins, Aur1_like subfamily. Yeast
                     Aur1p or Ipc1p is necessary for the addition of inositol
                     phosphate to ceramide, an essential step in yeast
                     sphingolipid synthesis, and is the target of several
                     antifungal compounds such as aureobasidin; cd03386"
                     /db_xref="CDD:239481"
     Site            order(117,125,151..153,188,194,198)
                     /site_type="active"
                     /db_xref="CDD:239481"
     Region          320..457
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
ORIGIN      
        1 msvlgggagg alakpaagpr daslalrvgw lavmgavffs tygfanwlaa qraavptfaf
       61 gwehaipfvp wtivpywsid llyalsflfw trrddlldhv krllavqlvs vacfvawplr
      121 fgferpeagg vagalftllm gfdkpynqap slhigllvvl wavyakhlrg taaravlhlw
      181 faaigvsvlt tyqhhaidvp tgaavgcfal flfplrdaag rlpgaegsps gagralarry
      241 algaglaalv algcvshapg walaagwgal alacvawiyr rgapgafqkd dagrfpvfir
      301 wlfaptvaga fvnsrlwtvr qpapvrider vsigrtpttr dmrrygftal vdltaemprw
      361 vaadaslaya avpqldlvap saaqlaaava alerlhregr dvlvccalgy grsvlcaaaw
      421 laarrgfgda realaavrtv rpravwsddg vavlqdwidr rrvtggv
//
LOCUS       WP_175803128             279 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia anthina].
ACCESSION   WP_175803128
VERSION     WP_175803128.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5), 4725 (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10897914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..279
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=30110
     Region          6..144
                     /region_name="AANH_superfamily"
                     /note="Adenine nucleotide alpha hydrolase (AANH)
                     superfamily; cl00292"
                     /db_xref="CDD:469708"
     Region          154..277
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 msyksmvvhl dtsarahsrl efalrlarrf gahltglfav ytpephsfyv magsadyfra
       61 hreqrderla alerlfhaea arakvpaawv raderanaav praarladlv iagqsdpndp
      121 eayiddqfpe nlvlsagrpv lflpctgefp svgervfvaw dgsreaaraa hdaipflgha
      181 krttvaavvd gdseaattri paadaalmla rhahdvtvld idtgtgpavg dtllsrayet
      241 gsdllvmgay ghprwrelvm ggatrtvlas mtmpvlmsh
//
LOCUS       WP_175803114             372 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia anthina].
ACCESSION   WP_175803114
VERSION     WP_175803114.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..372
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=39143
     Region          9..372
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mrhqravlla alasicapac aqstitlygi vdtgveffth asptggamvr lptisggdlp
       61 srwglrgeed lgggiktvft lesgfspasg tslqngrlfg rqsfvglkga wgqltvgrqm
      121 nmtmygmada dvigpaafsm gsfdgylaaa radnsveyrg kfadltvgvs ysfgrdglpa
      181 sncggqlpgd tmscralttm lkydrpnwga aliydeqrgg agatamtvvp glsgvafgns
      241 gdtdrryqan gyflvgkvkv gggwlhreik gdvrtvrtdl sylgvsvpyv awvfdaqvlh
      301 vrnrsydadg tmgifranyn lskrtalygl laymknsgrg avysvssssl apavpepgvg
      361 qagamvgirh lf
//
LOCUS       WP_175803165             340 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175803165
VERSION     WP_175803165.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..340
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35944
     Region          9..332
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 msqstcpard ivvvgfegvq slditgpmev favanrhlpg hvapyrltla sqhghdivth
       61 aglrlagpta laalparidt livaggseaa lrhaasdagv lpwlhtriah trriasictg
      121 afvlaaggwl dgkratthwn qcstlqalcp nvriepdaiy vsdppfhtsa gvtagidlcl
      181 alveadcgap talavarelv lfmhrpggqa qfsvgldvha natpqmrtll agitddptgd
      241 lgvaalaarm hmsertfsrn fvketglspa qfvlaarver akallersdw pleriaqqag
      301 fgsvdalqra fakrvgvspr dyrarfgrpa sadtretpqa
//
LOCUS       WP_175803173             301 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175803173
VERSION     WP_175803173.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..301
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32906
     Region          112..271
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mllnvnpfhr dtdrfnvsfk algelietvg tphfvprltq llndvvpldv ahversrvdg
       61 smptgyrcew igssgigtea aeisdvmtly yerfldsdpl faglrgktgt mlvvrdiaai
      121 ppgefrqriy ddvhighecv largtryaqh sialergrdr ppftlaemnr frsisdvlfp
      181 llelhastta arrvahptpe vhplaqfdar iaadgvklsr reyetckhll sgktvpetad
      241 vlgvrvatae syvkrafqkl gvrtkrelaa wgsavpafps aashgtaiaa ddndappaia
      301 g
//
LOCUS       WP_175803174             321 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175803174
VERSION     WP_175803174.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..321
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35751
     Region          6..316
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mktsfktfrf ltlekysmia ltsaietlrm anqlraaely rwcvysider avlasngiaa
       61 gparvldgaq plpdvlfvcg gwdvrdavdg rvmallrsla argvtlgglc tgayalmasn
      121 lldgyrcavh wevlsdlhad fpdvrfvddl famdrdritc tggtapldmm lyliardqgk
      181 vmarniseqf svdcvrevsd pqpipvasrv gfsreelvet vrlmeanide plsmpelarl
      241 agvsmrhlqr vfrdsldttp yeyyigirlr qarklirysn lpiasvtkrc gfqstthfsr
      301 afrsffghap sherragdpa p
//
LOCUS       WP_175803243             324 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175803243
VERSION     WP_175803243.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12168323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..324
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34698
     Region          22..201
                     /region_name="AraC_binding_2"
                     /note="AraC-binding-like domain; pfam14525"
                     /db_xref="CDD:434015"
     Region          251..322
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdialsrhap nrlgtlhapd everavahrl gphrmaahsr dpfhaelyev plhhgallel
       61 cygretridf gddadhflfr ltlsgacelr agqriaragp geltvsspal asrlstspdc
      121 rnlvlrlerg alerklqdml hatltrplqf dlaaggngag aalvpptfey lcrlgaqpgt
      181 gasattfgad ltawlmslll thlphsysaa largkpplpa hvrracdhve ahlgeplala
      241 alaavagvap rtlqhafrtf lnttpaayvr errlaavhaa lqrgdarsvt dvliahgihg
      301 fghfakayar ryghapsvta rqap
//
LOCUS       WP_175803253             214 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia ambifaria].
ACCESSION   WP_175803253
VERSION     WP_175803253.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..214
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22206
     Region          12..213
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mpaaskpvrp vrvysfplsg hahrirlfls llglpsdivd vdlaagaqre paflalnplg
       61 qvpvidddgt vladsnailv ylakrygdah wlpddaagaa tvqrwlsyaa gpiasgpaaa
      121 rlvtvfnapl dydaakrtaa kilavidgel agkpfaagaq ptiadiaayt yiahapeggv
      181 slepyphvra wlarvealpg fvgmpttrag llaa
//
LOCUS       WP_175803330             145 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175803330
VERSION     WP_175803330.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..145
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16456
     Region          11..145
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mqprlnfyta spnaikvmrn aeefiakssi ekplaelvrl rasqingcaf cvdmhttdar
       61 kggetvrrla tvvawretpf ftereraale wtealtlvad nhvpdsvwea vkphfsdtel
      121 felsmliati ntwnrfaiaf rkmpe
//
LOCUS       WP_175803297             311 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175803297
VERSION     WP_175803297.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..311
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33306
     Region          10..305
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mnlptpihrr ytgafsvapt iftesgeidm pgqkrcidfi idagadglci lanyseqfsl
       61 tdeererlia ailehvagrv pvivttthfn pticaarsra aqaagaamvm vmppyhgati
      121 rcgeaaieqf yaelsdaiai pimyqdapms gtqvsaafla riahtipnlr yfkiempqsa
      181 sklrelialg gdaiegpfdg eeaitlladl dagatgsilg ggypdglrpi laaylagrrd
      241 eavagyerwl plinyenrqa gllaakalmk eggviasdap rrplaplhpa traglieiar
      301 rldalvlrwa r
//
LOCUS       WP_175803342             232 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            ambifaria].
ACCESSION   WP_175803342
VERSION     WP_175803342.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..232
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25966
     Region          21..179
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnakstvarp rgrrplvedf dlrdhmldva iqlfaehgia attvaqiaaa agvtsamvhy
       61 yftnreqlld aiveerlaqv iafvwrptap riendpfalv aelvdrffdv thrmpwlpsi
      121 wlreivhegg llrermvrri plehvgrfae riraaqqagt lnpslepafl fhsiialvml
      181 plataklwqs arglppidrd vlhrhvrall gsgmqppvta pdararaprr ps
//
LOCUS       WP_175803373             134 aa            linear   BCT 11-JAN-2025
DEFINITION  PaaI family thioesterase [Burkholderia ambifaria].
ACCESSION   WP_175803373
VERSION     WP_175803373.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..134
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14457
     Region          15..134
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mdenavrell drllapwvrs lglvpvsisd dsvtmrlpfs gefrhsggii cgqvftaaad
       61 tamvvaisva lgefrpmttv slntnfmrpv rkgdvlvtar vlrmgrnlvf gevelfdedg
      121 kmavhatsty alvs
//
LOCUS       WP_175803395             732 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia ambifaria].
ACCESSION   WP_175803395
VERSION     WP_175803395.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..732
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79888
     Region          32..715
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 msassastpa ggplatwyat fgdwarsdga awlylfkall aafiatgvsm rldlpapkta
       61 mttvfivmqp qsgavlaksf yrvagtifgl iatltfvglf pqqpqlflla valwialcta
      121 gaarnrnfrs ygfllagytt aliglpasqh pdgafmsamt rvseviigiv sagvvsalvf
      181 pqytgqqmrt tvrtrfggfv dyvaaalsgk ldrahietih trfvadvvgf eaarsmavfe
      241 dpdtrmrsgr larlnsefms vssrfhalhq lmnrlraaga qaaidaiepy freiaplltr
      301 ngepvrtstd aaraaeqlla wrdalprrir atraaleaqp dfplldfdta aellyrfitd
      361 lheyaatyas lstatherer wieryeprtn vtamviaair tatvilvlgw fwietawpsg
      421 vtmtltaaat calasstprp tamsaqmgig talavctgfl lmfgiyphid gfpllcvala
      481 pllaigiymt mkpklagygm gyliffcfla gpdnithydp tsfmndalal vlamlvsaia
      541 favlfpptap wlkkrlfadl rhqvvaacha rlaglrtrfe sgardlmyqa htlsadqpdv
      601 qrdalrwmfa vletgnavld lraelatlps dprhapttpw rraietmrta lsklfskpsa
      661 arfdatlaav naaidatrht ldavtpsrde rhrlqrilsh lhfvrtalld pespleplnr
      721 nrpvrpqqga ss
//
LOCUS       WP_175803411             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia ambifaria].
ACCESSION   WP_175803411
VERSION     WP_175803411.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..359
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39308
     Region          8..355
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkhsferlrl dgvcrsftna egaqvaaldg ldldirrgef iallgpsgcg kstalnciag
       61 lqpltrggiw lddtridvlp perrgfgmvf qnyalfphms vldnvgfglt mrgvpkqetr
      121 rraqqalelv qlvghegklp gqlsggqqqr vaiaraivie pplvlmdepl snldtklrie
      181 mraeirriht qleratiyvt hdqdealsma drivvmkegv vqqvaspkdv ytrphnlhva
      241 rfmgyrnvlp ftlegmagdy vnvvaagvri tgvpmagfds kdvvialrpd dieraesgad
      301 nafdaavetv eyggrdslir aitpfgsiwa rvagefvege rlrlrvapar tlvyagdaq
//
LOCUS       WP_175803447             701 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia ambifaria].
ACCESSION   WP_175803447
VERSION     WP_175803447.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..701
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76057
     Region          7..701
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 msrknwaaap maivvgtagl saaeaqelsl paievsgqra tapfrapest satrtetdvm
       61 eipfavssvd kkliqtvaat rgedlydwva gvarqnnfgg lwdnyavrgf agdgntsgtd
      121 ylvngfswnr gisvprdtat lermevlkgp asalygrgdp gglisyttkq pqfarsntig
      181 vsagsygalr etldstgpvt kslayrfiam nedngsfrdt vsskrylfap sftwdigadt
      241 tlhyefetar qrapldrgvv avngqlgavp asrfmgeprd gdydvrnsgh qftlehrfna
      301 dwsvnagfaq rdtdlsgrss eafalqpdgr tlwrryrqva fhsndvqgrv evagkartag
      361 ightfvmgvd ayrfnydqfv srstptaaap yaidifdpvy gqpapvprta tnllerddgq
      421 glyaqdtlaf gshwkvlagl rwdrfhqsve nrlkgvtttq lqtalsprlg ivyeaspals
      481 lyantaysfr pnngadvngr afdpekgrgy eagvkwagtr wlatvaafyv nkrnvltadp
      541 anagfsraag evrsrgvefe wngelghgvr givnfayvda qvthdnvltp garlvdiprl
      601 sgsallmyet alplvdkaga gagviyvgrr agntantqdg fdlpayatlq lngyvqvnkh
      661 lrasvvlnnl fnrtyyvssy nnlwvtpgap rslfaslays f
//
LOCUS       WP_175803491             127 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia ambifaria].
ACCESSION   WP_175803491
VERSION     WP_175803491.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..127
                     /product="VOC family protein"
                     /calculated_mol_wt=14331
     Region          1..126
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 mplpmtrvil yardvallka fyqqyfalpv veeidsewvv ldagavelal hlagptfrra
       61 aapanakads stvkfvfrid tdidthrdrl ahddvtvrdl krydgypyrm ydgidpegnv
      121 fqvmqpe
//
LOCUS       WP_175803486             417 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia ambifaria].
ACCESSION   WP_175803486
VERSION     WP_175803486.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10396284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..417
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=43978
     Region          1..261
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Site            order(7,9..10,12,66..68,104..106,116,120,139..142)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187535"
     Site            order(82,106,116,120)
                     /site_type="active"
                     /db_xref="CDD:187535"
     Region          308..407
                     /region_name="DoxX_3"
                     /note="DoxX-like family; pfam13781"
                     /db_xref="CDD:463982"
ORIGIN      
        1 mnilvcgang figqalcarl eaaghrvlrg vrhavgphdv aidfatdldp dawlarldgv
       61 dvvinavgil adrrdatldt vhraapcalf tacsrvrvrr liqisalgve rgdtpyfask
      121 yaadtflqtl pldyrivrpa lvygatgtsa rffrmlaslp vhalpagghq rlrpvhvddl
      181 aelvarlvvs paaghsvida vgadeveyre mlsgyraalg fppaarialp gplvgaaaal
      241 fgtlpgamlt rdtwamlrgg ntgdpaalaa vlgrpprglr sfigadalal rrdalamwrr
      301 plllgalaiv wiwtaivsaf vhpqsdslam larahltglp alialyaaca ldfalgvatv
      361 aapsrrlwaa qgvlivaysa viavtmpgll aepfgpvlkn vpilaillil fseeeqr
//
LOCUS       WP_175803532            1082 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia ambifaria].
ACCESSION   WP_175803532
VERSION     WP_175803532.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..1082
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115816
     Region          1..1065
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mwivnlalrr pytfivmavm ivlatplalm rtpvdvlpav nipvisviwn yngfsasemt
       61 nritavheri ltttvnnieh iestslpgia vvkvflqpga nvqtaiaqtv ssaqaivrqm
      121 pqgatpplvi tysassipvi qlglssktls eqsladialn flrpqlitvr gaqipfpygg
      181 rtrvvaidld pqallakglt padivnavnt qnlvlptgta kmgqseyrid tnasadtiad
      241 indlpiqtvn gattylreva svrdgfapqt nvvrqngqrg vlmsilktgd astlkvvsdl
      301 kallpkvipt lpegltitpl fdqsvfvnaa vqgviheali aavltammil lflgnwrstl
      361 iiaisiplsi ftslialsal getinimtlg glalavgilv ddatvtieni erhlhlgtrr
      421 aapsvpsgpl ggqrpqeawg ssfstslhda ilegageiav pafvstlcic ivfvpmfflt
      481 gvarflfvpl aeavvfamla syvlsrtlvp tlamllfrpr qagtgpdrst srfarihhaf
      541 nnaferlraw yivllsmllv rrrfyamcfl gfcvlstglv fvlgrdffpn adsgnirlhl
      601 raptgyriee tarltdqver vireavppde lgaivdnlgl pvsginlsys nsgtigsldg
      661 ellialkpgh ratahyvqtl rtllprrfpg vefffqpsdi itqilnfgqp aaidvqvlgn
      721 dlasnmtias slmkkirhip gavdvhvlqr ndeptlvadm drtrmqqlsl saqnvaqnml
      781 islsgssqtt psfwinprtg vqyplqiqtp qynissiddl lgtpvsasvr tgmppqllgn
      841 lvrihpvasp avvthynirp aidlyvsveg rdlgsvagei drivsdarat lprgtelsvr
      901 gqvetmrtsy lglgagvama ivlvyllivv nfqswldpli iisampaala giawmlfvtg
      961 thlsvpaltg aimtvgvata nsilvvsfar qrlaagappl taaleagatr irpvlmtala
     1021 miigmvpmal glgegaeqna plgraviggl lfatvstllf vplvfggvha rlarrrarqa
     1081 gh
//
LOCUS       WP_175803621             257 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia ambifaria].
ACCESSION   WP_175803621
VERSION     WP_175803621.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..257
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28064
     Region          3..253
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 myrldiervs wspggalavl davtltvaag efvglvgpng sgktsllrcv fryarpdagr
       61 valdaqdvwr mrpralaqrv avlqqetpdd fgltvdelvg mgrtphqraf egenaddrri
      121 vdaalrdvdl ierraqrfas lsggekqral laralvqqpe lllldeptnh ldlrhqlell
      181 arvrrlgiat latihdlnla aaycdrlhvl ahgrvvasgt psdvltdall rdvfgvaalv
      241 drhpvtgrpr itplhpe
//
LOCUS       WP_175803656             294 aa            linear   BCT 11-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Burkholderia ambifaria].
ACCESSION   WP_175803656
VERSION     WP_175803656.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..294
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33565
     Region          77..261
                     /region_name="CE4_NodB_like_5s_6s"
                     /note="Putative catalytic NodB homology domain of PgaB,
                     IcaB, and similar proteins which consist of a deformed
                     (beta/alpha)8 barrel fold with 5- or 6-strands; cd10918"
                     /db_xref="CDD:213023"
     Site            order(81..82,176,180,216..218)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213023"
ORIGIN      
        1 misgkamlre ilsrcvmmfg idhmvrallw rdrvaillyh dpdpatldrh ltylkticdl
       61 vpldarglpg ngrpraaitl ddglagnarl lpifikhkvr ptiflcsriv crprrhwwlh
      121 paaerlgver lkrlandqrl aelrvhgfeq dgddeptgln lqqleamrpf vdfqahtrfh
      181 piltrcgdse ckeeiiesrh evealtgnrc ehfaypngny gkreinllka agyksartcd
      241 vgwndhrsda frlktiiidd raslrwficn ltgipsflgy lrkggglrgh fpqf
//
LOCUS       WP_175803661             163 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia ambifaria].
ACCESSION   WP_175803661
VERSION     WP_175803661.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 163)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..163
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17900
     Region          27..158
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mnasapaasa raddldwrwk pfdaltarel yaildarsav fvveqncvyr diddadqaaw
       61 hlaaydpagr lagylrvllp daqntdvrig rvlttapfrg aglgnalisr alehiraqwp
      121 dtqmslhaqa hlqrfygafg ftpnsdvhde dgiphvwmts arg
//
LOCUS       WP_175803666             311 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Burkholderia ambifaria].
ACCESSION   WP_175803666
VERSION     WP_175803666.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..311
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31478
     Region          2..310
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtilviaehd nasikaatln tvaaaakigg dihvlvaghn aqaaadaaak iagvskvlla
       61 dapqlaegla enveatalni akdyshilap ataygkniap riaakldvaq isditavdsa
      121 dtferpiyag naiatvqssd pikvvtvrat gfdpvaavgg saaverieaa adagksqfvs
      181 revtkldrpe ltsakiivsg grglgsgeny tkvlepladk lsaalgasra avdagyvpnd
      241 yqvgqtgkiv apqlyiavgi sgaiqhlagm kdskvivain kdpeapifsv adyglvgdlf
      301 alvpelvsel g
//
LOCUS       WP_175803770             400 aa            linear   BCT 11-JAN-2025
DEFINITION  benzoate/H(+) symporter BenE family transporter [Burkholderia
            ambifaria].
ACCESSION   WP_175803770
VERSION     WP_175803770.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..400
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41619
     Region          11..399
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mqpntspgai rsigndwsvs aitagflavl isyagplaif fqasqaahvs nemvtswvwa
       61 isigagvsgl faswklkvpi vtawsapgta llvglfpqlt lnqavgayit aaliilvigi
      121 tgyfdrlvrh iprgiacgmm agillpfgmh afsaataqpv lgfgmiaayv ifkrllprys
      181 ivlvlltgaa latllgmtql gsespsiarp ifiapewtlg ttlslalplv vvsltgqflp
      241 gmtilrvsgy htsarpiitt tsvmslvvac fggitivvaa itaalctgkd shedpdrryi
      301 agiangvfyl igglfagtiv tlffalpkaf vailaglali gaiganvhgi fededhreas
      361 vitflatasg mtwlglgsaf wgivigsvay avlskvrrra
//
LOCUS       WP_175803803             401 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175803803
VERSION     WP_175803803.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..401
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42271
     Region          17..385
                     /region_name="MFS_MJ1317_like"
                     /note="MJ1317 and similar transporters of the Major
                     Facilitator Superfamily; cd17370"
                     /db_xref="CDD:340928"
     Site            order(27..28,31..32,35,68,119..120,122..124,127,147,
                     150..151,154,228,231..232,235..237,240,267,271,320..321,
                     325,329,345,348..349,352..353,356)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340928"
ORIGIN      
        1 msvpspiagk paiprtvwal glvslfmdls selihallpi ylvstmgmsv valgilegaa
       61 eatamivkvf sgaisdwlgr rkgllllgyg laaftkplfp lastpavvvt arlldrvgkg
      121 irgaprdalv advappeirg acfglrqsmd tvgaflgpll aialmllfad rirtvlwfav
      181 vpafiaiali vfgvrepdra esqrrfrspl rwralrafpr sywfvvaaga tftlarfsea
      241 flvlraqqtg ldaawipavm vamsvtysls awpvgilsdr ldrrvllaag mvlliaadll
      301 lgigastism fvgvavwglh mgftqgilaa mvsetspaal rgtafgvfnl vsgtcmllas
      361 siagalwthf gasttflaga alvvvplclc rfmprpgtsa a
//
LOCUS       WP_175803815             231 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cenocepacia].
ACCESSION   WP_175803815
VERSION     WP_175803815.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 231)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..231
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=24589
     Region          5..226
                     /region_name="ArtM"
                     /note="ABC-type arginine/histidine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4160"
                     /db_xref="CDD:443325"
ORIGIN      
        1 mndflslivq sgpdvargiw itlellvlsc tlafalavpl avartsacrw lstpsrlfms
       61 vfrgtpllvq ifvlyyglaq fsivrasplw llvggsfsca lcaltlnlaa ymaedirggi
      121 agvpagekea alafgmsrfm ltwfvivpra igivaptlgn eivlqlksta lastitvldl
      181 tgvarrisie tyttdalmla givyvgitav lstvlkrveg rlnrhlgsvr a
//
LOCUS       WP_175803827             286 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia ambifaria].
ACCESSION   WP_175803827
VERSION     WP_175803827.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15202679
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..286
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30487
     Region          12..132
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          168..273
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 madlnpsrtl tyrpfvdtdl paahrlseav kwphrlddwr falqlgggfv aedesgvvgt
       61 algwrfddah aslgmvivsp erqgrgigre llarvvdslg prtiflhatp sgeplyvkfg
      121 feaiatidqh qgaafqppli slppgerlrp lgtndgprla alasraagye rgavidalld
      181 vangialdrd gellgfalfr rfgrghvigp vvapdalraq alishwlalh egmfvrldvp
      241 gdsglsdwlq glglprvdtv vamargaapa rdpalrafai vnqalg
//
LOCUS       WP_175803849             261 aa            linear   BCT 11-JAN-2025
DEFINITION  TniQ family protein [Burkholderia cenocepacia].
ACCESSION   WP_175803849
VERSION     WP_175803849.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Li,Z., Zhang,H., Xiao,R. and Chang,L.
  TITLE     Cryo-EM structure of a type I-F CRISPR RNA guided surveillance
            complex bound to transposition protein TniQ
  JOURNAL   Cell Res 30 (2), 179-181 (2020)
   PUBMED   31900425
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Kholodii,G.Y., Mindlin,S.Z., Bass,I.A., Yurieva,O.V.,
            Minakhina,S.V. and Nikiforov,V.G.
  TITLE     Four genes, two ends, and a res region are involved in
            transposition of Tn5053: a paradigm for a novel family of
            transposons carrying either a mer operon or an integron
  JOURNAL   Mol Microbiol 17 (6), 1189-1200 (1995)
   PUBMED   8594337
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10534787
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..261
                     /product="TniQ family protein"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=30087
     Region          1..125
                     /region_name="TniQ"
                     /note="pfam06527"
                     /db_xref="CDD:461938"
ORIGIN      
        1 mpdealsgwi hrvcmhhgik pgslmrrwgf eaptsaldfy pigrpillri asttmcnmed
       61 ldeatyldht ilgksrfscl tndfsesrpi yrycpsclkg devshfkisw rfaynficei
      121 hrcplfdacv ycgrrvdltw kfpcrpgqva iwetsfcyhc ttplhtepsn picdeianqm
      181 ivfqrwfher vrrggvsdlg ipelapmfvg rylrsipser ssivhyvgld mdklfgrdwr
      241 dlaqqipcmy ssgrvvpeee a
//
LOCUS       WP_175803885             243 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Burkholderia cepacia complex].
ACCESSION   WP_175803885
VERSION     WP_175803885.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..243
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=26912
     Region          13..218
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 msgqpsmien hllaalpved lahispqlvl vdmplgkvly esggalshvy fpttsivsll
       61 yvmedgssae iaivgndgli gialfmgget tpsraivqsa ghayrldari lkdefrrggs
      121 mqrlllrytq alitqmaqta vcnrhhsidq qlcrwlllsl drlpsselkm tqelianmlg
      181 vrrsgvtaaa lklqdaglir ynyghievld rsglekrvce cygvvrrefd rllpdlkrle
      241 krr
//
LOCUS       WP_175803961             790 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor [Burkholderia cepacia
            complex].
ACCESSION   WP_175803961
VERSION     WP_175803961.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 790)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 790)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..790
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85965
     Region          72..773
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msftfaarps rgrlalacaa afawpaayaa stddvraeat rgggvdrpat tataapaagg
       61 vaasaapagd tltavsvtaq rqpvdpdtpa vvtsitreqi dahtnvtted alkyvpnlmv
      121 rkryigdrns ifagrdfnel qsarglvyad gvllsnllgs syaypprwsl ippddiarvd
      181 vlygpfssly pgnaigstvl lttrrpeqle aslstqfftq ryhdgygfad sfggnhqtar
      241 ianrvgrfwf alsldrlenn gqpmqyaspn saynpklgaa vpvtgaatdl gpngkprtiv
      301 gaqtierteq lnetvrmgya ftdhvdatlt lghwenhyrq hgetflrdaa gnpvyggnvs
      361 iggqnmtvap nafapqrgdq enwlyalgln grldsgwrls gvvsaydvsr dvlraastvq
      421 ggagtlfqgd gtgwrtldlk aeapvvkght ftfgyhydny flrnvtynta dwlagpttsl
      481 asvyrgdtrt qalfgqdawr faprwlatlg lryerwdayg galgnargtl gyadrganal
      541 spkvalqwda tevwrfrlsf atgtrfptvg elfqgtisnn aivnnnpnlr pekaidwdft
      601 aerdvgvgvv rasvfqsdlr dsiysqttvs gattvtnvsn vdrvrvrgve lafsgenvgv
      661 rgldldanvs asnaqilada anpayvgsrf priprmranl lasyrfdehw ltsvgvrysg
      721 rqfntldnsd vnpdvyggts sftvvdlkar yrfdrhwtas vgidnvtdrr yytfhpypgr
      781 tfygelkwsl
//
LOCUS       WP_175804019             241 aa            linear   BCT 11-JAN-2025
DEFINITION  SMI1/KNR4 family protein [Burkholderia ambifaria].
ACCESSION   WP_175804019
VERSION     WP_175804019.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10558574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..241
                     /product="SMI1/KNR4 family protein"
                     /GO_process="GO:0042546 - cell wall biogenesis [Evidence
                     IEA]"
                     /calculated_mol_wt=27029
     Region          123..221
                     /region_name="SMI1_KNR4"
                     /note="SMI1 / KNR4 family (SUKH-1); pfam09346"
                     /db_xref="CDD:430545"
ORIGIN      
        1 mielpahaya aelkrfratg svwlaaheip agvevpptwl allsapddrv adelvqmwag
       61 vidrlpaiaq ffrdklarpv vfrsddgdvm llypytvesg dlnffiarmp lgerapvdes
      121 fwctlpddlr lfyanvhdgw tffpansigp mpigdqtalt dkldltpdet rklgvnpdlv
      181 wtifqngsgd ylcldlrdsa gdgsaagrlw whenptelep vdfwavmntw feifveeadk
      241 r
//
LOCUS       WP_175804029             212 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Burkholderia cepacia complex].
ACCESSION   WP_175804029
VERSION     WP_175804029.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..212
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23097
     Region          4..195
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mnayrlylsp gacslaahia leetgapfdv eivsvreqqn learylainp karvpvlaip
       61 geprvltetp ailtylarry pdaqllpldd plrearchew lawlvgwvhg vgygalwrpg
      121 rfiddpalhg avsahgrgti daanasieal ladgrtwaep gahsivdpfl lvlyrwggai
      181 gldmtrhpaw tahaqreaer paarralare aa
//
LOCUS       WP_175804051             512 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175804051
VERSION     WP_175804051.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..512
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52244
     Region          16..444
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,142,
                     145..146,149,273,276..277,280..282,285,313,317,371..372,
                     376,380,396,399..400,403..404,407)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtlsdsrrna valaavclts lmfgleissv pvilptlehv lhgdfngmqw imnaytiact
       61 tvlmaagtla drfgrkrvyv igtvlfgats llcglapsvp vlvagrllqg asggamlicq
      121 iavlshqfre grergrafgi wgivfgiglg fgpivggaiv alaswpwvfl vhaplaaval
      181 vliggavres rdphagtldv agivtlslav lglaftitqg aelgltsaag lgvlgatvla
      241 lagfvvaerv sarpmfdfsv friraftgai fgsmgmnfsf wpfmiylpiw fqvalgydsv
      301 taglallayt lptlvappfg erlalrygpg vvipcglfti sagfvlmrig sgvdhaswvt
      361 mlpgcviagi glgltntpvt ntttgavpgs ragmasgidm sarmislaln iatmgfvlva
      421 givaslkagv agavdagalr alaqqiasgr pdglqaiapa laradptgta lhaalvhgfg
      481 wvmvygaagv avlatasava faparrrgav ce
//
LOCUS       WP_175804166             468 aa            linear   BCT 11-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Burkholderia ambifaria].
ACCESSION   WP_175804166
VERSION     WP_175804166.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..468
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=48024
     Region          2..458
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mtmlslgeaa rlipgatvhg dpdttfervs tdsrtvgpgd lfvalkgdrf dahdflgdva
       61 argaaaalva hvpaglampv veggetraal galahgwrkr favplvavtg sngkttvkem
      121 iasifaaavg adarlatagn lnndigvplt llrlsgahrv avielgmnhp geteilarla
      181 aptvalvnna qrehqefmat veavalehaa vihaltpdgv avfpaddaya giwrvaatgn
      241 pildfalhdg erqveaqvtg rlhggelaid tpsgamtvhl ralgehnarn alaaaaaala
      301 agielaaikq glesfepvkg rlqvrqadvg slagatvvdd tynanpdsmr aaidvlaaqp
      361 aprvlvigdm gevgdegpaf hreigayare rgidalfalg dasrdactay gdtarhfgdv
      421 galvtallaa gygaqatvlv kgsrymkmer vvdaltnqpa agtvpaah
//
LOCUS       WP_175804175             784 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia ambifaria].
ACCESSION   WP_175804175
VERSION     WP_175804175.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 784)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 784)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..784
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85162
     Region          66..766
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msftfaarps rgrlalacaa afawpaaqaa aidgasaepv pggsgnpagr aasvaavvpa
       61 ppgdtltevs vtarrqpvdp dtpavvesit reqidahtnv ttedalkyap nlmvrkryig
      121 drnsvfagrd fnelqsargl vyadglllsn llgssyaypp rwsliapddi ervdvlygpf
      181 salypgnaig stvllttrrp dkleaslstq fftqryhdgy gladsfggnh qtarianrig
      241 kfwfslsldr lendgqpmqy aspnsaynpk lgaavpvsga vtdigpngkp rtivgaqnie
      301 rteqlnetvr mgyaftdrvd atltlghwen hyrqhgetfl rdaagnpvyg gnvsiggrnm
      361 tvapsafapq rgdqenwlya lglngrldsg wrlsgvvsay dvsrdvlraa stvqggagtl
      421 fqgdgtgwrt ldlkaeapev kghaftfgyh ydnyflrnvt yntadwlagp ttslasvyqg
      481 dtrtqalfaq dawrfapgwl atlglryerw dayggalgna ggtvgyadrg analspkval
      541 qwdatdvwrf rvsfatgtrf ptvgelfqgt isnnaivnnn pslrpekaid wdftaerdvg
      601 igvvrasvfq sdlrdsiysq ttvsgastvt nisnvdrvrv rgvelgfsgr nvglrgldvd
      661 anvsasnaqi ladtanpayv gsrfpriprm ranllasyrf dehwlasvgv rysgrqfntl
      721 dnsdvnpdvy ggtstftvvd lkaryrfdrh wtasvgidnl tdrryyvfhp ypgrtffgel
      781 kwsl
//
LOCUS       WP_175804105             308 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175804105
VERSION     WP_175804105.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..308
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33582
     Region          34..186
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <174..293
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mdmtdiaasr esgrlelasl igrfapadgs httavpalml hrhahpvdlg cgvsraalvi
       61 aaqgakrviv agqtyeydtq nclitsidlp ilsrvtrasp dapylclslt ldlqrivela
      121 aemrlpepea gpegegiala eltpplldaa lrllrlldtp adipvvapli ekellyrlmt
      181 sgqgtrlrhm avagsqthri araiewirdh yaepmrvdtl aqavnmsvss lhhhfkhvtt
      241 lsplqyqkql rlhearrlll rqggdvgsva aavgyesasq fsreysrlfg appmrdvvhl
      301 rkkellgt
//
LOCUS       WP_175804179             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175804179
VERSION     WP_175804179.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45785
     Region          21..426
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(34..35,38..39,42,81,139..140,142..144,147,167,
                     170..171,174,257,260..261,264..266,269,297,301,353..354,
                     358,362,378,381..382,385..386,389)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msasppavah atgsagavsh rrivfasfig taiefydfyv yataaalvig pvffphgsat
       61 aqalsafvtf giafiarpig sflfghfgdr igrkstlvas llvmgmstta igfvpgydti
      121 galapvllcv lrfgqgiglg gewggaalla tehapqgkrg wfgmfpqlgp svgflmsngl
      181 ffalalslsd eqfrswgwri pflvsavlva vglyvrlkit etpafqatld rnervrvpva
      241 tlvsqhwrpt llgalamvvc ytlfyistvf slsygvstlh iprqsflgll cfavvfmgla
      301 tplsawasdr fgrkpvliag aiaallsgfa mepllgsgsm plvalfltle lflmgvtfap
      361 mgallpelfp tnvrytgagv aynlggilga siapyiaqll aahgglswvg gyvsvaaais
      421 ligvllmret rdasll
//
LOCUS       WP_175804225             765 aa            linear   BCT 11-JAN-2025
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Burkholderia cenocepacia].
ACCESSION   WP_175804225
VERSION     WP_175804225.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 765)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 765)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 765)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..765
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=83567
     Region          212..613
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mkqrllvavi lsvfsgaavl gagrllhlda mtdpveitav iglilalcml wgvcasavll
       61 ktattldrvv agglfalval tglavagqfa gatlfaklek lpdsavglwt lrdywhafgd
      121 ikavkrslqi ataasilvpl vpvaaviaal vmkpkrelhg darfahsyei rryglldean
      181 grtrvkgdyr dptiivgryk gkyltfrgte fvmvaaktrs qkgvaivipn lltfsdsvvv
      241 ldvkgenfdl tsrfrqscgq kvfrwapfdq agythrwnpl fkiakspafv rvgrlqaiaa
      301 rlyhtadarn kffyeqasdl fmglalyqme mtgdctfgqv lrlattpdkk vrehltelmq
      361 hepqkgvpls gdclgalsrv laspdetmln ivatfnaglr lfsnpivdqa tsacdfeldr
      421 vrrelmsiyv vmpvrelava sllgnlfytq wiednldvlp gedptikyqc lgvgdeftal
      481 grievldkgn afiagywirl ltilqskaql epnelygpag artlitnhav lvayapgnqq
      541 dakelsetlg tftekatsks rnhgrntstg tstsdqgral mldqelkrme qheeivlgfq
      601 rpilcekaty ytddlfidrm rsvspmlaai dkrlpteeei kaawragelr atgiptnnpe
      661 tfhavlsaka ageirlarqa gakpltaael laldqqkpgp latdtalagf eadlaelgml
      721 vrddvremla girfdfnlaa tdvavdsqie paapadnevk evahg
//
LOCUS       WP_175804284             294 aa            linear   BCT 11-JAN-2025
DEFINITION  adenylate/guanylate cyclase domain-containing protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175804284
VERSION     WP_175804284.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..294
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=32241
     Region          <15..206
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 mesnwrnyts ddsddrlrei ldapagayee ldyipdrarl tytngfyvnc tavfidirgs
       61 snltsmhttp vlgkiyrayi secvallnty rqckeifiag dcvsgifntp gkvdilealv
      121 aaaslnslin hlnwrlekkg ytpikcgigm sygralmlks gytgsglndi vwmgdvvnda
      181 snlchqgnkn gqlpvqvatv vyqnldaypk sllspvyesf lpigithyqg dvihkgmqnw
      241 ldnkktvass nslaalmqia ggqiptpphs svdssqntla sllypstkkk inwl
//
LOCUS       WP_175804339             414 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia ambifaria].
ACCESSION   WP_175804339
VERSION     WP_175804339.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..414
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44139
     Region          12..414
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mteantqeqp aprtvvvigg gqaagwvlkt lraegfagrl vmiadephlp yerpplskav
       61 lagdadietv rvvrpdefdt lnveawqper aasidrarrv vktesgreie ydrlviatgg
      121 tsrrlpdalv ntsnlhylrt ldeaaalgek lrasrrvlvi gggwigleva atarklgvea
      181 vvvegaprlc grsvprivsd flldlhrang vdvrlgaala sldaqpddas kvratladgt
      241 tidadfavag iglalnasla sdaglalddg ivvdefgats dpaifacgdv anhhngwlkr
      301 rvrleswana qnqaiaaaka vlgvrapyae ipwfwsdqyd vnlqilgdlp adaqlvvrgd
      361 laarratlff lgdghvrgvi ainnarelkl arkwmnqgra vdtealadtt kala
//
LOCUS       WP_175804386             445 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: carotenoid oxygenase family protein [Burkholderia
            cepacia complex].
ACCESSION   WP_175804386
VERSION     WP_175804386.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Poliakov,E., Uppal,S., Rogozin,I.B., Gentleman,S. and Redmond,T.M.
  TITLE     Evolutionary aspects and enzymology of metazoan carotenoid cleavage
            oxygenases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1865 (11), 158665 (2020)
   PUBMED   32061750
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Sui,X., Kiser,P.D., Lintig,Jv. and Palczewski,K.
  TITLE     Structural basis of carotenoid cleavage: from bacteria to mammals
  JOURNAL   Arch Biochem Biophys 539 (2), 203-213 (2013)
   PUBMED   23827316
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Kloer,D.P. and Schulz,G.E.
  TITLE     Structural and biological aspects of carotenoid cleavage
  JOURNAL   Cell Mol Life Sci 63 (19-20), 2291-2303 (2006)
   PUBMED   16909205
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Wyss,A.
  TITLE     Carotene oxygenases: a new family of double bond cleavage enzymes
  JOURNAL   J Nutr 134 (1), 246S-250S (2004)
   PUBMED   14704328
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..445
                     /product="carotenoid oxygenase family protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006720 - isoprenoid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48912
     Region          8..439
                     /region_name="COG3670"
                     /note="Carotenoid cleavage dioxygenase or a related enzyme
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]"
                     /db_xref="CDD:442887"
ORIGIN      
        1 mtvfdlnrga lapvadevdi velrvtgaip reldgtllrn gpnppggrfe gndmlswwpe
       61 aamlhaiafd dgraagyrnr wartrrwaav hapgqvphlp dtnpnvnvlq hagellalae
      121 ggaplaitaa ldsfgvparh agfdgamtah pkvdpvtgel imfradwrap wlrygvvdaq
      181 gvprvdleie lgapsmmhdl aitetrslll dlnvgydfsl lkqghrmplr whddrparig
      241 vlprhggdvr wfgvepcfiq hvvnaydcda scivldavry psflrldtrt grfadnpvge
      301 lwryvidtan glidegplad ggielprine srtgrryryl yaveqpnnae mrgvmrfdha
      361 rgttthyavp agdqngepvf vprpggaded dgwllvmvyr aatdtsdvvi ldaraidagp
      421 vatvhlprrv pagfhgawvp rerrt
//
LOCUS       WP_175804400             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175804400
VERSION     WP_175804400.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32781
     Region          13..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..295
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(106,110,149,163,165,230,247,274)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(107..108,112..113,115..116,119,123,125..131,193,
                     224..228,235..236,239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mafdsrllsg igvlsaviea gtfarageam gltqpavsra varleervgi rifnrtarai
       61 tltdegrrfy eavapllagi eeaavdagrs rarvrgrlrv nvdgtfghyv laprmaefld
      121 rfpelsveis vrdrmgdlva dgfdvavrfg ipepssyrar lllethvltc asaayvarhg
      181 eprhprdlad ghrcvlirdp vtgrpygwef hrgdevvpfd stgrltvndt gallgacvgg
      241 egvaqllely ardilaegrl vqllpewade tfplyayhha snlvsakvrv fldfvreltg
//
LOCUS       WP_175804412             806 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia
            ambifaria].
ACCESSION   WP_175804412
VERSION     WP_175804412.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 806)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 806)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 806)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 806)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..806
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=84969
     Region          71..803
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mpvpttrtal haagparyar pvaavlalal alhagtgcaq tapvqvaavp vlvqaptsvp
       61 aplptpasda lfldvsvnge pthriarfqq iggrlyaasa dlndlgiatn drtndrtpep
      121 snvlvaldtl aglrydydag rqtldlrvpd alriphtfdt ralaaappat sgrgfvlnyd
      181 ayaqtiahap lavwsearyf dpygvfsstg vaylyddrrr yvrydtswsh snpgtltttq
      241 igdtisssls wtrslriggv qwrsnfglrp dlitfpvpal sgsavvptsv dlyvnnvrqf
      301 sgnvpsgpfv insvpgitga gnatvvtrda lgrsiatsip lyvdtrllap glasysaeag
      361 flrraygids fdyartpaas gslrygiser ltveahaeat agvynagaga lahlgergva
      421 naslalsapg rtgvqagigy qyvtprfsid aqtlrafgdy sdlgsregvp vsratdrvtv
      481 sfpflrrqtl sfsylglryp gvaasrigsi aylvnlgglt sitfsgfqdf rqrdtrgffv
      541 slsiglggnt svsanagrqn gdstytlsat rppdygggvg wnvqaganag mryaqgqlqy
      601 lgragevtll aqsfdghrna svdvtgaivl mngqlmtarr vddgfalvst dtgrvpvlhq
      661 nrmigetdra gyllvpdlna yqsnrvaidg talpadaria dttldvvpqa rsgvlahfav
      721 trysaasial rapdgtplpp glevrhvesg qrtivgydgl tfvdglvann hleisgggrd
      781 cavafayrrp ddgtlprigp ltcgpr
//
LOCUS       WP_175804424             344 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia ambifaria].
ACCESSION   WP_175804424
VERSION     WP_175804424.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..344
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36185
     Region          109..316
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mkivkpllia aavaatlsia stafaagaed arpdvatsgf laalngqkgp gletlspaka
       61 rqvlvdaqng akvdlsgidv snrtieqdgl svpitivrpq gatgtlpvfm ffhgggwilg
      121 dfptherlvr dlvvqsgava vfvnytpspe ahypvainqa yaatkwvaah gaeigvdgsr
      181 lavvgnsvgg nmaavvslma kdkggpairf qglmwpvtdh nfntgsynay qqghfltrpm
      241 mkwfwdaytk neaqrndiya splrastaql kglppaliqv aqfdvlrdeg eaygrkldaa
      301 gvdatttryd gtthdfglln alaadaptka atkalaneia trlk
//
LOCUS       WP_175804467             392 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia ambifaria].
ACCESSION   WP_175804467
VERSION     WP_175804467.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 392)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..392
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39877
     Region          168..370
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mtgravasar ritldkvgil igvltiiavv gmpfmvlrpn riaagtglsv faalpsaqga
       61 alaalwivga lwamtasrpa wrlaagctwl atlayavgaa aahvvapndm larvspaagv
      121 wlllfawavl vadalarlaf gpwrrlvala vaiaaisvpl asgwwdglsv mreyavrtdd
      181 fwreairhvs laggsvaaal vagvplgiac ariapvrtvv mpvlnivqti psiamyglmm
      241 aplgllaahv plaaalgirg igvapavlal flysllpias svvvgleqvp phvteaaram
      301 gmtrvqrllg vdlvlalpvi lsgvrivlvq nigltavaal iggggfgtfi fqgigqsaad
      361 lvllgaipti alalaaavvf eaattlakgr ta
//
LOCUS       WP_175804470             291 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175804470
VERSION     WP_175804470.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..291
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32234
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..284
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,220,237,264)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     214..218,225..226,229)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mellndmalf vevvkargfr saaqtlgmpn stlsrrisal ekaiglrllh rttrrielte
       61 agqlyferck rivdearlah eqlggllaep agvlrasfpv dfavtylapl ivefanrypk
      121 ltfdfeltsr rvdlvsepfd vairigpsed sqlvarrlat lrnylyaspg ylaragepre
      181 pedlarhacl glqksgswtl hdgtrsvava vsgrfavnsv gmlrrlatld agiivlseei
      241 laddvaagrl rrvmpewege pipvyamtet rllpaktqhf ieflrahlaq a
//
LOCUS       WP_175804471             370 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia ambifaria].
ACCESSION   WP_175804471
VERSION     WP_175804471.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..370
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39721
     Region          17..347
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(36,38,69,111,239,300,321,323..325)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(36,38,69,111,113,120,187,190,192,239,246,300,321,
                     323..324)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(38,113,187,190,192,324)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            192
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mkqlfvpara dkdapqlfap vrvgrytlan rlvmapmtrs raafdgtpga waaeyyaqra
       61 gvglivtegt qpsddgqgyl ttpgiytdah vagwktisdd vharggrlfi qlmhvgrmsh
      121 pdntphhrqg vapsaiapgv pmftatgmqe ipapraltta evrdtvndfr faarraieag
      181 adgveihgan gylvqqffap nantrtdeyg gsienrarfa ievaaaiade igadrtairl
      241 spgttlwgid egpegtdlyr ylatqldald laylhvmhqg desllaelra rwrgtlilnr
      301 pgrtrdaigv dvasgladle aygqmvlanp dfvtrvktga plndaqretf fggdargyvd
      361 ypvlsgaata
//
LOCUS       WP_175804483             370 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia ambifaria].
ACCESSION   WP_175804483
VERSION     WP_175804483.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..370
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39311
     Region          4..344
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,233,300,320,322..324)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,181,184,186,233,240,300,320,
                     322..323)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,181,184,186,323)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            186
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mssllstydl rglplpnrvv mgpmtrsrap srgqptalma eyyaqrasag livteatnvs
       61 htsaafeltp glvtdeqaag wkqvtnavha nggrifaqlw hggrvssltl lggdaplsps
      121 gvnddleqlq vwarlqngyy tkihatpsra mttdevaatv ddfgraaara maagfdgvei
      181 haangylphq flsstlnrrd dryggsvanr arfleeivda vggvmplsrv gvrispyaqy
      241 nnvrdadpda tyayvgrmld eagvaylhaa dtngwsgepd lprivertrk tfggtlivng
      301 gitpdaanal idagdadlva farayianpd lveriathap lavpksigwy ggeragyvdy
      361 arhdaaapta
//
LOCUS       WP_175804612             921 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175804612
VERSION     WP_175804612.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 921)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 921)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..921
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..921
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=100751
     Region          17..825
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnvqnlaaal rgglseqdrl lkldtplrpn tlvvqravgr atigrdyift ldvvssdsti
       61 elkkliaqpv tlwiqqasgg yrpihgyvyt arrlgadggl ttyqitlhaw mhvlkfrrdq
      121 riwidksved ivsdvlnqhp eargrfrfml sqplanrsyt rqsetdwnfv hrllenegly
      181 sywdqaddgk shtlvitdel dalpalspkt vlfyrsgtqs evdaltqwsg trslqsvalt
      241 trtfdyknpa arsnpkgtsv paagnqgalp sqlevyeytg aytyleqqrg drlsrirmee
      301 wesrakrfhg vggirgldag rrfelgdhpa hdrdsveqre fatiavswwi ennlpvtpas
      361 nfphslhrdl aearasrsds asfevphadg cvgyflveve aqrvtvpyrs pfehekpkmh
      421 letalvvgps geevhtdeln ririqfvwdr vnpgdqgasc wvrvvqadtg ggygsvhipr
      481 igeevlvdhv ggdcdrplvm grvyngaakp qwhsdgilsg yrskeysgag fnqlvmddat
      541 gqsraqlmss agnsilhlgy linqqgntrg aylgtgfdlr tdaygavrat sglyvtthpk
      601 satsqpldvr etqqqlvnae gmlesmseva eqhqadslkp ghdatraftd atrssvsgea
      661 sggrtagggt gsanafkepv mlfgspagig lstqqsahli adihvnlvsg qsthiaagks
      721 liasiadkis lfvqnagmkl faakgkveiq ahkddieiva qksvkvlsat dkievaaeke
      781 vlltsggayi rlkggdieih apgkievkga qhsfsgptsq ayampqfrps yqaqyilksq
      841 vdgspmmqha yeltlpsgrt vlghtndlge tipvftpsaq tvnlraleqe kvetepwkfa
      901 gggqpdiysd yvkerdansr a
//
LOCUS       WP_175804480             302 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175804480
VERSION     WP_175804480.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32753
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,219..224,
                     230..231,233..234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176122"
ORIGIN      
        1 mklsfealea ldaidrtgtf aeaaellhrv psalsylvqk legdlgvalf drsgrraklt
       61 hagrvvveeg rrllhaaeql elkaqraqqg wetelricid eilpfdalwp hvhafyglam
      121 dtrlrlstev lggtwdalva rradlvvgat geppelpgiv trpigtlkhv favapthpla
      181 alpeplsmas ivehrgavis dtsrelqprs vavdagqptl avptlaakla aqceglavgt
      241 lpdciaarai aqgklvarqv igmrdtthcy mawrsdeagr alrwwveqld rpdlvdrfla
      301 la
//
LOCUS       WP_175804754             835 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175804754
VERSION     WP_175804754.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..835
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=91178
     Region          16..763
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msgevllkvl rggyaqfdri vkldtplgdd wltplyvkin arlgrnfevt vdassvmgdk
       61 iklsalmlqp vtlwirqtdg gylpihgyvq rarrlgndgt vsyfqlqfss wlsflklssd
      121 rrdwqeasgw qiladvfdkh pqasgnygqe lraamrsysh rvqwetdwnf vhrsleevgv
      181 fprfdfakdg kshkvvmmdd lyfgpslpns emkfshagtd edfdgltqls eqqdaqsatl
      241 tlgtadykrp dldkqvsmpa adledlpgqg edylytgsqt waesdigqqq arirteewas
      301 rakryfaigs pryalpgywf kvsghpvlda lpeeerelsi iasdwliqnn lpgldaltrf
      361 prslrseieh vqaagtgatv shrdggvgff hveieaqrrk tpfrspfehe kpemhlqtai
      421 vvtdsdeeia tddgnrvrvr tsnsrndrnt kstswiraam pdagakrggy fplrkddqvl
      481 lgfvngdcdr pviisrlhgg atmpvwhthg llsgfrsrey ggdgfnqlvl ddasgqnrvq
      541 lsttsyashl hlgylieqsd ntrgsfvgsg fdlkseahga iravqglsis thpaavqpmn
      601 vsaatdqlaa seavfetvsq asetnraesl qdgsdalkaf temtqhsvpg atkggrtagg
      661 gtgnasgfak pallvsspag iglssqqsih asanqqvnlv agknvnlaaa ksllasvmdk
      721 islyaqnlgi kifatkgpie iqaqndaltm laqqdvkies asgrmilrae kelilnvggs
      781 yikitpdmie ngtsgqilek caswdkpgas tmtlrdplng tpvskhggya ddfsg
//
LOCUS       WP_175804796             194 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Burkholderia pyrrocinia].
ACCESSION   WP_175804796
VERSION     WP_175804796.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..194
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22341
     Region          18..185
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mespptsrtm tdpdrditai vtrertrlvs firrrirdpd daedilqdvf hefvqayrlp
       61 apieqvsawl fraarnrivd rfrkkkeqpl tdlfeaedea nseyrldlal pahdagpeal
      121 yartlvlkal qdaldelpan qrevfvahel dgrsfkemaa qsdvalntll arkryavlhl
      181 rarlqliyde ldnt
//
LOCUS       WP_175804872             472 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia ambifaria].
ACCESSION   WP_175804872
VERSION     WP_175804872.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..472
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=50778
     Region          83..470
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mtarpafpsp dasgaaaprs parvlrraaf vlgaavlgyg afaiafpart paaigdvvad
       61 wtganphpvv lqrpaaqpls avaqlgralf adpslsasgk qscaschspd haygppngld
      121 vqpgglamtq qgyrpppslm ylyrqpnfsi gpdagendaa psvaqqaaaa agvvkaqkva
      181 gtsaapqlvp qggmfwdgra dtlqqqafgp llnpvemana svdevarkla qsphraqfeq
      241 lfgarvfssp qllvseamfa iaryqvedps fhpynskydr wlegrarltq aelrglrlfn
      301 dpdnancagc hlsrpgkdgl ppmftdyqye algaprnhal aqnrnpafhd lgvcgpfred
      361 lkdqtqycgm fltptlrnaa trqvffhngv fhtldqvmaf ynersispqk fysrgadgkv
      421 deyddippqy ranvdvtdap fdrkpgdkpa mteqdikdiv aflgtltdep ar
//
LOCUS       WP_175804900             424 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia ambifaria].
ACCESSION   WP_175804900
VERSION     WP_175804900.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..424
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41806
     Region          5..>328
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpshadspav hhagsltifq gaalyigavl gtgvialpal aaevagpasl lawaalvvls
       61 gplaatfaal garypdaggv styarrafgp kaaaivgwcf yfavpagapa aamfggayva
      121 avtggghvtv ivtaaaliat vsaanafgvt vsgrmqlvls allvtlllaa vlasaphart
      181 anlhpfaphg wlavgqaaal lvwsfagwea ithlaaefrr pahdmprsaa iavvvvgfly
      241 lsvaaasvtv lgpsagasga plaeliaggi ggharvlaat aavlltlgtm nayfagaakl
      301 gaalgrdgal pawlaqgsqv ggvprrslgv iavlaavala attisdvgpk plvlvtsgcf
      361 vmvyglgaaa alkllprggi ayrcawislv avaglflttg wyilcpllla ggallylwta
      421 gprt
//
LOCUS       WP_175804959             118 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease [Burkholderia ambifaria].
ACCESSION   WP_175804959
VERSION     WP_175804959.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..118
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12819
     Region          47..111
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mpvrpmkpck hrgcgvlvag gkthcdqhvn eavkwkpdav rgnrhargyg sawerirlri
       61 lrsasglcqp clqagrvtsa tsvdhivpka rggtdcdenl qaicqdchaa ktarerlr
//
LOCUS       WP_175804980             681 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA cytosine methyltransferase [Burkholderia ambifaria].
ACCESSION   WP_175804980
VERSION     WP_175804980.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 681)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..681
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=73942
     Region          17..>232
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
     Region          <596..666
                     /region_name="AdoMet_MTases"
                     /note="S-adenosylmethionine-dependent methyltransferases
                     (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes
                     that use S-adenosyl-L-methionine (SAM or AdoMet) as a
                     substrate for methyltransfer, creating the product
                     S-adenosyl-L-homocysteine (AdoHcy); cl17173"
                     /db_xref="CDD:473071"
ORIGIN      
        1 mkrdnftmpl dlgseliidn faggggtstg lerafgrpvd iainhdpeal amhalnhpht
       61 khlcesvwev dpiavtnnrp vglvwlspdc khfskakgat pvsknirgla wvgmrwialt
      121 kprvlmlenv eefqdwgpli ieadgnarpd pkrkgktfes fvrqlrqhgy kvdwrelrac
      181 dngaptlrkr lflvarrdgl plafprptha eptsaevlrg ilaphrtaae cidfsiaaps
      241 ifdrqkglvh ntlrrvakgm wrhvlasptp fivpsadgvs apfvnehana snqrtmrade
      301 plrticaqvk gghfsvvapt mvklrgtsea hlradsveqp lstvsaggnh halasahlit
      361 igygeragqr prtqeitapl gtvvaggvkq aivaahitkf rtgsagasld dpmptvtans
      421 fvrrpggsap lgivsahlmh vthhgdrags tpahplptvt gahrgeqala aaffeqangg
      481 fwedndgrpa taplstiask ganqrlvtay lvkyyssggq wqdigapmht lptkarmglv
      541 qavkvpaacl seehaekahk caallrehlp eefiedadmv mmyhagawwv lvditlrmlk
      601 drelyraqgf pdsyiiheip dpkllfvdgv qvpgdprdvp riplsitari rmcgnsvspm
      661 qsealalvnf aheqkfahaa a
//
LOCUS       WP_175804999             242 aa            linear   BCT 11-JAN-2025
DEFINITION  chemotaxis protein CheW [Burkholderia ambifaria].
ACCESSION   WP_175804999
VERSION     WP_175804999.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..242
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=25507
     Region          81..236
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mnrdavatdd ttigvddcwn rigtrgdrsc erladclrcl ncpvyayhaa kllerplgat
       61 emadatrris afdatgahgg ddtrqaalaf rvadewlalp igvlreiagt rrihslpyrr
      121 hsavrgvvni rgtlriaisi gallgleagn ggsgggssgg ssggdgrftr llvaahqgep
      181 vvfpvdeveg vlrfgasewv pvpatvgras aglsrgvlsw rgksvglldd drlfdavtrs
      241 mr
//
LOCUS       WP_175805001             170 aa            linear   BCT 11-JAN-2025
DEFINITION  chemotaxis protein CheW [Burkholderia ambifaria].
ACCESSION   WP_175805001
VERSION     WP_175805001.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..170
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=18444
     Region          14..152
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mtraeshggt halflmfeld geryaldaad idevlplatt kvvpgapdwi agllmrggqp
       61 vpvidvpmla lgrrahvlrs trlvmvryrv epldrervig liveratqtl ridrtafras
      121 gvstartrwl ghvantpdgi vqqvsvsdli ddvarlylfd glpghggesa
//
LOCUS       WP_175805015             743 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia ambifaria].
ACCESSION   WP_175805015
VERSION     WP_175805015.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..743
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79727
     Region          52..743
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mtvnrttasp arrrrakvgv gvglgitlfa aqaaaaqgda papeadaaas atlpaiavsg
       61 eragafrare asvaglddap lrdtpasvsv vtraqlddqq akrlsdvvrn dasvvndyap
      121 vgyfegfair gfavdlasai ridgltvsge qnvplenker veilkglagi dsgvvapggv
      181 infvtkrsan vasvttgvds rgstsaavdl grrfgpgrqf gfrinaaken mhsyidgtng
      241 rrtfgsiaad wdispraslq fnaefqqwiq rsapgyqllg gtvvpsvntt skalgtqpwa
      301 kpvttdalnl narfdyrfnd dwnayiaagr srtmiddnsa faygcyyaps caagatspff
      361 fgangdydvy dfrspgeyrr nddlravttg kfatgplrhe ltlgvsvqrr vvhmanavyd
      421 yvgseniygp dvaftpspnt agpsypqlds wqygvfgldr isigehwqvl aggkevllrq
      481 rswssldgda thtdrsvflp qvalvykpvn vlslyasysk alslgdqapv ratnayaflp
      541 pveshqfelg akydwldrls ltaavfsisk pfqfadpdas gtsytfvqrg tqrhqgielg
      601 aagrlterls ltasvaaira raydsgspay eghqiinvpa lraslyadya vpgvaglnml
      661 ggveysggrn aneegtarvp swfvfnlgar yttkigghrt vlrvsvdnlf nkfywrdage
      721 qqgdaylfpg aprtarvslt ydf
//
LOCUS       WP_175805017             214 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia ambifaria].
ACCESSION   WP_175805017
VERSION     WP_175805017.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..214
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22137
     Region          12..213
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mpaaskparp vrvysfplsg hahrvrlfls llglpsdivd vdlaagaqre paflavnplg
       61 qvpvidddgt vladsnailv ylakrygdah wlpddaaaaa tvqrwlsyaa gpiasgpaaa
      121 rlvtvfnapl dhdaakrtaa kilavidgel agkpfaagaq ptiadiaayt yiahapeggv
      181 slepyphvra wlarvealpg fvgmpttrag llaa
//
LOCUS       WP_175805072             396 aa            linear   BCT 11-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Burkholderia
            ambifaria].
ACCESSION   WP_175805072
VERSION     WP_175805072.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 396)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 396)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 396)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..396
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41412
     Region          41..394
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mtqlfdtlgf idasavrara aardahgapl eaamrgdvaa vslvhvgkvf atprghaaal
       61 rdvtldvrrg evfgiigrsg agkstllrlv nglerpssgs vcvqgvdvga ldedglvalr
      121 rrtgmvfqhf nllsaktvfe nvalplkiag vpkaertrkv dalldlvgla akrdaypasl
      181 sggqkqrvgi aralvhdpev llcdeatsal dpettqsila lladinrrlg ltivlithem
      241 eviravcdtv avieqgevve tgpvwrvfgd prhgatrall stlvhdlpae laarvqplpe
      301 qaalpdgaqv vldvrytges ggepdvgala aalggsvrfl hggieriqgh aqgrlviaas
      361 pradevgqsp ahggavaall erarrhanha evlgyv
//
LOCUS       WP_175805124             701 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia ambifaria].
ACCESSION   WP_175805124
VERSION     WP_175805124.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..701
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75986
     Region          7..701
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 msrknwaaap maivvgtagl saaeaqelsl paievsgqrt tapfrapest satrtetdvm
       61 eipfavssvd kkliqtvaat rgedlydwva gvarqnnfgg lwdnyavrgf agdgntsgtd
      121 ylvngfswnr gisvprdtat lermevlkgp asalygrgdp gglisyttkq pqfarantig
      181 vsagsygalr etldstgpvt kslayrfiam nedngsfrdt vsskrylfap sftwdigadt
      241 tlhyefetar qrapldrgvv avngqlgavr asrfmgeprd gdydvrnsgh qftlehrfna
      301 dwsvnagfaq rdtdlsgrss eafalqpdgr tlwrryrqva fhsndvqgrv evagkartag
      361 ightfvmgad ayrfnydqfv srstptaaap yaidifdpvy gqpapvprta tnllerddgq
      421 glyaqdtlaf gphwkvlagl rwdrfhqsve nrlkgatttq lqtalsprlg ivyeassals
      481 lyantaysfr pnngadvngr afdpekgrgy eagvkwagtr wlatvaafyv nkrnvltadp
      541 anagfsraag evrsrgvefe wngelghglr givnlayvda qvthdsvltp garlvdiprl
      601 sgsallmyet alplvdkaga gagviyvgrr agntantqdg fdlpayatvq lngyvqvnkh
      661 lrasvvlnnl fnrtyyvssy nslwvtpgap rslfaslays f
//
LOCUS       WP_175805151             243 aa            linear   BCT 11-JAN-2025
DEFINITION  alanyl-tRNA editing protein [Burkholderia ambifaria].
ACCESSION   WP_175805151
VERSION     WP_175805151.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V.
  TITLE     Evolution of aminoacyl-tRNA synthetases--analysis of unique domain
            architectures and phylogenetic trees reveals a complex history of
            horizontal gene transfer events
  JOURNAL   Genome Res 9 (8), 689-710 (1999)
   PUBMED   10447505
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Cusack,S., Hartlein,M. and Leberman,R.
  TITLE     Sequence, structural and evolutionary relationships between class 2
            aminoacyl-tRNA synthetases
  JOURNAL   Nucleic Acids Res 19 (13), 3489-3498 (1991)
   PUBMED   1852601
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Schimmel,P.
  TITLE     Classes of aminoacyl-tRNA synthetases and the establishment of the
            genetic code
  JOURNAL   Trends Biochem Sci 16 (1), 1-3 (1991)
   PUBMED   2053131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..243
                     /product="alanyl-tRNA editing protein"
                     /GO_function="GO:0002161 - aminoacyl-tRNA editing activity
                     [Evidence IEA]"
                     /GO_function="GO:0002196 - Ser-tRNA(Ala) hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004813 - alanine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006419 - alanyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=26269
     Region          3..243
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
ORIGIN      
        1 mttqalfred ayltqcdavv aavgddgirl drtvfyplgg gqagdsgmlt lpdgdtiaia
       61 dtrkakfdga tpddavhvpa pghearvaal apgarvvagi dwqrryrhmr lhtaahlmca
      121 vlpypvdgcs vtadyvrldf atsdaidrad verrlaelvr gahavttewi tdaemterpe
      181 lvrtmsvkpp mglgrvrllr iasvdlqpcg gthvrntsei gdlrvaklek ksartrrvvl
      241 efa
//
LOCUS       WP_175805155             609 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 15 protein [Burkholderia ambifaria].
ACCESSION   WP_175805155
VERSION     WP_175805155.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Sakaguchi,M.
  TITLE     Diverse and common features of trehalases and their contributions
            to microbial trehalose metabolism
  JOURNAL   Appl Microbiol Biotechnol 104 (5), 1837-1847 (2020)
   PUBMED   31925485
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..609
                     /product="glycoside hydrolase family 15 protein"
                     /calculated_mol_wt=67677
     Region          1..592
                     /region_name="SGA1"
                     /note="Glucoamylase (glucan-1,4-alpha-glucosidase), GH15
                     family [Carbohydrate transport and metabolism]; COG3387"
                     /db_xref="CDD:442614"
ORIGIN      
        1 mpaliedyal vgdghtaali skdgsvdwlc wprfdsgacf aalvgtpehg rwllapaada
       61 aishtsrryr gdtliletdy esadgavtvi dfmppgngws elvrivvgrh gtmkmrmelv
      121 lrfdygfsip wvtqlsreng mkaiagpdtv vlrtpveltg knlhtlaeft vsaderipfs
      181 lgyaashlrl ppardplsml artenywlew sgrcqvqgry aaavrrslit lkalayeptg
      241 givaapttsl pekiggnrnw dyrycwlrda titllalmrg gyydearawr twlgrvmags
      301 peqiqimygi agerrlpeme ldwlpgyqds kpvrigngaa nqlqldvfge vmaalhlarv
      361 gglqaddtvw svqcalldhl ekiweepdeg iwetrggrrh ftfskvmawv afdraiksae
      421 mfrlpgsldr wralrdriha dvcdnawheg kqsfaqsygs deldasvllm pllgflpped
      481 privgtvdai erellhdglv mryrtteydd glppgegtfl acsfwlvdny allgriddah
      541 rlfsrllals ndlgllaeey dpvegrlvgn fpqafshval vhtamnlmhh eeamaraagq
      601 papavatgr
//
LOCUS       WP_175805169             810 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia
            ambifaria].
ACCESSION   WP_175805169
VERSION     WP_175805169.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..810
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=85248
     Region          79..807
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mpvpttrtal qaagparyar paaaalalal alalalragt acaqtapvqv taapvpvpvp
       61 vtvpapmpap apspasdalf ldvsvngept hriarfqqid grlyaasadl ndlgiatndr
      121 tpepsnvlva ldtlaglryd ydagrqtldl rvpdalriph tfdtralaaa ppatsgrgfv
      181 lnydayaqti ahaplavwse aryfdpygvf sstgvaylyd drrryvrydt swshsnpgtl
      241 tttqigdtis sslswtrslr iggvqwrsnf glrpdlvtfp vpalsgsavv ptsvdlyvnn
      301 vrqfsgnvps gpfvinsvpg itgagnatvi trdalgrsia tsiplyvdtr llapglasys
      361 seagflrray gidsfdyart paasgslryg vserltveah aeatagvyna gagalarlge
      421 rgvanaslal sapgrtgvqa gigyqyvtpr fsidaqtlra fgdysdlgsr egvpvsrttd
      481 rvtvsfpflr rqtlsfsylg lkypgvaasr igsvaylvnl ggltsvtfsg fqdfrqrdtr
      541 gffvslsigl ggntsvsvna grqngdstyt lsatrppdyg ggvgwnvqag anagmryaqg
      601 qlqylgrage vtllaqsfdg hrnasvdvtg aivlmngqlm tarrvddgfa lvstdtgrvp
      661 vlhqnrmige tnragyllvp dlnayqsnrv aidgtalpad ariadttldv vpqarsgvla
      721 hfavtrysaa sialrapdgt plppglevrh vesgqrtivg ydgltfvdgl vannhleitg
      781 ggrdcavafa yrrpddgtlp rigpltcgpr
//
LOCUS       WP_175805177             532 aa            linear   BCT 11-JAN-2025
DEFINITION  multicopper oxidase family protein [Burkholderia ambifaria].
ACCESSION   WP_175805177
VERSION     WP_175805177.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..532
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=57655
     Region          85..532
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mirrtflsha igvaaaslfa raawaqhaah agmagmdqmd dmpgmsgmag htqhakaapa
       61 alaaadalpa gaplaslrtl anesrepgtf ratlvaqpva rpllhgarpt tfwqfgtgtq
      121 gpvvgplidv regdtveirf vnklpqpsti hwhglpvppd qdgnpsdpva pgashvyrft
      181 lpkgsagtyw yhphphmmta eqvfrglagp fvvraaddpl agwpernlfv sdlklardgt
      241 iapndmmdwm ngregqfvlv ngarrpridv asderwrvwn acsarylrva fddgrafeha
      301 gtdgglfdap rrvtslllap geraellvra gdrasravlq aaeydrrkma mshddghgsl
      361 ppdpalplad vafapaaara lpatlravpa lgepvahkev afgeemdmda mmngpmhgrp
      421 agmrftinga tyaphratlt srrgdverwt irnatdmdhp fhlhgtqfqv ierasdgtrt
      481 pepfrawrdt vnvrsgetvt iltsqaepge rmfhchileh edlgmmgtlr vv
//
LOCUS       WP_175805185             520 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175805185
VERSION     WP_175805185.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..520
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54661
     Region          24..520
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mpsparssap pdvaallaal psriadvpar waaqapahpa liedarrlsy gqlsraveaa
       61 aerlarlgvr ggdrvmivae nsvaqivllf avarvdawal vsnarlsase ldaiaaharp
      121 kliafateas pdarahaarh datpadalpv digawshrvd pgapgepvaa dgaaqcaali
      181 yttgttgtpk gvmlshrnll figamsstlr rvspddvvyt vlpvshvygl asvclgslya
      241 gatlrlaprf speavrvala degvtifqgv pamhaklleh lhthahawra prlrfaysgg
      301 spldadlkar vervygvplh ngygmtessp titqtpldap rtdcsvgvpi pgvemrivap
      361 dgtdvphgev geirvrgpnv mlgyyrdada traavspdgw lgtgdlarqe adgsvtiagr
      421 skeliirsgf nvypveveqv lnahpdvvqa avvgravegn eevlafvelv pgasateaal
      481 hvwcaqrlap ykrparirvl dalpaastgk vlkhklrela
//
LOCUS       WP_175805216             419 aa            linear   BCT 11-JAN-2025
DEFINITION  sialidase family protein [Burkholderia ambifaria].
ACCESSION   WP_175805216
VERSION     WP_175805216.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 419)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..419
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44875
     Region          54..>241
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Region          101..150
                     /region_name="Sialidase propeller 2"
                     /note="Sialidase propeller 2 [structural motif]"
                     /db_xref="CDD:271234"
     Region          161..214
                     /region_name="Sialidase propeller 3"
                     /note="Sialidase propeller 3 [structural motif]"
                     /db_xref="CDD:271234"
     Region          281..>407
                     /region_name="COG4692"
                     /note="Predicted neuraminidase (sialidase) [Carbohydrate
                     transport and metabolism, Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443727"
ORIGIN      
        1 mvavksfaag calwlaalsp agahdapkta dphaahmsmq aapaqqkqpl atgaafdarh
       61 rlwvawvega hvvvahsdda grtlsapvtv nampepiyts aenrpkiats pdgrsvyvsw
      121 smpldapytg mvrfsrsldg gatwsvpvtv hrdrqaithr fdmmavdpag niaiawidkr
      181 dlvaakaagh ayegaavyya vsrdggasfe perkvtdhtc eccriamaid paghieavwr
      241 nvfpgqirdh alavlpvsas epvvpvratf snwhveacpe hgpalaitpd gtrhiawfgv
      301 vdgradvfys rigadgqprg tpwafganpa apaeqashaa lvargdvvwl awkafdgetm
      361 qiklrrsddr gehwsaprvi astsgasdnp qllddagriy lswrtrndgy rlipvegaq
//
LOCUS       WP_175805232             257 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia ambifaria].
ACCESSION   WP_175805232
VERSION     WP_175805232.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..257
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27991
     Region          1..>240
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mnllelddlc vaydtphgrr tvvdrlslal prgdigcllg asgcgkttvl raiagfepvr
       61 mgrivldgtp vaapsldvpp errrigmmfq dyalfphlst adnvafglrr mskaeqrsrv
      121 admlelvgla dagsayphel sggqqqrval aralapspel llldepfsnl dvdtrerlaf
      181 elrdilkrtg htailvthnq aeafaiadri gvmkdgrlaq wdtpyalhhh paspfvaefv
      241 rsdaladera ralargr
//
LOCUS       WP_175805238             356 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia ambifaria].
ACCESSION   WP_175805238
VERSION     WP_175805238.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..356
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=37322
     Region          23..356
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mtkqmnargs rsrarlahag lrvavaaacm ggsgaalaqd gvtlygvide faqyvntgng
       61 ytaaigsggq wgsrfgmkgg edlgggqkie falengfnpn dgslassgsm fnrqawvgia
      121 gqwgkvragr qnsplfndqg gqdafggvtq asgmdnltvf afrtsntlsy qspeiggfqg
      181 glyfgfgdag gvrsagssrq fdltyehgpf aafvagqwlk sttttttdrt imagasyaig
      241 katvyggfsa vkwadlgids rvyglslkyq lnpanyvalg yaylhdqtsq gnnadqlglm
      301 yeydlskrts fygalsylrn rnqagytlag aanpglplay pganargvql givhrf
//
LOCUS       WP_175805249             224 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175805249
VERSION     WP_175805249.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..224
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25609
     Region          16..218
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mpalanaqtl rniriltdlp esllahverh lmpwpehgnr mlffkgdped fvafvhrgrv
       61 yktlhepggr eiilghsvpg eligestllr ahrrsftaql shdcrisllh rqhfaplran
      121 adfmeriyeq lclhihqlsd faesaclyrl earlarhlln rmqgndvevp lpenqsilaa
      181 mlnvsrprln gtlqkmqrdg lirlhahgvt iekperlryi adan
//
LOCUS       WP_175805260             326 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH:quinone oxidoreductase family protein [Burkholderia
            ambifaria].
ACCESSION   WP_175805260
VERSION     WP_175805260.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Shimomura,Y., Kakuta,Y. and Fukuyama,K.
  TITLE     Crystal structures of the quinone oxidoreductase from Thermus
            thermophilus HB8 and its complex with NADPH: implication for NADPH
            and substrate recognition
  JOURNAL   J Bacteriol 185 (14), 4211-4218 (2003)
   PUBMED   12837796
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..326
                     /product="NADPH:quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34001
     Region          1..322
                     /region_name="QOR1"
                     /note="Quinone oxidoreductase (QOR); cd08241"
                     /db_xref="CDD:176203"
     Site            order(40..41,122,126,147,150..152,171..172,176,191,215,
                     237..238,240..241,262..264,314,316,318)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176203"
ORIGIN      
        1 mkalmctafg pidrlriddv aipepaagqv rirvkaasln fpdalivqgl yqvkpalpfs
       61 pgaefagvid avgdgvsawr pgdevvaftg hggfaeqcva dvhqiaalpp gmtfeqgaal
      121 vlaygtslha lqqrarlqqg etllvlgaag gvglaaieia kalgarviaa assadklalc
      181 rdagaddtid yasedlrrrv deltggrgad vvydpvggay seaalrataw rgrflvvgfa
      241 ageipkialn lallkerdil gvfwgdavrr dpaehavnmr qlaqwfaagk vrpaitervp
      301 lsgaadaiar manrqvkgkv vilpda
//
LOCUS       WP_175805290             500 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia ambifaria].
ACCESSION   WP_175805290
VERSION     WP_175805290.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..500
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52195
     Region          31..451
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msgwsgvtga agetpagapa eagggtvlta gavgfptala savglimasp viltatsgfg
       61 mggwafavam iiafvmmqaq attfseaaam lptagsvydy lscglgrfwa itgtisayfl
      121 vhvfagtaet ilsgimalvn feslnaalek hnsswlvgvg lvvtfaitni igikvfskle
      181 ivltagmwls lmifgilgla aaptvhldgw fggsavgtsv pavlslvgma mfmfvgcefv
      241 tplapemkap grtipramal glvgvaicmf lygaairrqv anvpvspdgl thlldtpgai
      301 pafalqvlgp fgrvwfgiaf lcagaatint lmaglprily gmaidgalpr cfaylhprfk
      361 tpvvgivaaa ivpiahawli hgnldsilhl vlaatcawgt ayllvtasvv mlrirrpdlp
      421 rpyrsplfpl pqivssvgiv laiwyitppg mnardiyvpf gamlgltaly alfwtvvvqr
      481 rhpfkpvpve evlrrehvas
//
LOCUS       WP_175805292             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175805292
VERSION     WP_175805292.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46402
     Region          23..427
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(35..36,39..40,43,82,140..141,143..145,148,168,
                     171..172,175,258,261..262,265..267,270,298,302,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mpdtmstlaq paahaprrvr nsrlasasmi gtslewydft iyntlaalvf nhlffpsvdp
       61 lagtilafst yavgyvsrpl ggfvfgnlgd rigrravlml tlvlmgvtta lmgalptyaq
      121 agilspillv alrfvqgval ggewagavll svehgdqkrr glsaswtqmg psfgtllgtg
      181 cialvtlstt sdtflswgwr vpfaasallv vfgfwlrrgv detpqfeqla eshataeapv
      241 aevlkchwrr lliaggsrig sdvlyalivv ftltyvttvl hlsrpvalta vmvgtacnal
      301 avpffgalsd rfgrrpvyla gaiagivwaf vfftmldtar pgaivaavai glvihavmyg
      361 pqgafvteqf ptrvryagss laytlagivg ggfaplviat lfrqtgttta vslyvtaalv
      421 vtsiallaar etahrplad
//
LOCUS       WP_175805361             301 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia ambifaria].
ACCESSION   WP_175805361
VERSION     WP_175805361.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..301
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31790
     Region          3..264
                     /region_name="17beta-HSD-like_SDR_c"
                     /note="17beta hydroxysteroid dehydrogenase-like, classical
                     (c) SDRs; cd05374"
                     /db_xref="CDD:187632"
     Site            order(9,11..14,34,63..65,91..94,114,141..143,157,161,190,
                     192..194)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187632"
     Site            order(115,143,157,161)
                     /site_type="active"
                     /db_xref="CDD:187632"
     Site            order(143..145,150,157,188..189,195,217,220)
                     /site_type="other"
                     /note="steroid binding site"
                     /db_xref="CDD:187632"
ORIGIN      
        1 mskvilitga ssgfgrltae alahaghivy asmrdtagrn aavtgqmsal areanidlrt
       61 leldvqsdas varaittvle qaggidvlih naghmafgpa eaftpeqyaq lydinvvstq
      121 rvnravlphf rerqqgllvw vssssaaggt ppylapyfga kaamdaiavl yarelsrwgi
      181 etsiivpgaf tqgtnhfaha glpadtaraa eydagpyanf grevqeafaa ivppdaradl
      241 vadaivdvva kpagkrpfrv hvdptedgan vgfavldrlr aemlhrvgls dllaprlrps
      301 s
//
LOCUS       WP_175805332             433 aa            linear   BCT 11-JAN-2025
DEFINITION  NCS2 family permease [Burkholderia ambifaria].
ACCESSION   WP_175805332
VERSION     WP_175805332.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..433
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45323
     Region          4..431
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mesikryfgf aeagtdfrte ilagvttflt mayiifvnpa ilgdagmpke svfvatclva
       61 alaslimgly anypiacapg mglnayfayt vvkgmgftwq aalgavfisg clfllvtlfr
      121 vreaivngip kslrisitag iglflgiisl ktsgvivgsp atlvtlgdlh khdtilaivg
      181 fftivtldhl rvrgailigi igvtilsfff ggnqfhgvfs appsidatlf kldigaalst
      241 giinvilvff lvelfdatgt lmgvanragl lvegkmnrln kalladstai vagsvlgtss
      301 ttayiesasg vqaggrtgvt aitvavlfla clfiaplagv vpayatapal lyvsclmlre
      361 mvdvpwddat eavpaaltal lmpftysian gvafgfisyg glklltgqar tvkpvvwiia
      421 avflfrffyl gse
//
LOCUS       WP_175805335             441 aa            linear   BCT 11-JAN-2025
DEFINITION  leucine-rich repeat-containing protein kinase family protein
            [Burkholderia ambifaria].
ACCESSION   WP_175805335
VERSION     WP_175805335.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Shen,K., Hines,A.C., Schwarzer,D., Pickin,K.A. and Cole,P.A.
  TITLE     Protein kinase structure and function analysis with chemical tools
  JOURNAL   Biochim Biophys Acta 1754 (1-2), 65-78 (2005)
   PUBMED   16213197
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
REFERENCE   7  (residues 1 to 441)
  AUTHORS   Hanks,S.K. and Hunter,T.
  TITLE     Protein kinases 6. The eukaryotic protein kinase superfamily:
            kinase (catalytic) domain structure and classification
  JOURNAL   FASEB J 9 (8), 576-596 (1995)
   PUBMED   7768349
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..441
                     /product="leucine-rich repeat-containing protein kinase
                     family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=46798
     Region          <2..>186
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          39..61
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          62..84
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          85..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..175
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          211..>378
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(214..217,220,222,238,240,269,287..290,345,349..350,
                     352,362..363)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
ORIGIN      
        1 mtttleqlqt gqlagarqlk lacgltefpr eifdladtle vldlsgnals alpddlsrlh
       61 rlrvlfasgn gftefpevlg tcaqldmigf kanrirtvpr gslpralrwl iltdneidal
      121 paeigdcsrl qklmlagnrl ralpaemaac rslelvrlsa nrldalpdwl lrlprlawla
      181 sagnpfgaap eaaasaepgv adidwtsltc dqklgegasg viyraqwrpd rhapravavk
      241 lfkgavtsdg lpdcemaacl hagrhpnmip vigkvrghpd gthglvmelv dpaltslagp
      301 psfasctrdv yaadarfepa aaarialgia svaahlharg imhgdlyahn ilhdgaggal
      361 lgdfgaasvy dvndraraar lerlevrafg yllgellarc eprawegsha ldalaaacln
      421 ddidarpsfg evsavlaast a
//
LOCUS       WP_175805459             555 aa            linear   BCT 11-JAN-2025
DEFINITION  S8 family peptidase [Burkholderia ambifaria].
ACCESSION   WP_175805459
VERSION     WP_175805459.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..555
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55442
     Region          243..522
                     /region_name="Peptidases_S8_13"
                     /note="Peptidase S8 family domain, uncharacterized
                     subfamily 13; cd07496"
                     /db_xref="CDD:173820"
     Site            order(250,318,322,389..391,417,419..420,490)
                     /site_type="active"
                     /db_xref="CDD:173820"
     Site            order(250,318,490)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173820"
ORIGIN      
        1 mrakrfnial ahsaharmla gmlsaaallp lagcgggggd gsnpsssnaa papapspapt
       61 ptpappttpp ttsggnactt qqaaaqmaaq ttapaeppvd hlivklktlt atramaaldt
      121 gtrldaviqr sitrwsaptt sgtarayaav tasqaslnvq vertlsdgaa vlsigqrias
      181 gdaaalaqaf aadgdvdyae pdhpmrirdt psdpsysqqw ylsdasvgin tppawtrtkg
      241 sptvvtavld tgyrphpdlv gnllpgynfi snintsnnsq trgtdasdpg dwvtqqeldd
      301 angpyyhcas epstsswhgt rvmgvigana nngigvagvs wlgrilpvrv lgkcggktsd
      361 iadamrwaag ipvagvatnp npakvinlsl ggvgacsatf qqaiddvnak gvtvvvaagn
      421 dglstafdqp ancrgvisvg atdatgrras fsnfgsdval sapgvsilst anggtttpga
      481 dtygtasgts latpqvsgiv glmlsmngnl tpaqiqqklq ggaraamlpa stsctalpag
      541 agiadagaav taaiq
//
LOCUS       WP_175805482             292 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia ambifaria].
ACCESSION   WP_175805482
VERSION     WP_175805482.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..292
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31682
     Region          35..275
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 mtglhqdhqd hqdapdstaa rvalwralhv eldapphvla devglrllap apgwqqrgdm
       61 dpqftrpfra sivararfie dlvveqaaqg vsqyvilgag ldsfvqrrpe masrltvfev
      121 dppapqawkr rrltelgfgv pdwlrfvpvd feakqswrda lvgagfdagk pavvvstgvs
      181 myltrdanaa alrevaslap gstfamtfll plehadpdvr palemaakga aasgtplisf
      241 fmpteirtla tdagfaraeh vsaaeltrry fadrtdglrp pnnaeellva tv
//
LOCUS       WP_175805573             425 aa            linear   BCT 11-JAN-2025
DEFINITION  GspE/PulE family protein [Burkholderia ambifaria].
ACCESSION   WP_175805573
VERSION     WP_175805573.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..425
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=45145
     Region          <36..424
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mhfpppgapl htqrppastd aspadpphsl daaqlddspa vrlltdtlha arvrdasdih
       61 vepfeagwri rvridgvlhe larppvhlrd alvtrikvla rmdiaerrlp qdgrlritvd
      121 aglrgdyrvs slptlfgekl vlrrletlpp dltlarlgfd arqaaameaa iraphglvlv
      181 tgptgsgktl slycalqmld rdahnvctve dpaeiqldgi nqvgvaekag ltfatalral
      241 lrqdpdvimv geirdaetad vaikaaqtgh lvlstlhtnd apaavarlld igvapynlaa
      301 alrlvtaqrl vrrlcvncrt rsdapahalr dagcdpaala sgwrpfvarg caachgigyr
      361 griglhqtmp vspemaeriv arasvgaltq caaaegvrsl rdaalahvrd gttsvaeala
      421 atpda
//
LOCUS       WP_175805575             270 aa            linear   BCT 11-JAN-2025
DEFINITION  ComF family protein [Burkholderia ambifaria].
ACCESSION   WP_175805575
VERSION     WP_175805575.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..270
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=28620
     Region          17..240
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mdrrfaprqm rvvlsqvral avrvvalalp nrcalcgnls havicsacda aywnearlrc
       61 dvcavplgsg rprphgsrgr hagvaasfay rcdacraspp pfdatlalad yrapldglar
      121 glkfharlal gaefaarlaq riddtdalrt aggfdviapv plshgrlvar gynqawaiar
      181 plarrlgvra datllarvte tapqsrldrr arrdnviaaf avtddlagrh valvddvmts
      241 gatlaaaaqa lkaagaarvt hlvalrtard
//
LOCUS       WP_175805579             311 aa            linear   BCT 11-JAN-2025
DEFINITION  MlaD family protein [Burkholderia ambifaria].
ACCESSION   WP_175805579
VERSION     WP_175805579.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..311
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=32881
     Region          1..289
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 menkshafwa glftialtla iagtvfwfnv drtvrvpydl lartnvtglf pdaavrfrgl
       61 dvgkvqsigf drthpgqiri rilvdrdapi tqstygslgf qgvtgiafvq ledtgrdlap
      121 lpsspksiaq ipmrpslfdq iqergdvllr qleqaaesan almspemreq lrataeslqh
      181 aadgaatlsk qlapavaalp qtmhqvdram asantllqpn gplvsnlnka gsaaeqvgva
      241 lnhlnarvqy dtlprfntla dsvgdasrql kdvagelgrn pssllfgspg aapgpgeagf
      301 vwpgkgaaag k
//
LOCUS       WP_175805597             283 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia ambifaria].
ACCESSION   WP_175805597
VERSION     WP_175805597.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..283
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29851
     Region          7..260
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtrstaalaa rgltvgyrdh vvidgldlsi aagrvtalcg pngcgkstll rtlaglqpar
       61 aghvdvngkp lasfrrrala reltmlaqfn qipsgltvre lvaygryayg gflrglsrad
      121 haaidealdt sglagdaerd vgalsggerq rawiamalaq qapivlldep ttyldihhql
      181 dildalraln rargltivwv lhdlnqaaay sdeivlmrag rlvaqgspda mlepaqlraa
      241 fgvdmlklah pqtgapmcvp aygppasgtp pafehavdrd iav
//
LOCUS       WP_175805620             308 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Burkholderia ambifaria].
ACCESSION   WP_175805620
VERSION     WP_175805620.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..308
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32109
     Region          7..272
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(34..35,38,90,103,105,134,167,253,256)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mtaafpeila lgeamiefnq sqpgrpeflq gfggdtsnfc iaaarqgast gfvsaigddp
       61 fgrlltgmwa aeqvdttyvr idrtaptgvy fvthgadghq fdylragsaa srytvadlpl
      121 dalaaakavh lsgislaisa aacdaafaai dharsngaqv sfdtnlrlkl wplpraravm
      181 realrqtdic lpswddvtal tgandrdaiv damlehgprv valklgkega yvatpnerrv
      241 vpgfaveavd atgagdcfgg afvarivagd dpfaaaryan aaaalsttgy gavapiphre
      301 vverlvqg
//
LOCUS       WP_175805648             358 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia ambifaria].
ACCESSION   WP_175805648
VERSION     WP_175805648.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..358
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=38578
     Region          42..351
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 maivmamava ipltarskem tnrvglppai reagspgesn airlgqriff dkrlsadgtv
       61 scaschqseh aftdglprsr gvgghtgtrn apsllnaplv ntqfwdgres sletqalepf
      121 vnpveqgldn ldsllgiira dtgyveafka afgvsehait tqhvaralas ferslvvgds
      181 aldryyfrgd atalspeavr gfllfmgrar csschtidpa aatftdeqfh tlhvgmsrid
      241 grlaeltqqv iklrkhgasv atlvlsnddi aqlgrfvvtl apddigkfrt pslrnvalta
      301 pymhdgsvat leeavdqeiy yrtaqsgnpl iltpkekhdl isflesltss talsklkk
//
LOCUS       WP_175805657             158 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Burkholderia ambifaria].
ACCESSION   WP_175805657
VERSION     WP_175805657.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..158
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=17580
     Region          1..>74
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
     Region          7..154
                     /region_name="typeII_sec_gspG"
                     /note="type II secretion system protein G; TIGR01710"
                     /db_xref="CDD:130771"
ORIGIN      
        1 mrcnqagftl iellitlail avlagialpt aqvsvqrvke felrrdlrei rtgidaykda
       61 adhgriekpa dstgyprnln vlvdgaedir dprkskiyfl rhiprdpfca denvgdadsw
      121 gkrsyasdat dpqegddvyd vfskstvvgl ngipyrrw
//
LOCUS       WP_175805662             311 aa            linear   BCT 11-JAN-2025
DEFINITION  1-phosphofructokinase family hexose kinase [Burkholderia
            ambifaria].
ACCESSION   WP_175805662
VERSION     WP_175805662.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..311
                     /product="1-phosphofructokinase family hexose kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008443 - phosphofructokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32457
     Region          4..306
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 mtdiatvtln pavdvstsve hivdthklrc arprrdpggg ginvartihr lggdcvalyl
       61 tggptgdvlt qlieaerlps mririagetr envcvtetat greyrflmpg plvteaewrd
      121 caarieamqp aprylvlsgs lppgapddly arlacnarar gsrvvvdaag ralqaaleag
      181 vhlvkpslge lsalagepld dtsacrkase lvagghadiv altlgargaw vvtrdralrl
      241 pgrpaavcst vgagdsfvgg mvwalargmp fddacryala asaasvehpg talctrddve
      301 rihaelaaqa s
//
LOCUS       WP_175805667             374 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia ambifaria].
ACCESSION   WP_175805667
VERSION     WP_175805667.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13386660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..374
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40342
     Region          13..>122
                     /region_name="YhgE"
                     /note="Uncharacterized membrane protein YhgE, phage
                     infection protein (PIP) family [Function unknown];
                     COG1511"
                     /db_xref="CDD:441120"
     Region          176..370
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 msrlpaifrl gvkelwslar dpillalivy tfstsiyvaa tarpetlhkv piaivdedas
       61 plsariaaaf fppqfasppi vdagtagrgl dngdytftld ippdfqrdvl aghhatvqln
      121 vdatrmtqaf sgggyvqqiv lgeidafvrr nrgtalppvd lamrmrfnpn ldevrfgalm
      181 elinnvtmls liltgaalir erehgtiehl lvmpvtaadi mlakvwsmgl vvaaaavasl
      241 tfvvrgalhv pipgsvplfv agmalhlfat tslgiflatl vrsmpqfgml lvlvllplql
      301 lsggltpres mprvvqdiml aaptthfvel aqrilyrgag ldavwpqfaa lfaigcvlfl
      361 lslkrfrnti gqmt
//
LOCUS       WP_175805689             546 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia ambifaria].
ACCESSION   WP_175805689
VERSION     WP_175805689.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..546
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58401
     Region          1..533
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mqydyiivgg gsggssvasr ladacpdati alieagphte rnllvnmpvg iaalvpfklg
       61 tnygyetvpq pglggrrgyq prgrgmggss ainamiytrg hpgdydewaq lgatgwgwqd
      121 vlpyfrraeg nergadawhg adgpltvsdl rfrnpfserf iqaahaagyp lnndfngatq
      181 egvgfyqvth rdgsrcsvar ayiygrnrpn lhvitdatvl rvgfdgkrav gvvvsrdgrv
      241 etlgaraevi lsagafnspq llmcsgigpa eqlrrhgiai vqdapdvgan lidhidfiin
      301 trvnsselvg iclrglakmt palaryfssr tgmmtsnvae aggfiksdps ldrpdlqlhf
      361 ctalvddhnr kmhwgfgysl hvcalrpfsr gtvalasgda rdaplidprf fsdtrdldll
      421 vrgaqamrri lsqaplasqg grelytradq seaelrativ ahadtiyhpv gtcrmgsdar
      481 avvdpqlrvr gvdglrvvda svmptliggn tnapsvmige raadfivatr kgavprgeaa
      541 aavhgr
//
LOCUS       WP_175805693             215 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia ambifaria].
ACCESSION   WP_175805693
VERSION     WP_175805693.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..215
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22780
     Region          3..215
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mnylpillqi avvylvaait pgpnffmisq lslagrrslg aasalgvgta siawatlaml
       61 glaavlhqve wlyetirigg avylvyfgik llrsgvrrda apadtaaasa plaaprlrdy
      121 lrayrsgllt cltnpkscaf wtsvfaamlp ahvplwfnga vlvtigvlsa gwyscvaflf
      181 aspraqrgyr rvrrpldalc gvalvglgak laadr
//
LOCUS       WP_175805696             215 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia ambifaria].
ACCESSION   WP_175805696
VERSION     WP_175805696.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122607
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..215
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23534
     Region          2..75
                     /region_name="GST_N_1"
                     /note="GST_N family, unknown subfamily 1; composed of
                     uncharacterized proteins, predominantly from bacteria,
                     with similarity to GSTs. GSTs are cytosolic dimeric
                     proteins involved in cellular detoxification by catalyzing
                     the conjugation of glutathione (GSH) with...; cd03043"
                     /db_xref="CDD:239341"
     Site            order(13,15..16,18..19,22..23,68,71..72)
                     /site_type="other"
                     /note="putative C-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(13,52..54,66..67)
                     /site_type="other"
                     /note="putative GSH binding site (G-site) [chemical
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(52,65..66,68..69,72)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239341"
     Region          88..200
                     /region_name="GST_C_3"
                     /note="C-terminal, alpha helical domain of an unknown
                     subfamily 3 of Glutathione S-transferases; cd03194"
                     /db_xref="CDD:198303"
     Site            order(91,98,158,161..162,165,169)
                     /site_type="other"
                     /note="putative N-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:198303"
     Site            order(91..92,95..96,99,135)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:198303"
     Site            order(98,102..103,106..107,166,169)
                     /site_type="other"
                     /note="putative substrate binding pocket (H-site)
                     [chemical binding]"
                     /db_xref="CDD:198303"
ORIGIN      
        1 mklvigdkny sswsmrpwll lahfgipfde iaielrrddt aariheyspt gkvpcliddh
       61 gtaiwdslai aetlaerypq fpmwpadple rvharcisae mhsgfaalrt qmgmnvrasm
      121 pgrgatpdal advaridalw sacieasggp flfgefgiad amyapvvmrf ntyapalspe
      181 aagyaarvta lpavqrwida arretnviae yepnp
//
LOCUS       WP_175805712             184 aa            linear   BCT 11-JAN-2025
DEFINITION  PaaI family thioesterase [Burkholderia ambifaria].
ACCESSION   WP_175805712
VERSION     WP_175805712.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..184
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=19004
     Region          20..149
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mtashagwaa ealdipgpad araqwqaclg ampiidhlga sldlsdpriv rlalvtrtqa
       61 hegglgtdal ngaiiaglld camsvtgvlh mrgrtcgtvq msiqfmkpvr taypvvecva
      121 mrrspsvvfv earltegrgr csvlatgvvg aatlaqrasg gdgrsnwser aalaallekd
      181 qtaa
//
LOCUS       WP_175805736             465 aa            linear   BCT 11-JAN-2025
DEFINITION  SLC13 family permease [Burkholderia ambifaria].
ACCESSION   WP_175805736
VERSION     WP_175805736.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..465
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48847
     Region          102..461
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 msggalggpg rgagmltggr vtaallaagl asvaalgarg tlsagdariv aivftcivlw
       61 atgavaslwv sllffflaat ctavptaeif sgfgssafwl vfsgaaigfa lkesglseri
      121 gialarrigg sylkallafa ilsfllslvm pstfgriail vpiaigycdv vklgahangr
      181 rgilllvivg syelaaavlp anlpnvimag ileqshgmhl rfseylllff pagvivrgav
      241 lvlaswwlfa dtvgeveipa arvalgrrew haivllaitl afwftdavhr iapgwvglgf
      301 alvyfgtspp aqlerftatl kmdllwfiaa iigltalvnh ldmrvpdtla ldalrdspml
      361 vyfaltalsi vvcfavtsna epalyvpivs rllahglhlk agllaqvmgy attvlpyqsp
      421 pivfgnalaq ldrgavlryc iatallgvvf vipvnalwwr ligll
//
LOCUS       WP_175805755             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_175805755
VERSION     WP_175805755.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32229
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdkfsalraf vevaeaggfs sagrrldlaa ssvvravdal easlgtvlln rttrqvtlsd
       61 agavyyarak qllealaead alvadrgdep sgplrvsvpv aygmhriaph vgaflarypr
      121 ldldlqltda rvdlvtsrid vairlgeaap saevvarqlg tfrryvvasp dyldahgtps
      181 tpgelvdhgc lrfhfggdqq awsfvdahga tkvlvtgrlk snhsevlraa aldgggiall
      241 pdwlvdadvr agrlrrlfeq ydvvpdaars ivtalylpnq rgskrvtafi dfveaqartp
      301 c
//
LOCUS       WP_175805758             370 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia ambifaria].
ACCESSION   WP_175805758
VERSION     WP_175805758.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..370
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39218
     Region          4..344
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,233,300,320,322..324)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,181,184,186,233,240,300,320,
                     322..323)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,181,184,186,323)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            186
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mssllstydl rglplpnrvv mgpmtrsrap srgqptalma eyyaqrasag livteatnvs
       61 htsaafeltp glvtdeqaag wkqvtdavha nggrifaqlw hggrvssltl lggdaplsps
      121 gvnddlellq vwarlqngyy tkihatpsra mttdevaatv ddfgraaara maagfdgvei
      181 haangylphq flsstlnrrd dryggsvanr arfleeivaa vggvmplsrv gvrispyaqy
      241 nnvrdadpda tyayvgrmld eagvaylhaa dtngwsgepd lpriiehtrk afggtlivng
      301 gitpdaanal idagdadlva farayianpd lveriathap lavpksigwy ggeragyvdy
      361 arhdaaapta
//
LOCUS       WP_175805852             396 aa            linear   BCT 11-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Burkholderia ambifaria].
ACCESSION   WP_175805852
VERSION     WP_175805852.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13537404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..396
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=42559
     Region          <29..98
                     /region_name="COG4253"
                     /note="Uncharacterized conserved protein, DUF2345 family
                     [Function unknown]"
                     /db_xref="CDD:443395"
     Region          <139..355
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          <272..>386
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          289..317
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(290,293..294,297..298,300,335,338..339,342..343,
                     345..346,369,372..373,376)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          322..363
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtsrlftaci aavigcatlp aahartyiap ttslgkgayv hqfvlrdpvt hqplpnaryr
       61 lflpgqviag lpvkpgqhds vvfgttddag rtvrirlpks hpqkqwvfnp vigdgdlges
      121 frlvdaggda plrgfpylld veheylacgh sdangytyya qsrtprtvnl ytgmlgdsad
      181 tdwcagpgaa iansanepga pdlytqylgs lvangdrigs elrqqivikl lslateerda
      241 drvaavldlg eipddrlndt gyrlvdagva vdrglamida hlakapdday aldskgwaly
      301 rlgrndealt wfdrsiaife kngdgdsdtr eawatglthk gevlwklgrq dearaafaqa
      361 rkiqpkntel aetltrlnvq ekpaeagasa sgttgt
//
LOCUS       WP_175805876             198 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent F420 reductase [Burkholderia ambifaria].
ACCESSION   WP_175805876
VERSION     WP_175805876.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..198
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20495
     Region          3..167
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mryaiigfgk ighalatafa rngievavat trapesfaad aaaigptiip ktlaeavrad
       61 iiflavrfes hpevakalrd wkgktvvdam ntqapleelg glpssafvan afsgarlvkg
      121 fnhlvaavlg qdpaihggrr vvflasdddg aaaeigalae klgfapiklg glsdggllvh
      181 argnqwgqli fkdlitfd
//
LOCUS       WP_175805891             453 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia ambifaria].
ACCESSION   WP_175805891
VERSION     WP_175805891.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..453
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49050
     Region          21..410
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,152,
                     155..156,159,257,260..261,264..266,269,297,301,350..351,
                     355,359,375,378..379,382..383,386)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtspalpgrd plasavskvk whvlplvlim fianyidrvn vgfvdrhlea sigigaaayg
       61 lgaglffvgy alfevpsnll mqrygariwl arimatwgvv aaamafvwnd tsfyalrfll
      121 gaaeagffpg vvlylsqwlp pqergkamai flggsafasv lsgpvtgall sihgfglqgw
      181 qwmfliegmf svalcgaswl llkshirdat wltaderaal qnaldeerat rdvrskvhvs
      241 attllrdpqi mlfcflyfgi qltiyaatfw lptiirkmgg ltdfqvglyn tipwmiaiga
      301 mygfavlsak wkhpqrwlsf alvlaacglf astshdpvws fasicfaalg fkaasalfwp
      361 ipqgyldtrv aaavialins ignlggfvap tafgylkqht gsitgglyal aiaslvaava
      421 alfarthrrs dpprglpade sftntamlrh aeh
//
LOCUS       WP_175805900             268 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia ambifaria].
ACCESSION   WP_175805900
VERSION     WP_175805900.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..268
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=28142
     Region          9..247
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mrarpivavt adrilrgahp nhtagekylv alvdgagala fvlpalgarq pvdaivasvd
       61 gllltgsysn vephhyggpa stpdtlhdpa rdatalplil aaidagvpml aicrgmqeln
      121 vayggtlhqr lhaspgfhdh rerdgdpler qygpahrirl apggllqria rgahdamvns
      181 lhdqgierlg aglaaeasap dglieavsvr garafalgvq whpewrfaeq plsrdifaaf
      241 gaacrarmth riraaggtmp spaasdid
//
LOCUS       WP_175805953             277 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia ambifaria].
ACCESSION   WP_175805953
VERSION     WP_175805953.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..277
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30504
     Region          3..142
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          153..275
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 msyktllvhl ddsdrckarv nlalelagrw nahliglyav cqdlfeplrr pdeplklavy
       61 erlceqrrkd aeerflmaae ragrsvewqa pagdvtgtai lharhadllv lgqenpddrm
      121 tfvarhfved vvmgsgrpai vvpyagdvrt lgenvligwd ggreaarata dalplltrar
      181 fvhvetvtrg hpdpdetpag vdvaaylerh girasfsttp rersvsvgat llnrvtdvha
      241 dllvmglysh armhervlgg atrtiletmt vpvllsh
//
LOCUS       WP_175805954              62 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein, partial [Burkholderia ambifaria].
ACCESSION   WP_175805954
VERSION     WP_175805954.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 62)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 62)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 62)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..62
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         <1..62
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
     Region          <1..51
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 disdvlaraa aecdadlivm gthgrrglrr allgsvaesl vriadrpvlv vregpggcag
       61 vl
//
LOCUS       WP_175805957             354 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase, partial [Burkholderia ambifaria].
ACCESSION   WP_175805957
VERSION     WP_175805957.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 354)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..>354
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
     Region          1..354
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mtdvvivsaa rtavgkfggs lakiaapelg atviravler sgvkpeevse vimgqvlaag
       61 sgqnparqsl ikaglpsavp gmtinkvcgs glkavmlaan aiaagdaeiv iaggqenmsa
      121 aphvlpgsrd gfrmgdaklv dtmivdglwd vynqyhmgit aenvakeygi treeqdafaa
      181 lsqnkaeaaq kagrfndeiv pvsipqrkge plqfatdefv rhgvtaesla glkpafakeg
      241 tvtaanasgl ndgaaavlvm saqkaaalgl tplarikaya nagvdpsvmg mgpvpasrra
      301 leragwtpgd ldlmeineaf aaqalavhkq mgwdtskvnv nggaiaighp igas
//
LOCUS       WP_175805995             294 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia
            cenocepacia].
ACCESSION   WP_175805995
VERSION     WP_175805995.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..294
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32073
     Region          111..271
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mllnvnaihr dndrfnvsfk algelietvg tphfvprltq llndvvpldv ahversrvda
       61 tmptgyrcew igssgigtas tdisdvmtly yerfldsdpl faglrgktgt mlvvrdiaai
      121 ppgefrqrlf ddvhighecv largtrysqh sialergrdr ppftlaemnr frsisdmlfp
      181 llelhastta arriahatpd ihplaqfdar laadgvklsk reyetckhll sgktvpetag
      241 ilgvgvasae syvkrafakl gvrtkrelaa wgsatavlpa agsyddgapp aipr
//
LOCUS       WP_175806009             523 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyl hydrolase family 79 C-terminal domain-containing protein
            [Burkholderia cenocepacia].
ACCESSION   WP_175806009
VERSION     WP_175806009.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 523)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 523)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11245732
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..523
                     /product="glycosyl hydrolase family 79 C-terminal
                     domain-containing protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=54769
     Region          424..519
                     /region_name="Glyco_hydro_79C"
                     /note="Glycosyl hydrolase family 79 C-terminal beta
                     domain; pfam16862"
                     /db_xref="CDD:465285"
ORIGIN      
        1 mqirsesmpv hvrdtrlnrv vksiplaaal lalmtggcws naiastpvkp ppaavhptlp
       61 ngtpvtltie savagaasls passglsfek aqlstglfsg dnrslialfr qlgpgvlrig
      121 gnsvnkttwd gskdpggqgm tpghiapsdv drladflnat gwrviyginf atesatqmss
      181 eaayvtrklg srlaglelgn epdlythngl rpstytfnqf ldewrtdara tqssgrnpal
      241 tgpassynfm hytipfaqni gggiqlltqh yytnsscpns atgyapsipg mlaadprlpg
      301 elqalvraas dngvsggarm deansfyscp hlsgapgvsn afasalwavd flftnarygm
      361 rgvnfhsgnt syyspiqtha aavtsvqpey yglwlfgqav dlssgtllet ridmsvqppl
      421 pikaydvlaq dgshrvliln esasdgdvtv qhlppnatra allrlsstgg lsdiaaadvs
      481 vngahlsadg twdspptptt qpvsngsmtv hvaagsalla ivr
//
LOCUS       WP_175806010             336 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [Burkholderia
            cepacia complex].
ACCESSION   WP_175806010
VERSION     WP_175806010.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..336
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35664
     Region          9..330
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 msqstcsard ivvvgfegvq slditgpmev favanrhlpa haapyrltla sqhgddivth
       61 aglrlagaaa laalparidt iivaggdeaa lrhaaseagv lpwlrtriad trriasictg
      121 afvlaaggwl dgkratthwn qcaalqalcp dariepdaly vsdppfhtsa gvtagidlcl
      181 alveadcgap talavarelv lfmhrpggqa qfsvgldiqa ratprmrsll adiaddpagd
      241 lgvaalaarm hmsertfarh ffketgvspa qyvlaarver akalleradw pleriaerag
      301 fgsvdalqra fakrvgaspr dyrarfgprr dkprte
//
LOCUS       WP_175806015             177 aa            linear   BCT 11-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Burkholderia cenocepacia].
ACCESSION   WP_175806015
VERSION     WP_175806015.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..177
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18806
     Region          1..165
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtpadlipsp lgdiavried dtltglyfvg qkyfpslaip ndvhtlatsp iarrvaeeia
       61 eyftgardtf svpihlrgta fqrrvwqell aipfgelvsy gditervglp msgaravgga
      121 vgrnpvsiiv pchrvvgasg sltgyaggid rkrallsleg aelsrgahhp mqqalaf
//
LOCUS       WP_175806017             430 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia cepacia complex].
ACCESSION   WP_175806017
VERSION     WP_175806017.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..430
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46422
     Region          17..419
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(31..32,35..36,39,71,121..122,124..126,129,149,
                     152..153,156,244,247..248,251..253,256,284,288,345..346,
                     350,354,370,373..374,377..378,381)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mqsavvgtvr aaasryrwtv callffatvi nymdrqilgl lapmlqhdig wsqvqygriv
       61 mafsafyalg llgfgrivdw lgtrvsyava mlvwsiaaml haavgsvtgf afvrallgig
      121 eggnfpaaik ttaewfprre ralatgifns ganigavfap aiipaiavay gwraafviig
      181 aigivwlavw lvmyrtadtr alaaeydepr deaealdaan anagaprwge lirkretwaf
      241 ligkfltdpv wwfylfwlpk wlnesrgmdm qhiglplvci yalttvgsig ggwlssmllr
      301 agwsvnrark tamlicaccv lpiafvsqvq slwiavlivg laaaahqgws anlfttasdl
      361 fprravasvv giggmagsig gvlfsevigq vlqrtghywv lfaigasayl ialavmhvlt
      421 pkmkpaklda
//
LOCUS       WP_175806035             212 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175806035
VERSION     WP_175806035.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..212
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23141
     Region          4..195
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mnayrlylsp gacslaahia leetgapfdv eivsvreqqn learylainp karvpvlaip
       61 gepraltetp ailtylarry pdaqllpldd plrearchew lawlvgwvhg vgygalwrpg
      121 rfiddpalhg avsahgrgti daanasietl ladgrtwaep gahsivdpfl lvlyrwgvai
      181 gldmtrhpaw tahaqreaer paarralare aa
//
LOCUS       WP_175805999            1068 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cenocepacia].
ACCESSION   WP_175805999
VERSION     WP_175805999.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..1068
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=114662
     Region          1..1036
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 miarlihwsv hhrflvllat vllaawgvhs lrqtpldalp dlsdtqvivk asypgkapqv
       61 vedqvtyplt ttllgvpgak tvrayssfgd afvyvlfddr tdpywarsrv leylsqvqsr
      121 lpagatvslg pdatgvgwvy eyalvdrtgr hdlgqlraln dwflkfelka vpdvsevasi
      181 ggmvrqyqvv ldpdklrayg itqaavaeal gkanqasggs vvelaeseym vrssgylrtl
      241 ddfrhvvlrt ddtgtpvllg dvariqvgpa mrrgiaelng qgevtggvvv mrsgknaltt
      301 idavkaklad lkrslpagve ivttydrsql iaravdnltd klieefvivg vvcavflfhl
      361 rsalvailsl plgvlaafiv mryqgvnanl mslggiaiai gamidaaivm ienahkhlea
      421 ydrahlgepi taarrwelva asaaevgpal ffslliitls fvpvfslegq egklfaplaf
      481 tktytiaaaa glsvtlvpvl mgylvrgrip hehanpinrv lirlyrplle atlrrpwaai
      541 gvavvalvlt avplsrlgge fmppldegdl lymptalpgi sadkasellq qtdrliktvp
      601 evdtvfgksg radtatdpap lemfettirf kprstwrpgm tpeklvdeld rtvrvpglsn
      661 vwvppirnrl dmlstgiktp vgvkisgpdl agidaiatqv eaavkrvpgv tsalaerlng
      721 gryvdvdidr laaaryglsv adiqsvvssa iggedvgevi agrerfpini rypreirdsl
      781 enlrqlpvvt argaqirlgd varvaiadgp pmirsenarl sgyvyvdlrg vdlstavram
      841 qqavarqval ppgysiawsg qfeyleraaa tlrtvvpvtl vvifvllfvt fdsaadalll
      901 mstvpfalvg gfwlvwalgh avsvatsvgf ialagvaaef gvvmllylkg alqrrldage
      961 pltdalllda iregavlrvr pkamtvavvl aglvpimigh gagsevmqri aapmvggmvt
     1021 apllsmfvip aawlllqrrr arsasrarrs davppgtnvp slptgesr
//
LOCUS       WP_175806039             251 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia cenocepacia].
ACCESSION   WP_175806039
VERSION     WP_175806039.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..251
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=26027
     Region          84..239
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mssdrsdsps aeptrdaaps spgpsrsaap llphdtpssa arrrflqsaa aaatvsaash
       61 vhsqpphaas tpaeprrdtv paqpvrldin graytlqlep rvtlldalre yagltgtkkg
      121 cdrgqcgact vlvdgrrina cltlavmheg arittaegla rggelspvqr afvecdafqc
      181 gyctsgqlcs atalldefaa gagsaatddv rrrpanlsdd eirermsgnl crcgaypniv
      241 aavraahaah g
//
LOCUS       WP_175806082             237 aa            linear   BCT 11-JAN-2025
DEFINITION  PadR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175806082
VERSION     WP_175806082.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 237)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..237
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25588
     Region          83..162
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mrhnpsrgha rcdghgahag pdwfagvlht igrhrrghdp fggggpfggr ggrggfgdfg
       61 ddgmprgrqf ssddlqllll alvaeqpshg yelikaldtr sngfyspspg mvypaltyle
      121 evgfvasqae gnrkryaltd agrahldaqr ervdtlfarl thlarkmefm rrafagesag
      181 neaqdesqag wlpefvearl alkrallhks aadadeqrri aaimrratae ieggaga
//
LOCUS       WP_175806083             273 aa            linear   BCT 11-JAN-2025
DEFINITION  siderophore-interacting protein [Burkholderia cenocepacia].
ACCESSION   WP_175806083
VERSION     WP_175806083.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..273
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=29746
     Region          5..266
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mqntsertvt rvrhtlkfrl lqvlrvhavt phllrvtlgg pdladfesas fddhvkvffp
       61 ppgaerpalp tlgangpefp agepkpvard ftprrfdraa reldlefvln hpgpasqwaa
      121 qarvgqwlgi ggprgsfvvp tgfdwhllig ddtalpaiar rleelpagar aavvlevadr
      181 taqisfdtra dvheiwrfra eadaadgdvl lnavrdlplp ssgdgyvwaa gealsmravr
      241 qhltgergvd ksriraaayw krgaaavhet led
//
LOCUS       WP_175806103             298 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175806103
VERSION     WP_175806103.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..298
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=31114
     Region          5..292
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 msillkgiia ypvtpfsadg gvdltaldal idrliadgvh aiaplgstge saylsdaewe
       61 avatasirav rrrvptvvgi sdlttagavr rarfaeqaga davmvlpvsy wklgndeiva
      121 hyraigdaig ipimlynnpa tsgvdmspdl iaticrsvdn vtmvkestgd lgrmhrlaql
      181 sdgtipfyng snpmalaala agaagwctaa pnlnaalpla lfdamrtgdl ararsvfhaq
      241 lpllqfivng glpvtvkagl rlrgfdagep rrpllplgda rmrelqrlla alpdgvaa
//
LOCUS       WP_175806104             226 aa            linear   BCT 11-JAN-2025
DEFINITION  MOSC domain-containing protein [Burkholderia cenocepacia].
ACCESSION   WP_175806104
VERSION     WP_175806104.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..226
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=24647
     Region          30..183
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
ORIGIN      
        1 msgdarpaia vaigavriga srplagtpha saidkrpvda rlwlgalgfa gdeqadarhh
       61 ggpdkavhhy aydhypwwag qigaravlaq pgafgenlst rgitehdvcl gdvftlggav
      121 lqvsqsrqpc wklnarfdhp rmaalvqhsg rtgwyyrvlq egwvaagdvl alharrypqw
      181 plstvldmaa lealcdvpll ppgwramlek rrterqvedw tkrldg
//
LOCUS       WP_175806121             324 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175806121
VERSION     WP_175806121.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..324
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37499
     Region          134..291
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mlhlidafvs diqtwlyvdv vqpllfkfnl mdydedtyda lywviigalq mvlmfallrp
       61 levllpverw knrravrvdv iytaisklgi ytlffffalq pvfdnfqawl rlhgvanvnl
      121 dylwpgvtsq pivafaiylv vldfagywyh rwqhkfgvww elhavhhsqr qmslwcddrn
      181 hllddvlqsc ffaaialvig vtpsqfvvlt avtnfvqsiq htnarlsfgw lgerllvspi
      241 fhrrhhavgy ghegtkygcn fgvlfpwwdm mfgtaswsrt veptgireqv egvsygdgfw
      301 sqhglafvri frrlfpakrg aasa
//
LOCUS       WP_175806160             273 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Burkholderia cenocepacia].
ACCESSION   WP_175806160
VERSION     WP_175806160.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..273
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28190
     Region          2..272
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mlktrvitai vmlavllpvt lfaplagfga ligvvlvfaa wewarllklg gagpvvyalv
       61 aalalaatap lgvdaassrp lfmaagvfwl lvgpfalrrk palaggvwrp fllvaglvvf
      121 aacwhalvaa ralgvpfvls lllvvwladi gayfagkafg krklaitisp gkswegaigg
      181 wfavmvvagv amavhafept lfsafaaryg mpgawaaltl lvaysvigdl fesllkrqag
      241 vkdssgllpg hggvldrvda llpvlplaml llg
//
LOCUS       WP_175806178             260 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cenocepacia].
ACCESSION   WP_175806178
VERSION     WP_175806178.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..260
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28263
     Region          7..260
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 msvadlaapg rigvraltie lgppharfaa ldtldvdiap gefvcvlgps gcgkstllga
       61 laghvaathg eivvdgervd rphpdrglvf qqhtlfpwkr vidnvafglk mkgvparerr
      121 reaaellelv glggfgahyp aqlsggmqqr veiarvlinr prvllmdepf galdaqtrrm
      181 mqtllldiws rigttvlfvt hdieealflg drilmlsprp arivadirvp larprtddst
      241 tepafvdikr rclallrdaa
//
LOCUS       WP_175806197             381 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia
            cenocepacia].
ACCESSION   WP_175806197
VERSION     WP_175806197.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..381
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42189
     Region          193..359
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <308..359
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mrittdigqd ldalrdvpaa ivldefawpp rpsrradfdg vargdaarre lglmlldlya
       61 vaaqsaigef ecrffsllqa lipfdaawtg vathvptgpv mhnsflyrlp hafftdwkrv
      121 rdcdplahrt lhgahgravr ltvvepglda rfrdwcvkyg laqlmcvctl drrfglttfm
      181 siyrqglnrp fsdddarcfe dviphlaaal tinraaqltr eradtvapaa ralcdnfgvl
      241 hhadhgfddv lrtewpswag arvpeplvah lrrqsgqpfv gdalriqcvp vaglfqiear
      301 prslldrlsp relaairyyg agrshkevaq qmaispttvr hylrcayrkl gmhdksqiag
      361 vlgatggatd deameaggmp r
//
LOCUS       WP_175806199             381 aa            linear   BCT 11-JAN-2025
DEFINITION  glycerate kinase [Burkholderia cenocepacia].
ACCESSION   WP_175806199
VERSION     WP_175806199.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..381
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38552
     Region          10..376
                     /region_name="GlxK"
                     /note="Glycerate kinase [Carbohydrate transport and
                     metabolism]; COG1929"
                     /db_xref="CDD:441532"
ORIGIN      
        1 mphhpsapvv viapdsfkgs lsaeqvadai atgirrarpd avvrccpmad ggegtldaml
       61 agggtrrtlr vagaslaare aavgvidart aivetaeivg itdpvgmsvp vdarstrgmg
      121 eairallddg vrrffvalgg sstndagagl laglglqcfd adgqpvepvp srladiarid
      181 asgldprlke tefvgmsdvd npltgahgat avfgpqkgvt aaqvatldaa larfadllea
      241 aldrrgrdlp gagaagglgf alhmlgaqfe agaevvarqv gldaalagah wlitgegrsd
      301 vqtlhgkapf iacrharaag vnasllsgai dpaalprlse hfsgcfspap gpitldvair
      361 daanllanea eqltrlkyga h
//
LOCUS       WP_175806220             119 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator [Burkholderia cenocepacia].
ACCESSION   WP_175806220
VERSION     WP_175806220.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..119
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=12849
     Region          1..119
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 matillvddd eealhafgll lehdghqvil arsgqealvk vseiavnlvi tdwsmpgmdg
       61 atlcrtlrtn pafsqlpivl msanqapade glwnaflqkp vswpmiaqtv qslvtmprt
//
LOCUS       WP_175806250             281 aa            linear   BCT 11-JAN-2025
DEFINITION  NRDE family protein [Burkholderia cenocepacia].
ACCESSION   WP_175806250
VERSION     WP_175806250.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Bard,F., Casano,L., Mallabiabarrena,A., Wallace,E., Saito,K.,
            Kitayama,H., Guizzunti,G., Hu,Y., Wendler,F., Dasgupta,R.,
            Perrimon,N. and Malhotra,V.
  TITLE     Functional genomics reveals genes involved in protein secretion and
            Golgi organization
  JOURNAL   Nature 439 (7076), 604-607 (2006)
   PUBMED   16452979
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..281
                     /product="NRDE family protein"
                     /GO_process="GO:0007030 - Golgi organization [Evidence
                     IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=30679
     Region          1..278
                     /region_name="Tango2"
                     /note="Uncharacterized stress-responsive protein, TANGO2
                     (Transport and Golgi organisation 2) family, contains NRDE
                     motif [General function prediction only]; COG3332"
                     /db_xref="CDD:442561"
ORIGIN      
        1 mcliafdwqp daaagpvftl aanrdeffrr tsaplswwed vpgvlagrdl eaggtwlgvs
       61 rdgrfaaltn yrapfdirag aptrgklvsd flggtpvapl dylaqlaeha avyngfnllv
      121 gdwrrrelaw fcnrapeges rvaapvaiap gvhalsnarl dtpwpkvvrk raelgtlltd
      181 nptpsldeli allrdphvad ddalphtgip iereralsaa fietpeygtr gttalrvtmk
      241 egvrltvevk ersdddgshr tvrpgafera ftfdidaarp r
//
LOCUS       WP_175806274             319 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cenocepacia].
ACCESSION   WP_175806274
VERSION     WP_175806274.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..319
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34282
     Region          83..292
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mplnpkiaqv ldmierakrp syhhqtpqqa raayeksapi ldvapapmhs veecvvptrd
       61 grtigarlyl pvapslaepl palvyyhggg ftvgsvdthd alcrmfarda qcavlsvgyr
      121 lapehrfpta vndaddalqw lhreaatfgi daarlavggd saggtlatvc avlardagir
      181 lalqlliypg vtghqdtash arlangyllt qdtiqwfftq yvrdradrdd wrfapldgtr
      241 dapsfagvap awiataeydp lsdegaayad klraagnavt lvcypgmihe ffkmggyvpe
      301 vraahadava alkaafdev
//
LOCUS       WP_175806301             398 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175806301
VERSION     WP_175806301.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..398
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42302
     Region          31..392
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msallpelas dsdshrldea ahavaqiaaq hadavdrdar cpveaieamr arrllgamvp
       61 thlggagasl ediasacsil gqacassamv famhqiqvac ivdhaadqgw hrlflqqlvr
      121 hqwllasats edgvggnlra sqcaleidgg gfrlhksapt isygdyadgi latarrdada
      181 paseqvlvtl lrdgytltrr gewdtlgmrg tcsngfvlda qgaavqclpv pfakiaeetm
      241 vpvshilwaa vwigvagdaf hrahqffraq arqtdgapsp aarriaesla lmqamqarvd
      301 nvlrlhanas arswsagmaw aaeintlkty vsatalevah qammicgmag ykqgtpfsig
      361 rhirdlhaap lmisndriaa ntaslllalr patlekht
//
LOCUS       WP_175806382             227 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cenocepacia].
ACCESSION   WP_175806382
VERSION     WP_175806382.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..227
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23901
     Region          24..223
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mtdvlplttn pdsglqyrlr pavgrpaarl lllhgvggne tnllnvadvi dprieiaflr
       61 gpltfgpsqh awfpvrfgpn gpeidaarad esrvqlitll halragdgaa pvlptviagf
      121 sqggimsasv gltspgdvsa favlcgrilp eidpliaprd alstlhalvm hgrfddklpv
      181 swadkadakl talgvahdtr lyatghelta emagdfgrwv gertgln
//
LOCUS       WP_175806408             281 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cenocepacia].
ACCESSION   WP_175806408
VERSION     WP_175806408.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..281
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=30806
     Region          1..258
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mttlasdsld ilhvskhytq rgatlavldd vslhvragef vtivgasgcg kstllrlvag
       61 ldtdytgeih aggervrdts lqrgivfqdh rlfpwltveq nigaalrnap ldaaakrrai
      121 aehialvgln gfehafpnql sggmaqrvai arglvnrprv llldepfgal daqtrakmqn
      181 ellriweqer itmilvthdv deavylgdrv vtmaprpgri arivdvalpr prrrdspafa
      241 rlrdtvladf ddseppgddg sggkridatr phrigewrla w
//
LOCUS       WP_175806412             302 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175806412
VERSION     WP_175806412.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32652
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdllatmriy arvvergtms gaardldmgq pavseriekl ekhlgtrllm rsartlacte
       61 egrifyersk alleaaelav asvsktahal dgtirlaapq cfgevvlpgv lmqirtaypk
      121 lhidlvlndd ivdpvtegvd isirvgqlgd ggfvayalga vgrmlvaaps ylerhgpidt
      181 kadlanhpfi rvkgvfaneq vplqrdggav eyarirtvmt ashwrpmfdt iaagggigvv
      241 qhpacadala hgrlvrllph ydvpdfalnv lvhaqrplpp rvravvdllk selpslltqg
      301 qr
//
LOCUS       WP_175806424             446 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia cenocepacia].
ACCESSION   WP_175806424
VERSION     WP_175806424.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..446
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47589
     Region          5..435
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mqassshepa rlkrtlglps vllfglayma plivygtygv lakasddtaa layllalvai
       61 aftalsygkl arlypaagsa ytytrrtfnp hlgfmigwat lldyfflpmv iwligaayln
      121 aafphvptwi wivafivlts glnivgiela arfnivlmvv qlaivamfvv lcwhyaaaaa
      181 gpggiamaep ffkphvpfga tmagaaiaay sylgfdavst lteetidpkk nmpraillia
      241 liggaifvia aytmqlahpg vdfkdtdsaa fevakmiggd lfvtvflagl ilaqfasgis
      301 aqasvgrlly amgrdeilpk rifgfihprv ktpainiala gvvglialkl dvatstsfin
      361 fgaflaftav nlcvirlyls gnhgerrigv fgglvfpaig avsdiwllvs lekaalvlgv
      421 vwfalglvyl cwitrlfrqa ppevai
//
LOCUS       WP_175806431             230 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Burkholderia cenocepacia].
ACCESSION   WP_175806431
VERSION     WP_175806431.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..230
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24640
     Region          160..229
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mttasqsrla tigrprrfgn kpthpvrrfg giaiaivlhl vliwalvngl atrvvqivqq
       61 pietriivpv kppppppppk pvekvvskpr vapppppfvp ppevrvqapp ptithqdvpa
      121 psapvheapp apapvpvakp vnreigvvcp nsdevrssiv ypteaqdnni tgdvtieftv
      181 dpdgrvanlr vaqpadpvln raalnavkrf hciaqgepvr vrvpfsfnln
//
LOCUS       WP_175806430             312 aa            linear   BCT 11-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175806430
VERSION     WP_175806430.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..312
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31887
     Region          79..285
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mnkrfraava aslmitagig gtlvapqavl aqqagastpg qaasggvpts aapataaaad
       61 havpppepat satvenpygl galwangdfv arfvlgllvv mslgswyimi tkfveqaran
      121 graksadeqv wnaptlaega aqlddaspfr fiaenaieag ehhdtallds vdrntwinln
      181 iersitsvsn rlqdglaflg tvgstapfvg lfgtvwgiyh altaigiagq asidkvagpv
      241 gealimtaig lavavpavlg ynflvrrnks vmervrdfga qlhtvllagg rratggvatp
      301 aaqspqalav qs
//
LOCUS       WP_175806462             157 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia cenocepacia].
ACCESSION   WP_175806462
VERSION     WP_175806462.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..157
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17065
     Region          3..153
                     /region_name="COG3865"
                     /note="Glyoxalase superfamily enzyme, possible
                     3-demethylubiquinone-9 3-methyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:443074"
ORIGIN      
        1 mtiqkitpfl wysteaeeaa afyagifpds rivrvtavpg tngtrmvefe lfgqpffams
       61 hprteafnha isllvscadq aeldrywsal ldnggtadgc gwlrdrygvs wqivpealip
      121 mmadrdavka grvaaammqm tkfdddalka afagtag
//
LOCUS       WP_175806501             195 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cenocepacia].
ACCESSION   WP_175806501
VERSION     WP_175806501.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..195
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20236
     Region          1..193
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msmlvsmaaf alassitpgp vnivalsaga rhglgaslry aagatlgfva lflliglglh
       61 aalarwpvlt tatqwsgiaf llymalrlal ddgrlsadpn vagpsaaaga amqwlnpkaw
      121 lacvaamgay aadgdraqvw qfaalylvic fasiacwgya gaslrhrlan arrmrvfnrl
      181 malllagsal flldv
//
LOCUS       WP_175806572             481 aa            linear   BCT 11-JAN-2025
DEFINITION  sialidase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175806572
VERSION     WP_175806572.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 481)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 481)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 481)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..481
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51024
     Region          144..428
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Region          177..238
                     /region_name="Sialidase propeller 2"
                     /note="Sialidase propeller 2 [structural motif]"
                     /db_xref="CDD:271234"
     Region          243..296
                     /region_name="Sialidase propeller 3"
                     /note="Sialidase propeller 3 [structural motif]"
                     /db_xref="CDD:271234"
     Region          311..364
                     /region_name="Sialidase propeller 4"
                     /note="Sialidase propeller 4 [structural motif]"
                     /db_xref="CDD:271234"
     Region          375..428
                     /region_name="Sialidase propeller 5"
                     /note="Sialidase propeller 5 [structural motif]"
                     /db_xref="CDD:271234"
ORIGIN      
        1 mrrmivshpl vtrlsaamal aaaavahaep vvvsgpspfa actiggpgtn yvnaevepwl
       61 avnpanpnnm igvwqqdrws nggahglvag ytfdagatwa rtpqpfsaca pgglkyeras
      121 dpwvsfgpdg taysvsisfn qsnnanavga svstdggqtw sspavliand epttqffndk
      181 esvtanpvka gtayavwdrl elpngnpyan lhtkayrgpt lfskttdggk twsaakvivd
      241 vpsrqqtign qivvdpksrt lydffdliqp pfskaagkva fikstddgat wtkpqviagl
      301 qtvgvtdpnt gepvrtgdii pepaidpasg qlyvvwqdsr fnggaydeia lstskdggat
      361 wsapqqvntp tgrpafnpsv rvdntgavmv thydfrdlqa gntttlptgf wrkishdgga
      421 tfaderrvgg pfdmklapna egffigdyqg ldvlpsssfh pffvqtnagn ltnrtdvffa
      481 p
//
LOCUS       WP_175806717             352 aa            linear   BCT 11-JAN-2025
DEFINITION  permease [Burkholderia cenocepacia].
ACCESSION   WP_175806717
VERSION     WP_175806717.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..352
                     /product="permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=37039
     Region          61..346
                     /region_name="YraQ"
                     /note="Uncharacterized membrane protein YraQ, UPF0718
                     family [Function unknown]; COG0701"
                     /db_xref="CDD:440465"
ORIGIN      
        1 mtttrtqpnp algwmtflli avaglfyvkw fpyynkafva aehhsigqsi lmgtsavape
       61 pslkaaldya waygkaiwqa mvlglllgsa vqallpahwv arvlgrtgfg svaaggllsl
      121 pgmmctccaa pvvaglrarh aspggavafw lgntvlnpaa lvfmgfvlgw hwsalrlvlg
      181 iamvfgigyl lnriarpedr siddaqlaal aaeqaaagnp fvrwmkllar mavrlvpeyi
      241 vlvlllgaar awlfphigpd ignhlgwiva favagmlfvi ptagevpiiq amlslgmgvg
      301 paaallmtlp pisvpslaml arsfkpymla ivatlvvvfg ivsgllaiaf gf
//
LOCUS       WP_175806755             557 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Burkholderia cenocepacia].
ACCESSION   WP_175806755
VERSION     WP_175806755.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60528
     Region          25..384
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          453..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mtpaslieqy gpresmeydv vivgggpagl saairlkqla aekgteigvc vlekgseiga
       61 hilsgavmdp raitelfpdw kergapldve vtedrflfls eksavttpnw alpdnfknhg
      121 nyvislgnvt rwlgaqaeal gveifpgfpa aeilynddgs vkgvatgnmg vgkdgepten
      181 fqlgmelhak ytlfaegcrg hlgrqliskf kldanadpqa ygigikelwe idpakhkpgl
      241 vihtagwplk sdtyggsfly hmdnnqvvvg fvvglgytnp ylspfeefqr ykthpsiraf
      301 leggkrvsyg araitaggll slpktvfpgg aligddagfl nasrikgsha aiktgmlaad
      361 aafdavqagr qsdelnaypd afkqswlyte lyrarnfkqw makglylgtl mvgleqkvmg
      421 gnvpwtlhhq hadhemlkpa sqcepieypk pdgkltfdrl ssvfisntnh eenqpahltl
      481 kdasvpvnvn lrtyagpear fcpaavyefv knddgserlv inaqncvhck tcdikdptqn
      541 ivwvtpeggg gpnypnm
//
LOCUS       WP_175806790             471 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatase PAP2/dual specificity phosphatase family protein
            [Burkholderia cenocepacia].
ACCESSION   WP_175806790
VERSION     WP_175806790.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Pulido,R. and Lang,R.
  TITLE     Dual Specificity Phosphatases: From Molecular Mechanisms to
            Biological Function
  JOURNAL   Int J Mol Sci 20 (18), 4372 (2019)
   PUBMED   31489884
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Patterson,K.I., Brummer,T., O'Brien,P.M. and Daly,R.J.
  TITLE     Dual-specificity phosphatases: critical regulators with diverse
            cellular targets
  JOURNAL   Biochem J 418 (3), 475-489 (2009)
   PUBMED   19228121
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   5  (residues 1 to 471)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12932297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..471
                     /product="phosphatase PAP2/dual specificity phosphatase
                     family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=50219
     Region          46..220
                     /region_name="PAP2_Aur1_like"
                     /note="PAP2_like proteins, Aur1_like subfamily. Yeast
                     Aur1p or Ipc1p is necessary for the addition of inositol
                     phosphate to ceramide, an essential step in yeast
                     sphingolipid synthesis, and is the target of several
                     antifungal compounds such as aureobasidin; cd03386"
                     /db_xref="CDD:239481"
     Site            order(121,129,155..157,192,198,202)
                     /site_type="active"
                     /db_xref="CDD:239481"
     Region          324..461
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
ORIGIN      
        1 msvlgggaga easdglaepa agardasfvl rlgwlaamga vffstygfan wlaarraavp
       61 tfafgwehai pfvpwtivpy wsidllyals fffwtrrddl ldhvkrlltv qlvsvacfla
      121 wplrfgferp daggmagalf tllmgfdkpf nqapslhigl lvvlwavyak hlrgtvarvv
      181 lhlwfaaigv svlttyqhha idvptgaavg clalflfplr daagrlpgad aspsaaaral
      241 arryafgaal valvalacvp rapgwalaag wvalalacva wayrrgapga fqkdahgrlp
      301 vfvggllapt iagafvnsrl wtrrqpapvr idervsigrt pttrdirrhg ftalvdltae
      361 mprwaaadas layasvpqld lvaptavqla qavaalerlh gegrdvlvcc algygrsvlc
      421 vaawvaarrg ltdardalaa vravrpravw sdesvavlqq widrrcgagq g
//
LOCUS       WP_175806816             774 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia cenocepacia].
ACCESSION   WP_175806816
VERSION     WP_175806816.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..774
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81505
     Region          <68..>194
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          203..764
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msapelsvhn asrralllgf asgglllafg vpslaqaaap vqppvsanpq yggagmphgl
       61 rddpnlfvai apdgtvtvtc irsemgqgvr tsvalvvade lgadwarvev aqavgdepry
      121 gnqntdgsrs lrqsfaalrr agaaartmle qaaaatwgvd vrqvkatvhe vvdtktgrkl
      181 gfgelaakaa alpvpdtksv alkapaefry igkgktalid grdivggraq ygidtrldgm
      241 lyavvarppv ygdtvasfda saagklpgvv kvvqlastpl psgfqplggv aviahdtwta
      301 iqaraqlkid wkhgpnagyd saeyrkalea aaaqpgdvir sdgdaaaala gaakrvraty
      361 yiphlahatm eppaavarva dgrcevwtct qapqttrdei akalglpter vtvnvtllgg
      421 gfgrkskpdy vveaallska vgapvkltft reddiahdyf havsleafdg gidasgkvva
      481 wqhrtvapsi qstfrpgvvh eqpgelaqgi adlpfaipnv rienpaaqah trigwfrsvy
      541 niphafgiqs fvselahaag rdpkdflldl igparrfeph itvknvnyge dpalypvdtg
      601 rlrrvvetva reagwgrklp kghglgiaah rsfvsytaav cevqvdadgk isvprvdiai
      661 dcgpqvnper vrsqlegavv mglgialhge itfkdgrpeq snfngfqvlr mneapreirv
      721 hlvapddyat plggvgepgl ppvapaltna ifaatgtrir slpvadqlak pqag
//
LOCUS       WP_175806839             214 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia cenocepacia].
ACCESSION   WP_175806839
VERSION     WP_175806839.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..214
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22885
     Region          1..203
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mkllhldssi ldgnsitrtl saavvadlha rhplaevtyr dlvrdeiahl tgpiaagfrd
       61 vatdafddda irehqvsdtl vteflasdii vigapmynfs vpsqlkawld riaqagrtfr
      121 ytehgpvgla sgkcvivasa rggfyaegpl agmdlqenyl nrffgflgvt dvrfvraega
      181 skgqrvrdeg ialaraaiad vlagvpapda rpvk
//
LOCUS       WP_175806915             203 aa            linear   BCT 11-JAN-2025
DEFINITION  cysteine hydrolase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175806915
VERSION     WP_175806915.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..203
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21135
     Region          24..192
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mqhptirtla gasaptsiaa artallvidf qneyfsgrlp ipdgpralgn arrviafadr
       61 agipvfhvqh vgtadspifa dgsdgfrfhs dlhpapqhtv vqktsvsvfp ttdldarlka
      121 agidtlivtg lmthacvaga ardavplgya vivvddacat rdldvadggt vphrdlhrat
      181 laalsdtfgd vltteqvlal dva
//
LOCUS       WP_175806923             219 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            cenocepacia].
ACCESSION   WP_175806923
VERSION     WP_175806923.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..219
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24251
     Region          29..180
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maevteraps krrtrgrpla dasvgpdvil raarrtfakr gydatsvrev arelgidaal
       61 iahhfgtket lwlavveqiv elaepmfdal ralrasslph rdrvrralel cvdhefaepd
      121 igmffstaat eeggrldrlq erivrpyhda mfplladave agairsvepn vlffmiasai
      181 gttvsyshmm leytslptrp eafreavlgv vfnflgdra
//
LOCUS       WP_175806958             264 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175806958
VERSION     WP_175806958.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..264
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27700
     Region          12..144
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          179..260
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mhrvthyrrt gegieaisle sdrafprhah defgvgvivs gahrswsgrg qvdalagdai
       61 mvnpgemhdg spleagtgrr wrmlylapal vagvaaeegl ggvelahpav rdarltaavg
      121 rlharivage tpplardeal vmlvagllar hanrtlpaag vapavrvvre rldaapaapv
      181 slaeladlsg vsrfqllrgf arelgitpha ylvqsrtrla rallasglpi adaaaeagfa
      241 dqshltrafa rqfgitpgrf tqaa
//
LOCUS       WP_175806977             319 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175806977
VERSION     WP_175806977.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18598969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..319
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35573
     Region          1..283
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          15..97
                     /region_name="cupin_MtlR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to MtlR, N-terminal cupin domain; cd06976"
                     /db_xref="CDD:380381"
ORIGIN      
        1 mmhpdlevvd vrrdesfkvw shgypyrtir whfhpefelh livathgkyf vgdhiglfgp
       61 ghlvllgpnl phnwvsdmae getverrnlv iqfdpsfvrr cmdafpecrd aqallddarr
      121 gvgfdaatsa aiaplfdell targmrrial fmtilerlcg aaertllasp aydqadvtpt
      181 rlshalsyig knlaselres dlaqltgqsv safsrafhrh tgmpfvqyvn rlriesacqm
      241 lladdasitd icfqagfnnv snfnrqfrav kgmapsefra lqrlnarsre lalhaaptgn
      301 plpprvltpg vpelmpqpg
//
LOCUS       WP_175807038             178 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein,
            partial [Burkholderia metallica].
ACCESSION   WP_175807038
VERSION     WP_175807038.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..>178
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
     Region          1..>178
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkilvpvkrv vdynvkvrvk sdntgvdian vkmsmnpfde iaveeavrlk eagvatevia
       61 vsvgvaqaqe tlrtalaiga drailvestd sveplavaki lkalvdkeqp qlvilgkqai
      121 dddsnqtgqm laalaglpqa tfaskvtvad gkatvarevd ggaetlsltl pavvttdl
//
LOCUS       WP_175807137             727 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cenocepacia].
ACCESSION   WP_175807137
VERSION     WP_175807137.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..727
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79192
     Region          41..727
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mmqgarvarf grwrpslylg lliaahpaaa fadaapaaga evrqdeaaaa qpagselkai
       61 avnasrgvad dpsvatvgkm plalreiprs vsvttrerid qqnlfsldev mqqsagvtvq
      121 pyvllttayf vrgfkvdsfe fdgvpvvigd masapqdisv yerveilrga ngllhgsgnp
      181 aatvnlvrkr pqyqfsahat asvgswdryr aeadiggpln aagtvrsrlv aayedrhffy
      241 dhakqdtrsi ysvtevdvtr dtlltfgaqy qtttsvpdms gvpmardgss lglsrstfld
      301 tawgrfnwdt trafasveqk lgagwkakvs geyqsvrsdl kyagsfgaid patgaggrlt
      361 gaayqfssys rsvdanvqgp vhafglthdl lfgvtyanss sgqmtapllg dvagtpvnvy
      421 rwnpssvpep gigpyqqsqq ndvsqkgvyg lgriklaepl tlvlggrmsw wnqdslgahy
      481 ntghqftpyg gliwdfardw swyasyaevf qpqtksmwgg giltpvkgrt yetgvkgela
      541 ggkldvslaa fridldnnpq vdlahpcagp scyyvnggsv rsqgfefean gritpwwsvw
      601 asytydtmry adnlanagtf apllnprhlf rlwtnydlpw qerrwsiggg vqvqssysaq
      661 angvtmsqgg yalasvrlgy rydkhwsaal nvnnlfdrty yqslsqpgwn nrygeprnvm
      721 ltvrgqf
//
LOCUS       WP_175807144             257 aa            linear   BCT 11-JAN-2025
DEFINITION  thioesterase II family protein [Burkholderia cenocepacia].
ACCESSION   WP_175807144
VERSION     WP_175807144.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..257
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=28465
     Region          17..250
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mstpatgsnw irelrlspcp raqlvcfpha ggtanffrgw sralpwdvdl lalqypgree
       61 rfgepclpsi dalagpaada lqryahaplv lfghslgaal ayevavrlea rgaaplyvav
      121 salppphrqr psdlhlqsdd alvgdvarls gehaalladp emraiylpmi rhdyraiety
      181 rrdrpprida plgvmlplad teldsdeaha wqdvaarpir vetfngdhfy lrhqypavia
      241 hlveridqsl rygkeyt
//
LOCUS       WP_175807169             446 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175807169
VERSION     WP_175807169.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..446
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47385
     Region          36..420
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(50..51,54..55,58,90,140..141,143..145,148,168,
                     171..172,175,269,272..273,276..278,281,309,313,364..365,
                     369,373,389,392..393,396..397,400)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtnpngaatp rgmqagppah aqaaapslda lytrlsrrii plilvcyffg yldrvnvgfa
       61 klqmvtdlhl tdaaygvgag lffvgylllq vpagwlvrri gvkrclagsm ltwgivsvat
      121 lttrdtasfy alrfllgvte asffpaviay fsvwfpshrl akvmallfla mplgvivggp
      181 lsgwimdath ggfglrgwqw mflieglpai vlgvyllarv teriddatwl tdaekrmira
      241 emaqeaagkr trlgaalrep tlwllfatsf lynignyglv fwmptmikal gslsnlqigl
      301 vsaipylvas vamvanaqhs vrtgerrwht alpvaiggia llaslgmrth pvlavacltv
      361 gvagimstla mfwslpsril ageaaaggag lvnigaavag fvgptlmgya tgltgstelg
      421 vallaftlfa aaalilsipr rlmvrt
//
LOCUS       WP_175807193             375 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia cenocepacia].
ACCESSION   WP_175807193
VERSION     WP_175807193.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..375
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=40730
     Region          7..375
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkrktlalsi aaaglcagha haqssvqlyg lmdlsfptyr thadangkhv igmgnegepw
       61 fsgsrwglrg aedigggtki ifrlesefvv angqmedegq ifdrdawvgv ederfgklta
      121 gfqntiarda atiygdaygt arltteeggw tnsnnfkqmi fyaagptgtr ynngvawkkl
      181 fsngifasag yqfsnstsfa tgsayqaalg ynggpfnvsg fynhvnhngf rnqtfsvggn
      241 ytfdivrlna gyfryngdqg plgqrhddsw tvsmkiapkg aldyelgyqq mriknaanna
      301 dgftpnanlg afsltngvan gfketiygsv fyhlskrtev ylagdymklh ggytvsstfg
      361 aknqleltsg irtrf
//
LOCUS       WP_175807197             404 aa            linear   BCT 11-JAN-2025
DEFINITION  cation:proton antiporter [Burkholderia cenocepacia].
ACCESSION   WP_175807197
VERSION     WP_175807197.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..404
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43598
     Region          13..390
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mksafsflpn wplapdavfw aglalfaagl cgelcyrawr lpritgyavi gliagsfgfg
       61 vidtstdets rllmdvalgl llfelgsrld lrwirrnpwl vasslaeatl tfvlvlfvml
      121 algvsgmval vlsaiaiats psmviqlkte lraegqvsqr litltalnsv yaivltklvt
      181 swlhqeaygn vfatilqply llagsfivay lvarscnylf rhmtatmrde hsfvalfglv
      241 mlaiavaqal klstlltlll agiiaknlea rpqlwpehfg tagwlltvvl fvltltsftw
      301 gdialgglla ivlivtrlva klagvvafak psglgmkqgv algialtpms alsyllvddt
      361 yqlypnfdph lraivmcsiv ilqlvspfvv yrclsavger sdgn
//
LOCUS       WP_175807212             707 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cenocepacia].
ACCESSION   WP_175807212
VERSION     WP_175807212.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..707
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76915
     Region          32..707
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mtvslarppv rprrvaaala claaslahad dssgdaavlp alnitaahds pqhltdtist
       61 galgirrqld tpfsttivts eelearqpyk lgdvfandas vsdnsgaysa wasymtvrgm
      121 qldwqngyki dglpfvtygi tmpyeqlerv ellkglggfl hgfvtpggvv nyvtkqpgae
      181 pvrsvdisyr stnvwtehvd lgqrfgpndm fgarlnathe egktyndgni rrnsvslalq
      241 anltrdlsvs fgalyqdrrt tgqtpsiftg sypggalpat isggstnlgg kdqylntnlq
      301 lytaglqyql apdwqldvay syskatrrrn estlylqdaa gnytdsryvg medhrfsqwr
      361 amvegkvrtg pfshqivlga swqkqandys ansvfvplga gnlyapnpyr yesphgfiqy
      421 rtseivqksl fasdtvqlte rwsvlagvry mnyeqrafqa sgaedpgyrq ngvvtptfav
      481 mfklapttta yvsyaeslep gsrvndvyan agqvlkplrs kqyelgikse harwsataal
      541 friersaeya naanvyvqdg esiiqgievg arakfgahwn agvdamllda wyangignng
      601 nrvagaprfv lagdlgyavp gvpgltlgvd akftgatplr aaggldapgf lvvnagaryl
      661 trvgrhdvtl rasidnvlnr ryweyqyady vkpgdprtvs lsakidf
//
LOCUS       WP_175807223             405 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175807223
VERSION     WP_175807223.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..405
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40629
     Region          32..399
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(42..43,46..47,50,82,132..133,135..137,140,159,
                     162..163,166,234,237..238,241..243,246,274,278,327..328,
                     332,336,352,355..356,359..360,363)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 msqssspess spfaappdah rvlplparqr artasmalff vagmmyaswg vhvptvrdkf
       61 alspgllsia lfavaggsiv amlsiarwia rvgsrtacla gglvmsacaa lilvvpdywm
      121 llavlalfgf smatldvamn aeasaveial gkpimsslhg mfsiggmgga aaggallsag
      181 mapavhlala aavgaavlvt aspavlphvp hheqahgggn rwrspalwml ggialialia
      241 egamydwatv ymrdvvaasp alasaayaaf sggmaiarfa gdavrarfga pqlvfasasl
      301 acagmigall lpysaavltg ftlmglglan mmpvlfaaaa rvkgihaaeg lahvaglayf
      361 gllfgpvaig avaqasnlti glsvvalcaa lvalvapkvl ahlki
//
LOCUS       WP_175807235             190 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Burkholderia cenocepacia].
ACCESSION   WP_175807235
VERSION     WP_175807235.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..190
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19765
     Region          15..169
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 manetrtdse rsldivalcg slraqsynaa lldaaarvap rgmhitrfdr lgefplfnpd
       61 aeyptpaavr dlidrlnaad gvliaspeya hgvtgvmkna ldwvvgceav vykpvavlna
      121 sprathadaa lretlsvmsa rivepasial pilgsqlnaa giaahppfas alvdalhalr
      181 taietsasgs
//
LOCUS       WP_175807249             437 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia cenocepacia].
ACCESSION   WP_175807249
VERSION     WP_175807249.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..437
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45600
     Region          53..433
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mlklnlvaai vfvmvataha qpsptpgpaa aaassatpig appsdtlpas sltlsdalav
       61 aarnnpalrg aradvdasag tlmqagarpn pevsflqegf sraertstal inqtielggk
      121 rrarldvasy greaanasld eqgaavradv iaafygllaa qrqlqvtees aaiaarsadl
      181 agrraqagkv spveatkaqv aaagvqievv targrvevar eklnavmgea rddrlavrgd
      241 letvppvepl saltvqldda plarvaraem lrsnaavsle rarripdvtv sagfkrvttg
      301 gvpdnqavvg vsipiplfnt nkgalleath kaeranadld rertrlrlel tqayanfeaa
      361 eqeaqrlkvd ilpaarlald amsrgyelgk fsfldvldaq rtlfqgqsqy vralagahaa
      421 radigrlvgt plaavaq
//
LOCUS       WP_175807091             470 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatase PAP2/dual specificity phosphatase family protein
            [Burkholderia metallica].
ACCESSION   WP_175807091
VERSION     WP_175807091.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Pulido,R. and Lang,R.
  TITLE     Dual Specificity Phosphatases: From Molecular Mechanisms to
            Biological Function
  JOURNAL   Int J Mol Sci 20 (18), 4372 (2019)
   PUBMED   31489884
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Patterson,K.I., Brummer,T., O'Brien,P.M. and Daly,R.J.
  TITLE     Dual-specificity phosphatases: critical regulators with diverse
            cellular targets
  JOURNAL   Biochem J 418 (3), 475-489 (2009)
   PUBMED   19228121
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   4  (residues 1 to 470)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   5  (residues 1 to 470)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12932297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..470
                     /product="phosphatase PAP2/dual specificity phosphatase
                     family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=50412
     Region          45..219
                     /region_name="PAP2_Aur1_like"
                     /note="PAP2_like proteins, Aur1_like subfamily. Yeast
                     Aur1p or Ipc1p is necessary for the addition of inositol
                     phosphate to ceramide, an essential step in yeast
                     sphingolipid synthesis, and is the target of several
                     antifungal compounds such as aureobasidin; cd03386"
                     /db_xref="CDD:239481"
     Site            order(120,128,154..156,191,197,201)
                     /site_type="active"
                     /db_xref="CDD:239481"
     Region          323..460
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
ORIGIN      
        1 msalgggard laesapaaga garhasfalr vgwlavmgav ffstygfanw laarraavpt
       61 fafgwehaip fvpwtivpyw sidllyalsf ffwtrradll dhvkrlltvq lisvacfiaw
      121 plrfgferpd aggaagalft llmgfdkpfn qapslhigll vvlwavyakh vrgtlarvvl
      181 hlwfaaigvs vlttyqhhai dvptgaavgc lalflfplrd aagrlpgada spgaagrala
      241 rryalgaalm awaavwsvpr aqgwalaagw ialalacvaw ayrrgnpgaf qkdaqgrfpv
      301 firwllapti agafvnsrlw tfrqpapvri gervsigrtp ttreirrhgf talvdltaem
      361 prwaaaeasl ayagvpqldl vaptaaqlaq avaalerlhg egrdvlvcca lgygrsvlca
      421 aawlamrrgl gdardalaav ravrphavws ddgvavlqqw idrrggvgrv
//
LOCUS       WP_175807256             431 aa            linear   BCT 11-JAN-2025
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Burkholderia cenocepacia].
ACCESSION   WP_175807256
VERSION     WP_175807256.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..431
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=46339
     Region          1..430
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 mtdqahsnwr letiavhggy rpdpttrava vpiyqtvaya fddtqhgadl fdlkvqgniy
       61 trimnpttdv leqriaaleg gigalalasg qaavtyaiqt iaeagdnivs asslyggtyn
      121 lfahtlpqyg ittrfadprd pssfeplida htkaifaesv gnplgnvtdi aalaevahrh
      181 giplivdntv pspyllrpfe hgadivvhsl tkylgghgts lggaivdsgk fpwaehadrf
      241 krlnepdvsy hgvvyteafg paayigrarv vplrnmgaai spfnafqilq gietlalrve
      301 risdnalkia qhlarhehve wvnyaglpeh pdhplvaryl sgrapgiltf gvkggrdgga
      361 kfqdalklft rlvnigdtks lathpastth rqlspaelak agvkeetvrl sigiehiddl
      421 ladldqalaq l
//
LOCUS       WP_175807266             208 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cenocepacia].
ACCESSION   WP_175807266
VERSION     WP_175807266.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..208
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22279
     Region          12..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mfdlttlttf tavvlglfli pgpavllvls rtvqdgrktg iltglgvasg dfvhtlfaav
       61 glsallmtsa lafnvvklvg aayliylgvr allekpsdps lpqvspvtpl kaylqaipae
      121 vlnpktalff lafmpqfvhp ergstfvqfa vlglifvvls slyttliacs irplgrivkr
      181 ltwltrwqgk iigsifialg lrvavqqr
//
LOCUS       WP_175807278             229 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cenocepacia].
ACCESSION   WP_175807278
VERSION     WP_175807278.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 229)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..229
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24689
     Region          1..229
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 mifqgfgpll wagtvetvkl avlslaasli lglagaaakl sanrvlksvg tfyttlirav
       61 pdlvlmlllf ygiqillnnv tdllgwdqid idpfaagvvt lgfiygayft etfrgaflav
      121 prgqlevgfa ygmsgwrvfh rilfpqmmrf alpgignnwq vlvkatalvs iigladvvka
      181 sqdagkstld fffftlaaga iylaittvsn vvlhhlekry svgvrrlal
//
LOCUS       WP_175807311             303 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175807311
VERSION     WP_175807311.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33625
     Region          7..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..295
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(111..112,114..115,118,122,124..130,223..228,
                     234..235,237..238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176104"
ORIGIN      
        1 mnthitlrqi eyfvsvadtg qisksanlcs vsqssmtial knleeavgvt lllrhpkgvr
       61 ltpagerflr hvqhattsid ravvaaqedp eqiaghvrig mtetistylm pslmsaisqr
      121 fgnlgvsive seretietml iddrldiall lvsntaevgd lkyetilrsp rrlwthpghp
      181 lqdarrvtle dvarenylll dmdehlrtvg kywgsygvap nvwmqsksie avrslvalgh
      241 gvtilsdlvy rpwslegnri srrnlsvtvp tmdvgavwrr ggatstpcra llelfrswrk
      301 tag
//
LOCUS       WP_175807355             326 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Burkholderia
            cepacia complex].
ACCESSION   WP_175807355
VERSION     WP_175807355.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..326
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35328
     Region          47..200
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <200..320
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 meidartppq prtppdhdar sparlptarl aaliaayaph dgmfdlplrg mraarasaps
       61 pqwnhgvhha clslvgqgak smrvgdatyg idesrmlvat adlpvtgrvt radpaepfly
      121 aqleldprri aaltpvvfph glpkavdyga ldtldatpei vdavarlmql iaqpddldll
      181 aplivdeili rllrgpsgar vaqigdagst tqrisravaw irdhyldpma vdalarqvem
      241 spstfhhhfr avtsmsplqc qkvlrlqear rlmclsamda rqacrsvgyv sasqfsreya
      301 rlfgdapgrd varlrgeavp lsrvap
//
LOCUS       WP_175807362             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175807362
VERSION     WP_175807362.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46222
     Region          22..420
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,150,
                     153..154,157,245,248..249,252..254,257,285,289,347..348,
                     352,356,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mkdnppvpha pprirrgqri alallmasgi vnyldrgtla vassairgdl glslaqmgll
       61 lsafswsyal cqfpvgglvd rigprrllgi glivwsfaqa sgglvstfgw fivarivlgi
      121 geapqfpsaa rvvsnwfplr argtptgifn aasplgtala plllsvlvas fdwrwafivt
      181 galglvvavv wfafyrdpvr aqlsaaerny ldadaqsvaa apkltfaewr slfshgttwg
      241 mligffgsvy lnwvyltwlp gyltmerhms lirtgfaasv pflcgfvgsl vagwlsdlvt
      301 rrsrspvvsr rnavvaamlg mvaftipavl vqsntvalac isvviflana asacswalat
      361 aaappsrias lgaiqnfggf iggalapilt giiaqkwsfv palltaaaia fagamaylll
      421 vrkpipeqaa naapgplpa
//
LOCUS       WP_175807369             281 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia cenocepacia].
ACCESSION   WP_175807369
VERSION     WP_175807369.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..281
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29956
     Region          10..257
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(24,105,107,109..110,138,189,210,213,226,228,257)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 msnvtfpgqr vgdftitais dgyltasldf lanidvsdaa gmqraagqqa psavhincyv
       61 vrgagrtvli dagaggikqw ggrlmdnlrl agvepaaidt vllthahpdh vgglvhadgh
      121 vafpnaelva hrrevafwrd dgnlsraser argnfriarq vfdaysdalr tfeegevlpg
      181 iaaiplpght dghtgyllas gdqgllvwgd ivhfphiqik rpdvsiafdq dasqaattrs
      241 rlldrvsseg lliagmhlge pgfarirras geyglfyetd a
//
LOCUS       WP_175806969             515 aa            linear   BCT 11-JAN-2025
DEFINITION  FGGY-family carbohydrate kinase [Burkholderia cenocepacia].
ACCESSION   WP_175806969
VERSION     WP_175806969.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..515
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=55485
     Region          3..448
                     /region_name="ASKHA_NBD_FGGY_RrXK-like"
                     /note="nucleotide-binding domain (NBD) of Rhodospirillum
                     rubrum xylulose kinase (RrXK) and similar proteins;
                     cd07804"
                     /db_xref="CDD:466806"
ORIGIN      
        1 meyvigvdig tqstkallvd rhgtivarrs agyqpdtprp lwaeqwpqvw fdavrdciag
       61 cvsdaraqgv padairavcv sslyggsgip vdidmrplhp cliwmdrrat aevdwvnehv
      121 nverlrvitg ngvdsyygft kmlwlrdqrp dvwanvryfl ppnayviyll tgevavdhss
      181 agniggvydv arrewsddal dmlgipatmm perlvdstdv vggllsqwta qlglpagtpv
      241 vaggvdaava tfaagatrtg qhvamigtsm cwgyvnrhvd arhglvsmph vfdgqrdlyv
      301 fggaitagas vawfrdqfch aeidaarllp hgdphvllee aaervpagad gvlflpylmg
      361 erspvwdaka sgafvglsla htrahlyrav legvafalrh nieagrrgav alddrlivvg
      421 gaahsalwmq iiadvtgfpv wtieqdveaa mgaallagvg aglvsrddaq ggwvtlvera
      481 rpdadrakty dgrfslytal ypalkpimhr lgtss
//
LOCUS       WP_175807372             190 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter small permease [Burkholderia cenocepacia].
ACCESSION   WP_175807372
VERSION     WP_175807372.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..190
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=19964
     Region          31..185
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mtrrtslnsa aaaggsaaap dgtpparpha apllrcvndv lfrvlagias sclavltvlv
       61 fyavvmryvf enapdfvepi alllviviam fgaamkvrdg ghigldslvr rlspkartvv
      121 iaiqhlslia faimimigcg smavetmgdr ipiiglpegv rylitmpaav aiiffslehl
      181 lalrrsssgq
//
LOCUS       WP_175807399             320 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175807399
VERSION     WP_175807399.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..320
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35168
     Region          7..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..291
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(111..112,114..115,118,122,124..130,221..226,
                     232..233,235..236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176122"
ORIGIN      
        1 matklsfevl evldaidrtg tfaeaaellh rvpstltylv qklesdmdve lfdrsgrrtk
       61 lteagravve dgrrlldaar hleakakgir dsweselrlc vdailpiqsl wpyvhafydl
      121 emntqlslst evlggvwdal vtrradlaig afgepphaan iaarpigtlr hvfvvapdhp
      181 laripeples etiagyrgvv isdtsrelqp qsvatrdgqp lvivptlaak lqalcegiav
      241 gmlpdfvake pihegrlvar rivgvrvftn gylawredkv gnalnwwiaq ldsadllerl
      301 ltprqeskgq pgtatcavry
//
LOCUS       WP_175807434             234 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia cenocepacia].
ACCESSION   WP_175807434
VERSION     WP_175807434.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..234
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25183
     Region          10..234
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mfqilraedr crthhgwles shsfssvcrd ghapvrppvg alcmlsedri aptrgfgmqp
       61 rrdveiltyv ldgelahrds lgcgaivrtg giqrvsagtg lvhsetnasr drplhllqiw
      121 lqpaerggrp gyeerrfadd ekrgrlrrva apdggddals vradarifag lidgdetaaf
      181 dvpagrsiyv hvvrgevevn gralaagdga riggvdavaf argrtaevll fdva
//
LOCUS       WP_175807438             455 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175807438
VERSION     WP_175807438.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..455
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46760
     Region          19..417
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(26..27,30..31,34,66,116..117,119..121,124,144,
                     147..148,151,273,276..277,280..282,285,313,317,369..370,
                     374,378,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mnadtglplp qrywaivcva lgitlavldg aianvalpti ardlhasdaa siwivnayql
       61 avtitllpla slgerigyrr iyiaglalft aaslgcalag slpmlavmrv iqgfgaagim
      121 svnaalvrmi ypssllgrgl sinamvvals saigptvasa ilsfaswpwl favnvpigia
      181 avlgslralp anplhdapyd fasalmnacv fgllitavdg lghgeghayv aaelavasvv
      241 gyffvkrqls qpapllpvdl mripmfalsv ytstasftsq mlafvalpfw lqnslgfsqv
      301 etglymtpwp lvivfaapla gvlsdrysag ilggiglalf aagllslati gahpgtvdiv
      361 wrmalcgagf glfqspnnra mlssaprers ggaggmlsta rltgqtlgaa lvalifglap
      421 drgptialyv atvfaavaav vsllriaspr pdtaa
//
LOCUS       WP_175807466             243 aa            linear   BCT 11-JAN-2025
DEFINITION  alanyl-tRNA editing protein [Burkholderia cenocepacia].
ACCESSION   WP_175807466
VERSION     WP_175807466.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V.
  TITLE     Evolution of aminoacyl-tRNA synthetases--analysis of unique domain
            architectures and phylogenetic trees reveals a complex history of
            horizontal gene transfer events
  JOURNAL   Genome Res 9 (8), 689-710 (1999)
   PUBMED   10447505
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Cusack,S., Hartlein,M. and Leberman,R.
  TITLE     Sequence, structural and evolutionary relationships between class 2
            aminoacyl-tRNA synthetases
  JOURNAL   Nucleic Acids Res 19 (13), 3489-3498 (1991)
   PUBMED   1852601
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Schimmel,P.
  TITLE     Classes of aminoacyl-tRNA synthetases and the establishment of the
            genetic code
  JOURNAL   Trends Biochem Sci 16 (1), 1-3 (1991)
   PUBMED   2053131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..243
                     /product="alanyl-tRNA editing protein"
                     /GO_function="GO:0002161 - aminoacyl-tRNA editing activity
                     [Evidence IEA]"
                     /GO_function="GO:0002196 - Ser-tRNA(Ala) hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004813 - alanine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006419 - alanyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=26403
     Region          3..243
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
ORIGIN      
        1 mttqalfred ayltqceaiv qavgddgirl drtvfyplgg gqagdtgtlt lpdgstiaia
       61 dtrkakfdga tpddavhvsa pgqeasvatl apgtrvvaei dwlrryrhmr lhtaahlmca
      121 vlpyavdgcs vtadyvrldf atfdaidrdd verrlagfvv gahpvttewi tddemaerpe
      181 lvrtmsvkpp mglgrvrllr ienvdlqpcg gthvrntsei gglrvaklek ksartrrlvl
      241 efa
//
LOCUS       WP_175807482             377 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175807482
VERSION     WP_175807482.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..377
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40449
     Region          1..365
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfsftdeqq qfadalrryl aeqygfearq aivrsdagvs daqwraftel gltalpvpda
       61 qggfgggpvd mlvvmqelgr alviepywat avgvealria gsgagddaal leavaqgqkr
      121 vavafhepqa rydlyeldth areqggtyrl tgtksvvqhg aqahvwivpa rvdgggiglf
      181 vverdaantk vvdyrtidgq raatitfdda parlltggar davaleqiad yatfllcaea
      241 vgaldelnra tveytktreq fgvpiarfqa lqhrmvdmli haeqarslty laavryangd
      301 adarrkavsa akarvgaaar fvgqqavqlh ggmgvtneva aahlfkrlsi iettlgdtdh
      361 hlaritalpd faqtdva
//
LOCUS       WP_175807566             213 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia cenocepacia].
ACCESSION   WP_175807566
VERSION     WP_175807566.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..213
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=21845
     Region          7..213
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mtqrslnial fgatgtigsr iaaeavrrgh rvtalsrhpg asgdgitaka adlfdaasia
       61 aalpghdvva saygpkqeda aqvvaaakal vagtrqaglk rlvvvggags levapgkqlv
      121 dtegfpdayk pqalahrdal dylktvtdld wtffapaali apgertgsfr tgvgklivda
      181 qgnskisaed yavafvdale qdsfvreiat vay
//
LOCUS       WP_175807579             343 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cenocepacia].
ACCESSION   WP_175807579
VERSION     WP_175807579.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..343
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36649
     Region          8..343
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkldstpitl tgcaktfrgt rvlepldlsi gagetlvllg psgcgktttl rliagldtpd
       61 aggtiafgdd dvtalpierr qvgmvfqnya lfpnltvrgn vgyglkirkt epralrervd
      121 ellammrlda hadkpvdqls ggqrqrvala ralavrprvl lldepltald aklrdvlrrd
      181 mnallrelgv ttvyvthdqa eamelgdriv vmgagrieqi gtpreiyyhp anrtvaqfig
      241 tlnrlagqwr dgalattgga ivtphaadew ffrpedaqla dpahaplrga vgacaflger
      301 trltiehaap dalvidvpgr ialargtavg ltiapegliv lga
//
LOCUS       WP_175807656             217 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cenocepacia].
ACCESSION   WP_175807656
VERSION     WP_175807656.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..217
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22535
     Region          20..216
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mqesqvktgl rsrrpgalvp lhdylplvlf vivstvtpgg attlatasga hfgyrrslpl
       61 magiaaglas maaaaaaglg svllalpalq lvmkavgsay liwlalrigr ggkprldvdv
      121 hrpqgfvsgv wmlwhnpkgw amtlgaaasf aalasgparl gvllgfafgv aamaslslwc
      181 fagllfarvl rterqwrcln aglgvllvas ivpmwlp
//
LOCUS       WP_175807661             306 aa            linear   BCT 11-JAN-2025
DEFINITION  bestrophin family protein [Burkholderia cenocepacia].
ACCESSION   WP_175807661
VERSION     WP_175807661.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..306
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33590
     Region          1..299
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 mivrprehwl rmllvwngsv lptilpqlvl tlsislvavw gggrvlgekv plnptpftli
       61 gltlaifagf rnnasyeryr egrqlwggvl tatrtlvsqa lcygavdrdd asrrafvrtv
      121 vafvytlkhq lrgtdpaadl rrlldgatya rvvasrfrpi vighalreaf aaradagqla
      181 dtrlwmldar lddlvamvsg ceriastpip fsydvllhrt iyaycvllpf glvdsigaat
      241 pfvtvfvayt lialdaiaha iaepfgdgpn hlaldamtrq iertllelnr eplpaevtpg
      301 psyrlt
//
LOCUS       WP_175807699             319 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Burkholderia cenocepacia].
ACCESSION   WP_175807699
VERSION     WP_175807699.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442595
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..319
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34538
     Region          5..295
                     /region_name="AKR_unchar"
                     /note="uncharacterized aldo-keto reductase (AKR)
                     superfamily protein; cd19103"
                     /db_xref="CDD:381329"
     Site            order(14..16,54,59,85,120..121,147..148,172,201..207,255,
                     270..275,278,281..282)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381329"
     Site            order(54,59,85,120)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381329"
ORIGIN      
        1 mtidnpkppt ialgtwawgd sgeagngyfg ssltraglea vadkahaagf clwdtamvyg
       61 mgrsetvlge vlkrfarsdy rlstkftpqa agtgadpvad mleqslarlg tdyvdlywih
      121 npadvarwtp hlvpllesgk ikhvgvsnhn lgeieqadri lreagfrvea iqnhysllyr
      181 dseragildy crdrgipffa ymvleqgals gkygpahplp egsnraqtyn rmlprlkalt
      241 dalaaigrkr gaaapdvata walakgttpi vgvtrpdhvd glarasritl aadeiaelea
      301 ladaadvntr gwwehemqv
//
LOCUS       WP_175807731             466 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175807731
VERSION     WP_175807731.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..466
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49450
     Region          42..449
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(51..52,55..56,59,91,141..142,144..146,149,169,
                     172..173,176,284,287..288,291..293,296,324,328,379..380,
                     384,388,404,407..408,411..412,415)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mstfdnvvag raateaaast pgaiiarler lpanamqira rvligtatff dgfdvitiaa
       61 tlpllihkwg lsptqigmli asgaigqlig aflfpalaek hgrvkaiaws savigitsia
      121 cgfaptfeif vllrilqglg lggelpvaat yineitrahg rgrfvllyei vfpigllvsm
      181 algawfvprf gweimyfvgg lplilslvlt hlvpesprwl asrgrlaeag ravgvfegsv
      241 rgelppvtqv aafdemvrqh pkrrmsdlfs aayrkrtlav atlwatcgfi qyglstwlpt
      301 iyknfyhapl qlalnlavig svmgvlgsla sallvdklgr kpvivwsfvl calslalagi
      361 yhassvyvva vfcslslglm asgfitayvy tpeqyptsir asgcglgsaw lkiasfaapm
      421 ivphaiiggn lapafyligi vpliaagtvh fvgietkgkv lealea
//
LOCUS       WP_175807735             298 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175807735
VERSION     WP_175807735.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..298
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32409
     Region          26..281
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mvkttmsdap epampgddes sgggassylv pglerglril aefsarepvl gapelskrig
       61 iprtttfrll qtlealgfle rvngdryfrl gvgvlrlgfe ylnsleltdl gtpvlerlrd
      121 stglsthlli rdqrdvvfva kaqsnasmfg svkvhvgtrl pahatvhghv lmgdltrdal
      181 rqlypekkle qftertpgtv delyervrhy arlgyavsea afesgisavt apvrdhsgsi
      241 vaaitatvpr seigeageke rlveavcgaa vdlsqrlnyr plesdptfah arhkvamf
//
LOCUS       WP_175807738             381 aa            linear   BCT 11-JAN-2025
DEFINITION  metallophosphoesterase [Burkholderia cenocepacia].
ACCESSION   WP_175807738
VERSION     WP_175807738.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..381
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=40818
     Region          113..381
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mrsffvrfia igvlfhlyvg mriipdafas plartiaalv lasfvvlipv gmfsrrfdeg
       61 waatlvgwag alvmgffssl lvltllrdfv llgvlvwrhl ghdgawpgaa pdtalgvlaa
      121 avfvtaigfv garrtaavkr vsipvaglpa aldgltivql sdihvgptik rpyierivra
      181 vnaldadlvv vtgdvvdgsv krlrehtapl gqmrsrhgtf lvtgnheyya gahawidefr
      241 rigltvllne hvlierggar avlagvtdft aggfdpahrs dpaqalagap rdvgtkilla
      301 hqprsaaaan ragftvqlsg hthggqflpw ppfvrlqqpv vgglnrfgdm wlytsrgtgy
      361 wgppnrfgvp seitlirltr g
//
LOCUS       WP_175807752             571 aa            linear   BCT 11-JAN-2025
DEFINITION  terminase large subunit [Burkholderia cenocepacia].
ACCESSION   WP_175807752
VERSION     WP_175807752.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..571
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64442
     Region          5..566
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 maresfplva ranqfardvv rgkvlacrwv klacqrhldd laasrsasfk ykfdsskaek
       61 klrliqllph tkgewaykrq lvslepwqlf glactfgwvk kktgfrrfre sywevprkng
      121 ksviaagvgi amftaddefg aevycgatte rqawevfrpa rlmvsrspml iehlgievna
      181 qalnrpedgs rfepiignpg dgaspscaik deyheddtnv qyetmltgmg arrqplmfii
      241 ttsgsniegp cydkrrqvie mlegtvpdde lfgwiwtidd gddwtdprvl akanpnigis
      301 vyqeylesqq qrainsarft ntfktkhlnv wtsakagyfn leawkacedr slmldqfegq
      361 dsvlaldmar kldlnsmarl fwrdidgrrh yfsvaprfwv pedtvrntdn rrmaeryqaw
      421 vnqgylletd gaeidyrdil eeakdanrlc pvqctpldph gatnlshqld degltpvtvv
      481 qnytnmsdpm keleaaisag rfhhdgnpim twcvsnvigk nlpgnddvvr pikqgndnki
      541 dgavalimai gramladrvd sgsiydqgvg v
//
LOCUS       WP_175807792             128 aa            linear   BCT 11-JAN-2025
DEFINITION  GtrA family protein [Burkholderia cenocepacia].
ACCESSION   WP_175807792
VERSION     WP_175807792.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..128
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=13642
     Region          12..128
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mirtfhaaer vrlirfgvsg vgstalhali aaamfalfda tpvianataf vcstafsyla
       61 ntlwsfsspv twgnfvrfla vamaglavtm llahgtdalg larawsivav vlcvppvtfv
      121 lhrlwtyr
//
LOCUS       WP_175807881             360 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia cenocepacia].
ACCESSION   WP_175807881
VERSION     WP_175807881.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..360
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38375
     Region          3..340
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,225,294,314,316..318)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,173,176,178,225,232,294,314,
                     316..317)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,173,176,178,317)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            178
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mptlfdplrl gaidvpnril mapmtrargt rehvptamma dyysqrasag liiseaigis
       61 rqglgwpyat glwttaqiag wrtvtdavhe aggriiaqlw hmgrvvhpsf lddappvsss
      121 ettapghaht ysgkqpytqa raletneipa iieqfaaaar halqagfdgv qlhasngyli
      181 dqflrdsanf rgdayggsis nrlrllieat ravadvagpg rtsvrlspng etqgvrdsdp
      241 lplfiaaaea lsavgigfle lrepplngsf gvgyldplaa kirpafkgpl vlnsdfdaar
      301 aqaeldagva davtfgrpfi snpdfprrla eaiplasddp atwftqdaqg yidypfaast
//
LOCUS       WP_175807888             297 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175807888
VERSION     WP_175807888.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32978
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..287
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,216..221,
                     227..228,230..231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176166"
ORIGIN      
        1 mdrlrametf vavveggnft eaarrleisa vmvgkyvrel eerlaarlle rttrrqsltd
       61 agrvfyddak ralehmriae tsverlrasp sgtlrisapi tfgacviapl aatfrqrypl
      121 vrvelelsnr nvdlidegfd lairigelgd adlvarpltr yrmvicaspg ylaqygrpet
      181 pqdlsahhcl fhtvwssrng wklgdddsth fsaesgftcn dgnglrmaai agaglllqpe
      241 vlvshdlasg alvqvlqgye pkphpvhivy rhdqrplpkl trfvahlleh vtereas
//
LOCUS       WP_175807908             220 aa            linear   BCT 11-JAN-2025
DEFINITION  O-methyltransferase [Burkholderia cenocepacia].
ACCESSION   WP_175807908
VERSION     WP_175807908.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..220
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23588
     Region          64..220
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mttlmldpla sllarlfdea daspatspaf anvsrdeqar lmrsktdyad lyarlkdypl
       61 pvsretgmll ymlargggak aivefgtsfg istlhlaaal rdngggrlit sefepskvvr
      121 aqanlaaagl adlveiregd alrtlahdlp davdlllldg akalypeila rveprlraga
      181 fvvadnaeys pdylayvrap engylsvpfg gdvelsmrtr
//
LOCUS       WP_175807916             709 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia cenocepacia].
ACCESSION   WP_175807916
VERSION     WP_175807916.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..709
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=76425
     Region          40..642
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mtdptanpsp ppappstppr rrriwrtlag allgltlaca gigawtidri wtqlpsvehl
       61 avyrpalplr ifsrdgdlla eygverrefv pleripplmr hallaaedak fyehgpvdig
      121 glaratfanv vtgqpgqggs titmqvarnf yltrdkvlsr klaeilmaak lerayskdkl
      181 lelymneiyl geraygfaaa ahvyfgkpld alsageaavl aglpkapsaf npvvnparat
      241 arrnyvlgrm halgqlddat yraavdapia lattpppgiv aapyvaerar rmmverfhdd
      301 aytlgldvtt tismrdqraa eaaldrtlsr qsrakrdmrn glegalvsld aatgdmlalv
      361 ggadfdrnvf dhalqayrqp gssfkpfvys aalekgyfpg vlvddtqrtl thaetgarpw
      421 rprnfgnrye gfipvrrglv rsknlvavsl mqatdaryvq qhavhfgfda qrnpaslpla
      481 lgagavtple lasaysvfan ggtrmeprli lsvkqrhgga myeatvpage rvvsarnafv
      541 mdsmlrdvvr agtargalal rrddaagktg tsngskdvwf agyssgivav awlgydtprp
      601 mgratgatla lpvwldymkt avdgrtpvaa tppqdvalvd gdfvyaeytr gtctadvpay
      661 irsrfacgga aagdapdapg dngkrdepmp aavdaaerer vldlfrtdd
//
LOCUS       WP_175807947             265 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: enoyl-CoA hydratase/isomerase family protein
            [Burkholderia cepacia complex].
ACCESSION   WP_175807947
VERSION     WP_175807947.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..265
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28422
     Region          17..259
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mttprfsspa dddapsilrd dadgiawlti hrphvanals adairrlcde lvtlddnpsi
       61 rvivirgage rafsagvdlg dpeirgmqpm rglarnvhel ilelrkptia aingyaiggg
      121 ceialacdlr iaadhatfal pearvgmgan fasvllprml phaiamellf tgrrfdtdea
      181 qragllnrvv pgaalddtvr elaqtiaana pltirriket atrsqglpva aalrldvgpd
      241 vyasedrieg araflekrkp vfkgr
//
LOCUS       WP_175807926             195 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            cenocepacia].
ACCESSION   WP_175807926
VERSION     WP_175807926.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..195
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20252
     Region          5..157
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgvsrqqaae nrhaivaaae rlfrvrgvda vgltelmkea gftqggfynh fkskdalvae
       61 vmdkamqdra dspnagsvak qvtaylsgah rdnveggcpl sgfagdaprl tdaaracyth
      121 gvaaylerle rmvategsva tdarddaiav lsqmvgalvl sravagtdpa ladeildaar
      181 rtlvgqpddp aavpa
//
LOCUS       WP_175807950             384 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175807950
VERSION     WP_175807950.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..384
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41840
     Region          1..384
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnfelelehr mirdlvarfv kdelipleaa vmareadgqc fglladerah ldersrqlgl
       61 wgldapldag gsdlpavamv gvneaigttv tpyilppdsp nlrmlcdaad aaqraryldp
      121 yargatraam aisepgagsd pgalsttavr dgdgwvlngr kiwishaaea dwtivmaltd
      181 rskgkrggms afiverdtpg fvierripmi gglstyeivl edcripgtql lgregagfap
      241 mqarlanrrl emaawcigra eravallcdh akqrttfgvp laerqavqww vadaltqiha
      301 crlmtyeaaa rvdagqdart qismvkvfat emastvidha mqtlgamgmt kemplqqmas
      361 earlmrifeg ptevhrwvva rsvl
//
LOCUS       WP_175807956             532 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Burkholderia cenocepacia].
ACCESSION   WP_175807956
VERSION     WP_175807956.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 532)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..532
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=55767
     Region          45..151
                     /region_name="SoxW"
                     /note="Thioredoxin-related protein SoxW [Posttranslational
                     modification, protein turnover, chaperones]; COG2143"
                     /db_xref="CDD:441746"
ORIGIN      
        1 mktvlrnlta aclfvaagaa laaatpagat vasaspdgah lppgiawqhg dvdaafalak
       61 regkplllyw gavwcpscnq vkstifsqqa fktrssffvp vyldgdtesa qklgerfkvh
      121 gyptmilfrp dgtevtrlpg eadldrymqa lslgmtaahp vrqtlatalk ngasltpdew
      181 rlladyswdt dgalpvpadr vaetlqslaq raraagakae sarfalksav vaasddptqa
      241 galdkaalad slrtvlhdaa lsradsdvlv aaparvvayl gggddaqrtk lrgaydtala
      301 rlstdttlss idrlmalhgr vllargdark gaplaapala dtarkqiaas vqgaanayer
      361 qalvsegadt ltdaglydes dallkaelpr sstpyyfmsg laanakargd kvaaldwyrk
      421 aydaasgpat klrwgatyfa navelapdds ariegiaasv laqadktrda fyganlralt
      481 kvvtqlnrwr gsgahdasvr svvkqfdgvc gklpagdpqa aactkliqpv ka
//
LOCUS       WP_175807978             285 aa            linear   BCT 11-JAN-2025
DEFINITION  ion transporter [Burkholderia cenocepacia].
ACCESSION   WP_175807978
VERSION     WP_175807978.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11997982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..285
                     /product="ion transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0034702 - monoatomic ion channel complex
                     [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30842
     Region          29..231
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
ORIGIN      
        1 misliqpsla tardavihva rrpsflrkld iavlvlivas vlvvmadsvq elhaqyghtl
       61 yaaewaftll fsaeyllrlc takkpaayar sffgivdlvs vlptylafff pglhalidvr
      121 llrvfrilgl siyleegqml iraltrarrk ifvfiggmfv lvvilgtvif lvegpehgit
      181 sipvgvywaa vtmsttgygd ltpvtplgrl itscaillgy giiafptgim gaelvasame
      241 rnranarpad gdrpccphcs vtlpvqrapd thahgsvpak grdar
//
LOCUS       WP_175807995             162 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia
            cenocepacia].
ACCESSION   WP_175807995
VERSION     WP_175807995.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 162)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..162
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18043
     Region          8..148
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mskncasvel dgvdramlrl lqedgalsna tlgeklslsv tpcwrrrkrl edervitgyq
       61 anldrralgm nvfafvqvtf nmhsdqdsdh fedvmrrhde vtschkitga adyilqvvaa
      121 dldayaefve rvlrkqagvs siqsslalre vkfssrvpvp da
//
LOCUS       WP_175808003             317 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175808003
VERSION     WP_175808003.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..317
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34471
     Region          11..70
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          100..296
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(114..115,117..118,121,125,127..133,225..230,
                     236..237,239..240)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176111"
ORIGIN      
        1 mysligktat frqlkaldmi arlgsvsraa eelnltqpav slqvrlleea vgaallqrvg
       61 rgvqltaage ivaryareil hlwseagdev aaltgdlggt lrigaittae ylippllvkf
      121 tatrphvkty fkvgnrddii rmlatheidl avmgsapkel rthavefakh pmvfvaapgh
      181 plmqrkrval kdlesahllv rergagtrst veslfknagh rfhvgselss neaikqmaea
      241 glgvaflslh acalelrtgl lgqlpfpgnp ierewyvvtl adrrisqvtg lfrdflikqg
      301 apvidgatva plerrrk
//
LOCUS       WP_175808017             423 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175808017
VERSION     WP_175808017.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..423
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45325
     Region          14..400
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(22..23,26..27,30,62,112..113,115..117,120,140,
                     143..144,147,225,228..229,232..234,237,265,269,327..328,
                     332,336,351,354..355,358..359,362)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mpndhrqrrh tlwllcalsf ilyvdrvnla ttagaikael glsntelgva fsafaysyai
       61 cqigggwiad rfgaritlig cgliwvvatf ttglvhsltl lfaarlllgi gegatlpaqa
      121 ravthwfpre rrgvvqgfth sfsrlgnavt ppivaalmtw lswraaffvi gavtlvwlaw
      181 wivgfrehpa gdddgrpraa rpvapsgptp wgplfrrmap tifvyfcygw tawlfftwlp
      241 tfflngqgln lkstalfasg vffagvvgdt lggwlcdriy rktgnlalsr qsvivtsfvg
      301 alvcllplaf vhstagvalc lsgsflclel tigpiwavps diapthagia sgmmnagsai
      361 sgilspilfg ylvdrtgswt vpfvgsvaml ligivaalri rpdrslsesm palvdapaap
      421 svr
//
LOCUS       WP_175808083             465 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175808083
VERSION     WP_175808083.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..465
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46878
     Region          27..462
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,153,
                     156..157,160,283,286..287,290..292,295,323,327,378..379,
                     383,387,403,406..407,410..411,414)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mnggraapaa gayasaaarp vlvmvalacg fvmamldvti vnvalkamet slsmsltalv
       61 wvvdaytlsf aallllggal anrygskavy vaglalfvga svlcaaaqss galvaarlaq
      121 gvgaalfmps slslltlafp pgptrtrmig iwgalvsaam algpcvggvl vdaigwrgif
      181 wvnlpvgaag lwltyrhiar aprhpgplna lghlfgalal aalsftlieg psagwrspai
      241 lagvattlaa taafalrery atsrilsptl lanrrfvags mlglainfgi laeifllsly
      301 lqnvrgasal vagfelfplm amfgignlas akvsarlgar rtlltglala algsvalvgv
      361 aampypvlal avglanfgag qaipamnlvv mqsadaadan laaaslnasr qigslvgiai
      421 asvilhvvdd pdratavgfa viaalyalgf aivfraihav aaeqp
//
LOCUS       WP_175808087             332 aa            linear   BCT 11-JAN-2025
DEFINITION  transketolase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175808087
VERSION     WP_175808087.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..332
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35411
     Region          21..331
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mstadnkprl ktsamiasia aegqatrsap fghaltelar tnanvigmta dlgkytdlhi
       61 fakafperyy qmgmaeqllm gaaagfaheg aqpfvttyav fatrraydfi hqaiaednld
      121 vklicalpgl ttgygpshqa aedlalmram pnmtvidpcd aldieqmvpa iaehkgpvya
      181 rllrgnvpav ldeydyrfel gkakllrdgn dvllissgim tmralevaka leadrvdvav
      241 lhvptikpld tatlvreaar kgrmvvvaen htvigglgea vatallgagv tvpfrqialp
      301 daylaagalp tlherygisa gamranirsw lg
//
LOCUS       WP_175808088             441 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175808088
VERSION     WP_175808088.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47363
     Region          33..435
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(46..47,50..51,54,86,136..137,139..141,144,164,
                     167..168,171,267,270..271,274..276,279,307,311,361..362,
                     366,370,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mrakypappv egemlqrdda rtfeaatyak varrlipflm lcylgayldr vnvgfaklqm
       61 lgdlrfsetv ygmgagiffl gyflfevpsn lilhrvgarr wlarimltwa visagfvfvk
      121 sptafyvlrf llgvaeagfa pgvilyltyw fpsarrakal slffmaipla giiggplsga
      181 imhslhgams magwkwlfll ealpsfvlgf aillylddgi agatwltdae kallarnvsa
      241 daahttahls irtfvadrrl wlmaaiyfcv vlgqygltfw lptiirkagv adplwvglft
      301 aipyacaiva lpligisadr rrerrfhlav pmlvaaagfa tlpmlgsvga sivclsiasa
      361 gilasssqfw slptallggm saaagiaavn cfanlagffs paivgwlndl tgkstaglvf
      421 isvaitagal lvflvprsvn r
//
LOCUS       WP_175808103             701 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cenocepacia].
ACCESSION   WP_175808103
VERSION     WP_175808103.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..701
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76051
     Region          22..701
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 msrrnwaaap maivvgttgm gaadaqetal ptievsaqra tapfrtrest satrseadvm
       61 eipfavssvd tkliqtvaat rgddlydwva gvsrqnnfgg lwdnyavrgf agdgntsgtd
      121 ylvngfswnr gmsvprdtvn lermevlkgp asalygrgdp ggiisyttkq pqfarantig
      181 vsagsygalr qtldstgpit kslayrfvam nenngsfrdt vsskrylfsp sftwdigadt
      241 tlhyefesar qrapldrgvl avngqlgaip asrflgeprd gdydvrntgh qftlehrids
      301 swsinagvaq rttdlsgrss eafalqpdgr tlwrryrqva fhsndlqgrl etagafrtgg
      361 ightlvmgvd ayrfnydqfv trstpsasap yaidifdpvy gqpaptprta tnllerddgq
      421 gvyaqdtlaf gphwkilagl rwdrfhqsid nrlkgvttsq lqtalsprig vvyemspaws
      481 lyantaysfr pnngadingr afdpekghgy eagakwagar wlttvsafyv tkrnvltadp
      541 anagfsraag evrsrgiefe wsgdlghglr gianlayvda evtrdsvlap gsrlvdvprl
      601 sgsallmyet alpfadkaga gagviyvgrr agntantqdg felpayatvq lngylqvnkh
      661 lrasvvlnnl fnrttyvnsy nslwvtpgap rslfaslays f
//
LOCUS       WP_175808122             475 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175808122
VERSION     WP_175808122.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..475
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50757
     Region          40..459
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(50..51,54..55,58,90,140..141,143..145,148,171,
                     174..175,178,287,290..291,294..296,299,328,332,388..389,
                     393,397,413,416..417,420..421,424)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mssidlgsvt pvsspirsas dvarlintvd ssvsharmiv llalggvfld aydlttlsyg
       61 iddvarefgl tpaltglvgs aimigtifgs liggwltdri gryqvfmadm lffvvaaiaa
      121 glapnvwvli garfvmglgv gidlpvamaf laefskfngr gnkasrlaaw cpmwyvassv
      181 cfllifglyf llpaehagwl wraslifgav palviilfrn rfmnesplwa anqgdlanaa
      241 rilresygih aheaddarre pspppvrirv lfqrpylgrt ivasvmnlci pfeytaiaff
      301 lpsilsqflg agvfetiaas lalnvlfaft ggllgmrlay rypsrhvaia gfalqtvalv
      361 alalaghphg alavgvvllm lgtwlfaegf gpgaqmmiyp tlsypatirg tgvgfgrslc
      421 gigqalalfv lpilqarlgt dmfwvvaisa vtpivfllii ryeptandvd desaa
//
LOCUS       WP_175808190             204 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Burkholderia cepacia
            complex].
ACCESSION   WP_175808190
VERSION     WP_175808190.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..204
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20984
     Region          19..204
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mspvantllp lagvlllsva spgpnfvivt stavlsrrag vmtglglaaa sgtwaaiaia
       61 glsllvthva wvhtalrlag aayliwlgvk mivtarqplp vsapaalsdw raarngyvvs
      121 mtnpksvafy gsifalmvpa hapawldlsv vvlsiaisaa wyctmallas hpsvrrllvr
      181 rkavldtaag lllmgvggrm lagr
//
LOCUS       WP_175808223             240 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD family hydrolase [Burkholderia cenocepacia].
ACCESSION   WP_175808223
VERSION     WP_175808223.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..240
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26156
     Region          6..233
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mrlakvsals fdlddtlwpf gpsvvraeat lrtwliehap ntasvlptqq alsalreeye
       61 rlcpdlasdy ramrigsirl aleranedvs ltesaydvfy aarnrvefye dalpalawls
      121 arfpliavtn gnadlrltgg geffrttlsa rafgfakpep eifhaaadal gvrpaellhv
      181 gddfhldivg alnaglqaaw vvrepreegg qappraetph lmlrdlamlc ralggpdtvs
//
LOCUS       WP_175808227             304 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia cenocepacia].
ACCESSION   WP_175808227
VERSION     WP_175808227.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..304
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32048
     Region          5..298
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhsrhevivi ggsfaglsaa mqlararrrv lvidagrprn rfaehahgff gqdgkppari
       61 vaeaaaqlaa yptvqriege artaerdahg rfhvtladgs rasadrlila tgirdelpal
      121 pglaerwgvt vlhcpychgy evsgqrlgvl athplsvhqa ilipdwgptt wftqgvvean
      181 eeeaallaar gvriehspvv eilgdaprid alrladgqvv pidalfigar tdmasdlarq
      241 lgcafdegpl gtairvdtwk qtsvagvyaa gdasslmtna tfasasgvaa gvgvhrslif
      301 glda
//
LOCUS       WP_175808254             374 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Burkholderia cenocepacia].
ACCESSION   WP_175808254
VERSION     WP_175808254.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..374
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37413
     Region          17..364
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mtgfidtftl ggpgptiaik dtidiaghpt raasralada ppaehhadvv rllldagwqi
       61 agkanmhela fgmtgindyt gtpvnpqdaa ripggsssgs aslvglgavd aalgtdtggs
      121 irgpaaccgv aglkptfgrv srrgvapaet tldcvgpfar eihtlvavma aialgfdrar
      181 aaasaagcav aqltveadpa iaaaldaavr asglrshdvv lddmpaafaa glsvinaets
      241 rafghlvatg rlgadldarl rmaatttpaa laeaeavrar ftaqvdaale hadvlvlptl
      301 palpitlqqa rdgvsviams slirpfnlsg hpalslplpl agsplkaglq vvgrkgadeq
      361 vcaiaahfea alaa
//
LOCUS       WP_175808259             167 aa            linear   BCT 11-JAN-2025
DEFINITION  aromatic-ring-hydroxylating dioxygenase subunit beta [Burkholderia
            cenocepacia].
ACCESSION   WP_175808259
VERSION     WP_175808259.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10791045
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..167
                     /product="aromatic-ring-hydroxylating dioxygenase subunit
                     beta"
                     /EC_number="1.14.-.-"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0009056 - catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=18705
     Region          7..167
                     /region_name="HcaF"
                     /note="3-phenylpropionate/cinnamic acid dioxygenase, small
                     subunit [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG5517"
                     /db_xref="CDD:444268"
ORIGIN      
        1 mmddrnalfs eqtfaravef vwreaemldr rdyrawldlw dpaghyvvpi dpdttdfaat
       61 lnyvfddhdm rekrvqrmvs gysasatdaa rtvrtvsrft lessgadtve lksaqvvvay
      121 krgvatlfaa dvthklhvda dgeiriaekv vrlidsteal saigfll
//
LOCUS       WP_175808264             372 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: porin [Burkholderia].
ACCESSION   WP_175808264
VERSION     WP_175808264.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..372
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=38289
     Region          21..372
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mnqpngralr lavplaalla cmaqpaaaqs svtlygridt aieyanagpn hvtrmgsgnl
       61 wasqwglkgv edlgggyati fkledgfnaa sgalsnssal fgreawvgit gpfggvqfge
      121 lytilhttlv tyslpglgag lawgnatnnf vgpaflrvrn smrytsprya gfllramaar
      181 gangaagqpa tlgdtygagi nyvrgglsvd vdymqqkfsp vaasalgats taangnytlg
      241 aisydfnvvk vaalylrhrg gpdvataids qsayphsdim elsatvpigr aslllsvghy
      301 rkvadsdgna dsygirfdyp lskrtvlytg aamvrngaha rfvvngaagg gvavakpgat
      361 asslvagilt sf
//
LOCUS       WP_175808269             446 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175808269
VERSION     WP_175808269.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..446
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47322
     Region          23..427
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(36..37,40..41,44,84,142..143,145..147,150,170,
                     173..174,177,259,262..263,266..268,271,298,302,355..356,
                     360,364,380,383..384,387..388,391)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 myptdtvqsp saaaapladr qlrriviasv agnamewydf fvygtaaalv fghvffppga
       61 splagslaaf aafalgfvar plggivfghv gdrygrkasl vwtllimgas tfaigllpty
      121 aqiglwapaa lvvlrllqgi asggewgggv lmisenappe qrgyyaawsq lgvgggfvls
      181 saaflaaqal pddafrtwgw rlpflasvai faigiyirrh lpesrdfeqa gkrgahthlp
      241 ivecirrhpk eillamglrv aenggayifl afslvygkyv gipngtmltg vmiamivemg
      301 amlawgrlsd rigrkpvyli galslvacaf pffwlldtrv tplvwlalti gtavshgami
      361 gtlpalvgel fstevrysgv alghevasif aggmspliat allaryhasw pvslflialg
      421 lvtvatlcvm retritpadg srrdpa
//
LOCUS       WP_175808308             327 aa            linear   BCT 11-JAN-2025
DEFINITION  thiamine pyrophosphate-dependent dehydrogenase E1 component subunit
            alpha [Burkholderia cenocepacia].
ACCESSION   WP_175808308
VERSION     WP_175808308.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..327
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=34635
     Region          6..327
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 mtastqlsrd tlldayrlmr tirefeerlh vefatgeipg fvhlyageea savgtilhlg
       61 lddyvatthr ghghciakgv dvhgmmaeiy gkktgvcrgk ggsmhiadls mgmlgangiv
      121 gaggplvcga alaakhkktg gvgvcffgdg asnqgvifes mnlasvwrlp aifvaenngy
      181 aeatssswsv atdniadran gfgmpgvivd gfdffavhea lgeaverarn gggptlvevk
      241 ftryfghfeg daqtyrapge vqklrdekdc lkhfetrvvr aealttddlr avdaqvkali
      301 ddavaqakaa plpdaadlla dvyvsyp
//
LOCUS       WP_175808301             749 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Burkholderia cenocepacia].
ACCESSION   WP_175808301
VERSION     WP_175808301.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..749
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=81364
     Region          43..744
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mnspleatpd arrdttsagr vrapegtfel srkrvdeldt ifgeggllar aldgyrprts
       61 qiemaravas ameasarrmp epeifetrkr parrlgdpdk tagpaaddaa aaesdsdagd
      121 ntliveagtg tgktyaylvp amlwggkviv stgtkhlqdq lfqrdiptvr nalavpvsva
      181 mlkgranylc hyylqrtadn grlpsrqdta ylqeivrfak itksgdkael asvpenapvw
      241 smvtstrdnc lgqecphyke cfvmqarrea qqadivvvnh hlffadimlr dtgmaellpn
      301 antiifdeah qlpetatlff getlsttqil elardtvaeg lshardavew vklggdlera
      361 ardlrlafad gqivrmslaq lgddhpmfga ldaldvalda lasalasqae raeslgaclr
      421 rarelqdlla gwvapgaaea aaqadaaaag dnaasdsdpn ekvrwvevfa htvqlhetpl
      481 svapifakqr agvprawvft satlsvrgdf thyaaqmgls srrsmtlasp fdyqsqglly
      541 vprnlpqpss paftdavfda alpaieasgg gvfmlcttlr avdriasklr dviesrgwnt
      601 pllvqgdasr telldrfray gnailvgsqs fwegvdvrgd alslvvidkl pfappddpvl
      661 aarldaltkk glspfavhql pqavitlkqg agrliraetd rgvlmicdtr lvdkpygrri
      721 wqslppfkrt reiavvqdff dehrsgkha
//
LOCUS       WP_175808373             535 aa            linear   BCT 11-JAN-2025
DEFINITION  multicopper oxidase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175808373
VERSION     WP_175808373.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..535
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=58080
     Region          88..535
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mrrrtflsra igvaaaslfa rtasaqhagh agmagmdsmd dmpgmsgmsg msahaqhgqr
       61 apaalaaada lpagaplatl rtlanesrep gtfratlvaq pvarpllrga rpttfwqfga
      121 gtqgpvvgpl idvregdtve irfvnklpqp stihwhglpv ppdqdgnpsd pvapgasrvy
      181 rftlpkgsag tywyhphphm mtaeqvfrgl agpfvvraad dplagwperh lfvsdlklar
      241 dgtiapndmm dwmngregqf vlvngarrpr idvasderwr vwnacsaryl riafddgrvf
      301 ehagtdgglf daprrvtsll iapgeraell vragdrasra vlqaaeydrr kmamshddgh
      361 gslppdpala ladvafapae aralpatlra vlplgepvah ktvafgeemd mdammkgaah
      421 grpagmrfti ngdtyaphra tltsrrgdve rweirnttdm dhpfhlhgtq fqviertsag
      481 srtsepfraw rdtvnvrsge tvsllvtqdm pgermfhchi lehedlgmmg tlkvv
//
LOCUS       WP_175808401             357 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [Burkholderia].
ACCESSION   WP_175808401
VERSION     WP_175808401.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..357
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38701
     Region          18..334
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mtpdvpaspl aepaprrirf givllpnftl tafsgfvdml rlsaddgdys kpvrcawsvi
       61 getlapvras cgiqitpwet fdaaepfdyv vvvggllhsg pqagpetldf irraatggat
      121 vvgictgvft lmragvldgy rtcvswfhyw dfierfpsad pdlliadrlf vidrrritcs
      181 ggrasidvaa aillrhfdha tvqkalrill vgemqkgnap qphppglepa thpkvkrail
      241 lmeqhvgral pleelackld lstrqlerlf kaetgkspqa fakqvrlrta awlltssdrt
      301 vadiasscgf adashlgref rkqfgvppat yrerggdvae vaampdasad pvediad
//
LOCUS       WP_175808433             666 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Burkholderia cenocepacia].
ACCESSION   WP_175808433
VERSION     WP_175808433.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..666
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70679
     Region          1..460
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          598..662
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(620,629..631,638)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            630
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mfdkilianr geiacrvaat ckrlgiasva iysdadanak hvaacdeavh iggsaaadsy
       61 lrieriieaa ratgaqaihp gygflsened faqaceaagi vfigppvdai aamgskaaak
      121 almhaaavpl vpgyhgddqd aanlhreadq igypvllkas aggggkgmrv versedfpaa
      181 lascqreaas sfgndrvlie kyltrprhve vqvfgdthgn tvylfdrdcs vqrrhqkvle
      241 eapapglhed vrqamgeaav aaaravgyvg agtvefimtg eafyfmemnt rlqvehpvte
      301 mvtgldlvew qlrvaagepl plkqeelrvq ghalearlya enpargflps tgtlkhlrlp
      361 pgvefdigaa vrvdsgvreg daitpfydpm iaklivhgad raealglmlr alracevvgl
      421 htnaaflqri vacepfaiad ldtgliernh dalfapqqpp ratlalacaa llarergaaa
      481 qenaspwssl pdwrlnggyr rtlewhaidr dadvtvtyed dgagtriaig daaaqpfawt
      541 hgatpldfdv tlggvrssgr vyadgdtfhv ftqgaaetfe wrnllahagd aeqgggrlta
      601 pmpgkviavl vepgqkveag tplivmeamk mehtigapsa gvvaevlygv gdqvadgaql
      661 lmmaeg
//
LOCUS       WP_175808514             314 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175808514
VERSION     WP_175808514.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..314
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=32274
     Region          21..261
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mmqlnvtegv lasslqvltt fdliwivaal vlggmakgit gigvplvamp ivsqfmpird
       61 avlllsmpii lgnipqaleg gqvlatarki aapiagtvfg niagvaills lnsghaqaas
      121 gallivvatl mlaapklnle pawrkpvgfv lgfgaavtes iasvpgplla tylissgasg
      181 raftkqiaii lvvsvvtllt tfsgaaqasg adlvisaaat lpaiagmwlv rplrdqmspe
      241 ifrrvvlllv lvaatqmiwk sgvfrhggss atdacirhai elhhmcmsrs ssppeahtca
      301 hsnsahmcdg ltlt
//
LOCUS       WP_175808527             234 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia cenocepacia].
ACCESSION   WP_175808527
VERSION     WP_175808527.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..234
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24733
     Region          130..231
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(133..134,167..168,171,175..176,179,221,225)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mtskllrvas igafamalga cttqsgltyd iravsvpgkp dnifrvscdg llgsanacar
       61 aaeefcqgkg ftplemidrv ysrapmkdpr eitficgkpq pvvqpapapq pqpapqpvqq
      121 rqvllqgdan fatdsaalts qarndldrfi aanrgmefar vsitgftdst ggaahnrtls
      181 earartvvey lranglqars fvaeglgaad pvasnataag raqnrrveir ldvk
//
LOCUS       WP_175808627             206 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175808627
VERSION     WP_175808627.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23212
     Region          9..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkpqrltreq srdqtrerll kaahriflkk gyvaasvedi aaaagytrga fysnfrsksd
       61 lllellernh eevqadfvai fegggtreqm esmalayyrt lfrddeysll wgeaklqaar
      121 dakfrvrfnq flhgkrvqma efiqrfaers gtplllpadt lafglmclcd gvqsyytadp
      181 qhvsadvaes vlggffarvv lgrapd
//
LOCUS       WP_175808628             231 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Burkholderia cenocepacia].
ACCESSION   WP_175808628
VERSION     WP_175808628.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..231
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24646
     Region          160..230
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mkveehlvas nsglatlgrp refgkkqqnp vrrfggiavv lllhavliya llnglatkvv
       61 qviqhpietr iiepvkpppp ppmpvvklpp pkfapppfvp ppevpvqapp qqatithqsa
      121 pvpsapavqa pvvappapak pvshevgvvc pnsdsmrasm qypkeaqenn itgdvtiefv
      181 vdaegnitne rvaqsadpvl draayntvkr fkcvaqgqav rvqvpfsfnl n
//
LOCUS       WP_175808631             544 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cenocepacia].
ACCESSION   WP_175808631
VERSION     WP_175808631.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 544)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..544
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58868
     Region          1..534
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 manallqidg fsarfgtkaa vqdlslsvgr gervalvges gsgksvtals ilrlaqqatl
       61 sgrilfdged llakterqmr girgadiamv fqepmtalnp lytigkqiae slglheglrp
      121 gdarergial lrrtgipepe rridsfphql sggqrqrami amalacrprl lladepttal
      181 dvtvrqqivd llielqeqea aargmavlli thdlnlvrrf aqrvavmeqg vlvetnttda
      241 lfaaprhayt rrlldsapqr dvepvaagaq tildvqdlav dyrvaakgwr avlgkttfra
      301 vhdvklnlrr getlgivges gsgkstlaat vlglqrpaag sieidgmpld alrttggrra
      361 lygrmqvvfq dpfgslsprm tveqivgegl avhrpqvagp arrarvaall qevglpaeam
      421 lryphefsgg qrqriaiara lavepellvl deptsaldvs iqkqvlnllt nlqkkyelsy
      481 lfithdlavm ramahrvvvm kagrvveegd tldvlhapsh pytrallass mlapvrgtqe
      541 stdd
//
LOCUS       WP_175808648             327 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175808648
VERSION     WP_175808648.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..327
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35374
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,161,163,226,243,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,190,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mnqiqtmrvf vcvaeqqsfr raahhlgvsn alvtrsiaml eghlntrlih rttrnlslte
       61 agvryldgcr alleefdhle ssvahavrep agtlrvvasg llsplaltpl vssfrhrype
      121 lrvqltvseg pldvldsgyd vgivtgtrld gnptlighal apnpfvacaa payldrrgep
      181 rvpddlpghd wvtlaphqha ptwqlvghdg vahsvtvrpa ctvnqlalvq aaavagagia
      241 vlpepcvada lnhgtlvrlm agyriddpdt qlslvypnrq yvpartrsfv ehalehfsap
      301 aareqadygf lrpvrgpers divtglq
//
LOCUS       WP_175808738             246 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cenocepacia].
ACCESSION   WP_175808738
VERSION     WP_175808738.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..246
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26357
     Region          5..239
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
     Region          <66..135
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 miqptpvvfi hgfigtfdvr gwhgphlcpd llgygahraa ppdaislaaq vehvrqtvem
       61 hfgmqpvdvv ghsvggaiam lfahahperv rrvvnvegnf tlddafwsas vgrmtpgead
      121 amldglraap pdwlrgaida pspgqlddar rwlahqpast lramgrsvie ttgdagylpa
      181 laqvfdrhpv wliagersra gwhvpafala rcagfdtiag cghlmaaerp dalratleri
      241 vckpsp
//
LOCUS       WP_175808803             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175808803
VERSION     WP_175808803.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33073
     Region          7..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(105,109,148,162,164,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(106..107,111..112,114..115,118,122,124..130,191,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 maqlpdfegl amfakvaehg sfaaaaratg vsvatvsrgv arleerlgar lfnrtsrqls
       61 ltefgrtise kageiyrqae eaessarems vqprglvrla vpmsfglrwv apllpgffca
      121 ypevsidlhl sdasvdliad gfdaalriaa lpdsslvarr lcavtqfvva spaylrregr
      181 pthprelaer pclpyayrar savwrftnda gdeesvmptg plrvtnadal vptlldglai
      241 aelpefiage yladgrleai lpgwslttgg lyfvtpsara rpakvtalsd yfaehlgnpv
      301 wrwpk
//
LOCUS       WP_175808808             310 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175808808
VERSION     WP_175808808.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33839
     Region          14..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,232,249,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,195,
                     226..230,237..238,241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mrssseklsg sisvfaavvd agtfsaaadv igmtppgvsr aiarlekrln irlfnrttrs
       61 vslteegrrf yeqvmphlag leeaataaag gvsavrgklr inldpvvyra ilgprldafm
      121 dahseleiel iardslgdlv mdgfdlavrf geprasslia rklldtgvvt vaapsyiarr
      181 grpakpedle drhhrclefr npetgkpfaw efhrkrkriv vdtrgrltvn dpgallnacl
      241 agsgiaqmll lgaepliadg rlinlfpewa deryplyayy psrhhvpakt rafldfmvel
      301 tgihggggar
//
LOCUS       WP_175808812             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175808812
VERSION     WP_175808812.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33537
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..288
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176113"
ORIGIN      
        1 mfdltslalf vraaelgsls raaqqshmsl stasrriall ehhfrvvlln rtvagveltp
       61 ageallrhat dlllrtdaiy selsdytkga vgrvrvfani saisqdlpdq lrtfsqryrd
      121 iklqiselrs sdilqalreg radvgivtsr tapegihlap ycmdrasvvv pddypltgds
      181 vdfsalldhd lvalddrsel trslvreaal lgksvrfrvq vqsfeamcrl iaagqgigil
      241 peravalfre pmrlrfirln dpwanrvmsv giragavplp trklfeflas fappslvsge
      301 agqsnd
//
LOCUS       WP_175808857             111 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia
            cenocepacia].
ACCESSION   WP_175808857
VERSION     WP_175808857.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..111
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12114
     Region          8..78
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mrrtlstssi fpkrlrearl rsglsqeqlg ieagidefsa sarvnqyetg khapklqtah
       61 rlaqvlhvpt sflyesndll arllvaaapl pqgslealle yaerlsrtaa s
//
LOCUS       WP_175808878             238 aa            linear   BCT 11-JAN-2025
DEFINITION  outer membrane protein [Burkholderia cenocepacia].
ACCESSION   WP_175808878
VERSION     WP_175808878.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..238
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=25825
     Region          80..238
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mikrfavpst lallfsgaaf adtvavpetk ktaelgdagy yatgrvigaf dnavnmelts
       61 prvtrrvggp etgsnvtgsl glgyqfgngw raegeyvfkr tnnftsywap fdananefhv
      121 saqrlmlngy kdfdlgrgfs vygtlgigva ivsadgwqtn dtrrfasktq tnlaysagag
      181 vsyainkrfs idlgyryvdm gnietgfntf anrvnardek lksklssnev figlrgrf
//
LOCUS       WP_175808910             430 aa            linear   BCT 11-JAN-2025
DEFINITION  NRAMP family divalent metal transporter [Burkholderia cenocepacia].
ACCESSION   WP_175808910
VERSION     WP_175808910.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..430
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46034
     Region          20..424
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 mndndflqpe paepapngvt wvrrlgpgli tgaadddpsg igtysqagaq fgfellwsll
       61 ltyplmtaiq lvsarigrvt gkglasnmrk hyppwllygt vvllitanvi niaadlsamg
      121 aavnlllpgp qqlyivclgg vsvalqvfvp ydrysrllkw taltllayva valivpvswa
      181 evgraivqph aqlsaayltt lvavlgttis pylffwqasq eveelravpd arplrrmprq
      241 aptqlrrisf dtwfgmgvsn viaffivlta aatlnahhid vktsadaara leplaghfay
      301 vlfalgivgt gllalpvlag saayaaagtf rwrnnlalqw gvapefyavi vlaivggiaf
      361 tfmhfdpira lywsavingv savpimvvmm lmarsrrvmg efavrgalaw ggwiatlama
      421 iaamgvfvpg
//
LOCUS       WP_175808912             448 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175808912
VERSION     WP_175808912.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..448
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48331
     Region          27..437
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(40..41,44..45,48,80,139..140,142..144,147,167,
                     170..171,174,268,271..272,275..277,280,308,312,363..364,
                     368,372,388,391..392,395..396,399)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mpsltqaaaa paaadsseda lyrkvmrril pllllcyvva yldrvnvgfa klqmlddlsl
       61 sdgvyalgas iffwgyflfe mpsnlllhry garfwiarim itwgivsssm afivplaqff
      121 hvqtttmfyt lrfllglcea gffpgvilym nywfparrqs vamsgflvai plsltlgsvl
      181 sgwlmeqthg lsgmsgwqwm llleglpsiv vafivlaclg dgppsakwls adekavlsrn
      241 leaeaahksh sigaalrspr vwlltfillt fntgfyglaf wlpsiirasg vqsplhigvl
      301 taipyltaif amvwnashsr rtgerrlhaa ipaliggvfl ilsaafahnv alsivfltia
      361 tcgilalmpi ywtfpgqils gtaaaagial insvgnlsgf tgsmitgvak qmtgninngt
      421 yalgacllvs cvliaaiprd ilqppvgr
//
LOCUS       WP_175808950             138 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein, partial [Burkholderia
            cepacia].
ACCESSION   WP_175808950
VERSION     WP_175808950.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         <1..>138
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
     Region          2..>138
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 eilrvdhvcr gfnktqgell vlddanlslr egeivgllgr sgsgkstllr iiaglieptg
       61 gevtylgkpl rgpaegvamv fqtfalfpwl tvlqnveagl ealgvgarer reralaaidl
      121 igldgfenay prelsggm
//
LOCUS       WP_175808989             263 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Burkholderia
            cepacia complex].
ACCESSION   WP_175808989
VERSION     WP_175808989.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..263
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27986
     Region          13..261
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mtlstiddtt iderkfvval argldllraf rpgetmlgnr dfaertglpk atvnrlaytl
       61 tvlgylryde tlgkyaldag vlslgyalls gsgtidlarp hmqalaraig aavslgcrdg
      121 ldmiyletir setaltlgla pgsrlsmlts smgraylavq pedvrralya elhraaggaa
      181 dadalvaaaq qavaefsagg ccysfrawha dvnaaavpfr epregrwlil scsgpassmd
      241 edvfrtqvgp qlkalaqrlg qtv
//
LOCUS       WP_175808990             136 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GFA family protein [Burkholderia cepacia complex].
ACCESSION   WP_175808990
VERSION     WP_175808990.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..136
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14960
     Region          5..131
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mahpepmegg cacgairyri agvptdagfc hcrlcqrttg aavvasasvp idafeylrge
       61 ptvyassawg errfcgrcga qleyrrsdap rtveinyatl depsrlrpaw hvwygdrflg
      121 ieidddlpky ddggre
//
LOCUS       WP_175808994             121 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: BON domain-containing protein [Burkholderia].
ACCESSION   WP_175808994
VERSION     WP_175808994.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..121
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=11962
     Region          59..>120
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mksivlralg vavvaaclsg svyaqssdaa ateapaaass apkaaaktak kanrklgyav
       61 rkaitkaggi dvanivvrsk ggaislegtv pdqaqidkae eaaksvkgvt svtnkltvqq
      121 q
//
LOCUS       WP_175809032             251 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Burkholderia].
ACCESSION   WP_175809032
VERSION     WP_175809032.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..251
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26039
     Region          1..251
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlttqrkkai ldalardgqv laaelsvqfg vsedtvrrdl relaaegllq rvhggalpas
       61 paiapfaqre alettekrri arraaqmiap gqvaivdggt tsallvgqlp adlrativth
      121 spsvavalaa hpsidvilig grlykhsiva vgaaamegia rihadlyfmg vtgvhpvagl
      181 stgdfeeaai kralaeraae tvvlasqskl raasqfvigd ltlaqtivve ketdaaltkp
      241 ieaagvtvvr a
//
LOCUS       WP_175809084             145 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SET domain-containing protein [Burkholderia cepacia
            complex].
ACCESSION   WP_175809084
VERSION     WP_175809084.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Qian,C. and Zhou,M.M.
  TITLE     SET domain protein lysine methyltransferases: Structure,
            specificity and catalysis
  JOURNAL   Cell Mol Life Sci 63 (23), 2755-2763 (2006)
   PUBMED   17013555
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Dillon,S.C., Zhang,X., Trievel,R.C. and Cheng,X.
  TITLE     The SET-domain protein superfamily: protein lysine
            methyltransferases
  JOURNAL   Genome Biol 6 (8), 227 (2005)
   PUBMED   16086857
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Yeates,T.O.
  TITLE     Structures of SET domain proteins: protein lysine
            methyltransferases make their mark
  JOURNAL   Cell 111 (1), 5-7 (2002)
   PUBMED   12372294
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459262
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..145
                     /product="SET domain-containing protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16087
     Region          9..140
                     /region_name="SET"
                     /note="SET domain-containing protein (function unknown)
                     [General function prediction only]; COG2940"
                     /db_xref="CDD:442183"
ORIGIN      
        1 mrrvvvrrst vhgrgvfatk plragerife ykgevttwrs avqryerrsd eahtflfgls
       61 ngrvidggrg gnsarwlnha cvpncetiev dgrvfvdavr dirtgeelli dyaleidadt
      121 ddddraayhc rcgvpacrgt mlggt
//
LOCUS       WP_175809103             895 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175809103
VERSION     WP_175809103.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 895)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 895)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..895
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..895
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=97952
     Region          15..827
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnsqalrsal lagpvqherl ikldtplgpd vllpqrvtgr srlgrhfeft vdtvsvsddl
       61 elkkliaqpv tlwiqqadqs yaphhgyvha arrlgsdsgv thhqivfasf lhflkfrrdq
      121 riwqdrsadd iiadvlnqhp qakgrftfkl yqplpprsfc mqyeddwnfv hrlmesegly
      181 gfweqdsdgk shrlvivdri dalpalsprt vrfhhagtgd eadtlvqfsg trtlrsvart
      241 trtfdykqpp tasnpkatht ptianqgdlp qqlevyeytg aytypeqsrg dhlskiwmee
      301 qeshakrfhg vggvrrmdag rvfefaehpe hdkddagqre favietawvi vnnlpvadep
      361 avfphslqae igsimqatdt drsrvrhpdg segffqirie aqrttvpfrs pfehakpsmh
      421 lqsatvvapq geevhtdeln rvkvrfhwdr lndgdekasc wlratasdsg ngygavhphr
      481 sgeevlvdfl ggdcdrpiiv gkvyngatsp qwhsngilsg yrskeyagag ynqlvlddat
      541 aqnrvhlyss qtnahlhlgy lidhtgnnrg sylgsgfdlr sdaygavran rglyvtthpk
      601 qaasqpldvd etreqlvraq glidamsqvs aqhqgesldp ghtalkqfsd atqnsvsgna
      661 sggrtagggt gnanafkepv mlfgspagig mstqqsaqfs adqhinlvsg qsthvaagks
      721 liasvldris lfaqnagmkl fagkgkvevq aqadnielta qkalkliavt qsiegaaake
      781 illtsggayi riadgnievh apgkidikga qhafsgpthl sqtmptlpns ngnydqafia
      841 hwagtdipva ntryqmfsng kllsegvtna agetgltqsh vphdvvvkfl gksng
//
LOCUS       WP_175809141             271 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: endonuclease/exonuclease/phosphatase family protein
            [Burkholderia cepacia complex].
ACCESSION   WP_175809141
VERSION     WP_175809141.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..271
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29926
     Region          13..268
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 msadalslpf aephaapdei tavswnlhkg rsplgftawn amrdwmqsth advyflqeam
       61 arrmprpmla pgfgapmddt vddvwhcqat eiaqaldwqi algpnvfkps wrhgnailsp
      121 hpldlggrwd isahrferrg llvaratlag arpvtllcah laltraarlr qmhwiahwiv
      181 rnagdgplml agdfndwrnd svalfgeigl sevatllges grtfpafspa laldkmfvrg
      241 ltplewhaps geaawlsdhl pyiarlrldp q
//
LOCUS       WP_175809139             404 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Wolbachia endosymbiont of Dipetalonema
            caudispina].
ACCESSION   WP_175809139
VERSION     WP_175809139.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dipetalonema caudispina
  ORGANISM  Wolbachia endosymbiont of Dipetalonema caudispina
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Wolbachia endosymbiont of Dipetalonema
                     caudispina"
                     /db_xref="taxon:1812112"
     Protein         1..404
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44429
     Region          7..403
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mlqkeilvwv lvslfyayqy ilrvipniia pglisrfnis itdigqfsgl yyvgytlahi
       61 pvglildrsg lklilpicti ltfigtlplv cfdewyfsil griivgvgss asaigifkva
      121 smyfsreksa kmaslsivig llgavygglp ldfllnkfgw nyviyffsaf gcllafllfv
      181 tipsngalkd ansnnilqdl kavicnkyii lisffgglmi gplegfadgw akaflcevye
      241 mkgdlassls sfvfvgfgig tlflafllek ypdkhyeivi tcslamivsf lllftqassl
      301 yvvlpalfvi gfasgyqvit iykaisyvtt dlvglatafs nmiimvfgyf fhvliakivs
      361 fywtgttieg npiygsglli kamsiipvcl lfavfgfiwl rkrs
//
LOCUS       WP_175809182             252 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [Burkholderia cepacia complex].
ACCESSION   WP_175809182
VERSION     WP_175809182.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..252
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27057
     Region          1..245
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mirleridks fgahrvlsgi dlalqpgsvt aligpsgsgk stllrcvnll evpeagalvv
       61 gdaridfvpa rrpsrdavfa vrkqtgmvfq nfqlfphlsv vqnvmeglvt vqrwsrerar
      121 eralalldkv giadkadawp atlsggqqqr vaiaralaps pqvllcdept saldpelsve
      181 vvevlrqlar egttmlmath dlrlaasiah davfladgri veagasrdlf grprdprtak
      241 fvatlaqgvp tf
//
LOCUS       WP_175809311             637 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent helicase [Wolbachia endosymbiont of Dipetalonema
            caudispina].
ACCESSION   WP_175809311
VERSION     WP_175809311.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dipetalonema caudispina
  ORGANISM  Wolbachia endosymbiont of Dipetalonema caudispina
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Wolbachia endosymbiont of Dipetalonema
                     caudispina"
                     /db_xref="taxon:1812112"
     Protein         1..637
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=74144
     Region          2..633
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mdeyflllns eqqlavtnvn gpilvlagag tgktrtiisr iayiirngya ssdgilavtf
       61 tnkaanemvs rvfkltgvnm pwlgtfhaia arilrrhaet iglnsdfiii dvdeqlrvik
      121 diisemnsgy llekhnavmn iiqqwkekcl lpsevrdiqs fgplymttlq iyhqyqerlr
      181 yfnfvdfgdl llynmqlfnq kieilfyyqk kfkyimvdey qdtntiqylw lkylaeghln
      241 iccvgdddqs iyswrgaeve niskfsndfk ntktfkleyn yrstshilat asyiinhnkt
      301 rlekklwttn fggekvnlvk lrdsqaeakf iseqilklnk yrfndiavlv ratfqtrvle
      361 eyfikylipy kiisgvrfye rqeirdilay lrliinhndd laferiinrp krsigvitlk
      421 kiytiardsk isffeaakvl vegnqvteki klslndflnk ikvwkkmvni kplykfievl
      481 idqsgymeml kiekmrgltr ienvkeliss lksfddvttf lehiglvmev dnmgdnnntv
      541 yvmtlhaakg lefpcvflpg weeglfphqk sfedksgkal eeerrlayvg itrakemlii
      601 scvskreinn qwqlmcasrf ikelprenvk vssivyc
//
LOCUS       WP_175809321             159 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DUF2280 domain-containing protein [Burkholderia
            cepacia complex].
ACCESSION   WP_175809321
VERSION     WP_175809321.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009432
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..159
                     /product="DUF2280 domain-containing protein"
                     /calculated_mol_wt=17737
     Region          1..149
                     /region_name="COG5556"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:444299"
ORIGIN      
        1 maalpdaikv fivqslacfd tisrtakavr eefgvdvspq qcerydptkr agstlskkyr
       61 eifertreef lndtsrigvs hravrlrald ravaeaerrn nlplmaqlle qaakesgday
      121 tnrrrlehtg enggpienrt vvvdesqvaa avakledey
//
LOCUS       WP_175809443             421 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SGNH/GDSL hydrolase family protein [Burkholderia
            cepacia complex].
ACCESSION   WP_175809443
VERSION     WP_175809443.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..421
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=43628
     Region          205..412
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(212,252,290,393,396)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(212,393,396)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(212,252,290)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 msfrssfaaa vlgaavlvap lavsaapagw vaawatalqp ipdlaapppl yrapdvagrt
       61 vrqivyptvs graarirvsn aygraplvve aaslaragdg aalaggaavp vrfggkasvt
      121 lapgqelesd pvaigvtaaq pyaislqmgp dqrmtvwhrv snqfnyvsaq gdhvsdpgta
      181 sfqtrftqya wvtelaveag sahasvaaig dsitdglrss vnrnrrwpda larrltasgv
      241 dsigvvnlgi sgnrllsdsa cygtslasrf erdalsrsgv kaaivligin dinfaamppr
      301 agldcdhpht qvtaaslidg yrrlieaahr qgvkvfgatl tpaalpagre airlevnrwi
      361 rsgggfdgvv dfdavlrdpa rpsvlqrryd sgdgihpsda gytamagavp verlqaavgg
      421 k
//
LOCUS       WP_175809462             211 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Burkholderia].
ACCESSION   WP_175809462
VERSION     WP_175809462.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..211
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22217
     Region          1..211
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mnlhtwwlfv atvfvvsaip gpnmllvmth garhglrrss atmagclsal vlmlavsaag
       61 lgavleawpa mfntlrfaga aylvylgvka wrarvddvsa advdavsqga sasravlfrn
      121 gflvagsnpk ailfaaallp qfinaaeptl pqfgilvvtf avievswylv yasfgtriga
      181 tlksqsvakv fnrltgglfv gfgammalvr h
//
LOCUS       WP_175809469             232 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Burkholderia].
ACCESSION   WP_175809469
VERSION     WP_175809469.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 232)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..232
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24877
     Region          6..228
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mnatppplve lshvaksyrr gnqivpvltd isldigegdf valmgpsgsg kstllnlvag
       61 idrpdsgelr vggldisqla eaqlaewraa nvgfifqfyn lmpvltafen velplmltpl
      121 srrerrerve lvldmvnlgd rtshypsels ggqqqrvaia ralitdpvli vadeptgdld
      181 rasatdvlam lqrmnaelgk tiimvthdah aagaarslvh lekgelidgh ag
//
LOCUS       WP_175809497             321 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Burkholderia cepacia complex].
ACCESSION   WP_175809497
VERSION     WP_175809497.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..321
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34620
     Region          86..293
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mntqatpntp dtatvtflda lnsatspaie tltpaearev lagaqrsvpv dvsgidvtrr
       61 tveqdglvvs lvvvkpqdsr gvlpvfmffh gggwilgdyp therlvrdlv vqsgsaavfv
      121 eytpspeary pvaineayaa tkwvaahgae igvdgarlav vgnsvggnma avvsqmakdr
      181 qgpairfqgl mwpvadhafd nasydafang yflsrdmmkw fwnaytideg erneryaspl
      241 rasldelkgl ppaliqtaqf dvlrdegeay gyrldqagnd vttiqykgti hdfgllnvla
      301 adaptraamq qmatalkthl q
//
LOCUS       WP_175809528             255 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome c1 [Wolbachia endosymbiont of Dipetalonema caudispina].
ACCESSION   WP_175809528
VERSION     WP_175809528.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dipetalonema caudispina
  ORGANISM  Wolbachia endosymbiont of Dipetalonema caudispina
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10490041
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Wolbachia endosymbiont of Dipetalonema
                     caudispina"
                     /db_xref="taxon:1812112"
     Protein         1..255
                     /product="cytochrome c1"
                     /EC_number="7.1.1.8"
                     /GO_function="GO:0008121 - ubiquinol-cytochrome-c
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29015
     Region          34..250
                     /region_name="Cytochrom_C1"
                     /note="Cytochrome C1 family; pfam02167"
                     /db_xref="CDD:426633"
ORIGIN      
        1 mpvrnmfavf ctlflvnlvy akefkplpnk kinwsfngit gffdresiqr gykvykevca
       61 achsmnkiaf rnlqdigfse edikqiassy qvkdgpndlg emfdrpgips dyfiapfntk
      121 eaaaasnnga vppdlsliik arhdganyvy slltgyqnsk qdennlyfnp yfptgklama
      181 pplfegivey nstkkqatve nmsydivnfl qwaaepeleh rhklgfkvia yliilttlfi
      241 ltnnkvwskl yknrk
//
LOCUS       WP_175809607             214 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Wolbachia endosymbiont of Dipetalonema
            caudispina].
ACCESSION   WP_175809607
VERSION     WP_175809607.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dipetalonema caudispina
  ORGANISM  Wolbachia endosymbiont of Dipetalonema caudispina
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Wolbachia endosymbiont of Dipetalonema
                     caudispina"
                     /db_xref="taxon:1812112"
     Protein         1..214
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23647
     Region          13..213
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mielegpeic vnknkknliv clhgwgssgs nfvylakims kflpdsyfiv pnapfkreig
       61 ngyqwfsled rseealyngv enatlivnhf idvklkkfgl kdtqlsligf sqgamlaihi
      121 alirpqscas vvsysgrfis pskvapkiks rpnmcvihgd adnivpfssl nlavkalkkn
      181 ginvegypik klehmineeg iklgvefikk nfts
//
LOCUS       WP_175809643             372 aa            linear   BCT 11-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Wolbachia
            endosymbiont of Dipetalonema caudispina].
ACCESSION   WP_175809643
VERSION     WP_175809643.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dipetalonema caudispina
  ORGANISM  Wolbachia endosymbiont of Dipetalonema caudispina
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Wolbachia endosymbiont of Dipetalonema
                     caudispina"
                     /db_xref="taxon:1812112"
     Protein         1..372
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42276
     Region          25..364
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mnvlgkliil lliflfsfpl ysyqfrtrak qavildlasd lfifehnsdd kmapssmskl
       61 mtlyiafayl kdgiismkdk fqvskkawer kgssmflkeg qfvtvkelle givivsgnda
      121 citlaegiag seedfvvemn eiarklglnn shfvnssgwp nenhfmsakd lailakrift
      181 dfpeyydlfs eqyftynsvs qknknlllfy nigvdglktg ytsvgaygiv asakqngrrv
      241 fvvvnglste rerieeakrl iqysldhfys kkiftkgdiv eeinvlygks kkvsvtvand
      301 viitysrnlq dkvkvyieyk dmivapikkg qevgkifiki pgmkqktmsl yavndvhkls
      361 yvekffrvlf kv
//
LOCUS       WP_175809654             208 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Wolbachia endosymbiont of
            Dipetalonema caudispina].
ACCESSION   WP_175809654
VERSION     WP_175809654.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dipetalonema caudispina
  ORGANISM  Wolbachia endosymbiont of Dipetalonema caudispina
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Wolbachia endosymbiont of Dipetalonema
                     caudispina"
                     /db_xref="taxon:1812112"
     Protein         1..208
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23044
     Region          6..207
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 madnnfivri lssaiillvf sfaiyfndls fyllifsiav lssfewynlt qgnkilyifa
       61 lllialpnas liylynlpqg kyvliwlilt iwnidiaayl fgknfggakv fpiisprktw
      121 sglfgailig iictvfgsvf lslfsifysp migivvaila qlgdftesli krvynvknsg
      181 gmipghggvl drmdsfifta pfiaiyvs
//
LOCUS       WP_175809756             339 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Wolbachia endosymbiont of
            Dipetalonema caudispina].
ACCESSION   WP_175809756
VERSION     WP_175809756.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dipetalonema caudispina
  ORGANISM  Wolbachia endosymbiont of Dipetalonema caudispina
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Wolbachia endosymbiont of Dipetalonema
                     caudispina"
                     /db_xref="taxon:1812112"
     Protein         1..339
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37950
     Region          3..318
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 metdiviiga gpigiftafq agmlnmrchi idildqvggq ctalypekli ydipgypvit
       61 grklierlik qalpfdpvyh lnqkvekils gddqdffvit nagievkcka vviaagngmf
      121 epnrphlsgi leyesksvfy nvnkisdfqn ktiviagggn saadwtiels kvtkkiyvih
      181 rrkefrcape trnklellks ygkielvtpy qlheltgnng klhtvivknl askekkgiya
      241 dfllpffgls mnlgpinnwg lklehsrivv dqstfrtnrd rvyaigdiat ylgklklils
      301 gfaesamacy diykvihnsp infqystlkg iyrrksnll
//
LOCUS       WP_175809788             159 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Wolbachia endosymbiont of Dipetalonema
            caudispina].
ACCESSION   WP_175809788
VERSION     WP_175809788.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dipetalonema caudispina
  ORGANISM  Wolbachia endosymbiont of Dipetalonema caudispina
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Wolbachia endosymbiont of Dipetalonema
                     caudispina"
                     /db_xref="taxon:1812112"
     Protein         1..159
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18145
     Region          43..154
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(48..49,82..83,86,90..91,94,144,148)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mwsrlvvmcc fcllltgiss cqkkevttin ktnffvkqmn ekrvffgydk fnideagadv
       61 lldvikvlqh npdikvtvtg htdnrgsyey nvalgerrad aakkfmvsca pylenrikta
      121 skgeteplvy vqddsknsky ekqhaknrrv eflfsetnk
//
LOCUS       WP_175809791             207 aa            linear   BCT 11-JAN-2025
DEFINITION  SURF1 family protein [Wolbachia endosymbiont of Dipetalonema
            caudispina].
ACCESSION   WP_175809791
VERSION     WP_175809791.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dipetalonema caudispina
  ORGANISM  Wolbachia endosymbiont of Dipetalonema caudispina
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10160031
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Wolbachia endosymbiont of Dipetalonema
                     caudispina"
                     /db_xref="taxon:1812112"
     Protein         1..207
                     /product="SURF1 family protein"
                     /GO_process="GO:0033617 - mitochondrial cytochrome c
                     oxidase assembly [Evidence IEA]"
                     /calculated_mol_wt=24600
     Region          16..185
                     /region_name="SURF1"
                     /note="SURF1 superfamily. Surf1/Shy1 has been implicated
                     in the posttranslational steps of the biogenesis of the
                     mitochondrially-encoded Cox1 subunit of cytochrome c
                     oxidase (complex IV). Cytochrome c oxidase (complex IV),
                     the terminal electron-transferring...; cd06662"
                     /db_xref="CDD:119401"
ORIGIN      
        1 mlkrvifili ipcllffslg lwqlyrlywk sniiksmslp vvhllfnddf akfnyrrvki
       61 dgilsdmely vfagrhgyyi lspmilttgy ymlvnegivk erkkkrtrse rvvvngilyc
      121 dnvkgkgwli kndaalnmwf tlsieeisde lgiklekcml wqedfsnklt mqpvkhleya
      181 itwfvlfliw liiyiiyyrq nkcyssn
//
LOCUS       WP_175809874             197 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Wolbachia endosymbiont of
            Dipetalonema caudispina].
ACCESSION   WP_175809874
VERSION     WP_175809874.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dipetalonema caudispina
  ORGANISM  Wolbachia endosymbiont of Dipetalonema caudispina
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Wolbachia endosymbiont of Dipetalonema
                     caudispina"
                     /db_xref="taxon:1812112"
     Protein         1..197
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=21799
     Region          40..189
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mklivnflla iflitqsgct tfiissvvat tatavamqdk slgnivddts liirinkgll
       61 khglfsfvkv kvsegrvlli gnvdspekql iaekiawqgk evkevineir vtpiqttsil
      121 dtiidsmita eirtrflrkk niksinysin tvdgvvylmg iaqnkselka aiaiarkvkg
      181 vkqvisyvry rhsklrr
//
LOCUS       WP_175809907             257 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: phytanoyl-CoA dioxygenase family protein
            [Burkholderia].
ACCESSION   WP_175809907
VERSION     WP_175809907.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..257
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28599
     Region          12..253
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mssplqsesi raqvaelrer gfvvarglvg eaqcatlrqi aerqlreaae piefeadlry
       61 pgapeskhap gghtvrrlld aysrdpafae raiapeigaw mrayfgeepv lsrahhncmm
      121 tkhpaygslt gwhrdfrywa ferpdmvsvw lalgpetnen galwlvpgsh taefgpeafd
      181 dakffrsdlp enrrmidaat cpslqtgdvv ffhsntlhsa gqnrsdqvkf slvytyhgas
      241 nrpvpgtrsa skpevqf
//
LOCUS       WP_175809934             381 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Burkholderia
            cepacia complex].
ACCESSION   WP_175809934
VERSION     WP_175809934.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..381
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40498
     Region          1..376
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfqhtedrr mladtlnrfi aeqyafpvrd riaqsaegfd ramwqrfael gtvgalfaea
       61 dggfggagfd iavvfeclgr glvvepflga llagralala ggaahrdrla alidgsasaa
      121 fahdepgshy elttvrtrae rsgdgwvltg akgvvdqaaq aaffvvsarv sgndddaagi
      181 glfvvpadap gvslrdykki dggraaevrf ervalpadaa lgapdaldge agaellervl
      241 gygllalsae algamdvake htldylrtrk qfglpigsfq alqhrmadll leveqarsav
      301 inaaaqldap ravreralaa akysigrigt lvaeesiqlh ggigmtwelp lshyakrlvm
      361 idhqlgdedh hlaryialsk q
//
LOCUS       WP_175809949             203 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Burkholderia cepacia complex].
ACCESSION   WP_175809949
VERSION     WP_175809949.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..203
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21981
     Region          6..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mesrtqrraa atrlailqaa etllteggld avtpeavatr advavqtlyn rvggrsalli
       61 avaeraleen reymdaayas dgdvatklrc vaaayarfak erphqfrilv eppnepeala
      121 riaalirqqn aklaalisrg ieegwvdadv epehastalw ammngvislm wrpdslrldv
      181 dhiddllgta islliggikr rgd
//
LOCUS       WP_175809954             177 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: 2,4'-dihydroxyacetophenone dioxygenase family protein
            [Burkholderia cepacia complex].
ACCESSION   WP_175809954
VERSION     WP_175809954.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14449000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..177
                     /product="2,4'-dihydroxyacetophenone dioxygenase family
                     protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20255
     Region          37..160
                     /region_name="cupin_DAD"
                     /note="2,4'-Dihydroxyacetophenone dioxygenase (DAD), cupin
                     domain; cd20302"
                     /db_xref="CDD:380436"
     Site            order(53..54,57,63,65,82,84,86,88,101,104..108,110..112,
                     129,135,137,145,148,151)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:380436"
     Site            order(77,79,94,115,130)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380436"
ORIGIN      
        1 mvdqtlaefw rnippianpf kpdalpeayi snaatedery yvpftetvss rplwispsqn
       61 kwcdilmake aglvnrhyhp hevfaytlsg kwgylehdwv atkgdfvyet pgeghtlvaf
      121 dhpepmraff ivkgpliwld eegnpdgyfd vhsyiamcka hyekvgfgar aieklfr
//
LOCUS       WP_175809989             164 aa            linear   BCT 11-JAN-2025
DEFINITION  TadE/TadG family type IV pilus assembly protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175809989
VERSION     WP_175809989.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..164
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=17096
     Region          5..>65
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mtavrpasgm rrrqrgatai efamvlpvff lilyaiityg mifaaqqnpt laategaraa
       61 lnyqqvgaag svqaaqqaal aaraqaacta atnlttwlkg stcsptqqgs csydptmlcv
      121 qitltypysq splippfpll gsllpvpstl tgtamvqisp vnii
//
LOCUS       WP_175809990             561 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia cenocepacia].
ACCESSION   WP_175809990
VERSION     WP_175809990.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..561
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=60512
     Region          28..560
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mksrldrwmm llaiaaagta qaqtrvggnp ldslpqinap ktgpnvtvqv apqapqlqel
       61 lsrhltpktf qvegvksvpf eeitrrftpl vgkditigel ietangvtkl yqergyalsf
      121 afvpaqtfed gvvritvveg yvsdvkvtgk pgamepkira iaahitadrp lrratferyv
      181 ntfgllpglt vkanvpppqt tdgattlela vdrkpfnvst gidfnhpgvq glitatengl
      241 trfgeqlsis alappgrdkq tyfafsgalp vgssglitrl dastyrgkpt dnpglpsyve
      301 rtvkneklgl sasypillnn qrsllgtvsg yashnedryq nqingasldt rsqvrvlqmq
      361 ldytsvqpkq vqklsvnvak gfnilgaska qditvgtttt svdspisltf vrtgatftqt
      421 newpfrigts vsvtgqyspd slptsdqisf gstryalgyq pgetsgdsgw gmslevnrgf
      481 tpgwtylksi tpyiaydmar vylhsgtpsp nrmssvgigv rltdsryysl dlnvakpvgd
      541 apvesasrsp rinaafsyql n
//
LOCUS       WP_175810005             231 aa            linear   BCT 11-JAN-2025
DEFINITION  PIG-L deacetylase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175810005
VERSION     WP_175810005.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..231
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25350
     Region          6..>159
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mpdptrwlvv sphlddavfs cgqllaqapg sivvtvfagi pphdtpappw dqragfrhad
       61 eavrarrded rralalldar pvwldflddq ygvpttstai atrvaaaida hpgfgvlapa
      121 glfhrdhlqv qeamlsllra ddpshvwrfy edvpyrridg lmarrviewr ergwtaqpva
      181 vpaagdtnsv aakaaavday asqvtlleph mraalrepet iwrlecdvts a
//
LOCUS       WP_175810015             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TolC family protein [Burkholderia cepacia complex].
ACCESSION   WP_175810015
VERSION     WP_175810015.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..439
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45873
     Region          55..435
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mlklnlnlva aivfvmvata haqplltpgp gaaaassatp igappsdtlp assltlsdal
       61 avaarnnpal rgaradvdas agalmqagar pnpevsflqe gfsraertst alinqtielg
      121 gkrrarldva sygreaanas ldeqgaavra dviaafygll aaqrqlqvte esaaiaarsa
      181 dlagrraqag kvspveatka qvaaagvqie vvtargrvev areklnavmg earddrlavr
      241 gdletvppve plsaltvqld daplarvara emlrsnaavs lerarripdv tvsagfkrvt
      301 tggvpenqav vgvsipiplf ntnkgallea thkaeranad ldrertrlrl eltqayanfe
      361 aaeqeaqrlk vdilpaarla ldamsrgyel gkfsffdvld aqrtlfqgqs qyvralagah
      421 aaradigrlv gtplaavaq
//
LOCUS       WP_175810036              96 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: type II toxin-antitoxin system RelE/ParE family toxin
            [Burkholderia].
ACCESSION   WP_175810036
VERSION     WP_175810036.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 96)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 96)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..96
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=10737
     Region          3..93
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mpqvifapaa igdmqrlref lkpknpdaar rageairqgv qalgahprmg rlvedlpeqy
       61 rewlidfgds gymaryrldg dtvtilavrh qkeagy
//
LOCUS       WP_175810055             561 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GMC family oxidoreductase [Burkholderia cepacia
            complex].
ACCESSION   WP_175810055
VERSION     WP_175810055.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..561
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=60984
     Region          10..539
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mstqrtlege fdyvivgagt agcvlanrlt edpdisvlll eaggkddyhw ihipvgylyc
       61 ignprtdwly ktqpeaalng ralsyprgrv lggcssingm iymrgqredy dnwaqetgda
      121 gwswdsvlpi fkrsedhhag asdahgaggy wrvekqrlrw qilesfaqaa qqtgipatdd
      181 fnrgdnagvg yfevnqkrgv rwntskaflr pamarpnltv itgahaqrvi fdgrravgve
      241 yhgggtdyva rarsevllts gavnspqlle lsgigdgrrl qalgidvvqd lpgvgenlqd
      301 hlqlrmafrv dgvrtlntls ahwwgklmig aeyallqrgp msmapsqlga faksdpddpa
      361 ltrpdlqyhv qplslerfge plhgfnafta svchlrpssr gsvhvtsadp asapaiapny
      421 lstdhdrhva analrltrri aaapalaryr peeilpgpqy rteaelidaa gavgttifhp
      481 vgtcrmgrad daravvdsrl rvrsiaglri vdasvmpfit sgntnsptlm iaerasdmir
      541 adrraaream avrteaavta a
//
LOCUS       WP_175810074             290 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: fumarylacetoacetate hydrolase family protein
            [Burkholderia cepacia complex].
ACCESSION   WP_175810074
VERSION     WP_175810074.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..290
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31285
     Region          72..280
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mrfaiykkng hrgiavehsg qwfgltaedt aypgdldsll aqgadlaeva arlargtpvd
       61 ldavrvlppf grpnkilcvg lnyldhsmet gfakqtyptv farfasslig hdqpialpaq
      121 ssqldyegel vavigkagrg itreraldhv agyslfndvt lrdyqfrtpq wtmgknfdgt
      181 ggfgprfvta delprgckgl riqtrlngav vqeastsdmi fdvetlvvll sevmtlqagd
      241 livtgtpagi gmarepqlwm kagdvcevei eqlgvlrnav mpaamvrcda
//
LOCUS       WP_175810263             384 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia cepacia].
ACCESSION   WP_175810263
VERSION     WP_175810263.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..384
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42036
     Region          1..384
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnfdlelehr mirdlvarfv qdelipleaa vmareadgqr fglldeerah ldersrqlgl
       61 wgldapldag gsdlpavamv gvneaigttv tpyilppdsp nlrmlcdvad daqrarylep
      121 yargitraam aisepgagsd pgalsttavr dgdgwvlngr kiwishapea dwtivmaltd
      181 rskgkrggms afivdrdtpg fiierripmi gglstyeivl ddcripaaql lgqegagfap
      241 mqarlanrrl emaawcigra eravamkcdh akqrktfgvp laerqavqww vadaltqiha
      301 crlmtyeaaa rvdagqdart qismvkvfat emassvidha mqalgamgmt kemplqqmas
      361 earlmrifeg ptevhrwvia rsal
//
LOCUS       WP_175810270             139 aa            linear   BCT 11-JAN-2025
DEFINITION  HIT family protein [Burkholderia cepacia].
ACCESSION   WP_175810270
VERSION     WP_175810270.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..139
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=14922
     Region          5..136
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 msydnnnpfa rilrgelpcv kvaeddttla imdlmpqadg hvlvipkeqa aqifdlsgda
       61 aaagirmtqr vaaavraale pdgvfigqfn gaaagqtvph vhfhviprwe gaelrmhare
      121 iadaatleal aqrirarfv
//
LOCUS       WP_175810287             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175810287
VERSION     WP_175810287.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33724
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdnlgdirlf vetasqgsls aagrklglsp aaasarlvkl egelhtqlfe rstrklrltd
       61 egrlylvhcq halqtledar aalqvgrasv sgalrvsats dfgrtvlrrw ldefnerhpn
      121 vtltlvlsds lshllqddid lairfgvpad ssmvakrmag nrralcaspd yiaahgmpsh
      181 pddlrehrfv vlssaagaan nwrfardget alfaapldss rqtndgslar ewaiegrgva
      241 mksiwdigad lqagrlklll pewrcpdvpv nalfqrtlym aprvrtlldf lekqfsease
      301 alapflr
//
LOCUS       WP_175810323             466 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Burkholderia cepacia].
ACCESSION   WP_175810323
VERSION     WP_175810323.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..466
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51706
     Region          4..440
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 meifdafhla rlqfaftvsf hivfpaisig masflavlew rylvtgdaay ksmfqfwski
       61 faigfgmgvv sgvvmayefg tnwagfsrva gnitgpllty evltafflea gflgvmlfgw
      121 qrvsprahff atlmvavgtl istfwilasn sfmqtpqgyk ienglvvpvd wfkivfnpsf
      181 pyrlvhmtia afivagfiva acgawhllkg rrdepvkrsf smalwmllvl apiqivvgda
      241 hglntreyqp akiaaieglw etekagtaln lvglpdmqae ttryaiqvph lgslilthsw
      301 dgeirglkef qpqdrpyspi ifwtfrimag lgmlmlltal lglllrkggr lyetrwfqwf
      361 vvamgpsgiv allagwitte vgrqpwtvyg vlrtvdsvap lsaqqvgvsl lifvvvyflv
      421 fgtgvyymlk lmkrgpaaqa gyielhrhpg lrksalstpl nvteae
//
LOCUS       WP_175810356             318 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cepacia].
ACCESSION   WP_175810356
VERSION     WP_175810356.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..318
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33453
     Region          80..293
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mlepeiaafv aavdawypad aaerapaeqr rlydrfaaew tpaalpaglv qqdavwqapd
       61 graialrryt saqgaprgtv lffhgggfvv gsldshalit aqlaadtgld viavdyrlap
      121 ehrapaaled clavtraard arwpfgpcah pltlagdsag gmlaaavata lrdageggvd
      181 gialvypmlg fepqsparet eayapmltld dvhryralyw sgglsdalgd gnpllrasvp
      241 laaarfdglp pvlaigaehd plrddarvyv eriraaggaa hywmgeglvh gcwralgtsp
      301 qaarmhrtvg gfllapha
//
LOCUS       WP_175810374             441 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175810374
VERSION     WP_175810374.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46848
     Region          33..412
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(46..47,50..51,54,86,136..137,139..141,144,164,
                     167..168,171,266,269..270,273..275,278,306,310,361..362,
                     366,370,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mrstgcetpd erkaipadss padldalyrr igwklmplll vaqvlayldr vnvgaaklqm
       61 agdlglsdtv ygigagiffv gyflfevpsn lmlhrvgarv wiarimvtwg ivsaaaawvh
      121 spatfylqrl ilgvaeagff pgivlyltyw fpahrrgrmt tlfmsatava givgnmlsgw
      181 imtnldgfaa lsgwqwtfvi eglptvvvgl avhyllpsrp ndarwlspee adavlrgldv
      241 naghaeetqr asrlsasemv llttiyflll vglygigfwl ptlvkdtglt klswigvcsa
      301 ipyliavlam nvgarsadra gnwaayvvgg agvasvgfil sasfsgalpa viaglslaaa
      361 gtltalplfw hlptmrltgt aaaagiatin cfgnlagfag piafgwlkdr hhdaigptml
      421 lalsalsaav ltaiyrrvar h
//
LOCUS       WP_175810531             241 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Burkholderia
            cepacia].
ACCESSION   WP_175810531
VERSION     WP_175810531.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..241
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26466
     Region          1..239
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 misiknvskw ygqfqvltdc ttevkkgevv vvcgpsgsgk stliktvngl epfqqgeilv
       61 ngqsvgdkkt nlsklrskvg mvfqhfelfp hlsitenltl aqikvlgrgk deasekglkl
      121 ldrvglkaha hkfpgqlsgg qqqrvaiara lsmdpiamlf deptsaldpe minevldvmv
      181 elaqegmtmm vvthemgfak kvahrvifmd kgaiveddrk ddffsnpkse rakdflakil
      241 h
//
LOCUS       WP_175810544             312 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cepacia].
ACCESSION   WP_175810544
VERSION     WP_175810544.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..312
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32218
     Region          78..282
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mpldpqaqal laafaqapai dfaqltvpay raslaaggaf apgdavaaee dwqipasgrq
       61 lsarlyrpaa dgplpltvff hgggfvacgi dshanlcrsl aarartlvls vdyrlapear
      121 fpaaahdacd avrwaaasar dlgaragala vagdsaggnl aavaalqlrg sgiaiahqll
      181 lypvvdcate hpsyeslgng yfltadmmrw fkrhyfddga drasplaspl aapdvagaap
      241 ativsaefdp lrdeaeayal rlaqagtpvt vvrwpgqlhg fasmlgaida adrvltfgad
      301 alrrafdate ap
//
LOCUS       WP_175810546             766 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Burkholderia cepacia].
ACCESSION   WP_175810546
VERSION     WP_175810546.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..766
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=83694
     Region          178..765
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 msyvvavram ceftarrgdl dlrftpapta legiaghgav tsnrgaryet eialtgtwgt
       61 ltvrgradgy dpaanrleei ktfrgsldam panhralhwa qakvyahlmc darglpeidv
      121 alvyfdivse retvltqtlg aaelaaffae qcacfvgwae retahraard aalralafph
      181 gqfrsgqrel avavyraard drclmaqapt gigktlgtvf pllkacgege ldhvyfltak
      241 tpgralalea aatlgagtpa lplrvlelva rdkacehpds achgescpla kgfydrlpaa
      301 rdaaieagll drdtvraaal ahdvcpyyls qelarwsdmv igdynyyydg samlhtlaqq
      361 nqwrvgvlvd eahnlldrar kmysasldpf afaaareaap aalrkafdrl arawgtvnra
      421 qaeryaaype ipgpivsalq nlvaavgehl adaprangda llrfhfeaiq fgvlaeafds
      481 asifdatlhg epmprqpald gvasagrrrr vqstlcvrnv ipagflapry eaacatvlfs
      541 gtlspfhfyr dtlglpgdtg wldvdgpfra eqltvrvash vstrwrdrdr slepivdlia
      601 aqyatrpgny lgflssfdyl grvvalmqar hpdvpvwaqa pgmtegerda flarfdaggr
      661 gvgfavlgga fsegvdlvge rligafiatl glpqvndvne qmrramdarf gngydymyly
      721 pglqkvvqaa grvirtehde gvvhliddry rrrevrdllp rwwrig
//
LOCUS       WP_175810552             310 aa            linear   BCT 11-JAN-2025
DEFINITION  AEC family transporter [Burkholderia cepacia].
ACCESSION   WP_175810552
VERSION     WP_175810552.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..310
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31457
     Region          18..305
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 migpillala pvallvacgh glrrtgfiay afwpqaerlc yyvllpalfa hglanarlqs
       61 lpvlplaaal vgstalaaal lllvrpfvrv dgagftsvfq gavrfnnyvg talaaglfga
      121 kgialaavcv aaivptvnlm cvlvfarygd trlgaaalvr qilsnplvva calgiamqag
      181 gvtfpaavep avralgvasm plgllcvgaa lkfdaarawl qpvcvasafk fmamplitla
      241 agrlfglgda altvallfqa lptssasyim arqlggdapl magitafqti aaalampvvl
      301 talasapafr
//
LOCUS       WP_175810561             826 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 2 protein [Burkholderia cepacia].
ACCESSION   WP_175810561
VERSION     WP_175810561.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 826)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 826)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 826)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 826)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..826
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..826
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90147
     Region          9..>626
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mtrtralpgw smlataagaa reprdlpaag ngwipaavpg tvaqslalag rldeavslde
       61 rdhwyrielr ghgprvlrfh glatlaqawl ddtpilrsds mfvahdvpvs ldgshrltlc
      121 fralaphlrd araprrarwr trlaepaalr tirtslfghm pgwfpphvpt gpwrpvdvld
      181 padgpvladc nlhariegdt gwldadltfa aplpdalaar lscgqhhatl eragpdrlra
      241 svavpnvcrw wphthgepvl ydialhigde rrplgatgfr tievdpgadg kgfglrvngv
      301 pvfargacws saaplalhad datyarllgl ardagfnmir vggtmtyead afhawcdrlg
      361 llvwqdfmfa nfdyalddpa fadnverear qflsrhgasp slavlcggse iaqqaamsgl
      421 gpkqrflelt adrlaghaaa crpdvpyvpd spdggvlpfm prervshyyg vgaylrpldd
      481 arradvrfas eclafsnvpc datlaelgwp gvheprwkaa vprdpgtswd fedirdhylq
      541 tlydvvpdrl rredparyfe lsravvadvm retfsewrrt gsrcagalvw qfqdvmpgag
      601 wgvidaahrp ksawhalrqv lqpvqvllvd eglngldvhv vnerpaplsa alelvalrdg
      661 rtavaragcp vriaahdtvr igsaellgrf fdwtyayrfg pcehdtvvat lrgddgtlls
      721 qafhfpsrth pavlarrelg leacvsrtgd twhvdidtrh varhvqidap gfvprddwfh
      781 lapgtparvv lvplgtagkn gaadgppave iravnaarav ratqag
//
LOCUS       WP_175810584             523 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175810584
VERSION     WP_175810584.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..523
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52363
     Region          37..448
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,157,
                     160..161,164,288,291..292,295..297,300,328,332,384..385,
                     389,393,409,412..413,416..417,420)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msqsspasra gaaaaprtgg smpaaatlav asatcslivl dtnvvavslp siarsfhasf
       61 adiewvvsay mtafaacllp aggladrfgr krmlgaglal fflaslgcgv apsagwliaa
      121 ravkgggaal lltaalavia nrfpegrera rawaiwgmcm giatavaplv ggaitqwigw
      181 rwvfllnlpv cmllaagarv aidesrdpha krvdaagsll fgaalacaia aligapshgw
      241 lsaatlgrla laaalfaafv gaerwqarpm idlalfrqpr fvgavlamfg yaacaqvmmt
      301 flplylqnaf gmsaidaglg mlpfafamia gpslgaalaa rvssggvlag glaligagnl
      361 ataaltaasd yrlvaigmfv tgcgagimng dtqkaimacv psnrtgmasg istttrfsai
      421 vtavgvlgav laastqarld rllsaapglr afadapfmss llagdlaral ervppsaaga
      481 lakaapvafa sgfadaltvs gvlalvvavv ackllaqpmr daa
//
LOCUS       WP_175810589             328 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175810589
VERSION     WP_175810589.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..328
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34803
     Region          6..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..302
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176149"
ORIGIN      
        1 medidlnlvt aldvllsegs vtgaarrlgl stsamsrtlt rlrvstgdql lvragrklvp
       61 tphaaalrdr vhaiatdara vlrpatadvd lathastfti raaasfmeml sgpvvaalge
      121 iapqvrirfv pkpdrdpqal rdgavdleig krgddapelh trmlfhdwhv avaraghplf
      181 asgritpary aacrhviasq lgdfggpadd ptdgagqgda vrvvvpgypd amrvaastdl
      241 ialvprsslg nafspgltda lglrsfeipv rlpgilvsal whprmhgdpv hrrlrdavia
      301 vcqraypdtr tphtsrppar rtgpraag
//
LOCUS       WP_175810686             468 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175810686
VERSION     WP_175810686.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 468)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..468
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49485
     Region          <229..467
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mhtlmlalrn lqrnrrrslt tllamivgvs aillfggfsr ditlglqtdf vqrsghlqiq
       61 rqgyylygtg dpaaygirry aalidllrrd pqlapmlqvv tptlqfggia gnfaagvsrt
      121 vmgfgaipdd qyrmqqwnay gfplrprafa lrgsaddaav vglgvarvlh lcgplhvpdc
      181 rdappgpaap aatgpdasap advlvlaqge agsqpagdga thievltasa ggapnvgrfs
      241 vvkaeqqgvk elddvylavr lpqaqrlvyg gaepratale iqlartadlp aararieqll
      301 rggfdgqpld vvdfatlnpf ydqtnrmfsv ifgfvfvlis aivlfvisnt mstaiiertv
      361 eigtlramgm rrggiqalfv cegallgvag aslgvlaala iaaavnhsgl awtpparida
      421 valtvrvwge wrtiavtfag lacvaglsaw lpsrhaarls ivdalrhv
//
LOCUS       WP_175810690             546 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Burkholderia cepacia].
ACCESSION   WP_175810690
VERSION     WP_175810690.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..546
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58036
     Region          13..527
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 maaatptgal valhhvsfrf ddgvtlfdsl dlsidrtptg ivgrngigks qlaqliagrc
       61 apstgtidrs tqvayvaqqh ddaaagprtv aqlaaldapl galarladgr aephdfdlig
      121 drwdlaerlr taldaaglhd vradtpaqal sggqrarval igallsgagl lvldeptnhl
      181 dapgrawlra aldgwrgglv ivshdralla dvqriveltp qgvrsyggny afyraqrdad
      241 qdaaqaaldn araergrarr rleqehdtiq rhaaaslrda ktanlssgak qsrkgaarni
      301 mgqvrrhqnd fkatldervq qaaarveada pvlvslpgte vsarrqlftl erarlpwgia
      361 gaadgitwsa sgpvrialtg pngcgkstll rmlagelvpc sgtctthvsa ayldqrlall
      421 dpersiveql glldtplaeg elrsrlallq ldaaratqpa rqlsggerlk aalacalwrg
      481 tpaqllllde ptnhldlesv raieaalagf pgaivvashd taflaaldpt htmqwhrdgw
      541 ryepva
//
LOCUS       WP_175810715             266 aa            linear   BCT 11-JAN-2025
DEFINITION  (Fe-S)-binding protein [Burkholderia cepacia].
ACCESSION   WP_175810715
VERSION     WP_175810715.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..266
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28303
     Region          <7..256
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mnerqypaaa pahvylfatc lvdlfvpeag ldavrllere gltvhyprgq sccgqpayss
       61 gnpdearrva aaqldlfaqa wpvivpsgsc agmirhhwpa lfaddpvygp qaraiaerty
      121 elaeflvhvl dvrlnaatag agpdervvlh tscaarremg trghgvalvd alpgvtrveh
      181 ereseccgfg gtfslkhpdi sgamvrdkva sacatgcdrl vsadcgclln ighaaaktga
      241 plpvehlasf lwrrtanaps lrgdqr
//
LOCUS       WP_175810728             318 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Burkholderia cepacia].
ACCESSION   WP_175810728
VERSION     WP_175810728.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..318
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33091
     Region          3..296
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(36..37,40,91,105,107,136,168,256,259,295)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(227,232,247,256..258,261,283,287)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 maeivvagel laefvaaerg qgfdapglfa gpfpsgapai fadqaarlga rvayagcvgr
       61 dafgdaivar lerdgvdvar irrvarptgt afvayrddgs rsfvyslsts aaacvdasdv
      121 dtamfdgcry fhvmgsslts esaiaavqrg vieaaragak vsfdpnvrpe mlsfrpmraa
      181 letmlaachl fmpseddlpf fcgpqpaera iagllathpl lervvlkrga rgsvafdrad
      241 rveapafqvd eidptgagdc fggtlvasfv agvpidaalr ranaagaiav trrgpmegns
      301 saaeidrflt ergiacpa
//
LOCUS       WP_175810759             339 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Burkholderia cepacia].
ACCESSION   WP_175810759
VERSION     WP_175810759.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..339
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36888
     Region          11..323
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(16..18,48,53,79,142..143,183..184,207,236..242,278,
                     295..298,303,306..307)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(48,53,79,142)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 mslkdtlpad nrlgfgaapl gnmfrdipdd eaiatveaaw argiryfdta psygaglaes
       61 rlgdalaghr rddyvistkv grivldemed aktrdygeks gifahgranr lvsdysadat
      121 lhsiedslkr lrtdrldivw vhdiaqdihg dewlaqfeva rkgafrvlgr lreegvigaw
      181 glgvnrvepi elvldlaepq pdgmllagry tlldheralq rvmpaaaarn vgivvggpys
      241 sgvlvggahf eyrkappdiv akveriraia arydvpvkaa alqfvlahpa taavipgasr
      301 periaedsaa ltfdipadfw remreqqlva adaplpidr
//
LOCUS       WP_175810764             136 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia cepacia].
ACCESSION   WP_175810764
VERSION     WP_175810764.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..136
                     /product="VOC family protein"
                     /calculated_mol_wt=15124
     Region          10..119
                     /region_name="VOC_like"
                     /note="uncharacterized subfamily of vicinal oxygen chelate
                     (VOC) family; cd07246"
                     /db_xref="CDD:319910"
     Site            order(10..15,17,32,48..49,51..53,64..66,68..73,79,100,105,
                     113..116)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:319910"
ORIGIN      
        1 marfqpdgwh tvtprivvpd peyliefmrs vfhaqgafrp glpaeirigd svvmvsgedg
       61 lrdpmsafly vyvedadlty rralaahaip leapadmpyg drramvkdrw gntwqiathl
      121 rdlsvdeirs rvaggg
//
LOCUS       WP_175810766             475 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175810766
VERSION     WP_175810766.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..475
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50815
     Region          40..459
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(50..51,54..55,58,90,140..141,143..145,148,171,
                     174..175,178,287,290..291,294..296,299,328,332,383,389,
                     393,397,413,416..417,420..421,424)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mssidlnavt passpirsas dvarlintvd ssvsharmiv llalggvfld aydlttlsyg
       61 iddvarefgl tpaltglvgs aimigtifgs liggwltdri gryqvfmadm lffvvaaiaa
      121 glapnvwvli aarfvmglgv gidlpvamaf laefskfngr gnkasrlaaw cpmwyvassa
      181 cfllifglyf llpaehagwl wraslifgav palviilfrn rfmnesplwa anqgdlanaa
      241 rilresygih aheaedarrv psqppvrirv lfqrpylgrt ivasvmnlci pfeytaiaff
      301 lpsilsqflg agvfetiaas lalnvlfaft ggllgmrlah rhasrhvaia gfalqfvalv
      361 alalaghphg alaigfvllm lgtwlfaegf gpgaqmmiyp tlsypasirg tgvgfgrslc
      421 gigqalalfv lpilqarlgt dmfwvvaisa atpivflliv ryeptardid ddgae
//
LOCUS       WP_175810788             574 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Burkholderia cepacia].
ACCESSION   WP_175810788
VERSION     WP_175810788.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..574
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64409
     Region          5..491
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mttlisalsl qletghgplf qdltftvklg driglighng cgktslldvl agsrepgvgs
       61 vqyaamcrlq hveqhlpprl adlttreall ksaggqraeh wrvdsllddl elataadlpv
      121 sdlsggqhtr lllgravlaq pnlllldeps nhldlpsllw lenflrrwqg gfilvshdar
      181 lldslsnrsw ilrdqrlysf dmpcsralva laeadataqa rhageqseid rlaasskrla
      241 iwgrehdnek lsrqaksmqr rveklkedqt fvsrgspwrl klqgrpfaad rlmafeglhv
      301 raqadepilf evhdlwlrpg dkvavlgsng tgkssllrqc wsdlqrgear mgwryhpaar
      361 iayydqslhq laddatlsda lykfapvgdr errqalisag fayvrhgqtv atlsggerar
      421 llflalsmas yhllwldept nhldmegkre laaalaafdg gfilvshdre liehscnrfw
      481 aihngrlqel pdaesayrnl ftsrepavpe qipttrnhtg vqstssdaea lwqrwcqlet
      541 llaaelvrkp khqkpqlqeq wreemrqler elgl
//
LOCUS       WP_175810793             319 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175810793
VERSION     WP_175810793.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..319
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32099
     Region          8..319
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtdrigrlqr fslvaallav iaffavfapg farpanladv lvnnfallai aalgmtlals
       61 igavdlslgt aidvaslvfv qlvahqvgvl pallgglgaa vlvgtfngal vaglgiapfl
      121 atlgtlfigq tvqqlatggg qpvyllnval pplfgtlahg tlagmpvplw cvvvlaaavh
      181 vvlahsafgr ysaalgaqpg varhsglpva atvvatfvas alvygvvgll lsstvkayvp
      241 qagngfllna igatfigttl sptrrpgvtg tllgvllisl vangllligw nfywqqvatg
      301 alilavlals fmgrrvraa
//
LOCUS       WP_175810800             472 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175810800
VERSION     WP_175810800.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..472
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=48608
     Region          6..466
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 msalpdraaq rhalaatlgd gwldgasaes cepyatdvtl hsgvalgvar pastadtsal
       61 arvavahrva lvaqgartgl vgaavpdrsg tqcvvsfdrm ravrafdaan rsitveagvr
      121 lsdinrvaad aglclpvdlg sdptagglvg anaggsrlik ygdvrrnvlg vevvladaag
      181 tvidalaplr krnagfdvtq cfigangahg lvtavsfala plersscaaf vafasydaal
      241 agllaferaf gemlsafefm saaavgcvaa afpalripfe adaaacyalv eiatgmpgld
      301 glleertiat ldtlagervv ldaacapaer fwrirdalpv avaqhgipls fdvsfprgal
      361 aafvadaeqw iaaahpslrc hafghfgdgg chlvvsipha daerygplqq valrgalyer
      421 vvraggcfsa ehgvgpvnva yyrkhvpaaq relaaaiqha vdplgligrv ry
//
LOCUS       WP_175810873             222 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175810873
VERSION     WP_175810873.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..222
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23540
     Region          29..187
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpprhvqvpa ppgqpaaqpa palrrrprqs raqassdalq qafvqlller gyakatirei
       61 aavagvsigt fyeyfgdkqs laalcihrhv laladrlrda vaglrgapra elaaalvdlq
      121 vdaigadaal wgalfalerq vsplaayrrh ydayvalwrd alahaadppp aarldgiarm
      181 ahtlcyggls qalltlgsaf divalrgelr amllaylaaa gr
//
LOCUS       WP_175810881             385 aa            linear   BCT 11-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Burkholderia
            cepacia].
ACCESSION   WP_175810881
VERSION     WP_175810881.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..385
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41053
     Region          17..299
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mstfsddaqs adkhavarks tfvsivlnvv latfqivvgt iahsqaliad gvhsisdlis
       61 dfvvlvanrh sgaspdadhn yghsryetva slflgailia vgvgmlwrag drlvnlenip
      121 avhfsalvva ltvlvskeal frymlrearr vrsamlvana wharsdaass lvvaigivgs
      181 lagvrlldpi aaaivgfmva rmgwtfgyda lqdlsdrald ttdtaeiral laatpgvrdv
      241 hdlrtrkmgd aalvdahilv dpmisvsegh yiaetararv lrdprvldal ihvdpendaa
      301 rrpalalppr geiaarleaa laqrglhaaa inlhylstgl eidvtlacdp hdtdaalagr
      361 ldadalkref garrigftrt mlaqa
//
LOCUS       WP_175810908             191 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Burkholderia cepacia].
ACCESSION   WP_175810908
VERSION     WP_175810908.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..191
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=20698
     Region          4..135
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(9,11,72..73,76)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            11
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(71,116..117,119..120,124)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(77,82..83,112,115..116,119..120,123,126)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(101..103,112..113,116..117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(101,117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(125,131..132)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          147..188
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
     Site            order(148..150,182..183,185..187)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 msrtfayarv stidqtaanq lreieaagfs vdkrrvvtes isgsvsaqqr pgfaelllki
       61 eegdvlivtk ldrlgrnamd vretvetlad rgirihclal ggvdltsaag rmtmqvlnav
      121 aeferdllie rtqagiarar aegkamgrps altkqqqddv rqhlsegasv aslakrygts
      181 rqtimrvrda a
//
LOCUS       WP_175810933             333 aa            linear   BCT 11-JAN-2025
DEFINITION  bestrophin family protein [Burkholderia cepacia].
ACCESSION   WP_175810933
VERSION     WP_175810933.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..333
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38125
     Region          9..322
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 mhlgrsykls efliwtrwki yellifgsvp vvlykffsit wlsipltivv llgtatsfiv
       61 gfknvqtynr aadaleiwtg ilgksrrwgq iardfvadee varklvyrhl awltalrydl
      121 rrprvwestt krynaeyrrf yrvpewekdi rellpqylsp aetaqalsss svttcvlslq
      181 gtslktlyla gqlnsgfyme lqktigdfvd lqsrserfkn fpyprqyatv sslfvrffcl
      241 slpfgllnef nrlndsvsgf mhgnmvwlvv pcsvavswmy tsleqvgest enpfeggand
      301 vpistlcsti erdlkamlge hesesssrti ial
//
LOCUS       WP_175810934             402 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175810934
VERSION     WP_175810934.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..402
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=41980
     Region          4..355
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 msqkilivga gfagvwgalg aarvldgagv tgsdveitlv spkpelqirp rlyesgpqqm
       61 aapllpllda vgvkflegsv eeidvrekta gvacadgekr liaydrlllt sgsklsrppv
      121 pglaehafsv dciedavald ahfaalaklp esparntvav vgcgftgiev aaelpkrlre
      181 wfgadaksrv vvigaqddig pdlgpnprph vaeafdslgv eavlgsrvvs iaadgvrtas
      241 gthieamtvi waggmraspl aaqvsshlda lgrvavtadl rvadaphvfv agdvararcd
      301 ddghdalmsc qhaivmgqfg ghnvaadlig vptltyrqpf yatcvdlgew gavysegwdr
      361 qiklthaegk arkqmintqw iyppapnrad alaagnplas fg
//
LOCUS       WP_175810943             216 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DsbA family oxidoreductase [Burkholderia].
ACCESSION   WP_175810943
VERSION     WP_175810943.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..216
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22648
     Region          6..205
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(14,17)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 mkpvevtvty dlicpwcwia ehrlaeaiea aglagavnvr fvpfelnptm paggidrkay
       61 rsakfgswar sqaldahvad agraaglvfd hariartpnt rlahrlvwfa qqrgsavalv
      121 dalfaayfrd grdigdtdvl veiaagagla gdavraflas gegldavval eeaavrdgia
      181 svpstrigst vvsgaqpadv fraalldaqr ardraa
//
LOCUS       WP_175810962             214 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia cepacia].
ACCESSION   WP_175810962
VERSION     WP_175810962.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..214
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24420
     Region          1..210
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mltvwgrrna fnvqkvmwlv delalehrhv paggqfgvld tpgflamnph grvpviddgg
       61 tvvweshsil rylaarygrp gfwhddpaeq sradrwmdws qttlqptfln gvfrgfyrtp
      121 peqrdtarve qsiaqcaqyf rtldavlagq pflvgdtltl adiaagthly ryfeldiarp
      181 dlphvqawye rlkarpayrt hvmipfddlr gkld
//
LOCUS       WP_175811043             161 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein, partial [Burkholderia
            cepacia].
ACCESSION   WP_175811043
VERSION     WP_175811043.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         <1..>161
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
     Region          13..>161
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 vqtnqpprlg eeilrvdhvc rgfnktqgel lvlddanlsl regeivgllg rsgsgkstll
       61 riiagliept ggevtylgkp lrgpaegvam vfqtfalfpw ltvlqnveag lealgvgare
      121 rreralaaid ligldgfena yprelsggmr qrvgfaralv v
//
LOCUS       WP_175811068             224 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator, partial [Burkholderia
            anthina].
ACCESSION   WP_175811068
VERSION     WP_175811068.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         <1..>224
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          1..51
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          60..224
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(63,92,106,108,171,188,215)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 vaaegsfaka gerlgigrsa vsrnvqklea qldarlllrt trctqltreg qlfyehcrpg
       61 ieqiaqalde mrelhsgppd faagridvaf rdgiledsql iarrlmpmrl lvcaspayas
      121 rhglprelve ltahrciglr gaagsveawt frveggvrrv vpearhgfnd pelamqaald
      181 geglaqlpay lacealregr llaclgafad edrghylcyp srkh
//
LOCUS       WP_175811143             734 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia cenocepacia].
ACCESSION   WP_175811143
VERSION     WP_175811143.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..734
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79751
     Region          33..717
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 msasspastp aggpfaawya afgdwartdg aawlylfkal laafiatgvs mrldlpapkt
       61 amttvfivmq pqsgavlaks fyrvagtifg liatltfvgl fpqqpqlfll avalwvalct
      121 agaarnrnfr sygfllagyt taliglpasq hpdgafmsam trvaeimvgi vsagvvsalv
      181 fpqttgeqmr ttvrkrfgsf vdyvaaalsg qldrahieti htrfvadvvg feaarsmavf
      241 edpdtrmrsg rlarlnsefm sassrfhalh qlmnrlhaag aqaaidaiep yfreiaplll
      301 ppagepvrts adaghaaaql lawrdalprr iratraalet qpdfplldfd taaellyrfi
      361 tdlheyaaty aslssather erwieryepr tnatamviaa irtatvilvl gwfwietawp
      421 sgvtltltaa atcalasstp rptamsaqmg mgtalavctg flltfgiyph idgfpllcva
      481 lapllaigif mtlkpklagy gmgyliffsf lagpdnithy dptgfmndsl alvlsmlasa
      541 iafavlfppt apwlkkrlfa dlrhqavaag harlaglrtr fesgardlmy qahtlsadqp
      601 dvqrdalrwm favletgnat idlrhelaml psdpryapam pwrraietmr salsalftrp
      661 saarfdatla atnaaidatr qtldafepsr eerhrlqril shlhfvrtal ldpesplepl
      721 nrnrpvrpqp gass
//
LOCUS       WP_175811154             400 aa            linear   BCT 11-JAN-2025
DEFINITION  benzoate/H(+) symporter BenE family transporter [Burkholderia
            cenocepacia].
ACCESSION   WP_175811154
VERSION     WP_175811154.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..400
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41404
     Region          11..399
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mqpntppgai rtlgndwsvs aitagflavl isyagplaif fqasqaahas neivtswvwa
       61 isigagvsgl faswklkvpv vtawsapgta llvglfpqlt lnqavgayit aaliilaigv
      121 sgyfdrlvrh iprgiacgmm agillpfgmh afsaasaqpa lafgmiaayv ifrrllprys
      181 ivlvlltgaa latllgmahl gnvspslarp ifiapewtlg ttlslalplv vvsltgqflp
      241 gmailrvsgy htparpiita tsvmsllvac fggitivvaa itaalctgkd ahedqdrryv
      301 aglvnsviyl igglfagtiv tlffalpkaf vailaglali gaisanvhgi fedenhreas
      361 vitflatasg mtwlglgsaf wgivigsvay gvlngvrrpa
//
LOCUS       WP_175811209             353 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia contaminans].
ACCESSION   WP_175811209
VERSION     WP_175811209.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..353
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37524
     Region          3..332
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,225,286,306,308..310)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,173,176,178,225,232,286,306,
                     308..309)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,173,176,178,309)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            178
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mpalfdpvtl gdltlpnriv mapltrsrag atrvpnalma ryyaeratag liiteatsvt
       61 pqgvgyadtp giwsdeqveg wkqvtqavha aggrivlqlw hvgrisdpvf lngdlpvaps
      121 aiaagghvsl vrpqrpyvtp raleldeipg ivaayrkgaq nakaagfdgv eihgangyll
      181 dqflqdstnh rtdayggpie nrarlllevv daaidvwgag rvgvhlaprg dahtmgdsdp
      241 aatfgyvare lgrrkiafif tresysgdhl sprlkeafgg plianeqftl dtaqaalasg
      301 nadaiawgkl fianpdlprr lelgaplnkp vpetfyaege tgytdypals daa
//
LOCUS       WP_175811313             249 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Burkholderia contaminans].
ACCESSION   WP_175811313
VERSION     WP_175811313.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26288
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkvlvavkrv vdanvkvgvk sdrtgvdian vkmsmnpfde iaveeavrlk eagvvtevia
       61 vsvgvvqaqe tlrtalaiga drailvesnd gveplgvaki lkalvdkeqp qlvilgkqai
      121 dddsnqtgqm laalaglpqa tfaskvtiad gratverevd ggaetlslql pavittdlrl
      181 nepryvtlpn imkakkkpld ivtpgdlgvd vtprlkvlkv neppkraagm kvpdvqtlva
      241 klkteakvl
//
LOCUS       WP_175811343             958 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia contaminans].
ACCESSION   WP_175811343
VERSION     WP_175811343.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 958)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..958
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..958
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=104183
     Region          42..957
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mknhglsrrg flkasvlagv avyvaplgsr afaalfeekl ltpvkwdsvt gvpqfridgi
       61 akvtgskvfa rdvraadmph wpqqqshali lrvtqadrty egfdlsllgd dlkpdrvvta
      121 ddlvrdgvaf ptfygddmll pagktpaylg havailiyhd farfrfakna lkfrddviry
      181 gavtgplerd pwgtfryvrv ggktaydddv ysslkdapif psmmrkhlpv wpdgkehgkl
      241 deqgmflagq ianeldhpsa dwlvfdreyn tqsvdtsale pdnancwyda atqslhlvvp
      301 tqsplevaen aaamvakcrf pvkklfvhpc ytvgygskdh fnvpfyglvc alyadgrpvr
      361 fandryeqfq tslkrhafkm hyriavdrnt gllqsfkgdf eangggrsnf spsvamvgat
      421 aaqsiyyfpk sdlaavaias raidagsarg ygtlqsmaat emavdeiaaq lnidpidfrl
      481 rnalrsgmkn tqgaipagal rvdevlersk qhplwtrraa rkaeyeaanp gkrygvgfac
      541 vqkdfgtgae asfakvefde ngkvslqhta aeigtgmsts qavavakwlg rpatdvrvav
      601 tewpdlpvet sgdpyimsqa dqdrlsanpr wspsyaspss atnsayyfth streaaravf
      661 ryglwpaams iwtrglgggq aapytiried arwvdgklta dgleplsfeq lakqayalgl
      721 ptgavvhvfn rwqwtdaefe vggtverlpi dglslrvgap rtgdngpvpg taapagatam
      781 rgtlaptang yrvldrkrvf ipptsrnnaa vtyytavgtl velavheatg kvdllthhsi
      841 mecgnqispq lvsgqlqggl amgighalhe ylplyedgpg ngtwnfnryq lprasdvavw
      901 tqtgdvlppl setdppkgva evvmipvvga ivngiahaig hrftdlpvtp qkiqevla
//
LOCUS       WP_175811396             473 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia contaminans].
ACCESSION   WP_175811396
VERSION     WP_175811396.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..473
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=50931
     Region          83..470
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mtarpafpsp daagtpapra psrllrraaf vlgaavigyg afaiafparv paaigtvvad
       61 wtganphpvv lqrpaaqpls avaqlgralf adpslsasgk qscaschspd haygppnald
      121 vqpgglamtq qgyrpppslm ylyrqpnfsi gpdagendaa psvaqqaasa agvvkaqkva
      181 gtsaapqlvp qggmfwdgra dtlqqqafgp llnpvemana svddvarkla qsshraqfeq
      241 lfgarvfstp qlavseamfa iaryqvedps fhpydskydr wlegrarltq aelrglrlfn
      301 dpdkancagc hlskpgkdgl ppmftdyqye algaprnral aqnrnpafyd lgvcgpfrdd
      361 lkdqtqycgm fltptlrnsa trhvffhngv fhtldqvmaf ynersiapqk fysrgadgkv
      421 deyddippky ranvdvtdap fdrkpgdkpa mtaqdindie aflgtlsdep vrh
//
LOCUS       WP_175811394             293 aa            linear   BCT 11-JAN-2025
DEFINITION  PilZ domain-containing protein [Burkholderia contaminans].
ACCESSION   WP_175811394
VERSION     WP_175811394.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..293
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30688
     Region          175..280
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mrlstdyvpl trddlaagvp lgfdlydadg aallpagttl hdaaqhaflf dhfrpvrrrd
       61 daeaaaeprm pdavphslrm glspgasigi rrrvgttrgl qrcrligiaa sgalfvepqp
      121 vaaldfargd dieavaigra avsrfgatve svqaagaaqy lvlsppgfvd rlrsraeprv
      181 pvriaaccag gsegaegigm vrdisvsgls iavdrpiaai geplrvqlpy aagdrvella
      241 ldgtvravha dpaapaltlh haafgetgad dlirlkallf drlmvssdtg rrr
//
LOCUS       WP_175811405             727 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia contaminans].
ACCESSION   WP_175811405
VERSION     WP_175811405.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..727
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79379
     Region          39..722
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mkpqpaierp sieparwrtw ldplgdaard waasdgliwl hlaktvfaal lamgiamrle
       61 msqprtamtt vfvlmqplsg mvfaksfyrv lgtaaglvaa lalgglfaqq pelymagitl
      121 wigtcialav rnrhfrwygf vlagytaali glpavmtpqt lfqsaltraa evalgiacsg
      181 avsalilpls sakalmrslg trhatfaaft agalagdvar gdferrfadf vddivgfean
      241 rafasfedph irarsrrlar lnsefmnact rlhalhqlvk rlrangsdav ldalaphvda
      301 laqrfaalrd erqrgiapas gallelrhfh salpkaaras rrdieahaag glldfdtaie
      361 llyrfigeyl gyadtyasld qddhafersv thyavktnsf fvgfaflrti vavgamsafw
      421 iasewpsgpl aviataiaca lsstsprapk fvaqmgvgaa fatavgyvfl cyvypniegf
      481 pllcaalapv lglgaflamr pglsgygigf avffcllagp dnaiaytpev linnglaivi
      541 amlacslvfa vvfpahmpwl tgriahdlrr qvtlacegpt erlaqrfqss thdlmaqlrt
      601 llvrrtrqhr dalrwmlstl evghavidlr delnafcesk ppqtlrwtgs idavlhelpr
      661 ffddptpghh artlksvnla iraaqhtlqa wyavpnerhr mqrivgclhf mrsalldkda
      721 pfnrhrh
//
LOCUS       WP_175811520             551 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia contaminans].
ACCESSION   WP_175811520
VERSION     WP_175811520.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..551
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=60170
     Region          1..537
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mtrsfdyvvv gagsagcvla nrlsdggrht vclleagpad kymwihvpig ygktmfhpvy
       61 nwgfhtdpdp nmhnrrlywp rgrtlggcss ingliyvrgq qqdydhwaal gnrgwswrec
      121 lpyfrklehn tlgegptrgt ggplwasair qrhelvdafv aasnrlgvrt vddfntgdqe
      181 gvgyyqlttr nglrcstava ylkpargrpn lhvetdaqal kvlfdgaqas gvryvqhgkm
      241 hevralrevi laagalqspq llqvsgvgpa allnrhgipv vadragvgen lqdhlqirli
      301 yevtkpittn delqswagra kmglqwalfr ggplaiginq ggmfcralpd esatpdiqfh
      361 fstlsadsag gsvhpfpgct ysicqlrpes rgtvrirtdd ardapsiqpn yldterdrrt
      421 tvagvrfarr vaatepmapl mkrevrpgad aqtddellef creygqtifh psgtvkmgva
      481 sdslavvder lrvygtrglr vvdcsimptl vsgntnvpiv mvaekasdmi ledaraadrg
      541 rsvapaaeal a
//
LOCUS       WP_175811527             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia contaminans].
ACCESSION   WP_175811527
VERSION     WP_175811527.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46977
     Region          28..433
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(39..40,43..44,47,86,144..145,147..149,152,172,
                     175..176,179,261,264..265,268..270,273,301,305,358..359,
                     363,367,383,386..387,390..391,394)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mqtrstldeh atiaasaper takhyllagw asmagttiew ydfflygtaa alvfnriffp
       61 sldpvvgtla afgtfavgfi grpmggivfg hfgdrigrks mlmitlllmg vpsmiiglip
      121 sydsigywaa alliamrflq gmavggewgg avlmavehap kgrkglfgsl pqtgvglgli
      181 lssvamaava alpeadmlsw gwrvpflasi alvglgwfir akvpespdfe kmqrqdkaek
      241 spvtaalrrh prevltivga raaentwfym vvtfalayat qqlhlpkaem lhaitagaal
      301 slvtmplcgh lsdrigqrrm faiglvlmca faapffmmlg tqqtsyawwa ivlglgvvfp
      361 ilyapesllf aqqfpaeiry sgislsvqla gvigggfapm iatsllkagg gqphyviayl
      421 vgfgvfalmc talmrpara
//
LOCUS       WP_175811589             482 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia contaminans].
ACCESSION   WP_175811589
VERSION     WP_175811589.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..482
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48382
     Region          21..421
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(28..29,32..33,36,68,118..119,121..123,126,148,
                     151..152,155,287,290..291,294..296,299,327,331,383..384,
                     388,392,408,411..412,415..416,419)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mdttaptpaf psalarvvat vstgfvvtql dvtivniala hlagdlhlpv aglqwvvday
       61 tlafavlmls ggalgdrfga rrlyitglvl falaslacga asapamliaa ralqgvgaaa
      121 mlpnslalln dacrhdphlr aravgrwtaa gsisiaagpv vggvliaawg wrgiflvnlp
      181 lcaaglaaal awiparraaa apaapsgsir aldlrgqfia iamlaaltga viewrplgft
      241 hpvvaggfal aavaalafva veartatpml plslfrhrtf saavlfgicv nltyygtvfv
      301 lalylqrarg esalqaglaf lpltggflls nlasgrvvar hgprapmlag alvaalgygs
      361 lhfidastpl aallvpflli ptgmgfavpa mttavlasva peragiasav lntarqagga
      421 mgvaafgala ggggagqvvd glrietavsv allitaalla trvrpdahrg apsarqavaa
      481 ad
//
LOCUS       WP_175811601             170 aa            linear   BCT 11-JAN-2025
DEFINITION  chemotaxis protein CheW [Burkholderia contaminans].
ACCESSION   WP_175811601
VERSION     WP_175811601.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..170
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=18089
     Region          14..152
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mtradpqnga halflmfeld geryaldaag idevlplavt kavpgapewi agllmrggqs
       61 vpvidvpmla lgrrahalrs trlvmvryra deaggertig liveratqtm ridraafrss
      121 gistartrwl gpvantpdgv vqqvsvsdlv ddvarlylfd glpghggesa
//
LOCUS       WP_175811626             356 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia contaminans].
ACCESSION   WP_175811626
VERSION     WP_175811626.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..356
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38525
     Region          26..265
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mttplptrlp pllrnalrpl ldpyrryrha klihaarvsl ailvsialst glnvphgews
       61 titvlivvgg lqhhgnirkk aaeralgtsi galaglglil lysflhapfa iyllmaigcg
      121 icayhaigka gyiallsait mvivaghgdn eivdglwrav nvlvgiaial afsfalplya
      181 tyswryklad alracaavha rlagdrqvsd dahlkemaal sallvqlrsl mpsvskecdi
      241 pvtqleaiqr glrlcigyle ilssavpard dlaareymri emktvnrrir dtlvgasral
      301 kfgtpsrlsp rrqpvdpphd apppqlsgyv sitaklagev dqlreklldt aqswni
//
LOCUS       WP_175811650             326 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia contaminans].
ACCESSION   WP_175811650
VERSION     WP_175811650.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 326)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..326
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34797
     Region          38..319
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mrppsrpltt dgvpaslaqp dapaatptrt aaagraprat wrahaplwlm capafalfaa
       61 lvlvplamtl vltfyrfdpa tgaiaafqfg nyaevlgssy fhtiflrtfg iaalttaicv
      121 aigtpeayvl skmrdpwrsl fllailapll vsvvvrafgw smllntsgvv nqalglvglg
      181 pykleyttfa ivialvhvml pfmvipvwta lqrldpqteh aalslgaspf ttlrrivlpq
      241 lmpgvlsgsl mvfglsasaf aipgllggrr lkvaatavyd eflgslnwpl gatiavlllv
      301 anlvvmltyy rvlerryars lggasr
//
LOCUS       WP_175811656             324 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175811656
VERSION     WP_175811656.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12168323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..324
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34633
     Region          22..200
                     /region_name="AraC_binding_2"
                     /note="AraC-binding-like domain; pfam14525"
                     /db_xref="CDD:434015"
     Region          251..322
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdialsrhap nrlgtlhapd everavahrl gphrmaargl dpfhaelyev plhhgallel
       61 cygretridf gddaehflfr ltlagacdlq agsvvaragp geltvsspal asrlstspdc
      121 rnlvlrlerg alerklqdml qatltrplqf dlaaggagag aalllptfey lcrlgaqpgi
      181 gtaattfgad lttwlmslll thlphsysda ltrgtpplpa hvrracdhvd ahlgeplala
      241 alaavagvap rtlqhafraf lhttpaayvr drrlaavhaa lqrgdarsvt dvliahgihg
      301 fghfakayar ryghapsita rqpr
//
LOCUS       WP_175811664             374 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Burkholderia contaminans].
ACCESSION   WP_175811664
VERSION     WP_175811664.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..374
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37612
     Region          18..373
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mtgfidtftl ggpgpttaik dtidiagypt raasralada ppamqhadvv rllldagwqi
       61 agkanmhela fgmtgindyt gtpvnpqdat ripggsssgs aslvglgmvd aalgtdtggs
      121 irgpaaccgv aglkptfgrv srrgvapaet tldcvgpfar dirtlvavma aiapgfdraq
      181 asasaagrtv ahvtvdadpa iaaaldaavr asgmhahavv ldempasfva gltvinaets
      241 rafghlvetg klgadldarl raaattapaa lkeaeavrar ftaqvdaale hadvlvlptl
      301 palpitlqqa rdgvsviams slirpfnlsg hpalslplpl agsplkaglq iigrkgadeh
      361 vcaiaahfea alas
//
LOCUS       WP_175811732             163 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia
            contaminans].
ACCESSION   WP_175811732
VERSION     WP_175811732.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..163
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17885
     Region          4..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 magitlddld lrilailqdd asvsnlklae ralsspptcm rrvrrlteag virrqvavld
       61 pvaigtavta lieisldrqt aedydafeay vcaepavtqc yrvspgpdfv vvadladvae
      121 ydefarrlft gasnvrnvrt ffsthrakfe anarvthamr kra
//
LOCUS       WP_175811754             442 aa            linear   BCT 11-JAN-2025
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Burkholderia contaminans].
ACCESSION   WP_175811754
VERSION     WP_175811754.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..442
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=47450
     Region          71..440
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 malgehlrqq laakalkrql eratdaaaap gvpgtlaaqt asarsrfesm pqyqqvrimr
       61 emgeklrvds pffrvhegva gattqiggre ylnfanynyl glagdpavss rakaaidryg
      121 tsasasrmva gerpvqrdle ralaafyetd dcvafvsgha tnvtvigalf gpgdlvvhds
      181 lahnsivqga qlsgakrlsf ahndwqalde llsrvrreyr hvliaiegly smdgdfpdlq
      241 rfvdvktrhg afllvdeahs lgvlgatgkg irehcgvapd qvdmwmgtms ktlagcggfi
      301 agcqplvdml rhlapgflys vglaptlaea slaalerlqa epervaqlqa rgrqfltear
      361 aaglntgtsa gfavvpvitg sslkaaqwan amfdeginvq pifypaveek sarlrffics
      421 thepeqisrt vavlsrlagr sa
//
LOCUS       WP_175811779             141 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Burkholderia contaminans].
ACCESSION   WP_175811779
VERSION     WP_175811779.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..141
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14873
     Region          23..117
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(45,48)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mlpagidpaa fnafdmqald agtfdaaigg agdalavvff wgvdcfncei akkamlaqpd
       61 airaldlkwf hcnvyehhql grrfglhgvp twfffhrgkr lgratgwhgl aqfqaavsaa
      121 rakiaasggd psgsdplags d
//
LOCUS       WP_175811786             517 aa            linear   BCT 11-JAN-2025
DEFINITION  S41 family peptidase [Burkholderia contaminans].
ACCESSION   WP_175811786
VERSION     WP_175811786.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..517
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55202
     Region          69..433
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mmpstrvvlr lavcaavtat llpcvssvga qqpasappas aasapaaspa kaqppspcpp
       61 dwepqicelk aavellkkqh ltdidigall datthagikt lpyarffdak eeqerrdder
      121 rardgtpgig ivfetrpdgl hivdvtpdap aekagvrpdd lvvamndtsi vgidaadlak
      181 lakgdagvpl kltvqrgpsh avlsfapvrt ilkphpatak rldgdilytr lssfpepavg
      241 dyvdavqaar ragppvkgvi ldlringgga lnaaigital fagrdrtamv tvergdanrr
      301 ryttnwpdye lpvmhgqdpl aplladdwwr tvplvvlvdg qsasaaeata aalkdlgrak
      361 llgmptygkg laqtgvdlid gtrlnftyar nlrpngcpmd gygvvpdwlv pprrdsdvdg
      421 vllwyreadl arapyadrla pdpfakvrke rqklreqral akidtaksaa lpqrefgtat
      481 dwqldqalaa lagrpvrtve arpqlmpaqp vceragn
//
LOCUS       WP_175811807             274 aa            linear   BCT 11-JAN-2025
DEFINITION  SH3 domain-containing protein [Burkholderia contaminans].
ACCESSION   WP_175811807
VERSION     WP_175811807.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..274
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27436
     Region          7..96
                     /region_name="YraI"
                     /note="Uncharacterized conserved protein YraI [Function
                     unknown]; COG4991"
                     /db_xref="CDD:444015"
ORIGIN      
        1 mrntivrglc vallgaavap givqaqstgy tnspaelfag papdypvvaq ippgtaldvf
       61 gclsdytwcd valpgvrgwi daqlidypyq ggyaplieyg aiigvpitgf aigaywdryy
      121 rhrpwfhdrd rwehraeprl gpggrppgqg rpqpggppqa apggpppvhd arpsaarggw
      181 ngairtpppa apapmpgaag nprpaapppa avmrpppapg gegrsmpvpv hpgggggggg
      241 gyggarpqgg gngggshggg ggggggggpe efrh
//
LOCUS       WP_175811822             309 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175811822
VERSION     WP_175811822.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34613
     Region          7..>143
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrflsieaf vrvaeassfa eaarqlgvts svvtnriqql ekfvnaplfh rstrhvrlse
       61 vgeafyreca evvgrvnelt dqmrelratp tgrlriqmlp gfaldhfgap lmefnrrypg
      121 iqldvivndr vvdpveegfd iafqifppis eslierrlft vrrlfcaspa yldahgapqh
      181 phdllqhtta lysgypsrnr wtmtrgdevv emelpgmirs nsvhllreya lsgggvvclp
      241 tlvaseglva grlvpiltdf qlaplsfaav ypatqrqalk vkalveflae tigdespwdr
      301 pllergwvr
//
LOCUS       WP_175811823             390 aa            linear   BCT 11-JAN-2025
DEFINITION  polysaccharide biosynthesis/export family protein [Burkholderia
            contaminans].
ACCESSION   WP_175811823
VERSION     WP_175811823.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..390
                     /product="polysaccharide biosynthesis/export family
                     protein"
                     /GO_function="GO:0015159 - polysaccharide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0015774 - polysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41352
     Region          84..255
                     /region_name="Wza"
                     /note="Periplasmic protein Wza involved in polysaccharide
                     export, contains SLBB domain of the beta-grasp fold [Cell
                     wall/membrane/envelope biogenesis]; COG1596"
                     /db_xref="CDD:441204"
ORIGIN      
        1 msrvrmnalc vsiiggaall agcagaipts gpsrsqidda gqapnatgiq vvdvtddvar
       61 kllaerthsd fsaalgngta fqrqlgvgdt ievsiweapp atlfgaaqsd aktgvgsgah
      121 atvlpdqmid gdgnvsvpfi glvraagrtp tqlqreimer lkymahdpqv lvklsrnvts
      181 yvtvvgdvan snrmqltarg ervldalasa ggvrqaidki tiqvtrgdkv vslpletvir
      241 dprqnvplha gdvvtalfqp ysftslgatg knqefnfeaq gitlaqalar agglqdsrsd
      301 prgvfifrle nasalqwpnv pvrttadgkv pvvyrvnlkd pnsffvaqsf midnkdllyv
      361 snapvteiqk vlnlvfsvay pvvtgvqtfk
//
LOCUS       WP_175811839             318 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175811839
VERSION     WP_175811839.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..318
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34751
     Region          35..186
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <147..296
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 msfeplftds gdrmqrrmve lhtrlapneg dtlaaidgvr firvsrpapr mpvlyepsii
       61 vvcqgrklgy lgersfvyda qqylvlsvpl pfecetfasq depflaisir vdlaviaela
      121 illdetlgaa vseplgvyst pldapladav lrllealasp hdtrvlgpai mreiayrvlt
      181 geqgdairaa lvqqhhfgri akalrrihad ltadldvetl areagmslav fhaqfkhvta
      241 tspmqyvkaa rlhqarlmmv qdgvgagaaa arvgyasasq fsrefkrlfg rspgdevrwm
      301 resgsrpvgd raaidltt
//
LOCUS       WP_175811842             177 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia contaminans].
ACCESSION   WP_175811842
VERSION     WP_175811842.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..177
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=17795
     Region          1..177
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mkkailstvv aaasiaafap aahaadglie ftgaltsatc kvnggekdft vtlptvstst
       61 latagswagr qafklaltec qpntgvvsay lepgptvdmt tgnlkldtgg atnvqialln
      121 gnydkinaag tngsqgvdkv nisagkadlq fyaqyqslgg atagaaksrv nytiayq
//
LOCUS       WP_175811866             262 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia contaminans].
ACCESSION   WP_175811866
VERSION     WP_175811866.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..262
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=27410
     Region          10..243
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mdrrkplvgi tadhtqigah ashtvgdkyv aaivdgaqaf amvlpalger qsvddvldtv
       61 dgllftgsys nvephrygge psapgtkhdp ardattlpll raaiaagvpv lavcrgfqel
      121 nvvcggtlhq rvhevpglad hredddapmd tqygpahvvr ltpggrlhal aggrdevhvn
      181 slhkqgiaql gsglaveava pdglieavsv vdapafalav qwhpewrhaq dplssaifra
      241 fgdacrarra artramaaaa la
//
LOCUS       WP_175811877             548 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Burkholderia contaminans].
ACCESSION   WP_175811877
VERSION     WP_175811877.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..548
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58373
     Region          13..529
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 maaatptgal valhhvsfrf ddgftlfdsl dlsidrtptg ivgrngigks qlaqliagcc
       61 apsagtierh tsvvyvaqqh ddgdvsagpr tvaqiaaldg plgalarlad graephdfdl
      121 igdrwdlaer lrtaldaagl hdvradtpaq alsggqlarv aligallsga gllvldeptn
      181 hldapgrawl raaldgwrgg vvivshdral lagvqrivel tpqgvrsygg nyalyraqrd
      241 aeqdaaqsal dnaraergrv rrrleqehdt iqrhaaaslr daksanlssm akqsrkgaar
      301 simgtvrrhq nefkatlder vqeaaarvea dapvlvslps tevsarrqlf tlerahlpwr
      361 iagaadaitw sasgpvrial tgpngcgkst llrmlagele prsgactthv saayldqrla
      421 lldldrsive qlglldtpla egdlrsrlal lqldavratq parqlsgger lkaalacalw
      481 rgtpaqllll deptnhldle svraieaala gfpgaivvas hdpaflaald pthtmqwhrd
      541 gwryepva
//
LOCUS       WP_175811891             191 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Burkholderia contaminans].
ACCESSION   WP_175811891
VERSION     WP_175811891.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..191
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=20475
     Region          4..135
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(9,11,72..73,76)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            11
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(71,116..117,119..120,124)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(77,82..83,112,115..116,119..120,123,126)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(101..103,112..113,116..117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(101,117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(125,131..132)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          147..188
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
     Site            order(148..150,182..183,185..187)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 msrtfayarv stsdqttanq lreieaagfs vdkrrvvses isgsvsadqr pgfaqllvkm
       61 eegdvlivtk ldrlgrnamd vratveglae rgirvhclal ggvdltsaag rmtmqvlnav
      121 aeferdllie rthagiarak aegkamgrps alsdeqradv mreldagasv aalarrfgts
      181 rqtimrvrda a
//
LOCUS       WP_175811916             531 aa            linear   BCT 11-JAN-2025
DEFINITION  MDR family MFS transporter [Burkholderia contaminans].
ACCESSION   WP_175811916
VERSION     WP_175811916.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..531
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56730
     Region          33..425
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(34..35,38..39,42,73,123..124,126..128,131,152,
                     155..156,159,285,288..289,292..294,297,325,329,382..383,
                     387,391,407,410..411,414..415,418)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mavhtaahhs sgqvlpfres llamigisfv tmlvaldqtv vgtalptiva elrgfdlyaw
       61 vatsyllssv itvpifgrlg dyygrkpfvi vsivvftgas vlcgmandml mlvlarglqg
      121 igggmlvgta facipdlfpd svvrlrwqvl mssafgiana vgpslggvlt qsfgwrsvfy
      181 vnlpvgllsl lfvwrylphl rhiehdrkmr ldwpgallia lslgalqlfv ewlpkygvas
      241 waslllvvav aagfglwhwe krcaqpilpf dmfgnralsa lfvlailagf smfsllfyap
      301 llfqggfgms pkeaglvitp lvvfitigsi mngrvvtrir npnamlhvgf vlfaitcagi
      361 vvsthttpkw vlmalmvagg iglgfvlpnl tvfaqqtagr ehlgiatall qslrmvggmi
      421 gtaltgtlvn qmysggvrda lsadhamqwh aqladpqili draaqgglva eltraghnga
      481 llleaaresl vgaihlgvam aavvavvsvw qcrrvppial rhkiephvaa d
//
LOCUS       WP_175811919             115 aa            linear   BCT 11-JAN-2025
DEFINITION  FmdB family zinc ribbon protein [Burkholderia contaminans].
ACCESSION   WP_175811919
VERSION     WP_175811919.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..115
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11079
     Region          1..76
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 mpiyayrcea cgfakdvlqk msdaplsqcp ecgkdafrkq vtaagfqlkg sgwyvtdfrg
       61 gsggtsapat asgdaaptga teaapaaaap aassssestt tsaapapaaa paass
//
LOCUS       WP_175811927             416 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia contaminans].
ACCESSION   WP_175811927
VERSION     WP_175811927.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..416
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43443
     Region          23..409
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtgdrvmaiv gaghaggraa qvlresgwgg rivligaeah lpyerpplsk gvltgersaa
       61 qcrlrdpeaw aadriepvva tveridpgar evrvsdggvf gydalllatg grarrlaipg
      121 atldgvfalr tlddaaalgt rlvpdarvvl igggfiglev aasarlrgcs vtvldaasrl
      181 lgravpeaia arvhalherq gvairvkrkp vaiertagga lavvlddgdt liadtvvagi
      241 giepadelar eagltvergi vvnerletsa rgiyaagdva vfpsvlsgrl vrqetwhgae
      301 tqarvaarnm lgagepyret pwfwsdqfda qlqvagepal geravarvlg ddaeihfhfd
      361 agarlvaasg fgrasgfvkd mrmarmlver gadvtpaava dvnvklksli geaggr
//
LOCUS       WP_175811997             555 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia contaminans].
ACCESSION   WP_175811997
VERSION     WP_175811997.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..555
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60193
     Region          1..550
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mhvsatpaap vtvftarril tmnpaqpsat hvavrdgril avgdaadaat wharfgactt
       61 ddtlrdkvlm pglveghchl megamwdavy vgyydrrgpd gtlwpglrsl davlerlaea
      121 eramtddgpl lawgfdpiff gtarltarel drvsaqrpia ilhasvhlmn vnsvmlarag
      181 idedtdidgv trdadgrptg elqefaamlp vyqtiggkla isasekphav wnfgrvaqla
      241 gvttatdlvn dlsadgnrtl hdvtadpdyp vrivpafapq rnparsadsv raeierntdk
      301 lhfgpvkfiv dgsiqgftar vrwpgyaggq pnglwlippv qlvdvfepfh raglqlhvht
      361 ngdeatdvvl damttllarh prpdhrhtlq hcqmadaaql krvralgmcv nffanhlyyw
      421 gdahydqtig pdrasrmdaa gsaqrlgipf alhsdapitp lnplftawca vqretasgrv
      481 lgegerlsvd dalhaitlga aytlrmdhlv gsieigkfad favldddpsv saparlkela
      541 vwgtvlggrv frspr
//
LOCUS       WP_175812051             211 aa            linear   BCT 11-JAN-2025
DEFINITION  DsbA family oxidoreductase [Burkholderia contaminans].
ACCESSION   WP_175812051
VERSION     WP_175812051.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..211
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22670
     Region          3..203
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(11,14)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 mqidlyteit cpwcivghhr ldkvlaerfp nlavdirqhp vlllpdapag glhipdllrs
       61 rygitdpkia ftrpereara sgfdldlgrq lrayptqaah avilaaagld tqhrlavais
      121 hayfiaakni adadvladia adygfdrdqa raialdpeqh rrveaeafks anagvrsvph
      181 fvfggsiain ggrsedeiaa aiqaasgvis l
//
LOCUS       WP_175812063             472 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia contaminans].
ACCESSION   WP_175812063
VERSION     WP_175812063.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..472
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=48489
     Region          6..466
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 msalpdraaq rhalaatlgd gwldgaspda cssyetdvtl hggialgiar pastadasal
       61 arvavahria lvaqgartgl vgaaipdrsg tqcvvsfdrm ravrafdaan rsitveagvr
      121 lsdinrvaae aglclpidlg sdpvagglvg anaggsrlik ygdvrrnvlg veavladaag
      181 tvidalaplr krnagfdvtq cfigangang lvtavsfala plersscaaf vafasydaal
      241 aglvaferaf gemlsafefm saaavgcvaa aypasripfq adaaacyalv eiatgmpgld
      301 alleertiat ldtlasehvv ldaacapaer fwrirdalpd avaqdgipls fdvsfprgal
      361 aafvadaeqw iaaahpslrc hafghfgdgg chlvvsipha sadrygplqq valrgalydr
      421 vvraggcfsa ehgvgpvnva yyrkhvpaaq rqvaaaiqha vdplglvgrv ry
//
LOCUS       WP_175812081             218 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia contaminans].
ACCESSION   WP_175812081
VERSION     WP_175812081.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..218
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22686
     Region          115..216
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(118..119,152..153,156,160..161,164,206,210)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mknihlalla svvslaacss asgptynaye lqprdgirtf rvdchgilss antcmkvatr
       61 mcgneavrrv dsttpyrdga dphsivfqcg aapapvaaaa apaavekvsl tgdayfatds
      121 avltsaataa ldtllnqqgd rhfsrvevdg ytdatgsdah nqalskrrad avagylrehg
      181 lkadsieaag hgetspaasn etaegrarnr rveislqk
//
LOCUS       WP_175812085             424 aa            linear   BCT 11-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Burkholderia
            contaminans].
ACCESSION   WP_175812085
VERSION     WP_175812085.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..424
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44782
     Region          1..407
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mknhltlsia vgmilgvvag ylchthiadp gtlktiagdf sivtdiflrv ikmiiaplvf
       61 vtlvsglagm dsgedvgrig lrsigwfvca slmslslglv manalqpgag lnltatagev
      121 ntglntaaln ardvithafp tslldamarn dilqilvfsl flgvalsalk hdkrvgvviq
      181 sidgmvpvml rltnyvmraa plgvfgaias svtlrgldvi ytygkligaf ylgllvlwml
      241 ligagyaflg rrvvsllkav repaliafst asseaayprl teqlerfgvd kkvvgftlpl
      301 gyafnldgsm myqafaaifi aqafgvhmpl seqvfmllvl mlsskgmasv prgsvvvvaa
      361 vapmfhlpva gvamvlaidq ildmgrtmtn vignsvatav iakwegrraa kpegavfdrp
      421 elna
//
LOCUS       WP_175812122             730 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia contaminans].
ACCESSION   WP_175812122
VERSION     WP_175812122.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 730)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..730
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78245
     Region          51..730
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mvtgtgaarr aravaagsaw vmaaaggaha qasgaaatpp agaaaavlpa idvtgkgdra
       61 ssglvglrtt agtktdtpva eipqtinlvt aqqiemtgat dlnqalryvp gfatfgadsr
      121 tdwyaalrgf tptlyvdgva apntavianw rvdpytidsi avlrgptsvl ygagepgaiv
      181 dahtkladge rvreagvqig ndarkqvmld igdaldpdgr yayrfvgvar dgnavtgpng
      241 drrvalapsf rwrpnadtsl tlsatflqds sdissnflpa sgtvlpnpng rlsqdiymga
      301 pgfndyrkkq wslgyalehr vnaiwslhqd vrwshlsldd atvfgigfmp rssttmmrya
      361 glfqlnysrf didnhaqarf gtgplehtll lgaqydrqtt tnsvwlalap slnlyrpvyr
      421 pvtdaifsgp tslghvdqyt amnvfgvyaq dqirwkrwtl tlggredfvn arfddrtagt
      481 qaqqdvsafs grvgltyqgd aglspyvsys tsfdpvigvr mygggmpkpt rgkqseaglr
      541 wqppgknlll saavyqidqt nvatptpvsl dptgttsvqt gkvrsrgiel savgkvtrel
      601 svvasyvyqd vknvqandas lnnwpvavpl prqmasmwad wtwrtgalsg lgigggvryq
      661 sasagapdns ltvpsvtlvd lalhyemphw rfalnvanlf drryvsgcqs yavcvfgner
      721 tvlatakydw
//
LOCUS       WP_175812101             315 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175812101
VERSION     WP_175812101.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..315
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34129
     Region          2..315
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhrigffvcr gydaldlggp lsafnqvata aghapydlhv isqpggpvpg ntglsvdtkp
       61 igrrtfdtvi fvggdidpmq tpeniaaark lgaraarvas vctgafllge tglldglrat
      121 thwryaarlq srfprakveg dsiyieegri wtsagiasgi dlalgmierd mgaevaravs
      181 rllvvpyrrp ggqsqfstms qmepesdrir ialnfarehl aealpverla eaaslslrqf
      241 grafrretge tpakaverlr veaarlrlqg gsepieqial avgftdperm rrafiklhgh
      301 ppqairresr sngar
//
LOCUS       WP_175812133             319 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia contaminans].
ACCESSION   WP_175812133
VERSION     WP_175812133.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..319
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33522
     Region          66..290
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mnmkaglvvl svllaaglls acspvrllna ltpsytfslf agipygsger qvldvylptr
       61 vlhhwpadas agapvvvfly ggswqsgerk dylfvgeala srgfvavlpd yrtypattfp
      121 gfvddaaqav awarehavaf ggdprrlflm ghsagaqiaa llatdgryla aqamrksdia
      181 gviglagayd flplrdttle rifpqevraa sqpirfiqgt eppmwlatae ndtvvepgnt
      241 trfaralqqm gdtvvvmryg nvshasivgv lgaplrgmas vlddlsafvd gvakasnagt
      301 tgrpptspaa aprssvsaq
//
LOCUS       WP_175812187             789 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia contaminans].
ACCESSION   WP_175812187
VERSION     WP_175812187.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 789)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 789)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 789)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 789)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..789
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..789
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=85808
     Region          133..396
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
     Region          544..787
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mvstltrlsw rdlwrmraqa maavlvvacg vasfvamrst ylvllraqqd yyashrfadl
       61 fvhlkrapla aatriaalpg vaavdarvva dvtldvpgla epatghvvsv perggpsldl
      121 lhlqrgryva pgrddevlvs aafaeanqlr tgqrigavln grwkqlrivg iaispeyvye
      181 tgagsifpdn rhygvlwmgt eavsaafrmd gafndlvlsl dggaivprvi aqvdrelasy
      241 gglgtitred qvsnrfisde iaqnritaty vpaiffcvtm fllqnvlnrl vdtqrtqigl
      301 mkafgygnar valhyfqfac liaaagaaig yaaglalgss ltalyaryyr fahleyhvda
      361 hvailavvvs fatalvgtaa gvmkaarlmp veamraplpp dfaigwlerf glyrhlgvtw
      421 rmiarnitrq plkallscia macasailvt ggfffdavdy lfdvqfqrve rqdvtvafaq
      481 plshraiyal qrlpgvlrve pfrdvpvris agyrsrrvsl sgiapaalmh rlvddrslpl
      541 rvppdgivis srladtlavh agdqvtvevl egkrqsrqvt lagrvgelvg iraymdqqal
      601 arllgeggnw sgawlqidar vsdrlyaalk rmpavnavav rqsvidsfrk imnesvrlst
      661 sinftfacii afgvafngmr iayserlqql aslrvlgftr mevawillge qfllaalatp
      721 aglllgyrvc afladrlatd lyrlplvvqp atfaqaflvt astvaasgwl varkigsldi
      781 vavlkares
//
LOCUS       WP_175812284             390 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia
            contaminans].
ACCESSION   WP_175812284
VERSION     WP_175812284.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..390
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42493
     Region          83..338
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 misieelqri tdaplhswlg tlavsvivll vvtvvhrlga rivkriaqpy plmsailryi
       61 drpslvvlal laleflwvqa ddgmsfvrgm rtaaavgsii sltwllvrla agvgdaiiqa
      121 hpidtsdnlq arrihtqakv lvrtvmvliv iigtgaalmt fpnvrqvgas llasagvagl
      181 vagiaarpvl gnliaglqia ltqpirlddv vviqgewgri eeitgsfvsv rlwdqrrlvv
      241 plqwiienpf tnwtrsssei igtvylsvdy rtplaplree larlvhaape wdgrvqvlqv
      301 tdatertmql ralvsaadss scwdlrcrvr egliaylqgr ypqclprsrm elyphdsapd
      361 apnperphar qpaastaant aadpqaaegr
//
LOCUS       WP_175812296             327 aa            linear   BCT 11-JAN-2025
DEFINITION  thiamine pyrophosphate-dependent dehydrogenase E1 component subunit
            alpha [Burkholderia contaminans].
ACCESSION   WP_175812296
VERSION     WP_175812296.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..327
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=34601
     Region          6..327
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 mtastelsrd tlldayrlmr tirefeerlh vefatgeipg fvhlyageea savgtilhlg
       61 lddyvatthr ghghciakgv dvhgmmaeiy gkktgvchgk ggsmhiadla mgmlgangiv
      121 gaggplvcga alaakhrktg gvgvcffgdg asnqgvifes mnlasvwrlp aifvaenngy
      181 aeatssswsv atdniadran gfgmpgvivd gfdffavhea lgeaverarn gggptlvevk
      241 ftryfghfeg daqtyrapge vqklrdekdc lkhfetrvvr aealttadlr avdaqvkali
      301 ddavaqakaa pvpdaadllt dvyvsyp
//
LOCUS       WP_175812307             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175812307
VERSION     WP_175812307.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33531
     Region          <29..74
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          103..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(113,117,156,170,172,231,248,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(114..115,119..120,122..123,126,130,132..138,199,
                     225..229,236..237,240)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mtsdpipapd kpldlldval faraallanv taagrefgvs aavasariaq lerqlgarll
       61 hrttrrislt qdgevfmaha dtllaaadaa rasvghgrte pygrlkvsms ssfgrqhvap
      121 vipaflrryp svsldlrlsd eivdlvddgy dvairlgalk dstlvarkla tnrrvlccsp
      181 aylaehgtpr hpadlaqhec vilgdqrdws fatpqgpltv rvsgrlvasn geairealvd
      241 gfgiaikstw dvgpllasga lvtvlddypf aediaiwavy psrahvplkt lafiaflagh
      301 fgdppywdra dgq
//
LOCUS       WP_175812326             330 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Burkholderia
            contaminans].
ACCESSION   WP_175812326
VERSION     WP_175812326.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..330
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=37093
     Region          13..285
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mdslaatfde ireayalgri gqqrqvgerv whlptddggi avklyalehh araakeaavl
       61 ahferhgdar fhvqalkrtt sgaslwtdhg shamltrwet grfrtydtfs paewdalgas
      121 laalhlsleq lhlpqldtir arlmaidada vrrslhdald raranhatdd lrryvdlalr
      181 mldryypgsi dafpaddpqh pihndynqfn ylftgtlppl ildweasiga preyelvrcl
      241 nhlpleaphl aeafvlayrr trpvdparia wavdaacvqh alklwivqgw ldepsrfgsh
      301 lngavtmasa mvdardrlvd ffsrcveagr
//
LOCUS       WP_175812371             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175812371
VERSION     WP_175812371.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33821
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..294
                     /region_name="PBP2_CrgA_like_2"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08471"
                     /db_xref="CDD:176160"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176160"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176160"
ORIGIN      
        1 mdridamkvf vatldegsla gagrklgrsp aavsraiafl eehtgtally rttrtirlse
       61 ageryaaacr rilsdleead mlvadersap rglltvtapv aagedvlral ldefierhpa
      121 vsirlqlldr pvslidegmd valriahltd stlvaipvga vrrvvvaspd ylakhpaiet
      181 padlaqhrii smthfgldsw sfpppapsal pqvvqfaprf iintirgava saiaghgvtr
      241 lfsyhvaepv rdgtlrivlr dsehaplpih lvtpygrlav pkvrafvdfa aprlrehfar
      301 laaitdgdrt dgd
//
LOCUS       WP_175812405             422 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia contaminans].
ACCESSION   WP_175812405
VERSION     WP_175812405.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..422
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44768
     Region          <213..357
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mvksaatpda fapgraqria ralvpaavlg alaalgfaal pavsqlpgav dsgtaalpqr
       61 vlsdtpfpta qhfvtselar tigerndage rndrsqqpgl faplsahrne mlgyanlfqf
      121 aapenqhgmr agdieltlsd tlnrldvppe vriqlgdlvs gkvamrasaq rgdyyrvayd
      181 tnngtphlta lelrvagrtf gaiwfrapga ehgayyaldg spleaaaftm pvkwtrissf
      241 fgerihplsq amafhtgvdl aapsgtpvda aadgvvsfvg tdpggygryv ivdhadgyst
      301 yyahlsayar glkvgetvkq gqrigsvgmt gaatgphlhf evrvandpvd plvtlasaqt
      361 alsdmqltaf rqeakqwrfr lasinttpfa faqsdgplwg dfatgpstlr avfdthysae
      421 rg
//
LOCUS       WP_175812445             701 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia contaminans].
ACCESSION   WP_175812445
VERSION     WP_175812445.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..701
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75996
     Region          22..701
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 msrrnwaaap maivvgttgm gaadaqetsl ptieisaqra tapfrtrest satrseadvm
       61 eipfavssvd tkliqtvaat rgddlydwva gvsrqnnfgg lwdnyavrgf agdgntsgtd
      121 ylvngfswnr gmsvprdtvn lermevlkgp asalygrgdp ggiisyttkq pqftrantig
      181 vsagsygalr qtldstgpvt kslayrfvam nenngsfrdt vsskrylfsp sftwdigadt
      241 tlhyefesar qrapldrgvl avngqlgvip asrflgeprd gdydvrntgh qftlehrlds
      301 swsinagvaq rntdlsgrss eafalqpdgr tlwrryrqva fhsndlqgrv etagsfrtgg
      361 ightlvmgvd ayrfnydqfv trstpnaaap yaidifdpvy gqpaptprta tnllerddgq
      421 gvyaqdtlaf gphwkilagl rwdrfhqsid nrlkgvttsq lqtavsprig vvyemspaws
      481 fyantaysfr pnngadvggn afdpekghgy eagakwagar slttvsafyv tkrnvltadp
      541 anagfsraag evrsrgvefe wsgdlghglr gianfayvda evtrdtvlap gsrlvdvprl
      601 sgsallmyet tlpfadkaga gagviyvgrr agntantqdg felpayatvq lngylqvnkh
      661 lrasvvlnnl fnrttyvssy nslwvtpgap rslfaslays f
//
LOCUS       WP_175812424             426 aa            linear   BCT 11-JAN-2025
DEFINITION  NRAMP family divalent metal transporter [Burkholderia contaminans].
ACCESSION   WP_175812424
VERSION     WP_175812424.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..426
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45372
     Region          14..426
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 msvpgddpqp aaggaprtat pwyrrlgpgl lagasdadps niavyaqags qfgfnmlwmi
       61 vvtlpmmvav qlasafigrr nraglvaair ehfsdrlakt livmvaivnv vnvgadlaam
      121 gdatalvagg rsywyapfyg laslalqmtl syeryarwlk wmtlgliayv lelgfvqidw
      181 rgvmhaivlp qiefthayat ttvavlgttl spylfvwqaa leveetastq hdtrreterr
      241 itfdtwvgml vtnavsfcim vigaavffsh grhdigttaq aaealrpiag eaafvvfafg
      301 ivgcgllaip afagsaaygc aeawrfregl nepvrrapaf yavlalcviv giaicvspid
      361 pikalywsav lngiaavpml alvmllahrr eaagqpgsgi vskafgwlav almaasvvtm
      421 vvdllt
//
LOCUS       WP_175812471             316 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia contaminans].
ACCESSION   WP_175812471
VERSION     WP_175812471.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..316
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=32923
     Region          15..159
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          173..311
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mntgtspvqa vqapqrvlia idgsnasaha layakalvpa naavhivsva enprtlvplg
       61 skamaflesa rvellrdasd alsrakaamd rgdlaidtev idlaarggdi vhaltdsvqa
      121 wqaelliiga rqhhgllrwv egtvsgplgk lvpcpllivp egfasvaehl ptrmlfavdg
      181 samaldalrt gltfsrpdte fraiyvvdrp palgdfvlgg aledaligeg nhalqgatal
      241 ldgaaghaqs qliqtdrida dvsrlivrda iewnadmivm gthgrrgvtg wlvgsvagrv
      301 aritktplll vpapsa
//
LOCUS       WP_175812498             209 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            contaminans].
ACCESSION   WP_175812498
VERSION     WP_175812498.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..209
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22806
     Region          3..196
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mqrvraevrr qdlvaatvav iaehgvkgat trriaeaagc plaslhyvfh skdellfavy
       61 eslidlirsd speppehgtl sdlaefnlrs vmawfeanpt yaktqselyt walrhqpdma
      121 igalrisqeg aranltaaep radakaldai arltivlidg llfswfaqed skrlaadvdh
      181 askmlaayaa slsdarpaak tsrksvrkh
//
LOCUS       WP_175812508             182 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Burkholderia contaminans].
ACCESSION   WP_175812508
VERSION     WP_175812508.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..182
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19939
     Region          3..165
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtaaelsall pamlprlwtf alrisgdrhd aedlvqgacv ralerahqlr pgtaplswmf
       61 sivqsiwlne lrarsvrrrs gmdwdddlle tvadptaptl eqqaldaqiv ravqqlpeaq
      121 rvvmllvavk glsydeaaea lgvrigtims rlsrarqtig alfddgkerp mkgaakrvdq
      181 ga
//
LOCUS       WP_175812528             902 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            contaminans].
ACCESSION   WP_175812528
VERSION     WP_175812528.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 902)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 902)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..902
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..902
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=98499
     Region          14..820
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mdsrnlmqli rggliqqdrl lkldtslgnd vllphqmvge srlgrdfefv vdvvtadskv
       61 elkkliaqpa tlwiqqgtas yaphhgyvht arrlgadggl tfhqitiasw mhflrfrrdq
      121 kiwqdkpvda ivtdvfnahp qsrgfyefhl srslpslsfc rqdetdwnfv hrllesegly
      181 gywkhdsdgk ahrlvitdql taldearplt fsragttias daltqwsgtr tlqstslttr
      241 tfdyknpsga fnskgtsipt mpnqgelpdq aevyqytgay tflaqergda lskarieewe
      301 srskrffgig gwraadagkr ftldahpdhd sdpteqrefv aiaarwvvrn nlpitqssar
      361 mrlsldqqia esgiddldga ahasptaags tgayqveiea qrttvpfrsp fehtkptthl
      421 etaivvgpqn eevytdelnr ikvrfiwdri ndgnesascw vrvaqsdtgs gygavhpprv
      481 geevlidyvg gdcdrpiaia rvyngaakpq whtngllsgy rskefggagy nqmvmddstg
      541 qnrmqlfssq gnsalhlgyl inhtgnargd ylgagfdlrt dsygavranr glyvstypka
      601 vdsqpldare tqqqlvraes lleslsdast ahdaeslqag ydslkqltda tqesttgaas
      661 ggrtagggtg sanvfkepvm lfgspsgial sanetahlsa aqhvniisgq sthlavgksl
      721 iasvanklsi fvqsagmklf agrgkievqa hsdnieltaq ksvkvlstta kvevaadqel
      781 fltsggayir iangdiqiha pgkidikgss hsldgptaqg yvlpglphag dapryheqfh
      841 lidddgetvm phtryeiese sgkkwsgfsd adgftqhiyt dqpeslsltv ykeveddsge
      901 ea
//
LOCUS       WP_175812568             189 aa            linear   BCT 11-JAN-2025
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Burkholderia
            contaminans].
ACCESSION   WP_175812568
VERSION     WP_175812568.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..189
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=20548
     Region          43..182
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 mtsftesrag lpddplqags papdnapdph peptpsiaag fevrvqyapi dagaelapiv
       61 rnpnvgavvn flgvvrnegd vddvialeve hyptmteqal wsiveeasar wqletirivh
      121 rvgriqlgqa vvlvvvaaah rgsafdacef lmdflkthap fwkkeirhdg vsgwveakah
      181 ddqamrrwg
//
LOCUS       WP_175812087            1293 aa            linear   BCT 11-JAN-2025
DEFINITION  type I polyketide synthase [Burkholderia contaminans].
ACCESSION   WP_175812087
VERSION     WP_175812087.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1293)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 1293)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   3  (residues 1 to 1293)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   4  (residues 1 to 1293)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1293
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..1293
                     /product="type I polyketide synthase"
                     /EC_number="2.3.1.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=136470
     Region          6..1293
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
ORIGIN      
        1 mnqsntqaqr iaiigmscrf pggascassy wallnsgrta iretprerfd idafyspdtd
       61 epgttysrva gyvddpfrfd rklfrtsaae amemdpqqrw mlelgwaale nagiapgrlr
      121 grnvgvfmti geadygrrtv wsgdpsritt ysklgnlram apgrvahilg lsgpvifvdt
      181 tcssslvaih laaqslqage cdvaiaggvn lilgpeetig iarlqamsas gqcrpfdasa
      241 dgyirgeggg vivmkrhdda lahgdridvv ligsavnsdg asngltapng aaqeavirra
      301 mmragvrpea vayveahgtg talgdpiela alrnvyarav ardkpilvgs vksqlghleg
      361 aagmagfika mlilrhrhvp aqvnfdtpnp rfhwegaqva ipregtplge gktlvgvsgf
      421 gitgtnvhli lsaaapvsda vapierervl tlsgrspdar rrvaaawrdw lastsvplrd
      481 achtssvrrd hfdhrvalvg ttkadfigal dafladnpsg nwhagepprk prvaflvpgq
      541 gawqpgvggn fyhgnglfrk hadaclrlld aetardvlda ivgrsaqavr hhpgqlahfv
      601 vcyalartwm elgvqpdlli ghslgehvaa viggvmslgd glaaveargr lfdtatpaga
      661 mlavaaaade laarfafgtd lfvagingpg qtvvsgtqea varvhdamva agkrvsllkt
      721 ydtpghspml rsmreafrra lepltltpps ipivstltga vateaiagve hwldlveqpv
      781 rfhdallaas dgktlfvevg pgaalaklar aaaggdwqca iasladgpeg deeteaigfa
      841 hgcarlyseg qkiawhklyg napppaeapg ytfdterfel pfpdlaeagr gvvrqrsdaa
      901 sseaarlpds saadradavp agaaqmlatl rtiaaavapd tvvlddglsl vgqgldslal
      961 telrvrlhqr lgkmppiaml argaslhtla awfgamdgda pdrevvatdp rrtagsgsda
     1021 glvvtlregt gplvalvhpv ggnvlcyqel aaswpgdptv vairhpyadq ghapaylsit
     1081 elasryraal lsahgrqpdl lggwsfggiv ahemaaqwes egesapplmi vdsplhdgef
     1141 atrlralvad lapddgtqav erwladprfd amldqdfyla dvrrraqpam fdhiarlhaa
     1201 savalarhqp kqvqtrigya lavrdkrgms salaaqqlgr lgsggvtvsv fdddhnsivc
     1261 apsvsrlahf fgggrdadtp haepeplmra tpa
//
LOCUS       WP_175812633             475 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia contaminans].
ACCESSION   WP_175812633
VERSION     WP_175812633.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..475
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51291
     Region          42..460
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(52..53,56..57,60,100,150..151,153..155,158,178,
                     181..182,185,296,299..300,303..305,308,335,339,388..389,
                     393,397,413,416..417,420..421,424)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mastqpdpla aagaarpaii dpgsisarld rlpptrtvwk lvillslgff felydllysg
       61 yvapglvksg ilsatthglf gttgvasfia alfsglfigt iacgfladrf grraiftwsl
      121 lwytaanvvm afqdtaagln fwrfvvglgl gvemvtigty iselvpkqir grafaceqav
      181 gfvavpvvaf layllvphap fgldgwrwvv ligahgalfv wwirrelpes prwlaqqgrv
      241 eeadrimhal eakveaeygr plpppapaep vpprgsfrdm wvqpyrsrti mmtifnvfqt
      301 vgfygfanwv ptllikqgit itsslmyssv ialaapigpl iglviadrfe rksvivamaa
      361 aivvcgllfs qttvgafliv lgigltlasn imsysfhayq aelfptsira ravgfvysws
      421 rfsaifssfv iaavlkgfgt fgvfafiaga mvivmaaigf mgprtkgial esisk
//
LOCUS       WP_175812640             742 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia contaminans].
ACCESSION   WP_175812640
VERSION     WP_175812640.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..742
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=82040
     Region          48..715
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mnrfvpllrd awlrcrarvv pfaaacgarf ralgagalhr lrhptrrgva ltlaaipvlg
       61 llvllafvpf tpsigdirka ridrparvls adgqliaefr pvnrewvplk qisphmvdal
      121 iatedhrfyt hhgidlrrti aaglhtfsgd rqggstitqq larnlypdev graptltrkv
      181 kelitafkie svyskdeile tylntvpfly naygvemaar tyfgksadql divesatlvg
      241 mlkgnsyynp vlnperavqr rnivldrmaq mhmltpqqla klqrqplrvd fepqsgqpgl
      301 aphfavqlrk wliawadrnn ydlysdglvv rttldarlqd matqaltrqt erlqaiadga
      361 wrgpsgcglr ndlfrgfirq tpdyrqardt gltdvaalkr lganrdfmra lcerktqvqa
      421 gfvaidprng airawvgspd fgsepfdhvs qarrqpgstf kpfvygaafa dgmrpgdtfv
      481 drpvaipidg ravwrptdae pptdepmtlr dalalsrnri taqvmqhega akvaqlaram
      541 gvrespldav pslalgtspv tlkemvsayg tianrgvyva pqmitriedr dgkvlaafgs
      601 apperalpep aaqtlvdvmr dvvdrgtgad irsrygirvd vagktgttqd nadgwfilmh
      661 pqlvagawvg fddgsvtlrs dywgagahsa lpivgtfyda alraraidph aqfspdfrpr
      721 sapaprrrtp hpglfdwlrf fr
//
LOCUS       WP_175812643             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia contaminans].
ACCESSION   WP_175812643
VERSION     WP_175812643.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21808
     Region          1..192
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mhettllifa avafvgiatp gptvllaltn gsrygvrsaa ygfagamlsd fvlivavalg
       61 lgallmasaf wfsvvkwlga aylayvgirl lmskgaldva aahsgdasgr nasifaksfl
      121 tavtnpkgyl ffsaflpqfl dpsaplapqy valavtfall dgvvmfgyal lgaravrllk
      181 ragalwlert cgamllalag slalyrrhaa
//
LOCUS       WP_175812669             441 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia contaminans].
ACCESSION   WP_175812669
VERSION     WP_175812669.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48331
     Region          30..433
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(43..44,47..48,51,83,133..134,136..138,141,161,
                     164..165,168,265,268..269,272..274,277,305,309,360..361,
                     365,369,385,388..389,392..393,396)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtaldaaagr spaapahaae ldrtykkvfw rivpflmlcy vvayldrvnv gfaklqmsqd
       61 lafsetvfgl gagifflgyf lfelpsnllm hrigariwia rimitwglls alfafvktpt
      121 qfyvlrfllg laeagfypgv ilyltywfps hrrakiiavf msaipvsgif gnplsgwime
      181 rfhggsgfhg wqwmfmieav pavlvgiati lyldnsirga kwlderekql ledeiaaqpq
      241 eqqkhghslk avfadprmww msliyfafvt gqygltfwmp tlvkstgitd tlqigllsai
      301 pfvvaivvmn lfghsadkrr errwhlivpa lmgalgfava asyshntavs ivflslaagg
      361 vltcaplfws lptaflagsa aaagiaiins vgnlagfasp yvigylkdvt hstasgmyvl
      421 aamlvigaia vwltpaklvn r
//
LOCUS       WP_175812709             336 aa            linear   BCT 11-JAN-2025
DEFINITION  inorganic phosphate transporter [Burkholderia contaminans].
ACCESSION   WP_175812709
VERSION     WP_175812709.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..336
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=35505
     Region          21..336
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 mhsiqlalwm aaalvlvalv fdfmngfhda ansiatvvst gvlkprqavv faaafnviay
       61 fifhlkvaqt vgkgtidpei vdhyvifgal vgaigwnvit wyygipssss haligglvga
      121 alaksgwssl nidgllktia fifispllgf ilgslfmlgv swlyfrtaps kvdrrfrrlq
      181 llsaglysvg hggndaqkti giiwmllias gyasatadap pawvigtcyl smglgtlfgg
      241 wrivrtmgqk itklkpvggf caetggamtl flasflgipv stthtitgai vgvgatqkls
      301 avrwgvagni vwawvltlpa aalfaaggww lghrif
//
LOCUS       WP_175812726             285 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175812726
VERSION     WP_175812726.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 285)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13673967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..285
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31338
     Region          24..159
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          <179..278
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mttpakhidt tghwlvarrd aetgieslha hfnghaydah dhddmlvgft eqgvqqfqch
       61 rsvhtsvpgr ailiepgalh dghapeaggf tygmlylpqa wveraarrld lpglgsveas
      121 fghtlvddhg lvdairqafl aihgnegkla rdqtldrlli rlggelrgql vlesavvppa
      181 iarvrdllhe hmdgniglde lahvagidrf rltrlfqraf gtsphaylvr lrlraarrll
      241 aagrtpaqaa advgfadqsh lgrwfrrayr itpaayrqlc tnvpd
//
LOCUS       WP_175812734             512 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia contaminans].
ACCESSION   WP_175812734
VERSION     WP_175812734.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..512
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52502
     Region          16..438
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,142,
                     145..146,149,273,276..277,280..282,285,313,317,371..372,
                     376,380,396,399..400,403..404,407)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtqsdsrrna valaavclts lmfgleissv pvilptlehv lhgdfngmqw imnaytiact
       61 tvlmaagtla drfgrkrvyv igtvlfglts llcglapnvp vlvagrllqg asggamlicq
      121 iavlshqfre grergrafgi wgivfgiglg fgpivggaiv alaswpwvfl vhaplatial
      181 vliggavqes rdphagrldv agivtlslav lglafyitqs aalgltsaag lgvlgatvla
      241 lagffiaera sarpmfdfsv friraftgai fgsmgmnfsf wpfmiylpiw fqvalgydsv
      301 taglallayt lptlvappfg erlalrygpg vvipgglfti aagfalmrig saadhaswit
      361 mlpgcviagi glgltntpvt ntttgavpss ragmasgidm sarmislaln iaamgfvlva
      421 givanlkagv agtigdaalr rlaqeiasgr tdglheiapa laqadptgaa lhaalvhgfg
      481 wvmvygaagv allatasava faparrgapv ce
//
LOCUS       WP_175812745             207 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia contaminans].
ACCESSION   WP_175812745
VERSION     WP_175812745.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..207
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22945
     Region          1..195
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mrllnivssp rgarsasiav anafvdayre tgatidvdtl nvweedlpdf dsdaigakyk
       61 gvanapmdea eqsiwrriqs lvtrfqeadr ivvgvpmwnf gypyklkqli dlvsqrnmlf
      121 tfdgnayapl leipralvih vrgqsrepga gadnpgfrhq adyiefwlrf igvsevrslt
      181 vehtwgaras dsieraqara vamaaaf
//
LOCUS       WP_175812807             341 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia contaminans].
ACCESSION   WP_175812807
VERSION     WP_175812807.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..341
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35614
     Region          10..341
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mgnlnpvada qtmtlkarht kwppelsifl vlvgislffe ivgwivvgqs flfnaerlei
       61 ivlqmavigi iavgvnlvii tsgidlssgs vvaaaavvsa slaqvsdfpr avfphltdlp
      121 iiwpvlagvc vgllvgllng sliamtgipp fiatlgtmva argfakwftn gmpvsmltdq
      181 faaigaganp viiflviaai fhvvlrytrf gkytyaigan rhgavvsgin vtrhlifvya
      241 iagllsgiag tvtaaraisg qsgmgvmyel daiaavvigg tslsgglgrv tgtvigvlil
      301 gvmtsgftfi ridayyqemv kgaiivaavi adqyrnkkkr r
//
LOCUS       WP_175812842             774 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia contaminans].
ACCESSION   WP_175812842
VERSION     WP_175812842.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..774
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81619
     Region          <68..>193
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          206..764
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msapelsvhn esrralllgf asgglllafg vpslvhaavp vqppvsanpq yggagmphgl
       61 rddphlfvai apdgtvtvtc irsemgqgvr tsvalvvade lgadwarvkv aqavgdepry
      121 gnqntdgsrs lrqsfaalrr agaaartmle qaaaaawgvd arqvkatvhe vvdtksgrkl
      181 gfgelaakaa alptpdpatv alkvqaefry igkgetalid grdivggrah ygidtrldgm
      241 lyavvarppa ygdtiasfda saaeklpgvv kvvqlaptpl psgfqplggv avvardtwta
      301 iqaraqlkid wkhgpnanyd saayretlea aaaqpgdvir ndgdaaaala gaakrvraty
      361 yiphlahatm eppaavarva dgrcevwtct qapqttrdev akalglster vtvnvtllgg
      421 gfgrkskpdy vveaallska agapvkltft reddiahdyf havsleafdg gidasgkvva
      481 wqhrtvapsi qstfragivh eqpgelaqgi adlpfaipnv rienpaaqah trigwfrsvy
      541 niphafgiqs fvselahaag rdpkdfllel igparrfeph itvknanyge dpalypidtg
      601 rlrrvvetva rgagwgrklp kghglgiaah rsfvsytaav cevqvdadgk itvprvdiai
      661 dcgpqvnper vrsqlegavv mglgialhge itfkdghpeq snfngfqvlr mneapreirv
      721 hlvapddfst plggvgepgl ppvapaltna ifaatgtrir slpvadqlak prag
//
LOCUS       WP_175812895             190 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia contaminans].
ACCESSION   WP_175812895
VERSION     WP_175812895.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..190
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=19004
     Region          30..190
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 meekintgrv arraailafv aaaapamaad geitfngkvl sstcsigagg gatgnknmtv
       61 klptvsvaal anagdvagrt pfsvqlsgct gdstkvstvf eagdtvdags grlnlvktga
      121 daiaknvqin llndsqkpik agvagpqqgs qvvalkggsa tlnyyaeyya tgkaeagaan
      181 sriqysldyq
//
LOCUS       WP_175812902             317 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-binding protein [Burkholderia contaminans].
ACCESSION   WP_175812902
VERSION     WP_175812902.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 317)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10598562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..317
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34514
     Region          25..150
                     /region_name="AAA_22"
                     /note="AAA domain; pfam13401"
                     /db_xref="CDD:379165"
ORIGIN      
        1 mftvaihdmv erigtwlddq idgatifgps rfgkssavdh wlqrllsery ggyvplvvws
       61 htdsgsatav grfyahllea srhrlaqarr splerqtmlv erwielaaqg ggrflvlvid
      121 eaqgmsqrew lwlvelhsll ekqrirlcvf siaslqffde plgmalagga hvaarfmlas
      181 apfhgvrtvd elayvmrgyd egsewpagsg csftaglapr pwaggfrmad qaealmlamq
      241 dalppryagp vdfpmktvah acrhvllrva sgadvdsets atawqaaven gghrtlmalv
      301 sataalrgag rresgha
//
LOCUS       WP_175812912             339 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-quinone oxidoreductase [Burkholderia contaminans].
ACCESSION   WP_175812912
VERSION     WP_175812912.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..339
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=35574
     Region          1..333
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(40..41,127,131,134,157,160..162,181..182,186,201,
                     225..226,247..248,250,272..274,322,327)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mkaieitefg apdvlklaer prpepkrgev likvaasgvn rpdvfqrkga yapppgasdl
       61 pgleiageiv ggdlsdaaln pfglklgdrv callagggya eyavapllqc lpvpdgltdi
      121 eaaslpetff tvwsnvfdra qlgageggeq etllvqggss gigvtaiqia halgfrvfat
      181 agtadkcrac ealgaerain yktedfvevv kslthdrgvd vildmvagsy vprelsalad
      241 ggrlvliall ggakadvnlg eilrrrltit gstlrprpve fkariaaqlk srvwplladg
      301 rikpviyrvl paadaaqaha lmessehtgk ivldwgtna
//
LOCUS       WP_175812922             392 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia contaminans].
ACCESSION   WP_175812922
VERSION     WP_175812922.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..392
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43075
     Region          8..369
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 malfssarpp rtilvaaprr igdvllttpl vrslkarwpe aqidmlvfrg tegvlehnpd
       61 vrrvivvaqr agfrerlrda lsmwrrydla caalssdrpr fyswfagrkr vglvdpnrvt
      121 wltrmmlngi ainhhesaht vvstlalapv igiepvsevv apgigddpar rarfdawlae
      181 spairagkpl vvlhpypmfr ykqwrldgwv emigwlrehg favalsggpa dsereyaeqv
      241 aaeaggdvln lvgrltfges aelvrrarlf igpdtgathv aaatgtdtia lfgpsdpvrw
      301 gpwpqhwpat enpwplrgsg rhgnvwllqg egdcvpcrhe gcerrvdsrs dclanlgaqr
      361 vkaaaaemlg lnppgpaeaf vdtsrlhrts sd
//
LOCUS       WP_175813054             469 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia contaminans].
ACCESSION   WP_175813054
VERSION     WP_175813054.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..469
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47781
     Region          18..444
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(25..26,29..30,33,65,115..116,118..120,123,144,
                     147..148,151,275,278..279,282..284,287,315,319,371..372,
                     376,380,396,399..400,403..404,407)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtaaaptraa arrvlaatcv sytlvlldas ivnvalidia htfgsrvagl qwivnaytla
       61 fasllmtggt lgdrlgdrdv yiaglavfva asalcgvaph lpalaiaral qgvgsamlvp
      121 cslallnraf pepaarasai slwmgcggia masgpliggl lihlfgwrsl ffvnlplgla
      181 giwlgrsvvr aavvdasrhf dwggqataiv aiaaligtli egpslgwrsa piiggavtsv
      241 vawsafiaie arrrepmlpl affrnrlfag stfvsmasaf vfygslfvls lfyrqvrgas
      301 pldtglaflp mtamvalggl csgrlvarfg argamcaafg lyaagalgmt gigattpawl
      361 avapmlaigf asgfispaat spalgtvdrr ragvaaaaln aarqsgsalg vaifgaciat
      421 lqpfpaamrv algiatglsa laaatwwita rpsrapgepa aqlqtatrr
//
LOCUS       WP_175813062             298 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia
            contaminans].
ACCESSION   WP_175813062
VERSION     WP_175813062.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..298
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=31142
     Region          5..292
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 msillkgiia ypvtpfsadg gvdlktldal ierliadgvh aiaplgstge saylsdtewe
       61 avasasirav rrrvptvvgi sdlttadavr rarfaeraga davmvlpvsy wkladdeiva
      121 hyraigaaig ipimlynnpa tsgvdmspdl iaticrtvdn vtmvkestgd igrmhrlaql
      181 sdgaipfyng snpmalaala agaagwctaa pnlnaalpla lfdamqagdl arartvfhaq
      241 lpllqfivng glpvtvkagl rlrgfdagep rkplmplgda rtrelehlla alpdgaat
//
LOCUS       WP_175813076             382 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia contaminans].
ACCESSION   WP_175813076
VERSION     WP_175813076.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..382
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41016
     Region          1..370
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masismrrvq kaygdhapvi rdvdleigah efcvflgpsg cgkstllrmi agledlsage
       61 lsidgrrvdd vpaaergvam vfqsyalfph mtvyenmafg lklarvpkae idrkvrdaar
      121 ilqldmlldr kpkalsggqr qrvaigraiv repgvflfde plsnldaalr gqtrieiarl
      181 hrqferasvv yvthdqteam tladkivllh agadtaqhgs iaqvgapldl yhhpssrfva
      241 gfigsprmnf lpavvtacda hrttvtltps getfvlprdg salgagatva lgirpehltl
      301 gaahdatsla rdvalverlg eqtyvhldqp gghsliakvp gdaqmrsger vlvhapaaac
      361 hlftedgrav pacadvhvhh ya
//
LOCUS       WP_175813156             372 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia contaminans].
ACCESSION   WP_175813156
VERSION     WP_175813156.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 372)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..372
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40610
     Region          1..371
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 maslsirdvy ktypngvpvl kgvdieiedg qflilvggsg cgkstllnmi agletvtsge
       61 icidgkvvnd lspkdrdiam vfqsyalyps mtvrenisfg lnirkvpkse qqqivdrvsq
      121 mlqiqhlldr kpgqlsggqr qrvamgrala rdpslflfde plsnldaklr iemraeikll
      181 hqrlgttivy vthdqieamt lgdriavmkd gvvqqfgapq eiydspsnlf vagfigappm
      241 nfingklveq gsgialevdt gvkrgalnlp fdaaklkslv gremilglrp eritdvrhah
      301 ngdashlqpf dvrvdvtept gpdthvfaqv ngkrivsrvh paanpqpdqt lsllfdvska
      361 vlfdpaseer ia
//
LOCUS       WP_175813154             436 aa            linear   BCT 11-JAN-2025
DEFINITION  replication-associated recombination protein A [Burkholderia
            contaminans].
ACCESSION   WP_175813154
VERSION     WP_175813154.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..436
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=47983
     Region          1..434
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 msdlfqvepr rplaealrpk tlaevigqth llgegkplrl afesgkphsm ilwgppgvgk
       61 ttlarltala fdcefialsa vlggvkdire smeqakdtln rtgrhtilfv deihrfnkgq
      121 qdallpfves glvtfigatt enpsfevnsa llsraqvyvl ksldddemrq llkraqeial
      181 dglsfddkav dtlvgyadgd arrflnlleq aqtaatsagt atidaefvss amtlnarrfd
      241 kggdnfydqi salhksvrgs spdgalywfc rmidggadpk ylarrivrma wedigladpr
      301 alqvandaae tyerlgspeg elalgqaviy lacaaksnag ynafnqamaf vkqdksrevp
      361 vhlrnaptkl mkelgyghay ryahdepnay aagetylpdg mreprwykpv prgleskiad
      421 klawlreldr eagkkd
//
LOCUS       WP_175813169             226 aa            linear   BCT 11-JAN-2025
DEFINITION  urease accessory protein UreF [Burkholderia contaminans].
ACCESSION   WP_175813169
VERSION     WP_175813169.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Soriano,A. and Hausinger,R.P.
  TITLE     GTP-dependent activation of urease apoprotein in complex with the
            UreD, UreF, and UreG accessory proteins
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11140-11144 (1999)
   PUBMED   10500143
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Moncrief,M.B. and Hausinger,R.P.
  TITLE     Purification and activation properties of UreD-UreF-urease
            apoprotein complexes
  JOURNAL   J Bacteriol 178 (18), 5417-5421 (1996)
   PUBMED   8808930
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..226
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23840
     Region          1..226
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 mtttelvall hlaspalpig afsysqglea aldanlihda dtardwiasg ltdvlahgel
       61 pflahqlarw hahdasalaa enawfiasre saelrreteq mgwslaqlca slewgdaarr
      121 atlaaiapia lptafayaaa ahdasadavl aayafgwven qtsaalkavp lgqlagqrii
      181 valrgaidat vrralatppd avntfapqlg ilsarhetqy srlfrs
//
LOCUS       WP_175813282             207 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD family hydrolase [Burkholderia contaminans].
ACCESSION   WP_175813282
VERSION     WP_175813282.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..207
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23210
     Region          3..>172
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mtikavvfdf ggvlidwspe ylyrelipdd aerrwflthv camdwvirqd ggqtieegta
       61 elvakfpehe alirafyarw hemiggvlee gaalvdrldv qgmplfgltn wsaqtfpyaw
      121 dnfpvlrrfk eivvsgrvkl vkpdpaiyre mhariephlp giaphelvfi ddnaknaaaa
      181 talgwhgihh tsaavtearl relgala
//
LOCUS       WP_175813321             324 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Burkholderia contaminans].
ACCESSION   WP_175813321
VERSION     WP_175813321.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..324
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37603
     Region          134..291
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mlhlidafvs diqtwlyvdv vqpllfkfnl mdydedtyda lywvivgalq mvlmfvllrp
       61 leallpverw tnrravrvdv iytaiaklgi yslffffalq plfdnfqawl rlhgvanlnl
      121 dylwpgvtsk pivtfaiylv vldfagywyh rwqhkfgiww elhavhhsqr qmslwcddrn
      181 hvlddviqsc ffaaialvig vtpsqfvvlt aftnfmqsiq htnarlpfgw lgerlfvspi
      241 fhrrhhavgy ghegtkygcn fgvlfpwwdm lfgtaswnrt veptgirdqv egvsygegfw
      301 aqhglafvri frrlfpakrg aasa
//
LOCUS       WP_175813364             258 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia contaminans].
ACCESSION   WP_175813364
VERSION     WP_175813364.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..258
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=28159
     Region          60..243
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 mkrilttcal agvltgnala aecfipspka pqtcvvdaaa lnrsvvqygd dsrlwrvfqk
       61 aeagkpivva aiggsitqga wataqdknyv srvfgwwqat fpqskmklvn agigqtnsvy
      121 gnerlqrdvl kykpdfviie fanndagtpe mqasykrlaq rilssptkpa vlmlftmgrd
      181 wsnsednqip vgrelhlpmv glrealmpee kagvldpvdr tadpvhpndl ghqviaqlva
      241 yrlqsslnnm heskqaak
//
LOCUS       WP_175813398             215 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            contaminans].
ACCESSION   WP_175813398
VERSION     WP_175813398.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..215
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22557
     Region          14..129
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          80..211
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mkdkpaqgpr gldkdaivaa alalleevge aafsvrklaq svgcdpmsvl yhfkskegls
       61 raianalsrs lvpvdaalpw rerlrdlarq yralalrypa afallqrhms tgpadlahie
      121 avhraladag ipraalpsvc vgwyasvigl aaaeaggltr aandvelaem ealsdtahpl
      181 vkaaallyaq ldpaavhdtm ldvlldgiak qaraa
//
LOCUS       WP_175813420             561 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia contaminans].
ACCESSION   WP_175813420
VERSION     WP_175813420.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..561
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=61159
     Region          10..539
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mttqrtlege fdyvivgagt agcvlanrlt edpdirvlll eaggkddyhw ihipvgylyc
       61 ignprtdwly ktqpeaalng ralsyprgrv lggcssingm iymrgqredy dswaqetgda
      121 gwswdsvlpi fkrsedhhag asdahgaggy wrvekqrlrw eilesfaqaa qqtgipatdd
      181 fnrgdnsgvg yfevnqkrgv rwntskaflr pamarpnltv itgaqaqrvi fdgrravgve
      241 yhgggtdyva raraevllts gavnspqlle lsgigdgrrl qalgidvvqd lpgvgenlqd
      301 hlqlrmafrv egvrtlntls ahwwgklmig aeyallqrgp msmapsqlga faksdsedpa
      361 ltrpdleyhv qplslerfge plhsfnafta svchlrptsr gsvhiasadp gaapaiapny
      421 lstdhdrhva analrltrri asapalaryr peeilpglqy rseaelieaa gavgttifhp
      481 vgtcrmgrad deravvdsrl rvrgiaglri vdasvmpfit sgntnsptlm iaerasdmir
      541 adrraareat pvrtepvvta a
//
LOCUS       WP_175813429             158 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia
            contaminans].
ACCESSION   WP_175813429
VERSION     WP_175813429.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..158
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17204
     Region          11..146
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtaklnpfaa apalmkhwmt vsvaaaqsle ptlvelvkir asqinacanc inmhaaeare
       61 qgeteqriyl lsawreapcy tdreraalgw tealtrlseg haaheaayaa lndhfsqeeq
      121 vkltlminmi ngwnrlavgf glwiepadak aaaakmva
//
LOCUS       WP_175813468             823 aa            linear   BCT 11-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Burkholderia contaminans].
ACCESSION   WP_175813468
VERSION     WP_175813468.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..823
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..823
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=86028
     Region          65..814
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 msrnwgwrta llalcvvlsa cggdgdspsm aaanmsaaaq sqgnrsgngg ndnsnendns
       61 ngneaarkna dirvvqyvnp ligtdyatdq padpvgsglg ggtfpgptvp fgmmqwspmt
      121 ptaqydsskg dgsgfsggyw ygdtsinafs ilhlsgtgcw anggylnvmp qlapgdagtp
      181 asfshaneta qagyygvtlg ngikaelttt lrtgfalfty palaqgqqat iaidptvlnn
      241 raqgttsdti sqvgdralsg tiagggfcwa ghavpvyyya efsqpfaakp alsnnspvtv
      301 tfnvdrkhpd vmmklgisfv seanaqanlr aenpetdaqg srnwrfdkvr saasaawnar
      361 lnaiqvtggs dadktkfyta lyhaslhpnv fndvngqypd fyasngaaaa ptrqvekgrt
      421 myanfsgwdi drsfiqlqal ldpvrtsdiv qslvldakac gafprwayfn tetavmpgda
      481 gsiivanaha fgatnfdtqa alsimknsta pgaacagtpv mssradydrl gyvpssgsgd
      541 nqtasntley avrdfavsrf atalgdtata gtllkssgnw qnlfdqgaiq pktsagawvt
      601 dgtgfmegns eqytwyvphd lagvvaqagg aapvvkrldt ffthlnigtv qpyfyvgnev
      661 tmavpwvyaw agapshtqrv lhaslanefg tgaaglpgnd dlgaisgwyv waalglypvv
      721 pgvsgvalss pqfekitvrv gqkdgsyrll hivapgagsg dsasfyvksl klngspyaaa
      781 wlpfeqiakg gklsyamtsd asattwgtda sampsfpqaa sap
//
LOCUS       WP_175813487             114 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia contaminans].
ACCESSION   WP_175813487
VERSION     WP_175813487.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..114
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12473
     Region          <30..109
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 mtklikdilp lgagigeftk ldfgmdesdw raaegksgny ivgwwegkag svefpetaad
       61 eavwlvegri altdvegnrk eftpgqgyll pagfagrwet iedakkfyvq leqs
//
LOCUS       WP_175813495             430 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia contaminans].
ACCESSION   WP_175813495
VERSION     WP_175813495.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..430
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46181
     Region          108..419
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 msfhfgtpla rharrrapml waallvagav haqpspftld aalqcatdhs asmqaaqasv
       61 hasaeaavka gqlpdpmlka gidnlpvngg qrftvgqdfm tmrrigieqe wvsgdkrrlr
      121 salaneqvgr eragylaqla svrqqtataw lnavyakqal alqqalldhm nheleatkas
      181 yrgakasaad vvqaramlaq tqdqllkaqq vyqtalials rwtavpvgdv agtppapesf
      241 vsslppdelr lsqpalitaa ddiavaeadt avanserspn wtwevayqqr ggaysnmvsv
      301 gvtiplplnr knrqnrdvae kaalatkarl myedtlrqvq adirtqsatl asgrarianl
      361 gdallpaadq rvqlanaayr agtgsladtf aarraqldaq lqvlelrrev sqtwaqleyq
      421 vvpstqaaaq
//
LOCUS       WP_175813639             209 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia contaminans].
ACCESSION   WP_175813639
VERSION     WP_175813639.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..209
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21857
     Region          1..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mshlswlpfi atslliivtp gqdmvlvmsr tlsggtragl vtaagvsvgl lvhtmlatlg
       61 lgallqasew lftalkviga lyllylgial lrtsgeltla ssrdgaqasr lrtfaqgals
      121 nvsnpkvalf ylaflpqfvp agtahpmlsl fvlgatfagl tllvkgpval fagllsasir
      181 rnpriltrmh rvsgvvllgl gvklalerr
//
LOCUS       WP_175813709             317 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175813709
VERSION     WP_175813709.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..317
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34123
     Region          9..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          99..294
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(111..112,114..115,118,122,124..130,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176117"
ORIGIN      
        1 maaflhglal ryfvevartg sisdasvrlh vavsaisrqi akleselgap lferrprgma
       61 lseagerlla faqrslleae hvmkdiggld alhgsllkia csegfaidfl pgtlanfkar
      121 hpgvdfsvwv vspadatrrv rdgdvdials fslapekgvr vdhterapif alvrhdhpla
      181 tqeavsladv arhphvlpea gttvrqlidi acaldgllle peltsnntaa mygyarrtga
      241 vmftgllsvr drcaadgfvv vpvtnpqlre rsiqvqtmag rdlpasvraf rdhlidamqa
      301 asapptaarg prrrpvr
//
LOCUS       WP_175813722             482 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia contaminans].
ACCESSION   WP_175813722
VERSION     WP_175813722.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..482
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51609
     Region          <24..71
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          59..470
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 msakhqalvt llvgmvsatv wafdplltds avpvtpvvdl lgagehvctf galptplhlq
       61 daveralcnh pktrqawanv kiqaaavgig raaylptlng swqgtrdivr nhvtglpqyd
      121 snygknlqia svslswvlyd fggrsaalrn anellaaaqa nqlatlqtvf gtvakdfyaa
      181 qaaqgtlsaa reveciarts adaaisrtdr gvaaisdqlq aqtayaeavv nrtkaesdwa
      241 savgtvasdm nlepatpivl pdvgdgvkpd hefgdsvaal iedaqlhypg isaavaqvea
      301 akakaaqtra eglphlnlva qynfnnqpts lqlgfpvfpa threwylgfq vtipifegfa
      361 rtyqvrqaea qtelqvdllv earqqvgldv wnayqslqga tknldnsanl lalakhayea
      421 aqrryqigvg nilellntqs mlanakkqri qalsdwrsar lqlasklgrl giwslssega
      481 rp
//
LOCUS       WP_175813923             397 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Wolbachia
            endosymbiont of Cruorifilaria tuberocauda].
ACCESSION   WP_175813923
VERSION     WP_175813923.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Cruorifilaria tuberocauda
  ORGANISM  Wolbachia endosymbiont of Cruorifilaria tuberocauda
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Wolbachia endosymbiont of Cruorifilaria
                     tuberocauda"
                     /db_xref="taxon:1812111"
     Protein         1..397
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43843
     Region          1..397
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(99..101,125,173,205,233,235..236,244)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(102,135,198,242..244,273,276)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            236
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mlrlakrmsl iklsptvavt dkvsrlkneg kkicilsage pdfdtpyhik kaaiqaindg
       61 ktkytavdgt yelkeaiink lkrdnnleyt lsqicvgaga kqvlfnlfma tinhgdeaii
      121 papcwvsyvd mvslfgglpi vvecmgnfkl tpkllrskit sktkwlvlns pnnpagvvyt
      181 ygelkeiaqi llehphvnii tddiyehivy dekfftiaqv epklyervfv vngvskayam
      241 tgwrigyiag rsdiikaisv lqsqstsnpn siaqaaavea lngnhaflke rvktfksrrd
      301 fvaqklssvs glstftpqga fylfiscknl lgkstksgki inndldfaey lledhlvavv
      361 pgvafslknf irvsyvtsqd qleigcnnii kacemls
//
LOCUS       WP_175814007             199 aa            linear   BCT 11-JAN-2025
DEFINITION  superoxide dismutase [Wolbachia endosymbiont of Cruorifilaria
            tuberocauda].
ACCESSION   WP_175814007
VERSION     WP_175814007.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Cruorifilaria tuberocauda
  ORGANISM  Wolbachia endosymbiont of Cruorifilaria tuberocauda
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Wolbachia endosymbiont of Cruorifilaria
                     tuberocauda"
                     /db_xref="taxon:1812111"
     Protein         1..199
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23178
     Region          4..194
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mnftlpdlpy dktalepyis aktldfhydk hhrgylnkln elvkstsiki eelimktygd
       61 snkisifnna aqvwnhtfyw nsmkrnggsk pkdnsllakk iqediggfdk fyeefssygv
      121 sqfgsgwvwl vlekgklkit ktsnsdlplv ygqvplltmd vwehayyldc qnrridyikv
      181 flnylinwdf aeenlkksm
//
LOCUS       WP_175814017             544 aa            linear   BCT 11-JAN-2025
DEFINITION  ribonuclease J [Wolbachia endosymbiont of Cruorifilaria
            tuberocauda].
ACCESSION   WP_175814017
VERSION     WP_175814017.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Cruorifilaria tuberocauda
  ORGANISM  Wolbachia endosymbiont of Cruorifilaria tuberocauda
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Li de la Sierra-Gallay,I., Zig,L., Jamalli,A. and Putzer,H.
  TITLE     Structural insights into the dual activity of RNase J
  JOURNAL   Nat Struct Mol Biol 15 (2), 206-212 (2008)
   PUBMED   18204464
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Wolbachia endosymbiont of Cruorifilaria
                     tuberocauda"
                     /db_xref="taxon:1812111"
     Protein         1..544
                     /product="ribonuclease J"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0004534 - 5'-3' RNA exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=60661
     Region          4..544
                     /region_name="RnjA"
                     /note="mRNA degradation ribonuclease J1/J2 [Translation,
                     ribosomal structure and biogenesis]; COG0595"
                     /db_xref="CDD:440360"
ORIGIN      
        1 mniskneflf lplggvgrig mnvslyhcqs kwimidlgig fadettpgie lliadvsfia
       61 qrkkdllgii ithahedhcg aipylweelq cpiyatnfta nflkeklkef qlesmvpvre
      121 vntnsslnlg pftvefinvt hsipeahsil istdigsvlh tgdwkfdhkp vvgltsninr
      181 lreigdkgdl lavicdstni lskcnpkseg eiydniyrii rqskklvavs lfasnvarie
      241 tisqaakald rkvvllgrsl wrivkvaqds gylidsahff eakdaadlpr eklllictgc
      301 qgepmaatsk lahkrhyafk iqrgdtiils sriipgnetr vhnmlnafve mgvevitekt
      361 ehihssghpt kselremysl ikpkmsipvh geyihthahv kfakecgvkk aimitpgdiv
      421 nlengekida idvnyfcidg tllrypegsv ikmrkrmrda gaivvtavvn kknkllvkpk
      481 vftpgafeak edaaiiqrit kavesafssr strkirnkie ssifsilney llkkpiikvq
      541 ieqv
//
LOCUS       WP_175814040             390 aa            linear   BCT 11-JAN-2025
DEFINITION  elongation factor Tu [Wolbachia endosymbiont of Cruorifilaria
            tuberocauda].
ACCESSION   WP_175814040
VERSION     WP_175814040.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Cruorifilaria tuberocauda
  ORGANISM  Wolbachia endosymbiont of Cruorifilaria tuberocauda
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Wolbachia endosymbiont of Cruorifilaria
                     tuberocauda"
                     /db_xref="taxon:1812111"
     gene            1..390
                     /gene="tuf"
     Protein         1..390
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=42722
     Region          10..390
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 mtqiveafgk phvnvgtigh vdhgkttlta aitkyyghfi aydqidkape erkrgitiat
       61 ahveyetdkr hyahvdcpgh adyvknmivg aaqmdaailv vsgvdgpmpq trehillakq
      121 vgvkyivvyi nkadvadhdm iglvemevre llskyefpgd dvpvvigsal kaledegney
      181 gkksigklme kldeyvavpp rpvdlpflmp iedvfsipgr gtvvtgriek geiktgeeie
      241 ivglkatrkt ictgvemfkk cldkgsagln vgillrgikr eevergqvls kpstitphqk
      301 fkaevyvlkk eeggrhtpff enyqpqfyir ttdvtgsikl lggkemvmpg dnvsievelq
      361 apvaldkglr favreggrtv gsgvvseile
//
LOCUS       WP_175814099             134 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydroneopterin aldolase [Wolbachia endosymbiont of Cruorifilaria
            tuberocauda].
ACCESSION   WP_175814099
VERSION     WP_175814099.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Cruorifilaria tuberocauda
  ORGANISM  Wolbachia endosymbiont of Cruorifilaria tuberocauda
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Illarionova,V., Eisenreich,W., Fischer,M., Haussmann,C.,
            Romisch,W., Richter,G. and Bacher,A.
  TITLE     Biosynthesis of tetrahydrofolate. Stereochemistry of
            dihydroneopterin aldolase
  JOURNAL   J Biol Chem 277 (32), 28841-28847 (2002)
   PUBMED   12039964
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Wolbachia endosymbiont of Cruorifilaria
                     tuberocauda"
                     /db_xref="taxon:1812111"
     Protein         1..134
                     /product="dihydroneopterin aldolase"
                     /EC_number="4.1.2.25"
                     /GO_function="GO:0004150 - dihydroneopterin aldolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0046656 - folic acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=15140
     Region          7..113
                     /region_name="FolB"
                     /note="Dihydroneopterin aldolase [Coenzyme transport and
                     metabolism]; COG1539"
                     /db_xref="CDD:441148"
ORIGIN      
        1 mkslcnlfiq dlrlwvhlgc sleeklhsql vsinvdfafk spplglitdr ledticylev
       61 vqsikslaqs kqfnliehft ydiyvaisnl vtqkmhiiss irvvthkvap pvpdlhggvt
      121 ftycnllqra eklm
//
LOCUS       WP_175814118             246 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Wolbachia endosymbiont
            of Cruorifilaria tuberocauda].
ACCESSION   WP_175814118
VERSION     WP_175814118.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Cruorifilaria tuberocauda
  ORGANISM  Wolbachia endosymbiont of Cruorifilaria tuberocauda
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Wolbachia endosymbiont of Cruorifilaria
                     tuberocauda"
                     /db_xref="taxon:1812111"
     Protein         1..246
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26913
     Region          20..245
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mshenigkel sfvkklntvn ssilkienla lvydnkkvld ginlsikkgd vvtilgpngg
       61 gktsllkvva ginknstgnv vfaddikisy mpqnfsisnl mpitveylll nsfskklekn
      121 qslltevvgl vgirnilksq vleisagqtq llllarclia epdliildep vsamdinara
      181 kfydiidkia kkrsisilmt shdlgsivpc sdyivcinhi iyyqgkpgei mknktlseif
      241 ssyiak
//
LOCUS       WP_175814142             368 aa            linear   BCT 11-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Wolbachia
            endosymbiont of Cruorifilaria tuberocauda].
ACCESSION   WP_175814142
VERSION     WP_175814142.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Cruorifilaria tuberocauda
  ORGANISM  Wolbachia endosymbiont of Cruorifilaria tuberocauda
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Wolbachia endosymbiont of Cruorifilaria
                     tuberocauda"
                     /db_xref="taxon:1812111"
     Protein         1..368
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=41903
     Region          1..362
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mlsklvilll vfsfpffsys yqfrtkakqa vildlssnsf ifehnsdekm apssmsklmt
       61 lyiafdclka giinmedkfr vskkawsrkg ssmflregqf vtvrkllegi ivvsgndaci
      121 tlaegisgse enfviemnei aqklalnnsh fvnssgwpde dhfmsakdlv vlakriltdf
      181 peyydlfseq yltynnisqr nenlllfhgi gvdglktgyt sagaygivas akrngrrvfv
      241 vvnglstgee rieeakrlir ysldhfytkk iftkddvvee vnvlygkskr vpvtvandvv
      301 itynhnlydq ikvhieyrdm vlapikkgqe mgkifiqipg ikqrtvplya vndvqelnyi
      361 ekffrilf
//
LOCUS       WP_175814214             205 aa            linear   BCT 11-JAN-2025
DEFINITION  SCO family protein [Wolbachia endosymbiont of Cruorifilaria
            tuberocauda].
ACCESSION   WP_175814214
VERSION     WP_175814214.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Cruorifilaria tuberocauda
  ORGANISM  Wolbachia endosymbiont of Cruorifilaria tuberocauda
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Wolbachia endosymbiont of Cruorifilaria
                     tuberocauda"
                     /db_xref="taxon:1812111"
     Protein         1..205
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23180
     Region          44..180
                     /region_name="SCO"
                     /note="SCO (an acronym for Synthesis of Cytochrome c
                     Oxidase) family; composed of proteins similar to Sco1, a
                     membrane-anchored protein possessing a soluble domain with
                     a TRX fold. Members of this family are required for the
                     proper assembly of cytochrome c...; cd02968"
                     /db_xref="CDD:239266"
     Site            order(77,81,163)
                     /site_type="other"
                     /note="Cu(I) binding site [ion binding]"
                     /db_xref="CDD:239266"
ORIGIN      
        1 migfirllsi ilivlaatfl sycfftkkgi fsltgginna evkigsefal inqdnqiirs
       61 kdfkdkymmi ffgfssckkv cpmnlgiise ilakldektn eklqtffiti dperdniekl
      121 kefhqqfdhr iqmltgerek ideviagykv ytskgvgege inhssviyli gpggkyiahf
      181 vadlnsnesq sdkiatkirk yidel
//
LOCUS       WP_175814223             197 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Wolbachia endosymbiont of
            Cruorifilaria tuberocauda].
ACCESSION   WP_175814223
VERSION     WP_175814223.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Cruorifilaria tuberocauda
  ORGANISM  Wolbachia endosymbiont of Cruorifilaria tuberocauda
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Wolbachia endosymbiont of Cruorifilaria
                     tuberocauda"
                     /db_xref="taxon:1812111"
     Protein         1..197
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=21660
     Region          40..189
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mklivnflla aflitqsgct tliisgvvat tatavamqdr slgnivddtt miirinksll
       61 khglfpsikv kvsegrvlli gnvdtpekql taekiawqek evkevineir vipiqtisml
      121 dsiidsmita eirtrllgkr niksinysin tadgavylmg iaqnkaelka viaiarkvkg
      181 vkqvvsyvrh rhsklrr
//
LOCUS       WP_175814271             262 aa            linear   BCT 11-JAN-2025
DEFINITION  TatD family hydrolase [Wolbachia endosymbiont of Cruorifilaria
            tuberocauda].
ACCESSION   WP_175814271
VERSION     WP_175814271.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Cruorifilaria tuberocauda
  ORGANISM  Wolbachia endosymbiont of Cruorifilaria tuberocauda
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Wolbachia endosymbiont of Cruorifilaria
                     tuberocauda"
                     /db_xref="taxon:1812111"
     Protein         1..262
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29424
     Region          2..253
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 miidshchli hfsddevpkv israrqsdvk ilhnicisid nipkllktsl shdqvyfsvg
       61 vhplnssien gkfiyvdelv efakskkvis igetgldfye sdsksnqkks ltshieaari
      121 tglplvihtr nadhdiidil ksemkigifs gvihcfassk elayqavdlg lyisfsgiit
      181 fksanllrei aqniprkftl vetdapylsp epyrgkrnep amikytlncl aelwnelpdk
      241 vaevttsnff rlftklnske il
//
LOCUS       WP_175814324              93 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Wolbachia endosymbiont
            of Cruorifilaria tuberocauda].
ACCESSION   WP_175814324
VERSION     WP_175814324.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Cruorifilaria tuberocauda
  ORGANISM  Wolbachia endosymbiont of Cruorifilaria tuberocauda
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Wolbachia endosymbiont of Cruorifilaria
                     tuberocauda"
                     /db_xref="taxon:1812111"
     Protein         1..93
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10347
     Region          <12..83
                     /region_name="COG5606"
                     /note="Predicted DNA-binding protein, XRE-type HTH domain
                     [General function prediction only]"
                     /db_xref="CDD:444337"
ORIGIN      
        1 metislnnns cntevkkkll niiskviekn awtqahaaek lgvdqpkisq ikngktdgfs
       61 lerllsflkk feheititit esqsikhehe sgs
//
LOCUS       WP_175814430             138 aa            linear   BCT 11-JAN-2025
DEFINITION  nucleoside deaminase [Wolbachia endosymbiont of Cruorifilaria
            tuberocauda].
ACCESSION   WP_175814430
VERSION     WP_175814430.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Cruorifilaria tuberocauda
  ORGANISM  Wolbachia endosymbiont of Cruorifilaria tuberocauda
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Wolbachia endosymbiont of Cruorifilaria
                     tuberocauda"
                     /db_xref="taxon:1812111"
     Protein         1..138
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=15172
     Region          1..136
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 melaieqakl aqkndevpig avivngsniv sfahniyndp tahaeilvir qackllstpv
       61 lcdvdmyvtl epcpmcaqai sfarirrvyf gaynpkgggi engakifqfc ryvpeiyggi
      121 leaecslllk dffeklrt
//
LOCUS       WP_175814705             324 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175814705
VERSION     WP_175814705.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12168323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..324
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34771
     Region          22..200
                     /region_name="AraC_binding_2"
                     /note="AraC-binding-like domain; pfam14525"
                     /db_xref="CDD:434015"
     Region          247..322
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdialsrhap nrlgtlhapd everavahrl gphrmaargr dpfhaelyev plhhgallel
       61 cygretcidf gddadhflfr ltlsgacelr agdgvaragp gqltvsspar asrlctspdc
      121 rnlvlrlerg alerklrdml hatltrpllf dlaaggngtg valvlptfey lcrlgaqpqi
      181 gastttfgad ltawlmslll thlphsysaa largtpplpa hvrracdhvd ahlgdplalt
      241 alaavagvap rtlqhafraf lnttpaayvr errlaavhaa lergdarsvt dvllahgihg
      301 fghfakayar ryghapsvta rqar
//
LOCUS       WP_175814717             360 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia diffusa].
ACCESSION   WP_175814717
VERSION     WP_175814717.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..360
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39289
     Region          1..358
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msfltltdlt ksfgeltava dvnlsveqge fvsllgpsgc gktttlqmia gfvdvtrgri
       61 aldgqdithm kpnrrglgiv fqsyalfphm svaenvgfgl dmrgvdkaer aeriraalal
      121 vrldalahrf prelsggqrq rvaiaravvi eppvllldep msnldaklre emqfelraiq
      181 hkigtttimv thdqsealsi sdrvvvmeag ritqtdtpyr ayerpenhfv sqfigkanll
      241 pgtivahdgd airidlghdl aetgrtahlp arerdvrigd avsvcirpek lrlcapgagr
      301 faatvtsrff lgsqwlyrvd salgevlvcc qnegaeplae gapvgvdwhs davrvmrrea
//
LOCUS       WP_175814776            1070 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia diffusa].
ACCESSION   WP_175814776
VERSION     WP_175814776.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..1070
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=114941
     Region          1..1040
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mferlirfai ahrwlvmlai aavaalgvfs yqklpidavp ditnvqvqin taapgysple
       61 aeqritypve tvmaglpgle qtrsisrygl sqvtvifkdg tdiyfarqlv neriqeakdk
      121 lpagiapamg ptstglgeiy lwtveadana rkpdgtryta adlrelqdwv irpqlrnvrg
      181 vtevnsiggy vkeyrvapnp aklmsygltl advvralern ndnvgagyie krgeqylvrv
      241 pgqartvddi anivltnvgg vpvrmkevgq vdigrelrtg aatsngeevv lgtvfmlmge
      301 nsrsvakava akmedvnrtl pagvkaipvy drtvlvekav atvkknlleg avlviavlfl
      361 flgniraali talviplsml mtftgmvnak vsanlmslga ldfgiivdga vvivencvrr
      421 lahaqsaagr pltrderfae vfgasqearr alifgqliim vvylpifalt gvegkmfhpm
      481 avtvvmalaa amvltvtfip aavalfiger veekenrlmg warrayepvl aafmtrparv
      541 mlgagaivla tlglatrlgs efipslnegd lavaalripg tslsqsvemq kaiektlkar
      601 fpeiervfar tgtaeiaadp mppnlsdgyi mlkpadqwpd pkkprdqlvr eieaalgelp
      661 gnayefsqpi qlrfnelisg vrsdvavkif gddmavlnqt geqiaaalqk vpgasevkve
      721 qttglpvltv nldrdklary gvtvadlqdt vaaavggqka gtlfqgdrrf divvrlpdel
      781 rsdieaikrl pialpapaag asaplaqapy vplaelatie vapgpnqisr edgkrrvvvs
      841 anvrgrdvgs fvadareqlq qdvrvpagyw vswggqfeql qsaserlklv vplalfmvfv
      901 llfvmfnnvk dgllvftgip falsggvvsl wlrgiplsit aavgfialsg vavlnglvmi
      961 sfirnlrdeg mpldaavreg altrlrpvlm talvaslgfl pmafatgtga evqrplatvv
     1021 iggilsstal tllvlpvlyr vshavswrav lrggfgagvl rrlgffkgna
//
LOCUS       WP_175814351             187 aa            linear   BCT 11-JAN-2025
DEFINITION  RlmE family RNA methyltransferase [Wolbachia endosymbiont of
            Cruorifilaria tuberocauda].
ACCESSION   WP_175814351
VERSION     WP_175814351.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Cruorifilaria tuberocauda
  ORGANISM  Wolbachia endosymbiont of Cruorifilaria tuberocauda
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Hirata,A., Okada,K., Yoshii,K., Shiraishi,H., Saijo,S.,
            Yonezawa,K., Shimizu,N. and Hori,H.
  TITLE     Structure of tRNA methyltransferase complex of Trm7 and Trm734
            reveals a novel binding interface for tRNA recognition
  JOURNAL   Nucleic Acids Res 47 (20), 10942-10955 (2019)
   PUBMED   31586407
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Caldas,T., Binet,E., Bouloc,P., Costa,A., Desgres,J. and
            Richarme,G.
  TITLE     The FtsJ/RrmJ heat shock protein of Escherichia coli is a 23 S
            ribosomal RNA methyltransferase
  JOURNAL   J Biol Chem 275 (22), 16414-16419 (2000)
   PUBMED   10748051
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Wolbachia endosymbiont of Cruorifilaria
                     tuberocauda"
                     /db_xref="taxon:1812111"
     Protein         1..187
                     /product="RlmE family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=21290
     Region          6..180
                     /region_name="RlmE"
                     /note="23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ
                     [Translation, ribosomal structure and biogenesis];
                     COG0293"
                     /db_xref="CDD:440062"
ORIGIN      
        1 mqrtskdgyr srsaykliei dnkfklfqrg qkvidlgafp ggwsqvasqk ganvvaidtk
       61 qvnlidgvey ikcdivnele ilkerlkdqr fdvilsdmap escgvrsldh irimflckla
      121 lnlanyclac ggkfvvkvfq gesdmdfcne lkkifkivky fkprssrses teiylvsldf
      181 tknrffs
//
LOCUS       WP_175814824             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175814824
VERSION     WP_175814824.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33503
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdyidklrif rsvvemrsft raadmhglar pvvsravadl earfgsrllh rttrqvslte
       61 taeriyerca avldeldsle aqaqshtrep egllrlvaht taalnrlvpl iagfkaahpk
      121 vrldvtlter pvdlvgegyd igivvpymlt settvvrlve ripvvivatp aylrthprpe
      181 tptdlaghaf ipmspslrrp alsfrvdgdt lvvplsfdis snspvfnrem vmhdfgigvv
      241 prtlveaela sgalvqlldg adlvdafvei klayanrall pakvkafidy taaycdrqdg
      301 ivpaaa
//
LOCUS       WP_175814872             495 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia diffusa].
ACCESSION   WP_175814872
VERSION     WP_175814872.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..495
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50617
     Region          21..436
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(28..29,32..33,36,68,118..119,121..123,126,148,
                     151..152,155,290,293..294,297..299,302,330,334,386..387,
                     391,395,411,414..415,418..419,422)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mdtttrspaf phglarivat vsigfvvtql dvtivniala hlagdlhlpv aglqwvvday
       61 tlafavlmls ggalgdrfga rrmyvvglvl falaslacga aitpamliaa ralqgvgaaa
      121 mlpnslalln decrhdpplr aravgwwtaa gaisiaagpv vgglliaawg wrgiflvnlp
      181 lcaaglaatf awvparhiga askqpttpmr svraldlrgq liaiamltal taaviewqpl
      241 gfthpvvagg falaalagla fvaveshtam pmlplslfrr rtfsaavlfg icvnltyygt
      301 vfvlalylqr vrgesawqag laflpltggf llsnlasgra varhgprapm lagalvaalg
      361 ygalhfidas tplplllvpf lliptgmgfa vpamttavla svehecagia savlntarqt
      421 ggamgvaafg avagsgaawq tveglhvetg vsagllvaaa llatlvrpda hrgasdarra
      481 vsqpiercsr pssga
//
LOCUS       WP_175814887             234 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia diffusa].
ACCESSION   WP_175814887
VERSION     WP_175814887.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..234
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25409
     Region          1..207
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mstllhiess prksrsasld varayleawr nahpehrvdv ldlwatplpe ldgdaldaky
       61 adlsgtplse gqqqawagfr qlaqrmhdad tllfsvplwn fsipyklkhf idavshrdvl
      121 fsfderglag llngkkavvi yargldysrq sstpaesfdf qrpfleawlr figitdiesi
      181 ivektlfgpe vdhagreaar kravtlvhaa sasasasasa sasasasasa svdg
//
LOCUS       WP_175814888             853 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: transglycosylase domain-containing protein
            [unclassified Granulicatella].
ACCESSION   WP_175814888
VERSION     WP_175814888.1
KEYWORDS    RefSeq.
SOURCE      unclassified Granulicatella
  ORGANISM  unclassified Granulicatella
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Carnobacteriaceae; Granulicatella.
REFERENCE   1  (residues 1 to 853)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..853
                     /organism="unclassified Granulicatella"
                     /db_xref="taxon:2630493"
     Protein         1..853
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=94377
     Region          35..744
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mseqnqtpdw reallsiwnk pilknmrfif niaysvlkni fviailalml igvfgggigl
       61 gyfasltsne epltqeqmsd aignlnliss fyyqdgtkis dvntdelriv kplseisqyv
      121 kdgiiateds sfydhngivp kalirallqe vassdsgatg gstltqqlik qqiltsevtf
      181 krkaneilya lrlekhftkd qileaylnvs pfgrnnngln iagieeaaqg vfgvsakdls
      241 lpqaaylvgm pqnpivytpy tnvatmkedv sagvermktv lfsmyrenki tkeqyeeala
      301 yditkdflpp keltsnrqsy lyqavhreav kvlmtkaaek nkltyndvkn dselyskyyd
      361 eaerelsssg yrvtstvdqk vydamqkaia engdligpty ntqyvdqstg etksqkepaq
      421 ngavlienkt grilgfvagr dfeanqvdha fsthrspgst ikpilvyapa iennliypas
      481 ivpdtkisia qgngtywqpt nygnsitnqf ltvryalfks lnnpvikiyq amlqkginag
      541 eylkkmgite gigedeyqni alsiggtrtg psvreqtsaf stlanggehh esyliekied
      601 srgnviyqhe dkaervfsda taflttnmlq diasstifyn ikgnmgfssd lagktgtsen
      661 eidnwfvayt ptvtlgswig ydnfynarya itggdgygep tmrsqrqwtn lmraayeanp
      721 eligketsft qpdsvyrdsv vsttgtkags fkgenggtys iggsmttdwf kkdfppmdpr
      781 ydfmvgatpe elsrfwnkss sssdkkkeek keqkkeekkp dttqapatqa pssqapattq
      841 apstqapatt qah
//
LOCUS       WP_175814889             444 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia diffusa].
ACCESSION   WP_175814889
VERSION     WP_175814889.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..444
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=48215
     Region          14..426
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mhriiivggg agglelatrl gdrysargnr paralvtlvd rnpthiwkpl lhevaagsmd
       61 pftqeleyaa qarwhgfefq qgeltsldra akritlspvn dsdgeellpa rdleydtlvi
      121 aigstthffg vqgaaenaia ldtvgeaerf rkrliaacmr aehqapaqpa pgapdepriq
      181 vvivgggatg velsaelrnt aqvlsvyglh kldpqhdvgi vliesgpril palqervsta
      241 ttelleklgv rlmlaervte vapgfvhtas gksvradltv waagikapsv lsnldglqvn
      301 klgqldvrrt lqtftddnvf algdcaacvw pgnernvppr aqaahqqasf llkaigcrld
      361 grqlpeftyr dfgslvslgh fsavgnlmgg liggnmlieg lfarfmymsl yrlhiaalhg
      421 yprmmldtfa hwlrrttlpr vklh
//
LOCUS       WP_175814949             157 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia diffusa].
ACCESSION   WP_175814949
VERSION     WP_175814949.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..157
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17025
     Region          3..153
                     /region_name="COG3865"
                     /note="Glyoxalase superfamily enzyme, possible
                     3-demethylubiquinone-9 3-methyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:443074"
ORIGIN      
        1 mtiqkitpfl wyateaeeaa afyagifpns rvvrvtavag tsgtrmvefe lfgqpfiams
       61 hprtetfnha islmvscadq teldrywgal ldnggtadgc gwlrdrfgvs wqivpdalip
      121 mmadrdeaka arvaaammqm tkfdvatlka ayagmag
//
LOCUS       WP_175815045             324 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175815045
VERSION     WP_175815045.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..324
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35588
     Region          13..72
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          101..301
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(111,115,154,168,170,232,249,280)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(112..113,117..118,120..121,124,128,130..136,197,
                     226..230,237..238,241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mktmtrdtgi dhlgamrafv rvvemgsfsa vakemhvsts tvarkitaie dalgvallhr
       61 sthsvtltea ghiyleravt liadlddtlr vvaelnsqps gplkltapva fgrrhlapli
      121 apflarypti qldvrltdnh ndlvaggfdl dihegenyld nlvvhrlsrn dsilcatpgy
      181 ldrsgrpatp ddlqhhnclr yvhpegdprw elvrgdarhs vlpagnlvtd hsellldatc
      241 aglgiaefei wlvrdllasg rleavlpryr lqskltgdyi yiaylanrrs saklrvlrdf
      301 laehlahige lsavelakir daga
//
LOCUS       WP_175815078             450 aa            linear   BCT 11-JAN-2025
DEFINITION  HD domain-containing protein [Granulicatella sp. 20925_1_28].
ACCESSION   WP_175815078
VERSION     WP_175815078.1
KEYWORDS    RefSeq.
SOURCE      Granulicatella sp. 20925_1_28
  ORGANISM  Granulicatella sp. 20925_1_28
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Carnobacteriaceae; Granulicatella.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437595
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Granulicatella sp. 20925_1_28"
                     /db_xref="taxon:3003686"
     Protein         1..450
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52268
     Region          8..420
                     /region_name="YdhJ"
                     /note="HD superfamily phosphohydrolase [General function
                     prediction only]; COG1078"
                     /db_xref="CDD:440696"
ORIGIN      
        1 mteafkrekv frdpvhdyih vqhpiileli nsrelqrlrr ikqtgasmyt fhtaehsrfs
       61 hslgvyeiar ricdnfarny atkeegdglw ddsnrlvvlc aallhdvghg pyshtfekif
      121 dtnheqitid iilseetevn qilrkvsstf pqevasviqk thpnpqvvql issqidadrm
      181 dyllrdayft gvnygtfdlt rilrvirpyk ggiaftysgm havedyivsr yqmymqvyfh
      241 pvsrgmevvl nhllkrasac yhselnplrh satflkpffe gtwtledylr lddgvlntyf
      301 shwlleedai lsdlsdrfin rrpfksvpfn rtndgaqier mkqiveevgf dpeyytainn
      361 sfdlpydfyr pdsikprtqi elverngnmv elsqvssivd aisgkvrgde rlyfpremvs
      421 gemqnglfmd dyaefqniaa qldvfsnqmk
//
LOCUS       WP_175815132             510 aa            linear   BCT 11-JAN-2025
DEFINITION  MDR family MFS transporter [Burkholderia diffusa].
ACCESSION   WP_175815132
VERSION     WP_175815132.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..510
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54322
     Region          23..483
                     /region_name="MFS_LmrB_MDR_like"
                     /note="Bacillus subtilis lincomycin resistance protein
                     (LmrB) and similar multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17503"
                     /db_xref="CDD:341046"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,281,284..285,288..290,293,321,325,377..378,
                     382,386,402,405..406,409..410,413)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341046"
ORIGIN      
        1 mnpaaadaas ppalnrpmlt lsimlatliq tldstianva lphmqgtlsa sqdeitwvlt
       61 syivaaaiat pltgwlsdrl smkrlltlsi agftiasalc glseslvqiv garllqgvfg
      121 aalvplsqsi lldinprekq gqamaiwgmg vmvgpilgpt lggwltdsyn wrwvffinvp
      181 igafalagvl tflparaprp hvkfdafgfa tlalaigafq amldrgeqld wfgsyeirie
      241 alvaalafaf flvhtatvgk asffksellr dpnfatgtlf ifvvgavlya trallppmlq
      301 nlmgypvatt glvtapsgag tmiamlfvgr llkyvdaral lfaglaisal alwqmmqyti
      361 vlseadivwp gviqgfglgl vfvplsalsf stlqpelrad gtatyslmrn igssigisiv
      421 qtlmtrntqv ahadlathit pfdpavqama gshvdialld rtinqqaami aylndfklmf
      481 vatllmipll llirppqkta sadiahaamd
//
LOCUS       WP_175815202             366 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia diffusa].
ACCESSION   WP_175815202
VERSION     WP_175815202.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Saurin,W. and Dassa,E.
  TITLE     Sequence relationships between integral inner membrane proteins of
            binding protein-dependent transport systems: evolution by recurrent
            gene duplications
  JOURNAL   Protein Sci 3 (2), 325-344 (1994)
   PUBMED   8003968
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004772
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..366
                     /product="ABC transporter substrate-binding protein"
                     /calculated_mol_wt=39861
     Region          62..364
                     /region_name="AfuA"
                     /note="ABC-type Fe3+ transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG1840"
                     /db_xref="CDD:441445"
ORIGIN      
        1 mpfapkqlta alaivlgtaa gavvaqvpag ypgnyqgvvd aakkegkliv ysttdtglvr
       61 plikdfesly gvkveyndmn stelynryis enaasstsad vlwssamdlq vklvndglma
      121 sydspesanv pqwaqyqkqa ygttfeplai vynkrlipen evpktradli kllttqadkf
      181 kgkvttydie ksgvgfnylt qdahvnekvt welvkaigat gpklqsstga mmerissgen
      241 ligyniigsy ayakakkdks igyvlpkdyt qvvsrlatis kkaknpnaak lwvdyllsqr
      301 gqtlianqan lyairadvtg etsaasltke lgdslkpiqi gtgllvyldq skrlaflkqw
      361 qqaikr
//
LOCUS       WP_175815214             551 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 32 protein [Burkholderia diffusa].
ACCESSION   WP_175815214
VERSION     WP_175815214.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..551
                     /product="glycoside hydrolase family 32 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=59991
     Region          41..536
                     /region_name="SacC"
                     /note="Sucrose-6-phosphate hydrolase SacC, GH32 family
                     [Carbohydrate transport and metabolism]; COG1621"
                     /db_xref="CDD:441228"
ORIGIN      
        1 mrstffrfsl riarlllact asaacthtsa apcdappepg tpqwrpavhy tpqrnwmndp
       61 nglvyengry hlfyqynplg hdwgnmswgh atstdlvhwr eqpvamrana teeifsgsiv
      121 adtrntsglg apgdtplval ytsvykegsg hapgtqaqsl aysldhgatw rpyahnpvlt
      181 ldpeskqfrd pkvswyapgr ywlmttvvad aqvvklyrsd dlihwsflsd ftlpdvphag
      241 vlwempdlvp lpvdddprhi kwvmivnvnp wsiaggsgam yfvgdfdgrt ftpdhvapag
      301 sdparfrwvd hgadfyaagt fsgtpgarpv aiawmsnwdy aakaptapwr gaatlprefa
      361 lktiggeptl vvtpaaafda wadgrpavhe gnlnvesatr alsdatrgiv qritvtiapq
      421 raaraglivr gsadgsigtr ivydtakrtl tldrsrsgtt dfagtfsreh ivdlplehgq
      481 lrleivvdrg svevfanggr valtdlifpp pdadrvavfa ehgsaafsgl tvtqlhgrdr
      541 tdevrdacas h
//
LOCUS       WP_175815227             255 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175815227
VERSION     WP_175815227.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..255
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=27626
     Region          42..250
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mhdhsvappd aaappdhspa dpplepgplp alsalfgqca wfralapehq alvlaqshae
       61 rheagdviaq rlapseywig vhrgllklai fnasgrgctf sgvpsggwfg egsvikrelr
      121 kyevvavqrs ivlfvpvdtf halldtslpf trfvihqlnn rmgefiasiq nsrlldvdar
      181 vaqalaqlfn palypdtgps laisqeelgm lvgvsrqrin qalqqleklg vlrlaynqie
      241 vvdlaalarv gmeqi
//
LOCUS       WP_175815231             550 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175815231
VERSION     WP_175815231.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..550
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=56509
     Region          15..273
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
     Region          299..547
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mqnhevsadd appkaqrgiq svevggrlld alarrrkplg lselaaaadl staqahtylv
       61 sltrlalvkr daltgnyepg plslrlglms ierqpayraa lphaarlaea vglsvalsvp
      121 gvlgptivri ehggyplhvn lhvgsvmsld ttatgrvfra fgdpaqldam aasqagagdt
      181 lagaegvqpt sdagawqael dairargier gvdrpspgvs amcvpvldae grlqlaltvi
      241 gstgsidvgw dgpiatalrd aarqataslg agrdappiap gvlpatqrmp ptladdtkaq
      301 rginaldstg elllalvsag ralplrdlaa aagmpaakaf phlvslqkig llsrddagcf
      361 gggplaqalg liamqrvspt rdaeaeival aaatdmsvaa atlgplgptv irleesarpq
      421 hvslqvgtvm slvntaigri faagmsddvl aglltdepvr lagratqvdd afrarlatir
      481 adeldfafda pvpgigtiaa pvfdhtgsir lviaiigssr gfprgpesel ahallaatrr
      541 lswrfgwiga
//
LOCUS       WP_175815255             291 aa            linear   BCT 11-JAN-2025
DEFINITION  PilZ domain-containing protein [Burkholderia diffusa].
ACCESSION   WP_175815255
VERSION     WP_175815255.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..291
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30452
     Region          173..278
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mrhitdhval arddvpagvp lgfdlydagg aallpagttl hdpaqhaflf dhfqpvrrrd
       61 dvepavpapd tvpgaarmgl sagaaigirr rvgatrvlqr crligigasg alfvepqpav
      121 vldfargddv eavaigrsav srfgatveav qstgaapfmv lsppgfvdrl rtraeprvqv
      181 riaarctggp vhaegigivr dlslnglsia ldralaaage plhvqlpyad edrvalltld
      241 gtvravhadp avpgwalhha afdetaaddr irlkallfdl smgatdadqv r
//
LOCUS       WP_175815262             766 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Burkholderia diffusa].
ACCESSION   WP_175815262
VERSION     WP_175815262.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..766
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=83928
     Region          178..765
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 msyvvavram ceftarrgdl dlrftpapta legiaghgav tskrgaryet eialtgtwgt
       61 ltvrgradgy dpvanrleei ktyrgsldam panhralhwa qakvyahlmc darglaeidv
      121 alvyfdivse retvltetlg asalaaffae qcacfvgwae retahraard aalraltfph
      181 gqfrsgqrel avsvyraard erclmaqapt gigktlgtvf pllkacgege ldhvffltak
      241 tpgralalea atalgagtpa lplrvlelva rdkacehpdr achgescpla qgfydrlpaa
      301 rdaaigtgll drdtvreaal ahdvcpyyla qelarwsdmm igdynyyydg samlhtlaqq
      361 nqwrvgvlvd eahnlldrar kmysasldpf afaaareaap aalrkafdrl arawgtlnra
      421 qaeryaaype ipgpivtavq nlvaaigehl tdaprangda llrfhfeaiq fgvladafdg
      481 asifdatlhg eplprqsgld gvapaarrrr iqstlcvrnv ipagflasry eaaratvlfs
      541 gtlspfhfyr dtlglpadtg wldvdgpfra eqltvrvash vstrwrdrdr slepivdlia
      601 aqyatrpgny lgflssfdyl grvvalmqtr hpdvpvwaqa pgmaeserda flarfdaggr
      661 gvgfavlgga fsegvdlvge rligafiatl glpqvndvne qmrramdarf gngydymyly
      721 pglqkvvqaa grvirtehde gvvhliddry rrrevrdllp rwwrig
//
LOCUS       WP_175815264             603 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia diffusa].
ACCESSION   WP_175815264
VERSION     WP_175815264.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 603)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12379621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..603
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62789
     Region          1..284
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
     Region          329..603
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 maswldytln glivgniyal lavglalifg vshlinfahg svymvgafig wlcltrfglp
       61 lpvalaavvv gcgalgiaie riglrplrha ariapllati gisfildqlv qlafgadpra
      121 vptplpdwhl riagatlgsl dlliagigia aaallygflr ftrlgwavra taqdrdaalq
      181 mgvdvdrvnq tvfaiacalg gvsgllvgmy ynsidpamgf qatlkgvval ligglgnvpg
      241 aiagslllgl vesygvalfg tsyrdlfafg llivflvwrp nglfsanral ppepmtgtfl
      301 aaakavrvpr pvivvliaaa avlpwlgasp yvlqtltnaw lygllalslt lvagtvgqis
      361 lghaallvig ayasallssd lgwspavtip cagaitavlg tllvypafrl rghyvsiatl
      421 gigevvslvi lnwdgltrgp lgitgiaplp wattaraayw ftfavlvvfa lvqvrllrsh
      481 lgrtlravre ddvaarahgi apnrykaiaf avggvaagvs ggiaahlysy inhqtfdsqv
      541 silaltmvil gglgnvlggi agaialiglp elfrwaadyr mliygvvlll lvrfrpqgll
      601 gav
//
LOCUS       WP_175815287             425 aa            linear   BCT 11-JAN-2025
DEFINITION  GspE/PulE family protein [Burkholderia diffusa].
ACCESSION   WP_175815287
VERSION     WP_175815287.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..425
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=45179
     Region          <21..424
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mhlpppgapl htqrppasid aspaetprsl daaqlddspa vrlltdtlha arvrdasdvh
       61 vepfeagwri rlridgvlhe harppahlrd alvtrikvls rmdiaerrlp qdgrlriavd
      121 ggmrgdyrvs slptlfgekl vlrrletlpp dltlarlgfd arqaaameaa iraphglvlv
      181 tgptgsgktl slycalqmld rdahnvctve dpaeiqlegi nqvgvaekag ltfatalral
      241 lrqdpdvimv geirdaetad vaikaaqtgh lvlstlhtnd aptavarlld igvapynlaa
      301 alrlvtaqrl vrrlcticrv rsdasaralr eagcdsaale sgwrpfvarg caachgigyr
      361 griglhqtmp vspamaeriv arasvgtlaq caasegvcsl rdaalahvrd gttsiaeala
      421 atpda
//
LOCUS       WP_175815273             325 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175815273
VERSION     WP_175815273.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..325
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34359
     Region          6..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..302
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176149"
ORIGIN      
        1 medidlnlvt aldvlltegs vtgaarrlgl stsamsrtlt rlrtatgdpl lvragrrlvp
       61 tphasalrdr vhaiaseara vlrpatadld matlsstfti raaasfmdml agpvvaaige
      121 iapgvrvrfv arldrdpgpl rdgtvdleig krgddapelh trelfhdghv avaraghplf
      181 aatritpary aacrhviasq lgdfggpand pagtlapaqv vqvvvpgypd amrvaagtdl
      241 ialvprsslg naftpglvda lglrtftipv rlpeilisal whprmqrdpv hrrlrdavid
      301 vckraypaar aprarargtq tgaad
//
LOCUS       WP_175815317             220 aa            linear   BCT 11-JAN-2025
DEFINITION  histidine phosphatase family protein [Burkholderia diffusa].
ACCESSION   WP_175815317
VERSION     WP_175815317.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..220
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24336
     Region          6..204
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mtttqilfir hgetawnrik riqghidipl adtglgqaqr lavrlareah egqridaiys
       61 sdlmraqqta qpfadalgls lrlreglrer aygvfqghds teietlfpda yaawqtrdpg
      121 fapdggesqr afyhrvlhal epivaahqge riacvahggv ldcvyrfang ldlsaprsyq
      181 llntsinvvd yvdgraqvvq wadvshldta sdddgyrkvl
//
LOCUS       WP_175815308             215 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175815308
VERSION     WP_175815308.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..215
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22644
     Region          14..129
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          80..209
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mkdkpaqgpr gldkdaivaa alalleevge aafsvrklaq svgcdpmsvl yhfkskegls
       61 raianalshs lapvdpslpw rerlldlarq yralalrhpa afallqrhms tgpadlahie
      121 tvhraladag iprsalptvc vgwyasvigl aaaeaggltr pandvelaem halsdtahpl
      181 vksaaplyaq ldpaavhdtm ldvlldgiaq hvrat
//
LOCUS       WP_175815328             275 aa            linear   BCT 11-JAN-2025
DEFINITION  carbon-nitrogen hydrolase family protein [Burkholderia diffusa].
ACCESSION   WP_175815328
VERSION     WP_175815328.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10166075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..275
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30340
     Region          12..272
                     /region_name="nit"
                     /note="Nit1, Nit 2, and related proteins, and the
                     Nit1-like domain of NitFhit (class 10 nitrilases);
                     cd07572"
                     /db_xref="CDD:143596"
     Site            order(50,106,123,127,138,163..164,166..167,186)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143596"
     Site            order(50,123,163)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143596"
     Site            order(124..125,144..146,164,167..171,173..174,194..195,
                     198..199,201..203,205..206,236,266..267,270..271)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143596"
ORIGIN      
        1 mtdharsatp frvaalqmvs tpdvarnlae agrliaeaag dgaqlvllpe yfcfmghrdt
       61 dklalaepyr dgpiqrflse aahrhgiwvi ggtlplkape pdrvlnttlv fdptgneaar
      121 ydkihlfnfe kgdesfdear tiragdtvvt fdapfgrvgl svcydlrfpe lyrrmgdcal
      181 ivvpsaftyt tgrahwemll raravenqcy vlaaaqggkh engrrtwghs mlidpwgeiv
      241 avrdegasvv tgaldpqria dvrqslpawr hrvla
//
LOCUS       WP_175815443             656 aa            linear   BCT 11-JAN-2025
DEFINITION  beta-galactosidase [Burkholderia diffusa].
ACCESSION   WP_175815443
VERSION     WP_175815443.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 656)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448998
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..656
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73239
     Region          1..606
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
ORIGIN      
        1 mhlgvcyype hwpreqward arrmaelglt rvriaefaws rmepepgryd wawldeaidt
       61 lasqqlkivl gtptaappkw lvdrhpeilp vgadgavwqf gsrrhydias pvyrehcvri
      121 adamarryga hpaviawqtd nelgchntlp sytraalegf rawlavrygd igalnrawgn
      181 vfwsmeyrgf deielprhtp tdanpahlld frryqsdeva rfhavqvdai rphapgrdvl
      241 hnfmgfftef dhyafarggl dvaawdsypv prtevlplde adkrrwartg hpdvsafshd
      301 lyrgvgngrm wvmeqqagpv nwgpynpvph agavrlwtwe afahgaelvs yfrwrqypha
      361 qeqlhsglna pddrlspggh evarvarela aldiglvtgt heparvallf dyaadwmiri
      421 qphgadfdyq qhafdwyral relgldvdiv aadadvsrya lvvaptlpvv pdrvveqaac
      481 gdahwlfgpr tgsrtaefai apglapgklr dvltvrigqv eslrpsltpr vafdgvdgha
      541 lkwrdhvdme satgidvlaa cddgvpalvr rgrvtmatac fdhallraiv arcardaglp
      601 vralpdgvrl rrrgrlvfal nygdapctlp apdcarfvlg gpelgavdva awvepd
//
LOCUS       WP_175815449             399 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar ABC transporter permease [Burkholderia diffusa].
ACCESSION   WP_175815449
VERSION     WP_175815449.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..399
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41836
     Region          25..399
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mntelsssta vppdaearrt hghplrqifv rykvlallfa vaaiwvffsv ltdgafvtpr
       61 nvsnllrqms itgmlacgmv fviiageidl svgsllgllg gvaaildvnr hwpvaatvpa
      121 vlalgvlvgl fngwwstyrr vpsfivglgg mlafrgillg vtggstiapv sdgfvfigqg
      181 ylpraagdgl avllfalval lvirqrgtrh ryrlavvplw qdvakvvgag avlfafvatl
      241 dryggipvpv llllallgaf swiatqtvfg rriyavgsnl eatrlsgvdt drvklaifal
      301 mglmcafagi vntarlaags psagtmgeld aiaacfiggt smrggsgtvy galigalvma
      361 sldngmsmld vdaywqmivk ggvlvlavwi dvvsrsnrr
//
LOCUS       WP_175815459             648 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 3 protein [Burkholderia diffusa].
ACCESSION   WP_175815459
VERSION     WP_175815459.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 648)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..648
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=70149
     Region          68..603
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mlsilavsgc gtshpesskq vrlaggaipl ihadgllfrd ldrsgvlepy kdwrrpaavr
       61 aadlvsrmtl eekagammha nppakeaagv pgagsvwdma avgrlvldrh vtfflnrlka
      121 dpaslanqqn alqaiaeqgr lgipvtissd prsqfsyaqg vsvdagaftk wpdpvgmaat
      181 gdpelvrrfa dsvrreylav girmalspqa dlavnprwhr ssgtfgsdpa asarfvrayv
      241 agmqdgesgi hrssvvsvik hwvgygatmn dgadahnyyg rlldidgani erhimpftga
      301 ftarvgavmp sygmpaapfr vrgsaepvep vgmgfnraml tdvlrgrmgf dgvvlsdwqi
      361 tddctrvcrn ganpgekpqf sdiampwgve aldkagrylk aidagvdqfg gtsdpeivvg
      421 lvrsgrldvs rvdaavrrim tqkfeqglfe dpyvdagras sivgnaefrr ialdaqhrsq
      481 vllkngrhll pvsrrmtkvf vygfdaeamr rrgftvvqrp eeadfavvgm atpfevlhpn
      541 fffgaryreg strfraddpa favlenaaav vptiasiyme rpidlsgian rataivanfg
      601 aapdaivdvl tgesdpvarl pydlvwtdrl heqtnepvsy rmgeglky
//
LOCUS       WP_175815513             137 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175815513
VERSION     WP_175815513.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..137
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14258
     Region          18..66
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mpfpvqtlsq lrpilvgfrk sagltqaqla arlgvtqqsy aqleanpsav sierlfkvln
       61 vlgvrltlvp gtpddttvpd dttpalkrap aargrspgss dvparppaaa kapsaaarkr
      121 saaatpgksr nptredw
//
LOCUS       WP_175815471             286 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia diffusa].
ACCESSION   WP_175815471
VERSION     WP_175815471.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15202679
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..286
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30290
     Region          12..132
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          168..273
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 madlnssstl tyrpfaetdl paalrlseav kwphrlddwr fafqlgsgfv aedesgivgt
       61 algwrfgesh aslgmvivsp erqgrgigre lfarvvdslg artillhatp sgeplyvkfg
      121 faaigtidqh qgaafqppli slppgerlrp lgtndgprla alasraagyp rdavidallg
      181 vangialdrd gellgfalfr rfgrghvigp viapdalraq alishwlalh egmfvrvdvp
      241 gdsglsdwlq glglprvdtv vamargaapa rdpalrafai vnqalg
//
LOCUS       WP_175815527            1055 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia diffusa].
ACCESSION   WP_175815527
VERSION     WP_175815527.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..1055
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114349
     Region          28..1032
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnarehepst dgtlartgaa shdgggfnls awalkhqqlv ifliglatif gvigytrlaq
       61 sedppftfrt mviqtywpga tarevqeqvt drigrqlqaa pyvdniksys rpgesmiffa
      121 mkdsapvdqv petwyqvrkk vgdiratlpk gvvgpffnde fgdvytniya legdgyspaq
      181 lhdyadklrt vllsvpgvak vdyfgdpaqh vfveisnaql trlaitpqql aqaidaqnav
      241 apvgtittad drvfvrpsga fkdtqaladl lidvngrtfr lgdvakvtrg yddppvtqmr
      301 tnghavlgig vtmqkggdvi dlgkaldaka aelqrglpag lklaavssmp havkhsvddf
      361 veavgeavai vlvvslvslg lrtgmvvvit ipivlavtal cmhafgigld kvslgtlvla
      421 lgllvddaii avemmavkle qgwsrtraaa faytstafpm ltgtlvtvsg flpialakss
      481 tgeytrsife vsaislivsw faavvlvpll gyhmlpehth rdghahgdev ydtgfyrrls
      541 gwisacidrr wivlgvtavl faiamvaftr vpqqffpnse rpellvdlrl pegasfdatl
      601 reakrlekal ngrpeidhvv dfvgtgaprf ylpldqqlqq pnfaqfvita kdvetrdqls
      661 hwleatlasr fptvrtrvar lengppvgfp ikfrvsgddi atvrgiaekv adkvradart
      721 rnvqfdwdep aersvsfeid qlkarqlgvt sedvssflam tlsgytvtqy rerdklidvd
      781 lrapkserid psklaglaip tphgpvplgt ighvrdtley gviwerdrqp tvtvqadvrg
      841 eapsigvtrd ldaalstlra tlpagyriei ggaaeesmkg qtsinaempl miiavltllm
      901 iqlkrfsrtf ivvltaplgl igvvaalllf gkpfgfvall gviamfgiim rnsvilvdqi
      961 dqdiaagqpr ftaivgatvr rfrpimltaa aavlalipll rsgffgpmat almggitiat
     1021 vltifflpal yatcfkvrad eresramdva ssetc
//
LOCUS       WP_175815535             744 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia diffusa].
ACCESSION   WP_175815535
VERSION     WP_175815535.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..744
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=78353
     Region          75..>209
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          217..737
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msrglieagk vagqaagagv srrsflkagi slgaaagggl llgfsmpaag ddarrsvigg
       61 dadesaragv fapnafvqid rsgkvtlvmp kvemgqgvyt alpmliaeel evplsnvtld
      121 happneklfl dpllggqltg gstsvryawe plrragatar tllvsaaakq wsvdpatcra
      181 engevrhlps grrasygqla daasklpvpk dvalkqpadf kligkpvkrl dspekvdgta
      241 qfgldvrlpg mlyavivnsp vfggtvasvd dtaakkipgv rqvvradnav avvgdhtwaa
      301 krgasalvvk wnegagakvs tkdivadlaq aaangkgava rkdgdvgkaf agaktridav
      361 yeqpllahat mepvnctvhv rgdgceiwvg tqvptravdt vqrltsfppe kivvhnhllg
      421 ggfgrrletd migqavkiak qvnapvkvvw treediqhdm yrpyyydris agldangkpv
      481 awqhrivgss ilarfappaf kdgvdpdave vatdlpydlp nqlidyvrqe prhvptafwr
      541 gvgptrstfv vesfidelaa qtktdpvqyr rallgktpra lnvldvatka agwgaplpkg
      601 qgrgvsvmha fgsffsivid vavesgevqv kravcavdcg mavnpgtiea qvqggiifgi
      661 tgalygeiti edgrvvqsnf tdyrmmrine tppievhlvk saeapggige pgtaataaal
      721 snaifaatgt rlrklpvgnq lkta
//
LOCUS       WP_175815638             313 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175815638
VERSION     WP_175815638.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..313
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34822
     Region          59..295
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          223..295
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpstapprly gmpersdrld fyirdqasrq aitephrhay fqiqfnlggd teqriggvtr
       61 pfprgalafv lphrehliph pegahfivin fsqaflradl dvdpldledv pahrfpeltp
      121 frfqehldfi ltgdafdear rlalcmldad rvrtfgsstl lrgyllqlig lvctqyagal
      181 dklaqrgaqr agrrdalarv lrhvranltr edltlaatae aaflspnyla hlvrketgst
      241 ftdlvterri alaqsllaht srriadiars vgfrdegyfa rrfrarvgvs pkayrdanaa
      301 lpaaddapaa gda
//
LOCUS       WP_175815643             646 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Burkholderia diffusa].
ACCESSION   WP_175815643
VERSION     WP_175815643.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 646)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 646)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 646)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19997826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..646
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72758
     Region          7..357
                     /region_name="AAA_15"
                     /note="AAA ATPase domain; pfam13175"
                     /db_xref="CDD:433011"
     Region          <201..498
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mlvglflrhy kvykninfvp ittgaglaaf lgqngvgkss ildaldkffn ggdwsinaqa
       61 kneggisted kvpyivpvfl iekgllshne eatakvisdy lwatmlkttd alsgfyalrs
      121 sllengfnse thllvtigrq hnrsvaylgs fhtdselnks lkasektqsn lndllekise
      181 ryayfyipve adptifskle sthvqkllde diqgairdai gsktintint slqsfinqis
      241 dslidyrykg tfkdrltmnd lvekvfeayf sikvlhkvsn sssipirems agekrralid
      301 lsysllrrna drkhniilai depdaslhns achelfskla eipyltnpns qvlitthwyg
      361 flpivqkgva hsitegagri efftfdlynf reqikqavkk sngelprdie lksyndmlqa
      421 ivsstvrpqp ynwilcegls dkiyldfylk dlvenhnlri iplggfkevr rafnylktpl
      481 ddpeykvkgk vlclvdtdah lenvsskpes ksidflrliy daekndvklv kiddqlvsps
      541 teiehalegd rfvrtvseid aefggkalkd ivassklvdd ascsyahldl tpsankrmmt
      601 eyfdvgdnkv kfaqayikan esvtsppewi kalrehfssp pkkkkr
//
LOCUS       WP_175815645             310 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175815645
VERSION     WP_175815645.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33618
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like_2"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08471"
                     /db_xref="CDD:176160"
     Site            order(102,106,145,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176160"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176160"
ORIGIN      
        1 mdklremevf vavvdrgsft aaseklglst aavsravhsl etrigtqlla rttrsvratd
       61 agtiyadacr kvldvitdae vniatdhenp vgtltisapv lfgqrfiapl vnafvlrypd
      121 vdvnavyvdr ttrlleegvd iairighlgd ssvfalplgv vrrrtyaapa ylaahgepah
      181 prdllhhdcv sctgvslple wvfhdngsrv pvrlrprmiv dlvpaavlaa vdcvgvtqll
      241 syqaapevrd grlrpiltaf ehepipvsll hverrgasgk vrafvdfvth tlrnnaelqg
      301 tdvnatrssr
//
LOCUS       WP_175815678             306 aa            linear   BCT 11-JAN-2025
DEFINITION  bestrophin family protein [Burkholderia diffusa].
ACCESSION   WP_175815678
VERSION     WP_175815678.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..306
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33397
     Region          1..306
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 mivrprehwf rmllvwngsv lptilpqlal tlaislvavw gggrllgekv plnptpftli
       61 gltlaifagf rnnasyeryr egrqlwggvl tatrtlvsqa lcygaidgdd aarqafvrkv
      121 vafvhalkhq lrgtdpaadl rtlldgatft rivaarfapi aivhelreaf aaradaghla
      181 dtrlwmldvr lddlvstvsg ceriastpip fsydvllhrt iyaycvllpf glvdsigaat
      241 pfvtvfvayt lialdaiaha iaepfgdgpn qlaldamtrt iertllelnr epllaevtps
      301 payrlt
//
LOCUS       WP_175815697             475 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175815697
VERSION     WP_175815697.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..475
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50615
     Region          40..459
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(50..51,54..55,58,90,140..141,143..145,148,171,
                     174..175,178,287,290..291,294..296,299,328,332,388..389,
                     393,397,413,416..417,420..421,424)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mssidlnavt pvsapirsas dvarlinstd ssvgharmiv llalggvfld aydlttlsyg
       61 iddvsrefgl tpaltglvgs aimigtifgs liggwltdki gryqvfmadm lffviaaiaa
      121 glapnvwvli garfvmglgv gidlpvamaf laefskfsgr gnkasrlaaw cpmwyvassv
      181 cfllifgmyf llpaehagwl wraslifgav palviilvrn rfmnesplwa anqgdlanaa
      241 rilresygih aheaddvpra psqppvrirv lfqrpylgrt ivasvmnlci pfeytaiaff
      301 lpsilsqflg agvfetiaas lalnvlfaft ggllgmrlay rypsrhvaia gfalqfvalv
      361 alalaghphg alavglvllm lgtwlfaegf gpgaqmmiyp tlsypaairg tgvgfgrslc
      421 gigqalalfv lpilqarlgt dmfwvvavsa atpivflliv rheptardid deaaa
//
LOCUS       WP_175815703             214 aa            linear   BCT 11-JAN-2025
DEFINITION  trimeric intracellular cation channel family protein [Burkholderia
            diffusa].
ACCESSION   WP_175815703
VERSION     WP_175815703.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..214
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22783
     Region          5..203
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mnshtayftl dlvgtfvfam sgavaarqkr ldlfgilsia fmvacgggiv rdvcigaipp
       61 aglsnwryla asvlatavai fayapvrrlr qpvlffdaig lglfavagaq kalsfghnae
      121 laillgivta vgggvmrdvv lsrlpaildr evyataalag agtqvlfssa hwtqwwtpwf
      181 atilcvairl aslrfgwrlp nfrgqrasel pdde
//
LOCUS       WP_175815714             226 aa            linear   BCT 11-JAN-2025
DEFINITION  urease accessory protein UreF [Burkholderia diffusa].
ACCESSION   WP_175815714
VERSION     WP_175815714.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Soriano,A. and Hausinger,R.P.
  TITLE     GTP-dependent activation of urease apoprotein in complex with the
            UreD, UreF, and UreG accessory proteins
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11140-11144 (1999)
   PUBMED   10500143
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Moncrief,M.B. and Hausinger,R.P.
  TITLE     Purification and activation properties of UreD-UreF-urease
            apoprotein complexes
  JOURNAL   J Bacteriol 178 (18), 5417-5421 (1996)
   PUBMED   8808930
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..226
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23934
     Region          1..226
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 mtttelvall hlaspalpig aysysqglea aldanlirda dtardwiasg ltdvlahgel
       61 pflahqlarw qahdadalar enawfvasre saelrreteq mgwslghlca slewgdaarr
      121 atlaslspva lptafayaaa ahdagadatl aayafgwven qtsaalkavp lgqlagqrii
      181 valrgaidaa vrralatppd aintfapqlg ilsarhetqy srlfrs
//
LOCUS       WP_175815769             301 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175815769
VERSION     WP_175815769.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..301
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32679
     Region          19..>115
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          <146..301
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msatrllpds arywrtpllp gadlltatyr dhtfaphwhd aytipvileg aerytcrgsg
       61 hvaetgtvpv inpgevhtgs ratdegwcyr vsyvpvdyir alasaiagrp qdapwfpsdv
      121 irdadlaarl alahrmmeag secmpafhph erpaadapaa aaarvydpla aetamldals
      181 tlitrhadar lqpavlaade prvdamrerl aadlsctvtl ddvaqaagls pfhaarlftr
      241 tigmpphawr nqlrlqrala plragvsiad vaaasgfvdq shfsrhfkrm fgvppgrwqa
      301 r
//
LOCUS       WP_175815747             395 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia diffusa].
ACCESSION   WP_175815747
VERSION     WP_175815747.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..395
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=42140
     Region          161..392
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mseitpspag lpgtssastd fsrsrpahtp easatqaaaa qvvtadgasp vtaasepgaa
       61 gttgaaaega avppkpgaap pgfgaqpdfd tprpppasaq nappaylkqs dtpwsvfgri
      121 iaararrifd ragqritqrt lrigvsarif hpepgakglr gktlqylees iahwvmsrdv
      181 lvfmiptvgh qgmlhpsnir lrdyakhldg lllqggadvs pqtyaasdar pewpgdrvrd
      241 myelelfhef vesgkpvlgv crgcqlinva fggslyqdia tdvptanahv sehydqhrha
      301 irfpdsstla smfpgrseai vnsihhqair dlgrdlniea vsagdgiieg iryrrapfvv
      361 gvqwhpefhr aggaelldct plldaflraa rdtrl
//
LOCUS       WP_175815793             503 aa            linear   BCT 11-JAN-2025
DEFINITION  HDOD domain-containing protein [Burkholderia diffusa].
ACCESSION   WP_175815793
VERSION     WP_175815793.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..503
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=54697
     Region          18..218
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 msitahlprt alldklwarm nergdfplls eslratmaam knddldftal vsvvlsdfal
       61 tqkvlrlans amymafggni ttvtralmvl gmdtvghlvv glklvdhfhq stprridakl
      121 elnrallsgc varkltehae lrggeeavvc tlmrqvgkll vvcyldsewd rirrraaeln
      181 gdeaaacvdv lgvgfdeigl eaaaswrlpd viragmadgd ggsahaagld eddidedrqr
      241 prdacaddsp ervrwlravs rcstdvagal ampagpqrda hiaalaqhya qeldidadal
      301 veiadrlare easdtvmrei velranadai araqpdpeac leagladlra lpsehvltpv
      361 lalaseslla glaftrtvmf vrredgafaa rlgfgpdvda aldrlcfder fepdvfhlai
      421 tnsvgifieq aqdpkmvkrl pawylnalpg trafvllpvr vgtktvglly gdwagaqpar
      481 kitqqemsvl nelarelgrf fpa
//
LOCUS       WP_175815799             257 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia diffusa].
ACCESSION   WP_175815799
VERSION     WP_175815799.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..257
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27883
     Region          1..>240
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mnllelddlc vaydtphgrr tvvdglslal prgdigcllg asgcgkttvl raiagfepvr
       61 mgrivldgap vaapsldvpp errrigmmfq dyalfphlsa adnvafglrr mpkaerrarv
      121 admlelvgla asgsayphel sggqqqrval aralapspel llldepfsnl dvdtrerlaf
      181 elrdilkrtg htailvthnq aeafaiadri gvmkdgqlaq wdtpyalhhh paspfvaefv
      241 rrdaladera ralsrgr
//
LOCUS       WP_175815808             445 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrolipoamide acetyltransferase family protein [Burkholderia
            diffusa].
ACCESSION   WP_175815808
VERSION     WP_175815808.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..445
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47551
     Region          2..445
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mgihvikmpd igegiaevel vawhvqpgqt iaedqpladv mtdkaaveip spvagkvlel
       61 ggrigemmav gselirleve gegnlkpgak ardagaevtq ppaavdvrae pssiaegset
      121 hasptatppa asrvpaetrr aehavppraa lapgerplas pavrqrawdm gielryvrgt
      181 geagrilhad ldayartggg aprgsqargy derndetdvp viglrraiar kmqeakrrip
      241 hfsyveeldv teleslrael nrrhgdtrgr ltplpllira maialrdfpq inaryddeag
      301 vvtrygavhv gvatqtdggl tvpvlrhaea rdvwsisaei arladavran raqrdeltgs
      361 titisslgal ggivstpvin hpevaivgvn riverpmird gaivarkmmn lsssfdhrvv
      421 dgadaaefiq avrgllerpa llfve
//
LOCUS       WP_175815859             101 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF485 domain-containing protein [Burkholderia diffusa].
ACCESSION   WP_175815859
VERSION     WP_175815859.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..101
                     /product="DUF485 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=11054
     Region          6..100
                     /region_name="YjcH"
                     /note="Uncharacterized membrane protein, DUF485 family
                     [Function unknown]; COG3162"
                     /db_xref="CDD:442396"
ORIGIN      
        1 mqhsfiesvt arrdyqqlvr arrrfsftlt almiatyygf illvalaphv laaplyrgat
       61 ttvgiaagva iilvaiglta cyvlranraf drrvdailqr s
//
LOCUS       WP_175815861             381 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia diffusa].
ACCESSION   WP_175815861
VERSION     WP_175815861.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..381
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40604
     Region          1..376
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfqhtedrr mladtlnrfi aeqyaftvrd riaqstdgfd ramwqrfael gavgalfpea
       61 dggfggagfd iavvfeclgr glvvepflga llagralsla gghahrerla alidgrasaa
      121 fahdepgshy elttvhtrae ragdgwvltg akgvvdqaaq aaffvvsarv sgrdddaagi
      181 glfvvpadap gvslrdyrki dggraaevrf ervalpadaa lgapdaldge agaallervl
      241 gygllalsae algamdvakd atldylrtrk qfglpigsfq alqhrmadll leveqarsav
      301 inaaaqldap rvvreralaa akysigrigt lvaeesiqlh ggigmtwelp lshyakrlvm
      361 idhqlgdedh hlaryialsk q
//
LOCUS       WP_175815888             396 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia diffusa].
ACCESSION   WP_175815888
VERSION     WP_175815888.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..396
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=42105
     Region          18..381
                     /region_name="MidA"
                     /note="SAM-dependent methyltransferase, MidA family
                     [General function prediction only]; COG1565"
                     /db_xref="CDD:441173"
ORIGIN      
        1 mnpkahepas lpapgpdala qsetlaaqlr deiaaaggwl pfdrfmeral yapglgyysg
       61 garkfgrrad dgsdfvtape lsplfaqtla npvaqalaas gtrrvmefga gtgklaagll
      121 aaldalgvel deylivdlsg elrerqrdti aaaapalaak vrwldalper fdgvvvgnev
      181 ldampvrlfa kadgvwlerg valdarhafv fddrpagaag lppvlatldv ddgyvtethe
      241 aalafthtvc tmlgrgavll vdygfpahey yhpqrdrgtl mchyrhhahd daflypglqd
      301 itahveftgi ydagvatgad llgytsqarf llnagitdal aaidpsdihq flpaanavqk
      361 liseaemgel fkviafsrgi dgtldafarg drshal
//
LOCUS       WP_175815949             486 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia diffusa].
ACCESSION   WP_175815949
VERSION     WP_175815949.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..486
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50123
     Region          31..475
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,156,
                     159..160,163,291,294..295,298..300,303,333,337,390..391,
                     395,399,415,418..419,422..423,426)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtdntlapca pagtaaaapp rshhgwalvv llvgailppl dyfivnlalp airdgigarp
       61 selqlvvsay acanavvqit ggrlgdlygr krmfmigmag fvvastlcgl agsgavlvgg
      121 rvlqglfaav lapqvlatir svfspqeqvr vmgfygfvfg laavigqlgg galislhpfg
      181 lgwraiflvn vpigvfallg swhfipesrp prgqridvpg tvllsllllm lvyplthgre
      241 agwplwmvac iagalpmlga llavearria gghdplldvr llrnpvvvlg ltlaflfyml
      301 safflsygiy lqgclgwspl asglailplg igflaspllm prlvdrfggh rvlmlgfaml
      361 aagvataaal agehapgpgf yagiaaigig qglvlpsvvr ivlaevdaar agvasgmvst
      421 mlqigaavga atlgglffar lgaqpgaldy vqgfrtamwa ltvvllvcva lsaalgpmhr
      481 rvragt
//
LOCUS       WP_175816015             770 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia diffusa].
ACCESSION   WP_175816015
VERSION     WP_175816015.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 770)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 770)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..770
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..770
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=83814
     Region          68..740
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mfrkklivta lgglltggav slpawaedga vaaapdakpa qqgaddaaaa aptaaratrr
       61 aaaretnlgt vtvtarrrke siqdvpvavs alsgdtirnn elrvvndvtk yvpnftgqst
      121 egrerprwfl rgvgsndpsd lslspigvyf ddvyinsvfg qgfplfdldr ievlrgpqgt
      181 lwgkntvgga lsitsqkptf dvsgygkigi gqynsrlaea aiggpigknd vlaarvsvyh
      241 enadsfytnt vqqgrfggfh dnavrfqvla vptsdtdflf nihgrnytgg gnawhaqgag
      301 pgganqfgfv gssdpytvsl napsndhist wgtsltahwr inpavtltsi tafeglhrwy
      361 qddedysafd aarshdrlss rqfsqefrle spqsdrlswl vgthlfteql aeqgaggglp
      421 gapspafyhl tdltqhtqsa aifgsvkyrf tdrfnvtggl rytierknin ltglqnagnv
      481 tfsnpgswwd pssvssplav sarqnqtntw raptwdltpe yalssnvray fryargfrsg
      541 gyngnaytqs tvstvspeyl tdyevgikse wfdkrlivna svfhydyrdi qvfalapnpf
      601 ggppvstlsn agqgradgfe lelkaqpvns lylfanlgml ntrytefryv ptavgnsfar
      661 sphttinagf dyrvpvsvgt ltaggdvnyr sreyfsatrq tmpqlwqggy tvlnahvsyt
      721 tpnqkyivtg yvtnltnkvy kklellpsyg aypvlygdpr tvgltftaki
//
LOCUS       WP_175816091             368 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia diffusa].
ACCESSION   WP_175816091
VERSION     WP_175816091.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..368
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39611
     Region          17..347
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(36,38,69,111,239,300,321,323..325)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(36,38,69,111,113,120,187,190,192,239,246,300,321,
                     323..324)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(38,113,187,190,192,324)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            192
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mkqlfvpapt dqdtpqlftp vrvgrytldn rlvmapmtrs raafdgtpga waaeyyaqra
       61 glglivtegt qpsadgqgyl ttpgiytdah vagwkrisdd vharggrlfi qlmhvgrmsh
      121 pdntphhrqg vapsaiapgv pmftatgmqe ipapraltta evrdtvndfr faarraieag
      181 adgveihgan gylvqqffap nanmrtdeyg gsienrarfa ievaaaiade igadrtairl
      241 spgttlwgid egpesaelyr ylatqldalg laylhvmhqg deslladlra rwrgtlilnr
      301 pgrtrdaiga dvvsgladle aygqmvlanp dfvtrvktga pmndaqretf fggdargyvd
      361 ypalsgaa
//
LOCUS       WP_175816216             564 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia diffusa].
ACCESSION   WP_175816216
VERSION     WP_175816216.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..564
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=61364
     Region          72..450
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mtrlaisprf gatvlvlafl agcttfskdg gfdavssias erigkvaviv rtdadraavd
       61 krtkellekp lsmddavqla llnnrglqas yaelglsead lvqagrlpnp rfsfsrtrag
      121 dgelslgrtf sanvfalltl platnierrr feqtrletad amlrvaadar rayveavaae
      181 qaanyaqqvr daasagaela lrmrqagnfs rldyareqaf hadavaqqak arqqavaare
      241 kltramglwg ertryalpgr lpdlpkarpd lpdleryams nrldiqaakl qtrgvasslg
      301 lskatrfvnt vdlgyvnnye takghehgye isveiplfdw ggakvaraea vymqsanrla
      361 qtaidarsev resyaaytts ydvakhyrde vvplrktisd elllryngml asvfellada
      421 reqvgavngy idalkdywla etdlqaavgg rlptaqpmqp mqpmqpmqpm qpmqpmqptq
      481 ptqptqptqp tqptqptqpt qptqptqptq ptqptqptqp tqptqptqpt qradapvapt
      541 tdaapqpass pvaqpapath pegh
//
LOCUS       WP_175816283             400 aa            linear   BCT 11-JAN-2025
DEFINITION  benzoate/H(+) symporter BenE family transporter [Burkholderia
            diffusa].
ACCESSION   WP_175816283
VERSION     WP_175816283.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..400
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41473
     Region          11..399
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mqpntspgai rsigndwsvs avtagflavl isyagplaif fqasqaahvs nemvaswvwa
       61 isigagvssl faswklkvpi vtawsapgta llvglfpqlt lnqavgayit aaliilvigi
      121 tgyfdrlvrh iprgiacgmm agillpfgmh afsaataqpv lgfgmiaayv ifkrllprys
      181 ivlvlltgaa latllgmahl gnvspsiarp ifiapewtlg ttlslalplv vvsltgqflp
      241 gmtilrvsgy htparpiita tsvmslvvac fggitivvaa itaalctgkd shedpdrryi
      301 agiangviyl igglfagtiv tlffalpkaf vailaglali gaiganvhgi fedeahreas
      361 vitflatasg mtwlglgsaf wgivigsvay avtswarrqa
//
LOCUS       WP_175816308             204 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175816308
VERSION     WP_175816308.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..204
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22340
     Region          11..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnthddfsge pavrdrllda aealiysggi hatgvdaivk rsgaarksfy shfeskealv
       61 vaalerrder wmhwfvdatl argksprahl lgmfdvlrdw fsqpdfhgca flnasgeiad
      121 addpirvvar mhkarllafv rerldayadd agierrglar iarqwlvlid gaigvalvsg
      181 eataardara taellletvs rask
//
LOCUS       WP_175816310             337 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Burkholderia diffusa].
ACCESSION   WP_175816310
VERSION     WP_175816310.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..337
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=37672
     Region          31..304
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mslptpsdtp arpeetdlfd rgasdwiisp eaafdawlam qdyrrssadv yraqwgafla
       61 wlrahqknla tvdtatianf vselpirktq rmrylrlier vldhirrtel astnparfia
      121 qdgeadwrqa rdneptgflt paerakllay lfspigvsgs aywkerrdra lvaaflgagv
      181 ktgearalti scinasgtsl qipsthpdfa rethlasfai alleawlver krqeipgelv
      241 fpashagrpm hkatmlraid aivesaglts srtaraspqt lrntyaaelf ehdvppervg
      301 kwlgfmrpis snrlhrawkn wrddlangda sqqdeth
//
LOCUS       WP_175816388             473 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Burkholderia diffusa].
ACCESSION   WP_175816388
VERSION     WP_175816388.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..473
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52454
     Region          5..446
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mdtafsaldl arlqfaftvs fhivfpalsi glasfiavle yrwlktgkqy yktlclfwsk
       61 ifavafgmgv vsgvvmsyqf gtnwsgfssf agavtgpllm yevmtaffle agflgimlfg
      121 wnrvsprahf gatlmvaigt listfwilas nswmqtpqgf eivdgrivpt dwfaiifnps
      181 fpyrlfhmai aafivaalvv aatgawhllk grrdkgvrkm fsmalwlllv laplqavigd
      241 qhgintlkhq pakiaaiegl wetekggtal nlfgipdmqa ettryavkvp hlgslilths
      301 wdgeirglkd fppedrpnst vvfwsfrimv glgfamigla alawllrrrg tlyeskwfqr
      361 falvmgptgf vsllagwvtt eagrqpwvvy gvmrtaqavs plsvqqvsls mmtfvivyfl
      421 vfgtgvyyml klmkagpalp dvkhdpkhdm pdtrpdhtar rpmsavdeli etv
//
LOCUS       WP_175816345             395 aa            linear   BCT 11-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Burkholderia
            diffusa].
ACCESSION   WP_175816345
VERSION     WP_175816345.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 395)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..395
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41377
     Region          40..393
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mtqlfdtlgf ieasavraga gvhahgahde aagradgvav slahvgkvfa tprgqaaalr
       61 dvtldvrrge vfgiigrsga gkstllrlmn glerpssgrv cvqgvdvgal dedglvalrr
      121 rtgmvfqhfn llsaktvfen valplkiagv pkaervrkve allelvglta krdaypasls
      181 ggqkqrvgia rslvhdpevl lcdeatsald pettqsilal ladinrrlgl tivlitheme
      241 virevcdtva vieqgevvet gpvwrvfgdp rhgatralls tivhdlpael aarvrplpeq
      301 aalpdgaqvv ldvrytgesg gepdvgalaa alggsvrflh ggidriqgha qgrlviaatp
      361 radeagqssa rggavaalle rarrhanhae vlgyv
//
LOCUS       WP_175816472             669 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Burkholderia diffusa].
ACCESSION   WP_175816472
VERSION     WP_175816472.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 669)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..669
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=72161
     Region          22..660
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mrddvhptan arathapgwp tptiqksher setfglqasa rpdydllsgt alalkreqnr
       61 vlcvhampvm etlheqivnt qsmivltdae glilhsigdd dflrraerva lrpganwaes
      121 rqgtnaigta laelcpmvvh gdqhflaanh fltcssvpil dpygdaigvl dvtgdhrsyh
      181 qhtmalakms vqmienhlft ttfqetlqvs fhgrpeflgt lmegivafta dgrflsanrs
      241 aqfqlgmpla alrahtlasl fdvtsaqlid rmrastephv slnlgngavv carvqfrral
      301 raegsrpaev hdgaapaarp paaqgaasls rlsyldtgdp qvaaviakvr kvigkdipvl
      361 itgetgtgke llaqaihnds prrdgpfvav ncasipetli eselfgyeeg aftgarrkga
      421 tgkllqangg tlfldeigdm pyplqvrllr vlqerivnpl gstkaigvdi aiicathrdl
      481 rdmiaqnrfr edlyyrlngl vvrlpplrdr tdlavvvqkm lqretlsgpg rrplsvapdv
      541 malfercawp gnfrqlanll rtaaamvddd ceircehlpd dffddvrhds gpaaqeacts
      601 pplaseapaf anaagdarlq dvaasaiaaa larhggnvsa aaralgvsrn tiyrkmpaag
      661 pdalepdep
//
LOCUS       WP_175816324             421 aa            linear   BCT 11-JAN-2025
DEFINITION  RHS repeat domain-containing protein [Burkholderia diffusa].
ACCESSION   WP_175816324
VERSION     WP_175816324.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..421
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47690
     Region          <29..338
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mtegpqyaal gmprikaldn llkqyagphy qydargnltq rwhngkegrf twdlfdrlth
       61 yederlkvdy tydalgrrls khsqahyeer reagphwnra ervkrnralq cgftlygwdg
      121 dtlaweskia dedgfgartt hyvyepgsfv pvaqavrdda ielldqpeyg dyyrqdedpl
      181 wlppppapai nslawyqcdh lgtpqeltde hseiawsaey rawgvaqeai rkasgkvpia
      241 npirfqgqyh dhesglqynr yryydpevgr fvskdpigya gglnsyqyap npvewidplg
      301 laklqkigry hgpkpeyenp ghhdpssgvf rgggagktsi lpcnakdlyk qaipdaegkh
      361 wyalddngvv hrfgnsndgk vhwngdtsqg rgielppevk rridamkkdg vssargcsig
      421 r
//
LOCUS       WP_175816220             336 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sodium:calcium antiporter [Burkholderia].
ACCESSION   WP_175816220
VERSION     WP_175816220.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schnetkamp,P.P.
  TITLE     The SLC24 gene family of Na/Ca(2)-K exchangers: from sight and
            smell to memory consolidation and skin pigmentation
  JOURNAL   Mol Aspects Med 34 (2-3), 455-464 (2013)
   PUBMED   23506883
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Besserer,G.M., Nicoll,D.A., Abramson,J. and Philipson,K.D.
  TITLE     Characterization and purification of a Na+/Ca2+ exchanger from an
            archaebacterium
  JOURNAL   J Biol Chem 287 (11), 8652-8659 (2012)
   PUBMED   22287543
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..336
                     /product="sodium:calcium antiporter"
                     /GO_function="GO:0008273 - calcium, potassium:sodium
                     antiporter activity [Evidence IEA]"
                     /GO_process="GO:0006874 - intracellular calcium ion
                     homeostasis [Evidence IEA]"
                     /calculated_mol_wt=35286
     Region          19..332
                     /region_name="ECM27"
                     /note="Ca2+/Na+ antiporter [Inorganic ion transport and
                     metabolism]; COG0530"
                     /db_xref="CDD:440296"
ORIGIN      
        1 mtlmlvelav mliviliaae lftnalehlg erlkisegvt gslfaavgta lpetmvplla
       61 laggtsnaav neeigvgail gaplmlatlt tflmtlavir srgltgtiap ertgfvrdln
      121 yfiaafalat iamfvphhvw avrallaaml vgiyvtyvlm tfrastqlvd aghgteapha
      181 mflsrvglpt nlatialqla lgvallvgga kgfihgvegv shllgisall lsliivpiat
      241 elpekvnsvl wirrkkdtla fgnitgamvf qgtllpaigi mltpweprpe vltgviitla
      301 aavwlrvnar arglaiwall angagyvgyl fvtltr
//
LOCUS       WP_175816481             311 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175816481
VERSION     WP_175816481.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..311
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34075
     Region          7..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,219,
                     221..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdkvhtmsvf akvvemgsft avanhldttv gnisravsvl ednlntrllq rstrrlvvtd
       61 agrrfyersv ailsdieqae aeardallep rgvlrvhavp glgrqlvsqa vlayrnaype
      121 vsvdlmlsqr mpnlleeqld vaiviartlp dsayvsqkig ashcilaasp dylarhpape
      181 cvedlvdhtc vllstvdyap dewhlqgsag dvtyrptgsh fsvndmdams tvlqegagig
      241 liaafsamdd lrkgslvrvl pefhtaqrnv yavyssrqfv dakikrfidv lkvrvgdrln
      301 ayaeelaitv v
//
LOCUS       WP_175816483             328 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-quinone oxidoreductase [Burkholderia diffusa].
ACCESSION   WP_175816483
VERSION     WP_175816483.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..328
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=35024
     Region          1..325
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(40..41,123,127,130,148,151..153,172,176,191,
                     215..216,237..238,240,263..265,314,319)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mkaitfkefg eaevlhlaev qapevrpddl lvrvhaagvn radlthrrgg ygrpnfgdst
       61 imgleiagev ietgssvqgy kvgdrvmgvv gggayaelar idwrmampip atidyvhaaa
      121 ipevfvtahe allhlgrlqr gdsvlihaaa ggvgsaavql ayatgatifa taeaskleri
      181 vqlgvdhaid yktqdfsevi asrtekrgvd vvidfvgapy fsrnvaslan ggrlvqvgil
      241 ggggdvsvsl eqilyrhlqi igtvmksrdq rekhamvqrf rehwldrfag gaglepvvds
      301 vfplanaaaa hrrmesavnv gkiiltmn
//
LOCUS       WP_175816484             313 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia diffusa].
ACCESSION   WP_175816484
VERSION     WP_175816484.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Grant Pearce,F., Hudson,A.O., Loomes,K. and Dobson,R.C.J.
  TITLE     Dihydrodipicolinate Synthase: Structure, Dynamics, Function, and
            Evolution
  JOURNAL   Subcell Biochem 83, 271-289 (2017)
   PUBMED   28271480
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Laber,B., Gomis-Ruth,F.X., Romao,M.J. and Huber,R.
  TITLE     Escherichia coli dihydrodipicolinate synthase. Identification of
            the active site and crystallization
  JOURNAL   Biochem J 288 (Pt 2) (Pt 2), 691-695 (1992)
   PUBMED   1463470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..313
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0009436 - glyoxylate catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33540
     Region          10..272
                     /region_name="DHDPS-like"
                     /note="Dihydrodipicolinate synthase family; cd00408"
                     /db_xref="CDD:188630"
     Site            order(12,44,47..49,136,164)
                     /site_type="inhibition"
                     /note="inhibitor site"
                     /db_xref="CDD:188630"
     Site            order(44,47..49,136,164,209)
                     /site_type="active"
                     /db_xref="CDD:188630"
     Site            order(48,53..54,82..83,107..108,116,120)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:188630"
     Site            164
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188630"
ORIGIN      
        1 msdniftgti palmtpctad rqpdfdalvk kgkelvalgm ravvycgsmg dwpllteaqr
       61 qegvarlvea gvptivgtga vnskeavsha ahaskvgahg lmviprvlsr gaspaaqkah
      121 faailnaapn lpaviynspy ygfatradlf felrrqhpnl igfkefggaa dmryaaenit
      181 sqddsvtlma gvdtqvfhgf vncgaagait gignalprev lqlvdlckka aqgdavarvr
      241 akeleaalav lssfdegcdl vlfykhlmvl ngdkeytlhf netdalsdaq rnyaeaqytl
      301 frnwyanwsk sia
//
LOCUS       WP_175816046             440 aa            linear   BCT 11-JAN-2025
DEFINITION  leucine-rich repeat-containing protein kinase family protein
            [Burkholderia diffusa].
ACCESSION   WP_175816046
VERSION     WP_175816046.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Shen,K., Hines,A.C., Schwarzer,D., Pickin,K.A. and Cole,P.A.
  TITLE     Protein kinase structure and function analysis with chemical tools
  JOURNAL   Biochim Biophys Acta 1754 (1-2), 65-78 (2005)
   PUBMED   16213197
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   6  (residues 1 to 440)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
REFERENCE   7  (residues 1 to 440)
  AUTHORS   Hanks,S.K. and Hunter,T.
  TITLE     Protein kinases 6. The eukaryotic protein kinase superfamily:
            kinase (catalytic) domain structure and classification
  JOURNAL   FASEB J 9 (8), 576-596 (1995)
   PUBMED   7768349
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..440
                     /product="leucine-rich repeat-containing protein kinase
                     family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=47136
     Region          <2..>193
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          39..61
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          62..84
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          85..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..175
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          214..436
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(214..217,220,222,238,240,269,287..289,298,345,
                     349..350,352,362..363)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
ORIGIN      
        1 mtttleqlqa gqlsgarqlk lacgltefpr eifdladtle vldlsgnals alpddlsrlh
       61 rlrilfasgn rftefpevlg tcaqldmigf kanrirtvpr gslpralrwl iltdneidal
      121 paeigdcsrl qklmlagnrl ralppemaac ralelvrlsa nrldelpgwl lrlprlawla
      181 sagnpfgtap esaasaepgv adidwtslal drklgegasg viyraqwrvd gqapravavk
      241 lfkgavtsdg lpdcemaacl hagrhpnmip vigkvhghpd gthglvmelv dpaltnlaep
      301 psfasctrdv yaaderfapa easrialgia svaahlharg imhgdlyahn ilhdgkggal
      361 lgdfgaasvy dvndrvraar lerlevrafg hllgellarc eprawegshv ldalaaacln
      421 eeidarpsfg eiaatlavkd
//
LOCUS       WP_175816493             212 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175816493
VERSION     WP_175816493.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..212
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24122
     Region          20..148
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdrqlrwgda srmdsvndgr nailratlda miehgidrls iddvarrani srrtlyryfg
       61 tkkeliqgvi gvenaaffde mqraltgfeh dfeayceesv cfavryrdrh hggfhhnyla
      121 tsvstevfgy ivenvapmwq rvleqpyrey aalhgaqvpa lddvialisr ialayslipa
      181 deqamraqmr ilwtfrrepa gkpaaarmka ar
//
LOCUS       WP_175816555             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia diffusa].
ACCESSION   WP_175816555
VERSION     WP_175816555.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21912
     Region          1..192
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mhqttllifa avafvgiatp gptvllaltn gsrygvrrat ygfagamlsd fvlivavalg
       61 lgallmssal wfsvvkwlga aylayvgirl ltskgsldvt vghggtahgr nasifaksfl
      121 tavtnpkgyl ffsaflpqfl dpsaplapqy valavtfall dgavmfgyal lgaravrllk
      181 rsgalwlert cgamllalag slalyrrhaa
//
LOCUS       WP_175816591             297 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia diffusa].
ACCESSION   WP_175816591
VERSION     WP_175816591.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..297
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30053
     Region          1..287
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mevgfcgpgl mgapmirhll aaghrvsvwn rtrakaeale kdgaqvvdtp relaervdtv
       61 fvcvldgrav cdvafgehgl lagdanarrl krivdhssip paatrdyaar aaalgvgwid
      121 apvsggvpga qagtlavmag ggaidldavr plidtyasri thmgdagagq taklcnqaiv
      181 tatvtaiaea vglaqasgid aarladalag gwadsvllqt fvprmtsggy ppigalstfq
      241 kdvdaiadaa rdtgavmpvs atvqqvlrlg aaqglagadf aafidivrpg ngrataq
//
LOCUS       WP_175816590             839 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia diffusa].
ACCESSION   WP_175816590
VERSION     WP_175816590.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 839)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 839)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..839
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..839
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=91141
     Region          57..777
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mpiikrpssh sdrnephytl rrspsgayyp ddddrgddrr aqrsggrgad rrsfgsrval
       61 wfvglfatla ivgalivgya lvvmapqlps ldaltnyqpk vplrvftadh vligefgeer
      121 rslvrfqdip dvmkkavlai edyrfyehgg vdflgilrag vadlmhggar qgastitmqv
      181 arnfflssek tytrkiyeml laykiekalt kdqilelymn qiylgqrsyg faaaarvyfg
      241 kdlkditlae aamlaglpka psaynpvvnp krakvrqeyi lkrmleigyi tqpqydqavk
      301 eeihvrtpgn qyavhgeyva emvrqmmyqq ykdetytrgl tvtttinsad qeaayqavrr
      361 gildyerrhg yrgpegsinl pvagddrdea iddaladhpd ngdlqsavvl aaspnavevq
      421 fvggatttig paglrfvsaa lspranatlr ikpgsivrvl kdgnagwqvv qlpqvegalv
      481 aiapqdgair slvggfdfnk skfnhvtqaw rqpgssfkpf iysasldkgl gpatiindap
      541 lyfppsvpgg tawepkdddq pdgpmsmrtg lqrsknlvsi rilasigtqy aqeyvtqrfg
      601 fdpaktppyl pmalgaglvt plqlatgyav fanggykvdp yliaevddar gqplqksqpv
      661 iaggtaprti egrnayvmns llhtvatagt gagtnalgrs dlqgktgttn dakdgwfagy
      721 qqslvavawm gfdqpkslgs refgaqlalp iwvnymrtal ngvpeqqmpm pdgltsidge
      781 lyyadrtpgn gfvasvdinp aanaisanda lgsagsegla pppvtqqekq qimdmfesk
//
LOCUS       WP_175816600             331 aa            linear   BCT 11-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Burkholderia diffusa].
ACCESSION   WP_175816600
VERSION     WP_175816600.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..331
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=34654
     Region          <9..324
                     /region_name="FAD_binding_2"
                     /note="FAD binding domain; cl46878"
                     /db_xref="CDD:481218"
     Region          48..74
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          79..109
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          114..136
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          173..196
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          209..232
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          240..266
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          299..325
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mtassptfpl hgahasdhaa lvarvaapda svrriallel adledpdlvp vfvaalrddp
       61 aavvrgeaar vlaaweqpvv vdtlchalld pdddvrataa hslselkdva sgavlcrwae
      121 haepfvrgaa lralrelrdp daftpalhal dapaaavrae aaavlgwlkd vralsplari
      181 attdthadvr riavgavgfa asddtavvta llaalhdaew qvreeaaatl gklrvavara
      241 plvaaldddy wqvrlravra lgqlrdaaaa pavaallsha isnlrkeaal algelrdpat
      301 lpalhealed rdpevrkavr iaiaqiggda r
//
LOCUS       WP_175816618             297 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175816618
VERSION     WP_175816618.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31329
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176112"
ORIGIN      
        1 mtpdqlitfa avaehlnisr aalalhlsqp avsgqlrllq defgeplyqr egrgirltpv
       61 geqlaqyaka qrdtfaqara frdavrglea gtlrigastt pasyllpyli aafqprvprv
      121 aihtmsgnta dvvaalasld vamiegppge alppgtavha whedeivavv paghplaape
      181 yeagvtldal aahplvlree gsgvrqlver afahggapmr vafeiagvea vkeavragmg
      241 vgfvsamslr hedaalvprs lapapltrhf silvphgaap srvatqfldm cithdek
//
LOCUS       WP_175816629             247 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia diffusa].
ACCESSION   WP_175816629
VERSION     WP_175816629.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..247
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26452
     Region          152..236
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mregtteqeg ggshpldnav whaltgeqhr falgdllarr fppalapfag madrsptafd
       61 alrglidahg paalvtpdei ptppgfsvvw ramlhqmiww gtldgapale hvrlteadvp
      121 emleliaate pgpfgtrtve fggyigvrrq grlvamagqr lragghaeis avcvdaafrg
      181 qglaaglirs lvatirarae tpflhvltsn hgaieryral gfatrrdmhl lvlgreetgt
      241 gqparrp
//
LOCUS       WP_175816771             137 aa            linear   BCT 11-JAN-2025
DEFINITION  SMI1/KNR4 family protein [Burkholderia diffusa].
ACCESSION   WP_175816771
VERSION     WP_175816771.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..137
                     /product="SMI1/KNR4 family protein"
                     /GO_process="GO:0042546 - cell wall biogenesis [Evidence
                     IEA]"
                     /calculated_mol_wt=15523
     Region          12..131
                     /region_name="SUKH_6"
                     /note="SMI1-KNR4 cell-wall; pfam14568"
                     /db_xref="CDD:434043"
ORIGIN      
        1 mqyddteeav sdndirefel laqvnfpeal krhylahngg ypvgveelig rdyvfpfqgf
       61 fplkygalti ekmrkdlved fglpnaipfa ydqgsnifyi stspvdfgav fqitaetkek
      121 ffvcetfdqf ldglrpa
//
LOCUS       WP_175816832             330 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175816832
VERSION     WP_175816832.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 330)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 330)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..330
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35952
     Region          2..184
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          214..296
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdslsdvlar lkprsqfyag ldaagewsfa fpeyegikfa avlqgacwgv iegvaqpvrf
       61 ekgdcfllns rrsivlstdl alepqdstai mdavardgia vhggggdvll isgffafsgd
      121 haalpfdalp plvnvprass qaevlrwsld qltaelrdpq pggalvsnhl lhlmlvqvlr
      181 lhlaatpagw fmalsdrrig aaigaihadp arhwtldela riaglsrtvf aqrfkrlvga
      241 ttihyltrwr mliaadrlra gresiasiaf slgyesesaf ctafkrtmcc sptqyrrrar
      301 aadpydlete ahggdrsert eknnmalcpi
//
LOCUS       WP_175816842             249 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Burkholderia diffusa].
ACCESSION   WP_175816842
VERSION     WP_175816842.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26318
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkilvpvkrv vdanvkvgvk sdqsgvdian vkmsmnpfde iaveeavrlk eagvatevia
       61 vsvgvtqaqe tlrtalaiga drailvesnd sveplavaki lkalvdkeqp qlvilgkqai
      121 dddsnqtgqm laalaglpqa tfaskvtiad gratvarevd ggaetlslql pavvttdlrl
      181 nepryvtlpn imkakkkple tvkpedlgvd vtprlktlkv aeppkraagv kvpdvktlve
      241 klkteakvl
//
LOCUS       WP_175816858             544 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia diffusa].
ACCESSION   WP_175816858
VERSION     WP_175816858.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..544
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58468
     Region          1..543
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 msetfdyvvv gagsggsvva arlaeaghtv cvleagpadt hpfihipagy iknlfndrlv
       61 wrfrsgpiag tdgrtieltq gkvvggsgsi ngmvynrgqp adfdgwaalg npgwgyddvl
      121 pffkkaetrv gpgddryrgr ngplivtdpi mpaplcdlfv eaveslgypy vadsnaeaqd
      181 gvgpwhfmid trgraprrrs aaraylhpai rkgrvalrtg spatrvlleg sravgvryrp
      241 ggtgaperev ranrevivaa galntprllq isgigdsahl raigiepqid lpgvganlvd
      301 hfnlrvavkv kgvatlnerg rglplareia ryflgrpsil smgpvpmrff frsepslsrp
      361 dlqvsftpgs yqeglpglld hypgmtlggh kqrpdsrgwv karsahidel pdvqpnyltd
      421 esdqramvav vkmaravlqa rpfapyyvde mfpgkdvrtd deiiafarqr ggtvyhhngt
      481 armgpdsdpm avvdarlrvr gvqglrvada svmpmpvsga tnaatimige kaadmlvqda
      541 ktas
//
LOCUS       WP_175816843             310 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Burkholderia diffusa].
ACCESSION   WP_175816843
VERSION     WP_175816843.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..310
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31425
     Region          2..310
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtilviaehd nasikaatln tvaaaakigg dihvlvaghn aqgaadaaak iagvskvlla
       61 dapqleagla enveatalni akdyshilap ataygkniap riaakldvaq isditavdsa
      121 dtferpiyag naiatvqssd pikvitvrat gfdpvaaegg sasvekieaa adagksqfvs
      181 revtkldrpe ltsasiivsg grglgsgeny tkvlepladk lsaalgasra avdagyvpnd
      241 yqvgqtgkiv apqlyiavgi sgaiqhlagm kdskvivain kdpeapifsv adyglvgdlf
      301 alvpelvnel
//
LOCUS       WP_175816882             724 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia diffusa].
ACCESSION   WP_175816882
VERSION     WP_175816882.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..724
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78178
     Region          33..724
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mlmetgaarr awavaaggtl cvaaaggaha qapnagatta vlppidvtgn aggssvglvg
       61 lrtaagtktd tpvaeipqtt nivtaqqiem tgaadlnqal ryvpgfatfg adsrtdwyaa
      121 lrgftptlyv dgvpapntav ianwrvdpyt idsiavlrgp tsvlygagep gaivdahtkl
      181 adgervreag vqignharkq fmvdvgdqld pdgryayrfv giardgnawt gpnadrrval
      241 apslrwrpta dtsltfsasf lqdsgdissn flpasgtvlp npngrlsqdi ymgdpsfndy
      301 rkkqwslgya lehrvdaiwt lhqdvrwshl slddatvfgt glvprsttnm mrfaglfqln
      361 ysrldidnha qarfgtgple htlllgvqfd rqtttnsvwl alapslnlyh pvyrpvtaai
      421 ftgptslghv dqytamnavg vyaqdqirwq rwtmtlggre drvntrfdgr tvgthsrqdd
      481 safsgrvgla yqgdaglspy vsystsfdpv igvriygggl pkptrgtqte aglrwqprgk
      541 nlmlsaavyr idqtnvvtpa panldptgtt svqtgkvrsr gielsalgkv trelsivasy
      601 myqdvknvqa ndaslnnwpv svplprqmas mwadwtwhag alsglgigag vryqsasaga
      661 pdnsltvssf tlydlamhye mrhwrfafnv anlfdrryvs gcqsyavcvf gnertvlasa
      721 rynw
//
LOCUS       WP_175816923             256 aa            linear   BCT 11-JAN-2025
DEFINITION  DsbC family protein [Burkholderia diffusa].
ACCESSION   WP_175816923
VERSION     WP_175816923.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Shao,F., Bader,M.W., Jakob,U. and Bardwell,J.C.
  TITLE     DsbG, a protein disulfide isomerase with chaperone activity
  JOURNAL   J Biol Chem 275 (18), 13349-13352 (2000)
   PUBMED   10788443
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Chen,J., Song,J.L., Zhang,S., Wang,Y., Cui,D.F. and Wang,C.C.
  TITLE     Chaperone activity of DsbC
  JOURNAL   J Biol Chem 274 (28), 19601-19605 (1999)
   PUBMED   10391895
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 256)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..256
                     /product="DsbC family protein"
                     /GO_function="GO:0003756 - protein disulfide isomerase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28104
     Region          39..245
                     /region_name="DsbA_DsbC_DsbG"
                     /note="DsbA family, DsbC and DsbG subfamily; V-shaped
                     homodimeric proteins containing a redox active CXXC motif
                     imbedded in a TRX fold. They function as protein disulfide
                     isomerases and chaperones in the bacterial periplasm to
                     correct non-native disulfide bonds...; cd03020"
                     /db_xref="CDD:239318"
     Site            order(39..43,45..72)
                     /site_type="other"
                     /note="dimerization domain [polypeptide binding]"
                     /db_xref="CDD:239318"
     Site            65..72
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239318"
     Site            order(120,123)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239318"
ORIGIN      
        1 mrrlakvtls licagyaala hadfpeelvk rfpaaqgakv erafpgfwsv akggdvffvr
       61 ddlsilisge vvdlnghrsl tqsirdanpp ridvaqlnlh daikfgsgsr rlyifsdpdc
      121 pycrklegtl tkltdvtiyi fpfplaghpn aaevsegiwc qkdraaawka yqdltlvtre
      181 pqlltawqdy lakhkqpaqp tcdnpiarnl efgrqwniag tpalvfedgt lipglvpapr
      241 leaqlaksha nltask
//
LOCUS       WP_175816968             881 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Burkholderia diffusa].
ACCESSION   WP_175816968
VERSION     WP_175816968.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 881)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 881)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 881)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 881)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 881)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 881)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 881)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..881
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..881
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=96809
     Region          79..723
                     /region_name="RloC"
                     /note="Wobble nucleotide-excising tRNase [Translation,
                     ribosomal structure and biogenesis]; COG4694"
                     /db_xref="CDD:443729"
ORIGIN      
        1 mskslvefkr flaksaptls eyekklanlm lggfdevaav gtaagrrgkv laklivdkge
       61 aappaleiaa deakanerei vrltkveveh frgfsekhtf efknpytfvy gpngtgkssl
      121 cealeyglla siheadskri pvsdyirnat srksekpvly gdtakergie vkadprsfef
      181 cfieknridg farvaantpa aqqarlaalf gleefnafat qfndsldpyl dcvgkngkvl
      241 adrakgiagh raileglpvk aktaetrgaa llgkypgckd ldeikatltg pegnggkqka
      301 nnteigrlqn lkaaadpgtd diltdadgll qlikekaese kflnqykdql slrdlygail
      361 gnrerfgnec pacaselyrd grlavpvdpy gnaeeklkqf daalkaegri kdirealnlg
      421 wrdllskiak lpasaaavgf vgapevgsfs akasdakdaa gietflrsvp akrellqalk
      481 datathngkv eqskiaikkl eddnlaiakd leeivaistl ivtnaksete akqaiekfnr
      541 eneelireae aekpgvarnl sysiayvslr ekllaynagl plalaadlne ktlkfynein
      601 kndhpsdklk slrlptavge rieiefengg gcdalqvlse ghirclglai llakittdrv
      661 pflifddvvn siddehrgai idlilnpeev gkrqlivtth gedfvkrlen avpmkkyeet
      721 vtridflvpf aakkitvkld sprhyltvav rsheegrtrd slsyvrkafe eelnrlwkki
      781 ankklsalvs vgmrgpgdpd lmslatglhq flskkdvtvf qevvphlgei lgygekhkle
      841 wnylnkgthe edraeefdaa ivrrmletvi kldeaieapq a
//
LOCUS       WP_175816963             272 aa            linear   BCT 11-JAN-2025
DEFINITION  ParA family protein [Burkholderia diffusa].
ACCESSION   WP_175816963
VERSION     WP_175816963.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..272
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29641
     Region          1..271
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mkiigicngk ggvgktttgr hliytaiers lrtlavdldp qgnltkslly mklvaqagpt
       61 vvgsalsweh mglpdvmpsa sahllyqneq pvepmkiidg vsmigatpel advltwpldc
      121 alvareslek ltagfdlcvi dtpptmsnlv lgglicsqyi vlptdlsids mtglletslk
      181 ldlvqrewnp aleligvlln kvnprraddl smrttvrnvf dgavlddelq dragvrltsf
      241 hpvwkyrrge sdrraaremq avcttifdrv gl
//
LOCUS       WP_175816990             767 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia diffusa].
ACCESSION   WP_175816990
VERSION     WP_175816990.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 767)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 767)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 767)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..767
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..767
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=84496
     Region          27..>215
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mqtviahdpn vnatdnehpv drpialkaga revliplkrl vaspynqrrt krdpatieai
       61 adnilavnll qnlvvhpmkv aakkaqtygv dagetrrqal llnvdrghit ldfevrcmvi
      121 seaeailasa sendlrvpph padqfyayka ladegrspef iatvfkvspk tvaghlklan
      181 vspklfelfa sdviqldqik alaitddher qeaawfgakg hwnqsasalr nvlkgdklsf
      241 gdrmvrfvsv aayeaaggvv erdlfaaqdd gfivnrdlls rlfdekiagt vetikaegwt
      301 wvearpkfdy ddrnqftqly akpipfsaee kakyeeterr anelsdqiea sddaeegdaa
      361 ylsdedrgkl eaecdelyav ihemddrdgq ftpeqmkvsg aiitvghdge leivrglirr
      421 edraearamm eeagqsvprs ltkkvkgvhs eklllnltah rtaavqsamv vdanialvav
      481 vhrlvldfvy drysdlsavr ikeeqpmnsm draapgiekl pqydqlslsv lavtrvlpkn
      541 pnelfgwlle qsqtallnil avctalslng vsrteeahpi ntiagaleld lsaywkptre
      601 syfdhvskdr ivaivgevvs keqgariakm kkgeaaqeae klladknwlp efmaaaevce
      661 arhyyrpged dkeadvdsea ggdeqapvla tdpssetepd dddspfanpd sapwpfpkgv
      721 dfvasapkqt iepqsecead dardaqrvaw pfpmpngtav taarlaa
//
LOCUS       WP_175817029             522 aa            linear   BCT 11-JAN-2025
DEFINITION  multicopper oxidase family protein [Burkholderia diffusa].
ACCESSION   WP_175817029
VERSION     WP_175817029.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 522)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..522
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=56304
     Region          45..522
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mkkvteqrrs rsergttsrr eflkaalaga aamalrpgnt gqawaadvsa stgsrpatql
       61 svvrrsievn graadvygir qpdgtsgirl ragdpfdvvl rneiaeptiv hwhgltppwa
      121 sdgvpdapmp migagmerrf nfpvrapgty wmhahslqeq qllaapliva dpgqsgrdeq
      181 evvlmlhdfs ftspqeilag ltrngkshas gheavppdtq sashahdggm tkdshdmpgm
      241 epagsmsahg vtgasatamd lndieydayl andrtlddpe vikverggkv rvrvingata
      301 taftvdfgsm ggtltavdgr avkpvsgrrf pvsmgqridv qltlprdara fpilalregs
      361 yertgvilqv adapvgklae kadvrgpvld lalesrlram tplssrrpgk afnlvltgdm
      421 akyqwglemq priavdrgdr vevtmrntsm mahpmhlhgh hfqvvaidgr rfpgalrdtv
      481 lvppgrsvtv aidadnvgqw aihchhlyhm atgmmttfay ka
//
LOCUS       WP_175817114             424 aa            linear   BCT 11-JAN-2025
DEFINITION  NupC/NupG family nucleoside CNT transporter [Burkholderia diffusa].
ACCESSION   WP_175817114
VERSION     WP_175817114.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Hirschi,M., Johnson,Z.L. and Lee,S.Y.
  TITLE     Visualizing multistep elevator-like transitions of a nucleoside
            transporter
  JOURNAL   Nature 545 (7652), 66-70 (2017)
   PUBMED   28424521
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Johnson,Z.L., Lee,J.H., Lee,K., Lee,M., Kwon,D.Y., Hong,J. and
            Lee,S.Y.
  TITLE     Structural basis of nucleoside and nucleoside drug selectivity by
            concentrative nucleoside transporters
  JOURNAL   Elife 3, e03604 (2014)
   PUBMED   25082345
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Munch-Petersen,A., Mygind,B., Nicolaisen,A. and Pihl,N.J.
  TITLE     Nucleoside transport in cells and membrane vesicles from
            Escherichia coli K12
  JOURNAL   J Biol Chem 254 (10), 3730-3737 (1979)
   PUBMED   374403
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..424
                     /product="NupC/NupG family nucleoside CNT transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005337 - nucleoside transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:1901642 - nucleoside transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=43862
     Region          1..422
                     /region_name="NupC"
                     /note="Nucleoside permease NupC [Nucleotide transport and
                     metabolism]; COG1972"
                     /db_xref="CDD:441575"
ORIGIN      
        1 mdilrsllgm lflllvayll snnrravsgr tliaalltqf aigalvlfvp sgraalaaaa
       61 ngvnrvldmg nhgiafvfgg lvdarmfqlf gdggfvfglr vlpmiifvta liavlyyvgv
      121 mkwivailga glakvlgvsr ieacsavati flgqsempal vkpfvrhmtg aeiftvmasg
      181 masvagsvlv gyaglgvkme yllaasfmav pggllfgkll fptvepsrvv vdgldfddkr
      241 aanvieaaas gasvglriai nvgamliafv glialmnliv ggvaafagfp qvtllgiigh
      301 lfaplawiig vpwhdsalag nfigeklifn efvaygdlsp ylkgsahvaa aglqvldpkt
      361 laivsfalcg fanfssiail aggfsavape rrsevarhgl raltaatlsn lmsaaiaglf
      421 fsln
//
LOCUS       WP_175817130             166 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia diffusa].
ACCESSION   WP_175817130
VERSION     WP_175817130.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..166
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=17913
     Region          1..149
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mitltvngvr htldidpstp llyalrndlh lhgakfgcgl gqcgactviv ddkpmfscli
       61 pvaaigerrv rtieslgtaa hpgklqqafi dhqaaqcgyc iagmimraqa llernpkpte
      121 relrthmepn lcrcgthmri laavrqvagl pepepsaapv minkei
//
LOCUS       WP_175817152             333 aa            linear   BCT 11-JAN-2025
DEFINITION  bestrophin family protein [Burkholderia diffusa].
ACCESSION   WP_175817152
VERSION     WP_175817152.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..333
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38389
     Region          9..321
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 mhmgksykls efliwtrwki yellifgsvp vvlykvfsvt wlsipltivv llgtatsfiv
       61 gfknvqtynr amdaleiwtd ilsksrrwgq fvrdfvtdde iartlvdrhl awltalrydl
      121 rrpriwestk krynaeyrrf yrvpewekdi sellpkylss teteqslssa ciatfvlslq
      181 gtslrtlhma ghlnsnfyme lqktvgdfid lqarserfkn fpyprqyatv sslfvrffcl
      241 slpfgllnef nrlndsvsgf mhgnmvwlvv pcsvavswmy tsleqvgest enpfeggand
      301 vpistlcsti erdlkamlge hardpssrti ial
//
LOCUS       WP_175817154             348 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175817154
VERSION     WP_175817154.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..348
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38477
     Region          35..89
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          119..316
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(129,133,172,186,188,251,268,295)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(130..131,135..136,138..139,142,146,148..154,215,
                     245..249,256..257,260)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mnhsepsehg arrdlasrad alsasfgasy agilafvava segsftkaae llgvgrpavs
       61 rnvqkleaql strlfqrttr tteltcegrr ffenchqgva qiveamndml elrqgpprgv
      121 irissavgfg rkivapllek fahaypdiii dlllddrpvd lvseridvsf rngriedssi
      181 iarqlipmqm alcaapsyva rhglpqsved ldrhecinfr fasgrlfewe fnvdgrvqky
      241 lptsrltfnd adlvlrsvln gsgiaqmagy qirdhlasne lvvalakhvp edrghyicyl
      301 srqhlptrir ifvdfmteqi raldlncmtr fnpevpvlss aasaglaa
//
LOCUS       WP_175817174             130 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia diffusa].
ACCESSION   WP_175817174
VERSION     WP_175817174.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..130
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14381
     Region          8..115
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mnatkayleh vaiwvkdirw hirffeevlg mtlrevdgtl daprqywalg glqfihapeh
       61 dgpegrlahl gvmcedleaa laeaqrfgvs empqgrnwlr lpdglaveli qarpascvaq
      121 alainpraea
//
LOCUS       WP_175817216             331 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            diffusa].
ACCESSION   WP_175817216
VERSION     WP_175817216.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..331
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=34988
     Region          40..312
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mqfdrrrefk fdlwsvllli plfavpfgtt nalffslthq ivigivaala vyimlrlgll
       61 aftvpafmav ggyaaamvak sgstnlvllm atafvvpaif alplgalvlr lrgtyfifit
      121 yifneilqli lfetptltgg sdgitsvpap tlfgvtlgsp amlvlvtvvv gifgalvtfa
      181 lthrfrpefs sieenetlaq slgvtvqlyr tigfivsagv sglagfalvd qlstanpssf
      241 asfsainyia yafiggrrtm lgavvgsvll vsmsnafssq aqyssalfgv lliavvmiap
      301 gglvgafqga fralktrnrr digqpakgek a
//
LOCUS       WP_175817222             310 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia diffusa].
ACCESSION   WP_175817222
VERSION     WP_175817222.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..310
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=32280
     Region          1..278
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mkvgfiglgk mgqgmarnll ksgvnlvvfd anpaavdmla sagaepavsa aeltrqvnvl
       61 fmslpgpaqi esvvfgaggi lenlhadltl fdlstsslsl vrrihdafgk agatmldapi
      121 sggpagaasg elalwiggdr rayehhlpll raignaprhv gdigagtvtk lthnlvgymi
      181 mqslaeafsm avkagvdpld lwealrlgmv gkgsplnmlv nqflpgkyep aafalklahk
      241 dvtlatalgr elgvpmrlas ltmeemteal anglgeqdsr sflklqlqra gveiavdpar
      301 lkqavnaaqs
//
LOCUS       WP_175817228             386 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia diffusa].
ACCESSION   WP_175817228
VERSION     WP_175817228.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..386
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43232
     Region          5..384
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 miadnadlnm irdsirkite efdlnywrqk gsdkeypwdf kdalaeggwl gilmpeqygg
       61 mglgltevgv vldelgqrcg fnansvfqyy vfppgpvihh gsdemkqefl prlangeemm
      121 cfgvsepdng vdtsrlktfa kkdgkrylvn grkvwisnak nadrillltr tsprnperpf
      181 dgmtlflsql kgkkgveinr idkimrnavd snemvfedfe vfeneivgee gqgfrclldg
      241 lnperiavay taiglgrgal nlavqytkdr vvfdrpigkn qavahplads wirleaadlm
      301 tqkaaklfde gkpcgpeana akflgseagf eaadramqfh ggfsmsteyh isrfwmearh
      361 lkiapvsqem vlnyvahkil glprsy
//
LOCUS       WP_175817258             297 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175817258
VERSION     WP_175817258.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32657
     Region          6..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mttenlndlr afvtvarers ftraaaqlgl srsalshaml alearlgvrl ltrttrsvat
       61 teagtrllnt lspmfselda elaslrslrd kpagtvrita sdhaivtvvw pklrtllrey
      121 pdiqlelsvd yaltnivaqn fdagvragdi vdkdmiavri gpdlrmavvg apayltakrp
      181 ptvpndltgh qcinlrlpth gglyawdfek ngrslsvrvq gqtvinntfl mlqaaldghg
      241 layvpldlad phiaagrlmp vlqdwwprip gfhlyyanrr qvtpafalvv ealryrs
//
LOCUS       WP_175817276             388 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia diffusa].
ACCESSION   WP_175817276
VERSION     WP_175817276.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..388
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41231
     Region          19..227
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          143..387
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 maipltyiar nlwtrrltta ltaggmalvi fvfatvqmld agltqtlvst gepdnavvir
       61 kgaeteiqsa idhqqanale mhpavalgpd grplvskeav vlislvktss gkpsnvvirg
      121 vspaglalrp hvklvagrmf tpgsseiivg saiakgfsgt qlgdslhfaq rdwtivgifd
      181 agasgfdsei wgdvdqlmqs frrtsyssmv lripsadgfa rfkadidvdp rltdeakreq
      241 tfygdqskal stfinilgit lstifsiaam igamitmyas vanrtaeigt lralgfkrmn
      301 vlaaflleal llgfvggvag lacaslmefa sfsttnfqtf adlsfrfvlt paivvktllf
      361 slvmglvggf lpamraarln ivdalraq
//
LOCUS       WP_175817280             264 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia diffusa].
ACCESSION   WP_175817280
VERSION     WP_175817280.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..264
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=27145
     Region          47..197
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mnqsrvkqtl vrttllaalt aglamslqgc vlgvlgaaag ggaliatdrr tlgaqtedre
       61 iqvkslsqin nglpdqshvn vtvfnrrvll tgevpnnask qraeeivrgi nnvngivnel
      121 svepssslss randsylegr vkseliatkg lsanyykvvs ergnvylmgl vtvdegnrga
      181 daasqvpgve kvvkvfqyiq pqdaqalqaa spsgasgaqa aapadaatvg avpdasvqst
      241 plqppapisn sssvhpgnpk atpq
//
LOCUS       WP_175817293             829 aa            linear   BCT 11-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Burkholderia diffusa].
ACCESSION   WP_175817293
VERSION     WP_175817293.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 829)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 829)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18415115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..829
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..829
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=91508
     Region          11..240
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          38..66
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          71..99
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(72,75..76,79..80,82,106,109..110,113..114,116..117,
                     140,143..144,147..148,151)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          104..134
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          129..819
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          139..167
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          173..201
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(174,177..178,181..182,184,208,211..212,215..216,
                     218..219,242,245..246,249..250,253)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          206..236
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          241..269
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          275..303
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          309..337
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          342..372
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          377..405
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mqqttdilga alahhqagrl gdakagyeql lagepahpda lhflglltcq agqpeegial
       61 mrrsidayps aiyhnnlgna lrergrldda ieqyreavrr qpeyaeahnn lgdalrearq
      121 pdasmqhcaq aialrpdyaq aynnlgnalk dlgqadaavl aygkaiehdp ryadaynnlg
      181 nvlttqrkfd aavdsyraav alspgraivh gnlgtallar gdldesiatl rraveldprd
      241 pqvhnclgsa lreagrndea ivhferviel sggdvdahln lsralksqnr ieesveagkr
      301 aieldprrae gyvnlahayy wldrvddaiv qyrhalefdp dsadihqnls ialcqarrvh
      361 ealesahaav alepgtarry ahladvlrkt gdvdaaiqcy rralecdpdn pgtytsllfc
      421 lagqtafdpd ayladarvfg armsmhaqpw rhrpaplngr rlrvgfvsgd frrhpvgifl
      481 esvvahldrs rlelvafttf dteddytarl kphfdgwhri tdlgteqtar riheeridvl
      541 vdlaghtahn rlpafawkpa piqvswlgff astgiaemdy flgdahvlpa aeeahfverp
      601 wrlpdsylcf tpppydvqvg plpmlrnghi tfgcfgklvk vtdevvrvws rllhtvpgak
      661 lllkayelav edicdatrar faahgidadr lilepgssrd ayfaaynrad vmlspfpypg
      721 gtttaeslwm gvpvlgmkge rfvthicesl lhaaglgdwi asdeadyiak avafsrdrge
      781 laamraglrq qmqrsplgda krfarhleda fhgmwdawla gtpgdapar
//
LOCUS       WP_175817302             141 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Burkholderia
            diffusa].
ACCESSION   WP_175817302
VERSION     WP_175817302.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..141
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15007
     Region          6..>127
                     /region_name="COG3576"
                     /note="Predicted flavin-nucleotide-binding protein,
                     pyridoxine 5'-phosphate oxidase superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442796"
ORIGIN      
        1 mnpaplgdea vafiheqafl ivatanaagd sdcsyrgrqp radgsfaplv dlpdrrtlvl
       61 pdfagnnlfn tignllvnpa iallfvdfvr qttwlvqgra tidedagsra hlwpdalryv
      121 vvdvesaqar adaglpplvl a
//
LOCUS       WP_175817332             334 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Burkholderia diffusa].
ACCESSION   WP_175817332
VERSION     WP_175817332.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10513792
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..334
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39076
     Region          177..308
                     /region_name="FA_hydroxylase"
                     /note="Fatty acid hydroxylase; pfam04116"
                     /db_xref="CDD:397991"
ORIGIN      
        1 mddlqfgtrn rrgdwapnqh lelapfwtrp lslrkivgwt igyvwpwnai aiattllwwy
       61 fvvpdmatmk tigwgwvfkl lvanwsgifl ffgyfefryy rrrvqerrfk yngrfpaeqp
      121 sdvfwfrsqn idnfmrsffv svpigtaiev gllwafangl tpmvewrehp vhlvaltlla
      181 pivhevhfyf vhraihwgpl ykwvhsvhhn svnpspwssl smhpvesavy fgvalwvlal
      241 pshpflavyf fhlagfgavv ghigfdrlem adgiapksha yahylhhkff evnycdngtf
      301 pldkwfgswh dgspegdrlm qerfnrkker vnat
//
LOCUS       WP_175817392             323 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175817392
VERSION     WP_175817392.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..323
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34824
     Region          13..80
                     /region_name="HTH_MlrA-CarA"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators MlrA and CarA; cd01104"
                     /db_xref="CDD:133379"
     Site            order(14..16,30,47..49)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133379"
ORIGIN      
        1 mpprkdrdtp hryrsgeaar larmpaatlr iwerrydvia ppktpsgqrm ysdddvqrir
       61 llktlvnqgh aigsiaslsr eelealslts thgpalpeag vslavigals iseaavermg
      121 iriaaridsl ddasehastp vdaliattts lhedvvsqla alaqklnaha vavvyafgta
      181 eavelarlsg felfrstegq tnpasiisrl aqavvkarqs neadrglwlr trrrfdeatl
      241 aslsglsttv kcecprhlse limqlgafer ysdecvsrsp adallhrhlg daanraaell
      301 etalaiilre eglggttpel kal
//
LOCUS       WP_175817408             316 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia diffusa].
ACCESSION   WP_175817408
VERSION     WP_175817408.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..316
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=33131
     Region          15..159
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          172..311
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mntstspvqa vpasqrvlia vdgstastha layakaflps naavhivsva enprtlvplg
       61 skataflesa rdellrdasd alsraqgais rddisidtev idlsthggdv vhalaesaqa
      121 wqaelmivgt rqhhgllgwi egtvsgplgk lvgcpllivp egfasvaehl prrmlfavdg
      181 spialhalqt glkfsrpete fraihvldrp tslgdfvpve tleaalvseg nralqkamal
      241 ldgtpahaqs qliqtdrtga dvphlivnda iewsadmivm gthgrrgvtg wlvgsvagrv
      301 aritktpvll vsapha
//
LOCUS       WP_175817435             167 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia diffusa].
ACCESSION   WP_175817435
VERSION     WP_175817435.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..167
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17564
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mysnilvald gsdtssrald aalnlasetg arltpvyvvd flvpaydtyg ydpsilidaf
       61 reeglrvtdd aakrmkardv agtprisnva pagedvaqhi vglageinad livmgthgrr
      121 gfqrlflgsv aervlrqarc pvlmipassa akasaettaa stekeps
//
LOCUS       WP_175817438             342 aa            linear   BCT 11-JAN-2025
DEFINITION  LOG family protein [Burkholderia diffusa].
ACCESSION   WP_175817438
VERSION     WP_175817438.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Naseem,M., Bencurova,E. and Dandekar,T.
  TITLE     The Cytokinin-Activating LOG-Family Proteins Are Not Lysine
            Decarboxylases
  JOURNAL   Trends Biochem Sci 43 (4), 232-236 (2018)
   PUBMED   29525484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..342
                     /product="LOG family protein"
                     /EC_number="3.2.2.-"
                     /GO_function="GO:0016799 - hydrolase activity, hydrolyzing
                     N-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0009691 - cytokinin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38139
     Region          154..318
                     /region_name="PpnN"
                     /note="Nucleotide monophosphate nucleosidase PpnN/YdgH,
                     Lonely Guy (LOG) family [Nucleotide transport and
                     metabolism]; COG1611"
                     /db_xref="CDD:441219"
ORIGIN      
        1 msttvkrapa gmakgnarrr papvaaiaka pgkrlrtrpd avvrkdgiqr isrrarrtak
       61 ipnrarandd atvlegsgmr girlqfdywk aeerlqneri ghavviygst rivapsvana
      121 rldeanrlla erphdpsrrr avaiasrlve ygvyyrvare fgrivahadr ctrtarlaiv
      181 tgggpgimea anrgayerga psigfnielp reqapnpyit pdlcfrfhyf airklhller
      241 akaavffpgg ygtfdelfev ltllqtrkia plpvvlvgea ywrravdlaf ladegmidrr
      301 dlelftyces aaaiwhaigs wyarrrerap arckasakpr av
//
LOCUS       WP_175817444             197 aa            linear   BCT 11-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Burkholderia
            diffusa].
ACCESSION   WP_175817444
VERSION     WP_175817444.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..197
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=20978
     Region          1..196
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mtyalilvnf avfiaeasgw pvlidlfalw pparpgvpat pgfhvwqllt ysvlhaslah
       61 iafnmfglym fgrdvervlg rarflalyla svlagaitql aviralppsd aptvgasagv
      121 fgaliayavl fpkrrvvllf ppvpmpawlf algyaltell sglsgdtsgv ahfahlggml
      181 galaclafwr tradera
//
LOCUS       WP_175817449             216 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia diffusa].
ACCESSION   WP_175817449
VERSION     WP_175817449.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..216
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=23621
     Region          3..144
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
     Region          136..>216
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mksdselkkd veqelewdps idavrigvev herivtltgh vasylekvav rkaveriegv
       61 rgivlelevq tddgkrrsde dvaiaarsll mwdaglgeqa vhvtvengcv tlsgevmwsy
      121 qmqeaerave rlrgvtriln eihvrphptq sdiagkiqaa lirhateeaa hvgitvqdgc
      181 vtltgevgsl serwlafdaa wsapgvrdvv dqltva
//
LOCUS       WP_175817493             146 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia diffusa].
ACCESSION   WP_175817493
VERSION     WP_175817493.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..146
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15617
     Region          17..146
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mtdgwvetgd wavlggdaar irdavfvreq rippewelde edplslhava yrvdaatgar
       61 ravatgrllr tatigrvavl adargqgags avlhalldaa rhrgepivrl yaqdaavsfy
      121 vrhgfaaige pfleigvphv emartp
//
LOCUS       WP_175817510             470 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia diffusa].
ACCESSION   WP_175817510
VERSION     WP_175817510.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..470
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49629
     Region          16..419
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(28..29,32..33,36,76,134..135,137..139,142,162,
                     165..166,169,251,254..255,258..259,262,290,294,346..347,
                     351,355,371,374..375,378..379,382)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msrpqspsaa qprpgraala afvgttiewy dfyiygtaaa lvfgkvffsr tmdpgvatll
       61 afvtfwagfa arplggivfg hlgdrvgrkt alvitlvmmg lattgigllp gyasigvwap
      121 aglvvlrvlq giavggewgg avliasenap khrsilyaaf aqqgsptgnl lataaffals
      181 alptpsflmw gwripfllsa vlviigmvir lrleesiemq rvlarkrtvk lplrdvvrdh
      241 wpvvllaagt lpvinvtyfr stfalswatk elgyaqgtfl gilsislvvq flmqpvgawf
      301 vskvdmrram cwilipeivl mpvmfhalat rsywvavagm cistipsamf ygavggvlar
      361 vfpanirytg lslayqlsal vvgggtpvla qailnatgsi vgvaiasgly alvslacmla
      421 llnrtgyrad elssaersda aewgtegasa espagetaqa gdrgalkpag
//
LOCUS       WP_175817549             407 aa            linear   BCT 11-JAN-2025
DEFINITION  RHS repeat domain-containing protein [Burkholderia diffusa].
ACCESSION   WP_175817549
VERSION     WP_175817549.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..407
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46469
     Region          <4..298
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mprikaldnl lkqyagthyq ydahgnltqr whngkegrft wdlfdrlthy ederlkvdyt
       61 ydalgrrlsk hsqahyeerr eagphwnrae rvkrnralqc gftlygwdgd tlaweskiad
      121 edgfgartth yvyepgsfvp vaqavrddai elldqpeygd yyrqdedplw lppppaptin
      181 slawyqcdhl gtpqeltdeh seiawsaeyr awgvaqeair kasgkapian pirfqgqyhd
      241 hesglhynrh ryydpssgrf vskdpiglag ginvhqyapn pvewvdplgl akmpdgvgrk
      301 passkpnqna kcpcrkewev nrfdricegr lngtsvkyyh dpdtelwwsa dtkghggsaw
      361 kvmaqvgndl vhkqdadiyg dymgkhkget gklmsmksmk crdskgg
//
LOCUS       WP_175817513             324 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Burkholderia diffusa].
ACCESSION   WP_175817513
VERSION     WP_175817513.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..324
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37437
     Region          134..275
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mlhlidafvs diqtwlyvdv vqpllfkfnl mgydedtyda lywviigalq mvlmfallrp
       61 leallpverw qnrravrvdv iytaisklgi ytlffffalq pvfdnfqawl rlhgvanvnl
      121 dylwpgvtsr pivafaiylv vldfagywyh rwqhkfgiww elhavhhsqr qmslwcddrn
      181 hlldnviqsc ffaaialvig vtpsqfvvlt avtnfmqsiq htnarlsfgw lgerllvspt
      241 fhrrhhavgy ghegtkygcn fgvlfpwwdm mfgtaswnrt veptgireqv egvsygdgfw
      301 aqhglafvri frrlvpakrg aasa
//
LOCUS       WP_175817557             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175817557
VERSION     WP_175817557.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33190
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..290
                     /region_name="PBP2_CrgA_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08475"
                     /db_xref="CDD:176164"
     Site            order(103,107,146,161,163,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176164"
     Site            order(104..105,109..110,112..113,116,120,122..128,190,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176164"
ORIGIN      
        1 mrnnlngiav fvaaaeadnf aqaaetlhit rsavgksiar learlgvvlf qrttrsqslt
       61 degalfyeyc lraveeihag eallesgkwq mkgrlrvsmp alfghlcvap iliglardhp
      121 eldldlsfsd rtidlveerv dlavrvgalp dssglvaral gehkmafcas paylarcgep
      181 atvdalaqhk alaytrygqm hrwqvvvdgr teelqpaarl lsddlcavld aavaglgvaw
      241 lpywlvrdei rrgalrellp dqpgvtyaih avwphtshlp lkvraaidal vnqlparlae
      301 veaqa
//
LOCUS       WP_175817598            1130 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha-1,4-glucan--maltose-1-phosphate maltosyltransferase
            [Burkholderia diffusa].
ACCESSION   WP_175817598
VERSION     WP_175817598.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1130)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1130)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 1130)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10571012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1130
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..1130
                     /product="alpha-1,4-glucan--maltose-1-phosphate
                     maltosyltransferase"
                     /EC_number="2.4.99.16"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0016758 - hexosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009313 - oligosaccharide catabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0030979 - alpha-glucan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=124119
     Region          31..>115
                     /region_name="AmyAc_family"
                     /note="Alpha amylase catalytic domain family; cl38930"
                     /db_xref="CDD:476817"
     Region          <77..650
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          461..646
                     /region_name="GlgE_dom_N_S"
                     /note="Alpha-1,4-glucan:maltose-1-phosphate
                     maltosyltransferase, domain N/S; pfam11896"
                     /db_xref="CDD:463388"
     Region          651..1005
                     /region_name="AmyAc_GlgE_like"
                     /note="Alpha amylase catalytic domain found in GlgE-like
                     proteins; cd11344"
                     /db_xref="CDD:200482"
     Site            order(704,708,719,721,764,796..797,799..800,834,836..837,
                     865,923,976..977)
                     /site_type="active"
                     /db_xref="CDD:200482"
     Site            order(782..784,791..793,806,839..842,844,847,869,871..872,
                     875,879)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200482"
     Site            order(836,865,923)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200482"
     Site            order(868..870,887,890..891)
                     /site_type="other"
                     /note="acceptor binding site [chemical binding]"
                     /db_xref="CDD:200482"
ORIGIN      
        1 mnvtppfaph lyfcdarlvg pldawpdtfa hvagmgfdhv liggfwaasv agfprhvadf
       61 hqpaatfatr agaletfsrl aqiahghglr vmlevvpdri aranplrveh pdwyvershd
      121 dalidprraa heldvahaqv gedsthdala awwcthlaaf adagaagfli daphhlpaaw
      181 wpgwraalrr arpdvtvlag vpghardala qfeaagfdav fssvrwwdlr spwfadehrl
      241 lrrigspiaf pdaydgprla ddwrdapdet varayhralw taaavgtgwl vpmgfergvt
      301 lplmardada tryraafdga rfdlsgaiad anawrratpl aaqrgeiaql sapgaaatal
      361 lrgtgpsleh ddtallialn pdldteapvd patilpgvpg gfthvatpdg arkhapvale
      421 aftlepggya lreawrappa ipradaaser talsaalvad riaiervepa vdggrfaikr
      481 vigetlvvha sifsdghahl aaalqwradd eddwrevpfv aepndrwhtr isldrlgrha
      541 frviawrddw aslvtdiakk raagqdvtle vreaqlllat alkladpadp raigqmerlt
      601 agfkdaspde rlaligapal adafaalryr pfvthdetvy pvdverraar fsswyemfpr
      661 sasndphrhg tfddviaqlp rirdmgfdvl yfppihpigt tarkgrnntl kagpddvgsp
      721 yasgshdggh tavhpqlgtl asfrtlvdaa raqgleiald faiqcspdhp wlaahpgwfa
      781 wrpdgslrfa enppkryqdi vnpdfyapda lpdlwvalrd avlfwvdagv rifrvdnpht
      841 kplpfwawmi advrgkhpdv vflseaftrp gmmyrlakvg fsqsytyftw retkrefidy
      901 lteltagppr effrpnffvn tpdinprhlq naprsqfvir aalaatlags wglysgfeig
      961 esaplpdsee yadaekyelr ardwnkaahi gaevarlnra rrehpalqth lgltfadadn
     1021 dqvlvfvkat pahdsvvaia isldpwhpqa anftldaslw rgfglvdgep ldaleqdaah
     1081 aetwrghrqy vsldphvrpy aiwrlapspg aaraaapepg darhpsgaha
//
LOCUS       WP_175817632             390 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia diffusa].
ACCESSION   WP_175817632
VERSION     WP_175817632.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..390
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42715
     Region          12..282
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 midgqillgh sipwgmvggg lgsqigyshr saalrdgsfq lvagafdida ergrqfgvkl
       61 gvdaqrcysd yrtmfeaeak radgiravsi atpnnthfei craalsaglh vvcekplcft
      121 teeaealqrl sveknrivgv aygysghqmi eqaremiarg dlgeirivqm qfahgfhseg
      181 veaasaaarw rvdpkfagps yvlgdigthp lyisevmape lkikrlmcsr qsfvksrapl
      241 ednaftimey dtgaigyvws savnagsmhg qkvrvigska svewwdehpn qlryeiqgqp
      301 aqvldrgmgy lhpqalredr igaghpeglf eawsnlyarf alamdaadrg dgqaleaihf
      361 pdvragvegv rwvencvrsa daggvwvdyr
//
LOCUS       WP_175817646             341 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia diffusa].
ACCESSION   WP_175817646
VERSION     WP_175817646.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..341
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35603
     Region          10..341
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mgnlnpvada qsmtiktrha kwppelsifl vlvgislffe vigwlvvgqs flfnaerlei
       61 ivlqmavigi iavgvnlvii tsgidlssgs vvaaaavvsa slaqvsdfpr avfphltdlp
      121 iiwpvlagvc vgllvgllng slialtgipp fiatlgtmva argfakwftn gmpvsmltdq
      181 faaigagayp viifvvvaai fhvvlrytrf gkytyaigan rhaavvsgin vtrhlvfvya
      241 iagllsgiag tvtaaraisg qsgmgvmyel daiaavvigg tslsgglgrv tgtvigvlil
      301 gvmtsgftfi ridayyqemv kgaiivaavi adqyrnkkkr r
//
LOCUS       WP_175817754             666 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Burkholderia diffusa].
ACCESSION   WP_175817754
VERSION     WP_175817754.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..666
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71008
     Region          1..460
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          598..662
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(620,629..631,638)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            630
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mfdkilianr geiacrvaat ckrlgiasva vysdadanak hvaacdeavh iggsaaadsy
       61 lrieriieaa ratgaraihp gygflsened fahaceaagi afigppvdai aamgskaaak
      121 almhaaavpl vpgyhgddqd aahlhreada igypvllkas aggggkgmrv versedfpaa
      181 lascqreaas sfgndrvlie kyltrprhve vqvfgdthgn tvylfdrdcs vqrrhqkvle
      241 eapapglhed vrqamgeaav aaaravnyvg agtvefimtg eafyfmemnt rlqvehpvte
      301 mvtgldlvew qlrvasgepl plqqdelrvh ghaiearlya enpargflps tgtlkhlrlp
      361 egvefaigas vridsgvreg daitpfydpm iaklivhgad raealgrmlr alracevvgl
      421 htnaaflqri vtcepfaiad ldtgliernh dalfapqqpp ratlalacaa llarerdtaa
      481 rqgaspwral pdwrlnggyr rtlewhaper eadvtvtyed dggskrlaag davaqpfawt
      541 rgatpldfdv tldgvrssgr vyadgdsfhv ftqgvaetfe wrnvlahagd aehgggrlta
      601 pmpgkviavl vepgqkveag tplivmeamk mehtigapga gvvaevlygv gdqvadgaql
      661 lmmaeg
//
LOCUS       WP_175817738             585 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia diffusa].
ACCESSION   WP_175817738
VERSION     WP_175817738.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..585
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=63828
     Region          8..585
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mtikrlsilq fsalvtlsaq aqqaptpndq aaaaranaeq nqqvqqrrda qqrdatvqap
       61 gvrsdvprpe aypvlptetp cfridrfald vpdslpaaak mhgasalpmd rfafardwlt
      121 hyagqcvgkq gvdlivkgvs qailargyit trvlvpeqdl stgtlklali pgvirhvrfe
      181 aeklrgtwkt afptrdgdvl nlrdieqgle qmkrvssqdv smriapgdmp gesdvvldvk
      241 rgkpwtvvas idnsgtratg klqgnvslgi dnplglndif nvgfnqdlef gdkrfgshgw
      301 nafysvpwgy wtgtlsayts tyfqplaavn qtfvasgnmk tvdfklnrvl trsrndvfgv
      361 qvrltrrfgd syiegttips shqnaaflef glndrhyfgs sqfdgslayr qglgwlgstd
      421 smfaaeggqt yrfkmvvlda nlstpfvigt qpfkyvttfh gqytgntvsy ldsvtigsry
      481 tvrgfdgetl lagsrgfywr nelqvpvaqt glsayagldy grvwgpepva lvgtqlagav
      541 igvkgsvmtr fggygydlfa gtpvykpsgf ptarvtvgfq ltaqf
//
LOCUS       WP_175817757             321 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia diffusa].
ACCESSION   WP_175817757
VERSION     WP_175817757.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..321
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34816
     Region          11..224
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(52..53,55,69..71,77,79..80,121,223)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(52,54..55)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(77,80,83,90)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(113,117..120,122)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(118..119,142..144,196..197)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          237..321
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 msaatltvrv arkwqeardi cgfefvsddg splprfdaga hidvylpgrl vrqyslcnhp
       61 epgdryqiav lrdaegrggs rtihddvrqg dtvrigmprn qfplapdaph hlllaggigv
      121 tpilcmaerl fssgtpfdmh ycarstdrma fverikaagf rdrarfhvdd gdpaqrldlp
      181 avlaaapdgt hlyvcgprgf mdavlnaare rnwaderlhy effggavass gadrafqvri
      241 assgkvidvp aectviaala angvdvltsc eqgvcgtcvt rvlegepdhr dsylteaeqa
      301 agdqfmpccs rsrsdllvld l
//
LOCUS       WP_175817761             728 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia diffusa].
ACCESSION   WP_175817761
VERSION     WP_175817761.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 728)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..728
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78225
     Region          51..728
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mpsrrpprra rtlrpwrasl palitlcvas gahadaepaa taspaapsgs stpapperel
       61 ptisvsasaa tdptvgyqpr tssvaggndr plkeipqsva vvsssvmqdq qarslddvlg
      121 nisgvtqtnt lggtrdafik rgfgsnndgs vlvdgvrtpv lhsylatidr vevlkgpasl
      181 lygmqdpggv inlvtrkpee tfggsisasr tshggsgaqf dltgplgkpg qvaggtlafr
      241 ltgeydtsry wrsfgrqrna liapalswhd antsidvsyq yvdytmpfdr gtvlvngrpd
      301 dtlryrryee awaqssgiqe tlrariehrf sdawrvraty gwgrdrydqy itratafnst
      361 tgalsrtsda nlgrndsdqi atlgllgnlt lagmnhalyi ggeyerqrsf rgdtirgtat
      421 kgfnlydpvy gllapggtvs tkqsdslskv htysmivqds vkitdrltav gglrwedwqq
      481 esgmgrpfvf adrshgnvwl pqfglayalt psltayanvs rsfkpnvasn vaaplapefg
      541 rvleaglkfn lkpgitgtla ayqidkrnva vtvgditsti gtarsrgiel dvagqltrhl
      601 sligsyaytn andrdsntpl vnvarhmgsl favydtaian lpgrwrfggg arlvgarpgd
      661 tansftlpgy vtvdafaaye ttigkfptri qlnvknlldk tyypssnsnl ivavgeprlv
      721 tltttvsf
//
LOCUS       WP_175817858             338 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175817858
VERSION     WP_175817858.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..338
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37946
     Region          25..335
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 msktppvppl psrsregihd lrivrygfll vddfslials aaidplrian mvvgrrvydy
       61 rligpgdavv rssdgirvvp dvslsdsgtf dvvfvvgpnp iprrrtgaiv dwlrrqarng
      121 talggldtgs yflaraglln gyrctihwed qdvlmeqfpk ltvstrlyei drdrytcsgg
      181 vapldlmvhl laaapgspal aarvlellva eprsreyrqq tslrqyigae hekldealql
      241 mesnveetls vpeiavhlqv sqrqlqrwfq drlgkspaqa yleirllrar qllyrtatsl
      301 eevcartgft stthfatryk eqfqispiad rrryqnal
//
LOCUS       WP_175817877             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia diffusa].
ACCESSION   WP_175817877
VERSION     WP_175817877.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33777
     Region          20..74
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          103..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(113,117,156,170,172,231,248,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(114..115,119..120,122..123,126,130,132..138,199,
                     225..229,236..237,240)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mtsdpipapd kpldlldvgl fvraallanv saagrefgvs aavasariaq lerqlgarll
       61 hrttrrislt qdgevfmara eallsaadaa rasvghgrse pygrlkvsms ssfgrqhvap
      121 vipaflrryp svsldlrlsd eivdlvddgy dvairlgalk dstlvarkla tnrrvlccsp
      181 aylaehgtpr hpadlaqhec vilgdqrdws fvtpqgpltv rvggrlvasn geairealvd
      241 gfgiaikstw dvrpllasga lvtvlddypf andvaiwavy psrahvplkt lafiaflaeh
      301 fgdppywdra der
//
LOCUS       WP_175817897             200 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Burkholderia diffusa].
ACCESSION   WP_175817897
VERSION     WP_175817897.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..200
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=22422
     Region          6..142
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,72..73,76)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(71,123..124,126..127,131)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(77,82..83,119,122..123,126..127,130,133)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(100..102,119..120,123..124,127,131,134,138)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(100,124,127,131,134,138)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(132,138..139)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 mrklyygris ttdgqtaasq yddarshgvg dtdifidegv sgyhvapger eqwrkvehdl
       61 rhggtlivrw ldrisrryde lhrtmqrlma lgvrvectln gmtfdgrekd piqkatrdav
      121 lafmaaqgea dyknraemqr rgvaiakaag kyrgrarshd yatikawrte sgasiretae
      181 rfgvgtatvk racaeptskr
//
LOCUS       WP_175817915             421 aa            linear   BCT 11-JAN-2025
DEFINITION  replication-associated recombination protein A [Burkholderia
            diffusa].
ACCESSION   WP_175817915
VERSION     WP_175817915.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..421
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=45969
     Region          1..420
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 mpdlfqsklh rpladilrps tlgsvigqah llgdgmplrq afdsgnphsm ifwgppgvgk
       61 ttlarltaha fnrefiglsa vlcgskdird aiaraqhlrd hasrhtilfv deihrfnkgq
      121 qdillpavas glvtligatt enpsfeinra llsrarvyvl kslsdadmrr llhraqeial
      181 hglkfddeav dtlidladgd arrflnlleq tqtaastagi atisaafvrs alapnarrfd
      241 kagehfydqi salhksvrgs npdaalywlc rmldggvdwk ylarriiaia wddigladpq
      301 airianaaaq ayerlgspdg elafaqavly lacaaksnag gmaflkaraf veqdtprdvp
      361 mhlragsekm mkpaghmyrn phaepnscaa gqtylpegip dphwyepapr gleikiekkl
      421 t
//
LOCUS       WP_175817925             313 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Burkholderia
            diffusa].
ACCESSION   WP_175817925
VERSION     WP_175817925.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..>313
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
     Region          26..>267
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mssisalieq ygpresmeyd vvivgggpag lsaairlkql aaekgteigv cvlekgseig
       61 ahilsgavmd praitelfpd wkeqgaplsv evtedrflfl seksavttpn walpenfknh
      121 gnyvislgnv trwlgtqaea lgveifpgfp aaeilynddg svkgvatgnm gvgkdgepte
      181 nfqlgmelha kytlfaegcr ghlgrqlisk fkldanadpq aygigikelw eidpakhkpg
      241 lvihtagwpl ksdtyggsfl yhmdnnqvvv gfvvglgytn pylspfeefq rykthpsira
      301 fleggkrvsy gar
//
LOCUS       WP_175818054             621 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF262 domain-containing protein [Klebsiella pneumoniae].
ACCESSION   WP_175818054
VERSION     WP_175818054.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Bair,C.L. and Black,L.W.
  TITLE     A type IV modification dependent restriction nuclease that targets
            glucosylated hydroxymethyl cytosine modified DNAs
  JOURNAL   J Mol Biol 366 (3), 768-778 (2007)
   PUBMED   17188297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..621
                     /product="DUF262 domain-containing protein"
                     /calculated_mol_wt=73460
     Region          21..598
                     /region_name="GmrSD"
                     /note="DNAse/DNA nickase specific for phosphorothioated or
                     glycosylated phage DNA, GmrSD/DndB/SspE family, contains
                     DUF262 and HNH nuclease domains [Defense mechanisms];
                     COG1479"
                     /db_xref="CDD:441088"
ORIGIN      
        1 magqyekait ikqaidsinl rhyllpaiqr kfvwsyrqic llfdsimrdy pinsfmmwdi
       61 rsasikndyk fyeflkeycq rfneenpcvp tnagfhdfka vidgqqrlts lyiglcgtya
      121 yknprvwwps aqddrflppr klyvdltapl dsddepmmky nfrfltdkey tdsltdnkhh
      181 wfclheifky eqidspddil fkvvvpelek rglissefsr ktllklytki rteslihyfn
      241 essqdidhvl dvfirtnsgg tklefsdllm siavahwqgd frreldeltk nihqnnemgf
      301 yierdwflkt slmlidsdvr fkvknftsee vgkiqqqwse ikscikqtfv lirrfginpq
      361 slisknavip vvywlykkqt nghplyttin llnknhners visqwfymvl lkgifgsqad
      421 alltsirdvm knslsdvhfp lekiidrykg snkdlrfdne yiesllniry gegrcrallh
      481 llfpemnpte vfhidhlhpr nhfsnkylek ldyianspek lsfyenpehw dtipnlhlln
      541 hsqntskqnt slkqwlshss nnytpsmllv sdeniefsrf qefynerrna lkqrllnrvf
      601 lttkidssps tmdtdeeilt d
//
LOCUS       WP_175818065             397 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Wolbachia
            endosymbiont of Dirofilaria (Dirofilaria) immitis].
ACCESSION   WP_175818065
VERSION     WP_175818065.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
  ORGANISM  Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Wolbachia endosymbiont of Dirofilaria
                     (Dirofilaria) immitis"
                     /db_xref="taxon:1812115"
     Protein         1..397
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43818
     Region          1..397
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(99..101,125,173,205,233,235..236,244)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(102,135,198,242..244,273,276)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            236
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mlelakrmsl iklsptvavt dkvnrlkseg kkicilaage pdfdtpghvk kaaiqamneg
       61 ktkytavdgt relkeaiink lkrdnnleyt lsqvcvgaga kqvlfnlfma tinpgdeaii
      121 papcwvsyvd mvslfdglpv vveckknfkl tsellknkit kktkwlilns pnnpagvvyt
      181 ydelreiaqm llehphvnvv tddiyehivy dekfftiaqv eprlydrvfv vngvskayam
      241 tgwrigyvag ssdvikaisi lqsqstsnpn siaqaaavea lngshgflke rvrilknrrn
      301 fmvkklgsvp glsmfipqga fylfiscegl lgkstksgri insdldfaey lledylvavi
      361 pgvafslknf irvsyatsqe qleigcnsiv kacemls
//
LOCUS       WP_175818178             236 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Wolbachia endosymbiont of
            Dirofilaria (Dirofilaria) immitis].
ACCESSION   WP_175818178
VERSION     WP_175818178.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
  ORGANISM  Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Wolbachia endosymbiont of Dirofilaria
                     (Dirofilaria) immitis"
                     /db_xref="taxon:1812115"
     Protein         1..236
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26054
     Region          3..>235
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mlinnisysy snqgdftlsn inievkrgnv tcllghsgcg kstilkliag ienpksgaif
       61 indrlvasnn tsiaiehrnv glifqhsalf phktvienit fairsaskke kyltaleilk
      121 llniakyenm ysnalsggqq qlvaiarvma qnpdvvllde pfsnldimlk cqtrhhvlsl
      181 frsknipvlm vthdpqealk vadsiyvmkn gkiiqsgvss diyhklkdht sakffs
//
LOCUS       WP_175818207             412 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Wolbachia endosymbiont of Dirofilaria
            (Dirofilaria) immitis].
ACCESSION   WP_175818207
VERSION     WP_175818207.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
  ORGANISM  Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Wolbachia endosymbiont of Dirofilaria
                     (Dirofilaria) immitis"
                     /db_xref="taxon:1812115"
     Protein         1..412
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45868
     Region          22..407
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mfqfiiitlm avfnttscya idieeaiska iknssklksq fyqyksaekq lkssglagfl
       61 pdinlqynfd snfnlynnkh nlpgkrltls qriigggsaf atfsqsshll kaekiqfqqs
      121 kqevalnavk vyvdvlrrta ilklkehker vslenlssik krlslgevtn aevllakakf
      181 sssvlervda egklklania yfhligenpn elseandklp yvpelneclq laktnnlslk
      241 aavykkraar maaiaetskw lpslnlnask nlnesvsldt llgttsitft ldvpifkrgi
      301 ntfniskarm nakksvydyy etvknierev tnawnnvlta kamikasqka ekaaalaleg
      361 veqevnlnlk stteflntkd tllkarsdlv eakgnyiisi ykllfainsi nl
//
LOCUS       WP_175818271             208 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Wolbachia endosymbiont of
            Dirofilaria (Dirofilaria) immitis].
ACCESSION   WP_175818271
VERSION     WP_175818271.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
  ORGANISM  Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Wolbachia endosymbiont of Dirofilaria
                     (Dirofilaria) immitis"
                     /db_xref="taxon:1812115"
     Protein         1..208
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22761
     Region          9..207
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mvdnnfiirv lssiiillif sfamyfsdls fyllvfsiav lssfewynlt rgsrilcvfa
       61 lalialpnas liylynlpqg kytlvwlilt vwsidvtayl fgknfggaki cpiispgktw
      121 lglfgaalag iicttfgsvf lslfsifysp vigltvaila qlgdftesli kraynvkdsg
      181 smipghggvl drmdsfifta pliaiyvn
//
LOCUS       WP_175818264             248 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Wolbachia endosymbiont of Dirofilaria
            (Dirofilaria) immitis].
ACCESSION   WP_175818264
VERSION     WP_175818264.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
  ORGANISM  Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142575
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Wolbachia endosymbiont of Dirofilaria
                     (Dirofilaria) immitis"
                     /db_xref="taxon:1812115"
     Protein         1..248
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27232
     Region          9..244
                     /region_name="SDR_c"
                     /note="classical (c) SDRs; cd05233"
                     /db_xref="CDD:212491"
     Site            order(13,15..18,37..39,66..68,98..100,122,149..151,166,
                     170,196,198..200,202..203)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:212491"
     Site            order(123,151,166,170)
                     /site_type="active"
                     /db_xref="CDD:212491"
ORIGIN      
        1 mgklegkial itgasgeigs avakrfireg ayvilvsrsv dnlrplygei ekleefkegs
       61 vkliqldlld fenvkilanm menlklsesg aldilvacig ilgklnpihd celeelqnvm
      121 ntnftanwyl lknldpvlkk sssgrvifmt sevtlspssy pywvpyaask aaleimvkiy
      181 asetkytklc vnavypegpi dsemykqafp gkdvpelvlp ekltdkfvel assdcnisge
      241 ilplsksv
//
LOCUS       WP_175818296             254 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome c1 [Wolbachia endosymbiont of Dirofilaria (Dirofilaria)
            immitis].
ACCESSION   WP_175818296
VERSION     WP_175818296.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
  ORGANISM  Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10490041
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Wolbachia endosymbiont of Dirofilaria
                     (Dirofilaria) immitis"
                     /db_xref="taxon:1812115"
     Protein         1..254
                     /product="cytochrome c1"
                     /EC_number="7.1.1.8"
                     /GO_function="GO:0008121 - ubiquinol-cytochrome-c
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28540
     Region          34..249
                     /region_name="Cytochrom_C1"
                     /note="Cytochrome C1 family; pfam02167"
                     /db_xref="CDD:426633"
ORIGIN      
        1 mlvknmfavf cvlslanlac aeefkpstnk kmnwsfngit gsfdresiqr gykvykevca
       61 achsmnrvaf rnlqdagfse edvkqiaasy qvkdgpndlg emfyrpgips dyfiapfntk
      121 eaaaasnnga vppdlslivk arhgganyvy slltgyqnge hdennlyfnp yfptgklama
      181 pplsegivky ddarqatven maydvvnflq waaepeleyr hklgfkvvay fiiltilfil
      241 tnnriwskly knkk
//
LOCUS       WP_175818345             370 aa            linear   BCT 11-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Wolbachia
            endosymbiont of Dirofilaria (Dirofilaria) immitis].
ACCESSION   WP_175818345
VERSION     WP_175818345.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
  ORGANISM  Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Wolbachia endosymbiont of Dirofilaria
                     (Dirofilaria) immitis"
                     /db_xref="taxon:1812115"
     Protein         1..370
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42134
     Region          7..364
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 msvldklail llvfsfpffs ysyqfrtkak qavildlasd sfifehnpde kiapssmskl
       61 mtlyiafayl kagvinmedk fqvskkawkr kgssmflreg qfvtvkelle givivsgnda
      121 citlaegiag seenfviemn eiaqklglsn shfvnssgwp deahfmsakd lvvlakrift
      181 dfpeyydlfs eqyltynevl qknknlllfy gigvdglktg ytsagaygiv asarrndrrv
      241 fvvvnglste kerieeakrl iqysldhfht kkiftkddii eevnvlygkd rkvpitvard
      301 viitysrnlh dkikvhveyk dmipapikkg qevgkifiki pgikqqtipl yavnevqeln
      361 yvekffrmlf
//
LOCUS       WP_175818387             138 aa            linear   BCT 11-JAN-2025
DEFINITION  nucleoside deaminase [Wolbachia endosymbiont of Dirofilaria
            (Dirofilaria) immitis].
ACCESSION   WP_175818387
VERSION     WP_175818387.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
  ORGANISM  Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Wolbachia endosymbiont of Dirofilaria
                     (Dirofilaria) immitis"
                     /db_xref="taxon:1812115"
     Protein         1..138
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=15043
     Region          1..136
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 melaveqakl ahkndevpig avivsgsniv ssthniyndp tahaeilvir qackllstpi
       61 lsdvdmyvtl epcpmcaqai sfarvrrvyf gaynpkgggi engvrifqfc shvpevyggi
      121 letecssllk dffkklrt
//
LOCUS       WP_175818381             269 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter permease [Wolbachia endosymbiont of
            Dirofilaria (Dirofilaria) immitis].
ACCESSION   WP_175818381
VERSION     WP_175818381.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
  ORGANISM  Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 269)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 269)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 269)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Wolbachia endosymbiont of Dirofilaria
                     (Dirofilaria) immitis"
                     /db_xref="taxon:1812115"
     Protein         1..269
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29159
     Region          8..262
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mfeiftqgff insltaivii slvtgtlgsf miwqrlsylg dslshssllg valalifris
       61 psisimliai vfaimlslnf nrlysvdail nivtnvvlss slilmsflps snssiisslf
      121 gdiltleqnd ivliflisav vtlilafrwr ywlmisinqd laivekvnvs lvrleflitl
      181 aifiavsaql igillvaafl lipassarli sktpvqmvvv atgfsvisgi sglmlsvsfd
      241 lltgptiilv aatyliiayf vrlvlnkfa
//
LOCUS       WP_175818407             272 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Wolbachia endosymbiont of Dirofilaria
            (Dirofilaria) immitis].
ACCESSION   WP_175818407
VERSION     WP_175818407.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
  ORGANISM  Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Wolbachia endosymbiont of Dirofilaria
                     (Dirofilaria) immitis"
                     /db_xref="taxon:1812115"
     Protein         1..272
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30988
     Region          3..245
                     /region_name="SDR_a4"
                     /note="atypical (a) SDRs, subgroup 4; cd05266"
                     /db_xref="CDD:187576"
     Site            order(7,9..11,30..32,60..62,85..87,111,115,134..137)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187576"
ORIGIN      
        1 mrlfcfgygy vakflsknll glgwkingts rnqgiqsinl fdyekinkdi fqnvthilvs
       61 ippdgddvle ryghyfqdir wlgylsativ ygdhfgnwvt eesetkpves rgksrlksek
      121 kwlnsklpvh ifrlagiygp grnmlvnlrl nkarnvqreg hlfsrihved isnilfssmq
      181 nmkpgeiync addlpatqse vityaaklln vsvpepievs slpdyaqsfy lgskkvsnvk
      241 ikkdlsisli ypnykvgles lyieelklht me
//
LOCUS       WP_175818408             214 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Wolbachia endosymbiont of Dirofilaria
            (Dirofilaria) immitis].
ACCESSION   WP_175818408
VERSION     WP_175818408.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
  ORGANISM  Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Wolbachia endosymbiont of Dirofilaria
                     (Dirofilaria) immitis"
                     /db_xref="taxon:1812115"
     Protein         1..214
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23328
     Region          12..213
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mielkgpeic asgnkknlvv clhgwgssgd nfvhlakvms kslpdscfiv pdapfkreig
       61 dgyqwfsled yseevlyngi knatlivnhf idtklrefgl kdiqlslvgf sqgamlaiht
      121 alarpqscas vvvysgrfll pskvipkiks kpnvcvihgd addivpfssl nlmvealkks
      181 gvnvegypih alghiineeg iklgvefikk nfks
//
LOCUS       WP_175818418             205 aa            linear   BCT 11-JAN-2025
DEFINITION  SCO family protein [Wolbachia endosymbiont of Dirofilaria
            (Dirofilaria) immitis].
ACCESSION   WP_175818418
VERSION     WP_175818418.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
  ORGANISM  Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Wolbachia endosymbiont of Dirofilaria
                     (Dirofilaria) immitis"
                     /db_xref="taxon:1812115"
     Protein         1..205
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23750
     Region          44..182
                     /region_name="SCO"
                     /note="SCO (an acronym for Synthesis of Cytochrome c
                     Oxidase) family; composed of proteins similar to Sco1, a
                     membrane-anchored protein possessing a soluble domain with
                     a TRX fold. Members of this family are required for the
                     proper assembly of cytochrome c...; cd02968"
                     /db_xref="CDD:239266"
     Site            order(77,81,163)
                     /site_type="other"
                     /note="Cu(I) binding site [ion binding]"
                     /db_xref="CDD:239266"
ORIGIN      
        1 mtkftrllpv mliallvvif lsycyftkry iftsiathnt evkigrdfvl inqdnqiihs
       61 qdfkdkymmi ffgfssckkv cpmnlgiise vltkldektn kklqtffitv dperdstekl
      121 kefqqqfdyr iqmltgerek idevitsykv yasktggeee inhssiiyli gpkgkyithf
      181 tadlnsdesq sdkiaaeikk yinel
//
LOCUS       WP_175818470             215 aa            linear   BCT 11-JAN-2025
DEFINITION  O-methyltransferase [Wolbachia endosymbiont of Dirofilaria
            (Dirofilaria) immitis].
ACCESSION   WP_175818470
VERSION     WP_175818470.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
  ORGANISM  Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Wolbachia endosymbiont of Dirofilaria
                     (Dirofilaria) immitis"
                     /db_xref="taxon:1812115"
     Protein         1..215
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24595
     Region          40..214
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 marngsvkss yirdlfvkey rkieeccile skkhsqisae egkllslfik ihrvssvvei
       61 gtlygyssic makalpeygh iytvesnfeh ssiarknfsa fnlnnkitli egnaseklse
      121 lstqapfdmi fidanksdyp kyldwaelyi kqdglivadn tllfntvfle sppkkvseks
      181 wyamrefnyr lsdekryysm liptdegmtv alklm
//
LOCUS       WP_175818532             390 aa            linear   BCT 11-JAN-2025
DEFINITION  elongation factor Tu [Wolbachia endosymbiont of Dirofilaria
            (Dirofilaria) immitis].
ACCESSION   WP_175818532
VERSION     WP_175818532.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
  ORGANISM  Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Wolbachia endosymbiont of Dirofilaria
                     (Dirofilaria) immitis"
                     /db_xref="taxon:1812115"
     gene            1..390
                     /gene="tuf"
     Protein         1..390
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=42980
     Region          10..390
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 maqiveafgk phvnvgtigh vdhgkttlta aitkyyghfv aydqidkape erkrgitiat
       61 ahveyetdkr hyahvdcpgh adyvknmivg aaqmdaailv vsgvdgpmpq trehillakq
      121 vgvkyivvyi nkadvadhdm iglvemevre llskyefpgd dvpvvigsal kalededsey
      181 gkksierlme kldeyvavpp rpvdlpflmp iedvfsipgr gtvvtgrier geiktgeeie
      241 ivglkatrkt ictgvemfkk cldkgcagln vgvllrgtkr eevergqvla kpnsitphkk
      301 fkaevyvlkk eeggrhtpff enyqpqfyir ttdvtgsikl legkemvmpg dnisieielq
      361 vpiamdkglh faireggrtv gsgvvseile
//
LOCUS       WP_175818630             424 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Wolbachia endosymbiont of Dirofilaria
            (Dirofilaria) immitis].
ACCESSION   WP_175818630
VERSION     WP_175818630.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
  ORGANISM  Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Wolbachia endosymbiont of Dirofilaria
                     (Dirofilaria) immitis"
                     /db_xref="taxon:1812115"
     Protein         1..424
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46037
     Region          1..421
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msnkigfltv falvissqig sgifmlpvsi apygiyslis wiisgtgavs lslvfatlca
       61 kfpetggphi ytkyafgstv affvgwtywv iswvsttalv ivgvgyltpf fyedvqsvrl
      121 llglllltvi tlinlreiaa agrvellltv ikvsvllaip mvalcffdrn nfiisekisn
      181 ltisqilars tlltvwcfvg velatapags indpaktipk avvlgticva iiyfinsfti
      241 mglingndla nskapyvdai rvmfsgswhl iisiiafifc vgslnswvls sgqvafglae
      301 dklmpqffak rnkhgspflg ivtssigtai lliltssnnf akqitsiidf svisflliyl
      361 tcslaflkvi ieernyckll vgviattfcc wiicetpint llisslftvs gtplylfwyr
      421 kvss
//
LOCUS       WP_175818631             424 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Wolbachia endosymbiont of Dirofilaria
            (Dirofilaria) immitis].
ACCESSION   WP_175818631
VERSION     WP_175818631.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
  ORGANISM  Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Wolbachia endosymbiont of Dirofilaria
                     (Dirofilaria) immitis"
                     /db_xref="taxon:1812115"
     Protein         1..424
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46722
     Region          1..421
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msdkigfltv falvissqig sgifmlpisl apygiyspms wmisglgaif falvfaflca
       61 kfpktggphv yvkyafgstv affigwtywi sswvsstavt iasigylapl fysdmqnirl
      121 llevvlilai mlinlrgvtt agrvelllti ikiialltip maalfffdrn nfiiseelss
      181 fttsqilahs tllalwcfvg lesvtasags vnnpgktipr aivlgticva viyfinnfai
      241 mglisgndla dsrapyadav kimfqgnwhv ivsvvafivs vsnlntwfla dgqialglae
      301 dklmprlftr rnkydapfyg imlstlgviv llvltsnknf veqvtliidv svvsflfiyl
      361 vssfaflkia mqekiyckll iggvailfcc wiiyeipirt llmsslfpls vtpiyllwyr
      421 ksir
//
LOCUS       WP_175818745             272 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175818745
VERSION     WP_175818745.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..272
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=29075
     Region          103..272
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mqldpsllpg dqyyicdndf vnyrldtsnl spsgypnvwk tsipgigval smqryssaav
       61 enlpfsfqsg pnsehttfpn ialaffrigv gvvsgeqeis fkalldapgl pkvalnvgpa
      121 rvnivndvyf escsaadkav tvqmgqeqie rikrgtateh pfgfdvrclg lkpnaaggsv
      181 rvyfegnavs dgllrlsstg tnaatgmgia lvsdtgvklp fskaralplk wnrsepegem
      241 yrfsgtakya ptsgtikpge adavmnfvie yn
//
LOCUS       WP_175818786            1068 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia sp. BCC0419].
ACCESSION   WP_175818786
VERSION     WP_175818786.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..1068
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=114561
     Region          1..1046
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 miariihwsv hhrflvllat vllaawgvhs lrqtpldalp dlsdtqvivk asypgkapqv
       61 vedqvtyplt ttllgvpgak tvrayssfgd afvyvlfddh tdpywarsrv leylsqvqsr
      121 lpagatvslg pdatgvgwvy eyalvdrtgr hdlgqlraln dwflkfelka vpdvsevasi
      181 ggmvrqyqvv ldpdklrayg itqaavaeal gkanqasggs vvelaeseym vrssgylrtl
      241 ddfrhvvlrt ddtgtpvllg dvariqvgpa mrrgiaelng qgevtggvvv mrsgknaltt
      301 idavkaklad lkrslpagie ivttydrsql iaravdnltd klieefvivg ivcavflfhl
      361 rsalvailsl plgvlaafiv mryqgvnanl mslggiaiai gamidaaivm ienahkhlea
      421 ydrahpgepi taarrwelva asavevgpal ffslliitls fvpvfslegq egklfaplaf
      481 tktytiaaaa glsvtlvpvl mgylvrgrip hehanpinrv lirlyrplle atlrrpwaai
      541 gvavvalvlt avplsrlgge fmppldegdl lymptalpgi sadkasellq qtdrliktvp
      601 evdtvfgksg radtatdpap lemfettirf kprsawrpgm tpeklvdeld rtvkvpglsn
      661 vwvppirnrl dmlstgiktp vgvkisgpdl agidaiatqv eaavkrvpgv tsalaerlng
      721 gryidvdidr laaaryglsv adiqavvssa iggedigevi agrerfpini rypreirdsl
      781 enlrqlpivt argaqirlgd vahvaiadgp pmirsenarl sgyvyvdlrg adlstavram
      841 qqavarqval ppgysiawsg qfeyleraaa tlrtvvpvtl vvifvllfvt fdsaadalll
      901 mstvpfalvg gfwlvwalgh avsvatsvgf ialagvaaef gvvmllylkg alqrrldagd
      961 pltdalllda iregavlrvr pkamtvavvl aglvpimigh gagsevmqri aapmvggmvt
     1021 apllsmfvip aawlllqrrr arsagrtrhs davpsgtnvp siptgesr
//
LOCUS       WP_175818857             191 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175818857
VERSION     WP_175818857.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..191
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20765
     Region          8..143
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtndassnsr erilaaatrl aqthgyggln yrdlanevgi kaasiyhhfe skadlgaava
       61 rrywedsaaa lddmlarsrd pldclrrypd tfrkaletgn rlclcsfmaa etndlpevvm
      121 kevlafadvn vawlskvlsa aavvssresk qraraifaai agaqliarsr gdlslydvli
      181 nnyrkagllp a
//
LOCUS       WP_175818501             263 aa            linear   BCT 11-JAN-2025
DEFINITION  biotin--[acetyl-CoA-carboxylase] ligase [Wolbachia endosymbiont of
            Dirofilaria (Dirofilaria) immitis].
ACCESSION   WP_175818501
VERSION     WP_175818501.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
  ORGANISM  Wolbachia endosymbiont of Dirofilaria (Dirofilaria) immitis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Chapman-Smith,A. and Cronan,J.E. Jr.
  TITLE     The enzymatic biotinylation of proteins: a post-translational
            modification of exceptional specificity
  JOURNAL   Trends Biochem Sci 24 (9), 359-363 (1999)
   PUBMED   10470036
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Wolbachia endosymbiont of Dirofilaria
                     (Dirofilaria) immitis"
                     /db_xref="taxon:1812115"
     Protein         1..263
                     /product="biotin--[acetyl-CoA-carboxylase] ligase"
                     /EC_number="6.3.4.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009374 - biotin binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_process="GO:0036211 - protein modification process
                     [Evidence IEA]"
                     /calculated_mol_wt=29476
     Region          10..259
                     /region_name="BirA2"
                     /note="Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme
                     transport and metabolism]; COG0340"
                     /db_xref="CDD:440109"
ORIGIN      
        1 mipetfegfh iyhykevyst ngkaldlidk gvldetiiva dkqtdgrgrt grswispegn
       61 fyvsliidfl ynytdaapiv nsniacwdnr enlskltelt fvtalavgdt llssigdgni
      121 qykwpndilv dgrkisgill ekksnsnwlv igigininya pfswttcvds yggslsnidl
      181 lkkiiihfnr lrkkwifdgf cairkmwlek afkmnkqisv klagklhkgi fididksgrl
      241 mlqkgdgsli yfdagelfvg stl
//
LOCUS       WP_175818889             586 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia sp. BCC0419].
ACCESSION   WP_175818889
VERSION     WP_175818889.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..586
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=63899
     Region          7..586
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mkmtrrlavl pittlitlaa qaqqapspsd qaaaaranae qnqqaqqrrd aqqrdatvqa
       61 pgmrsdvprp eaypvlptet pcfridrfel dvpdslpaas kaqgasalpm drfafardwl
      121 ahyagqcvgk qgvdlivkgl sqailargyi ttrvlvpeqd lssgtlklal ipgvirhvrf
      181 edeklrgtwk tafptrdgdv lnlrdieqgl eqmkrvssqd vsmriapgdm pgesdvvldv
      241 krgkpwtvva sidnsgtrat gklqgnvslg idnplglndi fnvgfnqdle fgdkrfgshg
      301 wnafysipwg ywtgtlsayt styfqplaav nqtfvasgnm ktvdfrlnrv larsrndvfg
      361 aqvrltrrfg dsyiegttip sshqnatfle fglndrhyfg ssqfdgslay rqglgwlgst
      421 dsmfaaeggq tyrfkmvvld anlstpfvig tqpfkyvttf hgqytgntvs yldsvtigsr
      481 ytvrgfdget llagsrgfyw rnelqvpiaq tglsayagld ygrvwgpepv alvgtqlaga
      541 vigvkgsvat rfggygydlf agtpvykpsa fptarvtvgf qvtaqf
//
LOCUS       WP_175818909             354 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175818909
VERSION     WP_175818909.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 354)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..354
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38573
     Region          12..335
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 msttashnvq siwytrcpvp tplgiaahlg wldhefagdg itvralqesq haalhhahvd
       61 hsldnafrqg gsipalwara sgadtrvval twvdeaqaiv alpeaglarp kdlrgrrigl
      121 prrdgeridi fraaalrgfv salsldglgp gdvewvdvpa snlrapvstp atrdaafshp
      181 aslssrrlya aeaaalvrgd vdaiyvkgsl gletahliga qpvvdigfhp dpqirinngs
      241 prpltvnast lerhpdivsr flarvtdveg wareheqevl gylgretgsg hdwlrlaygt
      301 dvhrrlrtdl deasiaaldd fkrflvdwrf lpadfdvraw idrraldgia tlsr
//
LOCUS       WP_175818947             341 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175818947
VERSION     WP_175818947.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..341
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36508
     Region          9..324
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mttsprrral iaaglgvlgv lgapalvrak prtvriskgy gvlylpllvm ekqrlferha
       61 arhgvrdvav ewvlldggns vndammagtl dfagagapgf ielwarargi pnvevigisg
      121 lsttslslna nrpglvslrd ftpsdriavp girtslsavv lqmvasrqlg arhfaqldsi
      181 tvnlphpqam qalirrengv tahftsppfs tlelrqpgih rvvssvdvlg pmtldvvfap
      241 krlvdaepal aaaflgalde anrliaqdpr aaaalyaass gvavshddvm rmlaapdtrf
      301 svlpnqlmdy veflylagti kakprawhem fapmlddyrs g
//
LOCUS       WP_175818967             343 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175818967
VERSION     WP_175818967.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..343
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=37739
     Region          33..92
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          123..323
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(138..139,141..142,145,149,151..157,249..254,
                     260..261,263..264)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 mthsapsrpa grsdpaphda dasdglrvqd ldlnllktfr avyeerhvgr aalrlgvtqp
       61 svsyalgrlr lmfrdalfvr tgtgveptpr aqrlaisvdk alailqdvld egsrftpdst
      121 qrvfrlhmsd faasaflptl laafdrrapg avietlhvde cqlnvalesg ridfalghfa
      181 dasshfqrta llhercvllm prrtaqrvgl pddfvldgaa pdalrfvavs shpqsmqlle
      241 rhelmprvra alpdfmvvpa llqdgdyali lpetiaitfa arqpcvlyei agagewavna
      301 ywhrrfdadp ghrwlrapll elfhigaqap fdawlapqpp aca
//
LOCUS       WP_175819000             743 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia sp. BCC0419].
ACCESSION   WP_175819000
VERSION     WP_175819000.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..743
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79664
     Region          30..743
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mtvnrttaap arrrrakvgl gvglgvtlfa vqaaaaqgda stsgaeaagt atlpaitvsg
       61 erghplware asvaglddap lrdtpasvnv itraliddql akrlsdvvrn dasvvndyap
      121 vgyfegfair gfpvdlasai ridgltvsge qnvplenker veilkglagi dsgvvapggv
      181 infvtkrsan vasvtggvds rgstsaavdl grrfgpdhqf gfrinaaken mhsyidgtng
      241 rrtfgsiaad wdispraslq lnaefqqwiq rsapgyqllg gtvvpsvktt skalgtqpwa
      301 kpvttdalnl narfdyqfnd dwkayiaagr srtmiddnsa faygcsyaas caagatspff
      361 fgangdydvy dfrspgeyrr nddlravttg kfatgplrhe ltlgvsvqrr vvhmadavyd
      421 yvgseniygp dltfspspns pgpsyprlda wqygvfgldr islgehwqvl aggkevllrq
      481 rswssldgdt thtdrsvflp qvalvykpvn vlslyasysk alslgdqapv ratnayaflp
      541 pveshqfevg akydwldrls ltaavfsisk pfqfadpdas gtsytfvqrg tqrhqgielg
      601 aagrvterlg ltasvaaira ravdsgspay eghqiinvpa lraslyadya vpgvaglnvl
      661 ggveysaarn aneegtarvp swfvfnlgar yttkigghrt vlrvsvdnlf nkfywrdage
      721 qqgdaylfpg aprtarvslt ydf
//
LOCUS       WP_175818968             322 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175818968
VERSION     WP_175818968.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 322)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 322)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12168323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..322
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34351
     Region          22..198
                     /region_name="AraC_binding_2"
                     /note="AraC-binding-like domain; pfam14525"
                     /db_xref="CDD:434015"
     Region          249..320
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mnialsrhap nrlgtlqapd everavahrl gphrmaasgr dpfhaelyev plhhgallel
       61 cygretridf gddadhflfr ltlagacelq agsvvaragp galtvsspal asrlrtspdc
      121 rnlvlrlerg alerklqdml httlarplqf dlaaggagaa lvlptfeylc rlgaqpgiga
      181 aspvfgadlt awlmslllth lphaysdall rgtpplpahv rracahvdah lgeplalaal
      241 aavagvaprt lqhafraflh ttpaayvrer rlaavhaalq rgdarsvtdv liahgihgfg
      301 hfakayarry ghapsvtarq ar
//
LOCUS       WP_175818980             317 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175818980
VERSION     WP_175818980.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..317
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34081
     Region          2..315
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhrigffvcr gydaldlggp lsafnqvata aghtpydlhv ispsggpilg ntglsidtkp
       61 igrrafdtvv fvggdiapmq tseniaaask laakasrvas vctgafllae tgsldglraa
      121 thwryaaqlq srfpltrvdg dsiyvvdghv wtsagiasgi dlalgmierd mspeiarevs
      181 rllvvpyrrp ggqsqfsams qmepesdrir ialnfarehl aealpverla daaslslrqf
      241 grafrretge tparaverlr veaarlrlqg gsepieqial avgftdperm rrafikllgh
      301 ppqairresr snaaaar
//
LOCUS       WP_175819016             223 aa            linear   BCT 11-JAN-2025
DEFINITION  O-methyltransferase [Burkholderia sp. BCC0419].
ACCESSION   WP_175819016
VERSION     WP_175819016.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..223
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23010
     Region          43..220
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mdqdrwnqvd ayfsatlvps daaldaalaa sdaaglpain vapnqgkllq llatirgarr
       61 ilevgtlggy stiwlaralp pggslvtlel npehakvatq niaragfaav vtvvvgsakd
      121 slarlvdage apfdfifida dkdnnpvyld aalklsrpgt vivvdnvvrg grvadpdnre
      181 pdvvgvrdgf arlaaapalm ttavqtvgqk gwdgfsisiv gaa
//
LOCUS       WP_175819042             206 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175819042
VERSION     WP_175819042.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22847
     Region          12..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtistddpgr rarkriqmla hlaatgarlf dahgydavtm eqiaaeadva krtlynhfpt
       61 keavlahwle gelardlahl qqdvarrktf asrigcvlda saawcehhpa yllaylrhrf
      121 lsigaaeper agengsdial vwrqliaagq qagelnrtlr adqlatwfhh lylaamlrwl
      181 tvpglslkre fqsvaklfie gaeakg
//
LOCUS       WP_175819066             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175819066
VERSION     WP_175819066.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33681
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdyidklrif rsvvemrsft raadmhglar pvvsravadl earfgsrllh rttrqvslte
       61 taeriyerca avldeldale veaqthtrep egllrlvaht taalnrlvpl iagfkaahpn
      121 vrldvtlter pvdlvgegyd igivvpymlt sestvvrlve ripvvivatp aylqaharpe
      181 tpadlahhpf vpispslrrp alsfrvdgnm ltvpfrfdis snspvfnrem vmhdfgigvv
      241 prtlveaqla sgalvqlleg adlvdafvei klayanrall pakvkafidy taaycdregw
      301 ivpaaa
//
LOCUS       WP_175819089             558 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175819089
VERSION     WP_175819089.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..558
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=60543
     Region          22..556
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 matvtpratn eslhptigaa rltlgnrill sfgvlfvlml vtagvsyerl rainaeavsi
       61 erdslpgvyl asslrgavne sfmllqqatf vetgpetvqr nlakiadalk dveslsvdyq
      121 nttfrdddrq rfmafrgayd hyvpllndaa qksrashdea vaayakvlpa wtevvrnanv
      181 lvqenrkfae qsakliresv qdtevvlata ltfmllsalg lgymlyrsvt vpmarlvevh
      241 dvmrtgnltr rldlrrrdef gtletgfnrm adeltelvsr aqqsslqvtt svaeiaatsr
      301 eqqataneta attteigats reifatsrdl lrtmnevagv aeqsatlagv sqsgltrmge
      361 tmrsvmdaag svnaklailn ekalninqvv atitkvadqt nllslnaaie aekageygrg
      421 favvateirr ladqtavaty dieqtvkeiq savsagvmgm dkfseevrrg mldvqqvggq
      481 lsqiiaevqt laprfqmvne gmqtqangae qitqalsqls eaaqqtaesl rqssqaiddl
      541 tlvanqlrts vsrfkvda
//
LOCUS       WP_175819090             170 aa            linear   BCT 11-JAN-2025
DEFINITION  chemotaxis protein CheW [Burkholderia sp. BCC0419].
ACCESSION   WP_175819090
VERSION     WP_175819090.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..170
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=18166
     Region          14..152
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mtradpqhga halflmfeld geryaldaag ieevlplavm kavpgapdwi agllmrggqp
       61 vpvidvpmla lgrraqalrs trlvmvryra ghadgertig liveratqtm ridraafrts
      121 gvstartrwl grvantpdgv vqqvsvsdli ddvarlylvd glsghggesa
//
LOCUS       WP_175819123             128 aa            linear   BCT 11-JAN-2025
DEFINITION  GtrA family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175819123
VERSION     WP_175819123.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..128
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=13604
     Region          11..128
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mirtchaaer arlirfgvsg lgstalhali aaamfalfda tpvianataf vcstafsyla
       61 ntlwsfsspm twgnfvrfla vataglavtm llahgtdalg larawsvvav mlcvppvtfv
      121 lhrlwtyr
//
LOCUS       WP_175819147             444 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [unclassified
            Burkholderia].
ACCESSION   WP_175819147
VERSION     WP_175819147.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..444
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=48023
     Region          14..426
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mhriiivggg agglelatrl gdrygargnr paralvtlvd rnpthiwkpl lhevaagsmd
       61 pftqeleyaa qarwhgfefq qgeltgldra akrvtlspln dsdgaellpa releydtlvi
      121 aigstthffg vqgapenaia ldtvgeaerf rkrliaacmr aehqapapta pgesaepriq
      181 vvivgggatg velsaelrnt aqvlsvyglh kldprhdvgi vliesgpril palqervsta
      241 taelleklgv rlmlservte vapgfvhtas gkavradltv waagikapsv lshldglqvn
      301 klgqldvrrt lqtftddnvf algdcaacaw pgnernvppr aqaahqqasf llkaigcrle
      361 grplpeftyr dfgslvslgh fsavgnlmgg liggnmlieg lfarfmymsl yrlhiaalhg
      421 yprmildtva hwlrrttlpr vklh
//
LOCUS       WP_175819200             472 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0419].
ACCESSION   WP_175819200
VERSION     WP_175819200.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..472
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48117
     Region          23..450
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,277,280..281,284..286,289,317,321,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msefaspaga hepavnwram savllavala tldtaianta lpaiaadlha spaasvwiin
       61 ayqlamvatl lpfaslgdiv ghkrvyvagl avftlaslgc slastlpmlt aarivqgfga
      121 saimsvnval irglfpahrl grgvgfnalv vgvsfavgpt iaslilsvaa wpwlfavnvp
      181 lgvfalavai pslpqtargk hafdpvaalf nvitfaslif algefaqrgp lsvvfaaaav
      241 afafgwllir rqaghpapml pvdlfrrpvf tlsaltavca faaqglafvs lpfyfetvlh
      301 rsavetgflm tpwsavvafa apiagrlsdr yppgllgaig lallsagmvs laalpvspgv
      361 idigwrmmlc gagfgffqsp nlkalmssap persggasgi iatarligqa tgaalvalsf
      421 giagrhgptl almlgagfag aasvasglrl fapshragmp vvperakepa te
//
LOCUS       WP_175819236             157 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175819236
VERSION     WP_175819236.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..157
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17062
     Region          3..153
                     /region_name="COG3865"
                     /note="Glyoxalase superfamily enzyme, possible
                     3-demethylubiquinone-9 3-methyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:443074"
ORIGIN      
        1 mtiqkitpfl wysteaeeaa afyagifpds rivrvtavpg tdstrmvefe lfgqpflams
       61 hprteafnha isllvscadq aeldrywsal ldnggtadgc gwlrdrygvs wqivpealip
      121 mmadrdavka trvaaammqm tkfddaalka afagtag
//
LOCUS       WP_175819261             487 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0419].
ACCESSION   WP_175819261
VERSION     WP_175819261.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..487
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52317
     Region          27..453
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mqtiavklhg iedvisfldt rpgiagragl vwwlslgglf ldafsnsals aglgpmtrel
       61 hlsaaqvawm tsfaswvaia fnpiggwmad rwgrvrplia akllsvigal lvvfapdfnt
      121 ilagrffvgm aygidfaiam amlaeftpgr lksrlntwqg mwytavclnl llallfhawq
      181 vgdsiwrysv aatavfgvai lalqcaflve spiwltrker lddaaramtr iygqpfvaap
      241 ahertpvvnp atrglanvll ifrgvylprt ilaatvqigq sieyfaigwy lplisaalfg
      301 kdfvyatlga lvfnlfgivg gfsssavgrr vglrrasafg faavcamlva lglfqarmpl
      361 wlsvvvpslf ilfhsagpga ngkslsslsf rgelragang ivgalgsiga algllvfplf
      421 raryglehtf lilaivpcva saicfairwd ptrtpvnpdn epdaphfgdd arvpsaflkp
      481 aiektqr
//
LOCUS       WP_175819264             520 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FAD-binding oxidoreductase [unclassified
            Burkholderia].
ACCESSION   WP_175819264
VERSION     WP_175819264.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..520
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=54842
     Region          54..508
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 miskeaikrg ynrgnyvvga htpppyalnl paaggapvea gmqrapvavs pqqvdalrav
       61 adevlvqpad vvawtrdwwa asmvaetggr patphavvvr vstveqvqav mriahaatlp
      121 vtasagrsnv tgaalpvrgg ivldvcglnr ligvdaesqi vdveagmfgd vfeatlqreh
      181 gltmghwpss fgistvggwi acrgagqlst rygkiedmvf gmdvvladgs lvtlggysra
      241 avgpdlqqlf igsegtlgii vrarlklhrl pdygraiayg fdtfaaglda creilqrgan
      301 paalrlydal esgvqfglpd tnvlliadeg apemvdavma igarvgdasg rrldgdaife
      361 kwldtryltg ksaegfkrsp gfvadtlemc grwrdlaaiy rdvvaalqav pgtlagsahq
      421 shayadgacl yfslrgdvav aeraawyraa wdaanavliq ynaalshhhg vgllrapylr
      481 dslgtafpvl qavkraldpt hilnpgklgl gdetgphvdr
//
LOCUS       WP_175819286             325 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175819286
VERSION     WP_175819286.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..325
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=35247
     Region          130..320
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mraadlfalg afvvilaagl alsawldrar htpeqrvrar mrhlasslag reagataapg
       61 valfnlprrq grararlqhy vtrvravgge rgmrivvaat iagalaaivv velvalpriv
      121 hpliyvglpl vamrasyral verfrlrfle afpdaidliv ravragipvt qaistvgdsa
      181 aepvrstfrt mgdslrvgad lkdvlthaad rlmiadfsff tvylllqret ggslgetlde
      241 lssiirtrrd irlktralta egrittkiis avpfvmigal flvnrayvml lfdthagrvm
      301 ltiaavllti glltirkisk ldtar
//
LOCUS       WP_175819336             255 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175819336
VERSION     WP_175819336.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..255
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26290
     Region          6..248
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mtadklaili avigagsyfq tvtgfglgmi vmgatsgfgl aplatvatlm svvslangat
       61 alpgrlhhid wravgaatlg ilpsvvagvv lleclsrsaa dllqlilgav vlygglsaal
      121 rptpltarsd nrsffvsglf ggllsgmfgv sgpplifqfy rqpltlvqir calivlfttt
      181 satrvlysac egqldrdiwl laalatpvvm lttvagrhyp pplspvalrr lafgvlmaig
      241 vgliatslpp llhrg
//
LOCUS       WP_175819347             324 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175819347
VERSION     WP_175819347.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..324
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35558
     Region          13..72
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          101..301
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(111,115,154,168,170,232,249,280)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(112..113,117..118,120..121,124,128,130..136,197,
                     226..230,237..238,241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mkkgaretgi dhlgamrafv rvvetgsfsa vakemhvsts tvarkvtaie ealgvallhr
       61 sthsvtltea ghiyleravt liadlddtlr vvaelnaqps gplkltapva fgrrhlaplv
      121 apflarypti qldvrltdnh ndlvaggfdl dihegenyld nlvvhrlsrn dsilcatpgy
      181 ldrcgrpatp ddlthhnclr yvhpegdprw alvngdtqhs vlpagnlvtd hsellleatc
      241 aglgiaefei wlvrdllasg qleavlpryr lqnrltgefi yiaylanrrs saklrvlkdf
      301 laehlaqige lsdrelakir dara
//
LOCUS       WP_175819401             226 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CDP-alcohol phosphatidyltransferase family protein
            [unclassified Burkholderia].
ACCESSION   WP_175819401
VERSION     WP_175819401.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Sciara,G., Clarke,O.B., Tomasek,D., Kloss,B., Tabuso,S.,
            Byfield,R., Cohn,R., Banerjee,S., Rajashankar,K.R., Slavkovic,V.,
            Graziano,J.H., Shapiro,L. and Mancia,F.
  TITLE     Structural basis for catalysis in a CDP-alcohol phosphotransferase
  JOURNAL   Nat Commun 5, 4068 (2014)
   PUBMED   24923293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Koga,Y.
  TITLE     From promiscuity to the lipid divide: on the evolution of distinct
            membranes in Archaea and Bacteria
  JOURNAL   J Mol Evol 78 (3-4), 234-242 (2014)
   PUBMED   24573438
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Koga,Y.
  TITLE     Early evolution of membrane lipids: how did the lipid divide occur?
  JOURNAL   J Mol Evol 72 (3), 274-282 (2011)
   PUBMED   21259003
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..226
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23934
     Region          37..213
                     /region_name="PgsA"
                     /note="Phosphatidylglycerophosphate synthase [Lipid
                     transport and metabolism]; COG0558"
                     /db_xref="CDD:440324"
ORIGIN      
        1 mdqrktatrp epppprtwda rlarslvrpl vdtpvtpnhl ttlrlligla gawclahggf
       61 gwsnagafli vlsnfvdhtd gelarisgks skighfydla adalvtvalf vsmgvgivaq
      121 ggqmaaspvl lgavagaava lifflrmrie siagkagtkq afaggfeted vlyllpivtl
      181 vdgvqpflla asigaplfaa wvvidwwriv rrsnvpqnpt eiqask
//
LOCUS       WP_175819410             289 aa            linear   BCT 11-JAN-2025
DEFINITION  SH3 domain-containing protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175819410
VERSION     WP_175819410.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..289
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29044
     Region          7..96
                     /region_name="YraI"
                     /note="Uncharacterized conserved protein YraI [Function
                     unknown]; COG4991"
                     /db_xref="CDD:444015"
ORIGIN      
        1 mkntivrslc vvlaglaaap gvadaqssay tnspaelyag papdypvvaq lppgtaldvf
       61 gclsnyawcd valpgvrgwi daqlldypyq gsyvplleyg aiigvpvtgf aigaywdryy
      121 rhrpwypdrd rwahrpeprl gpggmppghg rpqpgapmqv apggpppvhd trpsatrggw
      181 nganrvpppa apaptpmpgg agnarpaspp paapaptpmp ggagnarpas pppavlrppp
      241 apggeghpmp ppgrqggggg ggyarpqggg ngggnhgggg gggpdelrh
//
LOCUS       WP_175819435             314 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175819435
VERSION     WP_175819435.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..314
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33201
     Region          16..294
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mtplvqpdvs hdepaiaeri asamplmtpi hrrmgefvla npfraatmri delaqavnas
       61 iatanrfaka lgfdgypamr aalvrgfeat lgpverlrsa qeqesgvrga vwidavfdqa
      121 aanientrah ldaadveaav eaivgarrvl ilgagssafl aglmehglsv chdsvqslal
      181 lggpshaarr lytadsrdlv ialafpryvk dtvelarraa argagvlgis dgpqsplapi
      241 aslnlyvkae rrfaatseaa vltmiealid avalrthrsa ksaaemtefl lpwlvqpqaa
      301 lsaanpsfpr pkks
//
LOCUS       WP_175819516             695 aa            linear   BCT 11-JAN-2025
DEFINITION  M3 family metallopeptidase [Burkholderia sp. BCC0419].
ACCESSION   WP_175819516
VERSION     WP_175819516.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..695
                     /product="M3 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=76909
     Region          4..693
                     /region_name="Dcp"
                     /note="Zn-dependent oligopeptidase, M3 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0339"
                     /db_xref="CDD:440108"
ORIGIN      
        1 msasantnpl ldfsglprfg eirpehvtpa ldtlldtasr avetasaset pstwaavvet
       61 veqateplgr awgivghlna vadtpelraa ygenlprvte fwssvgqnla lyekykaiaa
      121 saeyatlsae rkkildnalr dfrlsgaelp edqkprfael qeqqaalska fsdhvldatn
      181 ayayfarnea elaglpgdai eaareaaqkd gkegwkftlh fpsyfpvlqy adnralretl
      241 yrayatrase lgpqygdgka ewdntaivad alklrreeaq mlgyrnfaev slapkmaesp
      301 qqviafledl atrarphadk dwdelrtfaa kelglaelap wdvayaaekl rqqryafsen
      361 evkqyfpepa alkglftvte tlfgvrikpd dapvwhkdvr ffrvenrdgs lvaqfyldly
      421 aregkrggaw mddarsrakr gsdvqtpvay ltcnfsapvg gkpacfthde vitlfhefgh
      481 glhhmltrvd elgvsgingv ewdavelpsq fmenfcwewd vlssmsshvd tgaalprelf
      541 dkmiaaknfq sglgtlrqiv fsmfdmllhv dfdpagatgv tafareiner yhvipqaafs
      601 rwpntfshif aggyaagyys ykwaevlsad ayaafeeaaa asgsvldaat gtryrreile
      661 vggsrpames fkafrgrepq idallrhngm aapah
//
LOCUS       WP_175819570             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175819570
VERSION     WP_175819570.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32631
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrfkqietf aavaakgsls aaahaegvap aiigrrldal eerlgvkllv rttrkltltf
       61 egsafledcq riindmqnae asvsaggvka sghlrisapa gfgrrhvapl vpefsgahpd
      121 vsvtldlsdr mvdlvnegfd cavrlgelpd sslvslklge nrrvcvaspa ylarrgtpat
      181 laelarhncl alaananqqr gwafleddkv vsirvngtme csdgavlhew clagyglawr
      241 swwevgedia agrlvsvlda faappigiha vfpqrrhlpl rvrlfldylk htyerpgywg
      301 e
//
LOCUS       WP_175819523             470 aa            linear   BCT 11-JAN-2025
DEFINITION  lactate utilization protein B [Burkholderia sp. BCC0419].
ACCESSION   WP_175819523
VERSION     WP_175819523.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..470
                     /product="lactate utilization protein B"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=51896
     Region          2..462
                     /region_name="LutB"
                     /note="L-lactate utilization protein LutB, contains a
                     ferredoxin-type domain [Energy production and conversion];
                     COG1139"
                     /db_xref="CDD:440754"
ORIGIN      
        1 mqvqsmhfka ragqkladqr lqqnlkklst kfvsaradam taidfpatra alkarrnral
       61 enldvwleaf eraatrrgtt vlfaetteda arlvadiarr hdvkkviktk smvseemrln
      121 avlaemgvqs ietdlgeyil qindneppsh iiapvvhkdk deiadlfart hqrerlteip
      181 dmtrearevl rphfmsadmg vtggnfviae tgsvaivtne gnegmctvmp rvhvavtgie
      241 kvlptledla tamrllprsa tgqktsnyfs lltgprgpgd edgpehnyvv lvdggrtgli
      301 ggefqemlrc ircgacmnhc pvyqkvggha ygwvypgpmg svltpsyvgl draldlpqaa
      361 tlcgecdsvc pvgiplshll rtlrekqver hlrpwreraa laawgffarr pmlyalttkl
      421 avrilerlgg nggtlrrlpm mggwmdtrdm ptptgrtfre lyaasqshlg
//
LOCUS       WP_175819615             294 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia sp. BCC0419].
ACCESSION   WP_175819615
VERSION     WP_175819615.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..294
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30310
     Region          3..286
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mqtavgfvgl gvmgtpmaln laragtplvv wsrshgsdda lrdagarvae diddvfvpcr
       61 tvilmlanda aidaalargs pafaarvggh tivnmgtnap dysraladdi aaasgryvea
      121 pvsgsrkpae acqlvvmlag apddvdavra lvkplcrdsf vcgdvpsalt mklavnlfli
      181 tmvtglaeat hfaqrhgidl arfadvlnag pmasdvsrvk lgklvaadfs vqaaitdvlk
      241 narlvaesar gigiasplld ichalyaete qaghgaadmv aviraieqrt gdar
//
LOCUS       WP_175819607             191 aa            linear   BCT 11-JAN-2025
DEFINITION  DinB family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175819607
VERSION     WP_175819607.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Cooper,D.R., Grelewska,K., Kim,C.Y., Joachimiak,A. and
            Derewenda,Z.S.
  TITLE     The structure of DinB from Geobacillus stearothermophilus: a
            representative of a unique four-helix-bundle superfamily
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 3), 219-224
            (2010)
   PUBMED   20208147
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..191
                     /product="DinB family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21550
     Region          31..176
                     /region_name="DinB"
                     /note="Bacillithiol/mycothiol S-transferase BstA/DinB,
                     DinB/YfiT family (unrelated to E. coli DinB) [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2318"
                     /db_xref="CDD:441892"
ORIGIN      
        1 msalpqnpma psgttarttl pavasdtlkm lvrykcwang ltfksvmdlp agealrqrpt
       61 rfgnmvhtln hayvvddifr hhlqgkkhty tsrntdhtpa vsdlwkavqe mdrwyidlvd
      121 twsdedlaqa vhfefvggge gvmtreqivl hvvnhatyhr gfvgdmmyqv pfappsndlp
      181 vfirdhyrga r
//
LOCUS       WP_175819661             164 aa            linear   BCT 11-JAN-2025
DEFINITION  arsenate reductase ArsC [Burkholderia sp. BCC0419].
ACCESSION   WP_175819661
VERSION     WP_175819661.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Messens,J. and Silver,S.
  TITLE     Arsenate reduction: thiol cascade chemistry with convergent
            evolution
  JOURNAL   J Mol Biol 362 (1), 1-17 (2006)
   PUBMED   16905151
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Mukhopadhyay,R. and Rosen,B.P.
  TITLE     Arsenate reductases in prokaryotes and eukaryotes
  JOURNAL   Environ Health Perspect 110 Suppl 5 (Suppl 5), 745-748 (2002)
   PUBMED   12426124
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Messens,J., Martins,J.C., Van Belle,K., Brosens,E., Desmyter,A., De
            Gieter,M., Wieruszeski,J.M., Willem,R., Wyns,L. and Zegers,I.
  TITLE     All intermediates of the arsenate reductase mechanism, including an
            intramolecular dynamic disulfide cascade
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8506-8511 (2002)
   PUBMED   12072565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..164
                     /product="arsenate reductase ArsC"
                     /EC_number="1.20.4.4"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030612 - arsenate reductase
                     (thioredoxin) activity [Evidence IEA]"
                     /GO_process="GO:0046685 - response to arsenic-containing
                     substance [Evidence IEA]"
                     /calculated_mol_wt=17527
     Region          4..143
                     /region_name="LMWP_ArsC"
                     /note="Arsenate reductase of the LMWP family; cd16345"
                     /db_xref="CDD:319973"
     Site            order(9,11..16,112,114)
                     /site_type="active"
                     /db_xref="CDD:319973"
ORIGIN      
        1 mttnvlilct hnaarsvlae gmlnlwaatl gkdvraysag sapsgrlnpf alealtnaga
       61 dvdgyrsksw defvgdgape mrvvitvcdr aaaetcpywp gspvkvhwgy adpsnavggd
      121 egkrlafdlt rqaigyrmlq llalplerms naelqdaltd isrn
//
LOCUS       WP_175819671             391 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Burkholderia sp. BCC0419].
ACCESSION   WP_175819671
VERSION     WP_175819671.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 391)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..391
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41780
     Region          4..386
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 mtalktlaia nyrslreliv plaalnvvtg pngsgkssvy ralrlladta qgrvipslar
       61 egglpstlwa gperfsraml ageepvtgtv rkgpvslklg facddfgysi dlglplpsrs
      121 qfaldpvvkr eciwggallr pstllvdrqg aqirartasg dwqtipqpva sfdsmmtefa
      181 dptgapemia vrerirswrf ydhfrtdaqa sarqshigth tpvladdgad laaalqtire
      241 igdaaaldaa iddafpgasv eidnpggrgr fdvlmrqpgl lrplaaaels dgtlryllla
      301 aalltprppa lmvlnepets lhpdllpalg rliaqaarrs qvlvvshaar liatlereag
      361 ceslvldkql gatalvdads rdlpawkwps r
//
LOCUS       WP_175819696             327 aa            linear   BCT 11-JAN-2025
DEFINITION  thiamine pyrophosphate-dependent dehydrogenase E1 component subunit
            alpha [Burkholderia sp. BCC0419].
ACCESSION   WP_175819696
VERSION     WP_175819696.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..327
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=34600
     Region          6..327
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 mtastqlsrd tlldayrlmr tirefeerlh vefatgeipg fvhlyageea savgtmlhlg
       61 lddyvatthr ghghciakgv dvhgmmaeiy gkktgvchgk ggsmhiadls mgmlgangiv
      121 gaggplvcga alaakhkktg gvgvcffgdg asnqgvifes mnlasvwrlp aifvaenngy
      181 aeatssswsv atdniadran gfgmpgvivd gfdffavhea lgeaverarn gggptlvevk
      241 ltryfghfeg daqtyrapge vqklrdekdc lkhfetrvvr aealttddlr avdaqvkali
      301 ddavaqakaa plpdaadlla dvyvsyp
//
LOCUS       WP_175819684             558 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 39 protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175819684
VERSION     WP_175819684.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14304616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..558
                     /product="glycosyltransferase family 39 protein"
                     /calculated_mol_wt=62448
     Region          24..375
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
     Region          450..555
                     /region_name="Arnt_C"
                     /note="Aminoarabinose transferase C-terminal domain;
                     pfam18583"
                     /db_xref="CDD:465810"
ORIGIN      
        1 mndtpsrlpl nritlvlllv alaivwfapl glrhlipsde gryaemarem fvtgdwitpr
       61 yngykyfekp plqtwlnalt fawfgigewq arlytavasf agvllvgytg arlfnplsgf
      121 laavvlassp ywnlmghfna ldmglafwma lslcslllaq rpglrpaavr gwmwacwaam
      181 afavlskglv glilpgavlv lytliardwa lwkrlylvsg lviffaivtp wfvlvqqrnp
      241 effnfffvvq qfrryltpeq nrpgplyyfv pvllvgflpw lsvawqsirh alrmprqpng
      301 fapmlvlliw safiflffsa shsklisyvl pvapalalii gaylplmtad rfrrhllgyl
      361 vffvaaafgi iflayqgdar tpnalyrafq mwlyaglava aaltltaawl nrragvaaal
      421 aafgaawlaf gtiggsghde fgryssgall apavraelak lppdtpfysv emldhtfpfy
      481 mghttimvqr qdelafgisv epnkwiptvg ewitrwnqdt halaimgpgq ydtlvkegvp
      541 mrviardnrr vivekpqs
//
LOCUS       WP_175819732             308 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Burkholderia sp. BCC0419].
ACCESSION   WP_175819732
VERSION     WP_175819732.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..308
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32135
     Region          7..272
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(34..35,38,90,103,105,134,167,253,256)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 maaafpeila lgeamiefnq sqpgrpeflq gfggdtsnfc iaaarqgast gfvsaigddp
       61 fgrlladmwa aeqvdttyvr idrtaptgvy fvthgadghq fdylragsaa sryatgdlpl
      121 dalaaakavh lsgislaist aacdaafaai dharrngakv sfdtnlrlkl wplpraravm
      181 realrqtdic lpswddvtal tgandrdaiv damlehgpqv valklgkdga yvatpherrv
      241 vpgfaveavd atgagdcfgg afvarivagd dpfaaaryan aaaalsttgy gavapiphrd
      301 averlmqg
//
LOCUS       WP_175819746             332 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175819746
VERSION     WP_175819746.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..332
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=36736
     Region          9..287
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mdalavtfde irdaygldrg gpptqvserv whlptdsgag vavklyaleh haravketai
       61 lahlekhgdt rfhvqtlkrt tsgaslwsgq hshamltrwe agqfktydtf spaewdalga
      121 slaalhlsfe plhlpsldti rarltsidad avrrslldal dradanatda anlrryvela
      181 lrmldryypg sidafpaedp qhpihndynq fnylftgtlp pliidweasi gapreyelvr
      241 clnhlpleap hlaeafvray grvrpvnpah iawavdaacl qhalklwivq gwlddpsrfa
      301 shlngavtma samvdarghl vdffsrcvea gn
//
LOCUS       WP_175819761             268 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175819761
VERSION     WP_175819761.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..268
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26777
     Region          1..264
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mlislvlggf vgavlgltga gggilavpal vvgmswpmqq atpvalvava gsaalgaleg
       61 frrglvryra allmavagvp lttlgvrlah vlpqrllltl faltmlvvag rllrqalrqa
      121 avdadasplc vgrinpdtgr lvwswpvgva lastgavtgl mtgllgvggg fvivpmlrkf
      181 tnvsmhgvva tslmvialvg tggvlatlvs gtrapldvtl wftvatalgm aagrgasrhl
      241 aarhvqagfa avlvcvalgl lakaafga
//
LOCUS       WP_175819767             342 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175819767
VERSION     WP_175819767.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10859374
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..342
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38656
     Region          3..98
                     /region_name="HTH_NolA-AlbR"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators NolA and AlbR; cd04788"
                     /db_xref="CDD:133415"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133415"
     Site            order(51,54,58..59,68,80,84,90,94,97..98)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133415"
     Region          <251..>305
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 mrlkvgelak rsgltvrtlh hyhaiglltp saradngyrl ydrddiarph qiqalrrfgl
       61 slaeigdyln qpgtplvdlv akqiasldrq laqtaqlrer larlhaqlaa gtepeladwl
      121 ttlelmtvyd kyfseaelar lpmyqksqag daewialvde vrvlhdagvp aedervrala
      181 arwmallvrd tnndprllak lnlmheheps mqskigista lrdyvlrass etkmrlfeky
      241 lapdeirfmr ahyreramew pqlmadvrda idagtqpdsp qgralaqrwl elfcsyaghd
      301 pathakfrqa lmnepaltkd swtddtllgf vraamaqlap vr
//
LOCUS       WP_175819793             350 aa            linear   BCT 11-JAN-2025
DEFINITION  microcin C ABC transporter permease YejB [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175819793
VERSION     WP_175819793.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 350)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..350
                     /product="microcin C ABC transporter permease YejB"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042884 - microcin transport [Evidence
                     IEA]"
                     /calculated_mol_wt=38214
     Region          1..349
                     /region_name="YejB"
                     /note="ABC-type microcin C transport system, permease
                     component YejB [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4174"
                     /db_xref="CDD:443333"
ORIGIN      
        1 mlayilrrll lmiptligvv titfavtqfv pggpveqvla qlrhgstrgg eaggggggyh
       61 gsqgvdpqqi eqirkqfgfd kppleryalm lksyatfdlg qsyfahrsvw avirsklpvs
      121 itlglwtvil tylvsvplgi skavrngsrf dtvtsvlvlt gyavpgfvlg vlllmlfggg
      181 tfwqvfpmrg ltsdnfddlt ligktldylw hialpvtasv ignfaivtil tkntfleeig
      241 rqyvltarak gaperdvlwk hvlrnaaipl ltglpaafvg aflngnllie tlfsldgmgq
      301 lsydsvirrd ypvvlgslfl ftliglltkl iadicyvlvd priqfsrldh
//
LOCUS       WP_175819795             544 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175819795
VERSION     WP_175819795.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 544)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..544
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59055
     Region          1..534
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 manallqidg fsarfgakaa vqdlslsvgr gervalvges gsgksvtals ilrlaqqatl
       61 sgrmlfdged llakterqmr girgadiamv fqepmtalnp lytigkqiae slrlheglrp
      121 gdarergial lrrtgipepe rridsfphql sggqrqrami amalacrprl lladepttal
      181 dvtvrqqivd llielqeqea aargmavlli thdlnlvrrf aqrvavmeqg vlvetnttda
      241 lfaapqhayt rrlldsapqr dvepvaagaq tildvqdlav dyriaakgwr avlgkttfra
      301 vhdvklnlrr getlgivges gsgkstlaat vlglqrpaag sieidgmpld alrktggrra
      361 lygrmqvvfq dpfgslsprm tveqivgegl avhrpqvagv arrariaall qevglpaesm
      421 lryphefsgg qrqriaiara lavepellvl deptsaldvs iqkqvlnllt nlqkkyklsy
      481 lfithdlavm ramahrvvvm kagrvveegd tldvldapsh pytrallass mlapvhgkqe
      541 rtdd
//
LOCUS       WP_175819812             290 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0419].
ACCESSION   WP_175819812
VERSION     WP_175819812.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 290)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..290
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30846
     Region          1..288
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mstlatgral rdakawlvtp alafiaalfi ypfayglvls fqpmngggal anyvqfftdt
       61 amwptvlvtl klavpatlln vgiavpvafa lrrnspyqkf vttllvipvt lgtvlvadgm
      121 ltyfgpngwf pqalqglhly tdevrlthny wgvllslivs gfpfafllml syisgidptl
      181 araaatlgan pwqqfrqiyl pllvpgltma aclsfvqafs vfpsavllga pagptrvisi
      241 aaaeaafesy dyslasaiai vmgfvqllvv asmlgarrff ytgavtggkg
//
LOCUS       WP_175819816             442 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0419].
ACCESSION   WP_175819816
VERSION     WP_175819816.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..442
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45859
     Region          17..420
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mlihhvepsl qdltaterra payawlvfgl tvglllsdym srqvlnavfp llkhawalsd
       61 tqlgslsgvv allvglltfp lsvladrfgr vrsivlmaal wsvatlgcal stnyaemlva
      121 rglvglgeaa ygsvgvalil sifparlrat ltgafmagga fgsvfgmalg glvgahlgwr
      181 wsfgvmaalg ivllvayrcv vterrlaacr vepcrpdada prdlrgsvra lmsglfasrs
      241 vicayvgsgl hlfvpgalfa wlpsylnryy amapdraavl aagfvllagv gmvgcgivtd
      301 rvgradgsrk wltaiaycvl tgvclavafr lppgplqlal icagmlvgag asgasgamva
      361 nltpaaihas afatltlann llgmapgpll tgwaadragl vgalqwipvv plaaavlfav
      421 grasyaadla rvererratr ls
//
LOCUS       WP_175819813             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175819813
VERSION     WP_175819813.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..359
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39255
     Region          8..355
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkhsferlrl dgvsrsftna qgaqvaalng ldleirrgef iallgpsgcg kstalnciag
       61 lqpltrggiw lddtridvlp perrgfgmvf qnyalfphms vldnvgfglk mrgvpkqetr
      121 rraqqalelv qlvghegklp gqlsggqqqr vaiaraivie pplvlmdepl snldtklrie
      181 mraeirriht qleratiyvt hdqdealsma drivvmkegv vqqvaspkdv ytrphnlhva
      241 rfmgyrnvlp ftlegmagdy vnvasggvrl agvpmagfda kevvvalrpd dieraeegad
      301 nafdatvetv eyggrdslir aitpfgaiwa rvageftege plrlrvapar tlvyagdvp
//
LOCUS       WP_175819864             282 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175819864
VERSION     WP_175819864.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..282
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29775
     Region          7..260
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtrstaalaa rglsvgyrdh vvidgldlsi aagrvtalcg pngcgkstll rtlaglqpar
       61 aghvdvngkp lasfrrrala reltmlaqfn qipsgltvre lvaygryayg gflrglsrvd
      121 haaidealet sgladdaerd vgalsggerq rawiamalaq qapivlldep ttyldihhql
      181 dildalraln rargltivwv lhdlnqaaay sdeivlmrag rlvaqgtpda mldparlraa
      241 fgvemlklah pqtgapmcvp aygpstdgap qaagvfardl av
//
LOCUS       WP_175819924             543 aa            linear   BCT 11-JAN-2025
DEFINITION  GspE/PulE family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175819924
VERSION     WP_175819924.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..543
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=58807
     Region          2..538
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mktehivqrw qsesdasgvd faqyvaglls adatllaqaa aclgigavda dalraartrf
       61 dllplhdalt wrvlpveldg apcvvvadpf arhvrdella rfgtrpvela msapgeverl
      121 lgdiesserl mddvtidtqg dslaqaiesi slasiakdes piirlvnttl ydalqsrasd
      181 ihleavpdgl siryridgvl qsirhipgle aaaqtlsrlk vlaaldiaek rvpqdgrfkv
      241 vmqgreidfr vsiipgthge navmrvldks qrgdrvsldv lgfdaptarr vralahrpyg
      301 lmlvtgptgs gksttlyavl sevntgddki itiedpveye lqgvlqipvn erkgltfarg
      361 lrsilrhdpd tvmvgeirde etasiavqsa ltghrvlstv handgfsvid rfiymgveps
      421 tflealngvv sqrlvrrica rcgdaahgad lrdapldelk rvvvpgagce tcrgtgyhgr
      481 iglaevltld aamkvaller siekrtrala dnadyqsmre aglaairarl ttfqevqrai
      541 ave
//
LOCUS       WP_175819974             137 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175819974
VERSION     WP_175819974.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..137
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15375
     Region          19..106
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(20..22,36,53..55)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mtttvekvvl ppipakryft igevselcgv kphvlryweq eftqlrpvkr rgnrryyqhh
       61 evllirrire llyeqgftin garnrldspg sergaaepve sdaqaadarg vdkggatvdv
      121 ialrqalldv idglkhd
//
LOCUS       WP_175819986             557 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Burkholderia sp. BCC0419].
ACCESSION   WP_175819986
VERSION     WP_175819986.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60516
     Region          25..384
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          453..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mtpaslieqy gpresmeydv vivgggpagl saairlkqla aekgaeigvc vlekgseiga
       61 hilsgavmdp raitelfpdw kergapldve vtedrflfls eksavttpnw alpdnfknhg
      121 nyvislgnvt rwlgaqaeal gveifpgfpa aeilynddgs vkgvatgnmg vgkdgepten
      181 fqlgmelhak ytlfaegcrg hlgrqliskf kldanadpqa ygigikelwe idpakhkpgl
      241 vihtagwplk sdtyggsfly hmdnnqvvvg fvvglgytnp ylspfeefqr ykthpsiraf
      301 leggkrvsyg araitaggll slpktvfpgg aligddagfl nasrikgsha aiktgmlaad
      361 aafdavqagr qsdelnaypd afkqswlyte lyrarnfkqw makglylgtl mvgleqkvmg
      421 gnvpwtlhhq hadhemlkpa sqcepieypk pdgkltfdrl ssvfisntnh eenqpahltl
      481 kdasvpvnvn lrtyagpear fcpaavyefm knddgsdrlv inaqncvhck tcdikdptqn
      541 ivwvtpeggg gpnypnm
//
LOCUS       WP_175819992             473 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia sp. BCC0419].
ACCESSION   WP_175819992
VERSION     WP_175819992.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..473
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50302
     Region          4..473
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 misseafvsa crdaigaayv ltdphdtepf ltdwrrrykg sacavlkpad taevaalvrl
       61 anthgvalvp qggntglagg atpdasgsqa vlsaarlnrv raldphnnti tveagvilad
      121 vqarareggr lfalslaaeg sctiggnlst naggtavlry gnarelclgl evvtpqgeiw
      181 dglrglrkdn tgydlrdlfi gaegtlgiit aavmklhplp aaqvtalaal esphaaldfl
      241 alaqraagpl ltgfelmsdf cmqlvgkhyp qlrypfaqth aqtvllelsd neseaharal
      301 feklmeeafe aglvvdavva enlaqsrafw dlrehiplaq adeglnikhd iavpissiar
      361 fidetdaaiq qaapgarmvt fghlgdgnlh ynvqmpeggd akaflaafqa pinrivydnv
      421 hrhhgtisae hgigqlkidd aqrykspvet tlmrtlktal dprglmnpgk vlr
//
LOCUS       WP_175820051             232 aa            linear   BCT 11-JAN-2025
DEFINITION  YoaK family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175820051
VERSION     WP_175820051.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..232
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=23334
     Region          6..211
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mkhedtilaa vagfvdtlsf valfglftah vtgnfvliga giagfgqgvv lklsvfpafv
       61 cgviasslia rsmaarpawq gtrvlhtvqa vlllgfcaag vwatpvtqpd slaalvagiv
      121 gtfamgvqna hprviaragg vpntvmtgnv tqaildavdm lspgtadsvr atararfakm
      181 lpaivafalg aacgalgfry vgflallvpv galatlalca aqasgtttqe ra
//
LOCUS       WP_175820055             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175820055
VERSION     WP_175820055.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33821
     Region          7..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..293
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(105,109,148,162,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(106..107,111..112,114..115,118,122,124..130,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mqhlpdleaw aifarvaetg sfakaadllg vsqptvskai arlekrlgam llyrtsrkls
       61 ltptgellrd rairlladae lieneataqa lephglvrvn apmsfgvhhl spvlpafler
      121 yprvdidlvl tdhivdivsg gfdvairiae lsdstlrsrr lcavrrplva spayldrrgr
      181 pthprdieqh vcltytnlpt pehwrfhhpa sgdevgvsvh grirtnnadv ilpalvgghg
      241 lalqpeflvw damqrgelee vmsdwkiadi nvnlvtppgm lraarvtvll dflaehfaha
      301 pwalpva
//
LOCUS       WP_175820058             293 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175820058
VERSION     WP_175820058.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..293
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31343
     Region          12..270
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 msasiktllt presdignlv vrrvlparaa rlvgpfiffd emgpavlpag rgidvlphph
       61 iglatvtylf dgtlmhhdsl gfrqkivpgd vnwmtagrgi vhserspded rpreqpvhgi
      121 qtwvalpveh edtapafvhh aadtlpsftr dgvtvrviag tafglaspva vfsptlyayg
      181 efasggqlal daehdergvy lvdgdltvdg tplapatmav lepgataala sahgarvmll
      241 ggahlpgerf iewnfvsser akidaaraaw adqtfgkvpg eedewtrqpe rka
//
LOCUS       WP_175820069             201 aa            linear   BCT 11-JAN-2025
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Burkholderia
            sp. BCC0419].
ACCESSION   WP_175820069
VERSION     WP_175820069.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Sciara,G., Clarke,O.B., Tomasek,D., Kloss,B., Tabuso,S.,
            Byfield,R., Cohn,R., Banerjee,S., Rajashankar,K.R., Slavkovic,V.,
            Graziano,J.H., Shapiro,L. and Mancia,F.
  TITLE     Structural basis for catalysis in a CDP-alcohol phosphotransferase
  JOURNAL   Nat Commun 5, 4068 (2014)
   PUBMED   24923293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Koga,Y.
  TITLE     From promiscuity to the lipid divide: on the evolution of distinct
            membranes in Archaea and Bacteria
  JOURNAL   J Mol Evol 78 (3-4), 234-242 (2014)
   PUBMED   24573438
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Koga,Y.
  TITLE     Early evolution of membrane lipids: how did the lipid divide occur?
  JOURNAL   J Mol Evol 72 (3), 274-282 (2011)
   PUBMED   21259003
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..201
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20965
     Region          28..196
                     /region_name="PgsA"
                     /note="Phosphatidylglycerophosphate synthase [Lipid
                     transport and metabolism]; COG0558"
                     /db_xref="CDD:440324"
ORIGIN      
        1 mslyalkpkf qnrlrpfans laergvtanq vtlfaaggsi vvgalaglgv faralfllip
       61 lwlfarmaln aidgmlareh gqkstlgayl nelgdivsdv alvlpflavp afapadvwlf
      121 altaviveca gligplvgat rrydgpfgks dralalgafa lwiglglpvg svaawlwrll
      181 ivlsivtavr rvqagiaeag g
//
LOCUS       WP_175820071             579 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia sp. BCC0419].
ACCESSION   WP_175820071
VERSION     WP_175820071.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 579)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..579
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=63265
     Region          10..579
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mkiirrgnla aaallfivtg vsaqeaprli vpgndqqtrq qeearerert vtapgvrssv
       61 tasagypalp setpcfrieh faldvpdalp aslksqgasa lpmdrfafar ewlehytgqc
      121 vgkqgldvlv kglsqailar gyvttrvllp eqdlstgtlk falipgvirh vrfadeklrg
      181 twktafptgd gellnlrdle qgleqmkrvs sqdvsmqivp advpgesdvv ldvkrgkpwt
      241 vvasidnsgt ratgrlqgnl slgvdnplgl ndifnigmsq dlefgdkrlg shgwngfysi
      301 pwgywtatls aytstyyqqi agvnqtfias gnsktvdfkl nrvlsrsqnd vfgaqfrlsr
      361 rfgqsfiedt eipqqrrnnt fvefgltdrh yfgnaqfdgt layrqgigaf gaqddilaad
      421 ggptyrykma vldanlsvpf aiaqqpfryv ttfhgqytgh tlyyiddlti gsrytvrgfd
      481 getmlaasrg fywrnelqap igqtgvaaya gldygrvwgp qpvalvgtql agavigvkgs
      541 vatrfggygy dlfagtpvyk psgfptnrvt lgfqltaqf
//
LOCUS       WP_175820121             540 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA synthetase [Burkholderia sp. BCC0419].
ACCESSION   WP_175820121
VERSION     WP_175820121.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
REFERENCE   3  (residues 1 to 540)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   4  (residues 1 to 540)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..540
                     /product="acyl-CoA synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016405 - CoA-ligase activity [Evidence
                     IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57652
     Region          48..539
                     /region_name="MACS_like_3"
                     /note="Uncharacterized subfamily of medium-chain acyl-CoA
                     synthetase (MACS); cd05971"
                     /db_xref="CDD:341275"
     Site            order(111,242..244,268,288,290,294,315..318,337..342,
                     345..346,362,422,434,437,443,445..448,477,506,511..512,
                     514,516)
                     /site_type="active"
                     /db_xref="CDD:341275"
     Site            order(193,196..201,203..204)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341275"
     Site            order(238,290..291,294,315,445..447,506,512)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341275"
     Site            order(315..318,337..342,362,422,434,437,443,448)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341275"
ORIGIN      
        1 mlpaadrydh llsrfrwdip arynigvdvc dkwadgsgrl alihetaqgd vsritfddlk
       61 nasnrlansf araglrrgdr igiflaqgpe taiahlaayk fgaiavplft lfgvdaleyr
      121 lanseaaalv tdaagyakia plraqllpal htvycigdda pdspgvlryd aalaaeapef
      181 vpadtaaddp aviiytsgtt gkpkgalhah rvllghlpgv emsqqcfprd arlfwtpadw
      241 awigglldvl lpswhhgvpv larrfekfdg daafalmarh gvthaflppt alklmhavaa
      301 preryalslk svasggeslg teltawgrda lgvtinefyg qtecnmvlss caalfdaqpg
      361 aigkavpgha vaivdadgtp lppgvegria vrrpdpvmfl eywrnpgatr dkfagdyllt
      421 gdtgtidadg fvrfvgrddd vitsagyrig pgpiedcllt hpavrmaavv gvpdatrtei
      481 vkafvvlnpg hvgddalisa lqahvrtrla aheypraiaf vdslpmtatg kivrralrda
//
LOCUS       WP_175819600             311 aa            linear   BCT 11-JAN-2025
DEFINITION  SPFH domain-containing protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175819600
VERSION     WP_175819600.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..311
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33447
     Region          2..284
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 mdsliiwvvl lviaivivsk tvkivpqqha wvlerfgryh atlspglniv lpfvdriayr
       61 hvlkeipldv psqvcitrdn tqlqvdgvly fqvmdpmkas ygssnfvlai tqlsqtmlrs
      121 vigkleldkt feerdfinhs ivsalddaaa nwgvkvlrye ikdltppkei lhamqaqita
      181 erekraliaa segrkqeqin lasgareaai qksegerqaa inqaqgeaaa ilavaeanaq
      241 aiqkianaiq sqggmdavnl kvaeqyvgaf snlakqgntl ivpsnlsdlg taissaltiv
      301 ksagaasgak g
//
LOCUS       WP_175820166             146 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175820166
VERSION     WP_175820166.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..146
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=15948
     Region          44..146
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 msgihhgydl fdefarvqrq mtsllgerpa giravrpgaf palnvgatdd aieivafapg
       61 maatdfdvsi dkdlltisge rkpapraegd dvrtyaqerf hgafrrvvel prdadpdqvs
      121 aryengclli rvgrreaskp raitiq
//
LOCUS       WP_175820192              93 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175820192
VERSION     WP_175820192.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..93
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10148
     Region          1..93
                     /region_name="COG5606"
                     /note="Predicted DNA-binding protein, XRE-type HTH domain
                     [General function prediction only]"
                     /db_xref="CDD:444337"
ORIGIN      
        1 mtneryanvw daiesepaqa anmklrselm ialkhriarl elsqaeaatq lgvtqprvsd
       61 lmrgkinlfg ldalvnmaaa vslrvdlqvr esa
//
LOCUS       WP_175820188             343 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175820188
VERSION     WP_175820188.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..343
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36641
     Region          8..343
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkldstpvtl tgcaktfrgt rvlepldlsi gagetlvllg psgcgktttl rliagldmpd
       61 aggtiafgdd dvtalpierr qvgmvfqnya lfpnltvrgn vgyglkirkt epralrervd
      121 ellammrlda hadkpvdqls ggqrqrvala ralavqprvl lldepltald aklrdvlrrd
      181 mntllrtlgv ttvyvthdqa eamelgdriv vmgagrieqi gtpreiyyhp anrtvaqfig
      241 tlnrlagqwr dgalettgga iatphaadew ffrpedaqla dpahaplrga vgacaflger
      301 trltiehaap dalvidvpgr ialargtavg ltiapeglia lga
//
LOCUS       WP_175820217             146 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175820217
VERSION     WP_175820217.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..146
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=15584
     Region          1..146
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mrfmlngqpf dfdgdpdtpl lwvirdsarl tgtkygcgig acgactvhld geaartcvlp
       61 aasvagravt tieglshdrs hpvqrawiek dvpqcgycqs gmvmataall arhrkptdaq
      121 ideavtnlcr catyqrirea ihvaag
//
LOCUS       WP_175820242             204 aa            linear   BCT 11-JAN-2025
DEFINITION  SCO family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175820242
VERSION     WP_175820242.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..204
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21871
     Region          46..199
                     /region_name="Sco1"
                     /note="Cytochrome oxidase Cu insertion factor,
                     SCO1/SenC/PrrC family [Posttranslational modification,
                     protein turnover, chaperones]; COG1999"
                     /db_xref="CDD:441602"
ORIGIN      
        1 mpsrlsrlir taaalaaava laacthdepr wnltnvtghl pdlsfkltgg dghpvdadaf
       61 rgrvalvyfg ythcpdvcpe tlarlmevla klgpqadnvr ilfvsvdpar dtpqamqsyv
      121 aafdaaharg ltgtdgqies lakryrvayq mekrdpsggy evthssavyi fdasgrarll
      181 atdrdspdai aadvrriidt astt
//
LOCUS       WP_175820220             182 aa            linear   BCT 11-JAN-2025
DEFINITION  peroxiredoxin [Burkholderia sp. BCC0419].
ACCESSION   WP_175820220
VERSION     WP_175820220.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Jeong,W., Cha,M.K. and Kim,I.H.
  TITLE     Thioredoxin-dependent hydroperoxide peroxidase activity of
            bacterioferritin comigratory protein (BCP) as a new member of the
            thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide
            peroxidase C (AhpC) family
  JOURNAL   J Biol Chem 275 (4), 2924-2930 (2000)
   PUBMED   10644761
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..182
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.24"
                     /GO_function="GO:0008379 - thioredoxin peroxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19534
     Region          29..170
                     /region_name="PRX_BCP"
                     /note="Peroxiredoxin (PRX) family, Bacterioferritin
                     comigratory protein (BCP) subfamily; composed of
                     thioredoxin-dependent thiol peroxidases, widely expressed
                     in pathogenic bacteria, that protect cells against
                     toxicity from reactive oxygen species by reducing...;
                     cd03017"
                     /db_xref="CDD:239315"
     Site            order(68,71,141)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239315"
ORIGIN      
        1 mkrklllgam aalvaghall aqaelkpgaa apdfrtqasl ggktytysla dalkqgpvvl
       61 yfypaaftkg ctieahafad avdrykayga tvigvsadni dtltkfsvse crskfpvaad
      121 pdakiireyd aklpaldran rvsyvisper kilyeytsls pdkhventla avkawadahp
      181 kq
//
LOCUS       WP_175820270             492 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA recombination protein RmuC [Burkholderia sp. BCC0419].
ACCESSION   WP_175820270
VERSION     WP_175820270.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..492
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=53769
     Region          <32..>189
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     Region          154..478
                     /region_name="RmuC"
                     /note="DNA anti-recombination protein (rearrangement
                     mutator) RmuC [Replication, recombination and repair];
                     COG1322"
                     /db_xref="CDD:440933"
ORIGIN      
        1 mtmtlllaav vvlavalava ivalvrgggg hddaavlgdq iedaahaqar averlerelr
       61 geivenargs rtelagsfaq lqqtlaaqlt svatvqnnqi egfaqqlgkl vagnaqqfda
      121 mresvqrqaq qareeqtgal rlfgdtlnrq ltqlteandr rigevratle qrlkeietnn
      181 aakleemrrt vdeklhatle qrlgesfklv sdrleqvhrg lgemqtlaag vgdlkkvltn
      241 vktrgtwgev qlealleqml tpdqyaknva tvpksterve fairlpgrda gtrdaapvwl
      301 pidakfpred yerlidaqer adavaveeaa ralearvrme artiaekyva pphttdfall
      361 flpteglyae ilrrpgltdl lqrdyrvtva gpttltalln slqmgfrtla ieqrssevwq
      421 vlgavktefg kfgdvlartk aqletvtrsi esaeqrtrvm srklkqveal pgdaaagllg
      481 aeeadgadad da
//
LOCUS       WP_175820274             301 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175820274
VERSION     WP_175820274.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14137101
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..301
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32547
     Region          19..150
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          <114..301
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          218..298
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msatrlpdsa rywrtplvpd adlltatyrd hafaphwhda ytipvilega erftyrgtgh
       61 vaetgtvpvi npgevhtgsr aadegwcyrv sympvefire lassiagrpq dapwfapdvi
      121 rdadlaarlt lahrmleags eralsshaha sgqpadapaa gtphiydpla aetamldals
      181 tliarhadvr pqpaplaade prvnamrerl aadlmsavtl ddvaqaagls pfhaarlftr
      241 tagmpphawr nqlrlqrala plragvpvad vaaasgfvdq shftrhfkrm fgvppgrwqa
      301 s
//
LOCUS       WP_175820280             465 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54 dependent transcriptional regulator [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175820280
VERSION     WP_175820280.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..465
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51368
     Region          1..118
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <135..438
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mgadqrhviy ysrepndalr shfdecgwrv dlaetvrdvr rvvqhgvata glldfspgfk
       61 psdlrelesc lsiqhigwia atrrgqlqda tlrhlirdyc fdyvtmpyet arivetvgha
      121 hgmvaltdpv sspvgagrse gemvgtcdam lglfrtirrv aatdapvfis gesgtgkelt
      181 aiaiherssr aqapfiainc gaipstllqa elfgyergaf tganqrkigr veaansgtlf
      241 ldeigdlple sqasllrflq egkierlgah vsipvdvrvi cathvdmeaa lregrfredl
      301 fhrlcvlkie epplrargkd ievlarhmle rfkgdahrrl rgfspdavas lygyswpgnv
      361 relinrvrra ivmsegrmit aadlelnaya tlapvsllea reaaerqaie qallrhrgrf
      421 adaarelgvs rvtlyrlmca hgmrdrgdtl agfsvplpel prhac
//
LOCUS       WP_175820319             226 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175820319
VERSION     WP_175820319.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..226
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24639
     Region          10..225
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mstltdvtrd rpgasaasla drayaliqrd iitmrlkpga alneadlvar tgigrtpvhq
       61 avhrlvlegl lsvmprkglm vqplslddiv avidvrrine ahcaelaarh atpddlahla
      121 allddgqacv dthdvegmme ldrafhqaia aaarnavlad ilralhersl rfwfvtlsep
      181 hhladvqheh ralfdrlsar daagaraave shidsfrstl lqhlrp
//
LOCUS       WP_175820347             769 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DNA translocase FtsK [unclassified Burkholderia].
ACCESSION   WP_175820347
VERSION     WP_175820347.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12144184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..769
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=83413
     Region          18..198
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          148..769
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 makapysaqa qalphrmskl lteirwilqv alcaflvmal lsysrrdpsw thaaqvdhis
       61 nwagrvgawt adiilllfgl saywlivplg rriavnyrri trhdaipdep erpigwltei
      121 fafvlvvlac dgiealrmws lkvqlprapg gvvgeavaga mshafgftgg tllllialai
      181 glslyfrfsw lsvaervgga ilsavnvakl rreaerdrkl geaaavrreg kveeervrie
      241 dhepvtivpp vvtpakserv ererqvplft dlpgdstlpp vslldpapkt qeaisadtle
      301 ftsrliekkl kdfgveasvv aaypgpvvtr yeiepatgvk gsqivnlakd larslslvsi
      361 rvvetipgkn ymalelpnqr rqtvhlseii gsevyaaass altlslgkdi ggkpvcadla
      421 kmphllvagt tgsgksvgin amilsllyka taeqvrlili dpkmlemsvy egiphllcpv
      481 vtdmrqagha lnwtvaemer ryklmsklgv rnlagynnki ddaakreeki pnpfsltped
      541 peplgrlpni vvvideladl mmvvgkkvee liariaqkar aagihlilat qrpsvdvitg
      601 likanvptri afqvsskids rtildqmgae sllgmgdmly lppgsglpvr vhgafvadde
      661 vhrvveklke hgepnyvegl leggtadgde gsagagtgeg ggesdplydq aveivvknrr
      721 asislvqrhl rigynraarl leqmeqsglv samsssgnre ilvpardae
//
LOCUS       WP_175820361             789 aa            linear   BCT 11-JAN-2025
DEFINITION  beta-N-acetylhexosaminidase [Burkholderia sp. BCC0419].
ACCESSION   WP_175820361
VERSION     WP_175820361.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 789)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 789)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 789)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 789)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 789)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 789)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..789
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..789
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=84750
     Region          62..565
                     /region_name="Chb"
                     /note="N-acetyl-beta-hexosaminidase [Carbohydrate
                     transport and metabolism]; COG3525"
                     /db_xref="CDD:442747"
ORIGIN      
        1 mtrhvgpaaa rcatssasta scceratdnd rpssrikddv smmkapasga trarhapsss
       61 rfilgllctl sccvptlaqa slplmpvpks letadgslav rgafglnwhg cnstlldrag
      121 rrfqrdvdrl agvdpddtvg psldidcrsg dpaskadagk eayrlaigtn gvqlradgpt
      181 gvlrglatlr qlirhagrev slplltvdda prfawrgimi dvarhfmtvs tlkrqidame
      241 lvklnvlhlh lsdneafrve slrypalqks aadgryytqa emrdlvayaa drgvrivpef
      301 dlpghtgaiv taypelgagr fdrhdpqsvm nvaldpaner tyrfvdrllg ematlfpdry
      361 lhvggdelgp kawsdnpaiv afarekqlas praleayfqa riraiaakyg kktigwdeva
      421 dlpdygdtvi qtwrtsngis kvaeaggkvi vssgyyldhq lpasayygvd ptdpgafgit
      481 aqeadaarki sprvrhvvdg fvvaprpplt paqqrlvlgg eaalwseqvt demldaklwp
      541 vsaaiaerfw spadvrdldd myarlfttqn alrllglqdr gnrermvarl apdragavet
      601 lldtvrpvqf ighdrtkraa lagkpagdrq tstgladaaa idtplahrfl gdvqrlvngd
      661 rsraapleaq lriwrdnptl yrdaaagrpe leaalpvsdd laemarggla aiealrngqt
      721 lpadaaarva avldraaaae qasstylrsa mmaqppadli vtitpgiral vkaaapasgt
      781 ggsnparqd
//
LOCUS       WP_175820374             251 aa            linear   BCT 11-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Burkholderia
            sp. BCC0419].
ACCESSION   WP_175820374
VERSION     WP_175820374.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..251
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25946
     Region          1..251
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlttqrkkai ldalardgqv laaelsvqfg vsedtvrrdl relaaegllq rvhggalpas
       61 pavapfaqre alettekrri arraaqmiap gqvaivdggt tsallvgqlp adlhativth
      121 spsvavalaa hpsidvilig grlykhsiva vgaaamegia rihadlyfmg vtgvhpvagl
      181 stgdfeeaai kralaeraae tvvlasqskl raassfvigd itlaqtivve ketdaaltkp
      241 ieaagvtvvh a
//
LOCUS       WP_175820459             136 aa            linear   BCT 11-JAN-2025
DEFINITION  GFA family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175820459
VERSION     WP_175820459.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..136
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14890
     Region          5..131
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mahpepmegg cacgairyri advptdagfc hcrlcqrttg aavvasasvp idafeylqge
       61 ptvyassawg errfcsrcga qleyrladap ttveinyatl depsrlrpaw hvwygdrfpg
      121 ieidddlpky ddggre
//
LOCUS       WP_175820432             243 aa            linear   BCT 11-JAN-2025
DEFINITION  DsbA family oxidoreductase [Burkholderia sp. BCC0419].
ACCESSION   WP_175820432
VERSION     WP_175820432.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..243
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25970
     Region          15..214
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(23,26)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 mttapaptar ptltveiwsd licpwcwigk rrfdealaaf ahadrvdval rayrlmpgqp
       61 vepveamlag kyrmapaqvd qmlrqvtdaa asvglrydlp gtlvgdtldg hrlvklaqas
      121 glahalterl yrayfcehgs lfdhaeltef aveaglersa veavlrsday rdeveadiar
      181 aaqiggrgvp lfvfggryav sgaqpadafa qaldqawrdg ivelggsdaa acgpdgcelp
      241 ars
//
LOCUS       WP_175820488             215 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175820488
VERSION     WP_175820488.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..215
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24265
     Region          1..213
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 mielddvrky ystrngqrlv ldgvnltinp gerigilgrn gagkstiirl isgselpssg
       61 risrsmavsw plafsggfqg sltgldnlrf vcriyqasfe nalpfveefs elgeylrepv
      121 kkyssgmrar lafaismave fdcflidevi avgdrrfhek ckyelfekrk dramilvshd
      181 aitvkeycdr acvleggrlh hfddvedayd fynhi
//
LOCUS       WP_175820519             275 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: carbon-nitrogen hydrolase family protein
            [unclassified Burkholderia].
ACCESSION   WP_175820519
VERSION     WP_175820519.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10166075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..275
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30490
     Region          12..272
                     /region_name="nit"
                     /note="Nit1, Nit 2, and related proteins, and the
                     Nit1-like domain of NitFhit (class 10 nitrilases);
                     cd07572"
                     /db_xref="CDD:143596"
     Site            order(50,106,123,127,138,163..164,166..167,186)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143596"
     Site            order(50,123,163)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143596"
     Site            order(124..125,144..146,164,167..171,173..174,194..195,
                     198..199,201..203,205..206,236,266..267,270..271)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143596"
ORIGIN      
        1 mtdharsatp frvaalqmvs tpdvtrnlae arrliaeaag egaqlvllpe yfcfmghrdt
       61 dklalaepyr dgpiqqflad aarrhgiwvi ggtlplkape pdrvlnttlv fdpsgnevar
      121 ydkihlfnfe kgdesfdear tiragdtvvt fdapfgqvgl svcydlrfpe lyrrmgdcal
      181 mvvpsaftyt tgrahwetll raravenqcy vlaaaqggkh engrrtwghs mlidpwgelv
      241 avrdegasvv lgtldpqria dvrqslpawr hrvlt
//
LOCUS       WP_175820526             469 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FAD-binding oxidoreductase [unclassified
            Burkholderia].
ACCESSION   WP_175820526
VERSION     WP_175820526.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..469
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50219
     Region          14..467
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mnhpappvat rrplppamld alraafgerv stadavrahh grdespfdpq lpdavvfars
       61 tddvrevvsl cslysvplip ygagsslegh llavrggvsl dlsemnrvls inaedltvtv
      121 epgitrkaln ealrdtglff pidpgadasi ggmtatrasg tnavrygtmr envlgltavl
      181 adgrvvktgs rarkssagyd ltrlfvgseg tlgviteitl rlhplpeavs aaictfptmg
      241 davrtvieti qigvpiarve fvdalavrsi nrhsnltlte aptlffefhg tdagvkeqae
      301 lvqalagqna gqgfewatrp edrtrlwsar hnayfamlql kpgcravttd vcvpisqlaa
      361 cveetevdlr asslpcpivg hvgdgnfhva ilidpdkpee laeaehindr iveralrlgg
      421 tctgehgvgl hkmrflpkeh gdnaidtmra iklaldprnl mnpgkiftc
//
LOCUS       WP_175820615             425 aa            linear   BCT 11-JAN-2025
DEFINITION  GspE/PulE family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175820615
VERSION     WP_175820615.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..425
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=44899
     Region          <36..415
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mhfpssgapl htqsspahsd appaaaphal daaqlddapa vrlltdtlha arvrdasdih
       61 vepfeagwri rlridgvlhe qarpplhlrd alvtrikvls rmdiaerrlp qdgrlriaid
      121 ggtrgdyrvs slptlfgekl vlrrletlpp dltlanlgfd arqaaameaa iraphglvlv
      181 tgptgsgktl slycalqmld rdahnvctve dpaeiqldgi nqvgvadkag ltfatalral
      241 lrqdpdvimv geirdaetad vaikaaqtgh lvlstlhtnd apaavarlld igvapynlaa
      301 alhlvtaqrl vrrlcvacrv hsdasaralr eagcdpaala agwrpfvarg csachgigyr
      361 griglhqtmp vspalaeriv arasvgelaq cvaaegvrtl rdaaftrvmd gttsiaeava
      421 atpaa
//
LOCUS       WP_175820627             468 aa            linear   BCT 11-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Burkholderia sp. BCC0419].
ACCESSION   WP_175820627
VERSION     WP_175820627.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..468
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=48018
     Region          2..460
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mtmlslgeaa rlisgatvrg dagvtfdrvs tdsrtagpgd lfvalkgerf dahdflgdva
       61 argaaaalva hapadvalpm ieggetraal galahgwrmr fplplvavtg sngkttvkem
      121 iasifaaavg tdarlatagn lnndvglplt llrlsaahrl avieigmnhp getevlarlt
      181 aptvalvnna qrehqefmat veavalehaa vihalppdgv avfpaddaya giwrvaatgn
      241 rildfalhda erqnaaqvvg rvhggelaid tpvgavtvrl ralgehnarn alaataaalg
      301 agvalsairq glesfepvkg rlqvkqasvg slagatvvdd tynanpdsmr aaidvlaahp
      361 aprvlvigdm gevgdegpaf hreigayare rgidalfalg dasrdactay gdtarhfgdv
      421 galvaallva gygaqatvlv kgsrymkmer vvdaltnqsa agtvpaah
//
LOCUS       WP_175820697             341 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0419].
ACCESSION   WP_175820697
VERSION     WP_175820697.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..341
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35572
     Region          10..341
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mgnlnpvada qtmtlksrht kwppelsifl vlvgislffe ivgwivvgqs flfnaerlei
       61 ivlqmavigi iavgvnlvii tsgidlssgs vvaaaavvsa slaqvsdfpr avfphltdlp
      121 iiwpvlagvc vgllvgllng tliamtgipp fiatlgtmva argfakwftn gmpvsmltdp
      181 faaigaganp viifvviaai fhvvlrytrf gkytyaigan rhaavvsgin vtrhlifvya
      241 iagllsgiag tvtaaraisg qsgmgvmyel daiaavvigg tslsgglgrv tgtvigvlil
      301 gvmtsgftfi ridayyqemv kgaiivaavi adqyrnkksr r
//
LOCUS       WP_175820766             707 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175820766
VERSION     WP_175820766.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..707
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77071
     Region          9..691
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mtypslrdwl fsgktfaasm lalylglyfq lprpywamas vyivsnpfvg atrskalyra
       61 lgtalgaaaa iffvppfvet pllfsiivat wcgtllylai sdrtarsyvf mlagytmplv
      121 alptvtdpst ifdvaiarte eivlgivcas vvgsavfpnr laptliertd awfkdaafyg
      181 retlsghiag kalsacrqrl aatitglefl lsqlgydhah prvlartqal agrmqlflpl
      241 mssladplia lmrdlhvrpp aldalladaa kwfdaplpav ktgsdgdmah dpvaddlrer
      301 iaalqppdsa laswdgalls nalwrlrqvi diwqdcrslr alianesgvw qpryrhwrlg
      361 gterffdrgm mlfstltvvf aivfacwlwi ssgwhdgaaa vtlvavscsf faaldepapl
      421 vfkfflstaa svvfaglylf vvlphvhdfa mlvlmfagpf iligtllprp qfnmvtmlva
      481 vntatfisiq sayeadffvf lnsnlagvag llfayvwtra trpfgaelav rrllrsgwed
      541 varsastqpl ddqrnhasrm ldrvtqllpr lgasddhrhp siesfrdlri alnaldlrrs
      601 rrrlsgdvpd aidrvlagvt dhytrcaaan arqpvppall atiddalqrv agrnlpgaap
      661 addaaapaap athrrlrdtl halvglrlsl ypaaaaqapq apdgara
//
LOCUS       WP_175820756             338 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175820756
VERSION     WP_175820756.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37930
     Region          59..210
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <223..319
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhpvpvryip gerdddvaia afdqaghrst rrsrenelrq tlaervarwt dgvdhldtai
       61 pnlsfhrrea ptlpmecmve psfglvvqga krvmqsgday iydtdrflit sldlpgstqi
      121 ieassdkpfl glglkldfrv maelmmqvap dhddapagrg lvvgdmtepl ydalnrllal
      181 lddpnaiavl apyiereiyy rlltsdqgar lrqiastgtq cnrvsrairw lrahydeslr
      241 vddlaaqvqm ssstfhhhfr qltgmsplqy qkrirlnear rlmlaerlda asaafrvgya
      301 sptqfnreys rlfgnsprrd idslrggtdl alaivasy
//
LOCUS       WP_175820805             510 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175820805
VERSION     WP_175820805.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..510
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54869
     Region          28..504
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mrllgtfngw rtrtpkltps rdtgaltvpd lldaradvra dhaplrlpsg arltygawra
       61 rsgsaalgly qnglrigarv alifdgldwl dyavaymavl rcgataihmn ghmpdaeiqr
      121 rlaecdcsil irsrfvappr gfsgqhftid ellrgdesls aipiapdsia eirytsgttg
      181 aakgylvshd nltfgrtlds mqalsgasgm lvpmtlgtst satllvialt stapmllcsp
      241 ldiesmgeli ereritafmi tpriaqeivd arlgerhdlg svrlvasass plspsmaasm
      301 lammpnatlq iacaqseasp allthtytkd rpfsvgrpsp ateirvvgpd lsdaadgelg
      361 elwlrtaapk rlfltapdin allrkdgwyr tgdlvrrdps geieffdrka dalvrdgqli
      421 ssihmeatlm ndanvreaai vsvdrgaepa qivafvalrd pnalqavkda llntvppaqf
      481 pdafvvvsal prtqngkvlk relrlnvgir
//
LOCUS       WP_175820819              89 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl carrier protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175820819
VERSION     WP_175820819.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..89
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=9747
     Region          11..85
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mtvpsdtvlr dtreqvhgvl ldimpalnaa diderrhlke lgadsvdrve iimslrerfg
       61 ldvamsrfsd vpdlhtlivl laalregaa
//
LOCUS       WP_175820832             374 aa            linear   BCT 11-JAN-2025
DEFINITION  Fic family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175820832
VERSION     WP_175820832.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..374
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40838
     Region          23..367
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mmsgdytfiw esadwpawrf dlpalatpla dvsraqgmla grladiglal rdeaslaalt
       61 edvvktsaie genlnvasvr ssiarrlgvd igalapvdrh vegvvdmvld atthsaapvt
      121 earlfgwhaa lfptgysgls ritvggwrsd asgpmqvvsg pigrqrvhfe appagrlthe
      181 igrflawlna apvepllira glahlwfvtl hpfddgngri aralgdlvla radrspqrfy
      241 slsaqiqrer nayydvlert qrgsldvtew lawflnalgr aidhahttld avlikarfwq
      301 rcagvamner qvkvmnrlld gfegkltttk waalakcsqd talrditelv eqgmlrrsas
      361 ggrstsyelv pfdg
//
LOCUS       WP_175820842             137 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175820842
VERSION     WP_175820842.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..137
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14808
     Region          6..137
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mryvsleskk delllaarvl mmilfvlfgw qklngfsgtv aymastgnpa pelaaviava
       61 velvggvlia igfytrplal lfaaytlata lighrywalq gmeqymamin fyknvsiigg
      121 llllalsgpg rysvdrk
//
LOCUS       WP_175820859             238 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0419].
ACCESSION   WP_175820859
VERSION     WP_175820859.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 238)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 238)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 238)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..238
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24674
     Region          29..235
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mtrrtvqlvg slvaiiaagw alargigaet fhqrsddlay yagqhmllva ysmtlaiavg
       61 vpagvllsrp rfqhqaerfm qvfnigntip slavlaialg ifgignvpai valflasllp
      121 vtrnayegmk nvpaalreaa kgigmtgwqs lvrvelpnal piivggvrta lainvgtapl
      181 ayligadslg slifpgiyld nqpllllgas ltailalvld gvvaagsrhw larhggaa
//
LOCUS       WP_175820891             302 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175820891
VERSION     WP_175820891.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33724
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          90..291
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(102,106,145,159,162,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 medfndlvaf mavarernft raaaqlgvsq salsrtvral earmgipllt rttrsvspte
       61 agerllesia prfqeieael eslramtdqp agnvritatd yaaneyvwpr lqpllrrypa
      121 lkvelvndyg ltdlvagryd igvrlgdqva kdmiaqriap dmtmsiigsp dylasrpaak
      181 tpqdltqhnc inlrlptrna llswelskgr relqvrvegq ltfnnvyqmv daalagfgla
      241 yvpndlvahh vdagrlgwvl edwfptfvgh hvyypsrrks sravelvvda lrsgyqrntr
      301 qa
//
LOCUS       WP_175820915             205 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [unclassified Burkholderia].
ACCESSION   WP_175820915
VERSION     WP_175820915.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..205
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21716
     Region          1..202
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtelivviti tllavispgp dfamvtrnsl mlsrrsgvlt acgiglgvtv hvsytllgvg
       61 llirqslwlf navkligaiy liylgakmlm tkaggvqadt rvaplsdlaa lrtgfltnal
      121 npkttvfivs lfmqavrpdt plivqigyga fiaaahagwf slvalcfsat avrdrllslr
      181 hwidrtfgcl lvgfgvalai arggr
//
LOCUS       WP_175820916             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175820916
VERSION     WP_175820916.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33603
     Region          23..80
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          111..303
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(124..125,127..128,131,135,137..143,233..238,
                     244..245,247..248)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176171"
ORIGIN      
        1 misdqngese sqsihaslps lmalrcfeaa arhehfsraa delclthgav sravrlledd
       61 lgvalferrs rrvfltdagr tlaqavhdgl glmrhaahal rteaararrs vlsceptllm
      121 rwliprwpdf qarhagvdih laaaggpfsf dsgidmairr ndfawpagyy aehlfaervg
      181 pvcrpdkvga wfasrrggrt lkpdaarlht rtrpdawsaw aaaanqpatn grgqqfdhfy
      241 fslqaavagl gvaigpwhlv rddiesgvlv apmgfvedgs dyylltqapv mdgsaqavll
      301 ewlrgmv
//
LOCUS       WP_175820936             327 aa            linear   BCT 11-JAN-2025
DEFINITION  ferritin-like domain-containing protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175820936
VERSION     WP_175820936.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10090058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..327
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36531
     Region          98..228
                     /region_name="Ferritin_like"
                     /note="Ferritin-like superfamily of diiron-containing
                     four-helix-bundle proteins; cd00657"
                     /db_xref="CDD:153097"
     Site            order(107,137,140,187,217,220)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 mndtltvmqd tadirwsmpv dalmsndyal reealnrlye kakaaqwdva tdvdwshdld
       61 panplgmpdp tlliygtelw gkladadkre vrhhaqgwll sqilhgeqaa licasklasa
      121 englsarlca aaqmmdearh veayaklvne kldvsypmsr slkgllhdti tssaldmtnl
      181 gmqvlvegia lsifqsvvay stdpfikdlf vriqrdearh favgritlcr vyaemsahel
      241 rereefvceg aavlyehlca ddiwepmgls krecsamvre spvsssirrs ifrrlvptir
      301 emglltptvq atfekldvld yaampln
//
LOCUS       WP_175820943             236 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175820943
VERSION     WP_175820943.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..236
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25391
     Region          7..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtaasiapvl elrdvsrvye gagrvvavrg atisigprdv valvgpsgsg kstllnlagf
       61 ldvpssgerw legrriddap dtlerirrer igfvfqqfnl ipvmsalenv elgcfawgtp
      121 rtrreraram ldavglaare rhrpgelsgg eqqrvalara lakepaivia deptasldst
      181 naravaelil dtnrtlgtaf liashddrlc ahlprriemr dgvpgvnrel vdvcva
//
LOCUS       WP_175820979             150 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia sp. BCC0419].
ACCESSION   WP_175820979
VERSION     WP_175820979.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 150)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 150)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..150
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17170
     Region          5..144
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 mtitvtffpv thadadtlva iriaamrdsl erigrfdpqr ardrflasfd palcrfieae
       61 ysrvgfytlr pmadhwlldh lyivpahqak gigavlreil aeadehrmpv rvgalrgsds
      121 nrfyerhgfv rtdeaewdiy yrrepgtatt
//
LOCUS       WP_175821014             483 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0419].
ACCESSION   WP_175821014
VERSION     WP_175821014.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..483
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48678
     Region          40..451
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(46..47,50..51,54,86,136..137,139..141,144,166,
                     169..170,173,297,300..301,304..306,309,337,340,393..394,
                     398,402,418,421..422,425..426,429)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msdrapaldr vnhvdrapta aadsprtslr aifptvaaas lgfaivqldv tvvnvaipsl
       61 gqafgssihg lqwivdaytl sfaallltsg tladrfgsrr lfayglalfl laslgcalap
      121 slaalvaarv aqgvgaamil ptslalitha casdaaarvk avawwsatgg aisaagptlg
      181 gllidslgwr aiffinlpic alglwltlrh vqdsaaartr lfdpagqiva vlvlglltgg
      241 iiragahgig dpyaagalia svalgalfva ierrvaapml qlaffriprv pgvlaigavt
      301 naafyglifs lslyfqnarg ftatesglal apltiimlan lasarlavry gfratvivgl
      361 avslagyvwl wqtlaahtpy allapglaam avgggiaipa ltstmlgsve agrsatasai
      421 lntarqvgaa igvaalgalv agqgaaivag asrafavaav lvaicvvlav rwpgdapdtg
      481 tra
//
LOCUS       WP_175821030             177 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TadE/TadG family type IV pilus assembly protein
            [unclassified Burkholderia].
ACCESSION   WP_175821030
VERSION     WP_175821030.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..177
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=18686
     Region          8..142
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mkklsirrsr trgavavefa lvlmpmimla tgvaefgrai yqyetltkat rdaarylsvw
       61 lptdsaypvs qaqclvvygs ttcgtsgtel vpglttsmvt icdaqhttgc gdasdpsqfa
      121 nlptydsnnn aasgtatgai nvvevkisgy qyqpipaypg lpsitfgniv tvmrqvs
//
LOCUS       WP_175821052             128 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175821052
VERSION     WP_175821052.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 128)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101108
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..128
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=14218
     Region          10..120
                     /region_name="HTH_MerR-like_sg3"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     transcription regulators from the MerR superfamily;
                     cd01282"
                     /db_xref="CDD:133388"
     Site            order(11..13,27,43..45)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133388"
     Site            order(57,60,64..65,74,94,98,104,108,111..112)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133388"
ORIGIN      
        1 mknpppqpll tigklaqltg asvrsirhyd ehgllasvra angyrlfpdn avtqvkqiqr
       61 miatgftldd irgfpdcmll iegarscdqi tdvqrerlea idrqiadlek rrarlvkmlr
      121 dgavppld
//
LOCUS       WP_175821075             403 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar ABC transporter permease [Burkholderia sp. BCC0419].
ACCESSION   WP_175821075
VERSION     WP_175821075.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..403
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42382
     Region          22..403
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mnselssstp atpdadarrp dgraprlalr yaftrykvla llfavvaiwa ffsvltdgaf
       61 vtprnvsnll rqmsitgmla cgmvfviiag eidlsvgsll gllggvaail dvnrhwpvaa
      121 tvpavlalgv liglfngwws tyrrvpsfiv glggmlafrg illgvtggst iapvsdgfvf
      181 igqgylprla gdglavllfv vatllvvrqr gtrrryrlpv aplwqdvaki vgagavlfaf
      241 vatldryggi pvpvllllvl lgvfswiatq tvfgrriyav gsnleatrls gvdtdrvklv
      301 ifalmglmca faglvntarl aagspsagsm geldaiaacf iggtsmrggs gtvygaliga
      361 lvmasldngm smldvdaywq mivkgavlvl avwidvvsrs nrr
//
LOCUS       WP_175821057             476 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0419].
ACCESSION   WP_175821057
VERSION     WP_175821057.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..476
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50871
     Region          40..459
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(50..51,54..55,58,90,140..141,143..145,148,171,
                     174..175,178,287,290..291,294..296,299,328,332,388..389,
                     393,397,413,416..417,420..421,424)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mssidlspvt pvsspirsas dvarlintvd ssvsharmiv llalggvfld aydlttlsyg
       61 iddvarefgl tpaltglvgs aimigtifgs liggwltdri gryqvfmadm lffvvaaiaa
      121 glapnvwvli aarfvmglgv gidlpvamaf laefskfngr gnkasrlaaw cpmwyvassv
      181 cfllifglyf llpaehagwl wraslifgav palviilfrn rfmnesplwa anqgdlanaa
      241 rilresygih aheaadarre pspppvrirv lfqrpylgrt ivasvmnlci pfeytaiaff
      301 lpsilsqflg agvfetiaas lalnvlfaft ggllgmrlay rypsrhvaia gfalqtvalv
      361 alalaghphg alavgvvllm lgtwlfaegf gpgaqmmiyp tlsypaairg tgvgfgrslc
      421 gigqalalfv lpilqarlgt dmfwvvaisa vtpivflliv ryeptaydvd desvaa
//
LOCUS       WP_175821135             198 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175821135
VERSION     WP_175821135.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21204
     Region          22..172
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 manpagvgrp refelgdaar damdvfwdrg yegaslpdlm agtglsrgsl ykafgdkkal
       61 llaaldlyma dglkatadil sqpgavkdai rdsllryarl svgeagrrgc lavamttela
      121 ardadvaert grmfrrlqql yagaivrgqa sgeiaeqdeq vlarllvcqi egmrvlgktg
      181 vpeddmlalv drtmrild
//
LOCUS       WP_175821127             448 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0419].
ACCESSION   WP_175821127
VERSION     WP_175821127.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..448
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48432
     Region          27..434
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(40..41,44..45,48,80,139..140,142..144,147,167,
                     170..171,174,268,271..272,275..277,280,308,312,363..364,
                     368,372,388,391..392,395..396,399)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mpsltqaaaa paaadsseda lyrkvmrril pllllcyvva yldrvnvgfa klqmlddlsl
       61 sdsvyalgas vffwgyflfe mpsnlllhry garfwiarim itwgivsssm afivplaqff
      121 hvqtttmfyt lrfllglcea gffpgvilym nywfparrqs vamsgflvai plsltlgsvl
      181 sgwlmeqthg lsgmsgwqwm llleglpsiv vafivlaclg dgpqsakwls adekavlsrn
      241 leseaahksh sigaalrspr vwlltfillt fntgfyglaf wlpsiirasg vhsplhigll
      301 taipyltaif amvwnashsr rtgerrlhaa ipaliggvcl ilsaafahnv alsivfltia
      361 tcgilalmpi ywtfpgqils gtaaaagial insvgnlsgf tgsmitgvak qmtgdinngt
      421 yalgacllis cvliasiprd ilrppvgr
//
LOCUS       WP_175821156             244 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175821156
VERSION     WP_175821156.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..244
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25361
     Region          127..235
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 mtavfvlhra dgapsstafs kqafgasdpf aahreiaweg pdamaagris fvgalnvpsf
       61 phietlvvve geltleaaga aplvlgpgqg avigcgtalr iaaqspvllt fcsaacetpt
      121 kqglfalhad adfkpsatlp aevllgpapq crsdnvftdd gagycagtwd stpyhrivrp
      181 hranefmfll dggvrfaapd gselslgagd alfvprgasi gwesservak fyvmqtvkps
      241 terd
//
LOCUS       WP_175821184             465 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0419].
ACCESSION   WP_175821184
VERSION     WP_175821184.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..465
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46506
     Region          27..459
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,153,
                     156..157,160,283,286..287,290..292,295,323,327,378..379,
                     383,387,403,406..407,410..411,414)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msgggaapaa gayasatarp vlvmvalacg fvmamldvti vnvalkamat slsmsltalv
       61 wvvdaytlsf aallllggal anrygskavy vaglalfvga svlcaaaqss galvaarlaq
      121 gvgaalfmps slslltlafp pgplrtrmig iwgalvsaam algpcvggvl vdaigwrgif
      181 wvnlpvgiag lwltyrhiar aprhpgplna lghlfgalal aalsftlieg psagwsspsi
      241 iagvaatlaa taafalrery agsrilspal lanrrfvags tlglainfgi laeifllsly
      301 lqnvrgasal vagfelfplm amfgignlas akvsarlgar rtlltglala algsvalvgv
      361 aampypvlai avglanfgag qaipamnlvv mqsadaadan laaaslnasr qigslvgiai
      421 asvilhvvdd pdrataagfa viaalyalgf aivfraihag gaeqp
//
LOCUS       WP_175821188             297 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            sp. BCC0419].
ACCESSION   WP_175821188
VERSION     WP_175821188.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 297)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..297
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30436
     Region          1..296
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mlsfivdvli rtadlllvsv glstlyslir fpniahvqya mlgafatlwl eraglpfala
       61 tavscalvga aatllnlfvf arllrsgsav amigslaism lavalvlgva gsrpqqyaqd
      121 vhppmviagv alsvpqlssi acgagalaif aallyrtglg ramralasnr alalatgida
      181 trvtnvitfa sgvlaalggt mlgatesvhv nlgygllipv fsaailgglg nplgaaagal
      241 liavaetval nvdfgglvdr pmqffpveyv gavsfaillv alifrpygif drevrrv
//
LOCUS       WP_175821212             233 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175821212
VERSION     WP_175821212.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..233
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26302
     Region          31..182
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkaksanlae srkkvvtrkr akpapkasvq rlpraerqar vlakaaeyfs eygltvqtra
       61 iadacgisqr llyrlfpska alleevyqre iaggfkavwf vqlkdrsrsl qerlnafycd
      121 yydsvltrrw lrlflyasla eyrmapnytd svvahsleii meevahttgl plpadahrta
      181 eigwqlhgav shlairrhiy fnenptpphe viamhvqafl nsvplllqaa vla
//
LOCUS       WP_175821217             164 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175821217
VERSION     WP_175821217.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..164
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=17777
     Region          3..157
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 meketftliv nnvryevcse prkllsdvlr edcrltgthv gcehgvcgac tvlidgtpar
       61 scltfavqad earittveai aldgrlsplq ralhechglq cgfctpgivt tfeawlrehp
      121 apteaevraa lsgnlcrctg yqqivrailq aaaemrgear hakn
//
LOCUS       WP_175821231             319 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Burkholderia sp. BCC0419].
ACCESSION   WP_175821231
VERSION     WP_175821231.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442595
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..319
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34401
     Region          5..295
                     /region_name="AKR_unchar"
                     /note="uncharacterized aldo-keto reductase (AKR)
                     superfamily protein; cd19103"
                     /db_xref="CDD:381329"
     Site            order(14..16,54,59,85,120..121,147..148,172,201..207,255,
                     270..275,278,281..282)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381329"
     Site            order(54,59,85,120)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381329"
ORIGIN      
        1 mttdnpktpt ialgtwawgd sgeagagyfg ssltqaglea vadkahaagf nlwdtamvyg
       61 mgrsetvlge vlkrfarsdy qlstkftpqa agagadpvad mleqslarlg tdyidlywih
      121 npadvarwtp hlipllesgk ikhvgvsnhn lseieqadri lgeagfrvea iqnhysllyr
      181 dseragildy crdrgipffa ymvleqgals gkygpahplp egsnraqtyn rmlprlkalt
      241 dtlaaigrkr gaaapdvata waiakgttpi vgvtrpdhvh glvrassitl aadeiaelea
      301 ladaadvntr gwweqemrv
//
LOCUS       WP_175821259             370 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF917 domain-containing protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175821259
VERSION     WP_175821259.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..370
                     /product="DUF917 domain-containing protein"
                     /calculated_mol_wt=39433
     Region          1..361
                     /region_name="COG3535"
                     /note="Uncharacterized conserved protein, DUF917 family
                     [Function unknown]"
                     /db_xref="CDD:442756"
ORIGIN      
        1 mttlfdavts qdvargavfl gtggggdpyv gelflrkqla aglqprlipv dalpddafvv
       61 avagigaptv lvehlvseaa lrkllkdaea myghpldaii saeigganam fplavsamtg
      121 lpvvdgdgvg ravphiemtt fsihgcpacp avfaddlgnh avvhavddrt aeaitraltt
      181 alngcvygvl ypmsgadvkr cavqgtvtqa leigrhirls rhtssepvae ivryldtrdd
      241 grrarllfvg kvsdvlhetr dgfhwgrlti eaigdrdnrm iieiqneflv arhngrtvav
      301 vpdllsvldt etaepltaem lrygarvsvv ayeapaallt aqslevlgpr qfglqdtwkp
      361 fmdetdaprt
//
LOCUS       WP_175821279             343 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175821279
VERSION     WP_175821279.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..343
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36729
     Region          23..326
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 msfsflparr alaatltaal afagavipqt ahaegriria eqfgvvylml nvardqqlie
       61 kegrkagldi kvdwvrlsgg aavndallsg avdvagagvg plltvwdrtr grqnvkgvas
      121 lgnfpyylvs snpnvktiad lsakdriavp avgvsvqsrv lqyaaakqwg dkqfdkldal
      181 tqaiphpdat aailansnvi tghfgnppfq eqelagnpna hivlnsydvl ggpssatvly
      241 atekfrddnp ktyrafvaal adaarqiaad peraadtyir vnaskidral llkilrnpqv
      301 qfktapqntl plaqfmhrtg airnepkswr dyffddpata ggs
//
LOCUS       WP_175821281             296 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175821281
VERSION     WP_175821281.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..296
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33657
     Region          1..>174
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          91..281
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,103,142,156,158,217,234,261)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(105..106,108..109,112,116,118..124,185,211..215,
                     222..223,226)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdlnavemfv tvvqagslsa aasrtgvplp tlsrrmrele kqlnvqller svrgtkltda
       61 gvrlyehasr giealaeake avvsaqhqlk gflrislppt fdiwwdllaa fqmrfpgirl
      121 fvytterrvd livdgidval rvgtiehesm varkilryrh rlvaspalle qygypstped
      181 lhllpcatwg laaymqpvwh lgdtpfhprp lfstndyahl rrralaghva telppflvde
      241 dlraqrlval ldayplqeqe inllypshrh pssvvrayle fcqeywkdpv radlyr
//
LOCUS       WP_175821289             306 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175821289
VERSION     WP_175821289.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 306)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 306)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 306)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..306
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32920
     Region          2..182
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          214..297
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdplsevlsl letrdsiftg lraggpwavd lpppdgikfn avvegscwlt vdgagppvrl
       61 hagdcfllaa prafslasdp svapvpvadv yrhvehgiah ygepadcfli ggrfayeegm
      121 plllgnlppv vivsgdsepa avlrwslqql arefgasspg gslmvrhlgh mmlvqilrry
      181 vdagangdvg wlagfadsrv saalaaihaa perrwtvdal aacchvsrst falhfkrrlg
      241 fgpleyvlrw riqlamrelr rsnasisaia qrlgydsdsa fghafkrivg csprayrhdv
      301 tnests
//
LOCUS       WP_175821290             176 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175821290
VERSION     WP_175821290.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..176
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=19278
     Region          47..172
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mttlndylaq krdawhakqq aarndpdfka tplkatvral grsgvreiri rdfqvisdsp
       61 pdfagynlgp aspelqlgvl gsclthitli qaaerglkid aievevtgdq hplaqqpgfe
      121 hvpvfphnir ytldivspep peairalhqa veavcpifnl lrlpqnidge lrhtsg
//
LOCUS       WP_175821295             255 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0419].
ACCESSION   WP_175821295
VERSION     WP_175821295.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..255
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=27732
     Region          3..235
                     /region_name="ArtM"
                     /note="ABC-type arginine/histidine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4160"
                     /db_xref="CDD:443325"
ORIGIN      
        1 mifslpflld tvmpkllaav pttlaltlvs gaasvllgvp lalaagarht plrwsarswl
       61 mlirgtpllv qlyllyygfg qivprewmrd swaspllrda fwyaivalsv nesayvatil
      121 rgaiagvpag eieaghaygm trmqvlrriv gprawrlalp altgeailll kstvlastvt
      181 vfdvmgtant lrfetlrvye plagaaivyv vlvalltipa arleqrvnry ltrvpddrmp
      241 arrrrassga waapn
//
LOCUS       WP_175821343             371 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia sp. BCC0419].
ACCESSION   WP_175821343
VERSION     WP_175821343.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..371
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39748
     Region          3..348
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,57,99,231,302,322,324..326)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,57,99,101,108,179,182,184,231,238,302,322,
                     324..325)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,101,179,182,184,325)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            184
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mntlftptqv gpyplahrvv mapltrmrtd ahnvpgdlmv dyyaqrassg gllisdatsv
       61 splgfayvga pgiytkahah gwrrvvdavh akggrifvql whagrqahpa nigaalpvap
      121 savrarehsa ihdengqvie veqvlprala ldeipgviee frhaaalakq agfdgvelha
      181 angylpdqfl rdgsnhrtda yggslenrar flfevldaig svweagriav rlspgssygt
      241 mcdsdphatf gyvarrldgy glaylhvvep rvrgnddvaa aasavsakdl rrvfkgtlia
      301 aggftadsah rmieagdadl vafgrlfisn pdlperlrvg aplnrydrst fyggdargyt
      361 dysfhgaapv i
//
LOCUS       WP_175821296             244 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0419].
ACCESSION   WP_175821296
VERSION     WP_175821296.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..244
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=25546
     Region          6..242
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 maaddsllal lafgdggygr vfasafaltf gvaaasfctg vllgiagalg klsryaalaw
       61 lvrlyttlvr alpellclll afyavapave nalrgsgivs sdfafdpfvv aalslgfiqg
      121 ayltdifraa lvnvpvgqie aahaygmtpw qtfarirlpa aarlalpgvg nvwlnatkda
      181 sfisvlgsft dllkasqlaa gatrhyvffy lvtaslflll sitstglfaa lerhanrgtr
      241 ratt
//
LOCUS       WP_175821433             953 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175821433
VERSION     WP_175821433.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 953)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 953)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 953)
  AUTHORS   Ingmer,H., Vogensen,F.K., Hammer,K. and Kilstrup,M.
  TITLE     Disruption and analysis of the clpB, clpC, and clpE genes in
            Lactococcus lactis: ClpE, a new Clp family in gram-positive
            bacteria
  JOURNAL   J Bacteriol 181 (7), 2075-2083 (1999)
   PUBMED   10094684
REFERENCE   4  (residues 1 to 953)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11909043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..953
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..953
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=104043
     Region          4..>54
                     /region_name="McsA"
                     /note="Protein-arginine kinase activator protein McsA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3880"
                     /db_xref="CDD:443088"
     Region          83..877
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mpalcdicha rpavaratvm qdgerktisi cdyhfrqlmr hqsmlnpfds llggggpssl
       61 fgglgdespl aaeipresvd ptdafseqtl ellqraaeka helhrselds ehllyaladt
      121 dvcaallkel klspediksy idahahtgta dpdapldkls isprvkkavq yafqasrdlg
      181 hsyigpehll iglasvpdsv agtllkkygv tpealrqkvv kvvgkgaedg rvdaptgtpn
      241 ldkfgrdlta iarqgkldpv lgraqeiest ievlarrkkn npvligepgv gktaivegla
      301 qrivngdvpe vlrnkrlvev ninsmvagak yrgefeerak qlidevtakq delilfidel
      361 htivgagqgg geggldianv lkpalargel sligattlne yqkyiekdaa lerrfqpvfv
      421 pepsveqtiv ilrglrdsle ahhqvtfadd afvaaaefad ryitsrflpd kaidlidqaa
      481 arvrigatsr pidiqegeaq iaqlkreqdy atsrkrfdea kqfeeqinak qkavdemmea
      541 wqrktgsetl evtvesvaev vsrltgipvs eltqeerqkl lkmeeqlrer vvgqsdavva
      601 vsdavrlsra glgqthrpia tflflgptgv gktelakala etvfgdeqai iridmseyme
      661 rhavarliga ppgyvgydeg gqltervrrr pysvilldei ekahpdvynv llqvfddgrl
      721 tdgkgrvvdf sntiiiatsn lgaaiimdnl tqpeaarktd kaireelmqv lkghfrpefl
      781 nridevivfh alskddirai vqiqldrvvr taaaqditlv mgdslvahlt eagyqpefga
      841 relkrqirqs ietklakeil adrlksgdkc evdydkdsde vtfntlaape akeakdtkda
      901 kdakqdadgk pksngkaaka agdtkpddap adapppaakp sgkkssgakk dah
//
LOCUS       WP_175821439             145 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175821439
VERSION     WP_175821439.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..145
                     /product="RidA family protein"
                     /calculated_mol_wt=16102
     Region          28..137
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 msqpthtrir mfntkdtypn qtldndlcqa vragntvyvr gqvgtdfdgn liglgdaraq
       61 aeqamknvkq lleeagsdit hvvktttyli dpryrepvyq evgkwlkgvy pistglvvsa
      121 lgqpqwlmei dviavipdnw qpnra
//
LOCUS       WP_175821472             210 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia sp. BCC0419].
ACCESSION   WP_175821472
VERSION     WP_175821472.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..210
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23131
     Region          1..210
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mtrvlyiegs pnkahsasie vcdafldayr hahpdheirk ldiwdlpmpe fdgaalaaky
       61 aglsgtaltp eqaaawqqie rlaapfhead kflfgvplwn fsipyklkhl idvisqkdvl
      121 ftfdaagftg klagkkaavv yarglayqsp gsftpaaefd lqrpymetwl kfvgvtditg
      181 ivvertlfgp dgkvdrsrai dearaiartf
//
LOCUS       WP_175821514             430 aa            linear   BCT 11-JAN-2025
DEFINITION  NRAMP family divalent metal transporter [Burkholderia sp. BCC0419].
ACCESSION   WP_175821514
VERSION     WP_175821514.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..430
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45785
     Region          22..430
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 msgidedarp aaeapppaak pwyrrlgpgl lagasdadps nvavyaqags qfgfnmlwmi
       61 vvtlpmmvav qlaaafigrr nreglvagir ehfsdrvart liamvvivnv vnvgadlaam
      121 gdatalvvgg rsywyaplyg iaslalqvml syeryarwlk wmtlgliayv lelgfvhvdw
      181 agvlhaivlp qiafthayat tavavlgttl spylfvwqaa leveettaeq qngerdtrre
      241 teqritvdtw tgmivtnavs fcimvigaav ffahgrhdig staqaaealr piageaallv
      301 fafgivgcgl laipafagsa aygcaeawrf reglnepvrr apafytvlal cvivgiaicf
      361 spidpiraly wsavlngiaa vpmlvlvmll sqkrdaagqp gsgpvsklfg wlavalmaas
      421 vvtmlvdvlt
//
LOCUS       WP_175821515             283 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175821515
VERSION     WP_175821515.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..283
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=31910
     Region          165..>243
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mqrrypgrhg erggppdwqa rnerayrgag ergipddpar wpeeddesay rrfasedvgp
       61 edwgsewter aarpvdqrrg gadpdwpggv rqpardperg yggpgrraeg regryggerp
      121 efrgqhrmgg yggergiddp ryggrapdls rfgseaerda lrqrrgpkgy trsderired
      181 vcerlahale idvsdvsvqv negrvelegt vparwmrhdi edladgcmgv rdvenrvrvr
      241 rdgehdtgmv lhpdqrtitp tqpaardpep gtvvpgrere prh
//
LOCUS       WP_175821565             139 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175821565
VERSION     WP_175821565.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..139
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14790
     Region          27..138
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mtpnqpflas qrdvllllar illvilfvmf gwkkivdfsg tiafmgsega papivsaais
       61 vvmelfvgia ilvgfqtrpl alllalytig tgiighhywt mtggeqinnm ihfykniais
      121 ggllalcaag pgrfsidrg
//
LOCUS       WP_175821567             539 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia sp. BCC0419].
ACCESSION   WP_175821567
VERSION     WP_175821567.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..539
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=59559
     Region          6..538
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 madtdtqkad ivvvgsgvag aivahqlama gksvilleag prmprweive rfrnqadktd
       61 fmapypsspw aphpeygppn dylvlkgehk fnsqyiravg gttwhwaasa wrfipndfkm
      121 ktvygvgrdw piqyddlehy yqraeeelgv wgpgpeedly sprkqaypmp plplsfneqt
      181 iksalngydp kfhvvtepva rnsrpydgrp tccgnnncmp icpigamyng ivhvekaeqa
      241 gaklidsavv ykletgpdkr ivaaiykdkt gadhrvegky fviaangiet pkillmsanr
      301 dfpngvanss dmvgrnlmdh pgtgvsfyan eklwpgrgpq emtsligfrd gpfrateaak
      361 kihlsnmsrv nqetqkifka gklmkheeld aqirdrsarf vqfdcfheil pqpgnrivps
      421 ktatdaigip rpeityaidd yvkrgavhtr evyataakvl ggtdvvfnde fapnnhitga
      481 timgadards vvdkdcrtfd hpnlfissss tmptvgtvnv tltiaalalr msdtlkkev
//
LOCUS       WP_175821582             556 aa            linear   BCT 11-JAN-2025
DEFINITION  S8 family peptidase [Burkholderia sp. BCC0419].
ACCESSION   WP_175821582
VERSION     WP_175821582.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..556
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55745
     Region          243..523
                     /region_name="Peptidases_S8_13"
                     /note="Peptidase S8 family domain, uncharacterized
                     subfamily 13; cd07496"
                     /db_xref="CDD:173820"
     Site            order(250,319,323,390..392,418,420..421,491)
                     /site_type="active"
                     /db_xref="CDD:173820"
     Site            order(250,319,491)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173820"
ORIGIN      
        1 mkakrfnfal arpaharmla gmlsaaallp lagcgggggd gsnpsssnaa papapaptpt
       61 ptpapapapt tppvssgtna ctsqqaavqm aaqtapvepp vdhlivklkt ltatramaai
      121 dngsrldavi qramtrwtap vagsarayas tvpqtpvnvq vertisngaa vlslgqrmaa
      181 tdaaalaqaf aadsdvdyae pdhpmqirdt psdplynqqw ylsdatagid lppawnvtkg
      241 sptvvtavld tgyrphgdlt gnliqqgysf isnvntsnng ltrssdatdp gdwvtqqeld
      301 nasgpfyhca sqpsnsswhg trvmgvigat anngagvagv swlskilpvr vlgkcggvts
      361 diadgmrwaa gipvngvpnn pnpakiinls lggvgacstt fqqaiddvta kgvtvvvaag
      421 ndglstgldq pancrgvitv gatdatgrra sfsnfgtdvs lsapgvnils tsntgtttpg
      481 sdtyglangt slaapqvtgv aalmlsvngn ltpaqilqkl qggtraakla agtsctalpa
      541 gsgildagaa vatanq
//
LOCUS       WP_175821597             306 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: bestrophin family protein [unclassified
            Burkholderia].
ACCESSION   WP_175821597
VERSION     WP_175821597.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..306
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33442
     Region          1..299
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 mivrprehwl rmllvwngsv lptilpqlvl tlaislvavw gggrvlgekv plnptpftli
       61 gltlaifagf rnnasyeryr egrqlwggvl tatrtlvsqa lcygavdrdd asrrafvrtv
      121 vafvyalkhq lrgtdpaadl rglldgatha rvaasrfrpv vivhalreaf aaradaghla
      181 dtrlwmldar ldelvamvsg ceriastpip fsydvllhrt iyaycvllpf glvdsigaat
      241 pfvtvfvayt lialdaiaha iaepfgdgpn hlaldamtrq iertllelnr eplpaevtpg
      301 psyrlt
//
LOCUS       WP_175821646             111 aa            linear   BCT 11-JAN-2025
DEFINITION  FmdB family zinc ribbon protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175821646
VERSION     WP_175821646.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..111
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11370
     Region          1..74
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 mpiydfecan cgpfsvmrri adrekpcccp dcgaeggrvv sapslalmgg arraahatne
       61 raahaprqsg dgpplrhrag csccsggaak lagaapdglk rpagrpwmis h
//
LOCUS       WP_175821624             252 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia sp. BCC0419].
ACCESSION   WP_175821624
VERSION     WP_175821624.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..252
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26148
     Region          1..245
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 msvskkfaav tgagsgigra aaialaqagf tvallgrtea slretqdair aaggdaqvfp
       61 advtdeasvd hafaqiaqrf grldvlfnna grnapvvsld ayeldvwnsv vatnltgvfl
      121 caraawrlmk tqtpqggrii nngsisahap rpdtiaytat khavtgitks laldgrryni
      181 acgqidigna atsltermtq gvpqadgsla pearmdvahv anavvqmanl pldtnilnmt
      241 imatampfvg rg
//
LOCUS       WP_175821640             466 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0419].
ACCESSION   WP_175821640
VERSION     WP_175821640.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..466
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48542
     Region          17..413
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,142,
                     145..146,149,273,276..277,280..282,285,313,317,369..370,
                     374,378,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mpspskhhal lvqvaaclgf vvvlvdvsvv nvaldtlria fgadvtdlqw vvnayalvfa
       61 sllliagalg drlgakhvfi agyaiftlss igcgltqsmr aliewrlvqg igaallvpns
      121 lavlrlafqd ttarsraigw wgagggiala agplvggllv agigwrsifl vnvpvgvagi
      181 wltwrfapet kaqrgrsldl pgqltgafal aaltfastev salgwssplv lgafalcigl
      241 sivfirlear npaamlpsal wqdrtvrsat vigmianlvf ygivftlsll fqsvwhmtpv
      301 rsgvallpmm gilmlmniva grlasrlgar tlatvgllis aagylamwpa iaaesfwlla
      361 vpmllagsgi altiptitaa tltavssahs gvasgllnaa rqvggvmgva ifgffvrqta
      421 wvpfmhgmer alvvsvlllv vgaatawrnl ghtpavarrq kgrsps
//
LOCUS       WP_175821681             293 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175821681
VERSION     WP_175821681.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..293
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32442
     Region          13..153
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mpahplpplt lhgvdhtarp twrlretvef yrdklglplv hvisargwgp athpdflhff
       61 fdsgngstia ffyylgsdep aemaarasar plpddhvada thtawlvdgp dalrawkrhl
      121 daqgldvsve trheviesvy vrdpngyfve fthklrplaa vdatdaqltl eaamtledaa
      181 raagrpldsv daiwnrkael vaergdaata pvrisvprva efaplvraal qhpdcrvheg
      241 keydsieadg pieferralg fkpalwygml tgglhgrier fdrdvlriap vrs
//
LOCUS       WP_175821727             414 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia sp. BCC0419].
ACCESSION   WP_175821727
VERSION     WP_175821727.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..414
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43981
     Region          12..414
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mteantpaqp apstvvvigg gqaagwvlkt lraegfagrl vmiadephlp yerpplskav
       61 lagdadietv rvvrsdefda lnveawqper aasidrarrv vktesgrqie ydrlviatgg
      121 tsrrlpdaiv ntpnlhylrt ldeaaalgek lrasrrvlvi gggwigleva atarklgvea
      181 vvvegaprlc grsvpqivsd flldlhrsng vdvrtgaala sldpqpndas kvratladgt
      241 tidadfavag iglalnasla sdaglalddg ivvdeygats dpaifacgdv anhhngwlkr
      301 rvrleswana qnqaiaaaka vlgvrapyae ipwfwsdqyd vnlqilgdlp adaqlvvrgd
      361 laarratlff lgdghvrgvi avnnarelkl arkwmnqgra vdtealadtt rala
//
LOCUS       WP_175821746             514 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175821746
VERSION     WP_175821746.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..514
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52088
     Region          90..493
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrrpeppaas iavaalatav alagcatssi dlapeasdrp wqpqtsaagd ivaapprasa
       61 qgahdytlpa spalasisap aaldaahayt lpelidlaes anpltriawn darnaalavg
      121 laksaylprl satamgayqa nhgststilg dsssnttvhg tisalslqwl lfdfggraar
      181 veaaeqasia snvaftavhq qvihdvtvsy yryeaarsra lsaqqgltna dailaasrar
      241 lkhgvgtvve laqatqnraq anlalvqang aesdsylalv salgisplsk ptiaalpkrp
      301 lppalgssvd aivsdaiarr pdlqgafave kanrakikaa qaafmpkifl sastsyasgg
      361 taisalpaig dqaptvnlng srygggvflg vtiplydggl rsailmqarn daesasarlt
      421 rtkeeavrqv vaaqnavqts lashdaakal vdaaqtsyda altayrngvg svtdatiaqs
      481 qllaarnaev dsyagalsaa aalalatgti gsaq
//
LOCUS       WP_175821752             128 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [unclassified Burkholderia].
ACCESSION   WP_175821752
VERSION     WP_175821752.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..128
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14576
     Region          7..122
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mhahlriarp vsnlarterm yrdaldlsvl arfedhdgfs gvilgregld hhfefthcpd
       61 hpiapsptpe dlivfylpdr peweaacera tahgfmpvts fnpyweisgq tfedadgyri
      121 vlqngtwr
//
LOCUS       WP_175821771             292 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175821771
VERSION     WP_175821771.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..292
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32181
     Region          1..276
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mgtsiralll sqmdsftpse qkvaqalldr ypslglgpia qfakqaevsd ptvfrfvvri
       61 gfpnyssfqq alydeidtam nsplarmdaf hsetgmrdsh aaifqrlses lattieglda
      121 aafdaavavl adpdvrvfcg ggrytaplas lfsftltyar phvqyvepnv nlasvaladm
      181 grddvlvifd frryqkdsir faqaahrlga rillitdewr spigefaeiv lriqgrpfam
      241 lqtnvpalal aealvigvtn rlpelarqrm ekieqlnagg iewdtnqrdl pe
//
LOCUS       WP_175821768             430 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia sp. BCC0419].
ACCESSION   WP_175821768
VERSION     WP_175821768.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..430
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=47129
     Region          4..412
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mttptriviv gggiaglqla trlgerlgrs graqitvvdr spthiwkpml htiaagtrdv
       61 qqqqviflah ardhgytyqp gelkgldrar rrvqlgeirs qdgdvvidar eleydvlila
      121 lgsqandfgv pgvrehcyfi dsqqqaetfn ealrmrvfrs iardepfrva ivgagatgve
      181 laaelsrlle vaeaygdetv rerlqltlle sgprilnafp prisasaqrr leqigfhvlt
      241 strvtsadan gfhygdgsfa eadlmvwaag vkapdfmqgl ggldtnranq ivvgptlqat
      301 gdehvfaigd cgsllpdghe rplpptaqva tqqaehlakh lpawldgtpi ppfafhdfga
      361 lvsisdydaf gtlgqfgffr ggfiqgrfaq fshlmlyrrh qqalhgfska tllwiaerin
      421 gwvqprirls
//
LOCUS       WP_175821808             140 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175821808
VERSION     WP_175821808.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..140
                     /product="RidA family protein"
                     /calculated_mol_wt=15262
     Region          1..129
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 maeavnppev wapfgafsma miqgdgrivh lkgqvaldrd gqvvgagdmr aqvrqtldni
       61 rdvlaalggq mrdvislvhy asdidafmqa gdirktyfae pypvtttvqv erlyrpdlli
      121 eiaaiaeipl arfrrplspa
//
LOCUS       WP_175821832             319 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175821832
VERSION     WP_175821832.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18598969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..319
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35517
     Region          1..283
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          15..97
                     /region_name="cupin_MtlR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to MtlR, N-terminal cupin domain; cd06976"
                     /db_xref="CDD:380381"
ORIGIN      
        1 mmhpdlevve vrrdesfkvw shgypyrtir whfhpefelh livathgkyf vgdhigsfgp
       61 ghlvllgpnl phnwvsdmae getverrnlv iqfdpsfvrr cmdafpecrd aqtllddarr
      121 gvgfdaatsa aiaplfdell sargmrrial fmtilerlcg aaertllasp aydqadvtpt
      181 rlshalsyig knlaselres dlaqltgqsv safsrafhrh tgmpfvqyvn rlriesacqm
      241 lladdasitd icfqagfnnv snfnrqfrav kgmapsefra lqrlnarsre lalhaaptgn
      301 plpprvltpg vpelapqpg
//
LOCUS       WP_175821902             312 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175821902
VERSION     WP_175821902.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..312
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33930
     Region          7..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..294
                     /region_name="PBP2_DntR_like_1"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     similar to DntR, which is involved in the catabolism of
                     dinitrotoluene; contains the type 2 periplasmic binding
                     fold; cd08460"
                     /db_xref="CDD:176149"
     Site            order(103,105..106,110,167,204,269)
                     /site_type="other"
                     /note="putative substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:176149"
     Site            order(104,107..108,111..112,115..116,118..119,122..123,
                     125..129,131,193,221..225,228..229,232..233,236)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176149"
ORIGIN      
        1 matsidlnll vvldallsen svvgaanalg lspsalsrsl arlrvmtgdp llvragrdlv
       61 ptpralelrd rvhalvveah svmcpcervd mstlkrtfsi raneafvetf apallehasr
      121 tapdvrlrfa pkpnkhvdal rngdidlevg vigqagpelr vqalfrdrfi gvvradhpla
      181 tgeitpqrfa sfpqvsvsrr gqfngpidtl ldslgivrtv ttvvssfpta lslargsdfv
      241 asvperqter srvgmysftl plpiadltvs qiwhprfdrd pahrwlrdcv rricaprvad
      301 aiapvsqava sm
//
LOCUS       WP_175821915             555 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175821915
VERSION     WP_175821915.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Kane,E.I. and Spratt,D.E.
  TITLE     Structural Insights into Ankyrin Repeat-Containing Proteins and
            Their Influence in Ubiquitylation
  JOURNAL   Int J Mol Sci 22 (2), 609 (2021)
   PUBMED   33435370
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Mosavi,L.K., Cammett,T.J., Desrosiers,D.C. and Peng,Z.Y.
  TITLE     The ankyrin repeat as molecular architecture for protein
            recognition
  JOURNAL   Protein Sci 13 (6), 1435-1448 (2004)
   PUBMED   15152081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12380330
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..555
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=58224
     Region          139..380
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          206..249
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          276..306
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(277,281..282,285..287,289..290,294,297,306,308,310,
                     319..320,323..325,327..328,333,336,345,347,349,353..354,
                     357..359,361..362,366,369,380)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          308..345
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          347..380
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          412..466
                     /region_name="Ank_4"
                     /note="Ankyrin repeats (many copies); pfam13637"
                     /db_xref="CDD:372654"
ORIGIN      
        1 mkklpphahp dhlkkqakal lrlyrqgdad avarfveflp aaanrthdet lalglrlhda
       61 qsciareygf aswadlgvfv ethalarqpr sllirrwldl aygadvtggf daarprvaaq
      121 llldhpdlvs adpaiacaag dldavkaala adpswiarag galklpplva vthsrlgqlp
      181 efaarlraca rhlldagadp nqrignrypp aslaepdesa plsalygaag vnrdpvltam
      241 lldagadpnd geslyhsven pactrllleh garvsgtnal rraldvpdaa alewllahgg
      301 dpnepagegp tkmwgapllr aiavrcparh vaallaagad prartaagvs ayrlamrtgl
      361 sdvaallraa gaeealdaqd afvaacarad addarriqar hrelpgalsd drlrllpdaa
      421 awgscdavkv mvelgwpiaa rggdwdasal nhavfrgdae llafllahga swrdlhgfgs
      481 dalgtlswas inepegvgda dwdacarvll ahgvppavrd psnpdgvlid gramrfseav
      541 tdvllgvdag lpast
//
LOCUS       WP_175821939             129 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175821939
VERSION     WP_175821939.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..129
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=13423
     Region          5..121
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mvtatrlgqp ycveigngrs lvrsdthkdg kggdagmrph ellesalaac vclsvdlaae
       61 ragvtlptct vdvaierldr etgfditvrf aaplseaqqt lvndavsasp vtrtlgkpir
      121 igpatiahd
//
LOCUS       WP_175821941             467 aa            linear   BCT 11-JAN-2025
DEFINITION  HdeD family acid-resistance protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175821941
VERSION     WP_175821941.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..467
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=51307
     Region          10..185
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mvrlvllllg ieylrtrwrg ltvlgwlwva agvgifvdal dgalhfpiel fawlfliegl
       61 atlavagsgv ggqrvlryvk giavvvaagl vfaghhhghf llsmifgtlf lvdgllqcts
      121 awmvryrrwn vafawgvvei llaifffqpy pthyagtvpy clglllmfgg mhmlslaarv
      181 rrltrnpafa tspapalapd lddapdlppf aqsewdgppa dgeraltvhv wtptgtskae
      241 ahrypvidry iaavdvngvi stghaalesp egiyislypg veidrspdef trilratren
      301 dvpglfqpdy ateskawcps tvrvrirnyd pakldafwss yrqnttynlt hrncsstvsn
      361 aleaaldgav wrlkgaragw gafvrllltp elwvaaqirk ravtmawtpg ltldyarals
      421 mladprpfaw wkvarsavsa imasrrawre qdsaalspgg seaasmk
//
LOCUS       WP_175821950             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175821950
VERSION     WP_175821950.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33650
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..291
                     /region_name="PBP2_CrgA_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08475"
                     /db_xref="CDD:176164"
     Site            order(103,107,146,161,163,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176164"
     Site            order(104..105,109..110,112..113,116,120,122..128,190,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176164"
ORIGIN      
        1 mtdrldgvtt fvqvvesgsf alaaerlamt rsavgkaiar lekrlgarll qrttrsqslt
       61 ddgqayydrc vralaeleaa eadldcgrhe argklrlsvp lafghhcvtp ivldlartyp
      121 hlridvsitd rfvdlveegi dlavrigala dstslavrrl gtqygslgaa psylarygmp
      181 ktlddlkhhr tiaysrsgvv qpwdlrapdg stvridmphq lsfddvqaia aagasgfgia
      241 wlpswlldqy vkrgemvvvl drcfvcegdi haiwpktryl prktrcvida laeaippmie
      301 rpdear
//
LOCUS       WP_175821985             433 aa            linear   BCT 11-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175821985
VERSION     WP_175821985.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..433
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46177
     Region          5..431
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 msvnddatfw rnarqhlvry ggtfepmiie rakgsfvyda dgraildfts gqmsavlghs
       61 hpeivsvige yagkldhlfs gmlsrpvvdl atrladitpa gldralllst gaesneaair
      121 maklvtgkye ivgfaqswhg mtgaaasaty sagrkgvgpa svgsfaipap fayrprfern
      181 gaydplaeld yafdlidrqs sgnlaafiae pilssggiie lpegymaalk rkceargmll
      241 ildeaqtgvg rtgtmfacqr dgvtpdiltl sktlgaglpl aamvtsaaie erahelgylf
      301 ytthvsdplp aavglrvldv vqrdglvara nvmgdrlkrg lldlmerfdc igdvrghgll
      361 lgveivkdrr tkepadglga kitrecmnlg lsmnivqlpg mggvfriapp ltvsdeeidl
      421 glslleqaia ral
//
LOCUS       WP_175822011             712 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175822011
VERSION     WP_175822011.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..712
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=77892
     Region          86..706
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msfapnggip nglgggalgs lsalgglagp iassvagslg plaglaghvd tvqramqlaq
       61 tgfslmdktp gaiaeainga atparltqln ryvtldtplg pdvllvsaav vdehvnrlpe
      121 ihldllshrh dlrpedligq qvkirfdqqa rlstlervva sgtgdndryf dgyvasfdra
      181 gnpgnvtqyh ltavpwfwfl trstdcrifq nktaqdilte ifqehgfadf vfdirtsqkp
      241 leyvvmyqes yynfcarlme qeglvwthry ekdkhflvig dtnllfrpid glatvpfaat
      301 easedsgidq lhegrrfgvg kvtfrdfnhq npssplmlve agpqnlkhar ldaterfehq
      361 slydhgddgn ryarfameae eaqahrytgg gyawrmttag avnvanhpvl ennqeyvilh
      421 vrheavndyt qhsaklpyrn sfsllpkkip yrapratpkp vihgtqsaiv vgpkgeeiyt
      481 ngsavkvnfp wdrrgkkdgs dsmwvrvsqp wagdgwgaaa iprikqevlv afnqgdpdnp
      541 vivgrvfnge qgnpyhgaag qtmgiksqth kgqgsneirm tdtngmqeff mhaqkdmntv
      601 vennethkvf gpmrtvlvat gseekqipqg nltetiaekr sttattvevt tpakdggggt
      661 qvhvaergil lkvqnssisl apegirlehn gsvilmtddg vtvngkridl nk
//
LOCUS       WP_175822019             446 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0419].
ACCESSION   WP_175822019
VERSION     WP_175822019.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..446
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47324
     Region          36..436
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(50..51,54..55,58,90,140..141,143..145,148,168,
                     171..172,175,269,272..273,276..278,281,309,313,364..365,
                     369,373,389,392..393,396..397,400)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtnpngaatp rgmqagppah aeavapglda lyarlsrrii plilvcyffg yldrvnvgfa
       61 klqmvtdlhl tdaaygvgag lffvgylllq vpagwlvrri gvkrclagsm ltwgvvsvat
      121 latrdtasfy alrfllgvte asffpaviay fsvwfpshrl akvmaflfla mplgvivggp
      181 lsgwimdath ggfglrgwqw mfvieglpai vlglyllvrv teriddatwl tdtekrmiha
      241 emaqeaagkr thlsaalrep tlwllfatsf lynvgnyglv fwmptmikal gslsnlqigl
      301 vsaipylvas vamvanaqhs vrtgerrwht alpvaiggva llaslgmrah pvlavaclta
      361 gvagimstla mfwslpsril ageaaaggag lvnigaavag fvgptlmgya tgltgstelg
      421 vallaftlfa asalilsipr rlmvrt
//
LOCUS       WP_175822048             203 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175822048
VERSION     WP_175822048.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..203
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22299
     Region          13..177
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msptspgsrd rgrprefdtd evidvaarvf weqgyhatsi dtlceatgvf rgslyrtfgd
       61 khgllvaafd ryaegaiarl kerlaadlpp rqalrdally yteigvrlse rrgcfitnsa
      121 vellpgddal rpyiestllr igtqfslava rgqqsgdfdr nldpeevgrf llcliqgmrv
      181 lgkssaseae lasiveiamr alt
//
LOCUS       WP_175822104             300 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175822104
VERSION     WP_175822104.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33660
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,223,240,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdlesirifl rvvergsfta aatqidmpls rvsrkirqle ddlgvqllyr ttrrvsvtea
       61 grdyyerclr aeeilldadr qvralrtepe gtlrvlvpya iglfelepal aefrrryplv
      121 qlvliydnsa ldlvehgfdv alragvltds gyvarslgws hakfaaspry ldragrphtp
      181 qdladhdilf vgrdtpgltl rltnaagdva dvpvrpvlis nesltvlrqa asgggialis
      241 thfttrrles neleivlpdw hrtddvelha lypkratlds kvrafveflt eiftawrtap
//
LOCUS       WP_175822132             535 aa            linear   BCT 11-JAN-2025
DEFINITION  multicopper oxidase family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175822132
VERSION     WP_175822132.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..535
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=57922
     Region          88..535
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mrrrtflsra igvaaaslfa rtawaqhagh agmagmdsmd dmpgmsgmsg maahaqhgtp
       61 apaalaaada lpagaplatl rtlanesrep gtfratlvaq pvarpllrga kpttfwqfga
      121 gtqgpvvgpl idvregdtve irfvnklpqp stihwhglpv ppdqdgnpsd pvapgasrvy
      181 rftlpkgsag tywyhphphm mtaeqvfrgl agpfvvraad dplagwterh lfvsdlklar
      241 dgtiarndmm dwmngregqf vlvngarrpr idvagderwr vwnacsaryl riafddgraf
      301 ehagtdgglf daprrvtsll iapgeraell vragdrasra vlqaaeydrr kmamshddgh
      361 gslppdpala ladvafapag aralpatlra vpplgepvah ktvafgeemd mdammkgaah
      421 grpagmrfti ngdtyaphra tltsrrgdve rweirnstdm dhpfhlhgtq fqvierasag
      481 srtsepfraw rdtvnvrsge tvsilvtqdm pgermfhchi lehedlgmmg tlkvv
//
LOCUS       WP_175822154             299 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia sp. BCC0419].
ACCESSION   WP_175822154
VERSION     WP_175822154.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..299
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31282
     Region          4..264
                     /region_name="17beta-HSD-like_SDR_c"
                     /note="17beta hydroxysteroid dehydrogenase-like, classical
                     (c) SDRs; cd05374"
                     /db_xref="CDD:187632"
     Site            order(9,11..14,34,63..65,91..94,114,141..143,157,161,190,
                     192..194)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187632"
     Site            order(115,143,157,161)
                     /site_type="active"
                     /db_xref="CDD:187632"
     Site            order(143..145,150,157,188..189,195,217,220)
                     /site_type="other"
                     /note="steroid binding site"
                     /db_xref="CDD:187632"
ORIGIN      
        1 mkevvlvtga ssgfglltaq alaraghtvy asmresagrn aprvaavaay aqehgvdlrs
       61 leldvgddvs vdaaiervia dhgrldvvih naghmvfgpa eaftpeqlaq lydinvvstq
      121 rvnraalphl rgqgrgllvw vssssarggt ppflapyfaa kaamdslavs yaaelarwgi
      181 etsivvpgaf trgtnhflha gkpadtavqa aydsgpyagv adqalkgraa lepadadaga
      241 vataivdiva aphgkrpyrv fvdpsqdgae evfrvgdrir remfrnigla dllaprvdg
//
LOCUS       WP_175822156             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175822156
VERSION     WP_175822156.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32757
     Region          13..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..295
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(106,110,149,163,165,230,247,274)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(107..108,112..113,115..116,119,123,125..131,193,
                     224..228,235..236,239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mgfdsrllsg igvlsaviea gtfarageam gltqpavsra varleervgi rifnrtarai
       61 tltdegrrfy etvapllagi eeaaldagqs karvrgrlrv nvdgtfghyv laprmaefld
      121 rfpdlsveis vrdrmgdlva dgfdvavrfg ipepssyrar llletrvltc aspayvarhg
      181 eprhprdlad ghrcvlirdp vtgrpyewef hrgkevvpfd aggqlmvndt ggllgaclgg
      241 agiaqllely ardivadgkl vlllpewtde tfplyayhha snlvaakvrv fldfvrelma
//
LOCUS       WP_175822173             106 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175822173
VERSION     WP_175822173.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..106
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11396
     Region          8..100
                     /region_name="COG5606"
                     /note="Predicted DNA-binding protein, XRE-type HTH domain
                     [General function prediction only]"
                     /db_xref="CDD:444337"
ORIGIN      
        1 markgnpqgt dnvlldlgfd daeelsakaa lalklnelin qrglsqteaa aitgmtqpkv
       61 sqvrryklqn islerlmqal vsldqhveiv vrpakqthah gitvaa
//
LOCUS       WP_175822256             269 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175822256
VERSION     WP_175822256.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..269
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29464
     Region          19..98
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(44,69)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(51..52,63,66,70..71)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          117..267
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mnqpssapvp pldatparal gefirahrer lspqavglpp gprrrtpglr reevaqlcgv
       61 sptwytwieq grpvsasada lariavalql skaeraylfe laaqrdpaep diaggdlppt
      121 laatvaaiat payvldrqwn alawnapaaa lfsgwldgeh drnllrftfm spaartlivd
      181 wetrarrlaa efradairhl tdaptralid altagsdafa qywasqdvfe regglrefdh
      241 padgrlvyqq itlkpahred lklvvlvrd
//
LOCUS       WP_175821951             379 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175821951
VERSION     WP_175821951.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..379
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41705
     Region          26..362
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 mstpvtnpda faehapevly rvvnrvalit lnrpaalnal syamigelta lfercrhddq
       61 ivavvlrgag ekgfcaggdv ralykmvaqr etwlpffvde yrldyaihtf pkpvvalmdg
      121 vtmgggmgla qgaalrvate rskiampetr iglvpdvgat hflsgmpael elyvgltgam
      181 lsgadalsak ladlcvpsaw ldtfetries vkwdgdvlpa lrkvfeppcn vvphaaldtq
      241 mpwivrhfdk rstverivat ltqdlardel arehrqwlqa tldalashsp tmlavtreal
      301 lrgrqmtlae sfrmelgiva raieegdfre gvrahlvdkd rkprwapasl velraervrh
      361 fltspwklfa hpladlgaa
//
LOCUS       WP_175822318             415 aa            linear   BCT 11-JAN-2025
DEFINITION  lactonase family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175822318
VERSION     WP_175822318.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..415
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44102
     Region          52..411
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 mpnrlrerda rastrgfplr fahwmkgfai vlslsathaf aqqssapadg vynllvgtyt
       61 gggsdgiyvy rfdtktgsva pvssaktvnp syllpsrdgr tvyavnelpg ddrpatqrgg
      121 vsafgfdakt galtfidrvs segndpcyla lspdgkylvt anysvaadpg gsfavlpird
      181 ggavdpavlt vhhegtgpvk grqdgahvhs tvfspdgryl fvqdlgadki ygyrytvdgs
      241 rgligptdtr ytpvkagsgp rhmvfgadgr fayvtselna svevfgyhdg kltpvetvpm
      301 tapgfkgkvg ggaihlspdg rflyvsnrgd andlviyavn kadgrlkhvg rqsslgktpr
      361 eflidptgkw livgnqdsdt fyvfsrdvet gqlganpqkv avgkpvdfkl vpvaq
//
LOCUS       WP_175822266             392 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia sp. BCC0419].
ACCESSION   WP_175822266
VERSION     WP_175822266.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..392
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44697
     Region          7..390
                     /region_name="COG3146"
                     /note="Predicted N-acyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:442380"
ORIGIN      
        1 mkheridyrt gilsspaevp adewnallar daqptpflrh efldalhvar cavddtgwsp
       61 hfvtltdprt grlaaaapvy akqhsygeyv fdwawadayq rndlpyypkl lcavpftpvq
      121 gtrllaaddd arrrlaatll afaeqsdvss lhvlfptgde arllesmgmm lregvqfhwl
      181 ndgyrhfddf latleqkkrk niraerrkvh dagvtfrrlt gdritdadwr ffsrcyrqty
      241 rehfsspyln ldffrtigat mpenlllvia eadgrpiasa lavyrrgehg ggtlygrywg
      301 alehvpclhf etayyqllef cieagldtfe ggaqgehkla rgflptvths ahwlahpafs
      361 davarflere tehihayvde lrehnpfrrg tg
//
LOCUS       WP_175822322             523 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia sp. BCC0419].
ACCESSION   WP_175822322
VERSION     WP_175822322.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..523
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56433
     Region          34..457
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msagpaglth dvpaapfern atmsdsvakp vdatfdqfgl aadilkaiae qgyttptpiq
       61 aqaipvvlag rdvmgaaqtg tgktasfslp iiqrllphas tsasparhpv raliltptre
      121 ladqvaanvh ayakhtslrs avvfggvdmn pqsaelrrgv eiliatpgrl ldhvqqktan
      181 lgqvqilvld eadrmldmgf lpdlqrilnl lpkerqtllf satfsgeikk lastylrnpq
      241 tievarsnst nanvtqivyd vaegdkqaav vqllrdrglk qvivfcnski gasrlarnle
      301 rdgvvasaih gdktqlermq aldafkrgei ealvatdvaa rgldiaelpa vinfdlpfsa
      361 edyvhrigrt gragatgdal slcspnerkq ladieklikr plevqtlrid kparqrhder
      421 ggertgerga erssergger ggrrerdehr gasgrrsgss ergahhrrhe apvddfflkp
      481 yepsasakqp ddaqaaqqpe kkgpkrqvaa llggfgmprk psa
//
LOCUS       WP_175822424             552 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Burkholderia].
ACCESSION   WP_175822424
VERSION     WP_175822424.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..552
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58887
     Region          18..538
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(31..32,35..36,39,77,135..136,138..140,143,163,
                     166..167,170,256,259..260,263..265,268,296,300,464..465,
                     469,473,489,492..493,496..497,500)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 matlggqvsh spmtgeekkv ifasslgtvf ewydfylags laayisksff sgvnptaafi
       61 ftllgfaagf avrpfgaivf grlgdlvgrk htflvtivim gvstfvvgfl pgyasigiaa
      121 pvifiamrll qglalggeyg gaatyvaeha panrrgfyta wiqttatlgl flsllvilgv
      181 rtfigeeafg nwgwrvpfva silllavsvw irlqlnespv flrikaegkt skaplteafg
      241 qwknlkivil aligltagqa vvwytgqfya lffltqtlkv dgasanilia ialligtpff
      301 lffgslsdki grkpiilagc liaaltyfpl fkalthyanp qlelatqkap itvvadpatc
      361 sfqfnpvgts kftsscdiak salskaglny envaapagal aeikvgdtvi qtydgkaada
      421 kaqgaafdkt lastlkgagy pakadpaqln wpmtivilti lviyvtmvyg piaamlvemf
      481 ptrirytsms lpyhigngwf ggflpatafa ivaakgniys glwypivial gtfvigllfv
      541 ketkdsdiya qd
//
LOCUS       WP_175822436             295 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175822436
VERSION     WP_175822436.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..295
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32790
     Region          7..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdellpmrlf vkvaelhsfa raatelnisn ssatrlvmgi edrlgarlln rttrslsltd
       61 aghlylaqir hvieeidrve etiasmhhep igslkiaapv mfgmhvlapa idafkarhpa
      121 ivpevtivdr hvdlvsegfd lglllsqhis nntlvkrpls rihrivcaap hyverhgapa
      181 hphdlashac lafhadfage ylsfdheqtr itvrpnksas snnigllrnw tlsgmgiavl
      241 pdflvqpdld tgrliallpg ylleelemnv aypsrrhfpr karlfvdhli dhfvs
//
LOCUS       WP_175822438             490 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia sp. BCC0419].
ACCESSION   WP_175822438
VERSION     WP_175822438.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..490
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52505
     Region          1..423
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfeslglae plvkavnelg ytsptpiqqq aipavlgggd llagaqtgtg ktagftlpil
       61 qrlhtfyteq rgakravral iltptrelaa qveesvrays kyvklrstvm fggvsinpqi
      121 dalkrgvdiv vatpgrlldh mqqktidlsn ldilvldead rmldmgfihd ikrvlaklpp
      181 krqnllfsat fsdeikalad slldspalie varrnttaes vaqkihpvdr drkrellthl
      241 irehnwfqvl vftrtkhgan rlaeqltkdg isamaihgnk sqsartrala efksntlqvl
      301 vatdiaargi didqlphvvn fdlpnvpedy vhrigrtgra gatgeavslv cvdekqllrd
      361 ierlikreip qeviagfepd pnvkpepiqq rrgqqqprgg gggggggnrq praggsgqpa
      421 akrdgnaqpk agqpkaapqk aakprtqgga gaggnsggrp asggnsarpa sgnaahpnrn
      481 rssrsgqrgh
//
LOCUS       WP_175822440             275 aa            linear   BCT 11-JAN-2025
DEFINITION  ferritin-like domain-containing protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175822440
VERSION     WP_175822440.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10090058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..275
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31790
     Region          44..162
                     /region_name="Ferritin_like"
                     /note="Ferritin-like superfamily of diiron-containing
                     four-helix-bundle proteins; cd00657"
                     /db_xref="CDD:153097"
ORIGIN      
        1 mdtktthvmp wriedidlnr idrqraaane dlllllcass fiesgsdlyt snlseffndd
       61 pevsswlnna weheelqhgr alkayiahvw pefdwdtafa nffaeysktc svdafektra
      121 lemvarcvve tgtatlyrai necsdepvlk eitdnirtde vrhykhffkf fkkynqvegn
      181 grlavlgala rrvmeikned seialrhvfa irypdrvgds qynreraari nslvrrnlsa
      241 dmcvkmllkp ldlpakiqpg vhypltkitr hvflr
//
LOCUS       WP_175822458             295 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: M48 family metallopeptidase [unclassified
            Burkholderia].
ACCESSION   WP_175822458
VERSION     WP_175822458.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..295
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32798
     Region          57..292
                     /region_name="YgjP"
                     /note="UTP pyrophosphatase, metal-dependent hydrolase
                     family [General function prediction only]; COG1451"
                     /db_xref="CDD:441060"
ORIGIN      
        1 mkqrprprpa vvaldhrqmd lplfdgpaaa psapaappap peaapaapld pgpapdrsrv
       61 rtfaldsrvl eyrlkrsarr tigftidgsg lsitaprwvt ladieaaiae kqrwifaklt
      121 ewktrteqra lpqidwrdga qlpylgktvt ialgagavaf dadalrlslp lpvqadmqqi
      181 kdrvqgwlqg eakrifgerl vvyaeklgvt ysmyalssaa trwgscssdg kirlnwrlih
      241 fpmsiidyvv ahelshlrem nhspafwqtv esifpefrea rhtlkhhppe llpsl
//
LOCUS       WP_175822510             254 aa            linear   BCT 11-JAN-2025
DEFINITION  ParA family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175822510
VERSION     WP_175822510.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..254
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28113
     Region          1..253
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mrrvvfnqkg gvgkstivcn laaisasegl htlvidldaq anstryllgd aaadaqpgva
       61 gffetaltfn frpvdvtsfi hatpfdgldv mpahpdldtl hgklesryki yklrdalnel
      121 dmydavyidt ppalnfytrs aliavercli pfdcddfsrr alytllenvk eiqqdhnaal
      181 evegivinqf qpraslpqrl vdelvdeglp vlasrlsasv kireshqqst pvihfepthk
      241 laqefralhr elag
//
LOCUS       WP_175822634             245 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: YoaK family protein [unclassified Burkholderia].
ACCESSION   WP_175822634
VERSION     WP_175822634.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..245
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=25024
     Region          22..>176
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mqpaqvtaag aaapdhlrge dvflasiagy vdtlgfvalf glftahvtgn filigsglag
       61 vgqglmikwl afpafiagiv aarlldhrmr vrghgprars lyalqtilla gfmlagvaas
      121 pignadapat ivcgllgaaa mgvqnahgrl tartvvantv mtgnvtqavi dafdwlvpia
      181 apaereaara rlrrtlppvv gfalgagaga saylyagfwa lalplaalgf ltwrsgrtge
      241 psasr
//
LOCUS       WP_175822579             381 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175822579
VERSION     WP_175822579.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..381
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40591
     Region          1..376
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfqhtedrr mladtlnrfi aeqyafpvrd riarsaegfd ramwqrfael gtvgalfaea
       61 dggfggagfd iavvfeclgr glvvepflga llagralala ggdvhrdrla alidgsasaa
      121 fahdepgshy elttvrtrae ragdgwvltg akgvvdqaaq aaffvvsarv sghdddaagi
      181 glfvvpadap gvslrdykki dggraaevrf drvalpadaa lgapdaldge agaellervl
      241 gygllalsae algamdvake htldylrtrk qfglpigsfq alqhrmadll leveqarsav
      301 inaaaqldap ravreralaa akysigrigt lvaeesiqlh ggigmtwelp lshyakrlvm
      361 idhqlgdedh hlaryialsk q
//
LOCUS       WP_175822572             492 aa            linear   BCT 11-JAN-2025
DEFINITION  ammonium transporter [Burkholderia sp. BCC0419].
ACCESSION   WP_175822572
VERSION     WP_175822572.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..492
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49876
     Region          85..489
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mrkllmsllm agsliaagvg saladdaasa aagstaaast paatasdasa aaapaasapa
       61 adasataaas apaapaapta pfsvdsskis agdtawmlts talvlfmtvp glalfyagmv
      121 rkknvlatvm qsfaitalit vlwtvvgysl aftpgngfig glsrvflhgm ayvkgdkatt
      181 ltvshlasti pesvyfvyqm tfaiitpali cgafadrmkf samlvfmalw slivyvpiah
      241 mvweptgwls adgvldfagg tvvhinagia glvsclvlgk rvgygresma phnlvltmig
      301 asmlwvgwfg fnagsavaad gragfamltt qvatacaalg wmfaewiakg kpsvlgivsg
      361 avaglvaitp aagfvgvaga lvigiaagvi cfwsatwlks klgyddslda fgvhgvggil
      421 galltgvfav kdiggmdgsl llqakgvlit lvysgvlsfv llklidltig lrvteeeere
      481 gldvilhgeh ve
//
LOCUS       WP_175822621             370 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia sp. BCC0419].
ACCESSION   WP_175822621
VERSION     WP_175822621.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..370
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39235
     Region          4..344
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,233,300,320,322..324)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,181,184,186,233,240,300,320,
                     322..323)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,181,184,186,323)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            186
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mssllsaydl rglalpnrvv mgpmtrsrap lrglptelma eyyaqrasag livteatnvs
       61 rasaafeltp glvddaqaag wkivtdavha nggrifaqlw hggrvssltl lggaaplsps
      121 gvnddleqlq vwaqlqngyy tkihatpsra mttdevvatv defrqaaara maagfdgvei
      181 haangylphq flsstlnrrd dryggsvanr arfleeivda vggvmplsrv gvrispyaky
      241 nnvrdadpda tlayvgrmld aagvaylhaa dtngwsgepd lprivdharr sfhgtlivng
      301 gispdaanal idagdadlva farayianpd lveriaarap laepkaagwy ggdragyvdy
      361 arhdaaqsha
//
LOCUS       WP_175822652             298 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175822652
VERSION     WP_175822652.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31447
     Region          3..61
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          90..282
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(100,104,143,157,159,217,234,261)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(101..102,106..107,109..110,113,117,119..125,186,
                     211..215,222..223,226)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdiealrtfv evadaggvsp aalrqglsks ivsrrlagle aelgvqliar strrvaltea
       61 gatfrdyaar acaeidlake tilpagdlcg rlrvaapmsl gpthfapila elarrhprlh
      121 ihasysdrfv dliaegfdca irvgtlqdsn lvarrvgplf gkfvaspnyv sthgspetpq
      181 ellthqalmq gneswqlldg dkvvtvrpqg rfkadsgval vgaavaglgv avlpeylvde
      241 hiasgalvpv mkrhppppag iyvvrpsgqh parkvralte llveclgqda nsagttaa
//
LOCUS       WP_175822660             200 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0419].
ACCESSION   WP_175822660
VERSION     WP_175822660.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..200
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21789
     Region          5..196
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mpiqeallkm smyvslvliv pgptntllls sglkvglrgt wplvvaealg yaiaisvwgf
       61 flsafaagrp wlydvvklas svyifflalk mwthsrvlqd vsiapvrfrd vfvatmmnpk
      121 allfsstlfp leafrsahyf awallvflvv lapigvgwss lgglltsqra waartstllr
      181 gaslvllmfs gtlvysvvnr
//
LOCUS       WP_175822712             357 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia sp. BCC0419].
ACCESSION   WP_175822712
VERSION     WP_175822712.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..357
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=37424
     Region          23..357
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkkarqvvvr vaarrvvgtl gvtaifsagl altsvgahad sgsqvqlygl igtyvgsikr
       61 sdtpqsavlt gsgglttsfw girgkedlgg gvgaifvles ffqpangaqg rsaadpfwsr
      121 nayvgfqgdf gqltfgrqrn paytaeslvn pfgsstvfsp lvlqtfvtsy ggtiigdtvw
      181 nntvkyttpt fkgfgatviy glggvagspg vgnlgvhlny qghgltavls gqrvrytaag
      241 pvraqyayla gaaydfklft lygawamtsd vsaptgshty eaglsipfsp adfllaewar
      301 tkrsgatqaa gslrntmsvg ynhllskrtd iyaiyaydkl sahpigntfa agirhtf
//
LOCUS       WP_175822726             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0419].
ACCESSION   WP_175822726
VERSION     WP_175822726.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22063
     Region          2..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 midfstlalf sgaclaltvt pgpdmllias rsvsqgrrag fatlagiqag tychalaaal
       61 glsqlfvavp laydavrfag aayllylawk tfrsdatals pvasqrrhst atifrqgltt
      121 nllnpkmalf vlalfpqfvr pehgsiavqi lvlatvlnli givvngavil sasrlsqrig
      181 arrrpskvpq yllgsvfvgl aarlavagrn
//
LOCUS       WP_175822755             238 aa            linear   BCT 11-JAN-2025
DEFINITION  outer membrane protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175822755
VERSION     WP_175822755.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..238
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=25654
     Region          80..238
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mikrfalpst lvllfsgaaf adavaapetk kaadasdagy yatgrvigaf dnavnmelts
       61 prvasrvggp etgsnvtgsl glgyqfgngw raegeyvfkr tnnftsywap fdananefhv
      121 saqrlmlngy kdfdlgrgfs vygtlgigva ivsadgwqtn dtrrfasktq tnlaysagag
      181 vsyainkrfs idlgyryvdm gnvetgfntf anrinardeq lksklssnev figlrgrf
//
LOCUS       WP_175822845             370 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175822845
VERSION     WP_175822845.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12117700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..370
                     /product="AraC family transcriptional regulator"
                     /calculated_mol_wt=40963
     Region          63..242
                     /region_name="Arabinose_bd"
                     /note="Arabinose-binding domain of AraC transcription
                     regulator, N-term; pfam12625"
                     /db_xref="CDD:432679"
     Region          292..369
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mtptvalgpl kynavgsidg damtgsdsls arpgrtqpsp satvpislvn gflasagmqr
       61 dgverylrga gipiellgep harvteeqfs tlyrtlaidl ddempgifsr plrggtlkyl
      121 clslldarnl etalhrfgqf fhillddffv eskrdelvaq vllrpndaig pigalgqelm
      181 lklvhgvcsw ligqkipllq iefacprprh avdhlyfftg avqfdcertl mrfsadylda
      241 pirqskrnlg kflarapgdw ifesfseqlv chrvrqylsa alpdlpvidq aaehlhcsvr
      301 tlsrhlaaeg ttfqvlkdel rrdiaiqrlt dtpdtiaaig adigfddpsa fhrafrhwtg
      361 stpgtyrrra
//
LOCUS       WP_175822800             843 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175822800
VERSION     WP_175822800.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 843)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 843)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..843
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=91967
     Region          1..801
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 malfdaprtl sisggalpmy gdrpiltpvk ltggetlgel feytlelktp delgfsqsia
       61 anidldklig teltvsiqie gvghfirgla gntgmaniga gtreitgiis hasilredgr
      121 sivyavtirp wlwlatknce crifqdmsvi eitdavlsay lfpvdkrltp prpnktwpkr
      181 diqrqhhesd wtflqrlwee wgifyffehe erkhrlvlcd aitalkphdd aystiryetp
      241 nsrrideehi halsvsnalt tgavtsvdyd ytrpradltv aredprntgl anqehytwgd
      301 yaqpqagagg lsgarneprt eaeyltlvqm eawrcqglra sgqgnlrglv tgrtfvlshy
      361 pqnaanceya viaarltiee vgeasgsgqr yhceadfvlq pthepfrllr tidkpritgv
      421 eyavvtcpen qeiwtdaygr vklqflwdrl gdndersscw vrvagawhgd qfggiflprr
      481 ghevevafan gdpdlpiivg satnafnmpp fdlpanhtla gyrskevgar rantlafddt
      541 hgkiqahlss degcsqlnlg yitriagnag rqdergrgae lrtdghgvfr aaqgmlltte
      601 arqnarahlt dmgettarle eaerwqstia qlaqqataqd anthqeevaa tlakqnaair
      661 gphdpsddgf pelgaphvvv agaagiqttt patthiasgq hvaltsgehi aasangsvlv
      721 saqdtvrqfa arggmksvaa dgdidiqalq kainllalle vnvtsdaihi kakkklvlng
      781 ggsyieleqg siksgtsgvw lahaathyfp qpdevpvelh vpkvcieclm kaaksgasvv
      841 prl
//
LOCUS       WP_175822859             408 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175822859
VERSION     WP_175822859.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..408
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43993
     Region          1..291
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mrlalvlmgg garaayqvgv lkalaeiare adpqrntlpf avvcgssaga inatsiasha
       61 ddfshgvrrl lefweplrae yvyrtdwlgi aaagarwlat mtfgwaarrs prglldntpl
      121 ahllqrelsf hrieqmlear qlhalaital syssgrhltf yqaaepiqaw rraqrtarlv
      181 dlsashllas saipfvfpav plvldgqiey fgdgsirqia plspaihfga hrivvvgaad
      241 prpeipaang agrprgyptl aqigqqvlas vfldsigsdi eriehinrmi ehlphqievd
      301 sgwrhvdvla iapserieli aakhlkqmpa tmrgllgaig gsqpagasfa syllfeeaft
      361 celielgyrd graqretlag wiahadgssa paagtppedg latgemrv
//
LOCUS       WP_175822876             423 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175822876
VERSION     WP_175822876.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..423
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45241
     Region          67..298
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mafskvlvgw maacalsaaq agtlpsvntg agtrgslaha ehfdygdsnl pqvsadlneq
       61 ilripadasg avtleatlfk pngpgpfplv vfnhgkntgd lhlqprsrpl afarefvrrg
      121 yaviapnrqg fagsdgtyqq egcnvgkngl aqaadvdatv rymsrqpyvd asrivvagts
      181 hgglvsvayg teaaagvrgi infsgglrqd lcdgwqrnlv eafdhygaht avrslwlygd
      241 ndsvwtpalv aqmhdayvsh gtqalfidfg rykddahrli vdrdgvpvww pavhaflael
      301 nlpttvryav adphepkatg yasidavnav pyvdeagreg yrrflnqhps rafavssega
      361 wswaeggddp malaldncak qgagacrlya vndrvvwnat ttqtadngdd htrdadtral
      421 asr
//
LOCUS       WP_175822881             241 aa            linear   BCT 11-JAN-2025
DEFINITION  copper homeostasis protein CutC [Burkholderia sp. BCC0419].
ACCESSION   WP_175822881
VERSION     WP_175822881.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Latorre,M., Olivares,F., Reyes-Jara,A., Lopez,G. and Gonzalez,M.
  TITLE     CutC is induced late during copper exposure and can modify
            intracellular copper content in Enterococcus faecalis
  JOURNAL   Biochem Biophys Res Commun 406 (4), 633-637 (2011)
   PUBMED   21362400
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Li,Y., Du,J., Zhang,P. and Ding,J.
  TITLE     Crystal structure of human copper homeostasis protein CutC reveals
            a potential copper-binding site
  JOURNAL   J Struct Biol 169 (3), 399-405 (2010)
   PUBMED   19878721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..241
                     /product="copper homeostasis protein CutC"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24495
     Region          8..237
                     /region_name="CutC"
                     /note="Copper homeostasis protein CutC [Inorganic ion
                     transport and metabolism]; COG3142"
                     /db_xref="CDD:442376"
ORIGIN      
        1 mnrhaassvl leviattvgd akvaaragad rlelvtaite ggltpsvgli eavvaavpip
       61 vnvivrphsr sfvydaddlr vierdvraav aagangvvfg aldargdvdl galahiaaaa
      121 dgraltfhra fdvardlnaa fdallrvpav tsvltsgghp svldavatit rlvrqaadtt
      181 ctvlagsglt idavgdfvra tgvravhfgs gvrprgevla pvdaqrverv raaldgaash
      241 v
//
LOCUS       WP_175822929             384 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Burkholderia].
ACCESSION   WP_175822929
VERSION     WP_175822929.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..384
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42017
     Region          23..384
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mqsipssaaa rqtqpatapr tqndafvrie nvvkkfgdst avdnvnltia knelfallgs
       61 sgcgkstllr mlagletats gkifvdgedl aslppyrrpv nmmfqsyalf phmtvesnva
      121 fglkqegtpk neirervada lalvqmskya krkphqlsgg qqqrvalars lvkrpkllll
      181 depmsaldkk irqktqlelv niiekvdvtc vmvthdqeea mtmasrlavm segkivqigs
      241 pgevyeypns rfsaefigst nlfegrvved epdhifvesd dletrmyvsh gvtgplgmpv
      301 gisvrpervh vsrekpgskh nwargvvtdi aymgsyslyh vrlpsgktvv snlssshlmn
      361 dgapawnddv fvswspasgv vltq
//
LOCUS       WP_175822978             341 aa            linear   BCT 11-JAN-2025
DEFINITION  XdhC family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175822978
VERSION     WP_175822978.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Leimkuhler,S. and Klipp,W.
  TITLE     Role of XDHC in Molybdenum cofactor insertion into xanthine
            dehydrogenase of Rhodobacter capsulatus
  JOURNAL   J Bacteriol 181 (9), 2745-2751 (1999)
   PUBMED   10217763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449431
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..341
                     /product="XdhC family protein"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=36258
     Region          6..317
                     /region_name="XdhC"
                     /note="Molybdoenzyme maturation factor PaoD (Mo cofactor
                     insertion), XdhC/CoxF family [Posttranslational
                     modification, protein turnover, chaperones]; COG1975"
                     /db_xref="CDD:441578"
ORIGIN      
        1 mesvdldvlk ssarwleegr rvllvtvvkt wgssprpega mlavredglv vgsvsggcie
       61 ddliarvhas giavdarpea lkygvtaeea hrfglpcggt iqlvlepltr dsgiaalcae
      121 veagrlvtrt malatgrasl spaqaadgla fdgerlvtih gpryrmlvig agqlsrylcq
      181 iavgldyqvt vcdpreeytd awdvpgtrvv rtmpddtvld mkldarsavi althdpkldd
      241 lalmealktp afyvgalgsr rnnaarrerl refdlnevel arlhgpagiy igsrtppeia
      301 isilaeitaa knnvslptil qvegakaare iaansgaacg l
//
LOCUS       WP_175822963             319 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: complex I NDUFA9 subunit family protein [unclassified
            Burkholderia].
ACCESSION   WP_175822963
VERSION     WP_175822963.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Parey,K., Wirth,C., Vonck,J. and Zickermann,V.
  TITLE     Respiratory complex I - structure, mechanism and evolution
  JOURNAL   Curr Opin Struct Biol 63, 1-9 (2020)
   PUBMED   32058886
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Babot,M., Birch,A., Labarbuta,P. and Galkin,A.
  TITLE     Characterisation of the active/de-active transition of
            mitochondrial complex I
  JOURNAL   Biochim Biophys Acta 1837 (7), 1083-1092 (2014)
   PUBMED   24569053
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..319
                     /product="complex I NDUFA9 subunit family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0010257 - NADH dehydrogenase complex
                     assembly [Evidence IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=33786
     Region          5..278
                     /region_name="NDUFA9_like_SDR_a"
                     /note="NADH dehydrogenase (ubiquinone) 1 alpha subcomplex,
                     subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs;
                     cd05271"
                     /db_xref="CDD:187579"
     Site            order(10,12..15,34..36,74..76,93,116..118,129,133,
                     156..159)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187579"
     Site            order(129,133)
                     /site_type="active"
                     /db_xref="CDD:187579"
ORIGIN      
        1 mdrqtvallg gtgfigsrlv nalidagkqv rigtrrrdha rhlqmlpvei veldaldtrt
       61 larfvagaqa ainligvlhg grgtpygpgf arahvalpaa laaacvevgv qrvlhmsalg
      121 adshgasmyq rskgdgeaal havaatdsla ltifrpsvvf gpgdaflntf anlqrtvpvl
      181 plampdarfq pvfvgdvvra fvntldlaga hgktyelggp tvytleqlvr ycgtlvgrqa
      241 rivrlpdala rlqasvfecl pgepvltrdn latmsvpnvl sgplapelgi spaslesiap
      301 aylgeatkrs rfdwfrsrr
//
LOCUS       WP_175822991             257 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: phytanoyl-CoA dioxygenase family protein
            [unclassified Burkholderia].
ACCESSION   WP_175822991
VERSION     WP_175822991.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..257
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28587
     Region          12..253
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mssplqsesi raqvaelrer gfvvarglvg eaqcaalrqi aerqlreaae piefeadlry
       61 pgapeskhap gghtvrrlld aysrdpafae raiapeigaw mreyfgeepv lsrahhncmm
      121 tkhpaygslt gwhrdfrywa fersdmvsvw lalgpetnen galwlvpgsh taefgpeafd
      181 dakffrgdlp enrrmidaat cpslqtgdvv ffhsntlhsa gqnrsdqvkf slvytyhgas
      241 nrpvpgtrsa skpevqf
//
LOCUS       WP_175823032             349 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175823032
VERSION     WP_175823032.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..349
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38397
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdhlqsmrvf vkvadlgsfa raasamdisn avatrhvadl egrlgtrlln rttrslslte
       61 sgqvylerar qildeledve qmvvarnhep vgtlrivapv vfglhnlapv lqsytenfpk
      121 vvpdltlvdr qvdlveegfd vgivvtrqmr sasivtrrlt tgcmtvcatp sylekhgvpi
      181 hpeqlaehpa lslpteywgd ervftgpdge vrvrptnviv anntamlrqf allgmgvail
      241 psyligsdia rgalvrllpd frlpqveini aypsrrhlpa kvrtfidhlv ehfshstdat
      301 igeqwaaqga tlppigvemr aeqpestdpn lqprlarspr trvavpspl
//
LOCUS       WP_175823036             204 aa            linear   BCT 11-JAN-2025
DEFINITION  CGNR zinc finger domain-containing protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175823036
VERSION     WP_175823036.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..204
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22545
     Region          12..204
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mvtrsdparh ghewraadfv gghpaldfln tvadtgktrd eeklvdwpav rawagkagll
       61 apddltrllr hprqdgpdel aalhrfrdda yiaiahltae ggggagaras drlavairea
      121 igrsafdavg grfawrpdar aasrwidava lgfehlmrsd dfarvrqcgr ctwffvdrgr
      181 gvgrrwcdmr tcgnrakvea frer
//
LOCUS       WP_175823092             260 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175823092
VERSION     WP_175823092.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..260
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=28380
     Region          14..218
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mlhlhssysa nailaalped siraiaphle lvrikagmld rvgepmrhlh fpttammsvq
       61 hlmedgamve vavvgregvv glgtlvggla assrvevrig gmayrvpscv mraefersaq
      121 tyrlllntcq atmaqiarsa lcnrhhsvse qlsrwlllah dridgdelav tqqtianmlg
      181 vrregvteaa gnlqeaglir qrrgritvld rhglehqace cyelicadyr rllgtrgnam
      241 patvrprmpd ghrgfpahga
//
LOCUS       WP_175823125             344 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175823125
VERSION     WP_175823125.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..344
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37130
     Region          33..328
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mtpttaptpa dapddqrrrl lraagaaala vpaitlgrka wsapplkklt fawnqnafcl
       61 tpivvaqerg ffeknglkve linysgstdq llesiatgka daavgmihrw lkpleagfdv
      121 kiigsshggc vrllgskaag vttlqalkgk tvgvsdlaap gkhffsilla kngvdperdi
      181 twrqypadll gvavdkgeiq aiadgdpnly llekrsngay telatnlsge yarkvccvig
      241 argdlvrndr psaaalarsi vqateythdn pneaakvfak yspkispedl rklyatltyt
      301 hhptnvdlqq eiafyaddfr risvlkkstd pqrfaqqvya nvlg
//
LOCUS       WP_175823145             548 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 32 protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175823145
VERSION     WP_175823145.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 548)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..548
                     /product="glycoside hydrolase family 32 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=59502
     Region          41..536
                     /region_name="SacC"
                     /note="Sucrose-6-phosphate hydrolase SacC, GH32 family
                     [Carbohydrate transport and metabolism]; COG1621"
                     /db_xref="CDD:441228"
ORIGIN      
        1 mkstsfrfsv riirlllvcm actqaaaapc hmqadngdng tpqwrpalhy tpqrnwmndp
       61 nglvyangry hlfyqynplg ndwgnmswgh atstdlvhwr eqpvamrana teeifsgsiv
      121 adtlntsglg tpghtplval ytsvykagsg hapgiqaqsl aysldqgttw qpyahnpvlt
      181 ldpeskefrd pkvswyapgg ywlmttvvad ahvvklyrsd dlvhwsflsd ftlpdvphag
      241 alwempdlvp lpldgdprri kwvmivnvnp wsiaggsgam yfvgnfdgrt fvpdrvapag
      301 sdpaqfrwvd hgadfyaagt fsgapgarpv aiawmsnwdy aakvpttpwr gattlprels
      361 lktidgepsl vvapaaafda wadgrpavhe gdvtvdsatr vlsaatrgvv qritvtlspq
      421 raaraglivr rsadgsigtr ivydtakrtl tldrsqsgea nfagtfsreh ivdlplehgq
      481 lrleivvdrg svevfanggr vtltdlifpp leadrvavfa ergratfagl tvtqletgda
      541 trgacasr
//
LOCUS       WP_175823164             247 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175823164
VERSION     WP_175823164.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..247
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=27001
     Region          34..242
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mhdhsdaaah padtlpepgp lpplatlfgq cawfrtlape hqalvlaqsh veqcdagdvi
       61 aqrlapseyw igvhrgllkl aifnvsgrgc tfsgvpsggw fgegsvikre lrkyevvaiq
      121 rstvlfvpvd tfhalldtsl pftrfvihql nnrmgefias iqnsrlldvd arvaqalaql
      181 fnpalypdtg pslsisqeel gmlvgvsrqr inqalqqlek lgalrlaynq ievvdldala
      241 rfgmeql
//
LOCUS       WP_175823169             218 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0419].
ACCESSION   WP_175823169
VERSION     WP_175823169.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..218
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23156
     Region          1..215
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msfrlylsfv aasavliyap gpvnlltmnq alragwrral pcvwggtlav llqlaltalc
       61 lnslvhldeh altvlrwaga aylvwlggkq wlsrapagaa aapadagaet asaapdtdtg
      121 ralfwrgvat sglnpktllf fpsffpqfis pnadwslnlq ylllaatfal lfaggvasma
      181 lfshrlsrtl qrparmramn rvtggllvgm gaimvgwn
//
LOCUS       WP_175823170             549 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175823170
VERSION     WP_175823170.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..549
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=56361
     Region          15..269
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
     Region          297..546
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mqnhevsadd appkaqrgiq svevggrlld afarrrkplg lselaaaadl staqahtylv
       61 sltrlalvkr daitgnyepg plslrlglms ierqpayrat lphaarlaet vglsvalsvp
      121 gvlgptivri ehggyplhmn lhvgsvmsld ttatgrvfra fgdptqldam aasqagagdt
      181 lagaeggsva pdaeaqhvel dairargier sidrpspgvs gmcvpvfdth grlqlaltvi
      241 gstgsidvdw dgpiaaalrd aarqataslg aaraepapap apgaarvppa laddakaqrg
      301 inaldstgel llalvsagra lplrdlataa gmpaakafph lvslqkigll srddagcfdg
      361 gplaqalgli amqrvsptrd aeaeivalag atdmsvaaat lgplgptvir leesarpqhv
      421 slqvgtvmsl vntaigrifa sgmsddvlad llanepvrla gapavpddaa fcarlaaira
      481 deldfafdap vpgigtiaap vfdhtgsirl viaiigssrg fprgpdsela qtlraatrrl
      541 swrfgwigg
//
LOCUS       WP_175823173             452 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0419].
ACCESSION   WP_175823173
VERSION     WP_175823173.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..452
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48758
     Region          35..438
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(47..48,51..52,55,87,137..138,140..142,145,165,
                     168..169,172,270,273..274,277..279,282,310,314,365..366,
                     370,374,390,393..394,397..398,401)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 msaplqahaa pavasgagst dsagndvlyr rigmrivpfl ficyivsild rsnigfaqlq
       61 mrqdlgltda myslgavlff vgyvlfevps nallrrfgar rtfarimflw gavsvamitv
      121 dsakqfyvlr fllglfeagf fpgvvfylty wyparrrasv lsifyagvav agmvggllsg
      181 wlmrgmsgvl glhgwqwmfa iegapaillg viawfwlcdr pehaswlsdd drqrlaadla
      241 adradapaha aaslrqvlae prtylfafiy fslttallml lfwmplmire fgihdvvhis
      301 llsivpnaig aagliaiarr sdrkrerrrh faacafggav alalltlhpp givammalls
      361 iaamlifaah pvfwavpsay fagagaaggi alissigvss gmitpwivgl irtrtgsmdp
      421 amlmiaallt acavamllgv ratprepaha pr
//
LOCUS       WP_175823199             236 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175823199
VERSION     WP_175823199.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..236
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25523
     Region          8..227
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mpprivppvl kaieqetmad kvyqqlreal msgrfapgqa lslrsvaeav gsstmpvraa
       61 ltrlraeral vdgpnralvv ppmtldmlde lrdvrialeg ciaeracgrm taaqiaavrk
      121 tcetmqahve agrsraylqs nfafhsaiya hgasentlai venlwmrvgp flnmvaldip
      181 hmrrsmdahr aivdalerrd gagvragial diggaahdla etlraeqtpr tvnakp
//
LOCUS       WP_175823214             862 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia sp. BCC0419].
ACCESSION   WP_175823214
VERSION     WP_175823214.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 862)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..862
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=93344
     Region          60..712
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mqpfqpsstr vnrrnvssvr alcarwvara qpvaaaaaar vkplaatawh hvrhptrrgv
       61 lltaaavpal favyvvvlip ftpgigdirk arvdqpaqvl sadgkllaef kpsnrewvsl
      121 kqisphmvda liatedhrfy ehhgldwkrt asaalhtfsg srqggstitq qlarnlypde
      181 igraptltrk vkeaitalki eavyskdqil etylntvpfl ynaygvemaa rtyfdksade
      241 ldvldsatlv gmlkgnsyyn pvlnperalq rrntvlgqmv kygklspaqf aqwqrrplri
      301 dferqkeppg paphfaqqlr kwliawadrn dyniysdgli vrttidsrlq qmatqaltlq
      361 gnqlqgiann awsgrdgcgt dnevfrtfmr espeykaaqd agkddaaamk mlaadrgflh
      421 alckaktdvq agflaidprd gqirawvgsr dftrepfdhv aqarrqpgst fkpfvygaaf
      481 asgmkpddtf idqpveiplk ggeiwrpndd vpptgkpmtl rdavalsrnr itaqvmekvg
      541 pgavarlard mgvrespler vpslalgtsp vtlkemvasy atiangglyv epqmvtrien
      601 rqgevlaeya papperalda etdktlldvm rdvvtrgtgg sirtrfgirg dvagktgttq
      661 dnadgwfilm qpglvagawv gfddgrvtlr sdywgqgahs alpivgdffq raqrarivdt
      721 kakfdtepsp gwfgslrerv tdlfdtwfpp epkkapapvr tqrierpaea degaasaasa
      781 asapdaasgg iveewvpase vaasaaalst gasqpqpqla qpptgastts gssagvgvap
      841 savpapppvp vpaapdatga sq
//
LOCUS       WP_175823285             198 aa            linear   BCT 11-JAN-2025
DEFINITION  YbhB/YbcL family Raf kinase inhibitor-like protein [Burkholderia
            sp. BCC0419].
ACCESSION   WP_175823285
VERSION     WP_175823285.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..198
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=20850
     Region          41..197
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mrvdrritpp apsgrpslfl lpallcaavf aalpahaegp ftvtsddltp garvrpanvf
       61 drgdckganr spqlawrnpp agtrsyavti fdpdapghgw whwavagipa tvtslpadas
      121 asgflrriga searndfgid gyggpcpppg kphryvvtvy alkgtdlris qgrpapmfeh
      181 eigtlsigta qltvtygq
//
LOCUS       WP_175823286             190 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: flavodoxin family protein [unclassified
            Burkholderia].
ACCESSION   WP_175823286
VERSION     WP_175823286.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..190
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=19787
     Region          3..185
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 msnivivyhs gyghtqklae avhagaqdag atarliavge lddagwaald aadaivfgap
       61 tymggpsaqf kqfadatskp wftqkwkdki aagftnsatm ngdkfstiqy fvtlamqhgm
      121 vwvgtgmmpa nskaatrndi nyvggftgll aqspadatpd egplpgdldt akafgqriae
      181 atarwvaggr
//
LOCUS       WP_175823291             211 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0419].
ACCESSION   WP_175823291
VERSION     WP_175823291.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..211
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22201
     Region          1..211
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mnlhtwwlfv atvfvvsaip gpnmllvmth garhglrrss atmagclsal vlmlavsaag
       61 lgavleawpa mfnvlrfaga ayliylgvka wrarvddtsa advdavsqga sasrgvlfrn
      121 gflvagsnpk ailfaaallp qfinaaeptl pqfgilvvtf avievswylv yaafgtriga
      181 tlksqsvakv fnrltgglfv gfgammalvr h
//
LOCUS       WP_175823299             243 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175823299
VERSION     WP_175823299.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..243
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26075
     Region          4..210
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mspillygip agcsfgsiva lewtsrpyrl sritmpglvt sdaflalnpv aetpafvtan
       61 gdvltesiai lghigaqald sglafrqgsa dfdrmnrmla wlnttffsaf galwyvyehd
      121 tegaekaalq aygrgkvlka hrqlealler gegpwllgar rtladayfag iarwadyhav
      181 ferdafplva alrerladda gvqfahaiee nlpppassaf eghvslddal asargivapa
      241 rai
//
LOCUS       WP_175823321             165 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175823321
VERSION     WP_175823321.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..165
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17874
     Region          5..164
                     /region_name="COG3865"
                     /note="Glyoxalase superfamily enzyme, possible
                     3-demethylubiquinone-9 3-methyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:443074"
ORIGIN      
        1 mnsriqritp flwfdrdaea aagfyvsvfd narivhvary gkagahasgn aegavmtvaf
       61 eldgqafval nggpvfqmtp avsfvvnchd qdeidhywar lseggdaraq qcgwlrdrfg
      121 vswqvvpvqm aelmagdpar aervmaqvmt mkkldlgalq raaag
//
LOCUS       WP_175823332             200 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA-3-methyladenine glycosylase I [Burkholderia sp. BCC0419].
ACCESSION   WP_175823332
VERSION     WP_175823332.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..200
                     /product="DNA-3-methyladenine glycosylase I"
                     /EC_number="3.2.2.20"
                     /GO_function="GO:0008725 - DNA-3-methyladenine glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=21993
     Region          3..187
                     /region_name="Tag"
                     /note="3-methyladenine DNA glycosylase Tag [Replication,
                     recombination and repair]; COG2818"
                     /db_xref="CDD:442066"
ORIGIN      
        1 msqrcnwvkt eadahyhdte wgvpshddrh lfemlilega qaglswstil nkragyreaf
       61 adfdvdavar ftpkriekll enpgivrnra kvesavtnar avqrireehg slaaflwsfv
      121 gdtpvqnawq syrnapaste qsdalskalk aygckfvgst icyalmqatg mvndheagcp
      181 chaqcaalgg kqparrrkag
//
LOCUS       WP_175823375             502 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175823375
VERSION     WP_175823375.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..502
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=53946
     Region          3..498
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mnlvaaldra aratpdkpfl vsesatitya aarershraa avlsalgvaa gdrvaamcfn
       61 tpafvdlmfg awrlgaafvp inhklqapev dyvlehsgst allfdvalap vverivhpar
      121 rlvtegeldg vpsfdtmcat mdglagiepa dddiaqilyt sgttgrpkgc vhshrtvtla
      181 amqaalatgi grhertlmam piwhssplnn wfggtlyagg tvvllreyhp lrflqtvere
      241 rvtlyfgapv sytlpldtid gfaafdlssv rawlygggpi gaaqaerlah ayrshaffhv
      301 ygmtetgpag ttlypdeqia kagsigrhgg pgvdlrvvrm dgvdaqpget geiwlktgcm
      361 mlgylddaaa traafapdgw yrtgdiarid qdgylfivdr lkdmivtgge nvyskevedv
      421 lgahpdiaea avvgvphpdw getvvahvvm ranaapdada lrtfcgerla aykvpreftf
      481 vqalprtptg klqkfllrvr ge
//
LOCUS       WP_175823388             325 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [unclassified Burkholderia].
ACCESSION   WP_175823388
VERSION     WP_175823388.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..325
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=34435
     Region          23..319
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mqrkvlygvl laalfaapfi gaypvfvmkv ltfalfaaaf nlligytgll sfghamflat
       61 agyatgyaiq tlgftpelgv lvgtfaatll glvvglfair rqgiyfamit lafaqmvyfi
      121 ylqapfthge dglqgvprgr lfglvdlsnd valyyvvlav ivaacafivr ivhspfgqvl
      181 vaikeneara islgydtdrf kllafilssg laglagslkv lvlgfetlsd ahwtmsglvv
      241 lmtlvggmgt lfgpllgaal ivaledrlgd igewlasttg vawfhslges ttivtglifi
      301 acvlafrrgi vgemvarikp lrass
//
LOCUS       WP_175823426             376 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia sp. BCC0419].
ACCESSION   WP_175823426
VERSION     WP_175823426.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..376
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=40684
     Region          7..376
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkrktlalsi aaaglcagtq ahaqssvqly glmdlsfpty rthadangkh vigmgnegep
       61 wfsgsrwglk gaedigggtk iifrlesefv vangqmedeg qifdrdawvg vederfgklt
      121 agfqntiard aatiygdayg saklsteegg wtnsnnfkqm ifyaagptgt rynngvawkk
      181 lfsngifasa gyqfsnstsf atgsayqaal gynggpfnvs gfynhvnhng frnqtfsvgg
      241 nytfsivrln agyfryngdq galgqrhdds wtvsmkiapk galdyelgyq qmriknaann
      301 adgftpnanl gafsltngva ngfketiygs vfyhlskrte vylagdymkl hggytvsstf
      361 gaknqlelts girtrf
//
LOCUS       WP_175823445             492 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Burkholderia sp. BCC0419].
ACCESSION   WP_175823445
VERSION     WP_175823445.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..492
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51928
     Region          3..487
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mhsdylahda iglaalvrdr qasprellda aigqaeavng ainaivlqdy eaarqraaaa
       61 pepgadtpfa gvpylvkdlg aavaglplsm gsrhyryfvp addspviars raaglnvfgk
      121 tntseigqmp ytepelfgac rnpwnldhtp ggssggagaa vaagivplah asdgggsiri
      181 pasccglfgl kpsrnpvlvd lpsngelvvq havsrsvrds allldvttgq tlppgapgtf
      241 lgaldtppgp lriglvvdpm lapaladdtr aalddaaall eslghhvepa tlpidyaraa
      301 etfltlwati aeemvlgara ltgrtprrge feaatwamav vgrrlartrl pdvlewqrql
      361 tvqvaglvsr ydvilcasla gppvkigelq ptpfesaqmk lvaalpvkpl lkemlaksse
      421 kafawagcte lfnltgqpam svplywnarg lpigvqfaar hadealllrl arqleqarpw
      481 fdrrpplmqa qr
//
LOCUS       WP_175823467             130 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: nuclear transport factor 2 family protein
            [unclassified Burkholderia].
ACCESSION   WP_175823467
VERSION     WP_175823467.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10577308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..130
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=13840
     Region          15..>74
                     /region_name="SnoaL_2"
                     /note="SnoaL-like domain; pfam12680"
                     /db_xref="CDD:432716"
ORIGIN      
        1 mntaqsassv hadlidryfa awnepdvarr ralidatyas daayrdplma gdghagidtm
       61 iaavqqrfpa yrfrrttdvd afgqhlrfsw alvspdgaai vkgsdfgtvd asgrlasvtg
      121 fidempaaas
//
LOCUS       WP_175823493             279 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Burkholderia sp. BCC0419].
ACCESSION   WP_175823493
VERSION     WP_175823493.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 279)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..279
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30182
     Region          33..279
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mlhpvfsarf sagrvarlar lltaallgvv llngaradta plkvgistsp qiealkiaak
       61 eakeqgldvk iveftdwntp naalankdid vnyfqhipfl enakkqggyn fisiapgtim
      121 kiglyskkvk sfaelkdgar vaiandpvng grgllllqra glitlkpgtd yratthdiva
      181 npkhlkiipl easqlarsld dvdlaqgyps fiklagttdp nsallfdgte nknfaiqwvv
      241 rpesandpri rkfisiyqhs pavrkaldna fgslyaiaw
//
LOCUS       WP_175823494             454 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: 2-hydroxycarboxylate transporter family protein
            [unclassified Burkholderia].
ACCESSION   WP_175823494
VERSION     WP_175823494.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..454
                     /product="2-hydroxycarboxylate transporter family protein"
                     /calculated_mol_wt=47782
     Region          28..453
                     /region_name="CitS"
                     /note="Na+/citrate or Na+/malate symporter [Energy
                     production and conversion]; COG3493"
                     /db_xref="CDD:442716"
ORIGIN      
        1 mqtsiqtpsh pepiaaagpa trerfwpagw wklmeirigi iplpvyvilf glivgfvvtg
       61 kvpgeismai avlaffgftc aelgkrlpll rnigaaaifa tfvpsaltyy hvlpkpvlnl
      121 tveftkstnf lylfiasiiv gsilsmdrrv liqgfvkifv plavgsiaaa ivgtavgtal
      181 glgarhtlly ivvpimaggv gegaiplsig yselmhlpqg emfamvlpsv mlgsltaiil
      241 sgaldmlgkr lphltgngrl qvgesgdmtp eneeirghvd vthiagagit aitlylvglm
      301 ahklfglpap vamlflavlv klaravsppl qegafvvykf fstavtypll faigvamtpw
      361 dkltaaftiv nvvtivstva tlmgtgfvvg rllkmypidt aivnachsgq ggtgdvailt
      421 aanrmqlmpf aqiatrigga ivvtvtlilv ahfg
//
LOCUS       WP_175823549             224 aa            linear   BCT 11-JAN-2025
DEFINITION  O-methyltransferase [Burkholderia sp. BCC0419].
ACCESSION   WP_175823549
VERSION     WP_175823549.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..224
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23911
     Region          65..219
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mttlihdpla sllarlfdea dasspatspd fanvsrdeqa rlmrsktdya dlyarlkdyp
       61 lavsretgtl lymlarsgga kaivefgtsf gistlhlaaa lrdngggrli tsefepskvv
      121 rahanlaaag ladlveireg dalrtlaadl pdsvdlllld gakalypeil arveprlrag
      181 afvvadnaey spdylayvra pengylsvpf ggdvelsmri vraa
//
LOCUS       WP_175823554             315 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175823554
VERSION     WP_175823554.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..315
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33970
     Region          2..315
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhtvavlalp dvvpfdlgva cdtfarvrap nieqayrvrv cseqprvggd lfelrppfrl
       61 daladadtim vpgtsvplap tsrrvldalr aatargrria sicsgafvla eaglldrlra
      121 tthwlaaael arrypnvdvd pnvlfvdngq iltsagaaag ldlclhmiqa dygaavavda
      181 arsavaprvr eggqaqfiap ewpaggdglq dlmdwlqanl rkpltldaia rkastsvrtl
      241 trrfqeqtgt spgqwlqtar vrhaqqllev telsiehvat eagfgsvtaf rerfarivgt
      301 spqryrqafr arada
//
LOCUS       WP_175823569             712 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia sp. BCC0419].
ACCESSION   WP_175823569
VERSION     WP_175823569.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..712
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=76679
     Region          40..642
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mtdptanppp ppappsappr rrrvgrtlag allgltlaca gigawtidri wtqlpsvehl
       61 avyrpalplr ifsrdgdlla eygierrefv pleripplmr hallaaedak fyehgpvdvg
      121 glaratfanv vtgqpgqggs titmqvarnf yltrdkvlsr klaeilmaak lereyskdkl
      181 lelymneiyl geraygfaaa ahvyfgkpld alsageaavl aglpkapsaf npvvnparat
      241 arrnyvlgrm halgqldevt yraavdapia lattpppgii aapyvaerar rmmverfhdd
      301 aytlgldvtt tismrdqraa eaalertlsr qprakreart glegalvsld aatgdmlalv
      361 ggadfnrnvf dhalqayrqp gssfkpfvys aalekgyfpg vlvddtqrtl thaetgarpw
      421 rprnfgnrye gfipvrrglv rsknlvavsl mqatdaryvq qhavhfgfda qrnpaslpla
      481 lgagavtple lasaysvfan ggtrmeprli lsvkqrhgga myeatvpage rvvsarnafv
      541 mdsmlrdvvr agtargalal rrddaagktg tsngskdvwf agyssgivav awlgydtprp
      601 mgratgatla lpvwldymkt avdgrtplda tppqdvalvd gdfvyaeytr gtctadvpay
      661 irsrfacgga aavdapdapn apagngkrde pmpaavdaae rervldlfrt dd
//
LOCUS       WP_175823598              94 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175823598
VERSION     WP_175823598.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 94)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 94)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..94
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10521
     Region          26..91
                     /region_name="AF2118"
                     /note="Predicted transcriptional regulator, contains an
                     XRE-type HTH domain (archaeal members contain CBS pair)
                     [Transcription]; COG3620"
                     /db_xref="CDD:442838"
ORIGIN      
        1 mdkryntmpl peqlalrrqa veevlahpew tlresvrhlk ktmrltsaem aklagvstkt
       61 iqdieqgrsd gtvqtmnrvf gmlglklgvv rqss
//
LOCUS       WP_175823603             347 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175823603
VERSION     WP_175823603.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..347
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37464
     Region          2..342
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mslefehvsf qypgarhgvd dvtlsaaqge llavmgrsgs gkstllrlaa glldgwrgri
       61 aiggddvagv pvwrrevgmv fqhyalfpnl svvdnvaygl rmrgvaadvr rrraldmler
      121 vglsahatrg iamlsggqqq rvalaralvi epklllldep laaldagirh qlrdeiralq
      181 racgattlfv thdqdealsm adrvaivdgg rvlqagtprd lyerpataqv arfvghstll
      241 rgrviahgei darfatlrae tgahrpgaev evlvrpehvq adppehsanr iegrrgdvry
      301 fgatqrydfi pdgsadvllc egrepaarsi aiephhllvl paspdap
//
LOCUS       WP_175823680             213 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175823680
VERSION     WP_175823680.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..213
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23905
     Region          7..211
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 meakldstad avaaslrdmi ingelaager lverdlaerf gisripmrea iqrleregll
       61 difrnrgavv rmlsasdvqe iydlrvlleg daiyrsvkrl ddetlarael vhrllgdatv
      121 prrqgelnre fhallysccg narqlksiae lrsqveryer lqatlladtp sfqvehddil
      181 qacrernarg aramtvahld sarrivlrlv dgg
//
LOCUS       WP_175823681             158 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175823681
VERSION     WP_175823681.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..158
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=17213
     Region          5..153
                     /region_name="OsmC"
                     /note="Organic hydroperoxide reductase OsmC/OhrA [Defense
                     mechanisms]; COG1764"
                     /db_xref="CDD:441370"
ORIGIN      
        1 masgehtyrv avewtgnrgt gtsgyreygr dhviragskp dipgssdpaf rgdaarwnpe
       61 dlllasasac hklwylhlcs eagirvlayv dhaegtmldg aeagrfteiv lrpqvtiqag
      121 ddreraahlh hdahakcyia nsvnfpirce pviefaae
//
LOCUS       WP_175823691            1285 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175823691
VERSION     WP_175823691.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1285)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 1285)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1285
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..1285
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=140220
     Region          1..806
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msilnqtrtl sisgaalpty gmdalpvfvp vrlkgteaig rieacrylvt lrtddayafs
       61 psvtanldld kvvgtevtvs iqldgkgrfi pglagnnglg nigagtreit glveaarivg
      121 qdrdsilyel elrpwlwrat ltqdsrlfqe mnvveitdav lskypytvdk rlagafrggy
      181 pkrdvqrqaf esdwaflqrl weewgiwwwf ehddgyhrlv lcdttgghhp hgpayetlry
      241 lppdskhide ehihalsvts rltagrvtvt dydytrprar lavteedprn tasadgeiya
      301 wgdysqplag aqglagqpkd tdlearhlar vqleaqrcag lrakgagnlr glivghtftl
      361 tgypqqaanr eylvvscald ieeiggragv aqtyrvetqf ellpanepfr lersvskpvl
      421 sgpekavvvg pagqevwtdq ygrvkvqfew drqgphders giwlrvlspw qgidmgatfi
      481 prighevavm hyygdpdlpv iagslvnafr qpaldmphnq gvsilrgreh qgtasghvai
      541 ddtqgqihtq iasdagtsql slgnlrrmlk kkgraeargk gfdlrtddwg vmralkglfv
      601 ttdgqpggag qakdakeaig rltgarelqe slsglaqrhd aqrhgadqse vvkainarnd
      661 aikgnpsgdp dhfpeltead ivlagpagis laaergvhia snedvavtsg rhvgiavgrs
      721 llasvsnafs lfvhkagmal iaaggkvrve aqtdgidmka kqsiqitstt dsihlhaaee
      781 ivlhagstev risergyvvk tagehtihag shqtdaaqvr pmrlpvtpeh pgqfaahfvl
      841 lehdsgfalp nqpyrvtldn grviegvsne lgetdvitsh diafgtvell aasdpdkvia
      901 vnraaivrdn atpytakapn adkrtatikg kkvstpeqgv tsesqpaafa tcdplnfglr
      961 fhhfvdgakq gdtppdmpvr rdveypvtka ytaaikkalt giewskfktl sgevsndlke
     1021 sialavgnvl ntalatgpfg lprgasgdpl rsngvtptid ivnekegrar ynmrpdvsas
     1081 figsrwsiai qereitkiis ssnnataldg slqafadlly hearhcqqtf wmmallqqhp
     1141 idyamfskai niyktnirkd vfevaektrl pddtrvmtgl hrmlvfhyyw tisymqnqtg
     1201 gadvkpdvqi aqaevckllr vspetaakmv sfeegyrsql heedayacae vvqtywdrpd
     1261 rafvrnpgtc tgeydaslkt igggi
//
LOCUS       WP_175823709             224 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175823709
VERSION     WP_175823709.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..224
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=23610
     Region          <36..224
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          62..92
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(63,67..68,71..73,75..76,80,83,92,127,129,133..134,
                     137..139,141..142,146,149,158,160,162,166..167,170..172,
                     179..180,184,187,196)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          94..125
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          127..158
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          160..196
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          198..223
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mffkriaiig sfalttltsa vaaadggale grlrgaadrg dagevrtlle rgaqidsrdg
       61 lgrtalliat hgnhveaarv lieagadvna kdaiqdspyl yagargyldi lrmtlahgad
      121 lrstnryrgt alipaaergh vdtvrtlida gvnvdhvnrl gwtalleaim lgdgseryvr
      181 ivqllvdgha nvdladsngv tplqharqrg ygaiervlva agar
//
LOCUS       WP_175823745             531 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175823745
VERSION     WP_175823745.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..531
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=55483
     Region          45..151
                     /region_name="SoxW"
                     /note="Thioredoxin-related protein SoxW [Posttranslational
                     modification, protein turnover, chaperones]; COG2143"
                     /db_xref="CDD:441746"
ORIGIN      
        1 mktvlrnlta aclfaaagaa laaaapagap vasaspdgah lppgiawqhg dvdaafalak
       61 regkplllyw gavwcpscnq vkstifsqqa fktrssffvp vyldgdtesa qklgerfkvh
      121 gyptmilfrp dgtevtrlpg eadldrymqa lslgmtaahp vrqtlatalk ngaaltpdew
      181 rlladyswdt dgalpvpadr vaetlqslaq raraagakae sarfalksav vaasddptqa
      241 galdkaalad slrtvlhdpa lsradsdvlv aaparvvayl ggddaqrtkl rgaydtalar
      301 lstdgtlssi drlmalhgrv llarggarng appaapalad tarkqiaasv qgaanayerq
      361 alvsegadtl tdaglydesd allkaelprs stpyyfmsgl aanakargdk aaaldwyrka
      421 ydsasgpatk lrwgatyfan avelapndsa riegiaasvl aqadktrdaf yganlraltk
      481 vvtqlnrwrg sgahdasvrs vvkqfdgvcg klpagdpqaa acakliqpvk a
//
LOCUS       WP_175823758             312 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia sp. BCC0419].
ACCESSION   WP_175823758
VERSION     WP_175823758.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..312
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33362
     Region          66..311
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mntlhlvdpe irplletwpt vtldadnlaq srqrvlplpp pdpagstler rtvpgpagap
       61 dvpvlvywpd gharplpaiv hmhgggyvrg aakdleavhr slvtqlgcal isvdyrlape
      121 tvfpgaiedc yaalgwvfrh adtlgidtar igvagesagg glaaalalla rdrgefplaf
      181 qhliypmldd rtctrtphph agefiwhaan nrfgwtsllg hapgidgvsp yaaaaratrl
      241 dglpptflsv gsldlflden ldyaqrllra gvptelhvlp ggvhgfdivp garvseaarr
      301 lshdalrrfl hg
//
LOCUS       WP_175823761             350 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia sp. BCC0419].
ACCESSION   WP_175823761
VERSION     WP_175823761.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..350
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=36966
     Region          4..350
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mqrkaflvga cvlcatsaha ssvtlygivd syvefdrvgs lssmrqsggg sstsrfgltg
       61 vedlgggtst kfvlesgfsp adgsfqggtl fyrqayvslq ntrygdlrlg rqytpafyvv
      121 ydgdpfglne rmsplallat stdtitsntt ppiprfnqaa sylspdwngl rvmatygfpt
      181 pnalstqagr nygaglqyri gglyvgagfq gdtsagnlap vvcpsttrhy vfaanyafar
      241 vklyaaflyg vgtaarlpaf stasvgasin vgaldrvlvs vvrrdvkgsa ndatalgvgy
      301 dhplskrtsl yarylymkng gdarntvvvg lqphpggteq vfalgiahrf
//
LOCUS       WP_175823791             173 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175823791
VERSION     WP_175823791.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..173
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19013
     Region          10..>86
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtkrarltre qrrldtrerl iataralfia kgfadtsveh iaegagytrg afyahfehkr
       61 eplieilrrd hdrlikrlrl aapkgdgcct vtdaadvaag weffplwvev ylyalrdagf
      121 rqiidsmhte laappnaang aagpsdhmss saelaavlgv allrtgarrd ept
//
LOCUS       WP_175823843             148 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175823843
VERSION     WP_175823843.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..148
                     /product="VOC family protein"
                     /calculated_mol_wt=16281
     Region          4..126
                     /region_name="VOC_like"
                     /note="uncharacterized subfamily of vicinal oxygen chelate
                     (VOC) family; cd07246"
                     /db_xref="CDD:319910"
     Site            order(4..9,11,26,40..41,48..49,51..53,72..74,76..81,87,
                     108,113,121..124)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:319910"
ORIGIN      
        1 maihevfpyl rakraedaia fyakafgaqe kfrlvepsgr ighaelqlgp ctlmisdafp
       61 eydlfaldpd gnapmalhlh vddadatiaa avaagarvtr apqdqfyger sgrirdpfgy
      121 dwlightiea vepdemqrry talmsgdr
//
LOCUS       WP_175823879             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0419].
ACCESSION   WP_175823879
VERSION     WP_175823879.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21430
     Region          2..205
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mlfiksvvmg lsiavpvgpi gmlciqrsls rgfqagfatg igaacadaiy gllgalgvag
       61 ivtafpmltv glkigggafl vwlawtiarq apaapagqre lprttvlrdf lttfgltlsn
      121 pmtivsfvgi faalgplpga qagamwttva wmvagvfvgs atwwlclssa tatlrarmsf
      181 afmhglsrvs aavvavfgai qlvagvrgli
//
LOCUS       WP_175823888             376 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0419].
ACCESSION   WP_175823888
VERSION     WP_175823888.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..376
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40998
     Region          183..376
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 migfsisrww smvtkeflqi rrdrvtlgmi avlpivqlal fgfainsdpr hlptivladd
       61 tsefsrslva gmrntgyfdv rgglfseraa rdalqkgsvq fvvsvphdfs rrlvrnehpe
      121 ilveadatdp aatgnaiaaf ntmtltvlnk dltgvlaiaa prdafsarvh riynpagitq
      181 yniipglmgv ilsmtmvmmt slaitrerer gtienilasp atsievicgk ivpyiligll
      241 qctiillaar fvfgvpfegn pvtvyclasl livanlmvgi aissvarnql qamqmtffyf
      301 lpsvllsgfm fpfagmpgwa rllgnglplt yfnrairgvl lkgsgwnevw pdaatmvvfa
      361 lvamtiglla yrttld
//
LOCUS       WP_175823998             316 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175823998
VERSION     WP_175823998.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..316
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32689
     Region          32..314
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          211..314
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(216..217,250..251,254,258..259,262,304,308)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mhrtiqvrra rwsaavspal aalfaaglva sgaafaqntg atvtpvgngt vattalpqan
       61 pnaggasgtv vhgtagtiap ppanatpgqv vvggkvpdea tkaavlqklr dtygatnvvd
      121 qvevgdvatp pnwsanvqkl lgaqlkqisk gqlkingtqi emkgevhnea qrqqlasdma
      181 ntlnptytik nglrvsaseq gvldqtlanr tiefetgsat ltpqgklild qmaaalakmq
      241 nrtvdiight dnsgnrtsni alsqaradav kgylitksip pqqmtttgvg pdqpiapndt
      301 adgrarnrri efrvgq
//
LOCUS       WP_175824005             110 aa            linear   BCT 11-JAN-2025
DEFINITION  YegP family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175824005
VERSION     WP_175824005.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..110
                     /product="YegP family protein"
                     /calculated_mol_wt=12044
     Region          2..58
                     /region_name="YegP"
                     /note="Uncharacterized conserved protein YegP, UPF0339
                     family [Function unknown]; COG3422"
                     /db_xref="CDD:442648"
     Region          55..110
                     /region_name="YegP"
                     /note="Uncharacterized conserved protein YegP, UPF0339
                     family [Function unknown]; COG3422"
                     /db_xref="CDD:442648"
ORIGIN      
        1 maakfelkka tngqyyfhlk sangeiilas eryeeksgar ngiasvrena plderyerkl
       61 ahngepmfnl kaanhqvigt setyssvqar engiaavkrd aptaetfdla
//
LOCUS       WP_175824030             198 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia sp. BCC0419].
ACCESSION   WP_175824030
VERSION     WP_175824030.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..198
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20797
     Region          1..188
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mttilqinsa arsqgaqstl laneltaklq qsnpganvvv rdlltdalph ldesvlgaff
       61 tpadkrtaeq naivaksdal iaelqaadii vigapmynfg issqlktyfd wiaragvtfr
      121 ytengpegli kgkkvhvvta rggkyagtpn dsqtpylrtf lgfigltdvs fifaeglnlg
      181 pdaqsaalas areaiaaa
//
LOCUS       WP_175824130             444 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0419].
ACCESSION   WP_175824130
VERSION     WP_175824130.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..444
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48573
     Region          33..436
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(46..47,50..51,54,86,136..137,139..141,144,164,
                     167..168,171,268,271..272,275..277,280,308,312,363..364,
                     368,372,388,391..392,395..396,399)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtaldaaasr spaaaaaaaq sgeldrtykk vfwrivpflm lcyvvayldr vnvgfaklqm
       61 sqdlafsetv fglgagiffl gyflfelpsn llmhrlgari wiarimitwg llsalfafvq
      121 tptqfyvlrf llglaeagfy pgvilyltyw fpshrrakii avfmsaipvs gifgnplsgw
      181 imerfhggsg fhgwqwmfmi eavpavlvgi atilyldnsi rgakwldere kqlledeiaa
      241 qpqeqqqhgh slkavfsdpr mwwmsliyfa fvtgqygltf wmptlvkstg itdtlqigll
      301 saipfvvaiv vmnlfghsad krrerrwhli vpalmgalgf avaasyshnt avsivflsla
      361 aggvltcapl fwslptafla gsaaaagiai insvgnlagf aspyvigylk dvthstssgm
      421 yvlaamlvig aiavwltpak lvnr
//
LOCUS       WP_175824141             392 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0419].
ACCESSION   WP_175824141
VERSION     WP_175824141.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 392)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..392
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39575
     Region          168..370
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mteraaasar rvtldkvgil iggltivavf glsfavlrpn riaagtglsv faalpamqga
       61 alaalwtaga lwamtasrpa wrlaagcagl atlayavgaa aahvvapddm larvspdagv
      121 wlllfawavl iadalarlaf gpwrrlaala vaiaavsvpl asgwwdglsv mreyavrsdd
      181 fwreairhvs laggsvaaal vagvplgiac ariatvrtva mpvlnivqti psiamyglmm
      241 aplgllaahv plaaalgirg igvapavlal flysllpias svvvglgqvp phvteaaram
      301 gmtraqrllr vdlvlalpvi lsgvrivlvq nigltavaal iggggfgtfi fqgigqsaad
      361 lvllgaipti alalaaavvf eaatslakgr ag
//
LOCUS       WP_175824168             315 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175824168
VERSION     WP_175824168.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..315
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33984
     Region          19..78
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          108..303
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(123..124,126..127,130,134,136..142,233..238,
                     244..245,247..248)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mgsidrrdst pqllnrlrmr qialllavde cstlraaaeq mgltqpaatk mlaelesalg
       61 qrlfdrigrg lvlnpagerv lgyfrgirgs mealnrelge lqlgsagrla igsimaaspg
      121 rltealvqlk arypllaidi avdtsdrlmp qlregvlevv igrnvgtdcd frvvddeala
      181 iiagrdhpla gagpvefdal ldyawilqpa gsparevver efrarhqpmp rglvetgsil
      241 ttmnlvdrsp mlgvipqtva qrnaahglva iidytleqkl psygslvrrd rplsipaqqf
      301 lalfhqdaag ddgga
//
LOCUS       WP_175824178             340 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175824178
VERSION     WP_175824178.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..340
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35584
     Region          11..109
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(55,58,62..63,72,91,95,101,105,108..109)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mgtdtprlna saaaarlgvs ikalrlyerh glvtpertpa gyraygpddl araadiaalr
       61 klglglaqva svldgdarsl daalaaheaa ldhgiqdlvi kldrvramra glargrmpad
      121 geltrlldpg sagvafslpw pwggewfecr dirplnyiig slgsgktrla lrladalpga
      181 vfvgldrldd dcaaasdalr adpalksrvd rtsallagrg atpsaaltal lvdleaegpr
      241 vrivdmieqg ldratqlali ahlracaaag mrplfvltrs saildltavg pdetillcpa
      301 nhspparvap ysgapgyeav atclatpevr eriarrpita
//
LOCUS       WP_175824185             431 aa            linear   BCT 11-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175824185
VERSION     WP_175824185.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..431
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=45727
     Region          3..415
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mkkkhnitky ivvamilgia vgyachsafp dpkmakevag yvsllsdvfl rlikmiiapl
       61 vfatltvgia qmgdgsavgr vgvkafgwff iasftslllg lltatllqpg shlslplpps
      121 daalnlktga ftlkdfvvhl vpksiaeama nneilqivvf siffgtalsa lgesgkrltg
      181 viddlaqvml kvtgavmlfa pvavfaalas titteglgil ltfakfmasf ylalvllwav
      241 ltlagvtflg kraftllrli repfllsfat asseaaypkl ldaldrfgvn rkissfvlpi
      301 gysfnldgsm myctfavlfi aqvygihlpl gtqitmllml mvtskgmagv praslvviaa
      361 tlnqfnlpea glllimgvdm fldmgrsatn avgnsiaaav vakwegqlda prdddsdgar
      421 vaevkvrets a
//
LOCUS       WP_175824205             433 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0419].
ACCESSION   WP_175824205
VERSION     WP_175824205.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..433
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45350
     Region          6..405
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mtspssrpaw tyenrlllil fmtfgfvffd rlalsflfpf msaelhltnt qlgmvssala
       61 ltwalsgaat gawsdargtr kpllvaavlg fsvcsalsgl vvgfasliaf ralmgiaegp
      121 vlplsqslmv esstpsrrgl nmgllqgsaa gllgamigpp vvigiatayg wreafyvsci
      181 pgfliafclw rwvrevppgg vrhvqadtaa vsaaggaavs rwallkerni llcvlisccf
      241 ltwfvvvisf apvflvesrh lspsdmgvvm tclgaawvfw gfavpaisdr igrkptmigf
      301 aliaavcpvv lihvgsvwal gtlvfvtytg lgcftlfmat ipaetvppra iasalglimg
      361 ageliggfva ptvagfaadk yglqfamwts ttgallacvl sfglvetapa vlrkralaga
      421 aagrldtqnl ggr
//
LOCUS       WP_175824199             155 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175824199
VERSION     WP_175824199.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..155
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16329
     Region          1..144
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mykrilvavd gsdtsrhafd aalalakahg aelqpfyvve naaiyynvpg ydpsvlrdql
       61 vaqgntlaqd faklmqaagv kgetrlneat slndvsslil dgakafgadl lvlgthgrrg
      121 frrlvlgsia eqcvrhatlp vllipaaana depta
//
LOCUS       WP_175824256             260 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter permease [Burkholderia sp. BCC0419].
ACCESSION   WP_175824256
VERSION     WP_175824256.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..260
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26489
     Region          4..259
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mfeydfmina faasgivavl agivgyflvl rgqtfaghal shvgftgatg avllglspiw
       61 gmvgftlaag igmgalgekl agrdvaigvi lsgalgfgll flhfytsfat qvtallfgnv
      121 lavsrdtlav lagigavsla alaliarpll faslqpelae akgvslrtvs mlflavcala
      181 vaaatqivgv llvftllvgp aaaaqnvstr lstgvllaal falfeawagv vlayhtdwpt
      241 sfwitalsal vygasllrra
//
LOCUS       WP_175824262             369 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175824262
VERSION     WP_175824262.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..369
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39625
     Region          1..354
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masvllrnia kryddtevlr nvnldiadge fvvfvgpsgc gkstlmrmia gledisngdl
       61 lidgakvndv psakrgiamv fqsyalyphm tlydnmafgl klagakkpei dqavkqaaki
      121 lhidhlldrk pkqlsggqrq rvaigraitr kpkvflfdep lsnldaalrv kmrlefarlh
      181 delkttmiyv thdqveamtl adkivvlsgg svqqvgtpnt lyhapanqfv agfigspkmn
      241 flkgtvesad aggvlvrfds getqrvavda aglqrgaavt vgvrpehllv daaaagvaar
      301 tmaveslgda aylyaesava pdgliaripp ldtyrtgdal hvhaqaehch lfdehgqafr
      361 rlsvhakaa
//
LOCUS       WP_175824281             293 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175824281
VERSION     WP_175824281.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..293
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31333
     Region          13..270
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mtdsikallk phvrdignlq vrrtlpalaa rlvgpfiffd hmgpaalpag tgldvrphph
       61 iglatvtylf dgailhrdsl gslqeivpgd vnwmtagrgi vhsertpdaq rasghtvhgi
      121 qtwvalpqah ettepsfehh aadtlpkrne dgvaltviag dafglqspvt tfsrtlyvaa
      181 efaaggrlel dasheeravy vvdgelaidg tpvpaeqmav lapgatvtlt sgsgaramll
      241 ggdridgery iewnfvassr daierakaaw trqemgkvpg etewiplpes kpr
//
LOCUS       WP_175824313             141 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia sp. BCC0419].
ACCESSION   WP_175824313
VERSION     WP_175824313.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..141
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15303
     Region          8..127
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mkpdpsdlsr hatdlgllfl rvaasvlllv vhglpkivhy taeaaaiedp fhlgrtlsil
       61 faifaevvcp ifmivglypr laalpvmivt lvalvfvhpd wplrdaqfaw mllilfgtia
      121 iagagryvlt vplpgvvrrr s
//
LOCUS       WP_175824323             323 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC0419].
ACCESSION   WP_175824323
VERSION     WP_175824323.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..323
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35536
     Region          38..190
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <188..307
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mstvptssrp palsprerkr lvtllrtlap degynltalp svrilrsnra lsrtpvlydp
       61 givivcqgsk rgyfggeryl ydehhylavs vpvpfsmetd atperpllal ylhldftlaa
      121 elaaqidrag laetvqapks mmstpmdeam hasvlrfvda mqrpldaavl gpallrelyf
      181 rvltgaqgda mrsalamrgq fgrigralrv ihadyaqpld vsqladaagm svpsfhshfk
      241 aitqvspmqy lkstrlhqar llmvrqdlta eaagyavgyt spsqfsrefk rlfgltpake
      301 tqrmrasfai pqafddavfv ssh
//
LOCUS       WP_175824326             221 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0419].
ACCESSION   WP_175824326
VERSION     WP_175824326.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..221
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22612
     Region          7..198
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtlhypllfa ylaaivllia tpgpvvmlvt gtvarrgfrq gvltavgana aslvmiagam
       61 lmvfgvvmvs arllaglhva gclfiavlai rtllgewrag rarggdgtva agpaagepvp
      121 qprglpgvvr gflvgianpk dllffvaffp qfvaitpdsr vslailaalw iavdftiltg
      181 ymaainhpai hrkqrwvvas salallaial aglgstlaga a
//
LOCUS       WP_175824353             424 aa            linear   BCT 11-JAN-2025
DEFINITION  NupC/NupG family nucleoside CNT transporter [Burkholderia sp.
            BCC0419].
ACCESSION   WP_175824353
VERSION     WP_175824353.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0419
  ORGANISM  Burkholderia sp. BCC0419
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Hirschi,M., Johnson,Z.L. and Lee,S.Y.
  TITLE     Visualizing multistep elevator-like transitions of a nucleoside
            transporter
  JOURNAL   Nature 545 (7652), 66-70 (2017)
   PUBMED   28424521
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Johnson,Z.L., Lee,J.H., Lee,K., Lee,M., Kwon,D.Y., Hong,J. and
            Lee,S.Y.
  TITLE     Structural basis of nucleoside and nucleoside drug selectivity by
            concentrative nucleoside transporters
  JOURNAL   Elife 3, e03604 (2014)
   PUBMED   25082345
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Munch-Petersen,A., Mygind,B., Nicolaisen,A. and Pihl,N.J.
  TITLE     Nucleoside transport in cells and membrane vesicles from
            Escherichia coli K12
  JOURNAL   J Biol Chem 254 (10), 3730-3737 (1979)
   PUBMED   374403
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia sp. BCC0419"
                     /db_xref="taxon:486878"
     Protein         1..424
                     /product="NupC/NupG family nucleoside CNT transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005337 - nucleoside transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:1901642 - nucleoside transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=43933
     Region          1..422
                     /region_name="NupC"
                     /note="Nucleoside permease NupC [Nucleotide transport and
                     metabolism]; COG1972"
                     /db_xref="CDD:441575"
ORIGIN      
        1 mdilrsllgm lflllvayll snnrravstr tmiaalltqf aigalvlfvp sgraalaava
       61 ngvnrvldmg nhgiafvfgg lvdarmfqlf gdggfvfglr vlpmiifvta lisvlyyigv
      121 mkwivailga glakvlgvsr ieacsavati flgqsempal vkpfvrnmts aeiftvmasg
      181 masvagsvlv gyaglgvkme yllaasfmav pggllfgkll fptvepsrvv vdgldfddkr
      241 aanvieaaas gasvglriai nvgamliafv glialmnlii sgaaafagfp qvtlvgiigh
      301 lfaplawiig vpwhdatlag nfigeklifn efvaygdlsp ylkggahaaa aglqvldpkt
      361 laivsfalcg fanfssiail aggfsavape rrsdvarlgl raltaatlsn lmsaaiaglf
      421 fslh
//
LOCUS       WP_175824468             419 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia cepacia].
ACCESSION   WP_175824468
VERSION     WP_175824468.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..419
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44987
     Region          <107..400
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msesakpspe qpslatiran lsaygleldr laarmrvhgp aadqtrqipd avcapqdvpa
       61 lnlnlvpaty ggcldvqslt srialmeylg yadaalalal pgpglatppv lalgsreqqa
      121 rffkrfrsst prwgafaite pdcgsdatam rttarktahg wvlngtkcfi tngaraddvi
      181 tfatinrqsg rfgvrafhvd rnvpgfsvvr ieqmvglras qlavlsytdc evpedallrr
      241 gdetplndaf sgaqhawdyf rpllsavmig acrrvrddls ayfeagghpv nqhqlaadvk
      301 avlldidrqi ttaqllcqha awktdqgiat smdasmakay asqvaarvtr taidfagldg
      361 iaafpsleqs yrdakafdim egtgdlqrlm iarsaqrsas lpwevttaas pcatqarss
//
LOCUS       WP_175824471             291 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            cepacia].
ACCESSION   WP_175824471
VERSION     WP_175824471.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..291
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30610
     Region          24..278
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mvvilnilsy vcllilialg laivfglmdi vnlahaewvt igaytlavaq slggphafwf
       61 alfaapavga mlgwclerlv irllyerpld tllatyaisl ivqkglelif gthpmlvyap
      121 lngalpvpgg sypayrlfvi gvavtvtvgc wllfaytrfg tqlraviqhp amaeavgidt
      181 rrlnrlafcg gaalaslagv lvapmisves hlgvaylaka ffvivlggig siagsllgsa
      241 fvgtaetlls yrmdpslasa ivlilsivli rfrpqgllpg fsaahqlhgk g
//
LOCUS       WP_175824476             345 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia cepacia].
ACCESSION   WP_175824476
VERSION     WP_175824476.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..345
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=36106
     Region          19..345
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mqtrkfrgsv gkwavtlgmc vsagiahaqs svslygvada fvgelhpaga agnawqvgsg
       61 gmttsywgms gaedlgggmk avftlesfyr inggqagsfp gqsffgrnaf vglsghfgel
      121 tlgrnsaplf vstllfnpfg nsfvfspivv hgflgsamga aslqsdtaid nsilyqtpev
      181 aglsgsllys nagiaghagq anysanvlyf agpfsataav qslhttslfl ngataqtawm
      241 vggayrlsvv klfaqyervd nnnhvtddtv qfgasvrigl gsilmswagt qrrpsigdhl
      301 rwstlalgyd yplskrtdvy aawrydtitd vssgnsvgag mrvkf
//
LOCUS       WP_175825380              61 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia cepacia].
ACCESSION   WP_175825380
VERSION     WP_175825380.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 61)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 61)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..61
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..61
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6862
     Region          4..>54
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 manshlkwpt velpvpferi ldvdavivah thldhwddaa kslipkrvvr ylcsmikmpt
       61 s
//
LOCUS       WP_175825594             248 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            multivorans].
ACCESSION   WP_175825594
VERSION     WP_175825594.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..248
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27338
     Region          27..184
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtaatartmt atakaerada srapagrksq qrvqdilrag rdvfaekgye hataaeiaqr
       61 vgvseatvfs yfrgkrelca rviadwydei iaafehgmpq eatvqqqfaf ivrthlrlml
      121 vngtglcalv lsegrakqha lsdeltalqr rytaplmsvl argqaagqvr rdmplsllrs
      181 mvfgpiehvl wdailghrkl dtettatqli dmlwaavqpp apeqaalvrf knevaeamkr
      241 leaspere
//
LOCUS       WP_175825759             224 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease [Burkholderia multivorans].
ACCESSION   WP_175825759
VERSION     WP_175825759.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..224
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25208
     Region          158..208
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mqpiitrdae kasglpryft gkpckhghla prytssttcv icqhaatqal raknpertrr
       61 qnaetrertr ekrnayhrew mkrnpeknra nvarwkranp dkvsalsaay harnaerlna
      121 rrrayrknnp hvgaassrrr raklrgaegs htaaeilala qkqnyrcacc gvsirrgyha
      181 dhitplakgg sdwitniqll cakcnkrkaa kdplawaaen glll
//
LOCUS       WP_175825866             342 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia sp. Bp9031].
ACCESSION   WP_175825866
VERSION     WP_175825866.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. Bp9031
  ORGANISM  Burkholderia sp. Bp9031
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia sp. Bp9031"
                     /db_xref="taxon:2184566"
     Protein         1..342
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=36752
     Region          201..342
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mlkyllittl ciagsmysva sqaqiprcyn detgadyqrs fsfgtvlvps dvpdgtvlat
       61 ttltmpyrcd anttspygys fyfmnnqrpt gipgvsyvlt slpapeslgl rftnletgev
      121 mmvyngatqd wapphtttkp iegryrikie likasdriyn avipngtvgi wqigaqnrar
      181 ptygykyqiy wneagkgklv impktctvtt pdirfplppv aasklgtvgm tagdtgfnig
      241 lncksgsnvy vtltdltnqg ntgnqltltp dssaqgvklr ilrngqpvgy gpdsaaignt
      301 nqwyvgpsat lsnipltaqy iatgkvssgt vkgvatftms yq
//
LOCUS       WP_175828645             473 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175828645
VERSION     WP_175828645.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..473
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48073
     Region          31..430
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,157,
                     160..161,164,288,291..292,295..297,300,328,332,385..386,
                     390,394,410,413..414,417..418,421)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mpdchpvslp vsittacrpt arerrftlal vaigmfmavl dttivnvalp amranlgatv
       61 aalawivday tlsfaalila ggalsdrfga khvylaglal fvaasagcgf apsvavlvaa
      121 rfvqgmgaal flpaslavvr stfdvpaera raiavwagia svavavgpvl ggvlvddfgw
      181 rsaflinvpt gavalagaav lvrasvarha rhfdwagqcv gaialgalcf avielptrgp
      241 gaaevrgall vaglaagalv iierrardpm vplawfrnrt fvamnlmgsl vyvgyfgllf
      301 vlslylhgrf gmsarqtglt llpfalslsl gnllsgklhg rvhpvrlman glgmaalamp
      361 alaaaltlra pwpvawaama afgtgtalsv apmiatvleq vpadaagvas gflnaarqag
      421 slfgvaiasa atillpnpta alwaiaavgc iayataalaa rtagtaravq rrg
//
LOCUS       WP_175828733             545 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 32 protein [Burkholderia cepacia].
ACCESSION   WP_175828733
VERSION     WP_175828733.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 545)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..545
                     /product="glycoside hydrolase family 32 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=59280
     Region          38..533
                     /region_name="SacC"
                     /note="Sucrose-6-phosphate hydrolase SacC, GH32 family
                     [Carbohydrate transport and metabolism]; COG1621"
                     /db_xref="CDD:441228"
ORIGIN      
        1 mistsfrfsa riarlllacv actqvaaapc hapaengtpq wrpalhytpq rnwmndpngl
       61 vydngryhlf yqynplgndw gnmswghats tdlvhwreqp vamranatee ifsgsivadt
      121 lntsglgtpg htplvalyts vykpgsghap giqaqslays ldqgttwqpy ahnpvltldp
      181 eskqfrdpkv swyapggywl mttvvadahv vklyrsddli hwnflsdftr pgvphdgalw
      241 empdlvplpl dgdpaqtrwv mivnvnpwsi aggsgamyfv gnfdgrtftp drvapagsdp
      301 aqfhwvdhga dfyaagtfsg apgsrpvaia wmsnwdyaak vpttpwrgam tlprelslkt
      361 idgeptlvva paaafdawad rrpavhegdl tvdsatrals patrgtvqri tvtieprhaa
      421 raglivrrsa dgsvgtrivy dtvkrtltld rsrsgeanfa gtfsrehivd lplehgrlrl
      481 eivvdrgsve vfanggrval tdlifpppda drvavfaehg ratfsgltvt qleaggdrhg
      541 acapr
//
LOCUS       WP_175828738             195 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cepacia].
ACCESSION   WP_175828738
VERSION     WP_175828738.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..195
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20223
     Region          1..193
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msmlvsmaaf alassitpgp vnivalsaga rhglgaslry aagatlgfva lflliglglh
       61 aalarwpmlt tatqwsgiaf llylalrlal ddgrlsaapd vagpsaasga amqwlnpkaw
      121 lacvaamgay aadgdraqvw qfaalylvic fasiacwgya gaslrhrlan arrmrvfnrl
      181 malllagsal flldv
//
LOCUS       WP_175828751             452 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175828751
VERSION     WP_175828751.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..452
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48483
     Region          32..423
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(44..45,48..49,52,84,134..135,137..139,142,162,
                     165..166,169,273,276..277,280..282,285,313,317,368..369,
                     373,377,393,396..397,400..401,404)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 msaplqadaa ravasgaaap dddalyrrig arivpflfic yivsildrsn igfaqlqmrq
       61 dlgltdamys lgavlffvgy vlfevpsnal lrrfgarrtf arimclwgav svamitvdsa
      121 khfyvlrfll glfeagffpg vvfyltywyp arrrasvlsi fyagvavagm vggllsgwlm
      181 rgmsgvlglh gwqwmfaieg apaillgvia wfwlcdrpeq arwlsdadrq rlaadlaadr
      241 agaagaagad apaphslrqv laeprtylfa fiyfslttal lmllfwmplm irefgihdvv
      301 qisllsvvpn aigaagliai arrsdrkrer rrhfaacafg gavalalltl hlpsivamma
      361 llsvavmlif aahpvfwavp sayfsgagaa ggialissig vssgmitpwl vglirtrtgs
      421 mdpamlmiaa llaacavaml lgvravprae aa
//
LOCUS       WP_175828755             418 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175828755
VERSION     WP_175828755.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..418
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44655
     Region          17..395
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(27..28,31..32,35,69,124..125,127..129,132,152,
                     155..156,159,234,237..238,241..243,246,270,274,325..326,
                     330,334,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 msvpaagvfr slrsfnyrvw aigslvsnvg twvqrtaqdw lvltqlthhd asavgtvmal
       61 qfgpqllllp wtgyaadrfd qrkllmvtqa lmgvlalvlg altvtgvarl ehvyvfaflf
      121 gcaaafdapv rqtfvaelvg drelanaval nstsfnaarm igpaaagfmi asvgtgwafv
      181 anglsffavl vsllllrede lranlragrs rgglldgfry vwrrddlkai lvmlfligtf
      241 glnfqlfist maasvfhvda rgfgvlssmm avgtvsgall aarreqprfr hlwfgaalfg
      301 lgctlaalap gywlfaaalv ltgiaaitfm nstnslmqls tepamrgrvm alrlavalgg
      361 tpigapvagw vanhlgprwa lgvgamsgfg aalvathfvk rrraqaqadr ardrfdgv
//
LOCUS       WP_175828768             862 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia cepacia].
ACCESSION   WP_175828768
VERSION     WP_175828768.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 862)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..862
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=93174
     Region          59..712
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mhpfqpsstr vnrrnvssvr dfcarwvara qpvaaaavar vkplaavawh hlrhptrrgv
       61 llagaavpal fvvyvvvlip ftpgigdirk arvdqpaqvl sadgkllaef kpsnrewvpl
      121 kqisphmvda liatedhrfy ehhgldwkrt asaalhtfsg srqggstitq qlarnlypde
      181 igraptltrk vkeaitalki eavyskdqil etylntvpfl ynaygvemaa rtyfdksade
      241 ldvldsatlv gmlkgnsyyn pvlnperalq rrntvlgqmv kygklspaqf aqlqrrplri
      301 dferqkeppg paphfaqqlr kwliawadrn dyniyadgli vrttidsrlq qmatqaltlq
      361 gnqlqgiann awsgrdgcgt dnevfrtfmr espeykaaqd agkddaaamk llaadrgfmr
      421 alcktktdvq agflaidprn gqirawvgsr dftsepfdhv aqarrqpgst fkpfvygvaf
      481 angmkpddtf idqpveiplk ggeiwrpndd vpptgkpmtl rdavalsrnr itaqvmekvg
      541 pasvarlard mgvrespler vpslalgtsp vtlkemvasy atvangglyv epqmvtrien
      601 rqgdvlaeya papperalda etdktllsvm rdvvtrgtgg sirtrfgirg dvagktgttq
      661 dnadgwfilm qpglvagawv gfddgrvtlr sdywgqgahs alpivgdffq raqrarivdt
      721 kakfdtepsp gwfaslrerv tdlfdtwfpp kpekapapar tqrverapea dtgtestasa
      781 asapeaasgg iveewvpase vaasaaalsa gasqaqpaqp pagastpggg ssglgaapaa
      841 apsaapaqpp vpaapdasga sq
//
LOCUS       WP_175828778             766 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Burkholderia cepacia].
ACCESSION   WP_175828778
VERSION     WP_175828778.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..766
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=83882
     Region          178..765
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 msyvvavram ceftarrgdl dlrftpapta legiaghgav tsnrgaryet eialtgtwgt
       61 ltvrgradgy dpvanrleei ktfrgsldam panhralhwa qakvyahlmc dardlaeidv
      121 alvyfdivse retvltqtlg aaelaaffae qcacfvgwae retahraard aalralafph
      181 gqfrsgqrel avavyraard drclmaqapt gigktlgtvf pllkacgege ldhvyfltak
      241 tpgralalea aatlgagtpa lplrvlelva rdkacehpdr achgescpla kgfydrlpaa
      301 rdaaieagll drdtvraaal ahdvcpyyls qelarwsdmv igdynyyydg samlhtlaqq
      361 nqwrvgvlvd eahnlldrar kmysasldpf afaaareaap aalrkafdrl arawgtvnra
      421 qaeryaaype ipgpivsavq nlvaaigehl adaprandda llrfhfeaiq fgvlaeafds
      481 asifdatlhg epmprqpald gvasagrrrr vqstlcvrnv ipagflapry eaacatvlfs
      541 gtlspfhfyr dtlglpgdtg wldvdgpfra eqltvrvash vstrwrdrdr slepivdlia
      601 aqyatrpgny lgflssfdyl grvvalmqar hpdvpvwaqa pgmtegerda flarfdaggr
      661 gvgfavlgga fsegvdlvge rligafiatl glpqvndvne qmrramdarf gngydymyly
      721 pglqkvvqaa grvirtehde gvvhliddry rrrevrdllp rwwrig
//
LOCUS       WP_175828791             442 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175828791
VERSION     WP_175828791.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024287
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..442
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47362
     Region          18..423
                     /region_name="MFS_KgtP"
                     /note="Alpha-ketoglutarate permease of the Major
                     Facilitator Superfamily of transporters; cd17367"
                     /db_xref="CDD:340925"
     Site            order(28..29,32..33,36,74,132..133,135..137,140,160,
                     163..164,167,249,252..253,256..258,261,289,293,346..347,
                     351,355,371,374..375,378..379,382)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340925"
ORIGIN      
        1 maisptgaag erprigsivg glagnliewy dflaysifsi yfapaffpad rptvqlmnta
       61 aiaavgyiar pagswlvgvy adrrgrkaal tksvlamcag smliavtpgy atigvlapal
      121 lvaarllqgl smggeygtsa tylseiappn rrgfyvgflq vsvvagqlva lglmlamqri
      181 fagtydlerw gwripffvgg llalfalymr rnvvesdafi asraraaktr mtadlaahwr
      241 elllaigitv ggtvafytyt vymqkylvns vglhketatw ictaalllym plqplfglvs
      301 drvgrrpvll wfgigctlls vpiftalghv heplaafalv faglvvlsgf tsvhmlvkae
      361 lfppqirala vglpyaltta ilggttefva lrlkasgnet mffwyvaaca aisllvywrm
      421 pethpakrgr lspaavaasa sr
//
LOCUS       WP_175828793             206 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175828793
VERSION     WP_175828793.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22284
     Region          3..169
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnassgaevr qhilniakpi mlhkgfsavg lneilaaagi pkgsfyhyfg skeafgeall
       61 eayfdsyhah ldnllkhpag tgaerlmtyw rnwlhtqcad dpqgkclavk lgaevsdlse
      121 amravlrqgt sqiierlagg ieagladgsl sgiadpshta ailyemwlga tllekihrdr
      181 kpleramvet rrmlnlppve hggaqs
//
LOCUS       WP_175828816             196 aa            linear   BCT 11-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Burkholderia
            cepacia].
ACCESSION   WP_175828816
VERSION     WP_175828816.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..196
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=20631
     Region          1..196
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mtaaliflnv avflvelggp qplidlfalw plqpsgepgt apfhvwqllt ysvlhasiah
       61 vafnmfglym fgrdvervlg rarflglyla svlaggltqi avlsaappsg tptigasagv
      121 fgilvsyavl fpqrrvvllf ppipmpawlf atgyalvell sgvsgdtsgi ahfahlggml
      181 gaivclafra rdarrs
//
LOCUS       WP_175828832             215 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175828832
VERSION     WP_175828832.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..215
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=23193
     Region          3..143
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
     Region          78..214
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mksdavlkhd veqalfwnpa idarridvdv rdrivtlrgt vdswaqklea qktalhvena
       61 ralvlelnva ppenacadqe laiaitfalg wqealrdhki rvevdhgcvt ldgevdhafq
      121 sraaermvsr migvvgvanr irvrtdhtvp dvgtriaeal arraqresag isidaadgiv
      181 tltgtvasla erraacgaaa svrgvrevvd rltva
//
LOCUS       WP_175828842             374 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175828842
VERSION     WP_175828842.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13386660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..374
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40445
     Region          13..>122
                     /region_name="YhgE"
                     /note="Uncharacterized membrane protein YhgE, phage
                     infection protein (PIP) family [Function unknown];
                     COG1511"
                     /db_xref="CDD:441120"
     Region          174..371
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 msrllvifrl gvkelwslar dpillalivy tfsasiyvaa tarpetlhkv piaivdedas
       61 plsariaaaf fppqfapppi vdaaaadrgl dngdytfsld ippdfqrdvl agrhatiqln
      121 vdatrmtqaf tgggyvqqiv sgeidafvrr yrgtpsppvd lamrmrfnpn ldevwfgalm
      181 elinnvtmls miltgaalir erehgtiehl lvmpvtaaei mlakvwsmgl vvtvaavasl
      241 tlvvggalhv pipgsiplfv agmalhlfat tsmgiflatl vrsmpqfgml lvlvllplql
      301 lsggltpres mplavqdiml aaptthfvel sqrilyrgag ldavwlqfav lfaigcalfl
      361 lslmrfrkti aqma
//
LOCUS       WP_175828870             144 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Burkholderia cepacia].
ACCESSION   WP_175828870
VERSION     WP_175828870.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..144
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=15703
     Region          42..144
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 msnvtrydpf siepvadlfq glfrplrgmt ltdepelasm kidvtesdda ykvnaelpgv
       61 akddidvqvt gstvsihaki ernkeqkdge rvirrerysg aisrsfslsg eiddanasat
      121 yqdgvlsltl pkkapvaqkk ltis
//
LOCUS       WP_175828945             321 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175828945
VERSION     WP_175828945.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..321
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35257
     Region          13..>176
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          98..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(108,112,151,165,167,232,249,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(109..110,114..115,117..118,121,125,127..133,194,
                     225..226,228..230,237..238,241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mqrqfddlll gsielfclaa elgsftlaan aasvtpaavs rsvarleerl gvrlfvrttr
       61 qirltdpgrr yfeqcrdala qlvdaereat gqqatpagll rismptpygh yrvlpllpaf
      121 rerypdvrve thlsnrnidf aeegydlair grapadsnlv arkledaelv vvatpgylkr
      181 aglpaaiddl haheciqfel pssgrpipwl fndgaeevdv attggygtsg dylggvtlar
      241 sgaglfqtyr fiveqdlhag tlvevlpglg grsrpfmlly pharflssrv rvfvdflveh
      301 leraptrrpa gtrakragts r
//
LOCUS       WP_175828968             450 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175828968
VERSION     WP_175828968.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..450
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47027
     Region          18..428
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mlihhvepsi qdvaaagrra payawlvfgl tvglllsdym srqvlnavfp llkqawalsd
       61 tqlgslsgvv allvglltfp lsvladrfgr vrsivlmaal wsvatlgcal sthytemlva
      121 rglvglgeaa ygsvgvalil sifparlrat ltgafmagga fgsvfgmalg glvgahlgwr
      181 wsfgvmaalg ivllvayrcv vterrlaayr teygteygte pcrrdtdtpr dlrgsvrvlm
      241 sglfasrsvi caylgsglhl fvpgalfawl psylnryyam apdraavlaa gfvllagigm
      301 vgcgivtdrv gktdgkrkwl taiaycvltg vclavafrlp pgplqlalic agmlvgagas
      361 gasgamvanl tpaaihasaf atltlannll gmapgplltg waadraglvg alqwipvvpl
      421 maavlfaigr asyvadlarv ererrasrls
//
LOCUS       WP_175828962             275 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cepacia].
ACCESSION   WP_175828962
VERSION     WP_175828962.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..275
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29223
     Region          66..269
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mtilyrgmdr aaldaaylnt kvvpdfpall asmqarsatl ydttrgrrdl rygaqpaqrf
       61 dwlscgrpda plfvfihggy wqhcakedfa yaasgplarg fdvilaeytl aplatmtgiv
      121 geigalldyl andpdaigta grpihlsghs agghltavyr ahpavvsala isplvdlepi
      181 slcvlndklq lsarevdays plrhvgpgap tvvavgdael pelvrqardy ataceaager
      241 ivhvglpgmr hfdvlddlak pdgamlaalq siapr
//
LOCUS       WP_175829010             128 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF805 domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175829010
VERSION     WP_175829010.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..128
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=14047
     Region          1..117
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 mnlkwflfsf egrigrlpww iyalvsalls vffdadshrs pdddlpllam lvlvvvavva
       61 awssiavgvk rlhdidksgw wmllmfvpiv galalfvmng fiagtphanr fgeppsaded
      121 epaprdpa
//
LOCUS       WP_175829015             127 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia cepacia].
ACCESSION   WP_175829015
VERSION     WP_175829015.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..127
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13367
     Region          20..127
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 miaslgilvp veddrfravv dfyrlalalp vhsegvsaag spwhrfvmgg atltvhtgsg
       61 grfpypefrp tghgialave vahvseavar lescrvgiln ewdygdgtva isvadpagnv
      121 ceiwgrp
//
LOCUS       WP_175829042             295 aa            linear   BCT 11-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Burkholderia cepacia].
ACCESSION   WP_175829042
VERSION     WP_175829042.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472037
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..295
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=31045
     Region          71..217
                     /region_name="TadD"
                     /note="Flp pilus assembly protein TadD, contains TPR
                     repeats [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG5010"
                     /db_xref="CDD:444034"
     Region          156..186
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrrideivkv vgvltmvgll gacsafkesg ygvgpqaera almdaaaqkq avpdtpgmyl
       61 gliermqsqg lyyaslahid ayekqygasp qtillradal rmtdqpaast avytqllntt
      121 laargyrglg liaggagdfp raaqalsqat vlaptdastl sdlayaklrc gdiegaripl
      181 mkaaeldqsn pkiisnlvly llasgrthda qklmaqqkls mdvrndirnd atkiataart
      241 wrrasqapas asvltpigsg svvdvsgsnv akrpspvani qgfdptapll qrfaq
//
LOCUS       WP_175829066             506 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Burkholderia cepacia].
ACCESSION   WP_175829066
VERSION     WP_175829066.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..506
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53802
     Region          13..490
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(70,72,76,79,83,116,119..120,129..136,141,144,147,
                     240,244,247,250,252,426,428..429,431..432,435,438..439,
                     441,443..446,455,459,461,475,482..487,489..490)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(156..159,167,182,185,215,232..235,238,256..258,290,
                     391,393,419)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(159,256,287,290)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnpvpaytsd advghyvdga pvsgrsgrfq dvlnpalgra vrrvaladds evqlavasah
       61 aafpewaatp pirrarvlhr flqlmnehrd alaaiitaeh gkvfsdaqge vargidiief
      121 acgvpqllkg dftdqvstgi dnwtmrqplg vvagitpfnf pcmvpcwmfp vaiatgntfv
      181 lkpserdpsa alfiadlltq aglpagvfnv vqgdkgavda lldhpdvqav sfvgstpiaa
      241 yvqqravqsg krvqalggak nhlvvmpdan leqavdalig aaygsagerc maisvavlvg
      301 dvadkivplv aerarklvig dgmspevemg pivtgdalkr iegyieqgvn egaqlvvdgr
      361 glrvpgreag fftggtlfdh vtpdmriyke eifgpvlgcv rvkdfgeavd linahefgng
      421 vscftsdggi arefarriqv gmvginvpip vpmawhgfgg wkkslfgdmh aygeegarfy
      481 trqksvmqrw sssigkgaef amptak
//
LOCUS       WP_175829128             539 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA synthetase [Burkholderia cepacia].
ACCESSION   WP_175829128
VERSION     WP_175829128.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..539
                     /product="acyl-CoA synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016405 - CoA-ligase activity [Evidence
                     IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57612
     Region          48..538
                     /region_name="MACS_like_3"
                     /note="Uncharacterized subfamily of medium-chain acyl-CoA
                     synthetase (MACS); cd05971"
                     /db_xref="CDD:341275"
     Site            order(111,241..243,267,287,289,293,314..317,336..341,
                     344..345,361,421,433,436,442,444..447,476,505,510..511,
                     513,515)
                     /site_type="active"
                     /db_xref="CDD:341275"
     Site            order(192,195..200,202..203)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341275"
     Site            order(237,289..290,293,314,444..446,505,511)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341275"
     Site            order(314..317,336..341,361,421,433,436,442,447)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341275"
ORIGIN      
        1 mlpatdrydd llsrfawdvp arynigvdvc dkwadgsgrl alihetaqgd vsritfddlr
       61 nasnrlansf vraglrrgdr igiflaqgpe taiahlaayk lgaiavplft lfgvdaleyr
      121 lanseaaalv tdaagyakia slraqlpalh tiycigddap dspgvlryda alaaetpdfv
      181 padtaaddpa liiytsgttg kpkgalhahr vlpghlpgve msqqcfprda rlfwtpadwa
      241 wigglldvll pswhhgvpvl arrfekfdgd aafalmarhg vthaflppta lklmrtvpap
      301 reryalslks vasggetlgt eltawgrdal gvtinefygq tecnmmlssc aalfdaqpga
      361 igkavpghav aivdadgtpl ppgvegriav rrpdpvmfle ywrnagatrd kfagdylltg
      421 dtgmidadgf vrfvgrdddv itsagyrigp gpiedcllth pavrmaavvg vpdatrteiv
      481 kafvvlnpgh agddalvqal qahvrtrlaa heypraiafv dslpmtatgk ivrralrda
//
LOCUS       WP_175829134             185 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Burkholderia cepacia].
ACCESSION   WP_175829134
VERSION     WP_175829134.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..185
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21286
     Region          9..176
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtdpdrdita ivmrertrlv sfirrrirdp ddaedilqdv fhefvqayrl papieqvsaw
       61 lfraarnriv drfrkkkeqp ltdlseaddd adseyrldlv lpahdagpea vyartlllea
      121 lqdaldelpa nqrevfiahe legrsfkema tqsgvalntl larkryavlh lrarlqlihd
      181 eldns
//
LOCUS       WP_175829144             331 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia cepacia].
ACCESSION   WP_175829144
VERSION     WP_175829144.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..331
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=36034
     Region          126..329
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 myslmagala mallcvaaal mlwrhgevkr gradvqrfid sriepaaraa galqsdarpv
       61 qnvasvpgaa raqsaapasr wahwreiate ylvnvasrag iedargkall allglvalgl
      121 vagnrggwla cvaalvcgas llvfwlvsri qrrrltivrq lpsfldgivr lvtlgnsvpa
      181 afqaalltte aplrgcldhv srmlrtgvei dramghiasv yqtkefelvg svlrlsvryg
      241 gradvmldrm stfmrdleqa erelaamsse trlsawvlvm lpiaigsfvi atnplylqsm
      301 wndytgrqll fiafmlqfag giwlyhmakl r
//
LOCUS       WP_175829172             302 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175829172
VERSION     WP_175829172.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32527
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdllatmriy vrvvergtms gaardldmgq pavserierl ekhlgtrllm rsartlvcte
       61 egrifydrsk alleaadeav asvsktetal dgtirlaapq cfgevvlpgv lmhvrtaypg
      121 lhidlvlndd ivdpvtegvd isirvgqlgd ggfvahavga vgrrlvaaps yldrcgpidt
      181 aadlanhpfi rvkgvfaser lpvqydggpl eyarirtimt tshwrpmfdt iaagggigvv
      241 qhpacadala agtlvellpr yaipdfalnv lvhaqrplpp rvravvdllk qdippllarp
      301 pr
//
LOCUS       WP_175829208             243 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia cepacia].
ACCESSION   WP_175829208
VERSION     WP_175829208.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..243
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26394
     Region          165..242
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mpdshdwldi dyrtlfrlhp drrierendp dcspgprfwl grcaernlag vradvpfpva
       61 eqlarladse tpsadftqpa hlerylslla pvphwniglv yalphalgfd tdahvelidg
      121 dsdagrhllh alstrgmpeg lfsmgfqgas dlwapwcaav vdgevasvaf aarlsevgae
      181 lglatapafr grglaaaata awsrlpslrt rtlfystdsd nrasrrvasr lgltlrgttl
      241 rva
//
LOCUS       WP_175829224             482 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175829224
VERSION     WP_175829224.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..482
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48535
     Region          21..421
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(28..29,32..33,36,68,118..119,121..123,126,148,
                     151..152,155,287,290..291,294..296,299,327,331,383..384,
                     388,392,408,411..412,415..416,419)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mdttipsstf ppalarvvat vstgfvvtql dvtivniala hlagdlrlpv aglqwvvday
       61 tlafavlmls ggalgdrfga rrlyiaglvl falaslacga atapamliaa ralqgvgaaa
      121 mlpnslalln dacrhdprlr aravgwwtaa gsisiaagpv vgglliaaws wrgiflvnlp
      181 lcaaglaaal agiparraaa tpaapsrsvr aldlrgqlia iamltaltga viewrplgft
      241 hpvvaggfal atlaalafva vetrtatpml plslfrhrtf saavlfgicv nltyygtvfv
      301 lalylqrarg esalqaglaf lpltggflls nlasgrvvar hgprapmlag alvaalgygs
      361 lhfidastpl avllvpflli psgmgfavpa mttavlasva peragiasav lntarqagga
      421 mgvaafgala ggggaaqvvd glqietavsv allvaaalva tlvrpdahrg assvrqavpa
      481 ad
//
LOCUS       WP_175829236             558 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Burkholderia cepacia].
ACCESSION   WP_175829236
VERSION     WP_175829236.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..558
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=60705
     Region          25..556
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 matvtpratn eslhptigaa rltlgnrill sfgvlfvlml vtagvsyerl rainseavsi
       61 erdslpgvyl asslrgavne sfmllqqatf vetdpesvqr dlakiaeaak didslsveyq
      121 nsifrdddrq rfatfrgtyd hylpllneav qrhrqshdda vagyvkvlpa waevvrnani
      181 lvqenrkfad qsakliresv qdtevvlata laimllsalg fgymlyrsvt vpmarlvevh
      241 dvmrtgnltr rldlrrrdef gtletgfnrm adeltelvar aqqsslqvtt svaeiaatsr
      301 eqqataneta attteigats reifatsrdl vrtmnevagv aeqsatlagv sqsgltrmge
      361 tmrsvmdaag svnaklailn ekalninqvv atitkvadqt nllslnaaie aekageygrg
      421 favvateirr ladqtavaty dieqtvkeiq savsagvmgm dkfseevrrg mldvqqvggq
      481 lsqiiaevqt lsprfqmvne gmqtqangae qitqalsqls eaaqqtaesl rqssqaiddl
      541 tlvanqlrts vsrfkvda
//
LOCUS       WP_175829292             280 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175829292
VERSION     WP_175829292.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 280)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..280
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29967
     Region          13..277
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mnallprapl pgrlsratgt latlvlclaa lpivtmitms fgssgtlefp prdfslhwyr
       61 aawqtfvtad agsaqsmgaa lttslvvaia tmlvatavsv paayalsryr frgktfveql
      121 valpivyplv mlglalllvf nalsvelglv rlvvahvilt lpftvkncaa svasigpefe
      181 eaaclmgasp rrafvdvvlp lmrpgvlagm lfafivsfne ftvtfflysv dtmtlpvwly
      241 srtvssldpt vfcfavftva idfaliwmle klvgdkgval
//
LOCUS       WP_175829371             316 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase, partial [Burkholderia anthina].
ACCESSION   WP_175829371
VERSION     WP_175829371.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 316)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..>316
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
     Region          1..316
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mtdvvivsaa rtavgkfggs lakvaapelg atviravler sgvkpdqvse vimgqvlaag
       61 sgqnparqsl ikaglpnavp gmtinkvcgs glkavmlaan aiaagdaeiv iaggqenmsa
      121 sphvlpgsrd gfrmgdaklv dtmivdglwd vynqyhmgit aenvakeygi treeqdafaa
      181 lsqnkaeaaq kagrfndeiv pvsipqrkge plqfatdefv rhgvtaesls glkpafskdg
      241 svtaanasgl ndgaaavlvm saqkaaalgl tplarikaya nagvdpsvmg mgpvpasrrc
      301 leragwtpgd ldlmei
//
LOCUS       WP_175829359             120 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein,
            partial [Burkholderia anthina].
ACCESSION   WP_175829359
VERSION     WP_175829359.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..>120
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
     Region          1..>120
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkvlvavkrv vdynvkvrvk sdntgvdian vkmsmnpfde iaveeavrlk eagvstevia
       61 vsvgvaqaqe tlrtalaiga drailvesnd sveplavaki lkalvdkeqp qlvilgkqai
//
LOCUS       WP_175829401             226 aa            linear   BCT 11-JAN-2025
DEFINITION  urease accessory protein UreF [Burkholderia cepacia].
ACCESSION   WP_175829401
VERSION     WP_175829401.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Soriano,A. and Hausinger,R.P.
  TITLE     GTP-dependent activation of urease apoprotein in complex with the
            UreD, UreF, and UreG accessory proteins
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11140-11144 (1999)
   PUBMED   10500143
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Moncrief,M.B. and Hausinger,R.P.
  TITLE     Purification and activation properties of UreD-UreF-urease
            apoprotein complexes
  JOURNAL   J Bacteriol 178 (18), 5417-5421 (1996)
   PUBMED   8808930
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..226
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23922
     Region          1..226
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 mtttelvall hlaspalpig aysysqglea aldanlihda dsardwiasg ltdvlahgel
       61 pflahqlarw hahdthalva enawfvasre saelrreteq mgwslaqlca slewgdaarr
      121 atlaaispia lptafayaaa ahdasadavl aayafgwven qtsaalkavp lgqlagqrii
      181 valrgaidaa vrralatppd avntfapqlg ilsarhetqy srlfrs
//
LOCUS       WP_175829419             269 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175829419
VERSION     WP_175829419.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..269
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29826
     Region          85..268
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mrtwrleran laaqmdvsra trlvaaiggn epnafaaeil klfddalsit qctifayefg
       61 nrprtmsvad hrggrylrdl adtyarhfya ldgnqqivst ahlgtrrhdl llhqqagdei
      121 dheayraacy rgpdvsdrla llmqpgdatw lsinlyrahr sgafqpreia aiealaplia
      181 qaarhhyala gaaqigipqr mlarlrhacp dlskreldvl rgvldgqtah eigetigvka
      241 ssvvtyqkra yrrlgissqr elfalcmqp
//
LOCUS       WP_175829523             324 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175829523
VERSION     WP_175829523.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..324
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35666
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdriqamevf trvvdansft raadtlampr asvttiiqnl eallgvrlmh rttrrlsltp
       61 egaayyehct kiiseiaead asfqtgnrkp sgvlrvhmps slgrrivlps lsifrqrypd
      121 itlelglsdr yvdpveegid cmirvgpled ssmvarrigm lkrvtcaspd ylahhgephe
      181 iadladhhav nfrashgara ipwvfmidgk pfevrmngsv tvndsdayvt cglegfgmiq
      241 ptlfmvlpnl ldgslvevlp dcnpkpkpis ivyphnrhls qkvrvfadwv aevfeatpsl
      301 eggenwrgrv gaqaaklqrg avaa
//
LOCUS       WP_175829540             318 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Burkholderia cepacia].
ACCESSION   WP_175829540
VERSION     WP_175829540.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..318
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33020
     Region          3..296
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(36..37,40,91,105,107,136,168,256,259,295)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(227,232,247,256..258,261,283,287)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 maeivvagel laefvaaerg qgfdspglfa gpfpsgapai fadqaarlga rvayagcvgr
       61 dafgdaivar lerdgvdvar irrvarptgt afvayrddgs rsfvyslsts aaacvdasdv
      121 dtamfdgcry fhvmgsslts esaiaavqrg vieaaragak vsfdpnvrpe mlsfrpmraa
      181 letmlaachl fmpseadlpf fcgpqpaera iagllathpl lervvlkrga qgsvafdran
      241 rvdapafqvd eidptgagdc fggtlvasfv agvpidaalr ranaagaiav trrgpmegns
      301 saaeidrflt ergiacpa
//
LOCUS       WP_175829551             155 aa            linear   BCT 11-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Burkholderia cepacia].
ACCESSION   WP_175829551
VERSION     WP_175829551.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..155
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=16717
     Region          1..153
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mfnavidapf gkvgirtdaa vvreivylpe svkpvdpdtp latravkqie ryfarasarf
       61 dlplaevgsa fqhrvwdvis dippgtvlty gqvakrigsa pravgqacga nyfplvipch
      121 rvvaagglgg fanhddngyy qkvkrwllah egvpy
//
LOCUS       WP_175829571             454 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia cepacia].
ACCESSION   WP_175829571
VERSION     WP_175829571.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..454
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=48587
     Region          161..436
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 menlqsrlls hrlesvirdf hqpvmiwqaa ilvgalcfaw vtarfvhgri darrraagra
       61 pgagaqslkr alfplfgsvf vgaaqlafdp fmstsllsla lvplfgigli yvlfffarrv
      121 fardghthaw lsivekivst vvwaamvltv lgiqrdvlgw ldsvqfrvan ahltllsvis
      181 galwvcvtlm vamwlgsvle drltrastld anlkvvlsrv grallvfaai liglslvgid
      241 vtvlgvfgga vgvglgfglq kiasnyvsgf iilldrslrl gdaisvgglq gvvtqirtry
      301 tvvrgldgne tlipneklit dvvqnqssyl trgyakvavq vaytsdveha lvlladaard
      361 vprvlaepap tpylvgfgad gidlelgfwi edsakgtsgv rstvnrniwr lfsehgisip
      421 fpqrevrvvg lpdsfpaagv aagngavdgr apaa
//
LOCUS       WP_175829589             271 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175829589
VERSION     WP_175829589.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..271
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28938
     Region          16..265
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtraalrasg demscaavgl tlkagartll dgftqafrpg eiwcvagpng agkttllatl
       61 aglqppaggh vaidgrplsa wppaqlaqrr almpqqlhda fsatvfdtvl lnrfpylggw
      121 gwerdgdrva ardalatfdl talasrdvls lsggerqrva laatlcqdap lmlldeplah
      181 ldlhhqidcl talaawldag prtvlfschd lnlarrfath allldgrgha wagpvhdvlt
      241 perasdafgy plvlirengr dallpawper q
//
LOCUS       WP_175829670             331 aa            linear   BCT 11-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175829670
VERSION     WP_175829670.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..331
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=34915
     Region          <14..324
                     /region_name="FAD_binding_2"
                     /note="FAD binding domain; cl46878"
                     /db_xref="CDD:481218"
     Region          48..74
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          79..109
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          114..136
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          208..232
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(224..225,228,231..232,255..256,259,262..263,266,
                     286..287,290,293..294,297,317..318,321,324..325)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          301..325
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mtafsstasl pgthdpdraa lalrlaapda svrrialiel adleesdlvp sfvaalcddp
       61 saevrseaar vlgaweqpdv vdalcgalld pdegvrataa qslselkdaa sgavlcrwad
      121 rpesfvrrav lrglrelrdp gafapalral daehaavrae avavlgwlrd pralpplari
      181 attdaaadvr raavgaigfa apddaatida llaalrdrew qvreeaattl gklrvaaard
      241 plaaaldddy wqvrlraara lgqlrdaaaa pavaallsha isnlrkeaal algelrdrat
      301 laalthaled hdpevrkavr iairqideas r
//
LOCUS       WP_175829672             256 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175829672
VERSION     WP_175829672.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..256
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28434
     Region          10..245
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mtspnvvpls vaplyvqikd tlrarildgt yaphsrmpse helcaafgvs ritvrqalgd
       61 lqkegllfkl hgkgtfvskp kafqnvtslq gfaeamssmg yeivnqvrsv rtvkadrhla
      121 tklnvpegap lveihrvrll nrepvsleqt wvpealgkrl agadlatrdi flvlendcgi
      181 plghadvsid ailaddeivd alqveesspv lrierlthda sgapidyeyl yfrgdafqyr
      241 lridrqktrk parkqr
//
LOCUS       WP_175829680             297 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175829680
VERSION     WP_175829680.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..297
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30025
     Region          1..287
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mevgfcgpgl mgapmirhll aaghrvsvwn rsrnkaealv kdgaqvagtp relaervdtv
       61 fvcvldgrav gdvvfgehgl lagdaaarrl qrivdhssip paatrdyaar aaalgvgwid
      121 apvsggvpga qagtlavmag graadldtvr plidtyasri thmgdagagq taklcnqaiv
      181 tatvtaiaea vglaqasgid aarlaealag gwadsvllqt fvprmtsggh apigalstfq
      241 kdvdaiadaa rdtgavmpvs atvqqvlrlg aaqglagadf aafidivrpg ngrrqas
//
LOCUS       WP_175829759             284 aa            linear   BCT 11-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Burkholderia
            cepacia].
ACCESSION   WP_175829759
VERSION     WP_175829759.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..284
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30483
     Region          1..284
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 mrlidwniqw grdadgvvdl srtvaairgl gdfdvlclqe vtrgfgalpg rpgadqfael
       61 aallpghtiv eaigadlppi eagaprrqfg naiatrlpvg rvfrqllpwp adagapsmpr
      121 valdvelqgp fgplrvvtth leyysarqrl aqvdalrdrh heacahaarp apaetaegpf
      181 satgqpcdai vcgdfnsafg sdaycrflap iadaprfvda wvarhpgrtp pptagvydta
      241 qwsegplacd fvfvtdtllp hvmrceidgd vrasdhqpvl leld
//
LOCUS       WP_175829840            1057 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cepacia].
ACCESSION   WP_175829840
VERSION     WP_175829840.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1057
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113200
     Region          1..1038
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mdfsrffidr pifavvlsiv ifaiglisip mlpageypev vppsvvvrat ypganpkeia
       61 esvaepleea ingvegimym ksvagsdgsl qvvvtflqgv dpdtaavrvq nrvsqalsrl
      121 pdevrqygvt tqkqsptplm yvslyspdns rdslylrnyl tlhvkdelsr ltgvgdvgls
      181 gsgdyamrlw ldpnrlasrg ltasdviaav reqnvqvsag qlgaeptpkk ndfllsinvr
      241 grlrtaqefg divlrngddg qvvklsdvar velgagdytl rsyfndkqsa vvgiflspga
      301 nalevakavy akfdelskrf ppgvayrpvw dptvfvrdsi ravqhtliea vvlvvlvvil
      361 flqtwrasii plvavpvsvv gtfawlyllg ysintltlfg lvlaigivvd daivvvenve
      421 rniaqglspr daahqamrev sgpivaialv lcavfvpmaf msgvtgqfyr qfavtiaist
      481 visainsltl spalaakllr phgapkdalt rgldrafgwl frpfnrffdr ssdryhgvvs
      541 htlkrrgvvf avyaallgat alllnavpgg fipvqdklyl fagaklpega slartsevte
      601 qmtkialgtd gvemvpafag lnalqgvntp nitnsyvilk pfdqrhrsaa qinadlnarf
      661 atigggitya lmpppiqglg ngsgyslyle drgglgygal qnaltafqaa vaktpgmsyp
      721 vssyqanipq levkvdrlka kaqgvaltdl fstlqvylgs myvndfnlfg rvyrvmaqad
      781 aghrqtaadi anlrtrnakg emvpigsmva vvpafgpdpv vryngypaan ligdadpkvm
      841 sssqaieklq qiakdvlppg ivlewtdlsy qqvtqsnaai vvfplavmlv flvlaslyes
      901 wtlplavili vpvcicaalf gvwlsggdnn vfvqvglvvl mglacknail ivefarelei
      961 qgkgvieaal eacklrlrpi vmtsvafiag svplliggga gsevraatgi tvfagmlgvt
     1021 lfglfltpvf yvairklagg tpavwsehhg tlegenr
//
LOCUS       WP_175829912             157 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia cepacia].
ACCESSION   WP_175829912
VERSION     WP_175829912.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..157
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16983
     Region          1..144
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mytkimiamd gspsskqalv egiklarlcg aslfvvfvvd rstlfayggr vepeellnei
       61 rhygesvlrd avqaisnaal rgdreiiete agqdvperlq ryvvdnsidl vvigthgrhg
      121 vrrlflgsva erflrgstcp vllvrgndva ratsaaa
//
LOCUS       WP_175829964             212 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cepacia].
ACCESSION   WP_175829964
VERSION     WP_175829964.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..212
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22421
     Region          19..205
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msasaavlai laalflgami pgpsfvlvar naiglsrrdg latalgmgig givfggvala
       61 glytllqave wlyvglkvag gayliymask iwrgadrpia mddpqamggg sarksfwtgl
      121 ttqlsnpkta iwygsifaal lpqhpplwcy lalpplvfgv efgwytival cfstrrprel
      181 ylrakkwvdr vaagaitllg lrlilnapka gi
//
LOCUS       WP_175829976             395 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia cepacia].
ACCESSION   WP_175829976
VERSION     WP_175829976.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..395
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42900
     Region          8..390
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mfdhlqrpef valraavlrf vddelrpier elrldsedvw prdvlrrvwq rsaalgfyta
       61 slpveiggqg lsiaetcalk adlaasgaal aphvlgelgg pprignmlky atpaqleryf
      121 kpvmrgekst cfaltephsg sdamsirtta vedgdslvin gtkhyisgap fadfaivmcv
      181 tdatatppqi tavlvdldlp gvrveheyvp msgqhidadi rfvdvrvpre nvfggvgngf
      241 rlgmsrinvn rllhcptmlg lamsayrasl dhartrrqfg gpiarfqaiq hmladmaaal
      301 wacesmiaht aaladagadl rmtasackly vsercfevad kavqihgnvg vtrghpveqt
      361 frklrmfril tgtseiqrna iakailepag agrea
//
LOCUS       WP_175829979             451 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175829979
VERSION     WP_175829979.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..451
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47835
     Region          22..426
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(35..36,39..40,43,83,141..142,144..146,149,169,
                     172..173,176,258,261..262,265..267,270,297,301,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 myptdtvqsp saarpladrq lrriviasva gnamewydff vygtaaalvf ghvffppgas
       61 plagslaafa afalgfvarp lggivfghvg drygrkaslv wtllimgast faigllptya
      121 qvglwapaal vvlrllqgia sggewgggvl misenappeq rgyyaawsql gvgggfvlss
      181 aaflaaqalp ddmfrtwgwr lpflasiaif aigiyirrhl pesrdfeqag qrgahthlpi
      241 vecirrhpke illamglrva enggayifla fslvygkyvg ipngvmltgv miamivemga
      301 mlawgrlsdr igrkpvylig alslvacafp ffwlldtrat plvwlaltvg tavshgamig
      361 tlpalvgelf stevrysgva lghevasifa ggmspliata llaryhaswp vslflvalgl
      421 vtvatlcvmr etrivraapa apatntrgdt a
//
LOCUS       WP_175829987             128 aa            linear   BCT 11-JAN-2025
DEFINITION  tautomerase family protein [Burkholderia cepacia].
ACCESSION   WP_175829987
VERSION     WP_175829987.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..128
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=13015
     Region          2..59
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
     Region          67..123
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mptlevflpa ghddarkael iarlsgatvd aigtplesvr vlltelpath iglggrtaad
       61 gappslpviv ailiagrtde qkraliaals daganvldap lqatrviikd ipntdfgigg
      121 rtaralgr
//
LOCUS       WP_175829994             569 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175829994
VERSION     WP_175829994.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..569
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=62030
     Region          22..529
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 msrtfdyivv gggsggcvva grltedpavt vcvleaggrg dgtlvnvptg avammptrvn
       61 nwafdtvpqh glggrigyqp rgkalggssa inamvyirgh rvdydgwaal gnegwayddv
      121 lpyfrlsehn erfddawhgr dgplwvsdlr tgnpfharyl eaaqqaglpl tddfngaqqe
      181 gigiyqvtqk hgerwsaara yllphigrrd nlavethaqv lrilfdgtra tgvevrqhge
      241 vrtlrarrev vlaagalqtp qllmlsgvgp ggelrqrgia vhadlpgvgr nlqdhpdfif
      301 gyrtrsvdtm gvsarggvrm lrelarfrre rrgmltsnfa egggflktra dldapdiqlh
      361 fvvalvddha rklhaghgls chvcllrprs rgsvtldsad plaapridpa ffddprdldd
      421 mvagfrltrq lmeapalagw ttrdlftanv dtddeirdvl rrrtdtvyhp vgtcrmghda
      481 lavvdpqlrv rglqglrivd asvmptlvgg ntnaptimia ekavdlirgv crtptrpqre
      541 pvrtatdtvp asraahetvq peetrhvva
//
LOCUS       WP_175830001             603 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175830001
VERSION     WP_175830001.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 603)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12379621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..603
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62779
     Region          1..289
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
     Region          329..603
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 maswldytln glivgniyal lavglalifg vshlinfahg svymvgafig wlcltrfglp
       61 lpvalaavvv gcgalgvaie riglrplrha ariapllati gisfildqla qlafgadpra
      121 vptplpdwhl riagatlgsl dlliagigia aaallygflr ftrlgwavra taqdrdaalq
      181 mgvdvdrvnq tvfaiacalg gvsgllvgmy ynsidpamgf qatlkgvval ligglgnvpg
      241 aiagslllgl vesygvalfg tsyrdlfafg llivflvwrp nglfsgnral ppepmtgtfl
      301 aaakavrvpr pvlvaliasa avlpwlgasp yvlqtltnaw lygllalslt lvagtvgqis
      361 lghaallvig ayasallssd lgwspavtip cagvitavlg tllvypafrl rghyvsiatl
      421 gigevvslvi lnwdgltrgp lgitgiaplp wastaraayw ftfavlvgfa lvqvrllrsh
      481 lgrtlravre ddvaarahgi apnrykaiaf aiggvaagvs ggiaahlysy inhqtfdsqv
      541 silaltmvil gglgnvlggi vgaialiglp elfrwaadyr mliyglvlll lvrfrpqgll
      601 gtv
//
LOCUS       WP_175830023             238 aa            linear   BCT 11-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Burkholderia
            cepacia].
ACCESSION   WP_175830023
VERSION     WP_175830023.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..238
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=25046
     Region          14..208
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mngipttfiv qgalwllvvf svvtwtlivv ktiqslrasa rnrhytrafw aansfheaaa
       61 ldgadspvge laatgfdalr raddssahdl ehswsrhdll erhlrqqihn arrraeagla
      121 vlasigstap fvglfgtvfg iihaltaith sasasidvva gpigealvat gigiavavpa
      181 vlaynffvrr vkaasadlda fatdfvtlaq kagfrvpaaa ttpaparrad garqeafa
//
LOCUS       WP_175830063             177 aa            linear   BCT 11-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Burkholderia cepacia].
ACCESSION   WP_175830063
VERSION     WP_175830063.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..177
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18760
     Region          1..165
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtpahlipsp lgdiavried daltglyfvg qkyfppvaiv teadalatpp iarkvaeeia
       61 eyftgtretf svpiqlrgta fqrrvwkell aipfgelvty gditervglp msgaravgga
      121 vgrnpvsimv pchrvvgasg sltgyaggid rkrallsleg aefergtghp vqqalaf
//
LOCUS       WP_175830099            1068 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cepacia].
ACCESSION   WP_175830099
VERSION     WP_175830099.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1068
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=114746
     Region          1..1046
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 miariirwsv hnrflvllat vliaawgvhs lgqtpldalp dlsdtqvivk asypgkapqi
       61 vedqvtyplt ttllgvpgak tvrayssfgd afvyvlfddr tdpywarsrv leylsqvqsr
      121 lpagatvslg pdatgvgwvy eyalvdrtgr hdpgqlraln dwflkfelka vpdvsevasv
      181 ggmvrqyqvv ldpdrlrayg itqaeianal gnanqasggs vvelaeseym vrstgylrtl
      241 ddfrhvvlrt ndagtpvllg dvariqvgpa mrrgiaelng qgevtgvvvv mrsgknaltt
      301 idavkaklad lkrslppgve ivttydrsql ieravgnlkd klieefvivg ivcavflfhl
      361 rsafvailsl plgvlaafiv mryqgvnanl mslggiaiai gamidaaivm ienahkhlea
      421 ydhahpgepv taarrwelva tsaaevgpal ffslliitls fipvfslegq egklfaplaf
      481 tktytiaaaa glsvtlvpvl mgylvrgrip hehanpinrv lirvyrplle atlrrpwvai
      541 gvavvalglt avplsrlgge fmppldegdl lymptalpgi sadkasellq qtdrliktvp
      601 evdtvfgksg radtatdpap lemfettirf kprsawrpgm tpeklvdeld ravkvpglsn
      661 vwvppirnrl dmlstgiktp vgvkisgpdl agidavakqv eaavkrvpgv tsalaerlng
      721 gryidvdidr laaaryglsv adiqsvvssv vggddvgevi agrerfpinl ryprevrdsv
      781 enlrqlpvvt argaqirlgd variaiadgp pmirsenarl sgyvyvdird tdlrsavram
      841 qqavaqqval ppgysiawsg qfeyleraaa rlrtvvpvtl vvifvllflt fgsaadalll
      901 mstvpfalvg gfwlvwalgh avsvatsvgf ialagvaaef gvvmllylkg alqrrldage
      961 pltdalllda iregavlrvr pkamtvavvl aglvpimvgh gagsevmqri aapmvggmvt
     1021 apllsmfvip aawlllqrrh arstgrvrhs davphgtnvp siptgesr
//
LOCUS       WP_175830087             336 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175830087
VERSION     WP_175830087.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..336
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35717
     Region          9..332
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 msqstcsard ivvvgfegvq slditgpmev favanrhlpd halpyrltla sqhgddivth
       61 aglrlagtap laalpgqidt ivvaggneaa lrhaaseagv lpwlrtriad trriasictg
      121 afvlaaggwl dgkratthwn qcatlqalcp dariepdaiy vsdppfhtsa gvtagidlcl
      181 alveadcgap talavarelv lfvhrpggqa qfsvgldiqa natprmrtll tgiaddptgd
      241 lgvaalaarm hmsertfarn flketgrspa qfvlaarver akalleradw pleriaersg
      301 fgsvdalqra fakqvgvsph dyrarfgvrr drqria
//
LOCUS       WP_175830101             430 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia cepacia].
ACCESSION   WP_175830101
VERSION     WP_175830101.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..430
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46560
     Region          38..419
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 msfhpgtpla rrarrrapml waallvagaa haqqpsftld aalqsatdhs asmqaaqasv
       61 rasseaavka gqlpdpmlka gidnlpvngg qrftvgqdfm tmrrigieqe wvsgdkrrlr
      121 salaneqvgr eragylaqla svrqqtataw lnavyakqal alqqalldhm nhefdatkas
      181 yrgakasaad vvqaramlaq tqdqwlkarq vyqtalials rwtavpasdv tgtppapesf
      241 vsslppdelr vsqpalitaa ddiavaeadt avanserrpn wtwevayqqr ggaysnmvsv
      301 gvtiplplnr rnrqnrdvae kaelatkarl myedtlrqvq adirtqsetl asgrerianl
      361 sasllpaadq rvqlanaayr agtgsladtf aarraqldaq lqvldlrrdv sqtwaqleyq
      421 vvpstmaaaq
//
LOCUS       WP_175830146             330 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175830146
VERSION     WP_175830146.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..330
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36784
     Region          3..327
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpraailayd dcyasslggf adilqianah wrrqrgdgnv qfewrfvspt gkpvmasngl
       61 qlntepirpr ekfdlvfips ahyasgkafd rllarqsaac dwlvsqwnag aylaanctgt
      121 fvlartglld erpatttwwl adqfrsrfpr vdlqlepvvt eadrlicaga sasyllqtih
      181 vierfcgaai aaqcaktmli dvsqtkqlpy lplladkeha dslvhraqyw lqknmtkdvk
      241 msemahelgv sertiirrfr aalnqpplry lqnlrieaar glleagdlgl eqitaqvgys
      301 dtssfcrlfk dkvglspgay rdrfrptges
//
LOCUS       WP_175830150             958 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia cepacia].
ACCESSION   WP_175830150
VERSION     WP_175830150.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 958)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..958
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..958
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=104133
     Region          42..957
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mknhglsrrg flkasvlagv avyvaplgsr afaalfeekl ltpvkwdsvt gipqfridgi
       61 akvtgskvfa rdvraadmph wpqqqshali lrvtqadrty egfdlsllgd elkpdrvvta
      121 ddlvrdgvaf pafygddmll pagktpaylg havailiyhd farfrfakna lkfrddviry
      181 gavtgplerd pwgtfryvrv ggktaydddv ysslkdapif psmmrkhlpv wpdgkehgkl
      241 deqgmflagq iaseldhpsa dwlvfdreyn tqsvdtaale pdnancwyda atqslhlvvp
      301 tqsplevaen aaamvakcrf pvkklfvhpc ytvgygskdh fnvpfyglvc alyadgrpvr
      361 fandryeqfq tslkrhafkm hyriavdrnt gllqsfkgdf eangggrsnf spsvamvgat
      421 aaqsiyyfpk sdlaavaias raidagsarg ygtlqsmaat emavdeiaaq lnidpidfrl
      481 rnalrsgmkn tqgaipagal rvdevlersk qhplwtrraa rkaeyeaahp gkrygvgfac
      541 vqkdfgtgae asfakvefde ngkvslrhta aeigtgmsts qavavvkwlg rpatdvqvav
      601 tewpdlpvet sgdpyimsqa dqdrlsanpr wspsyaspss atnsayyfth streaaravf
      661 ryglwpaams iwtrglgggq aapytiried arwvdgklta dgleplsfeq lakqahalgl
      721 ptgavvhvfn rwqwtdaefe vggvvdrlpi dglslrvgap ktgdngpvpg taapagatam
      781 rgtlaptang yrvldrkrvf ipptsrnnaa vtyytavgtl velavheatg kvellthhsi
      841 mecgnqispq lvsgqlqggl amgighalhe ylplyedgpg ngtwnfnryq lprasdvavw
      901 tqtgdvlppl setdppkgva evvmipvvga ivngiahaig hrftdlpvtp qkiqevla
//
LOCUS       WP_175830276             724 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cepacia].
ACCESSION   WP_175830276
VERSION     WP_175830276.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..724
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78666
     Region          23..724
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mttrmdhpra rrvttgrcss aplafsalcl asswanaqgs papaggmlpv ltvvgtkdad
       61 attegsgnya akwatiggkv aqsiketpns vsvltrermd dqnvttiqqa lrsvtgvssi
      121 dygdgtayfr argsqlgief dgvptlsglq yqlqfdlamy drveilrgpa gsidgmgepg
      181 gvvnlvrkrp qdqfhvgtet qvdsfgsvrq midvtgplnk dgtlrgravl vggtgtqsie
      241 rtrskevmay galdwdltpr ttlsfsggyq vspisgidyg aggvlnstrt altgrvpsey
      301 trnfspswny aytslqevna nlvhrfenaw qssttlfyrh elskayyays gpgatangla
      361 rfgdqrqrts ydwfgadtnv sgpvrlwgqt htltiganya vmtsgaqsgy ralsgpygga
      421 yslydpnavp avdvpytfgt nhrtvqygvy aqariklatp ltlvlggrea flqdrtqstl
      481 psvadwttna qvnhrflpsa gllwdivpsl tayanyarfl daqtqgtysg pglpprsgeq
      541 yevgikssll dgrlnanaal frinddnrav adpahqfyyv sagkarnqgi eleltgqptp
      601 dwnlyagyty lnahyendsp dltdgtdpkh lfklwtrytl sqgplrgfsi gggmlaqtri
      661 srgveqggya vfdaqagyrf tkhvtaslql nnvfnrryyi rppstyysvf gdarnvmltv
      721 rsdf
//
LOCUS       WP_175830248             139 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia cepacia].
ACCESSION   WP_175830248
VERSION     WP_175830248.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..139
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14760
     Region          27..138
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mtpnqpflas qrdvllllar vllvilfvmf gwkkivdfpg tiafmgsega papiisaais
       61 vvmelfvgva ilvgfqtral alllalytig tgiighhywt mtggeqinnm ihfykniais
      121 ggllalcaag pgrfsidrg
//
LOCUS       WP_175830349             330 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175830349
VERSION     WP_175830349.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..330
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35193
     Region          4..321
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mgallevdnl gvrftrkdap pvdavsgvsf sleagktlgi vgesgsgksq tvmallglla
       61 gngtttgaar yrgdnllemd aralnkvrgd riamifqdpm tslnpfltie rqmtetlqlh
      121 rklsrkeatk raiealesvr ipdaarrirm yphefsggmr qrvmiamall sepeiliade
      181 pttaldvtvq aqiidllrel nrergtaivl ithdmgvvag laddvmvmya grtveyapae
      241 sifaapshpy tigllnalpr ltdaddaplv aipgnppmpg tapagcafak rctyaeercg
      301 aarpaletyg avgavrachr pvadmtgglr
//
LOCUS       WP_175830355             470 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175830355
VERSION     WP_175830355.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..470
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47807
     Region          18..442
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(25..26,29..30,33,65,115..116,118..120,123,144,
                     147..148,151,274,277..278,281..283,286,314,318,370..371,
                     375,379,395,398..399,402..403,406)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtaavpnraa arrvlaatcv sytlvlldas ivnvaltdia htfgsriagl qwivnaytla
       61 fasllmmggt lgdrlgdrtv yvaglaifva asalcgiaps lpalaiaral qgvgsamlvp
      121 cslallnraf pepaarasai slwmgcggia masgpliggl lihlsgwrsl ffvnlplgla
      181 giwlaravtr aagdasrhfd wggqaaaiva iatligtlie gpslgwrsap ivggaatsav
      241 awvafiaiea rrrepmlpla ffrnrlfags tfvsmasafv fygllfvlsl fyrqirgasp
      301 ldtglaflpm tamvalgglc sgrlvarfga rgsmcaafal yaagalgmtg igaatpawla
      361 vapmlaigfa sgfispaats palgtvdrrr agvaaaalna arqsgsalgv aifgaciatv
      421 qpfpvamrvt llaavaisas ampmwwiatr tgkapkvgar tagirvaege
//
LOCUS       WP_175830385             158 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Burkholderia cepacia].
ACCESSION   WP_175830385
VERSION     WP_175830385.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..158
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=17384
     Region          5..153
                     /region_name="OsmC"
                     /note="Organic hydroperoxide reductase OsmC/OhrA [Defense
                     mechanisms]; COG1764"
                     /db_xref="CDD:441370"
ORIGIN      
        1 masgehkyrv avawtgnrgt gtsgyreygr dhviragskp eipgssdpaf rgdasrwnpe
       61 dlllasasac hklwylhlcs eagirvlayv ddaegtmvdr depgrfteiv lrphvtiqag
      121 ddreraehlh hdahakcyia nsvnfpirce ptiefaav
//
LOCUS       WP_175830376             432 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175830376
VERSION     WP_175830376.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..432
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46008
     Region          18..415
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,150,
                     153..154,157,249,252..253,256..258,261,289,293,351..352,
                     355,359,375,378..379,382..383,386)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 msstsgvaam tvgksavrwk ifvvmlslia inyvdrasls vampyisqef nigpamegli
       61 lssffwtyav mqipggmlad rfkpriviat atvfwgffqa iaalctnaps llltrlglga
      121 aeapiypagg klnaiwmtqt ergrgatlld ggaplgaalg avliagliav fgswrlafav
      181 agvgtvlagl lawhyirnsp rehagvndle aeyieashas dlaaepagas grsrdffkyr
      241 svwcmffgwm cfnsvfygll twmpnylhkv hgfdikqmgg stfiiffsgf vgellggwia
      301 dkwkaaggrp nvvmrtlfgi aaviatvsif svayvkdpvv cvallsstlf flrwcglywc
      361 ipsslgtrnk igflgglmnl ggniggvtvp ivvgaivqft gsyflalmvf aaagvgllvc
      421 ssaidyenkl pv
//
LOCUS       WP_175830388             382 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175830388
VERSION     WP_175830388.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..382
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41067
     Region          1..370
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masismrrvq kaygdhepvi rdvdleigah efcvflgpsg cgkstllrmi agledlsage
       61 lsidgrrvdd vpaaergvam vfqsyalfph mtvyenmafg lklarvpkae idrkvrdaar
      121 ilqldtller kpkalsggqr qrvaigraiv repgvflfde plsnldaalr gqtrieiarl
      181 hrqferasvv yvthdqteam tladkivllh agadtaqhgs iaqvgapldl yhhpasrfva
      241 gfigsprmnf lpavvtacda rrttvtltps getftlprdg salgagaavt lgirpehltl
      301 gaahdattla rdvalverlg eqtyvhldqp gghaliakvp gdaqvrtger vhvhapaaac
      361 hlftedgrav pacadvhvhh ya
//
LOCUS       WP_175830403             212 aa            linear   BCT 11-JAN-2025
DEFINITION  2-hydroxychromene-2-carboxylate isomerase [Burkholderia cepacia].
ACCESSION   WP_175830403
VERSION     WP_175830403.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Thompson,L.C., Ladner,J.E., Codreanu,S.G., Harp,J., Gilliland,G.L.
            and Armstrong,R.N.
  TITLE     2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class
            glutathione transferase from Pseudomonas putida
  JOURNAL   Biochemistry 46 (23), 6710-6722 (2007)
   PUBMED   17508726
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122490
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..212
                     /product="2-hydroxychromene-2-carboxylate isomerase"
                     /EC_number="5.99.1.4"
                     /GO_function="GO:0018845 - 2-hydroxychromene-2-carboxylate
                     isomerase activity [Evidence IEA]"
                     /GO_function="GO:0043295 - glutathione binding [Evidence
                     IEA]"
                     /GO_process="GO:1901170 - naphthalene catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23370
     Region          9..188
                     /region_name="DsbA_HCCA_Iso"
                     /note="DsbA family, 2-hydroxychromene-2-carboxylate (HCCA)
                     isomerase subfamily; HCCA isomerase is a glutathione (GSH)
                     dependent enzyme involved in the naphthalene catabolic
                     pathway. It converts HCCA, a hemiketal formed
                     spontaneously after ring cleavage of 1; cd03022"
                     /db_xref="CDD:239320"
     Site            15
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239320"
ORIGIN      
        1 mnaartaswy fdfvspfayl qqeqfdrlpa aaafeprpiv lgallshwgq kapaeiatkr
       61 vftyrhaqyr adklgiafrm ppahpfnpir plrlaiamgs spdairrifr hiwrdgqdvs
      121 tpegfaalce avgfpegvta veaqpvkdal rantddaiah gvfgvptfel dgdlfwgeda
      181 tdmfadcats rawldspevr risalpegir rg
//
LOCUS       WP_175830421             376 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia cepacia].
ACCESSION   WP_175830421
VERSION     WP_175830421.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..376
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=40767
     Region          7..376
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkrktlalsi aaaglcagtq ahaqssvqly glmdlsfpty rthadangth vigmgnegep
       61 wfsgsrwglr gaedigggtk iifrlesefv vangqmedeg qifdrdawvg vederfgklt
      121 agfqntiard aatiygdayg sarlsteegg wtnsnnfkqm ifyaagptgt rynngvawkk
      181 lfsngifasa gyqfsnstsf atgsayqaal gynggpfnvs gfynhvnhng frnqtfsvgg
      241 nytfdivrln agyfryngdq gplgqrhdds wtvsmkiapk galdyelgyq qmriknaann
      301 adgftpnanl gafsltngva ngfketiygs vfyhlskrte vylagdymkl hggytvsstf
      361 gaknqlelts girtrf
//
LOCUS       WP_175830444             476 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175830444
VERSION     WP_175830444.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..476
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49554
     Region          21..476
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mqnrnttaag gepagtplsg daleavlvae lgdalvtraa didpryftay nepagarpra
       61 lvrprsvddv srtlalcarl gqtvvpqggl tglargaval ggevvlsmer fagvealdaa
      121 agtmtvragt plqtvqeaae aagftfgvdl gargscqigg mlatnaggtr airygmmreq
      181 vlgleavlad gtvvssmnrm lknnagydlk qlfigsegtl gvvtravlrl hpllaapata
      241 lcrvrdydav ialwnrvrtl pevvsfeamw pafydyvarh tpgvsapfvg ddgfavliec
      301 atsapdgdah qaletglaag ieaglvedav latserqard lwtlreglai dalphlvnfd
      361 vslptgelgv faerceaalr mqwpdavclf fghvgdgnvh igvslagmsd adadaldhcv
      421 yavvrdmggs vsaehgigvl krpylahtrs daeiglmrcl kaaldpggil npgkvl
//
LOCUS       WP_175830449             537 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175830449
VERSION     WP_175830449.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..537
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53860
     Region          23..440
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,279,282..283,286..288,291,319,323,375..376,
                     380,384,400,403..404,407..408,411)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mdqpfsaast qsarrrawvl aavcmaaval plsfsggava tpaigrdlhg gtvamnwitn
       61 afmlafgscl maagaladqf grkrvfaigv ggftlmsval afapsmlavd llraaqglaa
      121 aaalaggtaa laqefdgaar trafsllgtt fgiglafgpv lagalighgg wrtifvtsav
      181 agglslgfgl prmhesrdph atgldwpgta aftaaltlft fgvieaparg wsnalviall
      241 agaalgacaf vaietrvarp mldlslfria rfvgvqvlpv stcccyivll vvlplrfigi
      301 dgfseidagw lmlaisapml vvplvaatlt rwltagvisg lglliaaagl vwldvalrgg
      361 agpaaiapml aigvgagmpw glmdglsvsv vpkeragmat gifsttrvag egialaivga
      421 vlaalaqtgl rqaagaastp eatlraaarl atgdlagaaa alpgvghaal lasyahafdr
      481 lliglavvtv lcavvvfvfl ggrrvaaeag dgtdghahad vpvrsridaa ctethgr
//
LOCUS       WP_175830457             779 aa            linear   BCT 11-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Burkholderia cepacia].
ACCESSION   WP_175830457
VERSION     WP_175830457.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 779)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 779)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18771781
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..779
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..779
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=84147
     Region          19..133
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Site            order(30..31,33,57,60..61,64..65,67..68,91,94..95,98..99,
                     102)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          55..85
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          178..754
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          211..237
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          245..271
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(247..248,251..252,254,278,281..282,285..286,
                     288..289,312,315..316,319..320,323)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          276..306
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          311..339
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mfstelpasa altpeqqlaq dialvmenal erqrsgafde arvlyeaile avpahgdahy
       61 nlavlmvdtg qaadavphfe aalgaspdng yywvsyihal hrsgqtaaaw iaveiaqqrg
      121 vhgpalngli aqlaspdivl ataavaaaps gidaaivlet aagrsdsgkp arrpnqtllq
      181 khaalfdknr haeatalark lvadypedga cwralsaslh regrfaemie aglrtvellp
      241 nevlvrilla dtlramnrla eadeqctrly qlqpdhpeam rirglvlfal rrtdealaac
      301 rravelapga aapcgtlgfv llelgatqea igwlkraiei nptdsvthss mlfciahsse
      361 fdpqalvaeh rkfgerydnq krkraavfsn prdparklqv gfvsgdlysh avasyavpvi
      421 ehlaadpgia mhfyhnhfee dhtserfkah attwrnvtgm sdsaflervr ndhidividl
      481 sghtgrnrlv alaqraapvq aswigypatt glaamdyylt drfvaphgaf ddqfveqivr
      541 lpaiapfmpp pncppvnvlp alhngyttya sfnrlnklsp hvievwarvl hadptarmal
      601 gaigsdgdqq tltewfaaag idagrltfhr rsnipvymqq hhgvdlclda fpytgstttl
      661 nalwmgvptv tipgatmagr gsagwlqhvg ldayiatded dfvaralalg rdtaalqalr
      721 aglrarcges aafrpavvaa glssalrtmw trwcagepat afdtplfddt ttaqaaaea
//
LOCUS       WP_175830483             423 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia cepacia].
ACCESSION   WP_175830483
VERSION     WP_175830483.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..423
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=43930
     Region          207..415
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(214,254,292,395,398)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(214,395,398)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(214,254,292)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 msfrssiaaa vlgaaafvsp lvasasaapa gwvaawatal qpipdlaapp plyrapdvag
       61 rtvrqivypt vsgraarirv snaygrfplv veaaslarag egaalsgdaa vpvrfggkvs
      121 vtlapgqele sdpvgidvra gqpyaislqm gpnqrmtvwh rvsnqfnyvs vpgehvsdpg
      181 aaafrtrftq fawvtelave tgsarasvaa igdsitdglr ssvnrnrrwp dalarrlaas
      241 gaesigvanl gisgnrllsd sacygtslas rferdalsra gvkaaivlig indinfaamp
      301 pragldcdhp htqvtaasli dgyrrlidaa hrqgvkvfga tltpaglpag reairlevnr
      361 wirsgggfdg vvdfdavlrd parpsvlqrr fdsgdgihps dagytamaaa vpveqlqaav
      421 ggk
//
LOCUS       WP_175830471             385 aa            linear   BCT 11-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Burkholderia
            cepacia].
ACCESSION   WP_175830471
VERSION     WP_175830471.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..385
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41041
     Region          17..299
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mstfsgdaqs adkhavarks tfvsivlnvv latfqivvgt iahsqaliad gvhsisdlis
       61 dfvvlvanrh sgaspdadhn yghsryetva slflgailia vgvgmlwrag drlvnlenip
      121 avhfsalvva ltvlvskeal frymlrearr vrsamlvana wharsdaass fvvaigivgs
      181 lagvrlldpi aaaivgfmva rmgwtfgyda lqdlsdrald ttdtaeiral laatpgvrdv
      241 hdlrtrkmgd aalvdahilv dpmisvsegh yiaetararv lrdprvldal ihvdpendaa
      301 rrpalalppr geiaarleaa laqrglhaaa inlhylstgl eidvtlacdp hdtdaalagr
      361 ldvdalkref garrigftrt mpaqa
//
LOCUS       WP_175830492             790 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia cepacia].
ACCESSION   WP_175830492
VERSION     WP_175830492.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 790)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 790)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..790
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=83399
     Region          74..753
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mirrpkaagk ggamrgallg palgaialfg lstgsaraqq padgtaatgg avppaavava
       61 pqvpqasqap avtlptvvvv gttpllgigt plqkvpanvq tvraaeldaq hratladffa
      121 anlqsvtise aqgnpyqtdv nyrgftaspl lgtpqglsvf vdgvrvnepf gdvvnwdilp
      181 tqaidrmqli pgsnpvygrn tlggalaitt kngksnpgge aevsggswgr ktaaieqggt
      241 igsnldyyat anvandggwa dhnasrvrqa fgklrytdsd ttlsisagga dnalygtqti
      301 prsfldnrkq aytypdlnrn sagyltlsgd rffgehvels gnayyrhlrn tnvssnnntd
      361 ygsvdddgtv davqgtnaqs tivtdsyggs lqltllgklg gmanqliagv aadvanssyv
      421 assqdayftd traaigvgdf epqtraktrn anlgvylsdt lsltphwtlt vsgrydwska
      481 qigdesgvqp lldgnhvfsr fnpalgvnwn pvagftayat ynegmrspta ielacadpaa
      541 pcslpndfia dpalkpvisk tfeagmrgri gaattwsaaa yrttltddiq fisspasaqg
      601 yfrnvgdtrr qgielagrtr fgplgvglsy syvdatyrss wtehspansa adangnvavk
      661 qgdhipgipa htvklrldya atprwdigan vtwrsgvyar gdennqdvng riagyvlvdl
      721 dmryritkrf evfasvtnlf dkryasfgvl gqnffngpnh tfdganpvne qfvgpgaprg
      781 awvgvryawd
//
LOCUS       WP_175830496             247 aa            linear   BCT 11-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Burkholderia
            cepacia].
ACCESSION   WP_175830496
VERSION     WP_175830496.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..247
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=25945
     Region          5..210
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mtiygiehvw tqgdpmtrav alllvamsia swtvivikai elvgirrraa raeahfrgpg
       61 gaagamhalg grdrpfvdlv ragqaaiahh easrhrlhdr idasdwlsrs lktsvdesaa
      121 rmqrglgvla sigstapfvg llgtvwgiyh allslgatge asldrvagpv gealvmtafg
      181 lcvaipavlg yntlvrlsrd ivarlnrfah glhlllltgs vpetaarpep atrmpadlqp
      241 aadgara
//
LOCUS       WP_175830521             318 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cepacia].
ACCESSION   WP_175830521
VERSION     WP_175830521.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..318
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33371
     Region          80..293
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mlepeiaafv aavdawypad aaerapaeqr rlydrfaaew tpaalpagiv qqdavcqapd
       61 graialrryt saqgaprgtv lffhgggfvv gsldshalit aqlaadtgld viavdyrlap
      121 ehrapaaled clavtraard arwpfgpcah pltlagdsag gmlaaavata lrdageggvd
      181 gialvypmlg fepqsparet eahapmltld dvhryralyw ngglsdalgd gnpllrasvp
      241 laaarfdglp pvlaigaehd plrddarvyv eriraaggaa hywmgeglvh gcwralgtsp
      301 qaarmhrtvg gfllapha
//
LOCUS       WP_175830547             433 aa            linear   BCT 11-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Burkholderia cepacia].
ACCESSION   WP_175830547
VERSION     WP_175830547.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..433
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46430
     Region          14..431
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 mslnddptfw rnarqhlvry ggtfepmiie rakgsfvyda dgraildfts gqmsavlghs
       61 hpeivsvige yagkldhlfs gmlsrpvvdl atrladitpd gldralllst gaesneaair
      121 maklvtgkye ivgfaqswhg mtgaaasaty sagrkgvgpa avgsfaipap ftyrprferd
      181 gaydylaeld yafdlidrqs sgnlaafiae pilssggiie lpegymaalk rkceergmll
      241 ildeaqtgvg rtgtmfacqr dgvtpdiltl sktlgaglpl aaivtsaaie erahelgylf
      301 ytthvsdplp aavglrvldv vqrdglvara nvmgdrlrrg lldlmerfdc igdvrgrgll
      361 lgveivkdrr tkepadglga kitrecmnlg lsmnivqlpg mggvfriapp ltvseeeidl
      421 glsllgqaie ral
//
LOCUS       WP_175830558             441 aa            linear   BCT 11-JAN-2025
DEFINITION  leucine-rich repeat-containing protein kinase family protein
            [Burkholderia cepacia].
ACCESSION   WP_175830558
VERSION     WP_175830558.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Shen,K., Hines,A.C., Schwarzer,D., Pickin,K.A. and Cole,P.A.
  TITLE     Protein kinase structure and function analysis with chemical tools
  JOURNAL   Biochim Biophys Acta 1754 (1-2), 65-78 (2005)
   PUBMED   16213197
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
REFERENCE   7  (residues 1 to 441)
  AUTHORS   Hanks,S.K. and Hunter,T.
  TITLE     Protein kinases 6. The eukaryotic protein kinase superfamily:
            kinase (catalytic) domain structure and classification
  JOURNAL   FASEB J 9 (8), 576-596 (1995)
   PUBMED   7768349
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..441
                     /product="leucine-rich repeat-containing protein kinase
                     family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=47004
     Region          <2..>186
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          39..61
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          62..81
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          82..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..175
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          214..>375
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(214..217,220,222,238,240,269,287..290,345,349..350,
                     352,362..363)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270622"
ORIGIN      
        1 mthtlellqa gqlagarqlk lacgltafpr eifdladtle vldltgnalt alpddlprlh
       61 rlrilfasgn rftafpsvlg aceqldmigf kanriqtvpr gslpralrwl iltdnaidel
      121 padigdcsrl qklmlagnrl rtlpagmaac ralelvrlsa ncldelpdwl lrmprlawla
      181 aagnpfgaap eaaasaepdi advdwaslac eqklgegasg viyraqwtae nrapravavk
      241 lfkgavtsdg lpdcemaacl hagrhpnmip vigkvrghpd gthglvmelv dpaltnlagp
      301 psfatctrdv yadstgfepa aalriahgia svaghlherg imhgdlyahn ilhdgaggal
      361 lgdfgaasly dvndrmrgar ferlevrafg yllgelldrc gqqawagrra ldalaaacln
      421 edvdarpsfv eitaalaaqt r
//
LOCUS       WP_175830570             512 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175830570
VERSION     WP_175830570.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..512
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52209
     Region          16..438
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,142,
                     145..146,149,273,276..277,280..282,285,313,317,371..372,
                     376,380,396,399..400,403..404,407)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtlsdsrrna valaavclts lmfgleissv pvilptlehv lhgdfngmqw imnaytiact
       61 tvlmaagtla drfgrkrvyv tgtvlfgats llcglapnvp vlvagrllqg asggamlicq
      121 iavlshqfre grergrafgi wgivfgiglg fgpivggaiv alaswpwvfl vhaplaaval
      181 aliggavqes rdphagsldv agivtlslav lglafyitqs aelgltsaag lgvlgatvla
      241 vagfflaera sarpmfdfsv friraftgai fgsmgmnfsf wpfmiylpiw fqvalgydsv
      301 taglallayt lptlvappfg erlalrygpg vvipgglfti aagfvlmrig saadhaswvt
      361 mlpgcviagi glgltntpvt ntttgavpsa ragmasgidm sarmislaln iaamgfvlva
      421 givaslkggv agaigdgalr rlaqeiasgr tdglheiapa laqadptgaa lhaalvhgfg
      481 wvmvygaagv avlatasava faparrgaav ce
//
LOCUS       WP_175830582             314 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175830582
VERSION     WP_175830582.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..314
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34917
     Region          7..314
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpedfhflll pgfsalgfms aveplrvanr frtelyrwhv isadgapvaa sngipvaaea
       61 acaevetvdt vfvvagfdpl vcytraigdw lrrqhrhgat lggidtgsfv laeaglfdas
      121 qpltlhweal aafrerypgl natqelfeid drritcaggt asidmmldli grrhgadlaa
      181 aiseqfvvsr irqrsdrqrl eiaarygvhn rkliqvigtm qrhmenplgs dalaqevsit
      241 rrqlerlfsa tlndtpthfy lnlrldrare llqqtdmsit svcvacgfes pshfsrtyra
      301 rfglsprsdr ratr
//
LOCUS       WP_175830686             204 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CGNR zinc finger domain-containing protein
            [Burkholderia cepacia complex].
ACCESSION   WP_175830686
VERSION     WP_175830686.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..204
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22535
     Region          13..204
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mvtrsdparp gyewraadfi gghpaldfln tvadtgktrd eeklvdwpav rawagkagll
       61 apddlarllr hprqdgpdel aalrrfrdda yvaiahltae gggsagaraa erlavairda
      121 igrsafdaig grfawrpdar aasrwvdava lgfehlmrsd dfarvrqcgr ctwffvdrgr
      181 gvgrrwcdmr tcgnrakvea frer
//
LOCUS       WP_175830699             279 aa            linear   BCT 11-JAN-2025
DEFINITION  polyphosphate kinase 2 family protein [Burkholderia cenocepacia].
ACCESSION   WP_175830699
VERSION     WP_175830699.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Motomura,K., Hirota,R., Okada,M., Ikeda,T., Ishida,T. and Kuroda,A.
  TITLE     A new subfamily of polyphosphate kinase 2 (class III PPK2)
            catalyzes both nucleoside monophosphate phosphorylation and
            nucleoside diphosphate phosphorylation
  JOURNAL   Appl Environ Microbiol 80 (8), 2602-2608 (2014)
   PUBMED   24532069
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Sureka,K., Sanyal,S., Basu,J. and Kundu,M.
  TITLE     Polyphosphate kinase 2: a modulator of nucleoside diphosphate
            kinase activity in mycobacteria
  JOURNAL   Mol Microbiol 74 (5), 1187-1197 (2009)
   PUBMED   19843229
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Nocek,B., Kochinyan,S., Proudfoot,M., Brown,G., Evdokimova,E.,
            Osipiuk,J., Edwards,A.M., Savchenko,A., Joachimiak,A. and
            Yakunin,A.F.
  TITLE     Polyphosphate-dependent synthesis of ATP and ADP by the family-2
            polyphosphate kinases in bacteria
  JOURNAL   Proc Natl Acad Sci U S A 105 (46), 17730-17735 (2008)
   PUBMED   19001261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..279
                     /product="polyphosphate kinase 2 family protein"
                     /EC_number="2.7.4.-"
                     /GO_function="GO:0008976 - polyphosphate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016776 - phosphotransferase activity,
                     phosphate group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006797 - polyphosphate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31776
     Region          7..277
                     /region_name="PPK2_rel_1"
                     /note="polyphosphate:nucleotide phosphotransferase, PPK2
                     family; TIGR03709"
                     /db_xref="CDD:274737"
ORIGIN      
        1 makqpslddf rvpystreke aaafkldafd pgakpfssgs keadrerlsv vsteldvqqe
       61 rlhtqqkkrv llvlqgmdts gkdgtvravf revdplglri vpfkaptpie aahdflwrvh
      121 aqvpaagela ifnrshyedv lvprvlgaig dkecerryrq irdfetmlfe ngttivkcfl
      181 hiskdeqrar lqariddptk hwkfdisdld arkhwdayqs ayrdalaats aehapwyvip
      241 anskthrnvm iaelllrtmt dmklefpppk pelegvkir
//
LOCUS       WP_175830735             396 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia cenocepacia].
ACCESSION   WP_175830735
VERSION     WP_175830735.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..396
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=42226
     Region          18..381
                     /region_name="MidA"
                     /note="SAM-dependent methyltransferase, MidA family
                     [General function prediction only]; COG1565"
                     /db_xref="CDD:441173"
ORIGIN      
        1 mnpkahepas lpapgpdala qsetlaaqlr deiaaaggwl pfdrfmeral yapglgyysg
       61 garkfgrrad dgsdfvtape lsplfaqtla qpvaealaas strrvmefga gtgklaagll
      121 aaldalgael deylivdlsg elrerqrdti eaavpalaak vrwldalper fdgvvvgnev
      181 ldampvrlfa kadgawrerg valdarhafv fddrpigaag lpavlapldv gdgyvtethe
      241 aalaftrtvc tmlgrgavll idygfpahey yhpqrdrgtl mchyrhhahd dpfvypglqd
      301 ltahveftgi yeaavatgvd llgytsqarf llnagitdal aaidpsdvra flpaanavqk
      361 liseaemgel fkviafsrgi dgtldafarg drshal
//
LOCUS       WP_175830739             252 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia cenocepacia].
ACCESSION   WP_175830739
VERSION     WP_175830739.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..252
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=26122
     Region          <5..87
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          85..240
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mssdrsdsps aepardaaps plgpgrsaap pplphdtpss aarrrflqsa aaaatvsaas
       61 hvhpqppyaa stpavprrdt vpaqpvrldi ngraytlqle prvtlldalr eyagltgtkk
      121 gcdrgqcgac tvlvdgrrin acltlavmhe garittvegl arggelspvq rafvecdafq
      181 cgyctsgqlc satalldefa agaasaatdd vrrrpanlsd deirermsgn lcrcgaypni
      241 vaavraahaa hg
//
LOCUS       WP_175830770             550 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Burkholderia cenocepacia].
ACCESSION   WP_175830770
VERSION     WP_175830770.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..550
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58624
     Region          13..531
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 maaatptgal valhhvsfrf ddgvtlfdsl dlsidrtptg ivgrngvgks llaqliagcr
       61 mpsagtierh ahvvyvaqqh dhdrddtaaa prtvaqiaal daplsalarl aeghatpndf
      121 dligdrwdla erlrmaldaa glhdvhadtp ahalsggqva rvaligalls gagllvldep
      181 tnhldapgra wlctaldgwr ggvvivshdr allagvqriv eltphgarsy ggnyalyraq
      241 rgaeqeaaha aldharterg hvrrrleqeh dtiqrhaaas lrdaktanls smarqsrkga
      301 araimgtvrr hqsdfkatld arvqeaaarv eadapvlvsl pgtevsarrq lftleraqlp
      361 wrvasdadai twsasgpvri altgpngcgk stllrmlage laprsgtctt hvsaayldqr
      421 lalldpersi veqlglldtp laegdlrsrl allqldatra tqparqlsgg erlkaalaca
      481 lwrgtpaqll lldeptnhld lesvraieaa lagfpgaivv ashdaaflaa lepthtmqwh
      541 rdgwryepva
//
LOCUS       WP_175830796             383 aa            linear   BCT 11-JAN-2025
DEFINITION  VanZ family protein [Burkholderia cenocepacia].
ACCESSION   WP_175830796
VERSION     WP_175830796.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009512
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..383
                     /product="VanZ family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=41137
     Region          23..117
                     /region_name="VanZ"
                     /note="VanZ-like family protein (function unknown)
                     [Function unknown]; COG5652"
                     /db_xref="CDD:444373"
ORIGIN      
        1 mnvpgthras plarqafaay aalivyasly pfegwvslgi gpfdylfapm qryvtafdvv
       61 tnvlgylpfg algvlalhpr wrgvaatlia gglgvllsgt mealqtylpt rvasnldlga
      121 nalgallgaa laapatgall drgalrrlrf awlepdgstp lllaalwpfa ivfpspflfg
      181 igdwpaalwe radasmqdal lawlpaawrv sewpervdgw lsdsaweavl gglmlfaala
      241 itslamrara prirllialv vatlvlkaaa tfmqsatglv vvwatpgarl gielgfaaal
      301 valrvpatwr allaalalla gvalvnllpv npffdftlsg wrqgryvhfn siarwlawiw
      361 pyaaliwlgq rvehawlpaa lrr
//
LOCUS       WP_175830810             265 aa            linear   BCT 11-JAN-2025
DEFINITION  ComF family protein [Burkholderia cenocepacia].
ACCESSION   WP_175830810
VERSION     WP_175830810.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..265
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=27508
     Region          17..235
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mvrgsaertl rvvlsqvrtl avrvaavmlp nrcalcgnls havicgacda aywneaqlrc
       61 evcalplgvg harsagggrl gagraglyqc dacrtapppf datlaladyr apldglargl
      121 kfharlalgg efaarlarlv ddtrgasgfd lvapvplshr rlvargynqa waiarplarr
      181 lgvpaeaall trvadtapqs rldrharrdn vmaafavagg vagrhialvd dvmtsgatla
      241 aaaqalkaag aarvtnlval rtard
//
LOCUS       WP_175830866             308 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Burkholderia cenocepacia].
ACCESSION   WP_175830866
VERSION     WP_175830866.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..308
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32190
     Region          7..272
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(34..35,38,90,103,105,134,167,253,256)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 maaafpeila lgeamiefnq sqpghpeflq gfggdtsnfc iaaarqgast gfvsaigddp
       61 fgrlladmwa servdttyvr idrsaptgvy fvthgadghq fdylragsaa sryeagdlpl
      121 dalaaakavh lsgislaist aacdaafaai dharrhgakv sfdtnlrlkl wplararavm
      181 realrqtdic lpswddvtal tgandrdaiv damlehgpqv valklgkega yvatpnerrv
      241 vpgfaveavd atgagdcfgg afiarivagd dpfaaaryan aaaalsttgy gavapiphre
      301 averlmqg
//
LOCUS       WP_175830870             316 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175830870
VERSION     WP_175830870.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..316
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33828
     Region          21..78
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          107..301
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(117,121,160,174,176,235,252,280)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(118..119,123..124,126..127,130,134,136..142,203,
                     229..233,240..241,244)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mtsdpaadpi papdkpldll dvalfvraal lanvtaagre fgvsaavasa riaqlerqlg
       61 arllhrttrr isltqdgevf maradallaa adaarasvgr grsepygrlk vsmsssfgrq
      121 hvapvipafl rrypsvsldl rlsdeivdlv ddgydvairl galkdstlva rklatnrrvl
      181 ccspaylaer gtprhpadlt qhecvilgdq rdwsfatpqg pltvrvggrl vasngeaire
      241 alvdgfgiai kstwdvgpll asgalvsvld dypfaddvai wavypsrahv plktlafiaf
      301 laehfgdppy wdrang
//
LOCUS       WP_175830877             332 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175830877
VERSION     WP_175830877.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..332
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=37005
     Region          14..287
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mdsravtfde irgaydlgrg gpptqvserv whlpadsgag vavklyaleh haravketvv
       61 lahlethgdt rfhvqtlkrt rsgeslwsgq hshamltrwe agqfktydrf sptewdalga
      121 slaalhlsle rlplpsvdti rarltsidad avrrslldtl dradanvtga anlrryvdla
      181 lrmldryypg sidafpaddp qhpihndynq fnylftgtlp plildweasi gapreyelvr
      241 clnhlpleap hlaqafvhay qrvrpvnpay iawavdaacl qhalklwivq gwlddpsrfa
      301 shlngavtma samvnardrl idffsrcvet gs
//
LOCUS       WP_175830889            1012 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding and (Fe-S)-binding domain-containing protein
            [Burkholderia cepacia].
ACCESSION   WP_175830889
VERSION     WP_175830889.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1012
                     /product="FAD-binding and (Fe-S)-binding domain-containing
                     protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=110103
     Region          24..539
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
     Region          492..1011
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mtsavspslv rpvhlvpsqg aalsplferl rremrgdvya drasrgryat dasiyqimpl
       61 gvvvprdqdd lrialdiard rkipvlarga gtsqcgqtvg ealvvdnskw lnrivafdaq
      121 artvtvepgi vldhlnawlk phglwfpvdv staaqctigg magnnscgsr sieygnmvhn
      181 vlaidailad gsecrfgsla qpvtdrrtld llhgveriak rerdeiverv pkvlrrvagy
      241 nldlfdcqnp raytddghan lahllvgseg tlahsrqitl klaplpahkt lgvvnfptfy
      301 qamdtaqhiv klkpvavelv drtmidlsme npafrpvier alvgrpqail lvefagesrd
      361 aqhaqldrla elmadlglpg svvkmtdaga qkalwevrka glnimmsmkg dgkpvsfied
      421 cavplehlae ytrrltdvfh khetegtwya hasvgtlhvr pildmrrdga trmreiaeea
      481 aalvreykga ysgehgdglc rgewvawqyg prlnaafaei kklfdpdnrf npdkivnppk
      541 mdarahfrfa pgyaalplrp aldwsawnvt rnpltgeeta pgsgtdithg lasavemcnn
      601 nghcrkfdag tmcpsyrvtr deqhvtrgra ntlrlavtgq lgadglagdd vkaaldlcvs
      661 ckgckrdcpt gvdmarfkie arhawnhkhg ttlrerlvay lpryapwaar mrgaiafvng
      721 vpvvassikr wiglapqral pgfarpflav tgagagastp trtgsatrev llfvdtfsny
      781 qepdnaraaq avleaagytv hfnvragarp lccgrtflaa glvdeaksea rrtldalrpy
      841 lergiaivgl epscllsmrd eflaygygde atrlashafl feeflvrehg agrlslplha
      901 idanealvhg hchqkafgaf tpvqtvlrwi pglkvspves sccgmagsfg yeaehyaasq
      961 amaelsllpa vraraegaiv vadgtscrhq iqdgaqaqav hvakvlaral rs
//
LOCUS       WP_175830933             487 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175830933
VERSION     WP_175830933.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..487
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51921
     Region          58..467
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(68..69,72..73,76,110,160..161,163..165,168,188,
                     191..192,195,307,310..311,314..316,319,346,350,399..400,
                     404,408,424,427..428,431..432,435)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mnsqsldlgg haggpesarp paasagagad aaavpgrrvt lgdfmddlpv galhrfvvwv
       61 igvglffdmy eiflvstigs alqheyglsr qsadfkllla safigmfvga mclgsladri
      121 grrkaflltl gwysafslvg afsvnadmlv acrfltgigv gaiypvadsf lseilpkdkr
      181 grlaawaytt syvavplvgf lalwlnplqv agiagwriil aigslgavyv llvqhrlpes
      241 prwllaqgrt adahaalrrf aesagvrvpe hfaepvepqr plglgerial lrgqpygary
      301 vmlaifhllq gfgyygfgtl agtvvksrgf dvtdstlfia lsfigypigs llsipllnwi
      361 errtlvivsi lsiavfglcf aysgntmliv gfgflttcas nvfsnayhvy qaeifparvr
      421 staigstyal srivsgalpf vllpvlvtyg agamfgvisv algivavtlr vfgplttrrs
      481 qdeinpv
//
LOCUS       WP_175830935             275 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cenocepacia].
ACCESSION   WP_175830935
VERSION     WP_175830935.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..275
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29181
     Region          66..271
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mtilyrgmdr aaldaaylnt kavpdfpall ascqarsaal yaatpsrrdl rygaqpaqrf
       61 dwlpcgqrda plfvfihggy wqhctkedfa yaasgplarg ydvvlaeytl apvatmtdiv
      121 aeigalldhl aadrdglgia grpihlsghs agghltalhr ahpavasala isplvdlepi
      181 alcclndklq ltahevdays plhhivpgap tvvavgdael pelirqadey ataceaager
      241 iartwlpgmq hfavlddlam pdgsmlaalh aiapr
//
LOCUS       WP_175830992             343 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia cenocepacia].
ACCESSION   WP_175830992
VERSION     WP_175830992.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..343
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37624
     Region          180..322
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mlaevrpdgf tmldtyrlaf adglfavrdg veirvaqgdg igaqllraql gddgalrlva
       61 ynhraapadq rrallaalaa afsdsachaa irldpaawpa valdalrasg vladggrclr
      121 dgwaqqadlw rvdpplpcat lptitdgrrh prrppaprgd vyardlpalg vrftlrgwqp
      181 aedaerlarw fdeprvrdgw pgaqpvqrga egpqeadphv tplvgcfdge pfayfeafwl
      241 kedalgphva ardydrglrm lvgepswrga hrvagwlpsv vhylflddlr teavgcavpa
      301 ghtrvadhla rhgfarqrrl altdaqplwm rtlretffsg rhv
//
LOCUS       WP_175831000             881 aa            linear   BCT 11-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Burkholderia cepacia].
ACCESSION   WP_175831000
VERSION     WP_175831000.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..881
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..881
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=93554
     Region          55..877
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mklrhvvgig clavlsgcgg dqastdasvl aqmsnaqgnq ndqgdqndqg esggagkrsv
       61 lrsvdpmigt anldinadws sgvrghghvy pgatvpfgmv qlgpdttgga htlpwnwdrt
      121 sgyqyddpli tgfththlsg tgigsggevr flptlapvdt atlakvaada sitynasfsh
      181 ddetagpgyy rvkmapagsg ntpwnvkgak ilaemtatah agvhrytyfp saaaqkrsmi
      241 vsidnpiggs tasgkiqvid aqtiagweit nnwannkpty fvarfskpfd tkhvafsadg
      301 fkayltfadg ndsgavtvkv gispssiada qsnlaaevga ksfdqvrgaa ervwadalgr
      361 irikggsadq rtmfytslyr tmlaptvynn adgsyvgtds tndgttsppt tskhanpgfd
      421 ysstfslwdt fraesplmtl vqpervdgwv kslltqfrqn gkgelpvwpl aqtetftmag
      481 hpsipliada ylkhltsagi ddiwaalttt qgasahgfdq yrqrgyvvag dnasvsttqd
      541 yafddwataa vgkaagksta dyrpylqrsq nyrnvfnptl nngwkfsqpk daqgnwvagf
      601 dptaaektdf sesnawidtw nifhdfpglv allggksqfi aqldrtfdpa npltflgnqg
      661 fpdltgrsgq ffagnepanh lpylydvagm psktqdrvrt vmddmysltl tagdrallsg
      721 dslkaaladp rrvrdsaipg nddcgqlsaw yvlsalgiys lnpvggvfyl gtplfaeati
      781 dipvasgggd ggalkfgksr rftvtahtag ggapssvnry vqsvslngvp lhrpyityde
      841 mkaggtldfv mgatpndgwv sqwngqdpns alapsltlag k
//
LOCUS       WP_175831008             421 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia cenocepacia].
ACCESSION   WP_175831008
VERSION     WP_175831008.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..421
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44557
     Region          167..358
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mvksvatpda vapgraqrvv ralvpaavlg alaafglaaa lpavsqlpga vdsgtaalpq
       61 rvlsdtpfpt aqhfvtsela rtigernehp drndrsvqpg lfaplsahrn dmlgytslfq
      121 faapdhqqgm ragdieltls dtlnrldvpp evriqlgdlv tgkvamrasa qrgdyyrvaf
      181 dtndgtprlt alelrvagrt fgaiwfrapg aehgayyald gspleaaaft mpvkwtriss
      241 ffgerihpls qamafhtgvd laapsgtpvd aaadgvvsfv gtdpggygry vivdhadgys
      301 tyyahlsafa rglktgetvk qgqrigsvgm tgaatgphlh fevrvandpv dplvtlasaq
      361 talsdmqlta frqeaaqwrl rlasisttpf afaqndgplw gdfatgpstl ravfdthysa
      421 s
//
LOCUS       WP_175831060             463 aa            linear   BCT 11-JAN-2025
DEFINITION  alkaline phosphatase [Burkholderia cepacia].
ACCESSION   WP_175831060
VERSION     WP_175831060.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Vimalraj,S.
  TITLE     Alkaline phosphatase: Structure, expression and its function in
            bone mineralization
  JOURNAL   Gene 754, 144855 (2020)
   PUBMED   32522695
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..463
                     /product="alkaline phosphatase"
                     /EC_number="3.1.3.1"
                     /GO_function="GO:0004035 - alkaline phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0106219 - zinc ion sensor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48097
     Region          28..463
                     /region_name="PhoA"
                     /note="Alkaline phosphatase [Inorganic ion transport and
                     metabolism, General function prediction only]; COG1785"
                     /db_xref="CDD:441391"
ORIGIN      
        1 mstikciaaa lavagfacga aqaagqaknv ifflgdgmgp ttvtasriyk vgesgqltme
       61 klartarikt fsndaqttds apsmaaymtg vkmnnevlsm ssdtravapg sdangnktvn
      121 ncapgngqpv atllelakar gkavgaittt elthatpaat yshichrdaq ydiaaqaapg
      181 gagynaalgd gvdvlmgggr nhwtpfdpva nkrgradgrn lldemkakgy tvvatkdqla
      241 qagngklvgl fsstshleye ldrvtgrgeg psqpslaemt skaidvlskn sngyflmveg
      301 gridhalhgt nakraledta afdeairval skvdlsntli vvtadhdhtm tingyskrgn
      361 pildisrnyr dgqpskdadg ntyttlvfgn ganrpnvras vdsatatnda ylqevgvrmg
      421 sagsethggg dvmlfadgad akafkgtidn tkvfglvrsa fgf
//
LOCUS       WP_175831069             302 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia
            cepacia complex].
ACCESSION   WP_175831069
VERSION     WP_175831069.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32685
     Region          9..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(105,109,148,162,164,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(106..107,111..112,114..115,118,122,124..130,191,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mtliddfpal dtfarivsag slsaaareld lslsvvskrl ahlesrlgvr llhrttrqqt
       61 ltddgaqfha qvlrilaeve haetlmrdrr gtvsgvlrvt apgelgrlri aplvaafqqr
      121 hpqltvqlml tdavvdllaa didvavrign ladstmiare lapnhrvlca spgylaahgw
      181 pahpaelrah rcivmgdqpr aewrfdgaqg gvavevtaal ltndggavrt lalegagial
      241 ksiwdvgadl dagrlvrvlp afeasaaplh avypgarhvp lrvrtfvdfl reqlrdawrr
      301 hd
//
LOCUS       WP_175831074             448 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175831074
VERSION     WP_175831074.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..448
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47993
     Region          21..440
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mptqpstpaa slalhddaha sqhsraqryl qllllviaag aiypmlylrq vyqptmlqff
       61 hiddvqlgyl ysslgtiflv sylpsgwlad rlsprwlicf sllatgalgl ayatgpsfdt
      121 lvlifggwgl ttgltfwaav ikrvnmiagp deqgrffgll dggrglveal latiaitlfa
      181 yvtqahggtd aagfrlvvhl yaffcialgv llalvkdpag tsdraaaakr rtgsdrqgnv
      241 ltdlktlaai pelwlvaaiv fcgyqvfwat ysfsaylheg nfglsataag fittlklwmr
      301 piggigggfl gdrvskvsvl fwalllaals lvgliaapah spqamlvvlv lfigiltyai
      361 rglywslldd ckvpthcagl aiglisvlgy spdvfvplin gyvtqtfpga hgyqlyfgyi
      421 aaialcgaga aaflkyrltr ihriqesa
//
LOCUS       WP_175831109             232 aa            linear   BCT 11-JAN-2025
DEFINITION  YoaK family protein [Burkholderia cenocepacia].
ACCESSION   WP_175831109
VERSION     WP_175831109.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..232
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=23310
     Region          6..211
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mkhedtilaa vagfvdtlsf valfglftah vtgnfvliga glagfgqgvi lklsvfpafv
       61 cgviasslia rsmaarpawq gtrvlhtvqa vlllgfcaag vwatpvtqpd slaalvagiv
      121 gtfamgvqna hprviaragg vpntvmtgnv tqaildavdi lspgtadsvr atararfakm
      181 lpaivafalg aaggalgfry vgflallvpv galamlalca aqsagpttqe ra
//
LOCUS       WP_175831112             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175831112
VERSION     WP_175831112.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33847
     Region          7..>158
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          95..293
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(105,109,148,162,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(106..107,111..112,114..115,118,122,124..130,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mqhlpdleaw aifarvaetg sfakaadllg isqptvskai arlekrlgam llyrtsrkls
       61 ltptgellrd rairlladae lieneasaqa lephglvrvn apmsfglrhl stvlpafler
      121 yprvdidlvl tdhivdivsg gfdvairiae lsdstlrsrr lcavrrplva spayldrrgr
      181 pthprdleqh vcltytnlpt pehwrfrhpa sgdevgvsvh grirtnnadv ilpalvgghg
      241 lalqpeflvw damqrgelee vmsdwkiadi nvnlvtppgi lraarvtvll dflaehfsha
      301 pwalpaa
//
LOCUS       WP_175831174             774 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia cenocepacia].
ACCESSION   WP_175831174
VERSION     WP_175831174.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..774
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81611
     Region          <68..>194
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          203..764
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msapelsvhn esrralllgf asgglllafg vpslaqaaap vqppvsanpq yggagmphgl
       61 rddpnlfvai tpdgtvtvtc irsemgqgvr tsvalvvade lgadwarvkv aqavgdepry
      121 gnqntdgsrs lrqsfaalrr agaaartmle qaaaatwgvd vrqvkatvhe vvdtktgrkl
      181 gfgelaakaa alpvpdtksv alkapaefry igkgktalid grdivggraq ygidtrldgm
      241 lyavvarppv ygdtvasfda saagklpgvv kvvqlastpl psgfqplggv aviardtwta
      301 iqaraqlkid wkhgpnagyd saeyrkalea aaaqpgdvir sdgdaaaala gaakrvraty
      361 yiphlahatm eppaavarva dgrcevwtct qapqttrdei akalglpter vtvnvtllgg
      421 gfgrkskpdy vveaallska vgapvkltft reddiahdyf havsleafdg gidasgkvva
      481 wqhrtvapsi qstfrpgvvh eqpgelaqgi adlpfaipnv rienpaaqah trigwfrsvy
      541 niphafgiqs fvselahaag rdpkdflldl igparrfeph itvknvnyge dpalypvdtg
      601 rlrrvvetva reagwgrklp kghglgiaah rsfvsytaav cevqvdadgk isvprvdiai
      661 dcgpqvnper vrsqlegavv mglgialhge itfkdgrpeq snfngfqvlr mneapreirv
      721 hlvapddyat plggvgepgl ppvapaltna ifaatgtrir slpvadqlak pqag
//
LOCUS       WP_175831244             309 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Burkholderia cepacia].
ACCESSION   WP_175831244
VERSION     WP_175831244.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..309
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=34679
     Region          28..291
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mdeptlwlsa pteayqqwqr teaagadrra fsprsivqhe amferfmrhl aaaqrslatf
       61 gpdhlesffa dldrrckpgt ttrlryqkll drlgrhlvdv gvrktnpaaa ytltqtwped
      121 epvpvyllea ddlrlqasir aieglddral rnraivglll stgitaqeir qaaavdldls
      181 parphllvpk rgprearrin ideftepala rwrnlsaaan sprlfpspra ggpmtdemlg
      241 rivrdellai dvrlpdmspr tlrntfarrl llagrsnddv tyllgltsqr tviriratip
      301 trpqaalqt
//
LOCUS       WP_175831311             297 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cepacia].
ACCESSION   WP_175831311
VERSION     WP_175831311.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..297
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32535
     Region          4..296
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 misrkdvtfp aeggvelaaw lylpesnepr paitmahgyg gtryhalvqf aqafaaagfv
       61 vlvhehrgfg asggeprqdi npwqqiadwr raisyleahp avdssriglw gasyagghai
      121 vlgatdrrlk avvsqvptis gyqqglrrvs pdalpaleel lnederaqfr geppryqala
      181 sadpaipaay rsqdavdfnl qpmpegawen kvtirstrwa rmyepgqwit rvsptpllmi
      241 varedkatpt dlalsayeqa lepkklvlip gghydlyqsq gaaarnaaia wfeehla
//
LOCUS       WP_175831379             790 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia cenocepacia].
ACCESSION   WP_175831379
VERSION     WP_175831379.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 790)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 790)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..790
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85999
     Region          72..773
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msftfaarps rgrlalacaa afawpaayaa atddvragta rgggvdrpat tataapaagg
       61 vaaasapagd tltavsvtaq rqpvdpntpa vvtsitreqi dahtnvtted alkyapnlmv
      121 rkryigdrns ifagrdfnel qsarglvyad gvllsnllgs syaypprwsl ippddiarvd
      181 vlygpfsaly pgnsigstvl lttrrpeqle aslstqfftq ryhdgygfad sfggnhqtar
      241 ianrvgrfwf alsldrlenn gqpmqyaspn stynpklgaa vpvtgaatdl gpngkprtiv
      301 gaqtierteq lnetvrmgya ftdhvdatlt lghwenhyrq hgetfmrdam gnpvyggnvs
      361 iggqnmtvap nafapqrgdq enwlyalgln grldsgwrls gvvsaydvsr dvlraastvq
      421 ggagtlfqgd gtgwrtldlk aeapavkght ftfgyhydny flrnvtyntt dwlagpttsl
      481 asvyrgdtrt qslfgqdawr faprwlatlg lryerwdayg galgnargtl gyadrganal
      541 spkvalqwda tevwrfrlsf atgtrfptvd elfqgtisnn aivnnnpnlr pekaidwdft
      601 aerdvgvgvv rasvfqsdlr dsiysqttvs gattvtnisn vdrvrvrgve lafsgenvgv
      661 rgldldanvs asnaqilada anpayvgsrf priprmranl lasyrfdehw ltsvgvrysg
      721 rqfntldnsd vnpdvyggts sftvvdlkar yhfdrhwtas agidnvtdrr yytfhpypgr
      781 tfygelkwsl
//
LOCUS       WP_175831352             352 aa            linear   BCT 11-JAN-2025
DEFINITION  S1C family serine protease [Burkholderia cepacia].
ACCESSION   WP_175831352
VERSION     WP_175831352.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..352
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37149
     Region          63..>217
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mridttryia alaclfsltl sgvgltssrd afaaatdasa lydklspivw rvvvvtpngk
       61 kigsavvigd ekvvtnchvl sdgvaaaivh gnmsygarlt epdaerdlcv lsvegfhlpg
      121 aqvaplsslk vgqhvyaigs pfarentmsd glisgfvrdp drgitsiqis apispgssgg
      181 glfdergrli gitarqisps qaeninfaip aewladvper arlqlaqrsg stnrtepvtt
      241 nkapedlvrp adfhrattsg aqvllsshas wskacvsrft phvtvvqppl hgsidiregd
      301 yaigpnspca gqmvhgtlvf yipeagfkgq etvryvadsv pgvirtalid vr
//
LOCUS       WP_175831328             491 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA recombination protein RmuC [Burkholderia cenocepacia].
ACCESSION   WP_175831328
VERSION     WP_175831328.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..491
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=53862
     Region          <31..>188
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     Region          153..491
                     /region_name="RmuC"
                     /note="DNA anti-recombination protein (rearrangement
                     mutator) RmuC [Replication, recombination and repair];
                     COG1322"
                     /db_xref="CDD:440933"
ORIGIN      
        1 mtmtlllaav vvlavalava ivalvrggrh ddaavlgdqi edaahaqara verlerelrg
       61 eivenargsr telagsfvql qqtlaaqlts vatvqnnqie gfaqqlgklv agnaqqfdam
      121 reslqrqaqq areeqtgalr lfgdtlhrql tqlteandrr igevratleq rlkeietnna
      181 akleemrrtv deklhatleq rlgesfklvs drleqvhrgl gemqtlaagv gdlkkvltnv
      241 ktrgtwgevq lealleqmlt adqyaknvat vpkstervef airlpgreag trdappvwlp
      301 idakfpredy erlidaqera davaveeaar alearvrmea rtiaekyvap phttdfallf
      361 lpteglyaei lrrpgltdll qrdyrvtvag pttltallns lqmgfrtlai eqrssevwqv
      421 lgavktefgk fgdvlartka qletvtrsie saeqrtrvms rklkqvealp gdtaagllga
      481 egaegadadd a
//
LOCUS       WP_175831383             211 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator transcription factor [Burkholderia cepacia].
ACCESSION   WP_175831383
VERSION     WP_175831383.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..211
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23125
     Region          13..206
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 msdaatkddl mpvvyivddd samrasldtl lrsmglrvat fastaelrat rwenvtscll
       61 ldvrlrgesg lvfqqaqdrp aipivvitgf advevcrkal kggavdflvk pftdqelida
      121 vnlalsldaa rrirndtrhe lqqsfelltr rerevlahvv sgalnkqiaa rlglslitik
      181 qhrasvmrkm nassladlvr ksetiglplt t
//
LOCUS       WP_175831490             136 aa            linear   BCT 11-JAN-2025
DEFINITION  GFA family protein [Burkholderia cenocepacia].
ACCESSION   WP_175831490
VERSION     WP_175831490.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..136
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14900
     Region          5..131
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mahpepmegg cacgairyri agvptdagfc hcrlcqrttg aavvasasvp idafeylrge
       61 ptvyassawg errfcgrcga qleyrrsdap rtveinyatl depsrlrpaw hvwygarfpg
      121 ieidddlpky ddggre
//
LOCUS       WP_175831544             220 aa            linear   BCT 11-JAN-2025
DEFINITION  Lar family restriction alleviation protein [Burkholderia cepacia].
ACCESSION   WP_175831544
VERSION     WP_175831544.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10627152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..220
                     /product="Lar family restriction alleviation protein"
                     /calculated_mol_wt=23783
     Region          72..125
                     /region_name="Lar_restr_allev"
                     /note="Restriction alleviation protein Lar; pfam14354"
                     /db_xref="CDD:464145"
ORIGIN      
        1 mtttsneksr adaltyrmte fdvlldgyqe slqdgplker vdarnelrla yrtallaasp
       61 veqpaaapid gllpcpfcgg epkrmmlsde vnfggdvivc tkcdcsthve fgeklglvea
      121 wnsrvahsrs pamaaeavag vfvkhskfgp wieiekpepg avtlytaprp aqadarvglt
      181 veqrealeia fsliglsgdp rvrkmhqvlh gllqganhae
//
LOCUS       WP_175831555             221 aa            linear   BCT 11-JAN-2025
DEFINITION  histidine phosphatase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175831555
VERSION     WP_175831555.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..221
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24331
     Region          6..204
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mattqilfir hgetawnrik riqghidipl adtglaqaqr laarlgrear dgaridavys
       61 sdlmraqqta qpfadalglp lllreglrer sygafqghds ieiealfpda yaawqtrdpg
      121 fapeggesqr efyhrvlhal epivaahpgg riacvahggv ldcvyrfang ielsaprtyq
      181 llntsinvvd yvdgraqvmr wadvlhleaa sddddgyrkv l
//
LOCUS       WP_175831565             215 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            cenocepacia].
ACCESSION   WP_175831565
VERSION     WP_175831565.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..215
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22674
     Region          14..129
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          80..209
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mkdkpaqgpr gldkdaivaa alalledvge aafsvrklaq svgcdpmsvl yhfkskegls
       61 raianalsrs lvpvepslpw rerlrdlarq yralalrypa afallqrhms tgpadlahie
      121 avhraltdag iphaalpsvc vgwyasvigl aaaeaggltr aandvelaem halsdaahpl
      181 vksaaplyaq ldpavvhdtm ldvlldgiaq rarta
//
LOCUS       WP_175831614             146 aa            linear   BCT 11-JAN-2025
DEFINITION  SMI1/KNR4 family protein [Burkholderia cepacia].
ACCESSION   WP_175831614
VERSION     WP_175831614.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10558574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..146
                     /product="SMI1/KNR4 family protein"
                     /GO_process="GO:0042546 - cell wall biogenesis [Evidence
                     IEA]"
                     /calculated_mol_wt=15984
     Region          8..136
                     /region_name="SMI1_KNR4"
                     /note="SMI1 / KNR4 family (SUKH-1); pfam09346"
                     /db_xref="CDD:430545"
ORIGIN      
        1 mpttptigtt vaeieaaets lgralphsfa twlllnngrs lgglsvfpvf darnprktwn
       61 sivrhysegw rawrdnfdht dadfshllpf aefgtgdyyc fdydrtgasc epavvlwshe
      121 tgettpvsdg ftaflsmqdg megggk
//
LOCUS       WP_175831630             207 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD family hydrolase [Burkholderia cepacia].
ACCESSION   WP_175831630
VERSION     WP_175831630.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..207
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23078
     Region          3..>172
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mtikavvfdf ggvlidwspe ylyrelipdv aerrwffthv ctmdwvvrqd ggqtieegta
       61 elvakfpahe glirafyarw qemiggvlde gaalvdrlda qgmplfgltn wsaqtfpyaw
      121 dnfpvlqrfr divvsgrvkl vkpdpaiyre mhariephlp giaphelvfi ddnaknaaaa
      181 talgwhgihh tsaaatearl relgala
//
LOCUS       WP_175831636             156 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia cenocepacia].
ACCESSION   WP_175831636
VERSION     WP_175831636.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 156)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..156
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17004
     Region          8..132
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mkrggaprtv scgvvildta grvflahatd tthwdipkgq gepgetpada alrelleetg
       61 iefaparlld lgrfayrhdk dlhlfavqva egeidparct ctslfpsrrd gsmipemday
      121 rwtapgdida yasrslarlf rtklslaelh rrlsga
//
LOCUS       WP_175831686             546 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175831686
VERSION     WP_175831686.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..546
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58523
     Region          1..533
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mqydyiivgs gsggsslagr ladacpdati alieagshte rnllvnmpvg iaalvpfklg
       61 tnygyetvpq pglggrrgyq prgrgmggss ainamiytrg hpgdydewaq lgatgwgwqd
      121 vlpyfrraeg nergadawhg adgplsvsdl rfrnpfserf iqaahaagyp lnddfngatq
      181 egvgfyqvth rdgsrcsvar ayiygrnrpn lhvitdatvl rvtfdgkraa gvavarngrv
      241 etldaraevi lsagafnspq llmcsgigpa eqlrrhgiav vqdapdvgtn lidhidfiin
      301 trvnsselvg vclrgiakmt palaryfssr tgmmtsnvae aggfiksdps lerpdlqlhf
      361 ctalvddhnr kmhwgfgysl hvcalrpfsr gtvtlatgda rdaplidprf fsdsrdldll
      421 vrgtqamrri lsqaplasqg grelytradq seaelrktiv ehadtiyhpv gtcrmgadah
      481 avvdpqlrvr gveglrvvda svmptlvggn tnapsvmige raadfivaar kggvsrgeaa
      541 aavhgr
//
LOCUS       WP_175831690             257 aa            linear   BCT 11-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Burkholderia cepacia].
ACCESSION   WP_175831690
VERSION     WP_175831690.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..257
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28552
     Region          12..253
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mssplqsesi raqvaelrer gfvvarglvg eaqcaalrqi aehqlreaae piefeadlry
       61 pgapeskhap gghtvrrlld aysrdpafae raiapeigaw mreyfgeepv lsrahhncmm
      121 tkhpaygslt gwhrdfryws ferpdmvsvw lalgpetnen galwlvpgsh taefgpeafd
      181 dakffrsdlp anrkmidaat cpslqtgdvv ffhsntlhsa gqnrsdqvkf slvytyhgas
      241 nrplpgtrsa skpevqf
//
LOCUS       WP_175831683             279 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Burkholderia cenocepacia].
ACCESSION   WP_175831683
VERSION     WP_175831683.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 279)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..279
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30208
     Region          33..279
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mlhpvfsarf sagrvarlar lltaallgvv llngaradta plkvgistsp qiealkiaak
       61 eakeqgldvk iveftdwntp naalankdid vnyfqhipfl enakkqggyn fisiapgtim
      121 kiglyskrvk sfaelkdgar vaiandpvng grgllllqra glitlkpgad yratthdiva
      181 npkhlkiipl easqlarsld dvdlaqgyps fiklagttdp nsallfdgte nknfaiqwvv
      241 rpesandpri rkfisiyqhs pavrraldna fgslyaiaw
//
LOCUS       WP_175831721             360 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia cenocepacia].
ACCESSION   WP_175831721
VERSION     WP_175831721.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..360
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38351
     Region          3..340
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,225,294,314,316..318)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,173,176,178,225,232,294,314,
                     316..317)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,173,176,178,317)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            178
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mptlfdplrl gaidvpnril mapmtrargt rehvptamma dyysqrasag liiseaigis
       61 rqglgwpyat glwttaqiag wrtvtdavhe aggriiaqlw hmgrvvhpsf lddappvsss
      121 ettapghaht ysgkqpytqa raletneipa iieqfaaaar nalqagfdgv qlhasngyli
      181 dqflrdsanf rgdayggsis nrlrllieat ravadvagpg rtsvrlspng etqgvrdsdp
      241 lplfiaaaea lsavgigfle lrepplngsf gvgyldplaa kirpafkgpl vlnsdfnaar
      301 aqaeldagva davtfgrpfi snpdfprrla eaiplasddp atwftqdaqg yidypfaast
//
LOCUS       WP_175831723             754 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: xanthine dehydrogenase family protein
            molybdopterin-binding subunit [Burkholderia cepacia complex].
ACCESSION   WP_175831723
VERSION     WP_175831723.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..754
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=80276
     Region          53..>205
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          214..754
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mtnhagvpne daestvsdsp siamsrrnfl gsmaaftlal sfhggtaraa avigkstarl
       61 sfepnafirv aadgkvtvis sylemgqgtf tglatlaaee ldvslsditv tgapadvehy
      121 inpvlaargf kvqatggsta magawvqmrh aaatartmfv aaaakrfgvp rnelvvengv
      181 vvhprsgrra tygslvaaas aepipkevvl kdharfrfig kngtrrldvp akvngsaiyt
      241 qdirlpgmlv aaiahppklw akirsidsak alavpgvvav vrvpgddeiq ggaavlarnt
      301 waarqgrdal kiewdergal tadsfmivak frelagtpgv vakargkvld gtpsgakvid
      361 aiyeqpylah apmeplncvv hltkdrceiw ngeqwhtgds naaakelgfa lnqvqlhqly
      421 aggsfgrran prsdfvreav riaiaarkag idapikmvwm reddmrgvqy rpltvhrvra
      481 ivdasgqlas whhrivgqsf mpspdpttvd dnlvegaadt gyaipnfrve qhsynafaip
      541 vawlrsvght htafvvetmi delaaaagkd pyafrrqllq ssprdlgvld lavekagwgk
      601 plpaskpgdr rargiavhas fgthvaqvae vtlhqdgsys vdrivcavdc gtvinpdiva
      661 sqiegaaalg lsflhqaitf kqgqvqesnf hdypilrmna mprvevymvs staaptgige
      721 pgtplpapav analaaitgr riralplrdd vlaa
//
LOCUS       WP_175831742             459 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175831742
VERSION     WP_175831742.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..459
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48411
     Region          41..440
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(54..55,58..59,62,94,144..145,147..149,152,172,
                     175..176,179,276,279..280,283..285,288,315,319,369..370,
                     374,378,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtishalrag ddapradaps saqlagddya asertlaraf rrilpfifvc yvisyldrtn
       61 vgfaaltmnk dlgltaeqfg vgaglffigy flfeipsnli mqkvgarvwi arimitwglf
      121 smatafvvgp ksfaaarfll glaeagftpg iylyfthwfp gkwrakvtaa flvgipvanm
      181 igspisgall elgglhglrs wqwllliegv pavmlgiacl fvladrpeka awlsdeekas
      241 lakrlafeqr digakhgstl rdamtnwrvf vlafvnfcgi vgslgvglwm pqiikqfgve
      301 havvgwltai pyaigagaml wwarlanraa nripyvagal alaaaalcas afihapvfkl
      361 ialcvtvsgi lafqatywai psgfltgraa agglalivsv gnlggfvgps migalkqfsg
      421 gftapliavs gvlllgalti awlgdpgsga geapvarea
//
LOCUS       WP_175831762             203 aa            linear   BCT 11-JAN-2025
DEFINITION  trimeric intracellular cation channel family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175831762
VERSION     WP_175831762.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..203
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=21173
     Region          1..196
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mhtlyliaiv aeamsgalmg mrrgmdrfgl alvgavtalg ggtvrdvllg hyplgwiahp
       61 eylvitlvaa tvaswaarhv armktlfvtv daiglaafti igcdigastg tapiivvlag
      121 aitgvcggml rdllcnempl ilreelyasv afvtgslyvg mqylgieagf atlvalaagf
      181 smrmlavrlg wkmrsfgaad veh
//
LOCUS       WP_175831816             558 aa            linear   BCT 11-JAN-2025
DEFINITION  alkaline phosphatase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175831816
VERSION     WP_175831816.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 558)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..558
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=58294
     Region          48..536
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 misrfvkqrn mavmaagala lasagvyaaq qdgnaqgesn grpsrvvkhv lllsidglhe
       61 qdlarcigan tcpnlavlak sgvtyanayt pglsdsfpgl aalvtggspk taglfydvsy
      121 drnlyapsdt tcsgkqgwnv vfdettgida qnggalvhld gggafnpqai phakvngqcv
      181 pvyphdyvkt ntvfeavkag vpnartawad khawgydwln gpsgtgvddl mrteinsidp
      241 atntdytdvy shtarfdnlh vqalirqigg rdssgtktap vptlfganfq tlsvaqkapv
      301 akgggyldad ftpngqvana ityvddaigh vvaalkqanl ysstavivts khgqspsdht
      361 klvkngdtlt klleannfld pngnfgqnnt ttgnlndgsg lvgtgfvqtd dvgliwlrdr
      421 sqrtavvqal kanlgcnapg icadgpqayv lygaaladrf gdpangrtpd ivvqpnpgvi
      481 ytsstkkdee hggnapddsh lgllvsypgi hrartvndvv gtkqvaptil allgadprll
      541 qavvaentrv lpglgigr
//
LOCUS       WP_175831840             312 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cenocepacia].
ACCESSION   WP_175831840
VERSION     WP_175831840.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..312
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33366
     Region          66..311
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mntlplvdpe irplletwpt vtlsadnlvq srqrvlplpp pdpagstler rtvpgpagap
       61 dvpvlvylpd gharplptiv hmhgggyvrg aakeleavhr llvthlgcal isidyrlape
      121 tvfpgaiedc yaalawvfrh adtlgidaar igvagesagg glaaalalla rdrgefplaf
      181 qhliypmldd rtctrpphph agefiwhaan nrfgwtsllg hapgidgvsp yaaaaratrl
      241 dglpptflsi gsldlflden ldyaqrllra gvptelhvlp ggvhgfdivp garvsetarr
      301 lshdalrrfl hg
//
LOCUS       WP_175831902             353 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia cenocepacia].
ACCESSION   WP_175831902
VERSION     WP_175831902.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..353
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=36958
     Region          4..353
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkriivvsal acvaadavaq ssvtlfgyig agvrwtdgvk ggsqvgfdnn aisgnifgik
       61 gaedlgggmq aifmlqsgfl tgtgalaksp gllfsqmayv glsgaygrvt fgrqlnaled
      121 igialdpnsa qgqslstipg vvwggnfftn dsrfnntiky vgtfggatvr gsyspggvag
      181 nqragsnvav gtsyrfrtll lgaayqttwn adasqwarti mggatwqvgp arlylsysdl
      241 avsaakagap errdripavg ivyqvtpflq lsgatyydfa qnlkntggan grkltsyaml
      301 qyflskrtsl yaefdrngfs gaykkdqtni gglslrpdgr tvtgvsvgmi tqf
//
LOCUS       WP_175831919             484 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia cenocepacia].
ACCESSION   WP_175831919
VERSION     WP_175831919.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..484
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51830
     Region          1..428
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfaslglie pllrnlqgln yqtptpvqak aipvvlggkd vmaaaqtgtg ktagfalpll
       61 qrlvqhgpav ssnrarvlvl vptrelaeqv lqsfveygkg ldlrflaayg gvsinpqmmk
      121 lrkgvdvlva tpgrlldlnr qnavqfdqvq tlvldeadrm ldlgfareld avfaalpakr
      181 qtllfsatfs deirkmaagi lrspvdisvs ppnataskik qwvvpvdkrn kpdlfmhlva
      241 qnkwehalvf vktrngvdyl almlekagya vdtihgdkpq parlralerf ktgevqmlva
      301 tdvaargldi ddlplvinvd lpivaqdyvh rigrtgraga sgvavslvca deapqlaaie
      361 alirqtlrre eepgfeaehr vpetsatgei ikkpkkpkkp kvqqaapvgr qtqpgkkppt
      421 qggegkrkpv aqhakpavgt gtdytigspf svqkprskpa gkagagkpag ksaggrgkpg
      481 kpsr
//
LOCUS       WP_175831779             289 aa            linear   BCT 11-JAN-2025
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175831779
VERSION     WP_175831779.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..289
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=32192
     Region          1..125
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mnanelvlyf dgrcplcvae irrldehdvr hrlafvdiae pgfdpaplgv dlpalnrelh
       61 arlpdgrmlt gidsilaaht llgrrglvrl lrvpamravf aslyrrlagn rqavsrwlgy
      121 raeacceggt csigrnaesa aanrppqdip rrivvrwmya aaivhllvgv vlpwiagasw
      181 ldayhrgier hfwsaaapga araqqvwwms llgatvqcaa vwmlalvhlg nrlrkrevwg
      241 wllaglliwa pqdmllswqa qvwghvvidv valvamvppl vwlwrrdta
//
LOCUS       WP_175831940             333 aa            linear   BCT 11-JAN-2025
DEFINITION  FHA domain-containing protein [Burkholderia cenocepacia].
ACCESSION   WP_175831940
VERSION     WP_175831940.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12811216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..333
                     /product="FHA domain-containing protein"
                     /calculated_mol_wt=35814
     Region          20..>163
                     /region_name="COG3456"
                     /note="Predicted component of the type VI protein
                     secretion system, contains a FHA domain [Signal
                     transduction mechanisms, Intracellular trafficking,
                     secretion, and vesicular transport]"
                     /db_xref="CDD:442679"
     Region          <20..86
                     /region_name="FHA"
                     /note="Forkhead associated (FHA) domain, binds pSer, pThr,
                     pTyr [Signal transduction mechanisms]; COG1716"
                     /db_xref="CDD:441322"
ORIGIN      
        1 mailkndasg dacllrayhv fgrddarcdt virdgsvsrv hahirwvggl welhdhssng
       61 tsvsgvslrd gehavlqqgd virfgragta pwrvealddp adtlwpirga aapivlaprq
      121 ilpvpaaqpv tivrspagew lcddtlppra lhdgdevstg dfawrlalar hgstvmlaap
      181 adpaapapll eflvsrneeh vrmllhvrgg vvdlgerahh yslvtlarar sadmqagyda
      241 atqgwieldr larmlgidas hvnvqihrar sqfaalpglg asqlverrrg svrfgevpfr
      301 vmrgehlece svpaagprig vpraapgpiv hcp
//
LOCUS       WP_175831950             834 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175831950
VERSION     WP_175831950.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..834
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=89760
     Region          14..796
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 madlaafirt pffqqdkrll alsfphddap svtdsygrqr parlvaerlv aheglgidft
       61 fevtllsgea gvtladmlgk llavsmvrpd gglryftgyc tefslvrndd siaeyravlr
      121 pwshflrtrv nnrlflgqsl qqqigtllad yqglapswew rvrgddsart mnvqggglge
      181 sdwnyivrhl eavgflywwe hdekglkliv gddstvqcpa vdgrspqirf qthdgpmaad
      241 aisqwsavrs lsagsysata fdfkaphaah aqiptlhppg vapqvehhey vghygfakqt
      301 ragdalarvr meeieaaatr fdaagnhhgi lpgrwfqlad hfsvasgspq dheylilear
      361 heaannylqa dgkpeyrnrf vaghrrtpwr pgrgfnsepv rvlapqtatv agakgagsvd
      421 vdeygrvciv yhwdraaqis arirvaagwa ggekgmiahp rvgsevlvmc ldgnpdrpvv
      481 sgttynaerm ppwalpdqhv ltglrsrels gdsgnaaggr snhvllddtp qqlqlklrsd
      541 tdaseltlgh nvridatqgr tdqrargfel rtdahgavra akgllvtsea rydarahatd
      601 igetvarldk ahdlheslsg sahdvkaqes gdqdavhqal raqndglrgs ggnpqqgefp
      661 efaqpflala spagilattt gsthvasdqh valtsgahts igagksmlvs aqeavrvaaf
      721 ekgirlvaaa adidiqalkd svnvlakldv kvdanritit akeevlingg tsytrwngsg
      781 ivhgtkgeft ahaashtfig pdslpvpara fpgtacapcm vnaasmaspf aaka
//
LOCUS       WP_175832000             430 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175832000
VERSION     WP_175832000.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..430
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46023
     Region          22..424
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(36..37,40..41,44,77,127..128,130..132,135,155,
                     158..159,162,256,259..260,263..265,268,296,300,351..352,
                     356,360,376,379..380,383..384,387)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnllnpatpa ydageaiprr rwlrvippll laciisymdr vniafampgg mnadlgmdat
       61 maglaggiff fgylflqipg grraalgsgk aliawslvsw avlsvltglv thtwqllalr
      121 fllgvaeggm lpvvltmvsh wfpdrergra namvilfvpl agmitaplsg filaaydwhh
      181 lffcagalsl lclvvwmlfa ddgpetarwv sprekayild tlrdeqerkr aagtpaaasf
      241 gellrhptiw lliainfcyq agiygytmwl ptllknlths gmgrigllam lpyiamvigm
      301 lvtsywsdrt gkrrlfvllp vvgfaaclal svlthasmav sfafligcgf flqaaagvfw
      361 aippklcsve aagsarglin algnlggfcg pyavgvltqh vsaaagvysl avtlavagll
      421 altlpkrceg
//
LOCUS       WP_175832051            1059 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cepacia].
ACCESSION   WP_175832051
VERSION     WP_175832051.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1059
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115413
     Region          11..1037
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mstpheegrf nlsawalrhq alvvyliala tlagilaytr laqsedppft frvmvirtfw
       61 pgatarqvqe qvtdrigrkl qetpaidflr sysrpgesli fftmkdsapv kdvpetwyqi
      121 rkkvgdigyt lppgvqgpff ndefgdvytn iwtlegdgft paqlhdyadq lrtvllrvpg
      181 vgkvdyfgdp dqrifievnn aqltrlgisp qqlgqainaq ndissagvlt taddrvfvrp
      241 sgqfdnvnai adtliringr tfrlgdlatv krgyddpvvt qmraagsgaa gsgsagkavl
      301 gigvtmqpgg dvirlgkald aeskdlqaql paglklvevs smphavahsv ddfleavaea
      361 vaivlvvslv slglrtgmvv visipvvlav talfmylfdi glhkvslgtl vlalgllvdd
      421 aiiavemmav kleqgytrar aaafaytsta fpmltgtlvt vsgflpiala ksstgeytrs
      481 ifevsaiali aswfaavvli pllgyhmlpe rkrhaheahl pddhehdiyd trfyrrlrgw
      541 idwcierrfv vllitgalfv vammgfslvp qqffpssdrp ellvdlrlpe gasfaatlre
      601 terlekvidk rpeidhsvsf vgsgaprfyl pldqqlqlpn faqfvitaks vkdreklatw
      661 lettlreqfp avrwrlsrle ngppvgypvq frvsgdsiat vrsiaekvaa tmrgdartvn
      721 vqfdwdepae rsvrfeidqk karelnvtsq dvssflamtl sgttvtqyre rdkliavdlr
      781 apkadrvdpa klaglalptp ngpvplgslg rfkptleygv vwerdrqpti tvqsdvraga
      841 qgidvthavd aklnalraql pvgyqinigg sveesakaqk sinaqmplma iavftllmiq
      901 lqsfsrvlmv vltaplglig vvatllmfgq pfgfvamlgv iamfgiimrn svilvdqieq
      961 diaaghgrvd aiigatvrrf rpitltaaaa vlalipllrs nffgpmatal mggitsatvl
     1021 tlfylpalya twfrvkrder dpqngpppgg ttpaapsga
//
LOCUS       WP_175832060             268 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia cepacia].
ACCESSION   WP_175832060
VERSION     WP_175832060.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..268
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26780
     Region          1..264
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mlislvlggf vgavlgltga gggilavpal vvgmswpmqq atpvalvava gsaalgaleg
       61 frrglvryra allmavagvp lttlgvrlah vlpqrlllal faltmlivag rllrqalrha
      121 agdadasplc vgrvnpdtgr lvwswpvgva lastgamtgl mtgllgvggg fvivpmlrkf
      181 tnvsmhgvva tslmvialvg tggvfatlvs gtrapldvtl wftvatalgm aagrgasrhl
      241 aarhvqagfa avlvcvalgl lakaafga
//
LOCUS       WP_175832061             386 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175832061
VERSION     WP_175832061.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..386
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41695
     Region          25..386
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mnsqsgapva gapssvsssg adaraenfvq ivdvvkkfgd teavrsvnlt vrqgelfall
       61 gssgcgkstl lrmlagletv tsgkilidge dlaqmppykr pvnmmfqsya lfphmsvesn
      121 vafglkqegt pkaelkerva aalelvqmsk yakrkphqls ggqqqrvala rslvkrpkll
      181 lldepmsald kqirqrtqie lvnilnkvgv tcimvthdqe eamtmanria vmsegqivqi
      241 gspnevyeyp nsrfsaefig stnlfdgvtv edepdhvyie spelpsrlyv shgisgplgm
      301 pvtvsvrper ialtrkppeg afnwargrig nvaymggysl yhvkldggkt vianvsslai
      361 seldtpslgd eiyvrwsata gvvlts
//
LOCUS       WP_175832114             106 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175832114
VERSION     WP_175832114.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..106
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11432
     Region          6..104
                     /region_name="COG5606"
                     /note="Predicted DNA-binding protein, XRE-type HTH domain
                     [General function prediction only]"
                     /db_xref="CDD:444337"
ORIGIN      
        1 mnhdastpyt ddvpddfdyy dvgeltaksi lvlklnalma srglteeeaa altemarpvv
       61 tpeqrerlrn vtldqlmltl asfgqhveiv vkpagefgpa gitvsv
//
LOCUS       WP_175832198             166 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia
            cenocepacia].
ACCESSION   WP_175832198
VERSION     WP_175832198.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..166
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18129
     Region          17..155
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mkldrgstsp adaapaldri drailrqlqq dasisnvsla akvklsapac lrrverlkem
       61 glirgivall dpkplgagml vvigfvldrs tpetfaafek aaqkvsgcve chvvtgefdy
      121 fmlvrtrdnd sfnrlhaeql lylpgvrqvr sfmvlkeils thalpv
//
LOCUS       WP_175832232            1068 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cenocepacia].
ACCESSION   WP_175832232
VERSION     WP_175832232.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..1068
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=114595
     Region          1..1046
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 miarlihwsv hhrflvllat vllaawgvhs lrqtpldalp dlsdtqvivk asypgkapqv
       61 vedqvtyplt ttllgvpgak tvrayssfgd afvyvlfddr tdpywarsrv leylsqvqsr
      121 lpagatvslg pdatgvgwvy eyalvdrtgr hdlgqlraln dwflkfelka vpdvsevasi
      181 ggmvrqyqvv ldpdklrayg itqaavaeal gkanqasggs vvelaeseym vrssgylrtl
      241 ddfrhvvlrt ddtgtpvllg dvariqvgpa mrrgiaelng qgevtggvvv mrsgknaltt
      301 idavkaklad lkrslpagve ivttydrsql iaraidnltd klieefvivg vvcavflfhl
      361 rsalvailsl plgvlaafiv mryqgvnanl mslggiaiai gamidaaivm ienahkhlea
      421 ydrahpgepl taarrwelva asaaevgpal ffslliitls fvpvfslegq egklfaplaf
      481 tktytiaaaa glsvtlvpvl mgylvrgrip hehanpinrv lirlyrplle atlrrpwaai
      541 gvavvalvlt avplsrlgge fmppldegdl lymptalpgi sadkasellq qtdrliktvp
      601 evdtvfgksg radtatdpap lemfettirf kprsawrpgm tpeklvdeld rtvrvpglsn
      661 vwvppirnrl dmlstgiktp vgvkisgpdl agidaiatqv eaavkrvpgv tsalaerlng
      721 gryvdvdidr laaaryglsv adiqsvvssa iggedvgevi agrerfpini rypreirdsl
      781 enlrqlpvvt argaqirlgd varvaiadgp pmirsenarl sgyvyvdlrg vdlstavram
      841 qqavarqval ppgysiawsg qfeyleraaa tlrtvvpvtl vvifvllfvt fdsaadalll
      901 mstvpfalvg gfwlvwalgh avsvatsvgf ialagvaaef gvvmllylkg alqrrldage
      961 pptdalllda iregavlrvr pkamtvavvl aglvpimigh gagsevmqri aapmvggmvt
     1021 apllsmfvip aawlllqrrr arsagrtrhs davppgtnvp slptgesr
//
LOCUS       WP_175832254             336 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175832254
VERSION     WP_175832254.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..336
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35733
     Region          9..330
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 msqstrsard ivvvgfegvq slditgpmev favanrhlpa haapyrltla sqhgddivth
       61 aglrlagaaa laalparidt iivaggaeaa lrhaaseagv lpwlrtriad trriasictg
      121 afvlaaggwl dgkratthwn qcatlqalcp dariepdaly vsdppfhtsa gvtagidlcl
      181 alveadcgap talavarelv lfmhrpggqa qfsvgldiqa ratprmrsll adiaddpagd
      241 lgvaalaarm hmsertfarh ffketgvspa qyvlaarver akalleradw pleriaerag
      301 fgsvdalqra fakrvgtspr dyrarfgprr dkprte
//
LOCUS       WP_175832259             263 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia
            cenocepacia].
ACCESSION   WP_175832259
VERSION     WP_175832259.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..263
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29343
     Region          32..87
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(33,58)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(40..41,52,55,59..60)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          104..263
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mtvttrtpfg dflrsrrkkl rpdavglhdg prrrtpglrr eevaeragig vdwyvrleqg
       61 rdvnpsdatl dalaralrld kaeaahlrtl arrdgsrafv pervppaiar lvahlqqpay
      121 vtgrrwdila wnaaaadllg fdrlapadrn ilvymfeapy aralfaaswa dearrmialf
      181 ranhdlyasd pafvalvarl ragsgefaqw wdthdvrsga sgekvlvhar rgtqryeyat
      241 fqanddpalk laiytpvsgd eqt
//
LOCUS       WP_175832268             521 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA cytosine methyltransferase [Burkholderia cepacia].
ACCESSION   WP_175832268
VERSION     WP_175832268.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..521
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=58481
     Region          1..502
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mtipvvdlfa gpgglgegfs avhdvdgnrv fdirvsiekd avahqtltlr alfrilardh
       61 vpdayydyir gdidrttlfn dqavaralel atqeahclel gvtpedeids lirtaidghd
      121 dwvliggppc qayslagrsr rrnvdpefes dpkhflyrey lriirdfqpa vfvmenvkgm
      181 ltsthngqri ferifddlse ptpgvhydir sfvtasrpgg lapeeyiira edfgvpqmrh
      241 rvillgvrsd ragqlhdlld gsqgrvsvrd vlaglptlrs klskeldsae awlqalktak
      301 salkgwrspv rtnieslmad avnqaqrinn vggkfirrdm kaprgladnf aswihddrig
      361 gvcqhesrgh mvsdlhrylf ascyakeyqy spklsmfppg llpnhrnldg envpfddrfr
      421 vqisgtpstt ivshiskdgh yyihydpsqc rsltvreaar lqtfpdnyff egtrtqqyhq
      481 vgnavppfla kqlgesvanf lqlpkraavq srsardlfel g
//
LOCUS       WP_175832363             656 aa            linear   BCT 11-JAN-2025
DEFINITION  arylsulfatase [Burkholderia cenocepacia].
ACCESSION   WP_175832363
VERSION     WP_175832363.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..656
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=69941
     Region          54..622
                     /region_name="PAS_like"
                     /note="Bacterial Arylsulfatase of Pseudomonas aeruginosa
                     and related proteins; cd16025"
                     /db_xref="CDD:293749"
     Site            order(64..65,102,163,165,270,413..414,473)
                     /site_type="active"
                     /db_xref="CDD:293749"
     Site            order(64..65,102,163,165,270,414,473)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293749"
ORIGIN      
        1 mkksasplha frfrvvcaai agavslascg gvdsdappsq agvtptptpt qaakrpnily
       61 imaddlgysd ihafggeint pnldalvasg rilsnhhtgt vcaitramlv sgtdhhlvge
      121 gtmgvptder rglpgyegyl ndralsfaql lkdagyhtyi agkwhigsgi vgsttgsgqt
      181 pdqwgfersy vllggaatnh fahesagssn ytedgryvqp gqpgqpggtg gspavfystd
      241 fytqklisyi dankqdgkpf fayaaytsph wplqvpdpwl hkyagvydag ydairnaria
      301 rqkalglipa dfkpfdglpe ttvaspatan ngtasakyin avhsaadgys dygpgkvdkl
      361 wsslspaerk aqarymeiya gmvenldyni glliqhlkdi geydntfimf qsdngaegwp
      421 idsgadptat dtanaqepty salgtdngkq naqrlqyglr waevsaapfr ltkgysgegg
      481 vstptivhlp gqsqalptlr afthvtdnta tflavagvtp psqpapplvn tltgvdqnkg
      541 kvvynnryvy pvtgqsllpv ltgsatgevh ttpfgdeayg raylrsadgr wkalwteppl
      601 gpldghwqly dlasdrgett dvsaqnpsvi gtlvdqwkty mgnvggvepl rprgyy
//
LOCUS       WP_175832384             299 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175832384
VERSION     WP_175832384.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..299
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32700
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..296
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(103,107,146,160,164,231,248,275)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(104..105,109..110,112..113,116,120,122..128,191,
                     222..225,229,236..237,240)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mqtdlgdlna fmavarasgf rdaarvtgls asglseavrr learlgvrll hrttrsvvpt
       61 eagerllarl apaltevaaa ldgidefrgr pagtlklnvp vsasrlvlpa ivprfleayp
      121 dirlevtade sfvdvlaagc dagiryderl eqdmiavpig priqrfataa apgyldrhgr
      181 prhprdllgh rclrgrfasg amppweyerd gevvrvepaa gpllvqigga telmvdaaia
      241 gtgilylfed wvrphfesga lepvlepwwr pfsgpflyyp grrlvppalr afidfikey
//
LOCUS       WP_175832411             273 aa            linear   BCT 11-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175832411
VERSION     WP_175832411.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..273
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30658
     Region          20..215
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mseqdmltdi hrlcdeiein gfaivrnlid rdtvtelsrh adsawrrgvd pdrphskvei
       61 agaeveavda vrsvaretrl lgtmlallgp niyvnytgft inppqapdka pmefhtdggr
      121 isrehaggae prysiktsvw ltdgtqlgvg nfyvipgshk wrtrpdadld alavpvlvnv
      181 gdaiiferrv whtrkpnlss ttrkvlfldy aprwmerkcp svalslnhyl epienqlfnn
      241 qanwsafapk khmipclalm kalgitrred rar
//
LOCUS       WP_175832413             279 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia cenocepacia].
ACCESSION   WP_175832413
VERSION     WP_175832413.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10549439
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..279
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31156
     Region          59..151
                     /region_name="Methyltransf_11"
                     /note="Methyltransferase domain; pfam08241"
                     /db_xref="CDD:462406"
     Region          <109..155
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 msfslssvry lawlksrlsl sgpvlllgrq mvfarrtdva wairaqgeep yaqppesdgp
       61 nivgldpdrf stytndvcvl rmllgdvdvd avdidgyqga dvihdltqpl pdglkskygl
      121 vidagtlehi inpvqvmenl vsalrpggti ihmtptagyv dhgyfqfgpl ffdtyyrskg
      181 mtidglclve qparrtnhtq wrfwawnkal krkkllsmdp lstfcaarrt vdcaasgstv
      241 qnfaeylead serahevrpw glvevaelrt rtdypleql
//
LOCUS       WP_175832457             341 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175832457
VERSION     WP_175832457.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..341
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36389
     Region          29..324
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mttsprrral iaaglgvlgg lgapalvrak prtvriskgy gvlylpllvm ekqrlferha
       61 arhgvrdvav ewvlldggns vndammagtl dfagagapgf ielwarargi pnvevigisg
      121 lsttslslna nraglaslrd ftpsdriavp girtslsavv lqmvasrqlg pthfaqldsi
      181 tvnlphpqam qalirrengv tahftsppfs tlelrqpgih rvvssvdvlg pmtldvvfap
      241 krlvdaepal avaflgalde anrliaqdpr aaaalyaass gvgvshddvm rmlaapdtrf
      301 svlpnqlmdy veflylagti takprawrem fapmlddyrs g
//
LOCUS       WP_175832459             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175832459
VERSION     WP_175832459.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47231
     Region          23..422
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,154,
                     157..158,161,256,259..260,263..265,268,295,299,349..350,
                     354,358,374,377..378,381..382,385)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnatdtldpa saeeqrimsk marrllpilv vmfliafidr qnvgfaklqm vhslgmteaa
       61 fglasslffi gyllfevpst lalhrygarv wlarimltwg litvlmgftt smpafcslrf
      121 vlgiaeagfy pgviyyltlw fpqsyrakvl giftlgsala nmlgslvggv llslngvwgl
      181 agwqwvfvat gipavvvaiv vfrvlpasfr earflderek qivaaalere kpaqaehgqp
      241 wkalldprvm lfaatymlms tslygvtywl ptivksfgvs sttngflsml pwalavvllv
      301 wlpsklrrak silrtiaiva algalgflls lvlpstplrf ialvlggaci pllypcfwsm
      361 ppryftgara aasvaainsi gnlggffsqn lmpfagkvtg tefgpmivpi vclallgvga
      421 lvawtrserg mvaara
//
LOCUS       WP_175832615             173 aa            linear   BCT 11-JAN-2025
DEFINITION  chemotaxis protein CheW [Burkholderia cenocepacia].
ACCESSION   WP_175832615
VERSION     WP_175832615.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..173
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=18420
     Region          14..155
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mtradpqnga halflmfeld geryaldaag idevlplavm kavpgapdwi agllmrgaqp
       61 vpvidvpmla lgrraqalrs trlvmvrhra ghaghadger tigliverat qtmridraaf
      121 rasgistart rwlgrvantp dgvvqqvsvp dlvddvarly lfdglpghgg esa
//
LOCUS       WP_175832637             479 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175832637
VERSION     WP_175832637.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..479
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48524
     Region          21..418
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(28..29,32..33,36,68,118..119,121..123,126,148,
                     151..152,155,284,287..288,291..293,296,324,328,380..381,
                     385,389,405,408..409,412..413,416)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mdtttsspaf ppalarivat vsigfvvtql dvtivniala hlaadlhlpv aglqwvvday
       61 tlafavlmls agalgdrfgt rrlyvaglll fafaslacga avapamliaa ralqgvgaaa
      121 mlpnslalln dacrhdprlr aravggwtaa gsiaiaagpv vgglliaawg wrgiflvnlp
      181 lcaaglaatf awvparreqa aparstrsld prgqfiaiam ltaltgavie wrplgfthpv
      241 vaggfvlaal aalgfvaves rtatpmlpls lfrhpafsaa vlfgicvnlt yygtvfvlal
      301 ylqrargesa lqaglaflpl tggfllsnla sgrvvarhgp rvpmvagalv aalgygslhf
      361 vdaatplgvl lvpfllipsg mgfavpamtt avlasvaper agiasavlnt arqaggaigv
      421 aafgalaggg gaaqvvsglr ietvvsvall vaaallatrv rtdanrgapr srqalsvhd
//
LOCUS       WP_175832640             128 aa            linear   BCT 11-JAN-2025
DEFINITION  GtrA family protein [Burkholderia cenocepacia].
ACCESSION   WP_175832640
VERSION     WP_175832640.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..128
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=13575
     Region          11..128
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mirtfhaaer arlisfgvsg vgstalhali aaamfalfda tpvianataf vcstafsyla
       61 ntlwsfsspv twgnfvrflt vamaglavtm llahgtdalg larawsivav vlcvppvtfv
      121 lhrlwtyr
//
LOCUS       WP_175832659             216 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175832659
VERSION     WP_175832659.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10583942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..216
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23396
     Region          25..168
                     /region_name="Pyridox_ox_2"
                     /note="Pyridoxamine 5'-phosphate oxidase; pfam12900"
                     /db_xref="CDD:432864"
ORIGIN      
        1 mtektdlsst prttirrlpe lashdrtmlh rivdeayvch iafgdgqnth ciptahwrrg
       61 ddlyihgsng srmvkalsag aqacvamtll dglvlarsaf nhsmnyrsav iygqfdvieg
      121 saekfaalda lmdkiapgrk hearpgnske inatsvlris maeaavkvsd slpsdkeedf
      181 glavwagilp lkttrgapvh adgnvvvpdy vrnwad
//
LOCUS       WP_175832717             135 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF427 domain-containing protein [Burkholderia cenocepacia].
ACCESSION   WP_175832717
VERSION     WP_175832717.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Lupas,A.N., Zhu,H. and Korycinski,M.
  TITLE     The thalidomide-binding domain of cereblon defines the CULT domain
            family and is a new member of the beta-tent fold
  JOURNAL   PLoS Comput Biol 11 (1), e1004023 (2015)
   PUBMED   25569776
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..135
                     /product="DUF427 domain-containing protein"
                     /calculated_mol_wt=14724
     Region          <41..129
                     /region_name="COG2343"
                     /note="Uncharacterized conserved protein, DUF427 family
                     [Function unknown]"
                     /db_xref="CDD:441912"
ORIGIN      
        1 mslnpdtpsr pvkspgpdhp iliephssrv vvkvagkvva dtrhalvlre asypavlyip
       61 redadmslle rtdhatycpy kgdcayysip aggersanav wtyehpnpav esirghlafy
      121 pdrvdsiees llvta
//
LOCUS       WP_175832668             822 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175832668
VERSION     WP_175832668.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 822)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 822)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 822)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..822
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87439
     Region          499..780
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mrhillgwll aavvsaahaa apapaaasaa sgaapaltpq earqalnvle nprdraqvet
       61 tlraiaavga lsapavqasa apaasgasaa aapaaltsng lasmlvrqgs rwatqignal
      121 qeslrslldi gsvgswwhdk lvsadqradl trtlgilvav llpalivewl akrllrrala
      181 tvaarradtl rhtasdsats devhapppdt stppdtaapd tadatpassq srgharrhtt
      241 llqrmpralv slalravpll vfvgvasltm sllveadtpi eaalealidt yvicrlitiv
      301 srlffqpdar qlrllhisda wadfvqrsia rivivvgact aaveiaanfg lseaghvall
      361 kavalvghvm isvlilqcrr pvaariraag adrpaftvvg naladawapv svfivmalwf
      421 vwaldvhngy rvlitlggrs iavmiamrmv sivvfgalar lfqrrdddrt lvhlhayryy
      481 pllrqivsga igivtvvlll qiwgvpifra fetgtighrl asalvtiaia aivalvvwea
      541 aniaierrlq rwtregnlvr aarlrtllpm lrsllfvmia lvvvltglse lgvnvgplla
      601 gasifgvalg fgsqklvqdf itgifllmen amqvgdwvtl agvsgtveyl sirtvrlrag
      661 dgslytipfs svttvnntnr glgnaavkvs iaygedidra iatlkeigaa lrddpkyhdg
      721 ilsdfsywgi dqvdgaalal agqmqctdsa rwgvqrefnr riaetfrerg irianpqrsv
      781 vayadgsrpv gseendprpd trntaatatp spspdeaerk pg
//
LOCUS       WP_175832933             303 aa            linear   BCT 11-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175832933
VERSION     WP_175832933.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..303
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34749
     Region          5..257
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mqanlrsrfh hdgfavidrl idpseiedlr eighrllggr tgyaeglmfd fypetngrda
       61 rpqllqlhwa syferrlstl rirraafeia qallgpevrf agdsfflkqp rtgtvtpwhq
      121 ddaftdarie hrevnfwipl qavsvdngcm qfipgshlyd vlphgplrgd vtahglecvg
      181 gfdpahavac plmpgdctvh agrtlhaaga nlsdqpryay alnfrlprrr ssvatnfpwh
      241 ntwrpsrier arasrslrgy wpylrrelyt fdfrnpfewr laggriarwl nvprrqlrep
      301 gpe
//
LOCUS       WP_175832820             348 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175832820
VERSION     WP_175832820.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..348
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37069
     Region          17..197
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          230..312
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mlysaiylrd stmmsddpfs dilrltnaes latggfsagg awavrfpapd kikffavvkg
       61 tcwvsidgee tpirfgsgdv glltakrsfv lasdpcvppv damalfsgag ksvvklgdgd
      121 gfaqigghvl ldpvtgslls dvlppwihvp aaspqavkvr wlleqlveer aadlpgaqlv
      181 saqlsqllfi qilrahlkts asltgwlraf gnpriapalr lmhgdparsw hldelaaaca
      241 msrttfashf rasagvaplt ylgewrmrla errlrdedip vallaqslgy ssesafshaf
      301 krmsghspta yrhiirtaae gagsgrggvr aavkatgatp qpfplepr
//
LOCUS       WP_175832938            1082 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cenocepacia].
ACCESSION   WP_175832938
VERSION     WP_175832938.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..1082
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114185
     Region          1..1059
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mwivrlalrr pytfvvlall ifiagplall rtptdifpsi dipvvsivws yngfsaedma
       61 kritsnyera ltsdvddieh iesqslngvs vvkiffhpga dinraiaeaa snaasilril
      121 ppgtlppnii tynastvpil qlglssdtla eqqlydlgns firtqlatvq gaavplpfgg
      181 kirqivvdld tralqakgla pidvvnaina qnlilpggta kigtheynvq mngstqtvaa
      241 lndlpvktig gnvvyvrdva hvrdgyapqt nivrvdgkra alltvektgs astltiidqv
      301 kamlpkiaag lpkalhiapl ddqsvfvkaa vqgvvreali aacltalmil lflgswratl
      361 iiaitiplav ltsllalsal gqtinimtlg glalavgilv ddatvaieni thhlelgapl
      421 eeailtgsge iavptfvstl sicivfvpmf lltgvarylf vplaeavifa miasyffsrt
      481 lvptlamalm rakgggrppr gvfaplvhva rfqaafehrf eavrlryral lsaaiarrrr
      541 faaafllaci astglyafag qdffpsvdtg eirlhlrapt gtrieetarl tdeveakirs
      601 vipanqlagv ldnigvpvsg inltydssdp igtedadvlv tlkpdhasta ayvaklrnvl
      661 aqafpgvtfa flpadivsqi lnfglpapid iqivgnkldq nravanalla klrgvrglvd
      721 ariqqpgdep ainvnvdrtk aiqagleqrd vaqnllials gssqttpnfw ldprngvsyp
      781 vlvqtpqytv nslqslanvp lpagtarspq tpaggpaaga paqnllgalg sfsratqqav
      841 vshynvqpvl difasvqgrd lggvtgdvtk lvdaaraqlp pgssivlrgq vqamhesftg
      901 llgglalais lvyllmvvnf qswldplviv gglpaslagi awmlfvtrtt lsvpaltgti
      961 lcigiatans ilvvnaarel laggeppwqa aldagfarfr pvvmtalaml igmlpmalgl
     1021 gdggeqnapl gravigglaf gtvstllfvp vlfgfvhawl arrrdaaaar haqhapdtpa
     1081 lr
//
LOCUS       WP_175832945             245 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: YoaK family protein [Burkholderia cepacia complex].
ACCESSION   WP_175832945
VERSION     WP_175832945.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..245
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=25006
     Region          22..233
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mqpaqvtaag aaapdrvrge dvflasiagy vdtlgfvalf glftahvtgn filigsglag
       61 vgqglmikwl afpafiagiv aarvldhrmr vrghgvrars lyalqtilla gfmlagvaas
      121 pigsadapat ivcgllgaaa mgvqnahgrl tartvvantv mtgnvtqavi dafdwlvpia
      181 apaereaara rlrrtlppvv gfalgagaga sayvyagfwt lalplaalgf ltwrsgrtge
      241 psasr
//
LOCUS       WP_175832950             348 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia cenocepacia].
ACCESSION   WP_175832950
VERSION     WP_175832950.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..348
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36801
     Region          68..319
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(82,165,167,169..170,197,251,272,275,288,290,319)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mktlfqhacv aqaarlliva gcagllapaa faqagvqpda hanaqpetqs ttpaatagrq
       61 ppgfyrqkig dftvialsdg thpfpvdtvf rdiskdeirr dldraflepp vqgsinaflv
      121 dtgskrilvd agagtlygdc cgkllddlra agyapgqide vllthlhkdh vggiasngam
      181 tfpnavvrvn aveaaywldp ankahapafl asffdaaaaa vapyaaagrf ktfrgdatla
      241 pgiravpmpg htpghtayli esghagllaw gdivhvaaiq lrdvdatvqy dsdaatarrt
      301 rrdtlkrvad rrylvgaahi afpglghlrr dgaqydwvpv nydatpvr
//
LOCUS       WP_175833008             430 aa            linear   BCT 11-JAN-2025
DEFINITION  NRAMP family divalent metal transporter [Burkholderia cenocepacia].
ACCESSION   WP_175833008
VERSION     WP_175833008.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..430
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45976
     Region          20..430
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 msgldedaqp aadapqaaak pwyrrlgpgl lagasdadps nvavyaqags qfgfnmlwmi
       61 vvtlpmmvav qlasafigrr nreglvagir qhyservakt livmvvivnv vnvgadlaam
      121 gdatalvvgg rsywyaplyg iaslalqvml syeryarwlk wmtlgliayv lelgfvhvdw
      181 gdllhaivlp hiafthdyat tavavlgttl spylfvwqaa leveettaeq qngernsrre
      241 teqritfdtw tgmivtnavs fcimvigaav ffargrhdig staqaaealr piageaafvv
      301 fafgivgcgl laipafagsa aygcaeawrf reglnepvrr apafytvlal cvivgiaicf
      361 spidpiraly wsavlngvaa vpmlvlvmll sqqrdaagqp gsgpvskvfg wlavalmavs
      421 vvtmivdvlt
//
LOCUS       WP_175831785             177 aa            linear   BCT 11-JAN-2025
DEFINITION  GbsR/MarR family transcriptional regulator [Burkholderia
            cenocepacia].
ACCESSION   WP_175831785
VERSION     WP_175831785.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Nazaret,F., Alloing,G., Mandon,K. and Frendo,P.
  TITLE     MarR Family Transcriptional Regulators and Their Roles in
            Plant-Interacting Bacteria
  JOURNAL   Microorganisms 11 (8), 1936 (2023)
   PUBMED   37630496
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Will,W.R. and Fang,F.C.
  TITLE     The evolution of MarR family transcription factors as
            counter-silencers in regulatory networks
  JOURNAL   Curr Opin Microbiol 55, 1-8 (2020)
   PUBMED   32044654
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Deochand,D.K. and Grove,A.
  TITLE     MarR family transcription factors: dynamic variations on a common
            scaffold
  JOURNAL   Crit Rev Biochem Mol Biol 52 (6), 595-613 (2017)
   PUBMED   28670937
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Grove,A.
  TITLE     Regulation of Metabolic Pathways by MarR Family Transcription
            Factors
  JOURNAL   Comput Struct Biotechnol J 15, 366-371 (2017)
   PUBMED   28694934
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 177)
  AUTHORS   Grove,A.
  TITLE     MarR family transcription factors
  JOURNAL   Curr Biol 23 (4), R142-R143 (2013)
   PUBMED   23428319
REFERENCE   6  (residues 1 to 177)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   7  (residues 1 to 177)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   8  (residues 1 to 177)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..177
                     /product="GbsR/MarR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20174
     Region          1..157
                     /region_name="GbsR"
                     /note="DNA-binding transcriptional regulator GbsR, MarR
                     family [Transcription]; COG1510"
                     /db_xref="CDD:441119"
ORIGIN      
        1 meltpiaerf ilhwgemgsr wgvnrtvsqi hallylagrp vaadeiaetl naarsnvsts
       61 lkelqawrla kvvhvlgdrr dhfetstdiw elfklivegr rqreieptlt vlrdcltspe
      121 ianesreteq rirdtlqfve tlttwsdeml rlkpdtlmka lgigakisqt vrrkpsk
//
LOCUS       WP_175833070             252 aa            linear   BCT 11-JAN-2025
DEFINITION  YoaK family protein [Burkholderia cenocepacia].
ACCESSION   WP_175833070
VERSION     WP_175833070.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..252
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=26670
     Region          11..243
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mpaqyfrnlt gkhrsatanr qlgfslafva gaanaggfla vkqytshmsg ivsaiadqta
       61 lgdvrlalag isslgsflig ascsailvnw grrrglhsqf mlpllveaal lllfgllgsh
      121 lalwetffvp vtvtllcfim glqnatitkl sgaeirtthi tgivtdlgie lgklfywnrs
      181 aidvdahavi anrsklriha tmlasffvgg lagaigfkhv gyvstvplaa vlvtlaivpv
      241 iddlltllrs qr
//
LOCUS       WP_175833089             343 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175833089
VERSION     WP_175833089.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..343
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36753
     Region          23..326
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 msfsflparr alaatltaal afagavipqa vhaegriria eqfgvvylml nvardqqlie
       61 kegrkagldi kvdwvrlsgg aavndallsg avdiagagvg plltvwdrtr grqnvkgvas
      121 lgnfpyylvs snpnvktiad lsakdriavp avgvsvqsrv lqyaaakqwg dkqfdkldpl
      181 tqaiphpdat aailansnvi tghfgnppfq eqelagnpna hivlnsydvl ggpssatvly
      241 atekfrddnp ktyrafvaal adaarqiaad peraadtyir vngskidral llkilrnpqv
      301 qfktapqntl plaqfmhrtg airnepkswr dyffddpata ggs
//
LOCUS       WP_175833093             174 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia cenocepacia].
ACCESSION   WP_175833093
VERSION     WP_175833093.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 174)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 174)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..174
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17778
     Region          <27..159
                     /region_name="TsdA"
                     /note="Thiosulfate dehydrogenase TsdA, contains C-terminal
                     cytochrome c domain [Inorganic ion transport and
                     metabolism]; COG3258"
                     /db_xref="CDD:442489"
ORIGIN      
        1 mrkplaclla acamtsgafg agfglgqpid raalaawdid vapdgsglpp gvgtvarggh
       61 vfadkcamch gaggeggvgd plvggvgsla sakpkktvgs ywpyattlfd yirrampyna
      121 pqslstddvy avtayvlhln givpaaarld artlprvrmp nrdgfvpdpr pgkl
//
LOCUS       WP_175833110             295 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            cenocepacia].
ACCESSION   WP_175833110
VERSION     WP_175833110.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..295
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30449
     Region          2..294
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mssfvihllt vgclyatmal glnlqagyag lvnfgfiafs glgayaagia sqlgwplpsa
       61 lalalaaaga laivvarlgr qlsadywgia tlaiaeilrt ialneswltg gaqgiggiap
      121 lfpglrapwa dlaflavtag claltyatyr rltasrfgra lkvmreepal avcfdydpla
      181 lktrasiaga lpaalagala awyigyvgpd amiasetfal wtvvmvgglg shvgvlvgtl
      241 ivqavyalap flkdwlavgs dltgavrlgl vglmllacvl wrphglvper levrp
//
LOCUS       WP_175833154             701 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cenocepacia].
ACCESSION   WP_175833154
VERSION     WP_175833154.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..701
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76081
     Region          7..701
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 msrrnwaaap maivvgatgm gaadaqetal ptievsaqra tapfrtrest satrseadvm
       61 eipfavssvd tkliqtvaat rgddlydwva gvsrqnnfgg lwdnyavrgf agdgntsgtd
      121 ylvngfswnr gmsvprdtvn lermevlkgp asalygrgdp ggiisyttkq pqfarantig
      181 vsagsygalr qtldstgpit kslayrfvam nenngsfrdt vsskrylfsp sftwdigadt
      241 tlhyefesar qrapldrgvl avngqlgvip asrflgeprd gdydvrntgh qftlehrids
      301 swsinagvaq rntdltgrss eafalqpdgr tlwrryrqva fhsndlqgrl ettgafrtgg
      361 ightlvmgvd ayrfnydqfv trstpsasap yaidifdpvy gqpaptprta tnllerddgq
      421 gvyaqdtlaf gphwkilagl rwdrfhqsid nrlkgvttsq lqtavsprig vvyemspaws
      481 fyantaysfr pnngadingr afdpekghgy eagakwagar wlttvsafyv tkrnvltadp
      541 anagfsraag evrsrgiefe wsgdlghglr gianlayvda evtrdsvlap gsrlvdvprl
      601 sgsallmyet tlpfadkaga gagviyvgrr agntantqdg felpayatvq lngyvqvnkh
      661 lrasvvlnnl fnrttyvssy nslwvtpgap rsllaslays f
//
LOCUS       WP_175833122             287 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia cenocepacia].
ACCESSION   WP_175833122
VERSION     WP_175833122.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..287
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=31033
     Region          2..213
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mtilvtgatg rigrqlvrql vdrgadvrvl vrdpakadfp aavtvaqgdm ldvdalraaf
       61 sgvrtlflln gvagdeftqa lialnlarea giervvylsv lhadrfvnvp hfavksgaer
      121 mieqmgfsat ilrpayfmdn datvkdvivg hgvypmpigg kgiamidard iaevaaleli
      181 rrhdapgklp vetlnlvgpd tltgpqlasi wsdtlgrpva yggddptpfe dnfakfmpkw
      241 mayemrlmae rfvsdgmvpe agdvarltai lgrplrtyrd fvaalvr
//
LOCUS       WP_175832988             945 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Burkholderia
            cenocepacia].
ACCESSION   WP_175832988
VERSION     WP_175832988.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 945)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 945)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 945)
  AUTHORS   Ingmer,H., Vogensen,F.K., Hammer,K. and Kilstrup,M.
  TITLE     Disruption and analysis of the clpB, clpC, and clpE genes in
            Lactococcus lactis: ClpE, a new Clp family in gram-positive
            bacteria
  JOURNAL   J Bacteriol 181 (7), 2075-2083 (1999)
   PUBMED   10094684
REFERENCE   4  (residues 1 to 945)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11909043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..945
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..945
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103361
     Region          4..>54
                     /region_name="McsA"
                     /note="Protein-arginine kinase activator protein McsA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3880"
                     /db_xref="CDD:443088"
     Region          83..877
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mpalcdicha rpavaratvm qdgerktisi cdyhfrqlmr hqsmlnpfds llggggpssl
       61 fgglgddspl aaeipresvd ptdafseqtl ellqraaeka helrrselds ehllyaladt
      121 dvcaallkel klspediksy idahahtgta dpdapldkls isprvkkavq yafqasrdlg
      181 hsyigpehll iglasvpdsv agtllkkygv tpealrqkvv kvvgkgaedg rvdaptgtpn
      241 ldkfgrdlta iarqgkldpv lgraqeiest ievlarrkkn npvligepgv gktaivegla
      301 qrivngdvpe vlrdkrlvev ninsmvagak yrgefeerak qlidevtakq delilfidel
      361 htivgagqgg geggldianv lkpalargel sligattlne yqkyiekdaa lerrfqpvfv
      421 pepsveqtiv ilrglrdsle ahhqvtfadd afvaaaefad ryitsrflpd kaidlidqaa
      481 arvrigatsr pvdiqegeaq iaqlkreqdy atsrkrfdea kqfeeqinak qkavdemmea
      541 wqrktgsetl evtvesvaev vsrltgipvs eltqeerqkl lkmeeqlrer vvgqsdavva
      601 vsdavrlsra glgqthrpia tflflgptgv gktelakala etvfgdeqai iridmseyme
      661 rhavarliga ppgyvgydeg gqltervrrr pysvilldei ekahpdvynv llqvfddgrl
      721 tdgkgrvvdf sntiiiatsn lgaaiimdnl tqpeaarktd kaireelmqv lkghfrpefl
      781 nridevivfh alskdnirsi vqiqldrvvr taaaqditlv mgsslvdhlt evgyqpefga
      841 relkrqirqt ietrlakeil adrlksgdkc evdydkdsne vkfntlaape akdtkdakpd
      901 adgkakpdgk aakaadakqd dtpadapppa akpgkkssga kkdah
//
LOCUS       WP_175833165             371 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175833165
VERSION     WP_175833165.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..371
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38622
     Region          22..345
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mgtpdtsrlt apaldaslvd wldanatqld tsaalkaeiv prladaglfr tgvpaslgga
       61 ggttadaiag iaavaehslt aafvlwgqrs fieyllqspn talrerwlpa lldgrcagas
      121 glsnamkyls gieslqidat phaeraddwr mtgrmawvtn lraerfvvaa avafgdgrps
      181 aivaipddap gltrspdldl ialrgsntaa lhldavpgda awlihpdaqt flsavrpafl
      241 glqcglsigl arrslaearr aaettrgilg sevescaael aaacaqlsag iadgslrlhp
      301 drlfalrial athvgtavnl eleasggrgy lrdaglgfer rwreaafipi vtpsvvqlka
      361 qlaartrsia a
//
LOCUS       WP_175833166             264 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cenocepacia].
ACCESSION   WP_175833166
VERSION     WP_175833166.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..264
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28611
     Region          1..255
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mtrplldarh ltlgydgerr ntvladvsls vgrgeivali gpsgtgkssl lralaglerp
       61 qsgtvsidgt tlqgphpria iafqdpcllp wlsternvaf glafehqerl trdqqrervr
      121 salhavglea aaslrpaqls ggmaqraala ralarqphal lldepfsald evtraamqrl
      181 lvnivattrc atvlvthdid ealrvadriv llgtqgrfid awhvdyphpr dafvselgtm
      241 ridilkalqa gmkrphasel qsln
//
LOCUS       WP_175833208             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175833208
VERSION     WP_175833208.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33732
     Region          12..>148
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          97..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,232,249,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,195,
                     226..230,237..238,241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mrssseklsg sisvfaavvd agtfsaaadv igmtppgvsr aiarlekrln irlfnrttrs
       61 vslteegrrf yeqvmphlag leeaataaag gvsavrgklr inldpvvyra ilgprldafm
      121 dahpeleiel iardslgdlv mdgfdlavrf geprasslia rklldtgvvt vaapsyiarr
      181 grpakpedle nrhhrclefr npetgkpfaw efhrkrkriv vdtrgrltvn dpgallnacl
      241 agsgiaqmll lgaepliadg rlinlfpewa deryplyayy psrhhvpakt rafldfiric
      301 sekprh
//
LOCUS       WP_175833210             246 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175833210
VERSION     WP_175833210.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..246
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27008
     Region          2..213
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mshdiepttt qqdtiyatlr qwvtvgrflp gerlkirnva aemgvgqmpv raalqrlaae
       61 galvnvpnag mivprltvpe fddllqmrml legeaaergc lrlepaelat lrklcqrmak
      121 alkhpadqpa rarksagdkp tlkqaavslk adqatdylaa nedfhvllyk aagspllfel
      181 idtlwlkagp isnrlfdtse asavlndahe dlmdaldrrd aaaarraver difvagqflr
      241 stlkrd
//
LOCUS       WP_175833216             198 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent F420 reductase [Burkholderia cenocepacia].
ACCESSION   WP_175833216
VERSION     WP_175833216.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..198
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20685
     Region          3..178
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mryaiigfgk ighalarafa rngievavat trdpqsftad aaaigptiip ttlaeavkad
       61 viflavrfes hpavakalad wngktvidam ntqapldeld glpssafvak aftgarlvkg
      121 fnhlaagilg qdpavhggrr vvflasddde aaaevgtlae qlgfapiqlg glseggwlvh
      181 argknwgrli fkdlvrfd
//
LOCUS       WP_175833234             385 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF4382 domain-containing protein [Burkholderia cenocepacia].
ACCESSION   WP_175833234
VERSION     WP_175833234.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10626736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..385
                     /product="DUF4382 domain-containing protein"
                     /calculated_mol_wt=38574
     Region          35..183
                     /region_name="DUF4382"
                     /note="Domain of unknown function (DUF4382); pfam14321"
                     /db_xref="CDD:433865"
ORIGIN      
        1 mnniiksalc aafvpfvlag cgggddgggt qtgtlhvamt dapscgfdhv yvtvsqvrvn
       61 ananaadnda gwstvslatp qkidllsltn gvladlgqta lpagqyqqvr lvlaqnqgnn
      121 lansvvptgg veqalatpsa tqsgykiiqp ftvqpntlvd lvldfnacks ivqrgngsya
      181 lkpvvtaipt vvsgaisgyv asaeggatvy aeqggkvvrg tvadssgkfv lspliqsstq
      241 gnydvvivqn nfasgivrsv pvvvntttav sastapitls astmstvsgt vtasanafvr
      301 alqtvdanay eitsinanmd tgaysrsvpa aapivgtysg slpvalaaap aaagqytiea
      361 daasgatqsa nvnattsqsn vnfgf
//
LOCUS       WP_175833260             327 aa            linear   BCT 11-JAN-2025
DEFINITION  ferritin-like domain-containing protein [Burkholderia cenocepacia].
ACCESSION   WP_175833260
VERSION     WP_175833260.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10090058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..327
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36562
     Region          98..228
                     /region_name="Ferritin_like"
                     /note="Ferritin-like superfamily of diiron-containing
                     four-helix-bundle proteins; cd00657"
                     /db_xref="CDD:153097"
     Site            order(107,137,140,187,217,220)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 mndtltvmqd tadirwsmpv dalmsndyal reealnrlye kakaaqwdva tdvdwshdld
       61 panplgmpdp tlliygtelw gkladadkre vrhhaqgwll sqilhgeqaa licasklasa
      121 edglsarlca aaqmmdearh veayaklvne kvdvsypmsr slkgllhdti tssaldmtnl
      181 gmqvlvegia lsifqsvvay stdpfikdlf lriqrdearh favgritlcr vyaemsshel
      241 rereeficeg aavlyehlca ddiwepmgls krecsamvre spvsssirrs ifrrlvptir
      301 emglltptvq atfekldvld yaampln
//
LOCUS       WP_175833271             721 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 28 protein [Burkholderia cenocepacia].
ACCESSION   WP_175833271
VERSION     WP_175833271.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 721)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 721)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 721)
  AUTHORS   Abbott,D.W. and Boraston,A.B.
  TITLE     The structural basis for exopolygalacturonase activity in a family
            28 glycoside hydrolase
  JOURNAL   J Mol Biol 368 (5), 1215-1222 (2007)
   PUBMED   17397864
REFERENCE   5  (residues 1 to 721)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 721)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..721
                     /product="glycoside hydrolase family 28 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73845
     Region          <40..>139
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          194..625
                     /region_name="Pgu1"
                     /note="Polygalacturonase [Carbohydrate transport and
                     metabolism]; COG5434"
                     /db_xref="CDD:444185"
ORIGIN      
        1 mtlpvcrpna rpnrrpralg llaallataa altacggdda stgggaasta ppatsvfqvg
       61 tttvdpnlpa epalpadtqv cstleaantl vsrpdgslpp eadpstagvg kavpaatanp
      121 dqariqaald acgaavdaev gatiaaadaa ataaqkaaaa pnvnlagasg eefakpkyra
      181 gkfavrlvvn hagpgngfis gpltlpsgvt lwidkgvtly asrdvkaysp naagpycgnt
      241 avsatkagss sncaalitgt nlvnaavvgd gridgrgyae lvtsdakypl mkvdltcsnt
      301 yaayksgtva pdgtacddgg tvvdskstvr nmtwwdlayl gnmvqngttg fgsqsnfrlm
      361 vfnyaknltl yritlnnspn fhvvpsgvdg ltiwnvkvqt ptlaafanpa gngnplyngq
      421 tfnadnvknt dafdpgaask ptsaalstgs tttsaapisf dgylknfvfa ynyvstgddd
      481 ialkgsnnpa pagsglfgid gnrdvradrk wgvviahnhi ywghgisigs etnggvtnvq
      541 vydnsfrdse eglriksdya rggevsnihy anicirdakn allftpyyst kavpaggply
      601 pnfhdislan vviegaagvk lqgfeantgg ygepafplvm sltdvvadtp dsiatiasda
      661 nltlrnvnlp vfpstanrva vngtavhaid pasvldcska fvdfpgidqs npfgstwapa
      721 l
//
LOCUS       WP_175833298            1063 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cenocepacia].
ACCESSION   WP_175833298
VERSION     WP_175833298.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..1063
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113415
     Region          1..1051
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnlgrlsvqq pvlaivlsiv ltiagalayf slavseypdi apptvviqat ypgasaetvs
       61 qtvstpiele vngvedmlym ysqatsdgsl nitvtfkpgt dvdkaqvlvq nrvalatprl
      121 pepvqrsgvs vrkssptqlg tiflyspdqr ydplyvsnya irnvadvlkr iegvgdinal
      181 gareysmriw ldpervasfg lspadliaav rsqntqlagg vvaqapitnq afqpnlifeg
      241 rlkrpedfsd ivvkqgkdgr lvrlkdvarv evgalayatd symlrhptia lqvlqqpgan
      301 avatmaavek kmaelsrdfp kgivynigyn ptafigdsih elvktiyeav vlvvfvvllf
      361 lqgwrpsiip ilsipvslvg tfaamavlgy sinnltlfgl vlavgivvdn aivvvenver
      421 hlaagagprd atlltmkevg galfaitlvl cavfvptsfi pgisgqffrq fgvtiavsta
      481 isfftsvtla palsammlka hagdhdapgp tsriatlfap alrvarrfsn afnrlfqrls
      541 daygrlvrkv vriipamtal yvvliaatgy llvsspkgfi paqdrgylvv lvrmpdgatl
      601 ertsavarki edialsvpgv arvpvfsgvn aatgtnsans aglfpvfqpw perkarglti
      661 dtiaaemrkr latiteasiv vampppvqgl gstggfamrl edrnglgtaa lakatqdlva
      721 aanrtpgmvg vytpysatsp qvhveldrek aemlgvpsqa indavetyfg styindfniv
      781 grtyrvtaqa dlpfrvgasd larlkvrnrd gemvpigsvt riddmlgvdr aprynlypat
      841 eingdtapgl gsgfaiktme tlakqvlppg isfewtdlsy qqttagntgl lvfplcvllv
      901 ylvlaaqygs wslpvsilli vpmcllaasl gvralgqdvn iltqigfivl vglaaknail
      961 ivevarqlea dgaelveavv eacvqrlrpi vmtslafilg vlplvisega gaemrqavga
     1021 avffgmigvt ffgllftpvf yvmvrrlamr ktavaavate avq
//
LOCUS       WP_175833333             374 aa            linear   BCT 11-JAN-2025
DEFINITION  Fic family protein [Burkholderia cenocepacia].
ACCESSION   WP_175833333
VERSION     WP_175833333.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..374
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40854
     Region          23..367
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mmsgdytfiw eaadwpawrf dlpalatpla dvsraqgmla grladvglal rdeaslaalt
       61 ddvvktsaie genlnvasvr ssiarrlgvd igalapvdrh vegvvdmvld atthsaapvt
      121 earlfgwhaa lfptgysgls ritvggwrtd asgpmqvvsg pigrqrvhfe appaarlpdq
      181 igrflawlna pqaepllira glahlwfvtl hpfddgngri aralgdlvla radrspqrfy
      241 slsaqiqrer nayydvlert qrgsldvtew lawflntlgr aidhahttld avlikarfwq
      301 rcagvamner qvkvmnrlld gfegkltttk waalakcsqd talrditelv eqgmlrrsas
      361 ggrstsyelv pfdg
//
LOCUS       WP_175833397             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175833397
VERSION     WP_175833397.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33940
     Region          <27..72
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          104..302
                     /region_name="PBP2_DntR_NahR_LinR_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators that are involved in
                     the catabolism of dinitrotoluene, naphthalene and
                     gamma-hexachlorohexane; contains the type 2 periplasmic
                     binding fold; cd08459"
                     /db_xref="CDD:176148"
     Site            order(110,112..113,117,174,210,277)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176148"
     Site            order(111,114..115,118..119,122..123,125..126,129..130,
                     132..136,138,200,227..231,234..235,238..239,242,256)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 mdnnvtmpad lpdlkllqlf dllydvrsvt rvaeqlgqsq ptvsiwlghl rehlhdplfi
       61 rtpggmaptp qadaligpcr eileslrrft aweiafdpat aqrrfricmt dashvtllpr
      121 llahvraqap gvrleaarid gnteralesg eadlaigyvp wlgggiyqqk lydqdwiclv
      181 nrhhprirgr lgakqyrseg hvaitagtga qlleqalrqa rierdvvlel pgflglgaiv
      241 qttdlittlp rhigetlaqg gdlavhacpi pvegfavrqh wharyhheag nrwlrgvvir
      301 lfgash
//
LOCUS       WP_175833408             310 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia cenocepacia].
ACCESSION   WP_175833408
VERSION     WP_175833408.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..310
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33420
     Region          30..285
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(45,131,133,135..136,165,219,240,243,254,256,285)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mnapirnvqp vivalgnegs gelvpsryav rigdvdvvli sdgvlplpts tmstnvsead
       61 rnawfdgrfl qrdmfdwaln ialvrsadrl ilidsgvgdg feyftragrs vmrvesagid
      121 laaitdivit hmhmdhvggl nvdgvkaklr pdvrihvsaa evafwknpdf sktvmpetvp
      181 palrkaaarf velygenivq fdrtvevaag vsarvtgght pghcvvdias ngekltfagd
      241 aifevnfdnp dwqngfehdp naavdvrlal fneaaetgsl laaahvafps ighvarngdg
      301 frfvpvvwdy
//
LOCUS       WP_175833456             446 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175833456
VERSION     WP_175833456.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..446
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47356
     Region          36..420
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(50..51,54..55,58,90,140..141,143..145,148,168,
                     171..172,175,269,272..273,276..278,281,309,313,364..365,
                     369,373,389,392..393,396..397,400)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtnpngaatp rgmqagppah aqaaapglda lyarlsrrii plilicyffg yldrvnvgfa
       61 klqmatdlhv tdaaygvgag lffvgylllq vpagwlvrri gvkrclagsm ltwgivsvat
      121 lttrdtasfy alrfllgvte asffpaviay fsvwfpshrl akvmaflfla mplgvivggp
      181 lsgwimdath ggfglrgwqw mflieglpai vlgvyllvrv teriddatwl tdtekrmiha
      241 emaqeaagkr trlgaalrep tlwllfatsf lynvgnyglv fwmptmikal gslsnlqigl
      301 vsaipylvas vamvanaqhs vrtgerrwht alpvaiggia llaslgmrth pvlavacltv
      361 gvagimstla mfwslpsril ageaaaggag lvnigaavag fvgptlmgya tgltgstelg
      421 vallaftlfa aaalilsipr rlmvrt
//
LOCUS       WP_175833470             727 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cenocepacia].
ACCESSION   WP_175833470
VERSION     WP_175833470.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..727
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79171
     Region          41..727
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mmqgarvarf grwrpslylg lliaahpaaa fadaapaaga evrrdeaaaa qpaggelkai
       61 avnasrgvad dpsvatvgkm plalreipqs vsvttrerid qqnlfsldev mqqsagvtvq
      121 pyvllttayf vrgfkvdsfe fdgvpvvigd masapqdisv yerveilrga ngllhgsgnp
      181 aatvnlvrkr pqyqfsahat asvgswdryr aeadiggpln aagtvrsrlv aayedrhffy
      241 dhakqdtrsi ysvtevdvtr dtlltfgaqy qtttlvpdms gvpmardgss lglsrstfld
      301 tawgrfnwdt trafasveqk lgagwkakvs geyqsvrsdl kyagsfgaid patgaggrlt
      361 gaayqfssys rsidanvqgp vhafglthdl lfgvtyanss sgqmtapllg dvagtpvnvy
      421 rwnpssvpep gigpyqqsqq ndisqkgvyg lgriklaepl tlvlggrmsr wnqdslgahy
      481 ntghqftpyg gliwdfardw swyasyaevf qpqtksmwgg giltpvkgrt yetgvkgela
      541 ggkldvslaa fridldnnpq vdlahpcagp scyyvnggsv rsqgfefean gritpwwsvw
      601 asytydtmry adnlanagtf apllnprhlf rlwtnydlpw qerrwsiggg vqvqssysaq
      661 angvtmsqgg yalasvrlgy rydkhwsaal nvnnlfdrty ylslsqpgwn nrygeprnvm
      721 ltvrgqf
//
LOCUS       WP_175833584            1057 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cenocepacia].
ACCESSION   WP_175833584
VERSION     WP_175833584.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..1057
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113342
     Region          1..1038
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mdfsrffidr pifavvlsiv ifalglisip mlpageypev vppsvvvrat ypganpkeia
       61 esvaepleea ingvegimym ksvagsdgsl qvvvtflqgv dpdtaavrvq nrvsqalsrl
      121 pdevrqygvt tqkqsptplm yvslyspdns rdslylrnyl tlhvkdelsr ltgigdvgvy
      181 gsgdyamrlw ldpnrlasrg ltasdviaav reqnvqvsag qlgaepspkk ndflvsinvr
      241 grlrtvrefs divlrngddg qvvklsdvar ielgagdytl rsyfndkhsa vvgiflspga
      301 naldvakavy akldelskrf ppgvayrpvw dptvfvresi ravqhtliea vvlvvlvvil
      361 flqtwrasii plvavpvsvv gtfawlyllg ysintltlfg lvlaigivvd daivvvenve
      421 rniaqgltpr daahqamrev sgpivaialv lcavfvpmaf msgvtgqfyk qfavtiaist
      481 visainsltl spalaakllr phgapkdalt raldrafgwl fhpfnrffer ssdryhgvvg
      541 rtlkrrgvvf avyaallaat allfnavpgg fipvqdklyl fagaklpega slartsavte
      601 qmtkialgtd gvemvpafag lnalqgvntp nitnsyvilk pfdqrhrsaa qinadlnarf
      661 aaidggitya lmpppiqglg ngsgyslyle drgglgygel qkaltafqaa vaktpgmsyp
      721 vssyqanipq levkvdrlka kaqgvaltdl fntlqvylgs myvndfnvfg rvyrvmaqad
      781 aghrqtaadi anlrtrnakg emvpigsmvt vgpaygpdpv vryngypaad ligdadpkam
      841 sssqaiaklq qiakdvlppg itlewtdlsy qqvtqsnaai vvfplavmlv flvlaslyes
      901 wtlplavili vpvcmcaalf gvwlsggdnn vfvqvglvvl mglacknail ivefarelei
      961 qgkgvveaal eacklrlrpi vmtsvafiag svplligsga gsevraatgv tvfagmlgvt
     1021 lfglfltpvf yvairklagg tpavwseqhg tlegenr
//
LOCUS       WP_175833604             414 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia cenocepacia].
ACCESSION   WP_175833604
VERSION     WP_175833604.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..414
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44080
     Region          12..414
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mseantqeqp apdtvvvigg gqaagwvlkt lraegfagrl vmiadephlp yerpplskav
       61 lagdagietv rvvrpdefda lnveawqper aasidrtrrv vktesgreie ydrlviatgg
      121 tsrrlpdalv ktphlhylrt ldeaaalgek lrasrrvlvi gggwigleva atarklgvda
      181 tvvegaprlc grsvpqivsd flldlhrsng vdvrlgaale sldaqpddas kvratladgt
      241 tidadfavag iglalnasla sdaglavddg ivvdeygats dpaifacgdv anhhngwlkr
      301 rvrleswana qnqaiaaaka vlgvrapyae ipwfwsdqyd vnlqilgdlp adaqlvvrgd
      361 laarratlff vgdghvrgvi avnnarelkl arkwmnqgra vntealadtt qala
//
LOCUS       WP_175833619             504 aa            linear   BCT 11-JAN-2025
DEFINITION  MDR family MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175833619
VERSION     WP_175833619.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..504
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52960
     Region          38..422
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(39..40,43,74,124..125,127..129,132,152,155..156,159,
                     284,287..288,291..293,296,324,328,381..382,386,390,406,
                     409..410,413..414,417)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mttdtlltpp aadagrrdap tglivaalll vmllsaldqt ivstalptiv gelggldqls
       61 wvvtayllss tvvlplygkl gdlygrkivl qaaivlflag salcgvaqdm tqlivlralq
      121 glgggglmvv tmaaigdlvp pdrraryqgm fggvyglati vgpllggflv ehlswrwift
      181 inlplgllal avigmafrph tahvkhridy mgaaflatal tcvilftseg gsllpwtspq
      241 lwmtlvlglv aiggfiyeer laaepimpld lfrhrtfvlv sligfvvgia lfgsvtfipl
      301 ylqvvkgstp sqagmqllpm mggmlvtsia sgrlisrlgs yrmfpiagtl tggvamalls
      361 tltldtplpt myaymallgi glgmvmpvlt lavqntvefr hmgvatsgat lfrsiggslg
      421 vaafgalfsh glqsrmthal pagtelppal gpaavhqlpd avrdaylhaf agslhvvyls
      481 aatviaiafv lawfvedapl rkhh
//
LOCUS       WP_175833633             319 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Burkholderia cenocepacia].
ACCESSION   WP_175833633
VERSION     WP_175833633.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442595
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..319
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34494
     Region          5..295
                     /region_name="AKR_unchar"
                     /note="uncharacterized aldo-keto reductase (AKR)
                     superfamily protein; cd19103"
                     /db_xref="CDD:381329"
     Site            order(14..16,54,59,85,120..121,147..148,172,201..207,255,
                     270..275,278,281..282)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381329"
     Site            order(54,59,85,120)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381329"
ORIGIN      
        1 mtidnpkppt ialgtwawgd sgeagngyfg ssltraglea vadkahaagf slwdtamvyg
       61 mgrsetvlge vlkrfarsdy rlstkftpqa agtgadpvad mleqslarlg tdyvdlywih
      121 npadvarwtp hlipllesgk ikhvgvsnhn lgeieqadri lreagfrvea iqnhysllyr
      181 dseragildy crdrgipffa ymvleqgals gkygpahplp egsnraqtyn rmlprlkalt
      241 dalaaigrkr gaaapdvata walakgttpi vgvtrpdhvd glarasritl aadeiaelea
      301 ladaadvntr gwwehemqg
//
LOCUS       WP_175833612            1613 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD-glutamate dehydrogenase [Burkholderia cenocepacia].
ACCESSION   WP_175833612
VERSION     WP_175833612.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1613)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1613
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..1613
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=179139
     Region          4..1610
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 meakneevva hllsdvvefa rarlpeatfr ivepflrhyy dfvdaddlqn rsiadlygaa
       61 mahwqtaqkf vpgserlrvy npileqhgwh sdhtvieivn ddmpflvdsv tmavnrlgla
      121 lhsalhpvfr iwrgagggie rvdaggatss dgqsqlasfi hfevdrcgda tlldtlredi
      181 arvlgdvras vedwpkivdi aratikemka reataediea raflewmaad hftflgqrdy
      241 alvsdgtgfg lrgiegsgfg ilreslrtsd apdvtplpqa aaeiitgpwp ifltkansra
      301 tvhrpgyldy vgvklvgadg kvtgerrfig lytstaymvs saeipivrrk canivrragf
      361 lpkghlgksl vtvletyprd elfqadedql ydialgilrl qehqrtrlfv rrdrfdrfvs
      421 clvfvprdky ntdlrrriak llvdayngvn veftpllses aiarihfvvh aepgtmpdvd
      481 treletrlvq vtrrwqddla dalldafgee qgnrllqrya esfpagyrdd ypartavrdi
      541 eliervkdsg qlamnlyrpi eagprafrfk vyragdpial srslpmlehl gvrvdeerpy
      601 riqtqdgaha wihdfglela ddtefdierv kglfedafdr iwsgriendd fnrlvlrahl
      661 sarevtilra yakylrqvgs tfsdayiera ltgnpaiarq lvelfllrfd prigdtrdvq
      721 aerllkaieg aldqvpnlde drilrqflgv inatertnyf ladangepkp ylsfkfnpak
      781 vpglpepkpm feiwvysprv egvhlrggrv argglrwsdr redfrtevlg lmkaqmvknv
      841 vivpvgskgg fvvknpppqs dreawmregi acyqtflrgl ldltdnlagn aivpppdvvr
      901 hdpddpylvv aadkgtatfs dyanaishey gfwlddafas ggsvgydhkk maitargawe
      961 svkrhfremg vdtqatdftv vgvgdmsgdv fgngmllsph irlvaafdhr hvfldpnpdp
     1021 atsfaerqrm falersswad ydtsvisagg gvyprtakti plspavqaal gidahalppt
     1081 elirailqap vdllynggig tyvkaareth aqvgdranda vrvngadlrc kvvgeggnlg
     1141 ctqfgriefa qrggrintda idnsagvdcs dhevnikill glvvsdgemt ekqrnallae
     1201 mtdevgllvl rdnyyqtqal siagryavel ldaearlmrw leragrlnrv ieflptddev
     1261 aerqaaklgl tsperavlla yskmwlydal lesdvpedpl vaamlvdyfp kplqqrfsep
     1321 mrrhplrrei lathltnalv nrvgcafvhr lmeetdakpg divracimar dvfdldavwr
     1381 didaldnrva ddvqarmfvd varlleraal wflrhlqsga vadggvagli arcrdavqri
     1441 apqlpsllpa ddlealserq rvlvdagvds alavrvasgd isaalldiae vaatcnrsle
     1501 lvagvyfslg tllnygwise raanlptpth wdmlaraaal aevarlkrtl atsalaespd
     1561 sttpdtivga wrarreaala ryehlladlr asggaslavl lvvvremavl era
//
LOCUS       WP_175833646            1084 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cenocepacia].
ACCESSION   WP_175833646
VERSION     WP_175833646.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..1084
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115465
     Region          3..1062
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mlkivrlalt rpytfvvlal liliagplaa vrtpidifpd iripvisvvw nyaglqpddm
       61 sgrvityyer tlgttvndvq hiesqsfrgy givkiffqpt vdirtataqv tsisqtvlkq
      121 mppgttppqi lnynastvpv lqialtsntl deqklgdyav nfirpqllsv pgvaiptpyg
      181 gktrevqidl dpqalqskgl saqdvahala qqnqiipagt qkigrfeyni klnnsplsld
      241 alndlpiksv ggttiyirdv ahvrdgyppq gnivrvdghr avlmsilkng sastldiiag
      301 vkaklplveq tlppglklvt mgdqstfvng avsgvaregi iaaaltslmi llflgswrst
      361 liiaasipla vlsaiallaa tgetlnvmtl gglalavgil vddatvtien vnwhleqgkd
      421 trtaivdgak qivmpalvsl lcicivfvpm lmldgisrfl fvpmakavif smvssfvlsr
      481 tfvpmlaqyl lkphasagha sgelaavmdp haghagahdv ppsrnplvrf qraferrfes
      541 vrasyrillg laltrrkpfv vaflcivaas fllapslgrn ffptidsgei alhvrapvgt
      601 rveetaaeld rientirgvi ppaqlremid niglpnsgin ltynnsgtlg pqdgdilisl
      661 srdhaptady vhtlrerlpr aypgttfsfl padivsqiln fgapapvdlq vagpnqqanl
      721 ayahelyrkl rliagvadpr iqqastypqf tvtvdrtrad qlgiteqdvt nsvvatlagt
      781 sqvdptywln prngvsypiv aqtpqyrmtt lsalqnlpvt gangqsqllg glatitrgvg
      841 navvshynie plfdiyattq grdlgavatd iddivkatak dlpkgstvtl rgqvqtmnga
      901 faglllglvg aivliylliv vnfhswadaf vivsalpaal agivwmlftt htplsvpalt
      961 gailcmgvat ansilvvsfa rerlaetgna laaaleagft rfrpvlmtal amiigmapma
     1021 lglgdggeqn aplgravigg lacatiatlf fvpvvfslvh rrdalkhdas rasspsasga
     1081 shvh
//
LOCUS       WP_175833667             306 aa            linear   BCT 11-JAN-2025
DEFINITION  bestrophin family protein [Burkholderia cenocepacia].
ACCESSION   WP_175833667
VERSION     WP_175833667.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..306
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33503
     Region          1..299
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 mivrprehwl rmllvwngsv lptilpqlvl tlaislvavw gggrvlgekv plnptpftli
       61 gltlaifagf rnnasyeryr egrqlwggvl tatrtlvsqa lcygavdrdd asrrafvrtv
      121 vafvytlkhq lrgtdpaadl rglldgptya rvaasrfrpv aivhalreaf aaradagqlt
      181 dtrlwmldar lddlvamvsg ceriastpip fsydvllhrt iyaycvllpf glvdsigaat
      241 pfvtvfvayt lialdaiaha iaepfgdgpn hlaldamtrq iertllelnr eplpaevtpg
      301 psyrlt
//
LOCUS       WP_175833687             322 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175833687
VERSION     WP_175833687.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..322
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35728
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,220,
                     222..225,232..233,236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdmlenmrlf vrvveagsft avakeidatt aqvsravsnl eahvqtrllh rttrhlglte
       61 sgeryferak silaeldyan aearnallrp sgkmrihamt glgqshvvss ivryqednpd
      121 vsveltlaqr mpnlveegyd vsivtasqlp dsgyvaqtcg tscsvlvasr eylaqhgtpq
      181 tpdelpnhvc lrldtpaspa gewrlersdg eeavyelqpa pfqvnvpdal cvavragrgi
      241 acvalytvld diregrlirv lpeyrlqtvs vyavyatrry ldakirtfld hlrttltpal
      301 endlreldrl ttehvpssrq ra
//
LOCUS       WP_175833726             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cenocepacia].
ACCESSION   WP_175833726
VERSION     WP_175833726.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21398
     Region          2..205
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mlfiksvvmg lsiavpvgpi gmlciqrsls rgfqagfatg igaacadaiy gllgalgvag
       61 ivtafpmltv glkigggafl vwlawtiarq apaapagqrd lprstvlrdf lttfgltlsn
      121 pmtivsfvgi faalgplpga regamwatva wmvagvfigs atwwlclssa taalrtklsf
      181 afmhalsrgs aavvavfgai qlvagvrgli
//
LOCUS       WP_175833728             190 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            cenocepacia].
ACCESSION   WP_175833728
VERSION     WP_175833728.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..190
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=20098
     Region          1..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          82..179
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam13305"
                     /db_xref="CDD:463838"
ORIGIN      
        1 maragitldk laeagaqlad etgfeqltga alarhfdvkl aslyshipsf ddlksrialf
       61 alqeladrat dalagrtgkd alaalanvyr dyarahpgrf aaarhpvspe raaasaggql
      121 vrmtaavlrg ydlpdtehah airllggffm gyvtlesagg fshsapdsda swsrsldald
      181 vmlrhwpspa
//
LOCUS       WP_175833779             727 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia cenocepacia].
ACCESSION   WP_175833779
VERSION     WP_175833779.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..727
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79051
     Region          39..722
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mkpqpaierp sieparwsaw ldplgnaard waatdgliwl hlaktvlaal lamgiamrle
       61 msqprtamtt vfvlmqplsg mvfaksfyrv lgtaaglvga lalgglfaqq pelymagitl
      121 wiggcialav rnrhfrwygf vlagytaali glpavmtpqt lfqsaltraa evalgiacsg
      181 avsalilpls sakalmrsls arhatfaaft agalagdvar gdferrfadf vddivgfean
      241 rafasfedph irarsrrlar lnsefmnact rlhalhqlvk rlrasqsdav ldalaphvda
      301 lalrfaalrd erqrgiapat gallelrrfh galpkaaras rrtledhaag glldfdtaie
      361 llyrfigeyl gyvdtyasld qddhafersv thyavktnaf fvgfaflrtv vavgamsafw
      421 iasewpsgsl aviataiaca lsstsprapk fvaqmgvgaa fatavgylfl cyvypnidgf
      481 pllcaalapv lglgaflamr pglsgygigf avffcllagp dntiaytpev linnglavvv
      541 amlacslvfa vvfpthmpwl tgriahdlrr qvtlacegap dglaqrfqss thdlmaqlrt
      601 llvrrtrqhr dalrwmlstl evghavidlr delhafcask ppqtlrwtgs idavlnelpr
      661 ffddptpsrh artlksvnla iraaqhtlqa wyavpdvrrs mqrivgclhf mrsalldkda
      721 pfnrhrh
//
LOCUS       WP_175833785             382 aa            linear   BCT 11-JAN-2025
DEFINITION  epoxide hydrolase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175833785
VERSION     WP_175833785.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..382
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42240
     Region          4..108
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          73..>199
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mhaepfdiai pdqalddlrr rvrdtrppnl tpaepwqqgv dgtwlrelaa ywadgfdwra
       61 aeralnrlpq fiadvggrrv hfvhrrgtgp kpyplvvthg wpgsafefha lidrlcdpaa
      121 fggdpddafd ivapslpgfl fspapaapgt salqvadcwa almaglgypr fgaqggdlga
      181 gvsvalgarh egvvdgihln ylpgsydppi daarpltdde qaflkqrgew aaleggyayv
      241 hmtkpqtlav alndsplgla awigekfraw sdcdgdvarr fshdtlltgi slywftscig
      301 ssmqmywenr lqpmrfapgq rlavpvgfar fpkeisrppr swlervfdvv qwtdmpsggh
      361 faameepdll addirrffrr fr
//
LOCUS       WP_175833786             321 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175833786
VERSION     WP_175833786.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..321
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35182
     Region          2..317
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhrigflisd gfqimalaaq svfeyanmgm dapfyamdny svdggdvrss lglpvatral
       61 rgrlgvdtwi vagvndplaa papagvvayl rrangrarri agictgafvl aeagllaqrr
      121 atthwafgrd mqrhypeirv eddrifivdg piwtsagmta gldlalamve kdlgadaars
      181 varklvmhqr raggqsqhse mldlapksdr iqnaldyarr nlgraltvea laeavhlspr
      241 qfsrvftlet gqspakaier lrleaarlmi eqsrhpldvi akengfrdrr hmreafvrgf
      301 gvppqalrrd arteadaret g
//
LOCUS       WP_175833789             551 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175833789
VERSION     WP_175833789.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..551
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=56694
     Region          15..270
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
     Region          300..548
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mqnhevsadd appkaqrgiq svevggrlld alarrrkplg lselaaaadl staqahtylv
       61 sltrlalvkr daltgnyepg plslrlglms ierqpayrat lphavrlaet vglsvalsvp
      121 gvlgptivri ehggyplhvn lhvgsvmsld ttatgrvfra fgdaaqldam aasqagagdt
      181 lagaesepaa pdadaqpvel dairargier sidrpspgvs gmcvpvldph grlqlaltvi
      241 gstgsidvdw dgpiaaalrd aarqataslg tahaepapap avapgvarvp paladdaktq
      301 rginaldstg dlllalvsag ralplrdlat aagmpaakaf phlvslqkig llsrddagcf
      361 dggplaqalg liamqrvspt rdaeaeival agatdmsvaa atlgplgptv irleesarpq
      421 hvslqvgtvm slvntaigri fasgmsddvl adllanepvr lagahaapdd aafrsrlati
      481 radeldfafd apvpgigtia apvfdhtgsi rlviaiigss rgfprgpdse laqtlraatr
      541 rlswrfgwig r
//
LOCUS       WP_175833816             288 aa            linear   BCT 11-JAN-2025
DEFINITION  MOSC domain-containing protein [Burkholderia cenocepacia].
ACCESSION   WP_175833816
VERSION     WP_175833816.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..288
                     /product="MOSC domain-containing protein"
                     /EC_number="1.7.-.-"
                     /GO_function="GO:0016661 - oxidoreductase activity, acting
                     on other nitrogenous compounds as donors [Evidence IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=31075
     Region          1..281
                     /region_name="YcbX"
                     /note="N-hydroxylaminopurine reductase subunit YcbX,
                     contains MOSC domain [Nucleotide transport and metabolism,
                     Defense mechanisms]; COG3217"
                     /db_xref="CDD:442450"
ORIGIN      
        1 mpaitelfvy pikscagial traqlletgl aydrhwlitd phgqmltqra hprlalirpt
       61 ldgdalvlna pgmpairtpl dgdatpatpk maatvwrdtv daidtgadta awlteflgvp
      121 tklarfgpda rrscnrkwtg eidthtqfad gypllvigqs slddlnarla akgapaipmn
      181 rfrpnivvsd ldayeedfve hldvdgdtpv rlrlvklctr cpmptidqat gapdpawphe
      241 ptdtmqtyra npdydgaltf ginaivvaga gawlevgqpv eaeigfgd
//
LOCUS       WP_175833802             545 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 32 protein [Burkholderia cenocepacia].
ACCESSION   WP_175833802
VERSION     WP_175833802.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 545)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..545
                     /product="glycoside hydrolase family 32 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=59199
     Region          38..533
                     /region_name="SacC"
                     /note="Sucrose-6-phosphate hydrolase SacC, GH32 family
                     [Carbohydrate transport and metabolism]; COG1621"
                     /db_xref="CDD:441228"
ORIGIN      
        1 mnstsfrffv rlvrllfacl actqavaapc happdngtpq wrpalhytpq rnwmndpngl
       61 vyangryhlf yqynplgndw gnmswghats tdlvhwreqp vamranatee ifsgsivadt
      121 lntsglgtpg htplvalyts vykpgsghap giqaqslays ldqgttwqpy ahnpvltldp
      181 eskefrdpkv swyaaggywl mttvvadahv vklyrsddli rwsflsdftl pdvphagalw
      241 empdliplpl dgdprrikwv mivnvnpwsi aggsgamyfv gnfdgrtfvp drvapagsdp
      301 aqfrwvdhga dfyaagtfsg apgarpvaia wmsnwdyaak vpttpwrgat tlprelalkt
      361 idgeptliva paaafdawad grpavhegdl tvdsatrals aatrgvvqri tvtispqraa
      421 raglivrrsa dgsigtrivy dtakrtltld raqsgeanfa gtfsrehivd lplehgqlrl
      481 eivvdrgsve vfanggrval tdlifpplda drvavfaeqg ratfagltvt qlktgddtrg
      541 acasr
//
LOCUS       WP_175833854             282 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia cenocepacia].
ACCESSION   WP_175833854
VERSION     WP_175833854.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..282
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30160
     Region          52..146
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 meanrpneaq salwngpsgr awvdaqapld rmfepfetll aeaaaasfat rvldvgcgtg
       61 avtlaiarrl gasaqctgid isarmidaar araerggvpa rfvcadvqth afepasvdli
      121 vsrlgvmffd dpvrafanlr qaarpgtpmr fvawrgaadn pfmttaeraa apllpnlpvr
      181 qpgapgqfaf gdrqriasvl sdsgwadvai epvdrvcvlp esalddyiar lgpvglalle
      241 tdeatrrrvi dtiraafery vhgaevrfea acwlvtarap fa
//
LOCUS       WP_175833969             262 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cenocepacia].
ACCESSION   WP_175833969
VERSION     WP_175833969.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..262
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28478
     Region          8..262
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mstpdiaspa pgrigvralt ielgppharf aaldtldvdi apgefvcvlg psgcgkstll
       61 galaghvaat hgeimvdger vdrphpdrgl vfqqhtlfpw krvidnvafg lkmkgvpaqe
      121 rrreaaelle lvglggfgah ypaqlsggmq qrveiarvli nrprvllmde pfgaldaqtr
      181 rmmqtllldi wsrigttvlf vthdieealf lgdrilmlsp rparivadir vplarprtdn
      241 sttepafvdi krrclallrd aa
//
LOCUS       WP_175834028             279 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia cenocepacia].
ACCESSION   WP_175834028
VERSION     WP_175834028.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..279
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=29098
     Region          9..247
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mrarpivavt adrilrgahp nhtagekyla avvdgagala fvlpalgarq padaivaaid
       61 gllltgsysn vephhyggaa sapdtlhdpa rdatalplir aaidagvpvl aicrgmqeln
      121 vayggtlhqr lhattgfddh rerpadpler qygpahvvql apggllqrva rgaheatvns
      181 lhdqgierlg aglaveasap dglveavsvr garafalgvq whpewryaeq plsrdifaaf
      241 gaacrarmth rmhaaggatp spaasdidid qrgrscnpn
//
LOCUS       WP_175834047             319 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cenocepacia].
ACCESSION   WP_175834047
VERSION     WP_175834047.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..319
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34349
     Region          83..292
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mplnpkiaqv ldmierakrp syhhqtpqqa raayeksapi ldvapapmhs veecvvptrd
       61 grtigarlyl pvapslaepl palvyyhggg ftvgsvdthd alcrmfahda qcavlsvgyr
      121 lapehrfpta vndaddalqw lhreaatfgi daarlavggd saggtlatvc avlardagir
      181 lalqlliypg vtghqdtesh arlangyllt qdtiqwfftq yvrdradrdd wrfapldgtr
      241 dapsfagvap awiataeydp lsdegaayad klrvagnavt lvcypgmihe ffkmggyvpe
      301 vraahadava alkaafdev
//
LOCUS       WP_175834109             229 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cenocepacia].
ACCESSION   WP_175834109
VERSION     WP_175834109.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 229)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..229
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25006
     Region          1..229
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 mflqgygpli lagtwqtvkl avlslalsfl lgllgagakl srhrvtngvg tvyttlirgv
       61 pdlvlmlllf yslqiwlnma tdalgwdqid idpflagvlv lgfiygayft etfrgaflsv
      121 prgqleagsa ygmtnwqvft rimfpqmmrf alpgignnwq vlvkstalvs iigladvvka
      181 sqdagkgtlr fffftliaga vylaittisn fvlmwlekry stgvrkadl
//
LOCUS       WP_175834112             392 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia cenocepacia].
ACCESSION   WP_175834112
VERSION     WP_175834112.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..392
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44575
     Region          7..390
                     /region_name="COG3146"
                     /note="Predicted N-acyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:442380"
ORIGIN      
        1 mkheridyrt gilsspaevp adewnallar daqptpflrh efldalhvar cavddtgwsp
       61 hfvtltdant grlaaaapvy akqhsygeyv fdwawadayq rnnlpyypkl lcavpftpvq
      121 gtrllaaddd arrrlaatll afaeqsdvss lhvlfptgde arllesmgmm lregvqfhwl
      181 ndgyrhfddf lgtleqkkrk niraerrkvh dagvtfrrlt gdqitdadwr ffsrcyrqty
      241 rehysspyln ldffrtigat mpenlllvia eadgqpiasa lavyrrgehg ggtlygrywg
      301 aiehvpclhf etayyqllef cieagldtfe ggaqgehkla rgflptvths ahwlahpafs
      361 davarflere tehihayvde lrehdpfrrs ag
//
LOCUS       WP_175834157             535 aa            linear   BCT 11-JAN-2025
DEFINITION  multicopper oxidase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175834157
VERSION     WP_175834157.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..535
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=58081
     Region          88..535
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mrrrtflsra igvaaaslfa rtasaqhagh agmagmdsmd dmpgmsgmsg msahaqhgqp
       61 apaalaaada lpagaplatl rtlanesrep gtfratlvaq pvarpllrga rpttfwqfgt
      121 gtqgpvvgpl idvregdtve irfvnklpqp stihwhglpv ppdqdgnpsd pvapgasrvy
      181 rftlpkgsag tywyhphphm mtaeqvfrgl agpfvvraad dplagwperh lfvsdlklar
      241 dgmiapndmm dwmngregqf vlvngarrpr idvasderwr vwnacsaryl riafddgrvf
      301 ehagtdgglf daprrvtsll iapgeraell vrsgdrasra vlqaaeydrr kmamshddgh
      361 gslppdpala ladvafapae aralpatlra vpplgepvah ktvafgeemd mdammkgaah
      421 grpagmrfti ngdtyaphra tltsrrgdve rweirnttdm dhpfhlhgtq fqviertsag
      481 srtsepfraw rdtvnvrsge tvsllvtqdm pgermfhchi lehedlgmmg tlkvv
//
LOCUS       WP_175834160             362 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia cenocepacia].
ACCESSION   WP_175834160
VERSION     WP_175834160.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..362
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40190
     Region          5..333
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mangnptqri lviridflgd mlcttaflra lkarwpgael hvvanrynaa alagnpdvht
       61 ihtyvysrqc erndrpgrmr affdrlrlvr rlrrlrfdlv ivpnggmhrs smqfarqlra
      121 kdcrwhdaet efddrkpehv aqrpmcheal sgfrlvpelg cadldrlels vhpdrarqea
      181 whcllgartk prvglfvsnk averrwpadr wrdlgerlap vadvivfrdp aigqaieddg
      241 wrdvnarhva pssvadlvaa aslldaivsa dsapvhlasa lgvpvaalfe drpekylrwh
      301 pigvphvilr agrtvdaigv daveravrhl lsqagqrdea paaearvqpa aataptiati
      361 as
//
LOCUS       WP_175834187             895 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            cenocepacia].
ACCESSION   WP_175834187
VERSION     WP_175834187.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 895)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 895)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..895
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..895
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=97909
     Region          15..827
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnsqalrsal lagpvqherl ikldtplgpd vllpqrvtgr srlgrhfeft vdtvsvsdgl
       61 elkkliaqpv tlwiqqadqs yaphhgyvha arrlgsdsgv thhqivfasf lhflkfrrdq
      121 riwqdrsadd iiadvlnqhp qakgrftfkl yqplpsrsfc mqyeddwnfv hrlmesegly
      181 gfweqdsdgk shrlvivdri dalpalsprt vrfhhagtgd eadtlvqftg trtlrsvart
      241 trtfdykqpp tasnpkatht ptianqgdlp qqlevyeytg aytypeqsrg dhlskiwmee
      301 qeshakrfhg vggvrrmdag rvfefaehpe hdkddagqre favietawvi vnnlpvadep
      361 avfphslqae igsimqaadt drsrvrhpdg segffqirie aqrttvpfrs pfehakppmh
      421 lqsaivvapq geevhtdeln rvkvrfhwdr lndgdekasc wlratasdsg ngygavhphr
      481 sgeevlvdfl ggdcdrpiiv gkvyngatsp qwhsngilsg yrskeyagag ynqlvlddat
      541 sqnrvhlyss qanthlhlgy lidhtgnnrg sylgsgfdlr sdaygavran rglyvtthpk
      601 qaasqpldvd etreqlvraq glidamsqvs aqhqgesldp ghtalkqfsd atqnsvsgst
      661 sggrtagggt gnanafkepv mlfgspagig mstqqsaqfs adqhinlvsg qsthvaagks
      721 liasvldris lfaqnagmkl fagkgkvevq aqadnielta qkalkliavt qsiegaaake
      781 illtsggayi riadgnievh apgkidikga qhafsgpthl sqtmptlpns ngnydqafia
      841 hwagtdipva ntryqmfsng kllsegvtna agetgltqsh vphdvvvkfl gksng
//
LOCUS       WP_175834194             324 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cenocepacia].
ACCESSION   WP_175834194
VERSION     WP_175834194.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..324
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35853
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdriqamevf trvvdansft raadtlampr asvttiiqnl eallgvrlmh rttrrlsltp
       61 egaayyehcm kiiaeiaead asfqagnrkp sgvlrvhmps slgrrvvlps lsifrqrypd
      121 itlelglsdr yvdpveegid cmirvgpled ssmvarrigm lkrvtcaspd ylarhgepne
      181 iadlvehhav nfrsshgara ipwvfmidgk pfevrmngsv tvndsdayvt cglegfgmiq
      241 ptlfmvlphl ldgslvevlp dsnpkpkpis ivyphnrhls qkvrvfadwi aevfestpal
      301 eggenwrgkl rvqtpdaqrg avva
//
LOCUS       WP_175834225             307 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase, partial [Burkholderia cenocepacia].
ACCESSION   WP_175834225
VERSION     WP_175834225.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 307)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         <1..307
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
     Region          <1..307
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 vcgsglkavm laanaiiagd aeivvaggqe nmsasphvlp gsrdgfrmgd aklvdtmivd
       61 glwdvynqyh mgitaenvak eygitreeqd afaalsqnka eaaqkagrfn deivpvsipq
      121 rkgeplqfat defvrhgvta eslaglkpaf skdgsvtaan asglndgaaa vlvmsaqkaa
      181 algltplari kayanagvdp svmgmgpvpa srraleragw tpgdldlmei neafaaqala
      241 vhkqmgwdts kvnvnggaia ighpigasgc rilvtllhem akrdakrgla slcigggmgv
      301 alaverv
//
LOCUS       WP_175834349             743 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia cenocepacia].
ACCESSION   WP_175834349
VERSION     WP_175834349.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..743
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=81851
     Region          67..715
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mnrfvpflrd awlrcrarvt plaaacrmrv ralgagmlhr lrhptrrgva ltlaaipvlg
       61 lllllafvpf tpsigdirka ridrparvls adgqliaefr pvnrewvplk qisphmvdal
      121 iatedhrfya hhgidwrrtl aaglhtfsgd rqggstitqq larnlypdev graptltrkv
      181 kelitafkie avyskdeile tylntvpfly naygvemaar tyfgksadql dltesatlvg
      241 mlkgnsyynp vlnperavqr rnvvlgrmaq mgmlspqqfa klqrqplrvd fepqtsqpgl
      301 aphfavqlrk wliawadrnn ydlysdglvv rttldarlqd matqaltrqt erlqaiadga
      361 wrgpsgcglr ndlfrgfmrq tpeyrqardt gladvatlkq lganrdfvra lcerktqvqa
      421 gfvaidprng airawvgspd fgsepfdhvv qarrqpgstf kpfvygaafa dgmrpgdtfv
      481 dgpvaipidg ravwrptdae pptgapmtlr dglalsrnri taqvmqrega akvaqlaram
      541 gvrdspldav pslalgtspv tlkemvsayg tianrgvyva pqmitriedr dgkvlaafgs
      601 apperalpap aaltlvdamr gvvdygtgad irsrygirid vagktgttqd ntdgwfilmh
      661 pqlvagawvg fddgsvtlls dywgagahsa lpivgsfyda alraraidph vqfspdfrpr
      721 sapapkrrap qhsglfdwlr ffr
//
LOCUS       WP_175834357             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cenocepacia].
ACCESSION   WP_175834357
VERSION     WP_175834357.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21951
     Region          1..192
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mhettlllfa avafvgiatp gptvllaltn gsrygvrraa fgfagamlsd fvlivavalg
       61 lgallmasaf wfsvvkwlga aylayvgirl lmskgtldva aaqrgtasgr nasifaksfl
      121 tavtnpkgyl ffsaflpqfl dplaplapqy valavtfall dgavmfgyal lgaravrllk
      181 rsgalwlert cgamllalag slalyrrhaa
//
LOCUS       WP_175834363             666 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Burkholderia cenocepacia].
ACCESSION   WP_175834363
VERSION     WP_175834363.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..666
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70760
     Region          1..460
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          598..662
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(620,629..631,638)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            630
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mfdkilianr geiacrvaat ckrlgiasva vysdadanak hvaacdeavh iggsaaadsy
       61 lrieriieaa ratgaqaihp gygflsened faqaceaagi vfigppvdai aamgskaaak
      121 almhaaavpl vpgyhgddqd aanlhreadq igypvllkas aggggkgmrv versedfpaa
      181 lascqreaas sfgndrvlie kyltrprhve vqvfgdthgn tvylfdrdcs vqrrhqkvle
      241 eapapglhed vrqamgeaav aaaravgyvg agtvefimtg eafyfmemnt rlqvehpvte
      301 mvtgldlvew qlrvaagepl plkqeelrvq ghalearlya enpargflps tgtlkhlrlp
      361 agvefdvgas vrvdsgvreg daitpfydpm iaklivhgad raealglmlr alracevvgl
      421 htnaaflqri vacepfaiad ldtgliernh dalfapqqpp ratlalacaa llarergaav
      481 qenaspwssl pdwrlnggyr rtlewhatdr eadvtvtyed dgagtriaig daaaqpfawt
      541 rgatpldfdv tlggvrrsgr vyadgdtfhv ftqgaaetfe wrnllahagd aeqgggrlta
      601 pmpgkviavl vepgqkveag tplivmeamk mehtigapsa gvvaevlygv gdqvadgaql
      661 lmmaeg
//
LOCUS       WP_175834218             260 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Burkholderia cenocepacia].
ACCESSION   WP_175834218
VERSION     WP_175834218.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..260
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28489
     Region          12..193
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(15,17,98)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(42,97..98)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            96..98
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 msklhassth lvlipsynpg akvdttvrna raqwnpvwvv vdgstdgsae rlqamaerdp
       61 glrvivlpen rgkgtavlag ldaaaasgft hvltmdsdgq hpadlipafm aasqaapdam
      121 vlgvpkfdas apqlrvqgrr lsnawadlet lwagigdsly gfrvypvapl aaimrrqpwm
      181 rgfdfdpeaa vrlcwagvrp iridapvryf drheggvshf hygrdnalla wmhlrlftgf
      241 amrlpmlvar rltrrrdqta
//
LOCUS       WP_175834372             208 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: trimeric intracellular cation channel family protein
            [Burkholderia cepacia complex].
ACCESSION   WP_175834372
VERSION     WP_175834372.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..208
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=20908
     Region          6..204
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mkrieqvvla adlagtavfa ieganaaiga gldlfgvmvl slvvalgggv irdlligarp
       61 psavsdwryp alafaaglfa fvfharvasf spsllttlda aglalfavag avkalefrvh
      121 pfiatlmgav tgcgggvvrd vllaripvvl vtdiyasaal lgavvvvscr rlgcppvvaa
      181 vlggvacfal rmaavrfgwq lpkiaaga
//
LOCUS       WP_175834399             421 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SGNH/GDSL hydrolase family protein [Burkholderia
            cepacia complex].
ACCESSION   WP_175834399
VERSION     WP_175834399.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..421
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=43627
     Region          205..412
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(212,252,290,393,396)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(212,393,396)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(212,252,290)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 msfrssfaaa vlgaavlvap lavsaapagw vaawatalqp ipdlaapppl yrapdvagrt
       61 vrqivyptvs graarirvsn aygraplvve aaslaragdg aalaggaavp vrfggkasvt
      121 lapgqelesd pvaigvtaaq pyaislqmgp dqrmtvwhrv snqfnyvsaq gdhvsdpgaa
      181 dfrtrftqya wvtelaveag sahasvaaig dsitdglrss vnrnrrwpda larrltasga
      241 dsigvvnlgi sgnrllsdsa cygtslasrf erdalsrsgv kaaivligin dinfaamppr
      301 agldcdhpht qvtaaslidg yrrlieaahr egvkvfgatl tpaalpagre airlevnrwi
      361 rsgggfdgvv dfdavlrdpa rpsvlqrryd sgdgihpsda gytamagavp verlqaavgg
      421 k
//
LOCUS       WP_175834405             232 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Burkholderia
            cepacia complex].
ACCESSION   WP_175834405
VERSION     WP_175834405.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 232)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..232
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24901
     Region          6..228
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mnaappplve lshvaksyrr gnqivpvltd itldigegdf valmgpsgsg kstllnlvag
       61 idrpdsgelr vggldisqla eaqlaewraa nvgfifqfyn lmpvltafen velplmlthl
      121 srrerrerve lvldmvnlgd rtshypsels ggqqqrvaia ralitdpvli vadeptgdld
      181 rasatdvlam lqrmnaelgk tiimvthdah aagaarslvh lekgelidgh ag
//
LOCUS       WP_175834407             445 aa            linear   BCT 11-JAN-2025
DEFINITION  carotenoid oxygenase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175834407
VERSION     WP_175834407.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Poliakov,E., Uppal,S., Rogozin,I.B., Gentleman,S. and Redmond,T.M.
  TITLE     Evolutionary aspects and enzymology of metazoan carotenoid cleavage
            oxygenases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1865 (11), 158665 (2020)
   PUBMED   32061750
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Sui,X., Kiser,P.D., Lintig,Jv. and Palczewski,K.
  TITLE     Structural basis of carotenoid cleavage: from bacteria to mammals
  JOURNAL   Arch Biochem Biophys 539 (2), 203-213 (2013)
   PUBMED   23827316
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Kloer,D.P. and Schulz,G.E.
  TITLE     Structural and biological aspects of carotenoid cleavage
  JOURNAL   Cell Mol Life Sci 63 (19-20), 2291-2303 (2006)
   PUBMED   16909205
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Wyss,A.
  TITLE     Carotene oxygenases: a new family of double bond cleavage enzymes
  JOURNAL   J Nutr 134 (1), 246S-250S (2004)
   PUBMED   14704328
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..445
                     /product="carotenoid oxygenase family protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006720 - isoprenoid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48668
     Region          8..439
                     /region_name="COG3670"
                     /note="Carotenoid cleavage dioxygenase or a related enzyme
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]"
                     /db_xref="CDD:442887"
ORIGIN      
        1 mtvfdlnrga lapvadevdi velrvtgaip reldgtllrn gpnppggrfe gndmlswwpe
       61 aamlhaiafe ngraagyrnr wartqrwaav hapgqaphlp dtnpnvnvlq hagellalae
      121 ggaplaitaa ldsfgvparh agfdgamtah pkvdpvtgel ilfradwrap wlrygvvdaq
      181 gvpcvdleie lgapsmmhdl aitetrslll dlnvgydfsl lqqghrmplr whddrparig
      241 vlprhggdvr wfgvepcfiq hvvnaydcda sclvldavry psflrldart grfadnpvge
      301 lwryvidtan glidegplad ggielprine srtgrgyryl yaveqpnnae mrgvmrfdha
      361 rgttmhyavp agdqngepvf vprpggaded dgwllvmvyr aatdtsdvvi ldaraidagp
      421 vatvhlprrv pagfhgawvp rerra
//
LOCUS       WP_175834406             388 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cenocepacia].
ACCESSION   WP_175834406
VERSION     WP_175834406.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..388
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41284
     Region          19..227
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          143..387
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 maipltyiar nlwtrrltta ltaggmalvi fvfatvqmld agltktlvst gepdnavvir
       61 kgaeteiqss idhqqanale mhpavalgpd grplvskeav vlislvktst gkpsnvvirg
      121 vspaglalrp hvklvagrmf apgsseivvg saiakgfsgt qlgdrlhfaq rdwtivgifd
      181 aggsgfdsei wgdvdqlmqs frrtsyssmv lripsadgfa rfkadidvdp rltdeakreq
      241 tfygdqskal stfinilgit lstifsiaam igamitmyas vanrvaeigt lralgfkris
      301 vlaaflleal llgfvggvag lacaslmqft sfsttnfqtf sdlsfrfvlt paivvktllf
      361 slvmglvggf lpamraarlk ivdalraq
//
LOCUS       WP_175834416             230 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia cenocepacia].
ACCESSION   WP_175834416
VERSION     WP_175834416.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..230
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24263
     Region          1..227
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mtaqwidipt gndsfggyla lpkrgkgpav iiiqeifgvn ahiravadqy aadgfvalap
       61 dvfwrtqprv eltyegadrd kgielmkktd vglavadiga aadalrarpe vagklaaigy
      121 cfggqlayra aatgkldaav syygggiqna ldlagqvtqp ilfhyaendh gipltavdqv
      181 kaafaghsha sfhvypgaeh gfnctdrasy nqraaalahg rtltflaehl
//
LOCUS       WP_175834478             376 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia anthina].
ACCESSION   WP_175834478
VERSION     WP_175834478.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..376
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40897
     Region          183..376
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 migfsvsrww smvtkeflqi rrdrvtlgmv avlpivqlal fgfainsdpk hlptivladd
       61 tsefsrsiva gmrntgyfdv rggqfseraa rdalqkgtvq fvvsvphdfs rrlvrnehpd
      121 ilveadatdp aatgnaiaaf ntmvrtvlnk dlkgplaiaa ppdvfsarvh kiynpagitq
      181 yniipglmgv ilsmtmvmmt slaltrerer gtienilasp atslevicgk ivpyiligls
      241 qctiillaar fvfsvpfegn pvtvyclasl lilanlmvgi aissvarnql qamqmtffyf
      301 lpsvllsgfm fpfagmpgwa rlvgnglplt yfnrairgvl lkgsgwseiw pdaatmvafa
      361 lvamaiglla yrttld
//
LOCUS       WP_175834513             203 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia anthina].
ACCESSION   WP_175834513
VERSION     WP_175834513.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..203
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21132
     Region          86..195
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(91..92,125..126,129,133..134,137,185,189)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 magaipsila llvsatavgs afaqappahr dirdlkatvl dvkgfssgln stvsdlsaka
       61 sglaarhdgl svredkatvr vsmlgdvlfd fdkasirssa eptlddilrl atsvpsgtiv
      121 ieghtdskgs aaynkmlsfr ranavagwlt shgmqkarls vkglgssrpv apntlkngad
      181 npdgralnrr vefvlpndak rtk
//
LOCUS       WP_175834525             282 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia anthina].
ACCESSION   WP_175834525
VERSION     WP_175834525.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..282
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28670
     Region          20..261
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mthfaltegv lvsslhglal ldlvgiaval llggmvkgit gigvplvamp ilsqflpirh
       61 avlllsmpii lgnipqaleg gevlatarki aapivgtvig nvvgvaills lnaghaqaas
      121 gallivaatl mlsapklnlp pawqkpvgfa lgfgaalmes iasvpgplla tylissgatg
      181 rvftkqiaii lvvsivtlit tfggathasg adlavsalas lpaiagmwlv rplrdrmspr
      241 ifrtvvllfv lvaasqmiwk sgvfrhaapp aaqmdnghag kq
//
LOCUS       WP_175834565             288 aa            linear   BCT 11-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Burkholderia
            anthina].
ACCESSION   WP_175834565
VERSION     WP_175834565.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..288
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=30067
     Region          182..>258
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mslsllpcat iwlalfaaaa lawhrplhgp sialaalgya galafgklsp vvlaplallv
       61 aagwgvapgr pravrlvahl afaalaials lhlipgfhnp rvieptrftp davpftmyln
      121 fdkplvglwl lwvlpwvapd vplsrvlrtg avaavgtaaa clagallfgm vgwapkwpas
      181 gwmwlvnnvl lvtlaeealf rgyiqggltr mlgrfawgpw aalaiaavlf gaahaaggwp
      241 wivlgtvagv gyglawrrgg llaaalahag lnvihfglft ypmlaaar
//
LOCUS       WP_175834484             368 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia anthina].
ACCESSION   WP_175834484
VERSION     WP_175834484.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..368
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39249
     Region          4..336
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(24,26,57,99,228,290,310,312..314)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(24,26,57,99,101,108,176,179,181,228,235,290,310,
                     312..313)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(26,101,176,179,181,313)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            181
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mtqplfepar igafampnri vmapmtrsra dehdapgdlh iayyaqraga glivaegtyp
       61 hadgkgycrt pgiatqyqid awrrvtdavh rengrivlql mhvgrvasrl nkapdadtva
      121 psalrangti hadgsgpvpl dtpraltrae ipdvidgfrq aainaraagf dgvelhassg
      181 ylpmqfllac snrrtddygg trerrarfti ealeamagai gaqrvglric pgnpyndmhd
      241 ddpastygtl ldavsplgla ylhvsrspdr rldafalarr hfrgpliand gfdahsaanv
      301 laaghadavs farhfianpd lvarlrdgap laafdrttly tpgargftdy pplgvadagg
      361 psiqrsas
//
LOCUS       WP_175834716             316 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175834716
VERSION     WP_175834716.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..316
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34275
     Region          12..69
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..300
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(108,112,151,165,167,232,249,279)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(109..110,114..115,117..118,121,125,127..133,194,
                     226..230,237..238,241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mnsqntqtlw phihsltvla vtgsftaaaq rlgiskaams qriadleaaa gvplvrrttr
       61 svrlteagqt lvdstreaye tiemnfarvk dlageprglv rvtmpvalgr qqivplfpaf
      121 iaqypgvrie lelsdrlfsl sqegfdlair htttapqthv awklcetrsl lvashaylar
      181 rgtpehpnal aehdclcylr gneptawsfe prdrrrarvs vpvrgcfaan nseamreaal
      241 gglgiallpd fsaqrdidag hlvpllgawr psgafgdsif airpyspvvp savrvlveyl
      301 rgklsggfsp gmaasr
//
LOCUS       WP_175834643            1616 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD-glutamate dehydrogenase [Burkholderia anthina].
ACCESSION   WP_175834643
VERSION     WP_175834643.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1616)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1616
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..1616
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=179513
     Region          4..1613
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 meakneevva hllsdvvefa rgrlpeatfr ivepflrhyy dfvdaddlqn rgiadlygaa
       61 mahwqtaqkf vpgserlrvy npileqhgwh sdhtvieivn ddmpflvdsv tmavnrlgla
      121 lhsalhpvfr iwrgsnggie rvnaggatsd dnrsqlasfi hfevdrcgdt alldtlredi
      181 arvlgdvras vedwpkivdi aratikelka restaediea raflewmvad hftflgqrdy
      241 alvsdgtgfg lrgiegsgsg llrealrpsg apdvtplppa aadiitgpwp ifltkansra
      301 tvhrpgyldy vgvklvgadg kvigerrfig lytstaymvs saeipivrrk canivrragf
      361 lpkghlgksl vtvletyprd elfqadedql ydialgilrl qehqrtrlfv rrdrfdrfvs
      421 clafvprdky ntdlrrriak llvdayngvn veftpllses aiarihfvvh aepgtmpdvd
      481 treletrlvq vtrrwqddla dalldafgee qgnrllqrya esfpagyrdd ypartavrdi
      541 eliervkesg qlamnlyrpi eaeprafrfk vyragdpial srslpmlehl gvrvdeerpy
      601 riqtqdaaha wvhdfglela ddtefdierv kglfedafdr iwsgriendd fnrlvlrahl
      661 sarevtilra yakylrqvgs tfsdayiera ltgnpaiarq lvelfllrfd patggtggtr
      721 dvqaerllka ietaldqvpn ldedrilrqf lgvinatert nyflrdadge pkpylsfkfn
      781 pakvpglpep kpmfeiwvys prvegvhlrg grvargglrw sdrredfrte vlglmkaqmv
      841 knvvivpvgs kggfvvknpp spsdreawmr egiacyqtfl rglldltdnl agnaivpppd
      901 vvrhdpddpy lvvaadkgta tfsdyanais heygfwldda fasggsvgyd hkkmaitarg
      961 awesvkrhfr emgvdtqttd ftvvgvgdms gdvfgngmll sphirliaaf dhrhvfldpn
     1021 pdpaasfaer qrmfalerss wadydtaais sgggvyprta ktiplspavq aalgidahal
     1081 pptelirail qapvdllyng gigtyvkatr ethqqvgdra ndavrvngad lrckvvgegg
     1141 nlgctqfgri efaqrggrmn tdaidnsagv dcsdhevnik illglvvtdg emtekqrnal
     1201 laemtdevgl lvlhdnyyqt qalsiagrys velldaearl mrwleragrl nrvieflptd
     1261 devaerqaak qgltsperav llayskmwly dalletdvpe dplvaamlvd yfpkplqqrf
     1321 gepmqrhplr reilathltn alvnrvgctf vhrlmeetda kpgdivraci mardvfdlda
     1381 vwrdidaldn rvaddvqarm fvdvarller aalwflrhlq sgavadggva gliarcrdav
     1441 qriapqlpsl lpadvldals erqrvlvdag vdsalavrva sgdisaalld iaevaatcnr
     1501 slelvagvyf slgtllnygw igeraaalpt pthwdmlara aalaevarlk ralassalse
     1561 ssdstapeti vhtwrerrea alqryehlla dlrasggasl avllvvvrem avlera
//
LOCUS       WP_175834753             311 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia anthina].
ACCESSION   WP_175834753
VERSION     WP_175834753.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..311
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=33054
     Region          12..155
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          168..307
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mqstqsippl arialavdpt pesqsaaryv rtllrpgmrv rivcaidnpr lvlpdiprid
       61 alltsaredl vreaqvvler tavlfagagv eleqaiidts vtggtvsnal andtstwqad
      121 vlvvganphh gllrlvegam sdtlatrarc allivpadya rpsdgplqrl mfavdgseps
      181 lhavhvglgf aapttllyaa yvvdravrlt divpvraled ayraegedal arigpvfhat
      241 gnptkrgive trptsddvah almrdavhwh aellvvgthg rrgiaawlig svarrvahla
      301 qvpvllvrga a
//
LOCUS       WP_175834775             315 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175834775
VERSION     WP_175834775.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..315
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34375
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdtlqnmrvf trvvetgsft aaaqslnstt gamsravsel earlrtrlmn rstrrlalts
       61 agesylrrcr qiladvdrae eeascaherp agvlrmhsfa svghhyvmpa ltryhtqfpd
      121 vsielslsqr mpdlfdgtsd mavvtasslp dselvshllg stfsilcasp eyvkrhgapv
      181 rpqdlgahac ltlctpafpt hewvlegadg veqihvtgpv qtntaeslal airdgigigm
      241 lplysaidal hdgtlvrvlp ghilqkmnvy alypsrrfvd akvrtwveml raqvpgmiar
      301 dvdmlnaigr epqaa
//
LOCUS       WP_175834791             254 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175834791
VERSION     WP_175834791.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..254
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=27653
     Region          41..249
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mhdhlvappd aaatppntag tpfepgplpa lstlfaqcaw fralapehqa lvlaqsraeq
       61 reagdviaqr lapseywigv hrgllklaif nasgrgctfs gvpsggwfge gsvikrelrk
      121 yevvavqrsi vlfvpvdtfh alldtslpft rfvihqlnnr mgefiasiqn srlldvdarv
      181 aqalaqlfnp dlypdtgpsl aisqeelgml vgvsrqrinq alqqlekrgv lrlaynqiev
      241 vdlaalarvg meqi
//
LOCUS       WP_175834836             424 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia anthina].
ACCESSION   WP_175834836
VERSION     WP_175834836.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..424
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41794
     Region          5..>328
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpshadspav hhagsltifq gaalyigavl gtgvialpal aaevagpasl lawaalvvls
       61 gplaatfaal garypdaggv styarrafgp kaaaivgwcf yfavpagapa aamfggayva
      121 avtggghttv ivtaaaliat vsaanafgvt vsgrmqlvls allvtlllaa vlasaphara
      181 anlhpfaphg wlavgqaaal lvwsfagwea ithlaaefrr pahdmprsag iavvvvglly
      241 lsvavasvtv lgpsagasga plaeliaggi gghaqvlaaa aallltlgtm nayfagaakl
      301 gaalgrdgal pawlahgsqv ggvprhslgv iallaavala attitdvgpk plvlvtsgcf
      361 vmvyglgaaa alkllprgsi ahrcawvslv avaglflttg wyllcpllla ggallylrma
      421 grrn
//
LOCUS       WP_175834900             231 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia anthina].
ACCESSION   WP_175834900
VERSION     WP_175834900.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 231)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..231
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=25009
     Region          23..231
                     /region_name="ArtM"
                     /note="ABC-type arginine/histidine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4160"
                     /db_xref="CDD:443325"
ORIGIN      
        1 mdlsvlssyg sllllgvltt vkllvisavf gfalaiavaf arlsanpvia rvskaftevi
       61 rgtpllvqiy liyygvgslf agwpalrdsv lwpflrdgfw yvafalvisv gayvgevlra
      121 glrgvpkgei eaaramgmrp smiarrvwlp raiqillptl agetvmllks talastvavm
      181 dvlgaanyir aqtlrtyepl laiaviyvvl afaierafgr lerrvpvrmp r
//
LOCUS       WP_175834903             264 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia anthina].
ACCESSION   WP_175834903
VERSION     WP_175834903.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..264
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28111
     Region          4..259
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mntrmtagra lvvgiawaai lflmlpllvs vpvsltpndy lsmpdgtlsl rhygallddd
       61 gwlssflqsg lialvssvis vtlgtlcaig lwkvasrrge fvrgvilfpl ivppivsala
      121 fyrlwgelgm ldsfpaails hvvlsvpyvv vavsaslatv glrieqasrs lganvaqtlr
      181 yvilpsikpg vlsaavfafi lswdelvvtl fissrhvytl prrmwdgmre nvdpaiasvs
      241 tlllaatcva iglsllrkra agpv
//
LOCUS       WP_175834908             463 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175834908
VERSION     WP_175834908.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..463
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=48332
     Region          8..463
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 msdlssnddv vaalrdalga dcvstgdaig arhftnygea agvrprallr prsvddvsra
       61 laicaahrqt vvpqggmtgl aagaepgahd vvlslermtg vveidadaat vtawagtple
      121 vlqqaaddag falgidlgar gscqiggnva tnaggnrvir ygttreqvlg levvladgtv
      181 lsslnkmlkn nagydlrqif vgsegtlgvv trvvlrlhpr laapstalca vrdtaaalal
      241 lraartacsd llsfeamwpa fygyvcahtp glraplpadd gvkvliecas gdaaqtaerf
      301 eavladwler gliddaalaq qaadaqafwt vreglaidal pglvnfdvgi ppretatfie
      361 acdhalktrw pgahvfffgh lgdsnlhvcv sapyaagesa hdvdavlypl vrdaggsvsa
      421 ehgigrykrd wlgcsrsdae iaamrrlkha fdplgllnpg kvi
//
LOCUS       WP_175834918             232 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175834918
VERSION     WP_175834918.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..232
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25960
     Region          21..179
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnakstvarp rgrrpsvddf dlrdhmldva mqlfaergia attvaqiaaa agvtsamvhy
       61 yftnreqlld aiveerlaqv iafvwrptas hlendpfalv telvdrffdv thrmpwlpsi
      121 wlreivhegg llrermlrri plehvgrfae riraaqqtgm lnpalepafl fhsiialvml
      181 plataklwqs arglppidrd vlhrhvcall gsgmqppaaa pdahahvrrr ps
//
LOCUS       WP_175834932             353 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia anthina].
ACCESSION   WP_175834932
VERSION     WP_175834932.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..353
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=39428
     Region          82..314
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mkpsqfakgf qarpdittse krtaldrlna idgivkseta tpaptksakk diapppvpev
       61 lldpstdesa qyrawrlenr yatgqvielp lktikhspfn prhfylkssi aelavnlakq
      121 gqqqaihvip dydnpgtyfv sdggrrvral keankesvka ividvpigiq syklgydlnv
      181 qrdsqtvfdn avvwrrfldd khfqsqkels ehlgldestv avalsigklp esvmqemvar
      241 pdrfgsnmay qvgryhnarg teatlrlink ivsddlstrq vsdivkgrva aqetpkpagr
      301 qryaqrleik lggksvgdlk sygedrielr lrglpkekrd aileqlerml lse
//
LOCUS       WP_175834991             469 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175834991
VERSION     WP_175834991.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..469
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47300
     Region          18..420
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(25..26,29..30,33,65,115..116,118..120,123,144,
                     147..148,151,274,277..278,281..283,286,314,318,370..371,
                     375,379,395,398..399,402..403,406)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtaaaptaaa arrvlaatcv sytlvlldas ivnvaltdia htfgshvagl qwivnaytla
       61 fasllmtggt lgdrlgdrtv yvaglavfvv asalcgvapt lpalaaaral qgvgsamlvp
      121 cslalinraf pepaarasai siwmgcggia masgpliggl lihlfgwrsi ffvnlplgla
      181 giacartiar aapdasrqfd wagqaaaiva iavligtlie gpslgwrtap iiggaaasvl
      241 awiafiaiea rrrdpmlplv ffhnrlfags tcvsmasafv fygllfvlsl fyrqirgatp
      301 ldtglaflpm tamvalgglg sgrlvarfga ratmcaafgl yaagalglla igaatpawaa
      361 vapmlaigfa sgfispaata palgtidrrr agvaaaalna arqsgsalgv aifgacigml
      421 qpfpvamhva lgmaavlsal aaatwwlatr paaasdarpg scsqpnvgr
//
LOCUS       WP_175835015             266 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Burkholderia
            anthina].
ACCESSION   WP_175835015
VERSION     WP_175835015.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..266
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28529
     Region          18..260
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mtpsrtlsal tgddapsilr ndedgvawlt ihrphvanal saeafrrlcd elvtldddpa
       61 vraivirgag erafsagvdl gdpemrgmrp mrglarnvhe lilelrkpti aaingyaigg
      121 gfeialacdl rvaadhasfa lpearvgmga nfasvllprm lpraiamell ftgrridade
      181 asrigllnrv vpgaalddtv relaqsiaan apltirrike tatrswglpv aaalrldvgp
      241 dvyasedrve garaflekrk pvfkgr
//
LOCUS       WP_175835034             415 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175835034
VERSION     WP_175835034.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10396284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..415
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=43583
     Region          1..261
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Site            order(7,9..10,12,31..33,66..68,104..106,116,120,139..142)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187579"
     Site            order(82,106,116,120)
                     /site_type="active"
                     /db_xref="CDD:187579"
     Region          308..407
                     /region_name="DoxX_3"
                     /note="DoxX-like family; pfam13781"
                     /db_xref="CDD:463982"
ORIGIN      
        1 mnilvcgang figralgarl eagghrvlrg vrraagprdv eidfakdvda dawlprlqgv
       61 dvvinavgil agrrgatlda vhraapcalf taccragvrr viqisalgve rgdtpyfask
      121 haadrflqtl plesrivrpa lvygacgtsa rffrmlaslp vhvlpagghq rlrpvhvddl
      181 aelvarlvda paagerviea vgadeveyrd mlggyraafg fppaarialp gplvgavatl
      241 sgaipgallt rdtwtmlrgg ntgdpaaita vlgrpprglr tfigadaavl rhdalamwrr
      301 plllgalaiv wiwtaivsaf vhprsdslam lahaqltglp alialyaaca ldfafgvatv
      361 vapsrrlwva qgalivaysa viavtmpall aepfgpvlkn vpilaillil fadee
//
LOCUS       WP_175835075             434 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175835075
VERSION     WP_175835075.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46230
     Region          27..425
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(40..41,44..45,48,80,130..131,133..135,138,158,
                     161..162,165,258,261..262,265..267,270,298,302,353..354,
                     358,362,378,381..382,385..386,389)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 msavpssrrp aahdsapvqa lyrklnwrll pllllcytfa yldrvnigfa klhmqsalgf
       61 sdaayglgag ifflgyvlfe ipsnlllpri garktisrim vlwgltsagm mfvhdttsfy
      121 vlrfllgvfe agfapgmify ltywygprrm agvmavvmla gpiggivgsp lstwlmttld
      181 gahgltgwqw mfvaeglpca vlgllvlkvl adrpadaawl sdreksllaa elhapaaghh
      241 afgqaardlr vyllafayft micgiyavsf wlpsilkang vndtmqigfy smipyigaag
      301 amivigrrsd rhgerrlhsa vsalvgaaal aaatyadghl avslacmtia tallwaaytv
      361 fwaipsqylt gnaaaggial intiglfggf lsptligeir tatgsmqagl lvivalmvag
      421 avalimnrlp aaar
//
LOCUS       WP_175835175             166 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrofolate reductase [Burkholderia anthina].
ACCESSION   WP_175835175
VERSION     WP_175835175.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11087044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..166
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17911
     Region          3..163
                     /region_name="DHFR_1"
                     /note="Dihydrofolate reductase; pfam00186"
                     /db_xref="CDD:425512"
     Site            order(7,24,29,59,99,105,118)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(9,16,46..48,66,100..103)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 mttltlivar arngiigrdn qlpwklpedl affkrttmga pivmgrkthe sigrplpgrr
       61 nivvtrdatr rfdgcdtvts ladalalaar dgvpeaflig gaqlytegla ladklvvtei
      121 dadfdgdasf papdpahwhe vsrdthqaaa pntfgyafvv yarkhg
//
LOCUS       WP_175835122             298 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia anthina].
ACCESSION   WP_175835122
VERSION     WP_175835122.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..298
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31199
     Region          32..284
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mqslsgssap spapapshan gaarraprvt gartiaalqw gvtlllcafl ivpvvmsvla
       61 gltvnyfrgl ssgltlrwle qvwqqyqgsv alslgvafat laivlavgvp agyalarsks
      121 rvarvieeal vlpvalpgla salallvvyg gftafrmslw fivvghvvft lpfmvravaa
      181 vaagadlrtl eegaaslgas fvtrfvtivl pnlrpgivag alavltlsig efnltwmlht
      241 pdtktlpvgl adtyaslrle vgsaytivfl lmtlpllvam qwlgvdpsgt ravkrrpr
//
LOCUS       WP_175835179             306 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia anthina].
ACCESSION   WP_175835179
VERSION     WP_175835179.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..306
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32200
     Region          49..287
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
ORIGIN      
        1 mtvittpaaa svtaapgsaa asaprmgrlr tadglelasy rwpagdgtap pratialvhg
       61 laehagryaa laarlnaagi evlatdlrgh gqspgkrawv erfdgylnda dalvaqaard
      121 dtplflmghs mggavaalya iervpargya ltglvlsspa lapgrdvprw mlamsriisr
      181 iwptfpairi daallsrdpa vvaanradpl vhhgavpart gaeildamar iergrgalht
      241 pvlvyhgtdd kltepdgsra fgarvgstdr tltlyeggfh etmndlerdr vidaliawih
      301 arapar
//
LOCUS       WP_175835208             890 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia anthina].
ACCESSION   WP_175835208
VERSION     WP_175835208.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 890)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 890)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..890
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..890
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=98313
     Region          14..793
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msaqdivrai kggliqqdrl lkldtplgpn mllpqrvvgr srigrhfdft ldvlstrsdv
       61 klksligqpv tlwiqqanls ylprhgyvym vrrlgseggl tsyqlgfasw mhflkfrrdq
      121 riwqdkpvde ilrdvfnahp hakgrfefal skplpprsyc tqyeddwsfv hrlmeeeglf
      181 giwkqaddgq shtltvtdgv dtceqlatrt vrfsrygans evdalvqwsd wrtlhsaalt
      241 trtfdyksps planpkgthi ptvshelpeq lemyeytgpy sylkqergdh ltkvrmeewe
      301 srakrfhgag glrgidagvw felaghpehe rdsgdrrqfv vvevvwlien nipgsshhan
      361 fahslrhqln eamtgqagep aglrlahhdg segfflteie aqrksvpyrs pfehckpvmq
      421 mqtamvvgqq gnaihtdemg rvkvqfhwdr igqrderssc wmrvsqpwgg qgfgmihvpr
      481 igdevivsfl dgcpdrpvit grvtngtnfv qwklpdnqal sglrsrdlgg aqanqvvadd
      541 tpgrlqvqvs sdheqsrlvv gyntridgha gratgrgagw elatdawgvl ranrgmlvtt
      601 eartgasapv kdmgetvqrl aqarelhdtl akaaiqaqaq dgqdqpavvd alrkqgdeig
      661 gqdggdypel skphlviasp agieattags thiasaehta ltggghvsvs sgssllasar
      721 nairffaykl girmisyagd idikalqknl nllakleitq tanritirat eevmlhggds
      781 yislksgkit vggelyevna qaqnmppkpm gvspnglpdv qandqrfrvl sptgkplpgv
      841 dyrlttpsgs hifrtdalgr spavntaeqe naefqlhwdd faaasdmpea
//
LOCUS       WP_175835232             457 aa            linear   BCT 11-JAN-2025
DEFINITION  HdeD family acid-resistance protein [Burkholderia anthina].
ACCESSION   WP_175835232
VERSION     WP_175835232.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..457
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=50249
     Region          <48..185
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mvrlvmlllg vdylrhratg lvwigalwva agavvvvdal dgalhfpvtl fawlfllegl
       61 atlavawtgv ggqrvlryvk giavvaaaml ifaghhhgnl ilslifgtlf lidgllqcvs
      121 awlvryrrwr vafawgaaei liavffyqpy pthyagtlpy clglflifgg anlltlaarv
      181 rrmkrnpafs vsrrsallpd tepaahaaqf drtewdgppa dheraltvhv wtptgsskap
      241 aqhhpvvdry iaavdvngti stghaalesp egiyislypa aeidrspsef grilratrdn
      301 dvpglfqpdy atesnawcas tvrvrirnyd paklrafwer yradvtynlt hrncsssvay
      361 aleaaidgav grlrgegagw gsflrvlvtp elwvaaqirk ramtmawtpg laldyarals
      421 mladprpfaw wtaarvaagr lsrqrrawra qdagapq
//
LOCUS       WP_175835245             736 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia anthina].
ACCESSION   WP_175835245
VERSION     WP_175835245.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..736
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=77543
     Region          28..>192
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          200..728
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mtieldnpgs vrpsrrtflk aagaaaavsl tigfewaglg rralaatppa adfapnaflr
       61 itpdgavtvi akhvelgqga ytgiativae eldadwsnvr vesapadakr yanlafgtmq
      121 gtggssamsn swqqlreagg karamlvsaa aarwkvpase lstadgvvth aksgktaayg
      181 tlvadasklp vpdkvvlkqp adfrlighri prvdasaksn gtahftldtt fpgmrvallq
      241 rpprfgatvk sfdataakav pgvvsvvqvp hgvavvatgf waakqgrdal kvewddthae
      301 krgsdeimre yrqladkpga sarkdgdada aiagaarkvs atyefpylah apmepldavv
      361 klsadgceiw agdqfqtvdq snaakvaglk peqvqihtly aggsfgrran awsdyvveav
      421 siakalgadg kpvklqwtre ddiqggfyrp myfhkmdagl tadgrlvgwr hrivgqsila
      481 gtpfepfmvk ngidatsveg aanlpyavpn vsveltttkv glpvlwwrvv gsshtayave
      541 afvdeaahaa gkdpyqfrrd llakeprmra vldlaaqkag wdpakplpkg rgrgiavaea
      601 fksyvaqvae vsidadgkvk vervvcavdc giainpdiva aqmeggigfg lgavlhsait
      661 lkdgqveqrn fdgyhvlrma empkvevhiv psaeaptgvg epgvapvgpa vanaifaatg
      721 krhyvlpfds adtaka
//
LOCUS       WP_175835381             234 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia anthina].
ACCESSION   WP_175835381
VERSION     WP_175835381.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..234
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25655
     Region          15..175
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mnaphrvtep nilyfgtpvv listlnpdgt anlapmssaf wlgwrcmlgl aassqttrnl
       61 lrtgecvlnl pssaqahavd riarttgtdp vpeskrargy vyepdkfgta gltetasqtv
      121 appralecpv hleavvaath gigddmpdlr drirvfevri qrvhvhpdll mdghpdrvdp
      181 dkwsplimsf qkfyglaphq vhpsrlaeip erayrssdve rsrdagmsmd aaqq
//
LOCUS       WP_175835374             166 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175835374
VERSION     WP_175835374.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..166
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18196
     Region          17..155
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mkldrgnaal adaapvldri drailrqlqq dasisnvsla akvklsapac lrrverlkem
       61 glirgivall dpkplgagml vvigfvldrs tpeafaefek aaqkvsgcve chvvtgefdy
      121 fmlvrtrdne sfnrlhadql lylpgvrqvr sfmvlkeils thalpl
//
LOCUS       WP_175835433             327 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Burkholderia anthina].
ACCESSION   WP_175835433
VERSION     WP_175835433.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..327
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38230
     Region          99..255
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mpaewmtwlh afmghdvdwk qvlligmtpv flvafmiefa iatqrgrrep frwkeivanl
       61 slgagyqvae tvmgilftga ifawvyrhrl fdvpvngwti vpifvivefc yywfhrtshr
      121 vrwfwaahvp hhsgevmnft tamrqsllna fvgvfvfylp pvwlgippav vlfllavdla
      181 yqyfvhteai grlprwfeyv fdtpsnhrah hgrnpryidr nyggvliifd rmfgtyveet
      241 epvdygitqq irsynflvln lhefvdmwrd vfapgplaqr irhlwmppew erpghrpiht
      301 wsverkgdae ddavevgdva dvvehra
//
LOCUS       WP_175835462             315 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175835462
VERSION     WP_175835462.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..315
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34024
     Region          19..78
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          108..303
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(123..124,126..127,130,134,136..142,233..238,
                     244..245,247..248)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mgsidrrdst pqllnrlrmr qialllavde cstlraaagk lgltqpaatk mlaelesalg
       61 qrlfdrvgrg lvlnpagerv lgyfrgirgs vealnrelge lqlgsagrla igsimaaspg
      121 rltealvqlk arypllaidi avdtsdrlmp qlregvlevv igrhvgtdcd frvvddeala
      181 iiagrdhpla gagpvefdal ldyawilqpa gsparevver efrarhqpmp rglvetgsil
      241 ttmnlvdrsh mlgvipltva qrnaehglva ildyvldqkl psygslvrrd rplsipaqqf
      301 lalfhrdgaa ddgda
//
LOCUS       WP_175835440             375 aa            linear   BCT 11-JAN-2025
DEFINITION  J domain-containing protein [Burkholderia anthina].
ACCESSION   WP_175835440
VERSION     WP_175835440.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10644999
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..375
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=42184
     Region          <210..250
                     /region_name="DnaJ"
                     /note="DnaJ molecular chaperone homology domain;
                     smart00271"
                     /db_xref="CDD:197617"
     Site            order(226..228,237,243..244,247..248)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
ORIGIN      
        1 mtarrgaeva iapghetasl skaqktfntl vkqiekrrer lgawdaitpa fqkkfvdgll
       61 pleqestalr iqlihlldda flqkglskae qrtlsdliad magdllhvsd daglkaiydr
      121 hrasahvgsa aaepaptkpe pepepkpapp edldalspde laermqaeld aqferdmaah
      181 aareaqrakr kkapkqsaaq arveaeqaes sksireiyrk lasalhpdre tdpqeqqrkt
      241 vlmqrvnhay akgnllqlle lqleieqidr raidglsear ltryngilee qlreldqeie
      301 hverdfrrty giasstkvap dtvirmltrd iagmqrsnqd lsvalrefed pdnvrdwlkd
      361 mkrrpvasrf dddsf
//
LOCUS       WP_175835513             237 aa            linear   BCT 11-JAN-2025
DEFINITION  PadR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175835513
VERSION     WP_175835513.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 237)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..237
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25685
     Region          83..162
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mrhnpsrgha rcdghgahag pewfaglwha igrhrrghdp fggggpfggr ggrggfgdfg
       61 ddgmprgrqf ssddlqllll alvaeqpshg yelikaldtr sngfyspspg mvypaltyle
      121 evgfvasqae gnrkryaltd agrahldaqr ervdtlfarl thlarkmefm rrafagetag
      181 seapdetqpg wlpefvearl alkrallhks aadadeqrri aaimrratae ieggtga
//
LOCUS       WP_175835551             137 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175835551
VERSION     WP_175835551.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..137
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15348
     Region          19..110
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(20..22,36,53..55)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mtttvekvvl ppipakryft igevselcgv kphvlryweq eftqlrpvkr rgnrryyqhh
       61 evllirrire llyeqgftin garnrldspg seraaavpad peapaadvra pgkpgttvdv
      121 valrqalldv ldglkhd
//
LOCUS       WP_175835635             128 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF805 domain-containing protein [Burkholderia anthina].
ACCESSION   WP_175835635
VERSION     WP_175835635.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..128
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=13968
     Region          1..115
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 mnlkwflfsf egrigrlpww iyalayaals alfdakqrgs saedlpllvl lvlfaiavvs
       61 iwssiavgvk rlhdidksgw wmllifvpiv gaialfvmng fiagtphanr fgeppsddrd
      121 eaapqgpa
//
LOCUS       WP_175835637             339 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia anthina].
ACCESSION   WP_175835637
VERSION     WP_175835637.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..339
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34894
     Region          36..338
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtqppvsptd agaqqtvtgr raralsgtrl gvsnylglag alvamialfs tlsshfltyd
       61 tfstianqip dlvvmsvgmt fvliiagidl svgsvlalaa smvsvaalkw qwgpfpaals
      121 giaiatvtgs ltgaitvgwr ipsfivslgv leaargvayq ltnsrtayig dafdflsnpi
      181 algispafli avavmiaaqf vltrtvfgry lvgigtneea vrlagvnprp ykilvfalmg
      241 alaglaslfq isrleaadpn agvglelqvi aavviggtsl mggrgsvist ffgvliisvl
      301 aaglaqigan eptkriitga vivvavvldt yrsrrtrar
//
LOCUS       WP_175835638             317 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia multivorans].
ACCESSION   WP_175835638
VERSION     WP_175835638.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..317
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34672
     Region          11..70
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          100..296
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(114..115,117..118,121,125,127..133,225..230,
                     236..237,239..240)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mysligktat frqlkaldmi arlgsvsraa eelnltqpav slqvrlleea vgaallqrvg
       61 rgvqltaage ivaryareil hlwseagdev aaltgdlggt lrigaittae ylippllvkf
      121 tatrphvkty fkvgnrddii rmlatheidl avmgsapkel rthavefakh pmvfvaapdh
      181 plmqrkrval kdlesahllv rergagtrst venlfktsgy rfhvgselss neaikqmaea
      241 glgvaflslh acalelrtgl lkqlpfpgnp ierewyvvtv adrrisqvtg lfrdflirqg
      301 apvidgatsa sherrrk
//
LOCUS       WP_175835821             254 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF899 domain-containing protein [Burkholderia anthina].
ACCESSION   WP_175835821
VERSION     WP_175835821.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..254
                     /product="DUF899 domain-containing protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28354
     Region          1..254
                     /region_name="COG4312"
                     /note="Predicted dithiol-disulfide oxidoreductase, DUF899
                     family [General function prediction only]"
                     /db_xref="CDD:443453"
ORIGIN      
        1 mtnhltgtra ewlaarrall daekaltrqs delarqrqal pwvrvdktyr fdtedgqatl
       61 adlfggrsql lvyhfmygpd ykagcpscsa iadgfdgfai hlanhdvtla avsraplanl
      121 layrqrmgwt fpwassvgnd fnfdfnvsft etqqrtgdve ynyaragham dmapppaavv
      181 qfaatcgtda atysldrpgm safvredgvv yhtystyarg ldglwgmyqw ldraplgrne
      241 tgpwwrrhde yarg
//
LOCUS       WP_175835671             338 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia anthina].
ACCESSION   WP_175835671
VERSION     WP_175835671.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..338
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38091
     Region          33..>120
                     /region_name="NurA2"
                     /note="NurA-like predicted nuclease, RNAse H fold [General
                     function prediction only]; COG2380"
                     /db_xref="CDD:441947"
     Region          171..316
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mqdtltkpag aadtvegeva aaldgaahaq ttpsvermld awrpddppaa llaefvalfn
       61 tdtrhdaatv svplggadpa avasyvarav regviddari dgdrlhlnas ratfwqnpqp
      121 wltasassgm plryaitngh rhpvrppspa geiyarympq vgmtfslrtv dvathaqlfs
      181 dwmnldrvah fwdqrgtrde haaylterla dphmhptigy fddtpfgyfe fywakedrla
      241 pfydahdydr glhlligdsr fqsagklhaw wsgvlhymfv deprtqrlvg eprvdhvrhi
      301 aymhrlgfyt lkefdfphkr aaltvmeret ffdtfrlp
//
LOCUS       WP_175835834            1148 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia anthina].
ACCESSION   WP_175835834
VERSION     WP_175835834.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1148)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 1148)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1148
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..1148
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=126585
     Region          49..565
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 msrlggtccl ppirtageqq yfdhamaals shkfwtaaad sstyrpsagl wapqrravgt
       61 avayigavag skpsesalik mptgtgksgv iatlacalpn vrrtliitpr rslvdqmlnd
      121 vhwrfwrhfd ldygttglra sqrgnavptn tqmiadgvmr llpsttttlc sypkgerliv
      181 vgtfsalaqi lrpprpahrl tghypierde aptdaprsse watpqadlvr avlsdfdlvi
      241 vdeghyepaf vwsqcirela rptvlfsatp yrndfkyfqv rgnfafnlgy eeatnqhlvr
      301 pvtfagaqhl pksgcspsef sdalkkfkts vldkqywpaa rgprrvivrc adheslirmr
      361 dalrglgssa vlihdnvkrd dadklefqsv nralrapesd pieywlhqwk llegvddstf
      421 aaiaiyepfs asratiqqig riirvldraa pgkevatvfa sadiqsdvqa rferythyeq
      481 hfakdpkral eqesnlpgll lqsvapyqyl agdfrervpl ddaleppkya dfavplrtsi
      541 yrysstatle ilakacaeam qledrynvti lqpgvaetgs vrlihyltck nsellvrhsl
      601 piwglgvmvl gligarvfil dtegividld alglepesae ylqrlipang ngiasrvsqa
      661 saigldlses avrsvtarmh dfasgffdls qssqalhsvr asmrlkdtpv trylsidras
      721 vsdysartqr rsvneyflwl qhlaaildsn apisgvferf arsvaapplq dalpmnvlfd
      781 fydlldtsld tagwhatkce slrqaetcvd vdgsgafsln vagnvlngki tyavtgnvrp
      841 kgrydiespe ldafvrdpns pstepaslvr alnkeqafrv ipsgsdltya krlfyqtgld
      901 idaiasgree gsplemltps pwleqvtsek gggsarrwva dsvfggvfae fglsnhgars
      961 nararplhal dpalaqelqt fdtmvcddgg qeqadfifkg egprrvvfvh akvndnlmsv
     1021 samqivgrqa maslafiarg arlqdrsaww sspwstddhr qvphrvlrss npnlpviwge
     1081 ikrgiqsaqy akeiwifagr tlskkelvrq ltrpagptpl slqmayylgt lqtsaaranv
     1141 amrifcss
//
LOCUS       WP_175835875             321 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia multivorans].
ACCESSION   WP_175835875
VERSION     WP_175835875.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..321
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34357
     Region          5..315
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpkvvgvfav pgvqlldvsa pldvfaqanv eygkafytlr viacesgpir sssgaqllpd
       61 wvapdvpari dtllvagapg agrvplrtdv lawlrsaavq srrygsictg afvlaetgll
      121 kgrhltthwa vaealaeahp titvdadaly vrdgklrtga gvtagldlal alveedlgrd
      181 iarrvasqlv mffkrpggql qfsrkgearp agrsvlqevq rwiaahpela hsvadlakha
      241 gmsprhfarl fraevgmtpa awveatrisa arqllenghd tpkqvaakcg fanvdtlrrs
      301 fakhvgitpa eyrkrqaivt e
//
LOCUS       WP_175836004             421 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia anthina].
ACCESSION   WP_175836004
VERSION     WP_175836004.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..421
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=44014
     Region          205..413
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(212,252,290,393,396)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(212,393,396)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(212,252,290)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 msfrssvvat vlgasvflsp laasaapagw vaawatalqp ipdlaapppl yrapdvagrt
       61 vrqivyptvs graarirvsn aygraplvie daglaragdg aalaersvap vrfggkasvt
      121 lapgqelesd pvaidvtagr pyaislrmgt nqrmtvwhrv snqfnyvstp gdhvddpgag
      181 afrtrftqya wvtelaveag sarasvaaig dsitdglrss lnrnhrwpda ltrrlsasga
      241 dslgvvnlgi sgnrllsdsa cygtslasrf erdalsrsgv kavivligin dinfaamppr
      301 agldcdnpht qvtaaslidg yrrlieaahr qgvkvfgatl tpaglpagre airlevnrwv
      361 rsgggfdgvv dfdailrdpa rpsvlqrryd sgdgihpsda gyaamaeavp meqlqaaagg
      421 k
//
LOCUS       WP_175836011             264 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DsbC family protein [Burkholderia cepacia complex].
ACCESSION   WP_175836011
VERSION     WP_175836011.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Shao,F., Bader,M.W., Jakob,U. and Bardwell,J.C.
  TITLE     DsbG, a protein disulfide isomerase with chaperone activity
  JOURNAL   J Biol Chem 275 (18), 13349-13352 (2000)
   PUBMED   10788443
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Chen,J., Song,J.L., Zhang,S., Wang,Y., Cui,D.F. and Wang,C.C.
  TITLE     Chaperone activity of DsbC
  JOURNAL   J Biol Chem 274 (28), 19601-19605 (1999)
   PUBMED   10391895
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..264
                     /product="DsbC family protein"
                     /GO_function="GO:0003756 - protein disulfide isomerase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28777
     Region          50..244
                     /region_name="DsbA_DsbC_DsbG"
                     /note="DsbA family, DsbC and DsbG subfamily; V-shaped
                     homodimeric proteins containing a redox active CXXC motif
                     imbedded in a TRX fold. They function as protein disulfide
                     isomerases and chaperones in the bacterial periplasm to
                     correct non-native disulfide bonds...; cd03020"
                     /db_xref="CDD:239318"
     Site            order(50..58,61..88)
                     /site_type="other"
                     /note="dimerization domain [polypeptide binding]"
                     /db_xref="CDD:239318"
     Site            81..88
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239318"
     Site            order(137,140)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239318"
ORIGIN      
        1 mnnrflrgrv rllvaalatt lpytstvyaa ddtaavqqvs dhlaatypkt pfrevkpapl
       61 pglyevsmgd tvaytdstgr yflfghlydm qdqvditeqr kaqgyktrfp aavlnhaikt
      121 vhgngervfa vfsdpdcpyc hqleqqlamv dnvtiytfly pleslhpdam tksiriqcsa
      181 dpakawrewm tenrlpplvs chhaindniv lgsrlgvtgt ptiiaedgrm lpgavsaaql
      241 sawldagtra apasasaqpq gaik
//
LOCUS       WP_175836080             540 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175836080
VERSION     WP_175836080.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 540)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..540
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54319
     Region          23..463
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,279,282..283,286..288,291,319,323,375..376,
                     380,384,400,403..404,407..408,411)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mdqpfsaast qsarrrawll aavcmaaval plsfsggava tpaigrdlhg gpvamnwitn
       61 afmlafgscl maagaladqf grkrvfaigv ggftlmsval afapsmlavd llraaqglaa
      121 aaalaggtaa laqefdgaar trafsllgtt fgiglafgpv lagcliahyg wraifvtgav
      181 agalslgvgl prmhesrdph atgldwpgta afttaltlft fgvieaparg wadplvvall
      241 agaalgaaaf vaietrvarp mldlslfria rfvgvqvlpv stcccyivll vvlplrfigi
      301 dgfseidagw lmlaisapml vvplvaatlt rwlspgvisg iglliaaagl vwlgialrgg
      361 agpaaiapml aigvgagmpw glmdglsvsv vpkeragmat gifsttrvag egialaivga
      421 vlaalahadl sqaaagvsda adttlraaar latgdlagaa avlpgvgraa llasythafd
      481 rlliglavvt vlcagvvfaf lgaravevda daqedtaahp hvdasarrrt epdcaetsgr
//
LOCUS       WP_175836088             505 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Burkholderia
            anthina].
ACCESSION   WP_175836088
VERSION     WP_175836088.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..505
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54329
     Region          3..503
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mnlvaaldra aratpdkpfl ihddttitya aarershraa avlsalgiaa gdrvaamcln
       61 tpafvdlmfg awrlgaafvp vnhklqapev dyvlahsgsk vilfdaalap vierlvhpaq
      121 rlvtegeldg vpnfdtmrae tdgiagiepa dddvaqilyt sgttgrpkgc vhshrtvtfa
      181 alaaalatgi grnertlmam piwhssplnn wfggtlyagg tvvllreyhp lrflqaiere
      241 rvtlyfgapv sytlpldtig qfatfdlssv rawlygggpi gvaqaerlar ayrshaffqv
      301 ygmtetgpag ttlypdeqia kagsigrqgg pgvdlrvvsv dgddardaqp getgeiwlka
      361 dsmmlgyldd aaatraafap dgwyrtgdia ridqdgylfi vdrikdmivt ggenvyskev
      421 edvlgahpai veaavvgvah pdwgetvvah vvmragtapd pdalrafcge rlaaykipre
      481 fvfaetlprt ptgklqkfll rtrrd
//
LOCUS       WP_175836097             418 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia multivorans].
ACCESSION   WP_175836097
VERSION     WP_175836097.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..418
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43628
     Region          24..412
                     /region_name="MFS_MJ1317_like"
                     /note="MJ1317 and similar transporters of the Major
                     Facilitator Superfamily; cd17370"
                     /db_xref="CDD:340928"
     Site            order(34..35,38..39,42,74,125..126,128..130,133,153,
                     156..157,160,238,241..242,245..247,250,284,288,342..343,
                     347,351,367,370..371,374..375,378)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340928"
ORIGIN      
        1 msdnqeaatp apladsrrwl nrtvagagvt salgdfcyet ttvilpgfla ilgvpaaalg
       61 viegladava sftkmvsgyl adklghrkrl vlagyaltpv gqifialatg wpllllgrlv
      121 swfgkglrgp lrdaiviqav saetrgrafg fhramdtiga vlgpllgvav lewaqsvhrs
      181 dpagpfrlvl wlsilpgmla vlaflamvdd peqspnpgrr fwgalralpa rfkqylgavg
      241 vfglgdfshs llilaatqll tpsfgvvraa qiagllyvgr nivqvlasyp agvwadrvga
      301 lrllaggyli gaataaliav lwwldaasvp llgvvfllag lyvavqdtle stvtadmvss
      361 dtlaisygal gsvngctrfl ssgmvgvlwt avspiagfgv aavlmfvgvv alrrlvrr
//
LOCUS       WP_175836107             353 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia multivorans].
ACCESSION   WP_175836107
VERSION     WP_175836107.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..353
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37789
     Region          125..329
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mspntdqlnd srreetlppc aalpgaiari anprvsghai dsapvsirls lldwllkatg
       61 qnkidelsdd iivagqkplp rnwlidlvfg kpaddvdirf rageaivppl rlyvpsgqrk
      121 arsgllylhg ggwvsgdpgm tdwwcshyaa rtgtivasvd yrlapqhrfp aglldaysal
      181 qalhgdadsl gierdsigva gdsaganlaa altllarnqp glpiamqili cpaldlrfds
      241 psmdensdap llsaamiray arrylgdpsa adspyvspll andlselppa liqvaehdpl
      301 rddgwryhar lkangvssqi teyagaphgl ttfpgltpls eralveasef qfk
//
LOCUS       WP_175836134             794 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Burkholderia
            cepacia complex].
ACCESSION   WP_175836134
VERSION     WP_175836134.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 794)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 794)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..794
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85573
     Region          107..791
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 msriratfqf vhskspratn karvdlsfll arqlaslvia revhmcmaid ipatssymsa
       61 iararahvpi mldlklvtta slaafslagh aqsiasnssp lpqqpipavg aqidiqsgpp
      121 adiklpaisv tshryrfttt dtaldsesat rtdtplinvp qsvqvvprkl ieeqdartla
      181 dalanvsgvm psqpaenglt anivrgfpae iyldglpmyg msaanspasl vgiqqidvlk
      241 gpsstlyggg lgsplgglin iqselpqtkr sgyvamrtgs ygtvnpyfdl tgaltssida
      301 riageyehag swidqvksdk wsikpsvlfk ldprttllvq gqfnhssqle ysglpasqal
      361 agqldryafp gapigqqrts fdsqlatvql qhefndnlkl svsgryyhns ipeygsfvyp
      421 slyapdpatp ttypilplnm qtstseatld anlqtkvnal ggrhellvgi nydhtdfssd
      481 mgftgvpvgs qnlaqpaydl afgalapltl tqtdryqtia ayvqdqatyg rfhltgslrf
      541 tqlrfheaeq gtndtyhhvs prigasfdlt qgvavyaays tafraafgyv glgspkpets
      601 rnveaglkla rtdiglsgtl avfqqtrqnv atpdpnnply siqagqqrar gfetdlvwep
      661 tsafsmlmty aytratvted naipvgdtla rvpkqsgria lryrflnsta rglsfgagit
      721 afgarevtlp ntvsvpgyal fdaqaeysfg rytigvsavn lanrhvyapy eylsfpvvmp
      781 vqprsvyltl kasi
//
LOCUS       WP_175836201             247 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease [Burkholderia multivorans].
ACCESSION   WP_175836201
VERSION     WP_175836201.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..247
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26970
     Region          <10..52
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mgskknkgkt cvycgvapst tgdhviaref fpkdardnlp kvpacakcnf dksklehyll
       61 tllpiggrhe galaaitdqv vprlaknaal drtlaagqrp ffvldegrpw qawvatpldv
      121 tkltdlacfi avglasyhwq iqlmprarad arrltekgrt mmaadlagpa agarvernlg
      181 ngvfyyqgay qrtnpmqtiw emsffggvei gpmnmsgest rsvtvvtsdr pdwlarfpdr
      241 kigggqk
//
LOCUS       WP_175836211              99 aa            linear   BCT 11-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Burkholderia
            multivorans].
ACCESSION   WP_175836211
VERSION     WP_175836211.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..99
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=11503
     Region          6..99
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mptkarmvrl tplaeadled iwsytfehws leqaehyvge laaaferlar gewigrstra
       61 gegyrryivg shvvfyrett ealdvirvlh qrmdvdrhl
//
LOCUS       WP_175836344             387 aa            linear   BCT 11-JAN-2025
DEFINITION  elongation factor Tu, partial [Burkholderia multivorans].
ACCESSION   WP_175836344
VERSION     WP_175836344.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     gene            1..>387
                     /gene="tuf"
     Protein         1..>387
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
     Region          1..387
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makekfertk phvnvgtigh vdhgkttlta aiatvlsskf ggeakkydei daapeekarg
       61 itintahiey etanrhyahv dcpghadyvk nmitgaaqmd gailvcsaad gpmpqtrehi
      121 llarqvgvpy iivflnkcdm vddaellelv emevrellsk ydfpgddtpi ikgsaklale
      181 gdkgelgeta imnladaldt yiptperavd gtflmpvedv fsisgrgtvv tgrvergvik
      241 vgeeieivgi kptvkttctg vemfrklldq gqagdnvgil lrgtkredve rgqvlakpgs
      301 itphthftae vyvlskdegg rhtpffnnyr pqfyfrttdv tgsielpkdk emvmpgdnvs
      361 itvkliapia meeglrfair eggrtvg
//
LOCUS       WP_175836354            1070 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia anthina].
ACCESSION   WP_175836354
VERSION     WP_175836354.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..1070
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=115073
     Region          1..1040
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mferlirfai ahrwlvmlai aavaalgvys yqklpidavp ditnvqvqin taapgysple
       61 aeqrvtypve tvmaglpgle qtrsisrygl sqvtvifkdg tdiyfarqlv neriqeakdk
      121 lpagiapamg ptstglgeiy lwtveadrna rkpdgtryta adlrelqdwv vrpqlrnvrg
      181 vtevnsiggy vkeyrvapnp aklmsygltl advvralern ndnvgagyie krgeqylvrv
      241 pgqartvddi anivltnvgg vpvrmkevgq vdigrelrtg aatsngeevv lgtvfmlmge
      301 nsrsvakava akmddvnrtl pagvqaipvy drtvlvekav atvkknlleg ailviavlfl
      361 flgniraali talviplsml mtftgmvnak vsanlmslga ldfgiivdga vvivencvrr
      421 lahaqavagr pltrderfae vfgasqearr alifgqliim vvylpifalt gvegkmfhpm
      481 avtvvmalaa amvltvtfip aavalfiger veekenrlmg warrayepvl aafmtrparv
      541 mlgaaaivvv tlglatrlgs efipslnegd lavaalripg tslsqsvemq ksiektlkar
      601 fpeiervfar tgtaeiaadp mppnlsdgyi mlkpadkwpd pnkprdqlvr eieealealp
      661 gnayefsqpi qlrfnelisg vrsdvavkif gddmavlnrt geqiaaalqk vpgasevkve
      721 qttglpvltv nldrdklary gvsvadlqds vaaavggqka gtlfqgdrrf divvrlpdel
      781 rsdieaikrl pialpapaag vsaplaaapy vplaelatid vapgpnqisr edgkrrvvvs
      841 anvrgrdvgs fvadareqlq qdvrvpagyw vswggqfeql qsaserlklv vplalfmvfv
      901 llfvmfnnvk dgllvftgip falsggvvsl wlrgiplsit aavgfialsg vavlnglvmi
      961 sfirnlrddg mpldaavreg altrlrpvlm talvaslgfl pmafatgtga evqrplatvv
     1021 iggilsstal tllvlpvlyr vshavswraa lrggfgtgvl rrlgffkgna
//
LOCUS       WP_175836357             133 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease, partial [Burkholderia multivorans].
ACCESSION   WP_175836357
VERSION     WP_175836357.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 133)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 133)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 133)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 133)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         <1..>133
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          <1..133
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 lvlipfwtsv lvrvaawivl lqneglinka ligsgllahp lallfnrvgv yismthillp
       61 fmilplysvm ksipptyqra avslgshpfa afwrvyvpqt ypgvgagall vfilaigyyi
      121 tpallggpnd qmv
//
LOCUS       WP_175836384             517 aa            linear   BCT 11-JAN-2025
DEFINITION  S41 family peptidase [Burkholderia anthina].
ACCESSION   WP_175836384
VERSION     WP_175836384.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..517
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55185
     Region          69..433
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mmpatrvvrr iaawstgaaa aaafvacasa araqsasapa atlppasppa aasqpspcpp
       61 dwepqlcelk aavevlkkqh ltdvdigall datvhdgikt lpyarffnak erqqqldder
      121 rardgtpgig ivfetrpdgl hiidvipdap aeqagvrpdd lvvamngqsv vgidssdvvk
      181 lakgdagvpl kltvqrgphh ttltfapvra ivkphpatak rldgdilytr lssfpepavg
      241 syidavqtar ragppvkgvi ldlringgga lnaaigital fagrdrtamv tlerdgtkrr
      301 rfttnwpdye lpvmhgqdpl aplqaddwwr tvplvvlvdg qsasaaeata aalkdlgrar
      361 llgmptygkg laqtgvdlid gtrlnftfar nlrpngcpmd gygvvpdwlv pprrdsdvdg
      421 vllwyrevdl arapyadrla pdpfaqvrta rqklrdarar akvdtsksaa lpqrafgtaa
      481 dwqlrqalda lagrpvqtid ppaqlmparp vcergds
//
LOCUS       WP_175836391             469 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175836391
VERSION     WP_175836391.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..469
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50289
     Region          14..467
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mnhpatpatt rrplppamld alraafgerv stadavrahh grdespfdpq lpdavvfahn
       61 adeirqvvsl calysvplip ygagsslegh llavrggvsl dlsemnrvls inaedltvtv
      121 epgitrkaln ealrdtglff pidpgadasi ggmtatrasg tnavrygtmr envlgltavl
      181 adgrvvktgs rarkssagyd ltrlfvgseg tlgviteitl rlhplpeavs aaictfptmg
      241 davrtvieti qigvpiarve fvdalavrsi nrhsnltlte aptlffefhg teagvkeqae
      301 lvqalagqns gqgfewatrp edrtrlwaar hnayfamlql kpgcravttd vcvpisqlaa
      361 cveetevdlr asslpcpivg hvgdgnfhva ilidpdkpee ldeaerindr iveralrlgg
      421 tctgehgvgl hkmrflpkeh gdnaidvmra iklaldprnl mnpgkiftc
//
LOCUS       WP_175836416             450 aa            linear   BCT 11-JAN-2025
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Burkholderia anthina].
ACCESSION   WP_175836416
VERSION     WP_175836416.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..450
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=48663
     Region          80..450
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 msktkttglp gltsalknkl iqqalerklr eagreqpaaa paagrrtaas vpeaytrfdq
       61 ypgyrqlrim sdgaarlgvr spffklhegt agaqtsiggh tyvnyasyny ldmsgdpvvs
      121 qaakdaidry gtsvsasrlv sgerpihrel eralaelygv ddaitfvsgh aanvttigyl
      181 fgprdlvihd elihnsvlqg iqlsgakrfs fahndadale qllteqrhqf ervlivlegi
      241 ysmdgdypdl prfvdikrrh raflmvdeah slgvmgktgr girehfglag davdiwmgtl
      301 skslagcggy iagetalieh lkflapgfly svgmpppvaa aslaalrrml elpervatlq
      361 argqyflaqa kaagidtgss agiavvpail gsslratkws dalfeqginv qpilypavpe
      421 qsarlrffis cihseaeidq viagmrrlla
//
LOCUS       WP_175836364             743 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia anthina].
ACCESSION   WP_175836364
VERSION     WP_175836364.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..743
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79846
     Region          48..743
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mtvnrttasp arrrraqvgl gvglgitlfa aqaaaapgda papdadasgs atlpaitvsg
       61 ergsafrvrn asvaglddtp lrdtpasvsv vtraqiddqq akrlsdvvrn dasvvndyap
      121 vgyyegfair gfpvdlasai ridgltvsge qnvplenker veilkglagi dsgvvapggv
      181 infvtkrsan vasvttgvds rgstsaavdl grrfgpdnqf gfrinaaken mhsyidgtng
      241 rrtfgsiaad wdispraslq lnaefqqwiq rsapgyqllg gtvvpsvntt skalgtqpwa
      301 kpvttdalnl narfdyqfnd dwkayiaagr srtmiddnsa fpygcsyaps caagttspff
      361 fgangdydvy dfrspgeyrr nddlravttg kfatgplqhe ltlgvsvqrr vvhmadavyd
      421 yvgsenvygp dvtfapspns agpsypqlda wqygvfgldr isigehwqvl aggkevllrq
      481 rswdsldgea thtdrsvflp qvalvykpvk vlslyasysk alslgdqapv ratnayaflp
      541 pveshqfelg akydwldrls ltaavfsisk pfqfadpdas gtrytfvqrg terhqgielg
      601 aagrlterls ltasvaaira raydsgspay eghqvinvpa lraslyadya vpgvaglnml
      661 ggveysaarn aneegtarvp swfvfnlgar yttkigghrt vlrvsvdnlf nkfywrdage
      721 qqgdaylfpg aprtarvslt ydf
//
LOCUS       WP_175836443             121 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia anthina].
ACCESSION   WP_175836443
VERSION     WP_175836443.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..121
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=11933
     Region          59..>120
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mksivlralg vaavaacltg svyaqssdaa ateapaaats spkaaaktak kanrklgyav
       61 rkaitkdggv nvsnlvvrsk ggaitlegtv peqaqidkae aaakgvkgvt svankltvqq
      121 q
//
LOCUS       WP_175836500             520 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175836500
VERSION     WP_175836500.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..520
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=55136
     Region          54..512
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 miskeaikrg ynrgnyvvga htpppyslnl pgagdapvaa gmqrapvavs pqqidalrav
       61 addvlaqpad vvawtrdwwa asmvaetggr patphavivr vstveqvqav mriahaatlp
      121 vtasagrsnv tgaalpvrgg ivldvcglnr ltgvdaesqi vdveagmfgd vfeetlqreh
      181 gltmghwpss fgistvggwi acrgagqlst rygkiedmvf gmdvvladgr lvtlggysra
      241 avgpdlqqlf igsegtlgii vrarlklhrl pdygraiayg fdtfaaglda creilqrgan
      301 paalrlydal esgvqfalpd tnvlliadeg aremvdavma istgvceagg rrldgeaife
      361 kwldtryltg ksaegfkrsp gfvadtlemc grwrdlaaiy rdvvaalqav pgtlagsahq
      421 shayadgacl yfslrgdvev aeraawyraa wdaanavliq ynaalshhhg vgllrspymr
      481 dslgtafpvl qsvkraldpk gilnpgklgl ddetgphvdr
//
LOCUS       WP_175836505             462 aa            linear   BCT 11-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Burkholderia
            anthina].
ACCESSION   WP_175836505
VERSION     WP_175836505.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..462
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47624
     Region          40..459
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mqpasparsa pqgldatdps hdlvygpndr papmvafvaa lqhllaiivp ivtpgllicq
       61 algvssrdtt livsmslvis giatfvqckr fgplgaglli vqgtsfnfvg pliaggsvmv
      121 kqgtpvetvm aaifgvviag sfvemsvsri lpfvkrlitp lvtgivvlli gltlikvgli
      181 smgggysama ngtfasagnl tlsclvlgti illnrvpivw vrstalvial vigyiaaavl
      241 grldftgvhq aalfqvptpl hfgigfswsl fipmliiylv tsleaigdvt atskiskepv
      301 egpvwmqrik ggvlvngans llagmfntfp ssvfaqnngv iqitgvasry vgiwiagmlv
      361 vlglfpvvag vlqavpepvl ggaamvmfga vaasginils gialdrrall iiavslalgl
      421 gvsqvpdiln slphalknvl esgvatggic alvmnwflpe qk
//
LOCUS       WP_175836541             837 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia anthina].
ACCESSION   WP_175836541
VERSION     WP_175836541.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 837)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..837
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=91928
     Region          36..763
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mtpstdnldi paraginihq fysldikgap vaaladiyaf dgacgigept qytirfthph
       61 hdlsrgefln rigafviqpp prdrwsqpes arrvqgvvtg falkatnrdq slyevvlesr
      121 lallrnapkc rffldktipe iieqilrehe fnqifarfef qlhrtyrkrg fvmqwgeddl
      181 afitrlcrrs giwfvceege hceqvrfgdd yahyrrdper ltvayrphsg leaggvesis
      241 alemhaktls aayivrtfnt emaisepiea vspirddrtt ygeayswgmp nqseddakee
      301 aqlrreaalt gqvayrgecd mldltpgsvl klsnrtlsda khgllvvrvt cgatrknayh
      361 vkfdaipsdr qyrmplmeet wpridgvitg tiassggwkd pyldgqgeyi vdlhldrdtr
      421 vpglqscpmr lakpfagpnq tgfhfglveg tvvgvsflwg cvdlpfishv lhtaqhtdpi
      481 vagapwgtrn tirtrsnntv elddregqeh vkvatehgkt qlnlgytvdr dqrlrgdgfe
      541 lrtddrghvr agggllvssd rqekaigqss dtrpmtnqfa ltqaqaqglt daaavahaei
      601 adlkaenawl kdelanlkta vialsapngi glatqgrvmv sagkdvsvgt ssrfnvnalr
      661 nvaiaagevl slfahkfgik lyaargkvqi qaqsdamemv aqkdmritsa dgtttvnaan
      721 gvvlggggta yikvqgdnve iggagclilk iieiqkegpg alslplpkfd qieianderf
      781 ilsdditgrp ivnrpykiql asgqiiegvt sdkgetslsr qdvarglkll lqnnkea
//
LOCUS       WP_175836582             261 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia anthina].
ACCESSION   WP_175836582
VERSION     WP_175836582.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..261
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=27083
     Region          9..241
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 merkplvgit adltqigaha shtvgdkyva aivdgalala mvlpalgdrq svddvletvd
       61 gllftgsysn vephlyggep sapgtkhdpa rdattlpllr aaiaagvpvl avcrgfqeln
      121 vvcggtlhqr vhdvpgladh redddapmdt qygpahavrl tpggvlhtla ggrddvhvns
      181 lhkqgiaqlg sglaveavap dglieavsvv dapafalavq whpewrhaqd plssaifraf
      241 gdacrarrda rtrataaaal a
//
LOCUS       WP_175836596             212 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia anthina].
ACCESSION   WP_175836596
VERSION     WP_175836596.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..212
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23182
     Region          4..195
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mnayrlylsp gacslaahia leetgapfdv eivsvreqqn ldarylainp karvpvlaip
       61 geprvltetp ailtylarry pdarllpldd plrearchew lawlvgwvhg vgygtlwrpg
      121 rfigdpalhg aisehgreli daanasieav ladgrtwaep gghsivdpfl lvlyrwgvai
      181 gldmtkhpaw gahaqreaer paarralare aa
//
LOCUS       WP_175836621             378 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia anthina].
ACCESSION   WP_175836621
VERSION     WP_175836621.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..378
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40224
     Region          1..373
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfqhtedrr mladtlnrfi aeqyafpvrd riaqsaegfd rtmwqrfael gavgalfpea
       61 dggfggagfd iavvfeclgr glvvepflga llagralsla ggaahadrla alidgsasaa
      121 fahdepgshy elttvrtrae rtadgwvltg akgvvdqaaq aaffvvsarv sgqdddaagi
      181 alfvvpadap gvslrdyrki dggraaevrf ervalpadav lgehageaga allervlgyg
      241 llalsaealg amdvakeatl eylrtrkqfa lpigsfqalq hrmadlllei eqarsavina
      301 aaqldaprav reralaaakf sigrigtlva eesiqlhggi gmtwelplsh yakrlvmidh
      361 qlgdedhhla ryialskq
//
LOCUS       WP_175836636             298 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia anthina].
ACCESSION   WP_175836636
VERSION     WP_175836636.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..298
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31004
     Region          1..294
                     /region_name="COG4120"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443296"
ORIGIN      
        1 mslfsflgal eiglifslva lgvlisfril nfpdltvdgs fplggavaat lisaghdpft
       61 stliaivaga lagfvtgwln vrlkimdlla silmmialys vnlrimgrpn vpliteptif
      121 tvlqpdwmpd yvlrpallai vvvvaklgld wffssqlgla mratganprm araqgiatgr
      181 atlagmalsn alvalagalf aqtqggadis mgigtivigl aaviigetll parrlvlttl
      241 avvlgaivyr ffialalnse figlkaqdln lvtaalvtia lvlpatrkkl larkngga
//
LOCUS       WP_175836659             401 aa            linear   BCT 11-JAN-2025
DEFINITION  zinc-dependent alcohol dehydrogenase [Burkholderia anthina].
ACCESSION   WP_175836659
VERSION     WP_175836659.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..401
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42092
     Region          1..401
                     /region_name="FDH_like_1"
                     /note="Glutathione-dependent formaldehyde dehydrogenase
                     related proteins, child 1; cd08283"
                     /db_xref="CDD:176243"
     Site            order(38..40,43,86,162,166,185..186,188..190,209..211,215,
                     229,253..255,303,320..322,345..347,387)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176243"
     Site            order(38,40,60,162)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
     Site            order(90..91,93,96,104)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
ORIGIN      
        1 mkavvfhgig diridtvrdp evahatdavv rltasaicgt dlhmvrgtlg gmkpgtilgh
       61 egvgiveavg rdvrnlrrge rvlipstiac gscvycragy taqcdvanpg gpragtafyg
      121 gpadtgpfdg lqadyartpl anaslirlpd vldddrailm sdifptgyfg aqlaevkpgd
      181 tvavfgagpv gqfaiasakl mgagrviaid riasrlemac aqgaesvdfs eedpvdtvlr
      241 ltggigvdrv idavgvdamr athgpaaadr daarafdaev daiaprrkpd grnwmpgdgp
      301 sqvlqwavra vakagtiavi gvyplqarvf pvgeamnrnl tikmgncnhr titpplielv
      361 rsgafdpasv ltrcepltna idayrafdvr epgwmkvklt p
//
LOCUS       WP_175836667             297 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175836667
VERSION     WP_175836667.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33105
     Region          6..>51
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mprdnlndll vfvavardrs ftraaarlgv sqsalsqtvr dlearlgvrl ltrttrsvst
       61 teageelfqa vaprideiem klaavsdfrd kpagvvrita tdhpidtiiw pkltrvlpdy
      121 pdirvelsvd yglsniveer ydigvrygdq vakdmiavri spdirmamva spayldgrkp
      181 pktpqdlldh dcvtlrlata kgiyawelkk grneiqarvs gritcntqph llqaaldgfg
      241 iafvtedtvl dhvrngklri vmpdwcpvfp gyhayypsrr qasrafsvvv dalrhrs
//
LOCUS       WP_175836681             242 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175836681
VERSION     WP_175836681.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..242
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25462
     Region          1..239
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mtdmiegkva aitgaasgig lesaraliaq gakvvlidra kerleslcae lgpnalalva
       61 dllnpsevsg llpriidlag glnifhanag ayiggevleg dpdawdrmln lninaafrsv
      121 havlphmvkq ksgdiiftgs iagivpvvwe piytaskfav qafvhttrrq lakhgirvgs
      181 vapgpvvtal lddwpkakme ealaagslmq pkevadavvf mltrprnvti rdlvilpnav
      241 dl
//
LOCUS       WP_175836740             404 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175836740
VERSION     WP_175836740.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..404
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42568
     Region          11..395
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(21..22,25..26,29,62,117..118,120..122,125,145,
                     148..149,152,235,238..239,242..244,247,271,275,328..329,
                     333,337,353,356..357,360..361,364)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 migmlcrerr fsvllagnam sqigdgvhef vfvitvlhaa hnnvalagiv yffrfipylv
       61 lgplggalsd rlprralmvf adlsravttg lfcvllaidr vdlvslglig mamtsfrtlf
      121 qpafqgtipa ivktehlpaa ngatqmatem gglvgpalgg vmlatvgnpg fvliidtaty
      181 llstlcvwca iaahtrddas lsqekltirs lygdfgqnlq dalqkrelfv tigysalcil
      241 fvgsalrili pallkgsgys dsmvgyamsf iafgalagav vcskvmrrfd trnlmlywsm
      301 ygialailpa cvvstptifa gcfmlgavga fadvilptni qnlstdanvg rnfslfstla
      361 ntsealsggl aglltlispv ggslvitgll iasvaylgki rvev
//
LOCUS       WP_175836752             314 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Burkholderia anthina].
ACCESSION   WP_175836752
VERSION     WP_175836752.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..314
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31742
     Region          2..314
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtilviaehd nasikaatln tvaaaaevgk fvggdihvlv aghnaqaaas aaakvsgvgk
       61 vlladapqla gdlaenieat vltvaanysh ifvpatacgk niapriaakl dvaqiseita
      121 vvsadtferp iyagnaiatv qssdpikvit vratgfdpva aeggsasvdk ieaaadaglt
      181 qfisrevtkl drpeltsaki ivsggrglgs genytkvlep ladklqaalg asraavdagy
      241 vpndyqvgqt gkivapqlyi avgisgaiqh lagmkdskvi vainkdeeap ifsvadyglv
      301 gdlfvelpgi vaal
//
LOCUS       WP_175836779             262 aa            linear   BCT 11-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Burkholderia
            anthina].
ACCESSION   WP_175836779
VERSION     WP_175836779.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..262
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=27525
     Region          33..237
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 minrtrkaal vtalflaaha ahaatdtvtn pygldalwkg gdviargtll ilvvmsmgsw
       61 yiiiaklleq trvlrrakaa ekgfwkarsl negtrqldag spfrfiaetg laafdhhega
      121 lleqvdlnhw vaaaieratt svssrlqdgl aflgtvgsta pfiglfgtvw giyhaltaig
      181 iagqasidkv agpvgealim taiglavavp avlgynwlvr rnkavmervr gfstelhivi
      241 ltgtttaaaa aaskaatlsr vg
//
LOCUS       WP_175836846             215 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175836846
VERSION     WP_175836846.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..215
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22603
     Region          14..129
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          80..209
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mkdkpaqgpr gldkdaivaa alalleevge aafsvrklal svgcdpmsvl yhfkskdgls
       61 raianalsrs lvpvdetlpw rerlrdlarq yralalrhpa afallqrhms tgpadlahie
      121 avhralvdag iactalpsvc vgwyasvigl aaaeaggltr pandvelaem nalsdaehpl
      181 vksaaplyaq ldpaavhdtm vdvlldgiaq haraa
//
LOCUS       WP_175836898             484 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia anthina].
ACCESSION   WP_175836898
VERSION     WP_175836898.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..484
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51827
     Region          1..424
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfeslglae plvravnelg ytsptpiqqq aipavlgggd llagaqtgtg ktagftlpil
       61 qrlhtfyaeq rgakravral iltptrelaa qveesvrays kylklrstvm fggvsinpqi
      121 dalkrgvdiv vatpgrlldh mqqktidlsn ldilvldead rmldmgfihd ikrvlaklpp
      181 qrqnllfsat fsdeikalad slldspalie varrnttaes vaqkihpvdr drkrellthl
      241 irehnwfqvl vftrtkhgan rlaeqltkdg isamaihgnk sqsartrala efknstlqvl
      301 vatdiaargi didqlphvvn fdlpnvpedy vhrigrtgra gatgeavslv cvdekqllrd
      361 ierlikreip qeviagfepd ptakpepiqq rrgqqprggn sggggggnrq praggsgqpa
      421 akrdgnaqpk aaktakpraa ggasgnagns gggrpaagng arpangnaah anrnrssrsg
      481 qrgh
//
LOCUS       WP_175836905             310 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175836905
VERSION     WP_175836905.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34264
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrlgdirlf veaaelgsls aagrklsltp aaasarlakl eaavatrlfd rstrqlrltd
       61 egrlylngcr qalqalddan allqagrhvv ggrvrlsats dfgrrrlldw ldeftarhpd
      121 vtfsltasds tvnlwqdeid lairfaappd galvarrlaa drrvpcaaps fierhgeprd
      181 phdlarfpcn vitvasgpmn twrftrgddt qtctvplata fetndgglar ewalrgrgiv
      241 lnsiwdvadd iragrlkvll pdwrhqsapl haiypgkrym aprvrvlldf lverfareea
      301 ahddllnacr
//
LOCUS       WP_175836923             311 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175836923
VERSION     WP_175836923.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..311
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32757
     Region          25..302
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mntpatpsas sgaeqlapva ppvldivari aecapelrea erkvaafila dlaraahasi
       61 galardaevs vatvtrfaka vgcrdvrelk vlvaqaaavg qrflvpsddg paddsspasv
      121 vydeirvala hnhqllrnts fdaaadllag aqmiyvygqg ggstaladel rfrlvrfgrp
      181 vasyqdsllq rmvsatlsrd avvvalsvsg rvpellescr lakrygakli aitapaspla
      241 kladhlipvv afetdfiykp stsryammma idvlvtgval rlgdagresl rrikhaldah
      301 rgggdrqpvg d
//
LOCUS       WP_175836929             268 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Burkholderia anthina].
ACCESSION   WP_175836929
VERSION     WP_175836929.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..268
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29101
     Region          12..193
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(15,17,98)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(42,97..98)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            96..98
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mskqhassth lvlipsynpg akvdttvrna raqwnpvwvv vdgstdgsae rlqamaerdp
       61 glrvivlpen rgkgaavlag ldaaaasgft hvltmdsdgq hpaqlipdfm aasqaapdam
      121 vlglpkfdas apqlrvqgrr lsngwadlet lwagigdsly gfrvypvapl aaimhrqpwm
      181 rgfdfdpeaa vrlcwagvpp irieapvryf geheggvshf hygrdnalla wmhlrlfagf
      241 varlpmlvar rltrrsrspl srspgrgd
//
LOCUS       WP_175836965             362 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia anthina].
ACCESSION   WP_175836965
VERSION     WP_175836965.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..362
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40009
     Region          9..332
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mgngkpagri lviridflgd mlcttaflge lkqrwpdael hvvanrynaa alagnpdvht
       61 vhtyvysrqc erndrpgrmr affdrlrlvr rlrrlrfdlv vvpnggmhrs siqfarqlgv
      121 kdsrwhdads efddrkpehv atrpmcheal sgfrlvpelg rtdldglvls vhpdralqdt
      181 wyrllgprtq prvglfvsnk aaerrwpveq wcelarrlap fadvivfrdp agmadadrda
      241 wrdvdarhvt pssvaeltaa aslldaivsa dsapvhlasa lgvpvaalfe drpekylrwh
      301 plgvphmilr agatvdaigv daleravrhl lnpaghqdap tsdamplpva asgdreagai
      361 as
//
LOCUS       WP_175837126             252 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Burkholderia
            anthina].
ACCESSION   WP_175837126
VERSION     WP_175837126.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..252
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=27369
     Region          5..252
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 msyarieksg avstvilnrp erlnaisgdl lddlhqalve vnaddgcnai vftgagrafc
       61 agddlkefgk qtesdasirs hveriqqitr dlmfngkpvi gavhgfavgg gfewllncdl
      121 vvasedlvcf fpemewgqfv tggvtqllpq svghqramel wllgerqsar qlhalglvnr
      181 vveagkvvdt arelatrvae rsvfsvsrlk rlltmelstd ltrsleleqs atvaafatpd
      241 aarrvqafaa rk
//
LOCUS       WP_175837038             243 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175837038
VERSION     WP_175837038.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..243
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27086
     Region          63..238
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <187..238
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mptssvpadh eaadwqralr acvdafdafa spsaivfyrl dqsgepadfe lfgmpesmhr
       61 tyiaryrmld plhpsrcaag eravvtlasq lpeerrdasa ywtrflrrhd vadvveiwlr
      121 deagrtvgaf sllrfgngea hgnstagrfa pgevdalarl qpvaeaalgp llrarrgihr
      181 igceerltyr eeqiarlvrd grsnkeiard lalgqptikt hlmrmyrklg vsnrtelvga
      241 lfl
//
LOCUS       WP_175836995             834 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia anthina].
ACCESSION   WP_175836995
VERSION     WP_175836995.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 834)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 834)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 834)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 834)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 834)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..834
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87839
     Region          1..834
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mtardwrage ltllvlalvl avaaltsvgf ladrlrqgle rdarqmlgad fvvradhpvd
       61 psfdreahal glrtattaif psmiaaaagg qasdaaptrl aavkavspgy plrgaveivp
      121 agvaaahkas aipapgtvwa dpalldalhl ragdtvrvgl rtftvaasis reldrgfsfv
      181 nfsprlmmra delaatglvg ygsrvtyrll vagdpqavar feayahgrvd ggklrgvgle
      241 slqegqpqvr qtldrarhfl tlvalltall aavaiamaaq rymrrhldgc atmrclgvsr
      301 rtlgalfale fvgigvvsgv agallgyggh wallaalgsl idvvlpaptl wpalvgigaa
      361 lvlllgfalp plapltrvpp vrvlrrdwgd asrtawaaya igvvlfagll ivaagnlklg
      421 livaggfaaa lvgfaliarl vlyaaaravr narvaagigw ryalaslhrr gtasalqita
      481 lalglmclll iaitrndlva gwrestppda pnqflidiqp dqrddvaawl vahgvrdaap
      541 apmvrgrlva ingkpvnpda ypsdearrlv drefnlsytt elpsdnriva gdwfgtsatp
      601 qisieaglak tlkvkpgdvl rfdvtgltvd apitsvrkld wgtfrvnffv lmpppvlkdf
      661 pavyltsfhl padraalldp liarypnlta idvapilaql qrmmlqvvga vqflfaftla
      721 agvlvlytal agsrdervre aallralgas raqvnavqra efivvgalag alasagaiav
      781 gwvlasrvfd frlavdpwlv pagiaagvac aaaagwlslh nvlrrpalqs lrda
//
LOCUS       WP_175837165             257 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175837165
VERSION     WP_175837165.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..257
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26761
     Region          17..254
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mttdqpdpsh laspspvera frllrfiaeg gstanlsdia rqidvnrvtv krlldsleaa
       61 eliephpsgg syrlglpflt laasalgttd ltararqilp glvaktglsa ylvvlegtei
      121 vyllgetpdt plvsrirvgs ripahratpg lamlasldsa alraryanpv dhrdapdwdt
      181 lastldavrs sgcawsfsgl eagidscaaa irdskgavla alsiagpdsa fsanpslrei
      241 veanvkaaaq tlsrssl
//
LOCUS       WP_175837169             146 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydroneopterin aldolase [Burkholderia anthina].
ACCESSION   WP_175837169
VERSION     WP_175837169.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Illarionova,V., Eisenreich,W., Fischer,M., Haussmann,C.,
            Romisch,W., Richter,G. and Bacher,A.
  TITLE     Biosynthesis of tetrahydrofolate. Stereochemistry of
            dihydroneopterin aldolase
  JOURNAL   J Biol Chem 277 (32), 28841-28847 (2002)
   PUBMED   12039964
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..146
                     /product="dihydroneopterin aldolase"
                     /EC_number="4.1.2.25"
                     /GO_function="GO:0004150 - dihydroneopterin aldolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0046656 - folic acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16453
     Region          23..133
                     /region_name="FolB"
                     /note="Dihydroneopterin aldolase [Coenzyme transport and
                     metabolism]; COG1539"
                     /db_xref="CDD:441148"
ORIGIN      
        1 mkpfdepfva iesprlrgrg wsvfvdelkv parigihahe hespqpivid arlgyrceps
       61 eqgewidydg ycarlasfls hkphtrllet lvadigvlsf rewpaleslt lsvykpkirp
      121 gtkrvgvsld wtrgdylrwt gaagql
//
LOCUS       WP_175837171             370 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia anthina].
ACCESSION   WP_175837171
VERSION     WP_175837171.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..370
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39453
     Region          17..347
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(36,38,69,111,239,300,321,323..325)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(36,38,69,111,113,120,187,190,192,239,246,300,321,
                     323..324)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(38,113,187,190,192,324)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            192
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mkqlfvpvra gqdapqlfap vrvgrytlhn rlvmapmtrs raafdgtpga waaeyyaqra
       61 glglivtegt qpsddgqgyl ttpgiytdah vagwkavsdr vhardgrlfi qlmhvgrmsh
      121 pdntphhrpg vapsavapgv pmftatgmqa ipapraltta evrdtvndfr vaarraieag
      181 adgveihgan gylvqqffap nantrtdeyg gsienrarfa levaaaiade igadrtairl
      241 spgttlwgid egpdsadlyr hlatqldalg laylhvmhqg ddalladlre rwhgtlilnr
      301 pgrardaiga dvaagvadle aygqmvlanp dfvtrvktga plndaqrdtf fggdargyvd
      361 ypvlsgavag
//
LOCUS       WP_175837174             392 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia anthina].
ACCESSION   WP_175837174
VERSION     WP_175837174.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 392)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..392
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39955
     Region          168..370
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mtdraagsar rvtldkvgil igvltivavf glpfmvlrpn riaagtglsv faalpavhga
       61 alatlwivga lwamtasrpa wrlaagcawl atlayavgaa athvvapddm larvspaagv
      121 wlllfawavl vadalarlaf gpwrrlaalv vaiaaisvpl asgwwdglsv mreyavrsdd
      181 fwreairhvs laggsvaaal vaglplgiac ariapvrtvv mpvlnivqti psiamyglmm
      241 aplgllaarv plaaalgirg igvapaalal flysllpias svvvglaqvp ehvseaaram
      301 gmtrvqrllr vdlvlalpvi lsgvrivlvq nigltavaal iggggfgtfi fqgigqsaad
      361 lvllgaipti alalaaavvf eaattlakgq sa
//
LOCUS       WP_175837212             416 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175837212
VERSION     WP_175837212.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..416
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43112
     Region          24..402
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(34..35,38..39,42,74,129..130,132..134,137,157,
                     160..161,164,236,239..240,243..245,248,272,276,329..330,
                     334,338,354,357..358,361..362,365)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mtaplpdsss psplpanlfr hapfqrfwgt rvmsslafqi lsvaigwyvy althsafalg
       61 lvglaqfvpm faltlvvgqv adrydrrria ticqsieala agvfllgaaq gwlvasgvya
      121 laavvgtara fespsvssll pavvprsdlp ratalstsan qaaqilgpaf ggllygvgap
      181 vafgtsvvaf aiaamlsgti plrsappare pvtlrsvfsg iafirrepai lgalsldlfa
      241 vlfggatall piyardilqv gpwglgalra apavgalagt lwltrfplkg rpgramfggv
      301 iafgiativf glsrhfalsl valaalgasd vvsvvvrlsl vqlrtpddml grvsavnslf
      361 igtsnqlgef esgvtaawwg apaaivvgga atiavaltwm kmfpqltnmk slereq
//
LOCUS       WP_175837262             369 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175837262
VERSION     WP_175837262.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..369
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38977
     Region          1..365
                     /region_name="LhgO"
                     /note="L-2-hydroxyglutarate oxidase LhgO [Carbohydrate
                     transport and metabolism]; COG0579"
                     /db_xref="CDD:440344"
ORIGIN      
        1 meqtdcvvig agvvglaiar elaargreti vleaadaigt gtssrnsevi haglyyprgs
       61 lkatscvrgr dllyefcdth hvphrrvgkl lvatsaaqvk qlkaiaaraa engvfdllpl
      121 trtdaqalep alecvealfs patgivdshq lmlallgdaq rhgamcalks pvesidvlrg
      181 grfvvrtggd apteieaacv vnsaglgaqa larrtrgldp rwvpplylar gnyfslsgra
      241 pfshlvypmp drvglgvhlt ldlagqarfg pdvewvdalr yevdparaqa fyasiraywp
      301 alpddalqpa yagirpklag pgeppadfiv qgaaqhgvrg lvnlfgiesp gltaslalaq
      361 rvgdmtsha
//
LOCUS       WP_175837319             106 aa            linear   BCT 11-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Burkholderia anthina].
ACCESSION   WP_175837319
VERSION     WP_175837319.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..106
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=11834
     Region          <5..>89
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Region          20..50
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          55..82
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkaglalndl nraielgytd psayctlati yleggayqks ldyfdqalkl npdqpfvyfn
       61 rarayetpgd iktsiadler glpynpdddm lsakikervv qlrtrp
//
LOCUS       WP_175837341             392 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia anthina].
ACCESSION   WP_175837341
VERSION     WP_175837341.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..392
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44600
     Region          7..390
                     /region_name="COG3146"
                     /note="Predicted N-acyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:442380"
ORIGIN      
        1 mkheridyrt gilsspsevp adewnaller daqptpflrh efldalhvar cavddtgwsp
       61 hfvtltdart grlaaaapvy akqhsygeyv fdwawadayq rnglsyypkl lcavpftpvq
      121 gtrllaaddd arrrlaatll afaeqsdvss lhvlfptgde aqlfesmgmm lregvqfhwi
      181 ndgyrnfddf latleqkkrk niraerrkvh dagvtfrrlt gdmitdadwr ffsrcyrqty
      241 rehysspyln ldffraigat mpenlllvia qadgkpiass lavyrrgang ggtlygrywg
      301 alehvpclhf etayyqllef cieagldtfe ggaqgehkla rgflptvths ahwlahpafs
      361 davarflere tehihayvde lrehdpfrrs ae
//
LOCUS       WP_175837397             238 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Burkholderia anthina].
ACCESSION   WP_175837397
VERSION     WP_175837397.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..238
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=25573
     Region          6..223
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mdlesilysq gfgsrrqcrg liesgrvtva gasatdpdas fdtdgfvftv ddtawpfhah
       61 aylalnkpag yecsrdpqhh asvfsllpap lvargvqcvg rldqdttgll llsddgqfvh
      121 aytspkrkvp ktyvatvrhp lddaqltalr agvqlhgepk piaavaadar dthalaltvl
      181 egkyhqvkrm vaaasnrvea lhresiggft lpddlapgaw rwlgeadlsa lrnpvktl
//
LOCUS       WP_175837389             309 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175837389
VERSION     WP_175837389.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33773
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..294
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdkldqvrif lqvaemgsfi kaahaldvpr atvsaavqql etalgtrllh rttrqvqlta
       61 dgalllergr rllaeadeld rlfrrrdrdv igrlnvdaps riarrviapa lpslfrrhpk
      121 lqlslgstdr sidlvqegvd cairvgrlad sslvvrplgq fvlincaspd ylrecgvpeh
      181 pdalahghwa igyaspttgr elaweycadg grhtlalpsr vivnnaetyi asciagmgli
      241 qiprfdvahl ldsgalvevm pgyraapmdv savyphrrhr srrlnafiew fgelmadaln
      301 dtgaaaggd
//
LOCUS       WP_175837453             298 aa            linear   BCT 11-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Wolbachia
            endosymbiont of Litomosoides sigmodontis].
ACCESSION   WP_175837453
VERSION     WP_175837453.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Litomosoides sigmodontis
  ORGANISM  Wolbachia endosymbiont of Litomosoides sigmodontis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     A novel family of ubiquitous heavy metal ion transport proteins
  JOURNAL   J Membr Biol 156 (2), 99-103 (1997)
   PUBMED   9075641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440813
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Wolbachia endosymbiont of Litomosoides
                     sigmodontis"
                     /db_xref="taxon:80850"
     Protein         1..298
                     /product="cation diffusion facilitator family transporter"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33114
     Region          1..292
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
ORIGIN      
        1 mtavhngkhs vaeskrliys iiivaitmft eiaggiisrs lallsdaghm ltdlfalvls
       61 wiahkfsakk sdlqrsygyh rlqiiaafvn gltlfliami iiiesvkrsi fpvniewkim
      121 liiatlglia nisvffilhn kcesninirs avlhvigdil gsiaailasi iimltgwqiv
      181 dpilsifvsv lilnsgykil knsyhilleg tpdgisaeei kskiiselpe vvdvhhihaw
      241 slsdnyfiit mhakvkenaq htnilyeikk illdkfeiah stveiehdec adnkiikh
//
LOCUS       WP_175837491             103 aa            linear   BCT 11-JAN-2025
DEFINITION  HU family DNA-binding protein [Wolbachia endosymbiont of
            Litomosoides sigmodontis].
ACCESSION   WP_175837491
VERSION     WP_175837491.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Litomosoides sigmodontis
  ORGANISM  Wolbachia endosymbiont of Litomosoides sigmodontis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Wolbachia endosymbiont of Litomosoides
                     sigmodontis"
                     /db_xref="taxon:80850"
     Protein         1..103
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=11420
     Region          1..96
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 mskediinkl kqacssqdve itksdlskvf dalmkiikgk ldkegeirlh gigtfstais
       61 qekqcrnpqn geimtvpqkt rvkfkasqtl lsilnkekee vvs
//
LOCUS       WP_175837494             362 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia anthina].
ACCESSION   WP_175837494
VERSION     WP_175837494.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 362)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..362
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39957
     Region          1..361
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtaflqiqrl rktyddvvai dqvsldvrkg efmtflgpsg sgksttlyiv agfqeptdgr
       61 vlldgkslls vapnqrhigm vfqrytlfph ltvgenvafp lrvrrrpead irakveqmlk
      121 lvhlaecrdr mpaqlsggqq qrvaiarala ydppvllmde plsaldkklr eeiqlelrri
      181 hqetgvtily vthdqeealr lsdriavfnq grieqvgtge elyanpasrf vasfignsnf
      241 lplkvtkhsg grmsgvlpng letasdvfhs tlavgdegal mirpeqmrls slqraggaag
      301 lpvtvrdvty lgdamhyava tpwqqeisir mpaahrhdsg ivigaqalvd wdardvrlfa
      361 qa
//
LOCUS       WP_175837512             196 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Wolbachia endosymbiont of
            Litomosoides sigmodontis].
ACCESSION   WP_175837512
VERSION     WP_175837512.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Litomosoides sigmodontis
  ORGANISM  Wolbachia endosymbiont of Litomosoides sigmodontis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Wolbachia endosymbiont of Litomosoides
                     sigmodontis"
                     /db_xref="taxon:80850"
     Protein         1..196
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=21513
     Region          30..188
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mrliislsla iflitqsgct tlmiggvvat ataitmqdks lgnivddttm airinkellk
       61 hglfssikvr vsegrvllig nvdtpdkqlt aekiawqqke vkevineirv tpiqatsild
      121 ttvdgmitae irtrllgkrn iksinysint vegvvylmgi aqnkaelkav taiarkvkgv
      181 kqvvsyvryr hsklrh
//
LOCUS       WP_175837584            2833 aa            linear   BCT 11-JAN-2025
DEFINITION  RHS repeat domain-containing protein [Burkholderia anthina].
ACCESSION   WP_175837584
VERSION     WP_175837584.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 2833)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2833
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..2833
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=297714
     Region          1526..2616
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mpadstnsqi pairtfqfds tnvgdlsssv nlfrgdinft qtllsmpgrt agdnldltls
       61 llyqsnvhes aitwnrdapt salglgwsmp aptivlndag slmpatrsyc yvsqsistdl
      121 arepttpfvf pmagaladsl anggtvppai vaafganglv lsaasrvsst gasawqladd
      181 anqqlynlal dgatlnvfdg gesyqlvnye fwkilyyacy erwvivkdng lrlsfgglsa
      241 kvghyaasvg nsiewgvrwa ssngpsgpss apvalwqgss gstdgqyqya rawhlstvsn
      301 pwgdgiayry ndwprtsagl lpnveqcvga gglpytkacy ltgmtdvfgr kvvlqygdkv
      361 wanttpqspr eyadphkavp dtqpnayqdr yetlylqria vadasgaplf sftfayrpss
      421 paggadspva nvtsttgalf gdtckrfltg valsnaages lpglgfdyyf datatgaspg
      481 alksityseg atatyvytkq aldicdrsls vspptgtafa gatprvffgk gyavvtwygt
      541 asgalsvevy swlgswrkwq ptsdsvlfrn stgldlstle vvacedffal sfapgsasns
      601 ttvyifqadn arpaqwipan ingvvtgynt psltyaspsg svsltggdtf liaattdvvr
      661 ettsydrvtw rwpnaawtve hftmqalala vacneyylll dmqgnvslfa ldaclnwnat
      721 prtpianfsa sspssvtlgp sdsfvavsnl lstsdtqisy tvtivqwdal yrpvlpmtth
      781 tfddrvdsed pgvqriagsi gnelvavagh vlrfngktwl enntlqadta ptgleqryay
      841 gpdyalrila ypngggdtta qvlsfdpntd fgawtrqpat ptqalpidfs etsnwpsggg
      901 tdwltlgqyl yfrgdacewd gvvghtpcad iqarvnealg gdgnyvlnae avideaprfl
      961 ayfvsdstsp esdqaaatll rngrvsisaq afaqeriyta degdvgagty pggagmfvay
     1021 pgadgnfdna sriilhsyag davegrlhhy avtglsidng lgqtsatcfa pepataacdp
     1081 tgqvfkyyts vvypgtgdps rpqfgrtvnr ylnglnvrdg sdfydmldgq lhqvdtydtt
     1141 gallastttq wkvyvaraas ptdasagtln lkggflcrtt qttiedgvts sqtaryvadg
     1201 ftapfsgnvv gtdtttyggt gqletfrntt lyayqmndpa paaallaqhr fgdiaqsvth
     1261 wrrdggeavv sqasastyal fpcvydgvvv paqagkfirs adgrvpfpft graagaapqg
     1321 wlpstatlay tpygqptetr damgvaqstl ygtdsafava lftnasverg ecayygfesy
     1381 etgsgwnvng crpvvgdaht gttslalapn gegtvsvqla panvdatyll gfwyktpagf
     1441 tpvagagfta tlsidgvagt prvapfadsg gtwvyrtlgi pvtagqsgvt lavaaanass
     1501 dvvlldnvfv tplvskmtvr vydpsyrlls atldaagttl rrrynpfqrl tatigtdqqv
     1561 ktmsiaflsr egnaggrfda aapnadlsvs pdlggtletf ltgdewrqrw aasnvatnwr
     1621 caggalqhta atndtltwqg gnfggastta fyteiaaqga lagvvgvtfg agyaiaydpa
     1681 vgfsftapdg stvqaplgap pnlpvqwllv lgngrvaffg dgqllfstsv nagdpaairl
     1741 stgpnpltlt nvamlagvrl avafrdgagr krqtqqwvgs davvsatiad algrtiaitr
     1801 sapasfggga tqplfgyras fvdvgaflaa tqdtwamtgd vadyyagqnd gvasrsndeg
     1861 ypyfgyrfea sprtrrieqg apgktyavhd lasttsaqrq ttqiafgant agafdlpany
     1921 vaqtvtgpvk nqvlrlrdth grevgssmsd stgvvsgqsl asvdfsatgs ttsisepnsf
     1981 tnapqqdpaa yvsalqrdga grtlestdtd saetaflcdr ssrvrfvqpa ldpdtlgfiy
     2041 fkydalgrvt eqgtvaqpwd asalsthasd pgwpggdvpf tvvrrndydg ngndptqigr
     2101 ktgsvaynla psniagarpv qvnesftyda ngrvtvatla vdgqpaasga igyaynnldq
     2161 ivsiaypsss planvyyryd qaahvtgigs spttptdias yaytpdgdve qeirnggtla
     2221 aaygyaspgw pvsqtvavag rgsasfsmgy gyyangapqs rtislafdtp ststtafnyd
     2281 aqgrlldasv dagatgseqv gqydangniw sltqdgaqay afvhtagtnr ldtltidgga
     2341 stsftydarg nltgtgtmtl aydtatnmvl gvaaanggmt qqfayngvdq rvmrwrggat
     2401 qadvyfnglg rrpllallgg twstfvygpt glvaavsdqr yfplkdaaqs iwavvdsrnq
     2461 lvarfayrtf gslassdgpn qaavpfrfmg reyddasgly nfsarlyspg lrrflsadpa
     2521 rqtaspylfv gnnplvfadp sgnkmtvgeq vgigvgmaal mvaglvlsff tfgaaeapva
     2581 vleegmadgl aagevggevg gnaladggaa sastpscfni tlsttsklaa tsanfltqvt
     2641 tntmfgvgfs gfeydcrpgn eftrkgfaqs leigaasgal fgamsfgyat laadaikaip
     2701 slaartgirm lvnvtegiaa ndltqmatng iehkpwslgl aeatwtgavg glpfgigdvl
     2761 lndgktmwdq arsqfsdrvg sarvgepvps glpgsqaqde kmplirarad ssdgthllss
     2821 pslnasygtm etq
//
LOCUS       WP_175837596              58 aa            linear   BCT 11-JAN-2025
DEFINITION  CsbD family protein [Burkholderia anthina].
ACCESSION   WP_175837596
VERSION     WP_175837596.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..58
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..58
                     /product="CsbD family protein"
                     /calculated_mol_wt=6326
     Region          1..56
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 mnkdqvkgri teakgklkev vgkvmgnrts rltgkaeqiv gktqasfgda kerlkkrr
//
LOCUS       WP_175837696             360 aa            linear   BCT 11-JAN-2025
DEFINITION  GTP cyclohydrolase II [Wolbachia endosymbiont of Litomosoides
            sigmodontis].
ACCESSION   WP_175837696
VERSION     WP_175837696.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Litomosoides sigmodontis
  ORGANISM  Wolbachia endosymbiont of Litomosoides sigmodontis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Ren,J., Kotaka,M., Lockyer,M., Lamb,H.K., Hawkins,A.R. and
            Stammers,D.K.
  TITLE     GTP cyclohydrolase II structure and mechanism
  JOURNAL   J Biol Chem 280 (44), 36912-36919 (2005)
   PUBMED   16115872
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Ritz,H., Schramek,N., Bracher,A., Herz,S., Eisenreich,W.,
            Richter,G. and Bacher,A.
  TITLE     Biosynthesis of riboflavin: studies on the mechanism of GTP
            cyclohydrolase II
  JOURNAL   J Biol Chem 276 (25), 22273-22277 (2001)
   PUBMED   11301327
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10089835
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Wolbachia endosymbiont of Litomosoides
                     sigmodontis"
                     /db_xref="taxon:80850"
     Protein         1..360
                     /product="GTP cyclohydrolase II"
                     /EC_number="3.5.4.25"
                     /GO_function="GO:0003935 - GTP cyclohydrolase II activity
                     [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009231 - riboflavin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41658
     Region          164..357
                     /region_name="GTP_cyclohydro2"
                     /note="GTP cyclohydrolase II (RibA). GTP cyclohydrolase II
                     catalyzes the conversion of GTP to
                     2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'
                     phosphate, formate, pyrophosphate (APy), and GMP in the
                     biosynthetic pathway of riboflavin. Riboflavin is the...;
                     cd00641"
                     /db_xref="CDD:238348"
     Site            order(167..173,182,184..186,193,195,197,215,217..218,
                     220..224,226,233..234,237,250,252,260..261,264..265,
                     267..268,271)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238348"
     Site            order(211..216,218,227,229,232,253..256,263,267,270,277,
                     289,291,312..314,317)
                     /site_type="active"
                     /db_xref="CDD:238348"
ORIGIN      
        1 mfignrsrnk veraisevrr gmpiiiydks nyllvtaaei lerdlfnqyk lisdkiyvtl
       61 psskvtcisq nvehgnkrll innfnelfql iscpkedytk elkhsktide caiallkase
      121 llpyalvidm nfkykhemrg wcekndvial dmlfinnfqq nqdvyevcrt slflkqtqrv
      181 niisyrtyng rkehyaivin npgenseplv rihsscytgd lldslscdcr sqlhqaiqim
      241 tdsgngiily lmqdgrgigl tnklraydmq rkyhldtvda nrilgfedde rsfvvaakml
      301 kklsikkiql ltnngrklse lkdndievtk clplimerni ynnsymetkf srlghelrvl
//
LOCUS       WP_175837776             481 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia anthina].
ACCESSION   WP_175837776
VERSION     WP_175837776.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..481
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51401
     Region          1..430
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Region          <403..>476
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
ORIGIN      
        1 msfaslglie pllrnlqnln yqtptpvqak aipavlsgnd vmaaaqtgtg ktagfalpll
       61 qrlvqhgpav ssnrarvlvl vptrelaeqv lqsfveygqg ldlrflaayg gvsinpqmmk
      121 lrkgvdvlva tpgrlldlnr qnavqfdqve tlvldeadrm ldlgfareln avfaalpaqr
      181 qtllfsatft ddiramaasi lrnpvnisvs ppnataskik qwvvpvdkrn kpelfmhlva
      241 ennwehalvf vktrngvdyl aamldeagya vdtihgdkpq parlralerf karevqmlva
      301 tdvaargldi ddlplvinvd lpivaqdyvh rigrtgraga sgvavslvca deapqlaaie
      361 alirqtlrre eepgfeaehr vpetsatgqi ikkpkkpkkp kmpqavpsam pasgkkprpq
      421 ggegkrkpag qsaaaagkgk svisgspfsv qkprakpagk paagarkpaa kpaggagkrr
      481 p
//
LOCUS       WP_175837819             300 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175837819
VERSION     WP_175837819.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..300
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30768
     Region          5..273
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mkhqigligv glmghgiarn ilkhgypltv vehpgnqpld ellrggvrtv ktarelarea
       61 dvvilcvtgs peveavltge qgvlaglkdn aivvdcstav pestvrmarl veaaggrlvd
      121 apmtrgakea hegrlnllvg aapslfdeir pvlacfaeni trvgelgagh smkllhnfvs
      181 lgtiallsea vacakrsgvd tavladvlan gggggvalnr lrpflasgdt sslpfhmana
      241 fkdlsyysam aegadaahai asavtdtyrd avasagahcp vlklsdvlga tgtaddgear
//
LOCUS       WP_175837908             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175837908
VERSION     WP_175837908.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32393
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..295
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(103,107,146,160,164,230,247,274)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(104..105,109..110,112..113,116,120,122..128,191,
                     221..224,228,235..236,239)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mqvdlgdlna fvavarakgf regartigas asglseavrr leaqlgvrll hrttrsvspt
       61 eagerllarl apalgevqaa ldvvntfrek pvgtlklnvp tsaarlvlps iiprflsayp
      121 eirlevvade sfvdilaagc dagiryderl eqdmiavpig prsqrfataa apdylarrgc
      181 pahprelldh aclrgrfasg ampaweyern gevvrvepsg plvvqiggav dlvvdaacag
      241 lgivylyedw lrphlasgal kpvldgwwrp fsgpylyypg rrfvpaplra fvdfiktdag
//
LOCUS       WP_175837926             203 aa            linear   BCT 11-JAN-2025
DEFINITION  SCO family protein [Wolbachia endosymbiont of Litomosoides
            sigmodontis].
ACCESSION   WP_175837926
VERSION     WP_175837926.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Litomosoides sigmodontis
  ORGANISM  Wolbachia endosymbiont of Litomosoides sigmodontis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Wolbachia endosymbiont of Litomosoides
                     sigmodontis"
                     /db_xref="taxon:80850"
     Protein         1..203
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22902
     Region          43..178
                     /region_name="SCO"
                     /note="SCO (an acronym for Synthesis of Cytochrome c
                     Oxidase) family; composed of proteins similar to Sco1, a
                     membrane-anchored protein possessing a soluble domain with
                     a TRX fold. Members of this family are required for the
                     proper assembly of cytochrome c...; cd02968"
                     /db_xref="CDD:239266"
     Site            order(76,80,161)
                     /site_type="other"
                     /note="Cu(I) binding site [ion binding]"
                     /db_xref="CDD:239266"
ORIGIN      
        1 mikfvrllss iivalsvvfl gycyftkkgi fapavihnvg vkvggdfslv nqdgqvihss
       61 dfkdkymmif fgfssckkvc pmnlgiisei lskldkkinn klqtffitid perdsierlk
      121 efqqqfdhri qmltgerkki devianykvy tskvgeeein hssiiyligp ggkyvahfaa
      181 dlnsdesqsd kiaaeikkyi nel
//
LOCUS       WP_175837941             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175837941
VERSION     WP_175837941.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33512
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..288
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mfdltslalf vraselgsls raaqqshmsl stasrrisll ehhfrvvlln rtvagveltp
       61 ageallrhat dlllrtdaiy selsdytkgs igrvrvfani saisqdlpdq lrafsqryrd
      121 iklqiselrs sdilqalreg radvgivtsr tategihlap ycmdrasvvv pedyslagds
      181 idfnallehd lvalddrsel trsivreaal lgksvrfrvq vqsfeamcrl iaagqgigil
      241 peravalfre pmhlrfirln apwanrimsv girtgavpqp trklfeflas fapaslaagd
      301 tgpsnn
//
LOCUS       WP_175838043             294 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia anthina].
ACCESSION   WP_175838043
VERSION     WP_175838043.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..294
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31537
     Region          12..270
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 msasiktllt presdignlv vrrvlparaa rlvgpfiffd emgpavlpag sgidvlphph
       61 iglatvtylf dgtlmhhdsl gfrqkivpgd vnwmtagrgi vhserspded rplaqpvhgi
      121 qtwvalpveh edtepvfvhh aadtlpsftr dgthvrviag tafgltspve vfsptlyaya
      181 aftaggtlal daehdergvy lvdgdltidg tplapatmav lepgarvala sangarvmll
      241 ggahlpgerf iewnfvsser akieaarnaw aaqtfgkvpg eedqwtrqpe rnah
//
LOCUS       WP_175838092             449 aa            linear   BCT 11-JAN-2025
DEFINITION  NCS2 family permease [Burkholderia anthina].
ACCESSION   WP_175838092
VERSION     WP_175838092.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..449
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46307
     Region          14..443
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 msatdtmpar tpanwlerrf alaargtsvr tetiagitsf laaayllvvi psllatggme
       61 rgaattatii vfvlfttlmg lyanlpflvg pgiggsviig vtlattehvg wqtglgiacv
      121 sgvlffllti fgargvvmrl ipvqiklglg asiglfvtml glrnagmvva nvktnafalg
      181 dfsrpgalva liglavaivl qarkvpgail iailvaaaag vplgvthlpa sfmslphsia
      241 piafkldirs altlaaapyl faffaaeffs tlgtalavga kanlldeqgn lpninrpflv
      301 dslaatlgpv fgipaltali esaagveagg rsglsslaaa vlfaamllfv pvalaipkea
      361 tapaliligl smfatirhth fddftdalpv msmvlltlms nsfgtgiagg llcyvlvkll
      421 agrwrdvswg lvvlalplgy yfwtvvkph
//
LOCUS       WP_175838118             227 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia anthina].
ACCESSION   WP_175838118
VERSION     WP_175838118.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 227)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..227
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22639
     Region          27..113
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          134..218
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mndsfdtrrr rfaplllaaa allagrayad datlgktlat qgsttgvaac igchgaqgeg
       61 naaagfprla gtnaaylsaq laafadgsrq npvmqplakl lsaherdavs ayfaslpapa
      121 aiaagtasie pantgawlat rgrwsdglpa caqchgaggl gvgtafpslv gqpaayiagq
      181 lnawkhgtra pgpmalmpmv agklsdadid avaayyargg attgdkq
//
LOCUS       WP_175838146             666 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Burkholderia anthina].
ACCESSION   WP_175838146
VERSION     WP_175838146.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..666
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70963
     Region          1..460
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          598..662
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(620,629..631,638)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            630
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mfdkilianr geiacrvaat ckrlgiasva vysdadanak hvaacdeavh iggsaaadsy
       61 lrieriieaa ratgaqaihp gygflsened fahaceaagi afigppvdai aamgskaaak
      121 almhaaavpl vpgyhgddqd aaylhreade igypvllkas aggggkgmrv versddfpaa
      181 lascqreaas sfgndrvlie kyltrprhve vqvfgdthgn tvylfdrdcs vqrrhqkvle
      241 eapapglhdd vrqamgeaav aaaravnyvg agtvefimtg eafyfmemnt rlqvehpvte
      301 mvtgldlvew qlrvasgepl plkqeelrvq ghalearlya enpargflps tgtlkhlrlp
      361 qgvefaigap vrvdsgvreg daitpfydpm iaklivhgad raealgrmlr alracevvgl
      421 htnaaflqri vacepfaiad ldtgliernh dalfapqqpp ratlalacaa lfarerdaaa
      481 regaspwrsl pdwrlnggyr rtldwhapdr eadvtvtyed ngggariaag daaaqpfawm
      541 rgatpldfdv tldgvrssgr vyadgdsfhv ftqgvaetle wrnvlahagd vehgggrlta
      601 pmpgkviavl vepgqkvetg tplivmeamk mehtigapga gvvaevlygv gdqvadgaql
      661 lvmaed
//
LOCUS       WP_175838271             268 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175838271
VERSION     WP_175838271.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..268
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28739
     Region          24..259
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mrelrpsrss dasergstst vsnrslergl ellrafgsga tllgngdlve ltglpkatvs
       61 rlartlveag ylehdpvrrg yrlglpllgl aqalrssstv lqaaaprire taqslhinvg
      121 iagpdrddmv ylesiryspr aslrtvvsgq rvpmaltslg raylaslpds acarqlaalr
      181 rnrqswpqir saiddavasv hslgfcvasw qpevvalatp leiaghrtla lnfsvrtlda
      241 pssvaerlsa rllklrdeiv aatlqlds
//
LOCUS       WP_175838307             369 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia anthina].
ACCESSION   WP_175838307
VERSION     WP_175838307.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..369
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39631
     Region          18..332
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mfspdsfppg papapwaltd dqrnlyiasq rfardrlepl lagspsvaaw qetvrlaaat
       61 ldlgamvlpe eagglgidrh glalvveala agpleralel tltapalmvl rmhnalgpvl
      121 trpvqayfdg ttaialsvpg idnatiwqlg plgdtvtltm riddkrrlll terprdqrps
      181 rstgiatlgt lvleqlhsde aaaetplavi tradsdsvpp aqtymteigl ylavlltgam
      241 qhsirfafdy astrqafrkp lashqlaaar lsdmliathg thlflqavsa arpsapvslv
      301 rqllrhvvae svsvsrefvq lcgghgyveg lppaarfqtg hwfafllqri daalswlaep
      361 rvaneevdg
//
LOCUS       WP_175838324             291 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            anthina].
ACCESSION   WP_175838324
VERSION     WP_175838324.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..291
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30534
     Region          3..278
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 matilnilsy vsilalvalg laiifglmdi vnlahaewvt igaytlavaq slggphafwl
       61 alfvapmvga vlgwflerlv irllydrpld tllatyaisl ivqkalelif gthpmlvyap
      121 ingavpvpgg sypayrlfvi gvaavvttgc wllftytrfg tqlraviqhp amaeavgidt
      181 rrlnrlafcg gaalaslagv lvapmisves hlgvaylaka ffvivlggig siagsllgsa
      241 fvgtaetlls yrvdpslasa ivlvlsivli rfrpqgllpg fsaahqlhgk g
//
LOCUS       WP_175838326             357 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            anthina].
ACCESSION   WP_175838326
VERSION     WP_175838326.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159223
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..357
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0015658 - branched-chain amino acid
                     transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37109
     Region          54..325
                     /region_name="TM_PBP1_LivM_like"
                     /note="Transmembrane subunit (TM) of Escherichia coli LivM
                     and related proteins. LivM is one of two TMs of the E.
                     coli LIV-1/LS transporter, a Periplasmic Binding Protein
                     (PBP)-dependent ATP-Binding Cassette (ABC) transporter
                     involved in the uptake of...; cd06581"
                     /db_xref="CDD:119323"
     Site            218..236
                     /site_type="active"
                     /note="TM-ABC transporter signature motif [active]"
                     /db_xref="CDD:119323"
ORIGIN      
        1 mlrqllasar rwlfqpaigi edispmaiga aivaaalvlp fclgsyllst vrdalimgll
       61 alsydllwgr agvltlghtt ffglgaygfa iatvqygqts avgvivglvc alvvaavlgy
      121 fllfagvrlh ffaiismavl ivvqqlatsw qsvtggdtgl lgipglsfsp vgqtldlsgp
      181 rgswytvvtv lavllvatwl vcrsrygkvl taiatnewra kacgyhtsgh lllvfvasag
      241 laaiagtlma acsgvvapdv fspvlatevi lwvaiggkgt lggpvlaavg ltllkqtvss
      301 attdgwplll galflccvlf lpngvrlggl iagarridri rrgrshlhra erveggr
//
LOCUS       WP_175838469             596 aa            linear   BCT 11-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Wolbachia endosymbiont of
            Litomosoides sigmodontis].
ACCESSION   WP_175838469
VERSION     WP_175838469.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Litomosoides sigmodontis
  ORGANISM  Wolbachia endosymbiont of Litomosoides sigmodontis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Wolbachia endosymbiont of Litomosoides
                     sigmodontis"
                     /db_xref="taxon:80850"
     Protein         1..596
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=66740
     Region          67..276
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
     Region          210..385
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
     Region          416..595
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mikflililv gyscygnevn dvknpvsdfl dtlhkikyms yskkdfakfl vqchkegtqe
       61 dfkkgfghnl ngadfsklyl ngsifngvsl igadfshtdl sgvsfinsdl rganfsnanl
      121 qgikikgtnl sfakfvsanl tdiifdqsdi scaefvssdl kkvrmhnmtg lhanfldvkm
      181 sffslldsnv gyvnfsdsei nntivqrsil dnanflgvds yklkiqfssl knaniygaei
      241 kesdftgsnl snvclnssti idsnfsranl sktqisyvnd dnssfvqsml sdskvkysyv
      301 sqvsfqdadl fnidfsfsel hqvdvsdsdi rygkfrdtrv ahsnmngsff dhslftfaki
      361 egtdlsstsm ykvkvrdsqv ynsrlfynsi dsseienstf fnliasnsnw stlkvtssnf
      421 vknnfessll rdntfektsf flsnfsnsti sdtsfhsssi ykgsvidahl vnckfdhsil
      481 idnkgqekla glesaitsie klqekilqge kfnvnysyfe fkdmnlrnvd fsnsilsrak
      541 finvnldkan leksdlrhai fnnsslidtn lsgsnldhss ffkadlksai lenvks
//
LOCUS       WP_175838487             277 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175838487
VERSION     WP_175838487.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..277
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30476
     Region          84..269
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          211..267
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 msaalstpdl plshvafvtn tlgdiaqaig tpqfmravyd tlvryvdfda vhldyercaa
       61 sgqrsigwig sfgrepelva qvmrhyyrsy asedvtyaai dsdsdmqllq vssqrvesel
      121 rhlffdagdi hdecvitgvt ggtrysisia rsrrlpsfsl kelsllkhls evvlpmasah
      181 krllgavcad egprdeldld lvaqwlpelq erltaremhv casfiqgmts aaiaqamglk
      241 tstvdtyakr afaklgvdsr rqlialvlrn asrrhaa
//
LOCUS       WP_175838496              84 aa            linear   BCT 11-JAN-2025
DEFINITION  cold-shock protein [Wolbachia endosymbiont of Litomosoides
            sigmodontis].
ACCESSION   WP_175838496
VERSION     WP_175838496.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Litomosoides sigmodontis
  ORGANISM  Wolbachia endosymbiont of Litomosoides sigmodontis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 84)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Wolbachia endosymbiont of Litomosoides
                     sigmodontis"
                     /db_xref="taxon:80850"
     Protein         1..84
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9353
     Region          1..82
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mefgnikwfn aekgygfikp evngsdvfvh istlersgir pdslrgenke rgikgervsy
       61 elkeergrng egkksainlk llgd
//
LOCUS       WP_175838499             237 aa            linear   BCT 11-JAN-2025
DEFINITION  DsbA family oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175838499
VERSION     WP_175838499.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..237
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25583
     Region          6..209
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(14,17)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 mkrlpvkity dficpwcwig hrnlvsalkd vaeaaepdia ylpyelnpsm pssgvdrkey
       61 rtrkfgswnr slqmdahvaa agrvagldfn ydkvaitpnt lrahrlmafa qgkgdpkrtd
      121 dlfeaifaay ftrgenigdv dvlvnvasgv gfdadevref lasrrgeddv lakevdaqsa
      181 gvrgvplfti ggatingaqp thvlkevmda eirtvapedv gldeadgcsg gsckfgg
//
LOCUS       WP_175838522             295 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175838522
VERSION     WP_175838522.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..295
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31498
     Region          8..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..292
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mridpyslel fisvvqegsi araasrnhia psalsrriad leaamgipll irspsgvelt
       61 eagrhafsra vsvhdqlqsl arevqslsge vagvvrlhan asaivgflpe rlkafqaryp
      121 lvqialteei sdevvracvd eradvgisac gklpgglesw hfvddplmvv lpldhelaal
      181 aaptfrdvlr fplvalqagg sldrtlkera daarmpltls vtvnsfdaqc rmveaglgig
      241 ivptsaasaf agsngfvrrp ldepwarera lhvhalrkss rlravqalid alagt
//
LOCUS       WP_175838602             241 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Burkholderia
            anthina].
ACCESSION   WP_175838602
VERSION     WP_175838602.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..241
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26467
     Region          1..239
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 misisnvtkr ygqfqvltec ttevrkgevv vvcgpsgsgk stliktvngl epfqqgkilv
       61 ngqsvgdkkt nlsklrskvg mvfqhfelfp hlsitenltl aqvkvlgrgk deandkgmkl
      121 ldrvglkaha hkfpgqlsgg qqqrvaiara lsmdpiamlf deptsaldpe minevldvmv
      181 elaqegmtmm vvthemgfak kvahrvifmd kgaiveddrk ddffsnpkse rakdflakil
      241 h
//
LOCUS       WP_175838607             280 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia anthina].
ACCESSION   WP_175838607
VERSION     WP_175838607.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 280)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..280
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29961
     Region          32..277
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mnalllrapm pgrlgrvtgv latlvlllaa lpiltmitms fgaagtlefp prefslhwyr
       61 aawqtfvssd agsaqsmgaa lttslvvava tmliatavsv paayalsryr frgktlveql
      121 valpivyplv mlglallivf nalpvelgiv rlvvahvilt lpftvkncaa svasigpdfe
      181 eaaclmgasp rralvdvvlp lmrpgilagm lfafivsfne ftvtfflysi dtmtlpvwly
      241 srtvssldpt vfcfavftva idfaliwmle klvgdkgval
//
LOCUS       WP_175838608             307 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia anthina].
ACCESSION   WP_175838608
VERSION     WP_175838608.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 307)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 307)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 307)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..307
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32127
     Region          32..304
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 maslpsprda vpaaapagta agagpalpgv ppwlllapil aflavlaaat vtvlrmsvgv
       61 sgdewrtftl qnyldladpy fttslwltlr lafqsmvcav llaipvalam artesrlarr
      121 lllagvllpl lvnlllqgyg wlvilgpagl lnrallatgv igrpllllyr ehgvllgliq
      181 tafplavlpl ssalravsra ydeaaatlga srwqtlrhvt lplampglvs gallvfayna
      241 safavplllg grrvpmlavl vhdqvaplln wpaasasgvv lmgatlvvma vsqrlvrtlq
      301 radevtr
//
LOCUS       WP_175838611             163 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia anthina].
ACCESSION   WP_175838611
VERSION     WP_175838611.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..163
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17323
     Region          1..144
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mytnimvavd gspsskrald eglkmagssg arlfavfvvd ksllityagr ldpdalldev
       61 rrdgaavlrn aertishaav ngeteiiete lgqdiaerlq ryvversidl avigthgrrg
      121 vrrlllgsva erflrgsscp vllvrsndva qaagaaarhr aag
//
LOCUS       WP_175838645             357 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia anthina].
ACCESSION   WP_175838645
VERSION     WP_175838645.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..357
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39174
     Region          1..357
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mstivsfknv qktydgetlv vknlnldieq gefltmlgps gsgkttclmm lagfetathg
       61 eillqgkpin ripperrnig mvfqsyalfp hksvaenlaf plkvrkvaks dietkvmral
      121 rmvnmekfah rmpaqlsggq qqriavaral vfepalvlmd eplgaldkql reqmqyeikq
      181 iheqsgltvv yvthdqgeam tmsdriavfn ngiiqqlaap selyekpena fvarfigesn
      241 elngvvssld hqrcvvrldg ghaihaspng giqlsgntsv slrperiavg eqargcdnvf
      301 dagvkdliyy gdhlrivmqv cgrndfivkl pndgaarnlr vgdsvaigwm adacral
//
LOCUS       WP_175838624             247 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175838624
VERSION     WP_175838624.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 247)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 247)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..247
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25481
     Region          2..201
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mkivviggsg ligsrvvtll geaghqalaa sprsgvntit gdglagaltd advvvdvana
       61 pswepqavld ffrtsarnlg kaevaagvrh hvalsivgcd rmpengyfaa kvaqeeaiea
      121 agvpytivra tqfmefiggi adfgteggtv rigdglfqpi aaedvsalva qvalagplng
      181 tveiagpdra pfaeivaryl ksvgdtravv tdrdaryygg rveeqslvpl gsarlgrigl
      241 dqwlars
//
LOCUS       WP_175838674             155 aa            linear   BCT 11-JAN-2025
DEFINITION  nucleoside deaminase [Burkholderia anthina].
ACCESSION   WP_175838674
VERSION     WP_175838674.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..155
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16943
     Region          1..149
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 msqketylvd sirlamenvr erktwpfgav lvrdgkvlar svnevdatcd psahaemqav
       61 raaskalgst dlsgsvvyas gypcsmclsa mylagvsevy yaysnedgep ydlsaargyv
      121 eiarpleare mklvyhrard egqdlyeawq avqag
//
LOCUS       WP_175838706             220 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia anthina].
ACCESSION   WP_175838706
VERSION     WP_175838706.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..220
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23989
     Region          7..192
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mpqdrhltly hsprsrsvga rmlleelgad yelhafdlst gkhhepdyva vnplgkvpal
       61 rhgdvivteq aavymyaael ypeaglspap gdalrgpylr wmtfygscfe palvdrsmnr
      121 asaaystspy gdfdavinvi atqldngpyl lgerftaadv lwasalnwtt mfklvaetpr
      181 mrayidrvfa rpaiqraqaa daalaaehdk areaaatags
//
LOCUS       WP_175838682             251 aa            linear   BCT 11-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Burkholderia
            anthina].
ACCESSION   WP_175838682
VERSION     WP_175838682.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..251
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26229
     Region          1..251
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlttqrkkvi ldalardgqv lavelsvqfg vsedtirrdl relaaegllq rvhggalpas
       61 pavapfaqre alepeekhri arraaqmiap gqvaivdggt tsallvsqlp pdlrativth
      121 spsvavalaa hpsidvilig grlykhsivs vgaaamegia rihadlyfmg vtgvhpiagl
      181 stgdfeeaai kralaeraae tvvlasqskl raasqfvige lalaqtivve retdaaltep
      241 ieatgvtvvr a
//
LOCUS       WP_175838820             235 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175838820
VERSION     WP_175838820.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..235
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25362
     Region          18..228
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mpsslapylp pleahpwfaa lppelrtqll eraalrrlpa ghalfrrgdp pcglyavlag
       61 sltigavdah gkealltvae pvtwfgeial fdgqprthda ialddtlllh vpqaallgil
      121 dttpqywrqf allmaqklrl sfltveamsv mpaaqrlatr llmiangygg isagrtrirl
      181 sqeklasmls ltrqttnqll kalqadgivr lhvgeielvd vdalrrasgl pdgma
//
LOCUS       WP_175838823             520 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Burkholderia
            anthina].
ACCESSION   WP_175838823
VERSION     WP_175838823.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..520
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54731
     Region          38..520
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mtspdrssap ldvaallaal pdriadvpar waarapahpa liedarrlsy gelaqavdaa
       61 agrlaslgvr ggdrvmivae nsvaqivllf avarvdawal mtnarlsage fdaiathaqp
      121 klivftteas pdarahaary datpagalpv digtwshrld anapdepvaa dsaaqcaali
      181 yttgttgapk gvmlshrsll fiaatsstlr rvspddvvyt vlpvshvygl asvclgslya
      241 gatlrlaprf speavrvala negvtifqgv pamhaklleh lhthahawha prlrfaysgg
      301 spldadlkar verrygvplh ngygmtessp titqtpldap rtdcsvgvpi pgvemrlvap
      361 dgtdvppgev geirvrgpnv mlgyyrnada traavspdgw lstgdlarqe adgavtiagr
      421 skeliirsgf nvypveveqv lnahpdvvqa avigravegn eevlafvelm pgaaateaal
      481 hawcadrlap ykrpahirvl dalpaastgk vlkhklrela
//
LOCUS       WP_175838837             369 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia anthina].
ACCESSION   WP_175838837
VERSION     WP_175838837.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..369
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39623
     Region          1..358
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masvllrnia kryddtevlr nvnldiadge fvvfvgpsgc gkstlmrmia gledissgdl
       61 lidgakvndv psakrgiamv fqsyalyphm tlydnmafgl klagakkpei dqavkqaaki
      121 lhidhlldrk pkqlsggqrq rvaigraitr kpkvflfdep lsnldaalrv kmrlefarlh
      181 delkttmiyv thdqveamtl adkivvlsng avqqvgtpne lyhapanqfv agfigspkmn
      241 flkgtvesad atgvlvrfgs getqhvavda aglqrgatvt vgvrpehliv gpaatgvaar
      301 tmaveslgda aylyaesava pdgliaripp ldtyrtgeal hvhaqaehch lfdengqafr
      361 rlgvhakaa
//
LOCUS       WP_175838767             159 aa            linear   BCT 11-JAN-2025
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Burkholderia
            anthina].
ACCESSION   WP_175838767
VERSION     WP_175838767.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..159
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=17295
     Region          1..143
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 matvrvqtdd fdlnaevgal rarnpkigav acfvgtvrdl negdsvaame lehypgmtek
       61 alekiaaeag rrwpgidvai vhrvgrllpl dqivmvatva shrgdafasc efvmdylkte
      121 apfwkkettp dgerwvdart tddaalarwg vesgntppr
//
LOCUS       WP_175838853             293 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175838853
VERSION     WP_175838853.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..293
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32005
     Region          9..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          105..270
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 madapdnllg aylrdrrekl dpaalglpta rrrtpglrre evaqrahvsa awytwleqgr
       61 ggapsadvld rlaralllnd aerehlflig lghppevryh assgvtprlq hvldsldasp
      121 aivrtatwdv vawndaaaat ltdyatlppp arnilrlifv dagmrdaqsn wervarfavg
      181 afradvargg athnvqafvd emrttsaefd amwrdhdirs hdegtkeirh pqagrigley
      241 safsvtgrpd lslviftpvs aadrarirtl vaaraqaqep areparispa paa
//
LOCUS       WP_175838873             567 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175838873
VERSION     WP_175838873.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..567
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=61830
     Region          22..534
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 msktydyivv gggsggcvva grltedpavt vcvleaggrg dsavvnvptg avamlptrln
       61 nwafdtvpqp glggrigyqp rgkalggssa inamvyvrgh rvdydgwaal gndgwayddv
      121 lpyfrlsehn erfddawhgr dgplwvsdlr tgnpfharyl daarqaglpl tddfngaqqe
      181 gvgiyqvtqk hgerwsaara yllphvgrrd nltvethaqv lrilfdgtra tgvevrqhge
      241 vrtlrarrev vlaagalqtp qllmlsgigp agelqrlgip vradlpgvgr nlqdhpdfil
      301 gyrarsvdtm gvsargglrm lrefarfrre rrgmltsnfa egggflktra gldapdiqlh
      361 fvvalvddha rrlhaghgls chvcllrprs rgsitlhstd plaapridpa ffddprdldd
      421 mvagfkltrr lmeapalaqw ttrdlftanv ttddeirdvl rrrtdtvyhp vgtcrmgrda
      481 lavvdpqlrv hgmqglrivd asimptligg ntnaptimia ekavdlmrgv qrtaararad
      541 trcepaeapa hhdaipsqle etrhvva
//
LOCUS       WP_175838882             194 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175838882
VERSION     WP_175838882.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..194
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21554
     Region          2..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 marprefded avldavmdtf wrygyeatsa qdlvqatglg rgslyaaytn kdglfeqaml
       61 rynrrsqenv dllrgpgpvl drlrtllvgv idddlkaark rgclatntai erasrdahva
      121 elvrenfrim ragireaier gqatgeidaa ghaedlawfv fnamqglrvl aktsadkdrk
      181 rlvaivdqtl rvlt
//
LOCUS       WP_175838885             182 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Burkholderia anthina].
ACCESSION   WP_175838885
VERSION     WP_175838885.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..182
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20611
     Region          1..171
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 maedartrlr tlfvakyahl rrrlefivgs rdgaadamqe twlrldtmnd paqianaday
       61 llrmaanvai dqhrreqrhl stgdvdalfe vgdelaepdr ivsarrdiea lqqvldtlps
      121 rqrailvaar idgllnreia erfgiseslv ekelrhalra crdglrqhma ledgstrgrr
      181 kf
//
LOCUS       WP_175838892             541 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia anthina].
ACCESSION   WP_175838892
VERSION     WP_175838892.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..541
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59271
     Region          2..537
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mqhadtvyln gllytgdaqr rfaqalatkd gkivavgrdd dirplagpat rmvdlagrlm
       61 lpglidghvh pleghqilgd fdlsgindpd ailqriraca datpnepwvy lgganlgafg
      121 aypsrelldr ivpdrpllvv gfdvhsgcln tkgleaagit adtpdptggv yerdasgapn
      181 gvvheaafyr vcpiipqlsp agypkslaka hamahgygit gwfdarveea elkayaaaqr
      241 agqlktymsa glyanprrdp reqierfvaw rreyerdnlr lhtvkifvdg vpesktaall
      301 epyagtddcg lalwsqdaln eiclladtag fdlhfhtlad ravrmtldal eyvqirngmr
      361 drraqlahlq lvdpadmgrf nrlgaiasvq tlwtaareeq qqlyrdllga ertarnypfr
      421 slrnagamla agsdwsvstm dpmqiiqtgv thrlidqpds ppwnpherld lltmleaytv
      481 ntayalrfdd ctgsleagkd aslaildrnp fdhpvgtfaq trvletcfrg evvyaapgwa
      541 d
//
LOCUS       WP_175838927             317 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175838927
VERSION     WP_175838927.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..317
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34169
     Region          11..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..290
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mderlrgvae fvdvveagsf aaaalrlgmt rsavakivar leqrlgarll qrttrqiglt
       61 deglvyyeqc rrllaelget eaaldagrre ptgrvrisvp vlfgrqcvap vvrrlveryp
      121 rleidvsfsd rvadlvndgf diavrigala dtsalvgrkl gvqrmgisas payldrhgrp
      181 sgldtlashv giaysrggqp tpwriigadg avhdhrpagr lrfddlqaia daaaagagla
      241 wlpcwlmapy vrdgrlalvm dsestsgaev fvvrpasrhv pskvrvvida fvdeiprmla
      301 sddadgervp prvvpap
//
LOCUS       WP_175838942             329 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175838942
VERSION     WP_175838942.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 329)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 329)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..329
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35060
     Region          14..205
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          237..320
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msepllpdvp dvhdlvsell lgmrlsgvqy rriqvprpfg lsfghapgra qfhfvgrgpv
       61 llrdaagttv qleagdaill phglthalms dpdaacreig gfevakicdt vasvgatsca
      121 ttepgagdal ifsacmeldl ggmqplvgtm pefmhvgtll arypeirpml damerescsa
      181 ragfagilar ladvvaafiv rgwvecgcgd atgwvqalre pklgraival hrdpgrnwsv
      241 aelaaeagvs rsvfaerfla atgmtpvryl telrmrlaaq wiardreaie avayrlgygs
      301 laafsrafkr vvgrppgavr aesdthadv
//
LOCUS       WP_175838932             649 aa            linear   BCT 11-JAN-2025
DEFINITION  arylsulfatase [Burkholderia anthina].
ACCESSION   WP_175838932
VERSION     WP_175838932.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..649
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=69308
     Region          47..615
                     /region_name="PAS_like"
                     /note="Bacterial Arylsulfatase of Pseudomonas aeruginosa
                     and related proteins; cd16025"
                     /db_xref="CDD:293749"
     Site            order(57..58,95,156,158,263,406..407,466)
                     /site_type="active"
                     /db_xref="CDD:293749"
     Site            order(57..58,95,156,158,263,407,466)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293749"
ORIGIN      
        1 miksasplla vrfrvvcaai agalslascg gvdsdpppqa satpeakrpn ilyimaddlg
       61 ysdihafgge intpnldalv asgrilsnhh tgtvcaitra mlisgtdhhl vgegtmgvpt
      121 derrglpgye gylndralsf aqllkdagyh tyiagkwhig sgivgsttgs gqtpdqwgfe
      181 hsyvllggaa tnhfahepag ssnytedgry vqpgqpgqpg gaggspavfy stdfytqkli
      241 syidsnkrdg kpflayaayt sphwplqvpd pwlhkyagvy dagydairna riarqkalgl
      301 ipadfkpfdg lpettaaspa tandgtasak yisavhsaad gyrdygagkv dklwsslspa
      361 erkaqaryme iyagmvenld yniglliqhl kdigeydntf imfqsdngae gwpidsgadp
      421 tatdtangqe pvyatlgtdn gkqnaqrlqy glrwaevsat pfrltkgysa eggvstptiv
      481 rlpgqtqslp tlrafthvtd ntatflavag vtppsqpapp lvntltgvdq nkgkvvynnr
      541 yvypvtgqsl lpvltgsasg evhttpfgde aygraylrsa dgrwkalwte pplgpldghw
      601 qlydvaadrg ettdvsaqnp svvstlvdqw ktymsnvggv eplrprgyy
//
LOCUS       WP_175838955             293 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175838955
VERSION     WP_175838955.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..293
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30170
     Region          10..289
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mststtqqnr tpvavlgigv mgtpiarnla rqgfdvrawn rtrakadala tdgvaafdtp
       61 agavdgahvv vtvlndadsv lqamqaaapa largtpwvqi stvgvrgias laafaqahgl
      121 vfydapvqgs rqpaeqaqlv vlasgpasar arvqpvfdai grrtvwvadd gstgassrlk
      181 lalnhyafal thavaeslkl agllgadprh vidvvsggpm dnayfqakga lilnddfraa
      241 ftivnavkda tliaqaarda gmqadiahas larfqraada ghgdkdmaas flt
//
LOCUS       WP_175838995             293 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Burkholderia anthina].
ACCESSION   WP_175838995
VERSION     WP_175838995.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..293
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30216
     Region          213..291
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mnvpissdav rradrrrlva laygiapagp haatiampsa arsreslkvv altvlvahsa
       61 iivalwhtaa sdtrstlpra laveveagea pktgpavqrr anvvtsappv rahasrdaaa
      121 hrdvrpsvpa prltghakpa qapapaverp dgdvvrttpa pkatptaaai asaetvpaap
      181 asaparavqp appaaepepv taprfaaayl hnpapdypdv aqrrgwegtt flnvhvlang
      241 rpdrvvlaas sghdafdaaa vaavtdwrfv pakrgaqavd gwvrvpvvfk len
//
LOCUS       WP_175839053             574 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia anthina].
ACCESSION   WP_175839053
VERSION     WP_175839053.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..574
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62564
     Region          9..560
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mqnqsthpaa apadfvltha kvytvdphrp waqavavrdg rivyvgdtag vhahvgaatr
       61 vvdaggrlvl pgfveshwhf ettafafqaf vnyedpqkvl galrayveah pdepaitgmg
      121 wvqatippgl lrketldaic adrpvcllst dfhsmwvnsk aleiagidas tppvqegasw
      181 fekdavtgep tglvvdgaay silmqrisaa gllptgidly lksippwqkk lcaagvttvf
      241 dagffdasgd qsllyetlqt meragdlklr vvgsvavige iddpvgtlvk yreqydsplv
      301 karalklfld gteanhtayl lepyadrpdt cgaptmpadt fnrylveadr ananvmvhcv
      361 gdaavrmale gfemvnrdnp prdrrhvith aflthpddip rfrragvman tqlqwgvvda
      421 yteqlrdhyg herwsnmykf rtfveagvtv sigmdglacq crcqhkpleh iesghtrqla
      481 gepdapvfpd iaerlsipql iaaytihgay qlgmehevgs ltpgkradlv vlendlfevg
      541 qydigridva ltmmggdvth vgedfgartg lgar
//
LOCUS       WP_175839030             340 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175839030
VERSION     WP_175839030.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..340
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35967
     Region          9..332
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpqstcpard ivvvgfegvq slditgpmev favanrhlpg hvapyrltla sqhghdivth
       61 aglrlagpta laalparidt livaggseaa lrhaasdagv lpwlrtrmad trrvasictg
      121 afvlaaggwl dgkratthwn qcstlqalcp nvriepdaiy vsdppfhtsa gvtagidlcl
      181 alveadcgap talavarelv lfmhrpggqa qfsvgldvha natpqmrtll agiaddptgd
      241 lgvatlaarm hmsertfarn fvketglspa qfvlaarver akallersdw pleriaqrag
      301 fgsvdalqra fakrvgvspr dyrarfgrpa sadtretpqa
//
LOCUS       WP_175839076             395 aa            linear   BCT 11-JAN-2025
DEFINITION  YncE family protein [Burkholderia anthina].
ACCESSION   WP_175839076
VERSION     WP_175839076.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..395
                     /product="YncE family protein"
                     /calculated_mol_wt=41508
     Region          50..268
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mhpnpfrlrr arllaaltla ttavaahaad wivsgndgky qrvegrdtyl aaapadtltl
       61 ldasvfppkv alqadvengi qgppqavait pdakvalvga ptrydpgakq lvydtflqvv
      121 sldasppavt rielgthpqg iaidrsgrla lvanvdgsvs ilridgthvt ldgnlkigkk
      181 rlagisfthd gkhalvslrd eqgvavlnvd dgkvtdsgtr lstgvapyti dvssdnrwav
      241 vsnvglaglp gytgtlagda dsialidvsr vpfrtvqylt vpslpegvai spngkwiavq
      301 amdgsnltpd npgrhklgkv vlfeirdgra vqvsevpgge aaqgivftad skhvivqfnv
      361 erqlalymve gdklrdtgkr ialsggpssl rtlpr
//
LOCUS       WP_175839087             213 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175839087
VERSION     WP_175839087.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..213
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24065
     Region          20..>116
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdrqlrwgda srmdsvddgr sailratlda miehgidrls iddvarrani srrtlyryfg
       61 tkkeliqgvi gvqnaeffde mqraltgfeh dfeayceesv cfavryrdrh hggfhhnyla
      121 tnlstdvfgy iveniapmwq rvlekpygdy vaahgtqavp alddiialis riglayclvp
      181 adepamraqm rilltfprep agkpvaarmk atr
//
LOCUS       WP_175839098             416 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175839098
VERSION     WP_175839098.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..416
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=44746
     Region          12..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          111..169
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          199..399
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(214..215,217..218,221,225,227..233,328..333,
                     339..340,342..343)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mddtelpnla clyavqrvae tgsvsraaat lfraqsaitr avqalettvg ealfdrkpsg
       61 mlatpvgrav lkrgervcae lgalanwcal rqsrrrasad gglpayllnt rrlqlfstla
      121 rhrhmpsaar tlgvtqpavs sairilesga gfalfhrhpr glllttdget fllhvrraln
      181 elrhvaddva alhgsiqgvv tvgalplgrt lilpeavarv vtrfpkvrvi tdesayealv
      241 agvragdidf ilgalrasdp asdlenervm senlvvlarh dhplasernl glrsladaqw
      301 ilprshspar glfeslfrrm klkppmptve sadlavirgl llhtdmlavl saqqlhyeca
      361 aglltvldvp mrettrdigl mtragsppsp aaralidair vvatevartp hataar
//
LOCUS       WP_175839123             262 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Burkholderia
            anthina].
ACCESSION   WP_175839123
VERSION     WP_175839123.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..262
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28652
     Region          5..255
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mseelkfevd qgiatitlnr pdklnaftea mqetwldale ecrtnpeirv vvmtgtgraf
       61 ttggdvdsfa ssasqtpami ksrvwdgiqr lprkiaeidk pvlaalngla tgggldiala
      121 cdirfaaesa rfaetyvrmg lipgvggayl lprivgmska lemfwtadwv saqdaerigl
      181 vnkvfpdtel mertyafarr vadgaplavq likrvmrfgl dkdlatahel vasnlsivrt
      241 sedhqealsa fkekrtpqfk gr
//
LOCUS       WP_175839107             494 aa            linear   BCT 11-JAN-2025
DEFINITION  PucR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175839107
VERSION     WP_175839107.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..494
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=53362
     Region          6..122
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          225..482
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mitvqelldt pslglkviag aagthrlitw ahavdlpdpw rwvsagnlvm ttgggmphap
       61 kdqvawleri aqtnasalvv apqadapkls rkmlnaadql mfpvlqasfe lefvtlsrhv
      121 iesvlraqrd sfkaserlfq tyaeamrqea dfsgrlaila aahgltlrie daasgtllvt
      181 saktaaaava adadsdadtq hverialggr vranlvirra grtapedplf vrslvgllgv
      241 elerlmitrd aqrdegaall rsllenetdf afvrpmlerr gltgtlvcls irpggaghwt
      301 pgdvrhapgl qdktpllled dgllalapdr rdtidallrn lgdgtvigvs gpiavatgfr
      361 esvrqarlam tqaleletev lrygdvdtgl imapkslaea ralvgrylgp liehdrlhdt
      421 sllatlmkfl endgnwkata ydlgihrqtl vyrlklveql tglkptttng tarfwialla
      481 gknaqllpaq tlrg
//
LOCUS       WP_175839127             264 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Burkholderia
            anthina].
ACCESSION   WP_175839127
VERSION     WP_175839127.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..264
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28030
     Region          6..253
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mtkqlvntai egavlviklc spedrnaltt elreqlgdav klaeknpavr avyltgegpt
       61 fcsggnlnml ktacdpwtvh rrfrnlndwl iplimlnkpv vigvrgqavg gglglaltgd
      121 lliagegakf ipgffrigvm pdigtmyhlp rligmaatkr llftgatlsa qealdlglaa
      181 kvvpdeqvde vglaeatrla ngpaevmgla ktlmarsfet slhdmfafeg fgqvlamsnp
      241 efvegldaal egrradfaha asnq
//
LOCUS       WP_175839138             291 aa            linear   BCT 11-JAN-2025
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Burkholderia
            anthina].
ACCESSION   WP_175839138
VERSION     WP_175839138.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..291
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=31632
     Region          3..283
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 maqiktvgia gsgtmgmgia ivaaragfvt rvydtrqdal drargqaesf lkksaergkl
       61 padavpeims rwhgttrled ladcdvviea vfedlkvkhe lfgaldkvcp phtlfasnts
      121 tisiteiagg sgrpdrfvgl hfclpaqlmk liemspgmnt sdetferawa faealgqrpv
      181 rtqdtpgfil nyflipfnnd airlveqgva epadidkaik talgypmgpm elldlvgmdt
      241 qrllceamyg lthepraacp plirrmiaag rlgkktgrgf htyndtkmfg a
//
LOCUS       WP_175839139             388 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia anthina].
ACCESSION   WP_175839139
VERSION     WP_175839139.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..388
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41947
     Region          12..384
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnileridsr irlsddermi vdsvqalard qiapraaeyd rtgtfpreni dainalglna
       61 mfipdqygga qlsftcyalc vreitkacaa tgiiwatnfh aikplieygt daqkarflpa
      121 vaggalasla itepgagsda tgmkttfred gdeivinggk tfitngdvad lyllfgkwdg
      181 iedpkraisv lilekgapgl svigvedkmg trasgtatls fdncrvpran lvgepgdglr
      241 illgslnrsr psvaahalgi araafedava yinerkqsgr kviefqgiqf mladlasela
      301 lceswlwqva gmidageadf gieasmlkmr asdaamritt davqllggyg ycsdyrverl
      361 mrdakitqiw egtnqvhrql igrsfilk
//
LOCUS       WP_175839141             516 aa            linear   BCT 11-JAN-2025
DEFINITION  tripartite tricarboxylate transporter permease [Burkholderia
            anthina].
ACCESSION   WP_175839141
VERSION     WP_175839141.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..516
                     /product="tripartite tricarboxylate transporter permease"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=55141
     Region          5..496
                     /region_name="COG3333"
                     /note="TctA family transporter [General function
                     prediction only]"
                     /db_xref="CDD:442562"
ORIGIN      
        1 migqtlhdlw ygfsvavlpq nlmwsffgvl vgnligvlpg mgalstiaml lpltytmhav
       61 pallmlagif ygsqyggaig aillnlpshp phavtcidgy pltkmgkggt algitmissf
      121 faasvgivvm ivaspwlvkv afefgpaeif simllgliag stmargsalk giamttlgll
      181 fgivgtdvnt gverftfgfi dlsnhlelva lamglfgvad flrnvnrvhh vgtqakvrlr
      241 dmrpslselk qsfmpmlrgt fvgtlfgaip gtgptittfl ayalerkvsk sperfghgai
      301 egvaspeast haktqvdfip tmslgipgda vmalllgall iqgyqpgpql itehpdlfwg
      361 liasfwignv lllilnvpmi gvwvkvlqvp frymypsalf fiavgvystn nslfevgevl
      421 afgllgavll sldfpvatil lgyvlgpmve enfrrsllls rgdllvffqr pisavfmsic
      481 illvvaqlff awrgardskr gthsdelpsi ggagie
//
LOCUS       WP_175839187             249 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Burkholderia anthina].
ACCESSION   WP_175839187
VERSION     WP_175839187.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26370
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkviaavkrv vdynvkvrvk sdhtgvdign vkmsmnpfde iaveaatrlk eagtatevva
       61 vtcglgqsqe tlrtalaiga drgvlvetda elqplavakl lkavidneqp qlvilgkqai
      121 dddagqtgql laalldwpqa tfashieisd glatvtrevd gglevislkl paivttdlrl
      181 nepryvtlpn imkakkkpld tvtpaalgvd paprlktlkv vepparkagv rvpdvatlve
      241 klkseakvi
//
LOCUS       WP_175839212             251 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175839212
VERSION     WP_175839212.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..251
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27806
     Region          25..233
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mkgtggdsap aeatqtvdrk salgealrrr ivnmelapga lideaalade fgmsrppire
       61 lirqmaaegy ieletnrapr vssmnfqslr sffiaapviy iattqlaaln atpddiarlr
      121 aiqaqfraai asgnvvnrvi yndefhleig riaqndylmp slrrllidha rlgkmfyryp
      181 ttdtmqhtle savvqhdqii dalerqdada agqlvrdhfe lsrrrmteya apqgmavsvn
      241 lgdpvlaqdr r
//
LOCUS       WP_175839216             241 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175839216
VERSION     WP_175839216.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..241
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26809
     Region          25..231
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mkpnlveaer edaqspaldr kavlaqtlrh rilsmelqpg atldevalge efglsrppvr
       61 elmrqmaaeg yieleanraa rvasmnfdsl rnyflaapmi yvgttklaam hatpaeidgl
      121 kriqerfrta vatgsvderv lqndefhlai gkmahnpyll pslcrllidh arlaktfyqp
      181 rdekmeaelv eaieqhdaii daierrdaqa ageivsahvy larrnmasyv apegvdvsid
      241 f
//
LOCUS       WP_175839220             187 aa            linear   BCT 11-JAN-2025
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Burkholderia
            anthina].
ACCESSION   WP_175839220
VERSION     WP_175839220.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..187
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=20446
     Region          41..180
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 mtsftesraa ppddpsragn hpdfadphte lppsiaagfe vrvqhaaida gaelapivrn
       61 pkvgavvnfl gvvrnegdvd dvialevehy ptmteqalws iveeasarwr leavkivhrv
      121 griplghtvv ivvvaaahra safdaceflm dflkthapfw kkeirhdgva gwvepkahdd
      181 qamrrwg
//
LOCUS       WP_175839286             931 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia anthina].
ACCESSION   WP_175839286
VERSION     WP_175839286.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 931)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 931)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..931
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..931
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=97489
     Region          15..875
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msvikefasl fgafnrlysl dgsgalaafq ierwtgresl sdlfqwnvda lstdpaldld
       61 amlgqrvair ttlangtttl rsglvaeaec igydaglary hlrivpwlaa lthardertf
      121 vnqtladvld tvfapyagia rwrltpdasr rldalgpvay rvqyrththy efvqhllaea
      181 gfgfcfvede dapaghtmlv fddsaqlaed dtsarrggvp rrasgtatda ddvvlgigqs
      241 lsltadritl issdyranha ttastnlgrp ngarelyddv gpeafdtlrd aedtarrqad
      301 aivsrasfwt gygtlrtara graltlvdtg wqavrgaaap dafllthveh iginnlpatv
      361 meaierqlgp lpataldprv lrhakaggya nrfdavprtq vwrptladgt gqrlnpvatt
      421 lgaqtaivvg ptgraqpgst gpvhadaqgr lrvrfhwqae ddagtyptra iqrlasdghg
      481 lqqvprighe vlvqfhhgli hrpivlgglf ngrgeggesp spggaagkpl dpsiytqagd
      541 hapsaqgnla sglspawhga gggtdrhnha galsgfksqg fdgqghnqlv tddsdgmgrl
      601 qmatthaatq lnlghlrhqs dnylgsfrgq gvelrsdayg amratrgllv ssyapagaaq
      661 pagdaaalqa llvrhtalvg rfdktadthg tlpfaaqrgv eqagqsslng saapldalaq
      721 sfattvgang yaqasadaaq rstgnalpht gdavlgiear gghgliagqa lqwaagetls
      781 lgsgtdfnla aaqqlrihsg qgigwlagas hadgvgmsli agkdgltlqa qrdvlglrar
      841 ddlklasasa aveiaakqtv hlavsggahv tieggdvtfg cpgkfvvyaa qhsfvgpdqm
      901 ntplpqfpek vcvecllham qsgsalagka i
//
LOCUS       WP_175839369             393 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpP1/FadL family transporter [Burkholderia anthina].
ACCESSION   WP_175839369
VERSION     WP_175839369.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Black,P.N. and Zhang,Q.
  TITLE     Evidence that His110 of the protein FadL in the outer membrane of
            Escherichia coli is involved in the binding and uptake of
            long-chain fatty acids: possible role of this residue in
            carboxylate binding
  JOURNAL   Biochem J 310 (Pt 2) (Pt 2), 389-394 (1995)
   PUBMED   7654173
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Munson,R. Jr. and Grass,S.
  TITLE     Purification, cloning, and sequence of outer membrane protein P1 of
            Haemophilus influenzae type b
  JOURNAL   Infect Immun 56 (9), 2235-2242 (1988)
   PUBMED   2842261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..393
                     /product="OmpP1/FadL family transporter"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40491
     Region          29..393
                     /region_name="FadL"
                     /note="Long-chain fatty acid transport protein [Lipid
                     transport and metabolism]; COG2067"
                     /db_xref="CDD:441670"
ORIGIN      
        1 msslarrnvr lalfatvvaa satsafatdg tyftgngass sgmggaaiaf pqdvasavdn
       61 paglaelgsr vefymvalpv sanstfgspd nhlysrkivv spgfgfnyqi apqwtfgvam
      121 tgagaasnyg rpvlpvpgag dakaslivvn tsptitykpr adlsigaslv lgveqlrlng
      181 ivapgadgal qpvpshgnan algigagvgv lwtpvpmvsv gasyftktwf tslsgykddv
      241 lassgghids psrygagvai rplpgltlam dylriewaga agynsagswg yrsqnvgrig
      301 vayelnpkwt vragysfann nvdsdhtlan mygpgissra vtlgasyaid knnlvtaafe
      361 ydipttiigt gpskgtnira syqgytigyt hkf
//
LOCUS       WP_175839312             289 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            anthina].
ACCESSION   WP_175839312
VERSION     WP_175839312.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 289)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..289
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30475
     Region          3..288
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mnlsalfgql lvglingsfy amlslgvavv fgllqivnfa hgtlymlgaf lawlalerig
       61 lnywaalvvi pllvafigal iergmlsrlr gldpiygfll tfgislvveg mftywygssg
      121 rpysppselr ggidvgvafv piyrlwivaa sllvclstwf liertrlgat mrsatenapl
      181 vqvfginvpv lvtltyagaa glaalagvla apvfqvsshm gsqllilvfa vvviggmgsi
      241 lgaivtgyal giiegvtkfv ypqgasivif vvmavvllvk pgglfgrkn
//
LOCUS       WP_175839311             347 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            anthina].
ACCESSION   WP_175839311
VERSION     WP_175839311.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..347
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=36643
     Region          39..319
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mndvtsgpas gqprrrnhst vvgslvvval laaapivvyp vfvmklmcyv lfaasfdlll
       61 gyagllsfgh aaflgtgayl tayaaqawgl dpllcllvgm aaaalvgtam gflairrkgi
      121 efamitlala qvvefiaqqa sftggedgih dvprgyvfgl idlnnataiy itmlvlfvvg
      181 mfvlwrtins pfghvlkair dhedraislg ydvnryklia fviasviagl aggmkaivfq
      241 latlddasfh vsgavilmvl lggvgtlygp lvgativval esalatselp apvitgavfi
      301 lcvlmfrrgv vgeivnwlad rhtrhalprr veaaprahts dahsidh
//
LOCUS       WP_175839391             414 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175839391
VERSION     WP_175839391.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..414
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42936
     Region          5..372
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mnrqfllcls rvgtcmgtma fagalpilrs awhmdaatag siqtafnlsn afallvtawl
       61 sdslgakrvy lastwagaaa liifaifars phtalplivl vgltqggaya pvlllvaels
      121 paaergrgmg qilaaasmgy llsvflsmwa ataygaaagf ticaigalag avsgqialkd
      181 venrrhstea sassepikwr svfgttslcl lvgyvahcwe llgswawtpt llatalrasn
      241 lgamttsliv agtihlsgmv atgvvgalsd rwgrarvlic vgaigalcsm lmgwseqwgp
      301 gwvialaatg sffiladsgv lsaamtdevp aaylgrvmgv rsilgfgvga fapmtfgatl
      361 dwthqwgway mplaaggiia alaafalrqs gqssaaeaqq pqssiihkrd fert
//
LOCUS       WP_175839398             209 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175839398
VERSION     WP_175839398.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..209
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22310
     Region          14..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mskstteqsp ravradaqrn ietllraale vfdssgvdap vreiaqkagv gigtiyrhfp
       61 krsdlvvaal csevdacada avdltakhga gdalvgwiec yvefvtnrrg laaalnsgdp
      121 afkalplyfl erlrpvvrsl ldaatsagei regilpdell cavgalsapl ecpeppdarr
      181 lvslfvdglr yganlqares vprevlrek
//
LOCUS       WP_175839421             412 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia anthina].
ACCESSION   WP_175839421
VERSION     WP_175839421.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..412
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=44561
     Region          3..382
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mfdpsaspei eavrdmvarf mhsevvpvle ayekrgefpr elvrkagaag lygavfpeav
       61 ggsdmgylaa tviqeemari dvrfahcnnq qgsscpsciy fggrpeqigk yvpdllaget
      121 igmmsltepg ggsdpdgnmk tfarrdgnvy risgqkmfas magetdvgvl fartdraags
      181 kgvsafivhp kqypgwhaqp idtvglskaf rttvlflddf vvpvedrlge egdgfkiamh
      241 glqpgrvtva gkalgvaras fedavryaqe rtlrgqpigr fqmiqsdiae mavaieasra
      301 lvykaaiamd esqpsnrmaa lakyhashta klcadkamqi fggyglarey rvswlrayad
      361 mfftgegsan vqkimiaeda lgykladrhh gkiglrdirr drvaagikaq aa
//
LOCUS       WP_175839407             168 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia anthina].
ACCESSION   WP_175839407
VERSION     WP_175839407.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..168
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=17519
     Region          9..163
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mshpasssrp lafrvngash tfddaapdap lllvlrndca lngpkygcgf gqcgactvlv
       61 dgqparscvv paaaangrdv ttleglgsra aphpiqrafi deqaaqcgyc lngmimstka
      121 lldrnpspdd aairaalrfn lcrcgthlei icavhraary lrgdgdea
//
LOCUS       WP_175839424             457 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175839424
VERSION     WP_175839424.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..457
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48206
     Region          21..424
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(34..35,38..39,42,81,139..140,142..144,147,167,
                     170..171,174,259,262..263,266..268,271,298,302,355..356,
                     360,364,380,383..384,387..388,391)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mrdfagsars vadaarrkel rrvllsscig saieyydfll yvaaaslifg rlffsnltpv
       61 matiaslgtl avgyvsrplg avffghfgdr ygrksvliat litmgvsttl igllptsaqi
      121 giwspaalvf lrmlqgvsvg gewgggalma fehapehrrg fasscsvagg pagtmlaagv
      181 lslfallpqs qflawgwrvp fllsavlvgv gfwmrirvae splfveaqrk rqatgakhkp
      241 plfdvlrapk pllvgfisml apftlyslva sfgltysrkh glpissvlai qatgavfcaf
      301 sevlcgylsd rvsrhsvlif gitagallay pyllllasgd vfkttagfll mnvcvigpvl
      361 gpsaaylaeq fdthsrytga slglqaastv gagfapitla sllvlnaggy qlilafivti
      421 cllsgavigi rantrrrrqg haistiiaap angdhrn
//
LOCUS       WP_175839480             198 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein, partial [Burkholderia
            anthina].
ACCESSION   WP_175839480
VERSION     WP_175839480.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         <1..>198
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
     Region          <1..198
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 aaegtsdlpr alqryvdyqe ridtvrnklg ssaiypsill vvgggvstfl ityvvprfat
       61 iyegtgralp wmsqmlldwg kfasahglpl alaalagvaa iflgvratia rvglvsllsr
      121 vpllgphlri yqlsrlyltl gmlleggipi vaametacgt vspsmrdall larsavqsge
      181 plsgafqarq lttpislr
//
LOCUS       WP_175839456             655 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein, partial [Burkholderia anthina].
ACCESSION   WP_175839456
VERSION     WP_175839456.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..>655
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
     Region          18..426
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 msteryqkit hdhlrrdafl yvrqsslrqv fentestkrq yalreravsl gwpierihvi
       61 dtdlglsgas aehrdgfqql vsevaighag ivlglevsrl arnnadwhrl ielaalthtl
      121 ildedgvydp ayfndrlllg lkgtmseael hvlnarlqgg mrnkarrgel elplpvglvy
      181 hpngsvvldp dqqihaslrl lfdtyrqths asmvvrrfrr egwsfprrir rgigkgevhw
      241 galntsrvlq ilhnpryaga fvygrtrtgr kadltstqlk vaqsdwqvli rdahigyidw
      301 defernqvtl rqsangfgsl vrgtvpregd gllqgrvicg icgnrmrvry qkvgdrmepy
      361 yvchdvaahd agkpcqsirg raiddaisal lletvgpaai evalavedei agrieqadsm
      421 rlkqlerary eaelarrrym nvdpanrmva daleadwndr lrrldvlqqe hdrqrrsdqd
      481 llgdearari raladdfaav wndrrvesie rkrmlgllie dvtlvksekv sihvrfrggr
      541 tttlavdkpr pmalvrktlp avvavidell etctdqqvat rlnelgytnw qqqaftarkv
      601 alvrttyglp srferlrsrg lltgaelaaq fkvsqttihq wgrqgllrrq vyghd
//
LOCUS       WP_175839513             151 aa            linear   BCT 11-JAN-2025
DEFINITION  ferritin-like domain-containing protein, partial [Burkholderia
            anthina].
ACCESSION   WP_175839513
VERSION     WP_175839513.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10090058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         <1..>151
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          5..109
                     /region_name="Ferritin_like"
                     /note="Ferritin-like superfamily of diiron-containing
                     four-helix-bundle proteins; cd00657"
                     /db_xref="CDD:153097"
     Site            order(20,23,68,98,101)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 rdnhhdsdfs afmsvwffee qkhslvlmey lrrfkpemmp tedelhavrf efdpapplet
       61 lmlhfcgeir lnhwyrraae whtepvikhi yetisrdear hggaylrymk kalvncgdva
      121 rsafakigvl masarrtekp lhptnlhvnq s
//
LOCUS       WP_175839540             275 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia arboris].
ACCESSION   WP_175839540
VERSION     WP_175839540.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..275
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28719
     Region          4..261
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 msgltigglt vhygrrnvlm slsagplprg citallgpng sgkstllrtl agltraasgs
       61 laldgaafvp glrdarshgv vylpqalpag vrlqvlesvv varratrhgf mpaarhagae
      121 ddgtaalavl arlgiealal rtldelsggq rqlvglaqal ardpqvllld eplsaldlnh
      181 qhqvmaalrd itrerqlvtv vvlhdisaal rgcdramllh rgrivrfgmp edvvtpvsla
      241 dvfgvaarie rcsrgqlqvl idglapndpv aaaar
//
LOCUS       WP_175839556             227 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia arboris].
ACCESSION   WP_175839556
VERSION     WP_175839556.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..227
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23868
     Region          51..221
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mttaqtaasa asasaaatga sapasvpaap atpasapaav erplvrfqqk plsvningks
       61 vgpmqvpegl mmieflheya gltgsrlgcg qgichacvvi vdkpdgtsee mrtcitgahf
      121 fhgrsirtie ghakrneage vvelspiqqk flehfsfqcg yctpgfvnaa tvlierlkre
      181 piakadvert itealdahic rcsgyvryye avkdvvlttp glvkdaa
//
LOCUS       WP_175839578             155 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [Burkholderia].
ACCESSION   WP_175839578
VERSION     WP_175839578.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..155
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=16180
     Region          13..140
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 msdahvsvdv aqqtrfrfev tfagttlapv ltdeppplge grgpnpirll aaavasclsa
       61 sllfaldkqh vdpqpiaahi dvdmvqneag rvrvgamavr lsigktwadl aaatrvldqf
      121 daycvvtesm ragipisvdv cdvngaalel aatdv
//
LOCUS       WP_175839608             295 aa            linear   BCT 11-JAN-2025
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Burkholderia
            contaminans].
ACCESSION   WP_175839608
VERSION     WP_175839608.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..295
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=31479
     Region          11..290
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mtdidvadfp vavigggvmg ngialnvams gfdvavvetd eqartsfnar lrrayqlarf
       61 vakpgsaare pfadiaarir vvaalpsrld vaiaiecite nvaskarlyr aledacpprt
      121 lfatntscis vatidtwtqr adrtvgihfm npaavrdave lirgprtsdq tidavagflg
      181 rlgkrfnvvn datgfvinrv lmvaineaig lvergvasaa dvdalfvrcl ghqtgplata
      241 dligldvird slivlrdesn drfyepkall sqlvaagslg hktgtgfhty rerka
//
LOCUS       WP_175839628             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia arboris].
ACCESSION   WP_175839628
VERSION     WP_175839628.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21514
     Region          2..205
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mlfiksvvmg lsiavpvgpi gmlciqrsls rgfqagfatg igaacadaiy gllgalgiag
       61 ivtafpmltv glkigggafl vwlawticrq ppaasavqrd lprttvlrdf lttfgltlsn
      121 pmtivsfvgi faalgplsaa rdgamwpava wmvagvfigs aawwlclssa taalrtklsf
      181 afmhglsrvs aaviavfgai qlvagvrgli
//
LOCUS       WP_175839644             334 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Burkholderia contaminans].
ACCESSION   WP_175839644
VERSION     WP_175839644.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..334
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36309
     Region          7..317
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(12..14,44,49,75,138..139,179..180,201,230..236,272,
                     289..292,297,300..301)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(44,49,75,138)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 mrisllsrlg fgtaplgnmy rdipheeala tvdaawdsgi ryfdaaplyg aglaelrlge
       61 alagrprday slgtkvgrlv ldehedatqr dlgekgglfr hglpnrivyd ytedgtlrsi
      121 daslerlrtd rldtvwihdp avdfhgdawr dvfdiamsga araltrlrde kviqgwglgv
      181 nriepcelal eradpdgfll agrytlldha galerlmpes aarglgiivg gpynsgvlag
      241 gthyeyqpat qamldrvari rricerfgvd vraaalqfsl ahpavaatip gasrpdridd
      301 nlrlaavsip aelwdtlkae rliaaqaptp vgrd
//
LOCUS       WP_175839642             371 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia contaminans].
ACCESSION   WP_175839642
VERSION     WP_175839642.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..371
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39547
     Region          5..349
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,236,303,323,325..327)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,103,110,183,186,188,236,243,303,323,
                     325..326)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(27,103,183,186,188,326)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mtqdplfqpl qlgaltlpnr ivmppmtrsr asqpgdeane lmaayyaqra saglivsegt
       61 yiaplgkgya wtpgihtpsq vagwrkvtda vhaahgrifa qlwhvgrlsh tsllggrqpv
      121 sssplqakgv nvfiagedgs tpgfvqasep raltideire ivdqyraaar haieagfdgv
      181 elhgangylv nqfidsnant rtdayggsle nrlrflrevt lalidgtgda srvgirlapl
      241 ttlngcvddd pettylaaak llgelgvgyl hiaeadwdda plmpvefkrq lraafpgvli
      301 yagaytaera reavaagwad lvafgrpfva npdlperlrt gaalaphdrn tlfgggergl
      361 tdyptlaqaa a
//
LOCUS       WP_175839654             314 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Burkholderia arboris].
ACCESSION   WP_175839654
VERSION     WP_175839654.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..314
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31456
     Region          2..314
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtilviaehd nasiraatln avaaaqalga agggavhvlv aghdaqaaad aaakiagvsk
       61 vlladaphla dglaenveat vmnvadaysh vvapataygk niapriaakl dvaqiseita
      121 vvsadtferp iyagnaiatv qssdpvkvit vrstgfdpva aeggnatvet ieaapdagqs
      181 qfvsrevtkl drpeltsani vvsggrglgs genfalvlep ladklqaalg asraavdagy
      241 vpndyqvgqt gkivapqlyv avgisgaiqh lagmkdskvi vainkdpdap ifsvadygvv
      301 gdlftlvpea vaal
//
LOCUS       WP_175839657             707 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia contaminans].
ACCESSION   WP_175839657
VERSION     WP_175839657.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..707
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=76125
     Region          21..639
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mtdhnasppp ppappprrrr vwrtlagall gltvacagig awtiqriwtq lpsvehlavy
       61 rpalplrifs rdgdllaeyg verrefvple ripplmrqal laaedakfyq hgavdfggla
      121 ratfanvvtg qpgqggstit mqvarnfylt rdkvlsrkla eilmatkler eyskdkllel
      181 ymneiylger aygfaaaanv yfgkpldals ageaavlagl pkapsafnpv vnparatarr
      241 nyvlgrmhal gqlddatyha avdapialat tpppgiiaap yvaerarrmm verfhddayt
      301 lgldvtttis mrdqraaess lartlsrqpr akrdarngle galvsldaat gdmlalvgga
      361 dfnrnvfdha lqayrqpgss fkpfvysaal ekgyfpgvlv ddtqrtlthe etgarpwrpr
      421 nfannyegfi pvrrglmrsk nlvavslmqa tdaryvqqha vhfgfdaqrn paslplalga
      481 gavtplelas aysvfanggt rmeprlilsv kqrhggamye atspagervv sarnafvmds
      541 mlrdvvksgt argalalrrd daagktgtsn gakdvwfagy ssgivavawl gydtprpmgr
      601 atgatlalpv wldymktavd grtpveatpp qdvalvdgdf vyaeytrgtc tadvpsyirs
      661 rfacggaaaa agasdapgnn gkpaestpaa vdaaerervl dlfrtdd
//
LOCUS       WP_175839667             290 aa            linear   BCT 11-JAN-2025
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Burkholderia
            contaminans].
ACCESSION   WP_175839667
VERSION     WP_175839667.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..290
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31582
     Region          1..121
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mgsselvlyf dgrcpicvae ikrlgardar hrlafvdiae pgfdpaplgv dlpamnrelh
       61 arlpdgrmlt gvdsilaaqa ltgcrslvrl lrvpavrgvl allyrrlarn rhavsrwlgy
      121 rteapcdgaa cgsgseraae ptadrpagda arrlvvtwmy gaaiahllvg mavpwvagap
      181 wldayhrvie lnfwagaapd aaraqqvwwm slmgatvqca svwmlalvhl gnrlrkrevw
      241 gwllaglliw apqdmlfslq ahvsghvaid aaalvamvpp lvwlwrrdav
//
LOCUS       WP_175839669             435 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia contaminans].
ACCESSION   WP_175839669
VERSION     WP_175839669.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10396284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..435
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=45629
     Region          19..279
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Site            order(25,27..28,30,84..86,122..124,134,138,157..160)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187579"
     Site            order(100,124,134,138)
                     /site_type="active"
                     /db_xref="CDD:187579"
     Region          326..425
                     /region_name="DoxX_3"
                     /note="DoxX-like family; pfam13781"
                     /db_xref="CDD:463982"
ORIGIN      
        1 mdtvlpstrp hgrtgahsmt vlvcgangfi gralcaqlea gghrvlrgvr hatglsdvai
       61 dfakdidpaa wlarlegvdv vinavgilad qrgatldavh raapcalfta ccragvrrvi
      121 qisalgverg dtryfaskca adrflqtlpi dfrivrpalv ygtdgasarf frmlaslpvq
      181 vlpagghqrl rpvhvddlae vvarcvdapa agrpvidvvg adeveyreml aryraalgfp
      241 paariglpgp lagvaavllg tlpgaiftrd twtmlrggnt gdpaaataml grpprgidgf
      301 igaeaaalrr dalamwrrpl lrgalaivwi wtaiasafih plhaslalla pahltglpal
      361 ialyaasald fafgiatvva psrrlwvaqa alivaysavi avtmpgllae pfgpvlknvp
      421 ilaillilfs eeeqa
//
LOCUS       WP_175839677             435 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia contaminans].
ACCESSION   WP_175839677
VERSION     WP_175839677.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46793
     Region          28..426
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(41..42,45..46,49,81,131..132,134..136,139,159,
                     162..163,166,261,264..265,268..270,273,300,304,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtsaspamad dretdtsieq ravrkaawrf ipllalayff nyldrtsvgf aaltmnrdlg
       61 ltatqfgwga gimfagycmf evpsnlalyr fgarrwlari mitwglmaaa talatgptsf
      121 yairlllgig eagffpgvif flavwfpasy rtrvlawftv stplssligg plstwllqld
      181 gvlglagwkw mfiveglpac algflvlrll fdspahaawl sdderaalqr aferdaaaag
      241 rkkrfgvalr dvrvyvlali sfgftmgsyg igiwlpqmlk ahgmstmqtg wlsavpyffa
      301 tiallwwakr vdrrggpvan laiglfigav algvsthflt lgpalvgitl aligtiagrt
      361 ifytlpsrfl sgqaaaggla linsigalgg fagpylvgyl kdsfgtftag mlglaivlai
      421 ttlltlslya fdrse
//
LOCUS       WP_175839683             212 aa            linear   BCT 11-JAN-2025
DEFINITION  2-hydroxychromene-2-carboxylate isomerase [Burkholderia
            contaminans].
ACCESSION   WP_175839683
VERSION     WP_175839683.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Thompson,L.C., Ladner,J.E., Codreanu,S.G., Harp,J., Gilliland,G.L.
            and Armstrong,R.N.
  TITLE     2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class
            glutathione transferase from Pseudomonas putida
  JOURNAL   Biochemistry 46 (23), 6710-6722 (2007)
   PUBMED   17508726
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122490
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..212
                     /product="2-hydroxychromene-2-carboxylate isomerase"
                     /EC_number="5.99.1.4"
                     /GO_function="GO:0018845 - 2-hydroxychromene-2-carboxylate
                     isomerase activity [Evidence IEA]"
                     /GO_function="GO:0043295 - glutathione binding [Evidence
                     IEA]"
                     /GO_process="GO:1901170 - naphthalene catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23325
     Region          8..188
                     /region_name="DsbA_HCCA_Iso"
                     /note="DsbA family, 2-hydroxychromene-2-carboxylate (HCCA)
                     isomerase subfamily; HCCA isomerase is a glutathione (GSH)
                     dependent enzyme involved in the naphthalene catabolic
                     pathway. It converts HCCA, a hemiketal formed
                     spontaneously after ring cleavage of 1; cd03022"
                     /db_xref="CDD:239320"
     Site            15
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239320"
ORIGIN      
        1 mnaartatwy fdfvspfayl qqeqfdrlpa aaafeprpiv lgallthwgq kapaeiaakr
       61 vftyrhaqyr aeklgiafrm ppahpfnpik plrlaiamgn spdairrifr hiwrdgqdvs
      121 tpegfaalce avgfpegvta vdsqpvkdal rantddaiah gvfgvptfal dgdlfwgeda
      181 tdmfadcats rawldspevr risalpegir rg
//
LOCUS       WP_175839707             531 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Burkholderia contaminans].
ACCESSION   WP_175839707
VERSION     WP_175839707.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..531
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=55401
     Region          45..151
                     /region_name="SoxW"
                     /note="Thioredoxin-related protein SoxW [Posttranslational
                     modification, protein turnover, chaperones]; COG2143"
                     /db_xref="CDD:441746"
ORIGIN      
        1 mktalrnlta acllaaagaa laaatptgap vasaapdgah lppgiawqhg dvdaafalak
       61 rtgkplllyw gavwcpscnq vkstifsqqa fkarssffvp vyldgdtesa qklgerfkvh
      121 gyptmilfrp dgtevtrlpg eadldrymqa lslgmtaahp vrqtlatalk ngasltpdew
      181 rlladyswdt dgalpvaadr vaetlqtlaq raraagakae sarfalksav vaasddpaqa
      241 galdkaalad slrtvlqdpv lsradsdvlv aaparvvayl ggddaqrakl rgaydtalar
      301 lstdttlssi drlmalhgrv llargdaskg aplaapalad tarkqiaasv qgaanayerq
      361 alvsegadtl tdaglydesd allkaelprs atpyyfmsgl aanakargdk aaaldwyrka
      421 ydsaigpatk lrwgatyfan avqlapddsa riegiaasvl aqagktrdaf yganlraltk
      481 vvtqlnrwrg sgahdasvks iakqfdgicg klpagdpqas acarliqpvk a
//
LOCUS       WP_175839766             213 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175839766
VERSION     WP_175839766.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..213
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23986
     Region          7..211
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 meakldstad avaaslrdmi ingeleager lverdladrf gisripmrea iqrleregll
       61 difrnrgavv rmlsasdvqe iydlralleg daiyrsvkrl ddetlarael vnrllgdaav
      121 prrqgelnre fhallysccg narqlktiae lrsqveryer lqatlladtp sfqveheeil
      181 qacrernara arsmtvahle sarrivmrlv egg
//
LOCUS       WP_175839778             243 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175839778
VERSION     WP_175839778.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..243
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27339
     Region          26..232
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 msrqklqtaa pdaesggsad rknimaetlr rrivsmelap gavvdelals eefglsrppv
       61 relmrqmaae gylelepnrp arvspmgyqs lrsfflaapl iyvattqlaa nhataeever
      121 lkaiqaqfra aieendlqar vlqndafhfe igriarnvyl mpslrrvlid harlgkifyr
      181 spttsdmqqd lekaveqhde iieaiaqrda qragelvrsh melsrrrmae yvipegldvp
      241 iqf
//
LOCUS       WP_175839788             339 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Burkholderia contaminans].
ACCESSION   WP_175839788
VERSION     WP_175839788.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..339
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=37878
     Region          31..304
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mslpaspdtp arpeetdlfd rgasdwivsp eaafdawlam qdyrrssadv yraqwgaflt
       61 wmrahqknla tidtatianf vgelpirktq rmrylrlier vldhirrtey astnparfia
      121 qdgeanwrka rdneptgflt paeratllay lfspigvsgs aywkerrdra lvaaflgagi
      181 ktgearalti scintsgtsl riesthpdfa rethlasfai alleawlter krqeipgelv
      241 fpashagrpm hkatmlraid aivesaglts srtaraspqt lrntyaaelf ehdvppervg
      301 kwlgfmrpis snrlhrawkn wrdgladsng dasdsdeth
//
LOCUS       WP_175839794             317 aa            linear   BCT 11-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Burkholderia
            contaminans].
ACCESSION   WP_175839794
VERSION     WP_175839794.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..317
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33693
     Region          23..301
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 msknpdvvse avaevtpama aaatrstwvs vavnlvlsig qvtvgilsrs qglvadgihs
       61 lsdlvadfvv llaghhsrkp vdekhpygrq rfetgaslal aailllvggg mlwsaiqkle
      121 hpeaiarvhv talwvalval aakeslfrym laiatrvkss mlvanawhar sdaasslvva
      181 cgivgnllgf plldpvaali vggmivkmga tfgwdalddl mdraadaedv qairatlvat
      241 rgvldvhdlr trktgdlilv dvhldidadl tvaqghdiav dararvmkhh rvlnvmthvd
      301 prkrenlpev asgmrvr
//
LOCUS       WP_175839802             521 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia contaminans].
ACCESSION   WP_175839802
VERSION     WP_175839802.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..521
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=55548
     Region          1..521
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 metydhivvg ggsagctvah rlvkagrrvl lledgpkdds lfiripatfi rvlgskrtvt
       61 fesepqpgaa grktyvpqgr tlgggssvna mlyvrgtrdd yddwaalgct gwgwddvlpv
      121 fkraeshlrl sepfhgtdgp lkvgdtrfrh plslafvkaa qeagiayndd fngaaqhgvg
      181 fyhttifdgq rgstaatyla dairhpnlrv ltgcrvtrir fddrratgve wrtesgatgs
      241 aaaradvvla agalstpkll mlsgigpgah lhahgidvlh dsrdvganyq dhlevsiygh
      301 shapvsllge drglkalrhg lqwmlcrtgl ltsnvvesga fvdttgsgrp diqfhvlptl
      361 vgdvdraplp ghglsinpcl lrprsrgsvq lrgndpaapi lfdsgalsdp advdglvrgv
      421 alarqiirap slarivreae tltdaalady vrrraktvyh pagtcrmgsd ahavvtprla
      481 vqgvdglric dasvmprivs gntnaptimi aercaafmla e
//
LOCUS       WP_175839823             397 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia contaminans].
ACCESSION   WP_175839823
VERSION     WP_175839823.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..397
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42659
     Region          1..364
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 maqitckals khydggpavl hpldleiadg efivllgpsg cgkstmlrmi agleaitgge
       61 lvigdevvnd lpsrernvam vfqnyalyph mtvydniafg lrrlkvpade idrrvrdvar
      121 ilsldalldr rpramsggqq qraaiarami ktpavflfde plsnldaklr tqlrgdikrl
      181 hqrlktttly vthdqleamt ladrvvlmrg ghieqigtpa elygqphtvf aagfvgtpam
      241 nfaagtierl ganvlldcng arwplastrf aalhdgqkvk vairpnhlrl vtepdptpst
      301 ltltgtvelv ellgaealvt ldwhgqpcaa lvpapmapaq gavvalrfde aalhlfdagt
      361 ernvtlpdan piahaappaa atrttppaat gwsmsrs
//
LOCUS       WP_175839864             313 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175839864
VERSION     WP_175839864.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..313
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35084
     Region          59..302
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          223..295
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpsiapprly gmpersdrld fyirdqasrq aitephrhay fqiqfnlggd teqriggvtr
       61 pfprgalafv lphrehliph pegahfivin fsqaflradl dvdpldledv pahrfpeltp
      121 frfqehldfi ltgdsydear rlalcmldtd rvrtfgsttl lrgyllqlig lvctqyagal
      181 dklaqrgaqr agrrdalarv lrhvranltr edltlaatae aaflspnyla hlvrketgst
      241 ftdlvterri alaqsllaht srriadiars vgfrdegyfa rrfrarvgls pkayrdanat
      301 lpdsddtppa ada
//
LOCUS       WP_175839944             430 aa            linear   BCT 11-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Burkholderia contaminans].
ACCESSION   WP_175839944
VERSION     WP_175839944.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..430
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44507
     Region          <217..408
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mlirlllrsl alslkfalai ivartlgfda vaayglavaa aviaskllgl gfspelnrrl
       61 sesdplpafg amrtlciayg glylllvatl aiatangdaa llarlglptr lawcvllval
      121 sehaafeang wlfslhrprv gslllfvrtg awagiagagl lvgilrsies vfalwfaana
      181 cvvalslrri gavarpacgs praarapavr ergvlsvwrh glpfyvggiv lsslqyaerf
      241 vggehlsada lgryvfawsi anaiqalafs tvvvaagprf vrvladaprt fsrlvvratv
      301 asvvvtsiva aaivalhrdl falahaprdt gqfallaill vsfvlrgaad vlwtaaialr
      361 tgfvvmvsmi tlalsylpla sslivhagal gaaiahltas agivaalali vartgrsraa
      421 asteaaphaa
//
LOCUS       WP_175839983            1068 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia contaminans].
ACCESSION   WP_175839983
VERSION     WP_175839983.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..1068
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=114618
     Region          1..1044
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 miahiirwsv hnrflvllat vliaawgvhs lrqtpldalp dlsdtqvivk asypgkapqi
       61 vedqvtyplt ttllgvpgak tvrayssfgd afvyvlfddr tdpywarsrv leylsqvqsr
      121 lpagatvslg pdatgvgwvy eyalvdrtgr hdlgrlraln dwflkfelka vpdvsevasi
      181 ggmvqqyqvv ldpdklrahg itqaevatal gnanqasggs vvelaeseym vrstgylrtl
      241 ddfrhvvlrt ndagtpvllg dvariqvgpa mrrgiaelng qgevtggvvv mrsgknaltt
      301 idavkaklad lkrslppgve ivttydrsql ieravgnlkd klieefvivg lvcavflfhl
      361 rsafvailsl plgvlaafiv mryqgvnanl mslggiaiai gamidaaivm ienahkhlea
      421 ydhahpgepi tparrwelva tsaaevgpal ffslliitls fipvfslegq egklfaplaf
      481 tktytiaaaa glsvtlvpvl mgylvrgrip hehanpinrv lirayrplle atlrrpwvai
      541 giavvalvlt avplsrlgge fmppldegdl lymptalpgi sadkasellq qtdrliktvp
      601 evdtvfgksg radtatdpap lemfettirf kprsawrpgm tpeklvdeld rtvkvpglsn
      661 vwvppirnrl dmlstgiktp vgvkisgpdl agidaiakqv eaavkpvpgv tsalaerlng
      721 gryidvdidr laaaryglsv advqsvvsta vggddvgevi agrerfpini ryprevrdsv
      781 enlrqlpvvt argaqirlgd variaiadgp pmirsenarl sgyvyvdlrg tdlqsavram
      841 qqavarqval ppgysiawsg qfeyleraaa klrtvvpvtl vvifvllflt fgsaadalll
      901 mstvpfalvg gfwlvwalgh avsvatsvgf ialagvaaef gvvmllylkg alqrrldage
      961 pltdalllda iregavlrvr pkamtvavvl aglvpimvgh gagsevmqri aapmvggmvt
     1021 apllsmfvip aawlllqrrr aqsaghawhs eavphgtnvp stptgesr
//
LOCUS       WP_175839987             336 aa            linear   BCT 11-JAN-2025
DEFINITION  sodium:calcium antiporter [Burkholderia contaminans].
ACCESSION   WP_175839987
VERSION     WP_175839987.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schnetkamp,P.P.
  TITLE     The SLC24 gene family of Na/Ca(2)-K exchangers: from sight and
            smell to memory consolidation and skin pigmentation
  JOURNAL   Mol Aspects Med 34 (2-3), 455-464 (2013)
   PUBMED   23506883
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Besserer,G.M., Nicoll,D.A., Abramson,J. and Philipson,K.D.
  TITLE     Characterization and purification of a Na+/Ca2+ exchanger from an
            archaebacterium
  JOURNAL   J Biol Chem 287 (11), 8652-8659 (2012)
   PUBMED   22287543
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..336
                     /product="sodium:calcium antiporter"
                     /GO_function="GO:0008273 - calcium, potassium:sodium
                     antiporter activity [Evidence IEA]"
                     /GO_process="GO:0006874 - intracellular calcium ion
                     homeostasis [Evidence IEA]"
                     /calculated_mol_wt=35523
     Region          19..332
                     /region_name="ECM27"
                     /note="Ca2+/Na+ antiporter [Inorganic ion transport and
                     metabolism]; COG0530"
                     /db_xref="CDD:440296"
ORIGIN      
        1 mtymflelaf mlivilvaae vftnalehlg erlkisegvt gslfaavgta lpetmvplla
       61 laggtanqav neeigvgail gaplmlatlt tflmtlavir srglrgtiap ertgfvrdmn
      121 yflaafslat aamfvphqnw avrallaaml vgiyvmyvvm tfrasnqlvd aghgteapht
      181 mflsrlgvpt nlatiglqll lgvvllvgga kgfihgvegv shvlgvsall lsliivpiat
      241 elpekvnsvl wirrrkdtla fgnitgamvf qgtllpaigi mltpweprpe vltgviitla
      301 aaawlrvnar trglaiwall angagyagyl vltlar
//
LOCUS       WP_175839996             306 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: bestrophin family protein [Burkholderia].
ACCESSION   WP_175839996
VERSION     WP_175839996.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..306
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33601
     Region          1..299
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 mivrprehwl rmllvwngsv lptilpqlvl tlaislvavw gggrvlgekv plnptpftli
       61 gltlaifagf rnnasyeryr egrqlwggvl tatrtlvsqa lcygavdrdd asrrvfvrqv
      121 vafvyalkhq lrgtdpaadl rgllddaaya riagsrfrpv vivhalreaf aaradagrla
      181 dtrlwmldar lddlvsmvsg ceriastpip fsydvllhrt iyaycvllpf glvdsigaat
      241 pfvtvfvayt lialdaiaha iaepfgdgpn hlaldamtrq iertllelnr eplpaevtpg
      301 rayrls
//
LOCUS       WP_175840006             318 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175840006
VERSION     WP_175840006.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..318
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33885
     Region          8..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..296
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(105,109,148,162,164,230,247,275)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(106..107,111..112,114..115,118,122,124..130,191,220,
                     225..228,235..236,239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdvsqrtrai lsfvhaadgg sfaaagrmlg itsaavsknv agleqalgvr lmnrttrtlk
       61 ltdegsvflr qarvaldald savdsivaqr lgpqgrvris tsaafgrehl qpvlpgllar
      121 ypglsveadf ddrivdvvrd gydivirggn vhdsalvsrp vfrmntvmva spaylashgi
      181 prapgdlvah rliarrflgg evatwsfrtr dgsivavdpg etalltfsap eavlqaardg
      241 lgiaqvgvhl awahlragal kvllhrhhlp gsyemamqyp hralkasrvq atvdylldaf
      301 aaneslhvpl kaldayga
//
LOCUS       WP_175840043             116 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia contaminans].
ACCESSION   WP_175840043
VERSION     WP_175840043.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..116
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=11648
     Region          44..>108
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mnktshlstl laastafllc aapltnaqaq assadsgmta esnqpvtdtw ittkvkgela
       61 ttdgvkstdi svktvdgvvt ltgvlptkva vkkavavtra ikgvkhvdas glkaka
//
LOCUS       WP_175840045             246 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia arboris].
ACCESSION   WP_175840045
VERSION     WP_175840045.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..246
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25479
     Region          10..239
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; pfam01925"
                     /db_xref="CDD:460386"
ORIGIN      
        1 mqihtltiiv lvfllagavk gmiglglpti amglltlamp psaaaslllv psfitnvwql
       61 wlgpsfgpll rrlwpllagl tigtltgglp alaagstwth aalgvvlily glwglaaarl
      121 papgrhekwl savvgyltgv vtaatgvfvv pavpylqalr lskddliqal glsftastiv
      181 lglqlrvtga lqtvdlgvsa lalvpalagm vggqyarrvm sekafkrcff vglmalgtym
      241 avsgwl
//
LOCUS       WP_175840057             308 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia contaminans].
ACCESSION   WP_175840057
VERSION     WP_175840057.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..308
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34098
     Region          1..304
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mtrhdiefqs egatlrgwyy epaqriadta typaivmahg fsgvkeqyld ryaevfaagg
       61 fgvllydhrn fgasdgyprq eidpvqqrrg yrdaisyllt rpdvdaerig iwgtsysggh
      121 vlevaaidrr vkcvvsqvpt isgyqsalrr trsdrvpaal arfdedrrqr fagaapailp
      181 avsadpatac amagamagad ayrfftesaa qfapnwknev tlrsaelsre nepgqyvdri
      241 sptpllmiva dqdlltptdl clkawgsale pkrllmikgg hftpyiehfe atsqaavewf
      301 tlhlrstr
//
LOCUS       WP_175840090             282 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175840090
VERSION     WP_175840090.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..282
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30547
     Region          19..239
                     /region_name="HTH_MerR-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     transcription regulators from the MerR superfamily;
                     cd04778"
                     /db_xref="CDD:133405"
     Site            order(21..23,37,53..55)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133405"
     Site            order(67,70,74..75,84,105,109,115,119,122..123)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133405"
ORIGIN      
        1 mskqthstpd eaapdsrney tvdelarvsd ttvrnvrayq drgllappek rgrvgiyddt
       61 hvarlklinh llargytlsn iqdlikaide ghdlrsilgl enaiggrwsh elpktyslaa
      121 laqmfgpqat tqlsrvtelg llerrglsfv akspalleaa aamtkegipp relldvisla
      181 rphfdaiarl lvdlvvkrld rydagtlppa tdvpelvdai wrlrplaavf vegetnrale
      241 taasaylggr vatildkkls deaarqsgap dtsdtqgdgd na
//
LOCUS       WP_175840082             504 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MDR family MFS transporter [Burkholderia].
ACCESSION   WP_175840082
VERSION     WP_175840082.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..504
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53110
     Region          38..422
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(39..40,43,74,124..125,127..129,132,152,155..156,159,
                     284,287..288,291..293,296,324,328,381..382,386,390,406,
                     409..410,413..414,417)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mttntlltpp aaetarrdap tgliiaalll vmllsaldqt ivstalptiv gelggldqls
       61 wvvtayllss tvvlplygkl gdlygrkivl qaaivlflag salcgvaqdm tqlivlralq
      121 glgggglmvv tmaaigdlvp pdrraryqgm fggvyglati igpllggflv ehlswrwift
      181 inlplgflal avigmafrph tahvkhridy mgaaflatal tcvilftseg gsllpwtspq
      241 lwmtlvlglv aiggfiyeer laaepimpla lfrqrtfvlm sligfvvgia lfgsvtfipl
      301 ylqvvkgstp sqagmqllpm mggmlamsii sgrlisrlgt yrpfpiagtl iggiamalls
      361 tlsldtplht myaymallgi glgmvmpvlt lavqntvefr hmgvatsgvt lfrsiggslg
      421 vaafgalfsh glqsrimqal pagtelppam gpaavhqlpd avrdaylhaf agslhvvyla
      481 aaaviaiafv lawfvesapl rkhh
//
LOCUS       WP_175840103             303 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175840103
VERSION     WP_175840103.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32576
     Region          11..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..291
                     /region_name="PBP2_CrgA_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08475"
                     /db_xref="CDD:176164"
     Site            order(103,107,146,161,163,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176164"
     Site            order(104..105,109..110,112..113,116,120,122..128,190,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176164"
ORIGIN      
        1 mderlrgvae fvdvvesgsf aaaalrlgvt rsavakvvar lerrlgarll qrttrqlglt
       61 deglvyyeqc rrllaelget eaaldagqre pagrlrvsvp vlfgrqcvap vmrrlverhp
      121 rleidvsfsd rvadlvndgf diavrigela dtsalvgrkl gvqrmgicas payldrhgrp
      181 agldalashv giaysrggqp tpwrvvgadg avhdhrpsgr lrlddlqaia eaaaagagla
      241 wlpcwlmapy lrdgrlalvm dsnsvsgaev favrpasrqv pskvrvvida lvdeiphmla
      301 sdd
//
LOCUS       WP_175840146             132 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: RidA family protein [Burkholderia].
ACCESSION   WP_175840146
VERSION     WP_175840146.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..132
                     /product="RidA family protein"
                     /calculated_mol_wt=13850
     Region          1..129
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mlrainppga tipgisqail veggqplyls ghvpfdaega vvgadhatql dqvfrniadt
       61 lraagvgfes varltiyvrd fdssllpqir evrdrwvnta cppasalvgv aslfrtdvlv
      121 evdafaivpa ak
//
LOCUS       WP_175840152             414 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia arboris].
ACCESSION   WP_175840152
VERSION     WP_175840152.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..414
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43768
     Region          14..414
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mteantpaqp gpgtvvvigg gqaagwvlkt lraegyagrl vmiadephlp yerpplskav
       61 lagdadietv rvvrpdefda lnveawqper aasidrarrv vttasgreie ydrlviatgg
      121 tsrrlpdaiv ktpnlhylrt ldeaaalgek lrasqrvlvi gggwigleva atarklgvda
      181 vvvegaprlc grsvpqivsd flldlhrsng vdvrtgaala sldaqpddas kvratladgt
      241 tidadfavag iglalnasla seaglavddg ivvdefgats dpaifacgdv anhhngwlkr
      301 rvrleswana qnqaiaaaka vlgvrapyae ipwfwsdqyd vnlqilgdlp adaqlvvrgd
      361 laarratlff vgdghvrgvi avnnarelkl arkwmnqgra vdtealadtt kala
//
LOCUS       WP_175840207             214 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia
            contaminans].
ACCESSION   WP_175840207
VERSION     WP_175840207.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..214
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22264
     Region          11..213
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 msaarkpasp irvysfllsg hahrvrlfvs llglpsetvd vdlaagaqre paflalnplg
       61 qvpviddggt viadsnailv ylakrygdah wlpddpagaa lvqrwlsyaa gpiasgpaaa
      121 rlvtvfgakl dqeaakrtaa kvldvidrel agkpfaagaq ptiadiaays yiahapeggv
      181 slepylhvra wlariealpg fvampttrag llaa
//
LOCUS       WP_175840247             964 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            contaminans].
ACCESSION   WP_175840247
VERSION     WP_175840247.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 964)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 964)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..964
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..964
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=105475
     Region          14..823
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnmielaqai rggliqqdrl lkseipslps ntllprravt hvelgrdfav eldmvstagd
       61 ielktliaqq mtlwiqqedk sylpingyih tgrrlgadgg ltayqvsfas wmhflkfrsd
      121 mrhwqdkpvd eivtdvfnah pqaqgqfqfm lskplpsrsy crqsetdwnf vhrllesegl
      181 ygfwrqandg kshtfvivdd ihnldkmspe tvrfyrsgan seanaftqws gsrtlqsvty
      241 ttrtfdykap assfspkgts lpsrldqgdl psqleiysyt gaytysdqdr gdhltqihle
      301 ewesrakrfh gaggvrgida glrfrlenhp ehdsdsesyr efvaikvsry iennlplsgq
      361 eknfphslkr rvdeamagys gdasltirhs dgsegfflvq veaqrvtvpy rspfehtkpv
      421 mhletamvvg pkgeevytda lnrikiqfiw drlnpgdeka scwvrvaqsd tgggyggihv
      481 prvgeevivg hvggdcdrpi vlhrvfngav rpqwhsngil sgyrtkeyag agfnelaldd
      541 atgqnrvrlm sstgnsllhl gylveqsgnm rgsylgsgfd lktdhygavr anrglyvsth
      601 skemssqald agesrgqlvn aeslmetlsd asvqaraegt kegygalkaf saameqntag
      661 tsaggrtagg gmgnangfsk pillmaspag ialstqqstq vaadqhvnlv sgesthvvag
      721 ksllatigek lsifvqnagm klfaahgkve lqaqgnamal aalkdvtits sngrvvlsae
      781 keiwvgaggs yikisgsgie ngtpgqilek caswektgaa satvplpvmp itkqesgdqh
      841 fvlrshdgkp vpnqkyrmsi gddviegttd asgktqvveg yvgqpvhfei vddvydehfv
      901 vrdafgepia nmpyqiraed grliegmtdd egktslftse kivkvdllyr pgnhddypad
      961 tgvn
//
LOCUS       WP_175840270             151 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia contaminans].
ACCESSION   WP_175840270
VERSION     WP_175840270.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 151)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12226222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..151
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16189
     Region          1..147
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 mtiafespdq pdvialiadl dayqdtlypp esrhaldvas lkqsnvlfav ardsggraig
       61 cgaivlnaef gelkrmyvsp rgrgqgvart lmtmlesrav dsgckvirle tgpyqpeama
      121 lyasagyqcr gpfgdyaddp lsvfmqkhia s
//
LOCUS       WP_175840280             541 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: amidohydrolase [Burkholderia].
ACCESSION   WP_175840280
VERSION     WP_175840280.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..541
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59167
     Region          2..537
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mqhadtvyln gllytgdaqr rfaqalatkd gkivavgrdd dirplagpat rtvdlagrlm
       61 lpglidghvh pleghqilgd fdlsgindpd ailqriraca datpdepwvy lgganlaafg
      121 ayptrelldr ivpdrpllvv gfdvhsgsln tkgleaagiq adtpdpsggv ierdasgapt
      181 gvvheaafyr vcpiipqlsp agypkslaka hamahgygit gwfdarveea elkayaaaqr
      241 agtlkvymsa glyanprrdp reqierfagw rreyacdnlr lhtvkifvdg vpesktaall
      301 epyagtddcg lalwsqdaln eiclladtag fdlhfhtlad ravrmtldal eyvqrrngmr
      361 drraqlahlq lvdpadmsrf nrlgaiasvq tlwtaareeq qqlyrdllga ertarnypfr
      421 slrnagamla agsdwsvstm dpmqiiqtgv thllidqpds ppwnpherld lltmleaytv
      481 ntayalrfdd ctgsleagkd asfaildrnp fahpvetfaq trvietrfrg evvyaapgwa
      541 d
//
LOCUS       WP_175840288             305 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175840288
VERSION     WP_175840288.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32796
     Region          11..70
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          100..295
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(115..116,118..119,122,126,128..134,226..231,
                     237..238,240..241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrnrineeit frklevllaf meagslakaa ealgvstvsv hralhtleeg mhcalfrheg
       61 rnlipteaaq vlaevagevl ktmtdgirst reaagygagq lkigslyslt irtvpevvia
      121 lkerrpelqa elvlgsnadl ldklrqgaid atlmalpepd aeigsialfe demffaapvd
      181 spyaqrdaid lhacgdepfv slgegfathh gfteafrtag vapnvvmrvg difslinlvs
      241 ggvgysllpg rvrdlfahki alvplagpti rqtiglsflh rrerdpnlla latvcrltvk
      301 aptar
//
LOCUS       WP_175840303             215 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Burkholderia].
ACCESSION   WP_175840303
VERSION     WP_175840303.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..215
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23244
     Region          7..203
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mtskhsltfy tadtpnghki aiyleeagia hdlvhvnlsa geqrspafla inpngkipai
       61 vdhdtglavf esgailgyla gktgclhpet laertavqqw lhfqiggigp mlgqlwwflh
      121 asktvnaeai dryrkevmrl ygvvngrlse saylasprys iadiaafpwl rataeldldv
      181 agfphverwl adiaarpavq rgliacrapa aeaah
//
LOCUS       WP_175840313             779 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            contaminans].
ACCESSION   WP_175840313
VERSION     WP_175840313.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 779)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 779)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..779
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..779
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=86015
     Region          1..740
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msmilptqay elklaphpap fsilkftgmd rvsqlyryei eftspaagip mdqvlgrpak
       61 fiadpvdpdm nylrkmfgen aaqfsakpma ytvhgvitqf deletsadet ryrvvleptl
      121 adldrgvtsr lfqkqsveei vtdtlrhygy ragvdfqfql rgqykrreyv tqyhettfaf
      181 iqricaeegi wfrweqkkdr avvvfgddld ayarkqrtvp yrrdsglesv gadaikalgr
      241 emkrvpeavr lhdynhrqag vsllveenta rddettnavd yhwgehyetp eegkrvarlr
      301 heaylaeqit fkgtgnpfwl eagevmrvep npvdakhgvf vtlveshggr nesyrvsfeg
      361 ipsdrvwrts vasvsrpvvd gilparitsp gnykyaylte qgwyviklpf dldewspggt
      421 srpvrfakpy sgdnyghhfp lidgaevaiv htdgdpnrpv iigamhdsvh pdlvnnlnht
      481 rnlirtaarn elrmedkegn ehvhlitpfq asqlnlgfmv dtdrkargkg aelatyghaa
      541 iraadgvlvs aeaqpgaagd qlamqdadat faqaeeilrs lndaanaaka lqaeanqqre
      601 fiekklsrlq kpvivasape gvgiasgqhv qvaarrqmfv tagdgfdlgv mkritvaage
      661 aisflaaklg irlfaakgkv qiqaqgdgme lmamrdmqms ssdgeititg rkgvtigdgs
      721 gayiklsggk ivlgspagei elkgnltvnd adggsfkfpt wsaaplnevk stlnfgfse
//
LOCUS       WP_175840315            1057 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia arboris].
ACCESSION   WP_175840315
VERSION     WP_175840315.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..1057
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113389
     Region          1..1038
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mdfsrffidr pifavvlsiv ifaiglisip mlpageypev vppsvvvrat ypganpkeia
       61 esvaepleea ingvegimym ksvagsdgsl qvvvtflqgv dpdtaavrvq nrvsqalsrl
      121 pdevrqygvt tqkqsptplm yvslyspdns rdslylrnyl tlhvkdelsr ltgigdvgvy
      181 gsgdyamrlw ldpnrlasrg ltasdviaav reqnvqvsag qlgaepspkk ndflvsinvr
      241 grlrtvqefs divlrngddg qvvklsdvar ielgagdytl rsyfndkhsa vvgiflspga
      301 naldvakavy akldelskrf ppgvayrpvw dptvfvresi ravqhtliea vvlvvlvvil
      361 flqtwrasii plvavpvsvv gtfaflhllg ysintltlfg lvlaigivvd daivvvenve
      421 rniaqglnpr daahqamrev sgpivaialv lcavfvpmaf msgvtgqfyk qfavtiaist
      481 visainsltl spalaakllr phgapkdalt raldrafgwl fhpfnrffer ssdryhgvvg
      541 rtlkrrgvvf vvyaallaat allfnavpgg fipvqdklyl fagaklpega slartsavte
      601 qmtkialgtd gvemvpafag lnalqgvntp nitnsyvilk pfdqrhrsaa qinadlnarf
      661 aainggitya lmpppiqglg ngsgyslyle drgglgygel qkalttfqaa vaktpgmsyp
      721 vssyqanipq levkvdrlka kaqgvaltdl fntlqvylgs myvndfnvfg rvyrvmaqad
      781 aghrqtaadi anlrtrnakg emvpigsmvt vgpaygpdpv vryngypaad ligdadpkvm
      841 sssqaiaklq qiakevlppg itlewtdlsy qqvtqsnaai vvfplavmlv flvlaslyes
      901 wtlplavili vpvcmcaalf gvwlsggdnn vfvqvglvvl mglacknail ivefarelei
      961 qgkgvieaal eacklrlrpi vmtsvafiag svplligsga gsevraatgi tvfagmlgvt
     1021 lfglfltpvf yvairklagg tpavwseqhg tlegenr
//
LOCUS       WP_175840338             133 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Burkholderia contaminans].
ACCESSION   WP_175840338
VERSION     WP_175840338.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..133
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=14608
     Region          16..133
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mslihaaavv dadapdyvvq lqagthamtg deapreggqd rgpapyefvl aglaqctaat
       61 lrmymqrktw patridvrte lhadrdgtqy vrrvvtldgp ldeaqrqrla eicektpvtq
      121 fikrgtridt tln
//
LOCUS       WP_175840369             184 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia
            arboris].
ACCESSION   WP_175840369
VERSION     WP_175840369.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..184
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20621
     Region          47..178
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtqriacasp pfapdiaasi erimhgrppl rlfttlards rlftkffaag lldkghldir
       61 qreividrtt alcrseyewg vhvtvfapaa altgeqirsl algsaddacw kdedrvlirm
      121 cdalhrhcdi dddlwnalcr hfsdearlel lmlagfyrtv syltnalrlp leahaarfps
      181 pate
//
LOCUS       WP_175840375             353 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alkene reductase [Burkholderia].
ACCESSION   WP_175840375
VERSION     WP_175840375.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..353
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37653
     Region          3..332
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,225,286,306,308..310)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,173,176,178,225,232,286,306,
                     308..309)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,173,176,178,309)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            178
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mptlfdpvtl gdltlpnriv mapltrsrag aarvpnalma ryyterasag liiteatsvt
       61 pqgvgyadtp giwsdeqveg wkqvtqavha aggrivlqlw hvgrvsdpvf lngdlpvaps
      121 aiapgghvsl vrpqrpyvtp raleldeipg ivaayrkgae nakaagfdgv eihgangyll
      181 dqflqdstnr rtdayggpie nrarlllevv daaidvwgag rvgvhlaprg dahtmgdsdp
      241 aatfgyvare lgrrkiafif tresysgdql sprlkeafgg plianeqftl dtaqaaleng
      301 sadaiawgkl fianpdlprr leigaqlnkp vpetfyaege tgytdypals daa
//
LOCUS       WP_175840378             216 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Burkholderia
            contaminans].
ACCESSION   WP_175840378
VERSION     WP_175840378.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10583942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..216
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23431
     Region          25..168
                     /region_name="Pyridox_ox_2"
                     /note="Pyridoxamine 5'-phosphate oxidase; pfam12900"
                     /db_xref="CDD:432864"
ORIGIN      
        1 mkdqavispt srttirrlpe lashdremlh rivdeayvch iafgpgedth ciptahwrrg
       61 ddlyihgsng srmikalaag aqasvamtll dglvlarsaf nhsmnyrsav iygrfetveg
      121 sadklaalda lmdkiapgrk haarpgneke inatsvlria laeaavkvsd smpsdkeedl
      181 alavwtgilp lkmtrgapvh aegnvpvpdy vrnwee
//
LOCUS       WP_175840395             500 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [Burkholderia].
ACCESSION   WP_175840395
VERSION     WP_175840395.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..500
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52289
     Region          22..451
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msgwsgvtga agdtsagspa eagggtalka gavgfptala savglimasp viltatsgfg
       61 mggwafavam iiafvmmqaq attfseaaam lptagsvydy lscglgrfwa itgtisayfl
      121 vhvfagtaet ilsgimalvn feslnaafek hnsswlvgvg lvvtfaitni igikvfskle
      181 ivltagmwls lmifgilgla aapavhldgw fggsevgtsv pavlslvgma mfmfvgcefv
      241 tplapemksp grtipramal glvgvaicmf lygaairrqv anvpvspdgl thlldtpgai
      301 pafalqvlgp fgrvwfgiaf lcagaatint lmaglprily gmaidgalpr cfaylhprfk
      361 tpvvgivaaa ivpifhawli ngnldsilhl vlaatcawgt ayllvtasvv mlrirrpdlp
      421 rpyrsplfpl pqivssvgiv laiwyitppg mnardiyvpf gamlgltaly alfwtlvvqr
      481 rhpfkpvpve evlrnehvas
//
LOCUS       WP_175840439             302 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175840439
VERSION     WP_175840439.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32683
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdllatmriy vrvvergtms gaardldmgq pavserierl ekhlgtrlll rsartltcte
       61 egrifyersk alleaaddav asvsktenal dgtirlaapq cvgevvlpgv lthvrtaypn
      121 lhidlvlndd ivdpvtegvd isirvgqlgd ggfvahpvgt vgrrlvaaps ylerhgpidt
      181 tadlanhpfi rvkgvfaser lplqrdgdal dyarirtimt tshwrpmfdt ivagggigvv
      241 qqpacadala agtlvellpr yvipdfalnv lvhaqrplpp rvravvdllk qdlppllarp
      301 ar
//
LOCUS       WP_175840456             325 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia
            contaminans].
ACCESSION   WP_175840456
VERSION     WP_175840456.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..325
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=35229
     Region          106..320
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mraadlfavg afvmilaigl vlsswfdras rtpaqrirar mrrlspslag rdglasaapg
       61 valfnlqrrq grprawlqrr vtrvravggk ggvrivvast iagaivaiva vkligppgfl
      121 rpliyaglpl vtmrasyral verfrirfle afpdaidviv ravragipvt qaismvgdga
      181 aepvratfrs mgdslrvgad lknvltqaad rlmiadfsff tvylllqret ggslgetlde
      241 lssiirtrrd irlktralta egrittniis avpfvmigal flvnrdyvml lftthpghmm
      301 ltiaaglltv gllvirkisk ldtar
//
LOCUS       WP_175840479             335 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia arboris].
ACCESSION   WP_175840479
VERSION     WP_175840479.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..335
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34146
     Region          20..335
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mnlpdssstp sttlaatagn apppramwaq lrrstlfypl vglivvciam miaspsflsa
       61 anlenvlrqv sinaiiavgm tcviltggid lsvgsvmals gtlaaglmva gvnavaalai
      121 giavglgfgf lngvfvafag mppiivtlat mgiarglali ytggypidgl pdwvaffgsg
      181 kvlgiqapvm imlvvyaiaw llldrmpfgr yvyaiggneq atrltgvrva rvklivytla
      241 gvtsalaaiv ltgrlmsgqp nagvgfelda iaavvmggts isggrgailg tlvgalllgv
      301 lnnglnmigv npyvqnvikg giillaiyis rersr
//
LOCUS       WP_175840481             201 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            contaminans].
ACCESSION   WP_175840481
VERSION     WP_175840481.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..201
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21816
     Region          4..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 magrprefdr dmalkramla fwrhgyegts msdlveamgi asariyaafg skealfqeav
       61 alyeqgeggf adralgeetd vraavermlr davaaytrrg qphgcmmvsa atnysaeneg
      121 imewlaahrr artqsiverl qlaaeqgqla rgtdikalad fyatqlhgis vqsrdgvske
      181 rllasigpam mplamavrdg a
//
LOCUS       WP_175840483             319 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175840483
VERSION     WP_175840483.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18598969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..319
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35482
     Region          1..283
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          15..97
                     /region_name="cupin_MtlR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to MtlR, N-terminal cupin domain; cd06976"
                     /db_xref="CDD:380381"
ORIGIN      
        1 mmhpdlevve vrrdesfkvw shgypyrtir whfhpefelh livatrgkyf vgdhigsfgp
       61 ghlvllgpnl phnwvsdmae getverrnlv iqfdpafvrr cmdafpecrd aqalldearr
      121 gvgfdaatsa aiaplfdell aargmrrial fmtilerlcg aaertllasp aydqadvtpt
      181 rlshalsyig knlaselres dlaqltgqsv safsrafhrq tgmpfvqyvn rlriesacqm
      241 lladdanitd icfqagfnnv snfnrqfrav kgmapsefra lqrlnarsrd lalhaaptgn
      301 pmpprvltpg apelapqpg
//
LOCUS       WP_175840599             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175840599
VERSION     WP_175840599.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33823
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..294
                     /region_name="PBP2_CrgA_like_2"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08471"
                     /db_xref="CDD:176160"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176160"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176160"
ORIGIN      
        1 mdridamkvf vatldegsla gagrklgrsp aavsraiafl eehtgtally rttrtirlse
       61 ageryaaacr rilsdleead mlvadersap rglltvtapv aagedvlral ldefierhpa
      121 vsirlqlldr pvslidegmd valriahltd stlvaipvga vrrvvvaspd ylakhpaiet
      181 padlaqhrii smthfgldsw sfpppapsal pqvvqfaprf ivntirgava saiaghgvtr
      241 lfsyhvaepv rdgtlrivlr dsehaplpih lvtpygrlsv pkvrafvdfa aprlrehfar
      301 laaitdgdrt dgd
//
LOCUS       WP_175840606             487 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia contaminans].
ACCESSION   WP_175840606
VERSION     WP_175840606.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..487
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52014
     Region          58..467
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(68..69,72..73,76,110,160..161,163..165,168,188,
                     191..192,195,307,310..311,314..316,319,346,350,399..400,
                     404,408,424,427..428,431..432,435)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mnshsldlgg naggpasarp paaaagvgad asarparrvt lgdfmddlpv galhrfvvwv
       61 igiglffdmy eiflvstiga alqneyglsr qstdfkllla safigmfvga mclgsladri
      121 grrkaflltl twysafslvg afsvnadmlv acrfltgigv gaiypvadsf lseilpkekr
      181 grlaawaytt syvavplvgf lalwlnplhv ggvagwriil aigslgavyv llvrhrlpes
      241 prwllaqgrt adayaaarrf aegtgvrvpe qfaepvepqr plglgerial lrrepygary
      301 vmlaifhlfq gfgyygfgtl agtvvksrgf dvtdstlfia lsfigypvgs llsipllnwi
      361 errtlvivsi lsiavfglcf aysgntvliv gfgflttcas nvfsnayhvy qaeifparvr
      421 staigstyal srivsgalpf vllpvlgrdg agamfgvisv algivavtlr vlgplttrrs
      481 qdeinpv
//
LOCUS       WP_175840658             396 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia arboris].
ACCESSION   WP_175840658
VERSION     WP_175840658.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..396
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41154
     Region          13..395
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mnanatsgnp gdpvvivgtg lagytvarew rkldgdtplv misrddgsfy skpalsnala
       61 qrktpeqlam adartmadql ratirthcav rridaakhei vlddgdvqry ralvlatgad
      121 arrvrcegdg addvlsindl adyarfrggl sdcrsvamlg agligcefan dlvaagltvt
      181 vidpadapls rllpaeagrv fgqalsdagv qlrlgtgvqs iarlargyrl altdggqvea
      241 dlvisaiglt prialardag ldvadgivtd awcrtsvpdi falgdcaaid grvrpyvlpi
      301 mhaaralaqc lhgtptrvaf pvmpivvktp aipavvvaad gggrwttevg igdarhatra
      361 lcadpdsgrl tgfalldaat aekavllktm asdaan
//
LOCUS       WP_175840641             388 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia contaminans].
ACCESSION   WP_175840641
VERSION     WP_175840641.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..388
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41993
     Region          1..386
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mqfdltddqr aiesaiekic arfgddywle rdraggfpad fhaaladagw lgiamdpahg
       61 gaglgmteaa lmmrtisasg aglsgasavh mnifglnpvq vfgtdaqkar flppliagrd
      121 kacfavtepd agldtthlst qarrdgdhyl lsgrkiwist aqvankmlii arttpldqva
      181 kptdglslfy tdldrscvev reidkmgrka vdsnmlfidn lrvpegdlig qegdgfryll
      241 hglnperili aaeaiglgqa alrratqyac ervvfgrpig qnqsiqhpla qawmqleaaw
      301 lmvmkaatry dagqscgaea naakylgaea afqacqtava thggmgyake yhverylrec
      361 miprlapvsp qlilcyiaek vlglpksy
//
LOCUS       WP_175840661             344 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia contaminans].
ACCESSION   WP_175840661
VERSION     WP_175840661.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..344
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37554
     Region          180..323
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mlaevrpdgf tmldtyrlaf adglfavrdg aeirvaqgdg igaqllraql gddgalrlva
       61 ynhraapadq rrallaalaa afsdsarhaa irldpaawpa valdalrasg vladggrcmr
      121 egwaqqadlw rvgphlpcat lptftdgrrh prrppaprgd vyardlpalg vrftlrgwqp
      181 aedtarlvrw fdeprvrdgw pgtqpgtdgt qgaapgtdph vvplvgcfdg epfayveayw
      241 lkedalaphv aardydrglr mlvgesrwrg phcvagwlps vvhylflddp rteavgcavp
      301 agharvadhl arhgfarqrr laladaqplw mrtlretffs grhv
//
LOCUS       WP_175840685             391 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia contaminans].
ACCESSION   WP_175840685
VERSION     WP_175840685.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..391
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=41195
     Region          <248..391
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mktilwrssw rigraivrlt magylvlafg thvaaqgadg ttaldcsvgn veetpwqmrt
       61 pltsttplna ilygrtvsif vkfkygtapv ahefvtaahw lpgsvvpdgi aqtnvegigf
      121 kwagvsddgt ertlrqgpqp matakfalns aggggsdsmi mrfrqflvld kpasqlpqgk
      181 livkslsgnp tvaiyaldlp kgaasiggsv tvpevtvppn lcklpktytg vgnvcigsec
      241 eihvpnrcei qsnwivpvtl gnfsisnfps vnatskpvsf dialsqcaas akpaisfrdk
      301 atkpnpdktl lqlsapagqt vargfnivmt naltgeriay gepgaaaeyp mrrtgdmavm
      361 plraqyirtg aegelapgya gggaefsftf p
//
LOCUS       WP_175840711             328 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia contaminans].
ACCESSION   WP_175840711
VERSION     WP_175840711.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..328
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34734
     Region          7..236
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mndndqrtvr fgiigagsia rrfaqslahv pgatlagawa rradaatdfc eayggtpaas
       61 ldallasdid aiyvatlhds haqytlaala ackavlcekp atlntaqldt vlraardagr
      121 lfmeamkppf fplyrqlrah lhddpigeir lvragcasss vpddhsvyrl draggalldi
      181 giyeaflavd wlgaaldvqt lgrvgatgvd lfaslnsvha nggiaqifcg ldvmgrgdal
      241 iaapgghvti hekwwnpara tiryadgrtv eldapvdggg lnyetahfce llragktesp
      301 imthdhsrqm iamtdaaraa lgvrysge
//
LOCUS       WP_175840748             467 aa            linear   BCT 11-JAN-2025
DEFINITION  HdeD family acid-resistance protein [Burkholderia arboris].
ACCESSION   WP_175840748
VERSION     WP_175840748.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..467
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=51624
     Region          10..185
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mvrlvllllg ieylrtrwrg ltvlgwlwva agvgifvdal dgalhfpiel fawlfliegl
       61 atlavagsgv ggqrilryvk givvvvaagl vfaghhhghf llsmifgtlf lvdgllqcts
      121 awmvryrrwn vafawgivei llavfffqpy pthyvgtvpy clglllmfgg mhmlslaarv
      181 rrltrnpafa tspapafvpd lddardrprf aqsewdgppa dgehaltvhv wtptgtskae
      241 aqrypvidry iaavdvngvi stghaalesp egiyislypg veidrspdef trilratren
      301 dvpglfqpdy ateskawcps tvrvrirnyd pvkldafwss yrqnvtynlt yrncsstvsn
      361 aleaaldgav wrlkgaragw gafvrllltp elwvaaqirk ravtmawtpg ltldyarals
      421 mladprpfaw wkvarsavsa imasrrawre qdsaalspgg seaasmk
//
LOCUS       WP_175840757             390 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia contaminans].
ACCESSION   WP_175840757
VERSION     WP_175840757.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..390
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42766
     Region          12..282
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 midgqillgh sirwgmvggg vgsqigyshr saalrdgsfe lvagafdidp ergrqfgvkl
       61 gvaaercypd yatmfdaear rpdgiravsi atpnnthfei craalnaglh vvcekplcft
      121 ieeaealqrl sveknrivgv aygysghqmi eqaremiarg dlgeirivqm qfahgfhseg
      181 veaasaaarw rvdpkfagps yvlgdigthp lyisevmape lkirrlmcsr qsfvksrapl
      241 ednaftimey dtgaigyvws savnagsmhg qkvrvigska siewwdehpn qlryeiqgqp
      301 aqvldrgmgy lhphalredr igaghpeglf eawsnlyarf alamdaadrg dvaavkairi
      361 pdvhagvegv rwvencvrsa dagsvwvdyr
//
LOCUS       WP_175840764             409 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            contaminans].
ACCESSION   WP_175840764
VERSION     WP_175840764.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 409)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..409
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41771
     Region          32..313
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mrsrtlagvv rwslfsacav lpawlwphga vlgylaqtaa lvvlalsynl qlgttgllsf
       61 ghaafaglga faaahwfnhf ggplpllplv ggvagagfgf aagllatrrs gtafamitlg
      121 lgecvaaaaw svpawfggig gvpidrasgt pwgawhfgap vqayaviaaw clasalamha
      181 ltrtplarla navrdnpvrv aalgsdprrv rlamvtcasf fagvagtltl idveiatpds
      241 vsmarsatvl iaaviggtga ffgpaagaav ltvlsivvag vsrawalylg vlfvvivvaa
      301 prgiagivqa lahalrrgap aaerwrmlca agacvfwgva lvcvaelgya wrfaqddgag
      361 fafgawsida dtpagwavac safgigtllw gwrarlvpgg qarkredgr
//
LOCUS       WP_175840769             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175840769
VERSION     WP_175840769.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33685
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..291
                     /region_name="PBP2_CrgA_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08475"
                     /db_xref="CDD:176164"
     Site            order(103,107,146,161,163,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176164"
     Site            order(104..105,109..110,112..113,116,120,122..128,190,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176164"
ORIGIN      
        1 mtdrldgvtt fvqvvesgsf alaaerldmt rsavgkaiar lekrlgarll qrttrsqslt
       61 ddgqayydrc vralseleaa eadldcgrne argklrlsvp lafghhcvtp ivldlarnyp
      121 hlridvsitd rfvdlveegi dlavrigtla dstslavrrl gtqygslgaa psylarygmp
      181 ktlddlkhhr tiaysrsgai qpwdlrapdg stvridmphq lsfddvqaia aagasgfgia
      241 wvpswlldqy vkrgemvvvl drcfvcegdi haiwpktryl prktrcvida laqaippmie
      301 rpvear
//
LOCUS       WP_175840771             379 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Burkholderia
            arboris].
ACCESSION   WP_175840771
VERSION     WP_175840771.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..379
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41840
     Region          26..362
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 mstpvtkhda faehapevlf rvvnrvalit lnrpaalnal syamigelaa lfercrtddq
       61 ivavvlrgag ekgfcaggdv ralyrmvaqr dtwlpffvde yrldyaihtf pkpvvalmdg
      121 vtmgggmgla qgaalrvate rskiampetr iglvpdvgat hflsrmpvel elyvgltgam
      181 lsgadaltak ladlcvpsaw ldtfetries vkwdgdalpl lrkvfeppcn vvphavldsq
      241 mpwivrhfdk rstverivat ltqdlareel srehrqwlqa tldalashsp tmlsvtreal
      301 lrgrqmtlae sfrmelgiva raieegdfce gvrahlvdkd rkprwapasl vevraervrh
      361 fltspwklfa hpladlgaa
//
LOCUS       WP_175840857             727 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia arboris].
ACCESSION   WP_175840857
VERSION     WP_175840857.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..727
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79095
     Region          55..727
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mmkgarvarf grwrpslylg lliaahpaaa fadaapaaga evkkeaaaaa paagelkais
       61 vnasrgvadd psvatvgkmp lalreipqsv svttreridq qnlfsldevm qqsagvtvqp
      121 yvllttayfv rgfkvdsfef dgvpvvigdm asapqdisvy erveilrgan gllhgsgnpa
      181 atvnlvrkrp qyqfsahasv svgswdryra eadiggplna agtvrsrlva ayedrhffyd
      241 hakqdtrsiy svtevdvtrd tlltfgaqyq ttssvpdmsg vpmardgssl glsrstfldt
      301 awgrfnwdtt rafasveqkl gagwkakvsg eyqsvrsdlk yagsfgaidp atgaggrltg
      361 gayqfssysr sldanvqgpv hafglthdll fgvtyansss gqmtapllgd vsgtpvnvyr
      421 wnpssvpepg igpyqqsqqn disqkgvygl griklaepvt lvlggrmsww nqdslgahyn
      481 tghqftpygg liwdfardws wyasyaevfq pqtksmwggg iltpvkgrty etgvkgelag
      541 gklnvslaaf ridldnnpqv dnahpcagps cyyvnggsvr sqgfefeang ritpwwtvwa
      601 sytydtmrya dnlanagasf spllnprhlf rlwtnydlpw qerrwsiggg vqvqsnysaq
      661 ssgvtmtqgg yalasvrlgy rydkhwsaal nvnnlfdrny ylslsqpgwn nrygeprnvm
      721 ltvrgqf
//
LOCUS       WP_175840827             437 aa            linear   BCT 11-JAN-2025
DEFINITION  leucine-rich repeat-containing protein kinase family protein
            [Burkholderia arboris].
ACCESSION   WP_175840827
VERSION     WP_175840827.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Shen,K., Hines,A.C., Schwarzer,D., Pickin,K.A. and Cole,P.A.
  TITLE     Protein kinase structure and function analysis with chemical tools
  JOURNAL   Biochim Biophys Acta 1754 (1-2), 65-78 (2005)
   PUBMED   16213197
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   5  (residues 1 to 437)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   6  (residues 1 to 437)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
REFERENCE   7  (residues 1 to 437)
  AUTHORS   Hanks,S.K. and Hunter,T.
  TITLE     Protein kinases 6. The eukaryotic protein kinase superfamily:
            kinase (catalytic) domain structure and classification
  JOURNAL   FASEB J 9 (8), 576-596 (1995)
   PUBMED   7768349
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..437
                     /product="leucine-rich repeat-containing protein kinase
                     family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=46295
     Region          <2..>186
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          39..61
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          62..84
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          85..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..175
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          211..>376
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(214..217,220,222,238,240,269,287..290,345,349..350,
                     352,362..363)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
ORIGIN      
        1 mthtleqlqa gqlsgarqlk lacgltefpr eifdladtle vldltgnals alpddlprlh
       61 rlrilfasgn rftafpdvlg acgqldmigf kanrigtvpr galpralrwl iltdndigel
      121 padigdcsrl qklmlagnrl ralpaemaac ralelvrlsa nrldalpdwl phlprlawla
      181 vagnpfgaap eaaasagpdv aaidwasltc eqklgegasg viyraqwrad gqpprtvavk
      241 lfkgavtsdg lpdcemaacl hagrhpnvip vigkvrghpd gthglvmelv dpaltnlagp
      301 psfasctrdl yaadtqfdpv eavriahgia svaghlharg imhgdlyghn ilhdgeggal
      361 lgdfgaasly evndrtlgar ferlevrafg yllgellerc ephagaldal aaaclnedvd
      421 arpsfgaita alaahlr
//
LOCUS       WP_175840865             373 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia contaminans].
ACCESSION   WP_175840865
VERSION     WP_175840865.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..373
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39588
     Region          17..354
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(37,39,70,112,240,308,328,330..332)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(37,39,70,112,114,121,188,191,193,240,248,308,328,
                     330..331)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(39,114,188,191,193,331)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            193
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mtldtspprr ttlpgatlfd plefggitlg nrivmapmtr sragagdapg ainatyyaqr
       61 asaglivteg tqisplgkgy pftpgiysda qidgwkrvtd avhreggrif aqlahvgrig
      121 hpdlqpdgal pvapsaiqpd gqaftpsgpk phpvpralgt delpglveey ahaaqaalra
      181 gfdgveihag ngylldqflr dgtnrrtdqy ggtidnrirl pldvvravgr vvgparvgvr
      241 ispvtphfgg iadsrpqalf dqfadrltgl atylhvvegi pqgaadqapp fdyralrraf
      301 ggfyianggy tkaraqqald dghadlvsfg ypfianpdfv triqhdrpla hadmstaygg
      361 seagytdypt let
//
LOCUS       WP_175840871             550 aa            linear   BCT 11-JAN-2025
DEFINITION  (2,3-dihydroxybenzoyl)adenylate synthase [Burkholderia arboris].
ACCESSION   WP_175840871
VERSION     WP_175840871.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..550
                     /product="(2,3-dihydroxybenzoyl)adenylate synthase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0008668 -
                     2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
                     [Evidence IEA]"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=59502
     Region          19..543
                     /region_name="EntE"
                     /note="2,3-dihydroxybenzoate-AMP synthase component of
                     non-ribosomal peptide synthetase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1021"
                     /db_xref="CDD:440644"
ORIGIN      
        1 mqssppslaa avpadapdwp ddfarryrda gywqdttffd aldacaqrhp dalaivdgac
       61 rlgyrdlldr irrlagglar lglargdavv vqlpngarfi etcfalfqlg vrpvlalpah
      121 rlyeigafcr fagaraylca sqlgdfdcrp laaalqadcp alehivmagd dhsftsfdal
      181 ydappvhaca ahaddiacfq lsggttgtpk liprrhreyl ynvracsaas gfdadtvyla
      241 alpmahnftl ccpgtigall aggrvvttar pepdqsfali aqervthtal vpplallwld
      301 eqpqrqadls slrvlqvgga rlmdhaaerv tpvlgcrlqq vfgmaeglic ctrlddsper
      361 iahtqgrpvs eadevrivde agepvapggi gelqvrgpyt irgyyrladh naaaftadgf
      421 yrsgdrvrrt adgdlvvegr dkdqinrgge kvsaeevenl llahpqvhda avvampdpml
      481 gertcafvva rapaptrltl krylrdcgla afkipdrief mprfpetgig ktskkslrdl
      541 lrrqlqaaaa
//
LOCUS       WP_175840873             257 aa            linear   BCT 11-JAN-2025
DEFINITION  thioesterase II family protein [Burkholderia arboris].
ACCESSION   WP_175840873
VERSION     WP_175840873.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..257
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=28734
     Region          17..250
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mtvhptdsiw irelrlspca raqlvcfpha ggtanffrnw sralpwdvdl lalqypgree
       61 rfgepclqsi ealagpaada lqryahaplv lfghslgaal ayevavrlea rgaaplyvav
      121 salppphrqr lsdlhlqsdd alvgdvarls gehaalladp emraiylpmi rhdyraiety
      181 rrdrpprida plgvmlplad teldndeaha wqdvaarpir ietfngdhfy lrhqypavia
      241 hlveridqsl rygkeyt
//
LOCUS       WP_175840883             249 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia arboris].
ACCESSION   WP_175840883
VERSION     WP_175840883.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..249
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26064
     Region          2..234
                     /region_name="17beta-HSD-like_SDR_c"
                     /note="17beta hydroxysteroid dehydrogenase-like, classical
                     (c) SDRs; cd05374"
                     /db_xref="CDD:187632"
     Site            order(8,10..13,33,51..53,75..78,98,125..127,140,144,173,
                     175..177)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187632"
     Site            order(99,127,140,144)
                     /site_type="active"
                     /db_xref="CDD:187632"
     Site            order(127..129,134,140,171..172,178,194,197)
                     /site_type="other"
                     /note="steroid binding site"
                     /db_xref="CDD:187632"
ORIGIN      
        1 mktvlitgcs sgfgleiarh flardwrvva tmrtpredal ppsanlrvlp ldvtnadsir
       61 aaidaagpid vlvnnagfga aapaeltpld tvralfetnt igtialaqav lpqfrergag
      121 vivnvtssvt lkalplvsay raskaavnaf tesmavelap fgvrthlvlp grapdtrfgd
      181 naranmygfe heayadfvgk aiarmldasa pithaedvae avwraatdps spmrmpagad
      241 aeawaaeag
//
LOCUS       WP_175840924             164 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia arboris].
ACCESSION   WP_175840924
VERSION     WP_175840924.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..164
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=17191
     Region          1..148
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 midivvndtr hslenvpedm pllwvlrdrl kltgtkfgcg kglcgactvh legqavracl
       61 ipavaangrh vttieglsad grhplqlawv aedvpqcgyc qpgqlmqaaa llkggkpvdd
      121 ativsamsgn icrcgtyari hraikraasg dpalkavaep akea
//
LOCUS       WP_175840957            1003 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia arboris].
ACCESSION   WP_175840957
VERSION     WP_175840957.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1003)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 1003)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1003
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..1003
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=106712
     Region          126..870
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mggaltsgam qvaaaanplv gkvaptasav mqalaaggnp aqiaasmaap aagmlnpvag
       61 qlasgamagm rgltasaspa aaagaapavd dhplagqsls dlasapqffv pgqtqgqpga
      121 lgsllpfset trllrlqsal tgnralsiaa ikggealsem prytldliaq npsidlkdvl
      181 nqavtvnial qdgserqihg ylvrfgfern dggvahyrgd lvpwlwylgk rvnsriyqqv
      241 tvldvlrkvf adygalvdyq thikqelkpe dfvvqfqesd lnfvsrller hglfyyfeyr
      301 qdghtlviad dsvscpdqah dpvvnynats gvqqadrlta lsasretqpg vvalhtfdyk
      361 hpksrpyvel ptladqgnap klevydgssa faykntsege aeakrrlevy ewqakvfrge
      421 sgcrgltvgr kfkidghfwf dpakqddnef lvvgididak nnfgdasaqp gsfrssltli
      481 rskipyrper rhdkpvmpgp qsaivvgpkg qeihtdgmgr ikvqfpwdry gkndqesscw
      541 irvsqpwagr gwgtvaiprv nqevivdfln gdpdrpiivg rmfnaeqtpp yalpdgahqm
      601 gfhsnstpgg ggfcevvihd kkgeelvnih sqkdmattvq nnhvtvvngp nqtnvvtqgq
      661 hasivrkais vqsqdehiqh taktavilha qeqhmalkak gpvqiesdte hvhvkgsqsi
      721 vlecgkakit lsadgqivld gtrivvlgsq svdlnpdgtt gpaspplvpv tdpadpepna
      781 aapvaggggg ggggaaaaap ahgknhakgp akkavatglg agvdklaaks ptlerdiskl
      841 qkdgwqiqyg panqgsstnk hgqpptivid sndrgnpkav vqglahetgh alyqgtpdys
      901 sktnyvnsel adegaatmnn ikvqreilth ggpdiqiagn pdnapaynaa ynqfvhngda
      961 gaaraaighv ygtgeyasvp vngqyvnyqt yygswydrny psh
//
LOCUS       WP_175840932             457 aa            linear   BCT 11-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Burkholderia
            arboris].
ACCESSION   WP_175840932
VERSION     WP_175840932.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..457
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47183
     Region          21..430
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mnsashpvdr vlprrqmltl glqhmlvayi gaiavpliva salkmspadt tvlistalfc
       61 sgistilqtv gvwklgvrlp ilqgvafssv gpviaigltp gvgfagvcga vigagiittf
      121 aaplvgrlrr lfppvvtgci vtviglqlfp vayqwagggd aaklqfgels flavalvvav
      181 vilavnrfan aflrnlsvli glvagsllai algmgnftnv aaapwftvpy pfhfgtpvfa
      241 ivpvltmvvv mivqmvesmg lfvaigdive kqvseedvvr glrangvasa iagtfaafpf
      301 iafmenvglv iltgvrsrwi vavsgvlmcv valvpkigai vastpsaalg gagiamfgvv
      361 vaagvqtlak vdfennrynv livgftiata lipvmapkvf ahmpdwtqpf lhsgvvlacl
      421 vsvllnavln gvpaaepves hahadaahrs pmarecd
//
LOCUS       WP_175841042             287 aa            linear   BCT 11-JAN-2025
DEFINITION  glycine betaine ABC transporter substrate-binding protein
            [Burkholderia arboris].
ACCESSION   WP_175841042
VERSION     WP_175841042.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Wolters,J.C., Berntsson,R.P., Gul,N., Karasawa,A., Thunnissen,A.M.,
            Slotboom,D.J. and Poolman,B.
  TITLE     Ligand binding and crystal structures of the substrate-binding
            domain of the ABC transporter OpuA
  JOURNAL   PLoS One 5 (4), e10361 (2010)
   PUBMED   20454456
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Gu,Z.J., Wang,L., Le Rudulier,D., Zhang,B. and Yang,S.S.
  TITLE     Characterization of the glycine betaine biosynthetic genes in the
            moderately halophilic bacterium Halobacillus dabanensis D-8(T)
  JOURNAL   Curr Microbiol 57 (4), 306-311 (2008)
   PUBMED   18661182
  REMARK    Erratum:[Curr Microbiol. 2009 Dec;59(6):65]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194542
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..287
                     /product="glycine betaine ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30686
     Region          30..284
                     /region_name="PBP2_OpuAC_like"
                     /note="Substrate binding domain of Lactococcus lactis
                     ABC-type transporter OpuA and related proteins; the type 2
                     periplasmic binding protein fold; cd13639"
                     /db_xref="CDD:270357"
     Site            order(39,41,87,115,145,149..150,195)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:270357"
ORIGIN      
        1 mklfgkllwt galsamvals asaladtkpt lkigyvegwd dsvatsnvaa rviekklgyq
       61 vqlvpvaagi mwqgvargdl datlsawlpv thgsywdeyk akvvdlganf pdakiglivp
      121 ayvkaksidd lnaekgsfng rivgidagag vmrktddaik syglnytlmp ssgsamtael
      181 srsvnankpv ivtgwaphwm fakwklrfle dpkkvfggae hvdsvvnpgl etkakpvvaf
      241 lkkfqwkpge idsvmlaiqn gskpeaaada wiaahadrvn awtegaq
//
LOCUS       WP_175841111             304 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia contaminans].
ACCESSION   WP_175841111
VERSION     WP_175841111.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..304
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32506
     Region          14..284
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mpmhpapspa plceidglki gfrghdgtvt davrdlsltl apgerlgivg esgsgksltg
       61 rallgllpda arwsartmrf aghdllamsp gerrrlcgsq mgmilqdpky slnpvmtvak
      121 qmgeafrlhe pglrgralre rivdalaavq irdparvada yphelsggmg qrvmiammvs
      181 tgprlliade ptsaldvavs mqvlavldam iarhdtgllf ishdlplvms fcdrvavmya
      241 grvvetcaar dlrdashpyt rgllaanppl anppdelpvl rrdpawlepa shggtpadrq
      301 eaar
//
LOCUS       WP_175841117             297 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175841117
VERSION     WP_175841117.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32837
     Region          6..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mprdnfadll afiavarers ftraaaqlgv sqsalshtir sletrlgvrl ltrttrsvap
       61 teagerllqn laprfdeiea elsalaelrd kpagtvrina tdyvirtllw pklapmlrdy
      121 rdlkvefvtd yglsdivaer fdigvrlgdq vakdmiavri spdlkmaivg apayfaerar
      181 pdtpqdlvth dcinlrlpth galyawelar gdeslqvrvd gqvtfngtye mldaalagyg
      241 layvpaelaa phveagrlhs vlddwcptfp ghhlyyasrr qssralaviv ealrmra
//
LOCUS       WP_175841148             146 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Burkholderia].
ACCESSION   WP_175841148
VERSION     WP_175841148.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..146
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15187
     Region          26..138
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mirsinraly rtaaqtpavs ailsvlvril iagvyvgagi skifnyagte qymahmgvpe
       61 allplvifve vagglaliag fmtrlaalgl aifsviaavi fhsggdqtqq tffmmnlsmt
      121 ggllalvlng agrasfdrgd raslpe
//
LOCUS       WP_175841164             291 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175841164
VERSION     WP_175841164.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..291
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32480
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..284
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,220,237,264)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     214..218,225..226,229)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mellndmalf vevvkargfr saaqalgmpn stlsrrisal ekaiglrllh rttrrielte
       61 agqlyferck rivdearlah eqlggllaep agvlrasfpv dfaviyltpl ivdfanrypk
      121 ltfdfeltsr rvdlvsepfd vairigesad sqlvarrlat frnylyaspr ylerageple
      181 pgdlarhqcm svqrlatwtl rrgeqavevp vggrfvvnsv gmnrqlavhd agiiqlpeev
      241 vaddvaagrl rrvlpewega lvpvfamtet rllpaktqvf ieflrahfaq g
//
LOCUS       WP_175841180             355 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [Burkholderia].
ACCESSION   WP_175841180
VERSION     WP_175841180.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..355
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38336
     Region          18..341
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mtpdvpaspl aepaprrirf givllpnftl tafsgfvdml rlsaddgdys kpvrcawsvi
       61 getlapvras cgiqitpwet fdaaepfdyv vvvggllhsg pqagpetlgf irnaaaagat
      121 vvgictgvft lmragvldgy rtcvswfhyw dfierfpaad pdlliadrlf vidrrritcs
      181 ggrasidvaa aillrhfdha tvqkalrill vgemqkgnap qphppglepa thpkvkrail
      241 lmeqhvgral pleelackld lstrqlerlf kaetgkspqa fakqvrlrta awlltssdrt
      301 vadiasscgf adashlgref rkqfgvppat yrerggevae agepaaadpv edlad
//
LOCUS       WP_175840790             469 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatase PAP2/dual specificity phosphatase family protein
            [Burkholderia contaminans].
ACCESSION   WP_175840790
VERSION     WP_175840790.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Pulido,R. and Lang,R.
  TITLE     Dual Specificity Phosphatases: From Molecular Mechanisms to
            Biological Function
  JOURNAL   Int J Mol Sci 20 (18), 4372 (2019)
   PUBMED   31489884
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Patterson,K.I., Brummer,T., O'Brien,P.M. and Daly,R.J.
  TITLE     Dual-specificity phosphatases: critical regulators with diverse
            cellular targets
  JOURNAL   Biochem J 418 (3), 475-489 (2009)
   PUBMED   19228121
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   5  (residues 1 to 469)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12932297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..469
                     /product="phosphatase PAP2/dual specificity phosphatase
                     family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=49988
     Region          43..217
                     /region_name="PAP2_Aur1_like"
                     /note="PAP2_like proteins, Aur1_like subfamily. Yeast
                     Aur1p or Ipc1p is necessary for the addition of inositol
                     phosphate to ceramide, an essential step in yeast
                     sphingolipid synthesis, and is the target of several
                     antifungal compounds such as aureobasidin; cd03386"
                     /db_xref="CDD:239481"
     Site            order(118,126,152..154,189,195,199)
                     /site_type="active"
                     /db_xref="CDD:239481"
     Region          321..459
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
ORIGIN      
        1 msalgggasg laepasaaga rdasfalrfg wlammgavff stygfanwla vrraavptfs
       61 fgwehaipfv pwtivpywsi dllyalsfff wtrradlldh vkrlltvqli svacfiawpl
      121 rfgferpdag gvagalftll mgfdkpfnqa pslhigllvv lwavyakhlr gtlarvvlhl
      181 wfaaigvsvl ttyqhhaidv ptgaavgcla lflfplrdaa grlpgadasp gaagralarr
      241 yalgaaaval valgcvsrap gwalaagwva lalacvawiy rrgapgafqk gahgrfpvvi
      301 rwllapaiag afvnsrlwtf rqpapvride rvsigrtptt rdvrrhgfta lvdltaempr
      361 wasidassla yatvpqldlv aptaaqlaqa vaalerlhge grdvlvccal gygrsvlcaa
      421 awlaarrglg dardalaavr avrphavwsd dgvavlqqwi drrrgagga
//
LOCUS       WP_175841186             441 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia arboris].
ACCESSION   WP_175841186
VERSION     WP_175841186.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48454
     Region          30..433
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(43..44,47..48,51,83,133..134,136..138,141,161,
                     164..165,168,265,268..269,272..274,277,305,309,360..361,
                     365,369,385,388..389,392..393,396)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtaldaaasr spaapahaae ldrtykkvfw rivpflmlcy vvayldrvnv gfaklqmsqd
       61 lafsetvfgl gagifflgyf lfelpsnmlm hrlgariwia rimitwglls alfafvktpt
      121 qfyvlrfllg laeagfypgv ilyltywfps hrrakiiavf msaipvsgif gnplsgwime
      181 rfhggsgfhg wqwmfmieav pavlvgiati lyldnsirsa kwlderekql leneiaaqpq
      241 eqqqhghslk avfsdprmww msliyfafvt gqygltfwmp tlvkstgitd tlqigllsai
      301 pflvaivvmn lfghsadkrr errwhlivpa lmgalgfava asyshntavs ivflslaagg
      361 vltcaplfws lptaflagsa aaagiaiins vgnlagfasp yvigylkdvt hstssgmyvl
      421 aamlvigaia vwltpaklvn r
//
LOCUS       WP_175841251             314 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Burkholderia contaminans].
ACCESSION   WP_175841251
VERSION     WP_175841251.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..314
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31538
     Region          2..314
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtilviaehd nasikaatln avaaaqalna vgggdvhvlv aghgaqaaan aaakiagvtk
       61 vlladapqla dglaenveat vmnvangyah ivasataygk niapriaakl dvaqiseita
      121 visadtferp iyagnaiatv qsgdpvkvit vratgfdpva seggratvek idaaadagts
      181 rfvsrevtkl drpeltsasi ivsggrglgs genytkvlep ladklqaalg asraavdagy
      241 vpndyqvgqt gkivapqlyi avgisgaiqh lagmkdskvi vainkdpeap ifsvadygvv
      301 gdlftlvpea aaal
//
LOCUS       WP_175841280             429 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia arboris].
ACCESSION   WP_175841280
VERSION     WP_175841280.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..429
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44939
     Region          8..410
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(21..22,25..26,29,61,111..112,114..116,119,139,
                     142..143,146,237,240..241,244..246,249,277,281,339..340,
                     344,348,364,367..368,371..372,375)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mkqksqawft vfllflvygi nyldrvalsi vapivqtdlg idaaqmglvf stffigyalf
       61 nfigglasdr lgpklvyvls vglwsvfcgm taltvgfvsl livrllfgma egplcsaank
      121 mvnnwlprda aatamgllsa gsplggaiag pivgllaaqf gwrpafwivc aiglawvvvw
      181 mmsttdrpaa pandasnalr apaatlaast tadaatpsht lahyvrqpri lataaaffsy
      241 nyvlffflsw fpsylvrahh lnikemsvat vvpwlvgtvg lacggaisdg lyrltgnlll
      301 srrivlvtcl lgagacvaia gavqstqgav vlmsvslffl yvtgaiywai vqdvvhparv
      361 ggvsgflhcm gslsgvigpa vtgliversg sfasafvlag aialvgavla gvfvrnarps
      421 evlrertah
//
LOCUS       WP_175841362             441 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia arboris].
ACCESSION   WP_175841362
VERSION     WP_175841362.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46990
     Region          9..414
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(22..23,26..27,30,69,127..128,130..132,135,155,
                     158..159,162,243,246..247,250..252,255,283,287,339..340,
                     344,348,364,367..368,371..372,375)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mgtsvkqpkr aalasfvgtt iewydfysya taaaivfgpl ffpgenrfis llasfgsfav
       61 gffarplggv mfgylgdrfg rkrsllatlm lmavstvaig llpthaqagv iapillvlmr
      121 vlqgiavgge wggavllage hapegkrtff asfaqlgsas glilsmlafg aistlskddm
      181 mswgwrvpfl assvllivgf virasvsesp efeevkksgn iaekplreal kywpllllai
      241 ganvygiagv yfsnifmisy atqflsldrs mvlhcmtiva vlqfvvqlaa aflaqrfgtt
      301 rvllitgawa aivpflmlpl vhmgtplsit vgvglatlae sgyysvvagf vsgifvarir
      361 ytaisiayqv cgalaggltp lvatiiaqnt apqwwplalq ymsaavlssl cvwlisrrvs
      421 iddvgaprkr ddalpraart a
//
LOCUS       WP_175841363             766 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Burkholderia contaminans].
ACCESSION   WP_175841363
VERSION     WP_175841363.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..766
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=83933
     Region          178..765
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 msyvvavram ceftarrgdl dlrftpapta legiaghgav tsnrgaryet eialtgtwgt
       61 ltvrgradgy dpvanrleei ktyrgsldam panhralhwa qakvyahlmc dargfqeidv
      121 alvyfdivse retvltqtlg avelatffae qcacfvgwae retahraard aalralafph
      181 gqfrsgqrel avavyraard erclmaqapt gigktlgtvf pllkacgege ldhvyfltak
      241 tpgralalea attlgagtpa lplrvlelva rdkacehpds achgescpla kgfydrlpaa
      301 rdaaieagll dretvraaal ahdvcpyyls qelarwsdmv igdynyyydg samlhtlaqq
      361 nqwrvgvlvd eahnlldrar kmysasldpf afaaareiap aalrkafdrl arvwgsvsra
      421 qaeryaafpe ipgpivsavq nlvaaigehl adaprangda llrfhfeaiq fgvlaeafds
      481 asifdatlhg epmprqpald gvvsagrrrr vqstlcvrnv ipagflapry eaacatvlfs
      541 gtlspfhfyr dtlglpgdtg wldvdgpfra eqltvrvash vstrwrdrdr slepiadlia
      601 aqyatrpgny lgflssfdyl grvvalmqar hpdvpvwaqa pgmaeserda flarfdaggr
      661 gvgfavlgga fsegvdlvge rligafiatl glpqvndvne qmrramdarf gngydymyly
      721 pglqkvvqaa grvirtehde gvvhliddry rrrevrdllp rwwrig
//
LOCUS       WP_175841375             864 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia contaminans].
ACCESSION   WP_175841375
VERSION     WP_175841375.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 864)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 864)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..864
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..864
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=93322
     Region          59..712
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mhpfqpsstr vnrrnvssvr afcarwvara qpvaaaavar vkpfaatawq hvrhptrrgv
       61 llagaavpal fvvyvvvlip ftpgigdirk arvdqpaqvl sadgkllaef kpsnrewvpl
      121 kqisphmvda liatedhrfy ehhgldwkrt asaalhtfsg srqggstitq qlarnlypde
      181 igraptltrk vkeaitalki eavyskdqil etylntvpfl ynaygvemaa rtyfdksade
      241 ldvldsatlv gmlkgnsyyn pvlnperalq rrntvlgqmv kygklspaqf aqlqrrplri
      301 dferqkeppg paphfaqqlr kwliawadrn dyniysdgli vrttidsrlq qmatqaltlq
      361 gnqlqgiann awsgrdgcgt dnevfrtfmr espeykaaqd agkddaaamk llaadrgfmr
      421 alcktktdvq agflaidprd gqirawvgsr dftnepfdhv aqarrqpgst fkpfvygvaf
      481 angmkpddtf idqpveiplk ggeiwrpndd vpptgkpmtl rdavalsrnr itaqvmekvg
      541 paavarlard mgvrespler vpslalgtsp vtlkemvasy atiangglyv epqmvtrien
      601 rqgdvlaeya papperalda etdktllsvm rdvvtrgtgg sirtrfgirg dvagktgttq
      661 dnadgwfilm qpglvagawv gfddgrvtlr sdywgqgahs alpmvgdffq raqrarivdt
      721 kakfdtepsp gwfaslrerv tdlvdtwfpp eakkapapar tqrverapda dtgaasaasa
      781 asapeaasgg iveewvpase vaasaaalse gasqpqpqpa qppagasaag gsstglgaap
      841 aavpsaapsp apvqaapdap gasq
//
LOCUS       WP_175841430             241 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Burkholderia
            arboris].
ACCESSION   WP_175841430
VERSION     WP_175841430.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..241
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26249
     Region          1..239
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mitldnvskw ygkhqvlsac saavskgevv vvcgpsgsgk stliktingl epfqkgsitv
       61 dgtrlgdpaa klaqlrarvg mvfqhfelfp hlsitdnltl aqikvlgrrk deavenamrl
      121 lervglkaha hkypgqlsgg qqqrvaiara lsmnpvamlf deptsaldpe minevldvmv
      181 elaregmtmv cvthemgfar kvahrvifmd qgavvedaas drffaaprse rardfldkil
      241 h
//
LOCUS       WP_175841492             450 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia contaminans].
ACCESSION   WP_175841492
VERSION     WP_175841492.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..450
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47853
     Region          22..421
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msaslaassl spqprslrll stddadadga rfaalldrla pelaadaarn dadgrfphen
       61 farlhragli aqvvprehgg agatlaqasr ivaavaradp atalvltmty lqhralgrad
      121 nrwpaqvrra vfdsavtqga linalrvepa lgspsrgglp etlarrdgdg wrlsghklys
      181 tgipalrwla vwartdepap rvgvflvprd rdadgdrirv ieswnhlglr asgshevvfd
      241 dvrlpadhav dvrapdawav saathadada qadqqawmva llgslydava rasrdwlvgf
      301 attrapsglg aplatlprvq eavgeiegwl hanrvllddh iartdaghap tvttsglvkr
      361 tvtehairvv eqalklsgnh glsrvnpler hyrdvlcsrv htpqddaiav aagravleaa
      421 spskteratk getetsgasv netergrgda
//
LOCUS       WP_175841494             558 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein [Burkholderia].
ACCESSION   WP_175841494
VERSION     WP_175841494.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..558
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=60569
     Region          27..556
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 matvtpratn eslhptigaa rltlgnrill sfgvlfvlml vtagvsyerl rainseavsi
       61 erdslpgvyl asslrgsvne sftllqqatf vdtesetvqr dlakisdalk dieslsvdyq
      121 sttfrdddrq rfatfrgayd ryvpllneav qksrvsreea vaayakalpa wtevvrnanv
      181 lvqenrkfae qsakmiresv qdtevvlata lafvllsalg lgyvlyrsvt vpmarlvevh
      241 dvmrtgnltr rldlrrrdef gtletgfnrm adeltelvar aqqsslqvtt svaeiaatsr
      301 eqqataneta attteigats reifatsrdl lrtmnevagv aeqsatlagv sqsgltrmge
      361 tmrsvmdaag svnaklailn ekalninqvv atitkvadqt nllslnaaie aekageygrg
      421 favvateirr ladqtavaty dieqtvkeiq savsagvmgm dkfseevrrg mldvqqvggq
      481 lsqiiaevqt laprfqmvne gmqtqangae qitqalsqls eaaqqtaesl rqssqaiddl
      541 tlvanqlrts vsrfkvda
//
LOCUS       WP_175841554             235 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia arboris].
ACCESSION   WP_175841554
VERSION     WP_175841554.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..235
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24639
     Region          51..149
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mslpasaakf dpsraqeyae qsrialagyd acheltacml asaigvtdar ilvagaggtg
       61 qeicvaaale pgwqftavdp svpmlalars nveaagfgar aafvedgvda lpdtpafdga
      121 tligvlhhvp gdeakaallh aiarrlkpga plvlagnhrr yadhprllda wqqrwrmkga
      181 tpdavraqla kilqgadppa aeeavfallr dagfdaplrf faslfwgawv avrra
//
LOCUS       WP_175841545             479 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia arboris].
ACCESSION   WP_175841545
VERSION     WP_175841545.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..479
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48426
     Region          21..418
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(28..29,32..33,36,68,118..119,121..123,126,148,
                     151..152,155,284,287..288,291..293,296,324,328,380..381,
                     385,389,405,408..409,412..413,416)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mdtttpspaf pstlarvvat vsigfvvtql dvtivniala hlaadlhlpv aglqwvvday
       61 tlafavlmls ggalgdrfga rrlyiaglvl falaslacga avspamliaa ralqgvgaaa
      121 mlpnslalln dacrhdprlr aravgwwtaa gsisiaagpv vgglliaawg wrgiflvnlp
      181 lcaaglaaaf awvparrepa apsrsvrald lrgqfiaiam ltaltgavie wqplgfahpv
      241 vaggfalaal aalafvaves rtatpmlpls lfrhrtfsaa vlfgicvnlt yygtvfvlal
      301 ylqrargesa lqaglaflpl tggfllanla sgrvvarhgs rapmlagalv aalgygslhf
      361 vdastplaal lvpflliptg mgfavpamtt avlasvaper agiasavlnt arqaggamgv
      421 aafgalaggg daaqvvsglr ietavsvall vaaallatrv rpdahrgasg ahqampaad
//
LOCUS       WP_175841581             291 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia arboris].
ACCESSION   WP_175841581
VERSION     WP_175841581.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..291
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31741
     Region          52..285
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mlkpevdslv phvpfsrrkf mqaalggtfa aavlpvsaqt vttdsagldv dtieirsgds
       61 svpayraqpv dktnlpviiv iheifgvhah iadvcrrfak lgylaiapdl farqgnvsky
      121 ptiqgvidni vskvpdrqvt edldatvawa gknggdlsrl gvtgfcwggr qawlyaehnp
      181 hvraavawyg fvegktdemt pfnpvdhass lkvpvlglyg ekdqnitqas ladmrkaiqt
      241 sdsklarese ivvypdagha ffadyrpsyv kgdaedgwkr siewfhkfgv m
//
LOCUS       WP_175841591             148 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GatB/YqeY domain-containing protein [Burkholderia].
ACCESSION   WP_175841591
VERSION     WP_175841591.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..148
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=15587
     Region          1..146
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 mslkeqised mkaamrakes erlatirllm aaikqreidd rvtlddaait avidkmikqr
       61 kdsisqfeaa grddlvakeq aelavlggym paqlsdaeva aevqaavaet gaagpqdmgk
      121 vmgvlkgkla gradmtavsa qvkaaltk
//
LOCUS       WP_175841620             511 aa            linear   BCT 11-JAN-2025
DEFINITION  catalase [Burkholderia arboris].
ACCESSION   WP_175841620
VERSION     WP_175841620.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..511
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56995
     Region          22..504
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 mssssnrvlr havaaicval saspyaaelt rdtgapigdn qnsqtagpag pvllqdsali
       61 eklqrfdrer ipervvharg tgafgefvps adlsdltkak vftpgtrtpv fvrfstvmgy
      121 rgspeqardp rgfavkfytq qgnwdmvgin lpvffirdgi kfpdfvhank psavigvqdp
      181 nlafdffaht peathmltml ytnagmpdsy rhmdgfavha fkfvnaqgdv hyvkfhwksq
      241 qgvhglrpqe iaasigrdwn mmtndlygtl kqgdfpkwdl yvqvlapkdl nrfdfdaldd
      301 tkvwagvper kvgtmtlnrv pdnyfqstee safapsrlvp giepsedrml qdrlfayadt
      361 qmyrlganyq dlpinrpvvp vvnnnqdgrm nagdrkgevn yepstqrela qdpqyksvrm
      421 tlngttqqea ihkkllfrqa geyyrglsqq dkddlitals gdlgqvknaq nqyamlsyfy
      481 kadadygtrl aqavhanvqq vqslaaklse n
//
LOCUS       WP_175841622             528 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MDR family MFS transporter [Burkholderia].
ACCESSION   WP_175841622
VERSION     WP_175841622.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..528
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56665
     Region          37..516
                     /region_name="MFS_LmrB_MDR_like"
                     /note="Bacillus subtilis lincomycin resistance protein
                     (LmrB) and similar multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17503"
                     /db_xref="CDD:341046"
     Site            order(39..40,43,75,125..126,128..130,133,153,156..157,160,
                     287,290..291,294..296,299,327,331,383..384,388,392,408,
                     411..412,415..416,419)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341046"
ORIGIN      
        1 madtpatmpa pphegrasvt dwiavaagal galmatldis itnsalpqiq geigatgteg
       61 twistgylms eivmiplaaw ltrvfglrnf lltnsalfia fsmmcgwshs lpmmiagrig
      121 qgftggalip taqtiirtrl plsqlpvgmt lfglivllgp lfgpvlggwl aenvnwswcf
      181 flnlpvclll mallvfglps drpqwhsffn adwlgifglt iglssltvvl eegqrerwfe
      241 sqmivtlsiv sfagmvlial sqrfakrpim rlslmrnpry asvivivsav gaglygvsyl
      301 lpqflaivag ynaeqagaim llsglpaflv mpilprllgk vdfrilvisg lllfclscml
      361 disltaqsvg hdfvwsqlir giaqmlammp lnqasmaava redsgdaagl ynmarnlggs
      421 iglaiigtvi drrttfhtaa lresvtansl igqdrlsaya anwfahtgdl aysnmralgq
      481 laqqiqiqav vmtysetfyl lglallacvp lalllrtprg pqpmssgh
//
LOCUS       WP_175841696             243 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Burkholderia].
ACCESSION   WP_175841696
VERSION     WP_175841696.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..243
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26318
     Region          164..243
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mtdtndwlei dyrtlfrlhp drrierendp dcspgprfwl grcasgtlag vradvpavla
       61 deltrmadse pplsdsvqpa hlerylarla pvshwniglv yalpnalefd tgahvalvdg
      121 dsdagrqlrq slsahgmpdg lrsmgfrsva dlwapwcaav vdgevvsvaf aarlsdtgae
      181 lglatapafr grglaaavta awsrlpslrt rtlfystdrd nrasqrvasr lglvlrgttl
      241 riv
//
LOCUS       WP_175841748             544 aa            linear   BCT 11-JAN-2025
DEFINITION  LVIVD repeat-containing protein [Burkholderia contaminans].
ACCESSION   WP_175841748
VERSION     WP_175841748.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Adindla,S., Inampudi,K.K. and Guruprasad,L.
  TITLE     Cell surface proteins in archaeal and bacterial genomes comprising
            'LVIVD', 'RIVW' and 'LGxL' tandem sequence repeats are predicted to
            fold as beta-propeller
  JOURNAL   Int J Biol Macromol 41 (4), 454-468 (2007)
   PUBMED   17681373
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..544
                     /product="LVIVD repeat-containing protein"
                     /calculated_mol_wt=56609
     Region          128..528
                     /region_name="COG5276"
                     /note="Uncharacterized secreted protein, contains LVIVD
                     repeats, choice-of-anchor domain [Function unknown]"
                     /db_xref="CDD:444087"
     Region          435..472
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
ORIGIN      
        1 mhalnrlaia lslgtlmlag cggddnvttg atpavsvady vvprvpgcsp gdtpetalqg
       61 qvpaalrqsg fvgfncnlkr vsqvqgegas wsaatytdrq ghtcfyhatm gaspafnnpd
      121 apprvnpgvp vidltdpakp vrvssltsta midpweslrv nvargilaad nglgggggpe
      181 vdlydvatdc trpqllasvp igtgadggil psvkpmgheg gfspdgftyy iggaysksyy
      241 avdvtiptrp klisaitmad lgfgavphgl svsqdgnray figlgntgta agsgappldn
      301 ansngdngff vidtsevqsr rpnaqmhria tvpvrdgsag qhtipfmvgg kpylvevdeg
      361 gsggiqdpga agvkaacnag mtpfplghiy dmsneaapkl vselrletha vqncskvipd
      421 ilglstftyg shycsvdnre natalacsyf hsgvrvfdir dpakpkeiay ynppsakspg
      481 agsahlmfgq yrpggpdwca srldfdfdrh llttacqdng llvlsfenga wpfpestkat
      541 eign
//
LOCUS       WP_175841698             473 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia contaminans].
ACCESSION   WP_175841698
VERSION     WP_175841698.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..473
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47809
     Region          31..430
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,157,
                     160..161,164,288,291..292,295..297,300,328,332,385..386,
                     390,394,410,413..414,417..418,421)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msdcnpvsvp aalaapgrpa areqrltltl vavgmfmavl dstivnvalp amraslgatv
       61 aqlawivday tlsfaalila ggalsdrfga khvylaglal fvgasaacgv assvavlvva
      121 rfvqgmgaal flpasltivr stfdvpaera raiavwagia svavavgpvl ggilvddfgw
      181 rsaflinvpa galafagtaa lvrasgtqgv ghfdwagqci gaiglgalcf vvielptrga
      241 gatdvraall vaalgaaalv vverrarhpm vplawfrnrv fvamnlmgsl vyvgyfgllf
      301 vlslylhgrl gmgarqtglt llpfalslsl gnllsgklhg qvrpvrlman glamaalaip
      361 aiaialalra pwpvvwaamv vfgtgtsmsv apmiatvleq vpadaagvas gflnaarqag
      421 sllgvalaga atillpdvad alwavagigc vayaiaalaa wtagrahaaq rtr
//
LOCUS       WP_175841767             435 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia contaminans].
ACCESSION   WP_175841767
VERSION     WP_175841767.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46693
     Region          25..427
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(39..40,43..44,47,79,129..130,132..134,137,157,
                     160..161,164,259,262..263,266..268,271,299,303,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mstahpsaav spddalhgnl yrkvtlrlit lfclcyfaay ldriniglak lqmldalkfs
       61 dtvyglgagl ffagyilfev psnlvlqrvg aklwiarimi twgllsgatm fvhtpmqfyi
      121 vrfllgaaea gflpgvllyl tqwypdarra rivalfmvgl plssmigspi sgwimrafdg
      181 thglggwqwl fllealpsvl lgfavlrwlp nsiesaqwls adekhalran ldadpsgnks
      241 halgkafsdp kvwalglidl cvllglnavs fwlptilrdt gvkdayhigw lmvipnaaav
      301 latlycgass drarerrwhi vvpfvvsava laiaassshg tfgtvllfsl inagaaaamp
      361 vvwalpstfl kgsaaaggia facsianlgg fgstyfigwl rdtfhsqsag lygfaacmlv
      421 gcalalaypa rlvnr
//
LOCUS       WP_175841772             395 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175841772
VERSION     WP_175841772.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..395
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=43701
     Region          27..84
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          116..318
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(131..132,134..135,138,142,144..150,244..249,
                     255..256,258..259)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrapldpnal pgdapdaava ldvldarlmr illvlltert vsraavrlnm sqpatsaalk
       61 rlrtllgdpl lvrsrygmvp tefgarliep lrnalrvidf iriqqprfda rtsvrtyrig
      121 cpdylnvlfv pklvalfrer apdaqlvfhp lgdgfddera ladgeldvvi dnrparssrf
      181 rqddlfddrv vclmrathpl arrgtmtaae faeapqlcpt pswleasgai drqlervalq
      241 rrivvtlphf elaahalvrt dmlltttyrl arhyakllpl aavalpaepp divyrmtwne
      301 sgecvegvrw lrgliaeatr awldadamqp avaavaavaa gavldvdard stpaaadtpe
      361 parrtrrrqa thchashprr vahaarihrl stksh
//
LOCUS       WP_175841808             141 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia arboris].
ACCESSION   WP_175841808
VERSION     WP_175841808.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 141)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..141
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15577
     Region          20..132
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04667"
                     /db_xref="CDD:467552"
ORIGIN      
        1 mpqtlapdnt sdtnavpike ratvvcyrde qvllvaraas rwalpggtik rgetpleaah
       61 relceetgit gqdltysmqf tglakihhvf faevgqdqtp qasneiekck wfpidsvdgl
      121 rasiptkriv elvhnheirk v
//
LOCUS       WP_175841861             391 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175841861
VERSION     WP_175841861.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..391
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43040
     Region          24..>204
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
     Region          116..318
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(131..132,134..135,138,142,144..150,244..249,
                     255..256,258..259)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrdaldpaal prdaadatga ldvldarlmr illvlltert vsraavrlnm sqpatsaalk
       61 rlrtllgdpl lvrsrygmvp tefgarliep lrnalrvidf iriqqptfda rtsvrtyrig
      121 cpdylnvlfv pklvalfrer apnaqlvfhp lgdgfddera ladgeldvvi dnrparssrf
      181 rqddlfddrv vclmrathpl arrsamtaad faaapqlcpt pswleasgai drqlervglq
      241 rqivvtlphf elaahalvrt dmiltttyrl arhyakllpl aavalpaepp divyrmtwne
      301 sgscaegvcw lrgliaeath awldaearlp avtaaaatgs dadartttpp vadtpeparr
      361 trrrqathch ashparvaqa arihriatkp h
//
LOCUS       WP_175841928             474 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia arboris].
ACCESSION   WP_175841928
VERSION     WP_175841928.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..474
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50643
     Region          3..460
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mqpsmeqsdl kcglkqrhmt mialggviga glfvgsgvvi qqtgpaails flitgglvvl
       61 vmrmlgemac ampavgsfye yarlafgnwr gpgkmagflt gwmywyfwvi vvaleavaga
      121 kliqfwlpdt pawiislall vvltltnlis vgsygefefw fssikvgaii vflflgglyv
      181 lglwpasmht tavlptllgh ggfmplgigp vmsgavaatg fyfgaeivti aaaeakepak
      241 avakatnsvi trvlvfyvgs valvvalvpw nsaqmatpyv salevmglpa aanvmnaivl
      301 tavlsalnsg lyaasrmlfa ltrhgdapaa lakvnkrgvp vraillgtvf gyasvvmsyv
      361 spdtvfaflv nsygtvalfv yvliafsqlr lrkrldpvaa srlrvkmway pyltwvaiig
      421 migilvamaf ipdqrkplwl gvaslgvlvv aygltrrsrr ehlddsella yppr
//
LOCUS       WP_175841882             120 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia contaminans].
ACCESSION   WP_175841882
VERSION     WP_175841882.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 120)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 120)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..120
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12431
     Region          31..118
                     /region_name="CytC552"
                     /note="Cytochrome c551/c552 [Energy production and
                     conversion]; COG4654"
                     /db_xref="CDD:443692"
ORIGIN      
        1 mknrqmkqmk qlmvqgaaia alvvgtlgva hadvgdglkv argnacmgch avdrklvgps
       61 fkdiaaryka dpqavaklsk kvkeggsgvw gaipmpahpr msdadvrsvv ewvlagapsk
//
LOCUS       WP_175841940             250 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175841940
VERSION     WP_175841940.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..250
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26647
     Region          10..247
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mlpadtptlr afallehlvq agdavsladl ardvdipkas lhrmlaslea gglvirepgr
       61 knayaigprl arlgtgvmlh agarrlrhai lerlvadlge tcnltalhdt evvyldrvea
      121 dwplrldlkp gsrvpaycsa sgklllallp rderaalvra malprhtpnt isdpelleae
      181 ldrtahkgva idneefvagi vciaapilge dgaciaavav hapvsrapls rlldhvprlq
      241 eaaraladtf
//
LOCUS       WP_175841945             255 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Burkholderia].
ACCESSION   WP_175841945
VERSION     WP_175841945.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..255
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26381
     Region          6..248
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mtadklaili avigagsyfq tvtgfglgmi vmgatsgfgl aplatvatlm svvslangat
       61 alpgrlhhid wravgaatlg ilpsvvagvv lleclsrsaa dllqlilggv vlygglsaal
      121 rptpltersd nrsffvsglf ggllsgmfgv sgpplifqfy rqpltlvqir calivlfttt
      181 satrvlysac egqldrniwl laafatpvvm lttiagrhyp pplspvalrr lafgvlmaig
      241 vgliatslpp llhrg
//
LOCUS       WP_175841964             561 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia contaminans].
ACCESSION   WP_175841964
VERSION     WP_175841964.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..561
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=61139
     Region          10..539
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mttqrtlege fdyvivgagt agcvlanrlt edpdirvlll eaggkddyhw ihipvgylyc
       61 ignprtdwly ktqpeaalng ralsyprgrv lggcssingm iymrgqredy dswaqetgda
      121 gwswdsvlpi fkrsedhhag asdahgaggy wrvekqrlrw eilesfaqaa qqtgipatdd
      181 fnrgdnsgvg yfevnqkrgv rwntskaflr pamarpnltv itgahaqrvi fdgrravgve
      241 yhgggtdyva raraevllts gavnspqlle lsgigdgrrl qalgidvvqd lpgvgenlqd
      301 hlqlrmafrv qgvrtlntls ahwwgklmig aeyallqrgp msmapsqlga faksdsedpa
      361 ltrpdleyhv qplslerfge plhsfnafta svchlrptsr gsvhiasadp gaapaiapny
      421 lstdhdrhva analrltrri asapalaryr peeilpglqy rseaelieaa gavgttifhp
      481 vgtcrmgrad deravvdsrl rvrgiaglri vdasvmpfit sgntnsptlm iaerasdmir
      541 adrraareat pvrtepavta a
//
LOCUS       WP_175841976             376 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia contaminans].
ACCESSION   WP_175841976
VERSION     WP_175841976.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..376
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=40631
     Region          7..376
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkrktlalsi aaaglcagtq ahaqssvqly glmdlsfpty rthadangnh vigmgnegep
       61 wfsgsrwglr gaedigggtk vifrlesefv vangqmedeg qifdrdawvg vederfgklt
      121 agfqntiard asaiygdayg saklsteegg wtnsnnfkqm ifyaagptgt rynngvawkk
      181 lfsngifasa gyqfsnstsf aigsayqaal gynggpfnvs gfynhvnhng frnqtfsvgg
      241 nytfsivrln agyfryngdq gplgqrhdds wtvsvkvapp galdyelgyq qmriknaann
      301 adgftpnanl gafsltngva ngfketiygs vfyhlskrte vylagdymkl hggytvsstf
      361 gaknqlelts girtrf
//
LOCUS       WP_175841977             262 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: enoyl-CoA hydratase/isomerase family protein
            [Burkholderia].
ACCESSION   WP_175841977
VERSION     WP_175841977.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..262
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=27854
     Region          6..256
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 msnedirier hdgivtlrln rpakrnslar phldflhetl dalagdpsvr clvltgtgsa
       61 fcagadvdew aeaerngeld tygwterahr fvqalaafpr ptiaalngst vgagtdigfa
      121 cdfrvastaa tlrcgytgmg yspdmggswf lprlarpdvv rrfiflnerw naqdalaagl
      181 vsevvdadaf aqhvaafaar laqgpsvafg qtkallaqsl tqslaeqlrg elaagvacgh
      241 sedgqealra svegrapnfv gr
//
LOCUS       WP_175841978             388 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia arboris].
ACCESSION   WP_175841978
VERSION     WP_175841978.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..388
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41887
     Region          31..381
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msavmetsag veegrpgaha araepaaraa sgaglqidrv srrygsvqal qettieiprg
       61 efltilgpsg sgkttlltiv agfehpttgd lrvggrsiva lppekrnfgm vfqgyalfph
      121 mtveqnvayp lmvrkqkgpd avkrvkaald lvrlghladr lprqlsggqq qrvaiaralv
      181 fdpdlvllde plgaldrklr gevqvelkal herlgatflf vthdqeeals msdriaimrd
      241 grleqigtpd glyeqpanrf vadflgksnf iegvafggda aathyrvgda rfvapacgar
      301 pddpllfalr pekiavsats cggtynevpg rirhwsyfgs syrfqietva lgcvtadvpa
      361 wrglasphtg mdvfvqwerd atcriasd
//
LOCUS       WP_175841984             264 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia arboris].
ACCESSION   WP_175841984
VERSION     WP_175841984.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..264
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28228
     Region          8..259
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mktrltagra lvvgvawaai lflmlpllvs vpvsltpsdy lsmpdgalsl rhyrvlldde
       61 gwvssflqsg lialvssvis vtlgtlcaig lwkiasrrge lvrgvilfpl ivppivsala
      121 fyrlwgemgm ldsypaails hvvlsvpyvv vavsaslatv glrieqasrs lganvaqtlr
      181 yvilpsirpg vlsaavfafi lswdelvvtl fissrnvytl prrmwdgmre nvdpaiasvs
      241 tlllvatcva iglsllrrra agsv
//
LOCUS       WP_175842035             729 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia contaminans].
ACCESSION   WP_175842035
VERSION     WP_175842035.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..729
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78391
     Region          26..729
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mpsrrpprra rplrpwrtsl palitlcvas gthasaaera daepsastsa stpappaare
       61 lpaisvsasa tadptvgyqp rttsiaggdn rsikeipqsv avvsssvmqd qqarslddvl
      121 gnisgvtqtn tlggtrdafi krgfgsnndg svlvdgvrtp vlhsylatid rvevlkgpas
      181 llygmqdpgg vinlvtrkpe dtfggsisas rtshggssat fdltgplgkp gqvaggtlaf
      241 rltgqydtsr ywrsfgrqrd aliapalswh dantsidvsy qyvdyttpfd rgtvlvngql
      301 ddalryrrye eawsqssgiq etlrariehr fsdawrvrat ygwgrdrydq titratafns
      361 atgaltrssd anlgrndsdq iatlgllgnv tlagmnhaiy iggeyerqrs frgdtirgka
      421 tkgfnlydpv ydllapggtp npkqsdsrsl vhaysmvvqd svkltdrlta vgglrwenwq
      481 qesgmgrpfv fadrsrgsvw lpqfglayal tpaltayanv srsfkpnvat nvaaplapey
      541 grvleaglkf slkpaitgtl avyqidkrnv avtvgdltst igtarsrgie ldvagqitrh
      601 lsvigsyayt nandrdsntp lvnvarhtgs lfavydtaia nlpgrwrfgg garlvgtrsg
      661 dtansftlpg yvtvdafaay ettigkfptr fqlnvknlld ktyypssnnn liiavgeprl
      721 vtltttvsf
//
LOCUS       WP_175842033             184 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: carboxymuconolactone decarboxylase family protein
            [Burkholderia].
ACCESSION   WP_175842033
VERSION     WP_175842033.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..184
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19916
     Region          42..177
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtnrlppfdp asatdeqkav ladilsgprg nlngpflgwi aspelaqhaq klgafcryrt
       61 glplrlsela ilvtaarwrs qaewhihhpi aldagvpaat adairlgvap ifesdddali
      121 yafaselydt rrvsnatfsr aqarfghetv vnlvallgyy alvamtlntf gmradgqtel
      181 pfpe
//
LOCUS       WP_175842126             306 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: dihydrodipicolinate synthase family protein
            [Burkholderia].
ACCESSION   WP_175842126
VERSION     WP_175842126.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..306
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33109
     Region          7..294
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 msrnaiqwtg vfpavstqfk pdfsldidat hrvvrnlvnd gvsglvvcgt vgentslsts
       61 eklqvieaar daaggkipvi agiaefttef arntvreaqr vgvdgvmvmp alvysakphe
      121 taahfravat stdlpvmvyn nppiykndvt pdvlialqdc enivcfkdss gdtrrfidlr
      181 navgdrfvlf aglddvvves iavgaegwvs gmsnafpkeg etlfrlakqk rfdealalyr
      241 wfmpllhlda rpdlvqcikl ceelvgrgsa itrpprlalq gdtlaevkai vakaletrpv
      301 lpdvgl
//
LOCUS       WP_175842087             357 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia contaminans].
ACCESSION   WP_175842087
VERSION     WP_175842087.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..357
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38524
     Region          4..334
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,226,287,308,310..312)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,174,177,179,226,233,287,308,
                     310..311)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,174,177,179,311)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            179
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 msqlftpvrv grytlenrlv mapmtrsraa fdgtpgewaa eyyaqrsslg livsegtqps
       61 ddgqgylttp giytdahvag wkaisdrvha rggrlfiqlm hvgrmshpdn tphhrqgvap
      121 saiapnaqmf tvkgmqdipv praltteevr atvhdfriaa rraidagadg veihgangyl
      181 vqqffapnan trtdvyggsi enrarfaiev ataiadeiga drtairvspg ntlggldega
      241 eardlyrhla teldrlglay lhvmhqgdea lladlrarwn gtlilnrpgr trdaigtdvt
      301 sgladleayg qmvlanpdfv trvktgapmn darretffgg dargyvdypa legvaaa
//
LOCUS       WP_175842089             319 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia contaminans].
ACCESSION   WP_175842089
VERSION     WP_175842089.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..319
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=36304
     Region          55..212
                     /region_name="Cfa"
                     /note="Cyclopropane fatty-acyl-phospholipid synthase and
                     related methyltransferases [Lipid transport and
                     metabolism]; COG2230"
                     /db_xref="CDD:441831"
     Region          <176..261
                     /region_name="PRK01008"
                     /note="queuine tRNA-ribosyltransferase; Provisional;
                     cl19224"
                     /db_xref="CDD:473152"
ORIGIN      
        1 mnnlvtskti asasplndrr rqpfaairgq lqndyesrvm eayqddpvnw skaigdrlwf
       61 qfgvyddpqs prpadldesg lryferqlki agletpgrqp inrildigcg wgtvlrdlse
      121 rfpgchrldg inisdrqley caevnaargv sdrinlfrcn aldidllpdf dapydlaimr
      181 gvishfpydl fesvmtklrr rlaangtviv sdnlynvdls eyrsdtpdlv drlackyrkt
      241 paylrqvfeq sgfrihdmqv lpnrtdatrw lldvqdnier hfptgavgal eelrvmcesl
      301 avaivkrqvs iysfalkhg
//
LOCUS       WP_175842140             389 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Burkholderia contaminans].
ACCESSION   WP_175842140
VERSION     WP_175842140.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..389
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39954
     Region          61..369
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mntikridpr rpfiitaagl kritlgeegs adanavhgla hghgaaaakp rravqdpkhv
       61 mlvvahgerg alddhsrqai aaaalladaq tevallafge lkddvaelgv dkllelagfd
      121 rrafdpesel qalqacvaal apkhvfvpdn atgdgdlgrr yaaaagasva ahvveidakh
      181 vgayaqagra fatralpdvi llaqnavdak lpfvgagerl aadfirpahd gaqpyrdlgl
      241 deidaaqval eeadfivsag ngvsdigafe rlagvfgaai gasrvavdng hftrdkqvga
      301 tgktveasvy iafgisgavq hlqgikdcrh viavnldgsa piarranltv vgdaqgtiaa
      361 lieqvqaara argespaavg trepegvaa
//
LOCUS       WP_175842237             211 aa            linear   BCT 11-JAN-2025
DEFINITION  cysteine hydrolase family protein [Burkholderia contaminans].
ACCESSION   WP_175842237
VERSION     WP_175842237.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..211
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22683
     Region          34..188
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mtrqhapdia tttrtnpgds psvpipalvp sstallvmhy qtdilglfpt vapellantr
       61 rlcdaarasg igvwfanlrf spgypevsqr nkngqgikql glfindgpcp elgrqpdepl
      121 iiahrasvff gtdlqarlve qgadslimvg iastgvmlss iahasdadfr lytvkdccyd
      181 pdpvvhehlf stafesrttv lsladalrll e
//
LOCUS       WP_175842266             398 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia arboris].
ACCESSION   WP_175842266
VERSION     WP_175842266.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..398
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42106
     Region          31..392
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msallpelaa dsdshrldea ahavaqiaaq hadavdrdar cpveaieamr arrllgamvp
       61 thlggagasl ediasacsil gqacassamv famhqiqvac ivshaadqgw hklflqqlvr
      121 hqwllasats edgvggnlra sqcaletdgg gfrlrksapt isygdyadgi latarrdada
      181 paseqvlvtl lrdgytltrr gewdtlgmrg tcsngfvlda hgaavqclpv pfakiaeetm
      241 vpvshilwaa vwigvagdaf hrahqffraq arqtdgapsp aarriaesla lmqamqarvd
      301 avlrlhanas tgswsagmar aaeintlkty vsttalevah qammicgmag ykqgspfsvg
      361 rhirdlhaap lmisndriaa ntaslllalr patlekht
//
LOCUS       WP_175842328             355 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia arboris].
ACCESSION   WP_175842328
VERSION     WP_175842328.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..355
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38942
     Region          1..353
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mdklivddlh lsyganpilk gvsfelkage vvcllgasgs gkttllrava gleqpsdgri
       61 qlddrvffdg aqrvdlpveq rslglvfqsy alwphrtvad nvgyglklrr vapaeqkrrv
      121 qsaldqlglg hlaerfphql sggqqqrvai aralvynppv illdeplsnl daklreeara
      181 wlrelivslg lsalcvthdq teamamsdri lllrngrieq egtpaelyga prslytaefm
      241 gsnnridarv aaidgecvtl sgdgwelral ardtlapgqd aqavirlerv qvtdgpganr
      301 lqadlvtsmy lgdrweylfh cgdmrlrafg hvpraagkhw iefptndcwa fakag
//
LOCUS       WP_175842329             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia contaminans].
ACCESSION   WP_175842329
VERSION     WP_175842329.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46354
     Region          23..428
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(35..36,39..40,43,82,140..141,143..145,148,168,
                     171..172,175,258,261..262,265..267,270,298,302,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mpdtmstlaq paahaprrvr nsrlatasmi gtslewydft iyntlaalvf nhlffpsvdp
       61 lagtilafst yavgyvsrpl ggfvfgnlgd rigrravlml tlvlmgvtta lmgalptyaq
      121 agilspillv alrfvqgval ggewagavll svehgdqkrr glsaswtqig psfgtllgtg
      181 cialvtlstt sgdflswgwr vpfaasallv vfgfwlrrgv detpqfeqla eshataevpv
      241 advlkyhwkr lliaggsrvg sdvlyalivv ftltyvttvl hlsrpvalta vmigtacnal
      301 avpffgalsd rfgrrpvyla galagivwaf vfftlldsar pgaivaavai glvihavmyg
      361 pqgafvteqf ptrvryagss laytlagivg ggfaplviaa lfrqtgttta vslyvstalv
      421 vtsiallvar etahkplad
//
LOCUS       WP_175842146             269 aa            linear   BCT 11-JAN-2025
DEFINITION  2OG-Fe(II) oxygenase family protein [Burkholderia contaminans].
ACCESSION   WP_175842146
VERSION     WP_175842146.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Kimura,H., Izawa,M. and Sumino,Y.
  TITLE     Molecular analysis of the gene cluster involved in cephalosporin
            biosynthesis from Lysobacter lactamgenus YK90
  JOURNAL   Appl Microbiol Biotechnol 44 (5), 589-596 (1996)
   PUBMED   8703429
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10504650
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..269
                     /product="2OG-Fe(II) oxygenase family protein"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /calculated_mol_wt=30091
     Region          <153..229
                     /region_name="2OG-FeII_Oxy"
                     /note="2OG-Fe(II) oxygenase superfamily; pfam03171"
                     /db_xref="CDD:397334"
ORIGIN      
        1 mklhasrlir dsyvyfkmpy allmhfdrla aaydaldrkq khafsfpeht dgflpfgley
       61 shtpdrpdlc drfcywvarr dahhgfalak safyremaay eacihaiaqd lldaicenlg
      121 gtpqppvrhs sylqfcayeq hhgshdrayl qdphedghll sfirptapgl vllpdsspis
      181 alprsdemiv lagsllealt dgevpamqha verprtrapr ksrmyfvnpd lsaahastiv
      241 nqrpldlral aegrhvafgn salcrpcaa
//
LOCUS       WP_175842332             366 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia arboris].
ACCESSION   WP_175842332
VERSION     WP_175842332.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Saurin,W. and Dassa,E.
  TITLE     Sequence relationships between integral inner membrane proteins of
            binding protein-dependent transport systems: evolution by recurrent
            gene duplications
  JOURNAL   Protein Sci 3 (2), 325-344 (1994)
   PUBMED   8003968
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004772
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..366
                     /product="ABC transporter substrate-binding protein"
                     /calculated_mol_wt=39817
     Region          62..364
                     /region_name="AfuA"
                     /note="ABC-type Fe3+ transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG1840"
                     /db_xref="CDD:441445"
ORIGIN      
        1 mpfapkhlaa alaivlgtaa gsavaqvpag ypgnyqgvid aakkegkliv ysttdtglvr
       61 plikdfesly gvkveyndmn stelynryis enaasstsad vlwssamdlq vklvndglma
      121 sydspespnv pqwaqyqkqa ygttfeplai vynkrlipes evpttradli kllttqadkf
      181 kgkvttydie ksgvgfnylt qdahvnekvt welvkaigat gpklqsstga mmerissgen
      241 ligyniigsy ayakakkdks igyvfpkdyt qvvsrlatvs kkaknpnaak lwvdyllskh
      301 gqtlianqan lyairadvtg etsaaslske lgdslkpiqi gtgllvyldq skrlaflkqw
      361 qqsikr
//
LOCUS       WP_175842374             233 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175842374
VERSION     WP_175842374.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..233
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25934
     Region          21..179
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnakstvarp rgrrpsvddf dlrdhmldva iqlfaergia attvaqiaaa agvtsamvhy
       61 yftnreqlld aiveerlaqa iafvwrptes rieddpfalv telvdrffdv thrmpwlpsi
      121 wlreivhegg llrermvrri plehigrfae riraaqqagt lnpalepafl fhsiialvml
      181 plataklwqs arglppidrd alhrhvrall gsgmqppaaa prtprapspg rps
//
LOCUS       WP_175842379             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175842379
VERSION     WP_175842379.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33379
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..288
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mlsedelall dairatgsls raaarlgkap stvshaarql etrfdallfd rrgyrlqltp
       61 aghvladeaa rlaldvarlt qrvrqvasgw edrlwivsde vlefdtllpv vrafdaldsg
      121 vslrfthevl ggtwealrdg radlvvgatn eppaiqgfkw felgamewvf avsprhplas
      181 angvltrdai gahravvvad ssrraagray gllggqavla vpsmrakila qrdalgvgwv
      241 prrrvtslla rgdlvekqta dprepnrlyv awhgdrdgra lqwwleqlre prlaqrlldg
      301 idvtg
//
LOCUS       WP_175842393             217 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            contaminans].
ACCESSION   WP_175842393
VERSION     WP_175842393.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..217
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24148
     Region          29..180
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maevterepa krrmrgrpqa gasvgpdvil raarrtfakr gydatsvrev arelgvdaal
       61 iahhfgtket lwlavveqiv elaqpmfdam ralrtsslph rervrraiel cvehefdepd
      121 lgmffstaat eegvrldrlq erlvrpyrdv mfpllaeave ageiraadpd vlffmvasav
      181 gsavsyshmi reftslptrq qefkqavltv alnilgg
//
LOCUS       WP_175842415             220 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Burkholderia].
ACCESSION   WP_175842415
VERSION     WP_175842415.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..220
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23515
     Region          1..217
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msfklylsfl aasvvliyap gpvnlltmnq alragwrral pcvwggtlav llqlaltalc
       61 lnslvhlneh altvlrwaga aylvwlgakq wlsrapagap aaaaeagtat gttiarqdtd
      121 tdralfwrgv atsglnpktl lffpsffpqf isptadwsln lqflllattf avlfaggvas
      181 malfshrlsr alqrparmra mnrvtggllv gmgaimvgwn
//
LOCUS       WP_175842427             452 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia arboris].
ACCESSION   WP_175842427
VERSION     WP_175842427.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..452
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48828
     Region          31..419
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(44..45,48..49,52,84,134..135,137..139,142,162,
                     165..166,169,269,272..273,276..278,281,309,313,364..365,
                     369,373,389,392..393,396..397,400)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 msaplqaqav asgagstdtt gddalyrrig rrivpflfic yivsildrsn igfaqlqmrq
       61 dlgltdamys lgavlffvgy vlfevpsnal lrrfgarrtf arimflwgav svamitvdsa
      121 khfyvlrfll glfeagffpg vvfyltywyp arrrasvlsi fyagvavagm vggllsgwlm
      181 rgmsgvmglh gwqwmfaieg apaillgvia wfwlcdrpeh ahwlsdadrr qlaadlaadh
      241 agagtgtqap rslrqvlaep rtylfafiyf slttallmll fwmplmiref gihdvvqisl
      301 lsvvpnaiga agliviarrs drkrerrrhf aacafggava lalltlhlps ivammallsi
      361 aamlifaahp vfwavpsayf sgagaaggia lissigvssg mitpwlvgli rtrtgsmdpa
      421 mlmiaallaa cavamllgvp rentgarada ph
//
LOCUS       WP_175842442             412 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175842442
VERSION     WP_175842442.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..412
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43973
     Region          17..395
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(27..28,31..32,35,69,124..125,127..129,132,152,
                     155..156,159,234,237..238,241..243,246,270,274,325..326,
                     330,334,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 msvpaagvfr slrsfnyrvw algslvsnig twiqrtaqdw lvltqlthhd asavgtvmal
       61 qfgpqllflp wtgyaadrfd qrkllmttqa lmgvlalvlg vltvtgvaql whvylfaflf
      121 gcasafdapv rqtfvaelvg drelanaval nstsfnaarm vgpaaagfli asvgtgwafl
      181 anglsffavl asllllrede lranvranrs rsslldgfry vwhrpdltai lvmlfligtf
      241 glnfqlfist maasvfhvda rgfgflssmm avgtisgall aarreqprfr hlwigaalfg
      301 lgctfaalap sywlfaaalv ltgvaaitfm nstnslmqls tepamrgrvm alrlavalgg
      361 tpigapvagw vanhlgprwa lgvgaasgfa aalvathfvt rqraqpragd sa
//
LOCUS       WP_175842456             291 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175842456
VERSION     WP_175842456.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..291
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32188
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..284
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,220,237,264)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     214..218,225..226,229)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mellndmalf vevvkakgfr saaetlgmpn stlsrrisal ekaiglrllh rttrrielte
       61 agqlyferck rivdearlah eqlggllaep tgvlrasfpv dfavtylapl ivefstrypk
      121 ltfdfeltsr rvdlvsepfd vairlgesed sqliarrlat lgnylyaspg ylarageprt
      181 pddlarhacl slaragtwtl hdgahivavp vssrfagnsv gmlrrlatld agiivlseai
      241 vaddlaagrl rrvmpewege pipvyamtet rllpaktqhf ieflrerfaq a
//
LOCUS       WP_175842558            1079 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia contaminans].
ACCESSION   WP_175842558
VERSION     WP_175842558.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..1079
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113803
     Region          1..1056
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mwivrlalrr pytfvvlall ifiagplall rtptdifpni dipvvsivws yngfsaedma
       61 kritsnyera ltsdvddieh iesqslngvs vvkiffhpga dinraiaeaa snaasilril
      121 ppgtlppnii tynastvpil qlglssntla eqqlydlgns firtqlatvq gaavplpfgg
      181 kirqivvdld tralqakgla pidvvnaina qnlilpggta kigtheydvq mngstqtvaa
      241 lndlpvktig gnvvyvrdva hvrdgyapqt nivrvdgkra alltvektgs astltiidqv
      301 kamlpkiaag lptalhispl ddqsvfvkaa vqgvvreali aacltalmil lflgswratl
      361 iiavsiplav ltsllalaal gqtinimtlg glalavgilv ddatvaieni thhlelgapl
      421 edailtgage iavptfvstl sicivfvpmf lltgvarylf vplaeavifa miasyffsrt
      481 lvptlamalm rakgqgrppr gvfarlarfq aafehrfeav rlryrallaa aiarrrrfaa
      541 afllacvast glfafagqdf fpsvdtgeir lhlraptgtr ieetarltde veakirgvip
      601 anelagvldn igvpvsginl tydssdpigt gdadvlitlk pnhastaayv aklrnvlaqs
      661 fpgvtfaflp adivsqilnf glpapidiqi vgnkldqnra vanallaklr gvrglvdari
      721 qqpgdepaid vnvdrtkail aglqqrdvaq nllialsgss qttpnfwldp rngvsypvlv
      781 qtpqytvnsl qalanvplpa gtarapqtpa ggpaagapaq nllgtlgsfs rttqqavvsh
      841 ynvqpvldlf asvqgrdlgg vtadvtklvd daraqlppgs sivlrgqvqa mhesfagllg
      901 glvlaialvy llmvvnfqsw ldplvivggl paslagiawm lfvtrttlsv paltgtilci
      961 giatansilv vntarellag gappwqaald agfsrfrpvl mtalamligm lpmalglgdg
     1021 geqnaplgra vigglafgtv stllfvpvvf gfvhawldrr reaatarraq pasdtpalg
//
LOCUS       WP_175842611             261 aa            linear   BCT 11-JAN-2025
DEFINITION  peptidylprolyl isomerase [Burkholderia contaminans].
ACCESSION   WP_175842611
VERSION     WP_175842611.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..261
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=27681
     Region          100..247
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mndvltevpa alringiaid gaavaaeaah hgdapdpfda arralavrel lrqravslal
       61 ldegapldda avdallarel thvpepdrad ceryyaqhpa rfrrndivya shvlfavtdr
      121 vplaplrqra eaaladvvaa pdtfealara ssncpsaevg gslgqllrgd tvpefeaalf
      181 dtdgigvlpk lvntrfgfhi vrierrvpgd avpfdeaaaq iaaylsarvr eramrqyvav
      241 laggarvegv afdgangplv q
//
LOCUS       WP_175842670             237 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia
            contaminans].
ACCESSION   WP_175842670
VERSION     WP_175842670.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..237
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26464
     Region          90..237
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          180..234
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mnlsasditp eelrlfgdiv arleelgpvv dvrtvvlpai tqllradfaa sfdcdvhtgl
       61 wrngfsynvd plqiaryeaw fqhidpvtsq lcarrvatcv devvsrcele rtefyndflc
      121 rdgmhhginv yafdgathvg dlriwrakgr pdfterdkll lngiepffrr allrrrhaca
      181 glteresdva rlvaagytdk dvartlgigv ptvrthlrrv makkgvanra slaaala
//
LOCUS       WP_175842693             273 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175842693
VERSION     WP_175842693.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..273
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30133
     Region          21..237
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mqttndllpg cdaresmdai dryrapaldk gldilellse qkegltrtei tkelgrnsse
       61 iyrmlerlva rryvmrstgg drytlslklf slahrhppms rliaealpsm qrfadsseqs
      121 chlsvydrgn llviaqvdgp gpwgvsvrlg srvgladtas grvmlafqga dqrahmlaeh
      181 rkikgdalls eqelayacqs irqdgylred srqaygvtdl sapilgpsgh aiavltcpym
      241 rridahaapt vdmvikmlhe tthllsthra gsy
//
LOCUS       WP_175842715             338 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia
            contaminans].
ACCESSION   WP_175842715
VERSION     WP_175842715.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..338
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=37098
     Region          115..320
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mhdwyalfdd vkrlgsfhsd aqlaealalt rsqisawrtg ksdlgtlakl rildalghdd
       61 vrsavlslfp ernrealirq hldlvarvnn gtlslpadsc tppqnglafa gnrllgalsn
      121 seldrlaphl vpvelvlgqv vhkqgeilsq vylpttaacv ifhstkagap lglamvgndg
      181 lvglpgcige praanrvivq gaghayrldv dvakreflra gmfqqlllry tqallaqmsq
      241 iavcthhhsp reqlcrwllq tldrmdsdel qvsrkvfpdv lgtdgalavd alrkleadga
      301 lryrpgqiri ldrsaiehha cechrvlkrd yarlfdit
//
LOCUS       WP_175842737             339 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA-binding protein [Burkholderia arboris].
ACCESSION   WP_175842737
VERSION     WP_175842737.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13774834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..339
                     /product="DNA-binding protein"
                     /calculated_mol_wt=37364
     Region          26..144
                     /region_name="KfrA_N"
                     /note="Plasmid replication region DNA-binding N-term;
                     pfam11740"
                     /db_xref="CDD:432038"
     Region          <133..>339
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
ORIGIN      
        1 msdlaadepr ltaeierlka dfpktrelyr eacallffrf gitptanrly qlvrkgsmst
       61 ptavlgefwa elreksrvri ehpdlpadlq aaagelvaal wnrsstdaaa aldalraeve
      121 aeraaaqaev aalkaelart eialeqrtaa llaaqvriqe leqaraadea srqalqaeie
      181 rltadnaegd ralaqaradf stqldrlrdd agraeerlra sekralqeid rerlvaarlq
      241 keldattsra eqrdaqqrkd ttalqaqlgd alhrcgvlqg qldgalatda argkeldalr
      301 remtvfarra plrgvktapa aqreerkart rkrtgeasr
//
LOCUS       WP_175842746             267 aa            linear   BCT 11-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Burkholderia
            contaminans].
ACCESSION   WP_175842746
VERSION     WP_175842746.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181070
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..267
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30138
     Region          27..258
                     /region_name="CE4_Ecf1_like_5s"
                     /note="Putative catalytic NodB homology domain of a
                     hypothetical protein Ecf1 from Escherichia coli and
                     similar proteins; cd10969"
                     /db_xref="CDD:213026"
     Site            order(69..70,154,158,200..202)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213026"
ORIGIN      
        1 mesyarsvpv vmyrhvsstp gefsitpgnf esqmhwlarn gyvtltadef acflqgaamp
       61 eksilltfdg gyldnyvhah tclvryglna imflvtgrvn dgparssrgr tsgevrshae
      121 cerlvlmgqs ddvtvrwsei dimraagtfe fhshthshlc wgqlcndpde ktdrirmdie
      181 mskrtltekm gmasahlcwp egcydgdcid aaraagfeyf yttrntqrnv pgsaphqihr
      241 itdngkngdw laekvqqyqh drwerss
//
LOCUS       WP_175842784             295 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia
            contaminans].
ACCESSION   WP_175842784
VERSION     WP_175842784.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..295
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=31568
     Region          3..290
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 msfegvhtpl vtpfdadgei dhallgrhaa dlagrvaglg iggttgeyya lsfdervrtf
       61 dtvaaaaggk tlltaginat ttkevlrlgr eakragldal lvaapyyaqp tqqellahll
      121 tiddaldmpi mlynfpartg teigdgilet llerknfvam kestgdiahl hhlsthfsgr
      181 lvlscgmddq aleffawgar swvggasnfl peahtdlfda cvtrgdfsag rklmaqllpv
      241 lellersgkf iqyvrygcel aglpvgvara plgalsgder dafaklvkpl lrdgr
//
LOCUS       WP_175842818             146 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Hsp20/alpha crystallin family protein [Burkholderia].
ACCESSION   WP_175842818
VERSION     WP_175842818.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..146
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=15843
     Region          44..146
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 msgihfgndl fdefarvqrq vanllgerpt giravrpgaf palnvgatdd aieivafapg
       61 maagdfdvsi dkdlltisge rkpapraege dvrtyaqerf hgafrrvvel prdanpdqvs
      121 aryengclli rvgrreaakp raitvq
//
LOCUS       WP_175842841             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175842841
VERSION     WP_175842841.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46135
     Region          13..417
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(25..26,29..30,33,72,130..131,133..135,138,158,
                     161..162,165,247,250..251,254..256,259,287,291,343..344,
                     348,352,368,371..372,375..376,379)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mtqslpsarq pgraataafi gtmiewydfy iyataaalvf gelyfpshdr fvstmasfat
       61 favgffarpl ggvifghlgd rigrkkalmt tlmmmgvatv cvgllpdysk vgmlapvllv
      121 alrvvqgiav ggewggavlm agehapqgrr tffasfaqlg spaglilsli afravtsmdk
      181 adflawgwrl pflassvllv vgilirlgvn espefarvke tnrtvklpva evfrsasglv
      241 llcigantig iagvyftntf miayttqyvg vsrslildsl favaiiqfia qpiaawtaer
      301 iggarflkia allamlspyp mfmlvqggts asliagiala vvcmagfysv iagfvsdvfp
      361 ahvrysaisl ayqicgaiag gltplvgtwl ahrfagqwwp lavfytclag isllcivald
      421 arraaqpaaa ealgsh
//
LOCUS       WP_175842845             356 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: porin [Burkholderia].
ACCESSION   WP_175842845
VERSION     WP_175842845.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..356
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=37472
     Region          23..356
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mtkqleargs dcrvrpvhag lritvavacl agsgtvlaqd gvtlygvide faqyvntgng
       61 ytaainsggq wgsrfglkgg edigggqkie falengfnpn dgslasagsm fnrqawvgia
      121 gqwgkvragr qnsplfndqg gqdafggvtq asgmdnltvf afrtsntlsy qspeiagfqg
      181 glyvgfgdag gvrsagssqq fdltyehgpf gafvagqwlk natatttdrt imagasyeig
      241 katvyggfsa vkwadfgids rvyglsvkyq fnpanyvalg yaylhdqssq gnnadqlglm
      301 yeydlskrts fygalsylrn rnqagytlag aanpglplay pganargvql givhrf
//
LOCUS       WP_175842869             211 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Burkholderia arboris].
ACCESSION   WP_175842869
VERSION     WP_175842869.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..211
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21981
     Region          138..210
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mnyaqpkppv rriggiafvv glhavivyal ltglatkvvd virqpietri ieeikppppp
       61 pppkriappp pkhvappppf apppdvhvaa ppspnaittq sttpvpsapv appappaaaa
      121 pvstsvgvvc pnstqvraai ryprealkdn ltgdvvvtfv vgtdgnvkdl svtqsaapvl
      181 draaenavrq fhcvaqgeev rvqvpfsfkl d
//
LOCUS       WP_175842881             327 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175842881
VERSION     WP_175842881.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13797492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..327
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36049
     Region          27..206
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          <222..323
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 makkpeffaq tptaldddad pfafkrdafs dvlelirirg ntvftcaasa pfglrfpagk
       61 yrlhiirsgs vaieveglde ryhasqgdlv mlmhghghvi sdrpgrsasl vtdlapqhyd
      121 rerltigsgd ttwlcgdfgf dgvlsqrlls vlppvlvlkg lrerpfewle lschfildea
      181 lspragaaam isrlldvifv qllrtwateg saghgwlsga idsrinpams aihadpgraw
      241 svsdlaelsn lsrsafadrf qrvvgqapls ylttwrldra aellrysrap vsdiagrvgy
      301 tseaafsraf rgryemspmq wrkvnae
//
LOCUS       WP_175842909             327 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia contaminans].
ACCESSION   WP_175842909
VERSION     WP_175842909.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..327
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34760
     Region          91..284
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mtsahwlplt evaddardav rafrelggrh ygsfsvdqsr vnfvraceln gltgdaavvh
       61 kdidvpvvgg sirvrlyrpp agaradgapl ivfihgggwv igsvdthdgi crhlarhggc
      121 avasveyrrs pehrwpvple dceqaldyla anasalavna crvimagdsa ggnmatlian
      181 aapaagpaii gqilfypvtd ltaslpsyqr iqggfplvae smlwfrehyv psgtpfdlpr
      241 lspllhaegr rqppmfiatv gldplcdegi ayascaarag stvehhhlpg hhhgiitaar
      301 tipaatclld raasfvrrla ekegldv
//
LOCUS       WP_175842935             213 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia arboris].
ACCESSION   WP_175842935
VERSION     WP_175842935.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..213
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=21832
     Region          7..213
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mtqrslnial fgatgtigsr iaaeavrrgh rvtalsrhpg asgdgitaka adlldaasia
       61 aalpghdvva saygpkqeda akvvavakal vagtrqaglk rlvvvggags levapgkqlv
      121 dsegfpeayk aqalahrdaf nylktvadld wtffapaali apgertgtfr tgvgklivda
      181 qgnskisted yavafvdale qdsfvreiat aay
//
LOCUS       WP_175842952             342 aa            linear   BCT 11-JAN-2025
DEFINITION  LOG family protein [Burkholderia contaminans].
ACCESSION   WP_175842952
VERSION     WP_175842952.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Naseem,M., Bencurova,E. and Dandekar,T.
  TITLE     The Cytokinin-Activating LOG-Family Proteins Are Not Lysine
            Decarboxylases
  JOURNAL   Trends Biochem Sci 43 (4), 232-236 (2018)
   PUBMED   29525484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..342
                     /product="LOG family protein"
                     /EC_number="3.2.2.-"
                     /GO_function="GO:0016799 - hydrolase activity, hydrolyzing
                     N-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0009691 - cytokinin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38199
     Region          150..318
                     /region_name="PpnN"
                     /note="Nucleotide monophosphate nucleosidase PpnN/YdgH,
                     Lonely Guy (LOG) family [Nucleotide transport and
                     metabolism]; COG1611"
                     /db_xref="CDD:441219"
ORIGIN      
        1 mstvvkripa gtargevrrr tagdpmpvdt rgrrtrtrpa aivghdgagr rprrapphaq
       61 ranctpaddd atilqrtgmr girlqldywk aeerlqneri ghavviygst rivapavana
      121 rlneanrlla arphdagrrr avaaasrlve hsvyyrvare fgrivghadr ctrtarlaiv
      181 tgggpgimea anrgayerga psigfnielp reqapnpyit pdlcfrfhyf airklhller
      241 akaavffpgg ygtfdelfev ltllqtrkip plpvilvgea ywrravdlaf ladegmidrs
      301 dldlftyces apdiwraigg wyarrrtarp vrrrtkpkpr am
//
LOCUS       WP_175842960             146 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: (2Fe-2S)-binding protein [Burkholderia].
ACCESSION   WP_175842960
VERSION     WP_175842960.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..146
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=15471
     Region          1..146
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mrfmlngqpf dfdgdpdtpl lwvirdsarl tgtkygcgig acgactvhld geaaracvlp
       61 aasvagrsvt tieglshdrs hpvqrawiek dvpqcgycqs gmvmataall arhgkptdaq
      121 ideavtnlcr catyqrirea ihvaag
//
LOCUS       WP_175842967             496 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: HDOD domain-containing protein [Burkholderia].
ACCESSION   WP_175842967
VERSION     WP_175842967.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..496
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=54892
     Region          18..275
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 msitehlprt alldklwarm sergdfplls eslratmaam knddldftal vrvvlsdfal
       61 tqkvlrlans amymafggni ttvtralmvl gmdavghlvv glklvdhfhh stprridakl
      121 elnrallsgc varklterae lrageeavvc tlmrqvgkll vvcyldsewd kirrraaelh
      181 gdesaacvav lgvgfdeigl eaatrwrlpd tirdgiaddh hhlnrvdafg relpadeeri
      241 ervnwlravs rcstdvasal ampdspqrda hidalaqhya laldtepdal veiaerlahe
      301 easdtvmrei velranadai araqaepeac leagladlra lpsehvltpv lalaseslla
      361 slaftrtvmf vrhddgtfaa rlgfgpdvda alyrlrfder fepdvfhlai tnsvgifieq
      421 aqepkmlkrl pawyldvfdd trafvllpvr vdtttvally gdwagaqpar kisqqemsil
      481 nelarelgrf fpapha
//
LOCUS       WP_175842984             198 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            contaminans].
ACCESSION   WP_175842984
VERSION     WP_175842984.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21265
     Region          22..172
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 manpagvgrp refeledaar daiavfwdhg yegaslpdlm agtglsrgsl ykafgdkkal
       61 llaaldlyma dglkatadil sqpgtvkeai rdsllryarl svgeagrrgc lavamttela
      121 ardpdvaert grmfrrlqql yagaivrgqa sgeiaeqdeq vlarllvcqv egmrvlgktg
      181 vseadmfalv drtmrfld
//
LOCUS       WP_175843032             211 aa            linear   BCT 11-JAN-2025
DEFINITION  SCO family protein [Burkholderia arboris].
ACCESSION   WP_175843032
VERSION     WP_175843032.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..211
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22773
     Region          53..206
                     /region_name="Sco1"
                     /note="Cytochrome oxidase Cu insertion factor,
                     SCO1/SenC/PrrC family [Posttranslational modification,
                     protein turnover, chaperones]; COG1999"
                     /db_xref="CDD:441602"
ORIGIN      
        1 msparsaphr rfsrlirtaa alaaavalaa cthdeprwnl tnvtghlpdl sftltggdgr
       61 pvdadafhgr ialvyfgyth cpdvcpetma rlmevlaklg pqadnvrilf vsvdpardtp
      121 qmmqsyvaaf daahargltg tdgqieslak ryrvayqmeq rdpsggyevt hssavyvfda
      181 tgrarllatd rdspdaiaad lrriidtasn t
//
LOCUS       WP_175843037             288 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia arboris].
ACCESSION   WP_175843037
VERSION     WP_175843037.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..288
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30555
     Region          12..278
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mkkiqgvysa prghwvgdgf pvrsmfsyqs hgthlspfll ldyagpatfe pataprgvgq
       61 hphrgfetvt ivydgevahr dstgaggvig pgdvqwmtaa sgilheefhs eaftkrggal
      121 emvqlwvnlp aadkmgapgy qtlldadipv velpdgagra riiageldgr rgparthtpi
      181 dvwdvrlvag gharfpvaeg rtlavvvlsg tvqvngetva reaqfvqlgr dgsdveiean
      241 gdakllilsg epidepivgy gpfvmnsqae irtaiedfng grfgqmpa
//
LOCUS       WP_175843106             294 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175843106
VERSION     WP_175843106.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..294
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32686
     Region          9..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="PBP2_CrgA_like_7"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08476"
                     /db_xref="CDD:176165"
     Site            order(100,104,143,157,159,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176165"
     Site            order(101..102,106..107,109..110,113,117,119..125,186,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176165"
ORIGIN      
        1 menlggfvvf vqvaetrsfv aagralglsa saigkriarl earlnvrlfh rstrsitlta
       61 egarflercr rviaeidaae qeltqsteap rgrlrvslpt igtlllplla dfmaaypeie
      121 ldidfsdriv dvvdegfdav lrtgrptdsr lssrllghfr qhlvaspdyl erhgaprtpa
      181 dlaqhrclhy rfpssgklei wplraprsgt ppevpvsmvs nnaetrqcfa mrglgiaclp
      241 effvrealea gtlravlaeh vvsrtpfyvl wpsgrhpapk qrafvdymve hlrl
//
LOCUS       WP_175842922             320 aa            linear   BCT 11-JAN-2025
DEFINITION  1-phosphofructokinase family hexose kinase [Burkholderia
            contaminans].
ACCESSION   WP_175842922
VERSION     WP_175842922.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..320
                     /product="1-phosphofructokinase family hexose kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008443 - phosphofructokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32798
     Region          4..306
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 mteivtvtln pavdvstsve hivdthklrc arprrdpggg ginvartvhr lggdcvalyl
       61 aggptgdvlt llldaehvpa vrmriagetr envcvtetat greyrflmpg psvtaaewrd
      121 caariaalqp aprylvlsgs lppgapddly atvartaaan gtrvvvdaag palraaldag
      181 vhlvkpslde lsalagepld easacgkaae lvaqgrvdiv altlgargaw vvtreralrl
      241 pgrpatvcst vgagdsfvgg mvwalargap fddacryala asaasvehpg talctradve
      301 rihaelvaqa sgaaiargta
//
LOCUS       WP_175843107             465 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sigma-54 dependent transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175843107
VERSION     WP_175843107.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..465
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51331
     Region          1..118
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <135..438
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mgadqrhviy ysrepndalr ghfdecgwrv dlaetvrdvr rvvqhgvata glldfspgfk
       61 psdlreletc lsiqhigwia atrrgqlqda tlrhlirdyc fdyvtmpyet srivetvgha
      121 hgmvaltdpv appvgagrse gemvgtcdam lglfrtirrv aatdapvfis gesgtgkelt
      181 avaiherssr aqapfiainc gaipstllqa elfgyergaf tganqrkigr veaanggtlf
      241 ldeigdlple sqasllrflq egkierlgah vsvpvdvrvi cathvdmeta lregrfredl
      301 yhrlcvlkie epplrargkd ievlarhmle rfkgdahrrl rgfspdavas lygyswpgnv
      361 relinrvrra ivmsegrmit aadlelndfa tlapvsllea reaaerqaie qallrhrgrf
      421 adaarelgvs rvtlyrlmca hgmrdrgdtl agfsaplpel phhac
//
LOCUS       WP_175843148             155 aa            linear   BCT 11-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Burkholderia contaminans].
ACCESSION   WP_175843148
VERSION     WP_175843148.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..155
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=16748
     Region          1..153
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mfnavvdapf gkvgirtdaa vvreivylpe avksvdpdsp lakravkqie ryferasarf
       61 dlplaevgsa fqhrvwdvis dippgtvlty gqvakrigsa pravgqacga nyfplvipch
      121 rvvaagglgg fanhddngyy qkvkrwllah egvpy
//
LOCUS       WP_175843115             303 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175843115
VERSION     WP_175843115.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32881
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..295
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,224..229,
                     235..236,238..239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mtfdlrqlra fttivscgsl graadalhvt qpalsrilkr ledqvgaplf erhskgvqlt
       61 afgeallpha tllqheaeha reeldamrgf akgtikvgtv gsiaslvlpv avgrvldrwp
      121 nlrveiiegv wdrlaeglnk heidlalsah gpdtdeivai pecrwedrsh ivaaphhplr
      181 algraptlad tlharwaipp rgtapfdhmr atfdahglal pgiavetrsv ttlkslvada
      241 gflswmaepm ygaeqragti dtlpvhevva vrtltafrrr hgilpgpagk lleelvaltr
      301 egr
//
LOCUS       WP_175843151             520 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Burkholderia
            contaminans].
ACCESSION   WP_175843151
VERSION     WP_175843151.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..520
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54778
     Region          24..520
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mpsslrssep ldvdallaal phriadvpar raahtpahpa liedarrlsy gdlsravdaa
       61 aallanlgvk ggdrvmivae ncvaqivllf aaarldawal vsnarlsase ldaiaaharp
      121 kliafttdas sdarthaerl gatpagtlpv digawsyrvd psapgepvaa dgaaqcaali
      181 yttgttgtpk gvmlshrnll fiaatssmlr rvspddvvyt vlpvshvygl asvclgslya
      241 gatlrlaprf speavrvala degvtifqgv pamhaklleh lhthghawra prlrfaysgg
      301 spldanlkar verlygvplh ngygmtessp titqtpldap rtdssvgvpi pgvemrivap
      361 dgtdvppgev geirvrgpnv mlgyyrnada thaavspdgw lstgdlarqe adgavtiagr
      421 skeliirsgf nvypveveqv lnahpdvvqa avigravegn eevlafverv pgstadeatl
      481 hawcaerlap ykrpahirvl dalpaastgk vlkhklrelv
//
LOCUS       WP_175843208             226 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175843208
VERSION     WP_175843208.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..226
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24836
     Region          10..225
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mstlpdvtrd rpaapaasla drayaqiqrd iitmhlkpga alneadlvar tgigrtpvhq
       61 avhrlvlegl lsvmprkglm vqplslddiv avidvrrlne ahcaelaarh atpddlarma
      121 allddgqacv dthdvegmme ldrafhqaia aaarnavlae ilralhersl rfwfvtlsep
      181 hhladvqheh relferlsar daagartave dhidsfrstl lqhlrp
//
LOCUS       WP_175843182             108 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia contaminans].
ACCESSION   WP_175843182
VERSION     WP_175843182.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..108
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11257
     Region          23..106
                     /region_name="CytC552"
                     /note="Cytochrome c551/c552 [Energy production and
                     conversion]; COG4654"
                     /db_xref="CDD:443692"
ORIGIN      
        1 mkhsilrvll atlligsgaa aradqtdgla laqrkncmac haigkplmgp sfrdiagkya
       61 argdavdyla qsivkgsvgv wssvpmpant qltnseahtl aqwvlsvr
//
LOCUS       WP_175843227             269 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175843227
VERSION     WP_175843227.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..269
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29908
     Region          85..268
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mrtwrlerpt lnaqldvsra trlvaaiggn epnafaaevl tlfddalsit qctifayefg
       61 nrprtmsvad rrggrylrdv adtyarhfya ldgnqqivst ahrgahrhdl llhqqagdei
      121 dheayraacy rgpdvsdrla llmqpddatw lsinlyrahr sgafqpreia aietlaplia
      181 qaakhhyala gatqigipqr mlarlrhacp elskreldvl rgvlegqtah eigetigvka
      241 ssvvtyqkra yrrlgissqr elfalcvqp
//
LOCUS       WP_175843233             403 aa            linear   BCT 11-JAN-2025
DEFINITION  benzoate/H(+) symporter BenE family transporter [Burkholderia
            contaminans].
ACCESSION   WP_175843233
VERSION     WP_175843233.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..403
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41430
     Region          15..403
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mnpsptasas raggrrffad tsvsalvagf vammtgytss lvlmfqagra ahltdaqiss
       61 wiwalstgma lttiglslrf rapvvvawst pgaalliasl pgvpypeaig afvvcavllt
      121 avgvsglfdt lmrkipagia aallagilfe igieifraaq fqtalvlamf ftyliikrla
      181 pryaivttli vgtaaagglg lldfsgfhia fakpvftmpa fsiasivsig iplfvvamas
      241 qnvpgiavlr adgyrtpssp liattglasl llapfgshgv nlaaitaaic tgpeahedre
      301 krytaavwcg tfylvagifg atiaalfaal pkalvvsvaa lalfgsimsg lanamqdvkq
      361 reaalvtfmv tasgltllsi gsafwglvag ivtqvilnar rpa
//
LOCUS       WP_175843234             422 aa            linear   BCT 11-JAN-2025
DEFINITION  sialidase family protein [Burkholderia arboris].
ACCESSION   WP_175843234
VERSION     WP_175843234.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..422
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45147
     Region          57..>244
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Region          104..153
                     /region_name="Sialidase propeller 2"
                     /note="Sialidase propeller 2 [structural motif]"
                     /db_xref="CDD:271234"
     Region          164..217
                     /region_name="Sialidase propeller 3"
                     /note="Sialidase propeller 3 [structural motif]"
                     /db_xref="CDD:271234"
     Region          <370..>418
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
ORIGIN      
        1 mvavksfaag cvlwlaaltp agahdmhdvs kaadphgahm smqaapaqqk qplatgaafd
       61 arhrlwvawv egahvvvahs ddagrtlsap vlvnampepv ytsaenrpki atspdgravy
      121 vswsmpldap ytgmvrfsrs ldggatwsvp vtvhrdrqai thrfdmmavd pagniaiawi
      181 dkrdlvaaka agqaydgaav yyavsrdgga sfeperkvtd htceccriam aidpagriea
      241 vwrnvfpgqi rdhalamlpv aasepvvpvr atfsnwhvea cpehgpalai tpdgtrhlaw
      301 fgvvdgradv fysrigadgl prgtpwafga nsaapgeqas haalaargdv vwlawkafdg
      361 dtmqiklrrs ddrgehwsap rviastsgas dnpqllddag riylswrtrn dgyrlvaveg
      421 aq
//
LOCUS       WP_175843243             392 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia contaminans].
ACCESSION   WP_175843243
VERSION     WP_175843243.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..392
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43020
     Region          8..369
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 malfssarpp rtilvaaprr igdvllttpl vrslkarwpe aqidmlvfrg tegvlehnpd
       61 vrrvivvaqr agfrerlrda lsmwrrydla caalssdrpr fyswfagrkr vglvdpnrvt
      121 wltrmmlngi ainhhesaht vvstlalapv igiepvsevv apgigndpar rarfdawlae
      181 spairagkpl vvlhpypmfr ykqwrldgwv emigwlrehg favalsggpa dsereyaeqv
      241 aaeaggdvln lvgrltfges aelvrrarlf igpdtgathv aaatgtdtia lfgpsdpvrw
      301 gpwpqhwpat enpwslrgsg rhgnvwllqg egdcvpcrhe gcerrvdsrs dclanlgaqr
      361 vkaaaaemlg lntpgpaeav vdtsrlhrts sd
//
LOCUS       WP_175843236             777 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor [Burkholderia].
ACCESSION   WP_175843236
VERSION     WP_175843236.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 777)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 777)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..777
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..777
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84492
     Region          59..759
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msstfaarps rgrlalacaa afawpaahaa stdeaaragt drpasagava paapagdtlt
       61 avsvtaqrqp vdpdtpavvt sitreqiesh tnvttedalk yapnlmvrkr yigdrnsvfa
      121 grdfnelqsa rglvyadgvl lsnllgssya ypprwslipp ddiarvdvly gpfsalypgn
      181 sigstvlltt rrpekleasl stqfftqryh dgygfadsfg gnhqtarian rvgrfwfals
      241 ldrlenngqp mqyaspnsay npklgaavpv tgaatdigpn gkprtivgaq tierteqlne
      301 tvrmgyaftd rveatltlgh wenhyrqhge tflrdaagnp vyggnvsigg qnmtvapnaf
      361 apqrgdqenw lyalglngrl dsgwrlsgvv saydvsrdvl raastvqgga gtlfqgdgtg
      421 wrtldlkaea pevkghtftf gyhydnyflr nvtyntadwl agpttslasv yrgdtrtqal
      481 fgqdawrfap gwlatlglry erwdayggal gnaggtlgya drganalspk valqwdatdv
      541 wrfrlsfatg trfptvgelf qgtisnnaiv nnnpnlrpek aidwdftaer dvgvgvvras
      601 vfqsdlrdsi ysqttvsgat tvtnvsnvdr vrvrgvelaf sgenvglrgl aidanvsasn
      661 aqiladaanp ayvgsrfpri prmranllas yrfdehwlas vgvrysgrqf ntldnsdvnp
      721 dvyggtssft vvdlkaryrl drhwtaslgi dnltdrryyv fhpypgrtfy gelkwsl
//
LOCUS       WP_175843254             871 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia contaminans].
ACCESSION   WP_175843254
VERSION     WP_175843254.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 871)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 871)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 871)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 871)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 871)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 871)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 871)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..871
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..871
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=91850
     Region          31..871
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mkgrqhaaqp pagqpghevh ahsgrfglrd lirqaarmta rdwrageltl lvlalvlava
       61 altsvgflad rlrqglerda rqmlgadfvv radrpvdpsf dqqaralglr tattaifpsm
      121 iasatggqat gaapsrlaav kavspgyplr gavdivpaga aaaqkaaaip apgtvwadpa
      181 lldalhlkag dtvrvglrtf kvaasisrel drgfsfvnfs prlmmradel aatgltgygs
      241 rvtyrllvag dqqavtrfea yaharvdggk lrgvgleslq egqpqvrqtl drarhfltlv
      301 alltallaav aiamaaqrym rrhldgcatm rclgvsrrtl galfalefag igivsgaaga
      361 vlgygghwal laalgglidv vlppptlwpa ligmgaalvl llgfalpplv pltrvppvrv
      421 lrrewgdasr tawaayavgv vlfaglliva agnlklgliv aggfagalvg falfarlvlf
      481 aaaravrnar vaagvgwrya laslhrrgta salqitalal glmcllliai trndlvagwr
      541 qstppdapnq flidiqpdqr advaaylaah gvrdavpepm vrgrlvaing kpvnpdayps
      601 eearrlvdre fnlsyttrlp sdnrivegdw fgtaatpqis ieaglaktln vkpgdvlrfd
      661 vtgltvdapi tsvrkldwgs frvnffvlmp ppvlkdfpav yltsfhlpas naalldplia
      721 rypnltaidv apilaqlqrm mlqvvgavqf lfmftlaagv lvlytalagt rdervreaal
      781 lralgasraq vnavqraefv vvgalagala sagaiavgwv lasrvfdfql avdpwlvpag
      841 iaagvacaga agwlslhnvl rrpalqslrd a
//
LOCUS       WP_175843264             216 aa            linear   BCT 11-JAN-2025
DEFINITION  SCO family protein [Burkholderia arboris].
ACCESSION   WP_175843264
VERSION     WP_175843264.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..216
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23542
     Region          63..191
                     /region_name="SCO"
                     /note="SCO (an acronym for Synthesis of Cytochrome c
                     Oxidase) family; composed of proteins similar to Sco1, a
                     membrane-anchored protein possessing a soluble domain with
                     a TRX fold. Members of this family are required for the
                     proper assembly of cytochrome c...; cd02968"
                     /db_xref="CDD:239266"
     Site            order(97,101,179)
                     /site_type="other"
                     /note="Cu(I) binding site [ion binding]"
                     /db_xref="CDD:239266"
ORIGIN      
        1 mntfpklfml tplligcall aghaaqaqes mdahahhhmm mqgmpgmktm mpamktstvt
       61 ytvpavtlvr ddgktvalkd elddgrpvvl tfiyttctsi cpvlsqtlsq lqqalgadrd
      121 kvhivsisid pendtparlh ayaakfgagp ewqhytgtla asvatqkafn vyrqdkmdhn
      181 pvmflraapg qswlrvdgfa ttddllhmyh slvasn
//
LOCUS       WP_175843286             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: replication-associated recombination protein A
            [Burkholderia].
ACCESSION   WP_175843286
VERSION     WP_175843286.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..436
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=47939
     Region          1..434
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 msdlfqvepr rplaealrpk tlaevigqth llgegkplrl afesgkphsm ilwgppgvgk
       61 ttlarltala fdcefialsa vlggvkdire smeqakdtln rtgrhtilfv deihrfnkgq
      121 qdallpfves glvtfigatt enpsfevnsa llsraqvyvl ksldddemrq llkraqeial
      181 dglafddkai dtlvgyadgd arrflnlleq aqtaatsagv atidadfvss amtlnarrfd
      241 kggdnfydqi salhksvrgs spdgalywfc rmidggadpk ylarrivrma wedigladpr
      301 alqmandaaa tyerlgspeg elalgqaviy lacaaksnag ynafnqamaf vkqdksrevp
      361 vhlrnaptkl mkelgyghay ryahdepnay aagetylpdg mreprwyqpv prgleskiad
      421 klawlreldr eagkkd
//
LOCUS       WP_175843290             372 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Burkholderia].
ACCESSION   WP_175843290
VERSION     WP_175843290.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 372)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..372
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40493
     Region          1..371
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 maslsirdvy ktypngvpvl kgvdieiedg qflilvggsg cgkstllnmi agletvtsge
       61 icidgkvvnd lspkdrdiam vfqsyalyps mtvrenisfg lnirkvpkne qqqivdrvsq
      121 mlqiqhlldr kpgqlsggqr qrvamgrala rdpslflfde plsnldaklr iemraeikll
      181 hqrlgttivy vthdqieamt lgdriavmkd gvvqqfgapq diydspsnlf vagfigappm
      241 nfingklveq gsgialeidt glarsalklp fdaaklkshv grevilglrp eritdarnah
      301 ngeasnlqpi dvrvdvtept gpdthvfaqv ngkrivsrvh paanpqpgqt qsllfdvska
      361 vlfdpaseer ia
//
LOCUS       WP_175843329             404 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid aminotransferase [Burkholderia contaminans].
ACCESSION   WP_175843329
VERSION     WP_175843329.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Alexander,F.W., Sandmeier,E., Mehta,P.K. and Christen,P.
  TITLE     Evolutionary relationships among pyridoxal-5'-phosphate-dependent
            enzymes. Regio-specific alpha, beta and gamma families
  JOURNAL   Eur J Biochem 219 (3), 953-960 (1994)
   PUBMED   8112347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..404
                     /product="amino acid aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43595
     Region          1..396
                     /region_name="PRK09257"
                     /note="aromatic amino acid transaminase"
                     /db_xref="CDD:181731"
     Site            order(102..104,130,183,214,243,245..246,254)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(105,140,207,252..254,290,293)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            246
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 myahiptypg dpilslfqtf qqdahpnkvn lsiglcydda gripvldstr iaaerlreag
       61 aphtylpmeg laayrqgvqr lvfgadcaal aegriatlqt lggsgairlg aefvkryfpd
      121 savwisdptw dnhrvifsaa gldvhtypyy dearndirvd amlatldalp prsvvllqpc
      181 chnptgldlg rdawqavidv larrglipfl dmayqgfgdg ldddawavra ivdaglpaiv
      241 gnsfsknfsl ygervgglsi vcagageaat vlsqlqagvr rtysspplfg aqlvstvlnd
      301 dalrarwede vaqvrtrikr mrgalkarld mrvpgrsfda lvaqrgmfsy tgiaaddver
      361 lrtghgvyll rsgrmciagl ndanvdhvan aiadvldgal rpaa
//
LOCUS       WP_175843381             163 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia contaminans].
ACCESSION   WP_175843381
VERSION     WP_175843381.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 163)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..163
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17446
     Region          18..147
                     /region_name="NUDIX_ADPRase"
                     /note="ADP-ribose pyrophosphatase; cd04673"
                     /db_xref="CDD:467557"
ORIGIN      
        1 msdsprspsr vpasvrpvpa vigivlrerd vllvrranpp dagcwgfpgg kievgesiad
       61 avvreiaeea tmdvealdaf taldafdyda ggdvrqhfvm vavlcrwlrg tpaasddald
      121 arwfdlaeld rddlpmsagv rdvarraieh aaayghaprp ant
//
LOCUS       WP_175843414             418 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: lipopolysaccharide biosynthesis protein
            [Burkholderia].
ACCESSION   WP_175843414
VERSION     WP_175843414.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..418
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45174
     Region          12..395
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mlkrfgnpdv akavanlvwl glerltqigv aiaisgllar yfgpdvfgkw qyantlllvl
       61 apltwvcgae ilvptivqrp paqlgavlgs afalriavsa aalaatwiai gagafdplvg
      121 amlaglavtm vfrepfvgvi nawlqsmtys kpqlvasmit alakallvwl lvraaagpar
      181 fawlwaleaa aigfalllyy rhrnggtlgw tldkplfrhf atagtvfwlg licmylflkl
      241 drlmlerhvs fadlgrysaa qqlnenwitl almlaqtiap afvyrvqdva rlrrnivrli
      301 amtaclmtag alvldaaapl ivgkvfgpgy easvdifrwa vwlsvpagie aignlivlky
      361 qakfvllskw llalaiaalv nlfaiprlgl ygalvglaag ylaaaavnfy yirfklrt
//
LOCUS       WP_175843383             331 aa            linear   BCT 11-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Burkholderia contaminans].
ACCESSION   WP_175843383
VERSION     WP_175843383.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..331
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=34942
     Region          <16..324
                     /region_name="FAD_binding_2"
                     /note="FAD binding domain; cl46878"
                     /db_xref="CDD:481218"
     Region          48..74
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          79..109
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          114..136
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          173..202
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          211..232
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          240..266
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          299..325
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mtdssfaaap aradasdvaa laarlaspda avrrvalfel adledpgfvp afiaalrddp
       61 sadvraeaar vlgaweqpdv vdalcgalld pdddvrtaaa qslselknsa sgavlcrwaa
      121 rpepfvrrav lrglrelrdp gafapalhal daehaavrae avavlgwlkd pralpplagi
      181 attdtaadvr rlavgaigfa apddastiha lflalrdhew qvreetattl gklrvatare
      241 plvaaldddy wqvrlraara lgqlrdaaaa pavaallaha isnlrkeaal algelrdrtt
      301 lpaltraled hdpevrkavr iairqidess p
//
LOCUS       WP_175843437             155 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175843437
VERSION     WP_175843437.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 155)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..155
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16726
     Region          16..128
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(17..19,33,50..52)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(64,67,71..72,81,99,103,109,113,116..117)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 msktvtqpss tsagpltigq vaemtglsth tlryyeqagl lraisrtaag hrlyapadld
       61 wlafvmrlka tgmpiaqmqa faalraqges tfgarrsllv ahhdavrahi aelqasldvi
      121 sdkivnyeaq erdmaqrarp shslseqdgh ngttr
//
LOCUS       WP_175843460             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175843460
VERSION     WP_175843460.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33582
     Region          17..74
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          103..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(113,117,156,170,172,231,248,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(114..115,119..120,122..123,126,130,132..138,199,
                     225..229,236..237,240)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mtshpipapd kpldlldval fvraallanv taagrefgvs aavasariaq lerqlgarll
       61 hrttrrislt qdgevfmaha dtllaaadaa rasvghgrte pygrlkvsms ssfgrqhvap
      121 vipaflrryp svsldlrlsd eivdlvddgy dvairlgalk dstlvarkla tnrrvlccsp
      181 aylaehgtpr hpadlaqhec vilgdqrdws fatpqgpltv rvsgrlvasn geairealvd
      241 gfgiaikstw dvgpllasga lvtvlddypf aediaiwavy psrahvplkt lafiaflagh
      301 fgdppywdra dgq
//
LOCUS       WP_175843461             288 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: hydroxymethylpyrimidine/phosphomethylpyrimidine
            kinase [Burkholderia].
ACCESSION   WP_175843461
VERSION     WP_175843461.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..288
                     /product="hydroxymethylpyrimidine/phosphomethylpyrimidine
                     kinase"
                     /EC_number="2.7.1.49"
                     /EC_number="2.7.4.7"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008902 - hydroxymethylpyrimidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008972 - phosphomethylpyrimidine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009228 - thiamine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009229 - thiamine diphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=30454
     Region          8..248
                     /region_name="HMPP_kinase"
                     /note="4-amino-5-hydroxymethyl-2-methyl-pyrimidine
                     phosphate kinase (HMPP-kinase) catalyzes two consecutive
                     phosphorylation steps in the thiamine phosphate
                     biosynthesis pathway, leading to the synthesis of vitamin
                     B1. The first step is the phosphorylation of...; cd01169"
                     /db_xref="CDD:238574"
     Site            order(8,15,17..18,20,24,27..28,31,34..39,41,44..48,53..54,
                     56,58..59,62,65,69..70)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238574"
     Site            order(14,26,47,83,214)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238574"
     Site            order(108,145,181,211,213)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238574"
ORIGIN      
        1 mpsnappivl tfglsdptgg sglqadlmtl asmgchgvsv ltgytvrdsa acdevtgldp
       61 dvvaaqarml ledmpvaafk igaatraevv saiaevvady dgvplvlapd ftlddehvla
      121 addlresiad llapqttllv adhatliala qpdgdaeapn ldaavshlls qgceyilsse
      181 tgshrlvntl ygeegqlred mwdrsphrlm gitdtlgaai aallangqep peavreaqey
      241 lyqavrdafr pgmgaylpdr ffwarsneds dtppavkadp vprtshrh
//
LOCUS       WP_175843480             319 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia contaminans].
ACCESSION   WP_175843480
VERSION     WP_175843480.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..319
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34442
     Region          83..292
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mplnpkiaqv ldmverakrp syhhqtpqqa raayeksapi ldvapapmhs veecvvptrd
       61 grtidarlyl plapslaepl palvyyhggg ftvgsvdthd alcrmfahda qcavlsvgyr
      121 lapehrfpta vhdaadalqw lhreaaafgi daerlavggd saggtlatvc avlardagir
      181 lalqmliypg vtgfqdtesh arlangyllt qdtiqwfftq yirdradrdd wrfapldgtr
      241 dapsfagvap awiataeydp lsdegaayae klraagnavt lvcypgmihe ffkmggyvpe
      301 vraahadaia alkaafddv
//
LOCUS       WP_175843513             451 aa            linear   BCT 11-JAN-2025
DEFINITION  uracil-xanthine permease family protein [Burkholderia contaminans].
ACCESSION   WP_175843513
VERSION     WP_175843513.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..451
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45924
     Region          9..423
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mphdpisppv darlpawqla lfglqhvlsm aaspitavfl iakvlalpad ltvqligatf
       61 facgigtllq slgagpigar mpfvmvpgga ptmlfagiaa qsglptaags allasafywv
      121 llpvftrclr lfprivvgam lllvsvnlir iyativvgqp dsadfaqpra lglalativa
      181 tvvvagafrg tlgrlavlig lmagatlgwa ldampaladv wrgplfthpv wlpfgmprfd
      241 vlaalpllif taismaeata qtvavgetcg kaislsrdvp ktirgdalas lagalfgtpl
      301 ivtsaenigv vqttgvrsry vtaaagaili vialfaplar layaipaavv ggtalvvftm
      361 igvmgirlla svdlharanq ytlaaalvvg lapilvpnly rhfgspvqiv lgngmaagtl
      421 aaiatqlafa alarlsgqtg taaatapsrd a
//
LOCUS       WP_175843538             333 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175843538
VERSION     WP_175843538.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37193
     Region          54..205
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <218..314
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhpapgqpve datiaaftpa isrstrysre ndlrqtlaer varwtegvdh lttaipnlsf
       61 hrreattqpm dcmvepsfgl vvqgtkrliq sgdvylcdan rflitsldlp gstqvieasr
      121 erpflgiglk ldfrvmaelm aqvaadheea pagrglvvge mneplydavn rllallddpn
      181 aiavlapyve reiyyrllts dqgarlrqia sagsqgnrvs raiqwlrihy deslrvddla
      241 aqvqmssstf hhhfrqltgm splqyqkwir lnearrlmls erldatsasf rvgyasptqf
      301 nreysrlfgn sprrdidslr sgtdvvlsaa aty
//
LOCUS       WP_175843545             315 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175843545
VERSION     WP_175843545.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..315
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35051
     Region          24..70
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          102..303
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(117..118,120..121,124,128,130..136,229..234,
                     240..241,243..244)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 medddrtasl diwlvrvlrt lllersvtqa alrlnqtqpa istalrklre tlndpilvrg
       61 ksgmvpteyg aslleaaara lrevdfiatp hgdfdpssar rtfrvaapdy lndffmptli
      121 erfrdaapha hleidslnpa ldhagalesg aldlvignwp kpdpqfarqd lfsdtivclm
      181 rdahplarvp ltreayaaaa hvaptpytgd krnaieigla rarltrrivt tlpyfgivpq
      241 vllqsdlift ttrrfathya qllplvvvtp pvpfpriksy llthpqpdrp tdiawlcalm
      301 qsvsdeltva rtrkr
//
LOCUS       WP_175843559             327 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175843559
VERSION     WP_175843559.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..327
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35459
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,161,163,226,243,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,190,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mnqiqtmrvf vcvaeqqsfr raahhlgvsn alvtrsiaml eghlntrlih rttrnlslte
       61 agvrylegcr alleefdhle ssvahavrep agtlrvvasg llsplaltpl vssfrhrype
      121 lrvqltvaee pldvldsgyd vgivtgnrle gnptlighal apnpfvacaa payldrrgep
      181 rlpddlpghd wvtlaahqha ptwqlvghdg vahsvtvrpa ctvnqlalvq aaavagagia
      241 vlpepcvada lnngtlvrlm agyriddpdt qlslvypnrq yvpartrsfv ahaldhfsaq
      301 tardrtdygf mrpargpers divtglq
//
LOCUS       WP_175843571             555 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia contaminans].
ACCESSION   WP_175843571
VERSION     WP_175843571.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..555
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60139
     Region          1..550
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mhvsatpaap vtvftarril tmnpaqpsat hvavrdgril avgdaadaat wharfgactt
       61 ddtlrdkvlm pglveghchl megamwdavy vgyydrrgpd gtlwpglrsl davlerlaea
      121 eramtddgpl lawgfdpiff gtarlaarel drvsaqrpia ilhasvhlmn vnsamlarag
      181 idedtdidgv trdadgrptg elqefaamlp vyqtiggkla isasekphav wnfgrvaqla
      241 gvttatdlvn dlsadgnrtl hdvtadpdyp vrivpafapq rnparsadsv raeierntdk
      301 lhfgpvkfiv dgsiqgftar vrwpgyaggq pnglwlippa qlvdvfepfh raglqlhvht
      361 ngdeatdvvl damttllarh prpdhrhtlq hcqmadaaql krvrtlgmcv nffanhlyyw
      421 gdahydqtig pdrasrmdaa gsaqrlgipf alhsdapitp lnplftawca vqretasgrv
      481 lgegerlsvd dalhaitlga aytlrmdhlv gsievgkfad favldddpsv saparlkela
      541 vwgtvlggrv frslr
//
LOCUS       WP_175843593             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175843593
VERSION     WP_175843593.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33847
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdnlgdirlf veaaslgsls aagrklglsp aaasarlvkl egelhtqlfe rstrklrltd
       61 egrlylvhcq halqtledar aalqagrasv sgalrvsats dfgrtvlrrw ldefnerhpn
      121 vtltlvlsds lshllqddid lairfgvpad ssivakrmad nrralcaspd yiaehgmpnh
      181 pddlrehrci vlssaagaan nwrfardget asftapldrs rqtndgslar ewaiegrgva
      241 mksiwdigad lqagrlklll qewrcpdvpv nalfqrtlym aprvrtlldf leprfsease
      301 alapflr
//
LOCUS       WP_175843648             273 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia contaminans].
ACCESSION   WP_175843648
VERSION     WP_175843648.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..273
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29162
     Region          12..259
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mstrssapta astatplldl ritrklygdr tiladvplqv argeivcvvg psgcgkstll
       61 rivagldtdf rgsvklggva ldgpspragv ifqeprllpw lsiadnvgfa agprggreps
      121 varlldevgl agvarqlpat lsggmaqraa iarglfgepd lllldepfsa vdaitrmrlq
      181 tllldvverh rtaaivvthd ldealylgdr vlmlapnpgr iddeihvgvv rprdrrdpal
      241 avlrarllda fqqlqdrade tkrrthdlqa sea
//
LOCUS       WP_175843669             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175843669
VERSION     WP_175843669.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33720
     Region          23..80
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          109..303
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(124..125,127..128,131,135,137..143,233..238,
                     244..245,247..248)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 misdqngeid sqsirtnlps lmalrcfeaa arhenfsraa delclthgav sravrlledd
       61 lgvalfqrrs rrvfltdagr klaqavhdgl glmrhaaqel rteaararrw vlsceptllm
      121 rwliprwpdf qarhagvdih laaaggpfsf dsgidmairr ddfawpagyh aerlfaekvg
      181 pvcrpdkvda wfsvrrgnrs lktdvpalht rtrpdawkew avaanqpaag grgqtfdhfy
      241 fslqaavagl gvaigpwhlv rddiesgvlv apmgfvedgs hyclltpepv vagsaqadvl
      301 gwlraav
//
LOCUS       WP_175843660             430 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia arboris].
ACCESSION   WP_175843660
VERSION     WP_175843660.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..430
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46334
     Region          38..419
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 msfdfstprt rracrrapvl waallvagav haqqspvtld aalqsatdhs asmqaaqasv
       61 larseaavka gqlpdpmlka gidnlpingg qrftvgqdfm tmrrigieqe wvsgdkrrlr
      121 talaneqvgr eragylaqla tvrqqtataw ldavyakqal alqqallghm nheleamqas
      181 yrgakasasd vvqaramlaq tqdqvlkaqq ayrtalvala rwtavpvadv tgtppapesf
      241 vsslppdelr lsqpalvaaa ddiavaeadt avanserspn wtweiayqqr ggaysnmvsv
      301 gvsiplplnr knrqnrdvae kaaletkarl myedtlrqvq adirtqsdtl asgrerianl
      361 stallpaadq rvqlataayr agtgtladtf aarraqldaq lqvldlrrdv sqtwaqleyq
      421 vvpsamaaaq
//
LOCUS       WP_175843672             211 aa            linear   BCT 11-JAN-2025
DEFINITION  DsbA family oxidoreductase [Burkholderia contaminans].
ACCESSION   WP_175843672
VERSION     WP_175843672.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..211
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22739
     Region          3..203
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(11,14)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 mqidlyteit cpwcivghhr ldkvlaerfp nlavdirqhp vlllpdapag glyipdllrs
       61 rygitdpkia ftrpereara sgfdldlgrq lrayptqaah avilaaagld tqhrlavais
      121 hayfiaakni adadvladia adygfdrdqa raiardpeqh rrveaeafks anagvrsvph
      181 fvfggsiain ggrsedeiaa aiqaasgvis l
//
LOCUS       WP_175843701             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia contaminans].
ACCESSION   WP_175843701
VERSION     WP_175843701.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..359
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38073
     Region          159..356
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mtkvflilvr nellgylrsr sslfwtlvfp vfllsvmlfa fggsgslgta divfavpggt
       61 tpysraceaq iveslthsdt vkatfdgrga aadrvtvvlg sdertpatir ydfngslavk
      121 aasrvveial arcaaqrlgl paaqarfena aparrpfdyg affatgilvm afmaiglnst
      181 ttaiaslrer ntfklyvcfp vsrgvflaal ivarmimmal salvlltvar vafgialpia
      241 tpdglralpi vllgaamvls igvllasrak slaaaelacn vtyypllffs dltipmhdap
      301 awlkavlafl ptnqfavalr galvdgapya qlapqllgma astalflfaa arlfrwhda
//
LOCUS       WP_175843718             298 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175843718
VERSION     WP_175843718.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32524
     Region          8..>51
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..290
                     /region_name="PBP2_LTTR_like_4"
                     /note="TThe C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08440"
                     /db_xref="CDD:176131"
     Site            order(109..110,112..113,116,120,122..128,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176131"
ORIGIN      
        1 mkidtlgvqa fvaiadggsf rqaadtlhvt qtaitqrlrk lesylgvalv erttrrttlt
       61 eigrrflpqa rrllnelsda lteiretgls qrgdvtiacv ptvgvqylpr ilrafsghrp
      121 hdrvkildha sasvlqavlr reaefgisia gdqhpelvsv plthdpyvlv crddhplakr
      181 rrirwaalqp hplifagevs gnrgllegal ktsgvslhsf yevqrsstal glvaeglgaa
      241 vvpklaiqkn aypmirtiel vepsvsrtlv lvtrknaqls paacalydmi veratpcp
//
LOCUS       WP_175843797             204 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Burkholderia].
ACCESSION   WP_175843797
VERSION     WP_175843797.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..204
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22307
     Region          1..199
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mklyywpktr afralwmlee igvvyelvpi dlrsheqgsd afvqvnpmak lpalddgsap
       61 faesgavlly ladccpgagl giapddplrg rflqwmfftp tclepamaek ftgasgnpva
      121 fgwgnitrvq ralaqalahn pwlvgdrfta adlllastlk iafdahllph egvlgdyvar
      181 aedrdafrra vaieqreaar llha
//
LOCUS       WP_175843800             316 aa            linear   BCT 11-JAN-2025
DEFINITION  ketopantoate reductase family protein [Burkholderia contaminans].
ACCESSION   WP_175843800
VERSION     WP_175843800.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..316
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32899
     Region          1..305
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkiailgaga lgcaigatlt egghetwlid rspehvnamr ahglrvddas gtrqvqvrat
       61 trpdeagvae vvivlvksfh tdaairgaqa lvgpetrvls lqnglghedi ladavgrerv
      121 lagktyvggv lrgighiesg vvgkhtiige ldgrvtdrvr riadafsnag ldtqvsdniv
      181 gtmwdkllvn vatgaltgit sltygqlyde pllkatslaa vaeaiaaaka agvalsmndp
      241 eqawslaaeg lpaafktsml qslekgsvte idfingsvvr wgarygvptp vnatlvacik
      301 gieramldrr kaeaqa
//
LOCUS       WP_175843866             211 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia contaminans].
ACCESSION   WP_175843866
VERSION     WP_175843866.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..211
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21955
     Region          1..207
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mnsttlllyv itvsavtvtp gptmllalnn gatrglriaa ygiagaalsd liligavgcg
       61 lgaimqaseh lfvmlkwaga vyllylawal whapatlpst dvvpadgarn grsafkrsll
      121 valsnpkgll ffsaflpqfi qpeanvaaqy atlailtati dvllmaiyaa sgyhamkams
      181 gralkwlnrg cagmlaglav alslyrrgmt a
//
LOCUS       WP_175843895             242 aa            linear   BCT 11-JAN-2025
DEFINITION  copper homeostasis protein CutC [Burkholderia contaminans].
ACCESSION   WP_175843895
VERSION     WP_175843895.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Latorre,M., Olivares,F., Reyes-Jara,A., Lopez,G. and Gonzalez,M.
  TITLE     CutC is induced late during copper exposure and can modify
            intracellular copper content in Enterococcus faecalis
  JOURNAL   Biochem Biophys Res Commun 406 (4), 633-637 (2011)
   PUBMED   21362400
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Li,Y., Du,J., Zhang,P. and Ding,J.
  TITLE     Crystal structure of human copper homeostasis protein CutC reveals
            a potential copper-binding site
  JOURNAL   J Struct Biol 169 (3), 399-405 (2010)
   PUBMED   19878721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..242
                     /product="copper homeostasis protein CutC"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24523
     Region          9..238
                     /region_name="CutC"
                     /note="Copper homeostasis protein CutC [Inorganic ion
                     transport and metabolism]; COG3142"
                     /db_xref="CDD:442376"
ORIGIN      
        1 mnrnaasssv lleviattvg dakaaaraga drlelvtait eggltpsvgl ieavvaavpi
       61 pvnvivrphs rsfvydaddl rvierdvraa vaagangvvf galdargdvd ldalariaaa
      121 adgrvltfhr afdvsrdlna afdallrvpa vtsvltsggh psvldavati trlvrqaags
      181 tctvlagsgl tvdavgdfvr atgvravhfg sgvrprgevl apvdqslver vraaidgaaa
      241 hv
//
LOCUS       WP_175843922             127 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia arboris].
ACCESSION   WP_175843922
VERSION     WP_175843922.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163535
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..127
                     /product="VOC family protein"
                     /calculated_mol_wt=14075
     Region          4..123
                     /region_name="GLOD5"
                     /note="Human glyoxalase domain-containing protein 5 and
                     similar proteins; cd07253"
                     /db_xref="CDD:319916"
     Site            order(4..11,28..29,44..48,66..77,82..83,86,95,102..105,
                     114,117..118,120,122)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319916"
ORIGIN      
        1 malidhldhl vltcvdpdkt khfytevlqm qletfgagrl afrfgnqkin lhvrgaefep
       61 kahvpvpgal dlcfiasvpl ddviahlqra awpivegpve rtgatqkirs vyvrdpdlnl
      121 ieiaeli
//
LOCUS       WP_175843941             546 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia contaminans].
ACCESSION   WP_175843941
VERSION     WP_175843941.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..546
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58422
     Region          1..528
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mqydyiivgg gsggsslagr ladacpdati alieagshte rnllvnmpvg iaalvpfklg
       61 tnygyetvpq pglggrrgyq prgrgmggss ainamiytrg hpgdydewaq lgatgwgwqd
      121 vlpyfrraeg nargadawhg adgpltvsdl rfrnpfserf iqaahaagyp lnddfngatq
      181 egvgfyqvth rdgsrcsvar ayiygrnrpn lhvitdatvl rvtfdgkraa gvavarngri
      241 etldaraevi lsagafnspq llmcsgigpa eqlrrhgiav vqdapdvgan lidhidfiin
      301 trvnsselvg vclrgiakmt palaryfssr tgmmtsnvae aggfiksdps lerpdlqlhf
      361 ctalvddhnr kmhwgfgysl hvcalrpfsr gtvalasgda rdaplidprf fsdsrdldll
      421 vrgtqamrki lsqaplasqg grelytradq seaelrktiv ehadtiyhpv gtcrmgsdar
      481 avvdpqlrvr gveglrvvda svmptlvggn tnapsvmige raadfivatr kgaaprgeaa
      541 aavhgr
//
LOCUS       WP_175843945             353 aa            linear   BCT 11-JAN-2025
DEFINITION  M48 family metallopeptidase [Burkholderia contaminans].
ACCESSION   WP_175843945
VERSION     WP_175843945.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Lew,R.A.
  TITLE     The zinc metallopeptidase family: new faces, new functions
  JOURNAL   Protein Pept Lett 11 (5), 407-414 (2004)
   PUBMED   15544561
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..353
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37308
     Region          138..321
                     /region_name="M48C_Oma1_like"
                     /note="Peptidase M48C, integral membrane endopeptidase;
                     cd07331"
                     /db_xref="CDD:320690"
     Site            order(204..205,208,261,265,305)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320690"
     Site            order(204,208,261,305)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320690"
ORIGIN      
        1 mrsnglhrla rvaaslsvga aalaagfaha tdagtsaata agsapaaapa sppanstpaa
       61 paqpataepa qptgatastk ayaqssqqvr ygdaiafrtl ipsplleqlt aneyaqivqa
      121 aadsnrllpa nqprvkrlra ivaklapysv kwndrvkswa wdvnairsrd irltclpggk
      181 vlmygglldr vrlnddelgv llahgiahal reharsnfsa tsqtslraaa lpplfgvgep
      241 lpqalnlger lqslhydptd eteadviggd iaaragfdpr aaitlwdkla vatrgnkatg
      301 fiythpysta rrqdllnrlp dlmplyakav gkrvdtlpdy agisaqrrki vrr
//
LOCUS       WP_175843467             164 aa            linear   BCT 11-JAN-2025
DEFINITION  arsenate reductase ArsC [Burkholderia arboris].
ACCESSION   WP_175843467
VERSION     WP_175843467.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Messens,J. and Silver,S.
  TITLE     Arsenate reduction: thiol cascade chemistry with convergent
            evolution
  JOURNAL   J Mol Biol 362 (1), 1-17 (2006)
   PUBMED   16905151
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Mukhopadhyay,R. and Rosen,B.P.
  TITLE     Arsenate reductases in prokaryotes and eukaryotes
  JOURNAL   Environ Health Perspect 110 Suppl 5 (Suppl 5), 745-748 (2002)
   PUBMED   12426124
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Messens,J., Martins,J.C., Van Belle,K., Brosens,E., Desmyter,A., De
            Gieter,M., Wieruszeski,J.M., Willem,R., Wyns,L. and Zegers,I.
  TITLE     All intermediates of the arsenate reductase mechanism, including an
            intramolecular dynamic disulfide cascade
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8506-8511 (2002)
   PUBMED   12072565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..164
                     /product="arsenate reductase ArsC"
                     /EC_number="1.20.4.4"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030612 - arsenate reductase
                     (thioredoxin) activity [Evidence IEA]"
                     /GO_process="GO:0046685 - response to arsenic-containing
                     substance [Evidence IEA]"
                     /calculated_mol_wt=17615
     Region          4..143
                     /region_name="LMWP_ArsC"
                     /note="Arsenate reductase of the LMWP family; cd16345"
                     /db_xref="CDD:319973"
     Site            order(9,11..16,112,114)
                     /site_type="active"
                     /db_xref="CDD:319973"
ORIGIN      
        1 mttnvlilct hnsarsvlse gmlnhwaekl gkdvrgysag sapsghlnpf alealtnagv
       61 dvngyrsksw defvgdgtpe mrivitvcdn aaaetcpywp gspvkvhwgy adpsnalggd
      121 egkrvafelt rqaigyrmlq llalpldrmt haelqtalta isqn
//
LOCUS       WP_175843948             442 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia arboris].
ACCESSION   WP_175843948
VERSION     WP_175843948.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..442
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46083
     Region          17..420
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mlihhvepsl qdltaterra payawlvfgl tvglllsdym srqvlnavfp llkhawslsd
       61 tqlgslsgvv allvglltfp lsvladrfgr vrsivlmaal wsvatlgcal stnyaemlva
      121 rglvglgeaa ygsvgvalil sifparlrat ltgafmagga fgsvfgmalg glvgahlgwr
      181 wsfgvmaalg ivllfayrcv vterrlaacr vepcrrdada prdlrgsvra lmsglfasrs
      241 vicaylgsgl hlfvpgalfa wlpsylnryy amapdraavl aagfvliagv gmvgcgivtd
      301 rvgradgsrk wltaitycvl tgiclaiafr lppgplqlal icagmlvgag asgasgamva
      361 nltpaaihas afatltlann llgmapgpll tgwvadragl vgalqwipvv plaaavlfai
      421 grasyaadlv rvererrasq ls
//
LOCUS       WP_175844047             204 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia
            contaminans].
ACCESSION   WP_175844047
VERSION     WP_175844047.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..204
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22681
     Region          1..204
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mmkligslss pyvrkarivl aekkidykle lenvwapetd ihasnplgkv pclvmedgaa
       61 vfdsrvicey vdtlspvgkl ippsgrerle vrcwealgdg vidaavairv ehtmrdeaqr
      121 saswiarqqr kiddglvams qglggktwcv gnhytladia lgcalgyldf rmpelnwrdr
      181 hpnldkhfak lllrpsfadt lpqn
//
LOCUS       WP_175844058             282 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia arboris].
ACCESSION   WP_175844058
VERSION     WP_175844058.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..282
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29835
     Region          7..260
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtrstaalaa rglsvgyrdh vvidgldlsi aagrvtalcg pngcgkstll rtlaglqpar
       61 aghvevngqp lasfrrrala reltmlaqfn qipsgltvre lvaygryayg gflrglsrad
      121 haaidealdt sgladdaerd vgalsggerq rawiamalaq qapivlldep ttyldihhql
      181 dildalrtln rargltivwv lhdlnqaaay sdeivlmrag rlvaqgtpda mldparlraa
      241 fgvemlklah pqtgapmcvp aygpttdgap qaagvfdrdl av
//
LOCUS       WP_175844086             243 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia arboris].
ACCESSION   WP_175844086
VERSION     WP_175844086.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008163
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..243
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26105
     Region          1..189
                     /region_name="COG3963"
                     /note="Phosphatidylethanolamine N-methyltransferase [Lipid
                     transport and metabolism]"
                     /db_xref="CDD:443163"
ORIGIN      
        1 mripewmlfl rtwlrnprrv galapsgpal aalitahvpr erasvielga gtgvftrall
       61 argvasdrlv lveadpafan alrhqfpalr imqmdaaqlg mtgdffgger adaivsglpl
      121 vampveqava ivhcafarhl aagggfyqft yvprcpipsr yleamrirav rvgvawmnfp
      181 pavvyrferc seadgcqwpd arplrdvvad apalhgidas rlsrlsalgp sdagpatvri
      241 sls
//
LOCUS       WP_175844114             260 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia contaminans].
ACCESSION   WP_175844114
VERSION     WP_175844114.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..260
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29322
     Region          7..260
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mltlsladlk ksitawrlwt llgwleirqr yarsrlgpfw ltismgvmit slgvvygtlf
       61 gqkineylpf laasivlwgl fsttivegsv ayinsapyir qmatpkliyi lqvvwrnliv
      121 lahnfviviv llaiygvksw etlpifipav lvyvlnatwi amvvgllsar frdlpqivsa
      181 llqvafyvtp iifrpdalnr fsfivewnpl aylidlvrgp ligqmpselt wgvtvgmaai
      241 gwpvamlmtg rylkripywv
//
LOCUS       WP_175844130             339 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia arboris].
ACCESSION   WP_175844130
VERSION     WP_175844130.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..339
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34818
     Region          36..338
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtqppvsptd agaqqdvtgr raralsgtrl glsnylglag alaamialfs vlsshfltyd
       61 tfstianqip dlvvmsvgmt fvliiagidl svgsvlalaa smvsvaalkw qwgplpaalm
      121 giavatatga ltgavtvgwr ipsfivslgv leaarglayq ltnsrtayig dafdflsnpi
      181 algispafli avavmiaaqf vltrtvfgry lvgigtneea vrlagvnprp ykilvfalmg
      241 alaglaslfq isrleaadpn agsglelqvi aavviggtsl mggrgsvist ffgvliisvl
      301 aaglaqigan eptkriitga vivvavvldt yrsrrsrar
//
LOCUS       WP_175844181            1059 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            contaminans].
ACCESSION   WP_175844181
VERSION     WP_175844181.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..1059
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=112606
     Region          14..789
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
     Region          <961..1054
                     /region_name="PRK13875"
                     /note="conjugal transfer protein TrbL; Provisional"
                     /db_xref="CDD:237537"
ORIGIN      
        1 mnmqnsiaal rggllqqdrl lkfdtplgpn vltvqravgr srigrayeft ldvlstdsdv
       61 elkkliaqpv tlwiqqgdlr yrpingyvht arrlgadggl ttyqlafadf thflkfrrdq
      121 rlwndttvdq iisdvlnqhp qaqghfrfal tkplpnrsyt rqhdtdwhfv hrlmenegly
      181 cawqqaddgk shtlvitdnl qafaplspet vrfyrgdaas epdaftqwsg trtlqsvtrt
      241 trtfdyknps qpsnpkgtsl ptmggqgelp dqlevyeytg aytyldqtrg dhltkvkmee
      301 wesrakrfha aggvramdag rrftladhpe hdrdpadqre faaievawwi ennlpvasds
      361 adfpyslrea ltqaqdnygt dpafrvqhdd gsagfylvev eaqrvsvpyr spfehhkpem
      421 hletaivvgp qgeevytdel nrirvqfvwd rlnpgnenas cwvrvvqsdt gggyggvhvp
      481 rigeevlidy vggdcdrpla vgrvynganq pqwhtdgils gyrskeysgg gynqlvmdda
      541 tgqnrvqlms ssansllhlg yiidqngnsr gsylgsgfdl rsdaygavra sqglyvtthp
      601 kaansqpldv keaqqqlvtg eslveamsdl seqhqaesmk daqdtmraft datqdsasgs
      661 asggrtaggg tgnanafkep vmlfgspsgi gmstqqslhm vandhvnvas gqsvhvaagk
      721 sligsigqkl slfvqnagmk lfagkgkvei qaqsdnievt aqkavkvvsa tdrieiaadq
      781 gilltsgggy iriqggniei hapgaidvkg ashtfagpas mgyplpsprp dqpgqlellh
      841 tygngqpvkg glfsvfdang gllkkgaldn nghmivsglp pgavqvkfge dprsqdqqss
      901 rfdvapwpak papaagaaet aqaqlgsflp aaagaagalt gvagaatqgg aalakaavgq
      961 gmgmaqqalg gmlpagasna lgaaktvagl assasqggaa lakavagqgl giaqqaatnm
     1021 lpagaqaals qagqlsaaaq qvsglaqtar saaavlkms
//
LOCUS       WP_175844184             324 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: phosphatase PAP2 family protein [Burkholderia].
ACCESSION   WP_175844184
VERSION     WP_175844184.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10627418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..324
                     /product="phosphatase PAP2 family protein"
                     /calculated_mol_wt=35191
     Region          113..286
                     /region_name="PAP2_3"
                     /note="PAP2 superfamily; pfam14378"
                     /db_xref="CDD:433919"
     Site            order(185,193,236..238,270,276,280)
                     /site_type="active"
                     /db_xref="CDD:238813"
ORIGIN      
        1 mrnrnaviya vswgtivvva ianfqwaklt gftigrgwpy sfindlcvvf gvslgligia
       61 tferyralth afrcrefava ifclmtfavw gqtasvtsyl giglnlpsia dpivrfdrai
      121 gfdwvsayhw vaahpalnvv fkyayysafa qlvalpvvla iarrpddive flvilfvssi
      181 vlllisipfp aesaflhygi sdpgtvatvs dytalrngtl rsinpyavqg lvsmpsfhtm
      241 laifftysvr rvrfvfpaai vlnavmiast itvgghylad mlagivcgfv vivvvrtwlr
      301 sgtrgeagrq mtpadagapi ssap
//
LOCUS       WP_175844253             236 aa            linear   BCT 11-JAN-2025
DEFINITION  PIG-L deacetylase family protein [Burkholderia contaminans].
ACCESSION   WP_175844253
VERSION     WP_175844253.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..236
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25971
     Region          7..>162
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mthaptrwlv isphlddgvf scgrllaaap gsivvtvfag ipprdtpapp wdrragfdra
       61 deamharrde drralahlda rpvwldfldd qygmpaaspe iaarvateid ahagfgvlap
      121 aglfhrdhlq vqqaalslld rarvshdaar rwrfyedvpy rriaglmaar vigwrergwi
      181 ahpdgapagd hapgiaakta avdtyasqva llephmradl repetywrle cdvtfa
//
LOCUS       WP_175844265             447 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CpaF family protein [Burkholderia].
ACCESSION   WP_175844265
VERSION     WP_175844265.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..447
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49161
     Region          44..412
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mahdiqfadg aapfsqtqqf hdiknaaheh lltrieelga efgrwsrqai nqfvdleids
       61 fvrlrripln esevravaea ltkelagfgp iedlladphv edilingynd iyvsrhgils
      121 klpirftdna hllrivrril apvgrrldes npmvdarlpd ggrvnvviep lsidgpvvsi
      181 rkfrkdplkp edllgngtyn eeigrlleaa vearcnvlvs ggtssgktsl lnalafhipm
      241 aervvtiedt aelslnhphv vrlesrpggf dgsgvvtird llrntlrmrp driivgevrg
      301 gevlemlqam ntghdgsmgt vhassprecl yrlemlagfa gfqgteaslr rqianaidfi
      361 vqigrlsngr rrilsitevt gmsdnivstq elyryearvt pegdeidhwe slgihphspk
      421 larfrntlvs sgggfggtfg rgggfnv
//
LOCUS       WP_175844281             561 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ShlB/FhaC/HecB family hemolysin secretion/activation
            protein [Burkholderia].
ACCESSION   WP_175844281
VERSION     WP_175844281.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..561
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=60352
     Region          35..560
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mksrldrwmm llviaaagta qaqtrvggnp ldslpqinap ksgpnvtvqv apqapqlqel
       61 lsrhltpktf qvegvksipf eeitrrftpl vgkditigel ietangvtkl yqergyalsf
      121 afvpaqtfen gvvritvveg yvsdvkvtgk pgameskira iaahitadrp lrratferyv
      181 ntfgllpglt vkanvpppqt tdgattlela vdrkpfnvst gidfnhpgvq glitatengl
      241 tsfgeqlsis alappgrdkq tyfafsgavp vgssglvtrl dastyrgkpt nnpglpstve
      301 rtvkneklgl sasypillnn qrsllgtvsg yaahnedryq sqtngntldn rsqvrvlqlq
      361 ldytsvepkq vrklsvnvak afdilgasks qtglvngvgv tyadptsltf vrtgatvtqt
      421 newpfrigts vsltgqyspd slptseqisf gstryalgyq pgeasgdsgw gmslevnrgf
      481 tpgwtylksi tpyvaydmar vylhsgtpsp nrmssvgigv rfsdsryysl dlnvakpigd
      541 apvesasrsp rinaafsyql n
//
LOCUS       WP_175844307             388 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Burkholderia
            contaminans].
ACCESSION   WP_175844307
VERSION     WP_175844307.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..388
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=41342
     Region          40..386
                     /region_name="AspB"
                     /note="Aspartate/methionine/tyrosine aminotransferase
                     [Amino acid transport and metabolism]; COG0436"
                     /db_xref="CDD:440205"
ORIGIN      
        1 mrhhrparlq hiagigvdrm gsiadhadvd llrlenldtd ipptaealaf treaierdsa
       61 nsylpfvgqd rlrasaaalv salsgqrfta dqvvvsaggl sgilntllat vetgdevivt
      121 dptyagllnr vrlaggvprq vpfaftpgge wkldqaalra aigpktrvml lmspsmpsgg
      181 vfdasdwqli aslcvrndll lildsamerl lfdgrtvihp aglpgmaert vtvgaaskel
      241 rmigwrvgwi vapgwlipdl vavslanvvv pvgiaqeaaa valehsasdl pgyvselekr
      301 rdtiaaelsg lpfgmpaggw smllrvsdfg ltgsqmserl lsrgvcatam tgwgvahgeq
      361 yvrfvfsnep verlrtlgnk vrraleda
//
LOCUS       WP_175844323             191 aa            linear   BCT 11-JAN-2025
DEFINITION  YbhB/YbcL family Raf kinase inhibitor-like protein [Burkholderia
            contaminans].
ACCESSION   WP_175844323
VERSION     WP_175844323.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..191
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=20438
     Region          29..186
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mrfdiflrss icatvlfaiv pavafadplt vtvddidhdg qfsnaqvyng fgcrgdnvsp
       61 rvswahvppg trsivvtmyd pdaptgglgw thwevvnipp setsirkgas gdarrmpvga
      121 letltdfges ryggpcppqg eshryvvtvs alsiarvdvk stsspavvay qmhgnilgqa
      181 ryvatyhrss n
//
LOCUS       WP_175844324             138 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175844324
VERSION     WP_175844324.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..138
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15547
     Region          19..108
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(20..22,36,53..55)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mtttvekvvl ppipakryft igevselcgv kphvlryweq eftqlrpvkr rgnrryyqhh
       61 evllirrire llyeqgftin garnrldspg gqraaaepve pevqaavdtr vpgkpgasvd
      121 vialrqalld vldglkhd
//
LOCUS       WP_175844218             372 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter periplasmic adaptor subunit [Burkholderia
            contaminans].
ACCESSION   WP_175844218
VERSION     WP_175844218.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Colclough,A.L., Alav,I., Whittle,E.E., Pugh,H.L., Darby,E.M.,
            Legood,S.W., McNeil,H.E. and Blair,J.M.
  TITLE     RND efflux pumps in Gram-negative bacteria; regulation, structure
            and role in antibiotic resistance
  JOURNAL   Future Microbiol 15, 143-157 (2020)
   PUBMED   32073314
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..372
                     /product="efflux RND transporter periplasmic adaptor
                     subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37961
     Region          41..363
                     /region_name="AcrA"
                     /note="Multidrug efflux pump subunit AcrA (membrane-fusion
                     protein) [Cell wall/membrane/envelope biogenesis, Defense
                     mechanisms]; COG0845"
                     /db_xref="CDD:440606"
ORIGIN      
        1 mvrrrlalla vasalplala acsgkapsdp rteaplvrta ivqaaapasr sftgtvaarv
       61 qsdlgfrvsg kvlarlvdtg qtvrrgqplm ridpvdlkla arardeavaa aqararqtae
      121 dearyrdlrg tgaisasayd qvkaaadaak aqlsaaeada gvarnatgya elvadgdgvv
      181 metlaepgqv vsagqpvvrl ahagsreavi qlpetlrpav gsvaqaelfg kpgsnvpatl
      241 rqlsdtadar trtfearyvl qgplaaaplg atvtiripdd araapqaglq vpigalldgg
      301 kgpgvwvvag epakvgwrpv tvehldddsa rvsgalkqgd rvvalgaqll hdgeavrvsa
      361 paatlasegg rp
//
LOCUS       WP_175844340             557 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Burkholderia arboris].
ACCESSION   WP_175844340
VERSION     WP_175844340.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60427
     Region          25..384
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          453..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mtpaslieqy gpresmeydv vivgggpagl saairlkqla aekgteigvc vlekgseiga
       61 hilsgavmdp rainelfpdw kergapldve vtedrflfls eksavttpnw alpanfqnhg
      121 nyvislgnvt rwlgaqaeal gveifpgfpa aeilynddgs vkgvatgnmg vgkdgepten
      181 fqlgmelhak ytlfaegcrg hlgrqliskf kldanaepqa ygigikelwe idpakhkpgl
      241 vihtagwplk sdtyggsfly hmdnnqvvvg fvvglgytnp ylspfeefqr ykthpsiraf
      301 leggkrvsyg araitaggll slpktvfpgg aligddagfl nasrikgsha aiktgmlaad
      361 aafdavqagr qsdelnaypd afkqswlhte lyrarnfkqw makglylgtl mvgleqkvmg
      421 gnvpwtlhhk hadhetlkpa sqcepieypk pdgkltfdrl ssvfisntnh eenqpahltl
      481 kdasvpvnvn lrtyagpegr fcpaavyefv knddgsdrlv inaqncvhck tcdikdptqn
      541 ivwvtpeggg gpnypnm
//
LOCUS       WP_175844354             313 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175844354
VERSION     WP_175844354.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34476
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdtlqnmrvf vrvvdagsft aaaqqmnstt ayasravsdl eahlrtrlln rttrrialte
       61 agerylqrce qilayvdqae aeagdaharp sgklkvhcft slgqhylvpa iaryrerypd
      121 vhveltlaqr mpdlldegyd vaivvgrdlp dsglvsqrlg esysvvcasp gyveahgvpq
      181 rpadlaqhvc lgmvapgfhf dewalagpng devvpitapp frvnvaeala vavregmgvg
      241 glplysaigw lrsghivrvm peyrshvmni yalypsrqyl dakirtwvdf lrdelpatlq
      301 adeaaleqyt rat
//
LOCUS       WP_175844371             398 aa            linear   BCT 11-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Burkholderia
            contaminans].
ACCESSION   WP_175844371
VERSION     WP_175844371.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..398
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41318
     Region          43..396
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mtqlfdtlgf idtsavragt aaathdaaaa saesagsasg aavslehvgk vfatahgqaa
       61 alrdltldvr rgevfgiigr sgagkstllr lvnglerpss grvrvqgvdv galdedglva
      121 lrrrtgmvfq hfnllsaktv fenvalplki agvpkaervr kveallelvg laakrdaypa
      181 slsggqkqrv giaralvhdp evllcdeats aldpettqsi lalladinrr lgltivlith
      241 emeviravcd tvavieqgev vetgpvwrvf gdprhgatra llstlvhdlp aelaarvqpl
      301 peqaalpdga qvvldvrytg esggepdvga laaalggsvr flhggieriq ghaqgrlvia
      361 aaphaddagq pasrggavaa llerarrhan haevlgyv
//
LOCUS       WP_175844393             390 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia arboris].
ACCESSION   WP_175844393
VERSION     WP_175844393.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..390
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43072
     Region          12..282
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 midgqillgh sirwgmvggg lgsqigyshr saalrdgsfq lvagafdidp ergrqfgvrl
       61 gvaaercypd yatmfdaear rpdgiravsi atpnnthfei craalnaglh vvcekplcft
      121 teeaetlqrl sieknrivgv aygysghqmi eqaremiarg dlgeirivqm qfahgfhseg
      181 veaasaaarw rvdpkfagps yvlgdigthp lyisevmvpe lrirrlmcsr qsfvksrapl
      241 ednaftimey etgavgyvws cavnagsmhs qkvrvigska siewwdehpn qlryevqgqp
      301 aqvldrgmgy lhpdalredr igaghpeglf eawsnlyarf alamdaadrg dtdalkqiry
      361 pdvhagvegv rwvencvrsa dagsvwvdyr
//
LOCUS       WP_175844477             305 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia arboris].
ACCESSION   WP_175844477
VERSION     WP_175844477.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..305
                     /product="VOC family protein"
                     /calculated_mol_wt=32379
     Region          <228..304
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 mktirsvlla amiagglava pvafaktpvt kavatpavav gpqydtthvc vapedfdrft
       61 dsfvatfggk kskqgvfqvt ptpsqtmsql vltpvgtisv fgfktpipyp fcaertgylv
      121 tdldvavksa rahgadvvvd tfpdpigrda ivrwpggvnm qlywhteaph ydaletvpen
      181 rvyvspesad tlvhdfvafs hgkvvsdvrn apgveigrpn dtyrriries gfgkmtvlat
      241 dghlpypfgr dmtgyevpdl aatlkkaeaa gvtvlvpaft sagrdaalvq fpggyvaeih
      301 sgaar
//
LOCUS       WP_175844529             201 aa            linear   BCT 11-JAN-2025
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Burkholderia
            arboris].
ACCESSION   WP_175844529
VERSION     WP_175844529.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Sciara,G., Clarke,O.B., Tomasek,D., Kloss,B., Tabuso,S.,
            Byfield,R., Cohn,R., Banerjee,S., Rajashankar,K.R., Slavkovic,V.,
            Graziano,J.H., Shapiro,L. and Mancia,F.
  TITLE     Structural basis for catalysis in a CDP-alcohol phosphotransferase
  JOURNAL   Nat Commun 5, 4068 (2014)
   PUBMED   24923293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Koga,Y.
  TITLE     From promiscuity to the lipid divide: on the evolution of distinct
            membranes in Archaea and Bacteria
  JOURNAL   J Mol Evol 78 (3-4), 234-242 (2014)
   PUBMED   24573438
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Koga,Y.
  TITLE     Early evolution of membrane lipids: how did the lipid divide occur?
  JOURNAL   J Mol Evol 72 (3), 274-282 (2011)
   PUBMED   21259003
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..201
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21074
     Region          28..196
                     /region_name="PgsA"
                     /note="Phosphatidylglycerophosphate synthase [Lipid
                     transport and metabolism]; COG0558"
                     /db_xref="CDD:440324"
ORIGIN      
        1 mslyalkpkf qntlrpfans laergvtanq vtlfaaggsi vvgalaglgv faralfllip
       61 lwlfarmaln aidgmlareh nqkstlgayl nelgdvvsdi alvlpflaip afapadvwlf
      121 altaviveca gligplvgvs rrydgpfgks dralalgafa lwiglgfsvg gvaawlwrll
      181 ivlsivtvvr rvqagiaekg g
//
LOCUS       WP_175844488             401 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Burkholderia cepacia complex].
ACCESSION   WP_175844488
VERSION     WP_175844488.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..401
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44961
     Region          118..378
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mkmselpavd rrvnladlsq faarlemktk dlreeilapr prksppvftt selaelcgle
       61 rnkmqyhynr ennplpagep qgngrsrlft laearrwvqe asniwqsplm tgrgthhaav
      121 lstanfkggs cktttamcia qglslrgrkv llvdldpqas lselcglyae kdvtwedtvl
      181 pyiyepdkvt laekvqstyw dgidlipann fmhdaeffip sqvvsnskye fwavlrkgle
      241 plrseydyiv ldsapslsyl tmngmiaada lvmplvpesl dfissvsfwt lfsavaetfs
      301 khevqksydf vsvllskvdn sttssshivr dwarqayeew lsvieipass vmsngalafs
      361 tvfdlsrgda vaktlarirq pltdycrwid dqyvanwraa q
//
LOCUS       WP_175844554             123 aa            linear   BCT 11-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Burkholderia
            contaminans].
ACCESSION   WP_175844554
VERSION     WP_175844554.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629346
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..123
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=13238
     Region          8..112
                     /region_name="DUF4440"
                     /note="Domain of unknown function (DUF4440); pfam14534"
                     /db_xref="CDD:434023"
ORIGIN      
        1 mdatrtaiep seialraaml andvealdal ldddlvftvp tgqiiskedd laahrakllr
       61 ldrldvqelh ayaigemilt ttkailaghf dgtafdgmfa ytrlwrrssa gwsvvaghas
      121 qva
//
LOCUS       WP_175844579             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175844579
VERSION     WP_175844579.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33942
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdkwtqieff vqvaelgsls kaaerlgmss aaasrclnal eerlgarlve rttrrlwltd
       61 agheyhrrcv ailtelsead aavneasvnp agtlrvtasv sfasiyiapa lpefhrrypn
      121 lnvqiiaanr ypdfieagid vairtrehea dsgitvrkla etrrvlaasp gylakhgapa
      181 tpdalcdhrl lvynlandpy vlhfrhgakt qsvtiksvld anegqviraa alaglgiliq
      241 plyiihddiv agklvpvltd wqlpaltvni ayqsrrhqpa kirvftefli erferlglar
      301 kwkevgr
//
LOCUS       WP_175844596             153 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: (2Fe-2S)-binding protein [Burkholderia].
ACCESSION   WP_175844596
VERSION     WP_175844596.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..153
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=16158
     Region          1..152
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mitltingse qhfdgnpdmp llwylrdvlg htgtkfgcgm alcgactvhl dgvairscit
       61 pvaaasgkrv ttieglstdl thplqqawqe lnvaqcgycq sgqimqaasl lktnphptda
      121 diddamsgni crcgtytrir aairlavrrg gaa
//
LOCUS       WP_175844731             292 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Burkholderia].
ACCESSION   WP_175844731
VERSION     WP_175844731.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 292)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..292
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32434
     Region          46..>93
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <89..289
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msaidsddie qqalqangka arrndarvwr stlipggemv tarftdhvya phwhdaytis
       61 viergaeryd yrgtrfvada gslpiinpge ihtgssaada gwqcrtfylp vdfvqgvaee
      121 agssrhdtpw fdpdiikdad lvgralrahr vletgtdmla veyalldavs tllkrygrmr
      181 ppsrpmsidr mrvermkarm ldeltasldl aeladvvgls kfhaarifsr evgmaphawr
      241 nqvrlaracd alragmpate vaaafgfadq shfnrhfkka ngvapsrwrd tr
//
LOCUS       WP_175844739             167 aa            linear   BCT 11-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Burkholderia arboris].
ACCESSION   WP_175844739
VERSION     WP_175844739.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12806325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..167
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=17558
     Region          22..165
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
     Region          63..126
                     /region_name="Pentapeptide_4"
                     /note="Pentapeptide repeats (9 copies); pfam13599"
                     /db_xref="CDD:433339"
ORIGIN      
        1 mssaeilykh dqwrkgaggm paglsgqads sayadldlgl aqfagssfsg ssfagtsfrq
       61 agwtgcrfsa ctfsgcdfae iaisgctfvd csfndaafqg stfngvkflg cqwngvrfdg
      121 ntwrsvqvld ctgttveahg lkgldvdftg syfehlafed teinggh
//
LOCUS       WP_175844752             466 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cytochrome ubiquinol oxidase subunit I
            [Burkholderia].
ACCESSION   WP_175844752
VERSION     WP_175844752.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..466
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51739
     Region          4..440
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 meifdafhla rlqfaftvsf hivfpaisig masflavlew rylvtgdaay ksmfqfwski
       61 faigfgmgvv sgvvmayefg tnwagfsrva gnitgpllty evltafflea gflgvmlfgw
      121 qrvsprahff atlmvavgtl istfwilasn sfmqtpqgyk ienglvvpvd wfkivfnpsf
      181 pfrlahmtia afivagfiva acgawhllkg rrdepvkrsf smalwmllvl apiqivvgda
      241 hglntreyqp akiaaieglw etekggtaln lfglpdmqae ttryaiqvph lgslilthsw
      301 dgeirglkef ppqdrpyspi ifwtfrimag lgmlmlltal lglllrkggr lyetrwfqwf
      361 vvamgpsgiv allagwitte vgrqpwtvyg vlrtidsvap lsaqqvgvsl lifvvvyflv
      421 fgtgiyymmk lmrrgpaaqa gyielhrhpg lrksalstpl nvteae
//
LOCUS       WP_175844756             189 aa            linear   BCT 11-JAN-2025
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Burkholderia
            arboris].
ACCESSION   WP_175844756
VERSION     WP_175844756.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..189
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=20578
     Region          43..182
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 mttftesrag lpddplrags pppidatdph tepapsiaag fevrvqyapi dagaelapiv
       61 rnpnvgavvn flgvvrkegd vddvvaleve hyptmteqal wsiveeasar wrlesvkivh
      121 rvgriplgqa vvlvvvaaah rasafdacef lmdflkthap fwkkeirhdg esgwveakah
      181 ddqamrrwg
//
LOCUS       WP_175844777             261 aa            linear   BCT 11-JAN-2025
DEFINITION  peptidylprolyl isomerase [Burkholderia arboris].
ACCESSION   WP_175844777
VERSION     WP_175844777.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..261
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=28088
     Region          100..247
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mndvlsdapv alringvaig ddaiaaeaah hgdapdplda arrslavrel lrqravslal
       61 ldegapldda avdallerel thlpepdrad ceryyaqhpa rfrrndivya shvlfamtdr
      121 vplaplrqra eqaladvvaa petfeavara ssncpsaevg gslgqllrgd tvpefevalf
      181 dtdgigvlpk lvntrfgfhi vrierrvegd avpfdeaagq iaaylservr qramrqyvai
      241 lagearvegv efdgangplv q
//
LOCUS       WP_175844783             159 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Burkholderia].
ACCESSION   WP_175844783
VERSION     WP_175844783.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..159
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16910
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mykkimvaid gsasskqala eavkvalasd thvsvvyvvd ksvlftyagr fdphalveei
       61 rddgrkvlre aeqiialaga kgeaelvete sigediaerl qryvkehgvd lavvgthgrr
      121 girrvllgsv aerfvrgskc pvllirgdda deaaaaaaa
//
LOCUS       WP_175844813             167 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Burkholderia].
ACCESSION   WP_175844813
VERSION     WP_175844813.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..167
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17830
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mysnilvald gsdtssrald aalnlaaetg arltpvyvvd flvpaydmyg ydpsilvdaf
       61 reeglrvted aarrlkardv agtpqisnve pagediphri vrladetead livmgthgrr
      121 gvqrlflgsv aervlrlatc pvlmipahcp aaqpaettaa stekeps
//
LOCUS       WP_175844829             157 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Burkholderia].
ACCESSION   WP_175844829
VERSION     WP_175844829.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..157
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16703
     Region          1..144
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mytnimvavd gspssnqale ealkiarscg arlfavfvvd ksllityagr mdpdalldev
       61 rrdgaavlrs aeraishaav ngeteivete lgqdiaerlq ryvvdrsidl avvgthgrrg
      121 vrrlflgsva erflrgsscp vllvrgndaa haavaaa
//
LOCUS       WP_175844846             197 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175844846
VERSION     WP_175844846.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..197
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21490
     Region          4..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 magrprefdr dtalkqamlv fwrrgyegts msdlvevmgi asariyaafg skealfqeav
       61 alyeqsdgsf adralgetdv raaietmlle aiatytrrgr phgcmvvssa tnysasnegv
      121 mawltehrra rtqsilerlr ealaqgqlkp gtdvdaladf yavqlhgisv qsrdgvskdr
      181 llasvgpamm pldlalr
//
LOCUS       WP_175844839             211 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Burkholderia].
ACCESSION   WP_175844839
VERSION     WP_175844839.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..211
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21850
     Region          7..190
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mslhypllfa ylaaivllia tpgpvvmlvt gtvarrgfrq gvltavgana aslvmiagam
       61 lmvfgvvmvs drllaglhva gcvfiavlai rtllgewrag rgaatgepvp qprglpgivr
      121 gflvgianpk dllffvaffp qfvgitpdsr vslailaalw iavdftiltg ymaainhpsi
      181 hrkqrwisas salallvial aglgstiaga v
//
LOCUS       WP_175844866             169 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: aromatic-ring-hydroxylating dioxygenase subunit beta
            [Burkholderia].
ACCESSION   WP_175844866
VERSION     WP_175844866.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10791045
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..169
                     /product="aromatic-ring-hydroxylating dioxygenase subunit
                     beta"
                     /EC_number="1.14.-.-"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0009056 - catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=18829
     Region          15..169
                     /region_name="HcaF"
                     /note="3-phenylpropionate/cinnamic acid dioxygenase, small
                     subunit [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG5517"
                     /db_xref="CDD:444268"
ORIGIN      
        1 mlkgfdkkpv ahgdaiaarm aveafhaeyc aalddgeler wpeffaeqcv yrvteyenae
       61 rglpvglvya egrdmlrdra vaisrtqmfa prrvlhlvtn vrildangee ivaqsnyill
      121 qtlvegattv hqagrlydrf arngsslllk erqavydtal iandlaypv
//
LOCUS       WP_175844890             151 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: carboxymuconolactone decarboxylase family protein
            [Burkholderia].
ACCESSION   WP_175844890
VERSION     WP_175844890.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..151
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16963
     Region          13..141
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mperisfgql parlldvvln veeyanhtgh dfklvelvra rvsqlngcay cldrhikegi
       61 hagedplryn llpvwhetpd lyspkeqaal rwaealtlis ehaiddalva atrehfdrde
      121 latltlivaq intwnrlakp fawqagvfqa g
//
LOCUS       WP_175844911             467 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Burkholderia].
ACCESSION   WP_175844911
VERSION     WP_175844911.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 467)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 467)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..467
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51571
     Region          192..465
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mtvnvaaqes tgtaqlvtrv yarlllvgfa ltpayliayl yffqdpslkf enhtfhelai
       61 aaatlegafv tyvcwrcysl sgepllrwlt lgflgfslvy alhgmftgma hhniwlflly
      121 gpasrltmsi lvfvgqltyg hkadsaairg rrrtwltwia lfgfvdiava avayspvagn
      181 lwvrlsmegg allffsvsvi alavrrirsp lmtiyaisvt sfalsslafi larpwnhmww
      241 lahaifaagf fllsfgvvqa fhttrsfski ysqaelfarl reamartera lqalqrtnek
      301 lehlaatdpl tgatnrrqfi esveaeisra krngapfsll aldldhfkai ndsyghqagd
      361 qvlqrfvnkc adairpydgv arvggeefmv llpqaeldta qsigerirta iagepfeagi
      421 gepitvtvsv gasefgrdge tidailrkad erlyrakhqg rnqvvag
//
LOCUS       WP_175844944             308 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia].
ACCESSION   WP_175844944
VERSION     WP_175844944.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 308)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 308)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 308)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..308
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32236
     Region          57..305
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 maslssprda gpagagtaga spdtapalag vppwlllapi laflavlaaa tltvfrmsvg
       61 vsgdewrtft lqnyadladp yfttslwltl rlafqsmvca vllaipvala martesrlar
      121 rlllagvllp llvnlllqgy gwlvmlgpag llnrallatg migrplqlly rehgvllgli
      181 qtafplavlp lssalravsr aydeaaatlg asrwqtlrhv tlplampglv sgallvfayn
      241 asafavplll ggrrvpmlav lvhdevapll nwpaasasgv vlmgatlvvm avsqrlvrtl
      301 qragevnr
//
LOCUS       WP_175844956             294 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia arboris].
ACCESSION   WP_175844956
VERSION     WP_175844956.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 294)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 294)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 294)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..294
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31583
     Region          15..259
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mpnvlstvah ppakaarrrp dwrnirllip amlllaiffl lpvlslllrs vlepapglqn
       61 yvqllgstty lrvfgntflv atvvtvvtva igfptawlla iaprklssvl fsilllsmwt
      121 nllartfawm vllqatgpin rvlmalgivs eplalvnnlv gvtigmtyim lpflvmplha
      181 tlrsidpstl raaavcgasr wqafwrilvp lampgiasga lmvfvmalgy fvtpallgga
      241 qymmlaelia qlvqqllnwg lagaaalvll avtlslyalq lrftgaartg mggr
//
LOCUS       WP_175844958             228 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175844958
VERSION     WP_175844958.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..228
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25071
     Region          5..223
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mqdlkidrna ktlreltldk lrgaivqgyf rpgarlvert lcdelgvsrt vvrevlrhle
       61 teglvetvsr qgpvvarldp aqvgeiyelr glleanaara caegatpdvv relreiravi
      121 eeafekqelp rvleyterfy etlfeaagkq vsltvvktln arinrlralt iampgrggds
      181 naemnrllda ierrdgdaas aasaahikrv selalaalaq qneavtdn
//
LOCUS       WP_175844946             354 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia arboris].
ACCESSION   WP_175844946
VERSION     WP_175844946.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 354)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..354
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38270
     Region          1..351
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtqlilqnvt krfhqayavd hvdlsvpdgk lvcflgpsgc gkttlmriia gletptagtl
       61 tfagrdltnv panrrdfgmv fqslalfphm tvaqniaypl rlrktakaaq arrvaellel
      121 iqlphmadrl vtqlsggqrq rvaiaraias sprlllldep lsaldaklre amqveirllq
      181 qrlgittimv thdqreamtm adeivvmekg riqqvgrpld iyrdpvnefv adfiglgnil
      241 pvacdgddai vlpggqrlal qraprtadav rllirpedvc lrtastqpag pntlagtitf
      301 vrdvgasiea tidcrgftlt aattpretpd lqvgmpvlae lpahacklia arga
//
LOCUS       WP_175844997             268 aa            linear   BCT 11-JAN-2025
DEFINITION  endo alpha-1,4 polygalactosaminidase [Burkholderia arboris].
ACCESSION   WP_175844997
VERSION     WP_175844997.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008090
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..268
                     /product="endo alpha-1,4 polygalactosaminidase"
                     /EC_number="3.2.1.109"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=29466
     Region          18..268
                     /region_name="COG3868"
                     /note="Predicted glycosyl hydrolase, GH114 family
                     [Carbohydrate transport and metabolism]"
                     /db_xref="CDD:443077"
ORIGIN      
        1 msgsafaaas arasqaatwk plvpgtswqw qidgnrinek vldgvnnprk mfdvdmeqtd
       61 agtiqrlkak giyvvcymev ggrednrgda arfpdsvlgn pvegyedher wldirqtail
      121 mplmlarldq akkkgcdgie pdlddsyrqe tgfpltrddq lrynaaliaa ahdrgmsmgl
      181 kngsgiatam akvadwalne qcnrfhecgd yasfiaqnka vfnveytrpd gmkladfcpa
      241 dnqanfdgil klssdtlsal praacrfe
//
LOCUS       WP_175845051             123 aa            linear   BCT 11-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Burkholderia arboris].
ACCESSION   WP_175845051
VERSION     WP_175845051.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629346
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..123
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=13341
     Region          12..114
                     /region_name="DUF4440"
                     /note="Domain of unknown function (DUF4440); pfam14534"
                     /db_xref="CDD:434023"
ORIGIN      
        1 mdairtvvep fetalraaml andvemldal lddalvftvp tgqviskedd laahrakllr
       61 lekldvhdmr acaigemilt ttratlaghf dgaafdgtfa ytrlwrragt gwrvvaghas
      121 qvm
//
LOCUS       WP_175845063             290 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: pirin family protein [Burkholderia].
ACCESSION   WP_175845063
VERSION     WP_175845063.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..290
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31540
     Region          15..280
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mttarsldrt ypalrttegg gfvvhrpfpt rllmdfdpfl lldemgpvdy apgeavgapd
       61 hphrgfetvt yaldgrfrhr dssghagtlg pgdvqwmtag agvvhsempd pafaqaggrs
      121 hgfqlwvnlp rrdkmiapry qeipadript aespdgrarv rviageafgv raaietrtpi
      181 lyqhftlepg atvtqpvpag yrvfaypidg tglygpdrqa vdarhmivyg ddgdtvtfaa
      241 gdtpldllli ggvplnepiv rygpfvmnte eeirqavvdy qtgrmgriea
//
LOCUS       WP_175845033             955 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia arboris].
ACCESSION   WP_175845033
VERSION     WP_175845033.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 955)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 955)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..955
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..955
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=103875
     Region          8..822
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mlrafvgald qnnrairfhw grhqdalahv lvpqnidlme glcvgieghl tclssrpdlp
       61 lssflglpls vqlmtdrgtp ypingiitdv ragqsdgslt cvqltlrdal sildqrvnsr
      121 afrsmsipdi letllhewqq rspalaqafd felvldrnry pkreqtrqag esdaafirrl
      181 crrdgifwya ragkhdgaaa dmpvhtlvfc ddptklpqaa agqvpyhrgt qsrerdsvtl
      241 wstaraltpg svrraswdyk tgrmaqseqe tivdqgeagn dlaklladsv idvphaadsd
      301 adqerlakar ilahehraec vhassdvrnv spgfwftlla hpevdtrpee qrqfvvtslh
      361 hratnnfskt lderaqalfa asrwsfdalp veegagvrye ntficvrrgv pltpaydprv
      421 dlppvhpfta kvvgqdgeev hcdelgrikv qilglhaddh ahaqgagtsg terdsawvrw
      481 vspwagpnyg mdmlpragme vlidhlhgdp dkmvvtgvlh ggpnmpttfs htgslpgnry
      541 lsgiktkevk adrynqlrfd dtpgqissql asehtytqln lgylteprdd gkgaprgdgl
      601 eartdaqavi raakgvyvta qqqgraegkm lertalqtli eqlqdlvrnl gdasaandad
      661 ntdlarieki tsqikgwdag snvdqggsag gapmvaiegp agvtvvsqda mvlgaqtnid
      721 avsagntqis agrrllmrvg dwmsafaakg mtlvtadgkl rieahkedvv vkaakriile
      781 ageeivfrsp kvntqasdea singgssysq wngggvvhgt sgvwrehaas hslvgpdnkp
      841 vkapdpltfk eleqqdslav vlrshpndgr playepytly kgaakiadgv tdehgqliia
      901 nhqkgtssyt vklhngheie vpvmeggltd ddqlaaqgwr avdgdpesrq rhaqg
//
LOCUS       WP_175845121             324 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sterol desaturase family protein [Burkholderia].
ACCESSION   WP_175845121
VERSION     WP_175845121.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..324
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37639
     Region          134..275
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mlhlldtfvs niqtwlyvdi vqpllfkfnl mdydedtyda lywvvigalq mvlmfallrp
       61 leallpverw knrravrvdv iytaisklgi ytlffffalq pvfdnfqawl rlhgvanmnl
      121 dylwpgvtsq pivafaiylv vldfagywyh rwqhkfgiww elhavhhsqr qmslwcddrn
      181 hllddvlqsc ffaaialvig vtpsqfvvlt aftnfmqsiq htnarlsfgw lgervlvspi
      241 fhrrhhavgy ghegtkygcn fgvlfpwwdm mfgtaswnrt veptgireqv egvsygdgfw
      301 sqhglafvri frrlfpakrg aasa
//
LOCUS       WP_175845190             262 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TatD family hydrolase [Burkholderia].
ACCESSION   WP_175845190
VERSION     WP_175845190.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..262
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28809
     Region          2..242
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mwidthchld aaefdadrda vaqaahtagv srivipsigr dnfttvrela qrtpgavyal
       61 gihpmytpqa rdedldrlrm eieaslddpr fvaigeigld yfvpgldedr qqffyqgqlk
      121 larefdlpvl chvrksqdrv laglrrfgvr rgiahafngs fqqaeaylaq glhlgfggnv
      181 tftralqirr latelpldal vvetdapdia pewayksrnt pdqvprigav laelrgldtd
      241 emslctsana laalprlals sa
//
LOCUS       WP_175845215             191 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: peptidylprolyl isomerase [Burkholderia].
ACCESSION   WP_175845215
VERSION     WP_175845215.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..191
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=20149
     Region          24..191
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mkrlllalgg aallatapaf aqsatahpvv qlktsqgdir velypekapk svanfldyvk
       61 agqyngtifh rvikgfmiqg ggyktnfeek ptrapiples rnglknltgt lamartsdpn
      121 sataqffint vdnsgldypn pdgngyavfg kvvsgldvvk kiegvattsr gpmqdvpaqp
      181 iviesasivs k
//
LOCUS       WP_175845290             158 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia arboris].
ACCESSION   WP_175845290
VERSION     WP_175845290.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 158)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..158
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=16740
     Region          13..142
                     /region_name="NUDIX_ADPRase"
                     /note="ADP-ribose pyrophosphatase; cd04673"
                     /db_xref="CDD:467557"
ORIGIN      
        1 msttgtaapv rpvpavigiv lrehdvllvr ranppdagcw gfpggkiepg epiadavvre
       61 iaeettidve aldaftalda fdydaggalr qhfimvavlc rwlrgtpaag ddaldarwfg
      121 ideldrddvp msagvrdvaq raieraavln naqrpsav
//
LOCUS       WP_175845295             256 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175845295
VERSION     WP_175845295.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..256
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28510
     Region          10..245
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mtppnvvpls aaplyvqikd tlrarildgt yaphsrmpse helcamfdvs ritvrqalgd
       61 lqkegllfkl hgkgtfvskp kafqnvtslq gfaeamssmg yeivnqlrsl rtvkadrhla
      121 tklnvpegap lieihrvrll nrepvsleqt wvpealgkrl agadlatrdi flilendcgi
      181 plghadvsid ailaddeivd alhveesspv lrierlthda sgapidyeyl yfrgdafqyr
      241 lrvdrqkark parnpr
//
LOCUS       WP_175845310             297 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia arboris].
ACCESSION   WP_175845310
VERSION     WP_175845310.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..297
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=29967
     Region          1..287
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mevgfcgpgl mgapmirhll aaghrvsvwn rsrdkaealv kdgaqvigtp relaervetv
       61 fvcvldgrav gdvvfgehgl lsgdaaarrl kriidhssip paatrdyaar aaalgvgwvd
      121 apvsggvpga qagtlavmag ggaadldavr plidtyasri thmgdagagq taklcnqaiv
      181 tatvtaiaea vglaqasgid aarlaealag gwadsvllqt fvprmtsggh ppigalstfq
      241 kdvdaiadaa rdtgavmpvs atvqqvlrlg aaqglagadf aafidivrpg ngrqqas
//
LOCUS       WP_175845319             182 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: peroxiredoxin [Burkholderia].
ACCESSION   WP_175845319
VERSION     WP_175845319.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122432
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..182
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0008379 - thioredoxin peroxidase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20211
     Region          4..174
                     /region_name="PRX_Typ2cys"
                     /note="Peroxiredoxin (PRX) family, Typical 2-Cys PRX
                     subfamily; PRXs are thiol-specific antioxidant (TSA)
                     proteins, which confer a protective role in cells through
                     its peroxidase activity by reducing hydrogen peroxide,
                     peroxynitrite, and organic hydroperoxides; cd03015"
                     /db_xref="CDD:239313"
     Site            order(4,55..56,59,119,129,142..144,146..148,152..153,160,
                     171..174)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239313"
     Site            order(53,87..88,110,112,124)
                     /site_type="other"
                     /note="decamer (pentamer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:239313"
     Site            order(54,57,130)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239313"
     Site            order(57,171)
                     /site_type="active"
                     /note="peroxidatic and resolving cysteines [active]"
                     /db_xref="CDD:239313"
ORIGIN      
        1 mktvgdklea ftvvaakpgf nhheengqsa fetvteasfp gkwkiiyfyp kdftfvcpte
       61 ivefakltkq feerdaillg gssdnefvkl awrrehkdld klnhyafgdv kgelidqlgv
      121 rdkeagvalr atfiidpdnt iqhvsvnnln vgrspeevlr ildglqtdel cpcnravgga
      181 tl
//
LOCUS       WP_175845369             220 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Burkholderia].
ACCESSION   WP_175845369
VERSION     WP_175845369.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122607
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..220
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24623
     Region          8..79
                     /region_name="GST_N_1"
                     /note="GST_N family, unknown subfamily 1; composed of
                     uncharacterized proteins, predominantly from bacteria,
                     with similarity to GSTs. GSTs are cytosolic dimeric
                     proteins involved in cellular detoxification by catalyzing
                     the conjugation of glutathione (GSH) with...; cd03043"
                     /db_xref="CDD:239341"
     Site            order(19,21..22,24..25,28..29,72,75..76)
                     /site_type="other"
                     /note="putative C-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(19,57..59,70..71)
                     /site_type="other"
                     /note="putative GSH binding site (G-site) [chemical
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(57,69..70,72..73,76)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239341"
     Region          92..205
                     /region_name="GST_C_3"
                     /note="C-terminal, alpha helical domain of an unknown
                     subfamily 3 of Glutathione S-transferases; cd03194"
                     /db_xref="CDD:198303"
     Site            order(95,102,163,166..167,170,174)
                     /site_type="other"
                     /note="putative N-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:198303"
     Site            order(95..96,99..100,103,139)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:198303"
     Site            order(102,106..107,110..111,171,174)
                     /site_type="other"
                     /note="putative substrate binding pocket (H-site)
                     [chemical binding]"
                     /db_xref="CDD:198303"
ORIGIN      
        1 mestgqttlt issrnyssws mrgwllakls glafetvsvp idaasraell llspsilvpc
       61 lthdgstvwd tlaiaeylne irpqarllpd drrarahcrs icgemhsgfs alrsalpmnl
      121 rahfpgfriw sraqhdiqri vtiwreclaa yggpwlfgae igiadamyap vvtrfltydv
      181 klepdiaeyc mrvlahpfva ewieaakaeh edideldmef
//
LOCUS       WP_175845398             356 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia arboris].
ACCESSION   WP_175845398
VERSION     WP_175845398.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..356
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38451
     Region          26..265
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mttplptrlp pllrnalrpl ldpyrryrha klihaarval ailvsialst glhvphgews
       61 titvlivvgg lqhhgnirkk aaeralgtsi galaglglil lysvvhapva iyllmsvacg
      121 fcayhaigka gyiallsait mvivaghgdn eivdglwrav nvlagiaial afsfalplya
      181 tyswryklad alracaavha rlagdrhvsd dahlkemaal sallvqlrsl mpsvskecet
      241 smtqleaiqr slrlcigyle ilssavpard dvaareymrv emkavnrrir dtlvgasral
      301 kfgtpsrlap rrrpvdpphd appsqlsgyv sitaklagev dqlreklldt aqswni
//
LOCUS       WP_175845411             175 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: flavin reductase family protein [Burkholderia].
ACCESSION   WP_175845411
VERSION     WP_175845411.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..175
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=18489
     Region          22..164
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 msenhagtga gadeqrrfrt alsmfatgva vitaprkegv pvgitvasfn svsldpplil
       61 fsvdrrslsl gdlagadgya vnvldetqqh lsncfakang dkwgwragtv dddgavllpd
      121 alatfecapy aqydggdhvi fvgrvtrhra rsegrpliff ggryraldga hapsv
//
LOCUS       WP_175845428             437 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TolC family protein [Burkholderia].
ACCESSION   WP_175845428
VERSION     WP_175845428.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..437
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45277
     Region          53..433
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mlklslavav afamaataya qpslspgpap saagsatpig appsgalspp sltlpdalav
       61 aarnnpalrg aradvdasag almqagarpn pevsflqegf sraertstal inqtielggk
      121 rrarldvasy gresasasld eqgavvradv iaafygllaa qrqlqvtees saiaarsael
      181 agrraqagkv spveatkaqv aaagvqievv targrvevar eklnavmgea rgdrlavlgd
      241 leavppvepl saltaqldds plarvaraem lrsnaavsle rarripdvtv sagvkrvttg
      301 gvpdnqavvg vsipiplfnt nkgalleath kaeranadld rertrlrlel tqayanfeaa
      361 eqeaqrlksd ilpaarlald amsrgyelgk fsfldvldaq rtlfqgqsqy vralagahaa
      421 radigrlvgt plaavaq
//
LOCUS       WP_175845433             214 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Burkholderia].
ACCESSION   WP_175845433
VERSION     WP_175845433.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..214
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22234
     Region          11..213
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 msaarkpasp irvysfllsg hahrvrlfls llglpsetid vdlaagaqre paflalnpfg
       61 qvpviddggt viadsnailv ylakrygdah wlpgdpvgaa avqrwlsyaa gpiasgpaaa
      121 rlvtvfgapl dpeaakrtaa kvldvidrel adkpfaagaq ptiadiaayt yiahapeggv
      181 slepyphvra wlarvealpg fvampttrag llaa
//
LOCUS       WP_175845434             314 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175845434
VERSION     WP_175845434.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..314
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32922
     Region          9..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..294
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,229,246,273)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,193,
                     223..227,234..235,238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 madlrdvnln rlaifvavvd agsltaaaer lglaktvvst hmqrlesevg anllvrttrr
       61 lsvtdagrvf ydacrdivra tetaldavss dagplrgtlr vsvpidygal vvapavvalr
      121 drhpalavel vandrvvdlv adnldvairi grladsnyra vqlgtyekwl vaspafiarh
      181 glprdpdala alpfvmlstl prphtlelgn vdgahaavrc vapvvsntat acraivlagg
      241 gfglltdfsa addvaagrlv rllpgwrtap agihavypst rlpspkvraf idamkgrige
      301 tppgapvcak rttg
//
LOCUS       WP_175845442             190 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Burkholderia arboris].
ACCESSION   WP_175845442
VERSION     WP_175845442.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..190
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19845
     Region          15..169
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mttdprpdvd rridivalcg slraqsynaa lldaaalvap rgmhvtrfdr lgefplfnpd
       61 aeypspaavr dlidrlnaad giliaspeya hgvtgvmkna ldwvvgceav vtkpvavlna
      121 sprathadaa lretlsvmsa rivepasitl pvlgsqldaa giaahppfrs aladalhalr
      181 aaiddtapgr
//
LOCUS       WP_175845471             326 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia arboris].
ACCESSION   WP_175845471
VERSION     WP_175845471.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 326)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..326
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34911
     Region          38..319
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mgqptrplpt dgapaalahs aaasvdavpt rtaaprprat wrahaplwlm capafalfaa
       61 lvlvplamtf vltfyrfdpa tgpiaafqfg nyaevlgssy fhtiflrtfg iavlttaicv
      121 avgtpeayvl skmrdpwrsl fllailapll vsivvrafgw smllntsglv nrtlglvglg
      181 pykleyttfa ivialvhvml pfmvipvwta lqrldpqteh aalslgaspf ttlrrivlpq
      241 lmpgvlsgsl mvfglsasaf aipgllggrr lkvaatavyd eflgslnwpl gatiavlllv
      301 anlvvmltyy rvlerryars lggasr
//
LOCUS       WP_175845487             322 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175845487
VERSION     WP_175845487.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 322)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 322)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12168323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..322
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34765
     Region          22..198
                     /region_name="AraC_binding_2"
                     /note="AraC-binding-like domain; pfam14525"
                     /db_xref="CDD:434015"
     Region          245..320
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdialsrhap nrlgtlqapd everavahrl gphrmaaygr dpfhaelyev plhhgallel
       61 cygretridf gddadhflfr ltragacelq agsvvaragp geltvsspal asrlrtspdc
      121 rnlvlrlerd aleyklqdml katltrplqf dlasggtgaa lvlptfeylc rlgaqpgigt
      181 aspvfgadlt awlmslllth lphsysdalv rgtpplpahv rracdhidah lgeplalaal
      241 aaiagvaprt lqhafraflh ttpaayvrer rlaavhaalq rgdarsvtdv liahgihgfg
      301 hfakayarry ghapsvtarq tr
//
LOCUS       WP_175845518             338 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [Burkholderia].
ACCESSION   WP_175845518
VERSION     WP_175845518.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 338)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..338
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36279
     Region          9..321
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mttsprrral iaaglgvlaa pslvrakprt vriskgygvl ylpllvmekq rlferhaarh
       61 gvrdvavdwv lldggnsvnd ammagtldfa gagapgfiel warargipnv evigisglst
      121 tslslnanrp glvslrdftp sdriavpgir tslsavvlqm vasrqlgpkh faqldsitvn
      181 lphpqamqal irrengvtah ftsppfstle lrqpgihrvv ssvdvlgplt ldvvfapkrl
      241 vdtepalava flgaldeanr liaqdpraaa alyaassgvg vshddvmrml aapdtrfsvl
      301 pnqlmdyvef lylagtikak prawhemfap mlddyrsg
//
LOCUS       WP_175845548             185 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: carboxymuconolactone decarboxylase family protein
            [Burkholderia].
ACCESSION   WP_175845548
VERSION     WP_175845548.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..185
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19352
     Region          40..178
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msayplhtid sapaeskpvl qqlqqtfgiv pniaaamaas pvlingfigl fervhasslt
       61 epqiqtlllt navtnasewp vafhtalalk qgvvpadvda irrgdlpada klaalsaiar
      121 tlidtrgria dadrqsflda gfsteqllev iavvaastit nyvgsvaqpa leapfdafaw
      181 haraa
//
LOCUS       WP_175845534             613 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp70 family protein [Burkholderia arboris].
ACCESSION   WP_175845534
VERSION     WP_175845534.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Fernandez-Fernandez,M.R. and Valpuesta,J.M.
  TITLE     Hsp70 chaperone: a master player in protein homeostasis
  JOURNAL   F1000Res 7 (2018)
   PUBMED   30338057
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 613)
  AUTHORS   Mayer,M.P. and Bukau,B.
  TITLE     Hsp70 chaperones: cellular functions and molecular mechanism
  JOURNAL   Cell Mol Life Sci 62 (6), 670-684 (2005)
   PUBMED   15770419
REFERENCE   3  (residues 1 to 613)
  AUTHORS   Bukau,B. and Horwich,A.L.
  TITLE     The Hsp70 and Hsp60 chaperone machines
  JOURNAL   Cell 92 (3), 351-366 (1998)
   PUBMED   9476895
REFERENCE   4  (residues 1 to 613)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   5  (residues 1 to 613)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   6  (residues 1 to 613)
  AUTHORS   Rensing,S.A. and Maier,U.G.
  TITLE     Phylogenetic analysis of the stress-70 protein family
  JOURNAL   J Mol Evol 39 (1), 80-86 (1994)
   PUBMED   7545947
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..613
                     /product="Hsp70 family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0051082 - unfolded protein binding
                     [Evidence IEA]"
                     /GO_function="GO:0140662 - ATP-dependent protein folding
                     chaperone [Evidence IEA]"
                     /calculated_mol_wt=65603
     Region          7..608
                     /region_name="DnaK"
                     /note="Molecular chaperone DnaK (HSP70) [Posttranslational
                     modification, protein turnover, chaperones]; COG0443"
                     /db_xref="CDD:440212"
ORIGIN      
        1 msdprysigi dlgtthcals yvdssasdge kitqqvlpia qltapgales rdllpsflyl
       61 pheseltqgd ltlpwtasra favgemartr gagtpirlvs sakswlchpg vdrraailps
      121 dappevsrvs plessirylt hlreawdhah pdapfadqdv tvtipasfdp aareltaeaa
      181 raagysrmtl leepqaalys wiqksqggwr kqvqvgdlil cvdvgggttd lsliavverd
      241 gnlelhrvav gehillggdn mdlalahvva rklaqqgtqa dpwqlralty acraaketll
      301 tdptadavpl vvpsrgskli ggsirteltr aeltqtileg ffpqveaaar pvsrarvglt
      361 qlglpyaqda gitrhlaafl grqvaaldal egvqrtlpqg atflhptavl fnggvfksal
      421 ltqrvldtln swlaaegapp arllegadld lavargaayy gfvkrgrgvr irggtarayy
      481 vaiesampav pgleppvqal cvapfgmeeg sdaalppqef glvvgepvqf rffgssvrrq
      541 dqvgtlldyw speelqelee iqatlpaegr tvgevvpvkl harvteagtl eleaipsgtn
      601 erwkvefdvr gaa
//
LOCUS       WP_175845557             656 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia arboris].
ACCESSION   WP_175845557
VERSION     WP_175845557.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..656
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=71068
     Region          75..483
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mtriqkiwql lvgkpldpld prtrhaiavt pllawvglga dglssscygp eeaflalgqh
       61 halalflala taatvfiial gynqvielfp tggggyrvat sllgskpglv sgaallvdyv
      121 ltvatslasg vdaffsllpv saqafkltte ivlilmmtgl nfrgmresim vllpifigfv
      181 ilhfalivyg vavhgsnlam ivpdavheah gmsqsvgafv mlallmrafs lgggtytgle
      241 avsnnvnmla dprvpngkvt mwymstslaf taggiillym lwharpvege tlnavvfgsv
      301 idhlglgsaf arhallaavl afeaglllvg aqtgfldgpa vlsnmasdsw vprhfrdlst
      361 rlvrqngiiv vglssllill wthgnvdvlv vlysinvflt fsmsllglct ywwrhrserg
      421 wfkhfflsal glsvtatvlv itliekftag gwltvlvtsa vialcfminr hyaetrtqla
      481 kedalfsgka pevdeatapg kpdplqptav llvgkhrgas mhallwvnrl fpghfrnvif
      541 lavgevdaka ydghehlerl rhaitesldy yvahcrrngi aadyriafgt npvvefmnla
      601 sstlddypns vcfasklifr rvnfltawlh nqtpvelqar lhvegkqmvl lpmnvg
//
LOCUS       WP_175845559             384 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Burkholderia].
ACCESSION   WP_175845559
VERSION     WP_175845559.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..384
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41428
     Region          19..363
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mnddykvelp eaaavargrr lrvgviglgi grkhiegwre hpdvdvvaia dpdakrvakv
       61 gdafgidary asadamfaae rldvvsvctp nkfhreltla afdagchvlc ekpmamnade
      121 gremliaaqr tgkrlminfs yrfsaqsral kaqvdggvfg dfyfgrtvwh rrrgipgfgg
      181 wfgtkalagg gplidlgvhr ldlalwlmgy pkpvwvmgsa ydpiartlaa ragktfdved
      241 laaamirfdn gatlaleasw atniqeaelm etrllgtrag llqknlnegy tfdahifveq
      301 hgaqfdmrln ppadgahsam ydyaeailcd vphpapgeeg livmeildai yasaaagepi
      361 rihapgpssv cappvldldl dvag
//
LOCUS       WP_175845618             425 aa            linear   BCT 11-JAN-2025
DEFINITION  epoxide hydrolase family protein [Burkholderia arboris].
ACCESSION   WP_175845618
VERSION     WP_175845618.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..425
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46731
     Region          39..143
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          110..>251
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 msstpfspmr rhllatsvaa gvsamlptal haatgasgir pftahipdea vadlrrriaa
       61 trwpgretva desqgvrlar mqallrywgt dydwrkgear lngfpmfite idgldihfih
      121 vrsrhenamp mimthgwpgs ifellkaigp ltdptahgas addafhvvvp slpgfgfsgr
      181 ptktgwgsdh iarawgelma rlgytrfvsq ggdcgsvish rmamqrvqgl agihvnmpat
      241 vppdiatlla tdspapasls pkekaayekl atfyrdncgy sammvtrpqt vgyaladsps
      301 gqaawmydki sqwtysggvp ersiprdeil ddislywltn tatsaaqiyw edhsnnfnav
      361 dislpaaitv fpgeiyqapr swaersyhnl iyfnevdkgg hfaaweepel farevragfr
      421 plrrv
//
LOCUS       WP_175845646             116 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: BON domain-containing protein [Burkholderia].
ACCESSION   WP_175845646
VERSION     WP_175845646.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..116
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=11698
     Region          44..>108
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mkktphlstl lavsaafllg aapltnavaq dasadngtqv hsnqpvtdtw ittkvkgela
       61 ttdgvkstdv svktvdgvvt ltgvlptria vkkaiavsra vkgvkhvdas glkaka
//
LOCUS       WP_175845677             309 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175845677
VERSION     WP_175845677.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34533
     Region          7..>143
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrflsieaf vrvaeassfa eaarqlgvts svvtnriqql ekfvnaplfh rstrhvrlse
       61 vgeafyreca evvgrvnelt dqmrelratp tgrlriqmlp gfaldhfgap laafnqrypg
      121 iqldiivndr vvdpveegfd iafqifppis eslierrlft vrrlfcaapa yvdahgapqh
      181 prdllqhtta lysgypsrnr wtmtrgdevv emelpgmirs nsvhllreya ltgggvvclp
      241 tlvasealva grlvpiltdy qlaplsfaav ypatqrqalk vkalveflae yigdespwdl
      301 pllergwvr
//
LOCUS       WP_175845684             252 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Burkholderia
            arboris].
ACCESSION   WP_175845684
VERSION     WP_175845684.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..252
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27344
     Region          4..250
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mhtivvqglt ksfgdnavlr gvdfrvarge vvvlmgpsgs gkttllrsln flelpdagtv
       61 svcgiditrt ggvalsrdeq krikairqrt amvfqsfnlf phrtalenvi eglvsvkgvr
      121 kgeavdrglh lldrvglahk ageyparlsg gqkqrvaiar glamepevil fdeptsaldp
      181 alredvlavm relagngmtm lvvthevrfa qdvadrvvfm engvvvedtt pdtfftasth
      241 prvrqflnli et
//
LOCUS       WP_175845721             212 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175845721
VERSION     WP_175845721.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..212
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23181
     Region          23..180
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtdrtkaetr tanddvpagk prtkpaevrl delmaaaetl flaqgveatt iseivehaqv
       61 akgtfyhyfe sksdmlaala qrytasfldr lqhavdacda ddwlarlraw irasietyaa
      121 tyrthdivyt nhhhhdrsna dknaileqlg aildggtrag twrlahpqvt alliyagvhg
      181 atdhiiaape tdraafvdav vddclrmlga da
//
LOCUS       WP_175845722             504 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175845722
VERSION     WP_175845722.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..504
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52489
     Region          14..449
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(20..21,24..25,28,60,110..111,113..115,118,139,
                     142..143,146,270,273..274,277..279,282,310,314,366..367,
                     371,375,391,394..395,398..399,402)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mpryrraalv laaclgtfla tldisivnva lptlqtaldt digglqwvvn ayalalsafm
       61 lsagplgdry ghkrvwlasv ilftagslvc agassigpll igraiqglag allipgampi
      121 lthafpdare rarviggwsa fsalalilgp llggllvehg gwqdiflvnv pigivavllg
      181 awgiperrhp ehaafdpfgq alsvvwlgll tygligigea gaayakvlap lagtavafal
      241 fvrvemrver pllpvwlfrd rrlvranlas fvlgfsgyss lfflslflqq aqgrapaaag
      301 wqlmpqfvmt aitsmlfgri asriplhtlm vtgygligam lavmagfgag tpyvpvgivl
      361 allgvgmgla vpatgmtvme lapaeragma satmnalrqt gmsmgiavlg smmsvgalhr
      421 mtavmqaagg ahadtlarqa vmehvfaagr pdmlgayrea mahgfsiavl csgilsvgva
      481 vmlvmrhere vqaavscvts sqpd
//
LOCUS       WP_175845733             483 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [Burkholderia].
ACCESSION   WP_175845733
VERSION     WP_175845733.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..483
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51821
     Region          1..429
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfaslglie pllrnlqgln yqtptpvqak aipavlsgkd vmaaaqtgtg ktagfalpll
       61 qrlvqhgpav ssnrarvlvl vptrelaeqv lqsfveygkg ldlrflaayg gvsinpqmmk
      121 lrkgvdvlva tpgrlldlnr qnavqfdqvq tlvldeadrm ldlgfareld avfaalptrr
      181 qtllfsatft ddiramaani lrspvdisvs apnataskik qwvvtvdkrn kpdlfmhlva
      241 ennwehalvf vktrvgvdyl aamldeagya vdtihgdkpq parlralerf ktrevqmlva
      301 tdvaargldi ddlplvinvd lpivaqdyvh rigrtgraga sgvavslvca deapqlaaie
      361 alirqtlrre eepgfeaehr vpetsatgqi ikkpkkpkkp kvqqevpvar pvagkkprpq
      421 aqggegkrkp aapqakpasn gvdytigspf svqkprskpa gkagagagkp agkpaggrgk
      481 rqp
//
LOCUS       WP_175845757             158 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175845757
VERSION     WP_175845757.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..158
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17896
     Region          4..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mttpldafdr kllmelqrda qtpqaelgar vnlstaavnr rlrrlaedgv ierytaviap
       61 dkvdhpltiv vnveveseqi gqldamkraf ercpqiqqcy yvtgewdfvl iltvrnmdqy
      121 naltrelffa nnnvkrfktl vsmsrvkvgl dvpvdpge
//
LOCUS       WP_175845793             468 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175845793
VERSION     WP_175845793.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..468
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47861
     Region          18..420
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(25..26,29..30,33,65,115..116,118..120,123,144,
                     147..148,151,274,277..278,281..283,286,314,318,370..371,
                     375,379,395,398..399,402..403,406)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtaavpdraa arrvlaatcv sytlvlldas ivnvaltdia htfgsrvagl qwivnaytla
       61 fasllltggt lgdrfgdrtv yvaglalfva asalcgiapt lpalavaral qgvgsamlvp
      121 cslalinraf pepaarasai slwmgcggia masgpliggl lihlsgwrsl ffvnlplgla
      181 giwlgrtvar aavdrsrhfd wggqaaaiva iaaligtlie gpslgwrsvp ivggavtsvv
      241 awiafiaiea rrrdpmlpla ffrnrmfags tfvsmasafv fygllfvlsl fyrqvrgasp
      301 ldtglaflpm tamvalgglc sgrivarfga rgtmcaafgl yaagalgmtg igattpawla
      361 vapmlaigfa sgfispaats palgtvdrrr agvaaaalna arqsgsalgv aifgaciatl
      421 qpfpvamraa lvmaialsaf aaatwwittr hapangesaa hlqaatrr
//
LOCUS       WP_175845805             506 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: peptide MFS transporter [Burkholderia].
ACCESSION   WP_175845805
VERSION     WP_175845805.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..506
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55170
     Region          7..485
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mmhspvsqtr sfttvfliem werfgyygma allvlfmvdr lgftdshanl twgaftalvy
       61 aapsiggwig dkvlgarrtm iigasvlcag ylmlavpndh ltymyaslgv ivvgnglfka
      121 naanlvrriy egddaridsa ftiyymavni gstvsmlatp wikdhwgwht afavccggml
      181 lailnfmlmh rtlahvgskp ddepirwkrl gavalggvgl alvtlyvlqh kqlavasvwt
      241 aafailaifa ymiakserse ragliaalvl igqvilffif yvqmstsltl falrnvdprf
      301 mlfgttlftw saaqfqalnp iwimllspvl vliyngvakg grdlpvaaky algfgavaag
      361 ylvftisgry avdgrvsswf mvwgyglysl gellvsglgl amiaryvpar msgfmmgayf
      421 vatgvsqylg svvanfaqmp shdlpatdsl plylslfekl gwlaaigmvl allllplmnr
      481 lsrqhqrcae erreealqaq gvaaaq
//
LOCUS       WP_175845771             463 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: amino acid permease [Burkholderia].
ACCESSION   WP_175845771
VERSION     WP_175845771.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..463
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49313
     Region          2..445
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mqqhtmrrel garqisfmal gmaigvglfl gsasaikaag pgalvaylig gamiflimra
       61 lgemavhrpv sgsfgayafe yvgpfagyvv gwsywllmvg vgvaettaig iymgfwfpdv
      121 pqwlwvvsai aaisgfnlln vkvygelefw faivkvvtiv lmiaggaliv ftgighhgep
      181 vglsnlwrhg gvfphgvlgv vsalpivays fagvemiglt agearepqkm iprainsvlw
      241 rilifyvgal fiimalypwn elgdhgspfv ttfeslglrq aagivnfvvv taalssfnci
      301 vfsgarmlss maenglapas faalsasgsp sravratvlf msvgvvlnyv iparvfgwlm
      361 sflsfdvavi wamivlthmr frralaarge tvafrlpgap vtswiclvfv afvfvmlgvd
      421 pstrgslvag avvmalmaia yrrsrplqaa arsarvalga erv
//
LOCUS       WP_175845835             255 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175845835
VERSION     WP_175845835.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..255
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27488
     Region          6..244
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 msgnvvksaa rvfevlelfs tlqrplsvre iatrcgypgs staalltsmk algylaydda
       61 thayaptarl vnlgealvds aagsrrhwha vakrlaarth eavviavqsd lyvqyidave
      121 gahtlpiqfy apigtrreic msslgwalls lqpdstirrl vsrsirrigk sgrtidedvv
      181 ldkveqtrrl gysysahtvt qgaamismvi adgwnglpla mgvagpveri darrdaivka
      241 mrealdarrp daaag
//
LOCUS       WP_175845866             212 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: 2-hydroxychromene-2-carboxylate isomerase
            [Burkholderia].
ACCESSION   WP_175845866
VERSION     WP_175845866.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Thompson,L.C., Ladner,J.E., Codreanu,S.G., Harp,J., Gilliland,G.L.
            and Armstrong,R.N.
  TITLE     2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class
            glutathione transferase from Pseudomonas putida
  JOURNAL   Biochemistry 46 (23), 6710-6722 (2007)
   PUBMED   17508726
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122490
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..212
                     /product="2-hydroxychromene-2-carboxylate isomerase"
                     /EC_number="5.99.1.4"
                     /GO_function="GO:0018845 - 2-hydroxychromene-2-carboxylate
                     isomerase activity [Evidence IEA]"
                     /GO_function="GO:0043295 - glutathione binding [Evidence
                     IEA]"
                     /GO_process="GO:1901170 - naphthalene catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23305
     Region          9..188
                     /region_name="DsbA_HCCA_Iso"
                     /note="DsbA family, 2-hydroxychromene-2-carboxylate (HCCA)
                     isomerase subfamily; HCCA isomerase is a glutathione (GSH)
                     dependent enzyme involved in the naphthalene catabolic
                     pathway. It converts HCCA, a hemiketal formed
                     spontaneously after ring cleavage of 1; cd03022"
                     /db_xref="CDD:239320"
     Site            15
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239320"
ORIGIN      
        1 mnaartaawy fdfvspfayl qqeqfdrlpp aaafeprpiv lgallahwgq kapaeiaakr
       61 vftyrhaqyr adklgiafrm ppahpfnpik plrlaiamgs srdairrifr hiwrdghdvs
      121 tpegfaalce avgfpegvaa veaqpvkdal rantdqaiad gvfgvptfal dgdlfwgeda
      181 tdmfvdcats rawldspevr risalpegir rg
//
LOCUS       WP_175845849             283 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia].
ACCESSION   WP_175845849
VERSION     WP_175845849.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..283
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29818
     Region          52..249
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mhpstapala dgvpirrnrp ahprvgrlll qallavfaly lllpiallli gavgeswtnt
       61 llpsgvtghw fadlaanrsf trafgvsfmv alaccalnav iglplayalh hraqagggfa
      121 trivmlmpva vpaltlgfgy iaifsgdtlp wlgtlplmia ahavltlpyl lqtllgdlrh
      181 lglarleaca atlgatplrq fvtivlpnlr hslfsglvmv aalsigefqi snliagfryr
      241 nypivllqaf ygatgmacaa tvvllvlavl atlvsvgtvq rlk
//
LOCUS       WP_175845945             257 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175845945
VERSION     WP_175845945.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..257
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27220
     Region          3..249
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mttyivdavd salklltyva ehpnlgvtel asqlginksr tyrmlctlel hrfvvqdart
       61 styalgpqaf vigvaasqqn alvraahrhm lalnqainet ivlrvregle svcvarcett
      121 havrtvgavg nrrpinfgas gkvllafapd avrdeylaql rrngqtddpa klaseldava
      181 rkgyavssge vtpgavgiav pvrdltgatv asvsvtgpev rvshadipdy lerlqacsha
      241 isaelgyvpa raalqpa
//
LOCUS       WP_175845978             209 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Burkholderia].
ACCESSION   WP_175845978
VERSION     WP_175845978.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..209
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21824
     Region          1..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mshlswlpfi atslliiltp gqdmilvmsr tlsggtragl vtaagvsvgl lvhtmlatlg
       61 lgallqasew lftalkviga vyllylgitl lrssgeltla sgssgaqasr lrtfaqgals
      121 nvsnpkialf ylaflpqfvp agtahpmlsl fvlgatfagl tflvkgpval fagllsssir
      181 rnpriltrmh rvsgvvllgl gvklalerr
//
LOCUS       WP_175845958             198 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175845958
VERSION     WP_175845958.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21644
     Region          6..158
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrysvehkhe trtrileaas rlfrqegygg sgigpltkaa gvtngafygh fkskgeafrn
       61 vvldgldqlr qgvarfkveh garwrrpfvs fylgprrtca lgescalpsl spevmraddd
      121 trdayeqalr qivdevssgl gdtpdddrai aflallsggv tlaravrdpe laqriadavg
      181 ryavviaert dvqpeqqp
//
LOCUS       WP_175845968             276 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MetQ/NlpA family ABC transporter substrate-binding
            protein [Burkholderia].
ACCESSION   WP_175845968
VERSION     WP_175845968.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 276)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..276
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29786
     Region          15..276
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mlhpvfsarf sagraarvlm aallgvalln garadtaplk vgistspqie alkiaakeak
       61 eqgldvkive ftdwntpnaa lankdidvny fqhipflena kkqggynfis iapgtimkig
      121 lyskkvksfa elkdgarvai andpvnggrg llllqragli tlkpgtdyra tthdivanpk
      181 hlkiipleas qlarslddvd laqgypsfik lagttdpnsa llfdgtenks faiqwvvrpe
      241 sandprirkf iaiyqhspav rraldnafgs lyaiaw
//
LOCUS       WP_175846070             175 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: flavin reductase family protein [Burkholderia].
ACCESSION   WP_175846070
VERSION     WP_175846070.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..175
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18683
     Region          12..164
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mettltgrpa ldplqlraaf gqfptgvtvi ttcaadgrkv gltansfssl sldpplvlws
       61 lrkvapsrpd flaathfain ilahdqidls rrfatpsadk fdgvlhadse sggvpcldga
      121 sarfvcrnvg hyeggdhllf igeieqfdaf gkaplvfhag qyraiadhpd llrti
//
LOCUS       WP_175846074             341 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Burkholderia].
ACCESSION   WP_175846074
VERSION     WP_175846074.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12168325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37651
     Region          31..203
                     /region_name="AraC_binding_2"
                     /note="AraC-binding-like domain; pfam14525"
                     /db_xref="CDD:434015"
     Region          247..334
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 maqfsetgwl gdaacfnhdn lllqsndvde vrarvadvfk phrltptggs ralhscmhha
       61 rwgnlslnll dygggvsiep gplehffllq iplrgdaaie cgsthfvssp gtaslisptl
      121 plkmqwgdac pqvilriere vmerhaqrhf gddrrapvef epefslsssq gtclaqllpi
      181 lagaistdah plrhplafeq lestllnlll hghpnsarng trhlptalap fyvrrveeyi
      241 rahldeplti erlaelagvs pstlfagfrn rhgitpmgfv rqlrlqhvre elladatpgl
      301 asvtdialkw gfahlgrfai eykrafgesp satlrmrrvr g
//
LOCUS       WP_175846129             263 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia arboris].
ACCESSION   WP_175846129
VERSION     WP_175846129.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..263
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27900
     Region          15..258
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 msaypsgrpa agiepplldl rivrklyggr tilanialqv argeivcvvg psgcgkstll
       61 rivagldadf rgsvtldgia lagpsarvgv ifqeprllpw lsiadnvgfa agprggreps
      121 varlldevgl agvarqlpat lsggmaqraa iarglfgepd lllldepfsa vdaitrmrlq
      181 tllldvvhrh rmaaivvthd ldealylgdr vlmlapnpgr vdgeihvdva rprdrrdpsl
      241 aaqrarllda fqrfhdravs daa
//
LOCUS       WP_175846149             428 aa            linear   BCT 11-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Burkholderia arboris].
ACCESSION   WP_175846149
VERSION     WP_175846149.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..428
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=45657
     Region          1..422
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 mdttdsivrr qnnlgpayrl fydepvhaks aegvwivdvd gkryldvynn vpsvghahpg
       61 vvaaissqma vlathtryve erileysdrl lalfpaaldk vmftctgsea ndlalrvara
      121 atngtgiivt rlayhgvtsa iaeispsfga gvplgqhvrt vpapdtyrty tngqvasafa
      181 esvaaavadm rrhgiqpaal ivdtifssdg ifgdpagflg pavdlirneg glfiadevqa
      241 gfgrtgsamw gferhgvvpd ivtlgkpmgn gypvagivar tplidafasr tryfntfggn
      301 pvasaaglav lnairdqglm lnvqstghyf rskllelqda cpligdirga gffigvdlvk
      361 drqtkaplsd dtpkvvngmr rkgvlisatg pygnvlklrp qlifqpdhvd lfmtnfeavl
      421 sdvtrsla
//
LOCUS       WP_175846164             277 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175846164
VERSION     WP_175846164.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..277
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29793
     Region          85..267
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          212..259
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mvaifaklgk vissagserf asdmhallvg siplattrmt ewtldepage vvhveslgaf
       61 gatrddgrgg apvapgerep athplrnriv aacdrqlihv dplmrrghgg evaplrgasa
      121 gyqchlvsrk anrryvislh rtashddfsl qemsflrnfa dtllplvewh astrrqgvre
      181 sgaprtgvag vpgvealrhe fesrlarasv vlsaresevc lgllagkmlr emagelgvke
      241 stvetyikra avklgisgrh gltkwmiddc vpytsaa
//
LOCUS       WP_175846186             319 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia arboris].
ACCESSION   WP_175846186
VERSION     WP_175846186.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..319
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=33563
     Region          10..224
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(53..54,56,73..75,81,83..84,124,223)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(53,55..56)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(81,84,87,93)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(116,120..123,125)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(121..122,145..147,196..197)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          237..319
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 msplrirver idaltpairr lhlvaanggp lpgfaagahi gvhvplsprs qrrayslvna
       61 ggsagpvdry eiavlrepag sggsqwmhac tpgeefdidp prndfplaad arrhllvagg
      121 igitpilama relthagrpf alhyaardag smayrdevaa lpdatcwfdn gepsrgmpla
      181 etigapesgk hlyvcgpagl ieatlaaarr lgwrddtlhc erfaapvatg gdapvevrla
      241 vsgrtlnvpa gtsildamie agldplydcr rgdcgvcavr lldgdpdhrd iclsdddrar
      301 ggfcpcvsra ngahlvldl
//
LOCUS       WP_175846198             730 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia arboris].
ACCESSION   WP_175846198
VERSION     WP_175846198.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 730)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..730
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78161
     Region          47..730
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mvtgtsaarr araiavggaw cmaaagsapa qaadaggapq agaagavlpa idvkgaadsa
       61 avglvgrrtt agtktdtpva eipqtinivt aqqiemtgaa dlnqalryvp gfstfgadsr
      121 tdwyaalrgf tptlyvdgvp alntavianw rvdpytidsi ailrgptsvl ygagepgaiv
      181 daqtkladge rvreagvqig ndarkqvmld vgdrldpdgk layrfvgvar dgnaatgpng
      241 drrvalapsf rwrpnadtsl tvsatflqds gdissnflpa sgtvlpnpng rlsqdiymgd
      301 psfndyrkkq wslgyalehr vngiwtlrqd vrwshlsldd atvfgngfap rsttnmmrta
      361 glfqlnysrl didnhaqarf gtgplehtll fgvqfdrqtt tnsvwlalap sldlyhpvyr
      421 pvtaaifsgp tslphinqyt amnavgvyaq dqirwqrwtl tlggredfvn ahfddrtagt
      481 qaqqnvsafs grvgltyqgd aglspyvsys tsfdpvvgvr mfggglpkpt rgaqteaglr
      541 wqppgrnlml naavyqidqt nvvtptpvnl drtgatsvqt gkvrsrgiel savgkltrel
      601 sivasyayqd vknvqandas lnnwpvsvpl prqmaslwad wtwhtgaltg vgigggvryq
      661 sasagapdns ltvpgatlyd lalhydmphw rfalnvanlf drryvsgcqs ynvcvfgner
      721 tvlasakynw
//
LOCUS       WP_175846212             459 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: amino acid permease [Burkholderia].
ACCESSION   WP_175846212
VERSION     WP_175846212.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..459
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49075
     Region          7..457
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mtqqqrsfda ivareqglrh altsgqmami aiggaigtgl flgsgfaigl agpsvlvsya
       61 igalialllm galaemtvah ptagsfgaya ehyvgplagf lvryaywfav vfaigteisa
      121 iavfmkywfp avpgwywvig fsalliavnl asvtlygtve yafsllkiaa ivvfivlgay
      181 lvwsapaasg igfanytahd gfmpkgpwgt wvavivaifs ymsieavaia ageardpqha
      241 vtrafrstvf rlvlfylltl slmlaivpwt aagtdespfv kvmaathvpy aagvinfvll
      301 iaalsamnsq lyvttrmmfs lsrarlapav fgrlgtngvp raalwistsg vavaavlval
      361 apdtaftvmm aiamfgalft wlmifvthlr frsqyrgpal afrmwghpfg sllgaglvaa
      421 ilfttaftre frmtmvvgvv fvvlltlaya lhyrhehar
//
LOCUS       WP_175846268             137 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [Burkholderia].
ACCESSION   WP_175846268
VERSION     WP_175846268.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..137
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14312
     Region          4..136
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mnsnrlndfa atllrvalgv lylahvaqkv fvftlpgtaq ffvsiglpgw laylttfvel
       61 agglallagf rvriaalvll pfmlgataah lphgwsfasp nggweypafw avtlavqall
      121 gggafaigar eaaaqrv
//
LOCUS       WP_175846298             308 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175846298
VERSION     WP_175846298.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34126
     Region          16..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          101..300
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(116..117,119..120,123,127,129..135,229..234,
                     240..241,243..244)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mmhpdlrrld lnlllvfdal yrhrsvaaaa helalspsal shalarlrda igdalfvrlg
       61 nemqptvrad diatwagdal damskglara rrfdpahsdr tfvfaatdyt afavlpafla
      121 riqhvaphlr irvvhsdrki svdelaagri dfalgyhees aadapgiedf dwfsddyvvi
      181 asaahpnihr rltldqylaa rhvvvtpwne srgvvdyvld rlglarhvav qlptvlaapf
      241 viaesellmt vpnraaqalr haapirifpa pfeiprytvk vyshakhart dahrwiraql
      301 ldarpgpv
//
LOCUS       WP_175846344             403 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: benzoate/H(+) symporter BenE family transporter
            [Burkholderia].
ACCESSION   WP_175846344
VERSION     WP_175846344.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..403
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41471
     Region          15..403
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mnpsptasas raggrrffad tsvsalvagf vammtgytss lvlmfqagra ahltdaqiss
       61 wiwalsigma lttiglslrf rapvvvawst pgaalliasl pgvpyaeaig afvvcalllt
      121 avgvsglfdt lmrripagia aallagilfe igieifraaq fqtalvlamf ftylivkrla
      181 pryaivttli vgtavagslg lldfsrfhia lahpvftmpa fsiasivsig iplfvvamas
      241 qnvpgiavlr adgyqtpssp liattglasl llapfgshgv nlaaitaaic tgpeahedha
      301 krytaavwcg tfylvagifg atiaalfaal pkalvvsvaa lalfgsimsg lanamqdvkq
      361 reaalvtfmv tasgltllsi gsafwglvag ivtqvilnar rpa
//
LOCUS       WP_175846356             528 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia arboris].
ACCESSION   WP_175846356
VERSION     WP_175846356.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..528
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56853
     Region          34..470
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msagpaglth dvpaapfern atmsdsvakp vdatfdqfgl aadilkaiae qgyttptpiq
       61 aqaipvvlag rdvmgaaqtg tgktasfslp iiqrllpqan tsasparhpv raliltptre
      121 ladqvaanvh ayakhtplrs avvfggvdmn pqsaelrrgv eiliatpgrl ldhvqqktan
      181 lgqvqilvld eadrmldmgf lpdlqrilnl lpkdrqtllf satfsgeikk lastylrnpq
      241 tievarsnst nanvtqivyd vaegdkqaav vqllrdralk qvivfcnski gasrlarnle
      301 rdgvvasaih gdktqlermq aldafkrgei ealvatdvaa rgldiaelpa vinfdlpfsa
      361 edyvhrigrt gragatgdal slcspnerkq ladieklikr plemqtlald kpsrqrhddr
      421 ggerggdrgg drgsdrsgdr hsgerggrrd rdehrgasgh rsagaerggr prrheapvdd
      481 fflkpyepsa pakqahdaqp eqqpekkgpk rqvaallggf gmprkpsa
//
LOCUS       WP_175846387             136 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: group II truncated hemoglobin [Burkholderia].
ACCESSION   WP_175846387
VERSION     WP_175846387.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Keppner,A., Maric,D., Correia,M., Koay,T.W., Orlando,I.M.C.,
            Vinogradov,S.N. and Hoogewijs,D.
  TITLE     Lessons from the post-genomic era: Globin diversity beyond oxygen
            binding and transport
  JOURNAL   Redox Biol 37, 101687 (2020)
   PUBMED   32863222
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Bustamante,J.P., Radusky,L., Boechi,L., Estrin,D.A., Ten Have,A.
            and Marti,M.A.
  TITLE     Evolutionary and Functional Relationships in the Truncated
            Hemoglobin Family
  JOURNAL   PLoS Comput Biol 12 (1), e1004701 (2016)
   PUBMED   26788940
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Wajcman,H., Kiger,L. and Marden,M.C.
  TITLE     Structure and function evolution in the superfamily of globins
  JOURNAL   C R Biol 332 (2-3), 273-282 (2009)
   PUBMED   19281958
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Vinogradov,S.N., Hoogewijs,D., Bailly,X., Arredondo-Peter,R.,
            Guertin,M., Gough,J., Dewilde,S., Moens,L. and Vanfleteren,J.R.
  TITLE     Three globin lineages belonging to two structural classes in
            genomes from the three kingdoms of life
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11385-11389 (2005)
   PUBMED   16061809
REFERENCE   5  (residues 1 to 136)
  AUTHORS   Wittenberg,J.B., Bolognesi,M., Wittenberg,B.A. and Guertin,M.
  TITLE     Truncated hemoglobins: a new family of hemoglobins widely
            distributed in bacteria, unicellular eukaryotes, and plants
  JOURNAL   J Biol Chem 277 (2), 871-874 (2002)
   PUBMED   11696555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10201300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..136
                     /product="group II truncated hemoglobin"
                     /GO_function="GO:0005344 - oxygen carrier activity
                     [Evidence IEA]"
                     /GO_function="GO:0019825 - oxygen binding [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15775
     Region          15..133
                     /region_name="TrHb2_PhHbO-like_O"
                     /note="Truncated hemoglobins, group 2 (O);
                     Pseudoalteromonas haloplanktis PhHbO like; cd14773"
                     /db_xref="CDD:381282"
     Site            order(47..49,55,58..59,62,73,82,85..86,89,91,95..96,99,
                     124,127..128,131)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381282"
ORIGIN      
        1 mtdvnddaps qptafelvgg earvremvdr fydlmdlepe faeiralhpq sldgsrdklf
       61 wflcgwlggp dhyisrfghp rlrarhlpfp iasverdqwl rcmawameda glpeplrerl
      121 mhsfydtadw mrnrpg
//
LOCUS       WP_175846403             211 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: carbonic anhydrase [Burkholderia].
ACCESSION   WP_175846403
VERSION     WP_175846403.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Lindskog,S.
  TITLE     Structure and mechanism of carbonic anhydrase
  JOURNAL   Pharmacol Ther 74 (1), 1-20 (1997)
   PUBMED   9336012
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10096752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..211
                     /product="carbonic anhydrase"
                     /EC_number="4.2.1.1"
                     /GO_function="GO:0004089 - carbonate dehydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22853
     Region          11..190
                     /region_name="beta_CA_cladeA"
                     /note="Carbonic anhydrases (CA) are zinc-containing
                     enzymes that catalyze the reversible hydration of carbon
                     dioxide in a two-step mechanism in which the nucleophilic
                     attack of a zinc-bound hydroxide ion on carbon dioxide is
                     followed by the regeneration of an...; cd00883"
                     /db_xref="CDD:238448"
     Site            order(33,35,42,44..46,58,61,83,88,98,101,180)
                     /site_type="active"
                     /note="active site clefts [active]"
                     /db_xref="CDD:238448"
     Site            order(42,44,98,101)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238448"
     Site            order(43..46,48,50..51,53,58..60,62,64,78..79,82..83,121,
                     180,182..183,185,187)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238448"
ORIGIN      
        1 mnrpksmlva niawaretre htpgffdala rgqnprvlwi gcadsrvpae tithcapgel
       61 fvhrnianlf hpdddnsasv leyavrvlkv dhvivcghyg cggvrasllp ppadlphvar
      121 riaplcalar rhrdtldgld dtaaadrlae lnvleqvrll raspivrgre rpplvhgwif
      181 sladgrllel dsgytappad vepalaaaal v
//
LOCUS       WP_175846580             142 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Burkholderia arboris].
ACCESSION   WP_175846580
VERSION     WP_175846580.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..142
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14909
     Region          23..106
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(45,48)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mvpagvdpaa fdafdmqald agtfdaaidg agdalavvff wgvdcfncei akkamlaqpd
       61 airaldlkwf hcnvyehhql grrfglhgvp twfffhrgkr lgratgwhgl aqfqaavsaa
      121 rakvaaaaag dppggdplag gd
//
LOCUS       WP_175846618             249 aa            linear   BCT 11-JAN-2025
DEFINITION  ferritin-like domain-containing protein [Burkholderia arboris].
ACCESSION   WP_175846618
VERSION     WP_175846618.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10090058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..249
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27330
     Region          <86..196
                     /region_name="Ferritin_like"
                     /note="Ferritin-like superfamily of diiron-containing
                     four-helix-bundle proteins; cd00657"
                     /db_xref="CDD:153097"
     Site            order(97,100,160,191,194)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 mtatgelpaa sqvadgerlg cldapvprgv araraylvdr ikraairqlh rsshgerwml
       61 smyligeeat ecalhedwtg qppdwlapri eqhladerrh aaafadalrq rgveasagph
      121 epdwlsqrki mrwrrlaqry aphfaqgvlv payatglcae qmamrvlarh catigdahpl
      181 ypllarvlad etrhvrlcsd tlrrlvepse aaslaallge iraieagfgv tgalamyaag
      241 waqslrpra
//
LOCUS       WP_175846620             205 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Burkholderia arboris].
ACCESSION   WP_175846620
VERSION     WP_175846620.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130209
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..205
                     /product="phosphatase PAP2 family protein"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22787
     Region          42..198
                     /region_name="PAP2_Aur1_like"
                     /note="PAP2_like proteins, Aur1_like subfamily. Yeast
                     Aur1p or Ipc1p is necessary for the addition of inositol
                     phosphate to ceramide, an essential step in yeast
                     sphingolipid synthesis, and is the target of several
                     antifungal compounds such as aureobasidin; cd03386"
                     /db_xref="CDD:239481"
     Site            order(98,106,138..140,170,176,180)
                     /site_type="active"
                     /db_xref="CDD:239481"
ORIGIN      
        1 mntwllrndr rpdvrqmlaa tfgmvaglai ffllergvtp ryvlvtalda ripfiawswf
       61 vyvaffpfvi alaayarpsa faafkeavli afvlgvvcfl lfpeavprpd vaeignafvr
      121 hrlarmwqld laangfpslh vavtclacrm ltdrrrivaa sigllicist ltlkqhtvad
      181 vlggvalami salwverraw rrrla
//
LOCUS       WP_175846648             451 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: uracil-xanthine permease family protein
            [Burkholderia].
ACCESSION   WP_175846648
VERSION     WP_175846648.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..451
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45633
     Region          9..423
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mphdpisppv darlpawqla lfglqhvlsm aaspitavfl iakvlalpgd ltvqligatf
       61 facgigtlvq slgagpvgar lpfvmvpgga ptmlfagiaa qsglptatga allasafywv
      121 llpvftrclr lfprivvgam lllvsvnlir iyativvgqp gsadfaqpra lglalativa
      181 tvaaagafrg tagrlavlig lvagatlgwa ldampaladv wrgplfthpv wlpfgmprfd
      241 llaalpllif taismaeata qtvavgetcg kaislprdvp ktirgdalas lagalfgtpl
      301 ivtsaenigv vqttgvrsry vtaaagaili vialfaplar layaipaavv ggtalvvfam
      361 igvmgirlla svdlharanq ytlaaalvvg lapilvpnly rqfgapvqiv lgngmaagtl
      421 aaiatqlafa alarlggrah agaaaapsrd a
//
LOCUS       WP_175846669             374 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia arboris].
ACCESSION   WP_175846669
VERSION     WP_175846669.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..374
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41882
     Region          87..327
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 masplvlihr ilgfaaarrg rtlsgsspqh ngerfanvap rpvegfgktl giawnmlvnk
       61 prntvpagtl pvdsltrael daapdrslyr lghstlllkl rgefwltdpv faeraspfrr
      121 vgpkrfhapp ialqdlpplr gvilshdhyd hldrdtvlal aattdvfvtt lgvgdrliew
      181 gidaskirql dwwqsmdvag ltltatpaqh fsgrslfdgn stlwaswviv dgdrriffsg
      241 dtgyfdgfre igerlgpfdi tlietgayda qwpyvhmqpe etvqahidlr grwlipihng
      301 tfdlamhrwq epfervtala ivrgvelstp rigervdlde phrgerwwrt vderaatpaa
      361 ksrrrqlcas qatk
//
LOCUS       WP_175846667             343 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia arboris].
ACCESSION   WP_175846667
VERSION     WP_175846667.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..343
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37319
     Region          70..270
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 makdtskdkk ptgnlhlaag llrglaqena aletrlpepv aapaatieaa pasttaaaap
       61 agtadlgapq kvlvkdcipn pfnprvfyse sslhelaltl kregqiepik vtrlpefpgk
      121 lvvidgqrrl ratsingddt inatfrtdht peqlytiayr anhdherqti fddavawkrl
      181 ldekvfsdqn tlaekigkdk asisktlsln alpntllerm asandvvglq aayflklife
      241 rlgeptadrl ltavidrkks vrdlenflra qsdgnkkagr trysvrhdfa lesraigqlk
      301 typdgrldlq lkgvdashqe aladklktvi dayvadlaaa apk
//
LOCUS       WP_175846712             214 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia arboris].
ACCESSION   WP_175846712
VERSION     WP_175846712.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..214
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24461
     Region          1..210
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mltvwgrrna fnvqkvmwlv delalahrhv paggrfgvld tpeflamnph grvpliddng
       61 tvvweshsil rylaarygrp gfwhddpaeq sradrwmdwa qttlqpafln gvfrgyyrtp
      121 peqrdtvrve qsiaqcaqyf rlldaalagq pflagdtitl adiatgthly ryfeldiarp
      181 dvpnvqawye rlkarpayrt hvmipfddlh gkld
//
LOCUS       WP_175846684             707 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia arboris].
ACCESSION   WP_175846684
VERSION     WP_175846684.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..707
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76886
     Region          9..691
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mtypslrdwl fsgktfaasm lalylglyfq lprpywamas vyivsnpfvg atrskalyra
       61 lgtalgaaaa iffvppfvet pllfsiivat wcgtllylai sdrtarsyvf mlagytmpli
      121 alptvtdpst vfdvaiarpe eivlgivcas vvgsavfpnr laptliertd awfkdaafyg
      181 retlsghlag kalsacrqrl aatitglefl lsqlsydhah prilaraqal agrmqlflpl
      241 mssladplia lmrdlhvrpp aldalladaa kwfdaplpav kagtdgdmah dpvadnlrar
      301 iaalqpadsa laswdgalls nalwrlrqvi diwqdcrslr alianeagvw qpryrhwrlg
      361 gterffdrgm mlfstltvvl aivfacwlwi ssgwhdgaaa vtlvavscsf faaldepapl
      421 vfkfflstaa svvfaglylf vvlphvhdfa mlvlmfagpf iligtllprp qfnmvtmlva
      481 vntatfisiq sayeadffvf lnsnlagvag llfayvwtra trpfgaelav rrllrsgwed
      541 varsastqpl ddqrnhasrm ldrvtqllpr lgasddhrhp siesfrdlri alnaldlrrs
      601 rrrlsgdvpd aidrvlagvt dhytrcaaan arqpappall atiddalhrv agrtlpgatp
      661 adgaaapatp athrrlrdtl halvglrlsl ypaaagqapq apdgara
//
LOCUS       WP_175846721             126 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cupin domain-containing protein [Burkholderia].
ACCESSION   WP_175846721
VERSION     WP_175846721.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..126
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13780
     Region          12..115
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 mtnitnlvdl mrapakltqs rvpsgllldg npmqtlshhy ispcgqfscg iwactpgrwt
       61 ieydeseyce mlsgvaivrd aegrervlra gdrfvippgf rgtwevvetc rkiyashapq
      121 agqpga
//
LOCUS       WP_175846730             344 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Burkholderia].
ACCESSION   WP_175846730
VERSION     WP_175846730.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..344
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36214
     Region          109..316
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mkivkpllia aavaaalsta paafaagadt vrpdaktsaf laalngqkgp gletlspaka
       61 rqvlvdaqng akvdlsgidv snrtieqdgl svpvtivrpq gatgtlpvfv fihgggwvlg
      121 dfptherlvr dlvvqsgava vfvnytpspe ahypvainqa yaatkwvaah gaeigvdgsr
      181 lavvgnsvgg nmtavvalma kdkggpairf qglmwpvtdh nfntgsynay qqghfltrpm
      241 mkwfwdaytk neaqrneiya splrasiaql kglppaliqv aqfdvlrdeg eaygrkldaa
      301 gvdatttryd gtihdfglln vladdaptka atkamaneia trlk
//
LOCUS       WP_175846735             316 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Burkholderia].
ACCESSION   WP_175846735
VERSION     WP_175846735.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..316
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34538
     Region          80..315
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mhawqeplgn lpealrarfa eigavwgqdi dahrdwvidt ytplvaaraa tdlgceierd
       61 ipygpdarqr ldvfvqhatr qgapadvvlf vhggafvrgr ksingliydn vprwfarhgy
      121 vavnveyrla pdapypagaq diaaaldwtr ahiasygghp grifivghsa ggahvatylg
      181 dplldarrge rvagavlisa rlaadtlpdn pnaagvrayf gddpsryaar splayaerid
      241 aplmivvaey enpyldayga affervarar qrerrpgrap rfmqmprhnh tsvvahfdsg
      301 etllgdamld ffsafa
//
LOCUS       WP_175846757             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175846757
VERSION     WP_175846757.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32663
     Region          1..>137
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          91..286
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,221,238,265)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     215..219,226..227,230)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 melndlrifv atvdagsfta aadqlmlskq fvsrrtmale aslgvrllhr ntrnlavtes
       61 gqefyvraqr ilaeiadaeq amsvrstelh gslkisapls fgithvspli aeflsahpav
      121 klnldltdrr vdligegfdl vlrigsleds tliaralgaw pmiacaspay lkrqgtpqtp
      181 adlaghtcll ygrerrigwe frvdgaartf dvqgplvann gevvrdaaia glgiallprf
      241 ivgaaldsga lvpvldayap spitlnavfp qhregfvtlr tfigflaerl gepaparasg
      301 agrtr
//
LOCUS       WP_175846752             471 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia arboris].
ACCESSION   WP_175846752
VERSION     WP_175846752.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..471
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50261
     Region          9..456
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mnqrqgfdti verekglhrg lstaqlsmia iggaigtglf lgsgfaigfa gpsvlvsyai
       61 galialllmg claemtvahp tsgsfgayae hyvspwagfl vryaywasiv favgtevtai
      121 avymkywfpa vpgwywivgf saaligvnlv svkvfgavey vfsmlkiaai vgfialgavv
      181 vfgapagsgi gfanytahgg ffpkgvwgmw vavivsifsy lsiemiavaa geardphqai
      241 trafratmlr lvffylltla lmlaivpwta agsdespfvk vmaathvpga agvinfvilv
      301 aalsamnsql yittrmmfsl sragyapkal grltghgvpa aalglsaigi alatvlnvly
      361 pdtsfvmmms vsmfgamftw lmifvthlff rrhhrgqala frmwgfpvts llgaalmlaa
      421 lvttyftref rmtlfcgvpf mivlsvvyav wyrgkgdapa geregvhvpg q
//
LOCUS       WP_175846759             555 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia arboris].
ACCESSION   WP_175846759
VERSION     WP_175846759.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..555
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59980
     Region          4..550
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mqasatpaap vtvftarril tmnpaqpsat hvavrdgril avgdatdaaa wharfgacta
       61 ddtlrdkvlm pglveghchl megamwdavy vgyydrrgpd gtlwpglrsl davldrlada
      121 eramtddgpl lawgfdpiff gtarltvrel drvsaqrpia ilhasvhlmn vngamlarag
      181 idedtdvdgv srdadgrptg elqefaamlp vyqtiggkla isasekphav wnfgrvaqla
      241 gvttatdlvn dlsadgnrtl hevtadpdyp vrivpafapq rnparsadsv lgeierntdk
      301 lhfgpvkfiv dgsiqgftar vrwpgyaggq pnglwlippa qlvdvfepfh raglqlhvht
      361 ngdeatdvvl damttllarh prpdhrhtlq hcqmadaaql qrvralgmcv nffanhlyyw
      421 gdahysqtig pdranrmdaa gsarrlgipf alhsdapitp lnplftawca vqretasgrv
      481 lgegerlpvd aalhaitlga aytlrmdhlv gsievgkyad favldddpsv caparlkela
      541 vwgtvlggrv frspr
//
LOCUS       WP_175846784             212 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175846784
VERSION     WP_175846784.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..212
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23805
     Region          20..158
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdrqlrwgda srmdsvndgr nailraalda miehgidsls iddvarrani srrtlyryfg
       61 tkkeliqgvi svqnaeffde mqralagfeh dfeaycaesv cfavryrdrh hggfhhnyla
      121 tslstdvfgf iveniapmwq rvldkpyray vavhgasapa lddlialvsr iglayclvpa
      181 depamraqmr ilwpprpepa akpvaarrkt aq
//
LOCUS       WP_175846800             463 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia arboris].
ACCESSION   WP_175846800
VERSION     WP_175846800.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..463
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49813
     Region          25..451
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mdndrpgrta svaathdfga qayrsdlder rkphglglst lvifglayml pmtvfttygl
       61 vtsetnghlt aayavtlvam lftarsyghm arlmpsagsa ytfasrnfgt sagfmvgwal
      121 lmdylfipmi sylaigiymk qifpgvpasv wivgsialvt glnivgirlv nrvnlilias
      181 qlvfiaifvi asahvatgag lsmaialpss gdaraifags ailclsflgf davttlseet
      241 reprrtvpra illctlasgl lfmliayagq rvfpdwhafk dldsaslelm grvggrtlsa
      301 ffvavyvagc fasamagqas vtrvlfamgr drvlpervfg hlharlrtpv ratlavgfvs
      361 lsalfitldl astmisfgal vafaivnlcv mrsylsrpeh rhaagwitfg lmpaigfamn
      421 vwlwsglsrq tfyvgigwlv lglcqlvwlt rgftrpaptl smn
//
LOCUS       WP_175846806             286 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Burkholderia].
ACCESSION   WP_175846806
VERSION     WP_175846806.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 286)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..286
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30211
     Region          1..286
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mnvyllqivn gigvgmlyfl lavglsivfg llrfvnfahg afyllgaylc yqalqwsanf
       61 wvalavvplv vgafawivek lvlrhvyaqq hefhilatvg lalvlqecai lawgplgdnv
      121 pppdalngvv iwggfvypky rlfviaftav laavlwwvle gtrlgstvra gsessemvsl
      181 lginvtrvfs lvfalgaata alagvlaapi rgvdpfmgie algvafvvvv vggmgnflga
      241 lvggllvgiv qslmstlwpe garlmiyvam aavlllrpng llgraa
//
LOCUS       WP_175846840             437 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia arboris].
ACCESSION   WP_175846840
VERSION     WP_175846840.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..437
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46574
     Region          26..424
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(40..41,44..45,48,80,130..131,133..135,138,158,
                     161..162,165,254,257..258,261..263,266,294,298,356..357,
                     364,380,383..384,387..388,391)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mppsnspavs aspasldaaa rpttvrwrif limlllvain yidraslsva mpliapefnl
       61 spaleglmls affwsyalmq ipvgvmldry htrgiiatat lawgafqalg aashswfllm
      121 ltrmglgfse spvfpagakl igtwltpher grgavlvdgg aplgsalgai lisgliawfg
      181 swriafviag vgtmlvgvlv wryirnhpse hpgvnaaele hitrenapak atgervplre
      241 lvkdrsvlam fagyscilav fyglltwmps ylhktygfni attggatfii fmsgfvgeli
      301 ggtigdrwka sgaspnlvmr tmfsgsslia aacilaaayi ananavvlll siamffirfc
      361 gmywslpaiv ggperagvlg gtmnfcgsmv gvvvpiligl ivqwsgsyfl allffvvmav
      421 liavfssmid yrprahg
//
LOCUS       WP_175846829            1063 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia arboris].
ACCESSION   WP_175846829
VERSION     WP_175846829.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..1063
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113402
     Region          1..1051
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnlgrlsvqq pvlaivlsiv ltiagalayf slavseypdi apptvviqat ypgasaetvs
       61 qtvstpiele vngvedmlym ysqatsdgsl nitvtfkpgt dvdkaqvlvq nrvalatprl
      121 pepvqrsgvs vrkssptqlg tiflyspdqr ydplyvsnya irnvadvlkr iegvgdinpl
      181 gareysmriw ldpervasfg lspgdliaav rsqntqlagg vvaqapitnq afqpnlifeg
      241 rlkrpedfsd ivvkqgkdgr lvrlkdvarv evgalayatd symlrhptia lqvlqqpgan
      301 avatmdavek kmaelskdfp kgivynigyn ptafigdsih elvktiyeav vlvvfvvllf
      361 lqgwrpsiip ilsipvslvg tfaamavlgy sinnltlfgl vlavgivvdn aivvvenver
      421 hlaagagprd atlltmkevg galfaitlvl cavfvptsfi pgisgqffrq fgvtiavsta
      481 isfftsvtla palsammlka htgdhhapap tsrmaalfap amhvarrfss afnrvfqrls
      541 daygrlvrkv vriipamaal yvvliaatgy llvsspkgfi paqdrgylvv lvrmpdgatl
      601 ertsavarki edialsvpgv arvpvfsgvn aatgtnsans aglfpvfqpw perkarglti
      661 dtiaaemrkr latvteasiv vampppvqgl gstggfamrl edrnglgtaa lakatqdlva
      721 aanrtpgmvg vytsysatsp qvhveldrek aemlgvpsqa indavetyfg styindfniv
      781 grtyrvtaqa dlpfrvgasd larlkvrnrd gemvpigsvt riddtlgvdr aprynlypat
      841 eingdtapgl gsgfaiktme tlakqvlppg isfewtdlsy qqttagntgl lvfplcvllv
      901 ylvlaaqygs wslpvsilli vpmcllaasl gvralgqdvn iltqigfivl vglaaknail
      961 ivevarqlea dgtelveavv eacvqrlrpi vmtslafilg vlplvisega gaemrqavga
     1021 avffgmigvt ffgllftpvf yvmvrrlamr ktaaatvate avq
//
LOCUS       WP_175846866             421 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia arboris].
ACCESSION   WP_175846866
VERSION     WP_175846866.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..421
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=43904
     Region          205..413
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(212,252,290,393,396)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(212,393,396)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(212,252,290)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 msfrssfaaa vlgavvfvsp laasaapagw vaawatalqp ipdlaapppl yrapdvagrt
       61 vrqivyptvs graaririsn aygraplvve aaslarageg aalaggaavp vrfggkssvt
      121 ltagqelesd pvaidvtsaq pyaislqmgp nqrmtvwhrv snqfnyvsap gdhvsdpgaa
      181 afrtrftqya wvtelaveag tarasvaaig dsitdglrss vnrnrrwpda larrlttsga
      241 dsvgvvnlgi sgnrllsdsa cygtslasrf erdalsrsgv kaavvligin dinfaampqr
      301 agldcdhpht qvtaaslidg yrrlieaahr qgvkvfgatl tpaalpagre airlevnrwi
      361 rsgggfdgvv dfdavlrdpa rpsvlqrryd sgdgihpsdt gytamadavp veqlravvgg
      421 k
//
LOCUS       WP_175846883             213 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Burkholderia].
ACCESSION   WP_175846883
VERSION     WP_175846883.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..213
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22688
     Region          1..213
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mnlhtwwlfv atvfvvsaip gpnmllvmth garhglrrss stmagclsal vlmlsvsaag
       61 lgavleawpa mfntlrfaga aylvylgvka wrarvdddtp aadvdtvarq aapasrwtlf
      121 rngflvagsn pkailfaaal lpqfinaaep tlpqfgilvv tfavievswy lvyasfgtri
      181 gatlksqsva kvfnrltggl fvgfgammal vrh
//
LOCUS       WP_175846905             405 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175846905
VERSION     WP_175846905.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..405
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40547
     Region          32..382
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(42..43,46..47,50,82,132..133,135..137,140,159,
                     162..163,166,234,237..238,241..243,246,274,278,327..328,
                     332,336,352,355..356,359..360,363)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 msessspess spfaappdah rvlplparqr artasmalff vagmmyaswg vhvptvrdkf
       61 alspgllsia lfavaggsia amltiarwit rvgsrtacla gglvmsacaa lilvvpdywm
      121 llavlalfgf smatldvamn aeasaveial gkpimsslhg mfsiggmsga aaggallsag
      181 mapaahlala aavsaavlva agpavlphvp hheqahgggn rwrspalwml ggialialia
      241 egamydwatv ymrdvvaasp alasaayaaf sggmaiarfa gdavrarfga pqlvcasasl
      301 acagmigall lpnpvavltg ftlmglglan mmpvlfaaaa rvkgihaaeg lahvaglayf
      361 gllfgpvvig avaqaanlti glsvvalcaa lvaaiapkvl ahlki
//
LOCUS       WP_175846935             784 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [Burkholderia].
ACCESSION   WP_175846935
VERSION     WP_175846935.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 784)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 784)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18771781
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..784
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=84595
     Region          19..>109
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Site            order(30..31,33,57,60..61,64..65,67..68,91,94..95,98..99,
                     102)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          55..85
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          173..759
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          215..241
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          249..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(251..252,255..256,258,282,285..286,289..290,
                     292..293,316,319..320,323..324,327)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          280..310
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          315..343
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mlsfdlsasa tltpeqqlaq dialvldnal erqragafdd aralyeaild avpahgdahy
       61 nlaillvdtg rpadavphfe aalganptng yywvsyihal hrsgqaaaaw iaveiaqqrg
      121 vhgpaldgli sqlampdtvl vtaavpaahp ggtaatiiae tvadaaagdd agkparrasr
      181 nllqkhaaly akgkyaeata haqrlvaeyp ddgacwrals aslhkggrfa elidaglrtv
      241 allpdevlvr illadtlrvm nrlaeadeqc qrllqlqpdh peamrirglv lfalrridea
      301 iaacrravel apsvaapygt lgfvlleqga tqealgwlrr sieidptdcv thssmlfcia
      361 hssdfdpqtl vaehrkfgqr ydnrkrkraa avfanprnpa rklrvgfvsg dlfghavasy
      421 alpvieqlat dpgiamhfyh nhvdedstse rfksratswr nvagmsdeaf lermrndgid
      481 iaidlsghtg rnrlvalaqr aapvqaswig ypattgvtai dyyltdrfva ppgafedqfv
      541 ekmvrlpaia pfmpppncpp vnvlpalhng yttyasfnrl nklsphviev warvlhadpt
      601 armalgaigs dgdqqtltew faragidanr ltfhrrsnip vymqqhhgvd lcldafpytg
      661 stttlnalwm gvptvtipga tmagrgsagw lqhvgldayi atdeddfvak alalghdtaa
      721 lqalrtglra rcaqsaafrp dvvaaglssa lrtmwtrwca nepvtafdtp lfddtataqa
      781 aaea
//
LOCUS       WP_175846964             235 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SGNH/GDSL hydrolase family protein [Burkholderia].
ACCESSION   WP_175846964
VERSION     WP_175846964.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Upton,C. and Buckley,J.T.
  TITLE     A new family of lipolytic enzymes?
  JOURNAL   Trends Biochem Sci 20 (5), 178-179 (1995)
   PUBMED   7610479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..235
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=24528
     Region          43..214
                     /region_name="FeeA_FeeB_like"
                     /note="SGNH_hydrolase subfamily, FeeA, FeeB and similar
                     esterases/lipases. FeeA and FeeB are part of a
                     biosynthetic gene cluster and may participate in the
                     biosynthesis of long-chain N-acyltyrosines by providing
                     saturated and unsaturated fatty acids, which it...;
                     cd01836"
                     /db_xref="CDD:238874"
     Site            order(53,90,118,209,212)
                     /site_type="active"
                     /db_xref="CDD:238874"
     Site            order(53,209,212)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238874"
     Site            order(53,74,118)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238874"
ORIGIN      
        1 mgypfataal gpllfaqgry vrrvtprlpe aagprdgvag egpplrvlvv gdsaaagvgv
       61 atqhdalsgq lanalaathr vswkllartg lttrelvdwl aaepaepfdv avtslgvndv
      121 tggvpparwl aqqaelvrll aarfrvghai lsavppmerf palpqplawy lglrakrlna
      181 alagwagtqp hctflrvdlp lerhlmaadg fhpgasacaa waaqvaasvr qraag
//
LOCUS       WP_175846992             222 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175846992
VERSION     WP_175846992.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..222
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23941
     Region          29..187
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpprhvqvpa ppgqpaaqpa palrrrprqs raqassdalq qafvqlller gyakatirei
       61 aavagvsigt fyeyfgdkqs laalcihrrv laladrlrdt vqrlrgvpra elaaalvdlq
      121 vdaiaadaal wgalfvlerq vsplaayrrh ydayvalwrd alahtadppp aerldglarm
      181 ahaicyggls qalltlgpal dfaaqrrelr tvllaylaaa da
//
LOCUS       WP_175846988             190 aa            linear   BCT 11-JAN-2025
DEFINITION  PadR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175846988
VERSION     WP_175846988.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 190)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..190
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=21190
     Region          5..97
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mstsrpspla lavlatltet pmhpygmlqq lkargydevv nvrqrtslyq tidrllrdgm
       61 itvhdterdg afpertlyal teaghtagqa wlhallaepa refpvfgagl aflplldaed
      121 arhqlelria rldaererle alrataqadq vprlfllqne halvllnael dwarsvvehl
      181 kigalrwvdg
//
LOCUS       WP_175847005             297 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia arboris].
ACCESSION   WP_175847005
VERSION     WP_175847005.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..297
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31910
     Region          29..290
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mnavpkkkgl grgleallgg saditeavki egapntlalg klqagkyqpr trmdegslqe
       61 laasiraqgv mqpilvrpis sdkyeiiage rrfraarlag ldevpvlvkd vsdqaaaama
      121 lieniqredl npleeahgiq rlldefgfth eqaaesvgrs rsavsnllrl lnlaspvqtm
      181 llagdldmgh arallavdga tqitlahqvv nkrmsvrete klvshttkea pavkarakdd
      241 ggrdtrrlee elsdllastv kiklgrrgrg qvlidfgnld alegilarlr gnvatee
//
LOCUS       WP_175847047             376 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: porin [Burkholderia].
ACCESSION   WP_175847047
VERSION     WP_175847047.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..376
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=40514
     Region          7..376
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkrktlalsi aaaglcagtq ahaqssvqly glmdlsfpty rthadangnh vigmgnegep
       61 wfsgsrwglr gaedigggtk vifrleseyv vangqmedsg qifdrdawvg iederfgklt
      121 agfqntiard aaaiygdpyg saklsteegg wtnsnnfkqm ifyaasptgt rynngiawkk
      181 lfsngifasa gyqfsnstaf atgsayqval gynggpfnvs gfynhvnngg ftnqtfsvgg
      241 nytfsivrln agyfryngdq gslgqrhdds wtvsvkvapp galdyelgyq qmrvknaann
      301 adgftpnanl gafsltngva ngfketlygs vfyhlskrte vylagdymkl hggytvsstf
      361 gaknqlelts girtrf
//
LOCUS       WP_175847110             206 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175847110
VERSION     WP_175847110.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22514
     Region          24..175
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msgieiakpl arrtrrpidg ataqehllra aeelfykegv rtvgveavve ragvnkmsly
       61 rqfsskdeli laylermdac fferldtsaa khpgqpkaql iqyfvdlaer atqkdyrgcp
      121 fvnvaaefpd ashparerva qnkeqlmkrl valcegagar qpqaladala lvvegiyaas
      181 qtyrhgetpi gtapalvtql ieaaca
//
LOCUS       WP_175847099             207 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: HAD family hydrolase [Burkholderia].
ACCESSION   WP_175847099
VERSION     WP_175847099.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..207
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23149
     Region          3..>172
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mtikavvfdf ggvlidwspe ylyrelipdd aerrwflthv camdwvirqd ggqtieegta
       61 ervaqfpahe alirafyarw hemiggvlee gaalvdrlea qgmplfgltn wsaqtfpyaw
      121 dnfpvlrrfk eivvsgrvkl vkpdpaiyhe mhariephlp giaphelvfi ddnaknaaaa
      181 talgwhgihh tsaastearl relgala
//
LOCUS       WP_175847117             306 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175847117
VERSION     WP_175847117.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33264
     Region          8..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(104,108,151,165,167,226,243,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(105..106,110..111,113..114,117,121,123..129,194,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mddflsphla lfvdvvdqqs fsaaarrlgv aassvtrrid rleaqlgirl lhrtthalrp
       61 teagqllygr atrmlaelrg lqedlhsqhd epsgllrvdc papfgrrhlm aalaafmqrh
      121 palqvdlvlt dsmvdlqgar lgadvdlavr igpledtrfv atvlapqrrv lcasgaylar
      181 rgapespdal aghdclawhg apppgawrfg errhvpaqpr frsnhseall eaaidglgla
      241 hlptwlagda lrdgrlhavl pqyaaapepa tihvlrqqar gsartsrlva flatwfaqpa
      301 wdaaws
//
LOCUS       WP_175847124             316 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia arboris].
ACCESSION   WP_175847124
VERSION     WP_175847124.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..316
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32726
     Region          32..314
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          211..314
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(216..217,250..251,254,258..259,262,304,308)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mhrtihvrra rlaaavspal aalfaaglvv sgaafaqntg atvtpvgngt vattalpqan
       61 pnagaasgtv vhgtagtitp ppanatpgqv vaggkvpdea tkaavlqklr dtygatnvvd
      121 qievgdvatp pnwsanvqkl lgaqlkqisk gqlkingtqi emkgevhnea qrqqlasdma
      181 ntlnptytik nglrvsaseq gvldqtlanr tiefetgsat ltpqgrlild qmaaalakmq
      241 nrtvdiight dnsgnrtsni alsqaradav kgylitksiq pqqmtttgvg pdqpiapndt
      301 adgrarnrri efrvgq
//
LOCUS       WP_175847168             308 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Burkholderia].
ACCESSION   WP_175847168
VERSION     WP_175847168.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..308
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33941
     Region          4..237
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msaieirhvk krykslqalk gvslsveege ffgllgpnga gkttlisila glaradegsi
       61 svrghdvvkd frgarralgv vpqelvfdpf ftvretlriq sgyfglrrnd dwidevmanl
      121 dltekadanm ralsggmkrr vlvaqalvhr ppvivldept agvdvelrqt lwkfisrlnr
      181 eghtivltth yleeaeslcd riamlrrgev valdrtdall rrfaglqlyl rlatgalpae
      241 lrglesdpaa rapgehllrl asyddveril aqcraagcsf deievrkadl edvfvqvmng
      301 adviegla
//
LOCUS       WP_175847256             369 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Burkholderia].
ACCESSION   WP_175847256
VERSION     WP_175847256.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..369
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39036
     Region          1..365
                     /region_name="LhgO"
                     /note="L-2-hydroxyglutarate oxidase LhgO [Carbohydrate
                     transport and metabolism]; COG0579"
                     /db_xref="CDD:440344"
ORIGIN      
        1 meqmdcvvig agvvglaiar elaargreti vleatdaigt gtssrnsevi haglyyprgs
       61 lkatscvhgr dllyafceth hvphrragkl lvatsaaqvk qlkaiaarav engvldlmpl
      121 traeaqtlep qlecvealfs pstgivdshq lmlallgdae rdgavcalks pvesidvlrg
      181 grfivrtggd apteidaacv insaglgaqa larrtrgldp rwvpplylar gnyfslsgra
      241 pfshliypmp draglgvhlt ldlggqarfg pdvewcdslr yevdparaga fytsirafwp
      301 glpddalqpa yagirpklag pgeppadfiv qgaaqhgvrg lvnlfgiesp gltaslalaq
      361 rvgemtayr
//
LOCUS       WP_175847260             215 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Burkholderia].
ACCESSION   WP_175847260
VERSION     WP_175847260.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..215
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22860
     Region          3..215
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtylpillqi avvylvaait pgpnffmisq lslagrrslg aasalgvgta svawatlaml
       61 glaavlhqve wlyeairigg avylvyfgfk llrsgvrrdt apadapdtta plaaphardy
      121 lrayrsglft cltnpkscaf wtsvfaamlp ahvplwfnga vlvtigvlsa gwyscvaylf
      181 aspraqrgyr rvrrpldalc gvalvglgak laadr
//
LOCUS       WP_175847313             126 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Burkholderia arboris].
ACCESSION   WP_175847313
VERSION     WP_175847313.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 126)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..126
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=13688
     Region          23..>80
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(33,36)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mpalnldtda driaerladp gtllvaclca ewcgtcrdyr tafdqladah pdacfawidi
       61 ethadrlddl dvenfptili edantarffg tvlphaaive rmlsdlsavp galhapklrd
      121 vlivea
//
LOCUS       WP_175847319             204 aa            linear   BCT 11-JAN-2025
DEFINITION  CGNR zinc finger domain-containing protein [Burkholderia arboris].
ACCESSION   WP_175847319
VERSION     WP_175847319.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..204
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22463
     Region          11..204
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mvtrseptpl ahtwgaadfv gghpaldfln tvadtgktrd edklvdwpav rawaepsgll
       61 apddlarllr hprldgpdel aalrrfrdda yaaivhltae gggsagaraa drlamairea
      121 igrsafdavg grfawrpdar easrwidaaa lgfeqlmrsd dfarvrqcgr ctwffvdrgr
      181 gvgrrwcdmr tcgnrakvea frer
//
LOCUS       WP_175847342             198 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Burkholderia arboris].
ACCESSION   WP_175847342
VERSION     WP_175847342.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..198
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=21467
     Region          4..135
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(9,11,72..73,76)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            11
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(71,116..117,119..120,124)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(77,82..83,112,115..116,119..120,123,126)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(101..103,112..113,116..117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(101,117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(125,131..132)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          147..188
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
     Site            order(148..150,182..183,185..187)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 msrtfayarv sttdqtaanq lreiesagfn vdkrrvvtec isgsvsaeqr pgfadllrrm
       61 eegdvllvtk ldrlgrnamd vratvealad rgirihclal ggvdltsaag rmtmqvlnav
      121 aeferdllie rtqagiarak adgkqmgrpa vlsnqqqadv rhalldgasv aslarrfsts
      181 rqtimrirda alaqqqaq
//
LOCUS       WP_175847365             420 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia arboris].
ACCESSION   WP_175847365
VERSION     WP_175847365.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..420
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44778
     Region          64..295
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mafskvlvgw maacalsaaq agtlpnantg sgslahaerf dysdanlpqv aadlneqilr
       61 ipadasgavt leatlfkpdg pgpfplvvfn hgknsgdlhl qprsrplafa refvrrgyav
      121 iapnrqgfag sdgtyqqegc nvgknglaqa advdatvrym shqsyvdasr ivvagtshgg
      181 lvsvaygtea asgvrgiinf sgglrqdlcd gwqrnlvdaf dqygahtavr slwlygdnds
      241 vwtpalvaqm hdayvshgtq aqfidfgryk ddahrlivdr dgvpvwwpav naflaqlnlp
      301 tgvryavanp hepkatgyas idavgavpyv deagregyrr flnqhpsraf avssegawsw
      361 aeggddpmal aldncakqga gacrlyavnd rvvwnasttq tadngndttr dtdtralasr
//
LOCUS       WP_175847370             547 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Burkholderia arboris].
ACCESSION   WP_175847370
VERSION     WP_175847370.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..547
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58317
     Region          13..528
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 maaatptgal valhhvsfrf ddgvtlfdsl dlsidrtptg ivgrngigks llaqliagrc
       61 apsagtierh tpvvyvaqqh dddaaanprt vaqiaaldap lgalahlang raephdfdli
      121 gdrwdlaerl rtaldaaglh dvhadtpaha lsggqlarva ligallsgag llvldeptnh
      181 ldapgrawlh aaldgwrggv vivshdrall agvqrivelt phgarsyggn yalyraqrda
      241 eqdaaqaald hartergrvr rrleqehdti qrhaaaslrd aktanlssma rqsrkgaars
      301 imghvrrhqd efkttlderv qqaaarvead apvlvslpgt evsarrqlft ldraqlpwhv
      361 agdadaitws asgavrialt gpngcgkstl lrmlagelap rsgactthvs aayldqrlal
      421 ldpersiveq lglldtplae gdlrsrlall qldatratqp arqlsggerl kaalacalwr
      481 gtpaqlllld eptnhldles vraieaalag fpgaivvash dpaflaalep thtmqwhhdg
      541 wryepvv
//
LOCUS       WP_175847393             436 aa            linear   BCT 11-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Burkholderia
            arboris].
ACCESSION   WP_175847393
VERSION     WP_175847393.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..436
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46549
     Region          64..423
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mrlspqglks lassiafgta arnvalgvml pvalastivv aeakpaakak aahaapaaeq
       61 ftgapatymp gavpppgvna rswvlvdats ntvlasgnad ervepasltk lmtaylvfea
      121 ldkkkismeq ivtpsdavrr vgrdesrmfi eankpvsvhd lvygmiiqsg ndaaialael
      181 vggsegqfvt lmndeaarlg mkgthfadvn gmpdpnhytt agdlaklsah lirdfpqyys
      241 ifsekefkyn nirqgnrnrl lwldptvdgl ktghtqaagf cliasakrai pgvdgqrrlv
      301 svmmgeqkeg ertqdsmkml nygysafdsv rlfkggqams tpriykgken tvqvgvkgdq
      361 watvprglgd kvktevdvng pliaplaegq qvgtvkvvad gktlsefpvv alqavpeagi
      421 fgriwdsill mfskkk
//
LOCUS       WP_175847405             378 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia arboris].
ACCESSION   WP_175847405
VERSION     WP_175847405.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..378
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40362
     Region          1..373
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfqhtedrr mladtlnrfi aeqyafpvrd riaqsaegfd ramwqrfael gtvgalfsea
       61 dggfggagfd iavvfeclgr glvvepflga llagralsla ggtahrdrla alidgsasaa
      121 fahdepgshy elttvrtrae rsgdgwvltg akgvvdqaeq aaffvvsarv sgqddeaagi
      181 glfvvpadap gvslrdyrki dggraaevrf ecvalsadaa lgthdgeaga ellervlgyg
      241 llalsaealg amdvakehtl eylrtrkqfg lpigsfqalq hrmadlllev eqarsavina
      301 aaqldaprvv reralaaakt tigrigtlva edsiqlhggi gmtwelplsh yakrlvmidh
      361 qlgdedhhla ryialskq
//
LOCUS       WP_175847443             303 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175847443
VERSION     WP_175847443.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33875
     Region          7..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..295
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(111..112,114..115,118,122,124..130,223..228,
                     234..235,237..238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mnthitlrqi eyfvsvadtg qisksanlcs vsqssmtial rkledavgvt lllrhpkgvr
       61 ltpagerflr hvqhatmsid ravsaaqedp eqisghvrig mtetisaylm pslmsaisrr
      121 fgnlsvsive sereaieeml vddrldiall lvsntaevgd lkyetmlrsp rrlwthpdhp
      181 lqdahrvtle dvarenylll dmdehlrtvg kywgsygitp nvwmqsksie avrslvalgq
      241 gvtilsdlvy rpwslegnri srrnlsvtvp tmdvgavwrr ggvtsapcra lldlfrswrr
      301 tae
//
LOCUS       WP_175847475             395 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175847475
VERSION     WP_175847475.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..395
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41119
     Region          22..389
                     /region_name="MFS_YajR_like"
                     /note="Escherichia coli inner membrane transport protein
                     YajR and similar multidrug-efflux transporters of the
                     Major Facilitator Superfamily; cd17472"
                     /db_xref="CDD:341025"
     Site            order(29..30,33..34,37,71,121..122,124..126,129,151,
                     154..155,158,221,224..225,228..230,233,260,264,308..309,
                     313,317,340,343..344,347..348,351)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341025"
ORIGIN      
        1 msnpsatssr mtapelratt slaaifalrm lglfmimpvf svyaktipgg dnvllvglal
       61 gaygvtqslf yifygwasdk fgrkpviatg lvifaigsfv aasahditwi ivgrviqgmg
      121 avssavlafi adltseqnrt kamamvggsi gvsfavaivg apivfhwvgm sglfaivgvl
      181 silaigvvlw ivpdaakpvh vpapfaevlh nvellrlnfg vlvlhatqta lflvvprllv
      241 dgglpvaahw kvylpvmgla fvmmvpaiiv aekrgkmkpv llggilaili gqlllgsaph
      301 tilivaailf vyflgfnile asqpslvskl apgsrkgaat gvynttqsig lalggivggw
      361 llkhggantv fytcsglvaa wliiaanmka pprka
//
LOCUS       WP_175847497             260 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein [Burkholderia].
ACCESSION   WP_175847497
VERSION     WP_175847497.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..260
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28432
     Region          12..193
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(15,17,98)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(42,97..98)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            96..98
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mstlhassth lvlipsynpg vkvdttvrna raqwnpvwvv vdgstdgsae rlqamaerdp
       61 glrvivlpen rgkgaavlag ldaaaasgft hvltmdsdgq hpadlipafm aasqaetdam
      121 vlgvpkfdas apqlrvqgrr lsnawadlet lwagigdsly gfrvypvapl aaimrrqpwm
      181 rgfdfdpeaa vrlcwagvrp iridapvryf grheggvshf hygrdnalla wmhlrlftgf
      241 avrlpmlvar rltrrrdqta
//
LOCUS       WP_175847511             312 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175847511
VERSION     WP_175847511.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..312
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32983
     Region          26..303
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mntpaspsap laaelhpatv appvldivar iaecapelre aerkvaafil adlaraahas
       61 igalardaev svatvtrfak avgcrdvrel kvlvaqaaav gqrflvpsdd apsddaspas
      121 mvydeirval ahnhqllrnt sfeaaadlla aakmtyvygq gggstalade lrfrlvrfgr
      181 pvasyqdsvl qrmvaatlsr dtvvvalsvs grvpellesc rlakrygakl iaitapaspl
      241 akladhlipv vafetdfiyk pstsryammm aidvlvtgva mrlgdagres lrrikhalda
      301 hrgggdrqpv gd
//
LOCUS       WP_175847560             416 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia arboris].
ACCESSION   WP_175847560
VERSION     WP_175847560.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..416
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43593
     Region          23..409
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtndrvmaiv gaghaggraa qvlresgwrg rivligaeah lpyerpplsk gvltggrsaa
       61 qcrlrdpdaw madgiepvvg tveridphvr evsvsggrvf scealllatg grarrlaipg
      121 atldgvfalr tlddaaalga rlvpdmrivl igggfiglev aasarmrgcr vtvldaaprl
      181 lgravpeaia trvhalheaq gvtirmnrtp vaiertsgga lavvlddgdm liadtvvagv
      241 giepadelar aaglavergi ivnaqletsa egiyaagdva vfpsvlsgrp vrqetwhgae
      301 tqarvaarnm lgagepyrdt pwfwsdqyda qlqvagepal gersvarvld ddaeihfhfd
      361 agarlvaasg fgrasgfike mrvarmlver gidvtpaava dvdvklkslv tagssr
//
LOCUS       WP_175847569             256 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: c-type cytochrome [Burkholderia].
ACCESSION   WP_175847569
VERSION     WP_175847569.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 256)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..256
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27426
     Region          43..134
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          140..228
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mesrvssrrl frpllavlmi ggaglmsaaq aqtkpteqeq ahaqqaplka pdtmaervrg
       61 ctachgvhgq gtdndyfprl agkpaeylyn qlvnfrdgrr kyppmnyllt ylnddylrei
      121 aehfsaerpp yptpakptlp aatlargkqi vtqgdpsrkl pacvachgag ltgmqpaipg
      181 lvglhadyls aqlgawrsgn rhakapdcmh diasklsded vtavtawlaa qpapanpvpa
      241 parsmktpla cgsepq
//
LOCUS       WP_175847572             115 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GFA family protein [Burkholderia].
ACCESSION   WP_175847572
VERSION     WP_175847572.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..115
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12786
     Region          1..>102
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mlyrgschcg dvkfeaegdl qgvmacncsi cqrkgalmwf vprdhmtlft pdenlatymf
       61 nkhvikhrfc krcgihtfge gvhpdgtama ainvrclegi dldalpvthy dgrsh
//
LOCUS       WP_175847603             304 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Burkholderia arboris].
ACCESSION   WP_175847603
VERSION     WP_175847603.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..304
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35090
     Region          85..242
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mrfdvellll alapvfllci aweawhlart raqdrvyawr dtlcnaalal mhqaadkiaw
       61 lfvipvyayc yqhyrlftwh dswlsfavlf vaqdflyyvf hrashrvrwl waahvvhhss
      121 ermnfstafr qslmypvagm wvfwlplafa gfppqqvvgi vlinlafqff vhtqaigklg
      181 wleyvlntps ihrahharna ryidrnyagv lviwdrlfgs yveethddpp qygiverlgs
      241 nnplvatfhe wgsmaadalr vdgwrnklra ilgppewasa yhaqiteaan qdprtvplaa
      301 ardq
//
LOCUS       WP_175847608             119 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DUF427 domain-containing protein [Burkholderia].
ACCESSION   WP_175847608
VERSION     WP_175847608.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Lupas,A.N., Zhu,H. and Korycinski,M.
  TITLE     The thalidomide-binding domain of cereblon defines the CULT domain
            family and is a new member of the beta-tent fold
  JOURNAL   PLoS Comput Biol 11 (1), e1004023 (2015)
   PUBMED   25569776
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..119
                     /product="DUF427 domain-containing protein"
                     /calculated_mol_wt=13044
     Region          6..113
                     /region_name="COG2343"
                     /note="Uncharacterized conserved protein, DUF427 family
                     [Function unknown]"
                     /db_xref="CDD:441912"
ORIGIN      
        1 msdaadprle ivpnrhrvrv ihrgityads hgaltvretg lpdihylprg dvnmrrlvks
       61 gtttacphrg qavhfdlqte dgvienaaws yeepneaasv lahyvafdaa ridslvets
//
LOCUS       WP_175847621             316 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Burkholderia].
ACCESSION   WP_175847621
VERSION     WP_175847621.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..316
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33281
     Region          85..291
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mshvpldpga arvvalares gasgpeagsp eqaraafrks rkalasqpvq issvrdlevv
       61 hpdgkfglrc yrgwgtddgs qlpcllffhs ggwvsgdldt hdnacraias tarisvmavd
      121 yrlapehpfp aaiedaqaay ayilehassl nidatkiavg gdsaggnlaa vlthilrdag
      181 ghqpiaqvll ypatdfaadt asleqfslgp tltkasldwf adqylpaged rldwkasplr
      241 aptfaalpaa yvvtcghdpl cdegaayaar lrdagvsvrh qhypgqihgf ltmgglipes
      301 tvligevavf ldqvfs
//
LOCUS       WP_175847628             198 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175847628
VERSION     WP_175847628.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21886
     Region          10..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 martrnenlh qqrreqvlaa atrvfkakgf hgartedica aadmsagavf ryfadkremi
       61 daiivaever ytqdverfln reglmrlari tadelagmtg qtegglgvds wlelardadr
      121 rpdfvaldrk lraefarvla sgqadgwvrp sldpvgaani vfslfngmwl dqslgtacdl
      181 ehmaaalgdf frtyvlvs
//
LOCUS       WP_175847655             305 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: dihydrodipicolinate synthase family protein
            [Burkholderia].
ACCESSION   WP_175847655
VERSION     WP_175847655.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..305
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33008
     Region          4..297
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mnaryqgvfp vvptifdayg aldldgqrrc ldfmidagsh glcihanyse qfalgdderd
       61 litrltlehv agrvpvivtt shfsaricae rnrqaqalga amvmvmppyh gatfrvpeaq
      121 vraffrevad gldiplmiqd apasgvalpa sllaslarei davsyfkiet agaasklrel
      181 ialggdaveg pwdgeegitl ladldagatg amtgggypdg irritdayfa grrdeaceqy
      241 arwlplinye nrqagfltak almkeggvia cdqprapwpe lhpqvrsgll daarrldplv
      301 lrwgr
//
LOCUS       WP_175847678             424 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175847678
VERSION     WP_175847678.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..424
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46119
     Region          9..403
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(21..22,25..26,29,61,111..112,114..116,119,139,
                     142..143,146,228,231..232,235..237,240,268,272,330..331,
                     335,339,354,357..358,361..362,365)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mklfratsiv lvmlcvmyfi tyldrvnvst aaagfgrefg lnkteiglvf safaypylvf
       61 qiiggwvsdr fgarrtllac gllwavatll tgmagglasl laarlllglg egatfpaats
      121 amsrwvprek rgfaqgitha fsrvgnavap aavvavmavy gwresfyicg visivwvavw
      181 alvytehpkd hpritqaela alpppkqkpa tvpwgplfrr mmpvtivyfc ygwtlwlfls
      241 wipqyflhsy nldlkksavf asavffagvi gdtlggivtd rvyartgslk rarswmvsic
      301 mlftllsllp llfthslyvs maclaagfff aemtigpmwa vpmdiapeys gtasgmmnsg
      361 salaailspv isgyvidrfg swelpfigsm vlmgvgvlla frmqpdnrfa dapaeqpapn
      421 rspa
//
LOCUS       WP_175847680             356 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: porin [Burkholderia].
ACCESSION   WP_175847680
VERSION     WP_175847680.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..356
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=37411
     Region          21..356
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mpihstriag rrrrllsavg asliactiad dataqssvsl ygladvyagt qkslgkpray
       61 amnsggftts fwgiggreel gggyalqfal eafmrpsngg agrfigdtff grnayvgvat
      121 pygvmragrn ttpyyisvvr fnpfstsfgf spalnqmykg vagqglvgdn gwsnsvlist
      181 pgehalqasl iyatgnepgh tganqwggsi tydahrafsa tlafqqakfd rtpgdlnasi
      241 agftqqdavl agvgydlkvv kftafyqyvh daidggglgt hsgqvgaavp igfgtvlasv
      301 maakshgrdr psrttwalgy dyrlskrtdv yvaylrdras gygngdsagl glrtaf
//
LOCUS       WP_175847685             363 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DUF917 domain-containing protein [Burkholderia].
ACCESSION   WP_175847685
VERSION     WP_175847685.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..363
                     /product="DUF917 domain-containing protein"
                     /calculated_mol_wt=37364
     Region          1..362
                     /region_name="COG3535"
                     /note="Uncharacterized conserved protein, DUF917 family
                     [Function unknown]"
                     /db_xref="CDD:442756"
ORIGIN      
        1 mgrilsskdv eaavkggsvf acggggwadh grelgtlavt igrpelvsid elpddawiat
       61 aaaigapggl tdwqmlgady vkaaqlvqda lgeplaglii gqngmsstln awlpsallgt
      121 kvvdavgdir ahptgdmgsl glasstapmi qaaaggnraq haymevvvrg atarvspvlr
      181 kaadmaggfi ascrnpiras yvrqhaalgg isralalgea iidaerrggs avidaicaat
      241 hgeiiasgkv erntleytre afdvglvylg sgaqravihv mnehmavdda hgeriatypd
      301 vittldaqgr pvsagqlkeg meihvlrvek ahiplsssvf dpavyppvea algisiadya
      361 lvr
//
LOCUS       WP_175847714             339 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sterol desaturase family protein [Burkholderia].
ACCESSION   WP_175847714
VERSION     WP_175847714.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..339
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38913
     Region          99..255
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mptelmtwlh aflgndvdwk qvlligmtpv fliafaieya vmtgrgrrep frwkeivanl
       61 slgagyqvae tvmgllftga ifawvyrhrl fdvpvngfti vpifvlvefc yywfhrtshr
      121 vrwfwaahvp hhsgevmnft tamrqsllna fvgvfvfylp pvwlgippav vlfllavdla
      181 yqyfvhteai grlprwfecv fdtpsnhrah hgrnpryidr nyggvliifd rmfgtyveet
      241 esvdygitqq iisynflvln vhefvdmwrd vfapgpvlqr lkhlwmppew erpghrpiht
      301 wsverkgeea gaaiphaapv deaaasgrki vqatgtrpg
//
LOCUS       WP_175847758             164 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: arsenate reductase ArsC [Burkholderia].
ACCESSION   WP_175847758
VERSION     WP_175847758.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Messens,J. and Silver,S.
  TITLE     Arsenate reduction: thiol cascade chemistry with convergent
            evolution
  JOURNAL   J Mol Biol 362 (1), 1-17 (2006)
   PUBMED   16905151
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Mukhopadhyay,R. and Rosen,B.P.
  TITLE     Arsenate reductases in prokaryotes and eukaryotes
  JOURNAL   Environ Health Perspect 110 Suppl 5 (Suppl 5), 745-748 (2002)
   PUBMED   12426124
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Messens,J., Martins,J.C., Van Belle,K., Brosens,E., Desmyter,A., De
            Gieter,M., Wieruszeski,J.M., Willem,R., Wyns,L. and Zegers,I.
  TITLE     All intermediates of the arsenate reductase mechanism, including an
            intramolecular dynamic disulfide cascade
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8506-8511 (2002)
   PUBMED   12072565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..164
                     /product="arsenate reductase ArsC"
                     /EC_number="1.20.4.4"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030612 - arsenate reductase
                     (thioredoxin) activity [Evidence IEA]"
                     /GO_process="GO:0046685 - response to arsenic-containing
                     substance [Evidence IEA]"
                     /calculated_mol_wt=17371
     Region          4..143
                     /region_name="LMWP_ArsC"
                     /note="Arsenate reductase of the LMWP family; cd16345"
                     /db_xref="CDD:319973"
     Site            order(9,11..16,112,114)
                     /site_type="active"
                     /db_xref="CDD:319973"
ORIGIN      
        1 mttnililct hnsarsvlae gmlnhwagkl gkdvraysag sapsgrlnpf alealtkagi
       61 dvdgyrsksw dafvgegape mrivitacds aaaetcpywp gspvkvhwgy adpsnatggd
      121 egkrvafelt rqaigyrmlq llalpvdrms daelqaalta isqc
//
LOCUS       WP_175847856             330 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Burkholderia arboris].
ACCESSION   WP_175847856
VERSION     WP_175847856.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..330
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34789
     Region          6..301
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(37..38,41,93,108,110,139,172,261,264,300)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(230,235,251,261..263,266,288,292)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mkaaldvvty geamamfvat epghlahagq ftkriagadl nvaiglsrlg frvgwmsrvg
       61 rdsfggyvld tlaregidas cvtvdprypt gfqlksrndd gsdptveyfr kgsaashlsc
      121 ddyvadyvlg arhlhltgva paisatscel afrlaremra agktisfdpn lrptlwpsad
      181 vmaktlnala tladwvlpgv aegrqltghd tpadiagfyl aqgargvvik lgaegayfrt
      241 adgregtvag ervgrvvdtv gagdgfavgv vsallegrsi eqavargnri galaiqvigd
      301 seglptreal drlenvsnri drleeivtaq
//
LOCUS       WP_175847842             302 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [Burkholderia].
ACCESSION   WP_175847842
VERSION     WP_175847842.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..302
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31411
     Region          76..282
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mtkrslaala asmlmsvavv dgfvapqlah aqasgaagta aqaaapsaap apapvavepv
       61 pppapaatva venpyglgal wkngdfvarf vlillvimsm gswyimitkf leqlranrra
      121 kmadaqlwta pslaegarll deaspfrfia etaieagehh edalleavdr ntwidvsver
      181 sitnvsnrmq dglaflatvg stapfvglfg tvwgiyhalt aigiagqasi dkvagpvgea
      241 limtaiglav avpavlgynf lvrrnksvme rvrnfgaqlh tvllagnrrp vraaspaasl
      301 an
//
LOCUS       WP_175847858             297 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175847858
VERSION     WP_175847858.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=30997
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mtpdqlitfa avaehlnish aavalhlsqp avsgqlrllq defgeplyqr dgrgirltpv
       61 geqlaqyaka qrdtfaqara frdavrglea gtlrigastt pasyllpyli aafqplaprv
      121 tiqtmsgnts dvvaalpsld ialiegppge alppgtavha whedeivaiv paghplaapg
      181 ydagvtldal aahplvlrea gsavrqlver afahggapmr vafeiagvea vkeavragmg
      241 vgfvsamslr hqdaalvlrs lapapltrhf silvphggap srvaaqfldm slaqdla
//
LOCUS       WP_175847861             206 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175847861
VERSION     WP_175847861.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23215
     Region          9..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkpqrltreq srdqtrerll kaahriflkk gyvaasvedi aaaagytrga fysnfrsksd
       61 lllellerdh sevqadfeai fegggtreqm esmslayyrt lfrddeysll wgeaklqaar
      121 dakfrvrfnq flhgkrvqma efiqrfaera gtplllpadt lafglmclcd gvqsyytadp
      181 qhvsadvaes vlagffarvv lgrapd
//
LOCUS       WP_175847865             342 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175847865
VERSION     WP_175847865.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10859374
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..342
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38668
     Region          3..98
                     /region_name="HTH_NolA-AlbR"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators NolA and AlbR; cd04788"
                     /db_xref="CDD:133415"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133415"
     Site            order(51,54,58..59,68,80,84,90,94,97..98)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133415"
     Region          <259..336
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 mrlkvgelak rsgltvrtlh hyhaiglltp saradngyrl ydrhdiarlh qiqalrrfgl
       61 slteigdhln qpgtplvelv akqialldrq laqtarlrer lvnlhaqlaa gtepeladwl
      121 ttlelmtvyd kyfseeelar mpmyrksqag daewialvge vhalheagvp aederarala
      181 srwmallvrd tnndprllak lnlmhehepa mqskigista lrdyvlrass etkmrifeky
      241 lapdeiqfmr ahygeramew pqlmgdvrda ietgtkpdsp qgralaqrwl elfcsyaghd
      301 pathakfrqa lvnepsltkd swtdetligf vreamaqlap ar
//
LOCUS       WP_175847875             386 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Burkholderia].
ACCESSION   WP_175847875
VERSION     WP_175847875.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..386
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41787
     Region          25..386
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mnsqsgapva gapfsvsssg adaraenfvq ivdvvkkfgd teavrsvnlt vrqgelfall
       61 gssgcgkstl lrmlagletv tsgkilidge dlaqmppykr pvnmmfqsya lfphmsvesn
      121 vafglkqegt pkselkerva salelvqmsk yakrkphqls ggqqqrvala rslvkrpkll
      181 lldepmsald kqirqrtqie lvnilnkvgv tcimvthdqe eamtmanrla vmsegqivqi
      241 gspnevyeyp nsrfsaefig stnlfdgvtv edepdhvyie spelpsrlyv shgisgplgm
      301 pvtvsvrper ialtrkppeg afnwargkis nvaymggysl yhvkldagkt vianvsslai
      361 seldtpalgd eiyvrwsata gvvlts
//
LOCUS       WP_175847790             158 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: molybdenum cofactor biosynthesis protein MoaE
            [Burkholderia].
ACCESSION   WP_175847790
VERSION     WP_175847790.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..158
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=17139
     Region          1..143
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 matvrvqadd fdlnaevaal rarnpkigav acfvgtvrdl negdsvaame lehypgmtek
       61 alekiaaeag rrwpgidvai vhrvgkllpl dqivmvatva shrgdafasc efvmdylkte
      121 apfwkkettp dgerwvdars tddaalarwg vesgntpr
//
LOCUS       WP_175847910             155 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: nucleoside deaminase [Burkholderia].
ACCESSION   WP_175847910
VERSION     WP_175847910.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..155
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17701
     Region          2..136
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mdfvkrtidl amknveeggr pfatvivrdg eivaespnlv aqtsdptaha eilavrdacr
       61 klgtehltdc eiyilaspcp mclgslyycs pkrviyittr edyapfyrdd rkyfeldtfy
      121 aeyakpiaer rlpmvqqkhs gaidvyrrwq elnak
//
LOCUS       WP_175847939             327 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: aldo/keto reductase [Burkholderia].
ACCESSION   WP_175847939
VERSION     WP_175847939.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..327
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35464
     Region          10..307
                     /region_name="AKR_AKR13C1_2"
                     /note="AKR13C family of aldo-keto reductase (AKR);
                     cd19078"
                     /db_xref="CDD:381304"
     Site            order(19..21,52,57,82,123..124,153..154,173,201..207,258,
                     275..280,283,286..287)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381304"
     Site            order(52,57,82,123)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381304"
ORIGIN      
        1 mqkralgnsg levsaiglgc mglsygygpa tdkasgiali raafergvtf fdtaeaygpf
       61 vneelvgeav apfrdqvvia tkfgfengea mkgvdsrpsh irevadaalk rlkvdridlf
      121 yqhrvdpnvp iedvagtvkd liregkvahf glseageqti rrahavqpva alqseyslww
      181 repearilpt leelgigfvp fsplgkgflt gaidanttfa dndfrnvvpr fseenrkana
      241 glvdllgria tdkgatraqi alawllarkp wivpipgttk lhrldenvga aavvltaddl
      301 aaieaalqqi rivgerypsh lqqrvdr
//
LOCUS       WP_175847974             199 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FMN-dependent NADH-azoreductase [Burkholderia].
ACCESSION   WP_175847974
VERSION     WP_175847974.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..199
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21567
     Region          1..197
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 marilalkss ingnqsqtat lidtflaqrq anghtdeviv rdlvgddlpv ldselfhalr
       61 gaenpgeraq qaialsdkli aelkrsdlll igapmynhnv ptqlknwfdl vararvtfry
      121 tetypmglve gvsaivfssr ggvhvgeatd avtpylravl glmgivdvef vyaegldmkp
      181 hgfnaglena rrqmaalha
//
LOCUS       WP_175847967             294 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175847967
VERSION     WP_175847967.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..294
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31429
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mlldnlalfl rivekgglaa agrevglspa tvserltale rhygaalltr ttraisltde
       61 grtlvdgarr llaeadeles rvrlgvqtls gpvrlsapad lgrervvpvv daflaehpgv
      121 tvdlhlgdgy vdlvgqgldf airrgtlads slrsrslgra rrvvcaspay laahgtpthp
      181 ddlaahdciv mrfgqemyae wpfsidgepk rvmvrgrrva ndgalvrawc vaghgialks
      241 lvdverdlas galvevlrdf spgevdlqiv ypggaaqprr vralierlan alta
//
LOCUS       WP_175847988             318 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sugar kinase [Burkholderia].
ACCESSION   WP_175847988
VERSION     WP_175847988.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..318
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32909
     Region          3..296
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(36..37,40,91,105,107,136,168,256,259,295)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(227,232,247,256..258,261,283,287)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 maeivvagel laefvaaerg qgfdspglfa gpfpsgapai fadqaarlga rvayagcvgr
       61 dafgdaivar lerdgvdvar irrvgrptgt afvayrddgs rsfvftlsts aaacvdasdv
      121 dsamfdgcry fhvmgsslts esaiaavqrg vieaaragak vsfdpnvrpe mlsfrpmraa
      181 ldqmlaachl flpseadlpf fcgpqpaera iagllathpl lervvlkrga qgsvafdras
      241 rvdapafpvd etdptgagdc fggtlvaslv agvpidvalr ranaagaiav trrgpmegns
      301 saaeidrflt ergiacpa
//
LOCUS       WP_175848006             169 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: flavin reductase family protein [Burkholderia].
ACCESSION   WP_175848006
VERSION     WP_175848006.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..169
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17868
     Region          10..165
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 msranppdfd aaafrqalgq fatgvtvitt rapsgqligi tassfnsvsl npplvlwsla
       61 hksastpvfr gnshyvvnvl aasqldlckr fstykgdrfe giahaagnsg mpvldgalaw
      121 fechnrsryd egdhvifvge vercgvravs dtapplvfhg ggfhgltpl
//
LOCUS       WP_175848018             293 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia arboris].
ACCESSION   WP_175848018
VERSION     WP_175848018.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..293
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31330
     Region          13..270
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mtdsikallk phvrdignlq vrrtlpalaa rlvgpfiffd hmgpatlpag tgldvrphph
       61 iglatvtylf dgailhrdsl gslqaivpgd vnwmtagrgi vhsertpdaq rasghtvhgi
      121 qtwvalpqah ettepsfehh padtlpkrne dgvsltviag dafglrspvt tfsrtlyvaa
      181 efaaggrlel dasheertvy vvdgelaidg tpvpaeqmav lapgaavtlt sgsgaramll
      241 ggdkingerf iewnfvassr daierakaaw trqemgkvpg etewiplpes kpr
//
LOCUS       WP_175848069             235 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia arboris].
ACCESSION   WP_175848069
VERSION     WP_175848069.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..235
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25063
     Region          18..228
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mpsplapylp qieanpwfaa lpsalradll agavlrrlpa ghalfrrgdp pcglyavlag
       61 sltigavdpq gkealltvae pvtwfgeial fdgqprthda ialddalllh vpqaallail
      121 datppywrqf allmaqklrl sfltvesmsv mpaaqrlavr llmiaegygg isagrtrvrl
      181 sqetlasmls itrqttnqll kalqadgvvr lhvgeielvd idalrrasgl gdgth
//
LOCUS       WP_175848120             717 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 28 protein [Burkholderia arboris].
ACCESSION   WP_175848120
VERSION     WP_175848120.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 717)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 717)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 717)
  AUTHORS   Abbott,D.W. and Boraston,A.B.
  TITLE     The structural basis for exopolygalacturonase activity in a family
            28 glycoside hydrolase
  JOURNAL   J Mol Biol 368 (5), 1215-1222 (2007)
   PUBMED   17397864
REFERENCE   5  (residues 1 to 717)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 717)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..717
                     /product="glycoside hydrolase family 28 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73390
     Region          194..621
                     /region_name="Pgu1"
                     /note="Polygalacturonase [Carbohydrate transport and
                     metabolism]; COG5434"
                     /db_xref="CDD:444185"
ORIGIN      
        1 mtsplsrpnr rpralgllaa llataaalta cggddsstgg gvastappat svfqvgtttv
       61 danlpaepal padtqvcgtl eaantlvsrp dgslppeadp stagvgkava aatanpdqar
      121 iqaaldacga avdaevgati aaadvaataa qkaaavpnan lagasgeela kpkyraskfa
      181 vrlvvnhags gngfisgplt lpsgvtlwid kgvtlyasrd vkayspnaag pycgntavsa
      241 tkagsssnca alitgtnlvn aavvgdgrid grgyaelvts dakyplmkvd ltcsntyaay
      301 kggtvapdgt acddggtvvd skstvrnmtw wdlaylgnmv qngttgfgsq snfrlmvfny
      361 aknltlyrit lnnspnfhvv psgvdgltiw nvkvqtptla afanpagngn plyngqtfna
      421 dnvkntdafd pgsaskptsv alstgsttts aaavsfdgyl knfvfaynyv stgdddialk
      481 gsnnpapags glfgidgnrd vradrkwgvv iahnhiywgh gisigsetng gvtnvqvydn
      541 afqdseeglr iksdyargge vsnirysnic irdaknallf tpyystkavp asgplypnfh
      601 dislanvvie gtagvklqgf eantggygep afplvmslsd vvadtpdgis tiasdanltl
      661 hnvnlpvfps tanrvvvngt avhtidpasv ldcskafvdf pgidqsnpfg stwapal
//
LOCUS       WP_175848138             424 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia multivorans].
ACCESSION   WP_175848138
VERSION     WP_175848138.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..424
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41686
     Region          5..>327
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mrshadspaa hhggsltifq gaalyigavl gtgvialpal aadvagpasl lawaalvvls
       61 aplaatfaal garypdaggv styarrafgp kaaaivgwcf yfavpagapa aamfggayva
      121 avtgggqttv iataaaliai vsaanafgvt vsgrmqlvls allvtlllaa vlasaphart
      181 anlhpfaphg wlavgqaaal lvwsfagwea ithlaaefrr pahdmprsag iavvvvglly
      241 lsvaaasvmv lgpsagasga plaeliaggi gghaqvlata aallltlgtm nayfagaakl
      301 gaalgrdgal pawlaqgsqv ggvprrslga iavlaaaala attlagvgpt plvlvtsgcf
      361 vmvyglgaaa alkllprgsv ayrcawisli avaglfvttg wyvvcpllla ggallylrmt
      421 vrrg
//
LOCUS       WP_175848147             201 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia arboris].
ACCESSION   WP_175848147
VERSION     WP_175848147.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..201
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20643
     Region          1..190
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mnllhidssi lgqgsvsrel saeivatlra rdpgltvtrl dlaatpighl taghlaaaqg
       61 apvddalqad vetgqralda flaadivvvg apmynfgias qlrawidril vagktfryde
      121 ngavglcgak klviassrgg vysagspvas ldhqetylkd afgfigitdi tfiraegvam
      181 gpdkrsdaia sakeavaala a
//
LOCUS       WP_175848173             205 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Burkholderia].
ACCESSION   WP_175848173
VERSION     WP_175848173.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..205
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22225
     Region          4..200
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mefltlsalp agmlfalvts vtpgpnntml lasgvnfgfr rtmphlfgis igvailmlcv
       61 gfglgeafkr lpllytilea asvayllyla wrigtsgevk ahgakprpmt fveaaafqwv
      121 npkawmmvlt aattvrlsad ygmnaawmsv vfiligfpci clwaafglgl rrflsnpral
      181 rifnvtmavl lilslyplia hllpq
//
LOCUS       WP_175848188             155 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Burkholderia].
ACCESSION   WP_175848188
VERSION     WP_175848188.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..155
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16301
     Region          1..144
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mykrilvavd gsdtsrhafd aalalakahg aelqpfyvve naaiyynvpg ydpsvlrdql
       61 vaqgnalaqd faklmqaagv kgetrlneat slndvsslil dgatafgadl lvlgthgrrg
      121 frrlvlgsia eqcvrhatlp vllipaaanv deqaa
//
LOCUS       WP_175848197             521 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GMC family oxidoreductase [Burkholderia].
ACCESSION   WP_175848197
VERSION     WP_175848197.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..521
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=55520
     Region          1..521
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 metydhivvg ggsagctvah rlvkagrrvl lledgpkdds lfiripatfi rvlgtqrtvt
       61 fesepqpgaa grktyvpqgr tlgggssvna mlyvrgtrdd yddwaalgca gwgwddvlpv
      121 fkraeshlrl sepfhgtdgp lkvgdtrfrh plslafvkaa qetgiayndd fngaaqhgvg
      181 fyhttifdgq rgstaatyla dalthpnlrv ltgcrvtrir fdgrratgve wrteggatgs
      241 aaaradvvla agalstpkll mlsgigpgah lsahgidvlh dsrdvganyq dhlevsiygr
      301 shapvsllge drglkalrhg lqwmlcrtgl ltsnvvesga fvdttgsgrp diqfhvlptl
      361 vgdvdraplp ghglsinpcl lrprsrgsvq lrsndpaapi lfdsgalsdp advdglvrgv
      421 alarqiirap slarivreae tltdaalady vrhraktvyh pagtcrmgnd adavvtprle
      481 vqgvdglric dasvmprivs gntnaptimi aercaefmla e
//
LOCUS       WP_175848203             434 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175848203
VERSION     WP_175848203.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45420
     Region          7..406
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mtsptssrsa wtyenrllli lfmtfgfvff drlalsflfp fmsaelhltn tqlgmvssal
       61 altwalsgaa tgawsdargt rkplliaavl gfsvcsalsg lvggfaslia fralmgiaeg
      121 pvlplsqslm vesstpsrrg lnmgllqgsa agllgamigp pvvigiatay gwreafyvsc
      181 ipgfliafci wrwvrevppg garhaqadga gapaasgavi nrwallkern illcvliscf
      241 fltwfvviis fapvflvesr hlspsdmgvv mtclgaawvf wgfavpaisd rvgrkptmiv
      301 faliaavcpi vlihvgsvwa lgalvfvtyt glgcftlfma tipaetvppr aiasalglim
      361 gageliggfv aptvagfaad kyglqfamwt satgailacv lsfglvetap avlrkralag
      421 aaagrldtqn lggr
//
LOCUS       WP_175848211             468 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia multivorans].
ACCESSION   WP_175848211
VERSION     WP_175848211.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..468
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47212
     Region          33..450
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(34..35,38,70,120..121,123..125,128,148,151..152,155,
                     277,280..281,284..286,289,317,321,373..374,378,382,398,
                     401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mselaspaga aepavnwram aavllavala tldtaianta lpaiatdlha spaasvwiin
       61 ayqlamvatl lpfaslgdiv ghkrvyvggl avftlaslgc alastlpqlt aarivqglga
      121 saimsvnial irnlfpahrl grgvgfnalv vgvsfavgpt iaslilsaaa wpwlfavnvp
      181 lgvlalavai pslpeavrgk hafdplaalf nviafsalif algefaqrgp lrvvlaaaav
      241 afafgallir reaghpapml pvdlfrrpvf alsavtavca faaqglafvs lpfyfetvlh
      301 rsavdtgflm tpwsavvala apiagrlsdr yppgllgaig lallgagmas laalpaapsa
      361 idigwrmmlc gagfgffqsp nlkalmssap persggasgi igtarligqa tgaalvalsf
      421 giaghhgptl alvlgaafac aasvasglrl farshragva vaserapk
//
LOCUS       WP_175848229             236 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: PadR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175848229
VERSION     WP_175848229.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..236
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25678
     Region          82..161
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mrhnhfrgha rcdghgtqal pdgfaglwya igrhrrghda fgggpfggrg grggfgdfgd
       61 dgmprgrqfs sddlqlllla lvaeqpshgy elikaldtrs ngfyspspgm vypaltylee
      121 vgfvasqaeg nrkryaltda grahldaqre rvdtlfarlt hlarkmefmr rafagesagn
      181 eaqdesqpgw lpefvearla lkrallhksa adadeqrria aimrrataei eggsga
//
LOCUS       WP_175848279             788 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia multivorans].
ACCESSION   WP_175848279
VERSION     WP_175848279.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 788)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 788)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..788
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..788
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85682
     Region          70..770
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mlltlaarpt rgrlalacaa afalpgayaa ssdsaptdpv rdpanrsars vvpaasavsa
       61 aaaepagdtl savsvtaqrq pldpdtpavv esmtreridt htnvttedal kyapnlmvrk
      121 ryigdrnsvf agrdfnelqs arglvyadgl llsnllgssy aypprwslia pddsarvdvl
      181 ygpfsalypg naigstvllt trrpdkleas lstqfftqry rdgygfadsf ggnhqtaria
      241 nrigrfwfsl sldrlendgq pmqyaspnas ynaklgravp vtgaatdigp ngkartivga
      301 qslerteqin etvrmgyaft drvdatltlg hwenhyrqhg dtflrdaagq pvyggnvaig
      361 gqnltiapga fapqrgdqen wlyafglngr lasgwrlsgi vsaydvsrdv lraastaqgg
      421 agtlfqgdgt gwrtldlkae apevhghaft fgyhydnyfl rnvtyntadw lngpvtslas
      481 vyrgdtrtqa lyaqdawrfa pgwlatlglr yerwdaygga lgnasgtfgy adrsanalsp
      541 kvalqwdatd vwrfrlsfat gtrfptvgel fqgtisnnai vnnnpnlrpe kaidwdftae
      601 rdvgvgvvra svfqsdlrds iysqttvaga stvtnisnvd rvrvrgvela fsgenvglkg
      661 laidanvsas naqiladaan payvgsrfpr iprmranlla syrfdehwla svgvrysgrq
      721 fntldnsdvn pdvyggtsaf tvvdvkaryr fdrhwtasvg idnltdrryy vfhpypgrtf
      781 ygelkwsl
//
LOCUS       WP_175848313             390 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: mechanosensitive ion channel family protein
            [Burkholderia].
ACCESSION   WP_175848313
VERSION     WP_175848313.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..390
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42420
     Region          83..339
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 misieelqri adaplhswlg tlavsvivil vvtvahrlga rivkriaqpy plmsailryi
       61 dkpslvvlal laleflwvqa ddgmsfvrgm rtaaavgsiv sltwllvrla agvgdaiiqa
      121 hpidtadnlq arrihtqarv lvrtvmvliv iigtgaalmt fpnvrqvgas llasagvagl
      181 vagiaarpvl gnliaglqia ltqpiriddv vviqgewgri eeitgsfvsv rlwdqrrlvv
      241 plqwiienpf tnwtrsssei igtvylsvdy rtplaplree larlvhaape wdgrvqvlqv
      301 tdatertmql ralvsaadss scwdlrcrvr egliaylqdr ypqclprsrm elyphesapd
      361 apnperphar apaastaant aadpqaaegr
//
LOCUS       WP_175848421             281 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia arboris].
ACCESSION   WP_175848421
VERSION     WP_175848421.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         1..281
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30089
     Region          6..258
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(20,104,106,108..109,137,190,211,214,227,229,258)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mieecqigef tlitlldgif lcgtemiqaa aspegeelfk naglpasgps pepinafalk
       61 rnnelwlida gcgrelgprf gkaadalcsa gysldqvqgv ilshlhedhi gglikddgta
      121 lypnatlfls eeelafwtda tsptkyprma daglfklats vlrsyegavq aikageqvip
      181 gvhliplhgh tpghsgvqie sgdqqvliwg dvihstllql ryphwsigfd vdpaqavqtr
      241 eqllarlasg ntlvagphvt gigkirscch ggykldltky r
//
LOCUS       WP_175848392             649 aa            linear   BCT 11-JAN-2025
DEFINITION  arylsulfatase [Burkholderia multivorans].
ACCESSION   WP_175848392
VERSION     WP_175848392.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..649
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=69391
     Region          47..615
                     /region_name="PAS_like"
                     /note="Bacterial Arylsulfatase of Pseudomonas aeruginosa
                     and related proteins; cd16025"
                     /db_xref="CDD:293749"
     Site            order(57..58,95,156,158,263,406..407,466)
                     /site_type="active"
                     /db_xref="CDD:293749"
     Site            order(57..58,95,156,158,263,407,466)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293749"
ORIGIN      
        1 msmsasrsvp frlrvvcaia agalslascg gvdgnpppla datpsakrpn ilyimaddlg
       61 ysdihafgge intpnldalv asgrilsnhh tgtvcaitra mlisgtdhhl vgegtmgvpt
      121 derrglpgye gylndralsf aqllkdagyh tyiagkwhig sgivgsatgs gqtpdqwgfe
      181 rsyvllggaa tnhfahepag ssnytedgry vqpgqpgqpg gtggnpavfy stnfytqkli
      241 qyidsnhsdg kpffayaayt sphwplqvpd pwlhkyagvy dagydairna riarqkalgl
      301 ipadfkpfdg lpettvaspa tandgtanak yvsavhsaad gyrdygagkv dklwsslspa
      361 erkaqaryme vyagmvenld yniglliqhl kdigeydntf imfqsdngae gwpidsgadp
      421 tatdtanaqe ptysalgtdn gkqnaqrlqy glrwaevsat pfrltkgysa eggvstptiv
      481 hlpgqtqqlp tlrafthvtd ntatflavag vtppsqpapp lintltgvdq nkgkvvygnr
      541 yvypvtgqsl lpvltgaang evhtapfgde aygraylrsa dgrwkalwte pplgpldghw
      601 qlydlttdrg ettdvsaqnp svvstlidqw kaymsnvggv eplrprgyy
//
LOCUS       WP_175848425             163 aa            linear   BCT 11-JAN-2025
DEFINITION  inorganic phosphate transporter, partial [Burkholderia arboris].
ACCESSION   WP_175848425
VERSION     WP_175848425.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia arboris
  ORGANISM  Burkholderia arboris
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia arboris"
                     /db_xref="taxon:488730"
     Protein         <1..>163
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
     Region          1..>163
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 ansiatvvst gvlkpqqavv faaafnviay fifhlkvaqt vgkgtidpei vdhyvifgal
       61 vgaigwnvit wyygipssss haligglvga alaksgwssl nidgllktva fifispllgf
      121 ilgslfmlgv swlyfrtaps kvdrrfrrlq llsaglyslg hgg
//
LOCUS       WP_175848588             596 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 15 protein [Burkholderia multivorans].
ACCESSION   WP_175848588
VERSION     WP_175848588.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Sakaguchi,M.
  TITLE     Diverse and common features of trehalases and their contributions
            to microbial trehalose metabolism
  JOURNAL   Appl Microbiol Biotechnol 104 (5), 1837-1847 (2020)
   PUBMED   31925485
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..596
                     /product="glycoside hydrolase family 15 protein"
                     /calculated_mol_wt=66807
     Region          3..586
                     /region_name="SGA1"
                     /note="Glucoamylase (glucan-1,4-alpha-glucosidase), GH15
                     family [Carbohydrate transport and metabolism]; COG3387"
                     /db_xref="CDD:442614"
ORIGIN      
        1 msatpiedya pigdgrsaal vardgsidwl cwpdfdsppc faaligtpen grfrlalrdp
       61 darvtrrylp gtailettfd tssgrivvid wmswaaddpc lirsvrgehg rvafdvelgv
      121 rfdygyalpw crrfgrrwrm mtggdamwvd tdarlevqdd rlvgtptiaa geridicisy
      181 arsydrapav pdayaslrdt hafwrawsrs qaaqgpygda ieralitikl ltsrrtggiv
      241 aaptsslper fggarnwdyr fcwlrdasft lralarcgyr deaagwrdwl vraiadhpsq
      301 lqvlyaadgs rradewqaeh lagyggarpv rfgnaaaqqq qldvygevlg alyqarrhgl
      361 ppdddawlle rrlidhlati wrepdegiwe vrsgrhqfts skamvwaave sayrsarafg
      421 hhapvddwrr wadtvrdevl argyhaqlgr fvdrfdgdgl dvslllipls gmldacdprv
      481 aatvaaiere lledglpfry rperfadgce gdegafvaag fwlvqvyrlq rrdddahalf
      541 erllalrndv gllseeydvh trrmcgnfpf tlahvalvna alalqrdaqq ddlgva
//
LOCUS       WP_175848458             539 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA synthetase [Burkholderia multivorans].
ACCESSION   WP_175848458
VERSION     WP_175848458.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..539
                     /product="acyl-CoA synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016405 - CoA-ligase activity [Evidence
                     IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57973
     Region          48..538
                     /region_name="MACS_like_3"
                     /note="Uncharacterized subfamily of medium-chain acyl-CoA
                     synthetase (MACS); cd05971"
                     /db_xref="CDD:341275"
     Site            order(111,241..243,267,287,289,293,314..317,336..341,
                     344..345,361,421,433,436,442,444..447,476,505,510..511,
                     513,515)
                     /site_type="active"
                     /db_xref="CDD:341275"
     Site            order(192,195..200,202..203)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341275"
     Site            order(237,289..290,293,314,444..446,505,511)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341275"
     Site            order(314..317,336..341,361,421,433,436,442,447)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341275"
ORIGIN      
        1 mlpaadrydd lltrfrwaip ahynigvdac dkwadgsgrl alihetadgd varftfddlr
       61 nasnrlanaf araglrrgdr iaiflaqgpe tavahlaayk lgaiavplft lfgadaleyr
      121 lanseaaalv tdtagyakia plrdrlpalh tcycigadaa datgvlryda vlaaespefa
      181 padtvaddpa liiytsgttg kpkgalhahr vllghlpgve msqqcfprda rlfwtpadwa
      241 wigglldvll pswhhgvpvl arrfekfdgd aafalmarhg vthaflppta lklmrtverp
      301 reryalslks vasggeslgt eltewgrdal gvtinefygq tecnmvlssc aalfearpga
      361 igkavpghtv aivdahgtpl ppgvdghiav rrpdpvmfie ywrnpdatrd kfagdylltg
      421 dtgaidedgf vrfvgrdddv itsagyrigp gpiedcllth pavrmaavvg vpdptrteiv
      481 kafvvlndgh vgddalvral qahvrtrlaa heypraiafv dslpmtatgk ivrralrda
//
LOCUS       WP_175848529             749 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia multivorans].
ACCESSION   WP_175848529
VERSION     WP_175848529.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..749
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=80850
     Region          <63..>196
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          204..748
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mrhdrtapmp piddaprrrf lkqsaallta gvavgfrlad ataagprasg dphpaagefe
       61 pnawvrvlpd dtiklvvhkh dsgtgtrtal aalvaeeldv dpfrvevvtp edpffadyih
      121 plwkvfstgg stsvameydr lreagatara mlveaaarqw nvrastctta dgavqhaasg
      181 rratygalas aaarlpapqr valkdpaqfr yigklrrkrg aaqkadgsfp ysidvslpgm
      241 lvavvtrapv idarvrsvda kaalampgvr dvllipprpd vlggnqagva vladdywsah
      301 raqaalkiew edslfetfds stlaarqaaw vddpaarvvp tirdgdpvna slagartvda
      361 tyampykaan plepinvtvw arnggieywg glqvpstame aaqviggipa qrvtlhervs
      421 ggsfgaresk ywlfeatwla vktgkpvklm nsredemral fyhaaschra ravldargnl
      481 aslwlrgvmp aspqqwepgy leradrmdfs ttealtkwef ayaaphrdig wirletgvpt
      541 gwyravsyip nvfaveslmd eaahaaardp vefrlahmrd rprhaavlre aatragwgqp
      601 lpdgvalgia tnqaydsyva vvarvvrdae gavrvakltc vadcgiavsp agveeqlygg
      661 lmwglghats dridirngrv qqsnfdtyrv mrmndmpetd ihvvqgdrak pggvgelssp
      721 avtpaianav frltgkrlre tpfdlsavs
//
LOCUS       WP_175848772             562 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxylesterase/lipase family protein [Burkholderia multivorans].
ACCESSION   WP_175848772
VERSION     WP_175848772.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..562
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=58436
     Region          47..540
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mnttkkvsda gaaasssrar rqrtslrlig gmtaltlaac sggddvsadp tvatvesgsl
       61 rgvasdnvls fkgipyaapp vgdlrwrapr paaswsglrd asayghdcmq lpfasdaapi
      121 rtapsedclv lnvwrpaena gaagarkwpv lvwihgggyt nggsspavyd gtqfakhglv
      181 fvslnyrlgr fgffahpalt ssqsneplgn ygymdqiaal qwvqrniaaf ggdpnnvtif
      241 gesaggesvh slitsplakg lfskaivesg sgrvnqtygr yltatgrgnv asgeqlgmaf
      301 aqsigiagnd vnaltqlral tadqvvngln lgtvsaanat wsagpmidgk lvidepgrly
      361 asgrynavsl lvgtndadla ipapaktkdd ayaifgsqnl aaarsvfdpt gtasvrdvvs
      421 eiarvelmhe parfvartvt ahgaasyvyr fsyvaqslkg kvsgavhaae ipyvfdtlta
      481 aygsqvtdqd ervaqlanay wadfaksgnp nasgrpvwqa ndassnavle ftsagtavad
      541 lpdplkaqld lvepvndaal gi
//
LOCUS       WP_175848777             481 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia multivorans].
ACCESSION   WP_175848777
VERSION     WP_175848777.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..481
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48568
     Region          19..428
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(26..27,30..31,34,66,116..117,119..121,124,146,
                     149..150,153,282,285..286,289..291,294,322,326,378..379,
                     383,387,403,406..407,410..411,414)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mdtatpafpr alarivatvs vgfvvtqldv tivnialahm aaalhlsvag lqwvvdaytl
       61 afavlmlsag algdrfgarr lyvaglalfa faslacgaav apamliaara vqgvgaaaml
      121 pnslallnda crhdparrar avgawtaags vsiaagpvlg galiaafgwr siflvnlplc
      181 aaglaaafaw ipadraaass apqartldvr gqlvaiamlt altgaviewr plglvhpvva
      241 ggfvlavlaa aafvaiesra atpmlplalf rrrtfnaavl fgicvnltyy gtvfvialyl
      301 qrvrgesalq aglaflpltg gfllanlasg ravarygpra pmlagalvaa lgygslhfvd
      361 gstplpallv pfllipsgmg favpamttav lasveparag iasavlntar qaggaigvaa
      421 fgavagsgga vpvvdglrid tgvsvallia aallatrvrp dahrdahrdt hggrrplqtt
      481 d
//
LOCUS       WP_175848783             540 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia multivorans].
ACCESSION   WP_175848783
VERSION     WP_175848783.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..540
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58145
     Region          1..532
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 metydyivvg agssgcvvas rlsedpavrv llveagadmk nfwvrtpaga gklfmdkrfn
       61 wafdtepvpt lggrtvywpr gkglggssai ngmiymrgqp sdfdhwaalg nagwswadvl
      121 pyfirsetne rgasdhhggh gplhvsdaai shpsaddfia aaeqagiars adlngppyeg
      181 vayrqytird grrhssydaf iepvrhrrnl tvrtgvrvmr vvieaghatg ievldrgvrr
      241 hiaaarevil sggalaspql lmlsgigdaa alhrhgiaat vdspdvgrnl qdhwfgslaw
      301 rvtpdssynh rlrglrkyle gmrylltrrg ylalgaapvt ayarsepgrp eadlqltvsp
      361 mtfkfsasge pvvddfpaig aavvlltpds rghmalkspd pldapafhpn ylsdpgdirr
      421 siaglrlmrr iantaplasr iveervpgaa vttdeqwlah lktygnsgwh qvgtcrmgvd
      481 aqavvdprlr vrgvarlrva dasimpkiva gntnaacimi gekaadlira datparavpa
//
LOCUS       WP_175848801             562 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia multivorans].
ACCESSION   WP_175848801
VERSION     WP_175848801.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..562
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=61307
     Region          10..539
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mstertlege fdyvivgagt agcvlanrlt edpdvrvlll eaggkddyhw ihipvgylyc
       61 ignprtdwly ktqpeaglng ralsyprgrv lggcssingm iymrgqrddy drwaretgda
      121 gwswdsvlpv fkrsedhhag asdahgaggy wrvekqrlrw eilesfaqaa qqtgipatdd
      181 fnrgdntgvg yfevnqkrgv rwntskaflr pamargnltv itgahaqrvi fegrravgve
      241 yrgggteyva rarievllts gavnspqlle lsgigdgrrl qalgievvqd lpgvgenlqd
      301 hlqlrmafrv qgvrtlntls arwwgklmig aeyallqrgp msmapsqlga faksdpddpt
      361 laspdleyhv qplsldrfge plhsfnafta svchlrptsr gsvhvasadp haapviapny
      421 lsteydrhva analrltrri asapalaryr peeilpgtry qteaelqeaa gavgttifhp
      481 vgtcrmgrad dpravvdsrl rvrgiaglri vdasvmpfit sgntnsptlm iaerasdmir
      541 adrraardaa asvhtdavvt pa
//
LOCUS       WP_175848815             432 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Burkholderia multivorans].
ACCESSION   WP_175848815
VERSION     WP_175848815.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 432)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..432
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47862
     Region          1..351
                     /region_name="COG3950"
                     /note="Predicted ATP-binding protein involved in virulence
                     [General function prediction only]"
                     /db_xref="CDD:443150"
ORIGIN      
        1 myidkitltn irgfstlefs larkdgrhag wtvftgdngs gkstllkava valtgrdtar
       61 alqpsfngwv kddsatqgti elsllhddga defspsgrtp qrafqakitl vregretfle
      121 gvgagtsssk ksaaqrgpws atargwfscg ygpfrrvfga speatrlmvs ptterfvtmf
      181 qeaaslfevd qwlrslshkk legktdegaq ldllvellrd dllpneitvd hvdsdglwlr
      241 drnnlklsws emsdgyraal alltdivrhl itvygvdgll ardddgklyv trpgivmide
      301 idahlhpewq qkigfwlkkh fpriqflvtt hsplicqaad dnglfvlpap gtndearalt
      361 deeynrvias rpdtilltsa fglqntrspl avesraeysr lqakrraggh lspdeserie
      421 qlklfaetde ei
//
LOCUS       WP_175848844             221 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein, partial [Burkholderia
            multivorans].
ACCESSION   WP_175848844
VERSION     WP_175848844.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 221)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         <1..221
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          <1..221
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 vlmdeplgal dkqlrehmqy elkalheklg vtfvyvthdq gealtmsdrv avfdkgivqq
       61 ldtvdrlyes pcnefvanfi gdsnrlrgti arvdgefcel qlgdgtrlvg rrigdvaega
      121 aaiacirper mslaahgang qvpdrvngda nghangaaan rltgearsli yfgdhvrvrc
      181 alpgqdecfv kmplgtgald afspgapvsl afapehlrvf a
//
LOCUS       WP_175848848             260 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease, partial [Burkholderia multivorans].
ACCESSION   WP_175848848
VERSION     WP_175848848.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         <1..>260
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          <66..260
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 nddgtaltpa gtrsklield arwgevaywq aiakngsays pfyllaaldh kqdgfghivh
       61 adpdqsiyla ifgrtfvigi avtlfalllg yplaywistl serranlami lvlipfwtsv
      121 lvrvaawivl lqneglinka ligsgllahp lallfnrvgv yismthillp fmilplysvm
      181 ksipptyqra avslgshpfa afwrvyvpqt ypgvgagall vfilaigyyi tpallggpnd
      241 qmvsyyvayf tnvtinwgma
//
LOCUS       WP_175848868             190 aa            linear   BCT 11-JAN-2025
DEFINITION  group III truncated hemoglobin [Burkholderia cenocepacia].
ACCESSION   WP_175848868
VERSION     WP_175848868.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Keppner,A., Maric,D., Correia,M., Koay,T.W., Orlando,I.M.C.,
            Vinogradov,S.N. and Hoogewijs,D.
  TITLE     Lessons from the post-genomic era: Globin diversity beyond oxygen
            binding and transport
  JOURNAL   Redox Biol 37, 101687 (2020)
   PUBMED   32863222
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Bustamante,J.P., Radusky,L., Boechi,L., Estrin,D.A., Ten Have,A.
            and Marti,M.A.
  TITLE     Evolutionary and Functional Relationships in the Truncated
            Hemoglobin Family
  JOURNAL   PLoS Comput Biol 12 (1), e1004701 (2016)
   PUBMED   26788940
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Wajcman,H., Kiger,L. and Marden,M.C.
  TITLE     Structure and function evolution in the superfamily of globins
  JOURNAL   C R Biol 332 (2-3), 273-282 (2009)
   PUBMED   19281958
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Vinogradov,S.N., Hoogewijs,D., Bailly,X., Arredondo-Peter,R.,
            Guertin,M., Gough,J., Dewilde,S., Moens,L. and Vanfleteren,J.R.
  TITLE     Three globin lineages belonging to two structural classes in
            genomes from the three kingdoms of life
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11385-11389 (2005)
   PUBMED   16061809
REFERENCE   5  (residues 1 to 190)
  AUTHORS   Wittenberg,J.B., Bolognesi,M., Wittenberg,B.A. and Guertin,M.
  TITLE     Truncated hemoglobins: a new family of hemoglobins widely
            distributed in bacteria, unicellular eukaryotes, and plants
  JOURNAL   J Biol Chem 277 (2), 871-874 (2002)
   PUBMED   11696555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..190
                     /product="group III truncated hemoglobin"
                     /GO_function="GO:0005344 - oxygen carrier activity
                     [Evidence IEA]"
                     /GO_function="GO:0019825 - oxygen binding [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21169
     Region          21..130
                     /region_name="TrHb3_P"
                     /note="Truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 3 (P); cd08916"
                     /db_xref="CDD:381257"
     Site            order(33,46,49..50,57,60..61,64..65,75,77..79,82..83,86,
                     89,93..94,97,121,124..125,128)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381257"
ORIGIN      
        1 mtalpaslep aparprdaep tednirdlvy afydrvradp llgpvfdakl agrwddhlpk
       61 mvtfwsslvl gtkgyrgnvq qahqpldgve pahfsrwlsl flktvearya ppaairfmep
      121 alriaqslql srfgwdyrip peqqalldai aprrrdtgdd phalpsrarg eprgepfptk
      181 iigrgidpda
//
LOCUS       WP_175848893             487 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cenocepacia].
ACCESSION   WP_175848893
VERSION     WP_175848893.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..487
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51916
     Region          58..467
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(68..69,72..73,76,110,160..161,163..165,168,188,
                     191..192,195,307,310..311,314..316,319,346,350,399..400,
                     404,408,424,427..428,431..432,435)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mnsqsldlgg haggpesarp paasagagad aaalpgrrvt lgdfmddlpv galhrfvvwv
       61 igvglffdmy eiflvstigs alqheyglsr qsadfkllla safigmfvga mclgsladri
      121 grrkaflltl gwysafslvg afsvnadmlv acrfltgigv gaiypvadsf lseilpkdkr
      181 grlaawaytt syvavplvgf lalwlnplqv agvagwriil aigslgavyv llvqhrlpes
      241 prwllaqgrt adahaalrrf aesagvrvpe hfaepvepqr plglgerial lrrqpygary
      301 vmlaifhllq gfgyfgfgtl agtvvksrgf dvtdstlfia lsfigypigs llsipllnwi
      361 errtlvivsi lsiavsglcf aysantvliv gfgflttcas nvfsnayhvy qaeifparvr
      421 staigstyal srivsgalpf vllpvlghyg asamfgvisv algivavtlr vlgplttrrs
      481 qdeinpv
//
LOCUS       WP_175848984             860 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia cenocepacia].
ACCESSION   WP_175848984
VERSION     WP_175848984.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 860)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 860)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..860
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..860
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=93047
     Region          74..712
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mqpfqpsptr vnrrnvssvr alcarwvara qsaaaaavar aeplaatawh hvrhptrrgv
       61 llaaaavpal faayvvvlip ftpgigdirk arvdqpaqvl sadgkllaef rpsnrewvpl
      121 kqisprmvda liatedhrfy khhgldwkrt asaalhtfsg srqggstitq qlarnlypde
      181 igraptltrk vkeaitalki eavyskdqil etylntvpfl ynaygvemaa rtyfdksade
      241 ldvldsatlv gmlkgnsyyn pvlnperalq rrntvlgqmv kygklspaqf aqlqrrplri
      301 dferqkeppg paphfaqqlr kwliawadrn dyniysdgli vrttidsrlq qmatqaltlq
      361 gnqlqgiann awsgrdgcgt dnevfrtfmr espeykaaqd agkddaaamk mlaadrgflh
      421 alckaktdvq agflaidprd gqirawvgsr dftrepfdhv aqarrqpgst fkpfvygaaf
      481 asgmkpedtf idqpveiplk ggeiwrpndd vpptgkpmtl rdavalsrnr itaqvmekvg
      541 pgavarlard mgvrespler vpslalgtsp vtlkemvasy atiangglyv epqmvtrien
      601 rqgevlaeya papperalda etdktlldvm rdvvtrgtgg sirtrfgirg dvagktgttq
      661 dnadgwfilm qpglvagawv gfddgrvtlr sdywgqgahs alpivgdffq raqrarivdt
      721 kakfdtepsp gwfgslrerv tdlfdtwfpp eakkapapvr tqrierpaet degaasaasa
      781 pdaasggive ewvpasevaa saaalssgas qpqppqfapp pagasaasas sagigvapsa
      841 vpapppasvp atpdatgasq
//
LOCUS       WP_175849038             311 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: dihydrodipicolinate synthase family protein
            [Burkholderia cepacia complex].
ACCESSION   WP_175849038
VERSION     WP_175849038.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..311
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33247
     Region          10..305
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mslptpihrr ytgafsvapt iftesgeidm pgqkrcvdfi idagadglci lanyseqfsl
       61 tddererlia ailehvagrv pvivttthfs paicaarsra aqaagasmvm vmppyhgati
      121 rcgeaaieqf yaelsdaiai pimyqdapms gtqvsaafla riahtipnlr yfkievpqsa
      181 aklrelialg gdaiegpfdg eeaitlladl dagatgsilg ggypdglrpi laaylagrrd
      241 daiaqyeqwl plinyenrqa gllaakalmk eggviasdap rrplaplhpa traglieiar
      301 rldarvlrwa r
//
LOCUS       WP_175849035             254 aa            linear   BCT 11-JAN-2025
DEFINITION  ParA family protein [Burkholderia cepacia].
ACCESSION   WP_175849035
VERSION     WP_175849035.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..254
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28092
     Region          1..253
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mrrvvfnqkg gvgkstivcn laaisasegs rtlvidldaq anstryllgd aaadarpgva
       61 dffetaltfn frpvdvasfi hptpfegldv mpahpdldtl hgklesryki yklrdalnel
      121 daydavyidt ppalnfytrs aliavercli pfdcddfsrr alytllenvk eiqqdhnatl
      181 evegivinqf qpraslpqrl vdelveeglp vlasklsasv kireshqqsr pvihlepghk
      241 laqeflalhr elag
//
LOCUS       WP_175849044             147 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Hsp20/alpha crystallin family protein [Burkholderia
            cepacia complex].
ACCESSION   WP_175849044
VERSION     WP_175849044.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..147
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=16037
     Region          43..147
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 msdiffptdl laefdrlqrq masaftgfpa slraprpgtf ppvnigstdd tieivafapg
       61 ldpakidisv drrlltisge rtppddgttd ddrrvyaner fmgafrrvve lpqhadpdki
      121 earyangclt isvgkseask praitvq
//
LOCUS       WP_175849045             141 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Hsp20/alpha crystallin family protein [Burkholderia
            cepacia complex].
ACCESSION   WP_175849045
VERSION     WP_175849045.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..141
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=15459
     Region          39..138
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 msdtnttelt trpadtrtav tnreaaqrdt prtriapavd ivedthgitl yadlpgvprd
       61 kldvrvhdgs laieaeavip tppglrlqhg evqhphfsra ftlspdfdvs ridaqlrdgv
      121 lklsiprree akprriqvma g
//
LOCUS       WP_175849052             441 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia cepacia complex].
ACCESSION   WP_175849052
VERSION     WP_175849052.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47391
     Region          33..435
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(46..47,50..51,54,86,136..137,139..141,144,164,
                     167..168,171,267,270..271,274..276,279,307,311,361..362,
                     366,370,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mrakypappv egemlqrdda rtfeaatyak varrlipflm lcylgayldr vnvgfaklqm
       61 lgdlrfsetv ygmgagiffl gyflfevpsn lilhrvgarr wlarimltwa visasfvfvk
      121 spaafyvlrf llgvaeagfa pgvilyltyw fpsarrakal slffmaipla giiggplsga
      181 imhslhgams magwkwlfll ealpsfvlgf aillylddgi agakwltdae kallarnvsa
      241 daahttahls irtfvadrrl wlmaaiyfcv vlgqygltfw lptiirkagv adplwvglft
      301 aipyacaiva lpligisadr rrerrfhlav pmlvaaagfa tlpmlgsvga sivclsiasa
      361 gilasssqfw slptallggm saaagiaavn cfanlagffs paivgwlndl tgkstaglvf
      421 isvaitagal lvflvprsvn r
//
LOCUS       WP_175849111             234 aa            linear   BCT 11-JAN-2025
DEFINITION  TerC family protein [Burkholderia cepacia].
ACCESSION   WP_175849111
VERSION     WP_175849111.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..234
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24551
     Region          12..191
                     /region_name="R_switched_YjbE"
                     /note="integral membrane protein, YjbE family; TIGR03717"
                     /db_xref="CDD:163429"
ORIGIN      
        1 mlefltslhw gavlqiviid illggdnavv ialacrnlpa nqrlrgvvwg tagaillrva
       61 litfavalld vpflklgggl lllwigiklm apaadahddi kpasrlwdav ktiviadavm
      121 sldnviaiag aaeqadpshr iplvifglvv svpiivwgst lvlklldrfp ivvalgagll
      181 gwiagglivn dpvgdrwpvl dtqpvlygas iacalfvvai gyalrrrsga prah
//
LOCUS       WP_175849138             334 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sugar-binding transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175849138
VERSION     WP_175849138.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..334
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35587
     Region          32..333
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mrpagrpagg ppapnriaiv skssekldla traawlyyva gdtqneiaek lqvsrpvaqr
       61 lvafaveknl irvrvdhqla dcldlgaqls kryglamcev vpvdadapda idrklavaga
      121 qvmerylnet rpmviavssg rtlkaavaqi aqidrpqhrl vsmvgaiaad gssnrydvaq
      181 yisektgskh fllpaplfad saaeraqwcn hrlyriveal sgqadvafvg ignigphcpl
      241 yedgfiteqe rdemtargav aellgvpida qgklidvstg trvtsvslat ppkrptiafa
      301 ggpkkrdavi aalrggwmsg lvtdetcara alda
//
LOCUS       WP_175849148             174 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: c-type cytochrome [Burkholderia cepacia complex].
ACCESSION   WP_175849148
VERSION     WP_175849148.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 174)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 174)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..174
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17775
     Region          <39..159
                     /region_name="TsdA"
                     /note="Thiosulfate dehydrogenase TsdA, contains C-terminal
                     cytochrome c domain [Inorganic ion transport and
                     metabolism]; COG3258"
                     /db_xref="CDD:442489"
ORIGIN      
        1 mrkplaclla acamtssafg agfglgqpvd raalpawdid vapdgsglpp gagtvarggh
       61 vfadkcamch gaggeggvgd plvggvgsla sakpkktvgs ywpyattlfd yirrampyna
      121 pqslsaddvy avtayvlhln givpadarld aralprvrmp nrdgfvpdpr pgkl
//
LOCUS       WP_175849170             255 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia cepacia
            complex].
ACCESSION   WP_175849170
VERSION     WP_175849170.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..255
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=27727
     Region          3..235
                     /region_name="ArtM"
                     /note="ABC-type arginine/histidine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4160"
                     /db_xref="CDD:443325"
ORIGIN      
        1 mifslpflld tvmpkllaav pttlaltlvs gaasvllgvp lalaagarht plrwsargwl
       61 mlirgtpllv qlyllyygfg qivprewmrd swaspllrda fwyaivalsv nesayvatil
      121 rgaiagvpag eieaghaygm trmqvlrriv gprawrlalp altgeailll kstvlastvt
      181 vfdvmgtant lrfetlrvye plagaaivyv vlvalltipa arleqrinry ltrqpdervp
      241 arrrrassga waapn
//
LOCUS       WP_175849172             244 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia cepacia
            complex].
ACCESSION   WP_175849172
VERSION     WP_175849172.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..244
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=25517
     Region          6..242
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 maaddsllal lafgdggygr vfagafaltf gvaaasfctg vllgiagalg klsryaalvw
       61 qarlytmlvr alpellclll afyavapaie nalrgsgivs gdfafdpfvv aalslgfiqg
      121 ayltdifraa lanvpvgqve aahaygmtpw qtftrirlpa aarlalpgvg nvwlnatkda
      181 sfisvlgsft dllkasqlaa gatrhyvffy lvtaalflll sitstgifaa lerhanrgtr
      241 ratt
//
LOCUS       WP_175849185             299 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175849185
VERSION     WP_175849185.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..299
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31080
     Region          4..264
                     /region_name="17beta-HSD-like_SDR_c"
                     /note="17beta hydroxysteroid dehydrogenase-like, classical
                     (c) SDRs; cd05374"
                     /db_xref="CDD:187632"
     Site            order(9,11..14,34,63..65,91..94,114,141..143,157,161,190,
                     192..194)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187632"
     Site            order(115,143,157,161)
                     /site_type="active"
                     /db_xref="CDD:187632"
     Site            order(143..145,150,157,188..189,195,217,220)
                     /site_type="other"
                     /note="steroid binding site"
                     /db_xref="CDD:187632"
ORIGIN      
        1 mkevilvtga ssgfglltaq alaraghtvy asmressgrn aprvaaiaay aqahrvdlrt
       61 veldvgddas vaaaidrvia dngrldvivh naghmvfgpa eaftpeqiaq lydinvvstq
      121 rvnraalphl rrqgrgllvw vssssarggt ppflapyfaa kaamdslavs yaaelarwgi
      181 etsivvpgaf tqgtnhfaha gkpadaavqa ayddgpyagv agqalqglaa lepadadagt
      241 vataiadiva apagkrpyrv fvdpsqdgae evfrvgdrvr remfrnigla dllvarvgs
//
LOCUS       WP_175849242             455 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175849242
VERSION     WP_175849242.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..455
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46946
     Region          19..447
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(26..27,30..31,34,66,116..117,119..121,124,144,
                     147..148,151,273,276..277,280..282,285,313,317,369..370,
                     374,378,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mnadtglplp qrywaivcva lgitlavldg aianvalpti ardlhasdaa siwivnayql
       61 avtitllpla slgerigyrr iyvaglalft aaslgcalag slpmlavmrv iqgfgaagim
      121 svnaalvrmi ypssmlgrgl sinamvvals saigptvasa ilsfaswpwl favnvpigia
      181 avigslralp snplhdapyd fpsalmnacv fgllitavdg lghgeghayv aaelavafvv
      241 gyffvkrqls qpapllpvdl mripmfalsi ytsmasftsq mlafvalpfw lqhslgfsqv
      301 etglymtpwp lvivfaapla gvlsdrysag ilggiglalf aagllslati gahpgtvdiv
      361 wrmalcgagf glfqspnnra mlssaprers ggaggmlsta rltgqtlgaa lvalifglvp
      421 drgptialyv aaafaavaal vsmlriappr pdaat
//
LOCUS       WP_175849252             191 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Burkholderia cepacia].
ACCESSION   WP_175849252
VERSION     WP_175849252.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..191
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=20820
     Region          4..135
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(9,11,72..73,76)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            11
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(71,116..117,119..120,124)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(77,82..83,112,115..116,119..120,123,126)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(101..103,112..113,116..117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(101,117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(125,131..132)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          147..188
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
     Site            order(148..150,182..183,185..187)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 msrtfayarv stsdqttanq lreietagfs vdkrrvvses isgsvsadqr pgfaqllvkm
       61 eegdvlivtk ldrldrnamd vrttveglae rgirvhclal ggvdltsaag rmtmqvlnav
      121 aefernllie rtqagiarar aegksmgrpc alsksqqdev rqqlsegasv aslarrysts
      181 rqtimrirds k
//
LOCUS       WP_175849335             289 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia cenocepacia].
ACCESSION   WP_175849335
VERSION     WP_175849335.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13484798
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..289
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=32601
     Region          2..>186
                     /region_name="PRK12678"
                     /note="transcription termination factor Rho; Provisional"
                     /db_xref="CDD:237171"
     Region          169..>249
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mqrrypgrhg erggspdwre rderayrgag ergipddpar wpeegyesay rrfasedvgp
       61 edwgsewter aarpadqrrg aadpdwpgga repargaehg ygdsgrgrra egregrygge
      121 rpeyrghhrm gwygserdig dprgdprygg sapdlsrfgr dterdalrhr rgpkgytrsd
      181 eriredvcer lahaleidvs dvtvqvkagr velegtvpar wmkhdiedla dgclgvqdve
      241 nrvrvrrdge hdtgmvlhpd qrtvtptqqa ardpepgtvv ggrereprh
//
LOCUS       WP_175849460             231 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cenocepacia].
ACCESSION   WP_175849460
VERSION     WP_175849460.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 231)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..231
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=24675
     Region          5..226
                     /region_name="ArtM"
                     /note="ABC-type arginine/histidine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4160"
                     /db_xref="CDD:443325"
ORIGIN      
        1 mndflsliaq sgpdvargvw itlqllvlsc tfafalavpl avartserrw lsvpsrlfms
       61 vfrgtpllvq ifvlyyglaq fsivrasplw llvggsfsca lcaltlnlaa ymaedirggl
      121 agvpagekea alafgmsrfm ltwfvvvpra igivaptlgn eivlqlksta lastitvldl
      181 tgvarrisie tyttdalmla givyvgitav lstvlkrveg rlnrhlgsvr a
//
LOCUS       WP_175849487             235 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175849487
VERSION     WP_175849487.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..235
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25155
     Region          18..228
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mpsslapylp qieanpwfaa lppalradll araalrrlpa ghalfrrgdp pcglyavlag
       61 sltigavdpq gkealltvae pvtwfgeial fdgqprthda ialddalllh vpqaallail
      121 datpqywrqf allmaqklrl sfltvesmsv mpaaqrlaar llmiangygg isagrtrvrl
      181 sqetlasmls itrqttnqll kalqadgivr lhvgeielvd idalrrasgl gdgtr
//
LOCUS       WP_175849524             450 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175849524
VERSION     WP_175849524.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..450
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46963
     Region          18..428
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mlihhvepsi qdvatagrrp payawlvfgl tvglllsdym srqvlnavfp llkqawalsd
       61 tqlgslsgvv allvglltfp lsvladrfgr vrsivlmaal wsvatlgcal sthytemlva
      121 rglvglgeaa ygsvgvalil sifparlrat ltgafmagga fgsvfgmalg glvgahlgwr
      181 wsfgvmaalg ivllvayrcv vterrlaayr sefgtecgae pcrrdtdtpr dlrgsvrvlm
      241 sglfasrsvi caylgsglhl fvpgalfawl psylnryyam apdraavlaa gfvllagigm
      301 vgcgivtdrv gktdgkrkwl taiaycvltg vclavafrlp pgplqlalic agmlvgagas
      361 gasgamvanl tpaaihasaf atltlannll gmapgplltg waadraglvg alqwipvvpl
      421 maavlfaigr asyvadlarv ererrasrls
//
LOCUS       WP_175849594             506 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Burkholderia cepacia].
ACCESSION   WP_175849594
VERSION     WP_175849594.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..506
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53826
     Region          13..490
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(70,72,76,79,83,116,119..120,129..136,141,144,147,
                     240,244,247,250,252,426,428..429,431..432,435,438..439,
                     441,443..446,455,459,461,475,482..487,489..490)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(156..159,167,182,185,215,232..235,238,256..258,290,
                     391,393,419)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(159,256,287,290)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnpvpaytsd advghyvdga pvsgrsgrfq dvlnpalgra vrrvaladds evqqavasah
       61 aafpewaatp pirrarvlhr flqlmnehrd alaaiitaeh gkvfsdaqge vargidiief
      121 acgvpqllkg dftdqvstgi dnwtmrqplg vvagitpfnf pcmvpcwmfp vaiatgntfv
      181 lkpserdpsa alfiadlltq aglpagvfnv vqgdkgavda lldhpdvqav sfvgstpiaa
      241 yvqqravqsg krvqalggak nhlvvmpdan leqavdalig aaygsagerc maisvavlvg
      301 dvadkivplv aerarklvig dgmspevemg pivtgdalkr iegyieqgvn egaqlvvdgr
      361 glrvpgreag fftggtlfdh vtpdmriyke eifgpvlgcv hvkdfgeavd linahefgng
      421 vscftsdggi arefarriqv gmvginvpip vpmawhgfgg wkkslfgdmh aygeegvrfy
      481 trqksvmqrw sssigkgaef amptak
//
LOCUS       WP_175849597             341 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175849597
VERSION     WP_175849597.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..341
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35675
     Region          10..341
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mgnlnpaada qtmtikarhm kwppelsifl vlvgislffe ivgwivvgqs flfnterlei
       61 ivlqmavigi iavgvnlvii tsgidlssgs vvaaaavvsa slaqvsdfpr avfphltdlp
      121 iiwpvlagvc vgllvgllng sliamtgipp fiatlgtmva argfakwftn gmpvsmltdq
      181 faaigaganp viiflviavi fhvvlrytrf gkytyaigan rhaavvsgin vtrhlvfvya
      241 iagllsgiag tvtaaraisg qsgmgvmyel daiaavvigg tslsgglgrv tgtvigvlil
      301 gvmtsgftfi ridayyqemv kgaiivaavi adqyrnkkkr r
//
LOCUS       WP_175849605             311 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            cepacia].
ACCESSION   WP_175849605
VERSION     WP_175849605.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..311
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=31724
     Region          1..309
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mhalalqvfn glsyglllfm lsagltlifs vqgvlnfaha sfymlgayvg ysiaahagfw
       61 palvlaplav gllgagcert llrrvqahgh tnellltfgl ayligegakl vwglaplpap
      121 vpplfdgapv svfglalpry rlfmmamsat mlvalgallr vsriglvvra althraavea
      181 lgydvprvmt glfgagtala alagvigapl aviepalaet vgsvvfavvv igglgslgga
      241 fvaslavgfa qtfaaasdts lrdlaswagi vlpdsvaavs iaqlaplvay lllvavlvar
      301 prglfgervd a
//
LOCUS       WP_175849611             461 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia cepacia].
ACCESSION   WP_175849611
VERSION     WP_175849611.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..461
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=49615
     Region          92..452
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mkprqptaga fahswlhlag afalaatlvt vagcdgqpga gtpsaqaasa sgvpdgahpv
       61 asatvaasga vvatnqpqtr aqvyegvrrm talgkqlffd ptlsgsgkla caschspdha
      121 fgppnaldvq lggddmkhpg fravpslkyl qgvpqftehf hdsddegdes vdagptgglt
      181 wdgrvdtgae qaripltspf emnsspakva qavkaapyaq efravfgvkv ldddaatfka
      241 vlraletfeq tpelfspyts kydaylagha qltpaemrgl qlfndekkgn caschisqra
      301 ldgtppqfsd fgliaiavpr nralpvnrdp rfhdlgacgp ertdlkgrde fcglfrtpsl
      361 rnvalrktff hngvyhtlee vmrfyverdi hpekfypvvn gkvqiyddlp krywpninre
      421 apfdrkrgeq palnaaeikd viaflgtltd gyrqtaapag h
//
LOCUS       WP_175849634             128 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF805 domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175849634
VERSION     WP_175849634.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..128
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=13950
     Region          6..116
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 mnvpalfslr gragrmqwws vtvpllvags vfdaladlpa aqraqtivdl agwafailmi
       61 wllvavsvrr whdigksgww tlvhaipvvg afvaiamngf irgddvhnrf dppsrgegnn
      121 daslrgyr
//
LOCUS       WP_175849638            1245 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia cepacia].
ACCESSION   WP_175849638
VERSION     WP_175849638.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1245)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 1245)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1245
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1245
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=132755
     Region          12..784
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
     Region          <884..>946
                     /region_name="PRK14959"
                     /note="DNA polymerase III subunits gamma and tau;
                     Provisional"
                     /db_xref="CDD:184923"
ORIGIN      
        1 mdlvaaltgy gqatrhiqid tampgafvve rfhgregise sfrfeidvls sepfldlapl
       61 igsavrlrla taagercwng yvthaayaes dgeftryrlt meswlallql rrnclyfvdl
      121 dvegiceqvf gdypeahrry erveplrafr lrgqyretdl dfvlrqlsea glsfriehgq
      181 dtgnapsgdh tvvvfdrhar lpdgsaiafn aqdvgdpdgv mtqfsdrrql vpdrvvttsw
      241 kaselvalag qaqqpadada pllpvrevyd gqragrfdts gdaqryaeqr ldalqlakrv
      301 yrgggssrtl evgrvhtlnd ylsgpvrfvp lsieheavnn lgaqigqlfg rgelekglyr
      361 nrfvavpegt pivpphrdrp tvhgvqtaiv vgepggrvss trdhqvriqf pwmrgvaplp
      421 ggltdtasrs npaghapgdh rsgilvrvae qaagpnfgha faprvgaevv vgfesgnida
      481 pvvlgqvygg rvrppfsage gsdanhsgsl tglqtqtldg qpgsrwvmdd aagqlrheln
      541 nstagtrlaq gylidqqgtm rgayrgegfe latqgwgvvr agagvlvsst arqfgastqm
      601 dvaerveqlk daektaqeld raatgalavg lsanaaltdf lkaidpaqgg kyagsvggqs
      661 atkpsgtqrd ggdpverfat pavlmespen ivvttpdsav syaaqhvhvt sqgdahvgag
      721 atvaaatgda aslysvaggl kaiagegpvs veahastmei ladqtvrvts tdervdvlaq
      781 daivlqqgpn ritlkggdii vetpgqfavk sgghpfpgpr aasvklpalp vlpqgdpcdf
      841 lvqalaaspa grgavaaggs aagaaggaaw sgaasgatvl madmpapgag slplvpqala
      901 dessrsmpap vpassgqnaa pgpslgystp ppvsselegm pkkgpaaqsg pcnlhvpaip
      961 telhtvdagc vsyfqtgedg kavlkdkkri wlnfsgteds ydigyapata tvtatvyikv
     1021 nlkdqywind gavymdpstg kpfsvpfnsd girkdrvmqi vdrpgglapi sgfkkriedg
     1081 lnrgnysmqp kkcplgsact ckvklkleve lvqigrchae vnlyplvtra nsanwgevqv
     1141 ewdeeqkryv pvspqhalvh etghlfgwpd eyfinggavf gryinsrhlv dlkmaqlddn
     1201 wqrttetnvm grgmftekpe ipkyymygfr dwfnkktgid wkvlk
//
LOCUS       WP_175849641             931 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia cepacia].
ACCESSION   WP_175849641
VERSION     WP_175849641.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 931)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 931)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..931
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..931
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=97569
     Region          15..875
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msvikefasl fgafnrlysl dgsgalaafq ierwtgresl sdlfqwnvda lstdpaldld
       61 amlgqrvair ttlangtttl rsglvaeaec igydaglary hlqivpwlaa lthardertf
      121 vnqtladvld tvfapyagia rwrltpdagr rldalapvay rvqyrththy efvqhllaea
      181 glgfcfvede dapaghamlv fddsaqlaed etsarrggvp rrssgtatda ddvilgigqs
      241 lsltadrvtl issdyranra ttastdlgrp ngprelyddv gpeafdtlrd aedtarrqad
      301 aivsracfwt gygtlrtara gralklvdag wqavrgaaap edflltrveh vginnlpptv
      361 meaierqlgp lpaakvdprv lrqaqaggya nrfdavprtq vwrptladgt gqrlnpvata
      421 lgaqtaivvg ptgsaqpgst gpvhadaqgr lrirfhwqae ddtgtyptra iqrlasdghg
      481 lqqvprighe vlvqfhhgli hrpivlgglf ngrgeggesp spggaagkpl dasiytqagd
      541 hapsaqgnla nglspawhga gggadrhnha galsgfksrg fdgqghnqlv addsdgmgrl
      601 qmatthaatq lnlghlrhqs dnylgsfrgq gvelrsdayg amratrgllv ssyapsgaaq
      661 pagdasalqa llarhaalvg rfdktadthg tlpfaaqrgv eqagqsslnr kaapldalaq
      721 sfattvgang yaqasadaaq rstgnalpht gdavlgiear ggqgliagqa lqwaagetls
      781 lgsgadfnla aaqqlrihsg qgigwlggas hadgvgmsli sgrdgltlqa qrdvlglrar
      841 ddlkvasasa dveiaakktv hlavsggahv tieggdvtfg cpgkfvvyaa qhafvgpdqm
      901 stplpqfpek vcvecllham qsgsalagka i
//
LOCUS       WP_175849699             547 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia cepacia].
ACCESSION   WP_175849699
VERSION     WP_175849699.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 547)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..547
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=58148
     Region          1..547
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mlclsllwga gvagvpgqah aqvpnagatm rdvetsrpal ppkaapdlei vpsesaaqpq
       61 pdagpriavr afqigghtvf dtatlqalva glagdaltfa dlqgaaerit ayyrergyvl
      121 araylpkqdi edgvvrieva egrygkieiq nhsraldavl rqplaalqpg dvvrgssler
      181 sllllddlag vgargtlrpg evpgttdlvv daergppasg slefdnfggv stgryrvggs
      241 vdvnaplrlg drlslrglvs derqryyraa yqvpvgpast rvgvaysslr yrvagrfsdl
      301 emsgrasvqt vyvaqplvra rdlsvtaqvq yenknlhdty gtfslqndkn vglwtfglsg
      361 nsqdgwlggg rngfsvmfgv grlrgndvfg snpltksigg fkklnvdaqr iqalggrfql
      421 ygqvsaqfas rnldssekfs lggpygvray algegsgdqg wqasaelryl aapgwqvsmf
      481 vdagavqlnr hpwtgerntq hmqaagigat wfgakrqvsl taalplgrgg dsptrapsvw
      541 vqaaqyf
//
LOCUS       WP_175849710             140 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Burkholderia cepacia].
ACCESSION   WP_175849710
VERSION     WP_175849710.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..140
                     /product="RidA family protein"
                     /calculated_mol_wt=15239
     Region          1..129
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 maeavnppev wapfgafsma viqgdgrivh lkgqvaldrd gqvvghgdmr mqvrqtldni
       61 ravlaamggq mqdvislvhy atdidafmqa gdirntyfaa pypvtttvqv erlyhpdlli
      121 eitavaeipl ahfrrpasra
//
LOCUS       WP_175849786            1613 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD-glutamate dehydrogenase [Burkholderia cepacia].
ACCESSION   WP_175849786
VERSION     WP_175849786.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1613)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1613
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1613
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=178835
     Region          4..1610
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 meakneevva hllsdvvefa rgrlpeatfr ivepflrhyy dfadaddlqs rsiadlygaa
       61 mahwqtaqkf vpgserlrvy npileqhgwh sdhtvieivn ddmpflvdsv tmavnrlgla
      121 lhsalhpvfr iwrgadggie rvdaggatpg dgqsqlasfi hfevdrcgda allntlrndi
      181 ahvlgdvras vedwpkivdi aratikemka restaediea raflewmaad hftflgqrdy
      241 alvsdgtgfg lrgiegtgfg ilreslrtsg apdvtplpqa aadiitgpwp ifltkansra
      301 tvhrpgyldy vgvklvgadg kvagerrfig lytstayfgs yteipivrrk canivrragf
      361 lpkghlgksl vtvletyprd elfqadedql ydialgvlrl qehqrtrlfv rrdrfdrfvs
      421 clvfvprdky ntdlrrriak llvdayngvn veftpllses aiarihfvvh aepgtmpdvd
      481 treletrlvq vtrrwqddla dalldafgee qgnrllqrya dsfpagyrdd ypartavrdi
      541 eliervkdsg qlamnlyrpi eaearafrfk vyragdpial srslpmlehl gvrvdeerpy
      601 riqtqdaaha wvhdfglela ddtefdierv kglfedafdq iwsgriendd fnrlvlrahl
      661 sarevtilra yakylrqvgs tfsdayiera ltgnpaiarq lvelfllrfd patgdtrdvq
      721 aerllkaieg aldqvpnlde drilrqflgv inatertnyf lvdangeskp ylsfkfnpak
      781 vpglpepkpm feiwvysprv egvhlrggrv argglrwsdr redfrtevlg lmkaqmvknv
      841 vivpvgskgg fvvknpppps dreawmregi acyqtflrgl ldltdnlagn tivpppdvvr
      901 hdpddpylvv aadkgtatfs dyanaishey gfwlddafas ggsvgydhkk maitargawe
      961 svkrhfremg idtqttdftv vgvgdmsgdv fgngmllsph irlvaafdhr hvfldpnpdp
     1021 atsfaerarl falersswad ydpaaisagg gvyprtakti plspavqaal gidahalppa
     1081 elirailqap vdllynggig tyvkaareth lqvgdranda vrvngadlrc kvvgeggnlg
     1141 ctqfgriefa qrggrintda idnsagvdcs dhevnikill glvvsdgemt ekqrnallae
     1201 mtdevgllvl rdnyyqtqal siagryavel ldaearlmrw leragrlnrv ieflptddev
     1261 aerqaaklgl tsperavlla yskmwlydal lesdvpedpl vaamlvdyfp kplqqrfsep
     1321 mrrhplrrei lathltnalv nrvgcafvhr lmeetdakpg divracimar dvfdldavwr
     1381 didaldnrva ddvqarmfvd varlleraal wflrhlqsga vadggvaeli arcrdaaerl
     1441 apqlpsllpa ddlealsgrq rvlveagvds alavrvasgd isaalldiae vaatsnrsle
     1501 lvagvyfslg tllnyswige raatlptpth wdmlaraaal aevarlkrtl aasalaespd
     1561 sttpetivga wrarreaala ryehlladlr asggaslavl lvvvremavl era
//
LOCUS       WP_175849997             251 aa            linear   BCT 11-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Burkholderia
            cepacia].
ACCESSION   WP_175849997
VERSION     WP_175849997.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..251
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26093
     Region          1..251
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlttqrkkai ldalardgqv lavelsaqfg vsedtvrrdl relaaegllq rvhggalpas
       61 pavapfaqre tletaekrri arraaemiap grvaivdggt tsallvsqlp adlrativth
      121 spsvavalaa hpsidvilig grlykhsiva vgaaamegia rihadlyfmg vtgvhpvagl
      181 stgdfeeaai kralaeraae tvvlasqskl raasqfvige ltlahtvvve ketdaaltkp
      241 ieaagvtvvr a
//
LOCUS       WP_175850143             370 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia cepacia].
ACCESSION   WP_175850143
VERSION     WP_175850143.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..370
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39179
     Region          4..334
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,233,300,320,322..324)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,181,184,186,233,240,300,320,
                     322..323)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,181,184,186,323)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            186
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mssllshydl rglplpnrvv mgpmtrsrap srgqptelma eyyaqrasag livteatnvs
       61 pasasfeltp glvtdeqaag wkqvtdavha nggrifaqlw hggrvssltl lggaaplsps
      121 gvnddleqlq vwaqlqngyy tkihatpsra mttdevadtv defrdaavra maagfdgvei
      181 haangylphq flsstlnrrd dryggsvanr arfleeivda vgavmplsrv gvrispyaky
      241 nnvrdadpdt tyayvgrmld eagvayvhaa dtngwsgepd lprivanark hfggtlivng
      301 giapdaanal idagdadlva farayianpd lverlaanap laapkavgwy ggdragyvdy
      361 arhdaagvsa
//
LOCUS       WP_175850108             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175850108
VERSION     WP_175850108.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32974
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..271
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(103,107,146,160,162,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(104..105,109..110,112..113,116,120,122..128,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mlnrldllki faaaaaaptf reaaarlgvs pqvvtravre leemlgetlf hrttrsirit
       61 afgqsfarda kaalstvdgl fgpaagqvde pagivritap sgmgrryvqp ilidlmqryp
      121 dlvpdlrlsd apspvvdeqi digvrvgaig dnrfvarmvg plpmwvvgap slimrlgepk
      181 srkelaampv tclidrangr pwpwvfrgeq qfvpsspayl tddteveiea vcagigfgqc
      241 seylvrphvq kgrlvrllps iepepwklhv yrprrgpmpr rirvvydelv aklahatsra
//
LOCUS       WP_175850170             234 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175850170
VERSION     WP_175850170.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..234
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25524
     Region          1..222
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 metvlsiqav skiypmgsvs vhalkdvtle leagefvvll gtsgsgkstl lnlmggldsp
       61 tsgiinyrdh rlstaterel trfrrehvgf vfqfynlipg ltarenvalv tdiaehpldp
      121 ddalrmvgid slagnfpsqm sggeqqrvai aravakrpdv llcdeptgal dfrtgrlvld
      181 vlervnrefg tltivvthna viaemanrvv rmssgtivee hrnvrrsdar gltw
//
LOCUS       WP_175849652             774 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia cepacia].
ACCESSION   WP_175849652
VERSION     WP_175849652.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Thurner,C., Vela,C., Thony-Meyer,L., Meile,L. and Teuber,M.
  TITLE     Biochemical and genetic characterization of the acetaldehyde
            dehydrogenase complex from Acetobacter europaeus
  JOURNAL   Arch Microbiol 168 (2), 81-91 (1997)
   PUBMED   9238099
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18097562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..774
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0005506 - iron ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81717
     Region          <42..>193
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          203..764
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msapelsvhn esrralllgf asgglllafg vpslvraavp nqppvsadpr yggagmphgl
       61 rddphlfvai apdgtvtvtc irsemgqgvr tsvalvvade lgadwarvkv aqavgdepry
      121 gnqntdgsrs lrqsfaalrr agaaartmle qaaaaawgvd arqvkatvhe vvdtksgrkl
      181 gfgelaakaa alptpdpatv plkapaefry igkgetalid grdivagrah ygidtrldgm
      241 lyavvarppa ygdtmasfda saaeklpgvv kvvplastpl psgfqplggv avvardtwta
      301 iqaraqlkid wkhgpnanyd saayrktlea aaaqpgdvir ndgdaaaala gaakrvraty
      361 yiphlahatm eppaavarva dgrcevwtct qapqttrdev akalglpger vtvnvtllgg
      421 gfgrkskpdy vveaallska vgapvkltft reddlahdyf havsleafdg gidasgkvva
      481 wqhrtvapsi qstfragvvh eqpgelaqgi adlpfaipnv rienpaaqah trigwfrsvy
      541 niphafgiqs fvselahaag rdpkdfllel igparrfeph itvknvnyge dpalypvdtg
      601 rlrrvvetva reagwgrrlp kghglgiaah rsfvsytaav cevqvdadgk itvprvdiai
      661 dcgpqvnper vrsqlegavv mglgialhge itfkdghpeq snfngfqvlr mneapreirv
      721 hlvapddfat plggvgepgl ppvapaltna ifaatgtrir slpvadqlak prag
//
LOCUS       WP_175850206             208 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cepacia].
ACCESSION   WP_175850206
VERSION     WP_175850206.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..208
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21687
     Region          1..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mshpswlpfi atslliivtp gqdmvlvmsr tlsdgtragl vtaagvsvgl lvhtmlatlg
       61 lgallqasew lftalkivga lyllylgitl lrssgeltla sgdgaqasrl rtfaqgalsn
      121 vsnpkvalfy laflpqfvpa gaahpvlslf vlgatfaglt flvkgpvavf agllsasirr
      181 npriltrmhr vsgvvllglg vklalerr
//
LOCUS       WP_175850222             440 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175850222
VERSION     WP_175850222.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..440
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47841
     Region          21..424
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,152,
                     155..156,159,256,259..260,263..265,268,295,299,349..350,
                     354,358,374,377..378,381..382,386)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mqtgfmdasa ierrtirkvv wrlipflmic yllafidrgn vgmaslqmnh dlemsaqvfg
       61 fgsslffisy fffevpsnla lqkygariwi arimitwgiv saatalvhna ttfyvlrfll
      121 gaaeagffpg vllylsywip aqyrarivat fmvaipaasf igspisalll qmdgvwglrg
      181 whwlfilegi ptvllgiacl fmltnkpdda kwlddderaw ltaalaaghk trkkvpslpl
      241 tqlfrnryvl clalvdtcas aagstlsvwq pqllksfglt vmetgllnsv pyavasvlmv
      301 ywgrrsdrvg errwhtvvpm lligvglfat slsgsllptv cmlcavlvga ysfkgpfwal
      361 atdmlsnstv aaglatvnai anllggglmv nvygwvkaat gsyalalmpl ailtlvsvat
      421 lllltrdhas gkligktgti
//
LOCUS       WP_175850226             459 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175850226
VERSION     WP_175850226.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..459
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48304
     Region          41..440
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(54..55,58..59,62,94,144..145,147..149,152,172,
                     175..176,179,276,279..280,283..285,288,315,319,369..370,
                     374,378,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtishalrag ddapradaps saqlagddya asertlakaf rrilpfifvc yvisyldrtn
       61 vgfaaltmnk dlgltaeqfg vgaglffigy flfeipsnli mqkvgarvwi arimitwglf
      121 smatafvvgp ksfaaarfll glaeagftpg iylyfthwfp gkwrakvtaa flvgipvanm
      181 igspvsgall elgglhglrs wqwllliegv pavmlgvacl fvladrpeka awlndeekas
      241 lakrlafeqr digakhgskl rdamtnwrvf vlafvnfcgi vgslgvglwm pqiikqfgve
      301 havvgwltai pyaigagvml gwarlanraa nripyiagal avaaaalcas afihapvfkl
      361 ialcvtvsgi lafqatywai psgfltgraa agglalivsv gnlggfvgps migalkqfsg
      421 gftapliavs avlllgalti awlgdpgaga geapaarep
//
LOCUS       WP_175850230             192 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175850230
VERSION     WP_175850230.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20188
     Region          26..159
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 marprspdkh dailaaaara laedgasatt ariarlagva egtvftyfet kdallnalyl
       61 nlkaglream mtgfpehapa eqavrhawng yvswgvanpd grralqqlgv sgriddahra
      121 agsegfggig allreqvaas galnrdeaha fcsalfasia etamesiard paradayrea
      181 gframwavlh tv
//
LOCUS       WP_175850236             706 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia cepacia].
ACCESSION   WP_175850236
VERSION     WP_175850236.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..706
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=76008
     Region          37..639
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mtdhtasppp ppvppprrrr awrtlagall gltlacagig awtvnriwtq lpsvehlavy
       61 rpalplrifs rdgdllaeyg verrefvple ripalmrhal laaedakfyq hgavdvggla
      121 ratfanvvtg qpgqggstit mqvarnfylt rdkvlsrkla eilmaakler eyskdkllel
      181 ymneiylger aygfaaaanv yfgkpldaln ageaavlagl pkapsafnpv vnparatarr
      241 nyvlgrmhal gqlddatyra avdapialat tpppgivaap yvaerarrmm verfhddayt
      301 lgldvtttis mrdqraaeaa lqrqlsrqpg akrdarngle galvsldaat gdmlalvgga
      361 dfnrnvfdha lqayrqpgss fkpfvysaal ekgyfpgvlv ddtqrtlthe etgarpwrpr
      421 nfgnryegfi pvrrglvrsk nlvavslmqa tdaryvqqha vhfgfdaqrn paslplalga
      481 gavtplelas aysvfanggt rmeprlilsv kqrhggamye attpegarvv sarnaflmds
      541 mlrdvvkagt argalalrrd daagktgtsn gskdvwfagy ssgivavawl gydtprpmgr
      601 atgatlalpv wldymktavd grtpvdatpp qdvalvdgdf vyaeytrgtc tadvppyirs
      661 rfacggaaaq dasdapagsg kpdapmpaav daaerervld lfrtdd
//
LOCUS       WP_175850249             219 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia cepacia].
ACCESSION   WP_175850249
VERSION     WP_175850249.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..219
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24785
     Region          1..207
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 miptlyahpf ssycqkvlta lyengtpfay rvlahddpkp mqelaalwpl krfpvlvdag
       61 rtvieasiii eylglnhpgp vrllpdepha alevrtmdrf fdnyvstpqq kvvfdalrpe
      121 aerdargvad aramldtsya wldrkmadre waagdrfsla dcgaapflfy adwthridps
      181 fanviayrkr llarpsfara vdearpyrpf fplgapdrd
//
LOCUS       WP_175850297             507 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175850297
VERSION     WP_175850297.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..507
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52703
     Region          14..449
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(20..21,24..25,28,60,110..111,113..115,118,139,
                     142..143,146,270,273..274,277..279,282,310,314,366..367,
                     371,375,391,394..395,398..399,402)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mpryrraalv laaclgtfla tldisivnva lptlqtaldt digglqwvvn ayalalsafm
       61 lsagplgdry ghkrvwlasv vlftagsvvc acasrlepll igraiqglag allipgampi
      121 lthafpdare raraiggwsa fsalalilgp lvggllvehg gwqdiflvnv pigivtvllg
      181 awgiperrhp qhaafdplgq alsvawlgll tygligigea gashvkvlap lagaavafvv
      241 fvrvetrver pllpvwlfrd rrlvranlas fvlgfsgyss lfflslflqq aqgrtpaaag
      301 wqlmpqfvmt aitsmlfgri aariplhalm vagyglvgam laamagfgag tpyvpvgial
      361 avlgvgmgla vpatgmtvme lapaeragma satmnalrqt gmsmgiavvg smmsvgalhr
      421 mtaamqaags aqadtlarqa vmehvfaagq pallgayrda mahgfsiavl csgilsigia
      481 vmlmmrretk kqpgraaaar vtssrpe
//
LOCUS       WP_175850252            1028 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Burkholderia cepacia].
ACCESSION   WP_175850252
VERSION     WP_175850252.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 1028)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 1028)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11534155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1028
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=104576
     Region          12..77
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          118..180
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(124..126,129)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          203..265
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(209..211,214)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          283..1026
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mteplasaal htielsvdgm hcggctgrvq ralaavpgvv daavdldaha atvtaqetvd
       61 aarlieavga agygasvrap vletaaaaha hpveaspapm aaaastaghp lpanstield
      121 idgmtcascv srvekalakv pgvtrasvnl ateratvdvt advsaaqlve tvkqagygat
      181 ptmtdagfta lapsspaapa sieldidgmt cascvsrvek alakvpgvtr asvnlatera
      241 tvdvapdvta arlaeavkqa gygatpvaga aippvastap adleldidgm tcascvgrve
      301 kalaavpgva rvsvnlater asvhgagald aatliaavtt agyraslada ssagatagad
      361 tqpasatqdp etrkrleair erdlviwsav lsapliapml vapfgihlmp ngwvqlvlas
      421 ivqfgfgarf yraawhavka rtgnmdllva lgtsaaygls lwmllrgtgh pghlyfeasa
      481 vivtlvrfgk wlesrakrqt tdairalnal rpdrarvveh gverdvplaq vrvgtrvsir
      541 pgervpvdgr ivsgrshvde slitgeslpv pkddgdpvta gsingegalv vettaigaet
      601 tlariirlve saqaekapiq rlvdrvsevf vpailgiavl tlagwliaga gtetailnav
      661 avlviacpca lglatpaaim agtgvaarrg vlikdaqale laqrttviaf dktgtltegk
      721 psvtafeavg vphdealala aavqrqsdhp laravvaahd advaargsav ppasaagara
      781 vagrgvearv ggqllalgst rwrdelgiav ppaldaraae leragntisw lmradapral
      841 laliafgdtv kpgardaiaa lsargvasvl vtgdnrgsaa avaaslgige vhaqvlpddk
      901 arvvaelkrt hggivamvgd gindapalaa advgiamatg tdvamhtagi tlmrgdpalv
      961 adaidisrrt yrkiqqnlfw afvynlvgvp laalgwlnpv iagaamafss vsvvtnalll
     1021 rrwkgrah
//
LOCUS       WP_175850484             442 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175850484
VERSION     WP_175850484.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..442
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46639
     Region          28..407
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(39..40,43..44,47,79,129..130,132..134,137,157,
                     160..161,164,262,265..266,269..271,274,302,306,355..356,
                     360,364,380,383..384,387..388,391)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 msthhaqals saatdanasl nrllfrklmp lliaayvisf ldrtniafak hsmgvdlgis
       61 saayglgagl ffltyalfei psnlimhrvg arfwitrimi twgalsvama fvrgetsfyv
      121 mrlllgvaea glfpgvmlyl tywfgreera ratgyfllgv cianivggpl agalieldgt
      181 lgfhgwqwlf vvegipaill afvvwtrlpd rpsaapwlap etgralerkl aaeqdagvaa
      241 hgghafgaal rdpqiwlaif vyfchqltiy tvifflpgii gaserlspva vglltslpwl
      301 aaalgagtlp rfaresrhsr rmlcaglaim aagmvgaaha splagllcvc vsasmffvvq
      361 sivftfpasr lagsalaggl glvntcgllg gfvgptvvga ieqatgnakn gltllaaalv
      421 vaafaslalr hgheradvrs rg
//
LOCUS       WP_175850496             862 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia cepacia].
ACCESSION   WP_175850496
VERSION     WP_175850496.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 862)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..862
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=93173
     Region          59..712
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mhpfqpsstr vnrrnvssvr dfcarwvara qpvaaaavar vkplaavawh hlrhptrrgv
       61 llagaavpal fvayvvvlip ftpgigdirk arvdqpaqvl sadgkllaef kpsnrewvpl
      121 tqisphmvda liatedhrfy ehhgldwkrt asaalhtfsg srqggstitq qlarnlypde
      181 igraptltrk vkeaitalki eavyskdqil etylntvpfl ynaygvemaa rtyfdksade
      241 ldvldsatlv gmlkgnsyyn pvlnperalq rrntvlgqmv kygklspaqf aqlqrrplri
      301 dferqkeppg paphfaqqlr kwliawadrn dyniyadgli vrttidsrlq qmatqaltlq
      361 gnqlqgiann awsgrdgcgt dnevfrtfmr espeykaaqd agkddaaamk llaadrgfmr
      421 alcktktdvq agflaidprn gqirvwvgsr dftsepfdhv aqarrqpgst fkpfvygvaf
      481 angmkpddtf idqpveiplk ggeiwrpndd vpptgkpmtl rdavalsrnr itaqvmekvg
      541 pasvarlard mgvrespler vpslalgtsp vtlkemvasy atvangglyv epqmvtrien
      601 rqgdvlaeya pgpperalda etdktllsvm rdvvtrgtgg sirtrfgirg dvagktgttq
      661 dnadgwfilm qpglvagawv gfddgrvtlr sdywgqgahs alpivgdffq raqrarivdt
      721 kakfdtepsp gwfaslrerv tdlfdtwfpp kpekapapvr tqrverapea dtgtesaasa
      781 asapeaasgg vveewvpase vaasaaalsa gasqpqpaqp pagastpggg ssglgtapaa
      841 apsaapaqpp vpaapdasga sq
//
LOCUS       WP_175850520             793 aa            linear   BCT 11-JAN-2025
DEFINITION  serine/threonine-protein kinase [Burkholderia cepacia].
ACCESSION   WP_175850520
VERSION     WP_175850520.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..793
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=80201
     Region          32..532
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
     Region          <569..>724
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
ORIGIN      
        1 mkdagsrdne hdtatrgdas gftvrplplg hrlgelqlde vlgiggfgiv yrafdrtlrr
       61 avaikeymps mlatrggdyt vslrserfaq afdagrgafl nearllaqfd hpglvkvlhf
      121 weshgtaymv mpfyegrtlk qlldggmris etqlrnivga llgaldtlhr aqcfhrdval
      181 dnvlirpngs ailldfgaar krigdlvddg ammikpgyap ieqytddpaf sqgpwtdlya
      241 lgavmhamit gelppaavvr sikdtyrpla srelpagevy spaflaavdh alqlripdrp
      301 esvaafaael glrdfdrtgs gygapavppv gdagrgegdk gaasvetgta paaaatsiga
      361 ggtasgsaap darpptqaga gpvstptdta saspgvsdgk petddgsstl kaatqgaaat
      421 vaagalaasa shasrpaakp vesdapngnv erakepaaar tdthdeagar sastdteiga
      481 rgaggsgeav tfatesagag vgaaaaaast tapypaasss assggasvpt gaqlgqppag
      541 srkrrlpvya ggavvaliav glaatylsrp arvadepapv asqpqagtsp pastpaaala
      601 qqgptpivvp psslpagssa qvppprvaae pastpaaeaa apapqvattv tnaapppaga
      661 spaiapagsl daservvnvp pseaavppvt tpspapkppd sqtavaavna lpaeqqprap
      721 kaqetvqvrf nvrpwgdvyv ngarrgaspp lrsvsltpgv yvieirngsl pplhrtvaid
      781 fgskpvnidy afe
//
LOCUS       WP_175850537             318 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cepacia].
ACCESSION   WP_175850537
VERSION     WP_175850537.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..318
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33566
     Region          80..293
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mlepeiaafv aavdawypad aaerapaeqr rlydrfaaew tpaalpagiv qqdavwqapd
       61 graialrryt saqgaprgtv lflhgggfvv gsldshalit aqlaadtgld viavdyrlap
      121 ehrapaaled clavtraard arwpfgpcah pltlagdsag gmlaaavata lrdtgegdvd
      181 gialvypmlg fepqsparet eahapmltld dvhryralyw ngdlsdalgd gnpllrasvp
      241 laaarfdglp pvlaigaehd plrddarvyv eriraaggaa hywmgeglvh gcwralgtsp
      301 qaarmhrtvg gfllapha
//
LOCUS       WP_175850554             267 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Burkholderia cepacia].
ACCESSION   WP_175850554
VERSION     WP_175850554.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..267
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27613
     Region          187..265
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mstaafgarq atgvrgaagd rarhrgacva lvfavvcalh aalfvllahq qivrreplqr
       61 qvmvatliaa vpeastmaaa kakpvaasra vqearsaprs sagsalrtnr qvasgrtrpp
      121 ahdapvpapa rpdpsppava qrdtsrgdaa armptqtqtp tptqpesrss svsapprfva
      181 hpdcalvkpd yppqslrlge hgtvlvelet datgqivaar vvtgsgyprl daaareavla
      241 srcaphvfdg apvptrarap iafnldd
//
LOCUS       WP_175850568             357 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia cepacia].
ACCESSION   WP_175850568
VERSION     WP_175850568.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..357
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38394
     Region          3..334
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,226,287,308,310..312)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,174,177,179,226,233,287,308,
                     310..311)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,174,177,179,311)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            179
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mdalftparv grytlqnrlv mapmtrsraa fdgtpgalaa eyyaqradlg livsegtqps
       61 ddgqgylttp giytdahvag wkavservha rgarlfiqlm hvgrmshpdn tphhrqdvap
      121 saiapgvpmf tmkgmqeipa pralttdevr gtvndfrfaa rraieagadg veihgangyl
      181 vqqffapnan trndayggsi enrarfaiev aeaiadeiga drtairlspg ttlwgidega
      241 dgpdlyryla tqldrlglay lhvmhqgnep lladlrarwn gtlivnrpgr trdaigtdva
      301 tgladleayg qmvlanpdfi trlktgapmn daqrdtffgg dargyvdypa ldgaaaa
//
LOCUS       WP_175850628             254 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF899 domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175850628
VERSION     WP_175850628.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..254
                     /product="DUF899 domain-containing protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28472
     Region          1..254
                     /region_name="COG4312"
                     /note="Predicted dithiol-disulfide oxidoreductase, DUF899
                     family [General function prediction only]"
                     /db_xref="CDD:443453"
ORIGIN      
        1 mtthltgtrd ewlaarrall daekaltrqg delarrrqal pwvrvdktyr fdtedgpatl
       61 gdlfrgrsql lvyhfmfgpd ykagcpscsa ladgfdgfav hlanhdvtla avsraplakl
      121 layrqrmgwr fpwassvgsd fnfdfnvsft etqqragave ynyalagham dmdpppapvv
      181 qfaatcgtda rtysldrpgm safvredgav yhtystyarg ldglwgmyqw ldraprgrne
      241 agpwwrrhde yarg
//
LOCUS       WP_175850601             143 aa            linear   BCT 11-JAN-2025
DEFINITION  GFA family protein [Burkholderia cepacia].
ACCESSION   WP_175850601
VERSION     WP_175850601.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..143
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15223
     Region          3..130
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mtrtysascl cgtvtvtlrg epaaranchc atcrdfygtp vlsatawppe qvavegghat
       61 fphpaksmsr tycascgeiv cgtnrfgmrv vptslaarah ggqlpgdlqp tmhlfyrhrv
      121 idvvdalpkf ldgwdgptld dan
//
LOCUS       WP_175850710             304 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175850710
VERSION     WP_175850710.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..304
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31793
     Region          5..298
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhdhhevivi ggsfagvsaa mqlararrrv lvidagrprn rfaahahgff gqdgkppaqi
       61 veeaaaqlaa yptvrriagd artaerdadg rfhvtladgs rasadrlila tgirdelpal
      121 pglaerwgvs vlhcpychgy evsgrrlgvl athplsvhqa ilipdwgptt wftqgvvean
      181 heeaalldar gvrierspvv eilgdaprie alrladgqvv pvdalfvgar tamasdlaqq
      241 lgcafddgpl gpvvrvdagk etsvagvfaa gdastpmsna tfasasgvma gvaahrsliv
      301 glra
//
LOCUS       WP_175850745             211 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175850745
VERSION     WP_175850745.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..211
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22471
     Region          5..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkvsktqvae nrlailqaaa rlyrergftg vgvaditrea glthgglyrh feskdalaae
       61 aaeyafewkl seletpdada ntdadgflrt gvanylspqh rdsvgqgcpv aalaadaare
      121 tgaiadafaq gigrymtlfa qrrpdgteaa qiepedrvra ismlstmvgg lilaratarg
      181 lpelsdeila tlrdhlaatw gldkanvdgr d
//
LOCUS       WP_175850764             430 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175850764
VERSION     WP_175850764.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..430
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46451
     Region          17..419
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(31..32,35..36,39,71,121..122,124..126,129,149,
                     152..153,156,244,247..248,251..253,256,284,288,345..346,
                     350,354,370,373..374,377..378,381)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mqsavvgavr aaasryrwtv callffatvi nymdrqilgl lapmlqhdig wtqvqygriv
       61 mafsafyalg llgfgrivdw lgtrvsyava mlvwsiaaml haavgsvmgf afvrallgig
      121 eggnfpaaik ttaewfprre ralatgifns ganigavfap aiipaiavay gwraafviig
      181 aigivwlavw lvlyrqadtr alaaeydepr deaealdaan anagaprwge lirkretwaf
      241 ltgkfltdpv wwfylfwlpk wlnesrgmdm qhiglplvci yalttvgsig ggwlssmllr
      301 agwsvnrark tamlicaccv lpiafvsqvq slwvavlivg laaaahqgws anlfttasdl
      361 fprravasvv giggmagsig gvlfsevigq vlqrtghywv lfaigasayl lalavmhmlt
      421 pkmkpaqlda
//
LOCUS       WP_175850765             177 aa            linear   BCT 11-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Burkholderia cepacia].
ACCESSION   WP_175850765
VERSION     WP_175850765.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..177
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18655
     Region          1..165
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtpahlipsp lgdiavried daltglyfvg qkyfppvaiv teadalatpp iarkvaeeia
       61 eyftgtretf svpiqlrgta fqrrvwkell aipfgelvty gditervglp msgaravgga
      121 vgrnpvsimv pchrvvgasg sltgyaggid rkrallsleg agfergtgds vqqalaf
//
LOCUS       WP_175850779             922 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia cepacia].
ACCESSION   WP_175850779
VERSION     WP_175850779.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 922)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 922)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..922
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=98910
     Region          18..834
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msiatalrnf asglvdwntr pvalhfgqaq havghllalh hadireglms gidgqltcis
       61 thahlaptlf lglpvsvrlt tdrgdvrain aivhdvqagq sdgeltvyql ricdalslmd
      121 rrinsrvfrs rnvidilgtl lnewrqrsaa larafdfdls glraerypar eltrqvnesd
      181 arfvrrllrr egitvfakaw avdnargstd erpihtlvfc ddplrlpesp agtvrlhprd
      241 sgtaqrdtvt lfahrqrlsp gkagrpswdy kkarmddsai atsidqgdag ndlarlltdv
      301 aidiphvgds wndhdrithd rilahqfaae rydgighvrd mpvgcwftlt gdpeldmkpa
      361 eqrqfvvtsv rhdvrnnlpk dltsrvttly aasrnlaqad pttpgdapeq sdtryenhft
      421 cvrrgvpltp sydpridlpp vhlltgtivg tqgeevfcda agrvrvrihg fdpadhehaq
      481 gagtngsagd sapirvgasl aggnfgtlfl prvgmevllg clsgdpdrlv iigvlsngan
      541 ppatfthtga lpgnryvsgi ktkeikgdry nqlrlddtps qisaqlaseh ahtqlnlgyl
      601 tqprkdghga grgegaelrt daaaalraaq gilfstyart ratggqldrd eliqlldqcm
      661 mlfnslgdha gqhggraadt agqekivdaf rhwkpdladt gsagdtsalm afgaqagslh
      721 vtprthvmya genidqiaqr hvqvasgeri nlhaghgvam fahsggvsai anrgkvtiqs
      781 qdddtqvdsa kniqltaagg klagmandqv vfvtsggayl klnggdielg cpgtftvksa
      841 ghawggpasm stdmpafdha plgrvpklvr stdgdavagf dgqtqrgaga psnlttdaag
      901 elpavhgdrf dtlsvqfikk dg
//
LOCUS       WP_175850793             336 aa            linear   BCT 11-JAN-2025
DEFINITION  sodium:calcium antiporter [Burkholderia cepacia].
ACCESSION   WP_175850793
VERSION     WP_175850793.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schnetkamp,P.P.
  TITLE     The SLC24 gene family of Na/Ca(2)-K exchangers: from sight and
            smell to memory consolidation and skin pigmentation
  JOURNAL   Mol Aspects Med 34 (2-3), 455-464 (2013)
   PUBMED   23506883
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Besserer,G.M., Nicoll,D.A., Abramson,J. and Philipson,K.D.
  TITLE     Characterization and purification of a Na+/Ca2+ exchanger from an
            archaebacterium
  JOURNAL   J Biol Chem 287 (11), 8652-8659 (2012)
   PUBMED   22287543
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..336
                     /product="sodium:calcium antiporter"
                     /GO_function="GO:0008273 - calcium, potassium:sodium
                     antiporter activity [Evidence IEA]"
                     /GO_process="GO:0006874 - intracellular calcium ion
                     homeostasis [Evidence IEA]"
                     /calculated_mol_wt=35425
     Region          19..332
                     /region_name="ECM27"
                     /note="Ca2+/Na+ antiporter [Inorganic ion transport and
                     metabolism]; COG0530"
                     /db_xref="CDD:440296"
ORIGIN      
        1 mtfmfvelav mlivilvaae vftnalehlg erlkisegvt gslfaavgta lpetmvplla
       61 laggtanpav neeigvgail gaplmlatlt tflmtlavir srgprgtiap ertgfvrdln
      121 yflaafslat aamfvphhns avrallaaml vwiyvmyvvm tfrasnrlvd aghgteaphk
      181 mflsrvglpt nlatialqll igvallvgga kgfihgvegv shvlgvsall lsliivpiat
      241 elpekvnsvl wirrgkdtla fgnitgamvf qgtllpaigi mltpweprle vltgvivtla
      301 aaawlrvnar trglaiwall angagyaayl fltlar
//
LOCUS       WP_175850857             509 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Burkholderia cepacia].
ACCESSION   WP_175850857
VERSION     WP_175850857.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..509
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53786
     Region          16..492
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(73,75,79,82,86,119,122..123,132..139,144,147,150,
                     243,247,250,253,255,428,430..431,433..434,437,440..441,
                     443,445..448,457,461,463,477,484..489,491..492)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(159..162,170,185,188,218,235..238,241,259..261,293,
                     393,395,421)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(162,259,290,293)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnanptprtg qdvptvklli dgafvesatk ewrdivnpat qqvlarvpfa tveevdaavq
       61 aahaayatwk ntpiaarmri mlkfqdlvrt nqqriaktlt aeqgktipda egdifrglev
      121 vehacsigtl qlgefaenva ggvdtytlrq plgvcagitp fnfpamiplw mfpmaivcgn
      181 tfvlkpseqd pmstmelvel aieagvpkgv lnvvhggkev vdaicthplv kaisfvgsta
      241 vgthvynlgs ahgkrvqsmm gaknhavvlp danreqtina lvgagfgaag qrcmatsvav
      301 lvgeardwlp dlvakakllk vnagaeagtd vgpvvskaak arilslieag vsegakleld
      361 grdvkvagye sgnfigptif sgvktdmsiy theifgpvlv vleadtldda ialvnanpfg
      421 ngvglftqsg aaarkfqsei digqvginip ipvpvpffsf tgsrgsklgd lgpygkqvvq
      481 fytqtktvta rwfdddttag pvnttirlh
//
LOCUS       WP_175850922             700 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia cepacia].
ACCESSION   WP_175850922
VERSION     WP_175850922.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..700
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73343
     Region          38..634
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mheaadqtra vaapprrltr aaaaliarid iftprgayva rsviaaalal gvayllelet
       61 pysaastvll vinpvqgavi gkgvwrvvgt iagmvvafvl mgcfaqqpll filgfafwlg
      121 vcvagmtllr hfrasgtvva gytiglatyg amqhpeltfe hvigrgstva igvlclslvs
      181 mllgtrdvha kldalvtrit advarviaaq rnglaaapad dkrhalfagi ygiddllalg
      241 kaesedlaqr aaavrhgmas lfgalaggmp plpadspgar avaslqprla aawqaaadal
      301 gdgpggatha rallgdarer lrdaldgial sdprdeaall iagerlieqi ddyraaldgl
      361 velqrsrpgy rparvrfhrd tgaalrngvr aacaivisga fwlatgwnqg dmmllvvapy
      421 callatagnp aagaqafikg tvlavpaafv cafgilprie gfpllvvalg lfwmpgiyat
      481 sapktalagl aylvafntlt gatnpfrpdv alflnqsvaw vlatfltllt frlilpgnla
      541 tdatrlrrti rddtlalvag rrvtaagwqq rqqhriaqlg allagqpaam tqasiealaa
      601 lhvgkellri rrgaardglp dparrcvrag laglarhaaa ppraarharr aahalaglaa
      661 aqpgntelkw lmaafadvhv llhtyaayft avperardaq
//
LOCUS       WP_175850998             378 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrolipoamide acetyltransferase family protein [Burkholderia
            cepacia].
ACCESSION   WP_175850998
VERSION     WP_175850998.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..378
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40212
     Region          1..376
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mieftlpsmg admdegtlle wkvkpgdvvk kgqvvaivdt skaavdvesw hegtvdelfv
       61 npgeripvgt pmatllepge appaerhtrq paapvaaaga aprrkispaa rklaqqhrvd
      121 pdsvtgtgpa gsvtladvdr tiaaagspaa gtpgerfpem rrviaaamer skreiphyyv
      181 setiplgkal awlaaenamr svtdrllpaa lllkavaltl rrfpelngfh regifrpaga
      241 vhlgvaislr qgglvapall dadakplnql mrelldltqr cragslrsse lsestitvtn
      301 lgdrgaaevf giiyppqval vgfgritvrp waedgglkim pvttttlsad hrvsdghrga
      361 lflvelgell qhpeelnq
//
LOCUS       WP_175851006             376 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia cepacia].
ACCESSION   WP_175851006
VERSION     WP_175851006.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..376
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40499
     Region          23..339
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mrtavlrqpr rlgsvcrvap apwaltddqr nlyiasqrfa rnrlepllag apsvaawqet
       61 vrlaaatldl gamvlpeehg glgidrhgla lvvealaagp leraleltlt aptlmvlrmh
      121 nalgpvlarp vqayfdgtta ialsvpsidn atiwqlgplg gagiltarid akrrlllter
      181 phdqrpsrst giatlgtlvl eqlhsdeaaa etplaviara dsdsvppaqk ymteiglyla
      241 alltgamqhs vrfafdyatt rqafrkplas hqlvaarlsd mlivthgthl flqavrtarp
      301 sapvplvrql lrhvaaesvs vsrefvqlcg ghgyveglpp aarfqtghwf afllqridta
      361 lgwlaepqma neevdg
//
LOCUS       WP_175851012             707 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia cepacia].
ACCESSION   WP_175851012
VERSION     WP_175851012.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..707
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=77104
     Region          87..>677
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msfapnggpp gglggspfas lsalgglagp vastvagnig plagvaghld tvqramqlaq
       61 tgfslmektp ssiadainta tgggakltql nryvtletpl gpdvllvsaa ivdeyvnrlp
      121 eihldllsha hdltpdklig qpvklkldhq aslstleriv atgggddvry fdgyvssfdr
      181 agnpgrvtqy hmtvvpwfwf ltrstdcrif qnktaqdilr eifqehgfad fafdihsgqk
      241 pleyvvmyqe syfnfcarlm eqegliwthr yekdkhilai gdsnlafkpi dglasvpfad
      301 sqssefngid qlhegrrfgv gkvtyrdfnh qqpssplmlv eagpqnldha rlgtteryeh
      361 qslydhsddg nryaryamea eeaqahrfvg rgfawrmtta grvsvtghpv lannqdyavl
      421 hvrheavndy tqhasklpyr nsfsllpiki pfrpqrttpk pvvngtqsai vvgpkgeqih
      481 tngscvklhf lwdrrgkmdg sdsmwirvsq pwagagwgaa aiprigqevi vsfnqgdpdn
      541 piivgrvfng eqgnpyhgaa gqtmgiksqt hkgeggnell msdvngaqml ymhaqkdmht
      601 vvqdaqstkv lkgdrtiqva qgnhettvsv gnqtdvvaqg ntlhqtpqgv htieakelwi
      661 kiggddgtki hmtgdtieiy kggsiirine smiiaqaptt hinpnng
//
LOCUS       WP_175851035             555 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175851035
VERSION     WP_175851035.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..555
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=59924
     Region          1..540
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 msydfiivga gsagcilanr lsesgrhsvl lleagerdas fwfkvpvgft ktyynrrynw
       61 myysepeaql adrklycprg kvvggsgsin amvyvrgqrs dyddwaaagn pgwayddvlp
      121 yfrklethaa gatdprhhga tgpihitsmk advhpivhef lkgcgelnlp rtddfngaqf
      181 egagiydlnt kngercsssf aylrpalgra nltlrpgalv rrvtfdgtra tgvvvagahg
      241 detlvaarev ilaagavdtp kllqlsgvgd pallarrrvp lvhalpavgr nlqdhlcvsf
      301 yfkanrptln demgtllgkm kiglrylltk rgplamsvnq aggffrgtdd ahepnlqlyf
      361 nplsyripks drasikpepy sgfliafnpc rptsrgtiei asnraedaak ihvnalttqk
      421 dldeavqgsk viralmrapa lksmtveeis pgpqvdsdea mlqyfreqsg siyhlcgsca
      481 mgpdaatsvv daslrvhglq alrivdasvf pnitsgnina ptmmvaekga dliladaghg
      541 easavsaser etvth
//
LOCUS       WP_175851055             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cepacia].
ACCESSION   WP_175851055
VERSION     WP_175851055.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22070
     Region          2..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 midlstlalf sgaclaltat pgpdmllias rsvsqgrrag fatlagiqag tychalaaal
       61 glsqlfvavp laydavrfag aayllylawk tfrsdatals pvasprrhst atifrqgltt
      121 nllnpkmalf vlalfpqfvr pehgsiavqi lvlatvlnli glvvngavil sasrlsqrig
      181 arrrpsklpq yllgsvfvgl aarlavaerq
//
LOCUS       WP_175851072             289 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia cepacia].
ACCESSION   WP_175851072
VERSION     WP_175851072.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..289
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32089
     Region          11..277
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mfldqlhper wtflwnalst lslklsagla llvvgwwlsk rignwlnrll snkervddtl
       61 rpilcdvavw girivaivga lsqlgietas ivavlgaagl aiglalqgtm qniaagimll
      121 llrpfkvgdy idggtgvagt vdevglfmtr ltkpdgicey vpnsalwgss irnytrnptr
      181 rldlevevsv hddidralda lrklaladpd vlrepepdvm vmrfddstav anmrvwthtd
      241 kfwamrwrla rqvrktlada dcvlpirare lhivhdaerr adstrvhal
//
LOCUS       WP_175851082             339 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Burkholderia cepacia].
ACCESSION   WP_175851082
VERSION     WP_175851082.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..339
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39262
     Region          99..255
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mptelmtwlh aflgndvdwk qvlligmtpv fliafaieya vmtgrgrrep frwkeivanl
       61 slgagyqvae tvmgllftga ifawvyrhrl fdmpvnglti vpifvvvefc yywfhrtshr
      121 vrwfwaahvp hhsgevmnft tamrqsllna fvgvflfylp pvwfgippav vlfllavdlv
      181 yqyfvhteai grlprwfeyv fdtpsnhrah hgrnpryidr nyggvlivfd rlfgtyveet
      241 epvdygitqq irsynflvln lhefvdmwrd vfapgpilqr lkhlwmppew erpghrpiht
      301 wsverkseed iaiaahamad dgapaqgrki vqatptrsg
//
LOCUS       WP_175851086             326 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175851086
VERSION     WP_175851086.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..326
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35335
     Region          12..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,232,249,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,195,
                     226..230,237..238,241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 medldgglvs gllvlaalae sgsfgraasr rgrtqpavsr aiqrledrlr aklvhrtsrh
       61 vevtdaghel lskvlpllqg ieeatagtsg qasvasgtlr vacdaafarl vlapelarfm
      121 kehpalhlkl etrndlsdlv sdgfdlairf gppsvstlvc rrlysprvlt vaapsylerr
      181 grprspqdlv ddghecilai dpatgrpfdw efwrdgektk vavtgsltvt dagtkigacv
      241 agfgiaqvid lgidthlrag tlepvltdwc detfplyvyy psrnhvpakv rtfidfvvgm
      301 mprlqsngyg acrqppsavl etlrre
//
LOCUS       WP_175851087             375 aa            linear   BCT 11-JAN-2025
DEFINITION  J domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175851087
VERSION     WP_175851087.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10644999
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..375
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=42757
     Region          <115..>201
                     /region_name="PspC_subgroup_1"
                     /note="pneumococcal surface protein PspC, choline-binding
                     form; NF033838"
                     /db_xref="CDD:468201"
     Region          <210..250
                     /region_name="DnaJ"
                     /note="DnaJ molecular chaperone homology domain;
                     smart00271"
                     /db_xref="CDD:197617"
     Site            order(226..228,237,243..244,247..248)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
ORIGIN      
        1 mtarrgaavv iapghetarl staqktfntl vqqiearrer lgawdavtpa fhkkfvdgll
       61 pleqaatalr isllnrldda flqkglskae qrtlsdvian mardlldvsd naqlkilynr
      121 hrasgdddrt aadrarpkqa pepapaptqe ddldtlspde laermqaeld eqfrrdmaeh
      181 eareaqrakr kkaprqsaaq arreaeqaes sksirdvyrk lasvlhpdre tdpkeqerkt
      241 vlmqrvnhay akgnllqlle lqleieqidr raidglgedr lmryngilee qvreldqeir
      301 hvethfrrty giassvkiap dtvmriltrd iagmqrsnqd ltiavrefdd pdnvrewlkd
      361 mkrrpassrf dddsy
//
LOCUS       WP_175851093            1014 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding and (Fe-S)-binding domain-containing protein
            [Burkholderia cepacia].
ACCESSION   WP_175851093
VERSION     WP_175851093.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1014
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1014
                     /product="FAD-binding and (Fe-S)-binding domain-containing
                     protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=110360
     Region          24..539
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
     Region          492..1013
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mtsavspslv rpvhlvpsqg aalsplferl rremrgdvya drasrgryat dasiyqimpl
       61 gvvvprdqdd lrialdiard rkipvlarga gtsqcgqtvg ealvvdnskw lnrivafdaq
      121 artvtvepgi vldhlnawlk phglwfpvdv staaqctigg magnnscgsr sieygnmvhn
      181 vlaidailad gsecrfgsla qpvtdrrtld llhgveriak rerdeiverv pkvlrrvagy
      241 nldlfdcqnp raytddghan lahllvgseg tlahsrqitl klaplpahkt lgvvnfptfy
      301 qamdtaqhiv klkpvavelv drtmidlsme npafrpvier alvgrpqail lvefagesrd
      361 aqhtqldrla elmadlglpg svvkmtdaga qkalwevrka glnimmsmrg dgkpvsfied
      421 cavplehlae ytrrltdvfh rhetegtwya hasvgtlhvr pildmrrdga trmreiaeea
      481 aalvreykga ysgehgdglc rgewvawqyg prlnaafaei kklfdpdnrf npdkivnppk
      541 mdarehfrfa pgyaalplrp aldwsawnvt rnpltgeeta pgsgtdvthg lasavemcnn
      601 nghcrkfdag tmcpsyrvtr deqhvtrgra ntlrlavtgq lgadglagdd vkaaldlcvs
      661 ckgckrdcpt gvdmarfkie arhawsrkhg ttlrerlvay lpryapwaar lrgaiafvng
      721 vpvvassikr wiglapqral pgfarpflad vgagagagas tptqtgsatr evllfvdtfs
      781 nyqepdnara aqavleaagy tvhfnvraga rplccgrtfl aaglvdeaks earrtldalr
      841 pylergiaiv glepscllsm rdeflaygyg deatrlasha flleeflvre heagrlslpl
      901 haidanealv hghchqkafg aftpvqtvlr wipglkvspv essccgmags fgyeaehyaa
      961 sqamaelsll pavraraega ivvadgtscr hqiqdgaqaq avhvakvlar alrs
//
LOCUS       WP_175851127             206 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175851127
VERSION     WP_175851127.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22854
     Region          12..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mptptddpgr rarkriqmla hlaatgarlf dahgyeavtm eqiaaqadva krtlynhfat
       61 keavlahwle gelardlahl qrdvarrntf vsrigcvlda saawceqhpa yllaylrhrf
      121 lsigvaepes gnengsniaf vwqqliaagq qsgelngtlr adqlatwfhh lylaamlrwl
      181 tvpglslkre fqavaklfve gaeakr
//
LOCUS       WP_175851173             326 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175851173
VERSION     WP_175851173.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12168323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..326
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34940
     Region          22..202
                     /region_name="AraC_binding_2"
                     /note="AraC-binding-like domain; pfam14525"
                     /db_xref="CDD:434015"
     Region          253..324
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdialsrhap nrlgtlhapd everavahrl gphrmaargr dpfhaelyev plhhgallel
       61 cygretridf gddaghflfr ltlagacelq agsvvaragp geltvsspal asrlstspdc
      121 rnlvlrlerg alerklqhml rapltrplqf dlaasgigtg tgaalvlptf eylcrlgaqp
      181 rigtasplfg adltawlmsl llthlphsys dalargtppl pahvrracdh vdahlgepla
      241 laalaavagv aprtlqhafr aflhttpaay vrerrlaavh aalqrgdtcs vtdvliahgi
      301 hgfghfakay arryghapsv tarqsr
//
LOCUS       WP_175851184             569 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175851184
VERSION     WP_175851184.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..569
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=61971
     Region          22..529
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 msrtfdyivv gggsggcvva grltedpavt vcvleaggrg dgtlvnvptg avammptrvn
       61 nwafdtvpqh glggrigyqp rgkalggssa inamvyvrgh rvdydgwaal gnegwayddv
      121 lpyfrlsehn erfddawhgr dgplwvsdlr tgnpfharyl eaaqqaglpl tddfngaqqe
      181 gigiyqvtqk hgerwsaara yllphigrrd nlavethaqv lrilfdgtra tgvevrqhge
      241 vrtlrarrev vlaagalqtp qllmlsgvgp ggelrqrgia vhadlpgvgr nlqdhpdfif
      301 gyrtrsvdtm gvsargglrm lrelarfrre rrgmltsnfa egggflktra dldapdiqlh
      361 fvvalvddha rklhaghgls chvcllrprs rgsvtldsad plaapridpa ffddprdldd
      421 mvagfrltrr lmeapalagw ttrdlftanv dtadeirdvl rrrtdtvyhp vgtcrmghda
      481 lavvdpqlrv hglqglrivd asvmptlvgg ntnaptimia ekavdlirgv crtsarpqre
      541 tvrittdtvp asraaheavq peetrhvva
//
LOCUS       WP_175851207             603 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175851207
VERSION     WP_175851207.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 603)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12379621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..603
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62881
     Region          1..284
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
     Region          329..603
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 maswldytln glivgniyal lavglalifg vshlinfahg svymvgafig wlcltrfglp
       61 lpvalaavvv gcgalgvaie riglrplrha ariapllati gisfildqla qlafgadpra
      121 vptplpdwhl riagatlgsl dlliagigia saallygflr ftrlgwavra taqdrdaalq
      181 mgvdvdrvnq tvfaiacalg gvsgllvgmy ynsidpamgf qatlkgvval ligglgnvpg
      241 aiagslllgl vesygvalfg tsyrdlfafg llivflvwrp nglfsgnrtl ppepmtgtfl
      301 aaakavrvpr pvlvaliala avlpwlgasp yvlqtltnaw lygllalslt lvagtvgqis
      361 lghaallvig ayasallssd lgwspavtip cagvitavlg tllvypafrl rghyvsiatl
      421 gigevvslvi lnwdgltrgp lgitgiaplp wastaraayw ftfavlvafa lvqvrllrsh
      481 lgrtlravre ddvaarthgi apnrykaiaf avggvaagvs ggiaahlysy inhqtfdsqv
      541 silaltmvil gglgnvlggi vgaialiglp elfrwaadyr mliyglvlll lvrfrpqgll
      601 gtv
//
LOCUS       WP_175851238             726 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cepacia].
ACCESSION   WP_175851238
VERSION     WP_175851238.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 726)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..726
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78009
     Region          43..726
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mvtgtgaakr amaiaaggal yvaaaggaha qasgaaaapp aavlpeidvt gkgdrsssgl
       61 vglrttagtk tdtpvaevpq tinivtaqqi emtgatdlnq alryvpgfat fgadsrtdsy
      121 aalrgftptl yvdgvaapht aviadwrvdp ytidsiavlr gptsvlygag epgaivdaht
      181 kladgervre agvqigndar kqfmvdvgdt ldpdgryayr fvgvardgna etgpngdrrv
      241 alapsfrwrp nadtsltlsa tflqdssdis snflpasgtv lpnpngrlsq diymgdpgfn
      301 dyrkkqwslg yalehrvnai wslhqdvrws hlslddatvf gngfaprstt nmmrtaglfq
      361 lnysrldidn haqarfgtgp lehtlllgvq ydrqtttnsv wlaiapslnl yhpvyrpvtd
      421 aifagptslg hvdqytamnt fgvyaqdqir wkrwmltlgg redfvnarfd drtagkqarq
      481 dvsafsgrvg ltyrgdagls pyvshstsfd pvigvrlygg glpkptrgtq teaglrwqpp
      541 grnlmlsaal yqidqtnvat ptpvnldptg ttsvqtgkvr srgielsavg kvtrelsiva
      601 syvhqdvknv qandaslnhw pvavplprqm asmwadwtwr tgalsglgfg ggvryqsasa
      661 gapdnsltvp svtlvdlalh yemphwrfal nvanlfdrry vsgcqsynvc vfgnertvla
      721 sakynw
//
LOCUS       WP_175851242             175 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia cepacia].
ACCESSION   WP_175851242
VERSION     WP_175851242.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..175
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=18597
     Region          20..162
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 metiatappt ldpmqlraaf gqfptgvtvi ttsaadgrkv gltansfssl sldpplvlws
       61 lrklapsrpd fvaathfain ilahdqidls rrfatpsadk fdgvphadse aggvpcldga
      121 sarfvcrnvg hyeggdhllf igqieqfdaf gkaplvfhag qyraiadhpd lfrav
//
LOCUS       WP_175851244             325 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia cepacia].
ACCESSION   WP_175851244
VERSION     WP_175851244.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..325
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=36595
     Region          113..322
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mntifygfvi ltfvavvlai eggyqwwnar hgaaarries rirsmsaggn vqqerlsilk
       61 krmldeskpf drlllrvprv hrldlviqqs gldwtlpkli mlstvftafa wlvlsfatlp
      121 qlavlplalf agcapvmyvl rcrgrrmrkl erqlpdicdm iaralrsghs ftstlgmvgd
      181 efpdpmggef rvtfdevnyg vslhdaltnl atrvpvqdlr yfviavliqr etggnlaell
      241 dsiaalirer fklfdkvrvl saegrlsawi lgllpfgtaa vmavlnrefl svlwedpagi
      301 rmvgtmlvsm lfglfwirri vrirv
//
LOCUS       WP_175851245             455 aa            linear   BCT 11-JAN-2025
DEFINITION  CpaF family protein [Burkholderia cepacia].
ACCESSION   WP_175851245
VERSION     WP_175851245.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..455
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50588
     Region          54..438
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mslreqmslh raqphaagse pagpahssvr dayqklrrei hlavlervel erlsrmpqea
       61 vrmeigalia rildeerlpa ndierrqlai dvydemfgfg pleallrdpg isdilvntyr
      121 qvyveragql eltdvtfydd ahlmkvieki vsrvgrride sspmvdarlp dgsrvnaiip
      181 psaidgplms irrfavnplk mddlvryhsl tppmaellda lsrakvnvlv sggtgsgktt
      241 llnilsgyip rnerivtied aaelqlqqph vlrletrppn iegkgeitqr tlvrnalrmr
      301 pdriilgevr gaealdmlna mntghegsla tihantprda ltrlenmisv sgltlppktm
      361 rqqiasaisv vvqaarltdg krkivsiqel tgmegdiinm qeiftfkrsg vdrdgsvrgh
      421 fcatgvrpkf verlqafgin lpdslydpsq ryetn
//
LOCUS       WP_175851268             281 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia cepacia].
ACCESSION   WP_175851268
VERSION     WP_175851268.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..281
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30256
     Region          10..257
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(24,105,107,109..110,138,189,210,213,226,228,257)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 matltfpgqq vgdftitais dgyltasldf lsnidpadas nmqrdagqka peavhincyv
       61 vrgagrtvli dagaggfrqw ggqlgtnlal agiepaaidt illthahpdh vgglvngage
      121 iafpnaelvv hrrevgfwqd dgnlsraser argnfavarr vfdaygdrlr lfedgqvlpg
      181 idalpipght dghtgyvles rdqgllvwgd vvhfphiqiq rpevsiafdh daslaaatrs
      241 rlldqvsseg lliagmhlge rgfariermn ggyrlryere e
//
LOCUS       WP_175851286             424 aa            linear   BCT 11-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Burkholderia cepacia].
ACCESSION   WP_175851286
VERSION     WP_175851286.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..424
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44641
     Region          1..407
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mknrltlsia igmvlgvaag yachtsiadp gtlktvagyf sivtdiflrl ikmiiaplvf
       61 vtlvsglagm dsgedvgrig lrsvawfvca slvslglglv manalqpgag lnlteaagea
      121 nlglntaaln ardvithafp tslldamarn dilqilvfsv flgialsalk hdprvgivir
      181 sidgmvpvml rltnyvmraa plgvfgaiap svalrgldvi ytygkligaf ylgllvlwti
      241 ligagylflg rrvgallkav repaliafst asseaayprl teqlekfgvd kkvvgftlpl
      301 gyafnldgsm myqafaalfi aqafgvhmpl sqqvfmllil mlsskgmasv prgsvvvvaa
      361 vapmfhlpaa gvamilaidq vldmgrtmtn vignsvattv iakweraraa qpdsavfdpr
      421 elna
//
LOCUS       WP_175851316            1054 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cepacia].
ACCESSION   WP_175851316
VERSION     WP_175851316.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1054
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115073
     Region          11..1032
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mstpheegrf nlsawalrhq alvvyliala tlagilaytr laqsedppft frvmvirtfw
       61 pgatarqvqe qvtdrigrkl qetpaidflr sysrpgesli fftmkdsapv kdvpetwyqi
      121 rkkvgdigyt lppgvqgpff ndefgdvytn iwtlegdgft paqlhdyadq lrtvllrvpg
      181 vgkvdyfgdp dqrifievnn aqltrlgisp qqlgqainaq ndissagvlt taddrvfvrp
      241 sgqfdnvnai adtliringr tfrlgdlatv krgyddpvvt qmraagpgsa gkavlgigvt
      301 mqpggdvirl gkaldaeskd lqaqlpaglk lvevssmpha vahsvddfle avaeavaivl
      361 vvslvslglr tgmvvvisip vvlavtalfm ylfdiglhkv slgtlvlalg llvddaiiav
      421 emmavkleqg ytraraaafa ytstafpmlt gtlvtvsgfl pialaksstg eytrsifevs
      481 aialiaswfa avvlipllgy hmlperkrqa heahlpddhe hdiydtrfyr rlrgwidwci
      541 errfvvllit galfvvammg fslvpqqffp ssdrpellvd lrlpegasfa atlreterle
      601 kvidkrpeid hsvsfvgsga prfylpldqq lqlpnfaqfv itaksvkdre klatwlettl
      661 reqfpavrwr lsrlengppv gypvqfrvsg dsiatvrsis ekvaatmrgd artvnvqfdw
      721 depaersvrf eidqkkarel nvtsqdvssf lamtlsgttv tqyrerdkli avdlrapkad
      781 rvdpaklagl alptpngpvp lgslgrfkpt leygvvwerd rqptitvqsd vragaqgidv
      841 thavdaklna lraqlpvgyq iniggsvees akaqksinaq mplmaiavft llmiqlqsfs
      901 rvlmvvltap lgligvvatl lmfgqpfgfv amlgviamfg iimrnsvilv dqieqdiaag
      961 hgrvdaiiga tvrrfrpitl taaaavlali pllrsnffgp matalmggit satvltlfyl
     1021 palyatwfrv krderdpqng pppggstpaa psga
//
LOCUS       WP_175851323             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175851323
VERSION     WP_175851323.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13300132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33689
     Region          39..>154
                     /region_name="PRK11242"
                     /note="DNA-binding transcriptional regulator CynR;
                     Provisional"
                     /db_xref="CDD:183051"
     Region          103..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(113,117,156,170,172,231,248,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(114..115,119..120,122..123,126,130,132..138,199,
                     225..229,236..237,240)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 masdpipapd kpldlldval fvraallanv saagrefgvs aavasariaq lerqlgarll
       61 hrttrrislt qdgevfmaha dtllsaadaa rasvghgrte pygrlkvsms ssfgrqhvap
      121 vipaflrryp svsldlrlsd eivdlvddgy dvairlgalk dstlvarkla anrrvlccsp
      181 aylaghrtpr hpadltqhec vilgdqrdws fttpqgpltv rvggrlvasn geairealid
      241 gfgiaikstw dvgpllasga lvtilddypf addvaiwavy psrthvplkt lafiaflaeh
      301 fgdppywdra dgr
//
LOCUS       WP_175851338             360 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: C40 family peptidase [Burkholderia].
ACCESSION   WP_175851338
VERSION     WP_175851338.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..360
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37414
     Region          <7..176
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mlriwvpvav vsllaacssv ppqsasrpas gmrittpraf papanfpkfv dhsvgqeeis
       61 iqamslvgvp yrwggntpts gfdcsglvry vigraadvnl prttadmsgr gvsvepeqia
      121 pgdliffntt grphshvgiy vgklrfvnap stggtvrldy ltnpywakrf dgirrvappr
      181 gaptpfdapt yeakrdeprn spavaaapvv vtaataprqp atassqaraa qvqapapttp
      241 vvttaavapa apaadpyepp psrmqaaqqq atsmndemta ttanaapaat aevgtqiptt
      301 altaaqaaaf daepppatts mpprsiepvq vwrastqsap vsprtstadd piarfangsy
//
LOCUS       WP_175851346             146 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia cepacia].
ACCESSION   WP_175851346
VERSION     WP_175851346.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..146
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15431
     Region          17..144
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mtdgvvetgd wavlggdaar irdavfvreq qippeweldd ddplslhava yrvdaatgvr
       61 ravatgrllp sgmigrvavl adargqgvgs avldalldaa rrrgeivvrl yaqdsavsfy
      121 lrhgftavge pfveagvphv emarap
//
LOCUS       WP_175851373             160 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia cepacia].
ACCESSION   WP_175851373
VERSION     WP_175851373.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..160
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17224
     Region          14..134
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mtsgdplfti asidaaqthp lraaillngd lnacelagdh apttlhvgvr dgqsnivava
       61 slceeprddd parpawrlrg mavhpavrgm gfgrvlvqvc vrhaqahgaa lvwctareva
      121 yrfyeklgfa adgemvtmpg rtdtafyvmr ryidrhspaa
//
LOCUS       WP_175851399             523 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175851399
VERSION     WP_175851399.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..523
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52460
     Region          37..448
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,157,
                     160..161,164,288,291..292,295..297,300,328,332,384..385,
                     389,393,409,412..413,416..417,420)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msqsspasra gaaaaprtgg rmpaaatlav asatcslivl dtnvvavslp siarsfhasf
       61 adiewvvsay mtafaacllp aggladrfgr krmlgaglal fflaslgcgv apsagwliaa
      121 ravkgggaal lltaalavia nrfpdgrera rawaiwgmcm giatavaplv ggaitqwigw
      181 rwvfllnlpv cmllaagarv aidesrdpha krvdaagsll fgaalacaia aligapshgw
      241 lsaatlgrla laaalfaafv gaerwqarpm idlalfrqpr fvgavlamfg yaacaqvmmt
      301 flplylqnaf gmsaidaglg mlpfafamia gpslgaalaa rvssggvlag gltligagnl
      361 ataaltaagd yrlvaigmfv tgcgagimng dtqkaimacv pssrtgmasg istttrfsai
      421 vtavgvlgav laastqarld rllsaapglr afadapfmss llagdlaral ervppsaaga
      481 lakaapvafa sgfadaltvs gvlalvvavv awkllaqpmr dga
//
LOCUS       WP_175851404             135 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF427 domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175851404
VERSION     WP_175851404.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Lupas,A.N., Zhu,H. and Korycinski,M.
  TITLE     The thalidomide-binding domain of cereblon defines the CULT domain
            family and is a new member of the beta-tent fold
  JOURNAL   PLoS Comput Biol 11 (1), e1004023 (2015)
   PUBMED   25569776
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..135
                     /product="DUF427 domain-containing protein"
                     /calculated_mol_wt=14636
     Region          20..129
                     /region_name="COG2343"
                     /note="Uncharacterized conserved protein, DUF427 family
                     [Function unknown]"
                     /db_xref="CDD:441912"
ORIGIN      
        1 mpvspdtpar pvktpgpdhp itieshprrv vvkaagriva dtrralalre aaypavlyip
       61 redadltlll rtdhatycpy kgdcayysip vggeravnav wtyeapypav dairghlaly
      121 pdrvdsiees ptgsd
//
LOCUS       WP_175851411             318 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175851411
VERSION     WP_175851411.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..318
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34975
     Region          4..>170
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,223,240,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 meslrsmrvf vraielgnfs avareegtgq ptiskivaaf ekelgvrlle rsttslaptd
       61 egrrfydrck rvideyasav aevrgqtvrp vgklvvnapl glgelrlnal vleflaawpe
      121 ievelqltdr vidlveegvd vairlghllp pdvvarpias sprllvatpk yvaqaprlrr
      181 pedlarhayv gyaradigne lafargdeqv avpvrgryrv nssmalrecf lagnavgsgp
      241 awlvqdlids gqlvrllpkw dmvpphalhl vyasrqylpl rtrtflqfme qripglpgfh
      301 attaatansa arasrqsr
//
LOCUS       WP_175851412             359 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia cepacia].
ACCESSION   WP_175851412
VERSION     WP_175851412.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..359
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38024
     Region          8..321
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mtappssdaf dawleanada ldvdpsraad ilpqlvrsrt vavgvpevmg gtggtiadai
       61 dtvaavaqrs ltaafvlwgh rtfieyvlqs dndalrvrwl tplldgevag atglsnamky
      121 lsdieplqmh aarsgnafvl ngslpwitnl rregfiaaaa fdhddgtpps vfaiphdarg
      181 versddldli glrasntaal rvsdtvldes yrlaadapaw larvrpaflg lqcgmsigla
      241 rrallatqda sapsraslga eirelettla dqaaqlkrgv ldgtflhspa tmfelrialv
      301 etvsqavsle vqatggrgyl rgqsgsarrv reasfipivt pslvqlksql arhrraaaa
//
LOCUS       WP_175851436             427 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175851436
VERSION     WP_175851436.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..427
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45350
     Region          15..415
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(26..27,30..31,34,69,116..117,119..121,124,148,
                     151..152,155,243,246..247,250..252,255,286,290,341..342,
                     346,350,366,369..370,373..374,377)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mnwavtrigg rfhygwlaaa vvflillaaa gtratpsvlm vplerelgws raaislaisv
       61 nialygltgp faaaamqrfg lrptiltalv tmsagvalss mmtqswqmvv iwglmvgcst
      121 gvvaltlsat fvtrwfharr glvmgiltas tatgqlvflp mlaaiaqrhg wrpvvlvvav
      181 aaaiviplva fllperpadv qlrpygepad appapdptke nplavafrtl ltasrsrdfw
      241 llffsfficg astngyvgth liamcsdygm tevqgaslla amgvfdlfgt tlsgwlsdry
      301 dnrvllfwyy glrglsliyl phafgidffg lplfamfygl dwiatvpptv rlatdvfgka
      361 aapvvfgwiv aghqlgaafa algagllras lgtytiasmi sgglcivgal ivlrinrgps
      421 raaaqaa
//
LOCUS       WP_175851480             294 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175851480
VERSION     WP_175851480.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..294
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32519
     Region          7..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="PBP2_CrgA_like_7"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08476"
                     /db_xref="CDD:176165"
     Site            order(101,105,144,158,160,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176165"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176165"
ORIGIN      
        1 menlsgivaf vrtaealsfv aagralgisa savgktiakl eqslgvrlfn rttrrvtlte
       61 egrhfyercq riledfrdae atvtasaqrp rgrlrvslpv igyrfllpvl pefrqrypdv
      121 eldldfndwm vdvveggfda airsgplsds slmsrrlgpf afvlcatpay laragtprtp
      181 rdleahecvr ycfpttgklq dwalaaadgt paklrtaltc nnmealrgtv laglgigymp
      241 dflardaleh gtlvtvlddy riapgqfsiv wpssrqlspk lrvfvdflce rlfr
//
LOCUS       WP_175851535             148 aa            linear   BCT 11-JAN-2025
DEFINITION  GatB/YqeY domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175851535
VERSION     WP_175851535.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..148
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=15605
     Region          1..147
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 mslkeqised mkaamrakes eclatirllm aaikqrevdd qitlddagit avidkmikqr
       61 kdsisqfqaa grddlvakeq aelvvlsgym peqlseaeva aevqaavaqt gaagpqdmgk
      121 vmgvlkgkla gradmtaisa lvkaalsk
//
LOCUS       WP_175851544             243 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia cepacia].
ACCESSION   WP_175851544
VERSION     WP_175851544.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..243
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26321
     Region          165..242
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mpdthdwldi dyrtlfrlhp dhrierendp dcspgprfwl grcaernlag vradvpfpva
       61 eelarladse tpsadftqpa hlerylalla pvphwniglv yalphalgfd tdahvelidg
      121 dsdagrhllh alstrgmpeg lfsmgfqgas dlwapwcaav vdgevasvaf aarlsevgae
      181 lglatapafr grglaaavta awsrlpslrt rtlfystdsd nrasqrvasr lgltlcgttl
      241 rva
//
LOCUS       WP_175851603             352 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175851603
VERSION     WP_175851603.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..352
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35522
     Region          16..348
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mlksatpava pdapstrpal sasarlragl ertgillvla alvvvftvne paflnvdnlf
       61 silqavsiva llgigvtitl aaggfdlsvg siaasaqmaa syvlvvwhgs alaavaacva
      121 lgvaaglfng vlitrlrvpd qlatlgtlfl laglqliptg grslatgsvl pdgteasgmf
      181 pdaflalgrl rvfdvvplpv lilaavpvla cvameatrwg rviyaiggne taarlagapa
      241 aryrvaayvv sgaiaalggv lisarvgrgd vsaghsllld avaaalvgya vwgakrpnvf
      301 gtvvgavfvg vllngltmln apyylqyfvk gallvlalaf tfgigrrada ra
//
LOCUS       WP_175851617             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175851617
VERSION     WP_175851617.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33987
     Region          23..80
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          109..303
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(124..125,127..128,131,135,137..143,233..238,
                     244..245,247..248)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 misdqngefd sqsmranlps lmalrcfeaa arhenfsraa delclthgav sravrlledd
       61 lgvalfqrrs rrvfltdagr klaqavhdgl glmrhaaqel rteaararrw vlsceptllm
      121 rwliprwpdf qvrhagidvh laaaggpfsf dsgidmairr ndfawpagyh aerlfaervg
      181 pvcrpdnvda wfsarrgsrs lktdvpqlha rtrpdawkew avaahqpavr grgqvfdhfy
      241 fslqaavagl gvaigpwhlv rddiesgvlv apmgfvedgs hyclltpepv vagraqadvl
      301 awlrava
//
LOCUS       WP_175851618             210 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia cepacia].
ACCESSION   WP_175851618
VERSION     WP_175851618.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..210
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23054
     Region          1..210
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mtcvlyiegs pnkaysasid vcnafldayr hahpdheirk ldvwdlampe fdedalaaky
       61 aglsgtaltp sqaaawqrie qlaapfhaad kflfgvplwn fsipyklkhl idaisqkdvl
      121 ftfddagftg klagkkaavv yarglgyqsp gsftpaaefd lqrpymetwl rfvgvtdvtg
      181 ivvertlfga dgkvdrsrvi dearsiargf
//
LOCUS       WP_175851674             199 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cepacia].
ACCESSION   WP_175851674
VERSION     WP_175851674.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..199
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21251
     Region          2..195
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mptfqvmlkm alyvslvlat pgptntllls sgirvgfrqs spllvaeasg cgfaislwgf
       61 flatfaatrp wlydvlklgs sayifylalq lwksphldgi rsgtigfrdm fvattmnpka
      121 llfataifpp qafvsvpfyl csiavftvla vtigsmwlvv ggvltarrsl athtgtllrg
      181 asvvlamfag tlafsvlnr
//
LOCUS       WP_175851688             411 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175851688
VERSION     WP_175851688.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 411)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..411
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42971
     Region          56..411
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mnselssstp atqdadarrs sgheaghpag rstgsqlrqv fvrykilall lavaaiwvff
       61 svltdgafvt prnvsnllrq msitgmlacg mvfviiagei dlsvgsllgl lggvaaildv
      121 nrhwpvaatv pavlalgvli glfngwwsty rrvpsfivgl ggmlafrgil lgvtggstia
      181 pvsdgfvflg qgylprvagd glalllfalv allvvrqrgt rrryrlavap lwqdavkivg
      241 agavlfafva tldryggipv pvllllallg vfswiatqtv fgrriyavgs nleatrlsgv
      301 dtdrvklaif almglmcafa givntarlaa gspsagtmge ldaiaacfig gtsmrggsgt
      361 vygaligalv masldngmsm ldvdaywqmi vkgavlvlav widvvsrsnr r
//
LOCUS       WP_175851699             388 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Burkholderia
            cepacia].
ACCESSION   WP_175851699
VERSION     WP_175851699.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..388
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=41503
     Region          40..377
                     /region_name="AspB"
                     /note="Aspartate/methionine/tyrosine aminotransferase
                     [Amino acid transport and metabolism]; COG0436"
                     /db_xref="CDD:440205"
ORIGIN      
        1 mhhhrpvrlq hiagigvdrm gsiadhadvd llrlenldtd lpptsealaf treaiqrdsa
       61 nsylpfvgqd rlrasaaahv salsgqrfma dqvvvsaggl sgilntllat vetgdevivt
      121 dptyagllnr irlaggvpkq vpftftpgse wkldqaalra aigpktraml lmspsmpsgg
      181 ffdasdwqli aslcvqndll lildsamerl lfdgrtvihp aglpgmaert vtvgaaskel
      241 rmigwrvgwi vapewlipdl vavslanvvv pvgiaqgaaa valehsasdl pgyvselerr
      301 rdtvaaelsg lpfgmpaggw smllrvadfg ltgsqmserl lrrgvcatam tgwgvahgeq
      361 yvrfvfsnep vdrlrtlgdk vrfaleda
//
LOCUS       WP_175851715             241 aa            linear   BCT 11-JAN-2025
DEFINITION  copper homeostasis protein CutC [Burkholderia cepacia].
ACCESSION   WP_175851715
VERSION     WP_175851715.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Latorre,M., Olivares,F., Reyes-Jara,A., Lopez,G. and Gonzalez,M.
  TITLE     CutC is induced late during copper exposure and can modify
            intracellular copper content in Enterococcus faecalis
  JOURNAL   Biochem Biophys Res Commun 406 (4), 633-637 (2011)
   PUBMED   21362400
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Li,Y., Du,J., Zhang,P. and Ding,J.
  TITLE     Crystal structure of human copper homeostasis protein CutC reveals
            a potential copper-binding site
  JOURNAL   J Struct Biol 169 (3), 399-405 (2010)
   PUBMED   19878721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..241
                     /product="copper homeostasis protein CutC"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24355
     Region          8..237
                     /region_name="CutC"
                     /note="Copper homeostasis protein CutC [Inorganic ion
                     transport and metabolism]; COG3142"
                     /db_xref="CDD:442376"
ORIGIN      
        1 msrnaassil leviattvgd akaaaragad rlelvtaite ggltpsvgli eavvaavpip
       61 vnvivrphsr sfvydaddlr vierdvraav aagasgvvfg aldargdvdl galariaaav
      121 dgraltfhra fdvsrdlnaa fdallrvpav tsvltsgghp svldavatit rlvrqtagst
      181 ctvlagsglt vdavgdfvra tgvravhfgs gvrprgevla pvdellvakv ratidgaash
      241 v
//
LOCUS       WP_175851817             493 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54 dependent transcriptional regulator [Burkholderia
            cepacia].
ACCESSION   WP_175851817
VERSION     WP_175851817.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..493
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=53142
     Region          21..139
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <157..464
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mvarspeang htvpemthvs vtapedgrkl fvimrspdep llaqlrglgw eisvaktaga
       61 aqnmtsgvsv aaglvdfsgf tsreypalka clsqpsigwi siaqagvtig pavrelirsy
      121 cfdyvtlplp yewishvlgh argmaaldrv dgaayaasig ehgmigncea mqqlfstirk
      181 vaktdasvfi sgesgtgkel talaihersg rgkglfiain cgaiphhllq selfgyerga
      241 ftganqrrag riesanggtl fldeigdmpv esqasllrfl qegkierlgg qesipvdvri
      301 isathvdldg aveagrfrad lyhrlcvlri hepplrargk didilahyvl qkykadsgrk
      361 isgftsaald amrryewpgn vrelinrvrr aivmaesrll tphdlgldtp getepvtleq
      421 aralaertai enallrndhr inkaaaelgi srvtlyrmmi ehglndhdnn ggngdngghd
      481 gapsgdaghq rvg
//
LOCUS       WP_175851846             443 aa            linear   BCT 11-JAN-2025
DEFINITION  carotenoid oxygenase family protein [Burkholderia cepacia].
ACCESSION   WP_175851846
VERSION     WP_175851846.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Poliakov,E., Uppal,S., Rogozin,I.B., Gentleman,S. and Redmond,T.M.
  TITLE     Evolutionary aspects and enzymology of metazoan carotenoid cleavage
            oxygenases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1865 (11), 158665 (2020)
   PUBMED   32061750
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Sui,X., Kiser,P.D., Lintig,Jv. and Palczewski,K.
  TITLE     Structural basis of carotenoid cleavage: from bacteria to mammals
  JOURNAL   Arch Biochem Biophys 539 (2), 203-213 (2013)
   PUBMED   23827316
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Kloer,D.P. and Schulz,G.E.
  TITLE     Structural and biological aspects of carotenoid cleavage
  JOURNAL   Cell Mol Life Sci 63 (19-20), 2291-2303 (2006)
   PUBMED   16909205
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Wyss,A.
  TITLE     Carotene oxygenases: a new family of double bond cleavage enzymes
  JOURNAL   J Nutr 134 (1), 246S-250S (2004)
   PUBMED   14704328
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..443
                     /product="carotenoid oxygenase family protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006720 - isoprenoid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48426
     Region          8..439
                     /region_name="COG3670"
                     /note="Carotenoid cleavage dioxygenase or a related enzyme
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]"
                     /db_xref="CDD:442887"
ORIGIN      
        1 mtvfdlnrga iapvadeael vdlrvtgavp hdldgtllrn gpnppggrfe gndvlswwpe
       61 aamlhaiafe ggratgyrnr wartqrwaav hapgqaphlp dtnpnvnvlq hagellalae
      121 ggaplaitaa ldslgaparh agfgggmtah pkvdpvtgel iafradwrap wlrygvadaq
      181 gvqrveieid lnapsmmhdl aitetrslml dlnvgydfsl lkqghrmplr whddrparig
      241 viprhggavr wfgiepcfiq hvvnaydcda scivldavry pwflrldart grfadnpvge
      301 lwryvidtan glidegplad ggiemprine srtgrryryl yaveqpnnae mrgvmrfdha
      361 sgtttryavp agdqnsepvf vprpggvded dgwllvmvyr aatdtsdvvi ldaraidagp
      421 vatvhlprrv pagfhgawvp rer
//
LOCUS       WP_175851943             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175851943
VERSION     WP_175851943.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33839
     Region          <27..72
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          104..302
                     /region_name="PBP2_DntR_NahR_LinR_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators that are involved in
                     the catabolism of dinitrotoluene, naphthalene and
                     gamma-hexachlorohexane; contains the type 2 periplasmic
                     binding fold; cd08459"
                     /db_xref="CDD:176148"
     Site            order(110,112..113,117,174,210,277)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176148"
     Site            order(111,114..115,118..119,122..123,125..126,129..130,
                     132..136,138,200,227..231,234..235,238..239,242,256)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 mdnnaamsad lpdlkllqlf dllydvrsvt rvaeqlgqsq ptvsiwlghl rehlhdplfi
       61 rtpggmaptp qadaligpcr eileslrrft aweisfdpat aqrrfricmt dashitllpr
      121 llahvraqap gvrleaarid gnteralesg eadlaigyvp wlgggiyqqk lydqdwvcla
      181 nrhhprirgr lgakqyrseg hvaitagtga qlleqalrqa rierdvvlel pgflglgaiv
      241 qttdlittlp rhigqtlaqa sdlavhacpi pvdgfavrqh wharyhheag nrwlrgvviq
      301 lfgasd
//
LOCUS       WP_175851956             587 aa            linear   BCT 11-JAN-2025
DEFINITION  fatty acyl-AMP ligase [Burkholderia cepacia].
ACCESSION   WP_175851956
VERSION     WP_175851956.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10148874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..587
                     /product="fatty acyl-AMP ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=62545
     Region          18..567
                     /region_name="FAAL"
                     /note="Fatty acyl-AMP ligase (FAAL); cd05931"
                     /db_xref="CDD:341254"
     Site            order(168,171..176,178..179)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341254"
     Site            order(195,217..219,292,295..298,323..327,332,385,445,456,
                     459)
                     /site_type="active"
                     /db_xref="CDD:341254"
ORIGIN      
        1 mtkcastihr liesledvag athrmtfvde agneagityr rfaeavfhqa galreldvre
       61 ndlvmlalpa svehavamma cvmtgalpct vpvparrata grqvidvace lyrprlviaa
      121 daqaaawrdd afpaastrvv dldtlsiaad asaravisak sgrdphhvql tsgstshpka
      181 avlshenvia nvlgiggsvr fdiaagdgta swlplyhdmg lltllsnlhy rapllmmqpn
      241 sfirnplgwl kriasaratt tsvptfalry cvrrfnaaam egvdlsacrn ifiggervdd
      301 ttlrdfaatf apyglaasal qpcygmaest lavsmhrawh egtvdgapyv iadtldrral
      361 ierrdaqpaa andgadtete tvlamgtpid gmafrivddg dhalanravg evairgtsvm
      421 lgylnpddgs iaapltadgw frtgdigyva dgqlhilgrk keviiirgsn yfphdieeal
      481 ashrtlrkst ciafglpdpe tgterlvvai earpadatpq traecqqlla srigfaaqdl
      541 cfvepgslpr ttsgklqrlk crdlyangal pvihaaaave agqgaya
//
LOCUS       WP_175851957             405 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175851957
VERSION     WP_175851957.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 405)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..405
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42512
     Region          18..230
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          144..>322
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnwstfawrn lwrnkrrtvl tmamigvaaf asslalgyvi atfdavregs idsgvghvqv
       61 lhhgyldlig erplqyglta deqataarav aalhgvatta rgidfdglis ngdlsygfvg
      121 egiepnrepp gffdyhtvls grylsptnag tevvvgaela rklgvhvgsv vqlmastahg
      181 ginatdaqiv gvmstgnkdv derivnvtfa aaqallrtdr asriavflsd tahtpaaaat
      241 lraalpaldv ktwdqlvsly hqvvalyknq fsvfgailcv tillsmsnwi lmsiverrre
      301 istlralgvp astvrgvliq etaflgllga aagiaaallt mvalnhaqih lpappgrvkp
      361 illeftvspa avaavegafv vlgvaaalla tlglakrnil eglap
//
LOCUS       WP_175851980             308 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease signature motif containing protein
            [Burkholderia].
ACCESSION   WP_175851980
VERSION     WP_175851980.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10052677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..308
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34808
     Region          174..265
                     /region_name="COG3183"
                     /note="Predicted restriction endonuclease, HNH family
                     [Defense mechanisms]"
                     /db_xref="CDD:442416"
ORIGIN      
        1 mttladlkpv tiqrvrdiae kvgvpmttqy dwcfkgdggp ylvniwhdnm dedgdeiffi
       61 dtasdwaqen idsaapvqln radavsalml eayyrkkpih vaildgvrrk kglretseah
      121 qreldpvlwy phhrnedrri vvirgkpqpa efdgyaedqe yekqhktpsa pavpekkvia
      181 pataiyerds avvraaklra adgccelcgk kgfvtasgay yleahhvipl ncggaddern
      241 vvaicaddhr qahfgedrhe lrdtmiwdvl atkyphdeef fegldekshq iaqnetsvrr
      301 leenkvet
//
LOCUS       WP_175852022             674 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Klebsiella pneumoniae].
ACCESSION   WP_175852022
VERSION     WP_175852022.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 674)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..674
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75621
     Region          21..664
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mnlqtlswra lpwvkatrpq wryalrngia mclalsiaya lvldepywam tsaavvsfpt
       61 vggvisksfg riagsllgac aalllaghtl ndpwlflfsi sgwlalctwa calftnnvay
      121 afqlagytca iiafpvinis dsyelwviaq srvcevivgi lcgglmmmil pstsdgsnll
      181 talktmharl lehasllwvp ettdairtah esvigqiltm nllriqafws hyrfrrqnpl
      241 lnyllhqqlr mtsvisslrr mllnwpdapa ntrqvlesll aelatphads yhvarilapl
      301 aprqdadyrh iafwarlryf criylessrw irrvenasai aefnvpaapp larhtdqaea
      361 llngvrtfca lvaigawgis tqwtscaaal tlasiccvly svsaspfrsl tllmqtlvll
      421 slfsfvvkfg lmvqvtdlwq fllflfpllt tmqllklqwp kyaglwgqli vfmgsfiavt
      481 nppvydyaaf fndnlskivg vgfawlafav lspgsdarkg rrhiralrrh fvdqlsrhpq
      541 hsehefeslv yhhvsqlsqs kdalarrwll rwgvvllncs hvvwqlrewe trsdplaqvr
      601 dlcinllrdv msergvqqrp lastlqelqr icdalnhhhq paarelaaai wrlycalsql
      661 eqapvagtig egtt
//
LOCUS       WP_175852063            1010 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding and (Fe-S)-binding domain-containing protein
            [Burkholderia cepacia].
ACCESSION   WP_175852063
VERSION     WP_175852063.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1010
                     /product="FAD-binding and (Fe-S)-binding domain-containing
                     protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=110245
     Region          24..539
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
     Region          492..1009
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mtsavspslv rpvhlvpsqg aalsplferl rremrgdvha drasrgryat dasiyqimpl
       61 gvvvprdqdd lrialdiard rkipvlarga gtsqcgqtvg ealvvdnskw lnrivafdaq
      121 artvtvepgi vldhlnawlk phglwfpvdv staaqctigg magnnscgsr sieygnmvhn
      181 vlaidailad gsecrfgsla qpvtdrrtle llhgveriak rerdeiverv pkvlrrvagy
      241 nldlfdcqnp raytddghan lahllvgseg tlaysrqitl klaplpahkt lgvvnfptfy
      301 qamdtaqhiv klkpvavelv drtmidlsme npafrpvier alvgrpqail lvefagesrd
      361 aqhaqldrla elmadlglpg svvkmtdaga qkalwevrka glnimmsmkg dgkpvsfied
      421 cavplehlae ytrrltdvfh rhetegtwya hasvgtlhvr pildmrrdga trmreiaeea
      481 aalvreykga ysgehgdglc rgewvawqyg prlnaafaei ktlfdpdnrf npdkivnppk
      541 mdarehfrfa pgyaalplrp aldwsawnvt rnpltgeeta pgsgtdithg lasavemcnn
      601 nghcrkfdag tmcpsyrvtr deqhvtrgra ntlrlavtgq lgadglagdd vkaaldlcvs
      661 ckgckrdcpt gvdmarfkie arhawnrkhg ttlrerlvay lpryapwaar mrgaiafvng
      721 vpvvassikr wiglapqral pgfarpflad tgagastpsq tgsatrevll fvdtfsnyqe
      781 pdnaraaqav leaagytvhf nvragarplc cgrtflaagl vdeakfearr tldalrpyle
      841 rgvaivglep scllsmrdef laygygdeat rlashaflfe eflvreheag rlslplhaid
      901 anealvhghc hqkafgaftp vqtvlrwipe lkvspvessc cgmagsfgye aehyaasqam
      961 aelsllpavr araegaivia dgtscrhqiq dgaqaqavhv akvlaralrs
//
LOCUS       WP_175852111             180 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia cepacia].
ACCESSION   WP_175852111
VERSION     WP_175852111.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..180
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=17881
     Region          23..180
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mklafssiaa ltiaaaaalp avshaadgti tingkigsqt ctidgngtgn kdftvalpkv
       61 stsalvsggm tagrtpfkig lkncspaagn vythfepgtt vnsttgqlfn aagtaknvei
      121 gllngdtsni algkadensk vvaltngaad lpyyaqyvat ggaagqgtvn tsvmysimyq
//
LOCUS       WP_175852121             108 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Burkholderia cepacia].
ACCESSION   WP_175852121
VERSION     WP_175852121.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..108
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11286
     Region          21..101
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(33,36)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mdteqrytan aptraevdal ggatviefga nwcgicagaq paitasfsvh pavrhlkied
       61 gpgrplgrsf gvklwptlvf lrdgvevarv vrpadakqie adgfaala
//
LOCUS       WP_175852134             457 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175852134
VERSION     WP_175852134.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..457
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48350
     Region          42..440
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(52..53,56..57,60,92,142..143,145..147,150,170,
                     173..174,177,277,280..281,284..286,289,314,318,369..370,
                     374,378,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mtqadvqsgt aralplsrga daphrpvald dvplnrfhvk iagltfgahf tegytlgtig
       61 yalaalgrqm pidafwmgmi gssaligifl gslvfgwlsd rmgrqkiflt sfviitaaaf
      121 aqffvtsple lcvlrvligf gmggdftvgh ailaefsprk hrgtllgsfs viwtigyvaa
      181 nvlglaygda tpdawrwlla saalpalivl vlrigtpesp rwllgkgrvq earaivakhf
      241 gphvmldgsa ephanagfar lfqrdlirrt ifncaffvcl vipyfaiytf lptilktidl
      301 aegfgadlll naflvlgali gigltirlsr rgfligsfav tcaslvalav lpsaaavami
      361 vafaiftltm safsnlvgvf ppecfptevr asgvglaiac srlgsaigtf llpagiatlg
      421 fhatmfalag vllvgmivsi awapetkhlt leeasgh
//
LOCUS       WP_175852223             652 aa            linear   BCT 11-JAN-2025
DEFINITION  arylsulfatase [Burkholderia cepacia].
ACCESSION   WP_175852223
VERSION     WP_175852223.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..652
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..652
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=69744
     Region          50..618
                     /region_name="PAS_like"
                     /note="Bacterial Arylsulfatase of Pseudomonas aeruginosa
                     and related proteins; cd16025"
                     /db_xref="CDD:293749"
     Site            order(60..61,98,159,161,266,409..410,469)
                     /site_type="active"
                     /db_xref="CDD:293749"
     Site            order(60..61,98,159,161,266,410,469)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293749"
ORIGIN      
        1 mkksasplha frfrvvcaai agalslascg gvdsdppsss tnpapplaak rpnilyimad
       61 dlgysdihaf ggeintpnld alvasgrils nhhtgtvcai tramlvsgtd hhlvgegtmg
      121 vptderrglp gyegylndra lsfaqllkda gyhtyiagkw higsgivgsa tgsgqtpdqw
      181 gfersyvllg gaatnhfahe pagssnyted gryvqpgqpg qpggaggspa vfystdfytq
      241 klisyidsnk rdgkpffaya aytsphwplq vpepwlhkya gvydagydai rnariarqka
      301 lglipadfkp fdglpettaa spatanngta nakyvsavhs aadgysdygp gkvdklwssl
      361 spaerraqar ymeiyagmve nldyniglli qhlkdigeyd ntfimfqsdn gsegwpidsg
      421 adptatdtan gqdpvystlg tdngkqnaqr lqyglrwaev saspfrltkg ysaeggvstp
      481 tivrlpgqtk qlptlrafth vtdntatfla iagvtppsqp applvntltg vdqnkgkvvy
      541 nnryvypvtg qsllpvltgs atgevhttpf gdeaygrayl rsadgrwkal wtepplgpld
      601 ghwqlydlas drgettdvsa qnpsvigtlv dqwktymsnv ggveplrprg yy
//
LOCUS       WP_175852149             294 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia cepacia].
ACCESSION   WP_175852149
VERSION     WP_175852149.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..294
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=30821
     Region          9..270
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mtsdptssta fvfagggslg aievgmlrel vasgerpdcv vgasagaina ayfagrpdad
       61 gvamlaalwc rirrqdimpf smrslvamll rnrphlvead alrlllernl pyrrieqaal
      121 plhivatdvl ngqevvlsag pvvdavqasa aipgvfpsvs iggvelvdgg vanntpisva
      181 ialgvkrivv lpagfacalr vpprsaiaha thaltlviar qlvrdlelyg araqihvvpp
      241 lcpldvssyd ysqcaqlidk aaertrawid sgglaqcaip gqlrehdhaa elsh
//
LOCUS       WP_175852261             330 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175852261
VERSION     WP_175852261.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..330
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35301
     Region          15..223
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(52..53,55,69..71,77,79..80,121,222)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(52,54..55)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(77,80,83,90)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(113,117..120,122)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(118..119,142..144,196..197)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          247..330
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 mqanrhqvri dalidaaqdi rcfrvsridg qpfdayepga hidvtapsgv trqyslcgnp
       61 dergsylfav kkeaqsrggs rslhddvqvg aelsigtprn lfrltddase hvliaagigi
      121 tpllsmayal hrrgaryrlh yfarsrehaa fvdelsaepf ashvtfhygv epdalaaalg
      181 rcvesvdaha hvytcgpgpf meavvaaaat rlpedsihle rfaaepvaad agntdaasat
      241 padefevrlh rsgqsvrvtp dtsivdalar igvevdtscg egvcgtcmvp vvdgepdhrd
      301 hclskaeras ntvicccvsr arsavlvldl
//
LOCUS       WP_175852249             338 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia cepacia].
ACCESSION   WP_175852249
VERSION     WP_175852249.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 338)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..338
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36365
     Region          9..321
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mttsprrral iaagigmlav pplvrakprt vriskgfgvl ylpllvmekq rlfeqhaarh
       61 gvrdvavdwv lldggnsvnd ammagtldfa gagapgfiel warargipnv evigisglst
      121 tslslnanra glvslrdftp sdriavpgir tslsavvlqm vasrqlgakh faqldsitvn
      181 lphpqamqal irrengvtah ftsppfstle lrqpgihrvv nsvdvlgplt ldvvfapkrl
      241 vdtdpalava flgaldeanr liaqdpraaa alyaassgvg vshddvmrml aapdtrfsvl
      301 pnqlmdyvef lylagtikak prawhemfap mlddyrsr
//
LOCUS       WP_175852267             454 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175852267
VERSION     WP_175852267.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..454
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47956
     Region          22..426
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(35..36,39..40,43,83,141..142,144..146,149,169,
                     172..173,176,258,261..262,265..267,270,297,301,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 myptdtvqsp saarpladrq lrriviasva gnamewydff vygtaaalvf ghvffppgas
       61 plagslaafa afalgfvarp lggivfghvg drygrkaslv wtllimgast faigllptya
      121 qvglwapaal vvlrllqgia sggewgggvl misenappeq rgyyaawsql gvgggfvlss
      181 aaflaaqalp ddafrtwgwr lpflasiaif aigiyirrhl pesrdfeqag rrgahthlpi
      241 vecirhhpke illamglrva enggayifla fslvygkyvg ipngvmltgv miamivemga
      301 mlawgrlsdr igrkpvylig alslvacafp ffwlldtrat plvwlaltvg tavshgamig
      361 tlpalvgelf stevrysgva lghevasifa ggmspliata llaryhaswp vslflvalgl
      421 vtvatlcvmr etrivraasa apaapatgtr gdta
//
LOCUS       WP_175852274             279 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175852274
VERSION     WP_175852274.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..279
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30790
     Region          9..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          105..270
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 madapdnllg aylrdrrekl dpaalglpat rrrtpglrre evaqrahvsa awytwleqgr
       61 ggapsadvld rlaralllnd aerehlflig vghppevryh atdhvsprvq hvldsldasp
      121 aivrsatwdv vawnnaaaat ltdyatlspe rrnilrlifv dphvrgvqan warvaqfavg
      181 afradvargg atqavqafvd emratsaefd alwrdhdirs heegtkeihh pavgrialey
      241 safavsgrpd qtlviftpet addrariral vaarekfei
//
LOCUS       WP_175852294             438 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia cepacia].
ACCESSION   WP_175852294
VERSION     WP_175852294.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..438
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45643
     Region          110..430
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mlklnlaatv vfamaataha qpslspapai sggappigap ppdarpstsl tladalaaaa
       61 rnnpalrgar advdasagal mqagarpnpe vsflqegfrr aertstalin qtielggkrg
      121 arldvasygr eaanasldeq gavvradvia afygllaaqr qlqvteesaa iaarsadlas
      181 rraqagkvsp veatkarvaa agvqievvta rgrvevarek lnavmgeard grlavlgdle
      241 avppveslpa ltaqlddapl ariaraemlr snaavslera rripdvtisa gvkrvttggv
      301 pdnqavvgvs ipiplfntnk galleathka aranadldre rtrlrleltq ayanfeaaaq
      361 eaqrlkddil paarvaldam srgyelgkfs fldvldaqrt lfqgqsqyvr aladahtara
      421 digrlvgtpl vpfapitq
//
LOCUS       WP_175852296            1074 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cepacia].
ACCESSION   WP_175852296
VERSION     WP_175852296.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1074
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=115219
     Region          1..1040
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mferlirfai ahrwlvmlai aavaalgvfs yqklpidavp ditnvqvqin taapgysple
       61 aeqritypve tvmaglpgle qtrsisrygl sqvtvifkdg tdiyfarqlv neriqeakdk
      121 lppgiapamg ptstglgeiy lwtveadaaa rkpdgtryta adlrelqdwv vrpqlrnvrg
      181 vtevnsiggy vkeyrvapnp aklmsygltl advvralern ndnvgagyie krgeqylvrv
      241 pgqartvddi anivltnvgg vpvrmkdvgv vdigrelrtg aatsngeevv lgtvfmlmge
      301 nsrtvakavt akmadvnrtl psgvkaipvy drtvlvekav atvkknlleg ailviavlfl
      361 flgnmraali talviplsml mtftgmvnak vsanlmslga ldfgiivdga vvivencvrr
      421 lahaqaaagr pltrderfae vfgasqearr alifgqliim vvylpifalt gvegkmfhpm
      481 aitvvmalaa amvltvtfip aavalfiger veekenrlmg warrayepvl aafmtrpvrv
      541 mlgagaivlv tlglatrlgs efipslnegd lavaalripg tslsqsvemq ksiektlkar
      601 fpeiervfar tgtaeiaadp mppnlsdgyi mlkpadrwpd pkkprdqlvr eieealaelp
      661 gnayefsqpi qlrfnelisg vrsdvavkif gddmavlnqt geqiaaalqk vpgasevkve
      721 qttglpvltv nldrdklary gvsvadlqdt vaaavggqka gtlfqgdrrf divvrlpdel
      781 rsdieaikrl pialpapaag asaplaaapy vplaelatid vapgpnqisr edgkrrvvvs
      841 anvrgrdvgs fvadareqlq qdvrvpagyw vswggqfeql qsaserlklv vplalfmvfv
      901 llfvmfnnvk dgllvftgip falsggvvsl wlrgiplsit aavgfialsg vavlnglvmi
      961 sfirnlrddg tpleaavreg altrlrpvlm talvaslgfl pmafatgtga evqrplatvv
     1021 iggilsstal tllvlpvlyr vshavswraa laggfgggfv sgvlrrlgff kgna
//
LOCUS       WP_175852330             211 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175852330
VERSION     WP_175852330.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..211
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22437
     Region          5..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkvsktqvae nrlailqaaa rlyrergftg vgvaditrea glthgglyrh feskdalaae
       61 aaeyafewkl seletpdada ntdadgflrt gvanylspqh rdsigqgcpv aalaadaare
      121 tgaiadafaq gigrymtlfa qrrpdgteaa qiepedrvra ismlstmvgg lilaratarg
      181 lpalsdeila tlrdhlaatw gldevnvdgh d
//
LOCUS       WP_175852374             215 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cepacia].
ACCESSION   WP_175852374
VERSION     WP_175852374.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..215
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22856
     Region          3..215
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mnylpillqi aavylvaait pgpnffmisq lslagrrslg aasalgvgta svawaslaml
       61 glaavlhqve wlyeairigg avylvyfgfk llrsgvrrda apadapdera plaaphardy
      121 lrayrsglft cltnpkscaf wtsvfaamlp ahvplwfnga vlvtigvlsa gwyscvaylf
      181 aspraqrgyr rvrrpldalc gvalgglgak laaer
//
LOCUS       WP_175852289             280 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175852289
VERSION     WP_175852289.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 280)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..280
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29947
     Region          13..277
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mnallprapl pgrlsratgt latlvlclaa lpivtmitms fgssgtlefp prdfslhwyr
       61 aawqtfvtad agsaqsmgaa lttslvvaia tmlvatavsv paayalsryr frgktfveql
      121 valpivyplv mlglalllvf nalpvelglv rlvvahvilt lpftvkncaa svasigpefe
      181 eaaclmgagp rrafvdvvlp lmrpgvlagm lfafivsfne ftvtfflysv dtmtlpvwly
      241 srtvssldpt vfcfavftva idfaliwmle klvgdkgval
//
LOCUS       WP_175852384             384 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175852384
VERSION     WP_175852384.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..384
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42028
     Region          23..384
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mqsipssaaa rqtqpapaar tqndafvrie nvvkkfgdst avdnvnltia knelfallgs
       61 sgcgkstllr mlagletats gkifvdgedl aslppyrrpv nmmfqsyalf phmtvesnva
      121 fglkqegtpk neirervaea lalvqmskya krkphqlsgg qqqrvalars lvkrpkllll
      181 depmsaldkk irqktqlelv niiekvdvtc vmvthdqeea mtmasrlavm segkivqigs
      241 pgevyeypns rfsaefigst nlfegrvved epdhifvesd dlearmyvsh gvtgplgmpv
      301 gisvrpervh vsrekpgskh nwargvvtdi aymgsyslyh vrlpsgktvv snlssshlmn
      361 dnapawnddv fvswspasgv vltq
//
LOCUS       WP_175852390             397 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia cepacia].
ACCESSION   WP_175852390
VERSION     WP_175852390.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..397
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=42076
     Region          18..382
                     /region_name="MidA"
                     /note="SAM-dependent methyltransferase, MidA family
                     [General function prediction only]; COG1565"
                     /db_xref="CDD:441173"
ORIGIN      
        1 mnpkahepas lpapgpdala qsetlaaqlr deiaaaggwl pfdrfmeral yapglgyysg
       61 garkfgrrad dgsdfvtape lsplfaqtla qpvaealaas gtrrvmefga gtgklaagll
      121 aaldalgagl deylivdlsg elrerqrdti taaapalaak vrwldalper fdgvvvgnev
      181 ldampvrlfa kaggawqerg valdarqafv fedrpaapag lpavlgglde agdgyvteth
      241 eaalaftrtv ctmlgrgavl lvdygfpahe yyhpqrdrgt lmchyrhhah ddpflypglq
      301 ditahveftg iydaaiatga dllgytsqar fllnagitda laaidpsdir eflpaanavq
      361 kliseaemge lfkviafsrg idgtldafar gdrshal
//
LOCUS       WP_175852402             546 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC-F family ATP-binding cassette domain-containing
            protein [Burkholderia].
ACCESSION   WP_175852402
VERSION     WP_175852402.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..546
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58067
     Region          13..527
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 maaatptgal valhhvsfrf ddgvtlfdsl dlsidrtptg ivgrngvgks qlaqliagrc
       61 apstgtidrs tqvayvaqqh ddaaagprtv aqlaaldapl galarladgr aephdfdrvg
      121 drwdlaerlr taldaaglhd vradtpaqal sggqrarval igallsgagl lvldeptnhl
      181 dapgrawlra aldgwrgglv ivshdralla dvqriveltp qgvrsyggny afyraqrdad
      241 qdaaqaaldn araergrarr rleqehdtiq rhaaaslrda ktanlssgak qsrkgaarni
      301 mgqvrrhqnd fkatldervq qaaarveada pvlvslpgte vsarrqlftl erarlpwgia
      361 gaadgitwsa cgpvrialtg pngcgkstll rmlagelvpc sgtctthvsa ayldqrlall
      421 dpersiveql glldtplaeg elrsrlallq ldaaratqpa rqlsggerlk aalacalwrg
      481 tpaqllllde ptnhldlesv raieaalagf pgaivvashd taflaaldpt htmqwhrdgw
      541 ryepva
//
LOCUS       WP_175852416             265 aa            linear   BCT 11-JAN-2025
DEFINITION  ComF family protein [Burkholderia cepacia].
ACCESSION   WP_175852416
VERSION     WP_175852416.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..265
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=27787
     Region          90..235
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mirssarrtm rvalsqvral aarvaavalp nrcalcgnls htmicvacda aywnearlrc
       61 gvcaiplgig qprshrsrga rassadayrc dacraapppf datlaladyr apldglargl
      121 kfhrqlalga efaarlarli ddtpgasgfd lvapvplshr rlvargynqa waiarplarr
      181 lgvradaall arvadtapqs rldrharrdn viaafavagg vagrhvalvd dvmtsgatla
      241 aaahalkaag aarvtnlval rtard
//
LOCUS       WP_175852491             293 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia cepacia].
ACCESSION   WP_175852491
VERSION     WP_175852491.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..293
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31566
     Region          13..270
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mtapikallk phvrdignlq vrrtlpalaa rlvgpfiffd hmgpatlppg tgldvrphph
       61 iglatvtylf dgailhrdsl gslqeivpgd vnwmtagrgi vhsertpdaq renghtvhgi
      121 qtwvalprah ettepsfehh padtlpkrne dgvsltvias dafglrspvt tfsrtlyvaa
      181 efaaggrlel dasheeravy vvdgelaidg tpvpaeqmav lapgaavtlt sgsgaramll
      241 ggdkidgerf iewnfvassr eaierakeaw trqemgkvpg etewiplpes kpr
//
LOCUS       WP_175852527             410 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175852527
VERSION     WP_175852527.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..410
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42904
     Region          12..394
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(22..23,26..27,30,65,112..113,115..117,120,145,
                     148..149,152,224,227..228,231..233,236,266,270,320..321,
                     325,329,345,348..349,352..353,356)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mtpieqevrr rwlpvlaggl imgaalgirh vqglflapvs ldhgwsreaf glalalqnli
       61 wgvaqpftgm iadrfgslrv ivagmllyaa glvtmahaat tgmftvgagl vigialsgsa
      121 fasiygalsr lfppdrrgwa lgvagaiggl gqfcmvpvaq eliggigwrh afialalvav
      181 vlaplavllr drpaqvagat agpdqsigea vreafahrgf wllnagffac gfqlafiath
      241 lpaylldhgl parhasvala lialtnvagt yacghlggll rrkyvlsvly lvraltmavf
      301 vaaplspasv yvfaavmgft wlgtvpltng visqvfgvry iatlfgfvff ghqlgsffgv
      361 wlgalvydat hsymplwigs ialgvlaall hlpindarva rpaagnaawa
//
LOCUS       WP_175852541             240 aa            linear   BCT 11-JAN-2025
DEFINITION  (Fe-S)-binding protein [Burkholderia cepacia].
ACCESSION   WP_175852541
VERSION     WP_175852541.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..240
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25860
     Region          <2..237
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mrvglfvtcl vdlmrpeigf salklirdag yevivppaqt ccgqpaynsg dralardlae
       61 ktlrefeqfd yvvapsgscg gmirahygdl frddpelmgr ytrfqqkvye ltdflvnvak
      121 vslapgeftg pvtyhdscsg lrelgvkaqp rallaqrgia vtemkdcehc cgfggtfavk
      181 ygdisaaiad ekcanvrasg agavvlgdlg cmlniegrlr rtgdrdtrvl hvaqvlagdv
//
LOCUS       WP_175852557             540 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175852557
VERSION     WP_175852557.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 540)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..540
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58889
     Region          10..537
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msepvvstqh epllalehlh vrfgdtvavd dvtleigrge rvalvgesgs gksvtalsil
       61 rllrdadvsg airfagqdla gkseremrgl rgsdiamifq epitalnply tigvqigeti
      121 vlhdgvsave arkraialla rtgiaepekr vdsyphqlsg gqrqramiam alacrprlll
      181 adepttaldv tiraqivdll lelqreeaek rgmaillith dlnlvrhfad rvavmehgrl
      241 vesgpverif aepehpytqr llnsrpqrav apvmpiapvv ldarhvsvqf arkrpgiagw
      301 fgsvpvtava dvsvsvrqge tlgivgesgs gkstlamall glqktaggti efqgralsty
      361 rgreqtalrs nmqvvfqdpf sslsprhtie rivgeglelh rpdmtpdarr akslavlrev
      421 gldrtvlhry phefsggqrq riaiaralvl eprilildep tsaldvsiqq qvlkllanlq
      481 qkynlgyvfi shdlevigam ahrvavmqgg avvesgevad iftrpshpyt qkllkavwka
//
LOCUS       WP_175852565             575 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Burkholderia cepacia].
ACCESSION   WP_175852565
VERSION     WP_175852565.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..575
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=63235
     Region          327..570
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mrtkltvknp kpasptrapv rsgslvarka vrpaappagd kparpkkaap aaagersfkp
       61 rgapgaerpg adrapakrap rdggaergtr apyrdnaage gakrsfgdrr pssdrpprrd
      121 ddarprragg dddkrssyrd kaagegakrn fgdrrpssdr pprrdddarp rraggdddkr
      181 ssyrdkaage gakrnfgdrr pssdrpprrd ddarprraga ddgkrpsyrd ktagegakrs
      241 fgdrrpssdr pprrdddarp rragadngkr psyrdktage gakrsfgdrp arpardgerr
      301 sfgavktaqp vkratadvdy gdetglmrls krmselgmcs rreadewiek gwvlvdgeri
      361 dtlgtkvrad qkieideras aaqaaqvtil lhkpvgyvsg qaedgyepaa vlitranrws
      421 gdhspvrfsp qhlhalapag rldidstgll vltqngviak qligeqsdid keylvrvrfg
      481 erlididqhf paeslaklrh gleldgvalk pamvswqnge qlrfvlregk krqirrmcel
      541 vgldviglkr vrmgrvtlga lpqgqwryls adetf
//
LOCUS       WP_175852573             163 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia cepacia].
ACCESSION   WP_175852573
VERSION     WP_175852573.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 163)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..163
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17358
     Region          18..147
                     /region_name="NUDIX_ADPRase"
                     /note="ADP-ribose pyrophosphatase; cd04673"
                     /db_xref="CDD:467557"
ORIGIN      
        1 msdsprsptg viasirpvpa vigivlrerd vllvrranpp dagcwgfpgg kieagesits
       61 aivreiveet tvdvealdvf taldafdyda ggnvhqhfvm vavlcnwlrg tpaagddald
      121 arwfdlaeld rddlpmsagv rdvarraier aaslgdarrp aip
//
LOCUS       WP_175852576             331 aa            linear   BCT 11-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175852576
VERSION     WP_175852576.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..331
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=34999
     Region          <14..324
                     /region_name="FAD_binding_2"
                     /note="FAD binding domain; cl46878"
                     /db_xref="CDD:481218"
     Site            order(34..35,38,41..42,66..67,70,73..74,97..98,101,
                     104..105,108,128..129,132,135..136,159..160,163,166)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          48..74
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          79..109
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          114..136
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          208..232
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(224..225,228,231..232,255..256,259,262..263,266,
                     286..287,290,293..294,297,317..318,321,324..325)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          301..325
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mtafsstvsl pgthdpdraa lalrlaapda svrrialiel adleesdlvp sfvaalcddp
       61 sadvrseaar vlgaweqpdv vdalcgalld pdegvrataa qslselkdaa sgavlcrwad
      121 rpesfvrrav lrglrelrdp gafapalral daehapvrae avavlgwlrd pralpslari
      181 attdaaadvr raavgaigfa apddaatida llaalrdrew qvreeaattl gklrvaaard
      241 plaaaldddy wqvrlraara lgqlrdaaaa pavvallsha isnlrkeaal algelrdrat
      301 lpalthaled hdpevrkavr iairqideas r
//
LOCUS       WP_175852578             256 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175852578
VERSION     WP_175852578.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..256
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28437
     Region          10..245
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mtspnvvpls aaplyvqikd tlrarildgt yaphsrmpse helcaafgvs ritvrqalgd
       61 lqkegllfkl hgkgtfvskp kafqnvtslq gfaeamssmg yeivnqvrsv rtvkadrhla
      121 tklnvpegap lveihrvrll nrepvsleqt wvpealgkrl agadlatrdi flvlendcgi
      181 plghadvsid ailaddeivd alyveesspv lrierlthda sgapidyeyl yfrgdafqyr
      241 lridrqkprk parkqr
//
LOCUS       WP_175852579             409 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175852579
VERSION     WP_175852579.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..409
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41949
     Region          8..396
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(18..19,22..23,26,61,108..109,111..113,116,139,
                     142..143,146,227,230..231,234..236,239,269,273,322..323,
                     327,331,347,350..351,354..355,358)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mpdsryrwvi vaagglmgci aigamfslpv flraiardtg wsmtgisgam tlgfiamafa
       61 smgwgslsdr vgtrpvvmtg avllsaslal asrapsllaf qltfglavgg ataaifapmm
      121 acvtgwfdth rslavslvsa gmgmapmtma plaawlvsvr dwrtsmllia alaavvmipv
      181 sllvrrapal dgahaapaas aapapagdpa amsvahalrs pqfivllltn ffccathsgp
      241 ifhtvsyavt cgiplivavs iysveglagm ggriafgilg drigakrtlv aglfaqalga
      301 lgydfvrtid gfyavatlfg fiyagvmply svlarenfpl rmmgtviggc amagslgmaa
      361 gpvagglivd tfgsygwlyv gsfaigvgaf lmammfrpfa karpetvaa
//
LOCUS       WP_175852591             402 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175852591
VERSION     WP_175852591.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..402
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40611
     Region          15..334
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mktlssdaal ppdgrasafa rstlvalvvf aaitpllllv apavagqlat qlglsasqig
       61 tyffvelgaf slatvpsyvw lgridarrva afaialfgag nlltalwmpg fvallalrav
      121 talgggslmv lcmtsaatse nsdrvyglwv vgqliagaig lfvlphvfaa fglralyval
      181 aglallaapl srgfpsslga rtapaqharg aaartpqgli vlaigavltf ylaigsvwtf
      241 asraaaeagl dpqstgnvla iasvmgiaga alascaggrl arramltagy allaaslval
      301 avmrqaggys aaifafkfaw tfvlpftlat vaqidtsgrl vatlnfviga glaagpllag
      361 lmldaggtmh alftiatava ivsfaalrhi drrthasvss qp
//
LOCUS       WP_175852606             366 aa            linear   BCT 11-JAN-2025
DEFINITION  C40 family peptidase [Burkholderia cepacia].
ACCESSION   WP_175852606
VERSION     WP_175852606.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..366
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37543
     Region          <7..176
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
     Region          <177..>360
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
ORIGIN      
        1 mpriwvpvav vsllaacssv ppqsasrpas gmkittpraf papanfpkfv dhsvgqeeis
       61 iqamslvgvp yrwggntpts gfdcsglvry vigraadvnl prttadmsgr gvsvepdqia
      121 pgdliffntt grphshvgiy vgklrfvnap stggtvrldy ltnpywakrf dgirrvappr
      181 gaptpfdapt yeakrdeprs apvvapapvv vtaaaprqpa ytqsqaaatr apapvmpaaq
      241 avstaavapa aasadpyepp pprmqtaqqq atsvsdgtgt aaatltanaa pagpaevgtq
      301 ipttaltaaq aaafdaeppp avaatsprgt epapvqvlra stqstpvspr tataddpiar
      361 fangsy
//
LOCUS       WP_175852608             153 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175852608
VERSION     WP_175852608.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..153
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16746
     Region          14..126
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(15..17,31,48..50)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(62,65,69..70,79,97,101,107,111,114..115)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 msktvskpsa tgpltigqva eltglsthtl ryyeqagllr aisrtaaghr lyapadldwl
       61 afvmrlkatg mpiaqmqefa alraqgeptf gerrrllvth rdavrahlae lqasldvisd
      121 kiayyeaqer daarrakpth spseqdghhg ttr
//
LOCUS       WP_175852653             310 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175852653
VERSION     WP_175852653.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..310
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33840
     Region          41..296
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 matdnhaara wppkhdapdp pdvrpadark prkmaghlag rawhalvwgl maffllnvml
       61 liatvavnsv atrwfgtplp qgftlhwyak awadfqlasv lwvtvevvga vvllsialgv
      121 paayalarvq frgkrfallv fllplmvppv tygipmatvm ykvglagtlp gvilanlmpa
      181 lpfvilvmtp fieqidpnle aaarifgant wryfrhvllp llvpgmlaag llvlvrtigm
      241 feltfftagp stqtlvvaly yavfstgvra pqsidamami ymaitlvwvv ialqfvsptq
      301 lvsrvkqerq
//
LOCUS       WP_175852654             290 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia].
ACCESSION   WP_175852654
VERSION     WP_175852654.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 290)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..290
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30764
     Region          11..288
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mstlpaggtp rdakawlvtp alafivalfi ypfayglvls fqpmngggal anyvqfftdt
       61 amwptvlvtl klavpatlln vgvavpvafa lrrnspyqkl vttllvipvt lgtvlvadgm
      121 ltyfgpngwf pqalqglhly tdevrlthny wgvllslivs gfpfafllml syisgidptl
      181 araaatlgan pwqqfrriyl pllvpgltma aclsfvqafs vfpsavllga pagptrvisi
      241 aaaeaafesy dyslasaiai vmgfvqllvv asmlgarrff ytgavtggkg
//
LOCUS       WP_175852727             744 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia cepacia].
ACCESSION   WP_175852727
VERSION     WP_175852727.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..744
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=78411
     Region          75..>209
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          215..737
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msrglieagk vagqaagagv srrsflklgm slgaaagggl llgfslpaag ddarrsvigg
       61 dgdetaragv fapnafvqid ragkvtlvmp kvemgqgvyt alpmliaeel evplssvtld
      121 happneklfl dpllggqltg gstsvryawe plrragatar tllvaaaakq wnvdpascra
      181 vngevqhpps grrvsygqla daaaklpvpk dvalkkpadf kligtpakrl dspekvdgta
      241 qfgldvrlpg mlyavivnsp vfggtvasid dtaakkipgv rqvvradnav avvgdhtwaa
      301 krgasalvvk wnegagakvs tkdivadlaq aaangkgava rkdgdvgkgf adaktrvdav
      361 yeqpllahat mepvnctvhv radgceiwvg tqvptravdt vqkltsfppe kivvhnhllg
      421 ggfgrrletd migqavkiak qvnapvkviw treediqhdm yrpyyydris agldangkpi
      481 awqhrivgss ilarfappaf qhgvdpdave vatdlpydlp nqlidyvrqe prhvptafwr
      541 gvgptrstfv vesfidelaa qtktdpvqyr rallgktpra lnvldvatka agwgpslptg
      601 qgrgvsvmha fgsffsivid vavdngevqv krvvcavdcg msvnpntiea qvqggiifgi
      661 tgalygeiti edgrvvqsnf tdyrmlrine tppievhlvk sgeapggige pgtaataaal
      721 snaifaatgk rlrklpvgdq lkta
//
LOCUS       WP_175852768             237 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: (2Fe-2S)-binding protein [Burkholderia].
ACCESSION   WP_175852768
VERSION     WP_175852768.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..237
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=24749
     Region          61..231
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mttaqtaasa asasaaatga sapaqasavp dsapasapav pasapapaav erplvrfqsk
       61 plsiningks vgpmqvpegl mmieflheya gltgsrlgcg qgichacvvi vdkpdgtsee
      121 mrtcitgahf fhgrtirtie ghakrneage vvelspiqqk flehfsfqcg yctpgfvnaa
      181 tvlierlkre pvakadvert itealdahlc rctgyvryye avkdvvlttp glvkdaa
//
LOCUS       WP_175852983             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175852983
VERSION     WP_175852983.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33608
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,223,240,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdfesirifl rvvergsfta asvqldlals rvsrkvrqle ddlgvqllyr ttrrvsvtea
       61 grdyyerclr aeeilldadr qaralrtdpe gtlrvlvpys iglfelepal aefrrryprv
      121 qlvliydnsp ldlvehgfdv alragmltds gyvarslgws haklaaspay ldragrpqtp
      181 qelaqhdily vgrdapgltl rltnaagdva dvpvrpvlis nesitvlrqa asgggialvs
      241 thytarrlek neleivlpdw hrtddvelha lyprratlds kvrafveflt evftgwrsap
//
LOCUS       WP_175853011             676 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia cepacia].
ACCESSION   WP_175853011
VERSION     WP_175853011.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..676
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=70680
     Region          30..590
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mkfalpdlpp raafrtvlrd arptlppgal afalrntaas llalyiafrm nlddpkwaas
       61 tvwivaqgsr gmglsksqyr ilgtaigavv alvligafaq tpelflpala awiglcagva
      121 tfqrnfraya avlagytaai vamdavsapl hafdiavarf lyvvvgilcg alfdtvfapg
      181 eplddvrtrl rryldraaav gagalrrepn vaavhrlfad aleldtaaey aatgappvrn
      241 aighlrmavl gvlsaqaagq alhdhaarsg gtpdplvada aqvldgvaas geagaaltal
      301 rarvddavra eaaepagsdp srlltldrla allagfdaaf agkarldlpn ppasrvryaf
      361 hhdpvlawhn gmrafiavli aaafwivtaw psgagfvait gvvcalfstr pnsvgatvgf
      421 lkgaacaava galcnfvllp avsgfemlay ilgvftigag iamrhpraag igsgfsiffw
      481 nftspdntar igdaaflnsa latllgiafg amvfalvfpg dpgasrrrlh cavradlari
      541 arnprawpas awlsrtadrl grelgfagrl patlierdlr dllaawtigd sllalaelaa
      601 repaarrava lvrgrvglad farleracga aarvllrrvt evdsddgral lrgvvllrti
      661 aetaaahdgf lrgrrd
//
LOCUS       WP_175853012             533 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175853012
VERSION     WP_175853012.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..533
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58350
     Region          6..529
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 msniydadvi vigagilgga vaqsltqqrk svivieagpd vkraalvraf rnygnksdyn
       61 gpypdlpwap ksstgrysdr yidsvgpvlq kpsflrlvgg ttwhwggatw rmlpndfrlh
      121 slygqgrdwp igydelepwy qlaeeqigvs gsdtddqsgq ggapfpprsk pypmrqqsws
      181 yltqqvadkv atighrfvde pnaratrpye grptcagnnn capicpigaq fsgdrpvlra
      241 vaqgarlltn avvyklehge nrkiaaihym tpdgkstrlt artfvlaahg veipklllms
      301 gaanasdqvg rnmmghtgra iamlareplw agrgptqqgs intrrdgafr rehgairhfl
      361 dntvpneivt rrliaqgivg dtldarirhd aarylkiasy veilpdprnr vtlgdrkdal
      421 glptprtdyd vydyslraas rvlddysdfq qvfgatevvn dvhawvpssh imgttimgnd
      481 padsvvdrdc rthdhpnlfi astavhpsss vvnptltgya lalrmaktig aev
//
LOCUS       WP_175853020             314 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175853020
VERSION     WP_175853020.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..314
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34942
     Region          14..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..298
                     /region_name="PBP2_DntR_NahR_LinR_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators that are involved in
                     the catabolism of dinitrotoluene, naphthalene and
                     gamma-hexachlorohexane; contains the type 2 periplasmic
                     binding fold; cd08459"
                     /db_xref="CDD:176148"
     Site            order(104,106..107,111,169,206,273)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176148"
     Site            order(105,108..109,112..113,116..117,119..120,123..124,
                     126..130,132,195,223..227,230..231,234..235,238,252)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 melseidlnl lllfqrlmqe rrvssvaeqm nmsqpgvsna laklrrrlgd plfvrgpggv
       61 vptpfalrla epvaqalstl haalnpetgf dplrashtmt igmtdigevv flpallehls
      121 kaapgialnt vrntsvnlsd emadgrvdla igllpqlqgg fyqrrlfdqr yvclfrrghp
      181 ledapltvdt wreaehlvvv sagtghgqvd ewlkrrrvkr rvrltvphfm svgyilqrtd
      241 liatvpehla lqlaapfsls wralpvtlpg apihmlwhtr vnqdegnrwl revvvslfse
      301 aethgrkpgp arrk
//
LOCUS       WP_175853156             442 aa            linear   BCT 11-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Burkholderia cepacia].
ACCESSION   WP_175853156
VERSION     WP_175853156.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..442
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=47107
     Region          3..408
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mnkrmsaagw illamaagil igymiytqlp dkqsaaeiag yislvsdvfl rlikmvigpl
       61 vfstlvvgia hmgdagsvgr vfvkalgwfv taslislllg llmanllrpg enlglplpdi
      121 gasahlatsk ftlkdfvghm vpksiaeama nneilqivvf smffgvalas lgergkilva
      181 aidqlahvml ritgyvmkla plavlaamas tvainglsil lkfavfmgdf ylslfllwgt
      241 lviagllflg rrvfkllvli keafmlsfat asseaaypki ldaldrfgvr rkissfvmpm
      301 gysfnldgsm myctfaslfi aqaygihlsl gtqvtmllil mltskgmagv praslvviaa
      361 tlhqfnipea glllilgvdt fldmgrsatn avgnsiasav vakwegelmp eaeaeanaar
      421 ldeeaearmn eaareadrvt aa
//
LOCUS       WP_175853181             340 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175853181
VERSION     WP_175853181.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..340
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36272
     Region          35..330
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mplrrltagp rgrppdpnrt aivskssekl dlatraawly yvagdtqnei aeklqvsrpv
       61 aqrlvafave knlirvrvdh qladcldlga qlskryglam cevvpvdada pdaidrklav
      121 agaqvmeryl netrpmviav ssgrtlkaav aqiaqierpq hrlvsmvgai aadgssnryd
      181 vaqyisektg skhfllpapl fadsaaeraq wcnhrlyriv dalsgkadva fvgvgnigph
      241 cplyedgfit eherdemttl gavaellgvp idaqgkridv stsgrvtsva latppklpti
      301 afaggpkkhd aviaalrggw lsglvtdetc araalaakaa
//
LOCUS       WP_175853228             535 aa            linear   BCT 11-JAN-2025
DEFINITION  multicopper oxidase family protein [Burkholderia anthina].
ACCESSION   WP_175853228
VERSION     WP_175853228.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..535
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=58037
     Region          88..535
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mirrtflsha igiaaaslft rtawaqhagh agmagmdqmd dmpgmsgmsg maghsqhgkp
       61 apaalaapda lpagaplasl rtlanesrea gtfratlvaq pvarpllhga rpttfwqfgt
      121 gtqgpvvgpl idvregdtve irfvnklpqp stihwhglpv ppdqdgnpsd pvapgasrvy
      181 rftlpkgsag tywyhphphm mtaeqvfrgl agpfvvraad dplagwpern lfvsdlklar
      241 dgtippndmm dwmngregqf vlvngarrpr idvagderwr vwnacsaryl rvafddgrmf
      301 ehagtdgglf daprqvtsll lapgeraell vraggrasra vlqaaeydrh kmamshddgh
      361 gslppdpala ladvtfapaa aralpatlra vpalgepvar kmvefgeamd mdammngpah
      421 grpagmrfmi ngvtyvphra tltsrrgdie rwdirnatdm dhpfhlhgtq fqvierasdg
      481 artsepfraw rdtvnvrsge tvtihvsqdm pgermfhchi lehedlgmmg tlkvv
//
LOCUS       WP_175853251             311 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: electron transfer flavoprotein subunit alpha/FixB
            family protein [Burkholderia].
ACCESSION   WP_175853251
VERSION     WP_175853251.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..311
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31523
     Region          2..310
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtilviaehd nasikaatln tvaaaakigg dihvlvaghn aqgaadaaak iagvskvlla
       61 dapqleagla enveatalni akdyshilap ataygkniap riaakldvaq isditavdsa
      121 dtferpiyag naiatvqssd pikvitvrat gfdpvaavgg sasvekieaa adagksqfvs
      181 revtkldrpe ltsakiivsg grglgsgeny tkvlepladk lsaalgasra avdagyvpnd
      241 yqvgqtgkiv apqlyiavgi sgaiqhlagm kdskvivain kdpeapifsv adyglvgdlf
      301 tlvpelvnel g
//
LOCUS       WP_175853246             309 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175853246
VERSION     WP_175853246.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33803
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..294
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdkldqvrif lqvaemgsfi kaahaldvpr atvsaavqql etalgtrllh rttrqvqlta
       61 dgalllergr rllaeadeld rlfrrrdrdv igrlnvdaps riarrviapa lpslfrrhpk
      121 lqlslgstdr sidlvqegvd cairvgrlad sslvvrplgq fvlincaspd ylrecgvpeh
      181 pdalahghwa igyaspttgr elaweycadg grhtlalpsr vivnnaetyi asciagmgli
      241 qiprfdvahl ldsgalvevm pgyraapmdv savyphrrhr srrlnafiew fgelmadaln
      301 dtsaaaggd
//
LOCUS       WP_175853277             269 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175853277
VERSION     WP_175853277.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..269
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29755
     Region          85..268
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mrtwrleran laaqldvsra tclvaaiggn epnafaaeil klfddalsit qctifayefg
       61 nrprtmsvad hrggrylrdl adtyarhfya ldgnqqivst ahlgtrrhdl llhqqagdei
      121 dheayraacy rgpdvsdrla llmqpgdatw lsinlyrahr sgafqpreia aiealaplia
      181 qaarhhyala gaaqigipqr mlarlrhacp dlskreldvl rgvldgqtah eigetigvka
      241 ssvvtyqkra yrrlgissqr elfalcmqp
//
LOCUS       WP_175853324             609 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 15 protein [Burkholderia anthina].
ACCESSION   WP_175853324
VERSION     WP_175853324.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Sakaguchi,M.
  TITLE     Diverse and common features of trehalases and their contributions
            to microbial trehalose metabolism
  JOURNAL   Appl Microbiol Biotechnol 104 (5), 1837-1847 (2020)
   PUBMED   31925485
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..609
                     /product="glycoside hydrolase family 15 protein"
                     /calculated_mol_wt=67613
     Region          1..592
                     /region_name="SGA1"
                     /note="Glucoamylase (glucan-1,4-alpha-glucosidase), GH15
                     family [Carbohydrate transport and metabolism]; COG3387"
                     /db_xref="CDD:442614"
ORIGIN      
        1 mpaliedyal vgdghtaali skdgsvdwlc wprfdsgacf aaligtpehg rwllapaada
       61 aithttrryr gdtliletdy esadgavtvi dfmppgngws elvrivvgrh gtmkmrmelv
      121 lrfdygfsip wvtqlsreng mkaiagpdtv vlrtpvaltg qnlhtlaeft vsaderipfs
      181 lgyaashlrl ppardplsml artenywlew sgrcqvqgry aaavrrslit lkalayeptg
      241 givaapttsl pekiggnrnw dyrycwlrda titllalmrg gyydearawr twlgrvmags
      301 peqiqimygi agerrlpeme ldwlpgyqds kpvrvgngaa nqlqldvfge vmaalhlarv
      361 gglqaddtvw svqcslldhl ekiwqepdeg iwetrggrrh ftfskvmawv afdraiksae
      421 mfrlpasldr wralrdqiha dvcdnawheg kqafaqsygs deldasvllm pllgflpped
      481 privstveai erellhdglv mryrtteydd glppgegtfl acsfwlvdny allgriddah
      541 rlfsrllals ndlgllaeey dpvggrlvgn fpqafshval vhtamnlmhh eeamahaagq
      601 pvpavatgr
//
LOCUS       WP_175853331             227 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175853331
VERSION     WP_175853331.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..227
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25475
     Region          7..197
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mngltgstla eqahekleel ivtlelapgs vwseaslaek lntgrtpvre aaqrlaashl
       61 lqivprhgim itvpnihdql lvletrrelq rliaqraarr slpeereqir eiaqkldaag
      121 esrdvvaylr cvyalnqlia qfsrnrfaae aiaplhalsr rfyfmyhkql ddlpsaslqh
      181 trvaravaag deqeagrssd lmmdyidaft rdcftrnfep hhsrvsa
//
LOCUS       WP_175853364             213 aa            linear   BCT 11-JAN-2025
DEFINITION  carbonic anhydrase [Burkholderia anthina].
ACCESSION   WP_175853364
VERSION     WP_175853364.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Lindskog,S.
  TITLE     Structure and mechanism of carbonic anhydrase
  JOURNAL   Pharmacol Ther 74 (1), 1-20 (1997)
   PUBMED   9336012
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10096752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..213
                     /product="carbonic anhydrase"
                     /EC_number="4.2.1.1"
                     /GO_function="GO:0004089 - carbonate dehydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22924
     Region          11..190
                     /region_name="beta_CA_cladeA"
                     /note="Carbonic anhydrases (CA) are zinc-containing
                     enzymes that catalyze the reversible hydration of carbon
                     dioxide in a two-step mechanism in which the nucleophilic
                     attack of a zinc-bound hydroxide ion on carbon dioxide is
                     followed by the regeneration of an...; cd00883"
                     /db_xref="CDD:238448"
     Site            order(33,35,42,44..46,58,61,83,88,98,101,180)
                     /site_type="active"
                     /note="active site clefts [active]"
                     /db_xref="CDD:238448"
     Site            order(42,44,98,101)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238448"
     Site            order(43..46,48,50..51,53,58..60,62,64,78..79,82..83,121,
                     180,182..183,185,187)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238448"
ORIGIN      
        1 mnrpksmlva niawaretre htpgffdala rgqnprvlwi gcadsrvpae tithcvpgel
       61 fvhrnianlf hpdddnaasv leyavrvlev dhvivcghyg cggvrasllp pptdlphvar
      121 riaplcalar rhrdtlggld daaaadrlae lnvleqvkll raspivqgrp rpplvhgwif
      181 svadgrltel dsgyttppaa aepehavaav afg
//
LOCUS       WP_175853441             321 aa            linear   BCT 11-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Burkholderia
            anthina].
ACCESSION   WP_175853441
VERSION     WP_175853441.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..321
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=34240
     Region          24..290
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mqvmphttrr fpsrlrvpll lagltaclta vaaptptpep ptiqavswlv vdgesaqila
       61 ehnadaqrqp asltklmtay ivlralrdgt lsrdeqvtvg asdvaevgsd earmylvpgq
      121 rvavkdlvqg livasandaa lvlaervggs lpgfeqmmnd tarqigmpht rfttpsgitt
      181 pgnhstardl stlalrltrd fpeyygysse qhfaygkfek rnknwllgmd psvdglktgh
      241 taaagyciva tasrpqrapa mkrrvfavvl gaptasaris gaarllndaf ssykdypaap
      301 asghhyvtra srprtgdtgg t
//
LOCUS       WP_175853456             310 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Burkholderia anthina].
ACCESSION   WP_175853456
VERSION     WP_175853456.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..310
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31451
     Region          2..310
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtilviaehd nasikaatln tvaaaaking dihvlvaghn aqgaadaaak iagvgkvlla
       61 dapqlasgla enveatvlni akdyshilap ataygkniap riaakldvaq isditavdsa
      121 dtferpiyag naiatvqssd pikvitvrat gfdpvaaegg sasvdkieaa adagksqfvs
      181 revtkldrpe ltsakiivsg grglgsgeny tkvlepladk lsaalgasra avdagyvpnd
      241 yqvgqtgkiv apqlyiavgi sgaiqhlagm kdskviiain kdpeapifsv adyglvgdlf
      301 elvpevvnav
//
LOCUS       WP_175853490             766 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Burkholderia cepacia].
ACCESSION   WP_175853490
VERSION     WP_175853490.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..766
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=83882
     Region          178..765
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 msyvvavram ceftarrgdl dlrftpapta legiaghgav tsnrgaryet eialtgtwdt
       61 ltvrgradgy dpvanrleei ktfrgsldam panhralhwa qakvyahlmc darglpeidv
      121 alvyfdivse retvltqtlg aaelaaffae qcacfvgwae retahraard aalralafph
      181 gqfrsgqrel avavyraard drclmaqapt gigktlgtvf pllkacgege ldhvyfltak
      241 tpgralalea aatlgagtpa lplrvlelva rdkacehpds achgescpla kgfydrlpaa
      301 rdaaieagll drdtvraaal ahdvcpyyls qelarwsdmv igdynyyydg samlhtlaqq
      361 nqwrvgvlvd eahnlldrar kmysasldpf afaaareaap aalrkafdrl arawgtvnra
      421 qaeryaaype ipgpivsalq nlvaavgehl adaprangda llrfhfeaiq fgvlaeafds
      481 asifdatlhg epmprqpald gvasagrrrr vqstlcvrnv ipagflapry eaacatvlfs
      541 gtlspfhfyr dtlglpgdtg wldvdgpfra eqltvrvash vstrwrdrdr slepivdlia
      601 aqyatrpgny lgflssfdyl grvvalmqar hpdvpvwaqa pgmtegerda flarfdasgr
      661 gvgfavlgga fsegvdlvge rligafiatl glpqvndvne qmrramdarf gngydymyly
      721 pglqkvvqaa grvirtehde gvvhliddry rrrevrdllp rwwrik
//
LOCUS       WP_175853594             288 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MOSC domain-containing protein [Burkholderia].
ACCESSION   WP_175853594
VERSION     WP_175853594.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..288
                     /product="MOSC domain-containing protein"
                     /EC_number="1.7.-.-"
                     /GO_function="GO:0016661 - oxidoreductase activity, acting
                     on other nitrogenous compounds as donors [Evidence IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=31031
     Region          1..281
                     /region_name="YcbX"
                     /note="N-hydroxylaminopurine reductase subunit YcbX,
                     contains MOSC domain [Nucleotide transport and metabolism,
                     Defense mechanisms]; COG3217"
                     /db_xref="CDD:442450"
ORIGIN      
        1 mpaiaelfvy pikscagial sraqlletgl aydrhwlitd pagqmitqrt hprlalirta
       61 lnsdalvlsg pgmreirtpl dgdgspatpk maatvwrdtv daidtgaeta awlteflgtp
      121 aklarfapda rrgcnrkwtg eidthtqfad gypllvigqs slddlnarlt akgapaipmn
      181 rfrpnivvsd ldayeedfve hldtegaapv rlrlvkpctr cpmptidqvt gapdpawphe
      241 ptdtmqtyra npnfggeltf ginaivvega ggwlevgqsl eaeigfgd
//
LOCUS       WP_175853668             430 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175853668
VERSION     WP_175853668.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..430
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46947
     Region          12..411
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(26..27,30..31,34,67,117..118,120..122,125,145,
                     148..149,152,241,244..245,248..250,253,281,285,337..338,
                     342,346,362,365..366,369..370,373)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mesakpvapq rwwylmpiif ityslayldr anygfaaaag idkdlgithg mssligslff
       61 lgyclfqvpg aiyaqrnsvk kliffslilw glcaaatgmv snipmlmvlr fvlgvveaav
      121 mpsmlmyisr wftrtersra ntflilgnpv tvlwmsvvsg ylvhsfgwre mfviegvpal
      181 awavvwwftv kdrpadapwm sdaekaelda rlkaeqahia pvrdykaafr ssvvlkccgi
      241 halwsigvyg fimwlpsilk saatidivsv gwlaavpyla aiilmllasw lsdrthnrkl
      301 fvwplllvgt ialvasylvg eshfwisftl lvvagatmya pygpffalvp elvpsnvlgg
      361 aigiinssga lgaflgswvv gylngatgnp sasyifmava lllsvilmit vpgrseqrsa
      421 geattslrrt
//
LOCUS       WP_175853728             227 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cepacia].
ACCESSION   WP_175853728
VERSION     WP_175853728.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..227
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23893
     Region          23..225
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mtdvlplttd pesglpyrlr paagrpvarl lllhgvggne tnllnlagii dprieiaflr
       61 gpltfgpgqh awfpvrfgpn gpeidaarad esriqlitll rafrardgag aalptviagf
      121 sqggimsagv glaspddvaa favlcgrilp eidpliaprd alrplhaliv hgrfddklpv
      181 awadtadakl talgvahdtr lydaghelta emagdfgrwv geragln
//
LOCUS       WP_175853752             333 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia anthina].
ACCESSION   WP_175853752
VERSION     WP_175853752.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..333
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34342
     Region          5..330
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 meaamtstrk dertplkrml srnagvtsia afflccvvaf slstntfylp nnllnivrqs
       61 apllivatam tlvittagid lsigstlalv galsaialka gipdvvviag gigvgcaiga
      121 ingyfiafag mpafivtlgt lsivrgvall ltqgysipie snglftslgr awvlgiplpa
      181 liaaatlfag wvalrhtrfg ryvigigtna esvrragvqv hgvimrvyil sgasaalagm
      241 litsrlgsgs snqgvgfeld viaavvlgst slfggigtiv gtvlgaltia vlgnglillh
      301 vspfytqiiq gtimllaiwm ntrifapqrr rkg
//
LOCUS       WP_175853788             472 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175853788
VERSION     WP_175853788.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..472
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=48548
     Region          6..466
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 msalpdraaq rhalaatlgd gwldgasaes cepyatdvtl hsgvalgvar pastadtsal
       61 arvavahrva lvaqgartgl vgaavpdrsg tqcvvsfdrm ravrafdaan rsitveagar
      121 lsdinrvaad aglclpidlg sdpaagglvg anaggsrlik ygdvrrnvlg vevvladaag
      181 tvidalaplr krnagfdvtq cfigangahg lvtavsfala plersscaaf vafasydaal
      241 agllaferaf gemlsafefm saaavgcvaa afpalripfe tdaaacyalv eiatgmpgld
      301 glleertiat ldtlagervv ldaacapaer fwrirdalpv avgqhgipls fdvsfprgal
      361 aafvadaerw iaaahpslrc hafghfgdgg chlvvsipha daerygplqq valrgalyer
      421 vvrggggfsa ehgvgpvnva yyrkhvpaaq relaaaiqha vdplgligrv ry
//
LOCUS       WP_175853815             720 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia anthina].
ACCESSION   WP_175853815
VERSION     WP_175853815.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 720)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..720
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..720
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77103
     Region          36..714
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mspppsrfts yisdtktgia ivdaardwag tsgvtwlyvf ktilaallal gvamklelpm
       61 prtamttvfv lmqpqsgmvl akslyricgt ivgllamlvl iglfgqapel flgatalwig
      121 lctagaarnr nfrtygfvla gytaaligip swqhpdaafl samtrvtevt igilssgavs
      181 alvfpqhvse qisrvnrerf arfaddvlsi lcgridkpfl ealsmrivde tvnseaarsa
      241 avferpdtrl rngrltrlna ermaastrlh alsqliarlr aaradlvlte idalmagiav
      301 pirverqnat hagdtealat slaellarcq aalpgrarva rnrlakggat ldfdtavell
      361 drfldsyiay aktylslrat ahereqwtvp yeprtnplia aiagiramll tlalgafwia
      421 tawpsgallv lnggaicalv assarpsrta fqmaigtaca avvglvvmfv vypvidgfpl
      481 lcvalappla lgcwmttrps lagygigyci yfcfltgpdn vvaydptsfm ndaialvlsm
      541 lmasvafelf lppttrglrk hlladlrrqv vfacidspat lrtrfesrtr dlmfqvrais
      601 rddpaanses iewflailei gsavvdlrga maidaapawl adathacrai qrlfeaptpk
      661 asavatqavq vaigalqrti qttdatrpas phvqtalgsl hfihsalvap dsplpapapa
//
LOCUS       WP_175853825            1084 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cepacia].
ACCESSION   WP_175853825
VERSION     WP_175853825.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1084
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115685
     Region          3..1062
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mlkivrlalt rpytfvvlal liliagplaa lrtpidifpd iripvisvvw nyaglqpddm
       61 sgrvityyer tlgttvndvq hiesqsfrgy givkiffqpt vdirtataqv tsisqtvlkq
      121 mppgttppqi lnynastvpv lqialtsntl deqkladyav nfirpqllsv pgvaiptpyg
      181 gksrevqidl dpqalqskgl saqdvahala qqnqiipagt qkigrfeyni klnnsplsld
      241 alndlpiksv dgttiyirdv ahvrdgyppq gnivrvdghr avlmsilkng sastldiiag
      301 vkaklplveq tlppglklvt mgdqstfvng avsgvaregi iaaaltslmi llflgswrst
      361 liiaasipla vlsaiallaa tgetlnvmtl gglalavgil vddatvtien vnwhleqgkd
      421 trtaivdgak qivmpalvsl lcicivfvpm lmldgisrfl fvpmakavif smmssfvlsr
      481 tfvpmlaqyl lkphasagha sgelaaimds haghagahda ppsrnplvrf qraferrfes
      541 vrasyrillg laltrrkpfv vaflcvvaas fllvpwlgrn ffptidsgei slhvrapvgt
      601 rveetaaefd rientirgvi ppaqlrevvd niglpnsgin ltynnsgtlg pqdgdilisl
      661 shdhaptady vrelrerlpr aypgttfsfl padivsqiln fgapapvdlq vagpnqqanl
      721 ayarelyrkl rlisgvadpr iqqastypqf tvavdrtrad qlgiteqdvt nsvvatlagt
      781 sqvdptywln prngvsypiv aqtpqyrmtt lsalqnlpvt gangqsqllg glatitrgvg
      841 navvshynie plfdiyattq grdlgavaad igsvvkatak dlpkgstvtl rgqvqtmnsa
      901 ftglllglag aivliylliv vnfhswadaf vivsalpaal agivwmlftt htpmsvpalt
      961 gailcmgvat anailvvsfa rerlaetgna lasaleagft rfrpvlmtal amiigmapma
     1021 lglgdggeqn aplgravigg lacatiatlf fvpvvfslvh rrdalkhdap rasfpsasga
     1081 shvh
//
LOCUS       WP_175853871             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175853871
VERSION     WP_175853871.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32480
     Region          7..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..276
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrfatmeaf vriietgsfs aaarqlrvgq psiskavaql eerlgtrlls rstrgltpte
       61 agqgfyerak raldeanead laatgagtgl tgrlrfsatv tfarlhvmpl lpafleahpa
      121 ltveailddr svdligenid ialrmgdpks mtvtgkriat srrvvvatsn yldrhgtper
      181 pgdlpkfpav iytqgggget wtfrkgekse vvtlknmist taaegvreav fagmglavst
      241 ewmfqpeidl hrvetvlrdw tlpsldlwav ypagrqatak arafaafise claktpfapa
      301 g
//
LOCUS       WP_175853928             326 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH:quinone oxidoreductase family protein [Burkholderia anthina].
ACCESSION   WP_175853928
VERSION     WP_175853928.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Shimomura,Y., Kakuta,Y. and Fukuyama,K.
  TITLE     Crystal structures of the quinone oxidoreductase from Thermus
            thermophilus HB8 and its complex with NADPH: implication for NADPH
            and substrate recognition
  JOURNAL   J Bacteriol 185 (14), 4211-4218 (2003)
   PUBMED   12837796
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..326
                     /product="NADPH:quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34141
     Region          1..322
                     /region_name="QOR1"
                     /note="Quinone oxidoreductase (QOR); cd08241"
                     /db_xref="CDD:176203"
     Site            order(40..41,122,126,147,150..152,171..172,176,191,215,
                     237..238,240..241,262..264,314,316,318)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176203"
ORIGIN      
        1 mkallctafg pidrlriddv aipepaagqv rirvkaasln fpdalivqgl yqvkpalpfs
       61 pgaefagvid avgdgvsqwr pgdevvaftg hggfaeqcva dvhqiaalpp gmtfeqgaal
      121 vlaygtslha lqqrarlqqg etllvlgaag gvglaaieia kalgarviaa assaeklalc
      181 reagaddtid yatedlrrrv deltggrgad vvydpvggay seaalrataw rgrflvvgfa
      241 ageipkialn lallkerdil gvfwgdavrr dpaqhmanmr qlaqwfaagk vrlaitervp
      301 lsgaadaitr ianrqvkgkv vilpda
//
LOCUS       WP_175853945             128 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia anthina].
ACCESSION   WP_175853945
VERSION     WP_175853945.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..128
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=13918
     Region          1..125
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mddyllfagr ffialmfvls ginkflffqh gldevraknl plprialsst iivqlvcgva
       61 imigfqttla slllavftla tavvfydfwn qqgnqrtlml tgflehisii ggfiiliaag
      121 pgrlaaha
//
LOCUS       WP_175854051             248 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175854051
VERSION     WP_175854051.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..248
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=26887
     Region          3..231
                     /region_name="ArtM"
                     /note="ABC-type arginine/histidine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4160"
                     /db_xref="CDD:443325"
ORIGIN      
        1 msidfdflid tlrqllaavp ttlglffasl vlggllslvi vtmrvsphwl pnrfarayil
       61 vfrgsplliq mflvyyglgq fgviresfmw pllrepyvca vlslalctag ytaeilrggl
      121 mavpvgqiea gysiglsgfa llrrvigpia lrqclpayst eavllvksta laslvtvwev
      181 tgvaqqiiqq tyrttevfvc aaliylglnf ivvrvlgale wrlsghlrap kqtgapaaaa
      241 rdarrvas
//
LOCUS       WP_175853966             477 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175853966
VERSION     WP_175853966.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..477
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47737
     Region          34..467
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(40..41,44..45,48,80,130..131,133..135,138,160,
                     163..164,167,291,294..295,298..300,303,331,334,387..388,
                     392,396,412,415..416,419..420)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msdrapalgg apaaiapphr tslraifptv aaaslgfaiv qldvtvvnva ipslghsfgs
       61 svhglqwivd aytlsfaall ltsgtladrf gsrrlfaygl alfllaslgc alapslaali
      121 aarvaqgvga amilptslal ithacandaa arvravawws atggaisaag ptlggllids
      181 lgwraiffin lpicaaglwl tvhhvrdsaa artrlfdpag qlvavlvlal ltggiiraga
      241 qgpgdpyaag alaasvalga lfvaierrva apmlqlaffr iarvpgvlai gaitnaafyg
      301 lifslslyfq nargftates glalapltii mlaniasarl avrhgfratv ivglavslag
      361 yvwlwrtlda htpyallapg laamaigggi aipaltstll gsveagrsat asailntarq
      421 vgaavgvaal galvagqgaa ivagasrafa vaaglvavci vlaarwpgda pepgtla
//
LOCUS       WP_175854053             240 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175854053
VERSION     WP_175854053.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..240
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=25368
     Region          1..235
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 mailemlgfg tegwggvlll aalmtialtl aalavgavig agiaaaklsr hrsarvlgdl
       61 yttvfrgvpe llviylfyfg gstlvttvgq wfgaegfvgv ppfvigalav gmisgayqae
      121 vyraavlavs kgeleaarsi gmprsmvlrr ilipqvlrfa lpgignvwql slkdsalisv
      181 tglaellrts qiaansthqy fvffvaggal ylvmtglsnr vfnraeaivg rsfrrnfarn
//
LOCUS       WP_175854054             390 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia anthina].
ACCESSION   WP_175854054
VERSION     WP_175854054.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..390
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42607
     Region          12..282
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 midgqillgh sipwgmvggg lgsqigyshr saalrdgsfr lvagafdida drgrqfgvkl
       61 gvdaarcyad yramfeaeas radgiravsi atpnnthfei craalnaglh vvcekplcft
      121 tgeaealqrl sveknrivgv aygysghqmi eqargmiarg dlgeirivqm qfahgfhseg
      181 veaasaaarw rvdpkfagps yvlgdigthp lyisevmvpa lkirrlmcsr qsfvksrapl
      241 ednaftimey dtgaigyvws savnagsmhg qkvrvigska svewwdehpn qlryeiqgqp
      301 aqvldrgmgy lhpdalredr igaghpeglf eawsnlyarf alamdatdrg dtdalkqirf
      361 pdihagvegv rwvehcvrsa daggvwvdyr
//
LOCUS       WP_175854075             204 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175854075
VERSION     WP_175854075.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..204
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22466
     Region          11..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mntphelsge pavrdrllda aealiysggi hatgvdaivk rsgaarksfy shfeskealv
       61 vaalerrder wmrwfvdatl argksarvql igmfdvlrdw fsqpdfhgca flnasgeiad
      121 addpvrvvar ehkerllmfv rerfdayade agierrglar larqwlvlid gaigvalvsg
      181 danaardara taellldtvs rssk
//
LOCUS       WP_175854115             309 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia anthina].
ACCESSION   WP_175854115
VERSION     WP_175854115.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..309
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33522
     Region          2..256
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msdmislgvi gigkiardqh lpaiaaepgf altacasrha evagvrnypd lrallaaere
       61 ldavslcapp qvryaqaraa leagkhvmle kppgatlgev aaldalarer gltlfatwhs
      121 rcasavepar awlatrsira vqvhwkedvr rwhpgqqwiw epgglgvfdp ginalsivtr
      181 ilprelvlre atlyvpsdaq mpiaaeldcm dtdgvpvrae fdwrhgpveq weiavdtsdg
      241 vlaisrggaq lsidgepvei gpereypaly ahfraliarg esdvdvrplr lvadaflfgr
      301 rvgtdafgr
//
LOCUS       WP_175854159             799 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia cepacia].
ACCESSION   WP_175854159
VERSION     WP_175854159.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 799)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 799)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..799
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..799
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84485
     Region          83..762
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mirrpkaagk ggamrrarra rhggamrgal lgpalgaial fglstasara qqpadgtaat
       61 ggavppaava vaqeapqasa vtlptvvvvg ttpllgigtp lqkvpanvqt vraaeldaqh
      121 ratladffaa nlqsvtisea qgnpyqtdvn yrgftaspll gtpqglsvfv dgvrvnepfg
      181 dvvnwdilpt qaidrmqlip gsnpvygrnt lggalaittk ngksnpggea evsggswgrk
      241 taaieqggti gsnldyyata nvandggwad hnasrvrqaf gklrytdsdt tlsisaggad
      301 nalygtqtip rsfldnrkqa ytypdlnrns agyltlsgdr ffgehvelsg nayyrhlrnt
      361 nissnnntdy gsvgddgtvd avqgtnaqst ivtdsyggsl qltllgklgg manqliagva
      421 advanssyva ssqdayftdt raaigvgdfe pqtraktrna nlgvylsdal sltphwtltv
      481 sgrydwskaq igdesgvqpl ldgnhtfsrf npalglnwnp vagftayaty negmrsptai
      541 elacadpaap cslpndfiad palkpviskt feagmrgrig aattwsaaay rttltddiqf
      601 isspasaqgy frnvgdtrrq gielagrtrf gplgvglsys yvdatyrssw tehspansaa
      661 dangnvavkq gdhipgipah tvklrldyaa tprwdiganv mwrsgvyarg dennqdvngr
      721 isgyvlvdld mryritkrfe vfasvtnlfd kryasfgvlg qnffngpnht fdganpvneq
      781 fvgpgaprga wvgvryawd
//
LOCUS       WP_175854165             317 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Burkholderia cepacia].
ACCESSION   WP_175854165
VERSION     WP_175854165.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..317
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33155
     Region          <123..301
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          237..315
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mwnglrlltr hgggggvnra rqrdgsridr yaflfmsamw ractrmgerg kagamstaaf
       61 garqatgvrg aagdrarrrg tcvasvfaav calhaalfvl laheqivrre plqrqvmvat
      121 liaaapeast taaakakpva ashavqeats aprssagsvs rmnrqvasgr prppahdapv
      181 paparpspsl pavaqrdtph ddaaarmptq tqtqpesrss svsapprfva hpdcalvkpd
      241 yppqslrlge hgtvlvelet daagqivaar vvtgsgyprl daaareavla srcaphvfdg
      301 apvptrarap iafnldd
//
LOCUS       WP_175854195             330 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia anthina].
ACCESSION   WP_175854195
VERSION     WP_175854195.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..330
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35274
     Region          4..321
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 maallevenl gvrftrkdvp pidavsgvsf sleagktlgi vgesgsgksq tvmallglla
       61 gngtttgaar yrgdnllemd tralnavrgd rvamifqdpm tslnpfltie rqmtetlqlh
      121 rklsrkeatk raiealesvr ipdaarrirm yphefsggmr qrvmiamall sepeiliade
      181 pttaldvtvq aqiidllrel nrergtaivl ithdmgvvag laddvmvmya grtveyapad
      241 sifaapshpy tigllnalpr ltdaddapli aipgnppmpg tapvgcafak rctyaeercg
      301 aarpaletyg vvgavrachr pladltgglr
//
LOCUS       WP_175854282             371 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia anthina].
ACCESSION   WP_175854282
VERSION     WP_175854282.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..371
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39492
     Region          5..349
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,236,303,323,325..327)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,103,110,183,186,188,236,243,303,323,
                     325..326)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(27,103,183,186,188,326)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mtqdplfqpl qfgaltlpnr ivmppmtrsr asqpgdeane lmaayyaqra saglivsegt
       61 yiaplgkgya wtpgihtpsq vagwrkvtda vhaahgrifa qlwhvgrlsh tsllggqqpv
      121 sssplqakgv nvfvagedgs tpgfvqasep ralsvdeire ivdqyraaar naieagfdgv
      181 elhgangylv nqfidsnant rtdayggsle nrlrflrevt qaliegtgda srvgirlapl
      241 ttlngcvddd pqttylaaat llgelgvgyl hiaeadwdda plmpvefkqq lraaypgvli
      301 yagaytaera reaiaagwad lvafgrpfva npdlperlrt gatltphdrn tlfgggaqgl
      361 tdyptlvqaa a
//
LOCUS       WP_175854304             379 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: enoyl-CoA hydratase/isomerase family protein
            [Burkholderia].
ACCESSION   WP_175854304
VERSION     WP_175854304.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..379
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41952
     Region          26..362
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 mstpvtnhda faehapevlf rvvnrvalit lnrpaalnal syamigelaa mlercrhddq
       61 ivavvlrgag ekgfcaggdv ralyrmvaqr etwlpffvde yrldytihtf pkpvvalmdg
      121 vtmgggmgla qgaalrvate rskvampetr iglvpdvgat hflsrmpael elyvgltgam
      181 lsgadaltak ladlcvpsaw ldtfetries vkwegdalpl lrkvfeppcn vvphaaldgq
      241 mpwivrhfdk rstverivat ltqdlareel srehrqwlqa tldaltghsp tmlyvtreal
      301 lrgrqmtlae sfrmelgiva raieegdfce gvrahlvdkd rkprwapasl velraervrh
      361 fltspwklfa hpladlgea
//
LOCUS       WP_175854316             129 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Burkholderia cepacia].
ACCESSION   WP_175854316
VERSION     WP_175854316.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..129
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=13463
     Region          5..122
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mvtatrlgkp ycveigngrs vvrsdtrkdg qggdagmrph ellesalaac vcmsidlaar
       61 ragvtlpact advtvdrldh etgfdialrf aaplshaqqt lvrdavrasp vartlgkpir
      121 vrpatiasg
//
LOCUS       WP_175854366             548 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NRAMP family divalent metal transporter
            [Burkholderia].
ACCESSION   WP_175854366
VERSION     WP_175854366.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..548
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=58751
     Region          48..452
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 mstpsnvspp iaveraavld eahlgdirga lgtiahhdtg trgswwarlr tllaiigpgl
       61 ivmvgdndag afgtytqagq nygttllwtl lllvpvlyvn qemvlrlgav tgvgharlif
      121 erfgkfwgaf svidlfllna ltivtefigi tfvldffglp kvagvcvaaa ltmaavstgd
      181 frrferfaig lcvlslllvp vlvsihppva qmtrdffvpn wpahaklsdv mllvigivgt
      241 tvapwqlffq qsyvidkrit prfmkyekad lwigiafvli gavamigfsa alfnghpeag
      301 nfadaggiia glekyagrts atlfavalld aciigaaavs lstayaigdv fkirhslhrg
      361 vsdakgfylv yfgivaaaat lvlipgsplg llteavqtla gvllpsatvf llvlcndrqv
      421 lgpwvnstkl nvftgaviwv lvllsiilta svmypdisge aivdvlvggt vlaitgyivt
      481 vlirrnkrvi epaidrtlrd twrmppldtl epqnmtlatr iwmavlrgyl viavglvivk
      541 vvqmtllk
//
LOCUS       WP_175854395             264 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Burkholderia].
ACCESSION   WP_175854395
VERSION     WP_175854395.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13673959
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..264
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27731
     Region          12..144
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          179..260
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mhrvthyrrt gegieaisle sdrafprhah defgvgvivs gahrswsgrg qvdalagdai
       61 mvnpgemhdg spieagtgrr wrmlylapal vagvaaeegl ggielahpav rdarltaavg
      121 rlharivage srplardeal vmlvagllar hanrtlptag vapairiare rldaapatpv
      181 slaelaglsg vsrfqllrgf arelgitpha yliqsrarla rallasglpi adaaaeagfa
      241 dqshltrafa rqfgitpgrf tqag
//
LOCUS       WP_175854405             140 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Burkholderia cepacia].
ACCESSION   WP_175854405
VERSION     WP_175854405.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..140
                     /product="RidA family protein"
                     /calculated_mol_wt=15257
     Region          1..129
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 maeavnppev wapfgafsma viqgdgrivh lkgqvaldrd grvvgqgdmr tqlrqtldni
       61 ravlaamggq mqdvislvhy atdidafmqa gdirntyfaa pypvtttvqv erlyhpdlli
      121 eitavaeipl arfrrpgpra
//
LOCUS       WP_175854441             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175854441
VERSION     WP_175854441.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33117
     Region          3..61
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 melrqlryfv avaeelhfgr aakrlfisqp alsfdirkfe ealgvqlfsr tnktvaltna
       61 gavllgearr lllqaaeaer ltvrsasgla grlrigfvhs mlyrglpdav rrfeadypgv
      121 evvlsemntq aqvqaiqrgq idlgyahwgh cppeveatpv yaepfmcclp aahplarrrq
      181 valaalaaep filfpreaap hyhdliiaqc vnagfsplir hearlwqtil smiefgmgia
      241 lvprvlqqvk sdrlafrplk daslesrtle lkrsgtaepv alrfadyvra sidalpalag
//
LOCUS       WP_175854452             309 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia cepacia].
ACCESSION   WP_175854452
VERSION     WP_175854452.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..309
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33757
     Region          8..301
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mtssstpryr gifpvvpttf tdtgeldfas qkravdfmid agsdglcila nfseqfaitd
       61 derdvltrti lehvagrvpv ivttshygtq vcaarslraq qlgaamvmam ppyhgatfrv
      121 peaqifdffa rvsdaidipi miqdapasgt vlsapflarm areieqvayf kietpgaank
      181 lrelirlggd aiegpwdgee aitlladlha gatgamtggg fpdgirpile awregrhdda
      241 yaryqawlpl inhenrqsgi ltakalmreg gviacerprh pmpelhpdtr aellaiarrl
      301 dplvlrwah
//
LOCUS       WP_175854450             382 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175854450
VERSION     WP_175854450.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..382
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41015
     Region          1..370
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masismrrvq kaygdhapvi rdvdleigah efcvflgpsg cgkstllrmi agledlsage
       61 lsidgrrvdd vpaaergvam vfqsyalfph mtvyenmafg lklarvpkae idrkvrdaar
      121 ilqldtller kpkalsggqr qrvaigraiv repgvflfde plsnldaalr gqtrieiarl
      181 hrqferasvv yvthdqteam tladkivllh agadtaqhgs iaqvgapldl yhhpasrfva
      241 gfigsprmnf lpavvtacda rrttvtltps getftlprdg salgvgaavt lgirpehltl
      301 gaahdattla rdvalverlg eqtyvhldqp gghsliakvp gdaqvrsger vlvhapaaac
      361 hlftedgrav pacadvhvhh ya
//
LOCUS       WP_175854544             289 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfurtransferase [Burkholderia anthina].
ACCESSION   WP_175854544
VERSION     WP_175854544.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..289
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30472
     Region          15..284
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mphthyttli saanlaerla aapgsvavfd crfdlvdpna geaayaaghi asaqylhldr
       61 dlsgrktgtn grhplpsrda latllanrgv kqgqqvvayd ahggayaarl wwllrwlghd
      121 svavldgglq aweaageplt tdvphpaagd frtgaplest vdaaavlanv tsparvvida
      181 rapdryrgen etidrvgghi pgarnrffkd nlnadgrfkt ghelretftt llagtepnrv
      241 ilqcgsgvta chnalaleia glhgaslypg swsewsadps rpvatgptp
//
LOCUS       WP_175854549             127 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia cepacia].
ACCESSION   WP_175854549
VERSION     WP_175854549.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..127
                     /product="VOC family protein"
                     /calculated_mol_wt=14221
     Region          1..126
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 mplpmtriil yvqdvtllka fyqrhfdlpv ieeidgewav ldagaielal hlagpafrha
       61 aepsnanpat nnvklvfrie tdidahrdrl ardgvtvrdv krfdgfpyrl ldgidpegnv
      121 fqvmqpd
//
LOCUS       WP_175854556             221 aa            linear   BCT 11-JAN-2025
DEFINITION  O-methyltransferase [Burkholderia cepacia].
ACCESSION   WP_175854556
VERSION     WP_175854556.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..221
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23668
     Region          65..219
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mttlihdpla sllarlfdea eaaspatspa fadlsrdeqa rlmrsktdyt dlyarlkdyp
       61 lpvsretgtl lymlarsrga raivefgtsf gistlhlaaa lrdngggrli tsefepskva
      121 raranltaag ladlveireg dalrtlaadl pdsvdlllld gakglypeil alvephlgag
      181 afvvadnaey spdylayvra pengylsvpf ggdvelsmri r
//
LOCUS       WP_175854582             391 aa            linear   BCT 11-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Burkholderia
            cepacia].
ACCESSION   WP_175854582
VERSION     WP_175854582.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..391
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40704
     Region          36..389
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mtqlfdtlgf vdasaaragi vaqhdaaaaa aggaavsleq vgkvfatprg qaaalrdvtl
       61 dvrrgevfgi igrsgagkst llrlvngler pssgrvrvqg vdvgaldedg lvalrrrtgm
      121 vfqhfnllsa ktvfenvalp lkiagvpkae rvrkvealle lvglaakrda ypaslsggqk
      181 qrvgiaralv hdpevllcde atsaldpett qsilalladi nrrlgltivl ithemevira
      241 vcdtvavieq gevvetgpvw rvfgdprhga trallstlvh dlpaelaarv qplpeqaalp
      301 dgaqvvldvr ytgesggepd vgalaaalgg svrflhggie riqghaqgrl viaaapradd
      361 aglpaargga vaallerarr hanhaevlgy v
//
LOCUS       WP_175854628             323 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175854628
VERSION     WP_175854628.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..323
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35507
     Region          38..190
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <186..313
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mslepasaqs pslpprdrkr lvtllralap degynltalp svrilrsnra lsrtpvlydp
       61 givivcqgck rgyfggeryl ydehhylavs vpvpfsmetd atperpllal ylhldftmaa
      121 elaaqidreg iaepvqaprs mmstpmdatm hasvlrfvea mgrpldaavl gpallrelyf
      181 rvltgaqgsa mrsalamrgq fgrigrslrv ihadyaqpld vpqladaagm svpsfhshfk
      241 aitqvspmqy lkstrlhqar llmvredlta eaagyavgyt spsqfsrefk rlfgltpake
      301 tqrmresfai paafddavfv ssh
//
LOCUS       WP_175854674             421 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia anthina].
ACCESSION   WP_175854674
VERSION     WP_175854674.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 421)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 421)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 421)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..421
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45461
     Region          <198..415
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mtiapsspst aalkrelkaa earkrtmall liaplaifll lifvvpigtl ltravqnpei
       61 atalpntita lsswdrkapp sdaayvalaa dmtkvadsda mgalarrlnt eipgyrslva
      121 ktaramplkd dndaaaaalt paqtraklid ldsrwgdvty wqsiakngsq lspfyllasl
      181 dhkqdgfghi vqadpdqsiy laifgrtfvi gvavtlfall lgyplaywis tlserranlv
      241 milvlipfwt svlvrvaawi vllqseglin kaligsglis hpltllfnrv gvyismthil
      301 lpfmilplys vmksipptyq raavslgshp faafwrvyvp qtypgigaga llvfilaigy
      361 yitpallggp ndqmvsyyva yftnvtinwg macalgglll aatlvlyavy grftrtnvsl
      421 g
//
LOCUS       WP_175854729             139 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175854729
VERSION     WP_175854729.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..139
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=14524
     Region          66..>138
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mkvfqlqars lhirrhrakr vgmaiaivaa tacvtavpdv faagddsaas ssmsssssts
       61 shsttgrkir datittkvka elvgtsglss gdihvktrhg ivmltgsvpd eqqrtqavgv
      121 vkqvdgvqdv rdqltirak
//
LOCUS       WP_175854761             392 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: YncE family protein [Burkholderia].
ACCESSION   WP_175854761
VERSION     WP_175854761.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..392
                     /product="YncE family protein"
                     /calculated_mol_wt=42027
     Region          <63..190
                     /region_name="8prop_heme_binding_protein"
                     /note="eight-bladed beta-propeller heme-binding domain in
                     cytochrome cd1 and similar proteins; cl49617"
                     /db_xref="CDD:483957"
     Region          63..96
                     /region_name="propeller blade"
                     /note="propeller blade [structural motif]"
                     /db_xref="CDD:467722"
     Region          70..105
                     /region_name="beta_rpt_yvtn"
                     /note="40-residue YVTN family beta-propeller repeat;
                     TIGR02276"
                     /db_xref="CDD:213697"
     Region          141..185
                     /region_name="propeller blade"
                     /note="propeller blade [structural motif]"
                     /db_xref="CDD:467722"
     Region          166..360
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mqprlrrhir fprpaivvaa alagfcaqga iaasavaavp gmppvinpdn lygearagrm
       61 saavagalpr iyvpnlrsnd vyvidpatyk vvdrfavgrs pqhvvpawdl rtlwvannae
      121 ertdgsltpi dpktgkpgpa vrvddpynmy ftpdgkdaiv vaeaharldf hdpgtmalks
      181 slevpqckgi nhadfsidgr yalftcefgg mlakidlvnr kvlgyleldr kgmpqdirva
      241 pdgkvfyvad mmadgiyvvd gdrfaktgfi ptgvgthgly psrdgtklyi anrgsnlvhg
      301 prhgkgsvsv ldfatrkvva nwpipgggsp dmgnvsadgk tlwlsgrfdd vvyaidttsg
      361 avrsipvgme phgltvwpqp gryslghtgn mr
//
LOCUS       WP_175854790             627 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia cepacia].
ACCESSION   WP_175854790
VERSION     WP_175854790.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..627
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=67509
     Region          12..543
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mlratasaaa adlivcngki atqddrqsfv talavkdgri laagsghdvm rhahagtqci
       61 dlngrtvipg lndshlhmir gglnfnlelr wdgvptlada lamlrrqvlr tpaphwvrvv
      121 ggwtefqfae krgptaaeln eiapdtpvfi mhlgdsalln aaalraigyg rdtsnppgge
      181 iqrdrlgrpt glliarpdma vlhealerap klghddqmns mrhfmrelnr lgvtsaidag
      241 gdfqafpddy gailalarrg emtvrvaysl fvqhagreld dyarwvtlak pgdgdaflrm
      301 ngagellvys aadfgnflep rpdlpaalea elaavvrllv rhrwpfrlha tydesigrfl
      361 nvleavnret pfdglrwffd hcetitdani ariaalgggv tvqhrmafqg eyfiarygaq
      421 aamrtppira mlaaglpvga gtdatriasy npfvslywmv sgrtvggtal ypernrlgrm
      481 ealrcytvgs awfsgeddck galvpghyad favltddyft idearitsls svltvvggri
      541 vhaddefasl apppppvspa wspvaefgga grrrsaesas lraaagaglp aagaarglgr
      601 afvqrlhaaa metaeqceas gypgfay
//
LOCUS       WP_175854786             216 aa            linear   BCT 11-JAN-2025
DEFINITION  DsbA family oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175854786
VERSION     WP_175854786.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..216
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22604
     Region          6..205
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(14,17)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 mkpvevtvty dlicpwcwia ehrlaeaiea aglagavnvr fvpfelnptm paggidrkay
       61 rsakfgswar sqaldahvad agraaglvfd hariartpnt rlahrlvwfa qqrgsavalv
      121 dalfaayfrd grdigdadvl veiaagagla gdavraflas gegldavval eeaavrdgva
      181 svpstrigst vvsgaqpadv fraalldaqr ardraa
//
LOCUS       WP_175854791             370 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia cepacia].
ACCESSION   WP_175854791
VERSION     WP_175854791.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..370
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39283
     Region          4..334
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,233,300,320,322..324)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,181,184,186,233,240,300,320,
                     322..323)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,181,184,186,323)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            186
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mssllshydl rglplpnrvv mgpmtrsrap srgqptelma eyyaqrasag livteatnvs
       61 pasasfeltp glvtdeqaag wkqvtdtvha nggrifaqlw hggrvssltl lggdaplsps
      121 gvnddleqlq vwaqlqngyy tkihatpsra mttdevadtv defrdaavra maagfdgvei
      181 haangylphq flsstlnrrd dryggsvanr arfleeivda vgavmplsrv gvrispyaky
      241 nnvrdadpdt tyayvgrmld eagvayvhaa dtngwsgepd lprivantrk hfggtlivng
      301 giapdaanal idagdadlva farayianpd lverlaanap laapkavgwy ggdragyvdy
      361 arhdaagvsa
//
LOCUS       WP_175854806             423 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175854806
VERSION     WP_175854806.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..423
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45430
     Region          91..415
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 maqsqhvkvi glphskeaya irdflkrgvv eyewceltsd tdcvrelgia plrdvrlpvv
       61 vfpdgtciyq ptlpeiaakl gwvsgprfie ydvsiygagp aglsaavyaa seglravvie
      121 rdaiggqagt sslienymgf pdgipgaela erarqqavkf gvellmmreg vhatfvdgki
      181 rvdmadgsil tarsnicatg ieyrslglpd epkflnagly ygagsseapm cegkhvfivg
      241 ggnsagqavm nfarharevt mivrgaslaa tlsrylidri erlpnvtvry gttvdalqgd
      301 grleaivlrt edgardvlpa thlfvcigga pntewardtd iirnpggylv tgsdlydcpd
      361 fervwplerr pyyletsvpg sfaagdvrsg svkrvasavg egamavtfvh rflgedahrp
      421 sgt
//
LOCUS       WP_175854887             402 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175854887
VERSION     WP_175854887.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..402
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=44089
     Region          27..84
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          116..318
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(131..132,134..135,138,142,144..150,244..249,
                     255..256,258..259)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrdtlepdal prgasdaaga ldvldarlmr illvlltert vsraavrlnm sqpatsaalk
       61 rlrtllgdpl lvrsrygmvp tefgarliep lrnalrvidf iriqqptfda rtsvrtyrig
      121 cpdylnvlfv pklvalfrer apnaqlvfhp lgdgfddera ladgeldvvi dnrparssrf
      181 rqddlfddrv vclmrathpl arhgamtaad fadapqlcpt pswleasgai drqlervglq
      241 rrivvtlphf elaahalvrt dmlltttyrl arhyakllpl aavalpvepp divyrmtwne
      301 sgacvdgvrw lrgliaeatr awldaeamlp avaavpagaa adagnsvtaa gdtadtsdap
      361 atadtpepvr rtrrrqakhc rashpprvah aarihrhatk sh
//
LOCUS       WP_175854913             520 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175854913
VERSION     WP_175854913.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..520
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=55307
     Region          54..508
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 miskeaikrg ynrgnyvvga htpppyslnl qtagstfaea gmqrapvvvs pqqvealrav
       61 adevltqpad vvawtrdwwa asmvaetggr patphavivr vstveqvqav mriahaatip
      121 vtasagrsnv tgaalpvrgg ivldvcglnr ligvdtesqi vdveagmfgd vfeetlqreh
      181 gltmghwpss fgistvggwi acrgagqlst rygkiedmvf gidvvladgs lvtlggysra
      241 avgpdlqqlf igsegtlgii vrarlklhrl pdygraiayg fdtfaaglda creilqrgan
      301 paalrlydel esgvqfglpd tnvlliadeg aremvdavma igarvgeegg rkldgdaifa
      361 kwldtryltg ksaegfkrsp gfvadtlemc grwrdlaaiy rdvvaalqav pgtlagsahq
      421 shayadgacl yfslrgdvav aergawyraa wdaanavliq ynatlshhhg vgllrspymr
      481 dslgtafpvl qavkrvldpk hilnpgklgl gdetgphvdr
//
LOCUS       WP_175855029             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175855029
VERSION     WP_175855029.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33591
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdyidklrif rsvvelrsft raadmlglar pvvsravadl earfgsrllh rttrqvslte
       61 taeriyerca avldeldsle aeaqsptrep egllrlvaht taalnrlvpl iagfkathpk
      121 vrldvtlter pvdlvgegyd igivvpymlt settvvrlve ripvvivatp aylrahshpq
      181 apadladhpf vpmspslrrp alsfridgdt ltvpfrfdis snspvfnrem vmhdfgigvv
      241 pktlvgeela sgalvqllpd adlvdafvei klayanrall pakvkafidy taaycdregw
      301 ivpaaa
//
LOCUS       WP_175855034             359 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Burkholderia cepacia].
ACCESSION   WP_175855034
VERSION     WP_175855034.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..359
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40119
     Region          12..194
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(15,17,102)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(49,101..102)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            100..102
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 msrhtrkplv slvvpfhdea eaidaffata lpilesidtt rfeivcvndg srddtldrli
       61 diaagdprvr ivdltrrfgk eaaltagide aagtavilid adlqdppali pamverwlag
      121 aevvaakrtd rmcdplmqrv aaalyyrvhn rlsevempen vgdfrlmdrq vvdalralpe
      181 rrrfmkglfa wvgyrteiie ytraprsggr skfsgwrrwn falegitsfs tvplrvwtyi
      241 glafaalsfi ygtfivmrtl lfgnpvhgya slisvmlfvg giqligigvi geylgriyhe
      301 skqrpvylvr rryraqrdaa ahpaskllqf plkrthaarr rtplpataag hgarkvsvk
//
LOCUS       WP_175855063             127 aa            linear   BCT 11-JAN-2025
DEFINITION  sirohydrochlorin chelatase [Burkholderia cepacia].
ACCESSION   WP_175855063
VERSION     WP_175855063.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..127
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=13204
     Region          1..>117
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 msshgivlfg hgardprwae pferlatrlr gaaspaahvs laflelmtpt lgdavaaqva
       61 agcshitvvp vffgqgghvr rdlpqlvdac raahpgieih cataigeddg vldaiaryci
      121 dqidgna
//
LOCUS       WP_175855062             419 aa            linear   BCT 11-JAN-2025
DEFINITION  sialidase family protein [Burkholderia anthina].
ACCESSION   WP_175855062
VERSION     WP_175855062.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 419)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..419
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44694
     Region          54..>241
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Region          101..150
                     /region_name="Sialidase propeller 2"
                     /note="Sialidase propeller 2 [structural motif]"
                     /db_xref="CDD:271234"
     Region          161..214
                     /region_name="Sialidase propeller 3"
                     /note="Sialidase propeller 3 [structural motif]"
                     /db_xref="CDD:271234"
     Region          281..>407
                     /region_name="COG4692"
                     /note="Predicted neuraminidase (sialidase) [Carbohydrate
                     transport and metabolism, Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443727"
ORIGIN      
        1 mvavksfaag calwlaalsp agahdapkaa dphaahmsmq aaptqqkqpl atgaafdarh
       61 llwvawvega hvvvahsdda grtlsapviv nampepiyts aenrpkvats pdgravyvsw
      121 smpldapytg mvrfsrsldg gatwsvpvtv hhdrqaithr fdmmavdpag niaiawidkr
      181 dlvaakaagq ayegaavyya vsrdggasfe perkvtdhtc eccriamaid paghieavwr
      241 nvfpgqirdh alavlpvsas apvvpvratf snwhveacpe hgpalaitpd gtrhlawfgv
      301 vdgradvfys rigadgrplg tpwafgensa vpaeqashaa lvahgdvvwl awkafdgegm
      361 qiklrrsddr gehwsaprvi aatagasdnp qllddagriy lswrtrndgy rlipvegaq
//
LOCUS       WP_175855110             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175855110
VERSION     WP_175855110.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33605
     Region          6..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mlrtglgelt tfitiaeqrs fsgaarilgv spsalshair hlearlgvrl fnrttrsval
       61 teageqlllr vrpavadled amndaatarn rpsgqirvsa sesaarplir hvlpgfvary
      121 pdihvefivd srlidivehs fdagirvred vprdmiavry gdavrfvava spdyltrhpa
      181 patpqdlthh rcirfrfesg alyrwdltrd gkrvsidvdg pmtlgnlslm vdaalagigi
      241 awvtqsrvae hlaagrlvrv lpeweqafds lclyypanrh pptalrlfve avrewaagad
      301 dalhd
//
LOCUS       WP_175855112             392 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia cepacia].
ACCESSION   WP_175855112
VERSION     WP_175855112.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..392
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44494
     Region          7..390
                     /region_name="COG3146"
                     /note="Predicted N-acyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:442380"
ORIGIN      
        1 mkheridyrt gilsspaevp adewnallar daqptpflrh efldalhvar cavddtgwsp
       61 hfvtltdert grlaaaapvy akqhsygeyv fdwawadayq rndlpyypkl lcavpftpvq
      121 gtrllaaddd arrrlaatll afaeqsdvss lhvlfptgde aallesmgmm lregvqfhwi
      181 ndgyrhfddf lgtleqkkrk niraerrkvh eagvtfrrlt gdritdadwr ffsrcyrqty
      241 rehysspyln ldffrtiggt mpenlllvia eaggqpiasa lavyrrgeng ggtlygrywg
      301 avehvpclhf etayyqllef cieagldtfe ggaqgehkla rgflptvths ahwlahpafs
      361 davarflere tehihayvde lrehdpfrrg ag
//
LOCUS       WP_175855236             688 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia anthina].
ACCESSION   WP_175855236
VERSION     WP_175855236.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..688
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=74601
     Region          22..679
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 msqatvaplr prdpfsidpr kllfsistfi aaalvllisf tvsfprpwwa lltvyvtaqp
       61 magafrpkvi yrlagiatga vvtvvvapnl qnspallvlc lalwigfciy lavldrtpra
      121 flfqmaafss avicfpyldd ptnifitavs rveemtvail cvtithmllk pannrpvihe
      181 ralsflgdac rwtvdafgmq htrlehehrr klaadvtelg miattlpfdq rfalatrdtv
      241 talqhrlaal lsiasaaanr ldqlralnav daetaalvda vvedlkasqe vgealdvgla
      301 arcralaaer lldptwtsll aanlfdrtad fidtlhaarg lvrtfaesda elerhpppvd
      361 gaqrfrlsrd hglallagaa tttaiiiyca vwillawpng sataafaali tcsfaaqddp
      421 apvigrylvs tlvtfplaal ylfvilprvd gagmliltla pafiwmgyiq adpartaral
      481 pmfscfivam gfldrfqadf alflntglaq vggivttlvv tklfrsastr wtayrivrqn
      541 wadlaqmadp hrpldaptwt aravdrlgqv aarmafanqg dalhavdgls dlrigrniiq
      601 vregldkgda qtrvaieaal eavsnlyrar adahhpippt aslmrtlnra igaasrnttg
      661 rddatllalv gmrcnlfphv qlvegatr
//
LOCUS       WP_175855254             423 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia cepacia].
ACCESSION   WP_175855254
VERSION     WP_175855254.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..423
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=43958
     Region          207..415
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(214,254,292,395,398)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(214,395,398)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(214,254,292)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 msfrssiaaa vlgaaafvsp lvasasaapa gwvaawatal qpipdlaapp plyrapdvag
       61 rtvrqivypt vsgraarirv snaygrsplv veaaslarag egaalsgdaa vpvrfggkvs
      121 vtlapgqele sdpvgidvra gqpyaislqm gpnqrmtvwh rvsnqfnyvs vpgehvsdpg
      181 aaafrtrftq fawvtelave tgsarasvaa igdsitdglr ssvnrnrrwp dalarrlaas
      241 gaesigvanl gisgnrllsd sacygtslas rferdalsra gvkaaivlig indinfaamp
      301 pragldcdhp htqvtaasli dgyrrlidaa hrqgvkvfga tltpaglpag realrlevnr
      361 wirsgggfdg vvdfdavlrd parpsvlqrr fdsgdgihps dagytamada vpieqlqtav
      421 ggk
//
LOCUS       WP_175855265             130 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia anthina].
ACCESSION   WP_175855265
VERSION     WP_175855265.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..130
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=12988
     Region          62..125
                     /region_name="BON"
                     /note="BON domain; pfam04972"
                     /db_xref="CDD:428229"
ORIGIN      
        1 mkhrfaivva gfvalsplvg haqsattaas aaaattpaaa assaspraak kadraadraf
       61 akrvrqaivk apgignaqvs vfakaktgdv tlaglitdes qdrvavdaar qvagvtsvks
      121 rlqlrleggq
//
LOCUS       WP_175855319             537 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175855319
VERSION     WP_175855319.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..537
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53835
     Region          23..437
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,279,282..283,286..288,291,319,323,375..376,
                     380,384,400,403..404,407..408,411)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mdqpfsaast qsvrrrawvl aavcmaaval plsfsggava tpaigrdlhg gtvamnwitn
       61 afmlafgscl maagaladqf grkrvfaigv ggftlmsval afapsmlavd llraaqglaa
      121 aaalaggtaa laqefdgaar trafsllgtt fgiglafgpv lagalighgg wrtifvtsav
      181 agglslgfgl prmhesrdph atgldwpgta aftaaltlft fgvieaparg wsnalviall
      241 agaalgacaf vaietrvarp mldlslfria rfvgvqvlpv stcccyivll vvlplrfigi
      301 dgfseidagw lmlaisapml vvplvaatlt rwlsagvisg lglliaaagl vwldvalrgg
      361 agpaaiapml aigvgagmpw glmdglsvsv vpkeragmat gifsttrvag egialaivga
      421 vlaalaqtgl rqaagaagtp eatlraaarl atgdlagaaa alpgvgqaal lasyahafdr
      481 lliglavvtv lcavvvfvfl ggrrvaaeag dgtdghahad vpvrsridaa ctethgr
//
LOCUS       WP_175855325             476 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175855325
VERSION     WP_175855325.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..476
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49594
     Region          21..476
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mqnrntpaag aepagaplsg daleavlvae lgdalvtraa didpryftay nepagarpra
       61 lvrprsvddv srtlalcarl gqtvvpqggl tglargaval ggevvlsmer fagvealdaa
      121 agtmtvragt plqtvqeaae aagftfgvdl gargscqigg mlatnaggtr airygmmreq
      181 vlgleavlad gtvvssmnrm lknnagydlk qlfigsegtl gvvtravlrl hpllaapata
      241 lcrvrdydav ialwnrvrtl pevvsfeamw pafydyvarr tpgvsapfvg ddgfavliec
      301 atsaprgdah qaletglaag ieaglvedav latserqard lwtlreglai dalphlvnfd
      361 vslptgelgv faerceaalr mqwpdavclf fghvgdgnvh igvslagmsd adadaldhcv
      421 yavvrdmggs vsaehgigvl krpylahtrs daeiglmrcl kaaldpggil npgkvl
//
LOCUS       WP_175855327             222 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175855327
VERSION     WP_175855327.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..222
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23589
     Region          29..187
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpprhvqvpa ppgqpaaqpa palrrrprqs raqassdalq qafvqlller gyakatirei
       61 aavagvsigt fyeyfgdkqs laalcihrhv laladrlrda varlrgapra elaaalvdlq
      121 vdaigadaal wgalfalerq vsplaayrrh ydayvalwrd alahaadppp aarldgiarm
      181 ahtlcyggls qalltlgpaf diaalrgelr avllaylaaa gr
//
LOCUS       WP_175855409             344 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia cepacia].
ACCESSION   WP_175855409
VERSION     WP_175855409.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..344
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37462
     Region          180..323
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mlaevrpdgf tmldtyrlaf adglfavrdg aeirvahgdg igaqllraql gddgalrlva
       61 ynhraspadq rrallaalaa afsdsarhas irldpaawpa valdalrasg vladagrcmr
      121 egwaqqadlw lvgphlpcat lpvftdgrrh prrppaprge vyardlpalg vrftlrgwqp
      181 aedaqrvarw fdeprvrdgw pgaqpgvdgg qgaapdadph viplvgcfdg epfayfeafw
      241 lkedalaphv aardydrglr mlvgesrwrg phcvagwlps vvhylflddp rteavgcavp
      301 agharvadhl aghgfarqrr laladaqplw mrtlretffs grhv
//
LOCUS       WP_175855416             550 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175855416
VERSION     WP_175855416.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..550
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=59727
     Region          27..550
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mrtpvfesng dvsadvvivg sgvvggliad qlvsqghsvl iiesglrier aqavenwrnm
       61 pfdnrvgsdf qglypqapna paplyfpknd yvglsgrdgq sfqqgylrtv ggttwhwaas
      121 swrhlpvdfr mkstygvgrd wpisydelep yycraeeqmg vagpsdpamq spsqrsrpyp
      181 mdmvpwghgd rrfaevvnah gyqsipipqa rstrpwhgrp vccgnnncqp icpigamyng
      241 ihhieraerk gakvlaesvv ykidtdannr vtavhwydts hkshkasgkm fvlacngiet
      301 prllllaane rnphgiangs dqvgrnmmdh sgfhctflan epmwlgrgpa qsscivgprd
      361 gdfrgqysan kmilnnisrv gpatqqalkl glvgkaldee irrraiygvd lsisleplpd
      421 pnnrltlskt rvdplglacp dihydvgdyv rrgydaackq lthigslfda vefnittsln
      481 annhimggti mgadpkssvv dgdcrahdha nlwlpgggam psasvvnttl smaalglkaa
      541 dsisaslakg
//
LOCUS       WP_175855418             430 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175855418
VERSION     WP_175855418.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..430
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=47064
     Region          4..412
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mttptriviv gggiaglqla trlgerlgrs graqvtvvdr spthvwkpml htiaagtrdv
       61 qqqqviflah ardhgytyqp geltgldrar rrvqlgeirs qdgervidar eieydvlila
      121 lgsqandfgv pgvrehcyfi dsqqqaetfn ealrmrvfrs iardepfrva ivgagatgve
      181 laaelsrlle vaqaygdatv rerlqltlle sgprilaafp pkisasaqrr leqigfhvlt
      241 strvtaadan gfhygdgsfa eadlmvwaag vkapdfmqal ggldtnranq vlvqptlqat
      301 adphvfaigd caslqldgqe rplpptaqva tqqaehlakh lpawldgkpm ppfafhdfga
      361 lvsisdydaf gtlgqfgffr ggfiqgrfaq fshlmlyrrh qqalhgfska tllwiaerin
      421 gcvqprirls
//
LOCUS       WP_175855469             328 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia cepacia].
ACCESSION   WP_175855469
VERSION     WP_175855469.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..328
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34266
     Region          7..324
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mndndhrpvr fgiigagsia rrfaqslahv pgatlagawa rradataafc gahggspaas
       61 leallasdid avyiatlhds haqytlaala agkavlcekp atlnaaqldt vlqaardagq
      121 lfmeamkppf splyrqlrah lqddpigeir lvragcasss vpgdhsvyrl draggalldi
      181 giyeaflavd wlgaaldvqt lgrvgatgvd lfaslnsvha hggiaqlfcg ldvmgrgdal
      241 iaaagghvti hekwwnpvra tisyadgrtv eldapaeggg lnyetahfcd llragktesp
      301 imthdhsrqm iamtdaaraa lgvrysge
//
LOCUS       WP_175855440             182 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Burkholderia anthina].
ACCESSION   WP_175855440
VERSION     WP_175855440.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..182
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20864
     Region          16..170
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtdstrshlk kllesryahw lrrferlvgt rdraadllhe twlklenasv pgtvsnseay
       61 lmrmannlai dqhrrdqhyv dqadidevle mpddradper ivgarltvdl laevlqelpp
      121 rrraillaar vegqlnreia ermgislrlv elelrqaigy clermnarge ggeshtsgrr
      181 kf
//
LOCUS       WP_175855510             542 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Burkholderia anthina].
ACCESSION   WP_175855510
VERSION     WP_175855510.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..542
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57828
     Region          13..523
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 maaatptgal valhhvsfrf ddgvtlfdsl dlaidrtltg ivgrngvgks llaqliagrr
       61 tphagtierh tpvayvaqqh ddapndtrtv aeiaaldapl aalarvadgh aeapdfdlig
      121 erwdlaerlr aaldaaglpd vradtpahtl sggqlarval igallsdagl lvldeptnhl
      181 dapgrawlra aldgwrggvv ivshdralla hvqriveltp hgvrayggny alyraqrdaa
      241 hdaaqaaleh artergrvrr rleqehdtiq rhaasslrda ktanlssgar qsrkgaargi
      301 mgtvrrhqnd fkatldarvq eaaarveaea pvlvslpgte vsarrqlftl draqlpwcad
      361 aitwsasgpv rialtgpngc gkstllrmla gelaprsgtc tthvsaayld qrlalldper
      421 siveqlgrld splaegdlrs rlallqldaa ratqpvqrls ggerlkaala calwrgtpaq
      481 lllldeptnh ldlesvraie aalagfpgai vavshdaafl aalepthtmq wqcdgwryep
      541 va
//
LOCUS       WP_175855549             208 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent F420 reductase [Burkholderia cepacia].
ACCESSION   WP_175855549
VERSION     WP_175855549.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..208
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21350
     Region          18..196
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mkiaflgggn fggnlaellv aaghdvvvgl rnpararpga ryriasleea athgdvviia
       61 vlyqacaevl pslahrlagk ivvdatnslk ddwsplplga dgsaaeaigh llpgarlvkc
      121 fntvfadimt pdridrggha vtafiagndv qanttvaeia esagfapvvt gplnnaryle
      181 amahlniqia igrgggtnag fvyhrala
//
LOCUS       WP_175855559             205 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cepacia].
ACCESSION   WP_175855559
VERSION     WP_175855559.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..205
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21622
     Region          1..202
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtelivvvti tllavispgp dfamvtrnsl mlsrrsgvlt algiglgvtv hvsytllgvg
       61 llirqslwlf navkligaiy lvylgvkmlm akagngqada paaplsdlaa lrtgfltnal
      121 npkttvfivs lfmqavrpdt plivqigyga fialahagwf slvavcfsat avrdrllslr
      181 hwidrtfgcl lvgfgvalai arggr
//
LOCUS       WP_175855568             475 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175855568
VERSION     WP_175855568.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..475
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50873
     Region          40..459
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(50..51,54..55,58,90,140..141,143..145,148,171,
                     174..175,178,287,290..291,294..296,299,328,332,383,389,
                     393,397,413,416..417,420..421,424)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mssidlnavt passpirsas dvarlintvd ssvsharmiv llalggvfld aydlttlsyg
       61 iddvarefgl tpaltglvgs aimigtifgs liggwltdri gryqvfmadm lffvvaaiaa
      121 glapnvwvli aarfvmglgv gidlpvamaf laefskfngr gnkasrlaaw cpmwyvassa
      181 cfllifglyf llpaehagwl wraslifgav palviilfrn rfmnesplwa anqgdlanaa
      241 rilresygih aheaedarrv psqppvrirv lfqrpylgrt ivasvmnlci pfeytaiaff
      301 lpsilsqflg agvfetiaas lalnvlfaft ggllgmrlah rhasrhvaia gfalqfvalv
      361 alalaghphg alaigfvllm lgtwlfaedf gpgaqmmiyp tlsypasirg tgvgfgrslc
      421 gigqalalfv lpilqarlgt dmfwvvaisa atpivflliv ryeptardid ddgae
//
LOCUS       WP_175855574             233 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175855574
VERSION     WP_175855574.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..233
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24347
     Region          41..224
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mkkhlepaph dvaapvepaa vagarapeas sapavatagv rrkkapdqvr aqllaaasei
       61 athhgvaalt ldavaeragv tkgalqyhfa nkqglldalf gqatgrfaaq maervaadag
      121 gagaaaraym havldesqpv astdvlrvlv asmitdqdtr erwsvpmrew trpdpvpleq
      181 aatlmicrla adglwisqll dsveisaelr aeierqldam shgafpkgrd gaa
//
LOCUS       WP_175855584             123 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175855584
VERSION     WP_175855584.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..123
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13555
     Region          12..117
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 midvssitda fapggeptqy rvspeklisg dplhtltpgf aspcgrfstg iwestpgcwh
       61 vayteaeyce ilegrsvitd legnrktlra ghrfvippgf rgtwevvert rkifvaydeq
      121 ppe
//
LOCUS       WP_175855631             482 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia cepacia].
ACCESSION   WP_175855631
VERSION     WP_175855631.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..482
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50528
     Region          25..478
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mshpaspaqa lpaqhaappa gglrrnylsl peliaqsigl vgvsggigvl ipavfatagn
       61 gtwlaylfai vallfaswsi svfardsasp galyayvsag igpvwgaicg wslliayava
      121 aagilqgtin tflvlgretg llggatplga vlgltvvtaf aawyiafrdi rlstrftlfv
      181 elatllliav vvigtiafgg hpvdraqltl egvkptqlql gmvlaffsft gfesatvlga
      241 eardpfraip ravlisvvgp ailfvigayg mvsafhgqtp pldrvdgpla vlahrlgagw
      301 vgvlidagva lsffaaffss inaaarivyt fgrqgvlhas tghahernat phvavalivv
      361 lalvtalvft argtalldsy gylssiatyg wllayvlvai gaplylrrqr rlrarhvais
      421 viavvllaip lagsvypvpe gvyawlpyvf vallaiglgw flvlrvrfpe rlremeaell
      481 tk
//
LOCUS       WP_175855735            1026 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia cepacia].
ACCESSION   WP_175855735
VERSION     WP_175855735.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1026
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=109761
     Region          14..788
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnvqnlaaal rggliqqdrl lkldtplgan vltvlravgr stigrdyaft ldvvspknai
       61 elkkliaqpv tlwlsqangr yrpihgyvyt vrqlgaeggl ttyqitlqaw mhvlkfrrdq
      121 kiwidktadd ivsdvlnqhp eargrfrftl sqplpnrsyt rqsetdwhfv hrlleseglf
      181 gyweqaddgq shtlvitdrl aacpalsptt vsfyhggtra eadaltqwag trtlqsvtht
      241 trtfdyknps qpsnpkgttv ptmagqgelp dqlevyeytg aytfqqqqhg drlshirmee
      301 wesrakrfhg agsvraidag rrfvlsghsv hdhdpadqre fatisvtwwi ennlpatrmq
      361 nyphslhrdi dkvrstragd lsltpphddg stgfylveve aqrvsvpyrs pfehhkpemh
      421 letaivvgpq geevytdsln rirvqfvwdr mnpgdenasc wvrvvqsdtg ggyggvhvpr
      481 igeevlidyv ggdcdrplav grvynganqp qwhtdgilsg yrskeysgsg ynqlvmddat
      541 gqnrvqlmss sansllhlgy iidqngnsrg sylgsgfdlr sdaygsvras qglyvtthpk
      601 aansqpldvk eaqqqlvtge slveamsgvs eqhqaeslkd aqdtmraftd atqesasgsa
      661 sggrtagggt gnanafkepv mlfgspsgig mstqqsvhmv andhvnvasg qsvhvaagks
      721 ligsigqkls lfvqnagmkl fagkgkveiq aqsdnievta qkavkvvsat gqveiaadqg
      781 illtsggayi rikdgnveih apgkidikga shtfagpasm gyplpsprpd qpgqlellhr
      841 yadgqpvkgg tfsvfdasgg llrngaldnn ghmivsglpa gaaqvkfghd prdqgqdasl
      901 fpverwpaqp qqnsaadaai aanqlggllp aaasaagaga stnaaglant agtlagfagq
      961 vmqgaptlas tiagqasgia qqaigkqlpa aaqaalsqas qltatarqlg nlaqtarnaa
     1021 palkrs
//
LOCUS       WP_175855743             873 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: S8 family peptidase [Burkholderia].
ACCESSION   WP_175855743
VERSION     WP_175855743.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 873)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 873)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10141191
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..873
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..873
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=97713
     Region          314..664
                     /region_name="Peptidases_S8_Subtilisin_like_2"
                     /note="Peptidase S8 family domain in Subtilisin-like
                     proteins; cd04847"
                     /db_xref="CDD:173793"
     Site            order(320,353,411,435,470,618)
                     /site_type="active"
                     /db_xref="CDD:173793"
     Site            order(320,353,618)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173793"
ORIGIN      
        1 maeplpllvf pekrvvppep rrgfpiggph lpgrqrqvar vnvqldelqa sfaryqasva
       61 gamagmepet vlvmeiagsv ddfkqavdaa glewlgewdl dgvqpdddfy evdsrgqrtd
      121 kllkgrlfls msneaglrel lslwaqwtqg ralprgkgkw gdvfsqllvi rrwgieetlr
      181 etgmihrwhe mvdpldaqqp itfqielfyr hteirrrqne ravrellaal dgrtlgpfid
      241 mneiafhavk aelpaerirq llgevgnpaa evdiqlfkfp gimyfrptgq slaiadeneg
      301 dpaefkeava elppvvalld gaplllhkal egkllfddpf dierlyqpge rrhgtsmasl
      361 ivngdlssgq seplrrkvyc tpimqpdpnh sdrgehmpdd vffedrihla vrrmfegagd
      421 vpaqaplvkv vnlsigdser pfihtpspwa rlldwlswky rvlfcvsagn fpddfdigvs
      481 ygefselsde dkvrttirav sqslssrrll spaeslnait vgalhtddsg eypemrridv
      541 mpnesvfspa mrlghgfrra ikpevlfpgg rqlyqtpnln gssvfridrs kvrpgqtvaw
      601 dsskpgelan vivtrgtsna talatrsaar iyemleqlre qegeavpepl iavlikalli
      661 hgakqsesak dlltsalkne rnsrqfreii aryigygaad iervltctaq ratvlgcgei
      721 renevheyaf plpiglsaqk lwrrlvvtla wftpinsdhr nlreaklela pggspwdets
      781 lrlsrqdgdr nqvlrgtvqh evlegeriis ayqdgeairi rvtckkdatv hlddvipygl
      841 avtlevkedi dipiyqqvrd rlkpqvvvga grr
//
LOCUS       WP_175855744             460 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia anthina].
ACCESSION   WP_175855744
VERSION     WP_175855744.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..460
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49585
     Region          3..451
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mkqpedqlhr gleerhinlm algatigvgl flgsatairt agpailltyl lggiviflim
       61 ralgemaitn pvagafsrya rdylgplagy ltgwtywfvw ivtcmaeita vgvymhmwvp
      121 gvpnwiwala altamgavnf iavklygefe fwfalikivt ivlmiigggl miafgigngg
      181 vatgisnlwa hggfmphgid gvigalpivm faylgvemlg ltagearnpe ksltkavnsv
      241 fwrvlifyig alfvimslyp wdqigtqgsp fvmtfsrlgi paaagiinfv vltaalsscn
      301 sglfstarml ynlaqqgqap aklgrvnrng vpvygvlvsv allligvlln ylapqhvfvw
      361 ltsvstfgai wtwcviliaq mrfrrtlsad kiarlpirvp fyplgsfial aflalvivlm
      421 afspdtrval vigpvwivll giayavfyan rpatpvstks
//
LOCUS       WP_175855745             333 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AAA family ATPase [Burkholderia].
ACCESSION   WP_175855745
VERSION     WP_175855745.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 333)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..333
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36967
     Region          88..332
                     /region_name="COG1223"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440836"
ORIGIN      
        1 maqadtlvel vkaassgdqp sfrkaaesli keerdkghri ladrlakslq qaalfqsaap
       61 aqgprngggv gggahkelif eiaperslds ivlaenvrdq lkelieeqhr aellhahnlr
      121 prhkvllagp pgngkttlae alafelmvpl ivvryetlig sylgetssrl kslldyartq
      181 rcvlffdefe tlgkergdth etgeikrvvs slllqmdelp dyvvvvaasn hpelldravw
      241 rrfqlrielp mptraqltaf vasigvrcqv nfgfaaetia krllglnfae veefclsvvr
      301 ravldrstdd akmitqtkld qwrerlkpsq qea
//
LOCUS       WP_175855771             727 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia anthina].
ACCESSION   WP_175855771
VERSION     WP_175855771.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..727
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79480
     Region          39..722
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mkpqpaierp sieparwrrw ldplgdaard waasdgliwl hlaktvlaal lamgiamrle
       61 msqprtamtt vfvlmqplsg mvfaksfyrv lgtaaglvaa lalgglfaqq pelymagitl
      121 wigacialav rnrhfrwygf vlagytaali glpavmtpqt lfesaltrag evalgiacsg
      181 avsalilpls saktlmrtlt arhvkfpafa agalsgelar gdferrfadf vdeivgfean
      241 rafasfedph irarsrrlar lnsefmnact rlhalhqlik rlranrsdav ldalaphlda
      301 lahriaalrd erqrgiastt gallelrrfh dalpkaarat rreleahaag gvldfdtaie
      361 lmyrfigeyl gyadtyasld qdnhalersv thyavktnaf fvgfaflrtl vavgamsafw
      421 lasewpsgsl aviataiaca lsstsprapk fvaqmgvgaa fatavgyvfl cyvypnidgf
      481 pllcavlapv lglgaflamr pglsgygigf avffcllagp dnavaytpev linnglavvv
      541 amlacsivfa vvfptrmpwl tgriahdlrr qvtlacegvr dglaprfqss thdlmaqlrt
      601 llvqrtrqhr dalrwmlatl evghavidlr delhafceak ppqtlhwtas idavlhelpr
      661 ffddptpghh artlksvnla ihaaqhtlha wyavpearhr mqrivgclhf irsalldkda
      721 pfnhhrh
//
LOCUS       WP_175855915             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175855915
VERSION     WP_175855915.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33340
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..290
                     /region_name="PBP2_CrgA_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08475"
                     /db_xref="CDD:176164"
     Site            order(103,107,146,161,163,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176164"
     Site            order(104..105,109..110,112..113,116,120,122..128,190,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176164"
ORIGIN      
        1 mrnnlngiav fvaaaeadnf aqaadalhit rsavgksiar leerlgvvlf qrttrtqslt
       61 degalfyehc lraveeihag ealletgkwq mkgrlrvsmp alfghlcvap ilielarahp
      121 eldldlsfsd rtidlveerv dlavrvgalp dssglvaral gehkmafcas paylercgep
      181 vtvdalvqhk alaytrhghv hrwqvvvdgr teelqpqarl lsddlravld aavaglgvaw
      241 lpywlvrdam rrgtlrellp dqpgvsyaih avwpytshlp lkvraavdal vsqlparlaa
      301 veara
//
LOCUS       WP_175855802             700 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia cepacia].
ACCESSION   WP_175855802
VERSION     WP_175855802.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..700
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73379
     Region          38..634
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mhdaadqtra vaapprrltr aaaaliarid iftprgayva rsviaaalal gvayllelet
       61 pysaastvll vinpvqgavi gkgvwrvvgt iagmvvafvl mgcfaqqpll filgfafwlg
      121 vcvagmtllr hfrasgtvva gytiglatyg amqhpeltfe hvigrgstva igvlclslvs
      181 mllgtrdvha kldalvtrvt advarviaaq rnglaaapad dkrhalfagi ygiddllalg
      241 kaesedlaqr aaavrhgmas lfgalaggmp plpadspgar svaslqprla aawqaaadal
      301 gdgpggatha rallgdarer lrdaldgial gdprddaall iagerlieqi ddyraaldgl
      361 velqrprpgy rparvrfhrd tgaalrngvr aacaivisga fwlatgwnqg dmmllvvapy
      421 callatagnp aagaqafikg tvlavpaafv cafgilprie gfpllvvala lfwmpgiyat
      481 svpktalagl aylvafntlt gatnpfrpdi alflnqsvaw vlatfltllt frlilpgnla
      541 tdatrlrrti rddtlalvag rrvtaagwqq rqqhriaqlg allagqpaam tqasiealaa
      601 lhvgkellri rrgaardglp dparrcvrag laglarhaaa ppraarharr aahalaglaa
      661 aqpgntelkw lmaafadvyv llhtyaayft avperardaq
//
LOCUS       WP_175855962             499 aa            linear   BCT 11-JAN-2025
DEFINITION  HDOD domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175855962
VERSION     WP_175855962.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..499
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=54934
     Region          18..221
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 msitehlprt alldklwarm nergdfplls eslratmaam knddldftal vrvvlsdfal
       61 tqkvlrlans amymafggni ttvtralmvl gmdavghlvv glklvdhfhh stprridakl
      121 elnrallsgc varklterve lrageeavvc tlmrqvgkll vvcyldsewd rirrraaeln
      181 gdeaaacidv lgvgfdeigl eaaarwrlpd viragmadhd hvvrtdafgn deddldagev
      241 sddgptervr wlreisrcst dvagalvmpa spqrdariaa laqhygaelg mepdalveia
      301 erlareeasd tmmreivelr anadaiaraq aepeacleag ladlralpse hvltpvlala
      361 sesllaglaf trtvmfvrhd dgmfaarlgf gpgvdtmldr lrfderfepd vfhlaisnsv
      421 gifieqarep kmlkrlpawy ldafddthaf vllpvrvgtt tvallygdwa gaqparkitq
      481 qemgvlnela relgrffpa
//
LOCUS       WP_175855983             343 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175855983
VERSION     WP_175855983.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..343
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36660
     Region          4..343
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkldstsitl trcaktfrgt rvlepldlsi gagetlvllg psgcgktttl rliagldtpd
       61 aggtiafghd dvtalpierr qvgmvfqnya lfpnltvrgn vgyglkirkt epralrarvd
      121 ellammrlda hadkpvdqls ggqrqrvala ralavrprvl lldepltald aklrdvlrre
      181 mnallrelgv ttvyvthdqa eamelgdriv vmgagrieqi gtprdiyyhp anrtvaqfig
      241 tlnrlagqwr dgtlvttgga vatphaadew ffrpedaqla dpahaplrga vgacaflger
      301 trltiehaap dalvidvpgr ialargtavg laiapeglia lga
//
LOCUS       WP_175856013             146 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Burkholderia cepacia].
ACCESSION   WP_175856013
VERSION     WP_175856013.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..146
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=15635
     Region          44..146
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 msgihfgsdl fdefarvqrq vaslladrps giravrpgaf palnvgatdg aieivafapg
       61 maaadfdvsi dkdlltisge rkpapggegd dlrtyaqerf hgafrrvvel prdadpdqvs
      121 aryengclli rvgrreaskp raitvq
//
LOCUS       WP_175856173             224 aa            linear   BCT 11-JAN-2025
DEFINITION  lytic transglycosylase domain-containing protein [Burkholderia
            cepacia].
ACCESSION   WP_175856173
VERSION     WP_175856173.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..224
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - lytic transglycosylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=23647
     Region          2..187
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 mrrrffwliv lslgiaqqvs aqqtpavpas apdvlasapa vasaplanan dqpneanrri
       61 tsyltkkfgv akeraaklad ivsvtatkys lppalvyaii siesrfqeka rgqhgatglm
      121 qvvpsahrgm lrnvkdltep nanveagsri lssyvkaagg nvqaglksys ggssayaakv
      181 mqrvdsfrfv lepdddakaa netkarmvpv sestststsa rnaq
//
LOCUS       WP_175856153             441 aa            linear   BCT 11-JAN-2025
DEFINITION  leucine-rich repeat-containing protein kinase family protein
            [Burkholderia anthina].
ACCESSION   WP_175856153
VERSION     WP_175856153.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Shen,K., Hines,A.C., Schwarzer,D., Pickin,K.A. and Cole,P.A.
  TITLE     Protein kinase structure and function analysis with chemical tools
  JOURNAL   Biochim Biophys Acta 1754 (1-2), 65-78 (2005)
   PUBMED   16213197
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
REFERENCE   7  (residues 1 to 441)
  AUTHORS   Hanks,S.K. and Hunter,T.
  TITLE     Protein kinases 6. The eukaryotic protein kinase superfamily:
            kinase (catalytic) domain structure and classification
  JOURNAL   FASEB J 9 (8), 576-596 (1995)
   PUBMED   7768349
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..441
                     /product="leucine-rich repeat-containing protein kinase
                     family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=47074
     Region          <2..>186
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          39..61
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          62..84
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          85..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..175
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          214..430
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(214..217,220,222,238,240,269,287..290,345,349..350,
                     352,362..363)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
ORIGIN      
        1 mtttleqlqa gqlagarqlk lacgltefpr eifdladtle vldlsgnals slpddlsrlh
       61 rlrilfassn rftvfpevlg tcaqldmigf kanrirtvpr hslpralrwl iltdnaidal
      121 paeigdcarl qklmlagnrl rvlpaemaac ralelvrlsa nrldtlpdwl lrlprlawla
      181 aagnplgaap eaaasaepgv adidwaslsc dqklgegasg viyraqwhad gqtpravavk
      241 lfkgavtsdg lpdcemaacl hagrhpnmip vigkvrdhpd gthglvmerv dpaltnlagp
      301 psfatctrdv yaddarftpa aavriahgia svaahlharg imhgdlyahn ilhdgeggal
      361 lgdfgaasvy dvndrahaar lerlevrafg yllgellarc epraregshe lealaaacln
      421 edvdarpsfd aiaaalaast r
//
LOCUS       WP_175856199             321 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175856199
VERSION     WP_175856199.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..321
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34514
     Region          11..224
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(52..53,55,69..71,77,79..80,121,223)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(52,54..55)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(77,80,83,90)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(113,117..120,122)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(118..119,142..144,196..197)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          237..321
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 msaatltvrv arkwqeardi cgfefvsddg splpgfeaga hidvhlpggl vrqyslcnhp
       61 ehadryqiav lrdadgrggs raihdevrqg dtlrigmprn qfplapdaph hlllaggigv
      121 tpilsmaerl fssgtpfdmh ycarstdrma fverinaagf rdrarlhvdd gapeqrfdla
      181 avlaaapagt hlyvcgprgf mdavlnaare rnwaearlhy effggavass gadrafqvri
      241 assgrvidvp aectviaala angvdvltsc eqgvcgtcat rvlegepdhr dsylteaeqa
      301 agdqfmpccs rsrsdllvld l
//
LOCUS       WP_175856234             475 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175856234
VERSION     WP_175856234.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..475
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51284
     Region          42..460
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(52..53,56..57,60,100,150..151,153..155,158,178,
                     181..182,185,296,299..300,303..305,308,335,339,388..389,
                     393,397,413,416..417,420..421,424)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mastqpdslt aagvahtaai dpgsisarld rlpptrtvwk lvillslgff felydllysg
       61 yvapglvksg ilsatthglf gttgvasfia alfsglfigt iacgfladrf grraiftwsl
      121 lwytaanvvm afqdtaagln fwrfvvglgl gvemvtigty iselvpkqir grafaceqav
      181 gfvavpvvaf layllvphap fgldgwrwvv ligahgalfv wwirrelpes prwlaqqgrv
      241 deadrimral eakveaeygr plpppapaep vpprgsfrdm wvqpyrnrti mmtifnvfqt
      301 vgfygfanwv ptllikqgit itsslmyssv ialaapvgpl iglviadrfe rksvivamaa
      361 aivvcgllfs qttvgafliv lgigltlasn imsysfhayq aelfptsira ravgfvysws
      421 rfsaifssfv iaavlkgfgt fgvfafiaga mvivmaaigf mgprtkgial eaisk
//
LOCUS       WP_175856235             215 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia anthina].
ACCESSION   WP_175856235
VERSION     WP_175856235.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..215
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22405
     Region          6..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mhtsgslygf lviggmlavt pgpnmvyvms rsiaqgrtag lislagvmmg ylfymfgaaf
       61 gittlflsvp yagtvlgvig aayllylawq avrpggrspf evktlpseqp lrllamgatt
      121 svlnpklaml fvsllpqfid yrqgsvfgqs lflgslliaa fasangmvai cssgiakflh
      181 grpalllaqr wamgivlggl gvemlvdasr mvgaa
//
LOCUS       WP_175856273             713 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia anthina].
ACCESSION   WP_175856273
VERSION     WP_175856273.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..713
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77598
     Region          9..701
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mtypslrdwl fsgktfaasm lalylglyfq lprpywamas vyivsnpfvg atrskalyra
       61 lgtalgaaaa ilfvppfvet pllfslivat wcgtllylai sdrtarsyvf mlagytmplv
      121 alptvtdpst ifdvaiarte eivlgivcas vvgsavfpnr laptliertd awfrdaafyg
      181 retlsghlag kalsacrqrl aatitglefl lsqlsydhah prvlaraqal agrmqlflpl
      241 mssladplia lmrdlhvrpa aldalladaa kwfdaplpai tagtdgeman dpvadnlrar
      301 itslqppdta ltswdgalls nalwrlrqvi diwqdcrslr alianesgvw qpryrhwrlg
      361 gterffdrgm mlfstltvvg aivfacwlwi qsgwhdgaga vtlvavacsf faaldepapl
      421 vfkfflataa svvfaglylf vvlphvhdfp mlvlmfagpf iligtllprp qfnmvtmlva
      481 vntatfisiq sayeadffvf lnsnlagvag llfayvwtra trpfgaelav rrllrsgwed
      541 varsastqpl ddqrnhasrm ldrvtqllpr lgasddhrhp siesfrdlri alnaldlrrt
      601 rrklsgdvpd aidrvlagvt dhytrcaaan arqpappall asiddalqrv agrnlpgaaa
      661 pddgttplpa aptspavhrw lrdtlhalvg lrlslypaas aqpphaapdg ara
//
LOCUS       WP_175856369             441 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175856369
VERSION     WP_175856369.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48536
     Region          30..433
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(43..44,47..48,51,83,133..134,136..138,141,161,
                     164..165,168,265,268..269,272..274,277,305,309,360..361,
                     365,369,385,388..389,392..393,396)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtafdaaasr tpaapaqaae ldrtykkvfw rivpflmlcy vvayldrvnv gfaklqmsqd
       61 lafsetvfgl gagifflgyf lfelpsnmlm hrigariwia rimitwglls avfafvktpt
      121 qfyvlrfllg laeagfypgv ilyltywfps hrrakiiavf msaipvsgif gnplsgwime
      181 rfhggsgfhg wqwmfmieav pavlvgiati lyldnnirsa kwlderekql leseiaaqpq
      241 eqekhghslk avfadprmww msliyfafvt gqygltfwmp tlvkstgitd tfqigllsai
      301 pflvaifvmn lfghsadkrr errwhlivpa lmgavgfava asyshntavs ivflslaagg
      361 vltcaplfws lptaflagsa aaagiaiins vgnlagfasp yvigylkdat hstssgmyml
      421 aamlvigaia vwltpaklvn r
//
LOCUS       WP_175856432             897 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia anthina].
ACCESSION   WP_175856432
VERSION     WP_175856432.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 897)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 897)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 897)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 897)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..897
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..897
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=95232
     Region          36..862
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mranhhiqpl eaparfalkp gyllvmatlg gwaasacave asaaradsfq vaqvqfndtl
       61 mmkprgqqld lerfakgnpv pageylvdly vnqtwtgrst vrfdaaagav satpcfdrtl
      121 vsrlglddqa ltdaaraelv rvqsgectdi dklvadatve fdmselrlnv sipqasllhn
      181 prgyvspelw dggvpsatlk ynanvfrnts sgyqstqgyl glnaganvgn whfrhngtys
      241 aqtqgdsryq slntyvqrdl pawrsqlkig etytdgtlfd svgmrgvtle tddrmlpdsm
      301 rgyapvvrgv atsnahvavs qngavlyetn vapgpfeind lyatgyggnl lvtvteadgr
      361 khsftvpyaa vvqslrpgis rfgialgqlr esqldrhpnf aqatyqrgis nlmtgyvgai
      421 vaenylaglv gaafntplga lavdvthasa hipgvsatsg qsvrvsysks vdatgtniav
      481 aayryssrgy wsmrdamvar emsaagadpn dvyrqrnqvq ltlnqslgen hgslfavgst
      541 vnywnrqgtt tqfqlgynns lrllgvnlsy nlsvsrqrdg ysgrlnnqvy anltvplgrr
      601 shaptlstgi ahdsqggttg qmsltgttgq snqfsygvna ntgggsttgg gnaqyrspfa
      661 tfsgsasggs gfssvsagis galvghsggi tlandlgetv alveakdavg aaitngtdvr
      721 idrrgyavlp yltpykmnti eldpkgipvd vemlttsqqv apransvvkv kfetvtgrav
      781 lmtirqpdgt pipfgsnvvd adgktvglag qggklfvrgl sdtgtltakw gnrktefcsf
      841 syqlpvkqnk seaytqvesi cegaaqtnna patderdnnr nsvntvgats haddash
//
LOCUS       WP_175856524             127 aa            linear   BCT 11-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Burkholderia anthina].
ACCESSION   WP_175856524
VERSION     WP_175856524.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629346
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..127
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=13764
     Region          12..118
                     /region_name="DUF4440"
                     /note="Domain of unknown function (DUF4440); pfam14534"
                     /db_xref="CDD:434023"
ORIGIN      
        1 mdavrdavra viepyeaalr aamltndvev ldtlldddli ftvpsgaiis knddlsahra
       61 kllrldaldt qetradaige liltttraml agrfdgtafs gtfaytrlwr rsgsswrvva
      121 ghasqie
//
LOCUS       WP_175856552             236 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia anthina].
ACCESSION   WP_175856552
VERSION     WP_175856552.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Upton,C. and Buckley,J.T.
  TITLE     A new family of lipolytic enzymes?
  JOURNAL   Trends Biochem Sci 20 (5), 178-179 (1995)
   PUBMED   7610479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..236
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=24767
     Region          43..231
                     /region_name="FeeA_FeeB_like"
                     /note="SGNH_hydrolase subfamily, FeeA, FeeB and similar
                     esterases/lipases. FeeA and FeeB are part of a
                     biosynthetic gene cluster and may participate in the
                     biosynthesis of long-chain N-acyltyrosines by providing
                     saturated and unsaturated fatty acids, which it...;
                     cd01836"
                     /db_xref="CDD:238874"
     Site            order(53,90,118,209,212)
                     /site_type="active"
                     /db_xref="CDD:238874"
     Site            order(53,209,212)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238874"
     Site            order(53,74,118)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238874"
ORIGIN      
        1 mgyplataal gpllflqgrh vrrvtprlpe aagprdgvag dgpplrvlvv gdsaaagvgv
       61 atqhdalsgq lartlaathr vgwkllartg lttqelvdwl atepaepfdv avtslgvndv
      121 tggvpparwq aqqaelvrll aarfrvghvi lsavppmerf palpqplawy lglrakrlna
      181 alaawaatrp hctflrvalp lerhlmaadg fhpgeaacsa waaqvasavl rqraga
//
LOCUS       WP_175856568             293 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175856568
VERSION     WP_175856568.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..293
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30128
     Region          10..289
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mststtqqnr tpvavlgigv mgtpiarnla rqgfdvrawn rtrakadala tdgiaafdtp
       61 agavdgahvv vtvlndadsv lqamqaaapa largtpwvqi stvgvrgias laafaqahgl
      121 vfydapvqgs rqpaeqaqlv vlasgpasar arvqpvfdai grrtvwvadd gstgassrlk
      181 lalnhyafal thavaeslkl agslgadprh vidvvsggpm dnayfqakga lilnddfraa
      241 ftivnavkda tliaqaarda gmqadiahas larfqraada ghgdkdmaas fla
//
LOCUS       WP_175856584             343 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175856584
VERSION     WP_175856584.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..343
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=37679
     Region          33..92
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          123..323
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(138..139,141..142,145,149,151..157,249..254,
                     260..261,263..264)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mtqaatgrpp arsdapspda dapdglrvqd ldlnllktfr avyeerhvgr aalrlgvtqp
       61 svsyalgrlr lmfrdalfvr tgtgveptpr aqrlagsvdk alailqdvld egsrfapdst
      121 qrvfrlhmsd faasaflptl laefdrrapg avietlhvde cqlnvalesg ridfalghfa
      181 dasshfqrta llhercvllm prrtaqrval pddfvldgda pdtlrlvavt shpqsmqlle
      241 rhglmprvra alpdfmvvpa llehgdyali lpetvaitfa arqpcalyei agavewpvna
      301 ywhrrfdadp ghrwlralll elfdigglap fdawlaphpp aca
//
LOCUS       WP_175856588             445 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175856588
VERSION     WP_175856588.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..445
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47204
     Region          22..426
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(35..36,39..40,43,83,141..142,144..146,149,169,
                     172..173,176,258,261..262,265..267,270,297,301,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 myptdtvqsp saarpladrq lrriviasva gnamewydff vygtaaalvf ghvffppgas
       61 plagslaafa afalgfvarp lggvvfghig drygrkaslv wtllimgmst faigllptya
      121 qvglwapaal vvlrllqgva sggewgggvl misenappaq rgyyaawsql gvgggfvlss
      181 aaflaaqalp ddmfrtwgwr lpflasivif aigiyirrhl pesrdfeqag krgahahlpv
      241 vecirrhpke illamglrva enggayifla fslvygkyvg ipngvmltgv miamivemga
      301 mlawgrlsdr igrkpvylig alslvacafp ffwlldtrat plvwlaltvg tavshgamig
      361 tlpalvgelf stevrysgva lghevasifa ggmspliata llahyhaswp vslflvalgl
      421 vtvvtlcvmr etrtvpaadp rgdaa
//
LOCUS       WP_175856618             437 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia anthina].
ACCESSION   WP_175856618
VERSION     WP_175856618.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..437
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45481
     Region          53..411
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mlkltlvvav afatattaya qpslspvpap aaagsatpig appsdtlpst sltlsdalat
       61 aarnnpalrg aradvdasag tllqagarpn pevsflqegf sraertstal inqtielggk
      121 rrarldvasy greaanasld eqgaavradv iaafygllaa qrqlqvaees aaiaarsadl
      181 agrraqagkv spveatkaqv aaagvqievt targrvdvar eqlnavmgea rgdrrvalge
      241 letvpaiapl paltaqldda plarvaraqm lranaaisle rarripdvtv sagmkrvttg
      301 gvpdnqavvg vsipiplfdt nrgalleath kaeranadld rertrlrlel tqayanfdaa
      361 aqearrlktd ilpgarlald amsrgyelgk fsfldvldaq rtlfqgqsqy vraladahaa
      421 radldrlvgt plaasaq
//
LOCUS       WP_175856629             175 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia anthina].
ACCESSION   WP_175856629
VERSION     WP_175856629.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..175
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=18514
     Region          22..164
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 msenhagtga aadaqrhfrt alsmfatgva vitaarkegv pigitvasfn svsldpplil
       61 fsvdrrslsl pdlavagsya invldetqqh vsncfakasg dkwgwradaa dddgavllpd
      121 alatfeckpy aqydggdhvi fvgrvtrhra rsegrpliff ggryrsldgv hapsa
//
LOCUS       WP_175856844             188 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175856844
VERSION     WP_175856844.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..188
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20629
     Region          1..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 metkptvreq vldhaitlmm qrgyngfsyr dlsdlvgvkt ssihyyfpsk ddlvleavaa
       61 ysdevlaamr aidpalpada klslytkmfg rtlgdgnlic lcgmlaadie tlpenvrqav
      121 qaffkanesw laalleqgak egtlqfsgep etaartlyaa fqgsvlasrl fhtrarledv
      181 eavwktrs
//
LOCUS       WP_175856681             317 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175856681
VERSION     WP_175856681.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..317
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34153
     Region          11..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..290
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mderlrgvae fvdvveagsf aaaalrlgmt rsavakivar leqrlgarll qrttrqiglt
       61 deglvyyeqc rrllaelget eaaldagrre ptgrvrisvp vlfgrqcvap vvrrlveryp
      121 rleidvsfsd rvadlvndgf diavrigala dtsalvgrkl gvqrmgisas payldrhgrp
      181 agldtlashv giaysrggqp tpwriigadg avhdhrpagr lrfddlqaia daaaagagla
      241 wlpcwlmapy vrdgrlalvm dsestsgaev fvvrpasrhv pskvrvvida fvdeiprmla
      301 sddadgervp prvvpap
//
LOCUS       WP_175856857             446 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia anthina].
ACCESSION   WP_175856857
VERSION     WP_175856857.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..446
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48116
     Region          5..436
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mstdsfgykq elqrsltlad lviygivfmi piapfaiygy vsdasggmvp layiigmvam
       61 fftalsykvl sedfpiagsa yayaqrgigd magfiagwml ildyllipal tyvvaaaals
      121 qlfpviprwv wivvflgigt mtnyvgvqat aavnkffmyt qmlvlivfav vglyalyhga
      181 gaghltfrpl fqpevfksel vfsavsvcal sflgfdaist lseevkgdsr ktvgnatiaa
      241 lllagalfvl qtwiagdlan gmkfksadta fyeiaelagg kplalltawa taltfglscs
      301 ivsqaaiarl lysmardrkm paflasvhpk yktpnaalil vaivslaial gfldhldtlt
      361 nfvnfgaltg fmilhvtvvv hyigrkrsra lfkhllspvi gfciigyvly smgaatwqlg
      421 igwfcvgavy yvvltrvlrr diglev
//
LOCUS       WP_175856962             207 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Burkholderia anthina].
ACCESSION   WP_175856962
VERSION     WP_175856962.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130209
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..207
                     /product="phosphatase PAP2 family protein"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22653
     Region          51..197
                     /region_name="PAP2_Aur1_like"
                     /note="PAP2_like proteins, Aur1_like subfamily. Yeast
                     Aur1p or Ipc1p is necessary for the addition of inositol
                     phosphate to ceramide, an essential step in yeast
                     sphingolipid synthesis, and is the target of several
                     antifungal compounds such as aureobasidin; cd03386"
                     /db_xref="CDD:239481"
     Site            order(97,105,137..139,169,175,179)
                     /site_type="active"
                     /db_xref="CDD:239481"
ORIGIN      
        1 mnslssidcr pdlrqmlaaa fgmvaglavf illergvtpr yvfatalder ipfiawswfv
       61 yvgffpfvia laayarppaf vafrdavlia faagivcfll fpeavprpdv aeignafvrq
      121 rltrmwqldl aangfpslhv avtclacrll terrravpia igvlicastl tlkqhtvadv
      181 lggvalamgs amwverrsvr grlawrk
//
LOCUS       WP_175857018             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia anthina].
ACCESSION   WP_175857018
VERSION     WP_175857018.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..359
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39172
     Region          8..355
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkhsferlrl dgvcrsftna egaqvaalsg ldldikrgef iallgpsgcg kstalnciag
       61 lqpltsggiw lddtridvlp perrgfgmvf qnyalfphms vlenvgfglk mrgvakqetr
      121 rraqqalelv qlvghegklp gqlsggqqqr vaiaraivie pplvlmdepl snldtklrie
      181 mraeirriht qleratiyvt hdqdealsma drivvmkegv vqqvaspkdv ytrphnlhva
      241 rfmgyrnvlp ftlegmagdh vnvtaagvri tgvpmagfdg kdvlvalrpd dieraaegad
      301 nafdatidtl eyggrdslir attpfgpiwa rvageftege rlrlrvapar tlvyagdaq
//
LOCUS       WP_175857196             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175857196
VERSION     WP_175857196.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32909
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdllatmriy vrvvergtms gaardldmgq pavseriekl ekflgarllm rsartltcte
       61 egrlfyersk alldaaedtv asvskientl sgtirvaapq cfgevvvpka lmqirttypr
      121 lhidlvlndn ivdpvtegvd islrvgqlgd ggfvahalgs idrvlvaapa yldrhgpiat
      181 kadlmnhpfi rvkgifaneq lplqsedgql eyariqtamt tshwrpmfdt ilagggigvv
      241 qqpacvnala rgelveilpq ytipgfalnv lvaqrplppr vrvivdllkq eipalltkre
      301 r
//
LOCUS       WP_175857272             179 aa            linear   BCT 11-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Burkholderia anthina].
ACCESSION   WP_175857272
VERSION     WP_175857272.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..179
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18939
     Region          1..167
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtpahlipsp lgdiairied daltglffvg qkyypslaia sdanadarta splarkvaee
       61 vaeyftgtre tfsvpihlrg tafqrsvwkq llaipfgelv sygditervg lpmsaaravg
      121 gavgrnpvsi mvpchrviga sgsltgyagg ierkrallsl egagfqrger hatqqslaf
//
LOCUS       WP_175857290             434 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175857290
VERSION     WP_175857290.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46645
     Region          9..417
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(22..23,26..27,30,69,127..128,130..132,135,155,
                     158..159,162,245,248..249,252..254,257,285,289,344..345,
                     349,353,369,372..373,376..377,380)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 maidsrvvrr vaaasvigat vewydfflyg vvagivfdkq yfptgdafvs tmlayatfav
       61 gfvtrplggv lfghlgdrvg rksaliltml imgvstagva flptyaqigm wapallltlr
      121 vlqgiglgge wggavlmaye yalphrrgly aslpqiglai glclaagvva vlsralpdaa
      181 flawgwriaf aaslllvaig fyirtrvadt pefvalkrqr rdtklpvvel lgnyrraill
      241 gmgaryidgv ffnvfavfsi gymtrnlsis rgdallgvms aavvmcvfip vfgslsdrlg
      301 rarvyrwgat lcglsvlpaf wllqtqssnl lavwlalvip fgifyamayg peaalfaelf
      361 danvrytgis fvyqvsgvfa sgltpivata llrvnggepw lvgvyvmlsa llsivsvrai
      421 ekrdrvagvt vram
//
LOCUS       WP_175857365             357 aa            linear   BCT 11-JAN-2025
DEFINITION  C40 family peptidase [Burkholderia anthina].
ACCESSION   WP_175857365
VERSION     WP_175857365.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..357
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36520
     Region          <6..175
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mlricvpvai vsllaacssv ppqsasrtsg mkittprafp apanfpkfvd hsvgqeeisi
       61 qamslvgvpy rwggntptsg fdcsglvryv lgraadvnlp rttadmssrg msidpdqvap
      121 gdliffnttg rphshvgiyv gklrfvnaps tggtvrldyl tnpywakrfd girrvappra
      181 tpapfdapty earrdapvaa papapvvtaa aprqpayaat qgsaapspap imptapvvaa
      241 aapaaaaadp yepppprmqa aqqqatttng dmnamtanaa pasptaetgs qipttaltaa
      301 qaaafdaepp saataaapsp rstepvqvlr aatqsapasa rtgtaddpia rfangsy
//
LOCUS       WP_175857384             751 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Burkholderia anthina].
ACCESSION   WP_175857384
VERSION     WP_175857384.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 751)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..751
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..751
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=81689
     Region          43..746
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mnspleatpd arrdvssagr arapegtfel srkrvdeldt ifgeggllar aldgyhprls
       61 qiemaravas ameasarrmp epeifetrkr parrlgdgdk aadsaadgvv aaesdsdsds
      121 gdntliveag tgtgktyayl vpamlwggkv ivstgtkhlq dqlfqrdipt vrnalavpvt
      181 vamlkgrsny lchyylqrta dngrlpsrqd taylqeivrf akitksgdka elasvpetap
      241 vwsmvtstrd nclgqecphy kecfvmqarr eaqqadivvv nhhlffadim lrdtgmaell
      301 pnantvifde ahqlpetatl ffgetlsttq ilelardtva eglshardav ewvklggdle
      361 raardlrlaf andqivrmsl aqlgddhpmf galdaletal dalasalasq aeraeslgac
      421 lrrarelqdl lagwvtpgaa eaaakadaaa agdkaatdgd pnekvrwvev fahtvqlhet
      481 plsvapifak qragvprawv ftsatlsvrg dfthyaaqmg lssrrsmtla spfdyqtqgl
      541 lyvprnlpqp sspaftdavf daalpaieas gggvfmlctt lravdriask lrdviesrgw
      601 ntpllvqgda srtelldrfr shgnailvgs qsfwegvdvr gdalslvvid klpfappddp
      661 vlaarldalt kkglspfavh qlpqavitlk qgagrlirae tdrgvlmicd trlvdkpygr
      721 riwqslppfk rtreiavvqd ffdehraqkr a
//
LOCUS       WP_175857397             208 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia anthina].
ACCESSION   WP_175857397
VERSION     WP_175857397.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..208
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21723
     Region          1..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mphvawlpfm atslliiltp gqdmvlvmsr tlsggtragl vtaagvsvgl lvhtmlatlg
       61 lgallqasew lftalkmiga lyllylgitl lrssgeltla gnggapasrl rtfaqgalsn
      121 vsnpkvalfy laflpqfvpa gaahpmlslf vlgttfaglt flvkgpvalc agmlstsirr
      181 npriltrmhr vsgtvllalg vklalerr
//
LOCUS       WP_175857432             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175857432
VERSION     WP_175857432.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32954
     Region          6..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 magdnlddla aflvvaeern ftragkrlgv sqsalsqtvr alearlgvrl ltrttrsvvp
       61 teagerlmgs igprieaiqh elmllsdlrd kpagvirlta teyaaeavlw paiarlvday
      121 pdikvevqvd ygltdivrdr fdagvrpget iaqdmiavri gppmrmavag spayfakrtp
      181 prtpqalidh scinlrlssh gglyawefek rgrklnarvd gqlvfnssnl ilraaldgrg
      241 layltegqma pcladgslvr vledwcepfs gyhlyypsrr qptpafallv ealrypprtd
//
LOCUS       WP_175857523             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175857523
VERSION     WP_175857523.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32774
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdkfsalrvf vevaeaggfs sagrrlelap ssvvrsvdal eeslgtvlln rttrqvtlsd
       61 agavyyvrak klledladad slvadrgdep sgplrvsvpv aygsrrigph iaaflarypk
      121 ldfdmrlsdd mvdlvaerid vairlgeaap tadvvarqlg sfrryvvash dylethgtpv
      181 eptdlanhhc lrfsyrgdqq fwtfagdett tkvvvtgrmk snnsevlrda vldgaglall
      241 pdwlvepdiq sgtllklfer yhvtpndars vvsalylpnq rgskrvnafi dlvaslvscp
      301 a
//
LOCUS       WP_175857514             446 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175857514
VERSION     WP_175857514.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..446
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47549
     Region          28..436
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(36..37,40..41,44,83,141..142,144..146,149,169,
                     172..173,176,264,267..268,271..273,276,305,309,364..365,
                     369,373,389,392..393,396..397,400)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mevarvshtr hvgtdeside krksaikgav fsefidmfdi ylpviilapi qsyflpknvs
       61 gghqeilesl vfittllgrp lgailfgria drvgrraasi lsvtgfgvat llialipgya
      121 sigiasywll vllrfvdgif lgggytgalp laieysrkeq rglvgglila gfpaayvain
      181 vmamvmfelf plggpdspya mwgwripfil gaamagllav yyirkvsese vwagksahkp
      241 qatsaarlvs gqqlrnlmqv llmmtgfwlt qnvvglflpt gillktlhls avemtatlmi
      301 syavlclayv gagmlgqwig rrtmlaaigv lsstvgavll yalieakgas lvhigllvcg
      361 laitvssawa vivtyinerf atgvratgfg vgyslsviip sfyafymnwl gavmpsryap
      421 iallviggiv acvgalmgpe tknael
//
LOCUS       WP_175857567             488 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175857567
VERSION     WP_175857567.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..488
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51407
     Region          26..445
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(36..37,40..41,44,84,134..135,137..139,142,162,
                     165..166,169,281,284..285,288..290,293,320,324,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 msnpyalavt aridrlppta tiwglvlmls vggffevydl fqmtylpagl vrdgifhvga
       61 kglfglsdqa tlgaatfvgl figeigvapl adrfgrravf tgalllytaa slamcaqdta
      121 agihlcrlia gigvgaelit igafltelvp kgmrgrafav cfaigylamp vlalaswllm
      181 praplgisgw rwiilaggsg avivwwlqsr lpesprwlam rgrtdeaeav lqtiearvar
      241 dygqplpdvp pvvtietana raasmwdary rgrtlmliaf naclsigffg fsqwlpslla
      301 aqgtpvtksl lyafviafay pvspfiagam adrierkwli vaaaigvalf gtafalsssa
      361 aavigfgili tfcnttlasn atayqaevfp tairsralgf vhsfgrltgv assyvvalil
      421 ehmgapgvfa ligasmlvvv lsigvfgprt nhrsldeiaa adgpqagagd asgapdryrg
      481 savrarqr
//
LOCUS       WP_175857576             314 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175857576
VERSION     WP_175857576.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..314
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34885
     Region          7..311
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpedfhflll pgfsalgfms aveplrvanr frtelyrwhv isadgapvaa sngipvaaea
       61 acadvaqvet vfvvagfdpl vcydraladw lrrqnrhgat lggidtgsfv laeaglfgas
      121 qpltlhweal aafrerypgl natqelfeid drritcaggt asidmmldli grrhgadlaa
      181 aiseqfvvsr irqrsdsqrl eiaarygvhn rkliqvidmm qrhmenplgs dalaqdvsit
      241 rrqlerlfsa tlndtptrfy lnlrldrare llqqtdmsit svcvacgfes pshfsrtyrs
      301 rfgvsprsdr rptr
//
LOCUS       WP_175857654             526 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Burkholderia
            anthina].
ACCESSION   WP_175857654
VERSION     WP_175857654.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..526
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=57655
     Region          25..519
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mkgvmeetmi agvevrstpd idlklrntal sspnrvavad syrsvtwgel drrvnriara
       61 lltrgialed kvallasnsv ayvelmlgil ragacvvpls tytspstcaa mvsdsgarll
      121 fvseyyatgm lplvddmklr ssdivrldda tldefvsgvd dtpppvspsl dqgfnliyss
      181 gttgtpkgil qsrgyrarea eviesrygln eqtrtiistp lcsnttlfll ftvlaaggta
      241 kvmekfdvng wltlaetwrp tdiilvpvqy trllahpdfs rfdlsslrnk fstgaplsaa
      301 vkleiltrwp aggltefygm teggvacelr ahehtgkldt vgrplgnvdl riigdgkvlp
      361 qgeigeiigr spsmmsgyhn reqatldasw fdgegqrfqr sgdigwided gfvhlldrkk
      421 dviisggfnv yavdlenvis qhrevvevav vaapsrnwge tpvacvilrn alepeiirqw
      481 aneklgkvqr iakvvvfdel prsqigkvlk relreqiare ygdklp
//
LOCUS       WP_175857696             302 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia anthina].
ACCESSION   WP_175857696
VERSION     WP_175857696.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..302
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32804
     Region          33..270
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 mkniaplrid vetfdwplaa rlsaaaqprs apasgvslyw lgqagfvieg aglrllidpy
       61 lsdslarkyr ntryphermm aapiapddla hvdlvlcthr htdhmdpdtl qplarrfpgl
      121 rfvvpaatld eavrrcgvet srlvavdagq sieplrgvri mpiasahetl dvdtqgrhpw
      181 lgyvieiagv rlyhsgdcvp ytglsdsvaa qrphvallpv ngrdderssn gvpgnftlde
      241 avslardagv rvmiahhhgl fdfntiapde idarilsegg alalyrartq cvwhvcahat
      301 aa
//
LOCUS       WP_175857716             243 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175857716
VERSION     WP_175857716.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..243
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26448
     Region          1..240
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mteqkkplvm itgasagigr ataqvfsaag ypllllsrra eqmqalglpd sacvqadvrd
       61 rlavadaier gearfgpvdc linnagvsrl srleeqdpde wrdlidinci gvlncmhalm
      121 pkmqarrhgt iinvssmagr kvyphhdvyg gtkhfvhait egarqsmsqh dvrvmaispg
      181 vtksdiehti tnpnafafws kgrdamgggi daevvartml fayelpqsvt lqemsitatr
      241 qey
//
LOCUS       WP_175857722             444 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175857722
VERSION     WP_175857722.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..444
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47640
     Region          23..426
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,154,
                     157..158,161,258,261..262,265..267,270,299,303,352..353,
                     357,361,377,380..381,384..385,388)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mthptrdaaq palvaqatrr acrrlmpfll lmyvlsfldr anigfakeam qvsigisnta
       61 yalgaglffl sysalelpsn lamhrygarl wlsrimvpwg lisaammfvr getsfyalrl
      121 llgvaeagfv pgvilyltyw fpdhmrgrmi glfyfgapla fifggpvsgl llqldgvgnl
      181 hgwqwmfmie glaasvvglv aywylddspe karwlpddek ralmatlane srekaahgga
      241 alrrvfvdpr liqytvvyfi vqmavfgvtf ylptqvahll gthigvkvgl vtaipwicai
      301 aasfwvpria dryrchrvva aitlavsglg iavsadsgpf vaivalcfaa sgfiavqpvl
      361 wtfptrrlag maaaggigli nglgllggfv apsvknfads vaannsggly vlaaltfvga
      421 igaamlrwpd epaangpaaa kefv
//
LOCUS       WP_175857755             157 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia
            anthina].
ACCESSION   WP_175857755
VERSION     WP_175857755.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..157
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17000
     Region          11..146
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtaklnpfaa apalmknwmt vsiaaagsle ptlielvkir asqinacanc lnmhtveare
       61 qgeteqrinl laawreapcy tdreraalgw tdaltrlseg haaheaayaa lndhfsqeeq
      121 vkltlminvi ngwnrlavgf glwidpadak aaakmva
//
LOCUS       WP_175857809             732 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia anthina].
ACCESSION   WP_175857809
VERSION     WP_175857809.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..732
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80207
     Region          32..715
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 msassptsph agglaawyaa fddwartdga awlylfkall aafisigvsm rldlpapkta
       61 mttvfivmqp qsgavlaksf yrvagtifgl iatltfvglf pqqpqlflla valwialcta
      121 gaarnrnfrs ygfllagytt aliglpasqh pdgafmsamt rvaeimvgiv sagvvsalvf
      181 pqytgeqmrt tvrkrfvsfv dyvsaalsgk ldrahiesih trfvadvvgf eaarsmavfe
      241 dpdtrmrsgr larlnsefms vssrfhalhq lmnrlravga qaaidaiepy freiaplltr
      301 hgepvrtstd aalaaeqlla wrdelprrir atratletqp dfplldfdta sellyrfitd
      361 lheyaatyas lstatherer wieryeprtn vtamviaair tatvilvlgw fwietawpsg
      421 vtltltaaat calasstprp tamsaqmgmg talavctgfl ltfgiyphid gfpllcvala
      481 pllaigifmt lkpklagygm gyliffcfla gpdsithydp tsfmndalal vlsmlvsaia
      541 favlfpptap wlkkrlfadl rhqvvaachv rlaglrtrfe sgardlmyqa htlsadqpdv
      601 qrdalrwmfa vletgnaald lrhelatlps dpryapatpw rraietlrta lsalfskpta
      661 erfdttlaav naaidatrqt ldafaparee rhrlqrilsn lhfvrtalld pespleplnr
      721 nrpvrpqpga ss
//
LOCUS       WP_175857815             473 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia anthina].
ACCESSION   WP_175857815
VERSION     WP_175857815.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..473
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50531
     Region          4..473
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mnspeafvsa crdaigaayv ltdphdtepf ltdwrrrykg aacavlkpad taevatlvtl
       61 anthgvalvp qggntglagg atpdasgsqa vlnlsrlnrv raldphnnti tveagvilad
      121 vqarareggr lfalslaaeg sctiggnlst naggtavlry gnarelclgl evvtpqgeiw
      181 dglrglrkdn tgydlrdlfi gaegtlgiit aavmklhplp aaqvtalaal esphaaldfl
      241 slaqraagpl ltgfelmsdf cmqlvgkhyp qlrypfdrth aqtvllelsd nesetharal
      301 feklmeeafe aglvvdavva enlaqsrafw dlrehiplaq adeglnikhd iavpissiar
      361 fidetdaaiq qaapgarmvt fghlgdgnlh ynvqtpeggd pkaflaeyqa pinrvvydnv
      421 hrhhgtisae hgigqlkidd aqrykspvet tlmrtlktal dprglmnpgk vlr
//
LOCUS       WP_175857871             237 aa            linear   BCT 11-JAN-2025
DEFINITION  PadR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175857871
VERSION     WP_175857871.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 237)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..237
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25715
     Region          83..162
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mrhnpsrgha rcdghgahag pewfaglwha igrhrrghdp fggggpfggr ggrggfgdfg
       61 ddgmprgrqf ssddlqllll alvaeqpshg yelikaldtr sngfyspspg mvypaltyle
      121 evgfvasqae gnrkryaltd agrahldaqr ervdtlfarl thlarkmefm rrafagetag
      181 seapdetqpg wlpefvearl alkrallhks aadadeqrri aaimrratae iegstga
//
LOCUS       WP_175857944             252 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Burkholderia
            anthina].
ACCESSION   WP_175857944
VERSION     WP_175857944.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..252
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26992
     Region          1..245
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mirleridks fgahrvlsai dlalqpgsvt aligpsgsgk stllrcvnll evpetgtlav
       61 gdarieftag hrpsrdavfa vrrqtgmvfq nfqlfphlsv vqnvmeglvt vqrwpreqar
      121 eralalldkv giadkadawp atlsggqqqr vaiaralaps pqvllcdept saldpelsve
      181 vvevlrqlar egttmlmath dlrlaasvah davfladgrv veagasrelf grprdprtak
      241 fvatlaqgvp al
//
LOCUS       WP_175858168             382 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia anthina].
ACCESSION   WP_175858168
VERSION     WP_175858168.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..382
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41126
     Region          19..363
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mnddykvelp evaaiargrr lrvgviglgi grkhvegwre hpdvdvvaia dpdakrlakv
       61 gdafgidary atadamlaae kldvvsvctp nvfhreltla afdagchvlc ekpmalnade
      121 grdmliaaqr agkrlminfs yrfsaqsral kaqvdsglfg dfyfgrtvwh rrrgmpgfgg
      181 wfgtkalagg gplidlgvhr ldlalwlmgy pkpvwvmgst ydpiarelaa ragktfdved
      241 laaalirfdn gatlaleasw atniqeaelm etrllgthag llqknlnegy tfdahvfieq
      301 ngaqfdmrln ppaegahsam ydyaeailcd vphpapgeeg livmeildai yasaaagepi
      361 rihapgpaav aapplldldv ag
//
LOCUS       WP_175858268             295 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175858268
VERSION     WP_175858268.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..295
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32398
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          90..290
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(102,106,145,159,162,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mpdlheldaf aavarhrnfr kaavergvsa salshalrgl eerlgvrlln rttrsvtpte
       61 agmqllsrle pairdiadal aelnafqaap tgklrlnvpr paarlllapi ltrfvktypr
      121 ieveivtdds lvdivgagfd agvrfgesla kdmiavpfgd alrfvvvasp eylsahgqps
      181 eprelmvhac igrrfpsgsr yaweferaeq altitaggpl vfdddemmvr aaldgaglay
      241 vyeayaeafi ttgrlvpvlr dwspkpsrff lyypslrqmp palrafidai rldqp
//
LOCUS       WP_175858361             336 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia anthina].
ACCESSION   WP_175858361
VERSION     WP_175858361.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..336
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35971
     Region          6..336
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 metiqplrfg vlgaariart fiagvapspl adviavasrd rekgrqfane lgvprshdsy
       61 dalladtdid avyvplpntl haewvikald agkhvlcekp iavskaetla mfdaarrngv
      121 flaeaypyra qpqtlelrrl ldegaigrvq tvfacfgfkf gdtanirldp ergggallda
      181 gsyavnmvrm vagekpvrvs avarwsetkv dltvtanlef angvlgqiac sfntafhrqa
      241 liagtdgile ttflnsppea gppeihlrrg vpsttpreti alpggsgfla etecfvravr
      301 agreqwngst eaesvdtiat leaiarsirs gawesv
//
LOCUS       WP_175858460             264 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Burkholderia anthina].
ACCESSION   WP_175858460
VERSION     WP_175858460.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..264
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28357
     Region          7..264
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mqrrfmlkfa aavgaamlft sahaqaetik vgvtggphaq imevvkkvaa ksgldirive
       61 fsdyvqpnaa lasgdldans yqhdpylqaq ikdrgyklik vadtvtfpmg iyskrvksla
      121 elkpgariav pndptnggra llllqkqgll klradaglka tpldivdnsr klkiveldaa
      181 qiprslgdvd aaaintnyam eaglkpkqda iaiegpngpy anilairead rskrwvakli
      241 aayhsvevkq fieqkfggav iaaw
//
LOCUS       WP_175858472            1602 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA translocase FtsK [Burkholderia anthina].
ACCESSION   WP_175858472
VERSION     WP_175858472.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13109227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1602
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..1602
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=162021
     Region          <9..112
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          <169..708
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <512..>763
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     Region          <668..>767
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          1000..1598
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 mhtvvfgwfg isavwflllf wrlvqamlpg ggglagrgsi rlwlgfaavf vasctltspl
       61 sgpdtnglgh afstgfahvl gpigtpvamv vlllaglpwl tgigwrqfaa wvdtsfgvkl
      121 ardvddddar gvadlprsal hrdddvvqpt tahtvnsmap rqngrysrpt lwkpdpqarp
      181 kprsksaprp ltepvapsgw lkptpvnrvp tppvpsttsp lpppttgsta slaraaanaq
      241 vprpdpaplp agfepvrprp tavrpaaaal kqpaaprtsv tprpvsatpp rtparpatgt
      301 gaagksadaa rrrpapptpa raplyawvqq paepitpsps vhdtlrsiea staqwamldn
      361 trstngsnat ataataagai aaassvaasa stavpggfvp atpqiaphdt drpdehaavp
      421 ayddnapivl dafmpaepsv qahaaasgam lsghtaqpev sdlhagteap aqhandesrh
      481 vadapvapaf htsidfapwe divsppfaai dasrkrpiaa spavsaepva agqssmaips
      541 aasdtarnfd aneaatttgi gapfesqpal sadttisads ghntrdvlsg tngmngakav
      601 eqvatpshpp vspvaetpar tladvmpvaa atpalaassa apahavtgtv wkndaavknv
      661 aaaaplsvst qrpmtpamda spapstsaia epassnaats tpwssplsar pfaaaptsst
      721 sstsstssts stagtsspva tpvvapvsat papaitpnrt paavapsfgg vtntasgsps
      781 qpaapavasv apsalasvts tvdgsgnras faapaiapaa sstlsaaagp vsgsitrssa
      841 paaaaapapt paantagvst aqpstpapsa sigtsfrata sqpiastpta aatatpsasp
      901 gatlaamsta satgsmaswt gavdaaaina atgatqpaam tppaaaivta pstgapaptg
      961 ttatatpatf gstpvapast laavaasaap ttsqspvtpa vsalpgalap satlgaampv
     1021 pvqsytpppa pattpaswsv sstgttpasa giaapviaaa plaaatiada slppatddaa
     1081 epatpaadas aptarqprpn afefhapasf nvelptldll epasddvqti seehlaqtgq
     1141 vieqrlqefk vpvtvvgasa gpvitrfeie palgvrgsqi vglmkdlsrg lgltsirvve
     1201 tipgktcmgl elpnakrqmi rlseilesrq yqhstsqlti amgkditghp vvtdlakaph
     1261 mlvagttgsg ksvainamil sllykatped vrlimidpkm lelsvyegip hllapvvtdm
     1321 klaanalnwc vgemekryrl msavgvrnla gfnqkirdaq akekkignpf sltpddpepl
     1381 stlplivvvi deladlmmva gkkieeliar laqkaraagi hlilatqrps vdvitglika
     1441 niptrvafqv sskidsrtil dqmgaesllg qgdmlflppg tgypqrvhga fvadeevhrv
     1501 veylkqfgep qyeegildgp atdgaaqdlf geapdaeadp lydeavafvv rtrrasissv
     1561 qrqlrigynr aarlveqmea aglvspmgin gsrevlvpaa ad
//
LOCUS       WP_175858473             609 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 15 protein [Burkholderia anthina].
ACCESSION   WP_175858473
VERSION     WP_175858473.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Sakaguchi,M.
  TITLE     Diverse and common features of trehalases and their contributions
            to microbial trehalose metabolism
  JOURNAL   Appl Microbiol Biotechnol 104 (5), 1837-1847 (2020)
   PUBMED   31925485
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..609
                     /product="glycoside hydrolase family 15 protein"
                     /calculated_mol_wt=67548
     Region          1..592
                     /region_name="SGA1"
                     /note="Glucoamylase (glucan-1,4-alpha-glucosidase), GH15
                     family [Carbohydrate transport and metabolism]; COG3387"
                     /db_xref="CDD:442614"
ORIGIN      
        1 mpaliedyal vgdghtaali skdgsvdwlc wprfdsgacf aalvgtpehg rwllapaada
       61 aithttrryr gdtliletdy esadgavtvi dfmppgngws elvrivvgrh gtmkmrmelv
      121 lrfdygfsip wvtqlsresg mkaiagpntv vlrtpvaltg knlhtlaeft vsaderipfs
      181 lgyaashlrl ppardplsml artenywlew sgrcqvqgry aaavrrslit lkalayeptg
      241 givaapttsl pekiggnrnw dyrycwlrda titllalmrg gyydearawr twlgrvmags
      301 peqiqimygi agerrlpeme ldwlpgyqds kpvrvgngaa nqlqldvfge vmaalhlarv
      361 gglqaddtvw svqcslldhl ekiwqepdeg iwetrggrrh ftfskvmawv afdraiksae
      421 mfrlpasldr wralrdriha dvcdnawheg kqafaqsygs deldasvlmm pllgflpped
      481 privgtvaai erellhdglv mryrtteydd glppgegtfl acsfwlvdny allgriddah
      541 rlfsrllals ndlgllaeey dpvggrlvgn fpqafshval vhtamnlmhh eeamaraagq
      601 pvpavatgr
//
LOCUS       WP_175858510             506 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Burkholderia anthina].
ACCESSION   WP_175858510
VERSION     WP_175858510.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..506
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53902
     Region          13..490
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(70,72,76,79,83,116,119..120,129..136,141,144,147,
                     240,244,247,250,252,426,428..429,431..432,435,438..439,
                     441,443..446,455,459,461,475,482..487,489..490)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(156..159,167,182,185,215,232..235,238,256..258,290,
                     391,393,419)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(159,256,287,290)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mttvpaftss ddvghyidga rvsgasgrfq dvfnpaagka arrvaladdn evaqavaaaq
       61 aafpawsetp pirrarvmhr flqlmnehrd tlaaiitaeh gkvfsdaqge vargidiief
      121 aagvpqllkg dftdqvstgi dnwtmrqplg vvagitpfnf pcmvpcwmfp valatgntfv
      181 lkpserdpsa alfiadllte aglpkgvfnv vqggknavda lidhpdvqav sfvgstpiah
      241 yvhqrasqng kraqalggak nhmvvmpdan ldqavdglig aaygsagerc maisvavlvg
      301 digdrivekl aqraktlvig dgmspevemg pivtgealkr iegyidigvq egaklvvdgr
      361 glkvpgreeg fftggtlfdn vttdmriyke eifgpvlacv rvkdfaeavn linahefgng
      421 vacytsdggi arefarriqv gmvginvpip vpmawhgfgg wkkslfgdmh aygeegvrfy
      481 tkqksimqrw sssigkgaef amptak
//
LOCUS       WP_175858506             228 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia anthina].
ACCESSION   WP_175858506
VERSION     WP_175858506.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..228
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23863
     Region          52..216
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mttaqtvasa asasaaatga sapnaasaap asapaaapap verplvrfqq kplsvningk
       61 svgpmqvpeg lmmieflhey agltgsrlgc gqgichacvv ivdkpdgtse emrtcitgah
      121 ffhgssirti eghakrndag evvelspiqq kflehfsfqc gyctpgfvna atvlierlkr
      181 epiakadveh titdalnahi crctgyvryy eavkdviltt pglvkdaa
//
LOCUS       WP_175858519             340 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia anthina].
ACCESSION   WP_175858519
VERSION     WP_175858519.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..340
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38294
     Region          6..331
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 msihhamdri lviridflgd mlcttallra lkqrwpdael hivanrynas vlagnpdvha
       61 vhtyvysrqc erndrpgrwh avvdrfrlir clrrlrfdla vvpnggmhrs svrfarwlgv
      121 rhcrwhdart gfddrrpaht htrpicheal sgfqlvpelg rsnldgltla vypdgarqqa
      181 whrrfgpsak prvglfvsnk aaerrwhddk wrdlgrrlge radvivfhdp aipqekrawq
      241 glsahhveps svsdliaaas lldvivsads apvhlasalg vavaalfedr pekylrwhpl
      301 gvphvilrag atvdaigvdv veravcrllr qparqrvvaa
//
LOCUS       WP_175858525             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175858525
VERSION     WP_175858525.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33921
     Region          23..80
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          110..303
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(124..125,127..128,131,135,137..143,233..238,
                     244..245,247..248)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 misnqngefe shemraslps lmalrcfeaa arhehfsraa delhlthgav sravrlledd
       61 lgvalferrn rrvfltdagr klaqavhdgl hlikqaanal radaaraqrw vlsceptllm
      121 rwliprwpdf qaayagvdih laaaggpfsf dngidmairr ndfawpagyh aerlfaekvg
      181 pvcrpdkvet wfsgsrddra lkrsaprlht rtrpdawkew aaaahrtags grgqvfdhfy
      241 fslqaavagl gvaigpwhlv rddlesgvlv apmgfvedgs yyclltpepv tagsassdll
      301 dwlrama
//
LOCUS       WP_175858527             210 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175858527
VERSION     WP_175858527.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..210
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22316
     Region          21..173
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 miqntarspg rprsfdetga lekaiqvfws kgydgvkidd lvagmgvgrp slyavfgdkr
       61 aiflrvlray aerkgasaak allapqslrd siegflryav esatekgsar gcllvcvapl
      121 vddpdvrqfl qnaaaggtal vegrfrdais ageipsdfpv avratqvtdl argltmraql
      181 gtprktllkd aeeaadlvlq prrgnaapes
//
LOCUS       WP_175858544             246 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175858544
VERSION     WP_175858544.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..246
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27345
     Region          24..206
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mntilpahpf ddalpalepa aaadtephar tlsehayhql rqhiieghyp pgaklrvehl
       61 kdvygvgagt lrealtrlvs dalvvaegqr gfrvtpmsvd dleaitrlri hievdalrds
      121 vrrgddawah rvrqsfdmls aweqpvsieh raaweacnrr fhealisaaa tpwtylilrm
      181 lsqqseryrr vciglgdskr dvhaehtclf eaamrradar aalaledhig atlavvrnap
      241 pgtlpf
//
LOCUS       WP_175858569             113 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FmdB family zinc ribbon protein [Burkholderia].
ACCESSION   WP_175858569
VERSION     WP_175858569.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..113
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10859
     Region          1..75
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 mpiyayrcea cgfakdvlqk msdaplsqcp ecgkdafrkq vtaagfqlkg sgwyvtdfrg
       61 gsggtsapat assdgaaapa daapaaaapa aassesttts aapapavapa ags
//
LOCUS       WP_175858581             391 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Burkholderia anthina].
ACCESSION   WP_175858581
VERSION     WP_175858581.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 391)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..391
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41746
     Region          4..386
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 mtalktlaia nyrslreliv plaaltvvtg pngsgkssvy ralrlladta qgrvipslar
       61 egglsstlwa gperfsraml ngdtpvtgtv rsgpvslrlg fagddfgyai dlglpvpsrs
      121 qfaldpvvkr eciwggallr pstllvdrqg aqirartasg dwhtvpqpva sfdsmmtefa
      181 dpvgapemia vrerirswrf ydhfrtdaqa parqshigth tpvladdgad laaalqtire
      241 igdaaaldaa iddafpgasv didnpggrgr fdmlmrqpgl lrplsaaels dgtlryllla
      301 aalltprppa lmvlnepets lhpdllpalg rliaqaaqrs qvlvvshaar liatlereag
      361 ceslvldkql gatvlvdadt rdlppwkwps r
//
LOCUS       WP_175858598             774 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: xanthine dehydrogenase family protein
            molybdopterin-binding subunit [Burkholderia].
ACCESSION   WP_175858598
VERSION     WP_175858598.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..774
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81545
     Region          <68..>194
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          203..764
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mnapelsvhn esrralllgf asgglllafg lpslahaaap vqppvspnpq yggtgmphgl
       61 rddphlfvai apdgtvtvtc irsemgqgvr tsvalvvade lgadwarvrv aqavgdepry
      121 gnqntdgsrs lrqsfaalrr agaaartmle qaaaatwgvd arqvkatvhe vvdtqsgrtl
      181 gfgelaakaa alpvpdpktv plkapaefry igkgetalid grdivggrah ygidtrldgm
      241 lyavvarppa ygdtvasfda saaeklpgvv kvvqlastpl psgfqplggv avvardtwta
      301 iqaraqlkid wkrgpnagyd svayrktlea aaaqpgdvir ndgnaatala satkrvraty
      361 yiphlahatm eppaavarva ggrcevwtct qapqttrdei akalglstec vtvnvtllgg
      421 gfgrkskpdy vveaallska agapvkltft reddiahdyf havslevfdg gldaagkvva
      481 wqhrtvapsi qstfragvvh eqpgelaqgv adlpfaipnv rienpaaeah trigwfrsvy
      541 niphafgiqs fvselahaag rdpkdfllel igparrfeph itvknvnyge dpalypvdtg
      601 rlrrvietva reagwgrklp eghglglaah rsfasytaav cevqvgaaga ifvprvdiai
      661 dcgpqvnper vcsqlegavv mglglalhge itfkdgqpeq snfngfqvlr mneapreirv
      721 hlvapddyat plggvgepgl ppiapaltna ifaatgtrir slpvadqlsk skag
//
LOCUS       WP_175858686             116 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175858686
VERSION     WP_175858686.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..116
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12629
     Region          8..78
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mprntstsst fskrlkqarl rsgltqeqlg ieagidefsa sarinqyekg khtpklqmgq
       61 rlasalhvpt sflyedddll anllataarl prdkkkallk caealvqapa pptkik
//
LOCUS       WP_175858680             342 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia anthina].
ACCESSION   WP_175858680
VERSION     WP_175858680.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..342
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=35855
     Region          16..342
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mqkslrgtas altltlamtt giaygqssva lygladafvg elhpagaags awqvgsggmt
       61 tsywgmsase dlggglkavf tlesffrmng gqigsfygqa ffgrnafvgl sghfgeltlg
      121 rntaplfvst llfnpfgnsf vfspivvhsy fgsaigsasl qsdtaidnsv lyqtpevggl
      181 sgsvlysnag vaghvgqany smnvlyfagp fsataavqsl htaslflnga taqtawligs
      241 ayrfraikvf aqyervdnnn rvtddtvqag asvrvgigsl lvswagtrrr pvagdhihws
      301 tvalgydhpl skrtdvyaaw ryetishvss gnglgagirm rf
//
LOCUS       WP_175858717             437 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175858717
VERSION     WP_175858717.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..437
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47915
     Region          27..430
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(41..42,45..46,49,81,131..132,134..136,139,159,
                     162..163,166,261,264..265,268..270,273,301,305,356..357,
                     361,365,381,384..385,388..389,392)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mssikgvahi rlvgesvneg lvyrkvtwrl ipllfmcyvv ayldrvnvgf aklqmlrdlq
       61 fsetvyglga giffigyflf evpsniilhk vgarvwiarv mvtwalisaa tmfvttptmf
      121 yvvrfalgva eaglfpgvil yltywypskr rskmialfmt gipvagvigg plsgwimhsm
      181 agvhgwagwq wlfllealps ivmavavlaf lddrvsdakw ldederelia rdvardqtqt
      241 qshslrdgft nprvwlmcgi yfffavglyg vgfflptlik nsgttdplti gllsmlpyaa
      301 avivmilvsr ssdarrerrw hitapaliga iawlfavgfk hdvmiamval tvvtccvivt
      361 isqfwclpta ilsgaaaaag iavvnsvgnl sgflgpffig wisdkthstd iglfvlagsl
      421 alggllvlrv krelvnr
//
LOCUS       WP_175858718             272 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175858718
VERSION     WP_175858718.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..272
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29311
     Region          6..257
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 msesvpgaqa vsralrvlra varsrtggin laqlvretel nkptahrlvl aliaegmveq
       61 dprslryfvg recyvlggia serfglgrea vdavarlarw sgdsaflsir sdvfsvcvlr
      121 edgdyplkth vlqpgtrhpl gvgagslaml aaldddevsr clkeneetlr ksyasfssaf
      181 lqrevaltre rgfsvneglv vsgswgvgva vhspaddvig alsiaavesr lpkdrqsevg
      241 rhlmkeakrl eahlarslam rpepkpkkts sg
//
LOCUS       WP_175858721             337 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175858721
VERSION     WP_175858721.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..337
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37046
     Region          3..322
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mfitvdivvy ngfkvlevtg pmsvfnyanf hlarrgisgg ydvkivatqc geicsdigvs
       61 lraskalstl alphtaivvg trlieeavde tpqivewlet sghrmqrtaa lcsgafflaa
      121 aglldgkrat thwasaqslq erypavqvep dcifiregpl wtsagvtagi dlaltlveed
      181 fgtgvaldva rdlvvylkrp ggqsqfsahl asqitthpgi rdlqewllgd ltrrvrteam
      241 asrlsmsvrn fnrcfqretg ttptrfiera rveaarrmle dgdfpaktia anagfrnyet
      301 mrkafqkllg vtpmsyrerf grgehhetvl ydgidat
//
LOCUS       WP_175858722             153 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175858722
VERSION     WP_175858722.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..153
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17120
     Region          1..141
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mqldvidiki lselqrdarl snvelasrvn lspspclarv kamersglir qrvtllspet
       61 lglnvnvfin vslenqrrew ldeferavvv ipgvmecylm tgdadyllrv lvrdtpalek
      121 livdelarip nvksirssfa lkqvmystai plg
//
LOCUS       WP_175858742             353 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia anthina].
ACCESSION   WP_175858742
VERSION     WP_175858742.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..353
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37791
     Region          3..332
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,225,286,306,308..310)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,173,176,178,225,232,286,306,
                     308..309)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,173,176,178,309)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            178
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mptlfdpvtl gdlnlpnrvv mapltraras vgrvpndlma ryyaerasag liiseatsvt
       61 pqgvgyadtp giwsdeqveg wkrvtqavha aggrivlqlw hvgrisdpvf lngdlpvaps
      121 aiaagghvsl vrpqrpfvtp raleldeipg ivaayrkgae nakkagfdgv eihgangyll
      181 dqflqdstnh rtdayggpie nrarlllevv daaidvwgag rvgvhlaprg dahtmgdsdp
      241 aatfgyvare lgrrkiafif treaysgdhl sprlkeafgg plianeqftl esaqetlasg
      301 hadaiawgkl fianpdlprr leldaplnkp vpetfyaege tgytdypals daa
//
LOCUS       WP_175858774             349 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia anthina].
ACCESSION   WP_175858774
VERSION     WP_175858774.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 349)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..349
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36921
     Region          1..341
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mselrihgls ksfgshtvlh didltvrrgs rlallgpsgs gkttllrvlc gfehaergtv
       61 eidgrrvaap glhlppeqrr igyvpqegal fphlsvadni afglpraarr rhhrvdelle
      121 mvglpasyas rvpqqlsggq qqrvalaral apepslvild epfsaldtsl rhetrtavad
      181 alaaagatsv lvthdqpeam tlgdevavmw qgrlvqtatp qtlyrqpvtr dvasfvgqav
      241 llagrvrdgr ivcvlgelpl vaplpdgpad amlrpeqigi vpaapagtag shaarveatq
      301 fagqdadvlv rldaaadtlv rarvqghrcp avgervalvv dgavmayar
//
LOCUS       WP_175858799             403 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia anthina].
ACCESSION   WP_175858799
VERSION     WP_175858799.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..403
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41449
     Region          8..390
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(18..19,22..23,26,61,108..109,111..113,116,139,
                     142..143,146,221,224..225,228..230,233,263,267,316..317,
                     321,325,341,344..345,348..349,352)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mpdsryrwvi vaaggllsci aigamfslpv flravardtg wsmtgisaam tlgfiamafa
       61 siawgslsdr igtravvatg avllaaslal asrapsllaf qlifglgvgs aagavfapmm
      121 acvtgwfdth rslavslvsa gmgmapmtms plaawlvsrh dwrasmltia vlaaavmipa
      181 slfvrrppal drppaepvaa gapvplsvgn alrspqfivl lltnffccat hsgpifhtvs
      241 yavtcgipli aavsiysveg lagmggriaf gllgdrfgak rmlaagllaq algalgyyfv
      301 rtldgfyava mlfgfiyagv mplysvlare nfplrmmgtv iggsamagsl gmaagpvagg
      361 livdalgsyg wlyigsfvig iaafavalmf rpfpkapsqt vav
//
LOCUS       WP_175858828             107 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia anthina].
ACCESSION   WP_175858828
VERSION     WP_175858828.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia anthina
  ORGANISM  Burkholderia anthina
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Burkholderia anthina"
                     /db_xref="taxon:179879"
     Protein         1..107
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11822
     Region          19..83
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mlyamstkpr trdrrnavat aigkrvkacr iaaeksqeel ayeacldrtr vsaiergign
       61 ptvetlatic yvlgitlsdl feplkmalkp tgehrgeapq prrrplr
//
LOCUS       WP_175859024             173 aa            linear   ENV 11-JAN-2025
DEFINITION  dihydrofolate reductase family protein [uncultured Streptococcus
            sp.].
ACCESSION   WP_175859024
VERSION     WP_175859024.1
KEYWORDS    ENV; RefSeq.
SOURCE      uncultured Streptococcus sp.
  ORGANISM  uncultured Streptococcus sp.
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; environmental samples.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="uncultured Streptococcus sp."
                     /db_xref="taxon:83427"
                     /environmental_sample
     Protein         1..173
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19735
     Region          9..167
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mavyfygcit mdgyladseh ridwlhqlgs vedtgyddfy rqmditimgk rtfeeiqdlq
       61 dvesfyqate nyvfthdrhl pvsnyqpvag dvvdfvhqid kgknvfvigg nslvgpllda
      121 dlfdhliiqi aplilgkgvp lftqeegqrf yqldslrqfg pfaelvfsrk sqk
//
LOCUS       WP_175859334             125 aa            linear   ENV 11-JAN-2025
DEFINITION  BlaI/MecI/CopY family transcriptional regulator [uncultured
            Streptococcus sp.].
ACCESSION   WP_175859334
VERSION     WP_175859334.1
KEYWORDS    ENV; RefSeq.
SOURCE      uncultured Streptococcus sp.
  ORGANISM  uncultured Streptococcus sp.
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; environmental samples.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="uncultured Streptococcus sp."
                     /db_xref="taxon:83427"
                     /environmental_sample
     Protein         1..125
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=14221
     Region          4..125
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mkrsikrlpd geftilkviw qlptpttsar imeklgpdnh wkpqtlltvl arltekgfld
       61 svrkgrerqy taliseeeyl eveasdflkr hsghsmggfv ktlfssnsfs eneldelrsl
      121 lnqgk
//
LOCUS       WP_175860355             232 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175860355
VERSION     WP_175860355.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..232
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25498
     Region          62..227
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <173..226
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mrsekagaeq farqtlnfms nllgvdsiaf yhiddetrea rfkllnvpag flsdylkyag
       61 dldplspvra qfvggatall snelgesdgd reyhrfmrlh gfrdtielff rcngqmvggl
      121 svllndcsav pdrrtellqr criaqpyieh niasgpqssa irirewlatd hglskrevav
      181 aelvaagrcn kmiggdlsia vttvkthlvh ifdkvgvdsr aaliakinaf ss
//
LOCUS       WP_175860362             315 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175860362
VERSION     WP_175860362.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..315
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33779
     Region          2..315
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhtvavlalp dvvpfdlgva cdtfvrvrsp dvapayhvrv cseqprvtgd lfelrppfrl
       61 dalagadtim vpgtseplap tsprvlaalr aaaargcria sicsgafvla eaglldglra
      121 tthwlaaael arrypdvdvd pnvlfvdngr iltsagaaag ldlclhmiqa dygaavavda
      181 arsavaprvr eggqaqfiap ewpaggdglh dlmdwlqanl rkpltldema rkastsvrtl
      241 trrfqeqtgt sprqwlqtar vrhaqqllev talsiehvat eagfgsvtaf rerfvrivgt
      301 spqryrqtfr araga
//
LOCUS       WP_175860486             200 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175860486
VERSION     WP_175860486.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21714
     Region          9..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdrirltrae rrdatrerli daaraifaek gyaaasvedi aaaaghtrgg fysnfrdkad
       61 vlfellrrdr deaaaalqwi vgshdpvdda qramlaywrr gatqpavhlm wldaqfqaar
      121 dprfrarfga llrdrqalaa acidayaara gvslplptpv lalgltalcd gmqshgaada
      181 ladavlvgfi ahtvfdrvrg
//
LOCUS       WP_175860458             663 aa            linear   BCT 11-JAN-2025
DEFINITION  beta-galactosidase [Burkholderia cepacia].
ACCESSION   WP_175860458
VERSION     WP_175860458.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 663)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 663)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 663)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448998
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..663
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=74058
     Region          1..622
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
ORIGIN      
        1 mrlgvcyype hwpesmwadd arrmkalgie qvriaefaws riepspgeyd wgwldravdv
       61 lgaagleivm ctptatppkw lvdrhpdila igadgrpraf gsrrhydfss ptyleasrqi
      121 ctavaerygr hpavrywqtd nelgchqtvv syspaalvrf rawlkarygt idalnrawgt
      181 vfwsmeyrhl devdapvgtv teahpshrld yrrfasdeva ryhrmqvdvi rahspgrpva
      241 hnfmqlftef dhyevardld vatwdsyplg aleeqwfape vkarwlrtgh pdfasfnhdl
      301 yrgmstlpfw vmeqqpgpvn waqwnpaplp gmvrlwswea fahgagcvsy frwrqapfaq
      361 eqmhaglntp dnrldeggre aqrvareiaa irdagadadp ngavrapval vfdyeakwlf
      421 evqpqgadfh yprfafeyya alrslgldvd ivsahapldg yqlvvvpplp vvpddfaarv
      481 aasgahavfg prtgsktvdl qipptlppgp lasilpvrvw rveslrpnvt epidgtlcdg
      541 aplagharhw rdfvelhddt rgvvrarfad ghpacvshgt lhywaalfdd attarlfadv
      601 aaeagltptp lgdgvrvsrr ggltyvfnyg dtphtidavp psafvlgtaq vgpqdvavyr
      661 srs
//
LOCUS       WP_175860491             223 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia cepacia].
ACCESSION   WP_175860491
VERSION     WP_175860491.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 223)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 223)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..223
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23447
     Region          31..130
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          130..222
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mkrtwmigaa lviagvaaag tlygpdlvdg mryqksmaai geadkvngga wprpqetcff
       61 chgvhgqsqn awypslsgqp atyiaaqlra fatdqrrnay mgplsreldd akiaalatyf
      121 arqaparnea vpddvaldkr gmalvearsc rachgaaltg kdpaprlagq gqlyletqla
      181 afrsgerhdp tgamnalaat lsgddtrava hylaglspdg aak
//
LOCUS       WP_175860501             475 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175860501
VERSION     WP_175860501.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..475
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51046
     Region          16..425
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(29..30,33..34,37,76,134..135,137..139,142,162,
                     165..166,169,251,254..255,258..260,263,294,298,351..352,
                     356,360,376,379..380,383..384,387)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mtttlrdepr grhqsrkaai sgwigsvley ydffiyatas alifpqiffp hgspttaiia
       61 slatygvgyv srpigafvlg hlgdtrgrkt vllfcmflmg istvgvgllp tyqqagliap
      121 allvtlrllq gfavageitg assmilehap fgrrgyfvsf tlqgvqagqv laaavflpla
      181 yympsaqfds wgwripflls alvivaglii rrevdespaf deavrnrsqa gspvadafrh
      241 hfpdmlrvac msmmnvipvv atifgaayav qpaygigfqk dvylwitvmg nivamivipf
      301 vgnlsdrigr rppiivgsla agllafayly aisirnvpla fvmsmlmwgv vyqgynavfp
      361 afypelfptr trvsamaiaq nlgtaataml palftavapp gahhvwlivg aiafgitvia
      421 slaawsaret srvhlndlgr anaqpvgkae ydllraeals hdrvvrepvp gsvgs
//
LOCUS       WP_175860531             308 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175860531
VERSION     WP_175860531.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34444
     Region          6..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..299
                     /region_name="PBP2_DntR_NahR_LinR_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators that are involved in
                     the catabolism of dinitrotoluene, naphthalene and
                     gamma-hexachlorohexane; contains the type 2 periplasmic
                     binding fold; cd08459"
                     /db_xref="CDD:176148"
     Site            order(102,104..105,109,168,206,274)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176148"
     Site            order(103,106..107,110..111,114..115,117..118,121..122,
                     124..128,130,195,223..227,230..231,234..235,238,252)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 mealdlnlip ylvalddtrn vsragdllgv sqprvstalg rlreyfgdpl fvrtsrgmep
       61 tpralallpa ardalaqier glvaphdfdp aasthtfsia lsdvgeivfl pkllqafamr
      121 aphanlrsvs lahdevgrgl eagsidlavg yfpdldgnnf fqqrlfthrf vclmrrghpf
      181 eqappftveq flacghavvr aegrsqevle kylakqrmqr ravletphfm slpfilsrtd
      241 liatvphaig yayaaehafi vpvepplalp rfdlkqhwhr kyhndprtaw lrgvvaslfn
      301 deqdewpk
//
LOCUS       WP_175860552            1012 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding and (Fe-S)-binding domain-containing protein
            [Burkholderia cepacia].
ACCESSION   WP_175860552
VERSION     WP_175860552.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1012
                     /product="FAD-binding and (Fe-S)-binding domain-containing
                     protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=110232
     Region          24..539
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
     Region          492..1011
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mtsavspslv rpvhlvpsqg palsplferl rremrgdvha drasrgryat dasiyqimpl
       61 gvvvprdqdd lrialdiard rkipvlarga gtsqcgqtvg ealvvdnskw lnrivafdaq
      121 artvtvepgi vldhlnawlk phglwfpvdv staaqctigg magnnscgsr sieygnmvhn
      181 vlaidailad gsecrfgsla qpvtdrrtle llhgveriak rerdeiverv pkvlrrvagy
      241 nldlfdcqnp raytddghan lahllvgseg tlahsrqitl klaplpahkt lgvvnfptfy
      301 qamdtaqhiv klkpvavelv drtmidlsme npafrpvieq alvgqpqail lvefagesrd
      361 aqhaqldrla elmadlglpg svvkmtdaga qkalwevrka glnimmsmkg dgkpvsfied
      421 cavplehlae ytrrltdvfh rhetegtwya hasvgtlhvr pildmrrdga trmreiaeea
      481 aalvreykga ysgehgdglc rgewvawqyg prlnaafaei ktlfdpdnrf npdkivnppk
      541 mdarehfrfa pgyaalplrp aldwsawnva rnpltgeeta pgsgtdithg laaavemcnn
      601 nghcrkfdag tmcpsyrvtr deqhvtrgra ntlrlavtgq lgadglagdd vkaaldlcvs
      661 ckgckrdcpt gvdmarfkie arhawnrkhg ttlrerlvay lpryapwaar mrgaiafvng
      721 vpvvassikr wiglapqral pgfarpflad vgadtgtstp sqtgsatrev llfvdtfsny
      781 qdpdnaraaq avleaagytv hfnvragarp lccgrtflaa glvdeaksea rrtldalrpy
      841 lergvaivgl epscllsmrd eflaygygde atrlasqafl feeflvrehe agrlslplha
      901 idanealvhg hchqkafgaf tpvqtvlrwi pglkvtpves sccgmagsfg yeaehyaasq
      961 amaelsllpa vraraegaiv vadgtscrhq iqdgaqaqav hvakvlaral rs
//
LOCUS       WP_175860578             355 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175860578
VERSION     WP_175860578.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..355
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38110
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,144,160,162,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdliqrmqvf vtladagtft etgkrlnltt ayvsraiasl ethlgirlln rttrsmclte
       61 agerylarar ditlavdase reargarlhp ygrlrahcga sianrfvipl varfqarype
      121 vsvdltlaph vpdlirgsyd vaiiampnlp sadqvaidvg rigsvlcaap ayvahhgmpd
      181 tpralvrhrc lqlvapaypa gewtltrgad aetvafepai tadvaaslai avregagigl
      241 lpefvaaddl rsgalvrvlp dyraddvrvf lvypsrrhid aktrawvdfm kvelrdalag
      301 prgghrdghq gggdatapdt agaaattplt rqpsprnarq ktspaplrph ahtrg
//
LOCUS       WP_175860609             244 aa            linear   BCT 11-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175860609
VERSION     WP_175860609.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 244)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 244)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..244
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26117
     Region          21..242
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 msssvstssg lrdkpayvae mgrglraalp vmlgfvpfal vlgaqaaqkg lslfevpmmt
       61 gmnfgggsef aalhlwtspp hialivamsf lvnsrhilmg aafepyirrl prrraffalf
      121 fmcdeswams ladararsat hisvpyyagi cvglyltwis mttlgaavgp tignveqygf
      181 dmaftavflv llrgmwkgmr asrpwfvslv vaaathlavp gawyvaagac aglvaallwe
      241 prda
//
LOCUS       WP_175860626             881 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia cepacia].
ACCESSION   WP_175860626
VERSION     WP_175860626.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 881)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 881)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 881)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 881)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..881
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..881
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=94372
     Region          53..860
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 miekrqprmq aetepklkpv callltiiag wqthayaaqt dsgelqiart efaqvefegg
       61 flnngsgaid vsryerrnvv ragmykpdvy vdgdwigrie lqfksapntv daqpcfdkaq
      121 leligvdfsk lpqdvratld edgaclrigq aiqeasvsyd fneqrldlsi pqismrrqar
      181 gyvspdqwse gipvgmldyn asvyhartdg qgestqgyvg vnggvnvgrw hfrhngsfnw
      241 ddrgrrkyen vatylqrdlt awssqlivgd aytsgdlfds tsfrgvrlyt ddrmlpesqr
      301 gyapvvrgva nthakvtvtq ngatlyettv apgafviddl yptgyggdlk vnvteadgsv
      361 hsftvpyaav plslrpgqnr ysfttgvvrn lpnttpyfaq atwqrgvtnl ltgyggvtfa
      421 qgylsamaga vlntslgavg vdvthattsi pgerrysgqs frisyakava atgtnvaiaa
      481 yrystngffa lndamqardq aqlgagaasv srqrnraslt vsqslgargg slnatasast
      541 ywnrsgsdvn ftvgysntfr dvaysvsatr qrdawgksst myyanlsipl gktrpmtlat
      601 slsrdtrgst qaqtslsgal gvdnnvsygl nvnhgnssgt sqtnggasiq yrgpiaelsg
      661 svsaaadyqq fsagargaiv ahrggvtlsq plsetfaiie apnaegarvt ntsgvridrr
      721 gyavvpyltp famndigidp kglstdvelk etsqriapla gavpmltfkt aygrsavira
      781 rqadgspvpf gatvtdadgk dvgtvgqggk llarglvdqg elkvqweadr gksvcalsys
      841 lpvrkraaty qplqslelpc vasevisyap avpnrvasar r
//
LOCUS       WP_175860665             555 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175860665
VERSION     WP_175860665.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..555
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=59977
     Region          1..540
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 msydyiivga gsagcilanr lsesgrhsvl lleagerdas fwfkvpvgft ktyynrrynw
       61 myysepeaql adrklycprg kvvggsgsin amvyvrgqrs dyddwaaagn pgwayddvlp
      121 yfrklethaa gatdpqhhga tgpihitsmk advhpivhef lkgcgelnlp rtddfngaqf
      181 egagiydlnt kngercsssf aylrpalgra nltlragvlv rrvtfdgtra tgvvvsgahg
      241 detlvaarev ilaagavdtp kllqlsgvgd pallarrrvp lvhalpavgr nlqdhlcvsf
      301 yfkanrptln demgtllgkm kiglrylltk rgplamsvnq aggffrgtdd vqepnlqlyf
      361 nplsyripks drasikpepy sgfliafnpc rptsrgtiei asnraedaak ihvnalttrk
      421 dldeavqgsk viralmrapa lksmtveeis pgpqvdsdea mlqyfreqsg siyhlcgsca
      481 mgpdaatsvv daslrvhglq alrivdasvf pnitsgnina ptmmvaekga dliladaghg
      541 easavsaser etvth
//
LOCUS       WP_175860696             294 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia cepacia].
ACCESSION   WP_175860696
VERSION     WP_175860696.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..294
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=30803
     Region          9..271
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mtsdptssta fvfagggslg aievgmlrel vasgerpdcv vgasagaina ayfagrpdad
       61 gvamlaalwc rirrrdimpf smrslvamll rnrphlvead alrlllernl pyrrieqaal
      121 plhivatdvl ngqevvlsag pvvdavqasa aipgvfpsvs iggvelvdgg vanntpisva
      181 ialgvkrivv lpagfacalr vpprsaiaha thaltlviar qlvrdlelyg araqihvvpp
      241 lcpldvssyd ysqcaqlidk aaertrawid agglaqcaip gqlrehdhaa vlsh
//
LOCUS       WP_175860700             574 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia cepacia].
ACCESSION   WP_175860700
VERSION     WP_175860700.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..574
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62666
     Region          7..560
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mqmqpthaat tpadfvltna kvytvdphkp waqavavrdg rivhvgdtaa vqayvgartk
       61 vvdaagrlvl pgfveshwhf ettafafqaf vndedpqkvl galrayvesh pdepaitgmg
      121 wvqatippal lrketldaic adrpvcllst dfhtmwvnsk aleiagidas tppvqegasw
      181 fekdaatgep tglivdgaay sllmqrisaa gllptgidly lksippwqkk lcaagvttvf
      241 dagffdasgd qsllyetlqt meragdlklr vvgsvavige iddpvgtlvr yreqydsplv
      301 karalklfld gteanhtayl lepyadrpdt cgaptmpadt fnrylveadr ananvmvhcv
      361 gdaavrmald gfdavnrmnp prdrrhvith aflthpddip rfrragvman tqlqwgvvda
      421 yteqlrdhyg herwssmykf rtfldegvtv sigmdglacq crcqhkpleh iesghtrqla
      481 gepdapvfpd iaerlsipql iaaytihgay qlgmehevgs ltpgkradlv vlendlfevg
      541 qydigridvg ltmmggrith vgddfgartg mqas
//
LOCUS       WP_175860714            1068 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cepacia].
ACCESSION   WP_175860714
VERSION     WP_175860714.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1068
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=114620
     Region          1..1046
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 miariirwsv hnrflvllat vliaawgvhs vgqtpldalp dlsdtqvivk asypgkapqi
       61 vedqvtyplt ttllgvpgak tvrayssfgd afvyvlfddr tdpywarsrv leylsqvqsr
      121 lpagatvslg pdatgvgwvy eyalvdrtgr hdpgqlraln dwflkfelka vpdvsevasi
      181 ggmvqqyqvv ldpdrlrayg itqaeianal gnanqasggs vvelaeseym vrstgylrtl
      241 ddfrhvvlrt ndagtpvllg dvariqvgpa mrrgiaelng qgevtggvvv mrsgknaltt
      301 idavkaklad lkrslppgve ivttydrsql ieravgnlkd klieefvivg ivcavflfhl
      361 rsafvailsl plgvlaafiv mryqgvnanl mslggiaiai gamidaaivm ienahkhlea
      421 ydhahpgepv taarrwelva ssaaevgpal ffslliitls fipvfsldgq egklfaplaf
      481 tktytiaaaa glsvtlvpvl mgylvrgrip hehanpinrv lirvyrplle atlrrpwvai
      541 gvavvalglt avplsrlgge fmppldegdl lymptalpgl sadkasellq qtdrliktvp
      601 evdtvfgksg radtatdpap lemfettirf kprsawrpgm tpeklvdeld rtvkvpglsn
      661 vwvppirnrl dmlstgiktp vgvkisgpdl agidaiakqv eaavkrvpgv tsalaerlng
      721 gryidvdidr laaaryglsv adiqsvvssa vggddvgevi agrerfpinl rypreirdsv
      781 enlrqlpvvt argaqirlgd variaiadgp pmirsenarl sgyvyvdirg tdlrsavram
      841 qqavaqqval ppgysiawsg qfeyleraaa rlrtvvpvtl vvifvllflt fgsaadalll
      901 mstvpfalvg gfwlvwalgh avsvatsvgf ialagvaaef gvvmllylkg alqrrldage
      961 pltdalllda iregavlrvr pkamtvavvl aglvpimvgh gagsevmqri aapmvggmvt
     1021 apllsmfvip aawlllqrrh arstgrvrhs davphgtnvp siptgesr
//
LOCUS       WP_175860739             922 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia cepacia].
ACCESSION   WP_175860739
VERSION     WP_175860739.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 922)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 922)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..922
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=98730
     Region          18..834
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msiatalrnf asglvdwnnr pvalhfgqaq havghllalh hadireglms gidgqltcis
       61 thahlaptlf lglpvsvrlt tdrgdvrain aivhdvqagq sdgeltvyql ricdalslmd
      121 rrinsrvfrs rniidilgtl lnewrqrspa larafdfdls glraerypar eltrqvnesd
      181 arfvrrllrr egitvfakaw avgnargtad erpihtlvfc ddplrlpesp agtvrlhprd
      241 sgtaqrdtvt lfahhqrlsp gkagrlswdy kkarmddsai atsidqgdag ndlarlltdv
      301 aidiphvgds wndhdrithd rilahqfaae rydgvghvrd mpvgcwftlt gdpeldmkpa
      361 eqrqfvvtsv rhdirnnlpk dlagrvialy aasrnlaqaa pptpadaseq adtryenhft
      421 cvrrgvpltp sydptidlpp ahlltgtivg tqgeevfcda agrvrvrihg fdpadhehaq
      481 gagtngsagd sapirvgasl aggnfgtlfl prvgmevllg clsgdpdrlv iigvlsngan
      541 ppatfthtga lpgnryvsgi ktkeikgary nqlrlddtps qisaqlaseh ahtqlnlgyl
      601 tqprkdghga drgegaelrt daaaalraaq gilfstyart catggqldrd eliqlldqcm
      661 mlfnslgdfa gqhggraadt agqekivdaf rhwkpdlada gsagdtsalm afgaqagslh
      721 vtprthvmya genidqiaqr hvqvasgeri nlhgghgvam fahsggvsai anrgkvtiqs
      781 qdddtqvdsa kniqltaagg klagmandqv vfvtsggayl klnggdielg cpgtftvksa
      841 ghawggpasm stdmptfdha plgrvpklvr atdgdavagf dghlqrasea lsnlttdaag
      901 elpavhgdqf etlsvqfikk ng
//
LOCUS       WP_175860803             273 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Burkholderia cepacia].
ACCESSION   WP_175860803
VERSION     WP_175860803.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..273
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27771
     Region          194..272
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mtgltieygv pparrhaara aprtgagvaa avaaawppsa spaarpdara akpgrwrvtg
       61 aialavaalh agvallaara paappvqppr plpmtveltr ppeplpqaah ppppvvpkpq
      121 qplkqaptpp kprsavahpa papaaaqpvm reaapvptap aaaaqaapsp apaapaapvr
      181 etapigdaay lrnpapdypa faqdqgwegr vvlrvhvlan gtpdsvdvrt ssgrrmldna
      241 avaavkrwtf vpakrgdeav dgwvnvpidf klg
//
LOCUS       WP_175860801             348 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia cepacia].
ACCESSION   WP_175860801
VERSION     WP_175860801.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 348)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..348
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38365
     Region          3..325
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mttlaaqata rdalwytrcp vptalgiavh rgwfdeefgp dgialhslqe tadagkresh
       61 fdhslpssfr qggnipalwa rargadtrvi glswtnefqa ivtlpdrgir tardlrgrrl
      121 glprhpisid fwraaalkgf lsaleleglg hgdaewvdlp dererrtgla sftrgpheyg
      181 ieiaalvrge vdavfvkgve gletvhlida qvvidlgahp dplvrigngt prtltvdral
      241 idarpdlvsr flsvvvgagd waarhpaetv ayigretras dewvryayga dvhrhletgl
      301 aqtsidglva fkdflvewgf leqdfdaraw idpapftrid rqrhawva
//
LOCUS       WP_175860805             358 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia cepacia].
ACCESSION   WP_175860805
VERSION     WP_175860805.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..358
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39273
     Region          12..335
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 msitashhvq siwytrcpvp tplgiaahlg wldsefagdg itvralqesq haalhrahvd
       61 hsldntfrqg gsipalwara sgadtrvval twvdeaqaiv alpetgltrp rdlrgrrigl
      121 prrdgeridi fraaalrgfv salsldglgp advewvdvpa snlrapvstp ltrdaafshp
      181 sslssrrlya aeaaalvrge vdaiyvkgsl gletahliga qpvvdigfhp dpqirinngs
      241 prpltvnast lerhpdivrr flarvtdveg wareheqevl gylgretgsg hdwlrlaygt
      301 dvhrrlrtdl deasiaaldd fkrflvewrf lpadfdvraw idrraldgia plsrdaar
//
LOCUS       WP_175860861              99 aa            linear   BCT 11-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Burkholderia
            cepacia].
ACCESSION   WP_175860861
VERSION     WP_175860861.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..99
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=11302
     Region          1..98
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mivrlsdfai deleavadyi ardnpqravt fvreirdkcm slaamplafp lvprferhgv
       61 rhrvygnyqi fyrvvgdppa ridillilhg ardyasilf
//
LOCUS       WP_175860883             793 aa            linear   BCT 11-JAN-2025
DEFINITION  serine/threonine-protein kinase [Burkholderia cepacia].
ACCESSION   WP_175860883
VERSION     WP_175860883.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..793
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=80151
     Region          37..310
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(42..43,45..48,50,63,65,115,131..134,138,140,177,179,
                     181..182,184,194..195,198,215..217)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(42..43,45..48,50,63,65,115,131..134,138,179,
                     181..182,184,194..195)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(46,138,140,177,179,181,198,215..217)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(59..60,107,112,117..120,132)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(194..202,211..214,215..217)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <371..723
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
ORIGIN      
        1 mkdagsrdne hdtatrgdas eftvrplplg hrlgelqlde vlgiggfgiv yrafdrtlrr
       61 avaikeymps mlatrggdyt vslrserfaq afdagrgafl nearllaqfd hpglvkvlhf
      121 weshgtaymv mpfyegrtlk qlldggmris etqlrnivga llgaldtlhr aqcfhrdval
      181 dnvlirpngs ailldfgaar krigdlvddg ammikpgyap ieqytddpaf sqgpwtdiya
      241 lgavmhamit gelppaavvr sikdtyrpla srelpagevy spaflaavdh alqlripdrp
      301 esvaafaael glrdfdrtgs gygapavppv gdagrgggdk gaasveagta saaaatsiga
      361 ggaasgsaap ptqagagpvs tptdtasasp gvsdgkpetd dvsstlkaat hgaaataaag
      421 alaasashas rpaakpvesd apngdverak epaaartdph detsarsarp dtdigargaa
      481 gsakadafaa egagagagag aasttapypa asssassass assggasvpp gaqhgqapag
      541 srkrrlpvya ggavvaliav glaatylsrp arvadeptpv asqpqagtsp pastpaatla
      601 qqgptpivvp psslpagssa qvppprvaae pastpaveaa apapqvattv tnaapppaga
      661 spaiapagsl daservvnvp pseaavppvt tpspapkppd sqtavaavta lpaeqqprap
      721 kaqetvqvrf nvrpwgdvyv ngarrgaspp lrsvsltpgv yvieirngsl pplhrtvaid
      781 fgskpvnidy afe
//
LOCUS       WP_175860894             191 aa            linear   BCT 11-JAN-2025
DEFINITION  DinB family protein [Burkholderia cepacia].
ACCESSION   WP_175860894
VERSION     WP_175860894.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Cooper,D.R., Grelewska,K., Kim,C.Y., Joachimiak,A. and
            Derewenda,Z.S.
  TITLE     The structure of DinB from Geobacillus stearothermophilus: a
            representative of a unique four-helix-bundle superfamily
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 3), 219-224
            (2010)
   PUBMED   20208147
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..191
                     /product="DinB family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21626
     Region          31..176
                     /region_name="DinB"
                     /note="Bacillithiol/mycothiol S-transferase BstA/DinB,
                     DinB/YfiT family (unrelated to E. coli DinB) [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2318"
                     /db_xref="CDD:441892"
ORIGIN      
        1 msappqnpia psvttdritl pasaadtlrm lvrykswang ltfksvmdlp agealrqrpt
       61 rfgnmvhtln hvyvvddifr hhlqgkehty tsrntdhtpa vsdlwkavqe mdrwyinlvd
      121 twsdadlaka vhfefvggge gvmtreqivl hvvnhatyhr gfvgdmmyqv pfappsndlp
      181 vfirdhyrda r
//
LOCUS       WP_175860952            1055 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cepacia].
ACCESSION   WP_175860952
VERSION     WP_175860952.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1055
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113063
     Region          1..1038
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mwivnlalrr pytfivmaim ivlatplalm rtpvdvlpai nipvisviwn ysgfsatemt
       61 nritsvheri ltttvnniqh vestslpgia vvkvflqpga nvqtaiaqtv ssaqaivrqm
      121 pqgatpplvi tysassipvi qlglssktls eqsladialn flrpqlitvp gvqipfpygg
      181 rtrvvaidld pqallakglt padivnavna qnlvlptgta kmgqteyrid tnasadtvad
      241 innlpvqtvn gattylreva svrdgfapqt nvvrqngqrg vlisilksgd astlkvvsdl
      301 kallpkvipt lpegltitpl fdqsvfvdaa vqgviheali aavltammil lflgnwrstl
      361 iiaisiplsi ftslialsal getinimtlg glalavgilv ddatvtieni erhlhlgtnl
      421 hdailegage iavpafvstl cicivfvpmf fltgvarflf vplaeavvfa mlasyvlsrt
      481 lvptlamllf rpqqasagpd rstsrfarih hafneaferl rawyivllsi llvrrrfyat
      541 cflgfcvlst glvfvlgrdf fpnadsgnir lhmraptgyr ieetarladq verviratvp
      601 pdelgaivdn lglpvsginl sysnagtigt ldgellialk pghratqhyv qalrtvlper
      661 fpgvefffqp sdiitqilnf gqpaaidlqv lgndlasnmt iasslmkkfr qipgavdvhv
      721 lqrndeptll admdrtrmqq lnlsaqnvaq nmlislsgss qttpsfwinp rtgvqyplqi
      781 qtpqynissv ddllgtpisa sgrtgmplql lgnlvqvrst anpavithyn irpaidvyvs
      841 vegrdlgava geidrivsda ratlprgtel tmrgqietmr tsylglgagv amaivlvyll
      901 ivvnfqswld pliiisampa alagivwmlf itgthlsvpa ltgaimtvgv atansilvvs
      961 farqrleaga ppltaaleag atrirpvlmt alamiigmvp malglgegae qnaplgravi
     1021 ggllfatvst llfvplvfgg vharlarrra rqagh
//
LOCUS       WP_175860927             472 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia cepacia].
ACCESSION   WP_175860927
VERSION     WP_175860927.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..472
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=50808
     Region          85..468
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mtarpvfpsp dasgasapra psrllrraaf aigaavlgyg afaiafpaqv paaigtvvad
       61 wtganphpvv lqrpaaqpls avahlgralf adpslsasgk qscaschspd haygppnald
      121 vqpgglamtq qgyrpppslm ylyrqpnfsi gpdagendaa psvaqqaasa agvvkaqkva
      181 gtsaapqlvp qggmfwdgra dtlqqqafgp llnpvemana siddvarkla qsshraqfek
      241 lfgarvfdsp qlavseamfa iaryqvedps fhpysskydr wlegrarltr aelrglrlfn
      301 dpdkancagc hlskpgkdgl ppmftdyqye algvprnqql aqnrnpafhd lgvcgpfrdd
      361 lkdqtqycgm fltptlrnsa trhvffhngv fhtldqvmaf ynersispqk fysrgadgkv
      421 deyddippky ranvdvtdap fdrkpgdkpa mtaqdirdie aflgtlndap ar
//
LOCUS       WP_175861001             826 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 2 protein [Burkholderia cepacia].
ACCESSION   WP_175861001
VERSION     WP_175861001.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 826)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 826)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 826)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 826)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..826
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..826
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90147
     Region          10..>626
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mtrtralpaw smlataagaa reprdlpaag ngwipaavpg tvaqslalag rldeaislde
       61 rdhwyrielr ghgprvlrfh glatlaqawl ddtpilrsds mfvahdvpvs ldgshrltlc
      121 fralaphlrd araprrarwr trlaepaalr tirtslfghm pgwfpphvpt gpwrpvdvld
      181 padgpvladc nlhariegdt gwldadltfa aplpdalaar lscgqhhatl eragpdrlra
      241 svavpnvcrw wphthgepvl ydialhigae rrplgttgfr tievdpgadg kgfglrvngv
      301 pvfargacws saaplalhad datyarllgl ardagfnmir vggtmtyead afhawcdrlg
      361 llvwqdfmfa nfdyalddpa fadnvdrear qflsrhgasp slavlcggse iaqqaamsgl
      421 gpkqrflelt adrlaghaaa crpdvpyvpd spdggvlpfm prervshyyg vgaylrpldd
      481 arradvrfas eclafsnvpc datlaelgwp gvheprwkaa vprdpgtswd fedirdhylq
      541 tlydvvpdrl rredparyfe lsravvadvm retfsewrrt gsrcagalvw qfqdvmpgag
      601 wgvidaahrp ksawhalrqv lqpvqvllvd eglngldvhv vnerpaplsa alelvalrdg
      661 rtavaragcp vriaahdtvr igsaellgrf fdwtyayrfg pcehdtvvat lrgddgtlls
      721 qafhfpsrth pavlarrelg leacvsrtgd twhvdidtrh varhvqidap gfvprddwfh
      781 lapgtparvv lvplgtagkn gaadgppave iravnaarav ratqag
//
LOCUS       WP_175861051             189 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia cepacia].
ACCESSION   WP_175861051
VERSION     WP_175861051.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..189
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20325
     Region          3..187
                     /region_name="COG3981"
                     /note="Predicted acetyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:443180"
ORIGIN      
        1 msaikllrpt tallpsyvaa leagwspdnv rkaiaareql daidvdaerf vdglddptas
       61 ggpiplpdgs tvarlpsivr wiwdgdfsga igfrwqagta elpsyvlghi gfsvvpwkrg
      121 ngyatqaldl mlgeakgegl pyveltvdpe niasqrviaa cngvlierfr kpaaygfaet
      181 lryrielnd
//
LOCUS       WP_175861069             184 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia
            cepacia].
ACCESSION   WP_175861069
VERSION     WP_175861069.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..184
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19838
     Region          42..177
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtdrlppfdp asatdaqkav ladilsgprg nlngpflgwi aspelaqhaq klgafcryrt
       61 glplrlsela ilvtaarwrs qaewhihhpi aleagvpaat ayairlgvap afesdddali
      121 hafaselydt rrvsdatfar aqarfghetv vnlvallgyy alvamtlntf gmradgqtel
      181 pfpe
//
LOCUS       WP_175861105             508 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Burkholderia cepacia].
ACCESSION   WP_175861105
VERSION     WP_175861105.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..508
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53846
     Region          16..491
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(72,74,78,81,85,118,121..122,131..138,143,146,149,
                     242,246,249,252,254,427,429..430,432..433,436,439..440,
                     442,444..447,456,460,462,476,483..488,490..491)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(158..161,169,184,187,217,234..237,240,258..260,292,
                     392,394,420)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(161,258,289,292)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnaavpqttl alptakllid gafvesqsae wgdivnpatq dvigrvpyat ldevdaaias
       61 aqrafqtwkt tpigarlrim lkfqdlvrrn leriahtlta eqgktlpdaq gdifrglevv
      121 ehacsigtlq qgefaenvag gvdtytlrqp igvcagitpf nfpgmiplwm fpmaivcgnt
      181 fvlkpseqdp lstmqlvela ieagvpqgvl nvvhggktvv drlcthpdik aisfvgstrv
      241 gthvynlgsq hgkrvqsmmg aknhavvlpd ahreqsinal vgagfgaagq rcmatsvvvl
      301 vgkardwlpd lvekakalkv nagaeagtdv gpvvskaake rilslidagv kegatllldg
      361 rdvkvpgyeq gnfvgptifs gvttdmsiyq eeifgpvvvv meadtlddai alvnrnpmgn
      421 gvglftqsga aarkfqseid igqvginipi pvpvpyfsft gsrgsklgdl gpygkqvvqf
      481 ytqtktvtar wfdddatagg vnttialr
//
LOCUS       WP_175861314             541 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia cepacia].
ACCESSION   WP_175861314
VERSION     WP_175861314.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..541
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59267
     Region          2..537
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mqyadtayln gllytgdaqr rfaqalatrd gkivavgrdd dirpligpat rtvdlagrlm
       61 lpglvdghvh pleghqilgd fdlsgindpd tilqriraca datpnepwvy lgganlaafg
      121 ayptrelldr ivpdrpllvv gfdvhsgcln tkgleaagih adtldpaggv yerdasgapn
      181 gvvheaafyr vcplipqlsp agypkslaka hamahgygit gwfdarveea elkayadaqr
      241 agtlkvymsa glyanprrdp reqierfaaw rhayecdnlr lhtvkifvdg vpesktaall
      301 epyagtddcg lalwsqdaln eiclladsag fdlhfhtlad ravrmtldal eyvrirngmr
      361 drraqlahlq lvdpadmsrf nrlgaiasvq tlwtaareeq qqlyrdllga ertarnypfr
      421 slrnagamla agsdwsvstm dpmqiiqtgv thllidqpds ppwnpherld lltmleaytv
      481 ntayalrfdd ctgsleagkd asfaildrnp fahpvetfaq traietcfrg evvyaapgwa
      541 d
//
LOCUS       WP_175861394             382 aa            linear   BCT 11-JAN-2025
DEFINITION  metallophosphoesterase [Burkholderia cepacia].
ACCESSION   WP_175861394
VERSION     WP_175861394.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..382
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=40982
     Region          113..381
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mrsffvrfia igvlfhlyvg mriipdafas pvvrtiaalv lasfvvlipv gmfsrrfdeg
       61 waatlvgwag svvmgffssl llltflrefv llgvfawrhl ghagawpgaa tgtalgvlaa
      121 aafvtvvgfv garrtaavkr vsipveglpa gldgltivql sdihvgptik rpyverivra
      181 vnaldadlvv vtgdvvdgsv krlrehtapl grmqsrhgsf lvtgnheyya gahawidefr
      241 rigltvllne hvlidhdgah avlagvtdft aggfdpahrs dpeqalagap revatkilla
      301 hqprsaeaan ragftvqlsg hthggqflpw ppfvrlqqpv igglsrfgdl wlytsrgtgy
      361 wgppnrfgvp seitlirltr gg
//
LOCUS       WP_175861320             780 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AAA family ATPase [Burkholderia].
ACCESSION   WP_175861320
VERSION     WP_175861320.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 780)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 780)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 780)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 780)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 780)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..780
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=88086
     Region          1..702
                     /region_name="RloC"
                     /note="Wobble nucleotide-excising tRNase [Translation,
                     ribosomal structure and biogenesis]; COG4694"
                     /db_xref="CDD:443729"
ORIGIN      
        1 mlkrikeisg vgpyisckaa avelkkltli ygsnsygkst lcdvlrtlet pdttpikerk
       61 tipasaaqkv llsvsedgqp evslrfqdds wtdpvpyamk fsvfdsgfis rnlftgqdie
      121 rrnkealtqf vlgeqgviha eqiaaeskaq aqkkselkil ekgfngipni qafintkvse
      181 sevaveaaia qlnvsidrkq kqianahkiv trpelvdcrf aigagdainq lneslklslq
      241 avdeeakrkl elhisthmqq rsdaqqwirq gleftggnec pfcsqplgeq anelidvyrk
      301 sfnetfktkf aelstnmksa fdrfqkysgv tyeakiqanl ntiqlypela dsdsfkplps
      361 alekaavdlt ksadafnqlw ddiqpkmaql ietkrkiphd eiegldstpl llseeaigna
      421 vaeyneitqk indeitafkr sieidklnqe inshnvelgt fglkkrriqm datceeykal
      481 sekisdldlk ikkdqqelsq qqsaflakff ekinhyfvkf gsrdftistd taldakghqp
      541 vislivkfkg kkiptsqlvr vfsesdrral alsifwarls imtdeeknkt ilifddpvts
      601 fddnrisvtm meiqsaldkf cqaiflthyp klarhmlvdm rltgsmavlk ltkdangtgl
      661 ctgteedfie tehhrkykkl rsfidgardr eidsdlrvfl etevheryrq qifdnglnkc
      721 qlgelitgle saealteeqa krlhqfreal ngphhawssr spddwaslaq emlsfiycdl
//
LOCUS       WP_175861437             329 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175861437
VERSION     WP_175861437.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..329
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=35779
     Region          64..320
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mvgpqgarpy vdafpardsi vnatsprtwl ppyvarggas patsavpdtr addrpaanaa
       61 qaathserll aidqvsleyr sgarivrath qvsfdvygsd rfvllgpsgc gkstllkaia
      121 gfiepvsgsi aldgrpvsgp gpdrvvvfqe fdqlppwktv aenvafplrv aaklsrvear
      181 eralhyldkv glgtfadayp htlsggmkqr vaiaralamq prvllmdepf aaldaltrrk
      241 mqeellrlwd efrftllfvt hsieealvvg nrilllsphp grvraelnsh ehsldnvdtg
      301 dfrdnvarih rllfdtdaph vpttedaas
//
LOCUS       WP_175861457             300 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175861457
VERSION     WP_175861457.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 300)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..300
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32301
     Region          14..284
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mpmnpaptpa plceidglki gfrghdgtvt davrdlsltl apgerlgivg esgsgksltg
       61 rallgllpda arwsartmrf aghdllamsp rerrrlcgsq mgmilqdpky slnpvmtvak
      121 qmgeafrlhe pglrgralre rivdalaavq irdparvada yphelsggmg qrvmiammvs
      181 tgprlliade ptsaldvavs mqvlavldam iarhdtglmf ishdlplvms fcdrvavmya
      241 grvvetcaar dlrnashpyt rgllaanppl tnppdelpvl rrdpawlepa ppadrqeaar
//
LOCUS       WP_175861604             138 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175861604
VERSION     WP_175861604.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12015107
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..138
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=14186
     Region          14..>98
                     /region_name="DAO"
                     /note="FAD dependent oxidoreductase; pfam01266"
                     /db_xref="CDD:426168"
ORIGIN      
        1 mgfnplrvvv vgggivgasi awhlarsgaq vtplekqpaa aggathwsfg wvgtgsalpe
       61 farlarelgp lpvtargalv wldsdaqtaa lideqraaga awssiqagem rvtrlsssvs
      121 apdrnparhp teegrara
//
LOCUS       WP_175861618             483 aa            linear   BCT 11-JAN-2025
DEFINITION  TldD/PmbA family protein [Burkholderia cepacia].
ACCESSION   WP_175861618
VERSION     WP_175861618.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..483
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=51945
     Region          10..481
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 midenrapga ravqaaqtlr snadfwslri vdetidehav rndvaqpfsr trergamlma
       61 ragtgagyaa tpdlspaglq aaldiatara rasapwalvd hrqaarpqts gtyaspdvda
      121 alpsraewie rlahecaaan lgariveraa svmivdteqc yltsdgvrid qrfrflmpel
      181 havahgdgdt qtrslgqsgt laqggldvla rygfdgagar vadealqlla apncptgrrd
      241 lllmpdqmml qihesighpl eldrilgder nfagssfvrp emvghyqygs pllnvtfdpe
      301 paaeaasyaf dddgtparkq ylirngvler llggalsqqr aglpgvansr asswnrapid
      361 rmanlnvepg dqsldalvag tehgilmrtn tswsiddhrn kfqfgcefgq liengrltqv
      421 vkrpnyrgis aqfwrslrav gdagtfgiyg tpycgkgepa qiirvghaap acvfadvdvf
      481 gga
//
LOCUS       WP_175861637             123 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175861637
VERSION     WP_175861637.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..123
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13514
     Region          12..117
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 midvssitda fapsgeptqy rvspekliag dplhtltpgf aspcgrfstg iwestpgcwh
       61 vayteaeyce ilegtsvitd legnrktlra ghrfvippgf rgtwevvert rkifvaydeq
      121 ppe
//
LOCUS       WP_175861640            1063 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cepacia].
ACCESSION   WP_175861640
VERSION     WP_175861640.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1063
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113449
     Region          1..1051
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnlgrlsvqq pvlaivlsiv ltiagalayf slavseypdi apptvviqat ypgasaetvs
       61 qtvstpiele vngvedmlym ysqatsdgsl nitvtfkpgt dvdkaqvlvq nrvalatprl
      121 pepvqrsgvs vrkssptqlg tiflyspdqr ydplyvsnya irnvadvlkr iegvgdinpl
      181 gareysmriw ldpervasfg lspgdliaav raqntqlagg vvaqapitnq afqpnlifeg
      241 rlkrpedfsd ivvkqgkdgr lvrlkdvarv evgalayatd symlrhptia lqvlqqpgan
      301 avatmdavek kmaelardfp kgivynigyn ptafigdsih elvktiyeav vlvvfvvllf
      361 lqgwrpsiip ilsipvslvg tfaamaalgy sinnltlfgl vlavgivvdn aivvvenver
      421 hlsagagprd atlltmkevg galfaitlvl cavfvptsfi pgisgqffrq fgvtiavsta
      481 isfftsvtla palsammlka hardhdvpap asrmaapfap amrvarrfsn afnrvfqrls
      541 daygrlvrkv vriipamgvl yvvliaatgy llvsspkgfi paqdrgylvv lvrmpdgatl
      601 ertsavarki edialsvpgv arvpvfsgvn aatgtnsans aglfpvfqpw perkarglti
      661 dtiaaemrkr laavteasiv vampppvqgl gstggfamrl edrnglgtaa lakatqdlva
      721 aanrtpgmvg vytpysatsp qvhveldrek aemlgvpsqa indavetyfg styindfniv
      781 grtyrvtaqa dlpfrvgasd larlkvrnrd gemvpigsvt ridntlgvdr aprynlypat
      841 eingdtapgl gsgfaiktme slakqvlppg isfewtdlsy qqttagntgl lvfplcvllv
      901 ylvlaaqygs wslpvsilli vpmcllaasl gvralgqdvn iltqigfivl vglaaknail
      961 ivevarqlea dgtelveavv eacvqrlrpi vmtslafilg vlplvisdga gaemrqavga
     1021 avffgmigvt ffgllftpvf yvmvrrlalr kaavatiate vvq
//
LOCUS       WP_175861642             339 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Burkholderia cepacia].
ACCESSION   WP_175861642
VERSION     WP_175861642.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..339
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36840
     Region          11..323
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(16..18,48,53,79,142..143,183..184,207,236..242,278,
                     295..298,303,306..307)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(48,53,79,142)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 mslkdtlpad nrlgfgaapl gnmfrdipde eaiatveaaw argiryfdta psygaglaea
       61 rlgdalaghr rddyvistkv grvvldemed aktrdygeks gifargranr lvsdysadat
      121 lrsiedslkr lrtdrvdivw vhdiaqdihg dewlaqfeaa rkgafrvlgr lreegvigaw
      181 glgvnrvepi elvldlaepq pdgmllagry tlldheralq rvmpaaaaqn vgivvggpys
      241 sgvlvggahf eyrkappdiv akveriraia arydvpvkaa alqfvlahpa taavipgasr
      301 periaedsaa ltfdipadfw remreqqlva adaplpidr
//
LOCUS       WP_175861662             342 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175861662
VERSION     WP_175861662.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..342
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34557
     Region          13..334
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mnrildrapp gaafarlpgt fgaqfwlrwg aalafavvca vfaassplfl tvanlanvlq
       61 qsavvgilgf gltavliggg pdpirggldl svaanmglca avqavalrdg apdgaalalm
      121 latgaavgal nafavialri vpllatlttm nlcagfelvl tqntsvaaas pvltflidsg
      181 pfdiphlapa llivallfgv llhrtrfglr laatgahrda araaglrvna yvaasyvlsg
      241 vsaalaalas sallsgsspg agenllavva vallgvvfsr rlvptipgtl laalfvgivg
      301 ngfqldnvss ywvngvegal ilfvvattal irrrhtehha hd
//
LOCUS       WP_175861659             574 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Burkholderia cepacia].
ACCESSION   WP_175861659
VERSION     WP_175861659.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..574
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64437
     Region          5..491
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mttlisalsl qletghgplf qdltftvklg driglighng cgktslldvl agsrepgvgs
       61 vqyaamcrlq hveqhlpprl adlttreall ksvggqraeh wrvdsllddl elataadipv
      121 sdlsggqhtr lllgravlaq pnlllldeps nhldlpsllw lenflrrwqg gfilvshdar
      181 lldslsnrsw ilrdqrlysf dmpcsralva laeadataqa rhageqseid rlaasskrla
      241 iwgrehdnek lsrqaksmqr rveklkedqt fvsrgspwrl klqgrpfaad rlmafeglhv
      301 raqadepilf evhdlwlrpg dkvavlgsng tgkssllrqc wsdlqrgear mgwryhpaar
      361 iayydqslhq laddatlsda lykfapvgdr errqalisag fayvrhgqtv atlsggerar
      421 llflalsmas yhllwldept nhldmegkre laaalaafdg gfilvshdre liehscnrfw
      481 aihngrlqel pdaesayrnl ftsrepavpe qipttrnhtg vqstssdaea lwqrwcqlet
      541 llaaelvrkp khqkpqlqeq wreemrqler elgl
//
LOCUS       WP_175861676             587 aa            linear   BCT 11-JAN-2025
DEFINITION  fatty acyl-AMP ligase [Burkholderia cepacia].
ACCESSION   WP_175861676
VERSION     WP_175861676.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10148874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..587
                     /product="fatty acyl-AMP ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=62610
     Region          18..567
                     /region_name="FAAL"
                     /note="Fatty acyl-AMP ligase (FAAL); cd05931"
                     /db_xref="CDD:341254"
     Site            order(168,171..176,178..179)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341254"
     Site            order(195,217..219,292,295..298,323..327,332,385,445,456,
                     459)
                     /site_type="active"
                     /db_xref="CDD:341254"
ORIGIN      
        1 mtkcastihr liesledvag athrmtfvde agneagityr rfaeevfhqa galreldvre
       61 ndlvmlalpa svehavamma cvmtgalpct vpvparrata grqvidvace lyrprlviaa
      121 daqaaawhdd afpaastrvv dldtlsiaad agaralisak sghdphhvql tsgstshpka
      181 avlshenvia nvlgiggsvr fdiaagdgta swlplyhdmg lltllsnlhy rapllmmqpn
      241 sfirnplgwl kriasaratt tsvptfalry cvrrfnaaam egvdlsacrn ifiggervdd
      301 atlrdfaamf apyglaasal qpcygmaest lavsmhrawh egtvdgapyv iadtldrral
      361 ierrdaqpaa andgadtete tvlamgtpid gmafrilddg dhalanravg evairgtsvm
      421 lgylnpddgs iaapltadgw frtgdigyvs dgqlhilgrk keviiirgsn yfphdieeal
      481 ashrtlrkst ciafglpdpe tgterlvvai earpadatpq traecqqlla srigfaaqdl
      541 cfvepgslpr ttsgklqrlk crdlyangvl pvihtaaaae agqgaya
//
LOCUS       WP_175861683             310 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175861683
VERSION     WP_175861683.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34012
     Region          14..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,232,249,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,195,
                     226..230,237..238,241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mrssseklsg sisvfaavvd agtfaaaadv igmtppgvsr aiarlerkln irlfnrttrs
       61 vslteegrrf yeqvmphlag leeaaaaaag rasvvrgklr inldpvvyra ilgqqldafm
      121 dahpdleiel iardslgdlv mdgfdlavrf geprssslia rklldtgvvt vaapsyiarr
      181 grpakpedle nrshrclefr npetgkpfaw efhrrrkriv vdtrgrltvn dpgallsacl
      241 agsgiaqmll lgaepliadg rlidlfpewa deryplyayy psrhhvpakt rafldfmvel
      301 tgihghagmr
//
LOCUS       WP_175861706             388 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Burkholderia
            cepacia].
ACCESSION   WP_175861706
VERSION     WP_175861706.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..388
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=41492
     Region          40..377
                     /region_name="AspB"
                     /note="Aspartate/methionine/tyrosine aminotransferase
                     [Amino acid transport and metabolism]; COG0436"
                     /db_xref="CDD:440205"
ORIGIN      
        1 mhshrpvrlq hiagigvdrm gsiadhadvd llrlenldtd lpptsealaf treaiqrdsa
       61 nsylpfvgqd rlrasaaahv salsgqrfta dqvvvsaggl sgilntllat vetgdevivt
      121 dptyagllnr irlaggvpkq vpftftpgse wkldqtalra aigpktraml lmspsmpsgg
      181 ffdasdwqvi aslcvqndll lildsamerl lfdgrtvihp aglpgmaert vtvgaaskel
      241 rmigwrvgwi vapewlipdl vavslanvvv pvgiaqeaaa valehsasdl pgyvselerr
      301 rdtvaaelsg lpfgmpaggw smllrvadfg ltgsqmserl lrhgvcatam tgwgvahgeq
      361 yvrfvfsnep vdrlrtlgdk vrfaleda
//
LOCUS       WP_175861726             281 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [Burkholderia].
ACCESSION   WP_175861726
VERSION     WP_175861726.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..281
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30440
     Region          10..257
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(24,105,107,109..110,138,189,210,213,226,228,257)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 matltfpgqk vgdftitais dgyltasldf lsnidpadas nmqrdagqke peavhincyv
       61 vrgagrtvli dagaggfrqw ggqlrtnlar agiepaaidt illthahpdh vgglvngage
      121 iafpnaelvv hqrevgfwqd danlsraser argnflvarr vfdaygdrlr lfddgqvlpg
      181 idalpipght dghtgyvles rdqgllvwgd vvhfphiqiq rpevsiafdh daslaaatrs
      241 rlldqvsseg lliagmhlge rgfariertn ggyrlryere e
//
LOCUS       WP_175861721             311 aa            linear   BCT 11-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Burkholderia
            cepacia].
ACCESSION   WP_175861721
VERSION     WP_175861721.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..311
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=32212
     Region          78..284
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mrkhfraala aslmiaagvs gtlvapqsvl aqekaaarve tasgaapiva apaasngser
       61 pvpppepats atvenpyglg alwangdfva rfvlgllvvm slgswyvmvt kfieqarang
      121 raksadeqvw naptlaegaa qlddtspfrf iaenaieage hhdtalldsv drntwielni
      181 ersitsvsnr lqdglaflgt vgstapfvgl fgtvwgiyha ltaigiagqa sidkvagpvg
      241 ealimtaigl avavpavlgy nflvrrnksv mervrdfgaq lhtvllaggr raagriatpa
      301 aqapqalavq s
//
LOCUS       WP_175861735             488 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175861735
VERSION     WP_175861735.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..488
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51818
     Region          26..447
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(36..37,40..41,44,84,134..135,137..139,142,162,
                     165..166,169,283,286..287,290..292,295,322,326,377..378,
                     382,400,403..404,407..408,411)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mshshaasia aridrlpata siwtlvlfls vggffevydl fqmtylppgl irdgifhags
       61 hgvlgisdqg algaatfagl fvgemfvsrl adrfgrralf tgalllytaa slamcvqtha
      121 lgilvcrfia gcgigaelit igafltelvp kavrgrafal cfavgylamp vlalvswlwv
      181 phdplgmsgw rwvvllggsg avfvwwlqsr lpesprwlah tgreaeaeav lrrleqaver
      241 esgrplpavp tpvaaatata aprtpsmwda rhrgrttmli afnaflsigf fgfsqwlptl
      301 laaqgasvtk slwyafviaf aypvspfvag lladrverkw livasafgva lfgtafamsa
      361 qapfviafgl lvtlsntvla sngtayqsev fpteirgral gfvhsigrlt giassfival
      421 lleragvsav fvliggsmli vmvsigvfgp rtnnraldei adgaehaaal rglaeaptgr
      481 vdgrrklg
//
LOCUS       WP_175861747             477 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175861747
VERSION     WP_175861747.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..477
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47730
     Region          34..420
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(40..41,44..45,48,80,130..131,133..135,138,160,
                     163..164,167,291,294..295,298..300,303,331,334,387..388,
                     392,396,412,415..416,419..420)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mserapalgg apaaiapphr tslrailptv aaaslgfaiv qldvtvvnva ipslghsfgs
       61 svhglqwivd aytlsfaall ltsgtladrf gsrrlfaygl alfllaslgc alaaslaali
      121 aarvaqgvga amilptslal ithacandaa arvravawws atggaisaag ptlggllids
      181 lgwraiffin lpicaaglwl tvhhvrdsaa artrlfdpag qlvavlvlal ltggiiraga
      241 qgpgdpyaag alaasvalga lfvaierrva apmlqlaffr iarvpgvlai gaitnaafyg
      301 lifslslyfq nargftates glalapltii mlaniasarl avrhgfratv ivglavslag
      361 yvwlwrtlga htpyallapg laamaigggi aipaltstll gsveagrsat asailntarq
      421 vgaavgvaal galvagqgaa ivagaarafa vaavlvavci vlavrwpgda pepgtra
//
LOCUS       WP_175861777             266 aa            linear   BCT 11-JAN-2025
DEFINITION  Fic family protein [Burkholderia cepacia].
ACCESSION   WP_175861777
VERSION     WP_175861777.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..266
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=29364
     Region          2..>247
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mpnqtsalln tidadkatid aarplpqhtv aslrekllle wtyhsnaieg ntltlretkv
       61 vlegitvggk slrehfeatn hrdaivyved ivakaealse rqirnihslv lkgidaeeag
      121 ryrrenvvia gasttppdfm hlpaemaali dwyeaagdrh pveraaelht rfvkihpfid
      181 gngrtgrlll nfelmkagyp paiirkedrl ayydaldkac isgdygditr lvaesaqrsl
      241 dtyldvlglr htpapdtapp spgfrp
//
LOCUS       WP_175861831             308 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175861831
VERSION     WP_175861831.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34156
     Region          16..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          101..300
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(116..117,119..120,123,127,129..135,229..234,
                     240..241,243..244)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mmhpdlrrld lnlllvfdal yrhrsvaaaa helalspsal shalarlrda igdalfvrlg
       61 nemqptvrad diatwagdal damskglara rrfdpaqsdr tfvfaatdyt afavlpafla
      121 riqqvaprlr irvvhsdrki svdelaagri dfalgyhees aadapgiedf dwfsddyvvi
      181 asaahpdlrr rltldqylaa rhvvvtpwne srgvvdhvld rlglarqvav qlptvlaapf
      241 liaesallmt vpnraaqalr haapirifpa pfeiprytvk vyshakhart dahrwirtql
      301 learpepa
//
LOCUS       WP_175861846             271 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175861846
VERSION     WP_175861846.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..271
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28894
     Region          16..265
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtraalratg demscaavgl tlkagartll dgftqafrpg eiwcvagpng agkttllatl
       61 aglqppaggh vaidgrplsa wppaqlaqrr almpqqlhda fsatvfdtvl lnrfpylggw
      121 gwerdgdraa ardalatfdl talasrdvls lsggerqrva laatlcqdap lmlldeplah
      181 ldlhhqidcl talaawldag pravlfschd lnlarrfath allldgrgha wagpvhdvlt
      241 perasdafgy plvlirengr dallpawper q
//
LOCUS       WP_175861882             552 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175861882
VERSION     WP_175861882.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..552
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58887
     Region          18..538
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(31..32,35..36,39,77,135..136,138..140,143,163,
                     166..167,170,256,259..260,263..265,268,296,300,464..465,
                     469,473,489,492..493,496..497,500)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 matlggqish spmtgeekkv ifasslgtvf ewydfylags laayisksff sgvnptaafi
       61 ftllgfaagf avrpfgaivf grlgdlvgrk htflvtivim gistfvvgfl pgyasigiaa
      121 pvifiamrll qglalggeyg gaatyvaeha panrrgfyta wiqttatlgl flsllvilgv
      181 rtfigeeafs swgwrvpfva silllavsvw irmqlnespv flrikaegkt skaplteafg
      241 qwknlkivil alvgltagqa vvwytgqfya lffltqtlkv dgasanilia ialligtpff
      301 lffgslsdki grkpiilagc liaaltyfpl fkalthyanp qleiatqksp itviadpaac
      361 sfqfnpvgts kftnscdiak salakaglny envaapagat aqikvgdtvi payegkaada
      421 kaqgaafdkt lgstlkaagy pakadpaqln wpmtivilti lviyvtmvyg piaamlvemf
      481 ptrirytsms lpyhigngwf ggflpatafa ivaakgdiys glwypivial atfvigllfv
      541 ketkdsniya qd
//
LOCUS       WP_175861922             309 aa            linear   BCT 11-JAN-2025
DEFINITION  MlaD family protein [Burkholderia cepacia].
ACCESSION   WP_175861922
VERSION     WP_175861922.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..309
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=32705
     Region          1..289
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 menkshafwa glftialtla iagtvfwfnv drtvrvpydl lartnvtglf pdaavrfrgl
       61 dvgkvqsigf drahpgqiri rilvdhdapi tqstygslgf qgvtgiafvq ledtgrdlap
      121 lpsspktiaq ipmrpslfdq iqergdvllr qlelaaksan almspemreq lrataeslqh
      181 aadgaatltk qlgpavtalp etmhevnram asantllqpn gplvsnlnka gtaaeqvgva
      241 lndlnarvqy dtlprfnala gsvgdasrql kdvagelgrn prsllfgspg aapgpgepgf
      301 vwpgatagq
//
LOCUS       WP_175861931             546 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Burkholderia cepacia].
ACCESSION   WP_175861931
VERSION     WP_175861931.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..546
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58057
     Region          13..527
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 maaatptgal valhhvsfrf ddgvtlfdsl dlsidrtptg ivgrngvgks qlaqliagrc
       61 apstgtidrs tqvayvaqqh ddaaagprtv aqlaaldapl galarladgr aephdfdrvg
      121 drwdlaerlr taldaaglhd vradtpaqal sggqrarval igallsgagl lvldeptnhl
      181 dapgrawlra aldgwrgglv ivshdralla dvqriveltp qgvrsyggny afyraqrdad
      241 qdaaqaaldn araergrarr rleqehdtiq rhaaaslrda ktanlssgak qsrkgaarni
      301 mgqvrrhqnd fkatldervq qaaarveada pvlvslpgte vsarrqlftl eharlpwgia
      361 aaadgvtwsa sgpvrialtg pngcgkstll rmlagelapr sgtctthvsa ayldqrlall
      421 dpersiveql glldtplaeg elrsrlallq ldaaratqpa rqlsggerlk aalacalwrg
      481 tpaqllllde ptnhldlesv raieaalagf pgaivvashd taflaaldpt htmqwhrdgw
      541 ryepva
//
LOCUS       WP_175861962             546 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175861962
VERSION     WP_175861962.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..546
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58461
     Region          1..533
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mqydyiivgg gsggsslagr ladacpdati alieagshte rnllvnmpvg iaalvpfklg
       61 tnygyetvpq pglggrrgyq prgrgmggss ainamiytrg hpgdydewaq lgatgwgwqd
      121 vlpyfrraeg nergadawhg adgplsvsdl rfrnpfserf iqaahaagyp lnddfngatq
      181 egvgfyqvth rdgsrcsvar ayiygrnrpn lhvitdatvl rvtfdgkraa gvavarngrv
      241 etldaraevi lsagafnspq llmcsgigpa eqlrrhgiav vqdapdvgtn lidhidfiin
      301 trvnsselvg vclrgiakmt palaryfssr tgmmtsnvae aggfiksdps lerpdlqlhf
      361 ctalvddhnr kmhwgfgysl hvcalrpfsr gtvtlatgda rdaplidprv fsdsrdldll
      421 vrgtqamrri lsqaplasqg grelytradq seaelrktiv ehadtiyhpv gtcrmgsdah
      481 avvdpqlrvr gveglrvvda svmptlvggn tnapsvmige raadfivaar kggvsrgeaa
      541 aavhgr
//
LOCUS       WP_175862024             520 aa            linear   BCT 11-JAN-2025
DEFINITION  S41 family peptidase [Burkholderia cepacia].
ACCESSION   WP_175862024
VERSION     WP_175862024.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..520
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55407
     Region          72..418
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mmpstravlr lavcaaataa flpcaspvga qqpaparpas apaasssssa spatarppsp
       61 cppdwepqic elkaavevlk rqhltdvdig alldatthag irtlpyarff dakeeqerre
      121 derrardgtp gigivfetrp dglhivdvip dapaeqagvr pddlvvamnd tsvvgidadd
      181 ltklakgdag vplkltvqrg pshamlsfap vrtilkphpa takrlagdil ytrlssfpep
      241 avgayidavq aarragppvk gvildlring ggalnaaigi talyagrdrt amvtvergda
      301 nrrryttnwp dyalpvmhgq dplaplqadd wwrtvplvvl vdgqsasaae ataaalkdlg
      361 rakllgmpty gkglaqtgvd lidgtrlnft farnlrpngc pmdgygvvpd wlvpprrdsd
      421 vdgvllwyre adlprapyad rlapdpfakv rkerqklreq ralakidsak saalpqrefg
      481 tasdwqlgqa laalagrpvr tvdakpqlmp aqpvceragn
//
LOCUS       WP_175862039             266 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175862039
VERSION     WP_175862039.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 266)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 266)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 266)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..266
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29673
     Region          9..258
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mssprpypsl ltslkiqmrv vfaltmreii trygrhnigf awlfaepmlf tvgiaalwnl
       61 lhetgqghei nvtafavtsy stvlvwrnti grctlavepn aallfhrnvr vidlflarit
      121 leivgttlsm lvltstliai giidppadvl nmaagwvllc wysaalglli gglceyselv
      181 erlwhpisyf qlpvsgafvm aswlppnlrd iamlfpapnc velfrygyfg sqitpyydvp
      241 ytimvcaflt wiglavvrdv strveh
//
LOCUS       WP_175862077             288 aa            linear   BCT 11-JAN-2025
DEFINITION  hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
            [Burkholderia cepacia].
ACCESSION   WP_175862077
VERSION     WP_175862077.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..288
                     /product="hydroxymethylpyrimidine/phosphomethylpyrimidine
                     kinase"
                     /EC_number="2.7.1.49"
                     /EC_number="2.7.4.7"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008902 - hydroxymethylpyrimidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008972 - phosphomethylpyrimidine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009228 - thiamine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009229 - thiamine diphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=30456
     Region          8..248
                     /region_name="HMPP_kinase"
                     /note="4-amino-5-hydroxymethyl-2-methyl-pyrimidine
                     phosphate kinase (HMPP-kinase) catalyzes two consecutive
                     phosphorylation steps in the thiamine phosphate
                     biosynthesis pathway, leading to the synthesis of vitamin
                     B1. The first step is the phosphorylation of...; cd01169"
                     /db_xref="CDD:238574"
     Site            order(8,15,17..18,20,24,27..28,31,34..39,41,44..48,53..54,
                     56,58..59,62,65,69..70)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238574"
     Site            order(14,26,47,83,214)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238574"
     Site            order(108,145,181,211,213)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238574"
ORIGIN      
        1 mssnappivl tfglsdptgg sglqadlmtl asmgchgvsv ltgytvrdsa acdevtgldp
       61 dvvaaqarml ledmpvaafk igaatraevv saiaevvady dgvplvlapd ftlddehvla
      121 addlresiad llapqttllv adyatliala qpdgdaeapn ldaavshlls qgceyilsse
      181 tgshrlvntl ygeegqlred mwdrsphrlm gitdtlgaai aallangqep peavreaqey
      241 lhqavrdafr pgmgaylpdr ffwarsneda dtppavkvdp vprtshrh
//
LOCUS       WP_175862120             465 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54 dependent transcriptional regulator [Burkholderia
            cepacia].
ACCESSION   WP_175862120
VERSION     WP_175862120.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..465
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51403
     Region          1..118
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <139..438
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mgvdqrhviy ysrepndalr ghfdecgwrv dlaetvrdvr rvvqhgvata glldfspgfk
       61 psdlrelesc lsiqhigwia atrrgqlqda tlrhlirdyc fdyvtmpyet srivetvgha
      121 hgmvalteta appvgtgrse gemvgtcdam lglfrtirrv aatdapvfis gesgtgkelt
      181 avaiherssr ahapfiainc gaipstllqa elfgyergaf tganqrkigr veaanggtlf
      241 ldeigdlple sqasllrflq egkierlgah vsvpvdvrvi cathvdmdaa lregrfredl
      301 fhrlcvlkle epplrargkd ieilarhmle rfkgdahrrl rgfspdavas lygyswpgnv
      361 relinrvrra ivmsegrmit aadlelnefa tlapvsllea reaaerqaie qallrhrgrf
      421 adaarelgvs rvtlyrlmca hgmrdrgdtl tgfsaplqel phhac
//
LOCUS       WP_175862153             740 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cepacia].
ACCESSION   WP_175862153
VERSION     WP_175862153.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..740
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80721
     Region          58..740
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mryevlepgr smtkgarvar sgrgrwrpsl ylglliaahp aaafadaapa agaevrkeea
       61 tavkpaagel kaisvtgsrg vaddpavatv gkmplalrei pqsvsvttre ridqqnlysl
      121 devmqqsagv tvqpyvlltt ayfvrgfkvd sfefdgvpvv igdmasapqd isvyerveil
      181 rgangllhgs gnpaatvnlv rkrpqyqfsa nasvsvgswd ryraeadigg plnaagtvrs
      241 rlvaayedrh ffydhakqdt rsiygitevd vtrdtlltfg aqyqttrsvp dmsgvpmard
      301 gsslglsrst fldtawghfd wdttrvfasv eqklgagwka kvsgeyqsvr sdlkyagsyg
      361 aidpstgagg almggayrfs sysrsidanv qgpvhafglt hdllfgvtya nsssgqmsaq
      421 llgnvagmpv nvyrwnpssv pepgvgpyqq sqqndvsqkg vyglgrikla epvtlvlggr
      481 mswwnqdglg ahyntghqft pyggliwdfa rdwswyasya evfqpqtksm wgggiltpvk
      541 grtyetgvkg elaggklnvs laafridldn npqvdlahpc agpncyyvng gsvrsqgfef
      601 eangritpww svwasytydt mryadnlana gtfapllnpr hlfrlwtnyd lpwqerrwsv
      661 gggvqvqsny saqangvtms qggyalasvr lgyrydkhws aavnvnnlfd rkyylslsqp
      721 gwnnrygepr nvmltvrgqf
//
LOCUS       WP_175862159             209 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cepacia].
ACCESSION   WP_175862159
VERSION     WP_175862159.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..209
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21965
     Region          1..207
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msfqtwmlfa aaylattlsp gpnvllvirn tvrygthgta atiagnlvaq gvvvvlvalg
       61 vgavlaampp lfvamkvaga aylmvlgvrq lrgerkagas tgatevaapd cgklfrealf
      121 vsgsnpktmi flsafmpqfi vhdrplalqf vvmyatiact vvivhsiysa gvrrfhrgfg
      181 msravralkr asgllfvglg iklltarqa
//
LOCUS       WP_175862162             634 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Burkholderia cepacia].
ACCESSION   WP_175862162
VERSION     WP_175862162.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 634)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 634)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..634
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=67774
     Region          8..634
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mpqpfvlpat agrtdllaqa harstavglr aherpdfspl srialrelld tnhalfshar
       61 pvmenlhaqi adtqslvllt dadgvilhsi gdadfiekan rvalctgvsw aegargtnai
      121 gtalasgqav avhgdehflr anhiltcsca pifdpfgrtl gtldvsgdpr gssphtlalv
      181 rmsaqlienh lftnqcaeal rlrfhaheec vdslfaglva fgpdggliaa nrsaqfqlga
      241 sfdalqhqas dalfgmrfsq laqqaarapg amfrltlstg vrvlarcefa eahktavavt
      301 ppapaarvrt adpdaitfat ldtgdarmaa vlervakirg rdlpllilgq tgtgkewlar
      361 alhqasprad gpfvavncaa lpdslieael fgyedgaftg arkrgspgki vqadggtlfl
      421 deigdmplaq qvrlmrvlqe ravmplggar avpvdvrvvc athrdlrami aegtfredlf
      481 yringlavtl palaartdlp alverilarl arsepmprri aadvldaftr hrwpgnlrqm
      541 tnvlrtagml aededeitlt hlpddfwldc ddapaapssa apaasagphe gttlqhhqaa
      601 vidavlarhg gnvsaaarel glarntvyrh lrrh
//
LOCUS       WP_175862167             379 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Burkholderia
            cepacia].
ACCESSION   WP_175862167
VERSION     WP_175862167.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..379
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41966
     Region          26..362
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 mstpvtnhda faehapevlf rvvnrvalit lnrpaalnal syamigelaa mlercrhddq
       61 ivavvlrgag ekgfcaggdv ralyrmvaqr etwlpffvde yrldytihtf pkpvvalmdg
      121 vtmgggmgla qgaalrvate rskiampetr iglvpdvgat hflsrmpael elyvgltgam
      181 lsgadaltak ladlcvpsaw ldtfetries vkwegdalpl lrkvfeppcn vvphaaldgq
      241 mpwivrhfdk rstverivat ltqdlareel srehrqwlqa tldaltghsp tmlyvtreal
      301 lrgrqmtlae sfrmelgiva raieegdfce gvrahlvdkd rkprwapasl velraervrh
      361 fltspwklfa hpladlgea
//
LOCUS       WP_175862223             252 aa            linear   BCT 11-JAN-2025
DEFINITION  YoaK family protein [Burkholderia cepacia].
ACCESSION   WP_175862223
VERSION     WP_175862223.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..252
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=26629
     Region          11..243
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mpaqyfrnlt gkhrsananr qlgfslacva gaanaggfla vkqytshmsg ivsaiadqta
       61 lgdvrlalag isslgsflig ascsailvnw grrrglhsqf mlpllveaal lllfgllgsh
      121 lalwetffvp vtvtllcfim glqnatitkl sgaeirtthm tgivtdlgie lgklfywnrs
      181 aidvdahavv anrsklriha tmlssffigg lagaigfkhv gyvstvplaa vlvtlaivpv
      241 iddllalvrs kr
//
LOCUS       WP_175862224             402 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175862224
VERSION     WP_175862224.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..402
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=42120
     Region          4..355
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 msqkilivga gfagvwgalg aarvldsagv tgsdveitlv spkpelqirp rlyesgpqqm
       61 aapllpllda vgvkfiegsv eeidvrektv gvacadgekr liaydrlllt sgsklsrppv
      121 pglaehafsv dciedavald ahfaalaklp esparntvav vgcgftgiev atelpkrlre
      181 wfgpdaksrv vvigaqddig pdlgpnprpy vaeafdslgv eavlgsrvvs iaadgvrtas
      241 gthieamtvi waggmraspl aaqvsshlda lgrvavtadl rvadaphvfv agdvararcd
      301 ddghdalmsc qhaivmgqfg ghnvaadlig vptltyrqpf yatcvdlgew gavysegwdr
      361 qiklthaegk arkqmintqw iyppapnrad alaagnplas fg
//
LOCUS       WP_175862235             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175862235
VERSION     WP_175862235.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32408
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdkfsalraf vevaeaggfs sagrrldlaa ssvvravdal easlgtvlln rttrqvtlsd
       61 agamyyarak qlleelaead alvsdrgdep sgplrvsvpv aygvrriaph vaaflarhpk
      121 ldldlqltde rvdlvagrid vairlgeaap saevvartlg rfhryvvash dylaahgtpa
      181 epgelvdhac lrfhfggdqq awsfvdahgt aqvrvtgrlk snhsevlrda aldgagiall
      241 pdwlveadvq sgrlrrlfeq ydvtpgtars vvtalylptq rgskrvtafi dfvetlvrap
      301 h
//
LOCUS       WP_175862289             230 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia cepacia].
ACCESSION   WP_175862289
VERSION     WP_175862289.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..230
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24160
     Region          1..227
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mtaqwidipt gndsfggyla lpkrgtgpav iiiqeifgvn shiravadqy asdgfvalap
       61 dvfwrtqprv eltyegadrd kgiellkktd vglavadiga aadalrarpe vagklaaigy
      121 cfggqlayra aaagkldaav ayygggiqna ldlagkvtqp ilfhyaendh giplaavdqv
      181 kaafaghgha sfhvypgaeh gfnctdrasy nqrasalahg rtltflaehl
//
LOCUS       WP_175862305             537 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175862305
VERSION     WP_175862305.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..537
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53807
     Region          23..437
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,279,282..283,286..288,291,319,323,375..376,
                     380,384,400,403..404,407..408,411)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mdqpfsaast qsarrrawvl aavcmaaval plsfsggava tpaigrdlhg gtvamnwitn
       61 afmlafgscl maagaladqf grkrvfaigv ggftlmsval afapsmlavd llraaqglaa
      121 aaalaggtaa laqefdgaar trafsllgtt fgiglafgpv lagalighgg wrtifvtsav
      181 agglslgfgl prmhesrdph atgldwpgta aftaaltlft fgvieaparg wsnalviall
      241 agaalgacaf vaietrvarp mldlslfria rfvgvqvlpv stcccyivll vvlplrfigi
      301 dgfseidagw lmlaisapml vvplvaatlt rwltagvisg lglliaaagl vwldvalrgg
      361 agpaaiapml aigvgagmpw glmdglsvsv vpkeragmat gifsttrvag egialaivga
      421 vlaalaqtgl rqaagaagtp datlraaarl atgdlagaaa alpgvgqaal lasyahafdr
      481 lliglavvtv lcavvvfvfl ggrrvaaeag dgtdghahad vpvrsridaa ctethgr
//
LOCUS       WP_175862308             476 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175862308
VERSION     WP_175862308.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..476
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49556
     Region          21..476
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mqnrnttaag gepagaplsg daleavlvae lgdalvtraa didpryftay nepagarpra
       61 lvrprsvddv srtlalcarl gqtvvpqggl tglargaval ggevvlsmer fagvealdaa
      121 agtmtvragt plqtvqeaae aagftfgvdl gargscqigg mlatnaggtr airygmmreq
      181 vlgleaalad gtvvssmnrm lknnagydlk qlfigsegtl gvvtravlrl hpllaapata
      241 lcrvrdydav ialwnrvrtl pevvsfeamw pafydyvarr tpgvsapfvg ddgfavliec
      301 atsaprgdah qaletglaag ieaglvedav latserqard lwtlreglai dalphlvnfd
      361 vslptgelgv faerceaalr mqwpdavclf fghvgdgnvh igvslagmsd adadaldhcv
      421 yavvrdmggs vsaehgigvl krpylahtrs daeiglmrcl kaaldpggil npgkvl
//
LOCUS       WP_175862342             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175862342
VERSION     WP_175862342.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33825
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdnlgdirlf vetasqgsls aagrklglsp aaasarlvkl egelhtqlfe rstrklrltd
       61 egrlylvhcq halqtledar aalqagrasv sgalrvsats dfgrtvlrrw ldefnerhpn
      121 vtltlvlsds lshllqddid lairfgvpad ssmvakrmad nrralcaspd yiaahgmpnh
      181 pddlrehrfv vlssaagaan nwrfardget alftapldts rqtndgslar ewaiegrgva
      241 mksiwdigad lqagrlklll pewrcpdvpv nalfqrtlym aprvrtlldf lekqfsease
      301 alapflr
//
LOCUS       WP_175862368             320 aa            linear   BCT 11-JAN-2025
DEFINITION  1-phosphofructokinase family hexose kinase [Burkholderia cepacia].
ACCESSION   WP_175862368
VERSION     WP_175862368.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..320
                     /product="1-phosphofructokinase family hexose kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008443 - phosphofructokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33080
     Region          4..306
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 mteivtvtln pavdvstsve hivdthklrc arprrdpggg ginvartvhr lggdcvalyl
       61 aggptgdvlt llleaehvps vrlriagetr envcvtetat greyrflmpg plvttaewrd
      121 caariaalqp aprylvlsgs lppgapddly atlartaaan gsrvvvdaag palraaldag
      181 vhlvkpslde lsalagepld easacrkage lvaqgradiv altlgargaw vvtreralrl
      241 pgrpaavcst vgagdsfvgg miwalargvp fddacryala asaasvehpg talctredve
      301 rihaelvaqa rgtamargaa
//
LOCUS       WP_175862406             463 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175862406
VERSION     WP_175862406.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..463
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48632
     Region          24..458
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(31..32,35..36,39,71,121..122,124..126,129,149,
                     152..153,156,277,280..281,284..286,289,317,321,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 meiaetfgde gfdiprryfa availvgvfm saldsaivni alptistdlr vsaasviwva
       61 ngyqvasaat mltcaslgsr igerrfytig lvlftiaslg cglastfgal vamrvlqgis
      121 yailisvgyg lyrvifppas lgtifgvnal vfavgtavgp algglivswa swpwlffinl
      181 pfgiaaiafs fvalgkdthr ergfdvpgav tsaaafglla lavdqigrws nrtvlvlava
      241 aavlmlafcv gqararhpll pldifrsrry tfavltsvtm fvsqgmalva lpfvlqhtya
      301 ysvlksalvf tpwpiavalc apfagrlanr fnatqlssvg vlmfclgigs limlpaqpsv
      361 vdflwrvalc gvgygfflpp nnkemfanaa knrtatasgv lstarttgqs igaalvavvi
      421 alvsgasgge gerqfpvyvf alacaiaals ffasvariyr qrg
//
LOCUS       WP_175862457             352 aa            linear   BCT 11-JAN-2025
DEFINITION  permease [Burkholderia cepacia].
ACCESSION   WP_175862457
VERSION     WP_175862457.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..352
                     /product="permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=36874
     Region          61..346
                     /region_name="YraQ"
                     /note="Uncharacterized membrane protein YraQ, UPF0718
                     family [Function unknown]; COG0701"
                     /db_xref="CDD:440465"
ORIGIN      
        1 mtttrtqpnp algwmtflli avaglfyvkw fpyynkafva aehhsigqsi lmgtsaaape
       61 pslkaaldya waygkaiwqa mvlglllgsa vqallpahwv arvlgrtgfg svaaggllsl
      121 pgmmctccaa pvvaglrarh aspggavafw lgntvlnpaa lvfmgfvlgw hwsalrlvlg
      181 vamvfgigyl lnriarpeda riddaqlaal aaeqaaagnp fvrwmkllar mavrlvpeyi
      241 vlvlllgaar awlfphigpd ignhlgwiva favagmlfvi ptagevpiiq amlslgmgvg
      301 paaallmtlp pisgpslaml arsfkpymla ivailvvvfg iasgllaval gf
//
LOCUS       WP_175862466             170 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia cepacia].
ACCESSION   WP_175862466
VERSION     WP_175862466.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..170
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=17092
     Region          1..170
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mkksilaava laalstsafa agtgtinftg eivagacgid sgsvnqtvnl gkvptnvfkq
       61 agdkstptnf dikltdcdts vaqnayftft gtssagqpkl latigsatnv girlqaasge
      121 yldngaeqka ptvlqngtnv arfaamyeat aagvtpgtae gvanftvryq
//
LOCUS       WP_175862534             356 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia cepacia].
ACCESSION   WP_175862534
VERSION     WP_175862534.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..356
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38640
     Region          1..340
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfvfdedqe aladsvkrll mtemtpelir elwttptgrs ddlwalfasq gltavsvpea
       61 hgglglseae wallaqtygy fgspeplldt alvsagvlar lpasdwrdal lrdiadgrar
      121 valvhpvnpy aadvhvaqtl lcehrgelhr vdpaqcawra vdsvdpsrrl ftldwepsaa
      181 triagadeaa plldraldhg afavaaqllg ltqrvldvai dysaqrkqfg kaigsyqalk
      241 hlladvairy efarpvvara aqaiaddhpq ravfvshakl aatsaaqlaa rhsmqvhgai
      301 gytweldlqi fmkriwalsg swgdsafhka rvadailgda lpigpaqtfd leetrq
//
LOCUS       WP_175862578             958 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia cepacia].
ACCESSION   WP_175862578
VERSION     WP_175862578.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 958)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..958
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..958
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=104241
     Region          42..957
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mknhglsrrg flkasvlagv avyvaplgsr afaalfeekl ltpvkwdsvt gipqfridgi
       61 akvtgskvfa rdvraadmph wpqqqshali lrvtqadrty egfdlsllgd elkpdrvvta
      121 ddlvrdgvaf pafygddmll pagktpaylg havailiyhd farfrfakna lkfrddviry
      181 gavtgplerd pwgtfryvrv ggktaydddv ysslkdapif psmmrkhlpv wpdgkehgkl
      241 deqgmflagr iadeldhpsa dwlvfdreyn tqsvdtsale pdnancwyda atqslhlvvp
      301 tqsplevaen aaamvakcrf pvkklfvhpc ytvgygskdh fnvpfyglvc alyadgrpvr
      361 fandryeqfq tslkrhafkm hyriavdrnt gllqsfkgdf eangggrsnf spsvamvgat
      421 aaqsiyyfpk sdlaavaias raidagsarg ygtlqsmaat emavdeiaaq lnidpidfrl
      481 rnalrsgmkn tqgaipagal rvdevlersk qhplwtrraa rkaeyeaanp gkrygvgfac
      541 vqkdfgtgae asfakvefde ngkvslrhta aeigtgmsts qavavvkwlg rpatdvqvav
      601 tewpdlpvet sgdpyimsqa dqdrlsanpr wspsyaspss atnsayyfth streaaravf
      661 ryglwpaams iwtrglgggq aapytiried arwvdgklta dgleplsfeq lakqahalgl
      721 ptgavvhvfn rwqwtdaefe vggvvdrlpi dglslrvgap ktgdngpvpg taapagatam
      781 rgtleptang yrvldrkrvf ipptsrnnaa vtyytavgtl velavheatg kvellthhsi
      841 mecgnqispq lvsgqlqggl amgighalhe ylplyedgpg ngtwnfnryq lprasdvavw
      901 tqtgdvlppl setdppkgva evvmipvvga ivngiahaig hrftdlpvtp qkiqevla
//
LOCUS       WP_175862579             237 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia cepacia].
ACCESSION   WP_175862579
VERSION     WP_175862579.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..237
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=24759
     Region          61..231
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mttaqtaasa asasaaatga sapaqasavp dsapasapav papapapaav erplvrfqsk
       61 plsiningks vgpmqvpegl mmieflheya gltgsrlgcg qgichacvvi vdkpdgtsee
      121 mrtcitgahf fhgrtirtie ghakrneage vvelspiqqk flehfsfqcg yctpgfvnaa
      181 tvlierlkre pvakadvert itealdahlc rctgyvryye avkdvvlttp glvkdaa
//
LOCUS       WP_175862596             377 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia cepacia].
ACCESSION   WP_175862596
VERSION     WP_175862596.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..377
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40217
     Region          1..366
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfsftdeqq qfadalrryl geqygfdarq aivrsdagvs ntqwsafael gltalpvpda
       61 qggfgggpvd mlvvmqelgr alviepywat avgvealria gsgagedaal leavaqgqkr
      121 vavafhepha rydlfeldth areqggtyrl tgtksvvqhg aqahawivpa rvddggiglf
      181 vverdaanak vadyrtidgq raatigfnet parlltggar daaaleqvad yatfllcaea
      241 vgaldelnra tveytktreq fgmpiarfqa lqhrmvdmli haeqarslty laavryasgd
      301 adarrkavsa akarvgaaar fvgqqavqlh ggmgvtneva aahlfkrlti iettlgdtdh
      361 hlariaalpd faqadaa
//
LOCUS       WP_175862602             243 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alanyl-tRNA editing protein [Burkholderia].
ACCESSION   WP_175862602
VERSION     WP_175862602.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V.
  TITLE     Evolution of aminoacyl-tRNA synthetases--analysis of unique domain
            architectures and phylogenetic trees reveals a complex history of
            horizontal gene transfer events
  JOURNAL   Genome Res 9 (8), 689-710 (1999)
   PUBMED   10447505
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Cusack,S., Hartlein,M. and Leberman,R.
  TITLE     Sequence, structural and evolutionary relationships between class 2
            aminoacyl-tRNA synthetases
  JOURNAL   Nucleic Acids Res 19 (13), 3489-3498 (1991)
   PUBMED   1852601
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Schimmel,P.
  TITLE     Classes of aminoacyl-tRNA synthetases and the establishment of the
            genetic code
  JOURNAL   Trends Biochem Sci 16 (1), 1-3 (1991)
   PUBMED   2053131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..243
                     /product="alanyl-tRNA editing protein"
                     /GO_function="GO:0002161 - aminoacyl-tRNA editing activity
                     [Evidence IEA]"
                     /GO_function="GO:0002196 - Ser-tRNA(Ala) hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004813 - alanine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006419 - alanyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=26353
     Region          3..243
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
ORIGIN      
        1 mttqalfred ayltqcdavv lavgedgirl drtvfyplgg gqagdtgtlt lpdgstiaia
       61 dtrkakfdga tpddavhvpa pgqearvaal vpgtrvaaei dwlrryrhmr lhtaahlmca
      121 vlpyavdgcs vtadyvrldf atsdpidrdd verrlaglvv gahpvttewi tddemagrpd
      181 lvrtmsvkpp mglgrvrllr ieqvdlqpcg gthvrntaei gelriaklek ksartrrlvl
      241 efa
//
LOCUS       WP_175862635             416 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175862635
VERSION     WP_175862635.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..416
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43089
     Region          24..402
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(34..35,38..39,42,74,129..130,132..134,137,157,
                     160..161,164,236,239..240,243..245,248,272,276,329..330,
                     334,338,354,357..358,361..362,365)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mtdsvpdpsp lsplpvnlfr hapfqrfwgt rvmsslafqi lsvaigwyvy althsafalg
       61 lvglaqfvpm faltlvvgqv adrydrrria ticqaveala agvfllgaaq gwlaapavya
      121 laaivgtara fespsvssll pavvprsdlp ratalstsan qaaqilgpaf ggllygvgap
      181 vafgtsvvaf avaavlsgti plrsappare pvtlrsvfsg iafirrepai lgalsldlfa
      241 vlfggttall piyardilqv gpwglgalra apavgalagt lwltrfplrg rpgramfggv
      301 iafgiativf glsrnfvlsl valaalgasd vvsvvvrlsl vqlrtpddml grvsavnslf
      361 igtsnqlgef esgvtaawwg apaaivvgga atiavaltwm rlfpqlatmk slerda
//
LOCUS       WP_175862638             551 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia cepacia].
ACCESSION   WP_175862638
VERSION     WP_175862638.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Gournas,C., Athanasopoulos,A. and Sophianopoulou,V.
  TITLE     On the Evolution of Specificity in Members of the Yeast Amino Acid
            Transporter Family as Parts of Specific Metabolic Pathways
  JOURNAL   Int J Mol Sci 19 (5), 1398 (2018)
   PUBMED   29738448
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Vangelatos,I., Vlachakis,D., Sophianopoulou,V. and Diallinas,G.
  TITLE     Modelling and mutational evidence identify the substrate binding
            site and functional elements in APC amino acid transporters
  JOURNAL   Mol Membr Biol 26 (5), 356-370 (2009)
   PUBMED   19670073
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146941
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..551
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59525
     Region          31..470
                     /region_name="AA_permease_2"
                     /note="Amino acid permease; pfam13520"
                     /db_xref="CDD:404414"
ORIGIN      
        1 msqaglrans tsdveatish dstghtlhrg ltwkdafwvt sgvpagvlft iggvcatigq
       61 pawaiwiaai tmgliqsaty aeisglfphk sggasvygai gwvrysklia pvsvwcnwla
      121 wspmlalgcg laasyaltsl fpanaavlhw qlkvadlgfi kpglslrina tfiiatilll
      181 itfklqhsga skaartqril giasltplli vgivpfvtgd vpmsnllpll plghdahgnl
      241 ttatfgswng qgvtmalgam fmagwasygf etavcytref rdprrdtaka ifwsgalclv
      301 vmtlvpmafq galgtqamld psigdgtgva aamakivggg awvanavvvm lmlsillivm
      361 tsmmgssrtl yqasvdgwlp kylshvnehg sptramwtdl gfnlvllmms dymtvlsisn
      421 vcymlfvfln lqsgwihrmd rgnwdrpfrc ptwllvagsi cgyanlvyvg aganlqgegt
      481 lrngliamll ivpvflfrhy wqdrgrfptq mqcdmelevp kramwlnlmp yaalvgaglt
      541 iwlsyyfawv k
//
LOCUS       WP_175862654             319 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Burkholderia cepacia].
ACCESSION   WP_175862654
VERSION     WP_175862654.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..319
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33449
     Region          <148..310
                     /region_name="PRK14959"
                     /note="DNA polymerase III subunits gamma and tau;
                     Provisional"
                     /db_xref="CDD:184923"
     Region          239..317
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mwsglrlltr hgggggvnra rqrdgsridr yaflfmsamw ractrmgerg kagamstaaf
       61 gtrqatgvrg aagdrvrrrg trvasvfaav cvlhaalfvl laheqivrre plqrqvmvat
      121 liaaapeast taaakakpva asravqeats aprssagsvs rmnrqvasgr prppahdapv
      181 paptqsgpsl paaaqrdtph ddtaarmptq tqaqtqpesr sssvsapprf vahpdcalvk
      241 pdyppqslrl gehgtvlvel etdaagqiva arvvtgsgyp rldaaareav lasrcaphvf
      301 dgapvptrar apiafnldd
//
LOCUS       WP_175862674             799 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia cepacia].
ACCESSION   WP_175862674
VERSION     WP_175862674.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 799)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 799)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..799
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..799
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84492
     Region          83..762
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mirrpkaagk ggamrrerra rhggamrgal lgpalgaial fglstasara qqpadgtaat
       61 ggavppaava vaqeapqapa vtlptvvvvg ttpllgigtp lqkvpanvqt vraaeldaqh
      121 ratladffaa nlqsvtisea qgnpyqtdvn yrgftaspll gtpqglsvfv dgvrvnepfg
      181 dvvnwdilpt qaidrmqlip gsnpvygrnt lggalaittk ngksnpggea evsggswgrk
      241 taaieqggti gsnldyyata nvandggwad hnasrvrqaf gklrytdsdt tlsisaggad
      301 nalygtqtip rsfldnrkqa ytypdlnrns agyltlsgdr ffgehvelsg nayyrhlrnt
      361 nissnnntdy gsvgddgtvd avqgtnaqst ivtdsyggsl qltllgklgg manqliagva
      421 advanssyva ssqdayftdt raaigvgdfe pqtraktrna nlgvylsdal sltphwtltv
      481 sgrydwskaq igdesgvqpl ldgnhtfsrf npalglnwnp vagftayaty negmrsptai
      541 elacadpaap cslpndfiad palkpviskt feagmrgrig aattwsaaay rttltddiqf
      601 isspasaqgy frnvgdtrrq gielagrtrf gplgvglsys yvdatyrssw tehspansaa
      661 dangnvavkp gdhipgipah tvklrldyaa tprwdiganv twrsgvyarg dennqdvngr
      721 isgyvlvdld mryritkrfe vfasvtnlfd kryasfgvlg qnffngpnht fdganpvneq
      781 fvgpgaprga wvgvryawd
//
LOCUS       WP_175862755             220 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: OmpA family protein [Burkholderia].
ACCESSION   WP_175862755
VERSION     WP_175862755.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..220
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22836
     Region          117..218
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(120..121,154..155,158,162..163,166,208,212)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mnklalalal sttalaacst asgptfsase lqprdgvrtf qvdchgllsg petcmkaark
       61 icgeepvrav dsaralrdks dpatlvfqcg aaqaeaaqaa apaaavveqv nlsgdalfat
      121 dhatlaptar esldrllser adhtysqvsv tgftdsvgsd dynlalskrr aesvaaylka
      181 hglktdsltv sgrgkadpva snatpegras nrrveirlqh
//
LOCUS       WP_175862760             321 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: PDR/VanB family oxidoreductase [Burkholderia].
ACCESSION   WP_175862760
VERSION     WP_175862760.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..321
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34489
     Region          11..224
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(52..53,55,69..71,77,79..80,121,223)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(52,54..55)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(77,80,83,90)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(113,117..120,122)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(118..119,142..144,196..197)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          237..321
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 msaatltvrv arkwqeardi cgfefvsddg splpgfeaga hidvhlpggl vrqyslcnhp
       61 ehadryqiav lrdadgrggs raihdevrqg dtlrigmprn qfplapdaph hlllaggigv
      121 tpilsmaerl fssgtpfdmh ycarstdrma fverinaagf rdrarlhvdd gapeqrfdla
      181 avlaaapagt hlyvcgprgf mdavlnaare rnwaearlhy effggavass gadrafqvri
      241 assgmvidvp aectviaala angvdvltsc eqgvcgtcat rvlegepdhr dsylteaeqa
      301 agdqfmpccs rsrsdllvld l
//
LOCUS       WP_175862771             449 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NCS2 family permease [Burkholderia].
ACCESSION   WP_175862771
VERSION     WP_175862771.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..449
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45929
     Region          14..443
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 msatdtmpar apanwlerrf alaargtsvr tetiagvtsf laaayllvvi psllatggme
       61 rgaattativ vfvlfttlmg lyanlpflvg pgiggsviig vtlattehvg wqtglgiacv
      121 sgilffllti lgargvvmkl ipvqiklglg asiglfvtml glrnagmvva naktnafalg
      181 dfsrpgalva liglavaivl qarkvpgail iailvaaaag vplgvthlpa sfvslphsia
      241 piafkldigs alslaaapyl faffaaeffs tlgtalavga kanlldeqgn lpninrpflv
      301 dslaatigpv fgipaltali esaagveagg rsglsslaaa vlfaamllfv pvalaipkea
      361 tapaliligl smfatirhth fddftdalpv msmvlltlms nsfgtgiagg llcyvlvkll
      421 agrrsdvswg lvvlalplgy yfwtvvkph
//
LOCUS       WP_175862781             390 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia cepacia].
ACCESSION   WP_175862781
VERSION     WP_175862781.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..390
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42715
     Region          12..282
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 midgqillgh sirwgmvggg lgsqigyshr saalrdgsfq lvagafdidp ergrqfgvkl
       61 gvaaercypd yatmfdaear rpdgiravsi atpnsthfei craalnaglh vvcekplcft
      121 teeaealqrl sveknrivgv aygysghqmi eqaremiarg dlgeirivqm qfahgfhseg
      181 veaasaaarw rvdpkfagps yvlgdigthp lyisevmape lkirrlmcsr qsfvksrapl
      241 ednaftimey dtgavgyvws savnagsmhg qkvrvigaka svewwdehpn qlryevqgqp
      301 aqvldrgmgy lhphalredr igaghpeglf eawsnlyarf alamdaadrg daaalknirf
      361 pdvhagvegv rwvencvrsa daggvwvdyr
//
LOCUS       WP_175862827             374 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Burkholderia cepacia].
ACCESSION   WP_175862827
VERSION     WP_175862827.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..374
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37521
     Region          17..364
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mtgfidtftl ggpgptiaik dtidiaghpt raasralada ppaaqhadvv rllldagwqi
       61 agkanmhela fgmtgindyt gtpvnpqdat ripggsssgs aslvglravd aalgtdtggs
      121 irgpaaccgv aglkptfgrv srrgvapadt tldcvgpfar dirtlaavma aiapgfdraq
      181 aaasvagcti aqirveadpa iaaaldaavr asglrshalv ldeipasfaa gltvinaets
      241 rafghlvdtg klgadldarl rtaatttpaa laeaeavrar ftaqvdaale ladvlvlptl
      301 palpitlqqa rdgvsviams slirpfnlsg hpalslplpl agsplkaglq ivgrkgader
      361 vcaiaahfea alaa
//
LOCUS       WP_175862832             454 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175862832
VERSION     WP_175862832.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..454
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48036
     Region          22..426
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(35..36,39..40,43,83,141..142,144..146,149,169,
                     172..173,176,258,261..262,265..267,270,297,301,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 myptdtvqsp saarpladrq lrriviasva gnamewydff vygtaaalvf ghvffppgas
       61 plagslaafa afalgfvarp lggivfghvg drygrkaslv wtllimgast faigllptya
      121 qvglwapaal vvlrllqgia sggewgggvl misenappeq rgyyaawsql gvgggfvlss
      181 aaflaaqalp ddmfrtwgwr lpflasiaif aigiyirrhl pesrdfeqag rrgahthlpi
      241 vecirrhpke illamglrva enggayifla fslvygkyvg ipngvmltgv miamivemga
      301 mlawgrlsdr igrkpvylig alslvacafp ffwlldtrat plvwlaltvg tavshgamig
      361 tlpalvgelf stevrysgva lghevasifa ggmspliata llaryhaswp vslflvalgl
      421 vtvatlcvmr etrivraasa apaapatgtr gdta
//
LOCUS       WP_175862838             279 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175862838
VERSION     WP_175862838.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..279
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30797
     Region          9..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          105..270
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 madapdnllg aylrdrrekl dpaalglpat rrrtpglrre evaqrahvsa awytwleqgr
       61 ggapsadvld rlaralllnd aerehlflig vghppevryh atdhvsprvq nvldsleasp
      121 aivrsatwdv vawnnaaaat ltdyatlspe rrnilrlifv dphvrgvqan warvaqfavg
      181 afradvargg atqavqafvd emratsaefd alwrdhdirs heegtkeihh pavgrialey
      241 safavsgrpd qtlviftpet addrariral vaarekyei
//
LOCUS       WP_175862862             331 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)H-quinone oxidoreductase [Burkholderia].
ACCESSION   WP_175862862
VERSION     WP_175862862.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..331
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=35108
     Region          1..325
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(40..41,123,127,130,148,151..153,172,176,191,
                     215..216,237..238,240,263..265,314,319)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mkaitfkefg eaevlqlaev papevrpddl lvrvhaagvn radlthrrgg ygrpnfgdst
       61 lmgleiagev ietgsavqgy evgdrvmgvv gggayaelar idwrmampip atidyvhaaa
      121 ipevfvtahe allhlgrlqr gdsvlihaaa ggvgsaavql ayatgatifa taeaskleri
      181 vqlgvdhaid ykaqdfsevv asrtgkrgvd vvidfvgapy fsrnvaslan ggrlvqvgil
      241 ggggdvsval dqilyrhlqi igtvmksrdp rekhamvrrf rehwldrfag gaglepvvds
      301 vfpladaaaa hrrmesavnv gkiiltmsen a
//
LOCUS       WP_175862863             311 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175862863
VERSION     WP_175862863.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..311
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34182
     Region          7..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,219,
                     221..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdkvhtmsvf akvvemgsft avanhldttv gnisravsvl ednlntrllq rstrrlvvtd
       61 agrrfyersi ailsdierae aeardallep rgvlrvhavp glgrqlvsqa vlayrnaype
      121 vsvdlmlsqr mpnlleeqld vaiviartlp dsayvsqkig vshcvlaasp eylahrpapa
      181 cveelvdhtc vllstvdyap dewrlqgrag eavyrpagsh fsvndmdams tvlregagig
      241 liaafsaidd lrkgslvrvl pefhtaqrnv yavyssrqfv dakikrfidv lklrvgdrle
      301 ayaeelaitv v
//
LOCUS       WP_175862877             145 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia cepacia].
ACCESSION   WP_175862877
VERSION     WP_175862877.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..145
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15412
     Region          23..136
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mtrtvdsgvi ffarlalaal flwggvmkll gysdfiaylh gmnvpyqqvv apivvaiegl
       61 gglllivgyk vrplallmav ytiatamvgh nfwdatsaav qhdmvihfwk nvaiaggfll
      121 lfvtgaggas idalrrpsss ygvlr
//
LOCUS       WP_175862885             344 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cepacia].
ACCESSION   WP_175862885
VERSION     WP_175862885.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..344
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36181
     Region          109..316
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mkivkpllia aavaavlsas ttafaagadt vrpdattstf laalngqkgp gletlspaka
       61 rqvlvdaqng tkldlsgidv snrtieqdgl svpvtivrpq gatgtlpvfv fihgggwvlg
      121 dfptherlvr dlvvqsgava vfvnytpspe ahypvainqa yaatkwvaah gaeigvdgsr
      181 lavvgnsvgg nmaavvalma kdkggpairf qglmwpvtdh nfntgsynay qqghfltrpm
      241 mkwfwdaytk neaqrneiya splrastaql kglppaliqv aqfdvlrdeg eaygrkldaa
      301 gvdatttryd gtihdfglln alagdaptka atkamanela trlk
//
LOCUS       WP_175862904             453 aa            linear   BCT 11-JAN-2025
DEFINITION  uracil-xanthine permease family protein [Burkholderia cepacia].
ACCESSION   WP_175862904
VERSION     WP_175862904.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..453
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46052
     Region          9..423
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mshdpiptpv darlpawqla lfglqhvlsm aaspitavfl iakvlalpad ltvqligatf
       61 facgigtllq slgagpigar mpfvmvpgga ptmlfagiaa qsglptaaga allasafywv
      121 llpvftrclr lfprivvgam lllvsinlir iyativvgqp gsadfaqpra lglalativa
      181 tvivagafrg tlgrlavlig ltagatlgwa ldampaladv wrgplfthpv wlpfgmprfd
      241 vlaalpllif taismaeata qtvavgetcg kpislsrdvp ktirgdglas lagalfgtpl
      301 ivtsaenigv vqttgvrsry vtaaagaili vialfaplar layaipaavv ggtalvvfam
      361 igvmgirlla gvdlharanq ytlaaalvvg lapilvpnly rhfsspvqiv lgngmaagtl
      421 aaiatqlafa afarlsgqas atpvaassps rdg
//
LOCUS       WP_175862963             356 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia cepacia].
ACCESSION   WP_175862963
VERSION     WP_175862963.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..356
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38413
     Region          12..265
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mttpfparlp pllrnalrpl ldpyrryrha klihaarval ailvsialst glnvphgews
       61 titvlivvgg lqhhgnirkk aaeralgtsi galaglglil lysaahapia iyllmalacg
      121 icayhaigka gyiallsait mvivaghgdn eivdglwrav nvligiaial afsfalplya
      181 tyswryklad alracaavha rvagdrqvsd dahlkemaal sallvqlrsl mpsvskecet
      241 smtqleaiqr slrlcigyle ilssavptrd dvaareymrv dmkavnrrir dtlvgasral
      301 kfgtpsrlap rrrpadpphd apppqlsgyv sitaklavev dqlreklldt aqswni
//
LOCUS       WP_175862983             240 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175862983
VERSION     WP_175862983.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..240
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=25402
     Region          1..235
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 mailemlgfg tegwggvlll aalmtialtl aalavgavig agiaaaklsr hrsarvfgdl
       61 yttvfrgvpe llviylfyfg gstlvttvgq wfgaegfvgv ppfvigalav gmisgayqae
      121 vyraavlavs kgeleaarsi gmprsmvlrr ilipqvlrfa lpgignvwql slkdsalisv
      181 tglaellrts qiaansthqy fvffvaggal ylvmtglsnr vfnraeaivg rsfrrnfarn
//
LOCUS       WP_175863037             251 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175863037
VERSION     WP_175863037.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..251
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=27256
     Region          38..246
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mhdplaappd apahpadals apgplpalst lfgqcawfrt lapehqalvl aqsrveqcea
       61 gdviarrlap seywigvhrg llklaifnas grgctfsgvp sggwfgegsv ikrelrkyev
      121 vaiqrstvlf vpvdtfhall dtslpftrfv ihqlnnrmge fiasiqnsrl ldvdarvaqs
      181 laqlfnpdly pdtgpslsis qeelgmlvgv srqrinqalq qleklgvlrl aynqievvdl
      241 galarvgmeq i
//
LOCUS       WP_175863056             288 aa            linear   BCT 11-JAN-2025
DEFINITION  MOSC domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175863056
VERSION     WP_175863056.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..288
                     /product="MOSC domain-containing protein"
                     /EC_number="1.7.-.-"
                     /GO_function="GO:0016661 - oxidoreductase activity, acting
                     on other nitrogenous compounds as donors [Evidence IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=31073
     Region          1..281
                     /region_name="YcbX"
                     /note="N-hydroxylaminopurine reductase subunit YcbX,
                     contains MOSC domain [Nucleotide transport and metabolism,
                     Defense mechanisms]; COG3217"
                     /db_xref="CDD:442450"
ORIGIN      
        1 mpaiaelfvy pikscagial sraqlletgl aydrhwlitd pagqmitqrt hprlalirta
       61 lnsdalvlsa pgmreirtpl dgdvspatpk maatvwrdtv daidtgaeta awlteflgtp
      121 aklarfapda rrgcnrkwtg eidthtqfad gypllvigqs slddlnarlt akgapaipmn
      181 rfrpnivvsd ldayeedfve hldtegaapv rlrlvkpctr cpmptidqvt gapdpawphe
      241 ptdtmqtyra npnfggeltf ginaivvdga ggwlevgqsl eaeigfgd
//
LOCUS       WP_175863059             355 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175863059
VERSION     WP_175863059.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..355
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38983
     Region          1..353
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mdklivddlh lsyganpilk gvsfelkage vvcllgasgs gkttllrava gleqpsdgri
       61 qldervffdg aqrvdlpveq rslglvfqsy alwphrtvad nvgyglklrr vapaeqkrrv
      121 qtaldqlglg hlaerfphql sggqqqrvai aralvynppv illdeplsnl daklreeara
      181 wlrelivslg lsalcvthdq teamamsdri lllrngrieq egtpaelyga prslytaefm
      241 gsnnridarv aavdgervtl agdgwelqal ardafapgqd aqavirlerv qvadgpganr
      301 lqadlvtsmy lgdrweylfh cgemrlrafg hvprtagkhw iefptndcwa fakag
//
LOCUS       WP_175862958             241 aa            linear   BCT 11-JAN-2025
DEFINITION  ZIP family metal transporter [Burkholderia cepacia].
ACCESSION   WP_175862958
VERSION     WP_175862958.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Dempski,R.E.
  TITLE     The cation selectivity of the ZIP transporters
  JOURNAL   Curr Top Membr 69, 221-245 (2012)
   PUBMED   23046653
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Guerinot,M.L.
  TITLE     The ZIP family of metal transporters
  JOURNAL   Biochim Biophys Acta 1465 (1-2), 190-198 (2000)
   PUBMED   10748254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..241
                     /product="ZIP family metal transporter"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24382
     Region          27..235
                     /region_name="ZupT"
                     /note="Zinc transporter ZupT [Inorganic ion transport and
                     metabolism]; COG0428"
                     /db_xref="CDD:440197"
ORIGIN      
        1 mtptaklall tlppvlaacf galaaawrap gpttssviqh ftggivfaaa alellpqdra
       61 halfpvvvgf vlgialmlai ralsgaietr fedarlpvsl vivtaidlvi dglvlgiafs
      121 asdesgiilt valtlevlfl alsvsavlaa agigrmlsiv vpvglaalls vaavagnaaf
      181 aglptniyaa llglgtvall ylvteellve ahevpetpfa taaffigfiv ffliegsvka
      241 g
//
LOCUS       WP_175863102             673 aa            linear   BCT 11-JAN-2025
DEFINITION  BCCT family transporter [Burkholderia cepacia].
ACCESSION   WP_175863102
VERSION     WP_175863102.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..673
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73083
     Region          3..503
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mpdsrpsprt tfkpqvvlpa lavigallvv callpseaga lfsagqqwvv ahfdwfyvla
       61 vtgflvflvl iaasdfgnir lgpddaepef sfvswtamlf aagmgiglmy fgvgepmqhf
      121 lkpptvdpgt paaareamlm tffhwgfhaw aiyglmglvl ayfgfrynlp ltlrsglypv
      181 lreringwig htvdafalvg tvagiattlg ygvmqisagl htvagwdtgs nafriglval
      241 vvilaglsaa sgldkgvrrl selnlllafl llafvavtgp tafllralgd nigqylsslv
      301 dlsfrtyaya spreegwfgg wtilywawwv swspfvgmfi arisrgrtir qfvigvllvp
      361 tafnlvwmtv fgnsaiwldt hgaagalaqt atnvdallfr ffdflplsqg lsiaaivlia
      421 vffvtsadsg afvidqiatr ghahspvwqr lfwaallgvt aavllvaggl galqamtlia
      481 alpvaiimia lcyglwrgla adrvhysqdv apatsfwtgq hwrhrlthil rqtteaearq
      541 fvaetvepal rkvadelrag gvdahvqrds ddavrltvpt adhrdfvygv rvtvksaaaf
      601 lvretagpea arthvygivt ffedgrlgyd veylrgdevi advlrqyery vslaadkrth
      661 llsrapghat eae
//
LOCUS       WP_175863113             541 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia cepacia].
ACCESSION   WP_175863113
VERSION     WP_175863113.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..541
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57725
     Region          20..463
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpgqgnahps vplsrsahpd aghgkfkkql sltdltfigl gaifgsgwlf aashvstiag
       61 pagifswllg gfavlllgiv ycelgaalpr aggvvrypvf shgpllgylm gfitliafss
      121 liaievvaar qyaaawfpgl taegssdptt igwlvqaall cfffylnyss vktfakanni
      181 isifkfivpl sviavlftff kpanltvhgf apfgmpgiem avsaggiifa ylgltpivsv
      241 asevrnpqrt ipialilsil lstliyvllq lafigsipta mlaggwhdis kaftlpyrdi
      301 alalgvgwla vmvvadamis psgcgniymn atprvvygwa ktgtffkvft rvdeasgipr
      361 aglwltfgla ifwtmpfpsw ealinivsaa lvlsyavapv svaalrrtap dlprpfrasa
      421 fgitgpasfv iaalivywsg wstvswllgl qivmfviyla crrwvptahl slaeqvrssa
      481 wlisfyaami vlsylggfgg tgrlahpydt vvvaavalvi yywgantgvr sdklqlddde
      541 d
//
LOCUS       WP_175863143             184 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia
            cepacia].
ACCESSION   WP_175863143
VERSION     WP_175863143.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..184
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19776
     Region          42..177
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtdrlppfdp asatdaqkav ladilsgprg nlngpflgwi aspelaqhaq klgafcryrt
       61 glplrlsela ilvtaarwrs qaewhihhpi aleaglpaat adavrlgvap afesdddali
      121 hafaselyds rrvsdatfar aqarfghetv vnlvallgyy alvamtlntf gmradgqtel
      181 pfpe
//
LOCUS       WP_175863164             523 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175863164
VERSION     WP_175863164.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..523
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52388
     Region          37..448
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,157,
                     160..161,164,288,291..292,295..297,300,328,332,384..385,
                     389,393,409,412..413,416..417,420)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msqsspasra gaaaaprtgg rmpaaatlav asatcslivl dtnvvavslp siarsfhasf
       61 adiewvvsay mtafaacllp aggladrfgr krmlgaglal fflaslgcgv apsagwliaa
      121 ravkgggaal lltaalavia nrfpegrera rawaiwgmcm giatavaplv ggaitqwigw
      181 rwvfllnlpv cmllaagarv aidesrdpha krvdaagsll fgaalacaia aligapshgw
      241 lsaatlgrla laaalfaafv gaerwqarpm idlalfrqpr fvgavlamfg yaacaqvmmt
      301 flplylqnaf gmsaidaglg mlpfafamia gpslgaalaa rvssggvlag glaligagnl
      361 ataaltaagd yrlvaigmfv tgcgagimng dtqkaimacv psnrtgmasg istttrfsai
      421 vtavgvlgav laastqarld rllsaapglr afadapfmss llagdlaral ervppsaaga
      481 lakaapvafa sgfadaltvs gvlalvvavv ackllaqpmr dga
//
LOCUS       WP_175863167             359 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Burkholderia cepacia].
ACCESSION   WP_175863167
VERSION     WP_175863167.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..359
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40118
     Region          12..194
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(15,17,102)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(49,101..102)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            100..102
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 msaharrpll slvvpfhdea etidaffaat lpilesvdti rfeivcindg srddtldrli
       61 diaagdprvr ivdltrrfgk eaaltagide atgtavilid adlqdppali pamverwlag
      121 aevvaakrtd rmcdplmqrv aaalyyrvhn rlsevempen vgdfrlmdrq vvdalralpe
      181 rrrfmkglfa wvgyrteiie ytraprsggr skfsgwrrwn falegitsfs tvplrvwtyi
      241 glafaalsfi ygtfivmrtl lfgnpvhgya slisvmlfvg giqligigvi geylgriyhe
      301 skqrpvylvr rryraqrdaa ahpaskllqf plkrthaarr rtplpataag hgarkvsvk
//
LOCUS       WP_175863179             191 aa            linear   BCT 11-JAN-2025
DEFINITION  glycerol-3-phosphate responsive antiterminator [Burkholderia
            cepacia].
ACCESSION   WP_175863179
VERSION     WP_175863179.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..191
                     /product="glycerol-3-phosphate responsive antiterminator"
                     /calculated_mol_wt=20227
     Region          9..185
                     /region_name="GlpP"
                     /note="Glycerol-3-phosphate responsive antiterminator
                     (mRNA-binding) [Transcription]; COG1954"
                     /db_xref="CDD:441557"
ORIGIN      
        1 mdkslgarla rhpviatlyg aeqadsfvds aaevgivanv dlrrlqavva alaragkfvi
       61 vnidscdgls qdkggveyla digvaslvst rvatiqranr aglitmqkvf vtdrstwprs
      121 mkaieqsdpn lvqlmpapml ahlseadrqa lppivasgfv gnaddvrsar rhgalavsts
      181 dstwwnfdps s
//
LOCUS       WP_175863209             421 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia cepacia].
ACCESSION   WP_175863209
VERSION     WP_175863209.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..421
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46007
     Region          1..225
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
     Region          237..373
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
ORIGIN      
        1 mtkhirivrg dtafdaylal peagrgpviv llqeifgvna eirevadlya aegyvviapd
       61 lfhpfgsnie lgygeadhak afdyytrldv tgavddirat vahartlpes tgrvgvlgfc
      121 lggklawlaa aqgdvdcavg yygvgieqsl elaeriacpl alhfgaddpl nppetvtair
      181 aaldgkpnak lyvyegagha fsrngptfvk aaamsahtrs lavfrkvlgp dydlgaladh
      241 hfhlefaard peetmrtmvp epyvnhvptm tggtgytelk rfythhfvhn npadmamapi
      301 srvvgvdrmv defiltfthd reidwllpgv aptgkrveip mvvvvafrgp klynehiywd
      361 qasvlvqlgl ldphglpvag vdvarklrde tlpsntlmar wreseparsg ydivigkkrr
      421 v
//
LOCUS       WP_175863227             330 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175863227
VERSION     WP_175863227.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..330
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36812
     Region          3..327
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpraailayd dcyasslggf adilqianah wrrqrgdgna qfewrfvspt gkpvmasngl
       61 qlntepirpr ekfdlvfips ahyasgrafd rllarqsaac dwlvsqwnag aylaanctgt
      121 fvlartglld erpatttwwl adqfrsrfpr vdlqlepvvt eadrlicaga sasyllqtih
      181 vierfcgaai aaqcaktmli dvsqtkqlpy lplladkeha dslvhraqyw lqknmtkdvk
      241 msemahelgv sertiirrfr aalnqpplry lqnlrieaar glleagdlsl eritaqvgys
      301 dtssfcrlfk dkvglspgay rdrfrpages
//
LOCUS       WP_175863247             302 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cepacia].
ACCESSION   WP_175863247
VERSION     WP_175863247.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..302
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31516
     Region          14..260
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mqteieapgp agplkgtlls pgsddapvvl ivpgsgptdr ngnapngvqa styrllaegl
       61 rdegiasvri dkrgmygsas aipdaddvti deyaadvrsw vtairartga srvwllghse
      121 ggwvalsaar qmddidglil vstagrplgp vlrqqlqsnp anapilanam silesleage
      181 rvdaaridpa lmplfrpqvq rflmseltld paallagymk pvlivqgard iqvavqdael
      241 lkqanpqaem aliadanhvl ktvrtsalqe nlaaysnpdl pladgvvaai safvhaatas
      301 rg
//
LOCUS       WP_175863257             281 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia cepacia].
ACCESSION   WP_175863257
VERSION     WP_175863257.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20139405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..281
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30378
     Region          <41..120
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
     Region          153..274
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 mdqyedfivr tmsadevams iewaaaegwn pgrhdpscfr eadpagffvg vwrgepvacl
       61 aavayderfg figlyivkpg frgkgfgiri wqhgmrylad rnigldgvva qqanylksgf
      121 alayrniryq grvdgigcah vtaaadvpfe qllaydrqcf paararfvsa wiaqpdaval
      181 vtvdagriag ygvvrrckag ckvgplfadd agvatglfra laarmpgevi vldvpetnpa
      241 avalaerhgm tsvfetarmy tkdappiaie rvfgvtsfel g
//
LOCUS       WP_175863341             304 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175863341
VERSION     WP_175863341.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..304
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32597
     Region          14..284
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mpmnpaptpa plceidglki gfrghdgtvt davrdlsltl apgerlgivg esgsgksltg
       61 rallgllpda arwsartmrf aghdllamsp rerrrlcgsq mgmilqdpky slnpvmtvak
      121 qmgeafrlhe pglrgralre rivdalaavq irdparvada yphelsggmg qrvmiammvs
      181 tgprlliade ptsaldvavs mqvlavldam iarhdtglmf ishdlplvms fcdrvavmya
      241 grvvetcaar dlrnashpyt rgllaanppl anppdelpvl rrdpawlepa shagapadrq
      301 eaar
//
LOCUS       WP_175863364             329 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175863364
VERSION     WP_175863364.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..329
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=35786
     Region          64..315
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mvgphgarpy vdafpardsi vnatsprtwl ppyaarggas patsavpdtr addrpaanaa
       61 qagthserll aidrvsleyr sgarivrath qvsfdvygsd rfvllgpsgc gkstllkaia
      121 gfiepvsgsi aldgrpvsgp gpdrivvfqe fdqlppwktv aenvafplrv aaklsraear
      181 eralhyldkv glgtfadayp htlsggmkqr vaiaralamq prvllmdepf aaldaltrrk
      241 mqeellrlwd efrftllfvt hsieealvvg nrilllsphp grvraelnsh ehsldnvdtg
      301 dfrdnvarih rllfdtdapy vpttedaas
//
LOCUS       WP_175863355             244 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175863355
VERSION     WP_175863355.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..244
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=25569
     Region          6..244
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 maaddsllal lafddggygr vfagafaltf gvaassfctg vllgiagalg klsrhaplaw
       61 larlyttlvr alpellclll afyalapave valrrgglvp dgfafppflv aalslgfiqg
      121 ayltdilraa lvnvpigeie aahaygmtpw qtftrirlpa aarlalpgvg nvwlnatkda
      181 sfisvlgsft dllkasqlaa gatrhyvffy lvtaalflll siastgifav lerhanrgtr
      241 rata
//
LOCUS       WP_175863386             707 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia cepacia].
ACCESSION   WP_175863386
VERSION     WP_175863386.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..707
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=79638
     Region          1..694
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 maiqsdlrft ftagnesfev veftlhegls etfllqvela sanpaidfge vldrngllti
       61 gqggqpvryv hgaissfvqr dtgfrrtrys avveprlarl klssdwrifq tlsvpeiata
      121 vlkahhqtld yeqrvtnehl areycvqagd tdyefieril reegffyafq hkadghrlih
      181 cdrlfifgrq qgepviynpt pggdqpqpsl rtfaytenvr tarqvqrdyt fkspryphey
      241 pregtdldhq grgyarydyp grykheasgk aftqdrlrgh rrdarvarvt gddarlqpgi
      301 afdltghsre dmnrgwrpvs lvhhgkqyts qaeegadaqq gthyryeaal vpddaewrae
      361 plprpridgp qpvtvvgpeg eeiytdaygr vkvqfpwdre gkydehsscw iqvaqnwaga
      421 twghmaipri gqevivvnld gdpdqpliig raynrlqlpp yelprhktrm tiksqthkge
      481 gynelrfede kdqeeiyvha qkdqnihvnh dettfvgndr seqvehdeti aigndrketv
      541 ghdeqvtigq drrhdigqdd flsigrnhti htgkdrteev gnhrrdktaa nhtmdigghl
      601 tqrvqghael eagqairqrt kayeiqaael levkgpggtv ridnggitle gvairvkgpm
      661 tqnsggaqna lalpaaprtg qgmdracamr adgscprkpc pcgkgav
//
LOCUS       WP_175863398             297 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175863398
VERSION     WP_175863398.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..297
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32320
     Region          25..280
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mvkttmsdap esaapgddes sggassylvp glerglrila efsarepvlg apelskrigi
       61 prtttfrllq tlealgfler vngdryfrlg vgvlrlgfey lnsleltdlg tpvlerlrdt
      121 tglsthllir dqrdvvfvak aqsnasmfgs vkvhvgprlp ahatvhghvl mgdltrdalr
      181 qlypekrleq ftertpgtvd elyervrhya rlgyavseaa fesgisavta pvrdhsgsiv
      241 aaitatvprs eigeageker lveavcgaav dlsqrlnyrp lesdptfaha rhkvamf
//
LOCUS       WP_175863407             468 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175863407
VERSION     WP_175863407.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 468)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..468
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49360
     Region          <229..467
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mhtlmlalrn lqrnrrrslt tllamivgvs aillfggfsr ditlglqtdf vqrsghlqiq
       61 rqgyylygtg dpaaygirry aalidllrrd pqlapllqvv tptlqfggia gnfaagvsrt
      121 vmgfgaipdd qyrmqqwnay gfplrprafa lrgsaddaav vglgvarvlh lcgplhvadc
      181 rdappgpaap aatgpdasap advlalaqge agsqpagdga thievltasa ggapnvgrfs
      241 vvkaeqqgvk elddvylavc lpqaqrlvyg gaepratale iqlartadlp aararieqll
      301 rggfdgqpld vvdfatlnpf ydqtnrmfsv ifgfvfvlis aivlfvisnt mstaiiertv
      361 eigtlramgm rrggiqalfv cegallgvag aslgvlaala iaaavnhsgl awtpparida
      421 valtvrvwge wrtiavtfag lacvaglsaw lpsrhaarls ivdalrhv
//
LOCUS       WP_175863413             304 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175863413
VERSION     WP_175863413.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33215
     Region          10..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..295
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(111..112,114..115,118,122,124..130,223..228,
                     234..235,237..238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 msrrdpmagl hvfmtvatag nftraaaalg ltpaavslai gqlegelnvk lfnrstrgvs
       61 lteagqhywr qteaayrqvv hardalrdar sepsgvlrvt alplartlvi apvlavfrer
      121 ypkvrleiry enelvdiakd gfdagirlad rlqpgtigvr iapalscalv aspgylaryg
      181 tpasiaaler hacirfrfse sgrlhkwllh dgrrevdldp egvfvtndad avidaaragv
      241 giafafmrer ieqdlragtl vevlpgacrt lppmwlyyvn rkhvpaklra fidvlrerdg
      301 agaa
//
LOCUS       WP_175863501             532 aa            linear   BCT 11-JAN-2025
DEFINITION  multicopper oxidase family protein [Burkholderia cepacia].
ACCESSION   WP_175863501
VERSION     WP_175863501.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..532
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=57604
     Region          85..532
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mirrtflsra igvaaaslfa raawaqhagh agmdsmddmp gmsdmsgmag hgqhgksapa
       61 alaaadalpa gaplaalrtl anesrdpgtf ratlvaqpva rpmlhgarpt tfwqfgagtq
      121 gpvvgplidv regdtveikf vnklpqpsti hwhglpvppd qdgnpsdpva pgasrvyrft
      181 lpkgsagtyw yhphphmmta eqvfrgltgp fvvraaddpl agwpernlfv sdlklardgt
      241 iapndmmdwm ngregqfvlv ngarrpridv agderwrvwn acsarylrva fddgrafeha
      301 gtdgglfdap rrvtslliap geraellvra gdrasravlr aaeydrrkms mshddghgsl
      361 ppdpalalad vafspatarv lpttlravps lgepvahkev afgeemdmda mmkggahgrp
      421 agmrftingd tyaphratlt sragdverwt irngtdmdhp fhlhgtqfqv ierasggsrt
      481 sepfrawrdt vnvrsgetvt ilvtqdmrge rmfhchileh edlgmmgtlk vv
//
LOCUS       WP_175863500             459 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia cepacia].
ACCESSION   WP_175863500
VERSION     WP_175863500.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..459
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49145
     Region          13..457
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mtqqqrsfdn ivareqglrh altsgqmami aiggaigtgl flgsgfaigl agpsvlvsya
       61 igalialllm galaemtvah ptagsfgaya ehyvgplagf lvryaywfav vfaigteisa
      121 iavfmkywfp avpgwywvig fsalliavnl asvtlygtve yafsllkiaa ivvfivlgay
      181 lvwsapvasg igfanytahg gfmpkgpwgt wvavivaifs ymsieavaia ageardpqha
      241 vtrafrstvf rlvlfylltl slmlaivpwt qagtdespfv kvmaathvpy aagvinfvll
      301 iaalsamnsq lyvttrmmfs lsrarlapav fgrlgtngvp raalwistsg vavaaalval
      361 apdtaftvmm aiamfgalft wlmifvthlr frsryrgpal afrmwghpfg sllgaglvaa
      421 ilfttaftre frmtmvvgvv fvvlltlaya lhyrhehar
//
LOCUS       WP_175863483             191 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Burkholderia cepacia].
ACCESSION   WP_175863483
VERSION     WP_175863483.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..191
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=20468
     Region          4..135
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(9,11,72..73,76)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            11
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(71,116..117,119..120,124)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(77,82..83,112,115..116,119..120,123,126)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(101..103,112..113,116..117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(101,117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(125,131..132)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          147..188
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
     Site            order(148..150,182..183,185..187)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 msrtfayarv stsdqttanq lreieaagfs vdkrrvvses isgsvsadqr pgfaqllvkm
       61 eegdvlivtk ldrlgrnamd vratveglae rgirvhclal ggvdltsaag rmtmqvlnav
      121 aeferdllie rthagiarak aegkamgrps alsneqravv lreldagasv aalarrfgts
      181 rqtimrvrda v
//
LOCUS       WP_175863548             392 aa            linear   BCT 11-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Burkholderia
            cepacia].
ACCESSION   WP_175863548
VERSION     WP_175863548.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 392)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..392
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40779
     Region          37..390
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mtqlfdtlgf vdasaaragt vaphdaaaaa aaggaavsle qvgkvfatpr gqaaalrdvt
       61 ldvrrgevfg iigrsgagks tllrlvngle rpssgrvrvq gvdvgalded glvalrrrtg
      121 mvfqhfnlls aktvfenval plkiagvpka ervrkvdall elvglaakrd aypaslsggq
      181 kqrvgiaral vhdpevllcd eatsaldpet tqsilallad inrrlgltiv lithemevir
      241 avcdtvavie qgevvetgpv wrvfgdprhg atrallstlv hdlpaelaar vqplleqaal
      301 pdgaqvvldv rytgesggep dvgalaaalg gsvrflhggi eriqghaqgr lviaatprad
      361 dagqpaargg avaallerar rhanhaevlg yv
//
LOCUS       WP_175863567             371 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia cepacia].
ACCESSION   WP_175863567
VERSION     WP_175863567.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..371
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39542
     Region          5..349
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,236,303,323,325..327)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,103,110,183,186,188,236,243,303,323,
                     325..326)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(27,103,183,186,188,326)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mtqdplfqpl qfgaltlpnr ivmppmtrsr asqpgdeane lmaayyaqra saglivsegt
       61 yiaplgkgya wtpgihtpsq vagwrkvtda vhaahgrifa qlwhvgrlsh tsllggaqpv
      121 sssplqakgv nvfiagedgs tpgfvqasep ralsvdeire ivdqyraaar haieagfdgv
      181 elhgangylv nqfidsnant rtdqyggsle nrlrflrevt qaliegtgda srvgirlapl
      241 ttlngcvddd pettylaaak llgelgvgyl hiaeadwdda plmplefkqq lraaypgvli
      301 yagaytaera reaiaagwad lvafgrpfva npdlperlrt gatlaphdrn tlfgggargl
      361 tdyptlaqaa a
//
LOCUS       WP_175863573             308 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175863573
VERSION     WP_175863573.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33533
     Region          9..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mhrtgmtele vvlavarrss frgaalelgm sttavssava glearlkvrl fnrstrsvsl
       61 tdagqryver iapalaeirs agedaaagpd tpsgtlrina pqgaahlllg plfhpyaqry
      121 pdvridivse srlidivaeg fdagirlaea vpqdmiaval srdirmlvva tpeylkrhgt
      181 prhprdllkh qsigmrmahg giyhwelern gqklqmdlpv rfalnelaai kqailfglgi
      241 gfisewfige eltsgalvpv lapwcpsfgg lrlyysghrf vparlralid lahelrltda
      301 plsvgrkg
//
LOCUS       WP_175863592             255 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175863592
VERSION     WP_175863592.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..255
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27502
     Region          6..244
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 msgnvvksaa rvfevlelfs alqrplsvre iatrcgypgs saaalltsmk algylsydda
       61 thayaptarl vnlgealvds aagsrrhwha vakrlalrth eavviavqsd lyvqyidave
      121 gshtipiqfy apigtrreic msglgwalls lqpdstirrl vsrsirrigk sgrtidedvv
      181 ldkveqtrrl gysysahtvt qgaamismvi adgwnglpla mgvagpveri earrdaivra
      241 mrealdaqrp daasg
//
LOCUS       WP_175863610             393 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia cepacia].
ACCESSION   WP_175863610
VERSION     WP_175863610.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..393
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=41818
     Region          4..393
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 mqsfqvrvla dgkvalqtie aaseadvrar iaaqggvald irrarlarrk rapkfalalf
       61 lqelstllda glvliealea lrdkndagka skqvidrils vmyqgqplsa alarqpdvfp
      121 gllvatiass edsgqlpavl kryqqyevri eqirkrvtga liypavvigv giaillfmaf
      181 fviprfavvf eslttlppta qamlwwatll rengaavgma vaaaavgagl avrsaaakra
      241 vqrlmwrapk mrdvcalfal trfyrtvgll iaggtpvida lelsgkvlpa hfgarlaaal
      301 telragrsvs tvfaahaltt svaerllrvg eqsgdlggmc ehiaqfhdga ldrsiemisk
      361 vfepvlmlav gatvgavvll lympifelag svg
//
LOCUS       WP_175863619             282 aa            linear   BCT 11-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Burkholderia cepacia].
ACCESSION   WP_175863619
VERSION     WP_175863619.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..282
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31347
     Region          11..263
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mtsiedrvaq avtpeliaaf reegavcikg ifspdevaal ragidanlaq psprakvasr
       61 pddpgwffed fcnwqhnday rdfivrspap svaaalmgte nvrlhhdhll vkepgtrqrt
      121 pwhqdqpyyn iegddnvsmw ipvdpvples tlefvagshr gpwlmprtfm dkeakwfpeg
      181 sladlpdieg draafpirhw alepgdmvcf rmltlhasgg tqnrrrafsi rfvgddirha
      241 prrwktspdf pglaeqlpdg apldhplfpv vwssgagqag vl
//
LOCUS       WP_175863635             382 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175863635
VERSION     WP_175863635.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..382
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41017
     Region          1..370
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masismrrvq kaygdhapvi rdvdleigah efcvflgpsg cgkstllrmi agledlsage
       61 lsidgrrvdd vpaaergvam vfqsyalfph mtvyenmafg lklarvpkae idrkvrdaar
      121 ilqldtller kpkalsggqr qrvaigraiv repgvflfde plsnldaalr gqtrieiarl
      181 hrqferasvv yvthdqteam tladkivllh agadtaqhgs iaqvgapldl yhhpasrfva
      241 gfigsprmnf lpavvtacda rrtavtltps setftlprdg salgagatvt lgirpehltl
      301 gaahdattla rdvalverlg eqtyvhldqp gghsliakvp gdaqvrsger vlvhapaaac
      361 hlftedgrav pacadvhvhh ya
//
LOCUS       WP_175863636             663 aa            linear   BCT 11-JAN-2025
DEFINITION  beta-galactosidase [Burkholderia cepacia].
ACCESSION   WP_175863636
VERSION     WP_175863636.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 663)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 663)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 663)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448998
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..663
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=74135
     Region          1..622
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
ORIGIN      
        1 mrlgvcyype hwpesmwadd arrmkalgie qvriaefaws riepspgeyd wgwldravdv
       61 lgaagleivm ctptatppkw lvdrhpdila igadgrpraf gsrrhydfss ptyleasrqi
      121 ctavaerygr hpavrywqtd nelgchqtvv syspaalvrf rawlkarygt idalnrawgt
      181 vfwsmeyrhf devdapvgtv teahpshrld yrrfasdeva ryhrmqvdvi rahspgrpva
      241 hnfmqlftef dhyevardld vatwdsyplg aleeqwfapd vkarwlrtgh pdfasfnhdl
      301 yrgmstlpfw vmeqqpgpvn waqwnpaplp gmvrlwswea fahgagcvsy frwrqapfaq
      361 eqmhaglntp dnrldeggre aqrvareiaa vrdagadadp ngavrapval vfdyeakwlf
      421 evqpqgadfh yprfafeyya alrslgldvd ivsahapldg yrlvvvpplp vvpddfaarl
      481 aasgahavfg prtgsktvdl qipptlppgp lasilpvrvw rveslrpnvt eridgtlcdg
      541 aplagharhw rdfvelhddt rgvvrarfad ghpacvshgt lhywaapfdd attarlfadv
      601 aaeagltptp lgdgvrvsrr ggltyvfnyg dtphtidavp psafvlgsaq vgpqdvavyr
      661 srs
//
LOCUS       WP_175863651             312 aa            linear   BCT 11-JAN-2025
DEFINITION  GGDEF domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175863651
VERSION     WP_175863651.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 312)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..312
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34474
     Region          44..311
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mtaappslsd lviervgfgl fvldramtvl mwnrfmqdhs gipaadvigr nlfdcfpdlp
       61 rawlsrkles vfqlgsfafs sweqrpylfr fehdrpitgg vdymqqdctf mpltrgrdve
      121 avcvtisdvt hvsvmqrere eavaklreha nrdgltgian rrffearlgd efarwqrygg
      181 dmsvllfdld hfktindrfg haagdavlre tarrvasivr aqdtfgrfgg eefalllpct
      241 nldeamlvad kvrdaigslp vdaegvsvpv tasvggacak agatacdvlv neadaalyra
      301 krlgrdrsva ya
//
LOCUS       WP_175863693             269 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175863693
VERSION     WP_175863693.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..269
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29881
     Region          85..268
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mrtwrleran laaqldvsra trlvaaiggn epnafaaeil klfddalsit qctifayefg
       61 nrprtmsvad hrggrylrdl adtyarhfya ldgnqqivst ahrstrrhdl llhqqagdei
      121 dheayraacy rgpdvsdrla llmqpgdatw lsinlyrahr sgafqpreia aiealaplia
      181 qaarhhyala gaaqigipqr mlarlrhacp dlskreldvl rgvldgqtah eigetigvka
      241 ssvvtyqkra yrrlgissqr elfalcmqp
//
LOCUS       WP_175863723             418 aa            linear   BCT 11-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Burkholderia cepacia].
ACCESSION   WP_175863723
VERSION     WP_175863723.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..418
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45279
     Region          12..395
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mlkrfgnpdv akavanlvwl glerltqigv aiaisgllar yfgpdvfgkw qyantlllvl
       61 apltwvcgae ilvptivqrp paqlgavlgs afalriavsa aalvatwiai aagafdplvg
      121 amlaglavtm vfrepfvgvi nawlqsmtys kpqlvtsmvt alakallvwl lvraaagpar
      181 fawlwaleaa aigfaltlyy rhrnggslgw tfdkplfrhf atagtvfwlg licmylflkl
      241 drlmlerhvs fadlgrysaa qqlnenwitl almlaqtiap afvyrvqdva rlrrnivrli
      301 amtaclmtag alvldaaapl ivgkvfgrgy easvdifrwa vwlsvpagie aignlivlky
      361 qakfvllskw llalaiaalv nlfaiprlgl fgalvglaag ylaaaavnfy yirfklrp
//
LOCUS       WP_175863748             349 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175863748
VERSION     WP_175863748.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 349)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..349
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37176
     Region          1..341
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mselrihgls ksfgshtvlh didltvrrgs rlallgpsgs gkttllrvlc gferaergtv
       61 eidgrrvaap dlhlppevrr igyvpqegal fphlsvadni afglpraarr rhhrvdelle
      121 mvglpasyas rapqqlsggq qqrvalaral apepslvild epfsaldtsl rhetrsavad
      181 alaaagatsv lvthdqpeam tlgdevavmw hgrlvqtaap qtlyrqpvtr dvasfvgqav
      241 llagrvrsmr iacalgelpl vvplpdgpad amlrpeqigi vpvtqadaar ghtarveaar
      301 fagqdadvvv rldadpevlv rarvpghrcp avgervalvv dgavmayar
//
LOCUS       WP_175863777             263 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175863777
VERSION     WP_175863777.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 263)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 263)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..263
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29385
     Region          9..252
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mkhdtplrrs ieiqirviga llmreiitry grhnvgfvwl fgepmmftlg viglwtatkt
       61 vhgsglpiaa falsgyssvl lwrncvnrcc lailpnhsll fhrnvrvidl fisraileia
      121 gatisiftlt ilfvtlgims vpsnislilm gwfllaffai glgfaigals ersemseriw
      181 htvsyllfal sgalfmvdwl pkkmqqyvlf lpmvhgvemm ragyfgdlvk physvsyvvv
      241 fdailmlvgl flvaetgkrv epe
//
LOCUS       WP_175863787             107 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Burkholderia
            cepacia].
ACCESSION   WP_175863787
VERSION     WP_175863787.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..>107
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
     Region          25..>104
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mtpaslieqy gpresmeydv vivgggpagl saairlkqla aekgteigvc vlekgseiga
       61 hilsgavmdp raitelfpdw kergapldve vtedrflfls eksavtt
//
LOCUS       WP_175863891             453 aa            linear   BCT 11-JAN-2025
DEFINITION  TldD/PmbA family protein [Burkholderia cepacia].
ACCESSION   WP_175863891
VERSION     WP_175863891.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..453
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=48435
     Region          19..452
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 mtgfdpmarr agidwhahft rladeaqrlk apaetvllgf ssetsdfvrf nggrirqtgr
       61 vtqgrlsvrl vdgarqvhsa ltvcgdpaad lpelaaalav lrdglrdapd dphllfdtss
      121 wlqethrtgr lpdadglarv vaecargldf vgfyaggtla rgfasstgsr gwyevenfnf
      181 swslydpsgr aiktayagdd wsdaafaarv eaaaarlpvl grtpkalapg ryrayfapda
      241 vhemtsllgw sgfsaralas arsplhrlya gevaldprvs itedfslgia pafnadgyrr
      301 dsvplvvggr gegqlvsart arehgrvpng adngespqsl tiaggtlada dvlaaldtgl
      361 yvgnlwylnf sdpiacrmtg mtrfatfwve ggrivapvda mrfddsfyrl fgseleqlga
      421 apallanddt ygeratggaq lpgllarafe ltl
//
LOCUS       WP_175863911             448 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175863911
VERSION     WP_175863911.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..448
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47951
     Region          21..440
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mptqpstpaa slalhddaht sqhsraqryl qllllviaag aiypmlylrq vyqptmlqff
       61 hiddvqlgyl ysslgtiflv sylpsgwlad rlsprwlicf sllatgalgl ayatgpsfdt
      121 lvlifggwgl ttgltfwaav ikrvnmiagp deqgrffgll dggrglveal latiaitlfa
      181 yvtqahggtd aagfrlvvhl yaffcialgv llalvkdpag asdraaaaqr rtgsdrqgnv
      241 ltdlktlaai pelwlvaaiv fcgyqvfwat ysfsaylheg nfglsataag fittlklwmr
      301 piggigggfl gdrvskvsvl fwalvlaals lvgliaapah spqamlvalv lfigiltyai
      361 rglywslldd ckvpthcagl aiglisvlgy spdvfvplin gyvtqtfpga hgyqlyfgyi
      421 aaialcgaga aaflkyrltr ihriqesa
//
LOCUS       WP_175863914             343 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-quinone oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175863914
VERSION     WP_175863914.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..343
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=35860
     Region          12..335
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(51..52,133,137,140,158,161..163,183..184,188,203,
                     227..228,249..250,252,274..276,324,329)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 msdtlspvpa dmaaveitrp ggpevlatar rpvprpkade vlirvhaagv ngpdvlqrkg
       61 lynpppgasd ipgleiagav vatgeavhdf apgdrvsalv tgggyaeyav ahhlttmklp
      121 pgldmieaaa mpetfltvwl nlvqrgrlqa gesvlihgga sgigttatmi akamgastvi
      181 ttvgseahra aslrlgadha vhyqeedfva evdritagkg vdvildiiag dyvarnyraa
      241 amngrilqvs alagpakeld vwpmmtkrlt higstlrsrt peekgaliae lerqlwphva
      301 agtvkpqvfr tfalddarga hvlidsgehv gkivlttaah raa
//
LOCUS       WP_175863917             463 aa            linear   BCT 11-JAN-2025
DEFINITION  alkaline phosphatase [Burkholderia cepacia].
ACCESSION   WP_175863917
VERSION     WP_175863917.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Vimalraj,S.
  TITLE     Alkaline phosphatase: Structure, expression and its function in
            bone mineralization
  JOURNAL   Gene 754, 144855 (2020)
   PUBMED   32522695
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..463
                     /product="alkaline phosphatase"
                     /EC_number="3.1.3.1"
                     /GO_function="GO:0004035 - alkaline phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0106219 - zinc ion sensor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48081
     Region          28..463
                     /region_name="PhoA"
                     /note="Alkaline phosphatase [Inorganic ion transport and
                     metabolism, General function prediction only]; COG1785"
                     /db_xref="CDD:441391"
ORIGIN      
        1 mstikciaaa lavagfacga aqaagqaknv ifflgdgmgp ttvtasriyk vgesgqltme
       61 klartarikt fsndaqttds apsmaaymtg vkmnnevlsm ssdtravapg sdangnktvn
      121 ncapgngqpv atllelakar gkavgaittt elthatpaat yshichrdaq ydiaaqaapg
      181 gagynaalgd gvdvlmgggr nhwtpfdpva nrrgradgrn lldemkakgy tvvatkdqla
      241 qagngklvgl fsstshleye ldrvagkgeg psqpslaemt skaidvlskn sngyflmveg
      301 gridhalhgt nakraledta afdeairial skvdlsntli vvtadhdhtm tingyskrgn
      361 pildisrnyr dgqpskdadg ntyttlvfgn ganrpnvras vdsatatnda ylqevgvrmg
      421 sagsethggg dvmlfadgad akafkgtidn tkvfglvrsa fgf
//
LOCUS       WP_175863939             822 aa            linear   BCT 11-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Burkholderia cepacia].
ACCESSION   WP_175863939
VERSION     WP_175863939.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..822
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=85689
     Region          63..813
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 msrnwglgaa llalcvglas cggdgdspsa aasnlsaatq sqgnedgngg nssngngndn
       61 dnaaskknad irvvqyvnpl igtdyatdqp adpvgsglgg gtfpgptvpf gmmqwspmtp
      121 taqydsrkgd gsgfsggywy gdtsinafsi lhlsgtgcwa nggylnvmpq lapgdagtpa
      181 sfshanetaq agyygvtlgn gikaeltttl rtgfarftyp alaqgqqati aidptvlnnr
      241 aqgstgdtis qagdralsgt iagggfcwag havpvyyyae fsqpfavkpa lsndspvalt
      301 fnvdrkhpdv mmklgisfvs eanakanlla enpgtdaqgn rnwrfdkvrr aasaawnarl
      361 naiqvtggsd adktkfytal yhaslhpnvf ndvngqypdf yasngasaap trqvekgrtm
      421 yanfsgwdid rsfmqlqall dpvrtsdivq slvldakacg afprwayfnt etavmpgdag
      481 siivanahaf gatkfdtqaa lsimkrsttp gaacagtpvm gsradydrlg yvpssgpgdn
      541 qtasntleya vrdfavsrfa talgdtatag tllkssgnwq nlfdrnavqp ktsagawvtd
      601 gtgfmegnse qytwyvphdl ggvvaqagga apvvkrldtf fthlnigtvq pyfyvgnevt
      661 mavpwvyawa gapshtqrvl htslanefgt gaaglpgndd lgaisgwyvw aalglypvvp
      721 gvsgvalssp qfekivvrvg qqdgsyrllh ivapgagsgd aasfyvkslk lngapyptaw
      781 lpfehiakgg klsysmtada saatwgtdas ampsfpqaag ap
//
LOCUS       WP_175863990             400 aa            linear   BCT 11-JAN-2025
DEFINITION  benzoate/H(+) symporter BenE family transporter [Burkholderia
            cepacia].
ACCESSION   WP_175863990
VERSION     WP_175863990.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..400
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41390
     Region          11..399
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mqsntppgai raigndwsvs aitagflavl isyagplaif fqasqaahvs nemvsswvwa
       61 isigagisgl faswklkvpv vtawsapgta llvglfpqlt lnqavgayit aaliilligv
      121 tgyfdrlvrh iprgiacgmm agillpfgth afaaaseqpv lafgmiaayv ifkrllprys
      181 ivlvlltgaa latalgmthl gnvspsiahp ifiapewtlg ttlslalplv vvsltgqflp
      241 gmtilrasgy htparpiita tsvmslvvac fggitivvaa itaalctgkd ahedagrryv
      301 aglangafyl vgglfagtiv tvffalpkaf vailaglali gaiganvhgi fedenhreas
      361 vitflatasg mtwlglgsaf wgivigsfsy avlnkvrrqa
//
LOCUS       WP_175864051             304 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175864051
VERSION     WP_175864051.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..304
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=33755
     Region          26..283
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mqnpqavpey lmqsdvvrer farlktrdvi ldvrhvgkrf atpqgecval ddisfrthrr
       61 efvcvigpsg cgkstliril agleaqtsge vlldgkpvqg pgadrgmvfq gytlfpwltv
      121 kknvmfglrm ngsssgeaer ealqwldlvg ltrfadvyph qlsggmkqrv aiaralanrp
      181 rillmdepfg aldaqtrarm qthlldiwrn idvtilfith dldeaiflad rilvlkanpg
      241 avqelievpv prprdysqvn spafvatkar lealihpkea vpandddgvk phmirmtdvs
      301 dnve
//
LOCUS       WP_175864112             424 aa            linear   BCT 11-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Burkholderia cepacia].
ACCESSION   WP_175864112
VERSION     WP_175864112.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..424
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44551
     Region          1..407
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mknrltssia igmvlgvaag yachtsiadp gtlktvagyf sivtdiflrl ikmiiaplvf
       61 vtlvsglagm dsgedvgrig lrsvawfvca slvslglglv manalqpgag lnltepagea
      121 nlglntaaln ardvithafp tslldamarn dilqilvfsv flgialsalk hdrrvgivir
      181 sidgmvpvml rltnyvmraa plgvfgaias svalrgldvi ytygkligaf ylgllvlwti
      241 ligagylflg rrvgallrav repaliafst asseaayprl teqlekfgvd kkvvgftlpl
      301 gyafnldgsm myqafaalfi aqafgvhmpl sqqvfmllil mlsskgmasv prgsvvvvaa
      361 vapmfhlpaa gvamilaidq vldmgrtmtn vignsvatav iakwegaraa qpdsaafdsr
      421 elna
//
LOCUS       WP_175864121             493 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175864121
VERSION     WP_175864121.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..493
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51155
     Region          20..468
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(27..28,31..32,35,67,117..118,120..122,125,145,
                     148..149,152,214,217..218,289..291,294,322,325,383..384,
                     388,392,408,411..412,415..416,419)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msrndpvspd prrwamfavl lvgaflppld ffivnvalps iraelgasss aeqlvissya
       61 glyavtlitg grlgdlfgrg rvfflgligf aiastlcgfa sspwtlivgr alqgvtaaim
      121 apqalasiqa ifpeaekpla lslygavfgl aavvgqalgg ilislnllnl gwrtiflvnl
      181 plailvvlfg ipllketraq harkldlggt alsmltlgal ivpliegrea gwpvwawvsl
      241 lavpalagff wryerrlgrr ggaplldpaa lrapglgral lialllysig affllfsvyl
      301 qnalhvdals aglvflpfgl gfllgplstp asarvigayv npfgmsleiv glvglawlid
      361 atpigmplaa aplavvlfvi gfgqglalpt lmrmvtgrva palsgmiagi asstlqvsts
      421 lsvaiiggif yttlgtrqdp aaiahafiva llsisvflav gaalgislar agaahtsmra
      481 aarpgfgper erp
//
LOCUS       WP_175864187             203 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cepacia].
ACCESSION   WP_175864187
VERSION     WP_175864187.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..203
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21362
     Region          1..189
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtlsalavfa fallvtagtp gpsvaalvar vltngvrdvl pflaamwlge alwltlavag
       61 lsafartfet glivlkllgv ayllflawkm wtaptgtgad dlprgqspwr mfvagmlvtl
      121 gnpkimlfyl allptivdlt hvgvlawael vatmlavlil adcfwsllaa rarafftsar
      181 akrianrtsa tamagaavai atr
//
LOCUS       WP_175864198             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175864198
VERSION     WP_175864198.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46368
     Region          23..428
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(35..36,39..40,43,82,140..141,143..145,148,168,
                     171..172,175,258,261..262,265..267,270,298,302,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mpdtmstlaq paahaprrvr nsrlatasmi gtslewydft iyntlaalvf nhlffpsvdp
       61 lagtilafst yavgyvsrpl ggfvfgnlgd rigrravlml tlvlmgvtta lmgalptyaq
      121 agilspillv alrfvqgval ggewagavll svehgdqkrr glsaswtqig psfgtllgtg
      181 cialvtlstt sgdflswgwr vpfaasallv vfgfwlrrgv detpqfeqla eshataevpv
      241 advlkyhwkr lllaggsrig sdvlyalivv ftltyvttvl hlsrpvalta vmigtacnal
      301 avpffgalsd rfgrrpvyla galagivwaf vffamldsar pgaivaavai glvihavmyg
      361 pqgafvteqf ptrvryagss laytlagivg ggfaplviat lfrqtgttta vslyvaaalv
      421 vtsiallvar etahrplad
//
LOCUS       WP_175864217             736 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia cepacia].
ACCESSION   WP_175864217
VERSION     WP_175864217.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..736
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=77387
     Region          57..>192
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          200..728
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mtieldntgs vrpsrrtflk aagaaaavsl tigfewaglg rralaatapa adfapnaflr
       61 itpdgavtvi akhvemgqga ytgiativae eldadwstvr vesapadakr yanlafgtmq
      121 gtggssaman swqqlreagg karamlvsaa aarwkvpage lttangvvth aksgkkaayg
      181 tlvadasklp vpdkvalkqp adfkligqri prvdaspksn gtahftldtt fpgmrvallq
      241 rpprfgatvk sfdataarav pgvvsvvqvp ggvavvgtgf waakqgrdal kvewdeahae
      301 krssdeimre yrqladkpgt sarkdgdada aiagaarkig atyefpylah apmepldavv
      361 kltadsceiw agdqfqtvdq anaartaglk peqvqihtly aggsfgrran awsdyvveav
      421 siakalgadg kpvklqwtre ddiqggfyrp myfhkldagl tadgklvgwr hrivgqsila
      481 gtpfeafmvk ngidatsveg aanlpyavpn vsveltttkv glpvlwwrvv gsshtayave
      541 afideaahta gkdpyafrrd llakeprmra vldlaaqkag wdpakplpkg rgrgiavaea
      601 fksyvaqvae vsvdadgkvk vervvcavdc giainpdiva aqmeggigfg lgavmhsait
      661 lkdgqveqrn fdgyhvlria empkvevhiv psaeaptgvg epgvapvgpa vanaifaatg
      721 krhyvlpfds adsaka
//
LOCUS       WP_175864258             212 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cepacia].
ACCESSION   WP_175864258
VERSION     WP_175864258.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..212
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22504
     Region          19..205
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtasaavlai laalflgami pgpsfvlvar naiglsrrdg latalgmgig givfggvala
       61 glytllqave wlyvglkvag gayliymask iwrgadrpia mddpqamggg rarksfwtgl
      121 ttqlsnpkta iwygsifaal lpqhpplwcy lalpplvfgv efgwytival cfstrrprel
      181 ylrakkwvdr vaagaitllg lrlilnapka gi
//
LOCUS       WP_175864263             360 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175864263
VERSION     WP_175864263.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..360
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39423
     Region          1..358
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msfltltdlt ktfgeltava dvnlsveqge fvsllgpsgc gktttlqmia gfvdvtrgri
       61 aldgqdithl kpnrrglgiv fqsyalfphm svaenvgfgl dmrgvdkaer aeriraalal
      121 vrldalahrf prelsggqrq rvaiaravvi eppvllldep msnldaklre dmqfelraiq
      181 rkigtttimv thdqsealsi sdrvvvmeag ritqtdtpyr ayerpenrfv sqfigkanll
      241 pgtivahdgd airidlghdl aetgrtahlp prerdvrvgd avsvcirpek lrlcapdagr
      301 faatvtsrff lgsqwlyrvd salgevlvcc qnegaeplte gapvgidwhs davrvmrrea
//
LOCUS       WP_175864269             324 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175864269
VERSION     WP_175864269.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12168323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..324
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34644
     Region          22..200
                     /region_name="AraC_binding_2"
                     /note="AraC-binding-like domain; pfam14525"
                     /db_xref="CDD:434015"
     Region          251..322
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdialsrhap nrlgtlhapd everavahrl gphrmaargr dpfhaelyev plhhgallel
       61 cygretridf gddaghflfr ltlagacelq agsvvaragp geltvsspal asrlstspdc
      121 rnlvlrlerg alerklqhml ratltrplqf dlaaggtgtg aalvlptfey lcklgaqprv
      181 gtasplfgad ltawlmslll thlphsysda largtpplpa hvrracdhvd ahlgeplala
      241 alaavagvap rtlqhafraf lhttpaayvr errlaavhaa lqrggtcsvt dvliahgihg
      301 fghfakayar ryghapsvta rqsr
//
LOCUS       WP_175864270             344 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175864270
VERSION     WP_175864270.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..344
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=37964
     Region          34..93
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          124..324
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(139..140,142..143,146,150,152..158,250..255,
                     261..262,264..265)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mthaatgrpa aptradsaph dsdlselrvq dldlnllktf ravyeerhvg raalrlgvtq
       61 psvshalgrl rlmfrdalfv rtgtgveptp raqrlaisvd kalailqdvl degsrftpds
      121 tqrvfrlhms dfaasaflpt llaafdrrap gavietlhvd ecqlnvales gridfalghf
      181 adasshfqrt allhercvll mprrtaqrva lpddyvldgt apdtlrfvav tshpqsmqll
      241 erhglmprvr aalpdfmvvp allrdgdyal ilpetiaitf aarqpcalye iagagewavn
      301 aywhrrfdad pghrwlrall lelfhigela pfdawlapqp paca
//
LOCUS       WP_175864272             324 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175864272
VERSION     WP_175864272.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..324
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34881
     Region          15..223
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(52..53,55,69..71,77,79..80,121,222)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(52,54..55)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(77,80,83,90)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(113,117..120,122)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(118..119,142..144,196..197)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          241..324
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 mqanrhqvri dalidaaqdi rcfrvsridg qpfdayepga hidvtapsgv trqyslcgnp
       61 dergsylfav kkeaqsrggs rslhddvrvg aelsigtprn lfrltddase hvliaagigi
      121 tpllsmayal hrrgaryrlh yfarsrehaa fvdelsaepf ashvtfhygv epdalaaalg
      181 rcvesvdaha hvytcgpgpf meavvvaaat rlpedsihle rfaaepvaad adptpadefe
      241 vrlhrsgqsv rvtpdtsivd alarigvevd tscgegvcgt cmvpvvdgep dhrdhclska
      301 erasntvicc cvsrarsavl vldl
//
LOCUS       WP_175864273             167 aa            linear   BCT 11-JAN-2025
DEFINITION  aromatic-ring-hydroxylating dioxygenase subunit beta [Burkholderia
            cepacia].
ACCESSION   WP_175864273
VERSION     WP_175864273.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10791045
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..167
                     /product="aromatic-ring-hydroxylating dioxygenase subunit
                     beta"
                     /EC_number="1.14.-.-"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0009056 - catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=18583
     Region          7..167
                     /region_name="HcaF"
                     /note="3-phenylpropionate/cinnamic acid dioxygenase, small
                     subunit [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG5517"
                     /db_xref="CDD:444268"
ORIGIN      
        1 mmddrnalfs eqtfaravef vwreaemldr rdyrawldlw dpaghyvvpi dpdttdfaat
       61 lnyvfddqdm rekrvqrmvs gysasaadaa rtvrtvsrft lesgsagtve lksaqvvvay
      121 krgvatlfaa dvthtlhvda vgemriaekv vrlidsteal saigfll
//
LOCUS       WP_175864307             358 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia cepacia].
ACCESSION   WP_175864307
VERSION     WP_175864307.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..358
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39342
     Region          12..335
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 msitashhvq siwytrcpvp tplgiaahlg wldsefagdg itvralqenq haalhrahvd
       61 hsldntfrqg gsipalwara sgadtrvval twvdeaqaiv alpetglkrp rdlrgrrigl
      121 prrdgeridi fraaalrgfv salsldglgp advewvdvpa snlrapvptp ltrdaafshp
      181 sslssrrlya aeaaalvrge vdaiyvkgsl gletahliga qtvvdigfhp dpqirinngs
      241 prpltvnast lerhpdivrr flarvtdveg wareheqevl gylgretgsg hdwlrlaygt
      301 dvhrrlrtdl deasiaaldd fkrflvewrf lpadfdvraw idrraldgia plsrdaar
//
LOCUS       WP_175864335             434 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175864335
VERSION     WP_175864335.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46511
     Region          25..417
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,156,
                     159..160,163,258,261..262,265..267,270,298,302,353..354,
                     358,362,378,381..382,385..386,389)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 metlvstvlp aarvsedaay rkvawrlmpl llfcylvsyl drvnvgfakl kmagdlglsd
       61 aayglgagif ffgyfifevp snlilhriga rvwiarimvt wgavsaltmf vttptafyam
      121 rfllgaaeag ffpgvilylt ywypahrrgr ittvfmtava lsgvvggpis gyilkafdgi
      181 ngwhgwqwly lleglpsiva gllvyalldd riaqakwlnd eerallernv naedavkshl
      241 slgavlanpr vwlmcaiyfs fviglygvgf wlptlihatg vadpltigll stvpyalavv
      301 amiaiarssd rlrerrwhla vpgamgtvgl vlavgwahqt glaiaaltla tmgiltaipl
      361 fwslptaflg gtaaaagiam insvgnlagf lgpylmgllk qltasndagl ymmagcmalg
      421 gllalslpka lvnr
//
LOCUS       WP_175864337              65 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CsbD family protein [Burkholderia].
ACCESSION   WP_175864337
VERSION     WP_175864337.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..65
                     /product="CsbD family protein"
                     /calculated_mol_wt=7350
     Region          1..65
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 mnedkikgqw kqlsgklkak wgkltdddla vadgnreyla gkiqerygia rdaaekqlke
       61 fdrel
//
LOCUS       WP_175864384             294 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175864384
VERSION     WP_175864384.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 294)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 294)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 294)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..294
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31756
     Region          19..289
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mpnvlstiah ppaanahkrr dwrsmrllip amlllviffl lpvlslllrs vleptpglhn
       61 yeqllgstty vrvfgntflv atvvtlvtli vgfpmawlla iaprklssvl failllsmwt
      121 nllartfawm vllqgtgpin ralmaigvih eplslvnnlt gvtigmtyim lpflvmplha
      181 tlrgidpstl raaavcgasr wqafwrilvp lampgvasga lmvfvmalgy fvtptllggp
      241 symmlaelia qlvqellnwg lagaaafvll avtlalyalq lrftgsarat tggr
//
LOCUS       WP_175864393             418 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175864393
VERSION     WP_175864393.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..418
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43958
     Region          6..411
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtssqkaplv ivgasyagth laaaarelgf dgpivligde phapyqrppl skglltgktg
       61 mgqlalrspd fyteqcidlr vgqrataldl aarrvrladg ehleygwlal atgarcrplp
      121 vpgaelqgvh qlrtlddala vqrrlgrcss acivgggfig levaaalisa gtrvtvvesq
      181 trllarafpa fmsdyvahah rrrgvslelg rsvrallgrq gsveavqfdd grtldcdlvv
      241 tgigvlpnae ladaagiacd dgvlvdalgr tsvrnvlavg dvanmaqppf pggparmrfe
      301 siqaasdgar aaasvlvgrp qplsavpwfw seqhdlrfqm aglpssgdqv vlrgapasdr
      361 ftvfylhdga maaahsvnrp sdhvlarkli aqrsripaat ladptadlrs midagqvn
//
LOCUS       WP_175864425             383 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia cepacia].
ACCESSION   WP_175864425
VERSION     WP_175864425.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..383
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40340
     Region          1..375
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnfeatpdqr aaaatyrava lrhfassprr gfdwatwral seaglwrtla agrdagadas
       61 lnvfiaafea ivtatrsvgf amalanqatv iralllhgtp aqrdrflpal msgavaatai
      121 sekgtgteir alqsrvtldg qdcrldghky nishapdaal ilvaasathd grsgtalvll
      181 dpqragvtrt apqetlgvtd lpigdmtfdg vpvgtddllc tpkdglrvlm diasmnralf
      241 gllcadvvgp flddalayvg ergalgvtld khqhvqrrlv dihvgaersr wmalaaldql
      301 ragdpsalas csiaklggar dltqaalhll aiygsdgyrr gplatfvada lamgtaggte
      361 emharnifsq mqrratashm haa
//
LOCUS       WP_175864469             314 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175864469
VERSION     WP_175864469.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..314
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34060
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrlrafevf vtvvsrggfa raadalgtsp anvtryvnel eahlgtrlln rssrtlslte
       61 ggetlyarck silddvaete glvssasvep rgrlrinapv sfgilylapl wpefmrkypg
      121 veldvglidr vvdivdegyd lairisrags tshaarklat sqnilcaspa ylarfgvpaa
      181 paelgghrci gytyastgdd wqlidergkl hsvkvdchmh tnngdtaraa alaghgviqq
      241 ptfligkdlg egrlvhvlpr yrlpdidila lypsrrhlsa rvrvmidflv dafsgvppwd
      301 rndgnwagaa pttd
//
LOCUS       WP_175864401             185 aa            linear   BCT 11-JAN-2025
DEFINITION  ester cyclase [Burkholderia cepacia].
ACCESSION   WP_175864401
VERSION     WP_175864401.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Sultana,A., Kallio,P., Jansson,A., Wang,J.S., Niemi,J., Mantsala,P.
            and Schneider,G.
  TITLE     Structure of the polyketide cyclase SnoaL reveals a novel mechanism
            for enzymatic aldol condensation
  JOURNAL   EMBO J 23 (9), 1911-1921 (2004)
   PUBMED   15071504
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..185
                     /product="ester cyclase"
                     /EC_number="5.5.1.-"
                     /GO_process="GO:0030638 - polyketide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=19696
     Region          57..184
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
ORIGIN      
        1 mktstvvsvv srialaaata aaalpavsat ddnlvqpktl ivdkslskhq aeqqiraarl
       61 ydtfwstgde aqarealaad ftdrtlpagr pqgiagplaa lkgfhgavpd vhadveqmiv
      121 agdrvithlh ftghftgsfn gvqgkgqvvd fiatdiyrvr dgkitdnwhl ednltflqql
      181 gvvar
//
LOCUS       WP_175864545             779 aa            linear   BCT 11-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Burkholderia cepacia].
ACCESSION   WP_175864545
VERSION     WP_175864545.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 779)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 779)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18771781
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..779
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..779
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=84044
     Region          19..133
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Site            order(30..31,33,57,60..61,64..65,67..68,91,94..95,98..99,
                     102)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          55..85
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          178..754
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          211..237
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          245..271
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(247..248,251..252,254,278,281..282,285..286,
                     288..289,312,315..316,319..320,323)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          276..306
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          311..339
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mfstelpasa altpeqqlaq dialvmdnal erhrsgafdd aralyeaild avpahgdahy
       61 nlavlladtg haadavphfe aalgaspdng yywvsyihal hrsgqtaaaw iaveiaqqrg
      121 vhgpalngli aqlaspdivl ataavaaaps gidaaivlet aagrsdsgks arrpnqtllq
      181 khaalfdknr haeatalark lvadypedga cwralsaslh regrfpemie aglrtvellp
      241 nevlvrilla dtlramnrla eadeqcmrly qlqpdhpeam rirglvlfal rrtdealaac
      301 rravelapga aapcgtlgfv llelgatqea igwlkraiei nptdsvthss mlfciahsse
      361 fdpqalvaeh rkfgtrydnq krkraavfsn prdparklqv gfvsgdlysh avasyavpvi
      421 ehlaadpgia mhfyhnhfee dhtserfkah attwrnvtgm sdsaflervr ndgidividl
      481 sghtgrnrlv alaqraapvq aswigypatt glaamdyylt drfvaphgaf ddqfveqivr
      541 lpaiapfmpp pncppvnvlp alhngyttya sfnrlnklsp hvievwarvl hadptarmal
      601 gaigndgdqq tltewfaaag idagrltfhr rsnipvymqq hhgvdlclda fpytgstttl
      661 nalwmgvptv tipgatmagr gsagwlqhvg ldayiatded dfvaralalg rdtaalqalr
      721 aglrarcges aafrpavvaa glssalrtmw trwcagepat afdtplfddm ttaqaaaea
//
LOCUS       WP_175864554             385 aa            linear   BCT 11-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Burkholderia
            cepacia].
ACCESSION   WP_175864554
VERSION     WP_175864554.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..385
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41009
     Region          17..299
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mstfsgdaqs adkhavarks tfvsivlnvv latfqivvgt iahsqaliad gvhsisdlis
       61 dfvvlvanrh sgaspdadhn yghsryetva slflgailia vgvgmlwrag drlvnlenip
      121 avhfsalvva ltvlvskeal frymlrearr vrsamlvana wharsdaass lvvaigivgs
      181 lagvrlldpi aaaivgfmva rmgwtfgyda lqdlsdrald ttdtaeiral laatpgvrdv
      241 hdlrtrkmgd aalvdahilv dpmisvsegh yiaetararv lrdprvldal ihvdpendaa
      301 rrpalalppr geiaarleaa laqrglhaaa inlhylstgl eidvtlacdp hdtdaalagr
      361 ldadalkref garrigftrt mpaqt
//
LOCUS       WP_175864563             423 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia cepacia].
ACCESSION   WP_175864563
VERSION     WP_175864563.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..423
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=44004
     Region          207..415
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(214,254,292,395,398)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(214,395,398)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(214,254,292)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 msfrssiaaa vlgaaafvsp lvasasaapa gwvaawatal qpipdlaapp plyrapdvag
       61 rtvrqivypt vpgraarirv snaygrfplv veaaslarag egaalsgdaa apvrfggkvs
      121 vtlapgqele sdpvgidvra gqpyaislqm ganqrmtvwh rvsnqfnyvs vpgehvsdpg
      181 aaafrtrftq fawvtelave tgsarasvaa igdsitdglr ssvnrnrrwp dalarrlaas
      241 gaesigvanl gisgnrllsd sacygtslas rferdalsra gvkaaivlig indinfatmp
      301 pragldcdhp htqvtaasli dgyrrlidaa hrqgvkvfga tltpaglpag realrlevnr
      361 wirsgggfdg vvdfdavlrd parpsvlqrr fdsgdgihps dagytamada vpieqlqtav
      421 ggk
//
LOCUS       WP_175864565             707 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cepacia].
ACCESSION   WP_175864565
VERSION     WP_175864565.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..707
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76804
     Region          29..707
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mtvslarppv rprrmaaala cvaaslahad dspggatvlp avnvtaahds pqhltdtvst
       61 galgtrrqld tpfsttivts eelearqpyk lgdvfandas vsdnsgaysa wasymtvrgm
      121 qldwqngyki dglpfvtygi tmpyeqldrv ellkglggfl ygfvtpggvv nyvtkqpgae
      181 pvrsvdvgyr stnvwtehvd lgqrfgpdgr fgarlnathe egrtyndgni rrdsvslalq
      241 anltrdlsvn vgalyqdrrt tgqtpsiftg sypggvlpat isggttnlgg rdqylntnlq
      301 lytaglqyqf apdwqldvay syskatrrrn estlylqdaa gnytdsryvg medhrfsqwr
      361 amvegkvrtg afshqiviga swqkqandys ansvfvplga gnlyapnpyr ydsphgfvqy
      421 rtseivqksl fasdtvqlta rwsvlagvry mnyeqrsfqa sgaedpgyrq ngvvtptfav
      481 mfklapttta yasyaeslep gsrvndvyan agqvlkplrs kqyelgikse harwsataal
      541 friersaeya naanvyvqdg esviqgiefg arakigarwn agvdamllda wyangignng
      601 nrvagaprfv lagdvgyavp gvpgltlgvd akftgatplr aaggldapgf lvvnagaryl
      661 trigrhdvtl rasidnvlnr ryweyqyady vkpgdprtvs lsakidf
//
LOCUS       WP_175864584             445 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrolipoamide acetyltransferase family protein [Burkholderia
            cepacia].
ACCESSION   WP_175864584
VERSION     WP_175864584.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..445
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47745
     Region          2..445
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mgihvikmpd igegiaevel vawhvevgqt ikedqpladv mtdkaaveip spvtgkviel
       61 ggrigemmav gselirleve gagnlkvgap vreskvetap vavapstava dapaespvrp
      121 atkhapaepr hakqaerkeh veppraalap gerplaspav rqrawdmgie lryvrgtgea
      181 grilhadlda yagtgggaar gargsrahgy derndetevp viglrraiar kmqeakrrip
      241 hfsyveeidv teleslrtdl nrrygdtrgk ltplpllira mvialrdfpq inarfddeag
      301 vvtrygavhm gvatqtdsgl tvpvlrhaea kdvwsisaei arladavrtn raqrdelsgs
      361 titisslgal ggivstpvin hpevgivgvn riverpmird gavvarkmmn lsssfdhrvv
      421 dgadaaefiq avravlerpa llfve
//
LOCUS       WP_175864592             257 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175864592
VERSION     WP_175864592.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..257
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27960
     Region          1..>240
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mnllelddlc laydtphgrr tvvdglslal prgdigcllg asgcgkttvl raiagfepvr
       61 mgrivldgap vaapsldvpp errsigmmfq dyalfphlsa adnvafglrr mpkterrmrv
      121 aemldlvgla dsgsayphel sggqqqrval aralapspel llldepfsnl dvdtrerlaf
      181 elrdilkrtg htailvthnq aeafaiadri gvmkdgrlaq wdtpyalhhh paspfvadfv
      241 rrdaladera ralargr
//
LOCUS       WP_175864631             521 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175864631
VERSION     WP_175864631.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..521
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53019
     Region          16..447
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,142,
                     145..146,149,282,285..286,289..291,294,322,326,380..381,
                     385,389,405,408..409,412..413,416)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtlsdsrrna valaavclts lmfgleissv pvilptlehv lhgdfngmqw imnaytiact
       61 tvlmaagtla drfgrkrvyv tgtvlfgats llcglapnvp vlvagrllqg asggamlicq
      121 iavlshqfre grergrafgi wgivfgiglg fgpivggaiv alaswpwvfl vhaplaaval
      181 aliggavqes rdphagsldv agivtlslav lglafyitqs aelgltsaag lgvlgvlgvl
      241 gvlgatvlav agfflaeras arpmfdfsvf riraftgaif gsmgmnfsfw pfmiylpiwf
      301 qvalgydsvt aglallaytl ptlvappfge rlalrygpgv vipgglftia agfalmrigs
      361 aadhaswvtm lpgcviagig lgltntpvtn tttgavpsar agmasgidms armislalni
      421 aamgfvlvag ivaslkggva gtigdgalrr laqeiasgrt dglheiapal aqadptgaal
      481 haalvhgfgw vmvygaagva vlatasavaf aparrgaavc e
//
LOCUS       WP_175864667             712 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia cepacia].
ACCESSION   WP_175864667
VERSION     WP_175864667.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..712
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=77917
     Region          86..>620
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msfapnggip nglgggglgs lsalgglagp vassvagslg plaglaghvd tvqramqlaq
       61 tgfslmdktp gaiaeainga anparltqln ryvtldtplg pdvllvsaav vdehvnrlpe
      121 ihldllshrh dlrpedligq qvkirfdqqa rlstlervva sgtgdndryf dgyvasfdra
      181 gnpgnvtqyh ltavpwfwfl trstdcrifq nktaqdilte ifqehgfsdf vfdirtsqkp
      241 leyvvmyqes yynfcarlme qeglvwthry ekdkhflvig dsnllfrpid glaavpfaat
      301 easedsgidq lhegrrfgvg kvtfrdfnhq npssplmlve agpqnlkhar ldaterfehq
      361 slydhgddgn ryarfameae eaqahrytgg gyawrmttag avtvanhpvl ennqeyvilh
      421 vrheavndyt qhsaklpyrn sfallpkkvp yraprstpkp vihgtqsaiv vgpkgeeiyt
      481 ngsavkvhfp wdrrgkkdgs dsmwvrvsqp wagdgwgaaa iprikqevlv afnqgdpdnp
      541 vivgrvfnge qgnpyhgaag qtmgiksqth kgqgsneirm tdtngmqeff mhaqkdmntv
      601 vennethkvl gpmrtvlvat gseekqipqg nltetiaekr sttattvevt tpakdggggt
      661 qvymaergil lkvmdssisl apegirlehk gsvilmtddg vmvngkridl nk
//
LOCUS       WP_175864719             799 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia cepacia].
ACCESSION   WP_175864719
VERSION     WP_175864719.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 799)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 799)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..799
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..799
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84507
     Region          83..762
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mirrpkaagk ggamrrarra rhggamrgal lgpalgaial fglstasara qqpadgtaat
       61 ggavppaava vapevpqapa vtlptvvvvg ttpllgigtp lqkvpanvqt vraaeldaqh
      121 ratladffaa nlqsmtisea qgnpyqtdvn yrgftaspll gtpqglsvfv dgvrvnepfg
      181 dvvnwdilpt qaiermqlip gsnpvygrnt lggalaittk ngksnpggea evsggswgrk
      241 taaieqggti gsnldyyata nvandggwad hnasrvrqaf gklrytdsdt tlsisaggad
      301 nalygtqtip rsfldnrkqa ytypdlnrns agyltlsgdr ffgehvelsg nayyrhlrnt
      361 nissnnntdy gsvgddgtvd avqgtnaqst ivtdsyggsl qltllgklgg manqliagva
      421 advanssyva ssqdayftdt raaigvgdfe pqtraktrna nlgvylsdtl sltphwtltv
      481 sgrydwskaq igdesgvqpl ldgnhtfsrf npalglnwnp vagftayaty negmrsptai
      541 elacadpaap cslpndfiad palkpviskt feagmrgrig aattwsaaay rttltddiqf
      601 isspasaqgy frnvgdtrrq gielagrtrf gplgvglsys yvdatyrssw tehspansaa
      661 dangnvavkp gdhipgipah tvklrldyaa tprwdiganv twrsgvyarg dennqdvngr
      721 isgyvlvdld mryritkrfe vfasvtnlfd kryasfgvlg qnffngpnht fdganpvneq
      781 fvgpgaprga wvgvryawd
//
LOCUS       WP_175864726             236 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175864726
VERSION     WP_175864726.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..236
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25465
     Region          7..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtaapltpvl elrdvtrvye gagrvvavrd atisigprdv valvgpsgsg kstllnlagf
       61 ldvpssgerw leghriddap dtlerirrer igfvfqqfnl ipvmsalenv elgcfawgtp
      121 rtrreraram ldavglaare hhrpgelsgg eqqrvalara lakepaivia deptasldst
      181 naravaelil dtnrtlgtaf liashddrlc ahlprriemr dgvpgvnrel vdvcva
//
LOCUS       WP_175864743             342 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175864743
VERSION     WP_175864743.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..342
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34476
     Region          13..334
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msrfldrapp gaafarlpgt fgaqfwlrwg aalafavvca vfaassplfl tvanlanvlq
       61 qsavvgilgf gltavliggg pdpirggldl svaanmglca avqavalrdg apdgaalalm
      121 latgaavgal nafavialri vpllatlttm nlcagfelvl tqntsvaaas pvlaflidsg
      181 pfgiphlapa llivallfgv llhrtrfglr laatgahrda araaglrvna yvaasyvlsg
      241 vsaalaalas sallsgsspg agenllavva vallgvvfsr rlvptipgtl laalfvgivg
      301 ngfqldnvss ywvngvegal ilfvvattal irrrhtehha hd
//
LOCUS       WP_175864739             363 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175864739
VERSION     WP_175864739.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..363
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39569
     Region          178..362
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mqmnglipsa widdvyaaal gdqrwetvld glrswvgvrm vtllsfddaa rvpaiekaag
       61 ddaswvaacy htyntefyry dpvvpvagnw pagrwfedvk hlsahqrahs efyqeflhpy
      121 gigsisglyi hrsegsgafl svqgglesqg lsddqrraie nmgmhisral qiqarigele
      181 arvaaaesal daipvpvfll gaqrelrytn raadqliaae palrvvngrf apegcvddvh
      241 wrhayarggl llrratgepl plalmpvpeq srlmrerpgv atlmtaadlr spsaraqrlr
      301 vfyglssaea dlavllccdg lspqecaglr gvsigtirtq iksiyaktav araaqltslv
      361 mqt
//
LOCUS       WP_175864753             342 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH:quinone reductase [Burkholderia cepacia].
ACCESSION   WP_175864753
VERSION     WP_175864753.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169595
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..342
                     /product="NADPH:quinone reductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=35718
     Region          1..327
                     /region_name="zeta_crystallin"
                     /note="Zeta-crystallin with NADP-dependent quinone
                     reductase activity (QOR); cd08253"
                     /db_xref="CDD:176215"
     Site            order(42,46,128,132,151..157,176..177,196..197,220..221,
                     225,242,245,250,268..270,314,318..319)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176215"
ORIGIN      
        1 mkaayyerqg nasevlrlgd fpvpqpgpge vrvrihasgl npsdikartg fsgpsafpmv
       61 iphqdgagvi davgagvapt rtgervwlfe aqyrrpfgta aeyavvpeaq avplpdnvsf
      121 evgaclgipa ltahrclfsd gdikgrailv qggagavgta aillakwaga wvattvstpg
      181 qadaarraga dlvinrrlqd vvaivksatr qrgvdrivev slqdnldidm rclanggiis
      241 syavgsaadq vplplldami agctfrfvyi ytvpaaaksa avsaicrcle dgayvptigm
      301 qfaldaivea hqaqesgqvi gkiivrpslv rshepadvqp nd
//
LOCUS       WP_175864775             339 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Burkholderia cepacia].
ACCESSION   WP_175864775
VERSION     WP_175864775.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..339
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36765
     Region          11..323
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(16..18,48,53,79,142..143,183..184,207,236..242,278,
                     295..298,303,306..307)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(48,53,79,142)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 mslkdtlpad nrlgfgaapl gnmfrdipde eaiatveaaw argirhfdta psygaglaea
       61 rlgdalaghr rgdyvistkv grivldemed aktrdygeks gifahgranr lvsdysadat
      121 lrsiedslkr lrtdrldivw vhdiaqdihg dewlaqfeaa rkgafrvlgk lreegvigaw
      181 glgvnrvepi elvldlaepq pdgmllagry tlldheralq rvmpaaaarn vgivvggpys
      241 sgvlvggahf eyrkappdiv akveriraia arydvpvkaa alqfvlahpa taavipgasr
      301 periaedsaa ltfdipadfw remreqqlva adaplpidr
//
LOCUS       WP_175864785             258 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia cepacia].
ACCESSION   WP_175864785
VERSION     WP_175864785.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10606006
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..258
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29378
     Region          90..232
                     /region_name="Methyltransf_23"
                     /note="Methyltransferase domain; pfam13489"
                     /db_xref="CDD:404385"
ORIGIN      
        1 mnhgsnrhpa alackvcsar apicglvdfs rcgadfiagk kvdpyagvpv yyhaceqcgf
       61 twapmfdnwt hddfaqhvyn adyarhdpey leirpqqhad lictsfadmr egrildfgsg
      121 lgllerklas rgftdvtsyd pfshpvppeg tfdtilsfev fehhpapfdl fdqimryrkr
      181 dgallfqtsl isreiiergi eqwwycvprn ghisfhtpqs ltllaqrhgl eygafspelh
      241 vvfdraatpr wldrflkp
//
LOCUS       WP_175864779            1063 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cepacia].
ACCESSION   WP_175864779
VERSION     WP_175864779.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1063)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1063)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1063
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1063
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113350
     Region          1..1051
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnlgrlsvqq pvlaivlsiv ltiagalayf slavseypdi apptvviqat ypgasaetvs
       61 qtvstpiele vngvedmlym ysqatsdgsl nitvtfkpgt dvdkaqvlvq nrvalatprl
      121 pepvqrsgvs vrkssptqlg tiflyspdqr ydplyvsnya irnvadvlkr iegvgdinpl
      181 gareysmriw ldpervasfg lspgdliaav raqntqlagg vvaqapitnq afqpnlifeg
      241 rlkrpedfsd ivvkqgkdgr lvrlkdvarv evgalayatd symlrhptia lqvlqqpgan
      301 avatmdavek kmaelardfp kgivynigyn ptafigdsih elvktiyeav vlvvfvvllf
      361 lqgwrpsiip ilsipvslvg tfaamaalgy sinnltlfgl vlavgivvdn aivvvenver
      421 hlsagagprd atlltmkevg galfaitlvl cavfvptsfi pgisgqffrq fgvtiavsta
      481 isfftsvtla palsammlka htgdhdvpap asrmaapfap amrvarrfsn afnrvfqrls
      541 daygrlvrkv vriipamgvl yvvliaatgy llvsspkgfi paqdrgylvv lvrmpdgatl
      601 ertsavarki edialsvpgv arvpvfsgvn aatgtnsans aglfpvfqpw perkarglti
      661 dtiaaemrkr laavteasiv vampppvqgl gstggfamrl edrnglgtaa lakatqdlva
      721 aanrtpgmvg vytpysatsp qvhveldrek aemlgvpsqa indavetyfg styindfniv
      781 grtyrvtaqa dlpfrvgasd larlkvrnrd gemvpigsvt riddtlgvdr aprynlypat
      841 eingdtapgp gsgfaiktme slakqvlppg isfewtdlsy qqttagntgl lvfplcvllv
      901 ylvlaaqygs wslpvsilli vpmcllaasl gvralgqdvn iltqigfivl vglaaknail
      961 ivevarqlea dgtelveavv eacvqrlrpi vmtslafilg vlplvisdga gaemrqavga
     1021 avffgmigvt ffgllftpvf yvmvrrlalr kaavatvate vvq
//
LOCUS       WP_175864827             374 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia cepacia].
ACCESSION   WP_175864827
VERSION     WP_175864827.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..374
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41828
     Region          87..327
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 masplvlihr ilgfaaarrg rtlsggspqh ngerfsnvap rpaeglgktl giawnmlfnk
       61 prntvpagml pvdsltrael daapdrslyr lghstlllkl rgefwltdpv faeraspfrr
      121 vgpkrfhapp ialedlpplr gvilshdhyd hldrdtvlal aattgvfvtt lgvgdrliew
      181 gidakkvrql dwwqsvdeag ltltatpaqh fsgrslfdgn stlwaswviv dddlrvffsg
      241 dtgyfdgfrt igerlgpfdv tlietgayda qwpyvhmqpe etvqahidlr grwlvpihng
      301 tfdlamhrwq epfervtala ivrgvelstp rmgarlalde phrgerwwrt vdervpsvat
      361 ksrrwplcts qatk
//
LOCUS       WP_175864810             188 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175864810
VERSION     WP_175864810.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..188
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20742
     Region          1..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 metkptvreq ildhattlmm lrgyngfsyr dlsdlvgvkt ssihyyfpsk ddlvleavaa
       61 ysdevlsamr aidpalpadv klslytkmfg rtlgdgnlic lcgmlaadie tlpenvrqav
      121 qaffkanegw laellkqgar egtlqfsgep etaartlyaa fqgsvlasrl fhtrarledv
      181 eavwkkrs
//
LOCUS       WP_175864832             322 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175864832
VERSION     WP_175864832.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..322
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34973
     Region          43..196
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <196..305
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 meidarttpl qrtapdhapr sltarlaali aayaphdgtf elpvrglria rvsaspphwn
       61 hgvhhaclsi vgqgakstrv gdaayvides rmlvttadlp vtgrvtrasp aepflyaqle
      121 lepariaalt psvfprglpk avdcgalgth dappeivdai arlmqliaqp ddidllapli
      181 vdeilirllr spsgarvaqv gqsdsttqri sravawirdh yldpmtvesl arqvdmspst
      241 fhhhfravts msplqcqkml rlqearrlmc lsamdaqqac rsvgyvsasq fsreyarlfg
      301 dapgrdvvkl rdqavplsri ap
//
LOCUS       WP_175864896             442 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia cepacia].
ACCESSION   WP_175864896
VERSION     WP_175864896.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..442
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45880
     Region          114..435
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mlklnlaaav vfamaataha qpslslspgp apavsggaap iaapppdarp stsltladal
       61 aaaarnnpal rgaradvdas agalmqagar pnpevsflqe gfrraertst alinqtielg
      121 gkrgarldva sygreaanas ldeqgavvra dviaafygll aaqrqlqvte esaaiaarsa
      181 dlasrraqag kvspveatka hvaaagvqie vvtargrvev areklnavmg eardgrlavl
      241 gdleavppve slpaltaqld daplariara emlrsnaavs lerarripdv tisagvkrvt
      301 tggvpdnqav vgvsipiplf ntnkgallea thkaaranad ldrertrlrl eltqayanfe
      361 aaaqeaqrlk ddilpaarva ldamsrgyel gkfsfldvld aqrtlfqgqs qyvraladah
      421 taradigrlv gtplapfapv tq
//
LOCUS       WP_175864911             252 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175864911
VERSION     WP_175864911.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..252
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27041
     Region          13..251
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mtdaskeels gkqvvaraas ilealegqts glslgdiaka tglpkstvqr lvgmlevrqf
       61 vaagatgirl gpaitrlaas ihtdvvtiaa paieaasrrv retidfsvyr gthvisifqh
      121 asdrelrvvs pigaafpiyc tahgkailst ftndeiktil rgeldsrnsr titdiptlls
      181 eiesvrktgl afdfeeheeg vcalgvsvdc atnerhaisi aaptlrfern lvelkaailk
      241 crieieayfg rk
//
LOCUS       WP_175864956             308 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia cepacia].
ACCESSION   WP_175864956
VERSION     WP_175864956.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..308
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=32047
     Region          42..294
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mssprlsrrh ftiaaasasl aactsfgdks rsdnasgatq prekpvkigi algggaargf
       61 shigvlkale argipveiva gtsagsvvga lyasgmsalq inkialdmdq aaisdwalpf
      121 rsrgllqgva lqnflnktln nrpiekmakp lgivatdlqs gqpilfqqgn tglavrascs
      181 vpsvfepvki gnreyvdggl vspvpasyar kmgasfviav disarpdgaa tnnpiemllq
      241 tftimgqtik tyeldkyadv virpnlaamg gsdfnqrnaa ilageeavar impelqrkla
      301 aargvtaa
//
LOCUS       WP_175865095             304 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Burkholderia cepacia].
ACCESSION   WP_175865095
VERSION     WP_175865095.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..304
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35019
     Region          85..242
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mrfdvellll alapvfllci aweawhlart raqdsvyawr dtlcnaalal mhqgadkiaw
       61 lfvipvyayc yrhyrvftwh dgwlsfavlf vaqdflyyvf hrashrvrwl waahvvhhss
      121 ermnfstafr qslmypvagm wvfwlplafa gfppqqvvgi vlinlafqff vhtqaigklg
      181 wleyvlntps ihrahharnp ryidrnyagv lviwdrlfgs yveetpddpp rygiverlgs
      241 nnplvatfhe wvsmagdalr vdgwrnklrt ifgppewasa yhaqiaeaan pdprtvppaa
      301 arnq
//
LOCUS       WP_175864976             233 aa            linear   BCT 11-JAN-2025
DEFINITION  YoaK family protein [Burkholderia cepacia].
ACCESSION   WP_175864976
VERSION     WP_175864976.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..233
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24334
     Region          7..222
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mdldgasrnl tvaalltlsg gyldaytyvg hghvfantmt gnvallginv sagewaaalh
       61 hvpplggfvv avfvahllgl aaqrgwmrht afasllveia flgvaasglv gassawlipg
      121 isfvatlqtl sfthleelsy tsvmttgnlr raaqklfvgl iprydagalh dsallatisf
      181 cflagavigg lvtrlvpefa lwgavlllag afaeilrraw rwretpgepp vaa
//
LOCUS       WP_175865145             138 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175865145
VERSION     WP_175865145.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12015107
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..138
                     /product="FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=14224
     Region          14..>98
                     /region_name="DAO"
                     /note="FAD dependent oxidoreductase; pfam01266"
                     /db_xref="CDD:426168"
ORIGIN      
        1 mginhlrvvv vgggivgasi awhlarsgaq vtllekqpaa aggathwsfg wvgtgsalpe
       61 farlarelgp lpvttrgalv wldsdaqtaa lideqraaga awssvqagem rvtrlsssvs
      121 apdrnparhp teegrara
//
LOCUS       WP_175865220             941 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Burkholderia
            cepacia].
ACCESSION   WP_175865220
VERSION     WP_175865220.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 941)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 941)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 941)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..941
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..941
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103169
     Region          82..876
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mpalcdicha rpavaratvm qdgerktisi cdyhfrqlmr hqsmlnpfds llgggssslf
       61 gglgdespla aevpresvdp tdafseqtle llqraaekah elrrseldse hllyaladtd
      121 vcaallkelk lspqdirsyi dehahtgtad pdapldklsi sprvkkavqy afqasrdlgh
      181 syigpehlli glasvpdsva gtllkkygvt pealrqkvvk vvgkgaedgr vdaptgtpnl
      241 dkfgrdltai arqgkldpvl graqeiesti evlarrkknn pvligepgvg ktaiveglaq
      301 rivngdvpev lrdkrlvevn insmvagaky rgefeerakq lidevtakqd elilfidelh
      361 tivgagqggg eggldianvl kpalargels ligattlney qkyiekdaal errfqpvfvp
      421 epsveqtivi lrglrdslea hhqvtfadda fvaaaefadr yitsrflpdk aidlidqaaa
      481 rvrigatsrp vdiqegeaqi aqlkreqdya tsrkrfdeak qfeeqinakq kavdekmeaw
      541 qrktgsetle vtvesvaevv srltgipvse ltqeerqkll kmeeqlrerv vgqsdavvav
      601 sdavrlsrag lgqthrpiat flflgptgvg ktelakalae tvfgdeqaii ridmseymer
      661 havarligap pgyvgydegg qltervrrrp ysvilldeie kahpdvynvl lqvfddgrlt
      721 dgkgrvvdfs ntiiiatsnl gaaiimdnlr qpeaarktdk aireelmqvl kghfrpefln
      781 ridevivfha lskenirsiv qiqldrvirt aaaqditlvm gdslvehlte agyqpefgar
      841 elkrqirqti etrlakeila drlksgdkce vdydkdsdev kfnklaapea keakdadgka
      901 kpngraaraa adakpdetpa aapppatkpg kkssgakkda h
//
LOCUS       WP_175865278             835 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia cepacia].
ACCESSION   WP_175865278
VERSION     WP_175865278.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..835
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=90785
     Region          16..789
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 masdmldnvl rggyaqfdri vkldtplgdn wltplyvkik arlgrnfevt vdassvvgdk
       61 iklsalmlqp vtlwirqidg gylpihgyvq qarrlgndga lsyfqlhfas wlsflklssd
      121 rrdwqetggw qiltdvfdkh pqasgnygqe lrtamrsysh rvqwetdwnf vhrsleevgv
      181 fprfdfakdg kshkvvmmdd lyfgpslpns emkfshagtd edfdgltqls eqqeaqsatl
      241 tlgsvdykrp dldkqastpa adldelpgqg eeylytgsqt waesdagqqq arirteewas
      301 rakryfaigs pryalpgywf kvsghplfda lpeeerelsi iasdwliqnn lpgidaltrf
      361 prslrseieh vqangagttv shrdggigff hveieaqrrk tpyrspfdhe kpemhlqtai
      421 vvtdsdeeih tddgnrvrvr tsnsrkdrnt kstswiraam pdagskrggy fplrkddqvl
      481 lgfvngdcdr pviisrlhgg atmpvwhthg llsgfrsrey ggdgfnqlvm ddssgqnrvh
      541 lysssysshl hlgylieqsd ntrgsflgng fdlksgayga vraeqglyvs tqpataqpln
      601 vtaatdplag aeavletvsk asetnraesl qdgqaalksf tdatqrtvag sasggrtagg
      661 gtgnangfak pvmllsspeg iaastqqsvh vtanqhanvv agknvnlaag kallvsvldk
      721 islfaqnlgi rifaakgsvd iqaqsgsasl vglqdvkies adgrliltaa kevwigaggs
      781 yisikgglie nvttgqilek cgswdkpsgg sgmkldplka tpvstdggrg slfsg
//
LOCUS       WP_175865270             468 aa            linear   BCT 11-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Burkholderia cepacia].
ACCESSION   WP_175865270
VERSION     WP_175865270.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..468
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=48001
     Region          2..458
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mtmlslgeaa rlipgatvhg dagvtfdrvs tdsrtvgpgd lfvalkgerf dahdflgdva
       61 argaaaalva hvpagvtmpa ieggetraal galahgwrkr falplvavtg sngkttvkem
      121 iasifaaavg adarlatagn lnndvglplt llrlsaahrl avieigmnhp getevlarlt
      181 aptvalvnna qrehqefmat veavalehaa vihalppdgv avfpaddaya giwrvaatgn
      241 rildfalhda erqndaqvtg rlhggelaid tpagavtvrl ralgehnarn alaataaalg
      301 agvalsaikq glesfepvkg rlqvkqaiag slagatvvdd tynanpdsmr aaidvlatqp
      361 aprvlvigdm gevgdegpaf hrevgayare rgidalftlg dasrdactay gdtarhfddv
      421 galvaallaa gygaqatllv kgsrymkmer vvdaltnqpa agtapaah
//
LOCUS       WP_175865291             255 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175865291
VERSION     WP_175865291.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..255
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27775
     Region          1..251
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mldiervsws pggaiavlds vtlsvadgef vglvgpngsg ktsllrcvfr yarphtgrva
       61 ldaqdvwrir pravaqriav lqqetpddfg ltvdelvgmg rtphkrpfda etaddrrive
      121 salhdvglve rraqrfasls ggekqralla ralaqqpell lldeptnhld lrhqlellar
      181 vrrlgiatla tihdlnlaaa ycdrlhvlah grvvasgapa dvlteallrd vfgvvalvdr
      241 hpvtsrprit plhpe
//
LOCUS       WP_175865317             468 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatase PAP2/dual specificity phosphatase family protein
            [Burkholderia cepacia].
ACCESSION   WP_175865317
VERSION     WP_175865317.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Pulido,R. and Lang,R.
  TITLE     Dual Specificity Phosphatases: From Molecular Mechanisms to
            Biological Function
  JOURNAL   Int J Mol Sci 20 (18), 4372 (2019)
   PUBMED   31489884
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Patterson,K.I., Brummer,T., O'Brien,P.M. and Daly,R.J.
  TITLE     Dual-specificity phosphatases: critical regulators with diverse
            cellular targets
  JOURNAL   Biochem J 418 (3), 475-489 (2009)
   PUBMED   19228121
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   5  (residues 1 to 468)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12932297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..468
                     /product="phosphatase PAP2/dual specificity phosphatase
                     family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=50034
     Region          43..217
                     /region_name="PAP2_Aur1_like"
                     /note="PAP2_like proteins, Aur1_like subfamily. Yeast
                     Aur1p or Ipc1p is necessary for the addition of inositol
                     phosphate to ceramide, an essential step in yeast
                     sphingolipid synthesis, and is the target of several
                     antifungal compounds such as aureobasidin; cd03386"
                     /db_xref="CDD:239481"
     Site            order(118,126,152..154,189,195,199)
                     /site_type="active"
                     /db_xref="CDD:239481"
     Region          321..458
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
ORIGIN      
        1 msefggdarg laaqasaaga rdasfalrlg wlavmgavff stygfanwla arrvavptfa
       61 fgwehaipfv pwtivpywsi dllyalsfff wtrradlldh vkrlltvqlv svacfiawpl
      121 rfgferpdag gvagalftll mgfdkpfnqa pslhigllvv lwavyakhvr gtlarvvlhl
      181 wfaaigvsvl ttyqhhaidv ptgaavgcla lflfplrdaa grlpgadasp gaagralarr
      241 yalgaaaval vglwcvprap gwalpagwva lalacvawiy rrgapgafqk dahgrfpvvi
      301 rwllaptiag afvnsrlwtf rqpapvride rvslgrtptt sdvrrhgfta lvdltaempr
      361 waaadaslay asvpqldlva ptaaqlaqav aalerlhgeg rdvlvccalg ygrsvlcaaa
      421 wlaagrgfgd ardalaavra vrphavwsdd gvavlqhwid hrrgaggv
//
LOCUS       WP_175865325             297 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia cepacia].
ACCESSION   WP_175865325
VERSION     WP_175865325.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..297
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31730
     Region          12..270
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 msasiktllt presdignlv vrrvlparaa rlvgpfiffd emgpavlpag rgidvlphph
       61 iglatvtylf dgslmhhdsl gfrqkivpgd vnwmtagrgi vhserspded rpreqpvhgi
      121 qtwvalpveh edttpafvhh padtlpsftr dgttvrviag tafglaspva vfsptlyaya
      181 efaaggtlal daeheergvy lvdgdlaidg aplapatmav lepgatvala sasgarvmll
      241 ggahlpgerf iewnfvsstr akidaaraaw adqtfgkvpg eenewtrqpe rkaqqaq
//
LOCUS       WP_175865334             243 aa            linear   BCT 11-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Burkholderia
            cepacia].
ACCESSION   WP_175865334
VERSION     WP_175865334.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..243
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=26511
     Region          4..211
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mqygignvwq qgdfvtrfia vvlltmsvls wsvlfaksiq lirlrrrgil verqfwqhgs
       61 ieeaqaslgr fvandpytal vdvareaadr htgsnmdsvl gpdewlgrcl gialnehivr
      121 mlrgltllas igstapfvgl fgtvwgiyha llaigaagqs sisqvagpvg eslvmtafgl
      181 fvaipavlgy naiargnrev tsrlhrfqhe lqtfftsgek irphartier paglsqpnir
      241 pvh
//
LOCUS       WP_175865407             119 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF485 domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175865407
VERSION     WP_175865407.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..119
                     /product="DUF485 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=12875
     Region          <41..114
                     /region_name="YjcH"
                     /note="Uncharacterized membrane protein, DUF485 family
                     [Function unknown]; COG3162"
                     /db_xref="CDD:442396"
ORIGIN      
        1 mnhplsatag tapepvapsh athpllrdar frehvrrrrl fawsltfvml alyfafiltl
       61 afsptllgap ivpgrptpwg ipvgfgmfva tfalvalyvf ranavhdtvv atlrhgdas
//
LOCUS       WP_175865447             730 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cepacia].
ACCESSION   WP_175865447
VERSION     WP_175865447.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 730)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..730
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78623
     Region          42..730
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mhsrrtprrg stlrpwhasl htliivcias gahaatkers daepaasasp mahsassteh
       61 qlpainvnas stvdptigyq prtssiaggs drplkeipqs vavvsssvmq dqqarslddv
      121 lgnisgvtqt ntlggtrdaf ikrgfgsnnd gsvlvdgvrt pvlhsylati drvevlkgpa
      181 sllygmqdpg gvinlvtrkp edtfggsisa srtshggsna qfdltgplgk pgqvaggtla
      241 frltgeydts rywrsfgrer naliapalsw hdantsidvs yqyvdytmpf drgtvlvngq
      301 lddalryrry eeawsqssgi qetlrtrieh rfsdawrvra tygwgrdryd qtitratafn
      361 sktgamtrss danlgrndsd qiatlgllgn vtlagmnhai yiggeyerqr sfrgdtirgk
      421 attgfnlydp vygllaaggt pnakqsdsrs vvhaystivq dsvkitdrlt avgglrwenw
      481 qqesgmgrpf vfadrsrgsv wlpqfglaya ltpaltayan vsrsfkpnva snvaaplape
      541 ygrvleaglk fslkpaitgt lavyqidkrn vavtvgdits tigtarsrgi eldvagqitr
      601 hlsvigsyay tnatdrdsnt pltnvarhtg slfavydtai anlpgrwrfg ggarlvgars
      661 gdtansftlp gyvtvdafaa yettigkfpt rfqlnvknll dktyypssns nlivavgepr
      721 lvtltttvsf
//
LOCUS       WP_175865454             321 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175865454
VERSION     WP_175865454.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..321
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34409
     Region          11..224
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(52..53,55,69..71,77,79..80,121,223)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(52,54..55)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(77,80,83,90)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(113,117..120,122)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(118..119,142..144,196..197)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          237..321
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 msaatltvqv arkwqeardi cgfefvsddg splpgfeaga hidvhlpggl vrqyslcnhp
       61 ehadryqiav lrdadgrggs raihdevrqg dtlrigmprn qfplapdaph hlllaggigv
      121 tpilsmaerl sssgmpfdmh ycarstdrma fverinaagf hdrarlhvdd gdpgqrfdla
      181 avlaaapagt hlyvcgprgf mdavlnaare rnwaearlhy effggavass gadrafqvri
      241 assgrvidvp aectviaala angvdvltsc eqgvcgtcat rvlegepdhr dsylteaeqa
      301 agdqfmpccs rsrsdllvld l
//
LOCUS       WP_175865482             521 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175865482
VERSION     WP_175865482.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..521
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=55818
     Region          1..521
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 metydhivvg ggsagctvah rlvkagrrvl lledgpkdds lfiripatfi rvlgtrrtvt
       61 fesepqagaa grrtyvpqgr tlgggssvna mlyvrgtrdd yddwaalgca gwgwddvlpv
      121 frraeshlrl sepfhgtdgp lkvgdtrfrh plslafvkaa qetgiayndd fngaaqqgvg
      181 fyhttifdgr rgstaatyla dalrhpnlrv ltgcrvtril fdgrratgve wrtasgatgs
      241 aaaradvvla agalstpkll mlsgigpgah lhahgidvrh dsrdvganyq dhlevsiygr
      301 shapvsllge drglkalrhg lqwmlcrtgl ltsnvvesga fvdttgsgrp diqfhvlptl
      361 vgdvdreplp ghglsinpcl lrprsrgsvq lrgndpaapi lfdsgalsdp advdglvrgv
      421 alarriirap slarivreae tltdtalady vrrraktvyh pagtcrmgnd ehavvtprls
      481 vqgvdglric dasvmprivs gntnaptimi aercaefmla e
//
LOCUS       WP_175865488             205 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cepacia].
ACCESSION   WP_175865488
VERSION     WP_175865488.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..205
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22255
     Region          4..194
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mefltlsalp agmlfalvts itpgpnntml lasgvnfgfr rtmphlfgis tgvailmlcv
       61 gfglgeafkr lpllytilev asvayllyla wrigtsgevk ahggkprpmt fieaaafqwi
      121 npkawmmvlt aattirlsgd ygmnaawmav vfiligfpci slwaafglgl rrflsnpral
      181 rlfnmtmavl lilslyplva hllpq
//
LOCUS       WP_175865499             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175865499
VERSION     WP_175865499.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33226
     Region          8..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(104,108,151,165,167,226,243,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(105..106,110..111,113..114,117,121,123..129,194,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mddflsphla lfvdvvdqqs fsaaarrlgv aassvtrrid rletqlgirl lhrtthalrp
       61 teagqllygr atrmlaelrg lqedlhsqhd epsgllrvdc papfgrrhlv aalaafmqrh
      121 palqvdlvlt dsmvdlqgar lgsdvdlavr igpledtrlv atvlapqrrv lcasaaylar
      181 rgepdapdal aghdclawhg vpppgawrfg errhapaqpr frsnhseall eaaidglgla
      241 hlptwlagda lrdgrlravl pqfaaapepa tihvlrqpar gtarasrlva flatwfaqpa
      301 wdaawa
//
LOCUS       WP_175865502             309 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia cepacia].
ACCESSION   WP_175865502
VERSION     WP_175865502.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..309
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31914
     Region          29..307
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          204..307
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(209..210,243..244,247,251..252,255,297,301)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mhrmnhvlaa llasglfigs ctafaqntga tvtpvgngtv attalpantg aapgtasgav
       61 vhgtagtast itpppaaatp gqvvvggkvp deatkaavlq klrdtygatn vvdqievgdv
      121 atppnwsanv qkllgaqlkq iskgqlking tqiemkgevh neaqrqqlas dmantlnpty
      181 tirnglrvsa seqgvldqtl anrtiefetg satltpqgkl ildqmaaala kmqnrtvdii
      241 ghtdnsgnrt snialsqara davkgylitk sippqqmttt gvgpdqpiap ndtadgrarn
      301 rriefrvgq
//
LOCUS       WP_175865512             410 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia cepacia].
ACCESSION   WP_175865512
VERSION     WP_175865512.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..410
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44179
     Region          1..291
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mrlalvlmgg garaayqvgv lkalaeiare adpqrhtlpf avvcgssaga inatsiasha
       61 ddfshgvrrl lefweplrad yvyrtdwlgi aaagarwlat mtfgwaarrs prglldnapl
      121 ahllqrelsf hrieqmlear llhalsital syssgrhltf yqaaepiqaw rraqrtarlv
      181 dlsashllas saipfvfpav plvldgqiey fgdgsirqia plspaihfga hrivvvgaad
      241 prpeipaang tglvrgyptl aqigqqvlas vfldsigsdi eriehinrmi ehlphqvevd
      301 sgwrhvdvla iapserieli aakhlkqmpa tmrgllgaig gsqpagasfa syllfeeaft
      361 relielgyrd graqrdtlag wialadggsa paagmgmprd dglatgeirv
//
LOCUS       WP_175865527             241 aa            linear   BCT 11-JAN-2025
DEFINITION  copper homeostasis protein CutC [Burkholderia cepacia].
ACCESSION   WP_175865527
VERSION     WP_175865527.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Latorre,M., Olivares,F., Reyes-Jara,A., Lopez,G. and Gonzalez,M.
  TITLE     CutC is induced late during copper exposure and can modify
            intracellular copper content in Enterococcus faecalis
  JOURNAL   Biochem Biophys Res Commun 406 (4), 633-637 (2011)
   PUBMED   21362400
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Li,Y., Du,J., Zhang,P. and Ding,J.
  TITLE     Crystal structure of human copper homeostasis protein CutC reveals
            a potential copper-binding site
  JOURNAL   J Struct Biol 169 (3), 399-405 (2010)
   PUBMED   19878721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..241
                     /product="copper homeostasis protein CutC"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24382
     Region          8..237
                     /region_name="CutC"
                     /note="Copper homeostasis protein CutC [Inorganic ion
                     transport and metabolism]; COG3142"
                     /db_xref="CDD:442376"
ORIGIN      
        1 msrnaassil leviattvgd akaaaragad rlelvtaite ggltpsvgli eavvaavpip
       61 vnvivrphsr sfvydaddlr vierdvraav aagangvvfg aldargdvdl galariaaaa
      121 dgraltfhra fdvsrdlnaa fdallrvpvv tsvltsgghp svldavatit rlvrqtagst
      181 ctvlagsglt vdavgdfvra tgvravhfgs gvrprgevla pvdellvakv ratidgaash
      241 v
//
LOCUS       WP_175865533             212 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia cepacia].
ACCESSION   WP_175865533
VERSION     WP_175865533.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..212
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23145
     Region          4..212
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mnayrlylsp gacslaahia leetgapfdv eivsvqkqqn learylaina karvpvleip
       61 geprvltetp ailtylarry pdaqllplgd plrearchew lawlvgwvhg vgygalwrpg
      121 rfigdpalhg avsthgrgvi eaanetieaa lvdgrtwaep gahsivdpfl fvlyrwgvai
      181 gldmarhpaw tahaqreadr pavrralare aa
//
LOCUS       WP_175865615             473 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175865615
VERSION     WP_175865615.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..473
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50362
     Region          2..473
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mmsseafvsa crdaigadhv ltdphdtepf ltdwrrrykg aacavlkpan taevaalvkl
       61 anahgialvp qggntglagg atpdasgsqa vlsvarlnrv raldphnnti tveagvilad
      121 vqarareggr lfalslaaeg sctiggnlst naggtavlry gnarelclgl evvtpqgeiw
      181 dslrglrkdn tgydlrdlfi gaegtlgiit aavmklhplp aaqvtalaal esphaaldfl
      241 alaqraagpl ltgfelmsdf cmqlvgkhyp qlrypfaqth aqtvllelsd neseaharal
      301 feklmeeafe aglvvdavva enlaqsrafw dlrehiplaq adeglnikhd iavpissiar
      361 fidetdaaiq qaapgarmvt fghlgdgnlh ynvqmpeggd pkaflaafqa pinrivydnv
      421 hrhhgtisae hgigqlkidd aqrykspvet tlmrtlktal dprglmnpgk vlr
//
LOCUS       WP_175865619             922 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia cepacia].
ACCESSION   WP_175865619
VERSION     WP_175865619.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 922)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 922)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..922
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=98730
     Region          18..834
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msiatalrnf asglvdwnnr pvalhfgqaq havghllalh hadireglms gidgqltcis
       61 thahlaptlf lglpvsvrlt tdrgdvrain aivhdmqagq sdgeltvyql ricdalslmd
      121 rrinsrvfrs rniidilgtl lnewrqrspa larafdfdls glraerypar eltrqvnesd
      181 arfvrrllrr egitvfakaw avgnargtad erpihtlvfc ddplrlpesp agtvrlhprd
      241 sgtaqrdtvt lfahhqrlsp gkagrpswdy kkarmddsai atsidqgdag ndlarlltdv
      301 aidiphvgds wndhdrithd rilahqfaae rydgighvrd mpvgcwftlt gdpeldmkpa
      361 eqrqfvvtsv rhdirnnlpk dlagrvialy aasrnlaqaa ppapanaseq adtryenhft
      421 cvrrgvpltp sydptidlpp ahlltgtivg tegeevfcda agrvrvrihg fdpadhehaq
      481 gagtngsagd sapirvgasl aganfgtlfl prvgmevllg clsgdpdrlv iigvlsngan
      541 ppatfthtga lpgnryvsgi ktkeikgary nqlrlddtps qisaqlaseh ahtqlnlgyl
      601 tqprkdghga drgegaelrt daaaalraaq gilfstyart catggqldrd eliqlldqcm
      661 mlfnslgdya gqhggraadt agqekivdaf rhwkpdlada gsagdtsalm afgaqagslh
      721 vtprthvmya genidqiaqr hvqvasgeri nlhgghgvam fahsggvsai anrgkvtiqs
      781 qdddtqvdsa kniqltaagg klagmandqv vfvtsggayl klnggdielg cpgtftvksa
      841 ghawggpast stdmptfdha plgrvpklvr atdgdavagf dghlqrasea lsnlttdaag
      901 elpavhgdqf etlsvqfikk ng
//
LOCUS       WP_175865628             498 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia cepacia].
ACCESSION   WP_175865628
VERSION     WP_175865628.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..498
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53589
     Region          72..450
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mtmlsispri gaaaavlafl agcttfskdg gfdavssvas erigkdavvv rtdadreavd
       61 trtkellakp lsiddavqva llnnrglqas yaelglsead lvqagrlpnp rfafsrtrag
      121 dgeltlgrtf sanvfalltl platnierrr feqtkletad amlkvaadar rayveavaae
      181 qaanyagqvr daasaaaela qrmrqagnfs rldyareqaf hadavaqhak arqqavaare
      241 kltramglwg ertqyalper lpdlpkarpn lpdlerfamr nrldiqaakl qtqgvasslg
      301 lskatrfvna vdlgyvndye tgkghehgfe isveiplfdw ggakvaraea vymqsanrla
      361 ktaidarsev rdsyaayvts ydvathyrde vvplrktisd elllryngml asvfellada
      421 reqvgavngy idalkdywla etdlqmavgg rlptpgdvpr atpsarpdsa snadaapqpa
      481 stpaaqsapa tqthpegh
//
LOCUS       WP_175865669             226 aa            linear   BCT 11-JAN-2025
DEFINITION  lytic transglycosylase domain-containing protein [Burkholderia
            cepacia].
ACCESSION   WP_175865669
VERSION     WP_175865669.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..226
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - lytic transglycosylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=23836
     Region          2..187
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 mrrrffwliv lslgiaqqvs aqqtpavpas apdvlasapa vasaplanad dqpneanrri
       61 tsyltkkfgv akeraaklad ivsvtatkys lppalvyaii siesrfqeka rgqhgatglm
      121 qvvpsahrgm lrnvkdltep nanveagsri lssyvkaagg nvqaglksys ggssayaakv
      181 mqrvdsfrfv lepdddakaa netkarmvpv sestststst sarnaq
//
LOCUS       WP_175865681            1059 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cepacia].
ACCESSION   WP_175865681
VERSION     WP_175865681.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1059
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115400
     Region          11..1037
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msvsyeegrf nlsawalrhq alvvyliala tlagilaytr laqsedppft frvmvirtfw
       61 pgatarqvqe qvtdrigrkl qetpaidflr sysrpgesli fftmkdsapv kdvpetwyqi
      121 rkkvgdigyt lppgvqgpff ndefgdvytn iwtlegdgft paqlhdyadq lrtvllrvpg
      181 vgkvdyfgdp dqrifievnn aqltrlgisp qqlgqainaq ndissagvlt taddrvfvrp
      241 sgqfdnvdai adtliringr tfrlgdlatv krgyddpvvt qmraagsgaa gsgaagkavl
      301 gigvtmqpgg dvirlgkald aeskdlqaql paglklvevs smphavahsv ddfleavaea
      361 vaivlvvslv slglrtgmvv visipvvlav talfmylfdi glhkvslgtl vlalgllvdd
      421 aiiavemmav kleqgytrar aaafaytsta fpmltgtlvt vsgflpiala ksstgeytrs
      481 ifevsaiali aswfaavvli pllgyhmlpe rkrhaheahl pddhehdiyd trfyrrlrgw
      541 idwcierrfv vllitgalfv vammgfslvp qqffpssdrp ellvdlrlpe gasfaatlre
      601 terlekvidk rpeidhsvsf vgsgaprfyl pldqqlqlpn faqfvitaks vkdreklatw
      661 lettlreqfp avrwrlsrle ngppvgypvq frvsgdsiat vrsiaekvaa tmrgdvrtvn
      721 vqfdwdepae rsvrfeidqk karelnvtsq dvssflamtl sgttvtqyre rdkliavdlr
      781 apkadrvdpa klaglalptp ngpvplgslg rfkptleygv vwerdrqpti tvqsdvraga
      841 qgidvthavd aklnalraql pvgyqinigg sveesakaqk sinaqmplma iavftllmiq
      901 lqsfsrvlmv vltaplglig vvatllmfgq pfgfvamlgv iamfgiimrn svilvdqieq
      961 diaaghgrvd aiigatvrrf rpitltaaaa vlalipllrs nffgpmatal mggitsatvl
     1021 tlfylpalya twfrvkrder dpqngppsgg tapaapsga
//
LOCUS       WP_175865683             342 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175865683
VERSION     WP_175865683.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10859374
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..342
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38615
     Region          3..98
                     /region_name="HTH_NolA-AlbR"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators NolA and AlbR; cd04788"
                     /db_xref="CDD:133415"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133415"
     Site            order(51,54,58..59,68,80,84,90,94,97..98)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133415"
     Region          <259..>305
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 mrlkvgelak rsgltvrtlh hyhaiglltp saradngyrl ydrhdiarlh qiqalrrfgl
       61 slveigdhln qpgtplvdlv akqialldrq laqtaqlrer lvslhaqlaa gtepeladwl
      121 ttlelmtvyd kyfseeelar lpmyqksqag daewialvde vralhdagvp aederprala
      181 srwmkllvrd tnndprllak lnlmheqepa mqskigista lrdyvlrass enkmrifeky
      241 lapdeirfmr ahygeramew pqlmgdvrda idagarpasp egralaqrwl elfcsyaghd
      301 pathakfraa mmnepaltqd twvddtligf vreamaqlap ar
//
LOCUS       WP_175865692             330 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Burkholderia cepacia].
ACCESSION   WP_175865692
VERSION     WP_175865692.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..330
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=36413
     Region          6..285
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mgplaatfde ileacalgrs gpprqvserv whlptddggv avklyaaghq araareaavl
       61 ahfethgdtr fhvqalkrta agaplwtgan ahamltrwet gqfrtydtfs paewealgas
      121 laalhlsler lqlpsldtir arliaidada vrrslldaln harsnenaan lrryvdlalr
      181 mldryypgsi dafpaddpqh pihndynqfn ylftgtlppl ildweatiga preyelvrcl
      241 nhlpleapql aeafvraylr vrpvdparia wavdaaclqh alklwivqgw lddpsrfash
      301 lsgavtmasa mvdardglvd ffsrcieagr
//
LOCUS       WP_175865751             310 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175865751
VERSION     WP_175865751.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..310
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33114
     Region          3..309
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mthrvamlvy pgfqvldaag pvsafemady arapyyavri vaarpglvrs ssgvswhaep
       61 lpdaadldtl lvaggdgvda amadaatcaf vrrcaargir vasvcsgsll laaagvldgr
      121 latthwgcge rfarafpqvr laldriyvnd gpfwtsagit agidltlali gedrgerlar
      181 avakrlvvyy rrpggqsqfs alieldsaqg rfkplldhir rnlgarlrvs dlaeqacmsp
      241 rqfarafqte tgltpakave klrveaaraa lesgaaslqr vanecgfgdt enmrrsfhrw
      301 lgvapsalrs
//
LOCUS       WP_175865770             455 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175865770
VERSION     WP_175865770.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..455
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49153
     Region          23..412
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,154,
                     157..158,161,259,262..263,266..268,271,299,303,352..353,
                     357,361,377,380..381,384..385,388)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnppspalpg rdplasavsk vkwhvlplvl imfianyidr vnvgfvdrhl easigigaaa
       61 yglgaglffv gyalfevpsn llmqrygarv wlarimatwg ivaaamafvw ndtsfyalrf
      121 llgaaeagff pgvvlylsqw lppqergkam aiflggsafa svlsgpvtga llsirgfglk
      181 gwqwmflieg lfsvalcgas wlllkshird atwltaeert alqnaldeer aardvrsnvp
      241 vratallrdp qimlfcflyf siqltiyaat fwlptiirkm ggltdfqvgl yntipwmiai
      301 gamygfavls skwkhpqrwl afalvlaacg lfastshdpa wsfasicfaa lgfkaaaslf
      361 wpipqgyldt rvaaaviali nsvgnlggfv aptafgylkq htgsitggly alaiaslvaa
      421 vaalfarthr rsdpprglpa dtaltnasml rhaeh
//
LOCUS       WP_175865855             520 aa            linear   BCT 11-JAN-2025
DEFINITION  S41 family peptidase [Burkholderia cepacia].
ACCESSION   WP_175865855
VERSION     WP_175865855.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..520
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55289
     Region          72..418
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mmpstravlr lavcaavtaa flpcaspaga qqpapappas apaasssssa spatarppsp
       61 cppdwepqic elkaavevlk rqhltdvdig alldatthag iktlpyarff dakeeqerre
      121 derrardgtp gigivfetrp dglhivdvip dapaeqagvr pddlvvamnd tsvvgidaad
      181 ltklakgdag vplkltvqrg pshamlsfap vrtilkphpa takrlagdil ytrlssfpep
      241 avgayidavq aarragppvk gvildlring ggalnaaigi talyagrdrt amvtvergda
      301 nrrryttnwp dyalpvmhgq dplaplqadd wwrtvplvvl vdgqsasaae ataaalkdlg
      361 rakllgmpty gkglaqtgvd lidgtrlnft farnlrpngc pmdgygvvpd wlvpprrdsd
      421 vdgvllwyre adlprapyad rlapdpfakv rkerqklreq ralakidsak saalpqrefg
      481 tasdwqlgqa laalagrpvr tidakpqlmp aqpvceragn
//
LOCUS       WP_175865876             321 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175865876
VERSION     WP_175865876.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..321
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34481
     Region          5..320
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpkvvgifav pgvqlldvsa pldvfaqana eygkpfytlr iiagesgpir sssgaqllpd
       61 wivpdiperi dtllvagaps agrialrtdv lawlraaavq skrygsictg afilaatgll
      121 kerhvtthwa aadalaeayp slavdadaly vrdgklrtga gvtagldlal alveedlgre
      181 iarrvaaqlv mffkrpggql qfsrkgearp agrsvlqevq rwiaanpele hsvaemakha
      241 gmsprhfarl fraevgmtpa awveatrisa arhllenghd tpkqvaakcg fanvdtlrrs
      301 ftrhvgitpa eyrkrqavla e
//
LOCUS       WP_175865906            1032 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cepacia].
ACCESSION   WP_175865906
VERSION     WP_175865906.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1032
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112004
     Region          5..1014
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msdfnlsala vrersvtlfl iilisiagvv aflklgraed ppftvksmtv itawpgataq
       61 emqdqvaepl ekrmqelrwy drtetytrpg lafttvtlld stppadvpee fyqarkklhd
      121 eagnlppgvi gplvndeysd vtfalfalka kgepqrvlvr daeglrqrll hvpgvkkvni
      181 igeqaeriyv sfshdrlatl gvtpqeifaa lnnqnvltpa gsidtagaqv firvegafdk
      241 lqtirdtpiv vqgrtlklsd vatvergyed patfqirnng epalllgvvm rdgwnglnlg
      301 naldaevasi nagmplgmsl tkvtdqavni hsavdefmvk ffvallvvmv vsfasmgwrv
      361 givvsaavpl tlagvfvvma atgksfdrit lgslilalgl lvddaiiaie mmvvkmeegy
      421 nrvqasayaw shtaapmlsg tlvtavgfmp ngfarstage ytsnmfwivg ialitswvva
      481 vvftpylgvk llpdiavieg gheaiyntrn yqrfrrflgr vigrkwmvag ivvasfvvav
      541 mgmglvkkqf fptsdrpevl vevqmpygts ieqtasatek veawlakqpe aqivtsyigq
      601 gaprfylams pelpdssfsk ivirtsdehq realkfrlrk vvaeglvpga qvrvtqlvfg
      661 pyspypvafr vmgpdagtlr aiaaqvertm kaspmmrtvn adwgprvptv hftldqnrlg
      721 sfgltsssva qqlqflltgi pvthvredir svelvarsag dtrldpqrie gftlignagq
      781 rvplsqvgkv dirmedpilr rrdrtptitv rgdiaeglqp pdvstamlaq lqpiiaklpg
      841 gyrieeagsi eeankatnal aplfpimial tlliiifqtr siaatmmvfa tsplgligvv
      901 ptlllfnqpf ginalvglia lsgilmrntl iligqieent ragmapfdav veatlqrsrp
      961 viltavaaml afiplthsvf wgtlaytlig gtfagtiltl vflpamysiw fkirpgaees
     1021 hsalepsasv ts
//
LOCUS       WP_175865974             224 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein,
            partial [Burkholderia cepacia].
ACCESSION   WP_175865974
VERSION     WP_175865974.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         <1..224
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
     Region          1..223
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 vdianvkmsm npfdeiavee avrlkeagva teviavsvgv tqaqetlrta laigadrail
       61 vesndsvepl avakilkalv dkeqpqlvil gkqaidddsn qtgqmlaala glpqatfask
      121 vtvadgkatv arevdggaet lsltlpavvt tdlrlnepry vtlpnimkak kkpletvkpe
      181 dlgvdvaprl ktlkvaeppk raagvkvpdv ktlveklkte akvl
//
LOCUS       WP_175865909             399 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid aminotransferase [Burkholderia cepacia].
ACCESSION   WP_175865909
VERSION     WP_175865909.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Alexander,F.W., Sandmeier,E., Mehta,P.K. and Christen,P.
  TITLE     Evolutionary relationships among pyridoxal-5'-phosphate-dependent
            enzymes. Regio-specific alpha, beta and gamma families
  JOURNAL   Eur J Biochem 219 (3), 953-960 (1994)
   PUBMED   8112347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..399
                     /product="amino acid aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42599
     Region          3..388
                     /region_name="PRK09257"
                     /note="aromatic amino acid transaminase"
                     /db_xref="CDD:181731"
     Site            order(107,142,209,254..256,292,295)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mslfsavqla prdpilglne afnadarptk vnlgvgvytn eegkipllra vreaekvrve
       61 aglprgylpi dgiaaydaav qklllgndsp liaagrvvta qalggtgalk igadflrtvn
      121 pnvkvaisdp swenhralfe aagfeviayp yydaatngvn fegmlsalng yeagtvvvlh
      181 acchnptgvd lteaqwqqvv dvvkarnlvp fldmayqgfg enieadaaav rlfaaadlna
      241 fvsssfsksf slygervgal siitsskeea trvlsqlkrv irtnysnppt hggavvaavl
      301 aspelyaswv qelgemrdri ramrnglver lkvsgvdrdf sfinaqrgmf sysgltsaqv
      361 drlrdefgiy avgtgricva alntrnldav anavaavlk
//
LOCUS       WP_175866012             167 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase, partial [Burkholderia cepacia].
ACCESSION   WP_175866012
VERSION     WP_175866012.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         <1..>167
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          45..>166
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 vgaqnsvkvd lsgievsnrt ieqdglsvpv tivrpegvkg kppvfmffhg ggwilgdfpt
       61 herlvrdlvv qsgavavfvn ytpspeaqyp vainqayaat kwvaahgdei gvdgsrlavv
      121 gnsvggnmaa vvslmakdkg gpairfqgll wpvtdhnfnd gsyiayq
//
LOCUS       WP_175866126             733 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia contaminans].
ACCESSION   WP_175866126
VERSION     WP_175866126.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 733)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..733
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..733
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80070
     Region          33..716
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 msasspastp aggpfaawaa afgdwartdg aawlylfkal laafialgvs mrldlpapkt
       61 amttvfivmq pqsgavlaks fyrvagtifg liatlafvgl fpqqpqlfll aiaiwialct
      121 agaarnrnfr sygfllagyt taliglpasq hpdgafmsam trvseviigi vsagvvsalv
      181 fpqytgeqmr ttvrkrfgsf vdyvasalsg qldrahieti htrfvadvvg feaarsmavf
      241 enpdtrmrsg rlarlnsefm sassrfhalh qlmnrlhaag aqaaidaiep yfreiapllt
      301 rhgepvrtsi daahsaeqll awrdalprri ratraeletq pgfplldfdt aaellyrfit
      361 dlqeyaatya slatathere rwieryeprt nrtaamiagi rtatvilalg wfwietawps
      421 gvmlvlnaaa tcalassapr ptamaaqmgm gtalavctgf lltfgiypri dgfwllcaal
      481 apllaigiym tlkpklagyg mgyliffcfl agpdsithyd pmsfmndala lllsmlvsai
      541 afavlfppta pwlkkrlfad lrhqavaach arlaglrtrf esgardlmyq ahtlsadqpd
      601 vqrdalrwmf avletgnaai dlrhelatlp pepryapttp wrraietmra alsslfarpd
      661 aerfdatlaa vndaidatrq tldaftptre erhrlqrils hlhfvrtall dpesplaaln
      721 rnrpvrpqpg ass
//
LOCUS       WP_175866134             409 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            contaminans].
ACCESSION   WP_175866134
VERSION     WP_175866134.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 409)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..409
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41826
     Region          32..313
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mrsrtlagvv rwslfsacvv lpawlwphga vlgylaqtaa lvvlalsynl qlgttgllsf
       61 ghaafaglga faaahwfnhf ggplpllplv ggvagagfgf aagllatrrs gtafamitlg
      121 lgecvaaaaw svpawfggig gvpidrasgt pwgawhfgap vqayaviaaw clasawamha
      181 ltrtplarla navrdnpvrv aalgsdprrv rlalvtcasf fagvagtltl idveiatpds
      241 vsmarsatvl iaaviggtga ffgpaagaav ltvlsivvag vsrawalylg vlfvvivvaa
      301 prgiagivqa lahalrrgap aaerwrmlca agacvfwgva lvcaaelgya wrfaqddgag
      361 fafgawsida dtpagwavac safgigtllw gwrarlvpgg qarkredgr
//
LOCUS       WP_175866154             194 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia contaminans].
ACCESSION   WP_175866154
VERSION     WP_175866154.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..194
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21153
     Region          7..161
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mdshiasvel kkayrllnhg ptvlvsarhd gvdnvmaaaw acaldflppk ltvvldktak
       61 trelversgt fviqvptaaq lrlthavgsh slaerpdklr eagvtlfdve ghdlpfvagc
      121 sgwlacklip ephnqqaydl figevvaaws dtrvfrdghw yfesadpalr slhyiaggnf
      181 yaigeslhvd pdak
//
LOCUS       WP_175866205             156 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia contaminans].
ACCESSION   WP_175866205
VERSION     WP_175866205.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 156)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..156
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17134
     Region          1..153
                     /region_name="MutT"
                     /note="8-oxo-dGTP pyrophosphatase MutT and related
                     house-cleaning NTP pyrophosphohydrolases, NUDIX family
                     [Defense mechanisms]; COG0494"
                     /db_xref="CDD:440260"
ORIGIN      
        1 mkrgaaprtv scgvvildaa grvflahatd tthwdipkgq gepgetpada alrelleetg
       61 ivfgadrlld lgrfayrhdk dlhlfavrva ddevdlahct ctslfpsrrd gsmipemday
      121 rwtlpadida yasrslarlf rtklslvelh qrlmgs
//
LOCUS       WP_175866207             265 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia contaminans].
ACCESSION   WP_175866207
VERSION     WP_175866207.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..265
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28985
     Region          11..261
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mrrgeppvkh mldiervsws pggaiivlds vtlsvaegef vglvgpngsg ktsllrcvfr
       61 yarpdagrva ldaqdvwrmr pravaqriav lqqetpddfg ltvdelvgmg rtphqrpfda
      121 etaddrrive salhdvglve rraqrfasls ggekqralla ralaqqpell lldeptnhld
      181 lrhqlellar vrrlgiatla tihdlnlaaa ycdrlhvlah grvvasgtpa dvlteallrd
      241 vfgvvalvdr hpvtgrprit plhpe
//
LOCUS       WP_175866236             462 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia contaminans].
ACCESSION   WP_175866236
VERSION     WP_175866236.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..462
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46410
     Region          25..450
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,151,
                     154..155,158,280,283..284,287..289,292,320,324,376..377,
                     381,385,401,404..405,408..409,412)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mahtgelaaq aqrtikrrgl tllilclavl vaqvdtavvn latrtigdyf hagvgalqwv
       61 vdsynltyav llltggllad lygrrrifma gtalftaasl lcalapsiav liaaralagv
      121 gaalllpasl aivrvvwrdp vergralgiw aacngvamai gptlggvlir hfgwrsiffv
      181 vvplsvaaml lavpavpess dprgrhfdga aqlagalslg alayaaivfr dspvacalag
      241 cvailsfiaf iaierrhgaa alvpldifri safrgaiaat tgmtfgmygv lfllplawqs
      301 igrldstgag lallpmalvf vvvspcsgpl servgtrttt aggvaviasg lvvigasags
      361 pgligaeigl altglgmgia tgplmtvavg avdaarsgta salvnvarms gatlgiavlg
      421 tlfavthggt aglraamfag aviqligata saisvhrgrp aa
//
LOCUS       WP_175866245             190 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            contaminans].
ACCESSION   WP_175866245
VERSION     WP_175866245.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..190
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=20121
     Region          1..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          82..179
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam13305"
                     /db_xref="CDD:463838"
ORIGIN      
        1 maragitldk lveagaqlad etgfeqltga alarhfdvkl aslyshipsf ddlksrialf
       61 alkeladrat dalagrtakd altalanvyr dyarehpgrf aaarhpvsae raaesaggql
      121 vrmtsavlrs yaipdaeqah airllggffm gyvtlesagg fahsapasda swsrsldald
      181 vmlrhwpaaa
//
LOCUS       WP_175866270             340 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA-binding protein [Burkholderia contaminans].
ACCESSION   WP_175866270
VERSION     WP_175866270.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13774834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..340
                     /product="DNA-binding protein"
                     /calculated_mol_wt=37347
     Region          26..144
                     /region_name="KfrA_N"
                     /note="Plasmid replication region DNA-binding N-term;
                     pfam11740"
                     /db_xref="CDD:432038"
     Region          <116..>337
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
ORIGIN      
        1 msdlaadesr ltaeierlka dfpktrelyr eacalmffrf gitptanrly qlvrkgsmst
       61 ptavlgefwa elreksrvri ehpdlpadlq aaagelvaal wnrssadaag aldalraeve
      121 aervaakaev aalqaelart etaleqrtaa llaaqvriqe leqaraadda srqaleaeie
      181 rltadnaegd ralaqaradf ttqldrlred agraeerlra sekralqeid rerlaaarlq
      241 keldaaalra eqrdaqqrke vaalqaqlgd amhrcgvlqg qldgaqatda argkeldalr
      301 remtalsrrs alrgakaapa aqrderrart rkradeappr
//
LOCUS       WP_175866293             236 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175866293
VERSION     WP_175866293.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..236
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25377
     Region          8..228
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 maprivppal kaveqetmad kvyqqlreal msgrfapgqa lslrsvaeav gsstmpvraa
       61 ltrlhaeral vdgpnralvv ppmtldmlde lrdvrialeg ciaeracgrm sdaqiaavrk
      121 icetmqahve agrsraylqs nfafhsaiya hgasestlai venlwmrvgp flnmvaldip
      181 hmlrsmdahr aivdalerrd gagvragial diggaahdla etlraeqapr tvnakp
//
LOCUS       WP_175866302             215 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia contaminans].
ACCESSION   WP_175866302
VERSION     WP_175866302.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..215
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23127
     Region          1..212
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msfrlylsfl aasavlvyap gpvnlltmnq alragwrral pcvwggtlav llqlaltalc
       61 lnslvhlder altvlrwaga aylvwlgckq wlsrtpagap aasarpagma tpdtdshral
      121 fwrgvatsgl npktllffps ffpqflipsa dwslnqqfll laatfavlfa ggvasmalfs
      181 hrlsralqrp armramnrvt ggllvgmgai mvgwn
//
LOCUS       WP_175866310             450 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia contaminans].
ACCESSION   WP_175866310
VERSION     WP_175866310.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..450
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47871
     Region          19..421
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msaslaassp saqprslrll ptddadadga riaalldrla pelaadaarn dadgrfphen
       61 farlhragli aqvvprehgg agatlaqasr ivaavaradp atalvltmty lqhralgrad
      121 nrwpaqvrra vfdsavtqga linalrvepa lgspsrgglp etharrdgdg wrlsghklys
      181 tgipalrwla vwartdepap rvgvflvprd rdadgdrirv ieswnhlglr asgshevvfd
      241 dvrlpadhav dvrapdawav saathadada qadqqawmva llgslydava rasrdwlvgf
      301 attrapsglg aplatlprvq eavgeiegwl hanrvllddh iartdaghap tvttsglvkr
      361 tvtehairvv eqalklsgnh glsrvnpler hyrdvlcsrv htpqddaiav aagravleaa
      421 srseteratk getetsgasv netergrgda
//
LOCUS       WP_175866312             275 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia contaminans].
ACCESSION   WP_175866312
VERSION     WP_175866312.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..275
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29423
     Region          23..270
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mvsaavless vassvaaasa vtaprgarid irrvshafdg pggalpvldd vtlsvaagef
       61 vallgpsgcg kstllrlvag ldaarhgtia qdgvpieqpd psrivvfqdp tlypwrrvra
      121 nvalglearg vartaqhrvd dalarvglqe fanvfphqls ggmaqrvala ralvndprll
      181 ildeplgkld sltrltmqae ltalwqrdgf sallvthdve ealflaqrvi vfgprparii
      241 aelhvdlpyp rhrgdprlae lrhdalrhlg fdasw
//
LOCUS       WP_175866318             363 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia contaminans].
ACCESSION   WP_175866318
VERSION     WP_175866318.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..363
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=38572
     Region          17..363
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mksraersir avvltgsata aclaapvaha qssvtiygim dagiefanha apeggnsvkl
       61 ksgnkntsrw glrgvedlgg glkavfrles gidlangasd dgpdsifarr atvglkgkwg
      121 eltlgrnftv tydymmpfdp mgysqnyswa sssmatggrk dgifsrssna vrydgefsgf
      181 kfgalygfgn vpgsvktssk ydfalgyetg pfaavvtfdr qngaadsvtp adtvnyiqgi
      241 haglsydfgn lktmagyrny krthrtsaan qlsdmywvgg syqftptfsl igavyhqnik
      301 ggtdadptlv smraqyalsk rtvlyaagaf aigkhgqkvg vsrdfngygt tqvgvtagiq
      361 qrf
//
LOCUS       WP_175866330             424 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia contaminans].
ACCESSION   WP_175866330
VERSION     WP_175866330.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..424
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41728
     Region          6..417
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpshvespaa hhagsltifq gaalyigavl gtgvialpal aaevagpasl lawaalvvls
       61 gplaatfaal garypdsggv styarrafgp kaaaivgwcf yfavpagapa aamfggayva
      121 avtggghttv ivtaaaliat vsaanafgvt vsgrmqlvls allvtlllaa vlasaphaht
      181 anlhpfaphg wlavgqaaal lvwsfagwea ithlaaefrr pahdmprsag iavvvvglly
      241 lsvaaasvtv lgpsaggsga plaeliaggi gghaqvlaaa aallltlgtm nayfagaakl
      301 gaalgrdgal pawlaqgsqv ggvprrslgv iallavvala attlsdvgpk plvlvtsgcf
      361 vmvyglgaaa alkllprggi ahrcawislv avaglflttg wyilcplmla ggallylqva
      421 aprq
//
LOCUS       WP_175866333             449 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia contaminans].
ACCESSION   WP_175866333
VERSION     WP_175866333.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..449
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=48448
     Region          62..424
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mlralataav lagltlaaha apaetvllpg appsrivdti gngtpqvagk idaatarfap
       61 dptlvalgrr iffdprlsep rgmscagchd pgrafaptls aaslagpgvp egsrpgrfsq
      121 rnapsllyvr yvprrhfyrd ddapapspfg glfsdgradt laeqirgplf dpnemnnrsp
      181 aallrkvdat elaadlaarf gapvrrdpeq lvramglaie aylqsdemap fasrfdaflr
      241 trkpmapaem rglalfrnpd kgncmschtl setssrpers lftdfgydai avprnralpa
      301 nrdprhfdng lcdtarrlrw peptqwcgyl rtpglrnvav kqtfmhngvf ttlrdavafy
      361 ntrstdpgfw yhgartfddv paayrgninv nstpmnrrpg tppalsdaei ddivaflgtl
      421 tdarytkvaa pvapaaasgl iirtavpar
//
LOCUS       WP_175866376             761 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia contaminans].
ACCESSION   WP_175866376
VERSION     WP_175866376.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..761
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=80809
     Region          <34..>162
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          176..742
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mnrsdliard gcltvirppa ppvkpapgqp gslssyvpal pevfvaildd grilafnghv
       61 dlgtgirtsl aqivaeeldv paarvtmvlg dtaatpnqgp tiasatiqis atplrcaaaq
      121 arhallalaa erfnvdaaql qiddatisan gqtatfatlv aarrialtld lntrtkdpal
      181 yrivgrsspr vdlpakatgq ltfvhdmrvp gmlhgrvvrp pyaghdsgsf vgdslidvdr
      241 asvadvpglv avvaigdfvg vvaereehai raarqlrvtw rplpalppld dpaaaiaaap
      301 akrrvlldeg dvdaaraqpd titlsrtyaw pfqmhgsigp scaladyrep gngritvwsg
      361 tqnpvslrhd latlvardea dfdvvrmeaa gcygrngadd vcgdalllsr avgrpvrvql
      421 sradehlwep kgagqsmqvs gtvtrdgrll gydfttryps ndapllaall tgtiapeprv
      481 femgdrtavs pyasphrrfv cedlaplvra swlrgvsalp nsfahdafvd ecaaltgvdp
      541 lafrlrhlqd tratellqav adragwtpra pgaphepats rlvrgrgiay aryvhsrfpg
      601 fgaawsawiv dlsvdrvsge iriervtvgq dtgtminpdg vrhqihgnvi qvlsrtlker
      661 vrfaggkvas rewasypilt faevpdvdvv lmprqgeppl gagesasvpg paavanalfd
      721 atgvrfyapp ftpetiraal rdagrlmtad gggvqvatgt a
//
LOCUS       WP_175866422             443 aa            linear   BCT 11-JAN-2025
DEFINITION  carotenoid oxygenase family protein [Burkholderia contaminans].
ACCESSION   WP_175866422
VERSION     WP_175866422.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Poliakov,E., Uppal,S., Rogozin,I.B., Gentleman,S. and Redmond,T.M.
  TITLE     Evolutionary aspects and enzymology of metazoan carotenoid cleavage
            oxygenases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1865 (11), 158665 (2020)
   PUBMED   32061750
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Sui,X., Kiser,P.D., Lintig,Jv. and Palczewski,K.
  TITLE     Structural basis of carotenoid cleavage: from bacteria to mammals
  JOURNAL   Arch Biochem Biophys 539 (2), 203-213 (2013)
   PUBMED   23827316
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Kloer,D.P. and Schulz,G.E.
  TITLE     Structural and biological aspects of carotenoid cleavage
  JOURNAL   Cell Mol Life Sci 63 (19-20), 2291-2303 (2006)
   PUBMED   16909205
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Wyss,A.
  TITLE     Carotene oxygenases: a new family of double bond cleavage enzymes
  JOURNAL   J Nutr 134 (1), 246S-250S (2004)
   PUBMED   14704328
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..443
                     /product="carotenoid oxygenase family protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006720 - isoprenoid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48337
     Region          8..439
                     /region_name="COG3670"
                     /note="Carotenoid cleavage dioxygenase or a related enzyme
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]"
                     /db_xref="CDD:442887"
ORIGIN      
        1 mtafdlnrga iapvadevdl vdlrvtgaip lelagtllrn gpnppggrfe gsdvlswwpe
       61 aamlhaiafe ggratgyrnr wartqrwaav hapdevrqlp dtnpnvnvlq hagellalse
      121 ggapfaitaa ldslgvparh aglgggmtah pkvdpvtgel iafradwrap wlrygvadaq
      181 gvqrvdleid lnapsmmhdl aitetrslll dlnvgydfsl lkqghrmplr whddrparig
      241 vlprhggavr wfdvepcfil hvvnaydcda scivldavry psflrldagt grfadnpvge
      301 lwryvidtan glidegplad ggiemprine srtgrryryl yaveqpnpve mrgvmrfdha
      361 sgtttryavp agdqnsepvf vprpggtned dgwllvmvyr aatdtsdvvi ldaraidagp
      421 vatvhlprrv pagfhgawvp rer
//
LOCUS       WP_175866465             314 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia
            contaminans].
ACCESSION   WP_175866465
VERSION     WP_175866465.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..314
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=34325
     Region          11..>232
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mqhpqqsnvt iegivpvmlt pfdeagaidy aglerliewy lahgadalfa vaqssemqfl
       61 slaeraelar fvvervggrv pvvasghisd dldaqaeelc aaaesgaqgv vlvtnrldpq
      121 rkgsaalldh lhrllarlps dlplglyecp apyrrllsdd elracidtgr fvmlkdvscd
      181 letvkrrval aegsplkiln anaaiawdam kagsagfngv ftnfhpdlyr wlrtqgesnp
      241 aladelstfl vvsavsealg ypalaklyhq rigtfasirc rvidydvrer fwaldavldk
      301 ivagtehfrr riaa
//
LOCUS       WP_175866481             374 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia contaminans].
ACCESSION   WP_175866481
VERSION     WP_175866481.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..374
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41787
     Region          87..327
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 masplvlihr ilgfaaarrg rtlsggspqh ngerfsnvap rpveglgktl giawnmlfnk
       61 prntvpagal pvdsltrael daapdrslyr lghstlllkl rgefwltdpv faeraspfrr
      121 vgpkrfhapp itledlpplr gvilshdhyd hldretvlal aattgvfvtt lgvgdrliew
      181 gidakkvrql dwwqsvdvtg ltltatpaqh fsgrslfdgn stlwaswviv dddlrvffsg
      241 dtgyfdgfrt igerlgpfdv tlietgayda qwpyvhmqpe etvqahidlr grwlvpihng
      301 tfdlamhrwl epfervtala ivrgvdlstp rmgerlalde phrgerwwrt vdervtsvaa
      361 ksrrwtlcas qaak
//
LOCUS       WP_175866560             281 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia contaminans].
ACCESSION   WP_175866560
VERSION     WP_175866560.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..281
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=30989
     Region          1..258
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mttlasdsld ilhvskhyaq rgaalavldd vslhvragef vtivgssgcg kstllrliag
       61 ldtdyageir agaervhdts lqrgivfqdh rlfpwltvaq nieaalrnap laaaakrrav
      121 adhialvgln gfehaypnql sggmaqrvai arglvnrprv llldepfgal daqtrarmqn
      181 ellriweqer itmilvthdv deavylgdrv vtmaprpgri erivdvalpr prrrdspafa
      241 rlrdtvladf ddheppgddr pggqridtpr phrigewrla w
//
LOCUS       WP_175866500             742 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia contaminans].
ACCESSION   WP_175866500
VERSION     WP_175866500.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..742
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=82010
     Region          48..715
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mnrfvpllrd awlrcrarvv pfaaacgarf ralgagalhr lrhptrrgva ltlaaipvlg
       61 llvllafvpf tpsigdirka ridrparvls adgqliaefr pvnrewvplk qisphmvdal
      121 iatedhrfyt hhgidlrrti aaglhtfsgd rqggstitqq larnlypdev graptltrkv
      181 kelitafkie svyskdeile tylntvpfly naygvemaar tyfgksadql divesatlvg
      241 mlkgnsyynp vlnperavqr rnivldrmaq mhmltpqqla klqrqplrvd fepqsgqpgl
      301 aphfavqlrk wliawadrnn ydlysdglvv rttldarlqd matqaltrqt erlqaiadga
      361 wrgpsgcglr ndlfrgfirq tpdyrqardt gltdvaalkr lganrdfmra lcerktqvqa
      421 gfvaidprng airawvgspd fgsepfdhvs qarrqpgstf kpfvygaafa dgmrpgdtfv
      481 drpvaipidg ravwrptdae pptdepmtlr dalalsrnri taqvmqhega akvaqlaram
      541 gvrespldav pslalgtspv tlkemvsayg tianrgvyva pqmitriedr dgkvlaafgg
      601 apperalpep aaqtlvdvmr dvvdrgtgad irsrygirvd vagktgttqd nadgwfilmh
      661 pqlvagawvg fddgsvtlrs dywgagahsa lpivgtfyda alraraidph aqfspdfrpr
      721 sapaprrrtp hpglfdwlrf fr
//
LOCUS       WP_175866562             135 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF427 domain-containing protein [Burkholderia contaminans].
ACCESSION   WP_175866562
VERSION     WP_175866562.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Lupas,A.N., Zhu,H. and Korycinski,M.
  TITLE     The thalidomide-binding domain of cereblon defines the CULT domain
            family and is a new member of the beta-tent fold
  JOURNAL   PLoS Comput Biol 11 (1), e1004023 (2015)
   PUBMED   25569776
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..135
                     /product="DUF427 domain-containing protein"
                     /calculated_mol_wt=14704
     Region          20..129
                     /region_name="COG2343"
                     /note="Uncharacterized conserved protein, DUF427 family
                     [Function unknown]"
                     /db_xref="CDD:441912"
ORIGIN      
        1 mpvssetsar pvktpgpdhp itvelhprrv vvkaagrvva dtrralalre aaypavfyip
       61 redadltllq rtnhatycpy kgdaayysip vggeravnav wtyeapypav dairghlafy
      121 pdrvdsieei ptgsd
//
LOCUS       WP_175866565             302 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175866565
VERSION     WP_175866565.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32639
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdllatmriy vrvvergtms gaardldmgq pavserierl ekhlgtrlll rsartltcte
       61 egrifyersk alleaadeav asvsktenal dgtirlaapq cvgevvlpgv lthvrtaypn
      121 lhidlvlndd ivdpvtegvd isirvgqlgd ggfvahpvga vgrrlvaaps ylerhgpidt
      181 tadlanhpfi rvkgvfaser lplqrdgdal dyarirtimt tshwrpmfdt ivagggigvv
      241 qqpacadala agtlvellpq yvipdfalnv lvhaqrplpp rvravvdllk qdlppllarp
      301 ar
//
LOCUS       WP_175866569             325 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175866569
VERSION     WP_175866569.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..325
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34498
     Region          6..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..302
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 medidlnlva aldvllsegs vtgaarrlgl stsamsrtlt rlriatgdrl lvragrklvp
       61 tphaaalrdr vhaiasdara vlrpatadvd iathastftv raaasfmeml sgpvvaalge
      121 iaplvrirfv pkpdrdpqal rdgtvdleig krgddapelh trmlfhdwhv avaraghplf
      181 asgritpary aacrhviasq lgdfggpadd stdkggpsht vhvvvpgypd amrvaastdl
      241 ialvprsslg nafspgltea lglrsfeipa rlpeilvsal whprmhgdpv hrrlrdavia
      301 vcqraypdgr aprpparrag traag
//
LOCUS       WP_175866631             605 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia contaminans].
ACCESSION   WP_175866631
VERSION     WP_175866631.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 605)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 605)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..605
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=64597
     Region          48..604
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mssamvrvla laigatplcv raqlagglpp gappglgaip pglavpraeq dpaqrllqeq
       61 rdrqrrdeia qppaqialpe qpampdlppg advetlpdva pmfliervef tgdtilgqpa
      121 ldriaapfvg kqlgrnrinl llrrlteafi srgyittray lgpqnlasgt lkinlvpgrv
      181 aaltlngkpl rprdpdekwy evrgggllte agtawafasa pgdplrlpdl eqgvdqinrl
      241 rrnqaeiril pgeapgdsvv aisnrsgdrl hydfgvdnyg ssqtgktryr agveadnvig
      301 lqeslsfnyv gttetnalvf saavpygyqt fsytvsmsey qqaigdvall egrtfsqmlg
      361 wndvlvrsss grlsvdvtln klrterdvng lplspqnltv lrvalnglvr faargqgaas
      421 twdvgvsqgl pwlaanhdas digiddahsq ftkldatgtl qfalgslags awayrgtlra
      481 qysrvalfgn eqiflggmss vrgfteggia gdsglfvrne aawqnvpawr dariepyvfl
      541 dggkahlnaq ggwptlvgag vgtraqwrlr sgtvsaevlv gqalaqpaal grkatvllat
      601 lnwsd
//
LOCUS       WP_175866639             431 aa            linear   BCT 11-JAN-2025
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Burkholderia contaminans].
ACCESSION   WP_175866639
VERSION     WP_175866639.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..431
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=46268
     Region          1..430
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 mtdqaasnwr letiavhggy rpdpttrava vpiyqtvaya fdntqhgadl fdlkvqgniy
       61 trimnpttdv leqriaaleg gigalalasg qsavtyaiqt iaeagdnivs asslyggtyn
      121 lfahtlpqyg ittrfadprd pasfeplida rtkaifaesv gnplgnvtdi aalakvahrh
      181 giplivdntv pspyllrpfe hgadivvhsl tkylgghgts lggaivdsgk fpwaehadrf
      241 krlnepdvsy hgvvyteafg paayigrarv vplrnmgaai spfnafqilq gietlalrie
      301 risdnalkia qhlarhenve wvnyaglpdh pdhplvaryl sgrapgiltf gvkggrdgga
      361 kfqdalklft rlvnigdtks lathpastth rqlspaelak agvkeetvrl sigiehiddl
      421 ladldqalaq l
//
LOCUS       WP_175866662             374 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD/NADP-dependent octopine/nopaline dehydrogenase family protein
            [Burkholderia contaminans].
ACCESSION   WP_175866662
VERSION     WP_175866662.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13367875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..374
                     /product="NAD/NADP-dependent octopine/nopaline
                     dehydrogenase family protein"
                     /calculated_mol_wt=39721
     Region          1..>136
                     /region_name="GpsA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0240"
                     /db_xref="CDD:440010"
     Region          187..333
                     /region_name="Octopine_DH"
                     /note="NAD/NADP octopine/nopaline dehydrogenase,
                     alpha-helical domain; pfam02317"
                     /db_xref="CDD:426715"
ORIGIN      
        1 mkvcvlgggh gchaaaidll ekghdvtwwr rdrepharlr elgvlnvtdy rgkravplgd
       61 apgairltgd laaalrgaql vvvplpatsh dalaaqvapl ledgqvvflp pgtfgsfvfa
      121 raaaeagnrs rvafaetgtl pylvrkhgdn dvvisayatr lptgvlpana agwafdvlra
      181 gypsvepved alsgalmnag pvihpplilm nagplehfda wdihnegtqp sirrvtnald
      241 aeriavreal gyraphfpla dhyategdew mygrgahgkl tdsgdwreki dlrnhrymle
      301 dtrlglsfiv scgrwagvpt pvaqgllsia savavrdlya qgrtlerlgi aalskaamra
      361 lldagmtgaa gvsa
//
LOCUS       WP_175866660             325 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia contaminans].
ACCESSION   WP_175866660
VERSION     WP_175866660.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 325)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 325)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 325)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..325
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34771
     Region          37..318
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mrqpsrpltt dgvpaslaqp dapaatptrt aagrapratw rahaplwlmc apafalfaal
       61 vlvplamtlv ltfyrfdpat gaiaafqfgn yaevlgssyf htiflrtfgi aalttaicva
      121 igtpeayvls kmrdpwrslf llailapllv svvvrafgws mllntsglvn qalglvglgp
      181 ykleyttfai vialvhvmlp fmvipvwtal qrldpqteha alslgaspft tlrrivlpql
      241 mpgvlsgslm vfglsasafa ipgllggrrl kvaatavyde flgslnwplg atiavlllva
      301 nlvvmltyyr vlerryarsl ggasr
//
LOCUS       WP_175866663             324 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175866663
VERSION     WP_175866663.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12168323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..324
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34591
     Region          22..200
                     /region_name="AraC_binding_2"
                     /note="AraC-binding-like domain; pfam14525"
                     /db_xref="CDD:434015"
     Region          251..322
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdialsrhap nrlgtlhapd everavahrl gphrmaargl dpfhaelyev plhhgallel
       61 cygretridf gddaehflfr ltlagacdlq agsvvaragp geltvsspal asrlstspdc
      121 rnlvlrlerg alerklqdml qatltrplqf dlaaggagag aalllptfey lcqlgaqpgi
      181 gtaattfgad lttwlmslll thlphsysda ltrgtpplpa hvrracdhvd ahlgeplala
      241 alaavagvap rtlqhafraf lhttpaayvr drrlaavhaa lqrgdarsvt dvliahgihg
      301 fghfakayar ryghapsvta rqpr
//
LOCUS       WP_175866671             374 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Burkholderia contaminans].
ACCESSION   WP_175866671
VERSION     WP_175866671.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..374
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37652
     Region          17..373
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mtgfidtftl ggpgptiaik dtidiagypt raasralada ppamqhadvv rllldagwqi
       61 agkanmhela fgmtgindyt gtpvnpqdat ripggsssgs aslvglgmvd aalgtdtggs
      121 irgpaaccgv aglkptfgrv srrgvapvet tldcvgpfar dirtlvavma aiapgfdraq
      181 asasaagrtv ahvtvdadpa iaaaldaavr asgmhahavv ldempasfva gltvinaets
      241 rafghlvetg klgadldarl raaattapaa lkeaeavrar ftaqvdaale hadvlvlptl
      301 palpitlqqa rdgvsviams slirpfnlsg hpalslplpl agsplkaglq iigrkgadeh
      361 vcaiaahfea alas
//
LOCUS       WP_175866678             304 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia contaminans].
ACCESSION   WP_175866678
VERSION     WP_175866678.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..304
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31744
     Region          5..298
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhdhhevivi ggsfaglsaa mqlararrgv lvidagrprn rfaahahgff gqdgkppaqi
       61 vdeaaaqlaa yptvqriagd vrtaerdadg rfhvtladgs rasadrlila tgirdelpal
      121 pglaerwgvs vlhcpychgy evsgqqlgvl ashplsvhqa ilipdwgptt wftqgvvdan
      181 eeeaalldar gvrierspvv eilgdaprie alrladgqvv pvdalfvgah tamasdlaqq
      241 lgcafddgpl gpvvrvdamk qtsvagvfaa gdastpmtna tfasasgvia gvaahrslif
      301 gldr
//
LOCUS       WP_175866750             167 aa            linear   BCT 11-JAN-2025
DEFINITION  aromatic-ring-hydroxylating dioxygenase subunit beta [Burkholderia
            contaminans].
ACCESSION   WP_175866750
VERSION     WP_175866750.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10791045
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..167
                     /product="aromatic-ring-hydroxylating dioxygenase subunit
                     beta"
                     /EC_number="1.14.-.-"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0009056 - catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=18709
     Region          7..167
                     /region_name="HcaF"
                     /note="3-phenylpropionate/cinnamic acid dioxygenase, small
                     subunit [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG5517"
                     /db_xref="CDD:444268"
ORIGIN      
        1 mmddrnalfs eqtfaravef vwreaemldr rdyrawldlw dpaghyvvpi dpdttdfaat
       61 lnyvfddhdm rekrvqrmvs gysasaadaa rtvrtvsrft lesgsagtve lksaqvvvay
      121 krgvttlfaa dvthklhvda egemritekv vrlidsteal saigfll
//
LOCUS       WP_175866793             450 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia contaminans].
ACCESSION   WP_175866793
VERSION     WP_175866793.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..450
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47617
     Region          5..407
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(20..21,24..25,28,60,110..111,113..115,118,138,
                     141..142,145,232,235..236,239..241,244,272,276,334..335,
                     339,343,358,361..362,365..366,369)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnhlrwkiva fllapltfvm tldraamava aptiqgelgl sivemsmilt iyfwayaigq
       61 ipagraaerf gsrgvlfgts tlwslmmivt pfgnafawlf gcrlvlggaq sadwsssvva
      121 lkrwfpager akgnaallag lylgpivsap ltawtivhfg whavfygfga lglllgaiww
      181 vgyrdapash plitqaeady iaagqppght vvsgslmrcl rlgrfwifgi qyfllvliqs
      241 fytvwlptyl mharglslka mgmvaslpwv avfvavfvag tvsdrllkkt dsiywartpv
      301 avagfvvsal alvaasraea maaviallcl sfaavgfvqv vvwsaaqdlg rpfagvmsgw
      361 tnvwgalsnv agpmalalvv kvtgswgsgm fvigaaaacg avlwlfvhpe rpllavaagd
      421 eppaaggrnt pcgdahetra dagrvsepad
//
LOCUS       WP_175866877             389 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Burkholderia contaminans].
ACCESSION   WP_175866877
VERSION     WP_175866877.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..389
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39956
     Region          61..369
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mntikridpr rpfiitaagl kritlgeegs adanavhgla hghgaaaakp rravqdpkhv
       61 mlvvahgerg alddhsrqai aaaalladaq tevallafge lkddvaelgv dkllelagfd
      121 rrafdpesel qalqacvaal apkhvfvpdn atgdgdlgrr yaaaagasva ahvveidakh
      181 vgtyaqagra fatralpdvi llaqnavdak lpfvgagerl aadfirpahd gaqpyrdlgl
      241 deidaaqval eeadfivsag ngvsdigafe rlagvfgaai gasrvavdng hftrdkqvga
      301 tgktveasvy iafgisgavq hlqgikdcrh viavnldgsa piakranltv vgdaqgtiaa
      361 lieqvqaara argespaavg trepegvaa
//
LOCUS       WP_175866893             834 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            contaminans].
ACCESSION   WP_175866893
VERSION     WP_175866893.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..834
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=91687
     Region          15..799
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mvsdllnkal rtqyvqhgri vrldtplged wlvplyvrgr aclgrdfeft idatstrlet
       61 iqakalirqs vtlwirqtdg sempihgyvt afsrlggdga ntyyqlrfns flallrlgsd
      121 rrdwietpaq qtvsdvlgky pqaagnftwq lrqalrsysq rmqwesdwny vhrtfeelgl
      181 fprfdiaqdg kshkvvimdd lfsvpelkqk tilfsrsvqn eefdglsewi dsqeiqsael
      241 dtgtfdykrp dlskhvtmpa fdlddvpglg eqyeytgsht wsdrdmgeaq anvvteewrs
      301 raqrfygvga lrcawpgryg vltghpvhda qpdqdremai lsvnwliqnn vpglenlmrf
      361 rrslraeveq arasgagssv rhddggvgff hveieaqrrr vafrspfehk kpimqlqtgi
      421 vggpeddeiy tdamlrakvr ltsnrlndgd qnvsawiraa mpdagrkrgg mfplrkndev
      481 ligfingdcd rpvilsrmhg gesmpewhth gltsgllsre yggegynqlm mddasgqnrv
      541 hlystsyssh lhlgyliqhs sntrgafigq gfdlkslgyg avraeqglyv stqpaatqpm
      601 sataaseqlt raeatletts kasqtnraqs qqdghnalkt ftdatqhpva gttkggrtag
      661 ggtgnangfa kpimllsspe giaastqgsa hitanqqanv vageninlaa grallasvle
      721 qislfaeklg vkiyaasgpi dlqaqndsms laasqdvkit agkkmylsad eiwigangsy
      781 ikltanmien atsgqivekc adwekagaas gtlknplhss pvsvdggrft lfsg
//
LOCUS       WP_175866855             285 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175866855
VERSION     WP_175866855.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 285)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13673967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..285
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31352
     Region          24..159
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          <179..278
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mttpakhidt tghwlvprrd aetgieslha hfnghaydah dhddmlvgft eqgvqqfqch
       61 rsvhtsvpgr ailiepgalh dghapeaggf tygmlylpqa wveraarrld lpglgsveas
      121 fghtlvddrg lvdairqafl aihgnegkla rdqtldrlli rlggelrgpl vlesavvppa
      181 iarvrdllhe hmdgniglde lahvagidrf rltrlfqraf gtsphaylvr lrlraarrll
      241 aagrtpaqaa advgfadqsh lgrwfrrayr itpaayrqlc tnvpd
//
LOCUS       WP_175866874             205 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            contaminans].
ACCESSION   WP_175866874
VERSION     WP_175866874.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22447
     Region          15..179
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msptstssgt rdrgrprefd tdevidaaar vfweqgyhat sidalceatg vfrgslyrtf
       61 gdkhglliaa fdryaegaia rlkerlaadl pprqalrdal lyyteigvrl serrgcfitn
      121 savellpgdd alrpyiestl lrigtqfsla iargqqsgdf drnldpeevg rfllcliqgm
      181 rvlgkssase aelasivdia mralt
//
LOCUS       WP_175866837             207 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia contaminans].
ACCESSION   WP_175866837
VERSION     WP_175866837.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..207
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23102
     Region          1..195
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mrllnivssp rgarsasiav anafvdayre tgatidvdtl nvweedlpdf drdaigakyk
       61 gvanapmdet eqsiwrriqs lvtrfqeadr ivvgvpmwnf gypyklkqli dlvsqrnmlf
      121 tfdgnayapl leipralvih vrgqsrepga gadnpgfrhq adyiefwlrf igvsevrslt
      181 vehtwgaras dsieraqara vamaaef
//
LOCUS       WP_175866913             402 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia contaminans].
ACCESSION   WP_175866913
VERSION     WP_175866913.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..402
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41969
     Region          17..390
                     /region_name="MFS_MJ1317_like"
                     /note="MJ1317 and similar transporters of the Major
                     Facilitator Superfamily; cd17370"
                     /db_xref="CDD:340928"
     Site            order(27..28,31..32,35,68,119..120,122..124,127,147,
                     150..151,154,227,230..231,234..236,239,266,270,319..320,
                     324,328,344,347..348,351..352,355)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340928"
ORIGIN      
        1 mqtetspril rqiprsvwvl gcvsllmdvs seiihsllpm flmvglgasa taigviegia
       61 eatapvvkvf sgtlsdylrn rkwlavagyg lgalskplfa iaptigvvvt arivdrigkg
      121 irgaprdalv aditpvhlrg aayglrqald tvgaflgpll avvimlawhd dfrlafwlav
      181 ipgvlavall afgidepara pgdarvnpir rdvvaqlgar ywwvvaigav falarfseaf
      241 lvlramgsgv svalvplvmv amnvvyawsa ypfgkladtt shaklmvagl vlliaadivl
      301 ahgthwgivl vgvalwglhm gmtqgllatm vaqaapadlr gtafgvfnlv sgvvtlvssv
      361 vagflwdrvg aaatfyagaa fsaativllv cvrtsfgagq ar
//
LOCUS       WP_175866920             430 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia contaminans].
ACCESSION   WP_175866920
VERSION     WP_175866920.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..430
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46203
     Region          38..419
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 msfhfgtpfa rrarrrapml waallvagav haqpspftld aalqsatdhs asmqaaqasv
       61 hasaeaavka gqlpdpmlka gidnlpvngg qrftvgqdfm tmrrigieqe wvsgdkrrlr
      121 salaneqvgr eragylaqla svrqqtataw lnavyakqal alqqalldhm nheleatkas
      181 yrgakasaad vvqaramlaq tqdqllkaqq vyqtalials rwtavpvgdv agtppapesf
      241 vsslppdelr lsqpalitaa ddiavaeadt avanserspn wtwevayqqr ggaysnmvsv
      301 gvtiplplnr knrqnrdvae kaalatkarl myedtlrqvq adirtqsatl asgrarianl
      361 gdallpaadq rvqlanaayr agtgsladtf aarraqldaq lqvlelrrev sqtwaqleyq
      421 vvpstlaaaq
//
LOCUS       WP_175866916             336 aa            linear   BCT 11-JAN-2025
DEFINITION  sodium:calcium antiporter [Burkholderia contaminans].
ACCESSION   WP_175866916
VERSION     WP_175866916.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schnetkamp,P.P.
  TITLE     The SLC24 gene family of Na/Ca(2)-K exchangers: from sight and
            smell to memory consolidation and skin pigmentation
  JOURNAL   Mol Aspects Med 34 (2-3), 455-464 (2013)
   PUBMED   23506883
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Besserer,G.M., Nicoll,D.A., Abramson,J. and Philipson,K.D.
  TITLE     Characterization and purification of a Na+/Ca2+ exchanger from an
            archaebacterium
  JOURNAL   J Biol Chem 287 (11), 8652-8659 (2012)
   PUBMED   22287543
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..336
                     /product="sodium:calcium antiporter"
                     /GO_function="GO:0008273 - calcium, potassium:sodium
                     antiporter activity [Evidence IEA]"
                     /GO_process="GO:0006874 - intracellular calcium ion
                     homeostasis [Evidence IEA]"
                     /calculated_mol_wt=35460
     Region          19..332
                     /region_name="ECM27"
                     /note="Ca2+/Na+ antiporter [Inorganic ion transport and
                     metabolism]; COG0530"
                     /db_xref="CDD:440296"
ORIGIN      
        1 mtfmflelaf mlivilvaae vftnalehlg erlkisegvt gslfaavgta lpetmvplla
       61 laggtanqav neeigvgail gaplmlatlt tflmtlavir srglrgtiap ertgfvrdmn
      121 yflaafslat aamfvphhnw aarallaaml vgiyamyvvm tfrasnqlvd aghgteapht
      181 mflsrlgvpt nlatiglqll lgvvllvgga kgfihgvegv shvlgvsall lsliivpiat
      241 elpekvnsvl wirrrkdtla fgnitgamvf qgtllpaigi mltpweprpe vltgviitla
      301 aaawlrvnar trglaiwall angagyagyl vltlar
//
LOCUS       WP_175866958             278 aa            linear   BCT 11-JAN-2025
DEFINITION  ion transporter [Burkholderia contaminans].
ACCESSION   WP_175866958
VERSION     WP_175866958.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11997982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..278
                     /product="ion transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0034702 - monoatomic ion channel complex
                     [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30206
     Region          27..234
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
ORIGIN      
        1 mmtpiqstfd alrgtvaryt hrpaflrnld vavlalivas vlvvmadsvh dlheryghal
       61 yaaewaftll ftveyvvrll sapkplqyar sffgivdlvs vlptylafff pglhalidvr
      121 llrllrvfri lglsiyleeg qmlmralara rrkifvfigg mfvltvilgt viflvegpen
      181 gitsipvgvy waavtmsttg ygdltphtpl grlitscail lgygiiafpt gimgaelvas
      241 alertrgnar aatgdepccp hcgvalperg asdtphsk
//
LOCUS       WP_175866969             452 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia contaminans].
ACCESSION   WP_175866969
VERSION     WP_175866969.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..452
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=48638
     Region          17..434
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mdnttpnlat draprlpriv ivgggagglh latrlgdtvg rrgqaevvlv drypthfwkp
       61 llheaasghr dpashtieya aqakrhgfrf vqgalqqvdr aartatiaav rdadgteilp
      121 qrelgyddlv lavgsvtnff nvpgaerhal plenldqaed frrkflaact kanhqaeqqp
      181 arraapicin vigagatgve laaalrdaiq qlttyrfkal vsardvhirl ieggprilpa
      241 lderlsgkmh aqlralnvdv ltdtrvaevg adavttstge rlasditiwa agvagpaflr
      301 qigdialnrs nqvivtdtlq mpddphvyaf gdcaacptgg angflppraq vayqqavylv
      361 nafarrvagk pvdgftfrda gtvvslghag aayqadisvr srslivdgla aiglykflyr
      421 khlfsvvgmk ralfqslshw lqsrnqpsik lh
//
LOCUS       WP_175866989             397 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia contaminans].
ACCESSION   WP_175866989
VERSION     WP_175866989.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..397
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42570
     Region          1..364
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 maqitckals khydggpavl hpldleiadg efivllgpsg cgkstmlrmi agleaitgge
       61 lvigdevvnd lpsrernvam vfqnyalyph mtvydniafg lrrlkvpade idrrvrdvar
      121 ilsldalldr rpramsggqq qraaiarami ktpavflfde plsnldaklr tqlrgdikrl
      181 hqrlktttly vthdqleamt ladrvvlmrg ghieqigtpa elygqphtvf aagfvgtpam
      241 nfaagtierl ganvlldcng arwplastrf aglhdgqkvk vairpnhlrl vtepdptpgt
      301 laltgtvelv ellgaealvt ldwhgqpcaa lvpapmapal gavvalrfde aalhlfdagt
      361 ernvtlpdan piahaappaa atrttppaat gwsmsrs
//
LOCUS       WP_175866997             177 aa            linear   BCT 11-JAN-2025
DEFINITION  2,4'-dihydroxyacetophenone dioxygenase family protein [Burkholderia
            contaminans].
ACCESSION   WP_175866997
VERSION     WP_175866997.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14449000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..177
                     /product="2,4'-dihydroxyacetophenone dioxygenase family
                     protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20065
     Region          37..160
                     /region_name="cupin_DAD"
                     /note="2,4'-Dihydroxyacetophenone dioxygenase (DAD), cupin
                     domain; cd20302"
                     /db_xref="CDD:380436"
     Site            order(53..54,57,63,65,82,84,86,88,101,104..108,110..112,
                     129,135,137,145,148,151)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:380436"
     Site            order(77,79,94,115,130)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380436"
ORIGIN      
        1 mvekavaefw qniapianpf kpdalpeayi anaatddery yvpftetvss rplwispsqn
       61 kwcdilmake aglvnrhyhp hevfaytlsg kwgylehewt atrgdfvyet pgeghtlvaf
      121 dhpepmraff ivkgpliwld eagnpdgyfd vhsyiamcka hyekvglgaq aieklfr
//
LOCUS       WP_175867109             327 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia contaminans].
ACCESSION   WP_175867109
VERSION     WP_175867109.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..327
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34845
     Region          91..284
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mtsahwlplt evaddardav rafrelggrh ygsfsvdqsr vnfaraceln gltgdaavvh
       61 edidvpvagg sirvrlyrpp agaradgapl ivfihgggwv igsvdthdgi crhlarhggc
      121 avasveyrrs pehrwpiple dceqaldyla tnasalavna crvimagdsa ggnmatlian
      181 aapaagpaii gqilfypvtd ltaslpsyqr irggfplvae smlwfrehyv ppdtpfdlpr
      241 lspllhaegr rqppmfiatv gldplcdegi ayascaarag stvehhhlpg hhhgiitaar
      301 tipaatclld raasfvrrla ekegldv
//
LOCUS       WP_175867194             236 aa            linear   BCT 11-JAN-2025
DEFINITION  PIG-L deacetylase family protein [Burkholderia contaminans].
ACCESSION   WP_175867194
VERSION     WP_175867194.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..236
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26053
     Region          7..>162
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mthaptrwlv isphlddgvf scgrllaaap gsivvtvfag ipprdapapp wdrragfhra
       61 deamharrde drralahlda rpvwldfldd qygmpaaspe iaarvvteid ahagfgvlap
      121 aglfhrdhlq vqqaalslld rarvshdaar qwrfyedvpy rriaglmaar vigwrergwi
      181 ahpdgapagd haqdiaakta avdtyasqva llephmradl repetywrle cdvtfa
//
LOCUS       WP_175867206             139 aa            linear   BCT 11-JAN-2025
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Burkholderia
            contaminans].
ACCESSION   WP_175867206
VERSION     WP_175867206.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..139
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15787
     Region          22..135
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 mtethlpnsw pqpyrlldaq pywdaladek ltyqrctacr esvwpahsfc thcgaksldw
       61 aqssgrgeiy sfstitrgpt pvwagivpyt vgfirmdegy flfsqideap eairigqrve
      121 vrfvqrgeqk lpvfvlskq
//
LOCUS       WP_175867252             472 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia contaminans].
ACCESSION   WP_175867252
VERSION     WP_175867252.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..472
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50852
     Region          8..462
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mqsegqfqhi aareqglrrt lsarqmamia iggaigtglf lgsgfaigfa gpsvlvsyai
       61 gafislllmg claemtvahp tsgsfgayae hyvspwagfl vryaywaciv lavgtevtai
      121 alymkywfpg vpgwmwivgf sallvfvnar svdvfgavey gfsvvkiaai vgfillgayv
      181 vfgnpelvgg gatragfhly tdhggffpkg vwgmwvaviv sifsylsiem iavaageaed
      241 peravtrafr stivrlvlfy lvtlalmlai vpwttagrde spfvkvmeai hlpgaaglin
      301 fvvliaalsa mnsqlyittr mmfslsragh apkalgevna rgvplgalml stlgialatv
      361 lsvlypdasf timmsvsmfg alfvwmmifv thycfrrrra alglpapafr mrgfpvltll
      421 gaglmlavtv ttyftpefhm tlifgipflv vlsvvyavwy rraqpvlqpe ak
//
LOCUS       WP_175867253             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175867253
VERSION     WP_175867253.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33142
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 melrqlryfv avaeelhfgr aakrlfisqp alsfdirkfe ealgvqlfsr tnktvaltna
       61 gevllgearr lllqaaeaer ltvrsasgla grlrigfvhs mlyrglpdav rrfeadypgv
      121 eivlsemnsh aqvqaiqrgq idlgyahwgh fppevdatpv yaepfvcclp adhplakrkq
      181 valatlaaep filfpreaap hyhdliiaqc vnagfsplir hearlwqtil smiefgmgva
      241 lvprvlqqvk serlafrplk daslesrtla lkrsgtaepv alrfadyvra sigalpaleg
//
LOCUS       WP_175867297             163 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia contaminans].
ACCESSION   WP_175867297
VERSION     WP_175867297.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 163)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..163
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17443
     Region          18..147
                     /region_name="NUDIX_ADPRase"
                     /note="ADP-ribose pyrophosphatase; cd04673"
                     /db_xref="CDD:467557"
ORIGIN      
        1 msdsprsptr ipasvrpvpa vigivlrerd vllvrranpp dagcwgfpgg kievgesiad
       61 avvreiaeea tmdvealdaf taldafdyda ggnvrqhfvm vavlcrwlrg tpaagddald
      121 arwfdlaeld rddlpmsagv rdvarraieh aaayghaprp ant
//
LOCUS       WP_175867300             238 aa            linear   BCT 11-JAN-2025
DEFINITION  YdcF family protein [Burkholderia contaminans].
ACCESSION   WP_175867300
VERSION     WP_175867300.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..238
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26740
     Region          9..238
                     /region_name="ElyC"
                     /note="Lipid carrier protein ElyC involved in cell wall
                     biogenesis, DUF218 family [Cell wall/membrane/envelope
                     biogenesis]; COG1434"
                     /db_xref="CDD:441043"
ORIGIN      
        1 milfdsfvll ficfmlcrkr rriiaiaava lfwllatgwl aapliawtea gvtpvehpdm
       61 hgrttlilig agtkrtdsgl rpppdgtari qkvaalyrtc rqqadhctvv msggdpqhhg
      121 eteaavygrq lvaegvapad lvlepdsrtt yenakftasi lrpqyddari lvtssyqmrr
      181 alldfqrfgi dpqpvyanrr raqtgwlprw rnvvnaeqal helvgiaqfh vyrwlgwf
//
LOCUS       WP_175867308             328 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia contaminans].
ACCESSION   WP_175867308
VERSION     WP_175867308.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..328
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34760
     Region          7..236
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mndndqrtvr fgiigagsia rrfaqslahv pgatlagawa rradaatdfc eayggtpaas
       61 ldallasdid aiyiatlhds haqytlaala agkavlcekp atlntaqldt vlraardagr
      121 lfmeamkppf fplyrqlrah lhddpigeir lvragcasss vpddhsvyrl draggalldi
      181 giyeaflavd wlgaaldvqt lgrvgatgvd lfaslnsvha nggiaqifcg ldvmgrgdal
      241 iaapgghvti hekwwnpara tiryadgrtv eldapvdggg lnyetahfce llragktesp
      301 imthdhsrqm iamtdaaraa lgvrysde
//
LOCUS       WP_175867313             157 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia contaminans].
ACCESSION   WP_175867313
VERSION     WP_175867313.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..157
                     /product="VOC family protein"
                     /calculated_mol_wt=16542
     Region          13..136
                     /region_name="VOC_like"
                     /note="uncharacterized subfamily of vicinal oxygen chelate
                     (VOC) family; cd07246"
                     /db_xref="CDD:319910"
     Site            order(13..18,20,35,49..50,57..58,60..62,81..83,85..90,96,
                     117,122,130..133)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:319910"
ORIGIN      
        1 mstsvkpipe gmrtltphli cagataaidf ykrafnaseq frlampdgrl ahaclvigds
       61 tlmlvdempe hgalgpnalk gtpvclhlyv pdtdaaiaka vaagatvtip aadmfwgdry
      121 gqvedpfghr wslathqrdl tpeqiaeama sappcgs
//
LOCUS       WP_175867324             282 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia contaminans].
ACCESSION   WP_175867324
VERSION     WP_175867324.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..282
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29845
     Region          7..260
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtrstaalaa rglsvgyrdh vvidgldlsi aagrvtalcg pngcgkstll rtlaglqpar
       61 aghvevngqp laafrrrala reltmlaqfn qipsgltvre lvaygryayg gflrglsrgd
      121 haaidealet sgladdadrd vgalsggerq rawiamalaq qapivlldep ttyldihhql
      181 dildalrtln rtrgltivwv lhdlnqaaay sdeivlmrag rlvaqgtpda mldparlraa
      241 fgvemlklsh pqtgapmcvp acgpttdgvp qpagvfdrdl av
//
LOCUS       WP_175867348             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175867348
VERSION     WP_175867348.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33857
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..294
                     /region_name="PBP2_CrgA_like_2"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08471"
                     /db_xref="CDD:176160"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176160"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176160"
ORIGIN      
        1 mdridamkvf vatldegsla gagrklgrsp aavsraiafl eehtgtally rttrtirlse
       61 ageryaaacr rilsdleead mlvadersap rglltvtapv aagedvlral ldefierhpa
      121 vsirlqlldr pvslidegmd valriahltd stlvaipvgt vrrvvvaspd ylakhsaiet
      181 padlaqhrii smthfgldsw sfpppapsal pqvvqftprf iintirgava savaghgvtr
      241 lfsyhvaepv rdgtlrivlr dsehaplpih lvtpygrlav pkvrafvdfa aprlrehfar
      301 laaitdgdrt dgd
//
LOCUS       WP_175867356             215 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia
            contaminans].
ACCESSION   WP_175867356
VERSION     WP_175867356.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..215
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24222
     Region          3..206
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 msyvlyyspg aasmavhwml ielgvpfetr lvdidtgaqh speylrlnpa grvptlvvdg
       61 kprtesaall mllaerhpep slaprpgspe raewfemmiy lansvlpamr nwfyaetdgd
      121 prcadmvkaf sqgqveasma hlddllsdgr sylindrlst vdllalmlmr wtrnmprpat
      181 twpnltryih tlramptfie lnaregltew mnpvs
//
LOCUS       WP_175867358             453 aa            linear   BCT 11-JAN-2025
DEFINITION  TldD/PmbA family protein [Burkholderia contaminans].
ACCESSION   WP_175867358
VERSION     WP_175867358.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..453
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=48441
     Region          19..452
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 mtgfdpmarq agidwhayfa rladdaqrlt apaetvllgf sgetsdfirf nggrirqtgr
       61 vtqgrlsvrl idgarqahsa ltvcgdpaad lreladalav lrdglrdaqd dphllfdtss
      121 wvqetrrtgc lpnadglari vaecargldf vgfyaggtla rgfasstgsr gwyevenfnf
      181 swslydpsgr aiktvyagdd wrdaafaakv daaaarlpvl grapkalapg ryrtyfapda
      241 ihemtsllgw sgfsaravas arsplhrlya gevaldprvs itedftlgia pafnadgyrr
      301 dsvplvvegr gagqlvcart areqggtpng adngespqsl tiaggtlada dvlaaldtgl
      361 yvgnlwylnf sdpiacrmtg mtrfatfwve ggrivapvda mrfddsfyrl fgseleqlga
      421 vpallasddt ygeratggaq lpgllarsfe ltl
//
LOCUS       WP_175867372             342 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175867372
VERSION     WP_175867372.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..342
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38597
     Region          3..98
                     /region_name="HTH_NolA-AlbR"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators NolA and AlbR; cd04788"
                     /db_xref="CDD:133415"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133415"
     Site            order(51,54,58..59,68,80,84,90,94,97..98)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133415"
ORIGIN      
        1 mrlkvgelak rsgltvrtlh hyhaiglltp saradngyrl ydrhdiarlh qiqalrrfgl
       61 slteigdhln qpdtplveiv ekqialldrq laqtaqlrer lvnlhaqlaa gtepeladwl
      121 ttlelmtvyd kyfseeelar lpmyqksqag daewialvde vralhdagvp aederarala
      181 arwmallvrd tnndprllak lnlmhehepa mqskigista lrdyvlrasa etkmrifeky
      241 lapdeirfmr ahygesamaw pqlmgdvrda idagarpdsp egrtlaqrwl tlfcsyagnd
      301 pathakfrqa mmsepsltkd swiddtligf vreamaqlap ar
//
LOCUS       WP_175867400             238 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Burkholderia contaminans].
ACCESSION   WP_175867400
VERSION     WP_175867400.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..238
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=25613
     Region          1..224
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mdlesilytq gfgsrrqcrg lieagrvava gasatdpdaa fdtdglvfsv ddtawpfhar
       61 aylalnkpag yecsrdpqhh asvfsllpap lvargvqcvg rldqdttgll llsddgqfvh
      121 aytspkrkvp ktyvatvrhp lddtqlnalr tgvqlhgepk piaavaayar aphalaltvl
      181 egkyhqvkrm vaaasnrvea lhresiggft lpddlapgaw rwlddadlsa lrnpvktl
//
LOCUS       WP_175867421             522 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia contaminans].
ACCESSION   WP_175867421
VERSION     WP_175867421.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..522
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56381
     Region          34..456
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msagpaglth dvpaapfern atmsdsvakp vdatfdqfgl aadilkaiae qgyttptpiq
       61 aqaipvvlag rdvmgaaqtg tgktasfslp iiqrllpqan tsasparhpv raliltptre
      121 ladqvaanvh ayakhtplrs avvfggvdmn pqmaelrrgv eiliatpgrl ldhvqqktan
      181 lgqvqilvld eadrmldmgf lpdlqrilnl lpkdrqtllf satfsgeikk lastylrnpq
      241 tievarsnst nanvtqivyd vaegdkqaav vqllrdrglk qvivfcnski gasrlarnle
      301 rdgvvasaih gdktqiermq aldafkrgei ealvatdvaa rgldiaelpa vinfdlpfsa
      361 edyvhrigrt gragatgdal slcspnerkq ladieklikr plevqtlald kparhrhder
      421 gserggdrns erggergger ggrrdrdehr gaagrrpaga erghhrrhea pvddfflkpy
      481 epsvpakqhd daqpaqqpek kgpkrqvaal lggfgmprkp sa
//
LOCUS       WP_175867484             276 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Burkholderia contaminans].
ACCESSION   WP_175867484
VERSION     WP_175867484.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 276)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..276
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29771
     Region          14..276
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mlyavfftrf sagrvtrlla aavlgvalln gahadtaplk vgistspqie alkvaakeak
       61 aqgldvkive ftdwntpnaa lankdidvny fqhipflena nkqggynfvs iapgtimkig
      121 lyskkvksfs elkdgakvai andpvnggrg llllqragli tlkpgadyra tthdivsnpk
      181 hlkiipleas qlarslddvd laqgypsfik lagttdpnsa llfdgtenki faiqwvvrpd
      241 svndprirkf isiyqhspav rraldnafgs lyavaw
//
LOCUS       WP_175867488             209 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia contaminans].
ACCESSION   WP_175867488
VERSION     WP_175867488.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..209
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21863
     Region          1..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mshlswlpfi atslliivtp gqdmvlvmsr tlsggtragl vtaagvsvgl lvhtmlatlg
       61 lgallqasew lftalkviga lyllylgial lrtsgeltla ssrdgaqasr lrtfaqgals
      121 nvsnpkvalf ylaflpqfvp agtahpmlsl fvlgatfagl tflvkgpval fagllsasir
      181 rnpriltrmh rvsgavllgl gvklalerr
//
LOCUS       WP_175867438             149 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Burkholderia contaminans].
ACCESSION   WP_175867438
VERSION     WP_175867438.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..149
                     /product="RidA family protein"
                     /calculated_mol_wt=16595
     Region          28..137
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 msqpthirir mfntkdtypn qtldndlcqa vragntvyvr gqvgtdfdgr liglgdpraq
       61 aeqamknvkq lleeagsdlt hivktttyli dpryrepvyq evgkwlkgvy pistglvvsa
      121 lgqpqwlmei dviavipdnw qpnrapeat
//
LOCUS       WP_175867550             191 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Burkholderia contaminans].
ACCESSION   WP_175867550
VERSION     WP_175867550.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..191
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=20699
     Region          4..135
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(9,11,72..73,76)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            11
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(71,116..117,119..120,124)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(77,82..83,112,115..116,119..120,123,126)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(101..103,112..113,116..117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(101,117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(125,131..132)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          147..188
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
     Site            order(148..150,182..183,185..187)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 msrvfaycrv stveqstenq rreiaaagfa iddrrvieea isgsvaaker pgfgrlidrl
       61 epgdvlvvtk ldrlgrnamd vratveqlah agvrvhclal ggvdltsaag rmtmqvisav
      121 aeferdllie rtksglqrak aegkefgrps slsdeqrrav lsrlaagetv aalarefsts
      181 rqtimrvrsa t
//
LOCUS       WP_175867576             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia contaminans].
ACCESSION   WP_175867576
VERSION     WP_175867576.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..359
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38126
     Region          159..356
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mtkvflilvr nellgylrsr sslfwtlvfp vfllsvmlfa fggsgslgta divfavpgga
       61 tpysraceaq iveslthsdt vkatfdgrga aadrvtvvlg ndertpatir ydfngslavk
      121 aasrvveial arcaaqrlgl paaqarfena aparrpfdyg affatgilvm afmaiglnst
      181 ttaiaslrer ntfklyvcfp vsrgvflaal ivarmimmal salvlltvar vafgialpia
      241 tpdglralpi vllgaamvls igvllasrar slaaaelacn vtyypllffs dltipmhdap
      301 awlkavlafl ptnqfavalr galvdgapya qlapqllgma vstalflfaa arlfrwhda
//
LOCUS       WP_175867610             220 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175867610
VERSION     WP_175867610.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..220
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24440
     Region          9..217
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mtlkvstdae laydeirsri fdgrlapgqk vshrglsdel gfgqmpvrsa lhlleseglv
       61 vvieksgtyv aspttsdlre ifemrlales taaflaarsg vtadlrdaae kmqdlierdv
      121 adimleqrig wvfhqalfaa arnvrissay gllraqtlal nelprsdaet vrrgtiehlh
      181 ifhaieandg klarqhmwnh ivdgtparik llkarhehek
//
LOCUS       WP_175867613             315 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175867613
VERSION     WP_175867613.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..315
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34129
     Region          2..315
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhrigffvcr gydaldlggp lsafnqvata aghapydlhv isqpggpvpg ntglsvdtkp
       61 igrrtfdtvi fvggdidpmq tpeniaaark lgaraarvas vctgafllge tglldglrat
      121 thwryaarlq srfprakveg dsiyieegri wtsagiasgi dlalgmierd mgaevartvs
      181 rllvvpyrrp ggqsqfsams qmepesdrir ialnfarehl aealpverla eaaslslrqf
      241 grafrretge tpakaverlr veaarlrlqg gsepieqial avgftdperm rrafiklhgh
      301 ppqairresr sngar
//
LOCUS       WP_175867627             175 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia contaminans].
ACCESSION   WP_175867627
VERSION     WP_175867627.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..175
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18812
     Region          12..164
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 metiatdrpa ldplqlraaf gqfptgvtvi ttcapdgrkv gltansfssl sldpplvlws
       61 lrkvapsrpd fvaathfain ilahdqidls rrfatpsadk fdgvlhvdse tggvpcldga
      121 sarfvcrnvg hyeggdhllf igqieqfdtf gkaplvfhag qyraiadhpd lfrvv
//
LOCUS       WP_175867633             730 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia contaminans].
ACCESSION   WP_175867633
VERSION     WP_175867633.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 730)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..730
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78337
     Region          51..730
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mvtgtgaarr aravaagsaw vmaaaggaha qasgaaatpp agaaaavlpa idvtekgdra
       61 ssglvglrtt agtktdtpva eipqtinlvt aqqiemtgat dlnqalryvp gfatfgadsr
      121 tdwyaalrgf tptlyvdgva apntavianw rvdpytidsi aalrgptsvl ygagepgaiv
      181 dahtkladge rvreagvqig ndarkqfmld vgdaldpdgr yayrfvgvar dgnavtgpng
      241 drrvalapsf rwrpnadtsl tlsatflqds sdissnflpa sgtvlpnpng rlsqdiymga
      301 pgfndyrkkq wslgyalehr vnaiwslhqd vrwshlsldd atvfgigfmp rssttmmrya
      361 glfqlnysrf didnhaqarf gtgplehtll lgaqydrqtt tnsvwlalap slnlyrpvyr
      421 pvtdaifsgp tslghvdqyt amnvfgvyaq dqirwkrwtl tlggredfvn arfddrtagt
      481 qaqqdvsafs grvgltyqgd aglspyvsys tsfdpvigvr mygggmpkpt rgkqteaglr
      541 wqppgknlll saavyqidqt nvatptpvsl dptgttsvqt gkvrsrgiel savgkvtrel
      601 svvasyvyqd vknvqandas lnnwpvavpl prqmasmwad wtwrtgalsg lgigggvryq
      661 sasagapdns ltvpsvtlvd lalhyemphw rfalnvanlf drryvsgcqs yavcvfgner
      721 tvlatakydw
//
LOCUS       WP_175867656             251 aa            linear   BCT 11-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Burkholderia contaminans].
ACCESSION   WP_175867656
VERSION     WP_175867656.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 251)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 251)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..251
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27209
     Region          15..208
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mlarlsatdr faliqgardy fptlmaifsw glvtgiamsk svmtlwqasa msllvyagss
       61 qlavlpllaa klpiwtillt aamvntrfvi fsaglaphfs ylplwrrlai gyfngdviyl
      121 lfqkqgfayg hvpgkeayfw gmalaswlsw qvsslagill asffpaswgl elagtlalip
      181 imvsavanrs tlaavavagi vsliafdlpy rlalplavla alaagctadf fveradwrri
      241 rtetvhekei e
//
LOCUS       WP_175867670             266 aa            linear   BCT 11-JAN-2025
DEFINITION  (Fe-S)-binding protein [Burkholderia contaminans].
ACCESSION   WP_175867670
VERSION     WP_175867670.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..266
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28299
     Region          <7..256
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mnerqypaaa pahvylfatc lvdlfvpeag ldavrllere gltvhyprgq sccgqpayss
       61 gnpeearrva aaqldlfaep wpvivpsgsc ggmirhhwpa lfaddrvhgp karaiaerty
      121 elteflvhvl dvrldalaap agadervvlh tscaarremg trvhgvalvd alpgvtrieh
      181 ereseccgfg gtfslkhpdi sgamvcdkva sacatgcdrl vsadcgclln ighaaeksga
      241 alpvehlasf lwrrtagaas lrgdkp
//
LOCUS       WP_175867694             468 aa            linear   BCT 11-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Burkholderia contaminans].
ACCESSION   WP_175867694
VERSION     WP_175867694.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..468
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=47823
     Region          2..458
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mtmlslgeaa rlipgatvrg dagvtfdrvs tdsrtagpgd lfvalkgerf dahgflgdva
       61 argaaaalva hvpagvtmpa ieggetraal galahgwrkr falplvavtg sngkttvkem
      121 iasifaaavg adarlatagn lnndvglplt llrlsaahrl avieigmnhp getevlarlt
      181 aptvalvnna qrehqefmat veavalehaa vihalppdgv avfpaddaya giwrvaatgn
      241 rildfalhda erqsdaqvtg rlnggelaid tpagavtvrl ralgehnarn alaataaalg
      301 agvalsaikq glesfepvkg rlqvkqaiag slagatvvdd tynanpdsmr aaidvlaaqp
      361 aprvlvigdm gevgdegpaf hrevgayare rgidalfalg dasrdactay gdtarhfgdv
      421 galveallaa gygaqatllv kgsrymkmer vvdaltnqpa agtapaah
//
LOCUS       WP_175867713             424 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia contaminans].
ACCESSION   WP_175867713
VERSION     WP_175867713.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..424
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44979
     Region          69..300
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mafskvlvgw maacalsaaq agtlpsadsg tgagasgsla haerfdysds nlpqvaadln
       61 eqilripada sgtvtleatl fkpngpgpfp lvvfnhgknt gdlhlqprsr plafarefvr
      121 rgyaviapnr qgfagsdgty qqegcnvgkn glaqaadvda tvrymshqsy vdasrivvag
      181 tshgglvsva ygteaapgvr giinfsgglr qdlcdgwqkn lvdafdqyga htavrslwly
      241 gdndsvwtpg lvaqmhgayi shgtqaqfid fgrykddahr livdrdgvpv wwpavnafla
      301 qlnlptsvry avanphepka sgyasidsvn avpyvdeagr egyrrflnqh psrafavsse
      361 gawswaeggd dpmalaldnc akqgagscrl yavndrvvwn natqtadsdd snardtgtpa
      421 lasr
//
LOCUS       WP_175867748             399 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid aminotransferase [Burkholderia contaminans].
ACCESSION   WP_175867748
VERSION     WP_175867748.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Alexander,F.W., Sandmeier,E., Mehta,P.K. and Christen,P.
  TITLE     Evolutionary relationships among pyridoxal-5'-phosphate-dependent
            enzymes. Regio-specific alpha, beta and gamma families
  JOURNAL   Eur J Biochem 219 (3), 953-960 (1994)
   PUBMED   8112347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..399
                     /product="amino acid aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42529
     Region          3..388
                     /region_name="PRK09257"
                     /note="aromatic amino acid transaminase"
                     /db_xref="CDD:181731"
     Site            order(107,142,209,254..256,292,295)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mslfsaiqla prdpilglne afnadarptk vnlgvgvytn eegkipllra vrdaekarve
       61 aglprgylpi dgiaaydaav qklllgndsp liaagrvvta qalggtgalk igadflrtln
      121 pnvkvaisdp swenhralfe aagfevvayp yydaatngvn fdgmlsalns yaagtivvlh
      181 acchnptgvd lteaqwqqvv dvvkarnlvp fldiayqgfg enieadaaav rlfaaadlna
      241 fvsssfsksf slygervgal siitsskeea trvlsqlkrv irtnysnppt hggavvaavl
      301 aspelhaswv qelgemrdri ramrnglver lkasgvdrdf sfineqrgmf sysgltsaqv
      361 drlrdefgiy avgtgricva alntrnldav anavaavlk
//
LOCUS       WP_175867978             501 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia diffusa].
ACCESSION   WP_175867978
VERSION     WP_175867978.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..501
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53126
     Region          27..474
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mkqaserpvd paggadprha drdamfashe sgyeqklkpr hvqmiamgga igtglflgag
       61 grlqsagpal avvylvcgvf aflimralge lvmhrptsgs fvsyarefmg erasfvagwm
      121 yylnwattgi vditavaiym kywavftevp qwvfalgalg ivsvmnmigv kvfgemefwf
      181 sivkvgtlal flaigavfla sghpvagqmp glhliadhgg ifphgilpav livqgvvfay
      241 asielvgvaa getadarkvl pkainsvmwr ialfyvgsvv lltmllpwta ysahespfvt
      301 ffsklgvpyv gtvmnvvvlt aalsslnsgl ystgrvlrsl amggsaprfv srmnargvpy
      361 ggilvtvavn aigvplnyiv paqafeivln maslgiittw gfivmcqilf rravnrgels
      421 pvsfrmpgap ftswltlgfl vsvlvlmafd ypggtwtvgm iplvvlalvv gwklakrgaa
      481 reaaaenaag aplgvdpasn v
//
LOCUS       WP_175867974             375 aa            linear   BCT 11-JAN-2025
DEFINITION  J domain-containing protein [Burkholderia diffusa].
ACCESSION   WP_175867974
VERSION     WP_175867974.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10154716
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..375
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=42523
     Region          <210..251
                     /region_name="DnaJ"
                     /note="DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock
                     protein 40) proteins are highly conserved and play crucial
                     roles in protein translation, folding, unfolding,
                     translocation, and degradation. They act primarily by
                     stimulating the ATPase activity of Hsp70s; cd06257"
                     /db_xref="CDD:99751"
     Site            order(226..228,237,243..244,247..248)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
ORIGIN      
        1 mtarrgaava iapghetarl skaqktfntl vkhiekrrer lgaweavmpa fqkkfvdall
       61 pleqeatalr irlihllddt flqkglskae qrtlsdliad mardllnvsd daalkiiynr
      121 haesgqvsna aaepeptete repqpqsqpa ddldslspde laermqaeld aqferdmaah
      181 aareaqrakr kkapkqsaaq arveaeqaes sksireiyrk lasalhpdre tdpleqqrkt
      241 vlmqrvnray ekgnllqlle lqleieqidr raidglsear ltryngilee qlreldqeiv
      301 hvendfrrty giassnkvap dtvlrmlard iagmqrsnqd lavalrefed pdqvrswlkd
      361 mkrrsassrf dedsy
//
LOCUS       WP_175868003             381 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Burkholderia
            diffusa].
ACCESSION   WP_175868003
VERSION     WP_175868003.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia diffusa
  ORGANISM  Burkholderia diffusa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Burkholderia diffusa"
                     /db_xref="taxon:488732"
     Protein         1..>381
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
     Region          25..356
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mtpaslieqy gpresmeydv vivgggpagl saairlkqla aekgteigvc vlekgseiga
       61 hilsgavmdp raitelfpdw keqgapltve vtedrflfls eksaittpnw alpenfknhg
      121 nyvislgnvt rwlgqqaeal gveifpgfpa aeilynddgs vkgvatgnmg vgkdgepten
      181 fqlgmelhak ytlfaegcrg hlgrqliskf kldanadpqa ygigikelwe idparhkpgl
      241 vihtagwplk sdtyggsfly hmdnnqvvvg fvvglgytnp ylspfeefqr ykthpsiraf
      301 leggkrvsyg araitaggll slpktvfpgg aligddagfl nasrikgsha aiktgmlaad
      361 aafdalqagr qsdelnaypd a
//
LOCUS       WP_175868103             266 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Burkholderia seminalis].
ACCESSION   WP_175868103
VERSION     WP_175868103.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..266
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27082
     Region          187..265
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mtgltieygv pparrhvara apraavvarp spvapsahad krpapasgwr gagaialava
       61 alhagvvlla arpaaappvq pprplpmtve ltrppeplpq aahpppivpp kplkqaptpp
      121 kpqipraavp hpaaapapsa vpqvareaap apapaalava tpapapapaa pvretapigd
      181 aaylrnpapd ypafaqdqgw egrvvlrvhv lasgtpdsve vrtssgrrvl dnaavaavkr
      241 wtfvpakrgd eavdgwvnvp idfklg
//
LOCUS       WP_175868149             834 aa            linear   BCT 11-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Burkholderia seminalis].
ACCESSION   WP_175868149
VERSION     WP_175868149.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18415115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..834
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=89179
     Region          8..32
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          31..261
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          38..66
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          71..99
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(72,75..76,79..80,82,106,109..110,113..114,116..117,
                     140,143..144,147..148,151)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          104..134
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          139..167
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          173..827
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          173..201
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          241..269
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(242,245..246,249..250,252,276,279..280,283..284,
                     286..287,310,313..314,317..318,321)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          274..304
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          309..337
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          343..371
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          377..405
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mesigpqlqa alahhqagrl veaktlydai ltaqpgqpda mhflgllacq lkqydaglal
       61 merslaarpd asyfnnlgnm lrecgrldda iahyrraval rpefpeahnn lgnalrdarv
      121 paeamasctr aielrpgyae aynnlgnvlq dlgeldaaaa sygkaiafht ayaeahsnlg
      181 hvlraqdkht eaiahyrral elspalpaar hglglslwal gelgeaarvl raavaaepgd
      241 adlhnnlagv lrdagdldga ashygraleh dpsmavahan lsgvlrrqar yaealrhaqh
      301 airlapglad ahnhagnayh glndldaada syrtalalnp adagaahnls vvllkrerhd
      361 dalaycrqal sagrpsaamh vnlgdilrgq gnvdaavpay rdalalvrdd addgaadvls
      421 rllfasaasa svppadylnd arrygrhlaa rstryphdvs eraararhrp lrvgfvsgdl
      481 rlhpvgifle svfahldrtr vaphvyatsd eedavtarlk phaaawrsia aldpqaaart
      541 ihddgidvlv dlaghtqasg lavfgwkpap vqaswlgffa stgcdaidyf igdaytlpes
      601 earhfveapw rlpdsylcft ppaddvpvgp lpmaanggvt fgcfgklvkl gddvvrvwsr
      661 vlhalpsarl llkareleha avrdataarf arhgidasrl afepasprad yfaaynridi
      721 alspfpypgg tttaealwmg vpvlgmrgtr fvthicesll haagvndwia gdeddyvaka
      781 vaaaadgarl aalradlrat llasplcdaa rfahhledaf hgmwarytet ahaa
//
LOCUS       WP_175868209             148 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Burkholderia
            seminalis].
ACCESSION   WP_175868209
VERSION     WP_175868209.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         <1..>148
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
     Region          17..>148
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 qygpresmey dvvivgggpa glsaairlkq laaekgteig vcvlekgsei gahilsgavm
       61 dpraitelfp dwkergapld vevtedrflf lsessavttp nwalpdnfkn hgnyvislgn
      121 vtrwlgqqae algveifpgf paaeilyn
//
LOCUS       WP_175868223             167 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Bartonella gabonensis].
ACCESSION   WP_175868223
VERSION     WP_175868223.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 167)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..167
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18930
     Region          9..>87
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(10..12,26,43..45)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mdkssdafrt isevaellel pqhvlrfwet rfrqikpmkr gggrryyrpa dvdllngikq
       61 llydqgytik gvqrllkeng vafvaafgng dldamnvvie kkhagqtfen tsnkpkkssf
      121 gllsfmrneg evsvgsvnly kdktdkallq etlfelieck rvldrar
//
LOCUS       WP_175868235             363 aa            linear   BCT 11-JAN-2025
DEFINITION  COX15/CtaA family protein [Bartonella gabonensis].
ACCESSION   WP_175868235
VERSION     WP_175868235.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..363
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=41375
     Region          29..349
                     /region_name="COX15-CtaA"
                     /note="Cytochrome oxidase assembly protein; pfam02628"
                     /db_xref="CDD:460629"
ORIGIN      
        1 mgqsemavkr lndnlltpvq krnrkqiqvw lysilllcla ivlvggatrl tgsglsitew
       61 kpvhgvippi gvdqwqeefl kyqqiaqykl lnpdmtlsaf kvifwwewah rvlgrlvglv
      121 allgliwfwa trrieknill plivvpilia fqgfigwwmv asgigqsnlt svsqyrlafh
      181 litaclviif vtylsrclse ysekpanqkv qyfaawlvif vlievylgal vaglhagkvy
      241 ntwplmdgqv ipdglfqhrp fwlnlfenpl tvqfihrffa yflfivsafh afyvqknvph
      301 sthsrraffi cvmimiqall giltllhevp islglihqgm alvvlcfava hwratkgayr
      361 vie
//
LOCUS       WP_175868359             212 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Bartonella gabonensis].
ACCESSION   WP_175868359
VERSION     WP_175868359.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..212
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23247
     Region          5..210
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msffpewpil iqfsvaslil alipgpdmml sigrtitqsk kagimcalgs atgfaiqvta
       61 valglsalif asprafvllk vagafyllwf aiqalrkqst fsiektssqy kssrrnylag
      121 iginllnpkv ilfnvtflpq finandpmat qkllilglsy ipislpitis tvfiahklfk
      181 slkqnplymr flnwliagtf tsfalhllit en
//
LOCUS       WP_175868367             332 aa            linear   BCT 11-JAN-2025
DEFINITION  complex I NDUFA9 subunit family protein [Bartonella gabonensis].
ACCESSION   WP_175868367
VERSION     WP_175868367.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Parey,K., Wirth,C., Vonck,J. and Zickermann,V.
  TITLE     Respiratory complex I - structure, mechanism and evolution
  JOURNAL   Curr Opin Struct Biol 63, 1-9 (2020)
   PUBMED   32058886
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Babot,M., Birch,A., Labarbuta,P. and Galkin,A.
  TITLE     Characterisation of the active/de-active transition of
            mitochondrial complex I
  JOURNAL   Biochim Biophys Acta 1837 (7), 1083-1092 (2014)
   PUBMED   24569053
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..332
                     /product="complex I NDUFA9 subunit family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0010257 - NADH dehydrogenase complex
                     assembly [Evidence IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=36534
     Region          12..286
                     /region_name="NDUFA9_like_SDR_a"
                     /note="NADH dehydrogenase (ubiquinone) 1 alpha subcomplex,
                     subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs;
                     cd05271"
                     /db_xref="CDD:187579"
     Site            order(18,20..23,42..44,86..88,101,123..125,136,140,
                     159..162)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187579"
     Site            order(136,140)
                     /site_type="active"
                     /db_xref="CDD:187579"
ORIGIN      
        1 mqldyalyqh pklitvfggs gfvgrhvvet ltkrgyrvri avrcpqkayy mlqigevgqt
       61 qmlktdikyr asvarallga daavflpgsl kqanqsnfks tqidgsynva eltaeagipl
      121 iymstlvane ntsclyshvk ftgeqiihnk hpqamiirps vifgpedcff ntladlsrfl
      181 pimplfgggq sklqpvyvgd vaefiarald gqaawgknyd lggpqiitfq nalenilkii
      241 hrkkiilsmp lstglliggi wgtigklpfi ptlvtanqir flqmdnivsq ealengytle
      301 gvgitpkaia aflpsylwrf rphgqfsqnl lv
//
LOCUS       WP_175868389              98 aa            linear   BCT 11-JAN-2025
DEFINITION  HPr family phosphocarrier protein [Bartonella gabonensis].
ACCESSION   WP_175868389
VERSION     WP_175868389.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Hu,K.Y. and Saier,M.H. Jr.
  TITLE     Phylogeny of phosphoryl transfer proteins of the
            phosphoenolpyruvate-dependent sugar-transporting phosphotransferase
            system
  JOURNAL   Res Microbiol 153 (7), 405-415 (2002)
   PUBMED   12405346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..98
                     /product="HPr family phosphocarrier protein"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=10437
     Region          11..97
                     /region_name="PtsH"
                     /note="HPr or related phosphotransfer protein [Signal
                     transduction mechanisms, Carbohydrate transport and
                     metabolism]; COG1925"
                     /db_xref="CDD:441528"
ORIGIN      
        1 mlskdtlpsq isrhfsicnk rglharasak fvqtvdnfna tvevekdgki vggssimglm
       61 mlaassgcnl tirvwgpeat dalnalenli nnnfgeen
//
LOCUS       WP_175868412             301 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter permease [Bartonella gabonensis].
ACCESSION   WP_175868412
VERSION     WP_175868412.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 301)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..301
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32864
     Region          11..288
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 midqlllpfq fsfmlkgmli viilsvpmam lscflilkrw allgdaisha vfpgvvvgym
       61 ttpwvivfla slpfawfqhm rpenitmtli tcgafvagmv calttgflgs nsrikqdtvm
      121 gvvfssmfgl glvlatsiys sldlnhilfg nllgvnwldi tqtaiisaiv tfilgakwrd
      181 fmlyifdsvq gramglrvsl lhytlltmis ltivaalkav givlvislli apgaiaylvt
      241 krfsfmlmia ilvaafsgfl giylslfigs dsastivlil tlifiaiftm iffhqntvqe
      301 t
//
LOCUS       WP_175868441             277 aa            linear   BCT 11-JAN-2025
DEFINITION  outer membrane protein [Bartonella gabonensis].
ACCESSION   WP_175868441
VERSION     WP_175868441.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..277
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=29992
     Region          82..277
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mnmkwlitas tfafvsvsaa qaadvivpps ptpvapvvva ptfswtglyl ggqiggfssk
       61 tkmdilargq kipvnkdilp klsgfmggly agsnidlgng lilgvdtdim wadksdtktg
      121 etfliaadhi nyikkmlkda sinigenvlk pdskqthsft fkqqwfgatr vrigfaaeri
      181 mpyvaggiay tqlqdtasis itdadsdkvi asgiltdekk tfigytlgag vdlamtnnii
      241 vraeyrysdf gkkkfsndky etsyktndfr vgvaykf
//
LOCUS       WP_175868502             428 aa            linear   BCT 11-JAN-2025
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Bartonella gabonensis].
ACCESSION   WP_175868502
VERSION     WP_175868502.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..428
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=48651
     Region          6..427
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mrlggrlqaa idvlkeietr yrpagealkd wglshrfaga gdravigtiv ydvlrrrysl
       61 qwrmesddir divfatlldt gkmtleqidn alegdrfapq llkakqrksw qkqqlvdapd
      121 yirgdipqwc qahlcplfgd nwiveaaala trpsldlrvn slkatpekvl kelaktklqs
      181 lpwfrqalrv apiekfdrhp nvqvepafqk ghfeiqdlgs qivahlveaq asmqvldyca
      241 gaggktlala snmnnrgqiy aydsdkgrla pifdrlrrag vrnvqiraqk eelksligqm
      301 drvlldapcs gtgtwrrrpd akwrltleqv kqrqteqrai lneaidylkp ngrlvyitcs
      361 lfadeneeqi shflqqhshf ypidmsalwq khfsfspdqp vfsnygltls pattqtdgff
      421 lsvlqkkh
//
LOCUS       WP_175868516             104 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF167 domain-containing protein [Bartonella gabonensis].
ACCESSION   WP_175868516
VERSION     WP_175868516.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..104
                     /product="DUF167 domain-containing protein"
                     /calculated_mol_wt=11951
     Region          1..83
                     /region_name="YggU"
                     /note="Uncharacterized conserved protein YggU,
                     UPF0235/DUF167 family [Function unknown]; COG1872"
                     /db_xref="CDD:441476"
ORIGIN      
        1 mfyqvdknnl ilfvylipks svdkiigiec rdsekqylvi rlravpedgk ankalikfla
       61 kqwkipsssi slksgavsry kqlyfsthle elkqiwqslr dcis
//
LOCUS       WP_175868594             262 aa            linear   BCT 11-JAN-2025
DEFINITION  ComF family protein [Bartonella gabonensis].
ACCESSION   WP_175868594
VERSION     WP_175868594.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..262
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=29826
     Region          15..222
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mfyfreaaln sgdilsqfie rfktmlyppi cpgckqnvst ygticsecwr dlqfitkpyc
       61 pvmgtpfvcd mgdgflsgea lrnsypfsrv rsvivhkgla rtlvtrlkyd dhielasfma
      121 nwmifagrev idecdviipi plhfrrfwqr rynqsaelar yiaasqkkll kpswlvrcrh
      181 trpqvslslr erklnvknaf kvshkvkkyl kgcsvllidd vfttgatvta aaaalkyaga
      241 rqvdvltfsr vlkedsifps sq
//
LOCUS       WP_175868637             363 aa            linear   BCT 11-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Bartonella
            gabonensis].
ACCESSION   WP_175868637
VERSION     WP_175868637.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..363
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=40124
     Region          1..261
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mrrlfynlff sfilslsstf alaqpfisvd vttghilkhn qaferwypas ltklmtayvi
       61 framsrgeis ankpitisey aakapayrsg ykagsvltld talsitmvks tndlaiamse
      121 avagsqkafv rkmnsearrl gmfgthfana sglpdpqnys tardiallav qirrefpqya
      181 hyfsipaidf gnnrkiqhns nnligrfygi dgmktgficd sgfnlvasat rnkrtiiavi
      241 lgannisere kkaaqlleig flhqgspqlt iatlkpygsn itqannmrqq tctpeaikmh
      301 ansyddqgni iltspfitas psfshplavh lihtpqtpki tvkplrkphs pykkranysi
      361 kkp
//
LOCUS       WP_175868611             863 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA translocase FtsK [Bartonella gabonensis].
ACCESSION   WP_175868611
VERSION     WP_175868611.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 863)
  AUTHORS   Jean,N.L., Rutherford,T.J. and Lowe,J.
  TITLE     FtsK in motion reveals its mechanism for double-stranded DNA
            translocation
  JOURNAL   Proc Natl Acad Sci U S A 117 (25), 14202-14208 (2020)
   PUBMED   32513722
REFERENCE   2  (residues 1 to 863)
  AUTHORS   Crozat,E., Rousseau,P., Fournes,F. and Cornet,F.
  TITLE     The FtsK family of DNA translocases finds the ends of circles
  JOURNAL   J Mol Microbiol Biotechnol 24 (5-6), 396-408 (2014)
   PUBMED   25732341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..863
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..863
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=95940
     Region          <360..861
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 mhnsktksis sssltddgtk sasredlsmk iteifpypev wkkaftlgkn vrftrtpeve
       61 ilrrrietdp ifakqfkift kqdrknitdi vhcnkkttnv sstkkvinpq sienktsvgh
      121 smvlkqlsqq amsrpsanip leedkqgmdk qehelhvknv lqkinsalhl sdnaffecgs
      181 lifehvdtqt skedntpidk snemipdvss afdesitaly rvleyrfpql ydsitsespa
      241 ermrgveqis dlmntnneam kkskechskl svedsshvln diealsdtgd tieneetnki
      301 iahntidsit kditknskel pamqandktk tlqstraplg nytsaflkni qpidcdvyef
      361 ppisllqkpv fhegtmipqe tlergaglle svledfgikg evihvhpgpv vtmyefepaa
      421 gvkssrvinl sddiarsmsa istrvavipg rnvigielpn avretvylre liqtrsfres
      481 efklalalgk gingepviae lakmphllva gttgsgksva intmilsily rmtpqqcrli
      541 mvdpkmlels vydgiphllt pvvtdpkkav talkwavrem eeryrkmakl gvrnidgfna
      601 rvalaaqkge timctvqsgf dketgamlyh eeamdltqlp yivvivdema dlmmvagkei
      661 enaiqrlaqm araagihlim atqrpsvdvi tgtikanfpt risfqvtski dsrtilgeqg
      721 aetllgqgdm lhmagggriv rvhgpfvsde evesvvahlk mqgkpdylat vtdnedenne
      781 dtsadstaev seeenfyees erlynqavki vmrdkkcsts yiqrrlsigy nkaaslverm
      841 eekgivgaan hvgkreilln egk
//
LOCUS       WP_175868674             298 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Bartonella gabonensis].
ACCESSION   WP_175868674
VERSION     WP_175868674.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..298
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33467
     Region          45..297
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mnddlskkrl grglaaligd inlnnnlars ssfdkltetg siserfvple siscntnnpr
       61 rhfteteldn laqsirqhgv vqpvvvrplk dhphrfelia gerrwraaqr vnlsqlpviv
      121 rdvddktale laiienvqra dlnpieeakg yemllnehgy tqvdlaqvig ksrshvantl
      181 rllklpekvq qfltdgqlsa gharciitvd npqdlaekii reglsvrqte ilayelanpk
      241 tkkrttmekd aetkslekll advigmkvii rhgkkggdlk ihyssleqld eicrrlqs
//
LOCUS       WP_175868685             169 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrofolate reductase [Bartonella gabonensis].
ACCESSION   WP_175868685
VERSION     WP_175868685.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11087044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..169
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=18539
     Region          5..168
                     /region_name="DHFR_1"
                     /note="Dihydrofolate reductase; pfam00186"
                     /db_xref="CDD:425512"
     Site            order(8,25,30,60,104,110,123)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(10,17,47..49,67,105..108)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 mtisicliaa vaensvigck gampwhlstd lqrfkaltfg kpvimgrktw dslkkplpgr
       61 tnivitrdct fsaeggvvah slsqacslai rvasqndvee ifiigggeif qqgfsfadki
      121 fltevlasie gdsffpifdk ekwtivqtqd ipkgdkdshp trfvvyerk
//
LOCUS       WP_175868753             786 aa            linear   BCT 11-JAN-2025
DEFINITION  LPS-assembly protein LptD [Bartonella gabonensis].
ACCESSION   WP_175868753
VERSION     WP_175868753.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..786
                     /product="LPS-assembly protein LptD"
                     /GO_process="GO:0015920 - lipopolysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90031
     Region          35..779
                     /region_name="LptD"
                     /note="LPS assembly outer membrane protein LptD (organic
                     solvent tolerance protein OstA) [Cell
                     wall/membrane/envelope biogenesis]; COG1452"
                     /db_xref="CDD:441061"
ORIGIN      
        1 mkaltrkkii ltklsafafr rvmaviltga lpycahaqsl msssqsrikn selplllsad
       61 eliynrdent vsaqgnvqve ydgnkvvaqk iiynqntgrl vaqgnveitq kdgnkiysnq
      121 idmtkdlgeg fvnalridsa nnvhftaqna trknnqvtif enatytacep csykpdrevl
      181 wkikarkiiw nnsvkkirfe nssfevfgvp iikfpnfely dptvkrasgl ltphffytdy
      241 lgmgmknsyf wnlaphydft lsstvytqqg lltegewrqr lkmgsynirf ahiyqmkphr
      301 fdndtidaqh knrymlatkg dfrinshwty gwdilaqsdr nfshayklen ysdptqlsqi
      361 ylngiagkny fdmrfyhfki qdsilndphy erhsqqawvl pridysftpd epiyngaltf
      421 hsniqsiyrr hadfsspdln enplntlrls gmagnslrlt nevewkkrfn trngliltpl
      481 fslradilti ngqenylenn alsamrgski rgmataglea rypflitaah sthiieptaq
      541 ifirnneqyi gqlpnedaqs fvfdattlfq rdkfsgydrv eggtranigl rysgnfndnw
      601 slygligqsf hlagknsfae kdlvnvgihs sleakrsdyv amfgathkng fsletrgrfd
      661 kktgkirrse ievsqkwklf wtsvqyayia sqpnyeypqe rqeisfqtgf kladywyins
      721 nagydlvsgt fvkrginlny adecfgvtfg yqqvmnpgsp pplqnfnfsl slrtiadigk
      781 kidpnl
//
LOCUS       WP_175868769             240 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Bartonella gabonensis].
ACCESSION   WP_175868769
VERSION     WP_175868769.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..240
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=26340
     Region          3..237
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 mienlallsf snggwgmiil ssagmtlsla lccgllglpl gllnammirs nikmakaiar
       61 lfstvfrglp elltlflvyy glqnliqnvf dyfnleitft inafvagvla lsmvlaafsc
      121 evwlgafnif dkgqyeaaka lglsrsttfc rivfpqlirn alpglsnnwl tllkdtslvs
      181 tialvdlmrq tnlavaatne pmlfylvacl lyllfsaffs ailrhletyt qigykkvlsq
//
LOCUS       WP_175868771             257 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Bartonella
            gabonensis].
ACCESSION   WP_175868771
VERSION     WP_175868771.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..257
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28665
     Region          16..255
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mnsknnlsis pnqpsvisir nfnkwygnfq vlhdinfdvq agehivicgp sgsgkstlir
       61 cinqleqaqk gsicihnvdi ntapiqqqkn vlrkigmvfq nfnlfphmsv iqncilapmt
      121 vqglskqqak erairylthv giekhcekyp lqlsggqqqr vaiaralcme pevmlfdept
      181 saldpesvge vleviaqlad tgitmlcvth emgfarkvse rilflengki vedtasdkff
      241 tnpksqrahe flakiky
//
LOCUS       WP_175868816             226 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Bartonella gabonensis].
ACCESSION   WP_175868816
VERSION     WP_175868816.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..226
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24827
     Region          1..224
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtailelvei errffeshkp livldkvnfi lnrgelvalv apsgagkstl lhiagllekp
       61 tagdvlvrgv scakrsdser tairrndigf iyqfhhllpe ftalenvmmp qmiaglnksi
      121 aedrarkllm ylrvshranh rpselsggeq qrvaiarava ngpsvllade ptgnldpvts
      181 ayvfqalsvl vrqsglaali athnyalakq mhrritlkdq kiielp
//
LOCUS       WP_175868779             271 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Bartonella gabonensis].
ACCESSION   WP_175868779
VERSION     WP_175868779.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..271
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29357
     Region          4..257
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 msnlvyrvlt afvfgvialy ltwlggasff lfawciggfl xxewmnitqe kwcilqkila
       61 sifyslfgff lvlnvsaslv fcilivlagv lalisiknsg wvfcgflyas fpvaalcflr
      121 dhevlgfqvv iflftivwgt diggyfigha lggpklapqf spnktwsgal ggtfvgvfcg
      181 iwvafgffdi nlaslfvpll tlvlsivsql sdlgqswlkr rfsvkdsgsl lpghggfmdr
      241 mdglvgatcl lyligslmsd mdapfnlfsm i
//
LOCUS       WP_175868640             312 aa            linear   BCT 11-JAN-2025
DEFINITION  site-specific tyrosine recombinase XerD [Bartonella gabonensis].
ACCESSION   WP_175868640
VERSION     WP_175868640.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Spiers,A.J. and Sherratt,D.J.
  TITLE     C-terminal interactions between the XerC and XerD site-specific
            recombinases
  JOURNAL   Mol Microbiol 32 (5), 1031-1042 (1999)
   PUBMED   10361305
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Cornet,F., Hallet,B. and Sherratt,D.J.
  TITLE     Xer recombination in Escherichia coli. Site-specific DNA
            topoisomerase activity of the XerC and XerD recombinases
  JOURNAL   J Biol Chem 272 (35), 21927-21931 (1997)
   PUBMED   9268326
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..312
                     /product="site-specific tyrosine recombinase XerD"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0006313 - DNA transposition [Evidence
                     IEA]"
                     /GO_process="GO:0007049 - cell cycle [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=35084
     Region          1..306
                     /region_name="xerD"
                     /note="tyrosine recombinase; PRK00283"
                     /db_xref="CDD:234713"
     Site            order(143,157..158,230,232,252,287)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:271175"
     Site            order(157,252,255,278,287)
                     /site_type="active"
                     /db_xref="CDD:271175"
ORIGIN      
        1 mksnivierf lemmsaerga sahtlaayqh dlqwaqdels shsvslfsaq kedligllsf
       61 mhtfgfaats qarrlsalrq fyqflyaegl raddpshdid tprqgrplpk iisedavtkf
      121 ldlaqlevnq adygskdylr alrlqllgem lyatglrise lvslpvqavr gkaysilvcg
      181 kgkkermvll skkayqvllq wldfrdqgtd akslylfpah setgyiarqv varelknlak
      241 ragiksesfs phvlrhafas hllqngadlr avqhllghsd isttqiythv leerlyrlvn
      301 ehhpladaqk ar
//
LOCUS       WP_175868875              69 aa            linear   BCT 11-JAN-2025
DEFINITION  cold-shock protein [Bartonella gabonensis].
ACCESSION   WP_175868875
VERSION     WP_175868875.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..69
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7421
     Region          1..57
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mstgtvkwfn ttkgfgfiqp sdssadvfvh isaversgls nlnerqknsy evlqvrrsgk
       61 faasnlaal
//
LOCUS       WP_175868892             206 aa            linear   BCT 11-JAN-2025
DEFINITION  J domain-containing protein [Bartonella gabonensis].
ACCESSION   WP_175868892
VERSION     WP_175868892.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..206
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=23240
     Region          150..>201
                     /region_name="DnaJ"
                     /note="DnaJ-class molecular chaperone with C-terminal Zn
                     finger domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0484"
                     /db_xref="CDD:440252"
ORIGIN      
        1 maitsklfds irissnkkqk sepeaqqcqw egcektgthk apagrnhegq ylhfciehvr
       61 aynknfnyfs glsnqdiakf qkdaltghrp twptdlsngt tkktaadyak irsgtaayqn
      121 rmrdpftlft krhsssnfsr klkpleakaf dtlglqanas aedikmkyke lvkkhhpdsn
      181 ggnraseerf rdvlhaynll kksglc
//
LOCUS       WP_175868897             260 aa            linear   BCT 11-JAN-2025
DEFINITION  SURF1 family protein [Bartonella gabonensis].
ACCESSION   WP_175868897
VERSION     WP_175868897.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Reeves,J.E. and Fried,M.
  TITLE     The surf-4 gene encodes a novel 30 kDa integral membrane protein
  JOURNAL   Mol Membr Biol 12 (2), 201-208 (1995)
   PUBMED   7540914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..260
                     /product="SURF1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0033617 - mitochondrial cytochrome c
                     oxidase assembly [Evidence IEA]"
                     /calculated_mol_wt=29317
     Region          21..260
                     /region_name="Shy1"
                     /note="Cytochrome oxidase assembly protein ShyY1
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3346"
                     /db_xref="CDD:442575"
ORIGIN      
        1 mskkaspmtk lqknscrcss llfgtlcicf fllfsalgiw qvqrlnwktn litsanqrvh
       61 lapikapqkd qwadvtfekn eyqpvvitgk flknknilvt avaqnttgyw vltplqttdn
      121 tltfinrgfi pmdernnfqs setlhtnass qqdsttnteq ttvigllrms ekngffprkn
      181 npvknvwytr dlpamaqklr lstvapyfid arkttpqanl pvagltiihf rnnhlvyait
      241 wfilaagvlg aflflvrqka
//
LOCUS       WP_175868907            1567 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD-glutamate dehydrogenase [Bartonella gabonensis].
ACCESSION   WP_175868907
VERSION     WP_175868907.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 1567)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1567
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..1567
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=178067
     Region          20..1562
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 mlqqktietk ntpdkiekil faqtdkedva yyenkelqka aaiavkafnl hkagknticf
       61 eqnltrnnrp itvitlvndn kpflldsiln lvnqhknhiy liahpildca sgkrislmqi
      121 hieslnkqqi ekleneltlv leqvnaavqd wkpmlekvek hihayqtglp shykkegeka
      181 ieflrwlkdd nfiflgmrty nfikdqkpik sfttsnielg iladasihiv ddesmkeppq
      241 evlsfmesdn llivtkansr skihrsvwld yiglkifdke gqlcgelriv glftssaytr
      301 silqipflke kaqtiiqrlg hnhadysgka lirvletypr demfrvdvdt ltenaklilq
      361 lderprlrvl vhtdsfgrfv silvyvprdq yssslrekvg ehfvelykgd ffesyplfle
      421 stlirvyyii hrkenetvpl heratleqhv rsiarswkds vqdialthkt teqqtrlase
      481 fpnsyrdlfs tedaikdagh ilslhddkpl fvtfyhapnk ekqnislrlf hrhealalsk
      541 rvpllenmgf rviaeqtlel pdgngqsvyl hdmqlestfq lcldfekdgq klaetfeaiw
      601 aqnadndafn altqtaeldw heivilrhyg rylqqagipy sqdrvaqtln aypditkely
      661 alfhlkfhqs htekeraknq qviqkrieek lqkvsglddd lilrrycnli daslrtnaft
      721 plsdgspqri latklnprqi eglpeprpyr eifvygpeve gvhlrfgpia rggirwsdra
      781 ldyrtevlsl vkaqqvknav ivpagakggf yphrlpqtsd raiiieaarq aytdfitall
      841 sitdnlvngk isaphdvifh ddpdpyfvva adkgtatfsd tanaisqanh fwlddafasg
      901 gsagydhkei gitakgawea vkrhfresfn hdiqtmpftc vgvgdmsgdv fgngmllskq
      961 tkliaafdhr difidpdpni eesyaertrl fklprsswqd ydqsklskgg gifsrkekti
     1021 tlspeaagai gfekqtgtpf eiisallkap vdllwfggig tyirattesd aqvgdranda
     1081 iritgeqvra kiigeganlg vtqrgrieyv snggrcntda idnsagvncs dievnlkivl
     1141 asalraktlt reernkllkk mtpqveqlvl rnnylqplal slaesqstad layqirfmhd
     1201 leqkklldrr vevlpdeqvl qqritqgkgl irpelavifa yakltlkeei ahssivddhy
     1261 fnaallnyfp tqiqenfeke vinhqlrrni iatliandii nrggptfvkq lhdsteqkte
     1321 niirvfiair dgfeipqlsd qidkldnkip glvqnklyaa mtpmlfettn wglhnmdlsr
     1381 pleeivktik qarnviekel thsqdndikq kieekarhys eegapkalak qlalleaapt
     1441 icdisliakq snsdliktag iyftlaqiir inrineasri ipvvdyydsm alsqakenis
     1501 eslrqiviki lksygkkedp fttwkkteed hihsvtnris aliendlnis rftfaavlis
     1561 qlqntgf
//
LOCUS       WP_175868960            1049 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Bartonella gabonensis].
ACCESSION   WP_175868960
VERSION     WP_175868960.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..1049
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113382
     Region          19..1030
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msqewnakqp mskaeqggli affirrpvft fvlnamiiia gfaawlnvdv relpdvdtpv
       61 ttvvtmfsga saetidrevt kviedavsrv sgvktissts sfgrsrvqin fnvgvdlnva
      121 asdirdalsr iayslpknad vpliikadsn aaammylvvt sptmsiddlt avvddqivda
      181 isavdgvgdv qvasarakif qididqakla sygltvadis rvladmttdv pvgslrnskq
      241 tlvvratarl ttpesfeqvv lkprvhlgdv ahvtlspdie nvilringkt giglgivrka
      301 qsntlnisag vravvdnlrs ivpssvhidv isddaifiks alhevevall iailsvilvi
      361 flflkdirvt lipavslpva ligtiaaiyl vgfslniltf lglvlatglv vddaivvlen
      421 ivrwrnmgig sraaavlgtr evffaviatt ltlvavfvpi sflpgqvggl frefgfvlai
      481 sillssvgal tlcpmlasrf lkehveekee kahhhftfly kwgsffhkay tyslhkclgk
      541 pwavvfaslv faalcvggyt klqqeltpae drafiflvin gpqgistqyl neqveqieen
      601 lqplrdtgei annysiagig gspntaflil llsswdkrlr sqqeivkdvn arvsqfpavl
      661 vfaaqgnslg vrgigqglqf ailgndyatl qpiadklvra lqadprfirp rltvdatqpq
      721 ffieinrkka sdlgidvtnl gdtlqamldg kkvgsinvdd hsydvklisr knpmkspsdl
      781 eniflktkds ryvplsviah lhekaiapql krekrmsavi lsanlapgit lgdayqtvqk
      841 iaspllskgt yvvplgeaet msetssnfmi vfgiafliil lvlaaqfesf isgfiimatv
      901 plgigcavia mllsgvslni ysqiglilli gvmakngili vefadqlrdk grsvreavee
      961 aanirlrpvc mtmicailgg iplvlakgag aearialgwv ivgglglati ftlyvtpvvy
     1021 lflgrfirpk aeedlrltke lnqvkrcie
//
LOCUS       WP_175868993             297 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome c1 [Bartonella gabonensis].
ACCESSION   WP_175868993
VERSION     WP_175868993.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10490041
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..297
                     /product="cytochrome c1"
                     /EC_number="7.1.1.8"
                     /GO_function="GO:0008121 - ubiquinol-cytochrome-c
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33612
     Region          48..285
                     /region_name="Cytochrom_C1"
                     /note="Cytochrome C1 family; pfam02167"
                     /db_xref="CDD:426633"
ORIGIN      
        1 mvnvfvgliv ivamsfsvqs vdsyaserld qeeerisfpl qipkkqewsf sgpfgfydka
       61 qlrrglkvyk qvcsschglk yvafrhlkal gydqeqikal aaqyevrdgp nregknfkrl
      121 ggatdyfpsp fmqeeegkfa lngtdppdls lmarargvfl pfpalitdvl thydtagpdy
      181 italltgyqe apkeveivdg ywynpyfiag nsltmappls dgvvtyedgt pqtveyyard
      241 vsaflmwaad phmeirkktg frvilfliif agliyilknr iwydleektk geikrkg
//
LOCUS       WP_175869007             318 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Bartonella gabonensis].
ACCESSION   WP_175869007
VERSION     WP_175869007.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..318
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=34771
     Region          1..318
                     /region_name="CeuB"
                     /note="ABC-type enterochelin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4606"
                     /db_xref="CDD:443656"
ORIGIN      
        1 mknywititl lillsilsif vgysdvtpsd lfaadphawl ifwqtrlprt isillvgaal
       61 alsgmimqll trnrfvepst agtvesaslg ilfimiflpd spvlgkmvva tlfamagtll
      121 fifllhcipl ksalivpltg imlsyiigsl snaiadyeml lpslqaylfg sfamilegky
      181 ellwlslplc ilayctadrf tvaslgedlt nnlglnyrvv mffglfivas itavivctig
      241 ripfvgliip nivssfmgdn mrhtapwvai sgaglvlicd llgriihpsf eipistimgv
      301 igsfifmill lrwrkrlg
//
LOCUS       WP_175869020             247 aa            linear   BCT 11-JAN-2025
DEFINITION  creatininase family protein [Bartonella gabonensis].
ACCESSION   WP_175869020
VERSION     WP_175869020.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Yoshimoto,T., Tanaka,N., Kanada,N., Inoue,T., Nakajima,Y.,
            Haratake,M., Nakamura,K.T., Xu,Y. and Ito,K.
  TITLE     Crystal structures of creatininase reveal the substrate binding
            site and provide an insight into the catalytic mechanism
  JOURNAL   J Mol Biol 337 (2), 399-416 (2004)
   PUBMED   15003455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..247
                     /product="creatininase family protein"
                     /EC_number="3.5.2.10"
                     /calculated_mol_wt=27843
     Region          8..241
                     /region_name="ArfB"
                     /note="Creatinine amidohydrolase/Fe(II)-dependent FAPy
                     formamide hydrolase (riboflavin and F420 biosynthesis)
                     [Coenzyme transport and metabolism]; COG1402"
                     /db_xref="CDD:441012"
ORIGIN      
        1 mvsntpflal lplgayeyhg ehlpfetdwi iaeafakalt lqtkeqyhia llpvekigys
       61 iehmdvigtq sltfsdavqr wieigencyh kginrlllln ahggnsplms ivitelrrrf
      121 smlavatsws rfglpqglie psqqhldihg gfietslmly lapekvhmek arnfhnkqad
      181 mitnyrylra ygphafgwtm rdlnpqgaag naskatpkag eaifshvlsq lrnllddinr
      241 fnintwq
//
LOCUS       WP_175869025             344 aa            linear   BCT 11-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Bartonella
            gabonensis].
ACCESSION   WP_175869025
VERSION     WP_175869025.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..344
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37876
     Region          7..342
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 meknalislk nvsrcfnkta gipavdnlsl eihtgeilgi igrsgagkst lirclnglek
       61 idtgslffeg inisnlsete wapyrqrigm ifqhfnllss qkvidnialp lkltginkkq
      121 rhkralelie lvglcgkeyc ypaelsggqk qrvgiarala anpkillsde atsaldpett
      181 qsilelladi nnrlnltvvl ithemevvrt iahrvvvlnq griveegrvk diftspqeet
      241 tiamlklvtp qlpekyakni kpigqeavie mniageiaqq pflhlledes glrarilhgg
      301 idtvqgetig rlflalpaqd qeafkkavqw ltekgqycev lgyv
//
LOCUS       WP_175869041             297 aa            linear   BCT 11-JAN-2025
DEFINITION  outer membrane protein [Bartonella gabonensis].
ACCESSION   WP_175869041
VERSION     WP_175869041.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..297
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=32778
     Region          <172..297
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mntkclials lftfitasta qaadtvvfqp skpnvsapss lssqitpvnv skpfswtgfy
       61 fggqvgyisn nntlnympea trgkwawvnr dlspelsgfe ggfyaganld lgddlvvgid
      121 tdmvwlgken tqtdnrrkil dkldsinatl qaagvpiiep snsqnemlah hndivvtsvt
      181 lkekwagalr arlgfashrl mpyiaggity tqmqyilsll aksqedstvf assdvfdktk
      241 tmigytagag fdfaitesmi mrteyrysef mkqkflndel einakmhdfr lgiaykf
//
LOCUS       WP_175869044             179 aa            linear   BCT 11-JAN-2025
DEFINITION  type II toxin-antitoxin system PemK/MazF family toxin [Bartonella
            gabonensis].
ACCESSION   WP_175869044
VERSION     WP_175869044.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Cook,G.M., Robson,J.R., Frampton,R.A., McKenzie,J., Przybilski,R.,
            Fineran,P.C. and Arcus,V.L.
  TITLE     Ribonucleases in bacterial toxin-antitoxin systems
  JOURNAL   Biochim Biophys Acta 1829 (6-7), 523-531 (2013)
   PUBMED   23454553
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10493638
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..179
                     /product="type II toxin-antitoxin system PemK/MazF family
                     toxin"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_process="GO:0006402 - mRNA catabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0016075 - rRNA catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=20232
     Region          63..174
                     /region_name="YifN"
                     /note="Uncharacterized conserved protein YifN, PemK
                     superfamily [Function unknown]; COG3692"
                     /db_xref="CDD:442907"
ORIGIN      
        1 msedknttpp ttppsltpve ichveaphia mehdhaawre heklklgdln apytkpphik
       61 prlksaprir qvfwcdfphd silpefwkkr pvlvlsknak lygnvtvlpf stksqpnnpa
      121 ayplqspieh kkawiicnyv ttvsvsrlsc shsgaprlse eefhkvvalm lqhlprlhp
//
LOCUS       WP_175869080             163 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Bartonella gabonensis].
ACCESSION   WP_175869080
VERSION     WP_175869080.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..163
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19028
     Region          1..138
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mdrldrkilh llqenatlsv adiakkvgls ttpcwrriqk leedgviqrr vavlspekvn
       61 ahvtvfvsir tsthshewfk rfskivqefr eviefyrmsg didyllrvvv pdieaydlfy
      121 kkliskidir dvsssfameq ikyttelpln yiklhektne qns
//
LOCUS       WP_175869084             290 aa            linear   BCT 11-JAN-2025
DEFINITION  DsbA family protein [Bartonella gabonensis].
ACCESSION   WP_175869084
VERSION     WP_175869084.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16062126
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..290
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=32900
     Region          76..105
                     /region_name="ScsC_N"
                     /note="Copper resistance protein ScsC N-terminal domain;
                     pfam18312"
                     /db_xref="CDD:465704"
     Region          134..287
                     /region_name="DsbA_Com1_like"
                     /note="DsbA family, Com1-like subfamily; composed of
                     proteins similar to Com1, a 27-kDa outer
                     membrane-associated immunoreactive protein originally
                     found in both acute and chronic disease strains of the
                     pathogenic bacteria Coxiella burnetti. It contains a
                     CXXC...; cd03023"
                     /db_xref="CDD:239321"
     Site            order(150,153)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239321"
ORIGIN      
        1 mihqpqnskg ilfskilapv mlsiliffps lsnatslpkt anhlnlenlk iqlledsnfl
       61 sklkekvtph idsyhiqqiv reyllthpei miemqlilqd klekqneyes qrqtstihll
      121 ekeifhsphd avlgnpngkk vlvdffdync qhcknsysni eglikeypdl rviikdlpil
      181 gpdsiavhtv vyafrkqfpe kypqihkall mhqgrvneak aikiavslga dekklhnaik
      241 dhnlqntfke niqiasklhi tgtpsyiigd kiligaasqd ilkqaidniq
//
LOCUS       WP_175869154             248 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Bartonella gabonensis].
ACCESSION   WP_175869154
VERSION     WP_175869154.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..248
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27002
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkiivavkrv vdynikirvk sdstgvdlsh vkmsmnpfde iaveeairqk esgkisevvl
       61 vsigpeatqe tlrtglamga drallvttdq tleplsiakv lkaivdeekp dmvflgkqai
      121 dddsnqtgqm laallgwgqa tfashlnien gyatvirevd ngtqtlclpl pmvmttdlrl
      181 neprytslpn imkakkkiie qktladlgid tkarltilsv eepkprqpgi kvanvaelvg
      241 alkqknci
//
LOCUS       WP_175869165             230 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Bartonella gabonensis].
ACCESSION   WP_175869165
VERSION     WP_175869165.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..230
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26108
     Region          1..215
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mltlfhspls tasrfirlil geygvatqli eeyewarrhe flalnpaghv pvfldehevp
       61 lsgpfvicey ldethgglrq enklfpenpl draevrrlnd wflnkfenea trhivrerih
      121 kremplaigg gapnsqilrn aranipphmn ylnwlcasrd slvgsalsya dlaaaasvsv
      181 ldflgeidwe qtpaakdwym riksrpsfrs lltdrvrgii asahyadldf
//
LOCUS       WP_175869202             263 aa            linear   BCT 11-JAN-2025
DEFINITION  tRNA1(Val) (adenine(37)-N6)-methyltransferase [Bartonella
            gabonensis].
ACCESSION   WP_175869202
VERSION     WP_175869202.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..263
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28551
     Region          10..254
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 mdkitnqsge tidsfhrgkf ylvqphkhgh rsgmdamlla slvptdlkgk vvdlgagaga
       61 aglavasrcp qvhvtlvers sfmvsyaqkt ltlkqnekla ervcllkadv tlkgnarike
      121 glidnsfdfa imnppfnnpv drktpdeqks dahvmpeamf dhwfrsaaai vkpsgylgli
      181 arpqslndil yalegrfggi ciipiharat taairilcya krgsraalsi lpalvihade
      241 gyafssrida inngcislwe llk
//
LOCUS       WP_175869217             243 aa            linear   BCT 11-JAN-2025
DEFINITION  SIMPL domain-containing protein [Bartonella gabonensis].
ACCESSION   WP_175869217
VERSION     WP_175869217.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Vig,E., Green,M., Liu,Y., Yu,K.Y., Kwon,H.J., Tian,J., Goebl,M.G.
            and Harrington,M.A.
  TITLE     SIMPL is a tumor necrosis factor-specific regulator of nuclear
            factor-kappaB activity
  JOURNAL   J Biol Chem 276 (11), 7859-7866 (2001)
   PUBMED   11096118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..243
                     /product="SIMPL domain-containing protein"
                     /note="The SIMPL domain is named for its presence in mouse
                     protein SIMPL (signalling molecule that associates with
                     mouse pelle-like kinase). Bacterial member BP26, from
                     Brucella, was shown to assemble into a channel-like
                     structure, while YggE from E. coli has been associated
                     with resistance to oxidative stress.; The SIMPL domain is
                     named for its presence in mouse protein SIMPL (signalling
                     molecule that associates with mouse pelle-like kinase).
                     Bacterial member BP26, from Brucella, was shown to
                     assemble into a channel-like structure, while YggE from E.
                     coli has been associated with resistance to oxidative
                     stress."
                     /calculated_mol_wt=26814
     Region          16..243
                     /region_name="YggE"
                     /note="Uncharacterized conserved protein YggE, contains
                     kinase-interacting SIMPL domain [Function unknown];
                     COG2968"
                     /db_xref="CDD:442208"
ORIGIN      
        1 mikiifkplk yckvkiaima fallatsfpi haeqskmkna tievvatges ftapdmvtid
       61 lavvtekkta qkalnannks mndivntlkn nnihandlqi sglslhpftp dnhqeekkne
      121 qlyrvtnflt vhirdlantg kildqiialg vnkidginft nadpnpfyke srkkaiveai
      181 kkaetiaqaa nvklgkiiki vednfhpmpn ltyqaldgty kettlsegqr gysvavtvtf
      241 sid
//
LOCUS       WP_175869225             458 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Bartonella gabonensis].
ACCESSION   WP_175869225
VERSION     WP_175869225.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..458
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50960
     Region          4..448
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mainelkrgm skrqviflal gsaigtglfy gsaqaiklag psvliaycia glaifmvmra
       61 lgemilhnpl pgsfaryaan yisplagflt gwtyvfemil vgladitafa tymgfwypdv
      121 apwvwalsit liitginlaa vevygelefw lssikviaii amiilgiaii flgwgesads
      181 savtihnlwk ngglfpngwf gflacfsvvv fafggieiig mavmevqnph qtiskainst
      241 pvrillfyim tlailmslyp wneiglmdsp fvsifenlgi syaanilniv vvtaaisamn
      301 sgmygacrmi hglsqegyal kkfqylskng ipvfvilmif aiflfgavln yfyheklffl
      361 iaamatfatv fvwimillsq ifmrikmpke eqnglsfpip fwpigsifsi lfmvfifill
      421 wyfdetrpvl ivgvswiawl vicfyalkly nfkqkklr
//
LOCUS       WP_175869416             387 aa            linear   BCT 11-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Bartonella
            gabonensis].
ACCESSION   WP_175869416
VERSION     WP_175869416.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..387
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43553
     Region          5..370
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mytvfrillt lwgilafntc graqnfqtpa sqvllldddt etilyekqsd lpffpaslak
       61 lmtaevvfhq lkegllkntq kfkvsenawr kggapsgttt mfakikteis isdllrglii
      121 vngndaaiil aegisgdeah faqlmnqrak iiglsqshfv natglpeegq fvtvrdmiil
      181 arhitqeypd yytlyrephf twnnifqrnk npliskeigv egfgfgysek egfsmvatiy
      241 knhqrlflai nglkdgkkht keierilqwg itafdlktif kkgetvgraf vyggkknfvp
      301 livkkpitfm lsnekevnit akikyhgplk apivsgqaig iiqiledkkv lvekpvfage
      361 nvqegsfftk vkdafyeiti gwlrkyl
//
LOCUS       WP_175869373             202 aa            linear   BCT 11-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Bartonella
            gabonensis].
ACCESSION   WP_175869373
VERSION     WP_175869373.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..202
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22944
     Region          3..189
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 misniycvgy nylkhahelg nvvqdepvif skpnsslilg sqidlpdfsk eihfeteivl
       61 riskdtfmvn erkaeecyda vtvdldltar dlqtklkekk lhwllskgfk gaayvsefik
      121 kekingpitf emklngktkq lgntkdmifs fekiisflsh yiqlrssdii ctgtpqgvgk
      181 lssfdeiely lknkliseik vk
//
LOCUS       WP_175869519             345 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Bartonella gabonensis].
ACCESSION   WP_175869519
VERSION     WP_175869519.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..345
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=38968
     Region          70..342
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mpkprpphlv keitrhgrii wyvrighgkr irirgtygtq efvdnyksal aelqglilpk
       61 sktgklvegs fawllkqyln ssnwhsysnt tkkqkeyilm kvcdtignvp yqtiekkhii
      121 agverrketp amaisflkal nglfnwaieq dllesnptvg vkrpalhnkn gfaawteedv
      181 ekyyqkwhhg thervwidvl lytglrrgda vrigwkdvkd niihlkteks kfqtdvflpi
      241 lpelaktlet gpigdetfic gkegkklvke sfgdafreac ntagikksah glrklaatra
      301 ansgatvsql kaifgwtnda maslytksad rkrlaleaik klqks
//
LOCUS       WP_175869420             257 aa            linear   BCT 11-JAN-2025
DEFINITION  TatD family hydrolase [Bartonella gabonensis].
ACCESSION   WP_175869420
VERSION     WP_175869420.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..257
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29021
     Region          2..255
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mlidthchld fedfsqdldn viqraldadv krmitisthv rkldkllaiv qsynqvfcsv
       61 gthpnhahee qnitaeelik lskhpkivaf geggldyhyd ystpeeqkki fqehiiasre
      121 tqiplvihsr nadidmenil reqikegdfp filhcyssgm qlaragielg gyisfsgilt
      181 fknafeirei akivpheqll vetdapflap iphrgktnep sfvcytaail aetiglsiee
      241 taqittrnaf clfnkmk
//
LOCUS       WP_175869546             161 aa            linear   BCT 11-JAN-2025
DEFINITION  crossover junction endodeoxyribonuclease RuvC [Bartonella
            gabonensis].
ACCESSION   WP_175869546
VERSION     WP_175869546.1
KEYWORDS    RefSeq.
SOURCE      Bartonella gabonensis
  ORGANISM  Bartonella gabonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Bartonellaceae; Bartonella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002778
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Bartonella gabonensis"
                     /db_xref="taxon:2699889"
     Protein         1..161
                     /product="crossover junction endodeoxyribonuclease RuvC"
                     /EC_number="3.1.21.10"
                     /GO_component="GO:0048476 - Holliday junction resolvase
                     complex [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0008821 - crossover junction DNA
                     endonuclease activity [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=17700
     Region          5..144
                     /region_name="RuvC"
                     /note="Holliday junction resolvasome RuvABC endonuclease
                     subunit RuvC [Replication, recombination and repair];
                     COG0817"
                     /db_xref="CDD:440579"
ORIGIN      
        1 mintilcfdl gtktgwalcg gsgdifsgtv dfksrrfegg gmrylrfkqw lneikqtags
       61 idavyfeevr rhvgtdaahv yggllatlta wcedheipye gipvctikkv ttgkgnaske
      121 eiikamrakg hapcddnead alailylike reilercpvt k
//
LOCUS       WP_175869787             177 aa            linear   BCT 11-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Burkholderia sp. BCC0397].
ACCESSION   WP_175869787
VERSION     WP_175869787.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..177
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18972
     Region          1..165
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtpahlipsp lgdiavried dvltglyfvg qkyfpplavv hdadalarsp varrvaeeia
       61 eyftgardtf svpihlrgte fqrrvwkell aipfgelvsy gditervglp msgaravgga
      121 vgrnpvsiiv pchrvvgasg sltgyaggie rkrallsleg aersrgarhp mqqtlaf
//
LOCUS       WP_175869811             191 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175869811
VERSION     WP_175869811.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..191
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20624
     Region          8..146
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtndassnsr ekilaaatrl aqthgyggln yrdlanevgi kaasiyhhfd skadlgaava
       61 rrywedsava lddmlagsrd pldclrrypd tfrkaletgn rlclcsfmaa etddlpevvm
      121 kevlafadvn vawlskvlsa aavvsaresk qraraifaai agaqliarsr adlslydali
      181 dnyrkagllp a
//
LOCUS       WP_175869823             293 aa            linear   BCT 11-JAN-2025
DEFINITION  ParA family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175869823
VERSION     WP_175869823.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..293
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32744
     Region          4..290
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mgvvvtvmnm kggvgkttas mhlgataaav rfgnpetkpr kvllidydpq fnlsqallfp
       61 ktyfeleqkn ktilsvlvdd dinlnpyhlq vpgnetppkl edvrtrvltf qngskldlvp
      121 stldlmyval gqanssikpi eerfskfise crkeydliii dchpagsvft ktslrnsdhv
      181 lipvvpqrya vrgiglmmtf ieakkqgang pkphilfnlt grtgisneeq qirsdkkyse
      241 yclnntpkry gafneldggn gfvwsnkkpy ssqawhnlys vtkeflsrve vik
//
LOCUS       WP_175869829             425 aa            linear   BCT 11-JAN-2025
DEFINITION  epoxide hydrolase family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175869829
VERSION     WP_175869829.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..425
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46602
     Region          39..143
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          110..>251
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 msstpfspmr rhllatsvaa gvsamlptgl haatgasgir pftahipdea vadlrrriaa
       61 trwpgretva desqgvrlar mqallgywgt dydwrkgear lngfpmfite idgldihfih
      121 vrsrhenamp mimthgwpgs ifellkaigp ltdptahgas addafhvvvp slpgfgfsgr
      181 ptktgwgsdh iarawgelma rlgytrfvsq ggdcgsvish rmamqrvqgl agihvnmpat
      241 vppdiatlla tdapapasls pkekaayekl atfyrdncgy sammvtrpqt vgyaladsps
      301 gqaawmydki sqwtysggvp ersiprdeil ddislywltn tatsaaqiyw edhsnnfnav
      361 dislpaaitv fpgeiyqapr swaersyhnl iyfnevdkgg hfaaweepel farevragfr
      421 plrrv
//
LOCUS       WP_175869855             334 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175869855
VERSION     WP_175869855.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 334)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 334)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..334
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35620
     Region          14..210
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          242..325
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msepllppip dvhdlvsell lgmrlsgvqy rriqvarpfg lnfghapgra qfhfvvrgpv
       61 llrdasgetm rleagdaill phggmhalvs dpdvpcrein gfevakicdt vasvasagvs
      121 patcattepg agdalifsac meldlggmqp lvgtmpkfmh vgtllarype irpmldamer
      181 eactaragfa gilarladvv aafivrgwve cgcgdatgwv qalrepklgr aivalhrdpg
      241 rnwsvaelat eagvsrsvfa erflaatgmt pvryltelrm rlaaqwiard reaieavayr
      301 lgygslaafs rafkrvvgkp pgavradgdv haea
//
LOCUS       WP_175869859             172 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175869859
VERSION     WP_175869859.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..172
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17904
     Region          40..168
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msayplhtid sapaeskpvl qqlqqafgvv pniaaamaas pvlingfigl fervhasslt
       61 epqiqtlllt navtnasewp vafhtalalk qgvlpadvda irrgelpada klaalsaaar
      121 tlidtrgrla dtdrqafvda gftaeqllev iavvaastit nyvgsvahal vr
//
LOCUS       WP_175869861             205 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175869861
VERSION     WP_175869861.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..205
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23184
     Region          1..192
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mklygfagtr sqralwglke ldadfefvsv nllegehkrp eflhlnpagk vpvlvdgdlv
       61 ipesaaivly ladkypekal lpvdpalrae ayrwvmfavt eleqplwrit rhtflyppek
      121 rspadielar edfatmavil dkhlegrefi vgdaltvadc vtaylidwas echliepfpq
      181 lraylerlya rpkapqriae arkaa
//
LOCUS       WP_175869862             240 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD family hydrolase [Burkholderia sp. BCC0397].
ACCESSION   WP_175869862
VERSION     WP_175869862.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..240
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26250
     Region          6..233
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mrlakvsals fdlddtlwpf gpsvvraeat lrawliehap ntesvlptqq alsalreeye
       61 rlcpdlasdy ramrigsirl aleranedvs ltdraydvfy aarnrvefye dalpalawls
      121 arfpliavtn gnadlrltgg geffrttlsa rafgfakpep eifhaaadal dvrpaellhv
      181 gddfhldivg alnaglqaaw vvrepraege qaslhpatph ltlrdlamlc ralgapdtvs
//
LOCUS       WP_175869867             304 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia sp. BCC0397].
ACCESSION   WP_175869867
VERSION     WP_175869867.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..304
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31822
     Region          5..298
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhshhevivi ggsfaglsaa mqlararrrv lvidagrprn rfaehahgff gqdgkppaqi
       61 vaeasaqlav yptvqriege ahtaerdadg hfhvtladgs rasadrlila tgirdelpal
      121 pglaerwgis vlhcpychgy evsgqrlgvl athplsvhqa ilipdwgptt wftqgvvdan
      181 eeeaallaar gvrierspvv eivgdaprid alrladgqvv pidalfigar tgmasdlaqq
      241 lgcafdegpl gpvvrvdalk qasiagvfaa gdastpmsna tlasasgvma gvaahrsliw
      301 glha
//
LOCUS       WP_175869876             337 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175869876
VERSION     WP_175869876.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..337
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35699
     Region          3..61
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..287
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 melhqleafs avmsagsvtg agellgrsqp avtrqiqele adlgyalfdr hgprvtptrr
       61 afllyeever slvglraiea raralgdeta epvriaatps laatlvpaal aalpddahap
      121 hyqlrsesae hvvhevlagt advgvvtlpm ahagldvhwi aqtpcvavlp addplvakpr
      181 ialrdlarrr ivtvanrhrl rqridaafaa arvdacvfie tnaslnavma aragigigiv
      241 dpatgvalpv dgvvaraldv dipfafgvat pagkartaav dalldalhrt trtllddvif
      301 hdaaahdall rgdrlrtdra arpprptrar rarpeaa
//
LOCUS       WP_175869899             167 aa            linear   BCT 11-JAN-2025
DEFINITION  aromatic-ring-hydroxylating dioxygenase subunit beta [Burkholderia
            sp. BCC0397].
ACCESSION   WP_175869899
VERSION     WP_175869899.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10791045
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..167
                     /product="aromatic-ring-hydroxylating dioxygenase subunit
                     beta"
                     /EC_number="1.14.-.-"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0009056 - catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=18722
     Region          7..167
                     /region_name="HcaF"
                     /note="3-phenylpropionate/cinnamic acid dioxygenase, small
                     subunit [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG5517"
                     /db_xref="CDD:444268"
ORIGIN      
        1 mmddrnalfs eqtfsravef vwreaemldr rdyrawldlw npaghyvvpi dpdatdfaat
       61 lnyvfddhdm rekrvqrmvs gysasatdaa rtvrtvsrft iesgsadtie lksaqvvvay
      121 krgvatlfaa dvthklhvda dgemriaekv vrlidsteal saigfll
//
LOCUS       WP_175869933             317 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175869933
VERSION     WP_175869933.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..317
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33451
     Region          9..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..294
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,229,246,273)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,193,
                     223..227,234..235,238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 madlrdvnln rlaifvavve agsltaaaer lglaktvvst hmqrlesevg anllvrttrr
       61 lsvtdagrvf ydacrdivra teaaldavss dagplrgtlr vsvpidygal vvapavvalr
      121 drhpalavel vandrvvdlv adnldvairi grladsnyra vqlgtyekwl vaspafvarh
      181 glprdpdala alpfvmlssl prphtleldn mrgghtsvrc vapvvsntat acraivlagg
      241 gfglltdfss addvaagrlv rllpgwrtap agihavypst rlpspkvraf idamktrlge
      301 tpaappvrap rskrsgg
//
LOCUS       WP_175869934             743 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia sp. BCC0397].
ACCESSION   WP_175869934
VERSION     WP_175869934.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..743
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79619
     Region          30..743
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mtvnrttaap arrrrakvgl gvglgvtlfa vqaaaaqgda stsgaeaagt atlpaitvsg
       61 erghplrare asvaglddap lrdtpasvnv itraliddqq akrlsdvvrn dasvvndyap
      121 vgyfegfair gfpvdlasai ridgltvsge qnvplenker veilkglagi dsgvvapggv
      181 infvtkrsan vasvtggvds rgstsaavdl grrfgpdhqf gfrinaaken mhsyidgtng
      241 rrtfgsiaad wdispraslq lnaefqqwiq rsapgyqllg gtvvpsvktt skalgtqpwa
      301 kpvttdalnl narfdyqfnd dwkayiaagr srtmiddnsa faygcsyaas caagaaspff
      361 fgangdydvy dfrspgeyrr nddlravttg kfatgplrhe ltlgvsvqrr vvhmadavyd
      421 yvgseniygp dltfspspns pgpsyprlda wqygvfgldr isigehwqvl aggkevllrq
      481 rswssldgdt thtdrsvflp qvalvykpvn vlslyasysk alslgdqapv ratnayaflp
      541 pveshqfevg akydwldrls ltaavfsisk pfqfadpdas gtsytfvqrg tqrhqgielg
      601 aagrvterlg ltasvaaira ravdsgspay eghqiinvpa lraslyadya vpgvaglnvl
      661 ggveysaarn aneegtarvp swfvfnlgar yttkigghrt vlrvsvdnlf nkfywrdage
      721 qqgdaylfpg aprtarvslt ydf
//
LOCUS       WP_175869936             396 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175869936
VERSION     WP_175869936.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..396
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43396
     Region          68..371
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 msfplepdgp lsrdvappqf gvdgeqaerd wplmthdeva avlaridgag epvrltwhsp
       61 rqfaaavlvr madgrglfvk rhhaslrdva gleeehrfia hlrergmpvv dvladrngat
      121 afasgewtye vhvlapgvdp yrgvmswqpf thpshayaag ralaelhras agydaparpv
      181 rtllssfrvl ssadlagale rwvdaqpllv ralgsrdwrg dvadaigpyh arlvpllpal
      241 pplwthgdwh asnllwtdag pgaqvrtvld fglsdrtcav mdlalaiern tvdwmapada
      301 rrieydqida lldgyesiap lsddayaalv allpivhtef alsevayfgc iidapaivdi
      361 aydgyligha rwfgerdgrq lldwlvqrrr gkqgav
//
LOCUS       WP_175869913             285 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175869913
VERSION     WP_175869913.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..285
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31273
     Region          9..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(32,57)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(39..40,51,54,58..59)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          105..270
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 madapdnllg aylrdrrekl dptalglpat rrrtpglrre evaqrahvsa awytwleqgr
       61 ggapsadvld rlaralmlne aerehlflig vghppevryh apasvtprlq hvldsldasp
      121 aiirtatwdv vawndaaaat ltdyatlppa arnilrlifv dgrvrdaqpn weriarfavg
      181 gfradvarsg atqavqtfvd emratstefd amwrdhdihs hhegtkeirh pqagrialdy
      241 safsvtgrpd lslviftpat padrariral vaareqaraa qapaa
//
LOCUS       WP_175869945             241 aa            linear   BCT 11-JAN-2025
DEFINITION  ZIP family metal transporter [Burkholderia sp. BCC0397].
ACCESSION   WP_175869945
VERSION     WP_175869945.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Dempski,R.E.
  TITLE     The cation selectivity of the ZIP transporters
  JOURNAL   Curr Top Membr 69, 221-245 (2012)
   PUBMED   23046653
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Guerinot,M.L.
  TITLE     The ZIP family of metal transporters
  JOURNAL   Biochim Biophys Acta 1465 (1-2), 190-198 (2000)
   PUBMED   10748254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..241
                     /product="ZIP family metal transporter"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24359
     Region          27..235
                     /region_name="ZupT"
                     /note="Zinc transporter ZupT [Inorganic ion transport and
                     metabolism]; COG0428"
                     /db_xref="CDD:440197"
ORIGIN      
        1 mtptaklall tlppvlaacf galaaawrap gpktssviqh ltggivfaaa alellpqdra
       61 halfpvvvgf vlgialmlai ralsgaietr feearlpvsl iivtaidlvv dglvlgiafs
      121 asdesgiilt valtlevlfl alsvsaalaa agigrtlsiv vpvglaalls laavagnaaf
      181 aglpaniyav llglgtvall ylvteellve ahevpetpfa tasffigfiv ffliegsvka
      241 g
//
LOCUS       WP_175869959             208 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0397].
ACCESSION   WP_175869959
VERSION     WP_175869959.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..208
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22136
     Region          12..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mfdlttlttf tavvlglfli pgpavllvls rtvqggrktg iltglgvasg dfvhtlfaav
       61 glsallmtsa lafnvvklag aayliylgvr allkkaadps lpqvspvtpl naylqaipae
      121 vlnpktalff lafmpqfvhp ergstfvqfa vlglifvvls slyttllacs irplgrivkr
      181 ltwltrwqgk iigsifialg lrvavqqr
//
LOCUS       WP_175870012             558 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175870012
VERSION     WP_175870012.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..558
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=60513
     Region          22..556
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 matvtpratn eslhptigaa rltlgnrill sfgvlfvlml vtagvsyerl rainaeavsi
       61 erdslpgvyl asslrgavne sfmllqqatf vetgpetvqr nlakiadalk dveslsvdyq
      121 nttfrdddrq rftafrgayd hyvpllndaa qksrashdea vaayakvlpa wtevvrnanv
      181 lvqenrkfae qsakliresv qdtevvlata ltfmllsalg lgymlyrsvt vpmarlvevh
      241 dvmrtgnltr rldlrrrdef gtletgfnrm adeltelvsr aqqsslqvtt svaeiaatsr
      301 eqqataneta attteigats reifatsrdl lrtmnevagv aeqsatlagv sqsgltrmge
      361 tmrsvmdaag svnaklailn ekalninqvv atitkvadqt nllslnaaie aekageygrg
      421 favvateirr ladqtavaty dieqtvkeiq savsagvmgm dkfseevrrg mldvqqvggq
      481 lsqiiaevqt laprfqmvne gmqtqangae qitqalsqls eaaqqtaesl rqssqaiddl
      541 tlvanqlrts vsrfkvda
//
LOCUS       WP_175870015             235 aa            linear   BCT 11-JAN-2025
DEFINITION  chemotaxis protein CheW [Burkholderia sp. BCC0397].
ACCESSION   WP_175870015
VERSION     WP_175870015.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..235
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=25170
     Region          80..229
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mnraaaatdd atldvddcwn rigtrgdrsc erlndclrcl ncpvyayhaa kllerpldva
       61 emadvtrrms afgtahardd dgdtrhaala frvadewlal pigvlreiag trpihslphr
      121 rhsavrgvvn irgtlriais igallgleag nagsgggdgr ftrllvaahq gepvvfpvde
      181 vegvlrfgas dwvpvpatvg rasaglsrgv lswrgksvgl ldddrlfdav trsmr
//
LOCUS       WP_175870064             372 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia sp. BCC0397].
ACCESSION   WP_175870064
VERSION     WP_175870064.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..372
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=39253
     Region          9..372
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mrhqrtalla asvsicapaw aqstitlygi vdtgveffth asptggamlr lptisggdlp
       61 srwglrgeed lgggikavfm lesgfamstg tslqngrlfg rqsfvgikge wgqltvgrqm
      121 tmtiygmada dvigpavfsv gsfdaylasa radnsveyrg kfsdltvgvs ysfgrdglsa
      181 sncggqlpgd mmscraisam lkydranwga aliydeqrgg agatamtvvp glssvafans
      241 gdtdrryqan gyvlvgrvkl gggwlhreik gdvrtvrtdl gylgvsvpyv awvfdaqish
      301 irnrsydadg tmgvfrvnyn lskrtavygl laymknsgsg aaysvssssi vpavpargvg
      361 qagamvgirh lf
//
LOCUS       WP_175870077             203 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175870077
VERSION     WP_175870077.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..203
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=21402
     Region          <49..203
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(77,79,83..84,87..89,91..92,96,99,108,110,112,
                     116..117,120..122,124..125,129,132,141,143,145,149..150,
                     153..155,157..158,162,165,174)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          77..108
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          110..141
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          143..174
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          176..201
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mrserfthai raaaaalala alagcahlpd qpaygkadpa alrrydgdwf daarvgrvdi
       61 lralhdagyp vdatdshgyt avilasydgq paaldyllsa gadacvgdrh gntalmgalf
      121 knepdiarrl idtrcpidqt ngagetalgf atlfnrfeli pllvaqganp nhvdrrgqsl
      181 lqlalthdnt yaadalrnag akp
//
LOCUS       WP_175870066             359 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175870066
VERSION     WP_175870066.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..359
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38557
     Region          4..359
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mitfdlseeq elarnamrsf aqgelrpiaq kldrdsaipv stldalwstg liqmqgnedq
       61 vrcpilnaiv leelaaadat lalalaapva ftqaildqgs qqqretllpl fygstfraaa
      121 ialmephfgs dvssltttav rdkdgwrlng rktlvplasa ashflviaqa egeraafivg
      181 rdtagmnvea pvptvglral emsdirfdgv fvpnsarlgn gagmnvqriv dssrvglaav
      241 mtglsrgvme yvipyakdrv vhgsalaskq siafriadmh idvaamrmmg wraafelagg
      301 qdatrssqla ytyaarqsms iadeglqifg ghgfvrehpi emwyrnsrav smlegvagv
//
LOCUS       WP_175870083             819 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175870083
VERSION     WP_175870083.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 819)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..819
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87015
     Region          496..777
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mrhillgwll aavvsaahaa apapaaasaa sgaapaltpq earqalnvle nprdraqvet
       61 tlraiaavga lsapavpase aaaasgasaa aapaaltsng lasmlvrqgs rwsaqignal
      121 qeslrslldi gsvgswwhdk lvradqradl thtlgillav llpalvvewl akrllrrala
      181 avaarradts rgttpdsaas deapapppdt stppdtaaad tapssspsqg harrhttllh
      241 rmpralvsla lravpllvfv gvasltmsll veadtpiesa lealidtyvi grlvtivsrl
      301 ffqpdarqlr llhisdawae faqrsiariv ivvgactaav eiaanfglte aghvallkav
      361 alvghvmisv lilqcrrpva ariraagadr ptftvvgnal adawapvsvf ivmalwfvwa
      421 ldvhngyrvl itlggrsiav miamrmvsiv vfgalarlfq rreddrtlvh lhayryypll
      481 rqivsgaigi vtvvlllqiw gvpifrafet gtighrlasa lvtiaiaaiv alvvweaani
      541 aierrlqrwt regnlvraar lrtllpmlrs llfvmialvv vltglselgv nvgpllagas
      601 ifgvalgfgs qklvqdfitg ifllmenamq vgdwvtlagv sgtveylsir tvrlragdgs
      661 lytipfssvt tvnntnrglg naavkvsiay gedieraiat lkeigaalrd dpkyhdgils
      721 dfsywgidqv dgaalalagq mqctdsarws vqrefnrria etfrergiri anpqrslvay
      781 adgsrpvgnd endlrpdtrn aaepaarpps pdaakrksg
//
LOCUS       WP_175870127             488 aa            linear   BCT 11-JAN-2025
DEFINITION  flippase [Burkholderia sp. BCC0397].
ACCESSION   WP_175870127
VERSION     WP_175870127.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..488
                     /product="flippase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52327
     Region          5..395
                     /region_name="MATE_Wzx_like"
                     /note="Wzx, a subfamily of the multidrug and toxic
                     compound extrusion (MATE)-like proteins; cd13128"
                     /db_xref="CDD:240533"
ORIGIN      
        1 mdkgilknvs infiglilpt fvslvtvpay ihalgveryg vvslvwtlig yfgildlgms
       61 maaqnhiska lasgnadesa rvfwsafwln lgtgiaggll iyfgafvyta yftkvsaamq
      121 hevylalpwl alaiplanvs wvfagainga erfgvfntnq tigtflfqll plgaawwiap
      181 nlqtvlaaav varliaavml gqasikvlgi rridppqwgt akglfnfggw mliasmtsmi
      241 adtldrvmlg agmgakfvty ytvpqnlvtr lnmlpnalvr tlfprlsavg rdhadtlarq
      301 sleflngvft pvgivaifal apfltlwvga dlaahsapvg rvlvisvwlv gqasvtrili
      361 qsqvnparaa faglvempff vgglwfgihh fgligaavvv aaralvdygv llylsairmr
      421 aivldmlahl afllaslfla qawpglvqsi gmcaavlvln vawsltmtpg lralvrdlfv
      481 rlnarrta
//
LOCUS       WP_175870155             559 aa            linear   BCT 11-JAN-2025
DEFINITION  glycerol-3-phosphate dehydrogenase/oxidase [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175870155
VERSION     WP_175870155.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Austin,D. and Larson,T.J.
  TITLE     Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol
            3-phosphate dehydrogenase of Escherichia coli K-12
  JOURNAL   J Bacteriol 173 (1), 101-107 (1991)
   PUBMED   1987111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..559
                     /product="glycerol-3-phosphate dehydrogenase/oxidase"
                     /EC_number="1.1.-.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0004368 - glycerol-3-phosphate
                     dehydrogenase (quinone) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=60838
     Region          35..>70
                     /region_name="Pyr_redox_2"
                     /note="Pyridine nucleotide-disulphide oxidoreductase;
                     cl39093"
                     /db_xref="CDD:476868"
     Region          55..548
                     /region_name="GlpA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0578"
                     /db_xref="CDD:440343"
ORIGIN      
        1 mmflpsrkpr tdrsgmtate plrvnrdehl arleadtfdv livgggvtga yaafdaslrg
       61 lrvalveksd fasgtsskss kmvhgglryi eqgnlglvrh sllerqrlrr narhlvqrlp
      121 flfpvmereg vfdrrlakaf esllwtydia ggwregilhq kltkaevlsh cptfnetylt
      181 ggflyfdarv ddarltlnlv rtaafhgaav anharvvelt rdghgtvdga ivhadgrerr
      241 vrarvvvmat gvwlrdwtga rkgdtsalqv rpakgvhvai pwlkirndct vtipvpgrnr
      301 ratitrwgnv sylgttdedy dgdlddvhct rqeldflleg arsalkvdls aadvvgsiag
      361 crplvgppgg ktiemkrnhe ihvapdglvt ivggklttsr hmaeqtidtv gkllgrrtrc
      421 rtksayllga agydpqaiva sgglaahlge rygtearfvg dladatpsll apiveglpys
      481 eaevlyavrh efarsvddvl srrtrarlma rdasaraapr vgailkaelg lsdaavasqv
      541 rdyvaavale kailmgehg
//
LOCUS       WP_175870163             302 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175870163
VERSION     WP_175870163.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32882
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdllatmriy vrvvergtms gaardldmgq pavseriekl ekhlgtrllm rsartlacte
       61 egrifyersk alleaaelav asvsktenal dgtirlaapq cfgevvmpav lmqirtaypk
      121 lhidlvlndd ivdpvtegvd isirvgqlrd ggfvayalga vgrvlvaaps yldrhgpldt
      181 kadlanhpfi rvkgvfaneq vplqrdggav dyarirtvmt tshwrpmfdt iaagggigvv
      241 qhpacadala hgrlvrllph ydipdfalnv lvhaqrplpp rvravvdllk talpplltkr
      301 dr
//
LOCUS       WP_175870182             142 aa            linear   BCT 11-JAN-2025
DEFINITION  TadE/TadG family type IV pilus assembly protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175870182
VERSION     WP_175870182.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..142
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=14522
     Region          8..132
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mtrgatgarh argvvslefv lmlpfllmvl igiidtslll cdkavitnas reaaragvml
       61 rvpmltttqi anvassytqn slitggtatt ptvtvtqang ttsgtaltvt vtytysgmvl
      121 gsafsaltgp vtisassvml ye
//
LOCUS       WP_175870178             476 aa            linear   BCT 11-JAN-2025
DEFINITION  CpaF family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175870178
VERSION     WP_175870178.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..476
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51276
     Region          85..465
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mtfgtrkrpt pdpapagsra apredvpaag pavspappaa ppaapargtt vadtqealir
       61 sgkfdairta vfasmnmsaa lmktrdevra gieqvaahtv ererlkitag eqvlivdail
      121 ndmfgvgpie plladdtvsd ilvngpdqvy veragrlelt plkfrdnahv tsvaqriaaa
      181 vgrrvdessp mvdarladgs rvnvvlppia mrgasisirk fakrditlar mahqgnishg
      241 mlqvlkvaca crlnivisgg tgsgkttlln alsqhieehe rivtiedaae lqllqphvvs
      301 letrpenteg lggisqrdlv rnalrmrpdr iilgeirgae afdvlqamnt ghdgsmttih
      361 ansprdaisr lesmvmmana nlqllsirrq iasavhlfvq vermrdgvrr vtriteivgm
      421 egevvitqdl fafrqdgdtt rdavkgvfea sslrpafapr aayygvedal sevfrq
//
LOCUS       WP_175870188             526 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0397].
ACCESSION   WP_175870188
VERSION     WP_175870188.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..526
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52741
     Region          37..467
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,160,
                     163..164,167,291,294..295,298..300,303,331,335,387..388,
                     392,396,412,415..416,419..420,423)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msqsspasra saaaaprtgt rlpaaatlav asatcslivl dtnvvavslp siarsfhasf
       61 adiewvvsay mtafaacllp aggladrfgr krmlftglai fflaslgcgi apsagwliaa
      121 ravkgggaal lltaalavia vianrfpdgr erarawaiwg mcmgiataia plvggaitqw
      181 igwrwvflln lpvclllaag arvaidesnd phakrvdaag sllfgaalac aiaaligaps
      241 hgwlsaatlg rlalaaalla afvgaerwqa rpmidlalfr qprfvgavla mfgyaacaqv
      301 mmtflplylq nafgmsaida glgmlpfafa miagpslgaa laarvssggv lagglaliga
      361 gnlataalta sgdyrlvalg mfvtgcgagi mngdtqkaim acvppnrtgm asgistttrf
      421 saivtavgvl gavlaastht rldsllsatp glrafadasf mssllagdla qalgrvppsa
      481 agalaqaapv afasgfaeal tvsgvlalga avvaytllaq pvrera
//
LOCUS       WP_175870223             250 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175870223
VERSION     WP_175870223.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..250
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26718
     Region          10..248
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mlpadtptlr afallehlvq agdavsladl ardvdipkas lhrmlaslea gglvirepgr
       61 knayavgprl arlgtgvmlh agtrrlrhai lerlvadlae tcnltalydt evvyldrvea
      121 dwplrldlkp gsrvpaycsa sgklllallp rderaalvrt malprhtpnt isdpelleae
      181 ldrtahkgia idneefvagi aciaapvlda dgaciaavav hapvsrapls rlldhvprlq
      241 eaaralaqtf
//
LOCUS       WP_175870231             112 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia sp. BCC0397].
ACCESSION   WP_175870231
VERSION     WP_175870231.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 112)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 112)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..112
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12505
     Region          26..>79
                     /region_name="Acetyltransf_7"
                     /note="Acetyltransferase (GNAT) domain; pfam13508"
                     /db_xref="CDD:463905"
ORIGIN      
        1 mhvvvfrdrc arvirivfdd arvtavayrd deaigelgid ddgdavrtps larlyvepay
       61 rrsgiahtll acasrefgrp iridtaarew pdsptwatlc rcleyeglvv vr
//
LOCUS       WP_175870290             541 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia sp. BCC0397].
ACCESSION   WP_175870290
VERSION     WP_175870290.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..541
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57633
     Region          20..463
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpgqgnahps vplsrsahpd aghgkfkkql sltdltfigl gaifgsgwlf aashvstiag
       61 pagifswllg gfavlllgiv ycelgaalpr aggvvrypvf shgpllgylm gfitliafss
      121 liaievvaar qyaaawfpgl tvegssdptt lgwlvqaall cfffylnyss vktfakanni
      181 isvfkfivpl avigvlftff kpanltvhgf apfgmpgiem avsaggiifa ylgltpivsv
      241 asevrnpqrt ipialilsil lstliyvllq lafigsipta mlaagwhdvs kafslpyrdi
      301 alalgvgwla vmvvadamis psgcgniymn atprvvygwa ktgtffkvft rvdeasgipr
      361 aglwltfgla ifwtlpfpsw ealinivsaa lvlsyavapv svaalrrtap dlprpfrasa
      421 fgltgpasfv iaalivywsg wstvswllgl qivmfaiyla crrwvptahl slaeqvrssa
      481 wliafyaami vlsylggfgg tgrlahpydt vvvaavalvi yywgantgvr sdklqlddde
      541 d
//
LOCUS       WP_175870236             234 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia sp. BCC0397].
ACCESSION   WP_175870236
VERSION     WP_175870236.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..234
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24459
     Region          23..225
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mtdalplttd pdsglqyrlr patgravarl lllhgvggne tnllnvgdai dprieiaflr
       61 gpltfgpnqh awfpvrfgpn gpeidaarad esrvqlitll halrardgaa palatviagf
      121 sqggimsasv gltspgdvsa favlcgrilp eidpliasrd alsalhaliv hgrfddklpv
      181 swadkadakl aalgvvhdtr lyaaghdlta emagdfgrwv geragldrsa sqpg
//
LOCUS       WP_175870308             314 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175870308
VERSION     WP_175870308.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..314
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33235
     Region          16..294
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mtpfvqpdvs hdepaiaeri asamplmtpi hrrmgefvla npfraatmri delaqavnas
       61 iatanrfaka lgfdgypamr aalvrgfeat lgpverlrsa qeqesgvrga vwidavfdqa
      121 aanientrah ldaadveaav eaivgarrvl ilgagssafl aglmehglsv chdsvqslal
      181 lggpshaarr lytadsrdlv ialafpryvk dtvelarraa argagvlgis dgpqsplapi
      241 aslnlyvkae rrfaatseaa vltmiealid avalrthrsa ksaaemtefl lpwlvqpqaa
      301 lsaanpsfpr pkks
//
LOCUS       WP_175870321             275 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175870321
VERSION     WP_175870321.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..275
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=30412
     Region          7..262
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 msatfptdap vrvsfrnvsm efytpqgrir vlddvslnir qgefisivgp sgcgkttlmn
       61 llggfaqpts gqvlldgrpv agpgpdrgvi fqeygvfpwl tvrqniafgl klsgskipra
      121 ghheivqrym almglkdfad hfpkqlsggm rqrlaiaray avqpqfllmd epfgalddqt
      181 rsamqnllle vlqtegktvl lithsvdeai ylssriivvt arparvravi dvpfgyprte
      241 svyedrrfge lrahiralvm eeyavqtqqt gqsmd
//
LOCUS       WP_175870363             366 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175870363
VERSION     WP_175870363.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Saurin,W. and Dassa,E.
  TITLE     Sequence relationships between integral inner membrane proteins of
            binding protein-dependent transport systems: evolution by recurrent
            gene duplications
  JOURNAL   Protein Sci 3 (2), 325-344 (1994)
   PUBMED   8003968
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004772
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..366
                     /product="ABC transporter substrate-binding protein"
                     /calculated_mol_wt=39877
     Region          62..364
                     /region_name="AfuA"
                     /note="ABC-type Fe3+ transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG1840"
                     /db_xref="CDD:441445"
ORIGIN      
        1 mpfapkhlaa alavvlgtaa gsavaqvpag ypgnyqgvid aakkegkliv ysttdtglvr
       61 plikdfesly gvkveyndmn stelynryis enaasstsad vlwssamdlq vklvndglma
      121 sydspespnv pqwaqyqkqa ygttfeplai vynkrlipen evpttradli kllttqadkf
      181 kgkvttydie ksgvgfnylt qdahvnekvt welvkaigat gpklqsstga mmerissgen
      241 ligyniigsy ayakakkdks igyvfpkdyt qvvsrlatis kkaknpnaak lwvdyllskr
      301 gqtlianqan lyairadvtg etsaasltke lgdslkpiqi gtgllvyldq skrlaflkqw
      361 qqsikr
//
LOCUS       WP_175870370             271 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175870370
VERSION     WP_175870370.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..271
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28860
     Region          21..266
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mvsaavless aaaapavtap rgaridirrv shafdgpgga lpvlddvsls vaagefvall
       61 gpsgcgkstl lrlvagldaa gqggiaqdgv pierpdpsri vvfqdptlyp wrrvranval
      121 gleargvart aqhrvddala rvglqdfanv fphqlsggma qrvalaralv ndprllilde
      181 plgkldsltr ltmqaeltal wqrdgfsall vthdveealf laqrvivfgp rparivaelh
      241 vdlpyprhrg dprlaelrhd alrhlgldas w
//
LOCUS       WP_175870371             344 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175870371
VERSION     WP_175870371.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..344
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37123
     Region          33..328
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mtpttaptpa dapddqrrrl lraagaaala vpaitlgrka wsapplkklt fawnqnafcl
       61 tpivvaqerg ffeknglkve linysgstdq llesiatgka daavgmihrw lkpleagfdv
      121 kiigsshggc vrllgakaag vttlqalkgk tvgvsdlaap gkhffsilla kngidperdi
      181 twrqypadll gvavdkgeih aiadgdpnly llekrsngay telatnlsge yarkvccvig
      241 argdlvrndr psaaalarsi vqateythdn pneaakvfak yspkispddl rklyatltyt
      301 hhptnvdlqq eiafyaddfr risvlkkstd pqrfaqqvya nvlg
//
LOCUS       WP_175870403            1082 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia sp. BCC0397].
ACCESSION   WP_175870403
VERSION     WP_175870403.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..1082
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115490
     Region          1..1065
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mwivnlalrr pytfivmaim ivlatplalm rtpvdvlpai nipvisviwn ysgfsatemt
       61 nritsvheri ltttvnniqh vestslpgia vvkvflqpga nvqtaiaqtv ssaqaivrqm
      121 pqgatpplvi tysassipvi qlglssktls eqsladialn flrpqlitvp gvqipfpygg
      181 rtrvvaidld pqallakglt padivnavna qnlvlptgta kmgqteyrid tnasadtvad
      241 indlpvqtvn gattylreva svrdgfapqt nvvrqngqrg vlisilksgd astlkvvsdl
      301 kallpkvipt lpegltitpl fdqsvfvnaa vqgviheali aavltammil lflgnwrstl
      361 iiaisiplsi ftslialsal getinimtlg glalavgilv ddatvtieni erhlhlgtrr
      421 aapsvpsspl ggqrpegawg ssfstnlhea ilegageiav palvstlcic ivfvpmfflt
      481 gvarflfvpl aeavvfamla syvlsrtlvp tlamllfrpq qastgpdhat srfarihhaf
      541 nhaferlraw yvvllssllv rrrfyalcfl gfcvlstglv fvlgrdffpn adsgnirlhv
      601 raptgyriee tarladqver viretvppde lgaivdnlgl pvsginlsys nagtigtldg
      661 ellialkpgh ratghyvqtl rtllpqrfpg vefffqpsdi itqilnfgqp aaidvqvlgn
      721 dlasnmtias slmkkirqip gavdvhvlqr ndeptlladm drtrmqqlnl saqnvaqnml
      781 islsgssqtt psfwinprtg vqyplqiqtp qynlssvdal lgtpisasgr tgmplqllgn
      841 lvqvrstanp avithynirp aidvyvsveg rdlgavagei drivadarat lprgtslamr
      901 gqietmrtsy lglgagvama ivlvyllivv nfqswldpli iisampaala giawmlfitg
      961 thlsvpaltg aimtvgvata nsilvvsfar qrlaagappl taaleagatr irpvlmtala
     1021 miigmvpmal glgegaeqna plgraviggl lfatvstllf vplvfggvhs rlarrrarqa
     1081 gh
//
LOCUS       WP_175870410             549 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175870410
VERSION     WP_175870410.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..549
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=56336
     Region          15..269
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
     Region          297..546
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mqnhevsadd appkaqrgiq svevggrlld afarrrkplg lselaaaadl staqahtylv
       61 sltrlalvkr daitgnyepg plslrlglms ierqpayrat lphaarlaet vglsvalsvp
      121 gvlgptivri ehggyplhmn lhvgsvmsld ttatgrvfra fgdptqldam aasqagagdt
      181 lagaeggsva pdaeaqhvel dairargier sidrpspgvs gmcvpvfdah ghlqlaltvi
      241 gstgsidvdw dgpiaaalrd aarqataslg aaraepapap apgaarvppa laddakaqrg
      301 inaldstgel llalvsagra lplrdlataa gmpaakafph lvslqkigll srddagcfdg
      361 gplaqalgli amqrvsptrd aeaeivalag atdmsvaaat lgplgptvir leesarpqhv
      421 slqvgtvmsl vntaigrifa sgmsddvlad llanepvrla gapaapddaa frarlaaira
      481 deldfafdap vpgigtiaap vfdhtgsirl viaiigssrg fprgpdsela qtlraatrrl
      541 swrfgwigg
//
LOCUS       WP_175870432             442 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0397].
ACCESSION   WP_175870432
VERSION     WP_175870432.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..442
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46553
     Region          28..407
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(39..40,43..44,47,79,129..130,132..134,137,157,
                     160..161,164,262,265..266,269..271,274,302,306,355..356,
                     360,364,380,383..384,387..388,391)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 msthhaqals saagdanasl nrllfrklmp lliaayvisf ldrtniafak hsmgvdlgis
       61 saayglgagl ffltyalfei psnlimhrvg arfwitrimi twgalsvama fvsgetsfyv
      121 mrlllgvaea glfpgvmlyl tywfsreera ratgyfllgv cianivggpl agalieldgt
      181 lgfhgwqwlf vvegipaill afvvwtrlpd rpsaapwlap etgralerkl aaeqdagvaa
      241 hgghafgval rdpqiwlaif vyfchqltiy tvifflpgii gasgrlspfa vglltslpwl
      301 aaalgagtlp rfareshhsr rmlcaglvvm aagmigaaha splagllcvc vaasmffvvq
      361 sivftfpasr lagsalaggl glvntcgllg gfvgptvvga ieqatgnakn gltllaaalv
      421 vaafaslalr hgheradvrs rg
//
LOCUS       WP_175870437             263 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175870437
VERSION     WP_175870437.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..263
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28924
     Region          13..260
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 metspdqand llfnqslekg lnvlrafsak rrtmtlaeva daagmtkssa qrmvytlekl
       61 gyirkhpvtr ryqltphvmr igfnylaadt lidvanpfls eltnltgett nltepdedem
      121 vyvarfvstk fvpihmpigs ripmyctgsg raflsalppn darvrlddmv rtphtprtvt
      181 alddlvalld sarregyatn qeelfigdms iaapvlgsqg qpvaavhvva ptsrwtfdda
      241 rrklapavid cargisnsir tle
//
LOCUS       WP_175870542             300 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia sp. BCC0397].
ACCESSION   WP_175870542
VERSION     WP_175870542.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..300
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32547
     Region          16..131
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
     Region          166..278
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 mnqepevkeq gatsalhyrr ftaadvpaah alstalrwpf raedwqfsae tsvafaaeed
       61 gvvigtamcw kygadraaig hvivsdahqg rgigrklmem lldelgprit flhatpagrp
      121 lyeklgfnvc gslsqyqgnv erpaavavpd gerlragsla dwprlveldt rasslereal
      181 lsallrrges vvlerdgeiv gfsvlrrfgr gyvvgpvvap rssddaraka ligywltkrd
      241 gefvridvpd gsslpdwlse qglkrvdtcs kmvrnapaae hdgaadptfg lyglvsqaml
//
LOCUS       WP_175870553             286 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia sp. BCC0397].
ACCESSION   WP_175870553
VERSION     WP_175870553.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15202679
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..286
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30514
     Region          12..132
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          165..273
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 msdlnpsrtl iyrpfaetdl paahrlseav kwphrlddwr fafqlgggfv aedesgvvgt
       61 algwrfddah aslgmvivsp erqgcgigre lmtrvvdslg trtvflhatp sgeplyakfg
      121 fdaigtidqh qgaafqppli slppgerlrp lgtndgprla alasratgye rgaviealld
      181 vangialdrd gellgfalfr rfgrghvigp vvapdalraq alishwlaln egmfvrldvp
      241 gdsglsdwlq glglprvdtv vamargatpe pdpalrafai vnqalg
//
LOCUS       WP_175870563             448 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0397].
ACCESSION   WP_175870563
VERSION     WP_175870563.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..448
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48372
     Region          27..437
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(40..41,44..45,48,80,139..140,142..144,147,167,
                     170..171,174,268,271..272,275..277,280,308,312,363..364,
                     368,372,388,391..392,395..396,399)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mpsltqaaaa paaadsseda lyrkvmrril pllllcyvva yldrvnvgfa klqmlddlsl
       61 sdsvyalgas iffwgyflfe mpsnlllhry garfwiarim itwgivsssm afivplaqff
      121 hvqtttmfyt lrfllglcea gffpgvilym nywfparrqs vamsgflvai plsltlgsvl
      181 sgwlmeqthg lsgmsgwqwm llleglpsiv vafivlaclg dgpqsakwls adekavlsrn
      241 leseaahksh sigaalrspr vwlltfillt fntgfyglaf wlpsiiraag vhsplhigvl
      301 taipyltaif amvwnashsr rtgerrlhaa ipaliggvcl ilsaafahnv alsivfltia
      361 tcgilalmpi ywtfpgqils gtaaaagial insvgnlsgf tgsmitgvak qmtgdinngt
      421 yalgacllvs cvlialiprd ilqppagr
//
LOCUS       WP_175870592             269 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175870592
VERSION     WP_175870592.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..269
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28432
     Region          13..258
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 msaapsvrpa giatplldlr iarklygdrt iladialqva rgeivcvvgp sgcgkstllr
       61 ivagldpdfr gsvtldgsal agpsarvgmi fqeprllpwl siadnvgfas garggrdpsv
      121 arlldevgla gvarqlpatl sggmaqraai arglfgepdl llldepfsav daitrmrlqt
      181 llldvvhrhr maaivvthdl dealylgdrv lmlapnpgrv ddeiqvdvar prdrrdpsla
      241 aqrarlldaf qrfhdhaasd tagipvtpa
//
LOCUS       WP_175870598             724 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia sp. BCC0397].
ACCESSION   WP_175870598
VERSION     WP_175870598.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..724
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77575
     Region          11..724
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mwtetgtgrr ataiaaggal cvaaaggaha qasapgaaaa vlpaidvrgp adasaaglvg
       61 rrtatgtktd tpideipqti nlvtaqqiem tgaadlnqal ryvpgfatfg adsrtdwyaa
      121 lrgftptlyv dglpapdtav ianwrvdpyt idsiavlrgp tsvlygagep gaivdahtkl
      181 adgervreag vqigndarkq amldvgdrld pdgktayrfv gvardgnavt gpngnrrval
      241 apsfrwrpna dtsltfsatf lqdsgdissn flpalgtvlp npngrlsqdl ymgdpsfndy
      301 rkkqwslgya lehhvnaiwa lhqdvrwshl slddatvfgn glaprsttnm mrfaglfqln
      361 ysrldidnra qarfgtgple htllvglqfd rqtttnsvrl alapsldlyh pvyrpvtaai
      421 fsgptslghv dqytamngvg vyaqdqirwq rwtltlggre dvvnarfddr aagthaqqdv
      481 safsgrvglt yrgdaglspy vsystsfdpv igvrmfgggl pkptrgaqte aglrweppgr
      541 nlmlnaavyq idqtnvvtpt pvnldptgtt svqtgkvrsr gielsavgkv trelsivasy
      601 ayqdvknvqa ndaslnhwpv svplprqmas lwadwtwhtg tlaglgvggg vryqsasaga
      661 pdnsltvpsa tlydlalhyd lprwrfavnv anlfdrryvs gcqsyavcvf gnertvlasa
      721 kynw
//
LOCUS       WP_175870660             149 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia sp. BCC0397].
ACCESSION   WP_175870660
VERSION     WP_175870660.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 149)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..149
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17026
     Region          3..143
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 mtvtffpvth ddadtlvair iaamrdsler igrfdpqrar drflasfdpa lcrfieaeys
       61 rvgfytlrpm adhwlldhly vvpahqgkgi gaavlreila eadehrmpvr igalrgsdsn
      121 rfyerhgfvr tdeaewdiyy rrepgaatt
//
LOCUS       WP_175870661             412 aa            linear   BCT 11-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175870661
VERSION     WP_175870661.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..412
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=42741
     Region          6..391
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mntknkglsl pmqmfgglvl gvacgvfapg faaklgflst mfghaikmvv mpliflsvtv
       61 gvfragrlre rlgkvalssi gffvfmtgla asfglllnfv frpglgasvt hsgsmpaala
      121 ssidwtkflv dlipanivaa lsagnslpvl vfgvifgaal saaperaepa iavfeallsg
      181 lfkmiqwvia wsplaifaai aqllsakgfa gahslvellg vaylgmavla vvltivirva
      241 gqsplavlrk vkeplilgft trsseitypl hlkklvelgv pygvastilp layifnrdga
      301 vlytalavgy ladayhlvws wplvitilil tiitidgaan vpsgaivait ivltsiglpa
      361 davllllgvd affdmgrtal nvygstaaaa vavrlsgsds maaepvtrqa sv
//
LOCUS       WP_175870677             220 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175870677
VERSION     WP_175870677.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..220
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22877
     Region          117..218
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(120..121,154..155,158,162..163,166,208,212)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mknihlalla svvsltacss asgptynaye lqsrngirtf qvdchgilst aktcmkvatr
       61 mcgnepvrlv dtttpyrdga dphsivfqcg aapapaaaav apapapvekv sltgdayfat
      121 dsavltpaat aaldtllnqq adrhfarvev dgytdatgsd ahnqalskrr anavagylre
      181 hglkadafaa tghgeanpaa sndtaegrar nrrveislqk
//
LOCUS       WP_175870689             236 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175870689
VERSION     WP_175870689.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..236
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25407
     Region          7..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtaaslspvl elrdvsrvye gagrvvavrg atisigprdv valvgpsgsg kstllnlagf
       61 ldvpssgerw legrriddap dtlerirrer igfvfqqfnl ipvmsalenv elgcfawgtp
      121 rtrreraram ldavglaare rhrpgelsgg eqqrvalara lakepaivia deptasldst
      181 naravaelil dtnrtlgtaf liashddrlc ahlprriemr dgvpgvnrel vdvcva
//
LOCUS       WP_175870705             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0397].
ACCESSION   WP_175870705
VERSION     WP_175870705.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..359
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38015
     Region          159..356
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mtkvflilvr nellgylrsr sslfwtlvfp vfllsvmlfa fggsgslgta diafdapgga
       61 tpysraceaq ivaslshsdt vkatfggrga paervtvvlg adertpatir ydfngslavk
      121 aasrvveial arcaaqrlgl paaqarfena aptrrpfdyg affatgilvm afmaiglnst
      181 ttaiaalrer ntfklyvcfp vsrgvflaal ivarmammal salvlltvar vafgialpia
      241 tpdglralpi vllgaamvls igvllasrtr slaaaelacn vtyypllffs dltipmhdap
      301 awlkaglafl ptnqfavalr galvdgapya qlapqllgmt vctalflfaa vrlfrwhda
//
LOCUS       WP_175870714             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175870714
VERSION     WP_175870714.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33676
     Region          23..80
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          111..303
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(124..125,127..128,131,135,137..143,233..238,
                     244..245,247..248)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 misdqngkfe sqsihaslps lmalrcfeaa arhehfsraa delclthgav sravrlledd
       61 lgvalferrs rrvfltdagr tlaqavhdgl glmrhaahal rteaararrs vlsceptllm
      121 rwliprwpdf qarhagvdih laaaggpfsf drgidmairr ndfawpagyh aehlfaermg
      181 pvcrpdkvga wfasrrggrt lkpdaarlht rtrpdawsaw aaaanqpaan grgqqfdhfy
      241 fslqaavagl gvaigpwhlv rddiesgvlv apmgfvedgs dyylltpapv mdgsaqavll
      301 ewlrgmv
//
LOCUS       WP_175870726             315 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia sp. BCC0397].
ACCESSION   WP_175870726
VERSION     WP_175870726.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..315
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32904
     Region          1..261
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mmqteietpg pagplkgtll spaaddvpvv livpgsgptd rngnnpygiq astyrllaeg
       61 lldqgiasvr idkrglygsa saiadaddvt iddyaadvra wvtairtrtg arrvwvlghs
      121 eggwvalsaa rqtadtcgli lvstpgrplg qvlaqqlqsn panaavlgna msilesleag
      181 ktvdatgidp almplfrpqv qrflmselai dpaallagyt kpvlivqgar diqigvqdaq
      241 rlkdaspcar ltivananhv lktvhtaald enlaaysnpd lplangvvea isafvlesta
      301 geldhpalsq rkder
//
LOCUS       WP_175870729             196 aa            linear   BCT 11-JAN-2025
DEFINITION  flavodoxin family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175870729
VERSION     WP_175870729.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..196
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=20726
     Region          9..189
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 miqhnppvkt vvvyhsgygh tqrmaaavad gagavlvaid adgnladdaw ntlasadail
       61 fgsptymggp swqfkkfada sskvwfesgw qnkifggftn sasingdkln tleyffllag
      121 qhggiwvsmd ikpanlkast rddlnrmgay iapmaqtpad aspdemspgd letarrygar
      181 vaaiagqlra gksrge
//
LOCUS       WP_175870775             315 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175870775
VERSION     WP_175870775.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..315
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=34228
     Region          11..>232
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mqhsqqsnvt iegivpvmlt pfddagaidy aglerliewy lahgsdalfa vaqssemqfl
       61 slaeraalar fvvervagrv pvvasghisd dldaqvaelc aaaesgaqgv vlvtnrldpq
      121 rkgsaalldh lhrllarlps dlplglyecp apyrrllsdd elracidtgr fvmlkdvscd
      181 latvkrrval aegsplkiln anaaiawdam kagsagfngv ftnfhpdlyr wlrtqgesnp
      241 aladelstfl vvsavsealg ypalaklyhq rigtfgsikc raidydvrer fwaldavldk
      301 ivagtehfrr riaal
//
LOCUS       WP_175870778             374 aa            linear   BCT 11-JAN-2025
DEFINITION  Fic family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175870778
VERSION     WP_175870778.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..374
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40854
     Region          23..367
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mmsgdytfiw esadwpawrf dlpalatpla dvsraqgmla grladiglal rdeaslaalt
       61 edvvktsaie genlnvasvr ssiarrlgvd igalapvdrh vegvvdmvld atthsaapvt
      121 earlfgwhaa lfptgysgls ritvggwrsd asgpmqvvsg pigrqrvhfe appaarlthe
      181 igrflawlna apaepllira glahlwfvtl hpfddgngri aralgdlvla radrspqrfy
      241 slsaqiqrer nayydvlert qrgsldvtew lawflntlgr aidhahttld avlikarfwq
      301 rcagvamner qvkvmnrlld gfegkltttk waalakcsqd talrditelv eqgmlrrsas
      361 ggrstsyelv pfdg
//
LOCUS       WP_175870834             707 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175870834
VERSION     WP_175870834.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..707
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76997
     Region          9..691
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mtypslrdwl fsgktfaasm lalylglyfq lprpywamas vyivsnpfvg atrskalyra
       61 lgtalgaaaa iffvppfvet pllfsiivat wcgtllylai sdrtarsyvf mlagytmplv
      121 alptvtdpst ifdvaiarte eivlgivcas vvgsavfpnr laptliertd awfkdaafyg
      181 retlsghiag kalsacrqrl aatitglefl lsqlgydhah prilartqal agrmqlflpl
      241 mssladplia lmrdlhvrpp aldalladaa kwfdaplpav ktgsdgdmah dpvaddlrar
      301 iaalqppdsa laswdgalls nalwrlrqvi diwqdcrslr alianesgvw qpryrhwrlg
      361 gterffdrgm mlfstltvvf aivfacwlwi ssgwhdgaaa vtlvavscsf faaldepapl
      421 vfkfflstaa svvfaglylf vvlphvhdfa mlvlmfagpf iligtllprp qfnmvtmlva
      481 vntatfisiq sayeadffvf lnsnlagvag llfayvwtra trpfgaelav rrllrsgwed
      541 varsastqpl ddqrnhasrm ldrvtqllpr lgasddhrhp siesfrdlri alnaldlrrs
      601 rrrlsgdvpd aidrvlagvt dhytrcaaan arqpvppall atiddalrrv agrnlpgaap
      661 adgaaapaap athrrlrdtl halvglrlsl ypaaaaqapq apdgara
//
LOCUS       WP_175870845             374 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia sp. BCC0397].
ACCESSION   WP_175870845
VERSION     WP_175870845.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..374
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41733
     Region          87..327
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 masplvlihr mlgfaaarrg qtlsgsspqh ngerfanvap rpaeglgktl giawnmlvnk
       61 prhtvpagal pvdsltrael daapdrslyr lghstlllkl rgefwltdpv faeraspfrr
      121 igpkrfhapp itledlpplr gvilshdhyd hldrdtvlal aattgvfvtt lgvgdrliew
      181 gidankvrql dwwqsmdvag ltltatpaqh fsgrslfdgn stlwaswviv dddlrlffsg
      241 dtgyfdgfre igerlgpfdv tlietgayda qwpyvhmqpe etvqahidlr grwlipihng
      301 tfdlamhrwq epfervtala lvrgielstp rmgerldlga phrgerwwrt vneraaapaa
      361 ksrrwqlcas qatk
//
LOCUS       WP_175870858             451 aa            linear   BCT 11-JAN-2025
DEFINITION  uracil-xanthine permease family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175870858
VERSION     WP_175870858.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..451
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45865
     Region          9..423
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mshdpisppv darlpawqla lfglqhvlsm aaspitavfl iakmlalpad ltvqligatf
       61 facgigtllq slgagpigar mpfvmvpgga ptmlfagiaa qsglptaaga allasafywv
      121 llpvftrclr lfprivvgam lllvsinlir iyativvgqp gsadfaqpra lglalativa
      181 tvvvagafrg tagrlavlig lmagatlgwa lgampaladv whgplfthpv wlpfgmprfd
      241 vlaalpllif taismaeata qtvavgetcg kaislrrdvp ktirgdalas lagalfgtpl
      301 ivtsaenigv vqttgvrsry vtaaagaili vialfaplar layaipaavv ggtalvvfam
      361 igvmgirlla svdlharanq ytlaaalvvg lapilvpnly rhfgapvqiv lgngmaagtl
      421 aaiatqlafa alarlsrqah agaaaapsrd a
//
LOCUS       WP_175870872             399 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid aminotransferase [Burkholderia sp. BCC0397].
ACCESSION   WP_175870872
VERSION     WP_175870872.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Alexander,F.W., Sandmeier,E., Mehta,P.K. and Christen,P.
  TITLE     Evolutionary relationships among pyridoxal-5'-phosphate-dependent
            enzymes. Regio-specific alpha, beta and gamma families
  JOURNAL   Eur J Biochem 219 (3), 953-960 (1994)
   PUBMED   8112347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..399
                     /product="amino acid aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42484
     Region          3..388
                     /region_name="PRK09257"
                     /note="aromatic amino acid transaminase"
                     /db_xref="CDD:181731"
     Site            order(107,142,209,254..256,292,295)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mslfsavqla prdpilglne afnadarptk vnlgvgvytn edgkipllra vrdaekarve
       61 aglprgylpi dgiaaydaav qklllgddsp liaagrvvta qalggtgalk igadflrtvn
      121 pnvkvaisdp swenhralfe aagfevvayp yydaathgvn fegmlsalns yaagtvvvlh
      181 acchnptgvd lteaqwqqvv dvvkarnlvp fldmayqgfg enieadaaav rlfaaadlna
      241 fvsssfsksf slygervgal siitsskeea trvlsqlkrv irtnysnppt hggavvaavl
      301 aspelhaswv qelgemrdri ramrnglver lkasgvdrdf sfinaqrgmf sysgltsaqv
      361 drlrdefgiy avgtgricva alntrnldav aqavaavlk
//
LOCUS       WP_175870886             835 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175870886
VERSION     WP_175870886.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..835
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=90703
     Region          16..789
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 magesllkvl rggyaqfdri vkldtplgdd wltplyvkin arlgrnfevt vdassvmgdk
       61 iklnalmlqp vtlwirqtdg gylpihgyvq rarrlgndgt vsyfqlqfss wlsflklssd
      121 rrdwqeasgw qiltdvfdkh pqassnygqe lraamrsysh rvqwetdwnf vhrsleevga
      181 fprfdfakdg kshkvvmmdd lyfgpslpns emkfshagtd edfdgltqls eqqdaqsatl
      241 tlgtadykrp dldkqastpa adldelpgqg edylytgsqt waesdagqqq arirteewas
      301 rakryfaigs pryalpgywf kvsghplfdt lpeeerelsi iasdwliqnn lpgidaltrf
      361 prslrseieq vkaagtgttv shrdggigff hveieaqrrk tpfrspfehe kpemhlqtai
      421 vvtdsdeeiv tddgnrvrvr tsnsrngrnt kstswiraam pdagskrggy fplrkddqvl
      481 lgfvngdcdr pviisrlhgg atmpvwhthg llsgfrsrey ggdgfnqlvm ddatgqnrvh
      541 lysssysshl hlgylieqsd ntrgsflgng fdlksgayga vraeqglyvs tqpataqpln
      601 vtaatdplag aeavletvsk asetnraesl qdgqtalksf tdatqrtvag sasggrtagg
      661 gtgnangfak pvmllsspdg iaastqqsvh vtanqhanvv agknvnlaag kallvsvldk
      721 islfaqnlgi kifaakgpvd iqaqsgsasl vglqdvkies adgrliltaa kevwigaggs
      781 yisikgglie nvttgqilek cgnwdkssga sgmirdplqa tpvstdggrg slfsg
//
LOCUS       WP_175870910             270 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia sp. BCC0397].
ACCESSION   WP_175870910
VERSION     WP_175870910.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..270
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=28040
     Region          9..247
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mrarpivavt adrilrgahp nhtagekyva avvdgagala fvlpafgarq padaivaaid
       61 gllltgsysn vephhyggaa sapdtlhdpa rdatalplir aaidagvpvl aicrgmqeln
      121 vayggtlyqr lhatagfddh rerpgdpler qygpahvvqf apggllqrva rgaheatvns
      181 lhdqgiarlg aglaieasap dglveavsvr garafalgvq whpewryaeq plsrdifaaf
      241 gaacrahmth rihaaggatp spaasdidid
//
LOCUS       WP_175870915             464 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0397].
ACCESSION   WP_175870915
VERSION     WP_175870915.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..464
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49124
     Region          16..419
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(28..29,32..33,36,76,134..135,137..139,142,162,
                     165..166,169,251,254..255,258..259,262,290,294,346..347,
                     351,355,371,374..375,378..379,382)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msrpqsppaa qprpgraala afvgttiewy dfyiygtaaa lvfgkvffss tmdpgvatll
       61 afvtfwagfa arplggivfg hlgdrvgrkt alvitlvmmg lattgigllp gyasigvwap
      121 vglvvlrvlq giavggewgg avliasenap khrsilyaaf aqqgsptgnl lataaffals
      181 alptpsflmw gwripfllsa vlviigmvir lrleesvdmq rvlarkrtvk lplrdvvrdh
      241 wvvvllaagt lpvinvtyfr stfalswatk tlgyaqgtfl gilsislvvq flmqpvgawf
      301 vskvdmrram cwilipeivl mpvmfhalat rsywvavagm cistipsamf ygavggvlar
      361 vfpanirytg lslayqlsal vvgggtpvla qailnetgsi vgvaiasgly alvslvcmla
      421 llnrtgyrad elstaersda aewgtegaga gappdergtl kpvg
//
LOCUS       WP_175870912             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175870912
VERSION     WP_175870912.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33001
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..284
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 melrqlryfv avaeelhfgr aakrlfisqp alsfdirkfe dalgvqlfsr tnktvaltna
       61 gevllgearr lllqaveaer ltvrsasgla grlrigfvhs mlyrglpdav rrfeadypgv
      121 evvlsemnth aqvqaiqrgq idlgyahwgh fppevesvpv yaepfvcclp aahplarrtq
      181 valaalatep filfprdaap hyhdliiaqc vnagfsplir hearlwqtil smiefgmgia
      241 lvprvlqqak sdrlaflalk daslesrtla lkrsgtaepv alrfagyvra sidalpaltg
//
LOCUS       WP_175870925             695 aa            linear   BCT 11-JAN-2025
DEFINITION  M3 family metallopeptidase [Burkholderia sp. BCC0397].
ACCESSION   WP_175870925
VERSION     WP_175870925.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..695
                     /product="M3 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=76868
     Region          4..693
                     /region_name="Dcp"
                     /note="Zn-dependent oligopeptidase, M3 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0339"
                     /db_xref="CDD:440108"
ORIGIN      
        1 msasantnpl ldfsglprfg eirpehvtpa ldtlldtasr avetasaset pstwaavvet
       61 veqateplgr awgivghlna vadtpelraa ygenlprvte fwssvgqnla lyekykaiaa
      121 saeyatlsde rkkildnalr dfrlsgaelp edqkprfael qeqqaalska fsdhvldatn
      181 ayayfakgea elaglpgdai eaareaaqkd gkegwkftlh fpsyfpvlqy adnralretl
      241 yrayatrase lgpqygdgka ewdntaivad alklrreeaq mlgyrnfaev slapkmaesp
      301 qqviafledl atrarphadk dwdelrtfaa kelglaelap wdvayaaekl rqqryafsen
      361 evkqyfpepa alkglftvte tlfgvrikpd dapvwhkdvr ffrvenrdgs lvaqfyldly
      421 aregkrggaw mddarsrakr gsdvqtpvay ltcnfsapvg gkpacfthde vitlfhefgh
      481 glhhmltrvd elgvsgingv ewdavelpsq fmenfcwewd vlssmsshvd tgaalprelf
      541 dkmiaaknfq sglgtlrqiv fsmfdmllhv dfdpagatgv tafareiner yhvipqaafs
      601 rwpntfshif aggyaagyys ykwaevlsad ayaafeeaaa asgsvldaat gtryrreile
      661 vggsrpames fkafrgrepq idallrhngm aapah
//
LOCUS       WP_175870917             324 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175870917
VERSION     WP_175870917.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..324
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37538
     Region          134..275
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mlhlidafvs diqtwlyvdv vqpllfkfnl mdydedtyda lywviigalq mvlmfallrp
       61 leallpierw knrravrvdv iytaisklgi ytlffffalq pvfdnfqawl rlhgvanvnl
      121 dylwpgvtsq pivafaiylv vldfagywyh rwqhkfgiww elhavhhsqr qmslwcddrn
      181 hllddvlqsc ffaaialvig vtpsqfvvlt avtnfmqsiq htnarlpfgr igerllvspi
      241 fhrrhhavgy ghegtkygcn fgvlfpwwdm mfgtaswnrt veptgireqv egvsygdgfw
      301 sqhglafvri frrlfpakrg aasa
//
LOCUS       WP_175870970             305 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175870970
VERSION     WP_175870970.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..305
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31764
     Region          38..290
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mssprlsrrh ftiacasasl aactsfgdks rsgtalpqek pvkigialgg gaargfshig
       61 vlkaleargi pieivagtsa gsvvgalyas gmsalqinki aldmdqasis dwalpfrsrg
      121 llqgvalqnf lnktlnnrpi ekmakplgiv atdlqsgqpi lfqqgntgla vrascsvpsv
      181 fepvkignre yvdgglvspv pasfarkmga sfviavdisa rpdgaatnnp iemllqtfti
      241 mgqtiktyel dkyadvvirp nlaamggsdf nqrnaailag eeavarimpe lqrklaaarg
      301 vatta
//
LOCUS       WP_175870969             540 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175870969
VERSION     WP_175870969.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 540)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..540
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59008
     Region          9..537
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msdavvskad epllslehlh vrfgdtvavd dvtlaigrge rvalvgesgs gksvtalsil
       61 rllhdaevgg airfagqdlm gkseremrgl rgsdiamifq epmtalnply tigvqigeti
      121 vlhdgvsave arkrtialla rtgiaeperr vdsyphqlsg gqrqramiam alacrprlll
      181 adepttaldv tiraqivdll lelqrdeaek rgmsillith dlnlvrhfae rvavmehgrl
      241 vesgpverif aapehpytqr llnsrpqrtv tpvmpiapvv ldarhvsvqf arkrpgfagw
      301 fgtvpvtava dvsvsvrqge tlgivgesgs gkstlamall glqktaggei efqgralsty
      361 rgreqtalrs nmqvvfqdpf sslsprhtie rivgeglelh rpdmtpdarr akslavlrev
      421 gldrtvlhry phefsggqrq riaiaralvl eprilildep tsaldvsiqq qvlkllanlq
      481 qkynlgyvfi shdlevigam ahrvavmqdg avvesgevse ifarpshpyt qkllkavwka
//
LOCUS       WP_175870975             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175870975
VERSION     WP_175870975.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32675
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrfkqietf aavaakgsls aaahaegvap aiigrrldal eerlgvkllv rttrkltltf
       61 egsafledcl riindmqnae asvsaggvka sghlrisapa gfgrrhvapl vpefsgahpd
      121 vsvtldlsdr mvdlvnegfd cavrlgelpd sslvslklge nrrvcvaspa ylarrgtpat
      181 laelarhncl alaananqqr gwafleddkv vsirvngtme csdgavlhew clegyglawr
      241 swwevgedia agrlvsvlda faappigiha vfpqrrhlpl rvrlfldylk htyerpgywg
      301 e
//
LOCUS       WP_175871069             363 aa            linear   BCT 11-JAN-2025
DEFINITION  C40 family peptidase [Burkholderia sp. BCC0397].
ACCESSION   WP_175871069
VERSION     WP_175871069.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..363
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37519
     Region          <7..176
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mlriwvpvav vsllaacssv ppqsasrsas gmkittpraf pppanfpkfv dhsvgqeeis
       61 iqamslvgvp yrwggntpts gfdcsglvry vigraadvnl prttadmsgr gvsvepdeia
      121 pgdliffntt grphshvgiy vgklrfvnap stggtvrldy ltnpywakrf dgirrvappr
      181 saptpfdapt yeakrdeprn ppavaaapvv vtaaaaprqp ayapsqarat rapapatltt
      241 pvvtaaavap aapaadpyep ppprmqaaqq qatsvadamp attanaapaa paevgtqipt
      301 taltaaqaaa fdaepppata stpprsiepa pvqvwraatq sapvsprtst addpiarfan
      361 gsy
//
LOCUS       WP_175871060             236 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175871060
VERSION     WP_175871060.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..236
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=24372
     Region          7..230
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          101..130
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(102,106..107,110..112,114..115,119,122,132,136..137,
                     140..142,144..145,149,152,161,163,165,169..170,173..175,
                     177..178,182,185,194)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          131..161
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          163..194
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mtkptnhlpk ralvaaafva sglfaaagaq aesldaivka vkfddiadig kqlksgkldp
       61 ntlapngdpi lviaareksd kvaaaiattp nvdlekedka genalmlasl ngdldlvkll
      121 idkgaevgkk gwaplhyaat ngqdavvkvl ldhdayidta spngttplmm aargnhastv
      181 tllldqgadp qvknqlgita lefakhynap daigilskrt trigaatpad aqksak
//
LOCUS       WP_175871104             749 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Burkholderia sp. BCC0397].
ACCESSION   WP_175871104
VERSION     WP_175871104.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..749
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=81434
     Region          43..744
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mnspleatpd arrdttsagr vrapegtfel srkrvdeldt ifgeggllar aldgyrprts
       61 qiemaravas ameasarrmp epeifetrkr parrlgdgdq aagpaaddav vtesdsdagd
      121 ntliveagtg tgktyaylvp amlwggkviv stgtkhlqdq lfqrdiptvr nalavpvtva
      181 mlkgrsnylc hyylqrtadn grlpsrqdta ylqeivrfvk ltksgdkael asvpenapvw
      241 smvtstrdnc lgqecphyke cfvmqarrea qqadvvvvnh hlffadimlr dtgmaellpn
      301 antiifdeah qlpetatlff getlsttqil elardtvaeg lshardavew vklggdlera
      361 ardlrlafan dqivrmslaq lgddhpmfga ldaldaalda lasalasqae raeslgaclr
      421 rarelqdlla gwvapgaaea aakadaaaag dkaasdgdpn ekvrwvevfa htvqlhetpl
      481 svapifakqr agvprawvft satlsvrgdf thyaaqmgls srrsmtlasp fdyqsqglly
      541 vprnlpqpss paftdavfda alpaieasgg gvfmlcttlr avdriasklr dviesrgwnt
      601 pllvqgdasr telldrfray gnailvgsqs fwegvdvrgd alslvvidkl pfappddpvl
      661 aarldaltkk glspfavhql pqavitlkqg agrliraetd rgvlmicdtr lvdkpygrri
      721 wqslppfkrt reiavvqdff derrsdkga
//
LOCUS       WP_175871129             154 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia sp. BCC0397].
ACCESSION   WP_175871129
VERSION     WP_175871129.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..154
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17207
     Region          15..128
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mtsqdvrfti cavraeetyp lraavlmagd eegsalhgdh apttmhfavr dnenivavas
       61 vckeeqsgvs naeawrlrgm avhpsvrglg fgrllvnlsl rhvreqhgtl lwctaresay
      121 qfyemlgfdr dpipismhgr ddmkfylmqr kieg
//
LOCUS       WP_175871211             208 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175871211
VERSION     WP_175871211.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..208
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22673
     Region          15..169
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mtdsthhyye psqghglphd plnaivgprp igwissrgsd gtlnlapysf fnafnyrppi
       61 igfsstaakd svrnvqetge fvwnlatrdl aermnqtcaa vpydvnefel ggltavssrl
      121 vnvprvaesg vnfeckvtdv irlrdhrgve tpatlvlgev iavhirhdll kdgifdtfga
      181 giilraggps ayvhvkpdsr fdifrpda
//
LOCUS       WP_175871217             296 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0397].
ACCESSION   WP_175871217
VERSION     WP_175871217.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 296)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..296
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31150
     Region          34..259
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mqslsgssap spapapaplh akraarhapr vagaraiaal qwgvtmllca flivpvvmsv
       61 lagltvnyfr glssgltlrw leqvwqqyhg svalslyvaf atlavgvpag yalarsksrl
      121 araieealvl pvalpglasa lallvvyggf tafrmslwfi vvghvvftlp fmvravaava
      181 agadlrtlee gaaslgasfv trfvtivlpn lrpgivagal avltlsigef nltwmlhtpd
      241 tktlpvglad tyaslrlevg saytilfllm tlpllvamqw lgvdpsgtra lkkrpr
//
LOCUS       WP_175871254             346 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175871254
VERSION     WP_175871254.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..346
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38166
     Region          15..323
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mvpvsrpaga trttqvaiva lppvsmsgvg pivdalnlan eidgrllyrw qvcswdgrpv
       61 plaggaqwha daafndaiac dwlivvserf qqfadyrlfl aslarvgqrt pvvtgihhgv
      121 wwlamagqls gyrvsvnwet yqqfaeqfer sivtqqifei drdratcagg qatvdfmlam
      181 igrehgvdla eriadalgag tlrsgeerqr ipfvtapger hprlndalll meanvedplt
      241 tdeiaglvgv srrqlerlfr qylgampsky ylnlrllkar tqlqrtsksv vqvslacgfs
      301 saahfsnayr erfgvtpred rrawlekqtg ggseprggal vergkd
//
LOCUS       WP_175871005             196 aa            linear   BCT 11-JAN-2025
DEFINITION  2'-5' RNA ligase family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175871005
VERSION     WP_175871005.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Remus,B.S., Jacewicz,A. and Shuman,S.
  TITLE     Structure and mechanism of E. coli RNA 2',3'-cyclic
            phosphodiesterase
  JOURNAL   RNA 20 (11), 1697-1705 (2014)
   PUBMED   25239919
  REMARK    Erratum:[RNA. 2014 Dec;20(12):2011]
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Arn,E.A. and Abelson,J.N.
  TITLE     The 2'-5' RNA ligase of Escherichia coli. Purification, cloning,
            and genomic disruption
  JOURNAL   J Biol Chem 271 (49), 31145-31153 (1996)
   PUBMED   8940112
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..196
                     /product="2'-5' RNA ligase family protein"
                     /EC_number="3.1.4.58"
                     /GO_function="GO:0004113 - 2',3'-cyclic-nucleotide
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0008664 - RNA 2',3'-cyclic
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=21469
     Region          18..190
                     /region_name="ThpR"
                     /note="RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA
                     ligase) [Translation, ribosomal structure and biogenesis];
                     COG1514"
                     /db_xref="CDD:441123"
ORIGIN      
        1 mtqltlpgfd apppvplhrf ffavmpdpaa agriagmaks mrletdslvg terlhitlgs
       61 lgdfayvpda tlalaravad rvdvpsfsvr fdkiisfngr pghqplvlmg ragledlidf
      121 rrqlrralkq eaglsilpas ftphvtllyg aqrpdeyrie pitwtvfdfv lvdswlgksh
      181 ydvlgrwplt tgspsg
//
LOCUS       WP_175871317             303 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia sp. BCC0397].
ACCESSION   WP_175871317
VERSION     WP_175871317.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..303
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31717
     Region          46..284
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
ORIGIN      
        1 msatttpaaa patpagsapa phmgrlrtad glelasyrwp aadgtappra tialvhglae
       61 hagryaalag rlnaagidvl aidlrghgqs pgkrvwverf dgylndadal vaeaargdap
      121 lflmghsmgg avaalyaier aaarghaltg lvlsspalap grdvprwmla vsrvisrvwp
      181 tfpairidaa llsrdpaiva anradplvhh davpartgae ildamarign grgalrvpvl
      241 vyhgtedklt epdgsrafga rvgspdrtlt lyeggfhetm ndlerdrvid aliawiharv
      301 par
//
LOCUS       WP_175871338             226 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175871338
VERSION     WP_175871338.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..226
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24669
     Region          10..225
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mstltdvtrd rpgasaasla drayaliqrd iitmrlkpga alneadlvar tgigrtpvhq
       61 avhrlvlegl lsvmprkglm vqplslddiv avidvrrine ahcaelaarh atpddlahla
      121 allddgqacv dthdvegmme ldrafhqtia aaarnavlad ilralhersl rfwfvtlsep
      181 hhladvqheh ralfdrlsar daagaraave shidsfrstl lqhlrp
//
LOCUS       WP_175871396             226 aa            linear   BCT 11-JAN-2025
DEFINITION  urease accessory protein UreF [Burkholderia sp. BCC0397].
ACCESSION   WP_175871396
VERSION     WP_175871396.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Soriano,A. and Hausinger,R.P.
  TITLE     GTP-dependent activation of urease apoprotein in complex with the
            UreD, UreF, and UreG accessory proteins
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11140-11144 (1999)
   PUBMED   10500143
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Moncrief,M.B. and Hausinger,R.P.
  TITLE     Purification and activation properties of UreD-UreF-urease
            apoprotein complexes
  JOURNAL   J Bacteriol 178 (18), 5417-5421 (1996)
   PUBMED   8808930
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..226
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23954
     Region          1..226
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 mtttelvall hlaspalpig aysysqglea aldanlirda dsardwiasg ltdvlahgel
       61 pflahqlarw qthdthalaa enawfvasre saelrreteq mgwslaqlca slewgdaarr
      121 atlaslspva lptafayaaa ahdasadatl aayafgwven qtsaalkavp lgqlagqril
      181 valrgaidaa vrralatppd svntfapqlg ilsarhetqy srlfrs
//
LOCUS       WP_175871452             327 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175871452
VERSION     WP_175871452.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..327
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35211
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,161,163,226,243,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,190,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mnqiqtvrvf vcvaeqqsfr raahhlgvsn alvtrsiaml eghlntrlih rttrnlslte
       61 agvryldgcr alleefdhle ssvahavrep agtlrvvasg llsplaltpl vssfrqrype
      121 lrvqltvaeg pldvldsgyd vgivtgtrld gspslighal apnpfvacaa payldrrgep
      181 rvpddlpghd wvtlaphqha ptwqlvghdg vahsvtvrpa ctvnqlalvq aaavagagia
      241 vlpepcvada lnhgtlvrlm agyriddpda qlslvypnrq yvpartrsfv ehalehfsap
      301 agreradygf lrpvrgpdha divtglq
//
LOCUS       WP_175871602             468 aa            linear   BCT 11-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Burkholderia sp. BCC0397].
ACCESSION   WP_175871602
VERSION     WP_175871602.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..468
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=47993
     Region          2..458
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mtmlslgeaa rlipgatvrg dagvtfdrvs tdsrtagpgd lfvalkgerf dahdflgdva
       61 argaaaalva hapagvalpm ieggetraal galahgwrkr fplplvavtg sngkttvkem
      121 iasifaaavg tdarlatagn lnndvglplt llrlsaahrl avieigmnhp getdvlarlt
      181 aptvalvnna qrehqefmat veavalehaa vihalppdgv avfpaddaya giwrvaatgn
      241 rildfalhda erqnaaqvvg rvhggelaid tpvgavtvrl ralgehnarn alaataaalg
      301 agvalsairq glesfepvkg rlqvkqasvg slagatvvdd tynanpdsmr aaidvlaahp
      361 aprvlvigdm gevgdegpaf hreigayare rgidalfalg dasrdactay gdtarhfddv
      421 galvaallaa gygaqatvlv kgsrymkmer vvdaltnqpa agtvpaah
//
LOCUS       WP_175871643             252 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175871643
VERSION     WP_175871643.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..252
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27098
     Region          1..245
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mirleridks fgahrvlsgi dlalqpggvt aligpsgsgk stllrcvnll evpetgtltv
       61 gearidfvpg rrpsrdevfa vrkqtgmvfq nfqlfphlsv vqnvmeglvt vqrwpreqar
      121 qralalldkv giadkadawp atlsggqqqr vaiaralaps pqvllcdept saldpelsve
      181 vvevlrqlar egttmlmath dlrlaasiah davfladgri veagasrdlf grprdprtak
      241 fvatlaqgvp af
//
LOCUS       WP_175871683             546 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia sp. BCC0397].
ACCESSION   WP_175871683
VERSION     WP_175871683.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..546
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58399
     Region          1..533
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mqydyiivgg gsggsslagr ladacpdati alieagshte rnllvnmpvg iaalvpfklg
       61 tnygyetvpq pglggrrgyq prgrgmggss ainamiytrg hpgdydewaq lgatgwgwqd
      121 vlpyfrraeg nergadawhg adgplsvsdl rfrnpfserf iqaahaagyp lnddfngatq
      181 egvgfyqvth rdgsrcsvar ayiygrnrpn lhvvpdatvl rvgfdgkrav gvvasrngrv
      241 etlgaraevi lsagafnspq llmcsgigpa eqlrrhgiav vqdapdvgtn lidhidfiin
      301 trvnsselvg vclrgiakmt palaryfssr tgmmtsnvae aggfiksdps lerpdlqlhf
      361 ctalvddhnr kmhwgfgysl hvcalrpfsr gtvalasgda rdaplidprf fsdsrdldll
      421 vrgtqamrri lsqaplasqg grelytrpdq seaelrativ ehadtiyhpv gtcrmgadar
      481 avvdpqlrvr gvdglrvvda svmptliggn tnapsvmige raadfivaar rggvprgeaa
      541 aavhgr
//
LOCUS       WP_175871696             348 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175871696
VERSION     WP_175871696.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..348
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37321
     Region          5..319
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtqnlltirn lavnfnglpa vdrinlsvap gevvgvvges gsgksvtmma lmglidapgk
       61 vtadevtfng vdllkaspka rrkivgkdia mvfqdaltsl npsytvgyqi kevlklhegl
      121 rgdalhrral elldqvgipd aknriasfph qmsggmnqrv miamavacnp klliadeptt
      181 aldvtiqaqi mdllvklqke rgmalvlish dlavvsevah rvavmyagei ietnrvpdif
      241 raphhpytea llaaipehnq garrlaalpg mvpgrddrps gclfaprcky vvddcrkarp
      301 aldtlvsgnd amrarcikpl nvsnldltal hgtgvsakaq tpvdrssr
//
LOCUS       WP_175871722             224 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF799 domain-containing protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175871722
VERSION     WP_175871722.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..224
                     /product="DUF799 domain-containing protein"
                     /calculated_mol_wt=23499
     Region          7..224
                     /region_name="COG4380"
                     /note="Uncharacterized conserved protein, DUF799 domain
                     [Function unknown]"
                     /db_xref="CDD:443506"
ORIGIN      
        1 mfktlsfkll svlsiaalls acaqpvqrpd ytafkksqpr silvlppvne ttdvgatygv
       61 lsqmtlplae sgyyvvpvav mdetfkqngl tnatdiqats paklreifga daalyskvtq
      121 ygsvyqlvds ttivsasakl vdlksgdvlw qgegratgke ignnmsvnaf gvvgalvqaa
      181 vkqvahsltd eahdvaglts trllsagppn gllygprspk ygtd
//
LOCUS       WP_175871752             212 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175871752
VERSION     WP_175871752.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..212
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23166
     Region          4..195
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mnayrlylsp gacslaahia leetgapfdv eivsvrqqqn learylainp karvpvlaip
       61 geprvltetp ailtylarry pdaqllplgd plrearchew lawlvgwvhg vgygalwrpg
      121 rfiddpalhg aisahgrgti daanasieta ladgrrwaep gahsivdpfl lvlyrwgvai
      181 gldmtrhpaw tahaqreaer paarralare av
//
LOCUS       WP_175871786             408 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175871786
VERSION     WP_175871786.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..408
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43965
     Region          1..291
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mrlalvlmgg garaayqvgv lkalaeiare adpqrntlpf avvcgssaga inatsiasha
       61 ddfshgvrrl lefweplrad yvyrtdwlgi agagarwlat mtfgwaarrs prglldntpl
      121 ahllqrelsf hrieqmlear qlhalaital syssgrhltf yqaaepiqaw rraqrtarlv
      181 dlsashllas saipfvfpav plvldgqiey fgdgsirqia plspaihfga hrivvvgaad
      241 prpeipaang agrprgyptl aqigqqvlas vfldsigsdi eriehinrmi ehlphqievd
      301 sgwrhvdvla iapserieli aakhlkqmpa tmrgllgaig gsqpagasfa syllfeeaft
      361 celielgyrd graqretlag wiahadgssa paagtppedg latgemrv
//
LOCUS       WP_175871804             381 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175871804
VERSION     WP_175871804.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..381
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40649
     Region          1..376
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfqhtedrr mladtlnrfi aeqyafpvrd riaqsaegfd ramwqrfael gtvgalfsea
       61 dggfggagfd iavvfeclgr glvvepflga llagralala ggdahrdrla alidgsasaa
      121 fahdepgshy elttvrtrae rsgdgwvltg akgvvdqaaq aaffvvsarv sghdddpagi
      181 glfvvpvdap gvslrdyrki dggraaevrf drvalpadaa lgapdaldge agaellervl
      241 gygllalsae algamdvake htldylrtrk qfglpigsfq alqhrmadll leveqarsav
      301 inaaaqldap ravreralaa akysigrigt lvaeesiqlh ggigmtwelp lshyakrlvm
      361 idhqlgdedh hlaryialsk q
//
LOCUS       WP_175871866             265 aa            linear   BCT 11-JAN-2025
DEFINITION  (Fe-S)-binding protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175871866
VERSION     WP_175871866.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..265
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28163
     Region          <9..255
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mnprpyptap ahvylfatcl vdlfvpeagl dtvrllereg ltvhyprgqs ccgqpayssg
       61 npdearrvaa aqldlfaqpw pvivpsgsca gmirhhwpal faddpvhgpk ahaiaertye
      121 laeflvhvld vqldavmada gpdervvlht scaarremgt rvhgvalvda lpgvtriehe
      181 reseccgfgg tfslkhpdis gamvrdkvas acatgcdrlv sadcgcllni ghaatkagaa
      241 lpvehlasfl wrrtagagsl rgdsq
//
LOCUS       WP_175871343             190 aa            linear   BCT 11-JAN-2025
DEFINITION  TMEM165/GDT1 family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175871343
VERSION     WP_175871343.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Thines,L., Stribny,J. and Morsomme,P.
  TITLE     From the Uncharacterized Protein Family 0016 to the GDT1 family:
            Molecular insights into a newly-characterized family of cation
            secondary transporters
  JOURNAL   Microb Cell 7 (8), 202-214 (2020)
   PUBMED   32743000
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Demaegd,D., Colinet,A.S., Deschamps,A. and Morsomme,P.
  TITLE     Molecular evolution of a novel family of putative calcium
            transporters
  JOURNAL   PLoS One 9 (6), e100851 (2014)
   PUBMED   24955841
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Demaegd,D., Foulquier,F., Colinet,A.S., Gremillon,L., Legrand,D.,
            Mariot,P., Peiter,E., Van Schaftingen,E., Matthijs,G. and
            Morsomme,P.
  TITLE     Newly characterized Golgi-localized family of proteins is involved
            in calcium and pH homeostasis in yeast and human cells
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 6859-6864 (2013)
   PUBMED   23569283
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..190
                     /product="TMEM165/GDT1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=19846
     Region          1..189
                     /region_name="Gdt1"
                     /note="Putative Ca2+/H+ antiporter, TMEM165/GDT1 family
                     [General function prediction only]; COG2119"
                     /db_xref="CDD:441722"
ORIGIN      
        1 msqaflistg avalaeigdk tqllslvlaa ryrkpvpiil gvlvatlvnh gfagalgewl
       61 gvlvtpsimr wtlalsfiam glwilvpdkl dedeanatrs rlgvfgatlv afflaemgdk
      121 tqiatvalaa rfqdyigvva gttigmmlan vpaillgdrf ahrlptklvh giaavlfvvl
      181 galallgigv
//
LOCUS       WP_175871871             531 aa            linear   BCT 11-JAN-2025
DEFINITION  MDR family MFS transporter [Burkholderia sp. BCC0397].
ACCESSION   WP_175871871
VERSION     WP_175871871.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..531
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56591
     Region          33..425
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(34..35,38..39,42,73,123..124,126..128,131,152,
                     155..156,159,285,288..289,292..294,297,325,329,382..383,
                     387,391,407,410..411,414..415,418)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mavhtaahhs sgqvlpfres llamiglsfv tmlvaldqtv vgtalptiva elrgfdlyaw
       61 vatsyllssv itvpifgrlg dyygrkpfvi asivvftgas vlcgmandml tlvlarglqg
      121 igggmlvgta facipdlfpd svvrlrwqvl mssafgiana vgpslggvlt qsfgwrsvfy
      181 vnlpvgllsl lfvwrylphl rhvehdrkmr ldwpgallia lslgalqlfv ewlpkygvas
      241 waslllvvav aagvglwhwe krcaqpilpf dmfgnralsa lfvlailagf smfsllfyap
      301 llfqggfgms pkeaglvitp lvvfitigsi mngrvvtrir npnamlhvgf vlfavacagi
      361 vvathttptw mlmalmvagg iglgfvlpnl tvfaqqtagr ehlgiatall qslrmvggml
      421 gtaltgtlvn qmysggvrna lsadqamqwh arladpqili draaqgglva eltraghnga
      481 llleaaresl vgaihlgvam aavvavvsvw qcrrvppial rrkiephvaa d
//
LOCUS       WP_175871904             491 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia sp. BCC0397].
ACCESSION   WP_175871904
VERSION     WP_175871904.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..491
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52448
     Region          1..388
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfeslglae plvkavnelg ytsptpiqqq aipavlgggd llagaqtgtg ktagftlpil
       61 qrlhtfyteq rgakravral iltptrelaa qveesvrays kyvklrstvm fggvsinpqi
      121 dalkrgvdiv vatpgrlldh mqqktidlsn ldilvldead rmldmgfihd ikrvlaklpp
      181 krqnllfsat fsdeikalad slldspalie varrnttaes vaqkihpvdr drkrellthl
      241 irehnwfqvl vftrtkhgan rlaeqltkdg isamaihgnk sqsartrala efksntlqvl
      301 vatdiaargi didqlphvvn fdlpnvpedy vhrigrtgra gatgeavslv cvdekqllrd
      361 ierlikreip qeviagfepd pnvkpepiqq rrgqqqprgg gggggggggn rqprgggsgq
      421 paakrdgnaq pkagqpkaaq kaakpraqgg agaggnsggr pagggnsarp asgnaahpnr
      481 nrssrsgqrg h
//
LOCUS       WP_175871954             369 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175871954
VERSION     WP_175871954.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..369
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39656
     Region          1..354
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masvllrnia kryddtevlr nvnldiadge fvvfvgpsgc gkstlmrmia gledisngdl
       61 lidgakvndv psakrgiamv fqsyalyphm tlydnmafgl klagakkpei dqavkqaaki
      121 lhidhlldrk pkqlsggqrq rvaigraitr kpkvflfdep lsnldaalrv kmrlefarlh
      181 delkttmiyv thdqveamtl adkivvlsgg avqqvgtpne lyhapanqfv agfigspkmn
      241 flkgtvesad aggvlvrfds getqrvavda aglqrgaavt vgvrpehllv daaaagvaar
      301 tmaveslgda aylyaesava pdgliaripp ldtyrtgdal rvhaqaehch lfdehgqafr
      361 rlsvhakaa
//
LOCUS       WP_175871919             234 aa            linear   BCT 11-JAN-2025
DEFINITION  TerC family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175871919
VERSION     WP_175871919.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..234
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24583
     Region          24..191
                     /region_name="R_switched_YjbE"
                     /note="integral membrane protein, YjbE family; TIGR03717"
                     /db_xref="CDD:163429"
ORIGIN      
        1 mlefltslhw gailqiiiid illggdnavv ialacrnlpa sqrlrgvvwg tagaillrva
       61 litfavalld vpflklgggl lllwigiklm apatdahddi kpadrlwdav ktiviadavm
      121 sldnviaiag aaeqadpshr ialvifglvv svpiivwgst lvlklldrfp vvvafgagll
      181 gwiagglivn dpvgdrwpvl dtpsvvygas iagalfvvai gyalrkrrsv phah
//
LOCUS       WP_175871973             520 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175871973
VERSION     WP_175871973.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..520
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54680
     Region          24..520
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mpspprsses ldvdallaal prriadvpah raaqspahpa liedarrlsy gdlaqaveaa
       61 aarlanlgvq ggdrvmivae ncvaqivllf aaaridawal vsnarlsaae ldaiaaharp
      121 kliafttdas adarahaerl gatpagalpv digawsyrvd asapaepvaa dgaeqcaali
      181 yttgttgtpk gvmlshrnll fiaatsstlr rvspddvvyt vlpvshvygl asvclgslya
      241 gatlrlaprf apeairvala degvtifqgv pamhaklleh lhthghawra prlrfaysgg
      301 spldanlkar verlygvplh ngygmtessp titqtpldap rtdssvgvpi pgvdmrivap
      361 dgtdvppgev geirvrgpnv mlgyyrnada traavspdgw lstgdlarqe adgavtivgr
      421 skeliirsgf nvypveveqv lnahpdvvqa avigraiegn eevlafvelv pgaaadetal
      481 hawctdrlta ykrpahirvl dalpaastgk vlkhrlrelv
//
LOCUS       WP_175872059             312 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175872059
VERSION     WP_175872059.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..312
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33900
     Region          7..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..294
                     /region_name="PBP2_DntR_like_1"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     similar to DntR, which is involved in the catabolism of
                     dinitrotoluene; contains the type 2 periplasmic binding
                     fold; cd08460"
                     /db_xref="CDD:176149"
     Site            order(103,105..106,110,167,204,269)
                     /site_type="other"
                     /note="putative substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:176149"
     Site            order(104,107..108,111..112,115..116,118..119,122..123,
                     125..129,131,193,221..225,228..229,232..233,236)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176149"
ORIGIN      
        1 matsidlnll vvldallsen svvgaanalg lspsalsrsl arlrvmtgdp llvragrdlv
       61 ptpralelrd rvhalvveah svmcpcervd mstlkrtfsi raneafvetf apallehasr
      121 aapdvrlrfa pkpnkhvdal rngdidlevg vigqagpelr vqalfrdrfi gvvradhpla
      181 tgeitpqrfa sfpqvsvsrr gqfngpidtl ldslgivrtv ttvvssfpta lslargsdfv
      241 asvperqter srvgmysftl plpiadltvs qiwhprfdrd pahrwlrdcv rricaprvad
      301 aiapvsqava sm
//
LOCUS       WP_175872061             175 aa            linear   BCT 11-JAN-2025
DEFINITION  aromatic-ring-hydroxylating dioxygenase subunit beta [Burkholderia
            sp. BCC0397].
ACCESSION   WP_175872061
VERSION     WP_175872061.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10791045
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..175
                     /product="aromatic-ring-hydroxylating dioxygenase subunit
                     beta"
                     /EC_number="1.14.-.-"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0009056 - catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=20130
     Region          20..175
                     /region_name="HcaF"
                     /note="3-phenylpropionate/cinnamic acid dioxygenase, small
                     subunit [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG5517"
                     /db_xref="CDD:444268"
ORIGIN      
        1 mstittrtgr psaephagga nfedfyslvq lnaryaavld ggdwdawpef fveqcrytvv
       61 prenhernlp lavmdfeskg mlkdrvygik etlffdpyyq rhviglplvt ylddtvieae
      121 tnyavlrtkt eqmsdvyntg ryldrivrtp hglrfesric vydsemipns liypi
//
LOCUS       WP_175872068             382 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175872068
VERSION     WP_175872068.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..382
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40179
     Region          1..367
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mtltaseaqh tttaayrdia erharsapcg afhrdawdal sdaglwrlpv prelggaggt
       61 whdfvdafea vaatlrsvgf amalanqatl iravvaygsd aqrtrhlpsl lsgaigatai
      121 sekgtgtevr aletclvrdg dhyrldghky nishapearl mmivatltgd gkpatalvli
      181 dperagvqrs apqatfgvad lpigdlalsg vridadellg tpgdglrllm diasmnralf
      241 gllcanvtqp fladalahag arktlgvald ahqhvqrrlv evqvgiertr staraaldll
      301 vaqrpealan csiaklggar dlaqaalhll aihgsdgyrr gplatfvada lamgsaggte
      361 emhyrnifsq mqrraaatar aa
//
LOCUS       WP_175872107             548 aa            linear   BCT 11-JAN-2025
DEFINITION  NRAMP family divalent metal transporter [Burkholderia sp. BCC0397].
ACCESSION   WP_175872107
VERSION     WP_175872107.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..548
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=58658
     Region          48..452
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 mstpsnvspp iavdrgavld eahlgdirga lgtiahhdtg argtwwarlr tllaiigpgl
       61 ivmvgdndag afgtytqagq nygttllwtl lllvpvlyvn qemvlrlgav tgvgharlif
      121 erfgkfwgaf svidlfllna ltivtefigi tfvldffglp kvagvcvaaa ltmaavstgd
      181 frrferfaig lcvlslllvp vlvsihppva qmtrdffvpn wpahaklsdv mllvigivgt
      241 tvapwqlffq qsyvidkrit prfmkyekad lwigiafvlv gavamigfss alfgghpeag
      301 nftdaggiia gleryagrts atlfavalld aciigaaavs lstayaigdv fkirhslhrg
      361 vtdakgfylv yfgivaaaat lvlipgsplg llteavqtla gvllpsatvf llvlcndrqv
      421 lgpwvnstkf nvftgaviwv lvllsiilta svmypdisge aivdvlvggt vlaiagylat
      481 vlirrnkrvv epavdrslrd twrmppldtl epqnmtlatr iwmavlrgyl viavglvivk
      541 vvqmtllk
//
LOCUS       WP_175872186             353 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia sp. BCC0397].
ACCESSION   WP_175872186
VERSION     WP_175872186.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..353
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37559
     Region          3..332
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,225,286,306,308..310)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,173,176,178,225,232,286,306,
                     308..309)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,173,176,178,309)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            178
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mptlfdpvtl gdltlpnriv mapltrsrag aarvpnalma ryyaerasag liiteatsvt
       61 pqgvgyadtp giwsdeqveg wkqitqavha aggrivlqlw hvgrisdpmf lngdlpvaps
      121 aiaaggnvsl vrpprpfvtp raleldeipg ivaayrkgae nakaagfdgv eihgangyll
      181 dqflqdstnr rtdayggpie nrarlllevv daaidvwgag rvgvhlaprs dahtmgdsdp
      241 aatfgyvare lgrrkiafif tresysgdql sprlkeafgg plianeqftl dtaqaalasg
      301 sadaiawgkl fianpdlprr leidaplnkp vpetfyaege tgytdypals daa
//
LOCUS       WP_175872196             442 aa            linear   BCT 11-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175872196
VERSION     WP_175872196.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..442
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=46963
     Region          3..408
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mnkrmsaagw illamaagil igyliytqfp dkqsaaeiag yislvsdvfl rlikmvigpl
       61 vfstlvvgia hmgdassvgr vfvkalgwfv taslvslllg llmanllrpg enlglplpdi
      121 gasahlatsk ftlkdfvghm vpksiaeama nneilqivvf smffgvalaa lgergkilva
      181 aidqlahvml kitgyvmkla plavmaamas tvavnglsil lkfavfmgdf yvslvllwat
      241 lvaagllflg rrvfkllvli keafmlsfat asseaaypki ldaldrfgvr rkissfvmpm
      301 gysfnldgsm myctfaslfi aqaynihlsl gtqvtmllil mltskgmagv praslvviaa
      361 tlhqfdipea glllilgvdt fldmgrsatn avgnsiasav vakwegelms eseanahaah
      421 ldaelerqnr apaygagqat st
//
LOCUS       WP_175872199             217 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175872199
VERSION     WP_175872199.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..217
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24067
     Region          29..180
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maevteraps krrtrgrpla dasvgpdvil raarrtfakr gydatsvrev arelgidaal
       61 iahhfgtket lwlavveqiv elaepmfdal ralrtsslpq rervrralel cvdhefaepd
      121 igmffstaat eeggrldrlq erivrpyhda mfrlladave agairpvdpn vlffmiasai
      181 gttvsyshmm leytslptrp eafreavlgv vfsilsv
//
LOCUS       WP_175872204            1057 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia sp. BCC0397].
ACCESSION   WP_175872204
VERSION     WP_175872204.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..1057
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113219
     Region          1..1038
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mdfsrffidr pifavvlsiv ifaiglisip mlpageypev vppsvvvrat ypganpkeia
       61 esvaepleea ingvegimym ksvagsdgsl qvvvtflqgv dpdtaavrvq nrvsqalsrl
      121 pdevrqygvt tqkqsptplm yvslyspdns rdslylrnyl tlhvkdelsr ltgigdvgvy
      181 gsgdyamrlw ldpnrlasrg ltasdviaav reqnvqvsag qlgaepspkk ndflvsinvr
      241 grlrtvqefs divlrngddg qvvklsdvar ielgagdytl rsyfndkhsa vvgiflspga
      301 naldvakavy akldelskrf ppgvayrpvw dptvfvresi ravqhtliea vvlvvlvvil
      361 flqtwrasii plvavpvsvv gtfaflhllg ysintltlfg lvlaigivvd daivvvenve
      421 rniarglspr daahqamrev sgpivaialv lcavfvpmaf msgvtgqfyr qfavtiaist
      481 visainsltl spalaakllr phgapkdalt raldrafgwl fhpfnrffer sadryhgvvg
      541 rtlkrrgvvf avyaallaat allfnavpgg fipvqdklyl fagaklpega slartsavte
      601 qmtkialgtd gvemvpafag lnalqgvntp nitnsyvilk pfdqrhrsaa qinadlnarf
      661 aaigggitya lmpppiqglg ngsgyslyle drgglgygel qkalaafqaa vaktpgmsyp
      721 vssyqanipq levkvdrlka kaqgvaltdl fntlqvylgs myvndfnvfg rvyrvmaqad
      781 aghrqtaadi anlrtrnakg emvpigsmvt vgpaygpdpv vryngypaad ligdadpkmm
      841 sssqaiaklq qiakdvlppg itlewtdlsy qqvtqsnaai vvfplavmlv flvlaslyes
      901 wtlplavili vpvcmcaalf gvwlsggdnn vfvqvglvvl mglacknail ivefarelei
      961 qgkgaveaal eacklrlrpi vmtsvafiag svplligsga gsevraatgv tvfagmlgvt
     1021 lfglfltpvf yvairklagg tpavwseqhg tlegenr
//
LOCUS       WP_175872248             296 aa            linear   BCT 11-JAN-2025
DEFINITION  peptidylprolyl isomerase [Burkholderia sp. BCC0397].
ACCESSION   WP_175872248
VERSION     WP_175872248.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..296
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=30939
     Region          135..283
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mmtkmkvlam vagslvlgep lvacaqddvi anaaqasvtq adiagllkav saegrerlaa
       61 dpaaldqvvr stlaqkavla eakskgwdkq pqvqaaveqe qrdivvrsyl asvnappady
      121 psdaelqsay dknraaftap ralhvaqiyi avppnadaat ldkarkqaad lasrarngdf
      181 aalakvssqd kasaanggdl gfvpdqmmvp avrqaadalk pgqvsapiqt pagfhvvkli
      241 eiraaaprpl advkeqlram lraqrtqqna qaylaklaan apinedalkk alasar
//
LOCUS       WP_175872206             215 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175872206
VERSION     WP_175872206.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..215
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23260
     Region          7..203
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mtsthsltfy tadtpnghki aiyleeagla hdrvqvnlsa geqrspayla inpngkipai
       61 vdhdtglavf esgailsyla aktgclqpdt laerttvqqw lhfqiggigp mlgqlwwflr
      121 asktgnaeai dryrkealrl ygvvngrlse sahlassrys iadiaaftwl rtaaeldldi
      181 agfphverwl aeiaarpavq rgliacraps aeaah
//
LOCUS       WP_175872264             414 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia sp. BCC0397].
ACCESSION   WP_175872264
VERSION     WP_175872264.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..414
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44026
     Region          12..414
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mseantqela apstvvvigg gqaagwvlkt lraegfagrl vmiadephlp yerpplskav
       61 lagdadietv rvvrpdefda lnveawqper aasidrarrv vktesgreie ydrlviatgg
      121 tsrrlpdaiv ntpnlhylrt ldeaaalgek lrasrrvlvi gggwigleva atarklgvea
      181 vvvegaprlc grsvpqivsd flldlhrsng vdvrtgaala sldpqpndas kvratladgt
      241 tidadfavag iglalnasla sdaglalddg ivvdeygats dpaifacgdv anhhngwlkr
      301 rvrleswana qnqaiaaaka vlgvrapyae ipwfwsdqyd vnlqilgdlp adaqlvvrgd
      361 laarratlff lgdghvrgvi avnnarelkl arkwmnqgra vdtealadtt rala
//
LOCUS       WP_175872275             287 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia sp. BCC0397].
ACCESSION   WP_175872275
VERSION     WP_175872275.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..287
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31368
     Region          30..270
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 mtdireddap dstaarvalw ralhveldap ppvladeigl rllapepgwq qrgdmdpqft
       61 rpfrasivar arfiedlvae qaargvsqyv ilgagldsfv qrrpdmasrv tvfevdppap
      121 qrwkqrrlve lgfgvpdwlr fvpvdfeakq swrdalvgag fdvgqpavvv stgvsmyltr
      181 eanaaalrev aslapgstfa mtfllplena dpdvrpgmem aakgarasgt pfisffmpdq
      241 iqalareagf akaehvsaae ltrryfaert dglrppnrae ellvatv
//
LOCUS       WP_175872331             288 aa            linear   BCT 11-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175872331
VERSION     WP_175872331.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..288
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=30093
     Region          195..>258
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mslsllpcat iwlalfaaaa fawhrplhgl siglaalgya galafgqlap vtlapfalli
       61 aagwgvlpar plavriaahl vfaalaials lhlipgfhnp rviaptrftp davpftmyln
      121 fdkplvglwl lwalpwvapd valsralrtg vvaavataaa clagalafgm vgwapkwpps
      181 gwlwlvnnll lvtlaeealf rgyvqggltr vlrayswgpw valaagavlf gaahaaagwq
      241 wivlgtvagv gyglawrrgg llaaalahag lnivhfglft ypmldaar
//
LOCUS       WP_175872486             173 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175872486
VERSION     WP_175872486.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..173
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18968
     Region          10..>86
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtkrarltre qrrldtrerl iataralfia kgfadtsveh iaegagytrg afyahfehkr
       61 eplieilrrd hdrlikrlrl aapkgdgcct vtdaadvaag wecfplwvev ylyalrdagf
      121 rqiidsmhtq laappnaang aagpsdhmss saelaavlgv allrtgarrd ept
//
LOCUS       WP_175872491            1055 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia sp. BCC0397].
ACCESSION   WP_175872491
VERSION     WP_175872491.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..1055
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114289
     Region          28..1032
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnapehrpst dgnrartgaa syddggfnls awalkhqqlv ifliglatif gvigytrlaq
       61 sedppftfrt mviqtywpga tarevqeqvt drigrqlqaa pyvdniksys rpgesmiffa
      121 mkdsapvdqv petwyqvrkk vgdirstlpk gvvgpffnde fgdvytnvya legdgyspaq
      181 lhdyadklrt allrvpgvak vdyfgdpaqh vfveisnaql trlaitpqql aqaidaqnav
      241 apvgtittad drvfvrpsga fkdtqaladm litvngrtfr lgdvakvtrg yddppatqmr
      301 tnghavlgig vtmqkggdvi dlgkaldaka aelqrglpag lklaavssmp havkhsvddf
      361 veavgeavai vlvvslvslg lrtgmvvvit ipivlavtal cmhafgigld kvslgtlvla
      421 lgllvddaii avemmavkle qgwsrtraaa faytstafpm ltgtlvtvsg flpialakss
      481 tgeytrsife vsaialivsw faavvlvpll gyhmlpehah rdghahgdav ydtgfyrrls
      541 gwisacierr wlvlgvtaal faiamaaftr vpqqffpnse rpellvdmrl pegasfdatl
      601 reakrlekvl dgrpeidhvv dfvgtgaprf ylpldqqlqq pnfaqfvita kdvetrdrls
      661 hwleatlasr fptvrtrvar lengppvgfp ikfrvsgddi atvrgiaekv adkvradart
      721 rnvqfdwdep aersvsfeid qikarqlgat sedvsgflam tlsgytvtqy rerdklidvd
      781 lrapkserid psklaglaip tphgpvplgt ighvrdtley gviwerdrqp tvtvqadvrg
      841 eapsigvtrd idaalatvra tlpagyriei ggaaeesvkg qtsinaqmpl miivvltllm
      901 iqlkrfsrtf ivvltaplgl igvvaalllf gkpfgfvall gviamfgiim rnsvilvdqi
      961 dqdiaagqpr faaivgatvr rfrpimltaa aavlalipll rsgffgpmat almggitvat
     1021 vltifflpal yatcfkvrrd esepramnva sseis
//
LOCUS       WP_175872540             457 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia sp. BCC0397].
ACCESSION   WP_175872540
VERSION     WP_175872540.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..457
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47657
     Region          234..410
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mrsdlrfrva reqgqpaprg vhrfpigral lrgivaaacv agaqgaaaqa fhdaapvapa
       61 taettdlgdv pffnsarttw gglhvsaaap ldiayashal svsagpgrdd pvarfgacva
      121 yrvlcdtarg avergyasrf dyglasalpa tgaqptfvhg svdlasaepf tlaqpdrgtr
      181 agaivgslra slaradlpag iaaqivrmla grvdpkqrga hgdtfrvafe pdhdatrpgr
      241 vrvtaldirf rgqrvaavwf apqagspgay yeldgmplag arfampvtat rissqfgtrv
      301 hpvsgarhvh sgvdlaapag ravhasergv vtfigtepsg ygkyvvirhd ggyasyyahl
      361 safeptlrtg arvmrgqrvg avgstgtatg phlhfevrrh arlvdpielv haakaaklkg
      421 aqrvafnrva rdartqlasa tfaqpvamsk avapqag
//
LOCUS       WP_175872534             401 aa            linear   BCT 11-JAN-2025
DEFINITION  benzoate/H(+) symporter BenE family transporter [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175872534
VERSION     WP_175872534.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..401
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41522
     Region          11..398
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mqpntppgai rtigndwsvs aitagflavl isyagplaif fqaaqaahas nemvsswvwa
       61 isigagmsgl faswklkvpv vtawsapgta llvglfpqlt lnqavgayit aaliilaigv
      121 sgyfdrlvrh iprgiacgmm agillpfgmh afsaataqpv lgfgmiaayv ifkrllpryg
      181 ivlvlltgaa latllgmthl gnvspslarp ifiapewtlg ttlslalplv vsltgqflpg
      241 mtilrvsgyh tparpiitat svmslvvacf ggitivvaai taalctgkda hedpdrryia
      301 giangviyli gglfagtivt vffalpkafv ailaglalig aisanvhgif edehhreasv
      361 itflatasgm twlglgsafw givigsvaya vlskvrgrqg d
//
LOCUS       WP_175872551             328 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175872551
VERSION     WP_175872551.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..328
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35146
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,146,160,162,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdliqsmqaf vtladagtft etgkrlgitt ahvsrlvasl ehrlgirlln rttrsmclte
       61 agerylarar ditlavdase reardarvhp hgrlrahcsa sianhfvipl igqfqarypd
      121 vsvdltlaph lpklvrdsyd vaviampslp sseqvaidvg rirsvlcasp ayldahgtpd
      181 spgalvhhrc vqlvapayhe riwtlwhgae aqtvdvdpsm tadvaaslai avregagigl
      241 lpdfvaaadl rsgalvrvlp dyqaeeigvf lvyasrqhld aktrawvdfm kaalrdafaq
      301 ahddayappp gkkghapgka gtwagaaa
//
LOCUS       WP_175872582             193 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175872582
VERSION     WP_175872582.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..193
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20609
     Region          14..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkskhsttde aplradaarn rerileaaea lflergaeas ldeiakranv gigtlyrrfp
       61 trdallaats derllslaea srarddklep dasvrafvke lvnhathyrg laallgtvlq
      121 egtagchagr eegrrllqra qmagtvrkdv svddlvcvvt aialaveqgg atksrvahlv
      181 dlfldgignt qaa
//
LOCUS       WP_175872609             339 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-quinone oxidoreductase [Burkholderia sp. BCC0397].
ACCESSION   WP_175872609
VERSION     WP_175872609.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..339
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=35479
     Region          1..333
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(40..41,127,131,134,157,160..162,181..182,186,201,
                     225..226,247..248,250,272..274,322,327)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mkaieitefg apdvlklaer prpepkrgev likvaasgvn rpdvfqrkga yapppgasdl
       61 pglevageiv ggdlsdaaln pfglklgdrv callagggya eyavaplpqc lpvpggltdi
      121 eaaslpetff tvwsnvfdra qlgageggeq etllvqggss gigvtaiqia halgfrvfat
      181 agtadkcrac ealgaerain yktedfvevv kslthdrgvd vildmvagsy vprelsalad
      241 ggrlvliall ggakaevnln eilrrrltvt gstlrprpve fkariaaqlk arvwplladg
      301 rikpviyrvl pageaaqaha lmesgehigk ivldwgana
//
LOCUS       WP_175872643             531 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia sp. BCC0397].
ACCESSION   WP_175872643
VERSION     WP_175872643.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..531
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57292
     Region          34..432
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msagpaglth dvpaapfern atmsdsvakp vdatfdqfgl aadilkaiae qgyttptpiq
       61 aqaipvvlag rdvmgaaqtg tgktasfslp iiqrllphas tsasparhpv raliltptre
      121 ladqvaanvh ayakhtslrs avvfggvdmn pqsaelrrgv eiliatpgrl ldhvqqktan
      181 lgqvqilvld eadrmldmgf lpdlqrilnl lpkerqtllf satfsgeikk lastylrnpq
      241 tievarsnst nanvtqivyd vaegdkqaav vqllrdrglk qvivfcnski gasrlarnle
      301 rdgvvasaih gdktqlermq aldafkrgei ealvatdvaa rgldiaelpa vinfdlpfsa
      361 edyvhrigrt gragatgdal slcspnerkq ladieklikr plevqtlrid kparqrhder
      421 ggertgertg ertgergger sserggergg rrerdehrga sgrrsgsser gghhrrheap
      481 vddfflkpye psasakqpdd aqaaqqpekk gpkrqvaall ggfgmprkps a
//
LOCUS       WP_175872646             415 aa            linear   BCT 11-JAN-2025
DEFINITION  lactonase family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175872646
VERSION     WP_175872646.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..415
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44241
     Region          52..411
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 mpnrlrerda rastrgfplr fahwmkgfai vlslsathaf aqqssvpadg vynllvgtyt
       61 gggsdgiyvy rfdtktgsva pvsstktvnp syllpsrdgr tvyavnelpg ddgpatqrgg
      121 vsafrfdakt galtfiervs segndpcyla lspdgkylvt anysvaadpg gsfavfplrd
      181 dgaagqavlt vhhegtgpvk grqdgahvhs tvfspdgryl fvqdlgadki ygyrytvdgs
      241 rgligptdtr ytpvkagsgp rhmvfgadgr fayvtselna svevfgyhdg kltpvetvpm
      301 tapgfkgkvg ggaihlspdg rflyvsnrgd andlviyavn kadgrlkhvg rqsslgktpr
      361 eflidptgkw livgnqdsdt fyvfsrdvet gqlganpqkv tvgkpvdfkl vpvaq
//
LOCUS       WP_175872651             403 aa            linear   BCT 11-JAN-2025
DEFINITION  benzoate/H(+) symporter BenE family transporter [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175872651
VERSION     WP_175872651.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..403
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41325
     Region          15..403
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mnpsptasag raggrrffad tsvsalvagf vammtgytss lvlmfqagra ahltdaqiss
       61 wiwalsigma lttiglslrf rapvvvawst pgaalliasl pgvpypeaig afvvcalllt
      121 avgvsglfdt lmkripagia aallagilfe igieifraaq fqtalvlamf ftylivkrla
      181 pryaivttli vgtavagglg lldfsrfhia laqpvftmpa lsiasivsig iplfvvamas
      241 qnvpgiavlr adgystpssp liattglasl llapfgshgv nlaaitaaic tgpeahedha
      301 krytaavwcg tfyliagifg atiaalfaal pkalvvsvaa lalfgsimsg lanamqdvkq
      361 reaalvtfmv tasgltllsi gsafwglvag vvtqvilnar rpa
//
LOCUS       WP_175872739             272 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175872739
VERSION     WP_175872739.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..272
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29312
     Region          18..266
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtgtaaphaa agdmhymavd ltlkagartl ldrftqafrp geiwcvagpn gagkttllat
       61 laglqppagg hveidgrpla awrpeqlaqr ralmpqqlhd afsatvfdtv llnrfpylgg
      121 wgwerdgdrt aardalatfd ltalasrdvm slsggerqrv alaatlcqda plmlldepla
      181 hldlhhqidc ltalaewlaa gprtvmfsch dlnlarrfat hallldgrgh awagpvhdvl
      241 tperasdafg yplvlireng rdallpawpa rq
//
LOCUS       WP_175872745             108 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia sp. BCC0397].
ACCESSION   WP_175872745
VERSION     WP_175872745.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..108
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11147
     Region          23..106
                     /region_name="CytC552"
                     /note="Cytochrome c551/c552 [Energy production and
                     conversion]; COG4654"
                     /db_xref="CDD:443692"
ORIGIN      
        1 mkqtilrvll atlltgsaaa vradqadgla laqrkncmac haigkplmgp sfrdiagkya
       61 argdagdyla qsivkgsvgv wggvpmpant qltsteahtl aqwvlsvr
//
LOCUS       WP_175872755             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175872755
VERSION     WP_175872755.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32755
     Region          13..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..295
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(106,110,149,163,165,230,247,274)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(107..108,112..113,115..116,119,123,125..131,193,
                     224..228,235..236,239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mgfdsrllsg igvlsaviea gtfarageam gltqpavsra varleervgi rifnrtarai
       61 tltdegrrfy etvapllagi eeaaldagqs karvrgrlrv nvdgtfghyv laprmaefld
      121 rfpdlsveis vrdrmgdlva dgfdvavrfg ipepssyrar llletrvltc aspayvarhg
      181 eprhprdlvd ghrcvlirdp vtgrpyewef hrgkevvpfd aggqlmvndt ggllgaclgg
      241 agiaqllely ardivadgkl vlllpewade tfplyayhha snlvaakvrv fldfvrelma
//
LOCUS       WP_175872776             459 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia sp. BCC0397].
ACCESSION   WP_175872776
VERSION     WP_175872776.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..459
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49051
     Region          7..457
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mtqqqrsfdd ivareqglrh altsgqmami aiggaigtgl flgsgfaigl agpsvlvsya
       61 igalialllm galaemtvah ptagsfgaya ehyvgplagf lvryaywfav vfaigteisa
      121 iavfmkywfp avpgwywvig fsalliavnl asvtlygtve yafsllkiaa ivvfillgay
      181 lvwsapaasg igfanytahg gfmpkgpwgt wvavivaifs ymsieavaia ageardpqha
      241 vtrafrstvf rlvlfylltl almlaivpwt qagtdespfv kvmaathvpy aagvinfvll
      301 iaalsamnsq lyvttrmmfs lsrarlapav fgrlgangvp raalwistsg vavaavlval
      361 apdtaftvmm aiamfgalft wlmifvthlr frsqyrgpal afrmwghpfg sllgaglvaa
      421 illttaftre frmtmvvgvv fvvlltlaya lhyrhqhar
//
LOCUS       WP_175872811             543 aa            linear   BCT 11-JAN-2025
DEFINITION  GspE/PulE family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175872811
VERSION     WP_175872811.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..543
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=58807
     Region          2..538
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mktehivqrw qsesdasgvd faqyvaglls adatllaqaa aclgigavda dalraartrf
       61 dllplhdalt wrvlpveldg vpcvvvadpf arhvrdella rfgtrpvela msapgeverl
      121 lgdiesserl mddvtidtqg dslaqaiesi slasiakdes piirlvnttl ydalqsrasd
      181 ihleavpdgl siryridgvl qsirhipgle aaaqtlsrlk vlaaldiaek rvpqdgrfkv
      241 vmqgreidfr vsiipgthge navmrvldks qrgdrvsldv lgfdaptarr vralahrpyg
      301 lmlvtgptgs gksttlyavl sevntgddki itiedpveye lqgvlqipvn erkgltfarg
      361 lrsilrhdpd tvmvgeirde etasiavqsa ltghrvlstv handgfsvid rfiymgveps
      421 tflealngvv sqrlvrrica rcgdaahgad lrdapldelk rvvapgagce tcrgtgyhgr
      481 iglaevltld aamkvaller siekrtrala dnadyqsmre aglaairarl ttfqevqrai
      541 ave
//
LOCUS       WP_175872872             734 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175872872
VERSION     WP_175872872.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..734
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79704
     Region          33..717
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 msasspastp aggpfavwta afgdwartdg aawlylfkal laafiatgvs mrldlpapkt
       61 amttvfivmq pqsgavlaks fyrvagtifg liatltfvgl fpqqpqlfll avalwvalct
      121 agaarnrnfr sygfllagyt taliglpasq hpdgafmsam trvaeimvgi vsagvvsalv
      181 fpqttgeqmr ttvrkrfgsf vdyvaaalsg qldrahieti htrfvadvvg feaarsmavf
      241 edpdtrmrsg rlarlnsefm sassrfhalh qlmnrlhaag aqaaidaiep yfreiaplll
      301 tpagepvrts adaghaaaql lawrdalprr iratraalet qpdfplldfd taaellyrfi
      361 tdlheyaaty aslstather erwieryepr tnatamviaa irtatvilvl gwfwietawp
      421 sgvtmtltaa atcalasstp rptamsaqmg mgtalavctg flltfgiyph idgfpllcva
      481 lapllaigiy ltlkpklagy gmgyliffsf lagpdnithy dptsfmndsl slvlamlvsa
      541 iafavlfppt apwlkkrlfa dlrhqavaag harlaglrtr fesgardlmy qahtlsadqp
      601 dvqrdalrwm favletgnat idlrhelatl psdpryapam pwrraietmr salsalfskp
      661 starfdatla atnaaidatr qtldavepsr derhrlqril shlhfvrtal ldpesplepl
      721 nrnrpvrpqp gass
//
LOCUS       WP_175872855             137 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175872855
VERSION     WP_175872855.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..137
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15375
     Region          19..106
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(20..22,36,53..55)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mtttvekvvl ppipakryft igevselcgv kphvlryweq eftqlrpvkr rgnrryyqhh
       61 evllirrire llyeqgftin garnrldspg seraaaepve sdaqaadare agkggatvdv
      121 ialrqalldv idglkhd
//
LOCUS       WP_175872914             304 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175872914
VERSION     WP_175872914.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32945
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          90..273
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(105..106,108..109,112,116,118..124,216..221,
                     227..228,230..231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdlaalaifr avvrengvtr aaaklnrvqs nvttrikqle eelgaalfvr dgrrlvltpa
       61 ghtllpyaer llaladeard avredtprgr lrlgtmesta asrlptllar yhhawpdvsl
      121 elltgttgcl idrvrdfeid aalfarppep dmlpdtfetv pifredlvll tprghppvrt
      181 prdvilptli afergcayrk yveqwyaahg vkparvlelg syhaivacva agagvavapr
      241 svldlqpetg niaahtipel egidtllawr rgyasaalaa lrdaladavr qpgdvakptv
      301 svpa
//
LOCUS       WP_175872939             579 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia sp. BCC0397].
ACCESSION   WP_175872939
VERSION     WP_175872939.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 579)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..579
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=63364
     Region          10..579
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mkiirrgnla aaallfivtg vsaqeaprli vpgndqqtrq qeearerera vtapgvrsgv
       61 tasaaypvlp setpcfrieh faldvpdalp aslksqgasa lpmdrfafar ewlehytgqc
      121 vgkqgldvlv kglsqailar gyvttrvllp eqdlstgilk fslisgvirh vrfadeklrg
      181 twktafptgd gellnlrdle qgleqmkrvs sqdvsmqivp advpgesdvv ldvkrgkpwt
      241 vvasidnsgt ratgrlqgnl slgidnplgl ndifnigmsq dlefgdkrlg shgwngfysi
      301 pwgywtatls aytstyyqqv agvnqtfvas gnsktvdfkl nrvlsrsqnd vfgaqfrlsr
      361 rfgqsfiedt eipqqrrnnt fvefgltdrh yfgnaqfdgt lvyrqgigaf gaqddmlasd
      421 ggptyrykma vldanlsvpf aiaqqpfryv ttfhgqytgn tlyyiddlti gsrytvrgfd
      481 getmlaasrg fywrnelqap igqtgmavya gldygrvwgp qpialvgtql agavigvkgs
      541 vatrfggygy dlfagtpvyk psgfptnrvt lgfqltaqf
//
LOCUS       WP_175872967             183 aa            linear   BCT 11-JAN-2025
DEFINITION  PadR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175872967
VERSION     WP_175872967.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 183)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..183
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20789
     Region          1..86
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          91..179
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 mslphallta laerpgsgse ladrfdrsig yfwqathqqi yrelgrleet gwieslpaes
       61 grgrkrayri lpagkkelrr wiaepedptp lrealmvrlr aeavlgpagl edeirrrial
      121 hqekldvylq ieardfstag dpasddsrtk rlqhlvlqag ianerfwvef sqhaldtlrl
      181 pkd
//
LOCUS       WP_175872962             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175872962
VERSION     WP_175872962.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33865
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdkwtqieff vqvaelgsls kaaerlgmss aaasrclnal eerlgarlve rttrrlwltd
       61 agheyhrrca ailtelsead aavneasvnp agtlrvtasv sfasiyiapa lpefhrrypn
      121 lnvqiiaanr ypdfieagid vairtrehea dsgitvrkla etrrvlaasp gylakhgapa
      181 tpdalgdhrl lvynlandpy vlhfrhgakk qsvtiksvld anegqviraa alaglgiliq
      241 plyiihddiv agklvpvltd wqlpaltvni ayqsrrhqpa kirvfaefli erferlglar
      301 kwkevgr
//
LOCUS       WP_175873003             393 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA-binding protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175873003
VERSION     WP_175873003.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13774834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..393
                     /product="DNA-binding protein"
                     /calculated_mol_wt=43299
     Region          25..143
                     /region_name="KfrA_N"
                     /note="Plasmid replication region DNA-binding N-term;
                     pfam11740"
                     /db_xref="CDD:432038"
     Region          <102..>349
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
ORIGIN      
        1 mtldemrqvi reeleslras garrqelslh ackrlffdlg irpsaanvrd ltqtgsasdi
       61 pkdidhfwer irsaskirld gaaipkavee kacallgaly eealkaards ldgdreqvra
      121 dmadaeqrlr datvrqetle galargearn eqlqarvtel evqlasqtth gsaseatllt
      181 tvarlekela aaagridaeq aqnaalrdri dalqaelqqr tehyaqqikd avaeaerrvk
      241 pmlveldslr smastyqsgl rdvqrkefdf lqqlssakar adrleeqlrt qsdeldratr
      301 dasslranrg mnpeiaallr rladagqlda dayaaigttl dheipaparc phcdgepels
      361 hgdegfevac pecehasgaw psrfeavarf aqp
//
LOCUS       WP_175872806             162 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175872806
VERSION     WP_175872806.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..162
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=17891
     Region          4..92
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 msvrrrarar gftlielmva msllallatv alpltdlvkr rsdeaelrra lvvirsalda
       61 ykeaasdgrv ehsvdasgyp adlrvlvdgv ddkkspdgar lyflrripad pmcecdgkap
      121 edtwetrsya sdpdsfssge dvfdirstnr keglngvpyn qw
//
LOCUS       WP_175873039             235 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175873039
VERSION     WP_175873039.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..235
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25077
     Region          25..210
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mkktvktgaa ttsgtartrr ptqaersqat rerviaaais llhkegysga ttlairread
       61 vsmgalqhqf ptkaelmaav qerltgdrfa qfksashgat tpleridrml dvagaligts
      121 lfaasmeiql arradkeldd avarvlepfd qgfralmddv vadfdtataa tikqfqvlag
      181 smirgltidv vtggepatar aafalwrdia lrqiadvtpp paaakaktak rrasr
//
LOCUS       WP_175873043             316 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175873043
VERSION     WP_175873043.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..316
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33845
     Region          16..73
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          104..304
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(119..120,122..123,126,130,132..138,233..238,
                     244..245,247..248)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mpeaspwgnr arlktrqlll lvaladegsi hraaaalnmt qpaaskllre leesigavlf
       61 erlprgmrpt lygdalirha raalgsldqa reelaalkag hlghvavgai tspglrlvpp
      121 avaavkgtha glhvsveidt snvllehlaq ekidivlgrl saehdklrlr yepltgesva
      181 avvrpghpll ahaplsladv qraawvvppa gsvlrhrfdl vfqraslapp anvvetaall
      241 fitqlieqsd miavlaedva hyyarhgivt vlplemdcrm ddfgiitrtd rlhspavtvm
      301 vdairaaate vygval
//
LOCUS       WP_175873071             234 aa            linear   BCT 11-JAN-2025
DEFINITION  MOSC domain-containing protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175873071
VERSION     WP_175873071.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12233312
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..234
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25782
     Region          26..183
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
     Region          180..219
                     /region_name="3-alpha"
                     /note="3-alpha domain; pfam03475"
                     /db_xref="CDD:460938"
ORIGIN      
        1 msddarpaia aavgavriga srplagtsha saidkqpvea rlwlgalgfa gdeqadarhh
       61 ggpdkavhhy ahdhyawwag qigardvlar pgafgenlst rgitehdvcl gdvftlggal
      121 lqvsqsrqpc wklnarfdhp rmaalvqqsg rtgwyyrvlq egwvgagdvl alherrypqw
      181 plstvldvly rrtldmaald alcdvpllpp gwrkmlekrr terqvedwtk rleg
//
LOCUS       WP_175873080             334 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175873080
VERSION     WP_175873080.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13300132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..334
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37366
     Region          29..>163
                     /region_name="PRK11242"
                     /note="DNA-binding transcriptional regulator CynR;
                     Provisional"
                     /db_xref="CDD:183051"
     Region          112..309
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(122,126,165,179,181,244,261,288)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(123..124,128..129,131..132,135,139,141..147,208,
                     238..242,249..250,253)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mpdtsirrpd addpfarsfs tcyacvvtfl avvtegsfar aadrlgvgrs svsrhvqrle
       61 drldarlfqr ttrsmsltre gelfyencrp giehlaqale dmrelrsgpp sghlrigstp
      121 gfgrkviapl lhdfhaqypd itldlllndr padfsadrid vafrdgrmed saivarrlip
      181 mqmivcasps yahrhglprh addlaqhrci nlctasgrvt ewefridgvt qqrqlaahht
      241 fndidlvvra aldglgiaql payqvcdlla dgrlvsclgq hapddgghyl cylsrkhlpt
      301 rirvfidymi eqtrardlqc lttmttmapl etid
//
LOCUS       WP_175873082             159 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175873082
VERSION     WP_175873082.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..159
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17884
     Region          11..144
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtqrinyiqq spelfrkfle lsnqlrssai eesirdlvsv rasqingcaf cvdmhvkear
       61 ihgerelrlh hlatwrestl fspreraala wtealttlsa hgvpddlydr argqlsekel
      121 sdltfevmai ngwnranvaf rtvpgssdka fgldkanla
//
LOCUS       WP_175873112             463 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175873112
VERSION     WP_175873112.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..463
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49247
     Region          129..443
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrgallvvca llggcatyhp qpiaplqiar qfedrslasd elhaylvrel ghdvapwplp
       61 rwnretltla awyyspaldi traqwgtaka gidvagaipn pvlqlpfqwa tpnpgpgapf
      121 ttgpaldipi etagkrgyri dqashlsesa rlaigneawk vgaqirdall alhadrersa
      181 lllrkveaeq qivamvtkrr avgesagpdv daavalqtqa qidlaagrta eqdaraqlaa
      241 aigipaaale hvafdfdgfd dtappppaad arrdailhra dllgsladya aaesalqlev
      301 akqypdihlg pgytydtgth kiafgvagit lpifdqnqgg iaqaeakrke aaartaalqd
      361 tilgdldhal tryrssidal klsdahqtaa rkqldsqeag faagdvdrlt ltqakadyqa
      421 seiarldaav avrqaagale damqrpltpd aartifplqq svr
//
LOCUS       WP_175873129             330 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175873129
VERSION     WP_175873129.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..330
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35308
     Region          4..321
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 maallevdnl gvrftrkdap pidavngvsf sleagktlgi vgesgsgksq tvmallglla
       61 gngtttgaar yrgdnlldmn tralnavrgd riamifqdpm tslnpfltie rqmtetlqlh
      121 rklsrkaaik raiealesvr ipdaarrirm yphefsggmr qrvmiamall sepeiliade
      181 pttaldvtvq aqiidllrel nrergtaivl ithdmgvvag laddvmvmya grtveyapae
      241 aifaapshpy tigllnalpr ltdavdaplv aipgnppmpg tapagcafak rctyaeercr
      301 aerpaletyg aanavrachr pvadligglr
//
LOCUS       WP_175873142             312 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia sp. BCC0397].
ACCESSION   WP_175873142
VERSION     WP_175873142.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..312
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33373
     Region          66..311
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mntlhlvdpe irplletwpt vtldadnlaq srqrvlplpp pdpagstler rtvpgpagtp
       61 dvpvlvywpd gharplpaiv hmhgggyvrg aakdleavhr slvtqlgcal isvdyrlape
      121 tvfpgaiedc yaalgwvfhh adtlgidttr igvagesagg glaaalalla rdrgefplaf
      181 qhliypmldd rtctrtphph agefiwhaan nrfgwtsllg hapgidgvsp yaaaaraarl
      241 dglpptflsv gsldlflden ldyaqrllra gvptelhvlp ggvhgfdivp garvseaarr
      301 lshdalrrfl hg
//
LOCUS       WP_175873145             350 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia sp. BCC0397].
ACCESSION   WP_175873145
VERSION     WP_175873145.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..350
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=36964
     Region          4..350
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mqrkaflvga cvlcatsaha ssvtlygivd syvefdrigs lssmrqsggg sstsrfgltg
       61 vedlgggtst kfvlesgfsp adgsfqggtl fyrqayvslq ntrygdlrlg rqytpafyvv
      121 ydgdpfglne rmsplallat stdtitsntt ppiprfnqaa sylspdwngl rvmatygfpt
      181 pnalstqagr nygaglqyri gglyvgagfq gdtsagnlap vvspsttrhy vfaanyafar
      241 vklyaaflyg vgtaarlpaf stasvgasin vgaldrvlvs vvrrdvkgsa ndatalgvgy
      301 dhplskrtsl yarylymkng gdarntvvvg lqphpggteq vfalgiahrf
//
LOCUS       WP_175873163             287 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175873163
VERSION     WP_175873163.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..287
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30411
     Region          4..>169
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
     Region          91..257
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(106..107,109..110,113,117,119..125,207..212,
                     218..219,221..222)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 matldvdavr vfllvaeles ftkaadfldt tqgvvsvklk rlegrlgyrl ldrtprsvrl
       61 sregnafves arefvaahdr alrgpalppa rlmlgvshnl vgteltalls mlhvfdpglt
      121 ievrvdnsrr llaeldgrnl daaivrhvdg rddgcviane qigwyaapsl hyepgtplrv
      181 aslpatcrvr amtsraldda gipwlevfvg ggvntvaaav saglavaala rpaapagsve
      241 vgtrfglppl pgsdvmlhsg slderakqal rviaasyrgk drvavta
//
LOCUS       WP_175873184             418 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175873184
VERSION     WP_175873184.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..418
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=46113
     Region          2..418
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 mpkfvllgln argdlqqfdl latdrhdaqq eaarcagqag vqivdvsiag raqtrlarsr
       61 pslrdllrsk rfdlplfvhe llallragls ltdaletlde hrrrshaaaa eeqghyvlpd
      121 lvrlmqegks fsmalaahpg cfsplfiami aaseqtggmt qalerylqyh aqvsvvrqkl
      181 isaslypall mvtgtvvaff lvwflaprfa hvyegmtqtd lpvlsawlln vglfvsdhtf
      241 aslgcllcil iaavtllvrp svqqqclawf grigwigetl klmqlarfyr slgmllqggv
      301 allpsldmtr ellplplqdg lersmiaiaq gkkmsesleq enlmttvasr llragerngq
      361 iagmleqaam fhereitqwv erfarlvepi lmlvmglgig tivvllylpv fdlagnlq
//
LOCUS       WP_175873174             558 aa            linear   BCT 11-JAN-2025
DEFINITION  alkaline phosphatase family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175873174
VERSION     WP_175873174.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 558)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..558
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=58340
     Region          40..536
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 misrfvkqrk mavmvagala lasagayaaq qdgnsqgeng anarrvvkhv lllsidglhe
       61 qdlarcigan tcpniavlak sgvtyanayt pglsdsfpgl aalvtggspk tvglfydvsy
      121 drnlyapsda tcsgkqgwnv vfdettgida qnggalvhld gggafnpqai phakvngqcv
      181 pvyphnyikt ntvfeavkag vpnahtawad khawgydwln gpsgtgvddl mrteinsidp
      241 atntaytdvy shtarfdnlh vqalinqieg rdstgtknap vptlfganfq tlsvaqkapv
      301 akgggyldad ftpngqvana ityvdnaigh vvaalkqanl ysstavivta khgqspsdht
      361 klvkngdtlt klleannfid pngnfgqnnt ttgnlndgsg lvgtgfvqtd dvgliwlrdr
      421 nqrtavvqtl kanlgcnapg icadgpqayv lygaaladrf gdpangrtpd ivvqpnpgvi
      481 ytsstkkdee hggnapddsh lgllvsypgv hrartvndlv gtkqvaptil gllgadprll
      541 qavvaentrv lpglgigr
//
LOCUS       WP_175873210             294 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia sp. BCC0397].
ACCESSION   WP_175873210
VERSION     WP_175873210.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..294
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31887
     Region          <9..294
                     /region_name="bifunc_ST_SDO"
                     /note="bifunctional sulfur transferase/dioxygenase Blh;
                     NF040641"
                     /db_xref="CDD:468609"
ORIGIN      
        1 msnapalsve gffdpathtv syllldtasr acalidsvld ydpksgrtht asadrliarv
       61 aelgatvhwl lethvhadhl saapylkarv ggriaigshv rrvqhvfgtl fnagpgfaed
      121 grqfdrlvdd gdtlalgalt iralhtpght pacmtycvdd atqraafvgd tlfmpdygta
      181 rcdfpggdar tlyrsiarvl alppdtrlyl chdyqpggrd vqfvttvaeq rranvhvkdg
      241 vteddfvamr tardatldmp vlmlpsvqvn mraghlpepe nngvrylkip ldai
//
LOCUS       WP_175873216            1059 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia sp. BCC0397].
ACCESSION   WP_175873216
VERSION     WP_175873216.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..1059
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115474
     Region          11..1037
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msvsheegrf nlsawalrhq alvvyliala tlagilaytr laqsedppft frvmvirtfw
       61 pgasarqvqe qvtdrigrkl qetpaidflr sysrpgesli fftmkdsapv kdvpetwyqi
      121 rkkvgdigyt lppgvqgpff ndefgdvytn iwtlegdgft paqlhdyadq lrtvllrvpg
      181 vgkvdyfgdp dqrifievnn aqltrlgisp qqlgqainaq ndissagvlt taddrvfvrp
      241 sgqfdnvgai adtliringr tfrlgdlatv rrgyddptvt qmrmagpgta gpgtngkavl
      301 gigvtmqpgg dvirlgkald aeskdlqaql pvglkltlvs smphavshsv ddfleavaea
      361 vaivlvvslv slglrtgmvv visipvvlav talfmylfdi glhkvslgtl vlalgllvdd
      421 aiiavemmav kleqgytrar aaafaytsta fpmltgtlvt vsgflpiala ksstgeytrs
      481 ifevsaiali aswfaavvli pllgfhmlpe rkrhaheahl pddhehdiyd trfyrrlrgw
      541 idwcierrfv vllitgalfv vammgfslvp qqffpssdrp ellvdlrlpe gasfaatlre
      601 terlekaidk rpeidhsvsf vgsgaprfyl pldqqlqlpn faqfvitaks vedreklatw
      661 lettlrdtfp avrwrlsrle ngppvgypvq frvsgdsiat vrsiaekvaa tmrgdartvn
      721 vqfdwdepae rsvrfeldqk karelnvtsq dvssflamtl sgttvtqyre rdkliavdlr
      781 apradrvdpa klaglalptp ngpvplgslg rftptleygv vwerdrqpti tvqsdvraga
      841 qgidvthavd aklntlraql pvgyqinigg sveesakaqt sinaqmplma iavftllmiq
      901 lqsfsrvlmv vltaplglig vvatlllfgq pfgfvamlgv iamfgiimrn svilvdqieq
      961 diavghgrvd aiigatvrrf rpitltaaaa vlalipllrs nffgpmatal mggitsatvl
     1021 tlfylpalya twfrvkrder dpqdgpppgg stpaapsga
//
LOCUS       WP_175873228             366 aa            linear   BCT 11-JAN-2025
DEFINITION  saccharopine dehydrogenase family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175873228
VERSION     WP_175873228.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..366
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40039
     Region          1..>43
                     /region_name="trkA"
                     /note="Trk system potassium transporter TrkA; PRK09496"
                     /db_xref="CDD:236541"
     Region          25..355
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mkiaivgagl ightiahmlr etgdyevvaf drdadalakl sregiatqrv dsadanaire
       61 avkgfdalvn alpyylavnv aaaakaagvh yfdltedvra thairelads sdrafmpqcg
      121 lapgfigiaa helvngfsev rdvkmrvgal peyptnalky nltwsvdgli neycqpceai
      181 rdgrkqwvqp leglehfsld gteyeafnts gglgtlcetl sgkvetldyk svrypghrel
      241 vqflledlrl stdrdtlksi mrravpstkq dvvlvfvtvt gvkdgqlvqd vftrkifakd
      301 vcgmhmsaiq ittagamcav ldlfrekklp qsgfipqekv slkaflsnrf gklyeggtme
      361 rmhava
//
LOCUS       WP_175873218             206 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175873218
VERSION     WP_175873218.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23165
     Region          9..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkpqrltreq srdqtrerll kaahriflkk gyvaasvedi aaaagytrga fysnfrsksd
       61 lllellernh aevqadfqai fegggtreqm esmalayyrt lfrddeysll wgeaklqaar
      121 dakfrvrfnq flhgkrvqma efiqrfaers gtplllpadt lafglmclcd gvqsyctadp
      181 qhvsvdvaes vlagffarvv lgrapd
//
LOCUS       WP_175873230             301 aa            linear   BCT 11-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175873230
VERSION     WP_175873230.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..301
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31378
     Region          75..281
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mtkrslaala asllmsvaai dglvapqlay aqasgsmtts dastpaaapa qattaaepap
       61 ppapatteav enpyglgalw kngdfvarfv lillvimsmg swyimvtkfv eqlranrrak
      121 ladaqlwsap slaegaklld easpfrfiae taieagehhd ealleavdrn twidvsvers
      181 itnvsnrmqd glaflatvgs tapfvglfgt vwgiyhalta igiagqasid kvagpvgeal
      241 imtaiglava vpavlgynfl vrrnksvmer vrnfgaqlht vllagskrpa rvpsaaaslv
      301 n
//
LOCUS       WP_175873254             290 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0397].
ACCESSION   WP_175873254
VERSION     WP_175873254.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 290)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..290
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30860
     Region          1..288
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mstlatgrap rdakawlvtp alafiaalfi ypfayglvls fqpmngggal anyvqfftdt
       61 amwptvlvtl klavpatlln vgiavpvafa lrrnspyqkf vttllvipvt lgtvlvadgm
      121 ltyfgpngwf pqalqglhly tdevrlthny wgvllslivs gfpfafllml syisgidptl
      181 araaatlgan pwqqfrqiyl pllvpgltma aclsfvqafs vfpsavllga pagptrvisi
      241 aaaeaafesy dyslasaiai vmsfvqllvv asmlgarrff ytgavtggkg
//
LOCUS       WP_175873255             362 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175873255
VERSION     WP_175873255.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 362)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..362
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39619
     Region          8..358
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkhsferlrl dgvcrsftna qgaqvaalng ldleirrgef iallgpsgcg kstalnciag
       61 lqpltrggiw lddtridvlp perrgfgmvf qnyalfphms vldnvgfglk mrgvpkqetr
      121 rrvqqalelv qlvghegklp gqlsggqqqr vaiaraivie pplvlmdepl snldtklrie
      181 mraeirriht qleratiyvt hdqdealsma drivvmkegv vqqvaspkdv ytrphnlhva
      241 rfmgyrnvls ftlegmagdy vnvasggvrl agvpmagfda kevvvalrpd dieraeegad
      301 nafdatvetv etveyggrds liraitpfga iwarvageft egeplrlrva partlvyagd
      361 vp
//
LOCUS       WP_175873263             310 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175873263
VERSION     WP_175873263.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5), 4725 (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10084616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..310
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=31565
     Region          1..>101
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          <198..286
                     /region_name="COG3945"
                     /note="Hemerythrin domain [General function prediction
                     only]"
                     /db_xref="CDD:443145"
ORIGIN      
        1 myrhllvtvd gapggidaig dalelaravg arvtfvlpaa spdsrlsgar lpehgakvea
       61 aaraqglsha iagagnpgag hpgagdaspg alaaelgcdl igvaalpvda daaacarrqq
      121 llatsgvpvl vcpshrapaa arviarclda hrmvgvllha lmasgdaaha pqrqavdvqr
      181 alaslaalqn erfgtadear lfaalrvrae cvaaeldeld rqrqrdaqal galarlaedg
      241 lpsaafdtal aryahgafeq mgrmegvifp aarrylgdad wagldeppad datapppgtn
      301 epadarrasd
//
LOCUS       WP_175873301             343 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia sp. BCC0397].
ACCESSION   WP_175873301
VERSION     WP_175873301.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..343
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37548
     Region          180..322
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mlaevrpdgf tmldtyrlaf adglfavrdg aeirvaqgdg igaqllraql gddgalrlva
       61 ynhraapadq rrallaalaa afsdsarhaa irldpaawpa valdalrasg vladggrclr
      121 dgwaqqadlw rvgpplpcat lptltdgrrh prrppaprgd vyardlpalg vrftlrgwqp
      181 aedaerlarw fdeprvrdgw pgaqpapcga egpqeadphv tslvgcfdge pfayfeafwl
      241 kedalaphva ardydrglrm lvgeprwrgp hrvagwlpsv vhylflddlr teavgcavpa
      301 ghtrvadhla rhgfarqrrl aladaqplwm rtlretffsg rhv
//
LOCUS       WP_175873319             422 aa            linear   BCT 11-JAN-2025
DEFINITION  YeaH/YhbH family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175873319
VERSION     WP_175873319.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11148708
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..422
                     /product="YeaH/YhbH family protein"
                     /calculated_mol_wt=48706
     Region          14..418
                     /region_name="DUF444"
                     /note="Protein of unknown function (DUF444); pfam04285"
                     /db_xref="CDD:427839"
     Site            order(254,317,344)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238119"
ORIGIN      
        1 mlhqiidrrl agknksianr erflrrvkny irravsdavr drsikdiqst qsitiprkdi
       61 aepnfrhapg grreyvhpgn edytrgdkip rpqggsgggg sqasnegegq ddfvfelsrd
      121 efmqyffddl elprlvkthl ltvpswknvr agwsaegtpn nidvvrslrs algrrialgs
      181 plvnelrele aqlevmksdp edrraeiatl eaeihhlkgr iwripfidpf dlryinrvkq
      241 pqpssqavmf clmdvsgsmd eqrkdlakrf fillylflkr nyerievvfi rhhtraeevd
      301 eetffhstes ggtvvssale lmrkvmnery sptewniyga qasdgdnwtd dspkcrkile
      361 ediltktryf ayiqvapeeq nlwleyaqla lsqphlamkk aesaadiypv frelfekqle
      421 ms
//
LOCUS       WP_175873322             339 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0397].
ACCESSION   WP_175873322
VERSION     WP_175873322.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..339
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34886
     Region          36..337
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtqppvsptd agaqqdvtgr rarmlsgtrl glsnylglag alaamialfs vlsshfltyd
       61 tfstianqip dlvvmsvgmt fvliiagidl svgsvlalaa smvsvaalkw qwgplpaali
      121 giavatatga ltgavtvgwr ipsfivslgv leaarglayq ltnsrtayig dafdflsnpi
      181 algispafli avavmiaaqf vltrtvfgry lvgigtneea vrlagvnprp ykilvfalmg
      241 alaglaslfq isrleaadpn agaglelqvi aavviggtsl mggrgsvist ffgvliisvl
      301 aaglaqigan eptkriitga vivvavvldt yrsrrtrvr
//
LOCUS       WP_175873390             321 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia sp. BCC0397].
ACCESSION   WP_175873390
VERSION     WP_175873390.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..321
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34675
     Region          11..224
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(52..53,55,69..71,77,79..80,121,223)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(52,54..55)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(77,80,83,90)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(113,117..120,122)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(118..119,142..144,196..197)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          237..321
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 msgatltvrv arkwqeardi cgfelvsddg sslphfdaga hidvhlpggl vrqyslcnhp
       61 eqrdryqiav lrdaegrggs raihdevrqg dtvrigmprn qfplasdaph hlllaggigv
      121 tpilsmaerl fsagmpfdmh ycarsadrma fverinaagf hdrarfhvdd gdpaqrfdla
      181 avlaaapegt hlyvcgprgf mdavlnaare rnwtdarlhy effggavats gadrafqvri
      241 assgkvidvp adctviaala angvdvltsc eqgvcgtcvt rvlegepdhr dayltddeka
      301 agdqfmpccs rsrtdllvid l
//
LOCUS       WP_175873392             248 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175873392
VERSION     WP_175873392.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..248
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27201
     Region          27..184
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtaapadtmt atakadradt prapagrksq qrvqdilrag revfaekgye hataaeiaqr
       61 vgvseatvfs yfrgkrelca rviadwydei iaafehgmpr dasvqqqfaf ivrthlrlml
      121 vngtglcalv lsegrakqha lsdeltalqr rytaplmdvl argqaagqvr adlplsllrs
      181 mvfgpmehvl wdailghrkl dtettatqli dmlwaavqpp apeqaalvrf rnevaeavrr
      241 legqasra
//
LOCUS       WP_175873410             208 aa            linear   BCT 11-JAN-2025
DEFINITION  trimeric intracellular cation channel family protein [Burkholderia
            sp. BCC0397].
ACCESSION   WP_175873410
VERSION     WP_175873410.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..208
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=21044
     Region          6..204
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mkrieqvvla adlagtavfa ieganaaiga gldlfgvmvl slvvalgggv irdlligarp
       61 psavsdwryp alafaaglfa fvfharvasf spsllttlda aglalfavag avkalefrvh
      121 pfiatlmgav tgcgggvvrd lllaripvvl vtdiyasaal fgavvvvscr rlgcppvvaa
      181 vlggvacfal rmaavrfgwq lpkiaegt
//
LOCUS       WP_175873434             392 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0397].
ACCESSION   WP_175873434
VERSION     WP_175873434.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 392)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..392
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39603
     Region          168..370
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mteraaasar rvtldkvgil iggltivavf glsfavlrpn riaagtglsv faalpamqga
       61 alaalwtvga lwamtasrpa wrlaagcagl atlayavgaa aahvvapddm larvspdagv
      121 wlllfawavl iadalarlaf gpwrrlaala vaiaavsvpl asgwwdglsv mreyavrsdd
      181 fwreairhvs laggsvaaal vagvplgiac ariatvrtva mpvlnivqti psiamyglmm
      241 aplgllaahv plaaalgirg igvapavlal flysllpias svvvglgqvp phvteaaram
      301 gmtraqrllr vdlvlalpvi lsgvrivlvq nigltavaal iggggfgtfi fqgigqsaad
      361 lvllgaipti alalaaavvf eaatslakgr ag
//
LOCUS       WP_175873445             776 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia sp. BCC0397].
ACCESSION   WP_175873445
VERSION     WP_175873445.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..776
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81999
     Region          73..739
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mirrpkaagr dgatrrgrra rcvgttlgal alfglppgsv raqqqadgaa ialpastvvl
       61 pavvvvgttp llgigtplsk vpanvqtvra aeldvqhrat ltdffaanlp svtisdaqgn
      121 pyqtdvnyrg ftaspllgtp qglsvfvdgv rvnepfgdvv nwdilptqai drvqlipgsn
      181 pvyglntlgg alaittkngk sspggeaevs ggawgrktas veqggtigpn ldyyatanva
      241 ndggwadhna srvrqafgkl ryidadttls iaaggadntl sgtqtiprsf lgnpkqayty
      301 pdrnrnsagy ltlsgdlffg ehvelsgnay yrhlrnants snnntdygsv dedgtvdtvq
      361 gsnaqstivt dsyggsvqlt llgklggman rlvagvsadv anssyvassq dasftdaraa
      421 igigefvrqt saktrnanvg vylsdalslt phwtltlsgr ydwskaqigd esgvqplldg
      481 nhvfsrfnpa vglnwnpvag ftayaayneg mrsptaiela cadpaapcsl pndfiadpal
      541 kpvisktfea gvrgrfgaat twsaaayrtt ltddiqfiss pasaqgyfrn vgdtrrqgie
      601 lagrtrlgpl gvglsysyvd atyrsswteh spansaadan gnvtvkpgdr ipgipahtvk
      661 lrldyeatpa wdiganvawr sgvyargden nadvngriag yvlvdldmry rvtkrfevfa
      721 svtnlfdkry vsfgalgqnf fngpnhtfdg ahpvneqfvg pgaprgewvg vryawd
//
LOCUS       WP_175873459              98 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175873459
VERSION     WP_175873459.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 98)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002085
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..98
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10306
     Region          1..98
                     /region_name="ManC"
                     /note="Mannose-6-phosphate isomerase, cupin superfamily
                     [Carbohydrate transport and metabolism]; COG0662"
                     /db_xref="CDD:440426"
ORIGIN      
        1 mslidfksva daqatawksm ivgevgpari kvlrmdaqpy eaevhdyneg llvldgtlml
       61 evdaetivvg agqmylarag tlhavlpgsh gtlaiidv
//
LOCUS       WP_175873499             205 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175873499
VERSION     WP_175873499.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22964
     Region          18..172
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkkplpsaap argpadhdvr dqivaaateh fsrygyektt vsdlakaigf skayiykffe
       61 skqaigemic anclheietd vrtavaeadl pteklrrmfk vfteaslrlf frdrklydia
      121 asaatenwqs vqayearvqk llqdvlqegr qngeferktp ldetataiyl vmrpylnpll
      181 lqynldttda apaqlsslvl rslap
//
LOCUS       WP_175873529             329 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175873529
VERSION     WP_175873529.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..329
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=35749
     Region          64..315
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mvgphdgrpy vdafpardsi vnatsprtwl ppyaarggaa paasavpdtr aaaqpaahaa
       61 pvgtpserll aidqvsleyr sgerivrath qvsfdvygsd rfvllgpsgc gkstllkaia
      121 gfiepvsgsi aldgrpvrgp gpdrivvfqe fdqlppwktv venvafplra aaklsraear
      181 eralhyldkv glgtfadayp htlsggmkqr vaiaralamq prvllmdepf aaldaltrrk
      241 mqeellrlwd efrftllfvt hsieealvvg nrilllsphp grvraelnsh ehsldnvdtg
      301 dfrdnvarih rllfdtdvph vpttedaas
//
LOCUS       WP_175873533             174 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia sp. BCC0397].
ACCESSION   WP_175873533
VERSION     WP_175873533.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 174)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 174)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..174
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17883
     Region          <27..159
                     /region_name="TsdA"
                     /note="Thiosulfate dehydrogenase TsdA, contains C-terminal
                     cytochrome c domain [Inorganic ion transport and
                     metabolism]; COG3258"
                     /db_xref="CDD:442489"
ORIGIN      
        1 mrkplaclla scamtsgtfg agfglgqpvd raalaawdid vapdgsdlpp gagtvarggh
       61 vfadkcamch gaggeggvgd plvggigsla sakpkktvgs ywpyattlfd yirrampyna
      121 pqslsaddvy avtayvlhln givpddarld artlprvqmp nrdgfvpdpr pgkl
//
LOCUS       WP_175873568             255 aa            linear   BCT 11-JAN-2025
DEFINITION  thioesterase II family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175873568
VERSION     WP_175873568.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..255
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27910
     Region          17..246
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 maadratpnp wfpsaiptag arlslfcvah agagasvfrd wcrplapaid vfavqlpgre
       61 srfdeephtr mdiaadeiaa amqpyldrpf alfghsmgga iafelaarle rkpvhlfvss
      121 wlpppparpr rfieratdaa lidsvsrygg mpdellrypd farafvrvlr admtlldayr
      181 pavvppgcpi tvlggaddpi vravelerwr ahervaavrv fpgghfylrd eqravldtig
      241 rqllgapadl qraal
//
LOCUS       WP_175873580             295 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            sp. BCC0397].
ACCESSION   WP_175873580
VERSION     WP_175873580.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..295
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30503
     Region          2..294
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mssfvihllt vgclyatmal glnlqagyag lvnfgfiafs glgayaagia sqlgwslpsa
       61 lalalaaaga laivvarlgr qlsadywgia tlaiaeilrt ialneswltg gaqgiggiap
      121 lfpglrapwa dlaflavtag cltltyatyr rltasrfgra lkvmreepal avcfgydpla
      181 lktraciaga lpaalagala awyigyvgpd amiasetfal wtvvmvgglg shmgvlvgtl
      241 ivqavyalap flkdwldvgs dltgavrlgl vglmllacvi wrphglvper levrp
//
LOCUS       WP_175873587             332 aa            linear   BCT 11-JAN-2025
DEFINITION  transketolase family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175873587
VERSION     WP_175873587.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..332
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35397
     Region          21..331
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mstvdnkprl ktsamiasia aegqatrsap fghaltelar tndnvigmta dlgkytdlhi
       61 fakafperyy qmgmaeqllm gaaagfaheg aqpfvttyav fatrraydfi hqaiaednld
      121 vklvcalpgl ttgygpshqa aedlalmram pnmavidpcd aldieqmvpa iaahkgpvya
      181 rllrgnvpav ldeydyrfel gkakllrdgn dvllissgim tmralevaka leadrvdvav
      241 lhvptikpld tativreaer ngrmvivaen httigglgea vatallgagv avpfrqialp
      301 daylaagalp tlhdrygisa gamranirsw lg
//
LOCUS       WP_175873611             221 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0397].
ACCESSION   WP_175873611
VERSION     WP_175873611.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..221
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22636
     Region          7..198
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtlhypllfa ylaaivllia tpgpvvmlvt gtvarrgfrq gvltavgana aslvmiagam
       61 lmvfgvvmvs arllaglhva gclfiavlai rtllgewrag rarggdgtva gepaagepvp
      121 qprglpgvvr gflvgianpk dllffvalfp qfvaitpdsr vslailaalw iavdftiltg
      181 ymaainhpai hrkqrwvvas salallaial aglgstlaga a
//
LOCUS       WP_175873622             141 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175873622
VERSION     WP_175873622.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..141
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15369
     Region          8..127
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mkpdqpdlsr haidlgllfl rvaasvlliv vhglpkivhy tteaaaiedp fhlgrtlsil
       61 faifaevvcp ifmivglypr laalpvmivt lvalvfvhpd wplrdaqfaw mllilfgtia
      121 iagagryvlp lplpgvmrrp s
//
LOCUS       WP_175873633             423 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia sp. BCC0397].
ACCESSION   WP_175873633
VERSION     WP_175873633.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..423
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45320
     Region          91..415
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdqpqhvriv glprsrdaya irdflqrrmi aydwceltsd adcaqalgia plrdirlpvv
       61 ifpdgsrlyq ptlaeiaarl gwvarprfve ydvsiygagp aglsaavyaa seglravvie
      121 rgavggqagt sslienymgf pdgipgaela erareqavkf gvelltmreg vhatfvdgki
      181 rveladgsil varanicatg ieyrslglpe esaflnaglf ygagsseapm cageqvfivg
      241 ggnsagqaam nfsrharqvt mlvrgaslad tlsrylidri ertpnievry rssvaalhgd
      301 gwldaielcs adgtrerlpa trlfvcigga pntdwakdtd iirnpggylv tggdlydcpa
      361 fervwplerr pyhletsvpg sfaagdvrsg svkrvasavg egamavtfvh rflgedahrl
      421 aga
//
LOCUS       WP_175873636             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175873636
VERSION     WP_175873636.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33067
     Region          7..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdtllsmrvf trivetgsft rasdttgltt prvsallsal eqhlgcrlln rttrrislte
       61 dgqayyersv avlreiddme asvsqarnvp rgrlkvnlpp amakqvvvpa lpafldahpg
      121 imielgvtdr qidlvgegvd cvvrigaldd sgmiarrigs lttctcgspa yfarcgepat
      181 vddlaqhlav shisadtgrp rvwdyvvdge privqmcgtv avndadnyie cgvagiglik
      241 tslylvepyl ksgrlrevlt gfnappkpis vlyppnrhip vklkvfvdwl aglfeqiptl
      301 qgkrg
//
LOCUS       WP_175873638             370 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia sp. BCC0397].
ACCESSION   WP_175873638
VERSION     WP_175873638.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..370
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39280
     Region          4..344
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,233,300,320,322..324)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,181,184,186,233,240,300,320,
                     322..323)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,181,184,186,323)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            186
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mssllsaynl rglalpnrvv mgpmtrsrap srglptelma eyyaqrasag livteatnvs
       61 rasaafeltp glvdeaqaag wkivtdavha nggrifaqlw hggrvssltl ldgaaplsps
      121 gvnddleqlq vwaqlqngyy tkihatpsra mttdevvatv defrqaaara maagfdgvei
      181 haangylphq flsstlnrrd dryggsvanr arfleeivda vggvmplsrv gvrispyaky
      241 nnvrdadpda tlayvgrmld aagvaylhaa dtngwsgepd lprivdharr sfhgtlivng
      301 gispdaanal idagdadlva farayianpd lveriaarap laepkaagwy ggdragyvdy
      361 arhdaaqsha
//
LOCUS       WP_175873640             637 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia sp. BCC0397].
ACCESSION   WP_175873640
VERSION     WP_175873640.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..637
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=67578
     Region          5..543
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mlratepars adlvvfngki atqdeqrsfv ralavkdgti vatgddrdvl rhahddttci
       61 dlngrtvipg lidahlqaih ggmnfnlevr wdgvpslada ldllgrqvrr tpapywarva
      121 ggwtalqfae krgptaaeln eiapdtpvfi qhlgdcawln aaalralgyg rdtpdppgge
      181 lrrdrhgrpt glllaradpa vlfaalarap mldaadrvns trqfmhalnr vgvtsaidag
      241 gdglaypddy aavatlarrg elttriayal garhagreld dfakwialta pgdgdaflra
      301 sgagarllcs avdlgnflep rvdlpasiev elaaivrllv hhrwpfrlha tydesigrfl
      361 dvfeavdrdt pfgglrwcfd rcetisdani arvaalgggi tvqprmafqg eafiarhgaa
      421 aatrappira mlaaglpvga gsgatgaasy npfvalywmv sgrsvggtal yparnrlgrm
      481 ealrrytvgs awfsadehrk galvpgryad favlsddyft vdarripalt svltvvdgkv
      541 vhaeqefspl apppppvspa wspvaaggvd daacadaasa dardaphasa agdacavpgi
      601 dacrarghgr rfarprypta saaaerceaf grccvaf
//
LOCUS       WP_175873643             348 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia sp. BCC0397].
ACCESSION   WP_175873643
VERSION     WP_175873643.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..348
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36763
     Region          68..319
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(82,165,167,169..170,197,251,272,275,288,290,319)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mrnmsrhacv ahaarlliva gcagllapaa faqagvqpda hanaqpeaqs tapapaagqq
       61 ppgfyrqkig dftvialsdg thpfpvdtvf rdiskdeirr dldraflepp vqgsinaflv
      121 dtgskrilvd agagtlygdc cgkllddlra agyapgqide vllthlhkdh vggiasngam
      181 tfpnavvrvn aveaaywldp ankaqapafl asffdaaaaa vapyvaagrf ktfrgeatla
      241 pgiravpmpg htpghtayli esghagllaw gdivhvaaiq lrdvnatvqy dsdagtarrt
      301 rrdtlkrvad rrylvgaahi afpglghlrr dgaqydwvpv nydatpvr
//
LOCUS       WP_175873703             557 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Burkholderia sp. BCC0397].
ACCESSION   WP_175873703
VERSION     WP_175873703.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60591
     Region          25..384
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          453..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mttqdllaqy gpresmeydv vivgggpagl saairlkqla aekgteigvc vlekgseiga
       61 hilsgavmdp raitelfpdw kergapldve vtedrflfls eksavttpnw alpenfknhg
      121 nyvislgnvt rwlgaqaeal gveifpgfpa aeilynddgs vkgvatgnmg vgkdgepten
      181 fqlgmelhak ytlfaegcrg hlgrqliskf kldanadpqa ygigikelwe idpakhkpgl
      241 vihtagwplk sdtyggsfly hmdnnqvvvg fvvglgytnp ylspfeefqr ykthpsiraf
      301 leggkrvsyg araitaggll slpktvfpgg aligddagfl nasrikgsha aiktgmlaad
      361 aafdavqagr qsdelnaypd afkqswlyte lyrarnfkqw makglylgtl mvgleqkvmg
      421 gnvpwtlhhq hadhemlkpa sqcepieypk pdgkltfdrl ssvfisntnh eenqpahltl
      481 kdasvpvnvn lrtyagpear fcpaavyefm knddgsdrlv inaqncvhck tcdikdptqn
      541 ivwvtpeggg gpnypnm
//
LOCUS       WP_175873717             200 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175873717
VERSION     WP_175873717.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22233
     Region          1..157
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrankrqlvv dkatelfsrh gfhpvgvdwi iddsgvarmt lyrhfaskde lirevlvqry
       61 dlivgsidaq lqhvvdpver iktifdwyaa wfrtpefagc lferalaefg tayapisnva
      121 iryrrkmvew iaeliealvp aetanrlatv fmmlldgatv earafndsaa aarawqaaha
      181 lleqamhata spadgtgspt
//
LOCUS       WP_175873726             424 aa            linear   BCT 11-JAN-2025
DEFINITION  NupC/NupG family nucleoside CNT transporter [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175873726
VERSION     WP_175873726.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Hirschi,M., Johnson,Z.L. and Lee,S.Y.
  TITLE     Visualizing multistep elevator-like transitions of a nucleoside
            transporter
  JOURNAL   Nature 545 (7652), 66-70 (2017)
   PUBMED   28424521
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Johnson,Z.L., Lee,J.H., Lee,K., Lee,M., Kwon,D.Y., Hong,J. and
            Lee,S.Y.
  TITLE     Structural basis of nucleoside and nucleoside drug selectivity by
            concentrative nucleoside transporters
  JOURNAL   Elife 3, e03604 (2014)
   PUBMED   25082345
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Munch-Petersen,A., Mygind,B., Nicolaisen,A. and Pihl,N.J.
  TITLE     Nucleoside transport in cells and membrane vesicles from
            Escherichia coli K12
  JOURNAL   J Biol Chem 254 (10), 3730-3737 (1979)
   PUBMED   374403
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..424
                     /product="NupC/NupG family nucleoside CNT transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005337 - nucleoside transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:1901642 - nucleoside transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=43934
     Region          1..422
                     /region_name="NupC"
                     /note="Nucleoside permease NupC [Nucleotide transport and
                     metabolism]; COG1972"
                     /db_xref="CDD:441575"
ORIGIN      
        1 mdilrsllgm lflllvayll snnrravstr tmiaalltqf aigalvlfvp sgrtalaaaa
       61 ngvnrvldmg nhgiafvfgg lvdarmfqlf gdggfvfglr vlpmiifvta lisvlyyigv
      121 mkwivailga glakvlgvsr ieacsavati flgqsempal vkpfvrnmts aeiftvmasg
      181 masvagsvlv gyaglgvkme yllaasfmav pggllfgkll fptvepsrvv vdgldfddkr
      241 aanvieaaas gasvglriai nvgamliafv glialmnlii sgaaafagfp qvtlvgiigh
      301 lfaplawiig vpwhdatlag nfigeklifn efvaygdlsp ylkggahaaa aglqvldpkt
      361 laivsfalcg fanfssiail aggfsavape rrsdvarlgl raltaatlsn lmsaaiaglf
      421 fslh
//
LOCUS       WP_175873737             123 aa            linear   BCT 11-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175873737
VERSION     WP_175873737.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629346
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..123
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=13475
     Region          8..114
                     /region_name="DUF4440"
                     /note="Domain of unknown function (DUF4440); pfam14534"
                     /db_xref="CDD:434023"
ORIGIN      
        1 mdairtviep cetalraaml andvealdal lddelvftvp tgqiiskedd laahrakllr
       61 ldtldvhemh araidemilt ttratlaghf dgtafagtfa ytrlwrrsda nwrvvaghas
      121 qvm
//
LOCUS       WP_175873770             532 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia sp. BCC0397].
ACCESSION   WP_175873770
VERSION     WP_175873770.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..532
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57957
     Region          1..449
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mkssiqrnig pfalmltglg siigsgwlfg awkaakiagp aaicawiiga vvilaialty
       61 aelgamfpes ggmvryarys hgslvgfisa wanwiaivsv ipieaeasiq ymstwpypwa
      121 halfvngelq tlglllsavl vvvyfmlnyw gvkafarant aitifkflip gltilglmlt
      181 sfhsenlgta snasfapygw savltavats givfafngfq spvnlagear npsrsvpfav
      241 itsillalvi yvllqmayig svnpadvakg wahfnfsspf aelaialnln wlaillyvda
      301 fispsgtgtt ymatttrmiy amernntmpk mfgnvhpiyg vprqamwfnl lvsfvflfff
      361 rgwsslaavi svatvisylt gpislmalrr aatdierpls iplmkliapf afvcaslily
      421 wakwpltgei illmivalpv yfyfqaksgw tgwgadlkaa wwlvaylptm avlsligske
      481 fgghgvlpyg wdmlivaais lvfyfwgvnt gyrtqylder esheeilegv gv
//
LOCUS       WP_175873783             316 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175873783
VERSION     WP_175873783.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..316
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32665
     Region          32..314
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          211..314
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(216..217,250..251,254,258..259,262,304,308)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mqrtiqvrra rwsaavspal aalfaaglva sgaafaqntg atvtpvgngt vattalpqan
       61 pnaggasgtv vhgtagtiap ppanaapgqv vvggkvpdea tkaavlqklr dtygatnvvd
      121 qvevgdvatp pnwsanvqkl lgaqlkqisk gqlkingtqi emkgevhnea qrqqlasdma
      181 ntlnptytik nglrvsaseq gvldqtlanr tiefetgsat ltpqgkqild qmaaalakmq
      241 nrtvdiight dnsgnrtsni alsqaradav kgylitksip pqqmtttgvg pdqpiapndt
      301 adgrarnrri efrvgq
//
LOCUS       WP_175873797            1055 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175873797
VERSION     WP_175873797.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..1055
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=111595
     Region          14..827
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnmqntiaal rggllqqdrl lkldtplggn vltvqravgh srigrayeft ldvlstdsdl
       61 elkkliaqpv tlwiqqgdrs yrpvngyvht arrlgadggl ttyqltfadf thflkfrrdq
      121 riwndttveq iisdvldqhp qakghfrfal skplpnrsyt rqhdtdwhfv hrlmedegly
      181 cawqqaddgk shtlvitdnl hafaplspea vrfyhggaas eadaftqwsg trtlqsvtrs
      241 trtfdyknps qpsnpkgtsl ptmggqgelp dqlevyeytg aytyldqtrg dhltkvkmee
      301 wesqakrfhg vggvraidag rrftlsdhpe hdrdpadqre faaigvewwi ennlpvasgs
      361 adfpyslrea ltqaqegyga dpafrvphdd gstgfylvev eaqrvsvpyr spfehkkpem
      421 hletaivvgp qgeevytdel nrirvqfvwd rlnpgnenas cwvrvvqsdt gggyggvhvp
      481 rigeevlidy vggdcdrpla vgrvynganq pqwhsdgils gyrskeysgg gynqlvmdda
      541 tgqnrvqlms ssansllhlg yiidqsgnsr gsylgsgfdl rsdaygavra sqglyvtthp
      601 kaqnsqpldv keaqqqlvtg eslveamsgv seqhqaeslk eahdtmraft datqdsksgs
      661 aaggrtaggg tgsanafkep vmlfgspsgi gmstqqslhm vandhvnvas gqsvhvaagk
      721 sligsigqkl slfvqnagmk lfagkgkvev qaqsdnievt aqkavkvvsa tgqieiaadq
      781 gilltsgggy iriqggniei htpgavdvkg ashtfagpas mgyplpsprp dqpgqlelfh
      841 kyvngeavkg glftvkdvng svlkkgaldn sgytvvsglp pgavrvefgk dpresdqpan
      901 yfkqakwpae pvesspeaaq aaatgqlasq lqgmapaaat aamglvsggg agaalgglas
      961 salpaaagal ggagavsalq tassmagaak qvagmvqaar qgglaalaap vanaasgalp
     1021 gvagiagkga atvasaagat gmklptsgfg gplks
//
LOCUS       WP_175873839             123 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175873839
VERSION     WP_175873839.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..123
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=13088
     Region          9..106
                     /region_name="DoxX_2"
                     /note="DoxX-like family; pfam13564"
                     /db_xref="CDD:433313"
ORIGIN      
        1 mskmswrqvl plllaaffva gslsniiapr siideylkwg yppgfhfvtg slelmtafll
       61 arartrlwgs vlgctvmlaa latvtlhgey ghgvaplvaa tlsgavgwia wrerfavgsg
      121 ara
//
LOCUS       WP_175873857             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175873857
VERSION     WP_175873857.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33779
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..291
                     /region_name="PBP2_CrgA_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08475"
                     /db_xref="CDD:176164"
     Site            order(103,107,146,161,163,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176164"
     Site            order(104..105,109..110,112..113,116,120,122..128,190,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176164"
ORIGIN      
        1 mtdrldgvtt fvqvvesgsf alaaerldmt rsavgkaiar lekrlgarll qrttrsqslt
       61 ddgqayydrc vralaeleaa eadldcgrhe argklrlsvp lafghhcvtp ivldlartyp
      121 hlridvsitd rfvdlveegi dlavrigtla dstslavrrl gtqygslgaa psylaryemp
      181 ktlddlkhhr tiaysrsgvv qpwdlrapdg stvridmphq lsfddvqaia aagasgfgia
      241 wlpswlldhy vkrgemvvvl drcfvcegdi halwpktryl prktrcvida laeaippmie
      301 radear
//
LOCUS       WP_175873871             632 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Burkholderia sp. BCC0397].
ACCESSION   WP_175873871
VERSION     WP_175873871.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..632
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=67488
     Region          8..632
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mpqpfvlpat agrtdllaqa harstavglr aherpdfspl srlalralld tnhtlfshar
       61 pvmedlhaqi aetqslvllt dadgvilhsi gdadfiekan rvalcngvsw aegargtnai
      121 gtalasgqav vvhgsehflr anhiltcaca pivdpfgrtl gtldvsgdpr gssphtlalv
      181 rmsaqlienh lfanqcgeal rlrfhahedc vdslfaglva fgpdggliaa nrsaqfqlga
      241 sfdalqhqas dalfgmrfgq laqqaarapg atfrltlstg vrvlarcefp eaqkttvavt
      301 ppapaarvra pdpdaitfat ldtgdarmaa vlervakirg rdlpllilgq tgtgkewlar
      361 alhqasprad gpfvavncaa lpdslieael fgyedgaftg arkrgspgki vqadggtlfl
      421 deigdmplaq qvrlmrvlqe ravmplggar avpvdvrvvc athrdlrami adgtfredlf
      481 yringlavtl palaartdlp alverilarl arsepmprrl aadvldafar hrwpgnlrqm
      541 tnvlrtagml sedeaeitla hlpddfwldc ddapaapaal tpsagkregt tlqshqaami
      601 davlarhggn vsaaarelgl arntvyrylr rh
//
LOCUS       WP_175873858             379 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175873858
VERSION     WP_175873858.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..379
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41719
     Region          26..362
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 mstpvtnhda faehapevly rvvnrvalit lnrpaalnal syamigelaa lfercrhddq
       61 ivavvlrgag ekgfcaggdv ralykmvaqr etwlpffvde yrldyaihtf pkpvvalmdg
      121 vtmgggmgla qgaalrvate rskiampetr iglvpdvgat hflsgmptel elyvgltgam
      181 lsgadalsak ladlcvpsaw ldtfetries vkwdgdvlpa lrrvfeppcn vvshaaldgq
      241 mpwivrhfdk rstverivat ltqdlardel arehrqwlqa tldalashsp tmlavtreal
      301 lrgrqmtlae sfrmelgiva raieegdfre gvrahlvdkd rkprwapasl velraervrh
      361 fltspwklfa hpladlgaa
//
LOCUS       WP_175873905             706 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175873905
VERSION     WP_175873905.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..706
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=77284
     Region          86..>678
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msfapnggip nglgggalgs lsalgglagp iassvagslg plaglaghvd tvqramqlaq
       61 tgfslmdktp gaiaeainga anparltqln ryvtldtplg pdvllvsaav vdehvnrlpe
      121 ihldllshrh dlrpedligq qvkirfdqqa rlstlervva sgtgdndryf dgyvasfdra
      181 gnpgnvtqyh ltavpwfwfl trstdcrifq nktaqdilte ifqehgfadf vfdirtsqkp
      241 leyvvmyqes yynfcarlme qeglvwthry ekdkhflvig dtnllfrpid glatvpfaat
      301 easedsgidq lhegrrfgvg kvtfrdfnhq npssplmlve agpqnlkhar ldaterfehq
      361 slydhgddgn ryarfameae eaqahrytgg gyawrmttag avnvanhpvl ennqeyvilh
      421 vrheavndyt qhsaelpyrn sfsllpkkip yrapratpkp vihgtqsaiv vgpkgeeiyt
      481 ngsavkvnfp wdrrgkkdgs dsmwvrvsqp wagdgwgaaa iprikqevlv afnqgdpdnp
      541 vivgrvfnge qgnpyhgaag qtmgiksqth kgqgsnellm sdvngaqmly mhaqkdmhtv
      601 vedaqwtqvl kgdrtvevgk gnhttaiavg nlsdvvvqgn tlhqtpqgvh tleakelwik
      661 iggdggtrih mtadsidiyk gesvihldds niniqaartd inpkng
//
LOCUS       WP_175873952             388 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Burkholderia sp. BCC0397].
ACCESSION   WP_175873952
VERSION     WP_175873952.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..388
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40009
     Region          60..368
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mntikridpr rpfiitaagl kritlgeegs adanaaqwsa hghgaaakpr ralqdpkhvm
       61 lvvahserga lddhsrqaia aaavladaqt evallafgel kddvaelgvd kllelagfer
      121 rafdpeselq alqacvaala pkhvfvpdna tgdgdlgrry aaaagasvat hvveidakhv
      181 gayaqagraf atralpdvvl laqnaveakl pfvgagerva adfirpahda aqpyrdlgld
      241 eidaaqvale eadfivsagn gvsdigafer lagvfgaaig asrvavdngh ftrdkqvgat
      301 gktveasvyi afgisgavqh lqgikdcrhv iavnldgsap iakranltvv gdaqatiaal
      361 ieqvqaaraa rgespaavgt repegvaa
//
LOCUS       WP_175873983             162 aa            linear   BCT 11-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175873983
VERSION     WP_175873983.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..162
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=17113
     Region          62..162
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mkdspnnsvi rtisrspvlv salltcslty iagvfvwggq fvfglplgps sgalpeivky
       61 dlltrlfvgs laapivetfl fqwlpirlir rtfggsawsa tgasalvfga ahgysvlyva
      121 valwgglifa tvfvlrdypg grpflvvata haarntlasi li
//
LOCUS       WP_175873978             376 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia sp. BCC0397].
ACCESSION   WP_175873978
VERSION     WP_175873978.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..376
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=40680
     Region          7..376
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkrktlalsi aaaglcagpq ahaqssvqly glmdlsfpty rthadangkh vigmgnegep
       61 wfsgsrwglk gaedigggtk iifrlesefv vangqmedeg qifdrdawvg vederfgklt
      121 agfqntiard aatiygdayg saklsteegg wtnsnnfkqm ifyaagptgt rynngvawkk
      181 lfsngifasa gyqfsnstsf atgsayqaal gynggpfnvs gfynhvnhng frnqtfsvgg
      241 nytfsivrln agyfryngdq galgqrhdds wtvsmkiapk galdyelgyq qmriknaann
      301 adgftpnanl gafsltngva ngfketiygs vfyhlskrte vylagdymkl hggytvsstf
      361 gaknqlelts girtrf
//
LOCUS       WP_175874001             404 aa            linear   BCT 11-JAN-2025
DEFINITION  cation:proton antiporter [Burkholderia sp. BCC0397].
ACCESSION   WP_175874001
VERSION     WP_175874001.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..404
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43640
     Region          13..390
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mksafsflpn wplapdavfw aglalfaagl cgelcyrawr lpritgyavi gliagsfgfg
       61 vidtstdets rllmnvalgl llfelgsrld lrwirrnpwl vasslaeatl tfvlvlfvml
      121 algvsgmval vlsaiaiats psmviqlkte lraegqvsqr litltalnsv yaivltklvt
      181 swlhqeaygn vfatilqply llagsfivay lvarscnylf rhmnatmrde hsfvalfglv
      241 mlaiavaqal klstlltlll agiivknlea rpqlwpehfg tagwlltvvl fvltltsftw
      301 gdialgglla ivlivtrlaa klagvvafak psglgmkqgv algialtpms alsyllvddt
      361 yqlypnfdph lraivmcsiv ilqlvspfvv yrclsavger sdsn
//
LOCUS       WP_175874028             190 aa            linear   BCT 11-JAN-2025
DEFINITION  PadR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175874028
VERSION     WP_175874028.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 190)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..190
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=21159
     Region          5..97
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mstsrpspla lavlatltet pmhpygmlqq lkargydevv nvrqrtslyq tidrllrdgl
       61 itvhdterdg afpertlyal teaghtagqa wlhallaepa refpafgagl aflplldaed
      121 arhqleqria rldaererle alrataqadq vprlfllqne halvllnael dwarsvvehl
      181 kigalrwvdg
//
LOCUS       WP_175874112             133 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175874112
VERSION     WP_175874112.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..133
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=13699
     Region          59..>132
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mkvfqlqars prirrqralr tgmavaiaaa tacvvvapna vaagddaass smssshsstg
       61 tkirdatitt kakaelvgts glsagdihvk trhgtvtltg svpdeqqrtq avgvvkqvdg
      121 vhsvrdqlti rpk
//
LOCUS       WP_175874135             149 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175874135
VERSION     WP_175874135.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..149
                     /product="RidA family protein"
                     /calculated_mol_wt=16513
     Region          28..137
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 msqpthtrir mfntkdtypn qtldndlcqa vragntvyvr gqvgtdfdgn liglgdaraq
       61 aeqamknvkq lleeagsdit hvvktttyli dpryrepvyq evgkwlkgvy pistglvvsa
      121 lgqpqwlmei dviavipdnw qpnhaqeat
//
LOCUS       WP_175874154             185 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Burkholderia sp. BCC0397].
ACCESSION   WP_175874154
VERSION     WP_175874154.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..185
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21301
     Region          1..185
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mttsnqhaap tpessaqqld rtwremqgkl rrrarllckg dihradells dtalkvhiyl
       61 qrspervrnl sgflflalnh afldgarrrl resgmlefdp awdddhavel aghapsveqh
      121 lllrqqllrl eqalsmlspq qqmlftlkfe edrpylhiaa tlgineplar krvellrkkl
      181 reela
//
LOCUS       WP_175874170             159 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175874170
VERSION     WP_175874170.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..159
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16874
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 myekimvavd gsassrqala eavkvalagd thvsvvyvvd ksvlftyagr ldphalveei
       61 rddgrkvlre aeqiialaga kgeaelvete sigediaerl qryvkergid lavvgthgrr
      121 girrvllgsv aerfvrgakc pvllirgdda dapvaaaaa
//
LOCUS       WP_175874180             214 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator transcription factor [Burkholderia sp. BCC0397].
ACCESSION   WP_175874180
VERSION     WP_175874180.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..214
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23597
     Region          9..204
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mdaesqspiv yivdddedmr tslswllasv kiqahcyrgp aeflaqfdps vpgcmvldvr
       61 mpevsgfdlq aelnrrgvsl piifvsghgd ipmsvralqn gaidfvekpy nsqqmleriq
      121 rairvasdth qenqhrqami qriraltpre revlngvieg kaskliarel gitaktvdvy
      181 rasikeklga ssiasllkdv ieaqfamagq qppv
//
LOCUS       WP_175874129             950 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175874129
VERSION     WP_175874129.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 950)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 950)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 950)
  AUTHORS   Ingmer,H., Vogensen,F.K., Hammer,K. and Kilstrup,M.
  TITLE     Disruption and analysis of the clpB, clpC, and clpE genes in
            Lactococcus lactis: ClpE, a new Clp family in gram-positive
            bacteria
  JOURNAL   J Bacteriol 181 (7), 2075-2083 (1999)
   PUBMED   10094684
REFERENCE   4  (residues 1 to 950)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11909043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..950
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..950
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103716
     Region          4..>54
                     /region_name="McsA"
                     /note="Protein-arginine kinase activator protein McsA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3880"
                     /db_xref="CDD:443088"
     Region          83..877
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mpalcdicha rpavaratvm qdgerktisi cdyhfrqlmr hqsmlnpfds llggggpssl
       61 fgglgdespl aaeipresvd ptdafseqtl ellqraaeka helrrselds ehllyaladt
      121 dvcaallkel klspediksy idahahtgta dpdapldkls isprvkkavq yafqasrdlg
      181 hsyigpehll iglasvpdsv agtllkkygv tpealrqkvv kvvgkgaedg rvdaptgtpn
      241 ldkfgrdlta iarqgkldpv lgraqeiest ievlarrkkn npvligepgv gktaivegla
      301 qrivngdvpe vlrnkrlvev ninsmvagak yrgefeerak qlidevtakq delilfidel
      361 htivgagqgg geggldianv lkpalargel sligattlne yqkyiekdaa lerrfqpvfv
      421 pepsveqtiv ilrglrdsle ahhqvtfadd afvaaaefad ryitsrflpd kaidlidqaa
      481 arvrigatsr pidiqegeaq iaqlkreqdy atsrkrfdea kqfeeqinaq qkavdemmea
      541 wqrktgsetl evtvesvaev vsrltgipvs eltqeerqkl lkmeeqlrer vvgqsdavva
      601 vsdavrlsra glgqthrpia tflflgptgv gktelakala etvfgdeqai iridmseyme
      661 rhavarliga ppgyvgydeg gqltervrrr pysvilldei ekahpdvynv llqvfddgrl
      721 tdgkgrvvdf sntiiiatsn lgaaiimdnl tqpeaarktd kaireelmqv lkghfrpefl
      781 nridevivfh alskddirai vqiqldrvvr taaaqditlv mgdslvahlt eagyqpefga
      841 relkrqirqt ietklakeil adrlksgdkc evdydkdsde vkfntlaape akeakdttda
      901 kqdadgkpka ngkaakaagd akpddapada pppaakpsgk kssgakkdah
//
LOCUS       WP_175874215             252 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia sp. BCC0397].
ACCESSION   WP_175874215
VERSION     WP_175874215.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..252
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26252
     Region          1..245
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 msvskkfaav tgagsgigra aaialaqagf tvallgrtea slretqdair aagsdaqvfp
       61 vdvtdetsvd hafaqiaqqf grldvlfnna grnapvvsld dyeldvwnsv vatnltgvfl
      121 caraawrlmk tqtpqggrii nngsisahap rpdtiaytat khavtgitks laldgrryni
      181 acgqidigna atsltermtq gvpqadgsla pearmdvahv anavvqmanl pldtnilnmt
      241 imatampfvg rg
//
LOCUS       WP_175874242             413 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175874242
VERSION     WP_175874242.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..413
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45184
     Region          69..387
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mtlneswltp lvgilvllaa agaitavvhf llfrvvarla rlsatrvdda lfefgafkwl
       61 nrivpfvvik lglgavpgip tvaaqvvdkv lfalivflvt mtisatlsal ehthrttqrd
      121 qprlslkgam qlvklvmfit aalvvigdat gkqiglllsg igamsavlml ifkdtllglv
      181 agvqlssndm lrigdwitmp sagadgtvid itlntvkvan fdhtiitvpt wklitesyqn
      241 wrgmteaggr rikralfvda tsvrfltnde ierlerltll kdyledkvda ieqwngtlga
      301 agdcpanrrq ltnlgtfray vanylkghpr irgdmtnmar qlpltaegip lelycftdtt
      361 twvdyetiqa dlfdhliavl pefglrvyqh psgfdmrqmv daaqaglhap raa
//
LOCUS       WP_175874244             199 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0397].
ACCESSION   WP_175874244
VERSION     WP_175874244.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..199
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20531
     Region          1..198
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mplhdylplv lfvivstvtp ggattlatas gahfgyrrsl plmagiaagl asmaaaaaag
       61 lggvllalpa lqlamkavgs aylmwlavri grggkprldv dvhrpqgfvs gvwmlwhnpk
      121 gwamtlgaaa sfaalasgpa rlgvllgfaf gvaamaslsl wcfagllfar vlrterqwrc
      181 lnaglglllv asivpmwlp
//
LOCUS       WP_175874251             554 aa            linear   BCT 11-JAN-2025
DEFINITION  S8 family peptidase [Burkholderia sp. BCC0397].
ACCESSION   WP_175874251
VERSION     WP_175874251.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..554
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55593
     Region          241..521
                     /region_name="Peptidases_S8_13"
                     /note="Peptidase S8 family domain, uncharacterized
                     subfamily 13; cd07496"
                     /db_xref="CDD:173820"
     Site            order(248,317,321,388..390,416,418..419,489)
                     /site_type="active"
                     /db_xref="CDD:173820"
     Site            order(248,317,489)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173820"
ORIGIN      
        1 mkakrfnfal arpaharmla gmlsaaallp lagcgggggd gsnpsssnaa papapaptpt
       61 ptpapapttp pvssgtnact sqqaavqmaa qtapveppvd hlivklktlt atramaaidn
      121 gsrldaviqr amtrwmapvt gsarayastv pqtpvnvqve rtisngaavl slgqrmaatd
      181 aaalaqafaa dsdvdyaepd hpmqirdtps dplynqqwyl sdatagidlp pawnvtkgsp
      241 tvvtavldtg yrphgdltgn liqqgysfis nvntsnnglt rssdatdpgd wvtqqeldna
      301 sgpfyhcasq psnsswhgtr vmgvigatan ngagvagvsw lskilpvrvl gkcggvtsdi
      361 adgmrwaagi pvngvpnnpn pakiinlslg gvgacsttfq qaiddvtakg vtvvvaagnd
      421 glstgldqpa ncrgvitvga tdatgrrasf snfgadvsls apgvnilsts ntgtttpgsd
      481 tyglangtsl aapqvtgvaa lmlsvngnlt paqvlqklqg gtraaklaag tsctalpags
      541 gildagaava tanq
//
LOCUS       WP_175874280             834 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175874280
VERSION     WP_175874280.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..834
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=91708
     Region          15..799
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mvsdllnkal rtqyvqhgri vrldtplged wlvplyvrgr aclgrdfeft idatstrlet
       61 iqakalirqs vtlwirqmdg sempihgyvt afsrlggdga ntyyqlrfns flallrlgsd
      121 rrdwietpaq qtisdvlgky pqaagnfswq lrqalrsysq rmqwesdwny vhrtfeelgl
      181 fprfdiaqdg kshkvvimdd lfsvpelkhk tisfsrsvqd eefdglsewi dsqeiqsael
      241 dtgtfdykrp dlskhvtmpa fdlddvpglg eqyeytgaht wsdrdmgetq anfiaeewrs
      301 raqrfhgvga lrcawpgryg vltghpvhdg qseqdremai lsvnwliqnn vpglenlmrf
      361 rksvrteveq arangtgssv rhddggvgff hveieaqrrc vafrspfehk kpvmqlqtgi
      421 vggpeneeiy tdamlrakvr ltsdrlndgd qnvsawiraa mpdaghkrgg mfplrkndev
      481 ligfingdcd rpvilsrmhg gesmpewhth gltsgllsre yggegynqlm mddasgqnrv
      541 hlystsyssh lhlgyliqhs gntrgafigq gfdlkslgyg alraeqglyv stqpaatqpl
      601 svtaaseqlt raeamlatts kasqtnraqs qqdghdalkt ftdatqhpva grtkggrtag
      661 ggtgnangfa kpimllsspe giaastqgsa hitankqtnv vagedinlaa grallasvle
      721 qislfaeklg vkiyaasgpi dlqaqndsms laasqdvkit agkkmylsad eiwigangsy
      781 ikltanmien atsgqivekc anwekagaas gtlknplhss pvsadggrft lfsg
//
LOCUS       WP_175874314             192 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175874314
VERSION     WP_175874314.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20239
     Region          26..159
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 marprspdkh eailaaaara laedgatatt sriarlagva egtvftyfet kdallnalyl
       61 slkaelream mtgfpehapa eqavrhawng yvswgvanpd grralqqlgv sgriddahra
      121 agaegfggig tllheqvaas galdrdeaha fcaalftsia etamesiard paradayrea
      181 gfralwavlh av
//
LOCUS       WP_175874323             462 aa            linear   BCT 11-JAN-2025
DEFINITION  NCS2 family permease [Burkholderia sp. BCC0397].
ACCESSION   WP_175874323
VERSION     WP_175874323.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..462
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46746
     Region          22..457
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 msdtpvqptv gvgaeetdfg ttgvidryfg isargstqrr eiiagvttfl amvysvfvvp
       61 gmfgkagfdt savfvavclt tafgsllmgl waklpiaigc aisltaftaf glvlgkglpp
      121 tvalgavflm glvftgisvt gvrswilrnl pagvahgtgi giglflllia sndvglvikn
      181 pgaglpvslg qitafpvims vvglaaifgl ekrrvpggil lvvvaislig lvfdpavkyr
      241 gifalpslsa pghasligam dikgalsmav lpsvlalvmt avfdatgtir avagqagqld
      301 engriinggr altadsvssi fsgflggapa aayiessvgv aagaktglaa avvgllflvv
      361 mffsplaglv psyatapalm yvgllmlgsv sklhmddmvd amsglvcavf ivltanivtg
      421 imlgfstlvi grlasgefrk lnvgtvliaa vlvtfylggw ai
//
LOCUS       WP_175874339             712 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia sp. BCC0397].
ACCESSION   WP_175874339
VERSION     WP_175874339.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..712
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=76778
     Region          53..642
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mtdptanppp ppappsappr rrrvwrtlag allglalaca gigawtidri wtqlpsvehl
       61 avyrpalplr ifsrdgdlla eygverrefv pleripplmr hallaaedak fyehgpvdvg
      121 glaratfanv vtgqpgqggs titmqvarnf yltrdkvlsr klaeilmaak lereyskdkl
      181 lelymneiyl geraygfaaa ahvyfgkpld alsageaavl aglpkapsaf npvvnparat
      241 arrnyvlgrm halgqldevt yraavdapia lattpppgiv aapyvaerar rmmverfhdd
      301 aytlgldvtt tismrdqraa eaalertlsr qprakreart glegalvsld vatgdmlalv
      361 ggadfnrnvf dhalqayrqp gssfkpfvys aalekgyfpg vlvddtqrtl thaetgarpw
      421 rprnfgnrye gfipvrrglv rsknlvavsl mqatdaryvq qhavhfgfda qrnpaslpla
      481 lgagavtple lasaysvfan ggtrmeprli lsvkqrhgga myeatvpage rvvsarnafv
      541 mdsmlrdvvr agtargalal rrddaagktg tsngskdvwf agyssgivav awlgydtprp
      601 mgratgatla lpvwldymkt avdgrtplda tppqdvalvd gdfvyaeytr gtctadvpay
      661 irsrfacgga aavdapdapn apagngkrde pmpaavdaae rervldlfrt dd
//
LOCUS       WP_175874367             187 aa            linear   BCT 11-JAN-2025
DEFINITION  RHS repeat domain-containing protein [Burkholderia sp. BCC0397].
ACCESSION   WP_175874367
VERSION     WP_175874367.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..187
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20239
     Region          <9..142
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mgdannyeqy awdasgnlia lrkcngqvvv qsfdalnrlv srtfpggvgn vqynydlrgl
       61 ktasqfgdgs htiinsydgl gqltqtsagg ktlryrydaa snvidvawpd gfhvstqydg
      121 fgrpsqllen gtaslakysy dapnrragsp vhaqpvgrhy aierdgslrs flkpslmcar
      181 lrpastp
//
LOCUS       WP_175874398             196 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia sp. BCC0397].
ACCESSION   WP_175874398
VERSION     WP_175874398.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008163
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..196
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=20919
     Region          11..184
                     /region_name="COG3963"
                     /note="Phosphatidylethanolamine N-methyltransferase [Lipid
                     transport and metabolism]"
                     /db_xref="CDD:443163"
ORIGIN      
        1 mtwpnawrvs alfvrewvgr paavgalcps srhlaremad tvpdgdglvv elgggtgait
       61 aallergvap rrlvvversp afvqhlrrrf pgisivsgda rqlerllppg atvdaivscl
      121 plrtlprqdv taivdqcqrv lsadgvmiqf tydlrppgrh plgdsafvac dsrivwanlp
      181 parivtvrca aaayag
//
LOCUS       WP_175874414             283 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175874414
VERSION     WP_175874414.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..283
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31031
     Region          111..271
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mllnvnsfhr dnnrfnvsfk algelietvg tphfvprltq llndivpldv ahversrvdg
       61 tmptgyrcew igssgigaas teisdvmtly yerfldsdpl faglrgktgt mlvvrdiaai
      121 ppgefrqrlf ddvhighecv largtrysqh sialergrdr ppftlaemnr frnisdvlfp
      181 llelhastta arriahappd vhplaqfdar laadgvklsk reyetckhll sgktvpetag
      241 ilgvrvasae syvkrafakl gvrtkrelaa wgsaatalps agt
//
LOCUS       WP_175874421            1068 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia sp. BCC0397].
ACCESSION   WP_175874421
VERSION     WP_175874421.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..1068
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=114561
     Region          1..1046
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 miariihwsv hhrflvllat vllaawgvhs lrqtpldalp dlsdtqvivk asypgkapqv
       61 vedqvtyplt ttllgvpgak tvrayssfgd afvyvlfddh tdpywarsrv leylsqvqsr
      121 lpagatvslg pdatgvgwvy eyalvdrtgr hdlgqlraln dwflkfelka vpdvsevasi
      181 ggmvrqyqvv ldpdklrayg itqaavadal akanqasggs vvelaeseym vrssgylrtl
      241 ddfrhvvlrt ddtgtpvllg dvariqvgpa mrrgiaelng qgevtggvvv mrsgknaltt
      301 idavkaklad lkrslpagve ivttydrsql iaravdnltd klieefvivg ivcavflfhl
      361 rsalvailsl plgvlaafiv mryqgvnanl mslggiaiai gamidaaivm ienahkhlea
      421 ydrahpgepi taarrwelva asavevgpal ffslliitls fvpvfslegq egklfaplaf
      481 tktytiaaaa glsvtlvpvl mgylvrgrip hehanpinrv lirlyrplle atlrrpwaai
      541 gvavvalvlt avplsrlgge fmppldegdl lymptalpgi sadkasellq qtdrliktvp
      601 evdtvfgksg radtatdpap lemfettirf kprsawrpgm tpeklvdeld rtvkvpglsn
      661 vwvppirnrl dmlstgiktp vgvkisgpdl agidaiatqv eaavkrvpgv tsalaerlng
      721 gryidvdidr laaaryglsv adiqavvssa iggedigevi agrerfpini rypreirdsl
      781 enlrqlpivt argaqirlgd vahvaiadgp pmirsenarl sgyvyvdlrg adlstavram
      841 qqavarqval ppgysiawsg qfeyleraaa tlrtvvpvtl vvifvllfvt fdsaadalll
      901 mstvpfalvg gfwlvwalgh avsvatsvgf ialagvaaef gvvmllylkg alqrrldage
      961 pltdalllda iregavlrvr pkamtvavvl aglvpimigh gagsevmqri aapmvggmvt
     1021 apllsmfvip aawlllqrrr arsagrtrhs davpsgtnvp siptgesr
//
LOCUS       WP_175874422             336 aa            linear   BCT 11-JAN-2025
DEFINITION  sodium:calcium antiporter [Burkholderia sp. BCC0397].
ACCESSION   WP_175874422
VERSION     WP_175874422.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schnetkamp,P.P.
  TITLE     The SLC24 gene family of Na/Ca(2)-K exchangers: from sight and
            smell to memory consolidation and skin pigmentation
  JOURNAL   Mol Aspects Med 34 (2-3), 455-464 (2013)
   PUBMED   23506883
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Besserer,G.M., Nicoll,D.A., Abramson,J. and Philipson,K.D.
  TITLE     Characterization and purification of a Na+/Ca2+ exchanger from an
            archaebacterium
  JOURNAL   J Biol Chem 287 (11), 8652-8659 (2012)
   PUBMED   22287543
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..336
                     /product="sodium:calcium antiporter"
                     /GO_function="GO:0008273 - calcium, potassium:sodium
                     antiporter activity [Evidence IEA]"
                     /GO_process="GO:0006874 - intracellular calcium ion
                     homeostasis [Evidence IEA]"
                     /calculated_mol_wt=35400
     Region          19..332
                     /region_name="ECM27"
                     /note="Ca2+/Na+ antiporter [Inorganic ion transport and
                     metabolism]; COG0530"
                     /db_xref="CDD:440296"
ORIGIN      
        1 mtfmfvelaf mlivilvaae lftnalehlg erlkisegvt gslfaavgta lpetmvplla
       61 laggtsnqav neeigvgail gaplmlatlt tflmtlavir srglrgtiap ertgfvrdmn
      121 tflaafslat vamfvphhnw avrallaaml vglyvmyvvm tfrastqlvd aghgteapha
      181 mflsrvglpt nlativlqll igvallvgga kgfihgvegv shvlgvsall lsliivpiat
      241 elpekvnsvl wirrgkdtla fgnitgamvf qgtllpaigi mltpweprpe vltgviitla
      301 aaawlrvnar trglalwall angagyagyl vltltr
//
LOCUS       WP_175874467             920 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175874467
VERSION     WP_175874467.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..920
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=99018
     Region          18..816
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msitktfrnf asglavgnkr pvdlhfgqaq ravghllvlh hadireglms giegqltcvs
       61 tydhlppalf lglpvsvrlt tdrgniqain aivhevrtgq sdgeltvyql hvcdalslmd
      121 rrtnarlfrs rsvpeilatl mnewkqrspa larafdfdls tlqvdrypar eltrqvnesd
      181 arfirrllrr egitvfakaa pvdgrrgltd erpihtlvfc ddphrlpdap agtvrlhprd
      241 asveqrdtvt lfaydqslsp gkvrrpswdy ktarvddfaa vagidqgesg ndlarlltdi
      301 aidiphvgds wndharithd rmlahqfaaa rcegigtvrd mlvghgftla gdpeldmksi
      361 drrrflvtsi rhvvwnnlpt dlssrasglf tasrnltptv pppdasgqtd tryensftcv
      421 qrgvplkpay dptidvppvh lltgtivgtq geevfcdkag rvrvlihgld padhahaqga
      481 gtnglagdsa plrvvaslag ecfgalflpr vgmevllgnl sgdpdrlvii gvlsnganpp
      541 atfsdtgglp gnryvsgikt reirgrrhnq lrlddtpsqi saqlasehah tqlnlgyltq
      601 prkdghgsdr gegaelrtda aaalraaqgm llttyarsra tggqldrdel irlldqcmal
      661 fkslgdhagq hggqsadtag qdnianafrh wkpggsesga tgdasafmaf gaqagslnvt
      721 pkthvmyage nidqiaqqhm qitsgerinl haghgvamfa hgdgvsaiah qgkvalqsqn
      781 ddtqiesgkn iqltaadgrl agtasdeivf vtsggaylkl hgsdielgcp gkftvksdgh
      841 awdgpasmsv dlptfdqrpl grvpklirpt dgnaapgfeg qvrkasgtls nlttdtagel
      901 pavdtdrfer lavqftkknv
//
LOCUS       WP_175874533             206 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0397].
ACCESSION   WP_175874533
VERSION     WP_175874533.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22188
     Region          9..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdsprltrae rrdatrerll gaahaifaek gyaaasvedi ataaghtrga fysnfrgkad
       61 vlfellrrdr ddaaatlqri vgshdpddda qramlaywrr gttqpaaqlm wldaqlqaar
      121 dprfrarfga llrdrqalaa acidayaara gvslplptpv lalgltalcd gmqshgaada
      181 rstvdaladt vlvgfithtv fdrvrg
//
LOCUS       WP_175874551             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0397].
ACCESSION   WP_175874551
VERSION     WP_175874551.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34383
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..287
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,222,239,266)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     216..220,227..228,231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mnkfsdmstf vavveagsfs eaarrlgttk sivsariqkl elrlactllk rgrslqltdp
       61 gqrffeqsrq llqelerieg evneagasls gnlklsvpvt fvarylapll srfaemypal
      121 cldveaddrl snlqdghfda airigqlads sliarpvtvn rhlicaspgy lerrgvpvhp
      181 ddlpqhdgll ylnrephgmw slpleyekqs frvrvrmrtd sgfqllagai aglglailpt
      241 flasdalvag elvsvlpeya psggqvnvvy rktvrtspki qalvqfldea ighparwdvp
      301 liergllphp sht
//
LOCUS       WP_175874584             177 aa            linear   BCT 11-JAN-2025
DEFINITION  2,4'-dihydroxyacetophenone dioxygenase family protein [Burkholderia
            sp. BCC0397].
ACCESSION   WP_175874584
VERSION     WP_175874584.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14449000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..177
                     /product="2,4'-dihydroxyacetophenone dioxygenase family
                     protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20122
     Region          37..160
                     /region_name="cupin_DAD"
                     /note="2,4'-Dihydroxyacetophenone dioxygenase (DAD), cupin
                     domain; cd20302"
                     /db_xref="CDD:380436"
     Site            order(53..54,57,63,65,82,84,86,88,101,104..108,110..112,
                     129,135,137,145,148,151)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:380436"
     Site            order(77,79,94,115,130)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380436"
ORIGIN      
        1 mvdkavsefw qnipaianpf kpdarpeayi pnaatddery yvpftetvss rplwispsqn
       61 kwcdilmake aglvnrhyhp hevfaytlsg kwgylehewt atrgdfvyet pgeghtlvaf
      121 dhpepmraff ivkgpliwld dagnpdgyfd vhsyiamcka hyekvglgaq aieklfr
//
LOCUS       WP_175874585             433 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0397].
ACCESSION   WP_175874585
VERSION     WP_175874585.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0397
  ORGANISM  Burkholderia sp. BCC0397
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Burkholderia sp. BCC0397"
                     /db_xref="taxon:486876"
     Protein         1..433
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45367
     Region          7..406
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mtspsssrpa wtyenrllli lfmtfgfvff drlalsflfp fmsaelhltn tqlgmvssal
       61 altwalsgaa tgawsdargt rkpllvaavl gfsvcsalsg lvggfaslia fralmgiaeg
      121 pvlplsqslm vesstpsrrg lnmgllqgsa agllgamigp pvvigiatay gwreafyvsc
      181 ipgfliafcl wrwvrevppg gvrhvqadtt avpaaggaav srwallkern illcvliscc
      241 fltwfvviis fapvflvesr rlspsdmgvv mtclgaawvf wgfavpaisd rigrkptmig
      301 faliaavcpv vlihvgsvwa lgalvfvtyt glgcftlfma tipaetvppr aiasalglim
      361 gageliggfv aptvagfaad kyglqfamwt sttgallacv lsfglvetap avlrkralag
      421 aagrldtqnl ggr
//
LOCUS       WP_175874705             190 aa            linear   BCT 11-JAN-2025
DEFINITION  PadR family transcriptional regulator [Burkholderia sp. BCC0097].
ACCESSION   WP_175874705
VERSION     WP_175874705.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..190
                     /product="PadR family transcriptional regulator"
                     /calculated_mol_wt=21081
     Region          7..97
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          <48..175
                     /region_name="AphA_like"
                     /note="Putative AphA-like transcriptional regulator;
                     pfam14557"
                     /db_xref="CDD:317018"
ORIGIN      
        1 mstshpspla lavlatltet pmhpygmlqq lkargydevv nvrqrtslyq tidrllrdgl
       61 iavhdterdg afpertvyal teaghtagqa wlhallaepa refpafgagl aflplldaed
      121 arhqlelria rldaererle alrataqadq vprlfllqne halvllnael dwarsvvehl
      181 kigalrwvdg
//
LOCUS       WP_175874706             476 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FAD-binding oxidoreductase [Burkholderia].
ACCESSION   WP_175874706
VERSION     WP_175874706.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..476
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49773
     Region          20..476
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mptsnrtaag sapdgrplpd davdavlaae lgdalvtraa didpryftay nepagvrpra
       61 lvrprsiddv srtlalcarl gqpvvpqggl tglargaval ggevvlsmer fagvealdaa
      121 agtitvragt plqtvqeaae aagftfgvdl gargscqigg mlatnaggtr airygmmreq
      181 vlgleavlad gtvvssmnrm lknnagydlk qlfigsegtl gvvtravlrl hpllaapata
      241 lcrvrdydav valwnrlrtl pevvsfeamw pafydyvarh tpgvtapfig dggfvvliec
      301 atsapggdah qaletglavg leaglvddav latserqard lwtlreglai dalphlvnfd
      361 vslptgelga faerceaalr vrwpaltclf fghvgdgnvh igvslaemtd adadaldhcv
      421 yavvrdmggs vsaehgigvl krpylahtrs gaeielmrrl kaaldprgil npgkvl
//
LOCUS       WP_175874730              92 aa            linear   BCT 11-JAN-2025
DEFINITION  HU family DNA-binding protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175874730
VERSION     WP_175874730.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..92
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=9473
     Region          1..92
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 mikqelidav aaqtgaskaq tgetldtlle vikkavskgd avqligfgsf gsgkraartg
       61 rnpktgetik ipaaktvkft agkafkdavn kr
//
LOCUS       WP_175874780             472 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0097].
ACCESSION   WP_175874780
VERSION     WP_175874780.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..472
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51092
     Region          39..457
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(49..50,53..54,57,97,147..148,150..152,155,175,
                     178..179,182,293,296..297,300..302,305,332,336,385..386,
                     390,394,410,413..414,417..418,421)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mastdslpqa qapspsidpg sisarldrlp ptrsvwklvv llslgfffel ydllysgyva
       61 pglvksgils atthglfgtt gvasfiaalf sglfigtiac afladrfgrr aiftwsllwy
      121 taanvvmafq dtatglnfwr fvvglglgve mvtigtyise lvpkqirgra faceqavgfv
      181 avpvvaflay llvphaplgl dgwrwvvlig ahgalfvwwi rrelpesprw laqqgrvdea
      241 drimraleak veaeygrplp ppapaepvpp rgsfrdmwvp pyrsrtimmt ifnvfqtvgf
      301 ygfanwvptl likqgitits slmyssvial aapigpligl viadrferks vivamaaaiv
      361 vcgllfsqtt vgaflivlgi gltlasnims ysfhayqael fptsirarav gfvyswsrfs
      421 aifssfviaa vlrgfgtfgv fafiagamvv vmaaigwmgp rtkgialeti sk
//
LOCUS       WP_175874797             722 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia sp. BCC0097].
ACCESSION   WP_175874797
VERSION     WP_175874797.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..722
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77485
     Region          53..722
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mpsrrtpcra rtlhpwrtrl salltlcvag gahaagaepv apapaaapaa ehelpaisin
       61 asaavdptig yqprttsiag gdaralkeip qsvavvsssv mqdqqtrsld dvlgnisgvt
      121 qtntlggtrd afikrgfgsn ndgsvlvdgv rtpvlhsyla tidrvevlkg pasllygmqd
      181 pggvinlvtr kledtfggsi sasrtnhggs naqfdltgpl gkpgqvaggt lafrltgeyd
      241 tsrywrsfgr ernaliapal swhdantsid vsyqyvdytm pfdrgtvlvn gqlddalryr
      301 ryeeawsqss gvqetlrtri ehrfsdawrv ratygwgrdr ydqyitrata fnsktgaltr
      361 ssdanlgrnd sdqiatlgll gnvtlagmqh aiyvggeyer qrsfrgdtir gkattgfnly
      421 dpvygllasg gmpnakqsds rsvvhaysti vqdsvkitdr ltavgglrwe nwqqesgmgr
      481 pfgfadrsrg svwlpqfgla yalapaltay anvsrsfkpn vasnvaapla peygrvleag
      541 lklslkpait gtlavyqidk rnvavtvgdl tstigtarsr gieldvagqi trhlsvigsy
      601 aytnandrdg ntplvnvarh tgslfavydt aianlpgrwr fgggarlvga rsgdtansft
      661 lpgyvsvdaf aayettigkf ptrfqlnvkn lldktyypss nsnlivavge prlvtltttv
      721 sf
//
LOCUS       WP_175874805             248 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175874805
VERSION     WP_175874805.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..248
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27231
     Region          27..184
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtaapadtmt atakadradt prapagrksq qrvqdilrag revfaekgye hataaeiaqr
       61 vgvseatvfs yfrgkrelca rviadwydei iaafehgmpr easvqqqfaf ivrthlrlml
      121 vngtglcalv lsegrakqha lsdeltalqr rytaplmdvl argqtagqvr adlplsllrs
      181 mvfgpmehvl wdailghrkl dtettatqli dmlwaavqpp apeqaalvrf rnevaeavrr
      241 legqasrg
//
LOCUS       WP_175874876             228 aa            linear   BCT 11-JAN-2025
DEFINITION  lytic transglycosylase domain-containing protein [Burkholderia sp.
            BCC0097].
ACCESSION   WP_175874876
VERSION     WP_175874876.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..228
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - lytic transglycosylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=23896
     Region          1..185
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 mrrrffwliv lslgiaqhaa aqqapalpas apeaaasasg dasaplandq pneanrrits
       61 yltkkfgvak eraakladiv svtatkyslp palvyaiisi esrfqekarg qhgatglmqv
      121 vpsahrgmlr nvkdltepna nvevgsrils gyvkaaggnv qaglksysgg ssayaakvmq
      181 rvdsfrfvle peddaksant andannakah mvpvsdpspa ptanrnak
//
LOCUS       WP_175874910             316 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Burkholderia].
ACCESSION   WP_175874910
VERSION     WP_175874910.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..316
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34483
     Region          5..225
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mqpilsvsdl sktyasgfqa lkhvtldirp geifallgpn gagkttligs icgivtpteg
       61 rvtvgghdir dqyraaremi glvpqelttd afetvwatvs fsrglfgkap dpayiektlk
      121 alslwdkrdn klmtlsggmk rrvmiakals heprilflde ptagvdvelr rdmwklvdsl
      181 resgvtillt thyieeaeem adrigiilgg elvlveekre lmrklgkkql tvqlehplae
      241 mppalapfgl ertedgaalv ytydsqrdda siaklinalg sagigfrdlh ttqssledif
      301 vslidnrrng vqgaga
//
LOCUS       WP_175874911              98 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cupin domain-containing protein [Burkholderia].
ACCESSION   WP_175874911
VERSION     WP_175874911.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 98)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002085
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..98
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10286
     Region          1..98
                     /region_name="ManC"
                     /note="Mannose-6-phosphate isomerase, cupin superfamily
                     [Carbohydrate transport and metabolism]; COG0662"
                     /db_xref="CDD:440426"
ORIGIN      
        1 mslidfksva daqaaawkst ivgevgpari kvlrmdaqpy eaevhdyneg llvldgmlml
       61 evdaetvvvg agqmylahag trhavlpgsh gtlaiidv
//
LOCUS       WP_175874935             551 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia sp. BCC0097].
ACCESSION   WP_175874935
VERSION     WP_175874935.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Gournas,C., Athanasopoulos,A. and Sophianopoulou,V.
  TITLE     On the Evolution of Specificity in Members of the Yeast Amino Acid
            Transporter Family as Parts of Specific Metabolic Pathways
  JOURNAL   Int J Mol Sci 19 (5), 1398 (2018)
   PUBMED   29738448
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Vangelatos,I., Vlachakis,D., Sophianopoulou,V. and Diallinas,G.
  TITLE     Modelling and mutational evidence identify the substrate binding
            site and functional elements in APC amino acid transporters
  JOURNAL   Mol Membr Biol 26 (5), 356-370 (2009)
   PUBMED   19670073
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146941
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..551
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59517
     Region          31..464
                     /region_name="AA_permease_2"
                     /note="Amino acid permease; pfam13520"
                     /db_xref="CDD:404414"
ORIGIN      
        1 msqaglranr tsdveatish dstghtlhrg ltwkdafwvt sgvpagvlft iggvcatigq
       61 pawaiwiaai tmgliqsaty aeisglfphk sggasvygai gwvrysklia pvsvwcnwla
      121 wspmlalgcg laasyaltsl fpanaavlhw qlkvadlgfi kpglslrina tfiiatilll
      181 itfklqhsga skaartqril giasltplli vgivpfvtgd vpmsnllpll plghdaqgnl
      241 taatfgswng qgvtmalgam fmagwasygf etavcytref rdprrdtaka ifwsgalclv
      301 vmtlvplafq galgtqamld psigdgtgva aamakivggg awvanavvvm lmlsillivm
      361 tsmmgssrtl yqasvdgwlp kylshvnehg sptramwtdl gfnlvflmms dymtvlsisn
      421 vcymlfvfln lqsgwihrmd rgnwdrpfrc ptwllvggai cgyanlvyvg aganlqgegt
      481 lrngliamll ivpvflfrhy wqdrgrfpaq mqrdmelevp krapwlslmp yaaligaglt
      541 iwlsyyfawv k
//
LOCUS       WP_175874861             111 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase, partial [Escherichia coli].
ACCESSION   WP_175874861
VERSION     WP_175874861.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>111
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
     Region          <1..111
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 arwseidfet smwtipaere aidgvkhsqr gskmrtphlv plshqalail kdvyklsgdr
       61 dfvfigdhdh rkpmsentvn kalrvmgydt kvevcghgfr tmacsslies g
//
LOCUS       WP_175874944             314 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC0097].
ACCESSION   WP_175874944
VERSION     WP_175874944.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..314
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34980
     Region          7..314
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpedfhflll pgfsalgfms aveplrvanr frtelyrwhv isadgapvaa sngipvaaea
       61 acadvprvdt vfvvagfdpl vcytrtlgdw lrrqhrhgat lggidtgsfv laeaglfdps
      121 qpltlhweal aafrerypgl natqelfeid drritcaggt asidmmldli grrhgtdlaa
      181 aiseqfvvsr irqrsdsqrl eiaarygvhn rkliqvigtm qrhmenplgs dalaqevsit
      241 rrqlerlfsa tlndtptrfy lnlrldrare llqqtdmsit svcvacgfes pshfsrtyra
      301 rfgmsprsdr ratr
//
LOCUS       WP_175874982             325 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Burkholderia].
ACCESSION   WP_175874982
VERSION     WP_175874982.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 325)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 325)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13797492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..325
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35265
     Region          23..198
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          <211..316
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mgeavfatid nplffcespa midpltevvt llqpgarysk yvrgaspwai srtvagepfy
       61 cavldggcri aidghapiel lagdfmlipa aygvamssle ppppgvdtap pvmldhgeyr
      121 igdpanpvdt rmmagncsfg spdaallvsl lprfvhvrge prlttlvqlv rdesraqrpa
      181 reivlarlle vllieamrft tgthaspglv rgladsrlaa alrrmherpa hpwtivelak
      241 eaalsrstff erfsravgva pmeylltwrm alakdllrrn egriaeiaar vgyssastfs
      301 vafarhvgrp paqyardeqa mvses
//
LOCUS       WP_175874989             437 aa            linear   BCT 11-JAN-2025
DEFINITION  leucine-rich repeat-containing protein kinase family protein
            [Burkholderia sp. BCC0097].
ACCESSION   WP_175874989
VERSION     WP_175874989.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Shen,K., Hines,A.C., Schwarzer,D., Pickin,K.A. and Cole,P.A.
  TITLE     Protein kinase structure and function analysis with chemical tools
  JOURNAL   Biochim Biophys Acta 1754 (1-2), 65-78 (2005)
   PUBMED   16213197
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   5  (residues 1 to 437)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   6  (residues 1 to 437)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
REFERENCE   7  (residues 1 to 437)
  AUTHORS   Hanks,S.K. and Hunter,T.
  TITLE     Protein kinases 6. The eukaryotic protein kinase superfamily:
            kinase (catalytic) domain structure and classification
  JOURNAL   FASEB J 9 (8), 576-596 (1995)
   PUBMED   7768349
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..437
                     /product="leucine-rich repeat-containing protein kinase
                     family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=46515
     Region          <2..>193
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          39..61
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          62..81
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          82..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..175
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          211..>378
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(214..217,220,222,238,240,269,287..290,345,349..350,
                     352,362..363)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
ORIGIN      
        1 mthtleqlqa gqlsgarqlk lacgltefpr eifdladtle vldltgnals alpddlprlh
       61 rlrilfasgn rftafpdvlg acerldmigf kanrirtvpr galpralrwl iltdnaidel
      121 padigdcgrl qklmlagnrl ralpaemaac ralelvrlsa nrldalpdwl prlprlawla
      181 vagnpfgaep eaaasagpdv aeidwaalsc eqklgegasg viyraqwrad ghpprtvavk
      241 lfkgavtsdg lpdcemaacl hagghpnlip vigklrghpd gthglvmalv dpaltnlagp
      301 psfasctrdv yaadarfepa qalriahgia svaghlharg imhgdlyahn ilhdgaggal
      361 lgdfgaasly dpdertrgar ferlevrafg yllgellerc ephagaldal aaacvnedvd
      421 arpsfdeita alaasmr
//
LOCUS       WP_175875082             548 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NRAMP family divalent metal transporter
            [Burkholderia].
ACCESSION   WP_175875082
VERSION     WP_175875082.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..548
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=58662
     Region          48..452
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 mstpsnvspp iaaersavld dahlgdirga lgtishhdtg argtwwarlr tllaiigpgl
       61 ivmvgdndag afgtytqagq nygttllwtl lllvpvlyvn qemvlrlgav tgvgharlif
      121 erfgkfwgaf svidlfllna ltivtefigi tfvldffglp kvagvcvaaa ltmaavstgd
      181 frrferfaig lcvmslllvp vlvsihppva qmtrdffvpn wpahaklsdv mllvigivgt
      241 tvapwqlffq qsyvidkrit prfmkyekad lwigiafvlv gavamigfss alfsghpeag
      301 nftdaggiia glekyagrts atlfaialld aciigaaavs lstayaigdv fkirhslhrg
      361 vtdakgfylv yfgivaaaat lvlipgsplg llteavqtla gvllpsatvf llvlcndrqv
      421 lgpwvnstkl nvftgaviwv lvllsiilta svmypdisge aivdvlvggt vlaiagylat
      481 vlirrnkrvv epgidrslrd swrmppldtl epqnmtlatr iwmavlrgyl viavglvivk
      541 vvqmtllk
//
LOCUS       WP_175875106             473 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54 dependent transcriptional regulator [Burkholderia
            cenocepacia].
ACCESSION   WP_175875106
VERSION     WP_175875106.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cenocepacia
  ORGANISM  Burkholderia cenocepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia cenocepacia"
                     /db_xref="taxon:95486"
     Protein         1..473
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51987
     Region          35..134
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <171..471
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mnhccqlsms glrdverlvs alpfiavrhd pvapsrplvy lsqqhdaalv dvlasrgwdv
       61 wraktvadal nlvkanrpha givdfdsfas pdvasfeall rdprvgwval adgerlrnit
      121 iarlirhccf dyvrnaaayt tigylvghay gmlkladgdp aeeapppgga migacgamrr
      181 lfatirkvan teaavfiage sgtgkeltaa aihrqssrad apfvavncaa ipttllqael
      241 fghergaftg ahqrkigrie aahggtlfld eigdmpfesq asllrflqeg rierlgghas
      301 ipvdvrivsa thvdleaamq agrfradlyy rlcvlridep plrmrgrdim lladdvlrry
      361 rddgsyrirg ftpcaieaih typwpgnvre linrirfavv mtngplisaa dlelrpytsl
      421 rqptlaqarr qaerhaieet llrhrhqhad vaaelgisra tlyrlmtahg lhs
//
LOCUS       WP_175875146             175 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia sp. BCC0097].
ACCESSION   WP_175875146
VERSION     WP_175875146.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..175
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19254
     Region          28..142
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 mpapirirpa tredaaamaa vevaaaqrfr eigmadiadg eptdaaavlv riddgrayva
       61 vdpqrtcvgf afyrlldarr lyleeldvap shagqrigar lieqvmacaa rehveqvlls
      121 tfrdapwnap yytrlgfrii ddaalddtlr airahhvalg ldetrrvfmr ravaa
//
LOCUS       WP_175875158             783 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC0097].
ACCESSION   WP_175875158
VERSION     WP_175875158.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 783)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..783
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=86276
     Region          19..736
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mrtiqdvlkh pnsvvtqplh leiaaldapv svlsfvltee mntpfladit vtsqdkridg
       61 ativgqpavf tieehasvpa laavidpvrh aartvhgvvt qwtrvrtsrd eatyqvhlkp
      121 rfalleevhd savlldrsfr ellsdmivdr slfqsfdvef elegldgkle qtvmyeetva
      181 nfidrhcrra gvyyyfkqak kedgpqrdtl vfgntprgym ralevplmph sgltswheav
      241 ltlevtralv pqtvrewdhn yrvpddplqv esivahddps vygsvnrsie hfhsveegqa
      301 ladarrdell trqvrltgts nvigmtpgmv vritndevde aphgmvitkl vtigsrsqsv
      361 vntfeaipah rtyrpeyvpe khwrwiagml igvvesgdde pyawmdeygr yrvrllfarh
      421 sgkrgtnsmp lrvlrtsasy qgglhipllp rsevrvvatq gncdrlliag alhdharrdl
      481 ghgkegwysr avfrspllgn klrfedlkdh egirlatvfg qsslnmghlv drdknkrgqg
      541 felttqnwgt lrapkglfvs adaaggsgtp hldmpaaiaq lktalqrvtd laaattqaka
      601 dpadratqaa lldgldqlrd agllasapgg iafvtpkslq qsagenvivt agrdmdvsiv
      661 rrlrmvagdl islcahklgi kifskgkiel qaqgasmdlf sdeqlhvssa ganvlvsakt
      721 ramvacggas mtiengnvvf ncpgefrira ssfvfegprh tsinlpqlpv sdyspssrys
      781 htr
//
LOCUS       WP_175875174             215 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC0097].
ACCESSION   WP_175875174
VERSION     WP_175875174.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..215
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23257
     Region          7..211
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mtsahsltfy tadtpnghki aiyleeagla hdrvqvnlsa geqrsptyla inpngkipai
       61 vdhdaglavf esgailgylv ektgclqpet laertavqqw lhfqiggigp mlgqlwwflh
      121 asktgnaeai dryrkealrl ygvvngrlse saylassrys iadiaafpwl rtageldldv
      181 agfphverwl aeiaarpavq rgliacrapv aeaah
//
LOCUS       WP_175875225             287 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase
            [Burkholderia].
ACCESSION   WP_175875225
VERSION     WP_175875225.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..287
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31506
     Region          30..280
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 mteireddap dgtaarvalw ralhveldap phvltdeigl qllapepgwq qrgdmdpqft
       61 rpfrasivar arfiedlvie qaargvrqyv ilgagldsfv qrrpemasfv tvfevdqpap
      121 qrwkqrrlve lgygvpdwlr fvpvdfeakq swrdalvgag fdagqpavvv stgvsmyltr
      181 eanaaalrev aslapgstfa mtfllplena dpdvrpglem aakgarasgt pfisffmpdq
      241 iralareagf akaehvsaae ltrryfadrt dglrppnhae ellvatv
//
LOCUS       WP_175875256             365 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC0097].
ACCESSION   WP_175875256
VERSION     WP_175875256.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..365
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39903
     Region          35..343
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mltgyrpimp pllplapqap vpvdrtlakv asashfvfll vpnfsmiafv nalevlrian
       61 qlsgkplyrw svisvdgrpv pasngltlsv dvpeapgpad ivfvcagnev qhattpahlq
      121 rvrqfahaga llgsictgay vlakagllag htcvihweyl haqaesfidv tfersifrid
      181 rdritcaggv aplemmlylv glsmgdafmq ristylavdr vrhpgalqpp agygstsrll
      241 aevlqlmeah ietplslval aqragvrerr llrlfrsavg qpvmqhyrll rlrrarqllq
      301 qsamlltdia vacgfqslsv ftsayrktfg ltpgqerrqa qsrtfggdar ehaaerhdtv
      361 vamrr
//
LOCUS       WP_175875259             540 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GMC family oxidoreductase [Burkholderia].
ACCESSION   WP_175875259
VERSION     WP_175875259.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..540
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58712
     Region          1..531
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mswdfiiiga gsagcvlanr lsadphhrvl lleaggsdnr faikipalam kamndpetdw
       61 mfptepdptr ndrtevvprg kvlggsssin atwyvrgnrg dydhwaalgn tgwsydellp
      121 yfrkvecnrd gvsetygktg aiviseirgv ppltrvflda meelgypkna dfnaeptegv
      181 ailhstqhrg lrwsaargyl dparrrpnlr vltgalvrrv lienrvavgv efdldgqrrv
      241 erchgevils asainspkil mhsgvgpadq lnlagipviv enravgrnlq ehpacqvkay
      301 vnvrtanqef nalgmlkygt rfllsrsgqa tfsysgvglv rtrpelaypd iqyhfgafss
      361 sytdqgirme peaainlqpn vnnsrsrgev klkssdplap psiqfnmlad aydretliag
      421 ariaraalrs rafapyvtge ckpgddvqtd dewqaylren aggsfhpcgt ckmgvdadav
      481 vapdlkvigv drlrvvdssi ipqipsgnln aislvigekg admilaahra ataveaaqht
//
LOCUS       WP_175875287             307 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175875287
VERSION     WP_175875287.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33624
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,160,162,223,240,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mnqlqamrvf trvvelssfs laarqlgmsa aavtrsvgml eahlnmrlln rttrslslte
       61 tgreyldgcr tiiekldeie snlaqvnrdp hgtlriaasa tsvaaglgal lstyriehpr
      121 vrfdvttfdi qvdmveggyd vcfcddhrlv nstfvsrtlt svrdvivasp dylarhgtpv
      181 epvelnthcl ltvsngaarn wefsdvdgss riytgnalas tsntmvriaa lnhmgiaqlp
      241 hplvaddlas galvpilery dvnggprrvs ilypsrnyls tkvrsfidyv vdhyrapert
      301 amqlaaa
//
LOCUS       WP_175875290             314 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0097].
ACCESSION   WP_175875290
VERSION     WP_175875290.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..314
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34747
     Region          8..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..298
                     /region_name="PBP2_DntR_NahR_LinR_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators that are involved in
                     the catabolism of dinitrotoluene, naphthalene and
                     gamma-hexachlorohexane; contains the type 2 periplasmic
                     binding fold; cd08459"
                     /db_xref="CDD:176148"
     Site            order(104,106..107,111,169,206,273)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176148"
     Site            order(105,108..109,112..113,116..117,119..120,123..124,
                     126..130,132,195,223..227,230..231,234..235,238,252)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 melsdidlnl lvlfqrlmhe rrvssvaeqm nmsqpgvsna laklrrrlgd plfvrgpggv
       61 vptpfalrla epvshalatl haalnpetgf dplhatrtlt igmtdigevv flpallehls
      121 rsapgialnt vrntsvnlgd emadgrvdla igllpqlkgg fyqrrlfdqr yvclfrrghp
      181 legvpltvda wrdaehlvvv sagtghgqvd ewltrrrvkr qvrltvphfm svgyilqrtd
      241 liatvpehla lqlaapfslg wralpvtlpg apihmlwhtr vnqdegnrwl rdvvvelfae
      301 tgartrkaaa arrk
//
LOCUS       WP_175875321             303 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175875321
VERSION     WP_175875321.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33938
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,223,240,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdlesirifl rvvergsfta aatqldmpls rvsrkikqle ddlgvqllyr ttrrvsvtea
       61 grdyyerclr aeeilldadr qvralrtepe gtlrvlvpya iglfelepal aefrrryplv
      121 qlvliydnsa ldlvehgfdv alrtgvlsds gyvarslgws hakfaasphy ldragrprtp
      181 qdladhdilf vgrdtpgltl rltnaagdva dvpvrpvlis nesvtvlrqa asgggialis
      241 thfttrrles neleivlpdw hrtddvelha lypkratlds kvrafveflt evftawrtas
      301 qsl
//
LOCUS       WP_175875424             222 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0097].
ACCESSION   WP_175875424
VERSION     WP_175875424.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..222
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22706
     Region          13..217
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mpvrstgcck eramfiksvv mglsiavpvg pigmlciqrs lsrgfqagfa tgigaacada
       61 iygllgalgv agivtafpml tvglkiggga flvwlawtia rqapaapagq rdlprttvlr
      121 dflttfgltl snpmtivsfv gifaalgplp gaqegamwat vawmvagvfi gsamwwlcls
      181 sasaalrtkl sfafmhalsr gsaavvavfg aiqlvagvrg li
//
LOCUS       WP_175875468             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175875468
VERSION     WP_175875468.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46422
     Region          23..427
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(35..36,39..40,43,82,140..141,143..145,148,168,
                     171..172,175,258,261..262,265..267,270,298,302,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mpetmstlaq paahaprrvr nsrlatasmi gtslewydft iyntlaalvf nhlffpsvdp
       61 lagtilafst yavgyvsrpl ggfvfgnlgd rigrravlml tlvlmgvtta lmgalptyaq
      121 agilspillv alrfvqgval ggewagavll svehgdqkrr glsaswtqig psfgtllgtg
      181 cialvtlstt sdaflswgwr vpfaasallv vfgfwvrrgv detpqfeqla eshataevpv
      241 advlkyhwkr lliaggsrig sdvlyalivv ftltyvttvl hlsrpvalta vmigtacnal
      301 avpffgalsd rfgrrpvyla gaiagivwaf vffalldsar pvaivaavai glvihavmyg
      361 pqgafvteqf ptrvryagss laytlagivg ggfaplviaa lfrqtgttta vslyvtaalv
      421 vtsialvaar etahrpled
//
LOCUS       WP_175875532             260 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Burkholderia].
ACCESSION   WP_175875532
VERSION     WP_175875532.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..260
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27472
     Region          13..255
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 misstgmdlq ltfitiliaf tgvflisfmk gafgggfsiv gipllslvmd pvtaggmlap
       61 lfiamdlfal rywkpstwsk pdlmlllpgl vtgigvgylt frlldhraia ivmaaitlif
      121 vglwwaggaa ltvrprstpk aitaglasgv ttmvahsggp plamyllplg lgkevyagtt
      181 slfftvgnat kavpwlllar ptgnvwivmm vclcaipagv vagwrlhakl dqrqvyracy
      241 gllvlaavkl lwdgvtgyla
//
LOCUS       WP_175875523             387 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175875523
VERSION     WP_175875523.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..387
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42768
     Region          10..385
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mqttqhdpyq direavrdlc sqfpgeyfrq iddargypda fvdaltkagw laalipqeyg
       61 gsglglteas iimeeinrag gnsgachgqm ynmgtllrhg saeqkraylp kiasgelrlq
      121 smgvtepttg tdttkiktta errgdryvin gqkvwisrvq hsdlmillar ttpladvkkk
      181 segmsifvvd lhdaighglt vrpipnmvnh etnelffdnl eipaenlige egqgfkyild
      241 glnaertlia aecigdgywf idkvsryake rvvfgrpigq nqgvqfpiar afvnveaasl
      301 mrfdaarrfd ahapcgaqan makllaadas weaanaclqf hggfgfacey dverkfretr
      361 lyqvapistn lilayvaehi ldlprsf
//
LOCUS       WP_175875549             214 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC0097].
ACCESSION   WP_175875549
VERSION     WP_175875549.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..214
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24485
     Region          1..210
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mltvwgrrna fnlqkvmwlv delalahrhv paggrfglld tpeflamnph gripvidddg
       61 tvvweshsil rylaarhgrp gfwrddpaeq sradrwmdwa qttlqpafln gvfrdyyrtp
      121 peqrdtvrie qsiaqcaqyf rlldtvlagq pflagdaitl adiaagthly ryfeldiarp
      181 dvphvvawye rlkarpayrt nvmipfddlr gklg
//
LOCUS       WP_175875551             122 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: response regulator transcription factor
            [Burkholderia].
ACCESSION   WP_175875551
VERSION     WP_175875551.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..122
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13284
     Region          5..>119
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mhdktvciid delamrqsle slvrsmgvra rlyasaeafl ehgasgtshc ivcdiqmagm
       61 sgiellavlr egccdvpiif vtahpsarrv learrlgalc vlekpfdpre lvqwvmralt
      121 gc
//
LOCUS       WP_175875568             315 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia sp.
            BCC0097].
ACCESSION   WP_175875568
VERSION     WP_175875568.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..315
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=34253
     Region          11..>246
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mqhpqqsnvt iegivpvmlt pfddagaidy aglerliewy lahgsdalfa vaqssemqfl
       61 slaeraalar fvvervagrv pvvasghisd dldaqvtelc aaaesgaqgv vlvtnrldpq
      121 rkgsaalldh lhrllarlps dlplglyecp apyrrllsdd elracidtgr fvmlkdvscd
      181 lamvkrrval aegsplkiln anaaiawdam kagsagfngv ftnfhpdlyq wlrthgesnp
      241 aladelstfl vvsavsealg ypalaklyhq rigtfgsikc raidydvrer fwaldavldk
      301 ivagtehfrr riaas
//
LOCUS       WP_175875584             462 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia sp. BCC0097].
ACCESSION   WP_175875584
VERSION     WP_175875584.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..462
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49510
     Region          35..450
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mdndrsgrta saaamhdfga daqrgdmdar kphllglstl vifglaymlp mtvfttyglv
       61 tsetnghlta ayavtliaml ftarsyghma rlmpsagsay tfasrnfgts agfmvgwall
      121 mdylfipmis ylaigiymkq ifpavpasvw ivgsialitg lnivgirlvn rvnliliasq
      181 lvfiavfvia sahvaagegl smavalpssg daraifagsa ilclsflgfd avttlseetr
      241 eprrtvprai llctlasgll fmliayvgql vfpdwhafkd ldsasldlmr rvggrtlsaf
      301 fvavyvagcf asamagqasv trvlfamgrd rvlpesvfgh lharlrtpvr atlavgvvsl
      361 salfvtldla stmisfgalv afaivnlcvm rsylgrpehr haggwiaygl mpaigfamnv
      421 wlwsglsrqt fyvgigwlvl glcqlvwltr gftrpaptls mn
//
LOCUS       WP_175875600             339 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: aldo/keto reductase [Burkholderia].
ACCESSION   WP_175875600
VERSION     WP_175875600.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..339
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36961
     Region          13..323
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(16..18,48,53,79,142..143,183..184,207,236..242,278,
                     295..298,303,306..307)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(48,53,79,142)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 mslkdrlpgn kilgfgtapl gnmfrnipda eaaatveaaw qhgiryfdsa pfygaglaei
       61 rlgdalahhp rdeyvlstkv grlildeied vsardlgekg glfehgrpnr ivndysadat
      121 lrsiedslkr lrtdrldivw vhdiaqdfyg dewlaqfeva rkgafrvlsk lreegvinaw
      181 glgvnrvepi elvldlaepq pdgmllagry tlldheralq rvmpaaaaqn vgivvggpys
      241 sgvlaggthf eyqkaspeil akvdrikaia trydvpvkaa alqfsmshpa tvavipgasr
      301 periaedqaa lnvaipadfw rdmreqglia anaplptdq
//
LOCUS       WP_175875622             205 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Burkholderia].
ACCESSION   WP_175875622
VERSION     WP_175875622.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..205
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21802
     Region          1..202
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtewivvvti tllavispgp dfamvtrnsl mlsrrsgvlt acgiglgvtv hvcytllgvg
       61 llirqspwlf navkligaiy liylgakmll tkaggvqadr rvaalsdlaa lrtgfltnal
      121 npkttvfivs lfmqavrpdt plivqlgyga fiaaahagwf alvamcfsat avrdrllslr
      181 hwidrtfgcl lvgfgvvlav arggr
//
LOCUS       WP_175875635             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0097].
ACCESSION   WP_175875635
VERSION     WP_175875635.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..359
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38102
     Region          159..356
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mtkvflilvr nellgylrsr sslfwtlvfp vfllsvmlfa fggsgslgta diafdvpggt
       61 tpynqacrae ivaslshsdt vkatfggrgt paervtvvlg adertpatir ydfngslavk
      121 aasrvveial arcaaqrlgl paaqarfena aptrrpfdyg affatgilvm afmaiglnst
      181 ttaiaalrer ntfklyvcfp vsrgvflaal ivarmammal salvlltvar vafgialpia
      241 tpdglralpi vllgaamvls igvllasrtr slaaaelacn vtyypllffs dltipmhdap
      301 awlkaglafl ptnqfavalr galvdgapya qlapqllgmt vctalflfaa arlfrwhda
//
LOCUS       WP_175875649             405 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0097].
ACCESSION   WP_175875649
VERSION     WP_175875649.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 405)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..405
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42715
     Region          18..230
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          144..>322
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnwstfawrn lwrnrrrtvl tmamigvaaf asslalgyvi atfdavregs idsgvghvqv
       61 lhhgyldlig erplqyglta deqtaatqai arlpgvatta rgidfdglvs ngdlsygfvg
      121 egiepnrepp gffdyhtvls grylsptnag tevvvgaela rklgvhvgsv vqlmastahg
      181 ginatdaqiv gvmstgnkdv derivnvtft aaqallrtdr asriaiflkd tagtpaaaat
      241 lraalptldv ktwdqlvsly hqivalyknq fsvfgailcl tillsmsnwi lmsiverrre
      301 istlralgvp aatvrgvliq etallgllga aagialallt mvalnhaqih lpappgrvkp
      361 illeftvspv avaavetafv vlgvaaalla tlglakrnil eglap
//
LOCUS       WP_175875650             236 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175875650
VERSION     WP_175875650.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..236
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25524
     Region          7..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtisslapvl elrdvtrtye gagrvvavrg atisigqrdv valvgpsgsg kstllnlagf
       61 ldvptsgerw legrriddap dtlerirrer igfvfqqfnl ipvmsalenv elgcfawgtp
      121 rtrreraram ldavglaare rhrpgelsgg eqqrvalara lakepaivia deptasldst
      181 naravaelil etnrtlgtaf liashddrlc ahlprriemr dgvpgvnrel vdvcva
//
LOCUS       WP_175875651             587 aa            linear   BCT 11-JAN-2025
DEFINITION  fatty acyl-AMP ligase [Burkholderia sp. BCC0097].
ACCESSION   WP_175875651
VERSION     WP_175875651.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10148874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..587
                     /product="fatty acyl-AMP ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=62431
     Region          23..567
                     /region_name="FAAL"
                     /note="Fatty acyl-AMP ligase (FAAL); cd05931"
                     /db_xref="CDD:341254"
     Site            order(168,171..176,178..179)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341254"
     Site            order(195,217..219,292,295..298,323..327,332,385,445,456,
                     459)
                     /site_type="active"
                     /db_xref="CDD:341254"
ORIGIN      
        1 mtkyastihr liesledvag amhrmtfvdd tgheagityr hfagevfrqa galrelgvre
       61 ndlvmlalpa svehavamma cvmtgalpct vpvparraaa grqvadvace lyrprlvvaa
      121 naqasawrdd afpaaatrvv dlatlssaad agaralissk sgrdphhvql tsgstshpka
      181 avlshenvia nvlgiggsvr fdiaagdgta swlplyhdmg lltllsnlhy rapllmmqpn
      241 sfirnplgwl kriasaratt tsvptfalry cvrrfnaaam dgvdlsacrn ifiggervdd
      301 atlrdfaatf apyglaasal qpcygmaest lavsmhrawh egavdgapyv iadtldrral
      361 ierrdaqpaa andgqdtete tvlamgtpid gmafrilddg dhalanravg evairgtsvm
      421 lgylnpddgt iaapltadgw frtgdigyva dgqlhilgrk keviiirgsn yfpheieeal
      481 ashsalrkst ciafglpdpe tgterlvvai earpvdatpq trtecqqlla srigfaaqdl
      541 cfvepgslpr ttsgklqrlk crdlyangal pvipasaave avqgafa
//
LOCUS       WP_175875659             347 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia].
ACCESSION   WP_175875659
VERSION     WP_175875659.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..347
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34898
     Region          13..301
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtwlrtlfrh slawpvltla llfaldvayr pgflsivlld ghlfgapidi lnraaplviv
       61 slgmtlviat rgidisvgai vaiagaaaat vleadpsqvg aalaaalgvg llagawngll
      121 vafvgmqpii atlilmvagr gvaqlltggq iipigapgyl algggylatv pcavwialat
      181 igasallvnr talglfirai gvnpvatrlv glrsgaivfg vylcsgvmsa lagilassnv
      241 rsadgnnagl lleldailav tlggtsllgg rfslagsvlg aliiqtltyt tysigvppea
      301 tlvvkavvvi avtliqsdaa rallvrhasr llpsarsrat ttgatpr
//
LOCUS       WP_175875677             412 aa            linear   BCT 11-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Burkholderia sp.
            BCC0097].
ACCESSION   WP_175875677
VERSION     WP_175875677.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..412
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=42588
     Region          6..391
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mnmknkglsl pmqmlgglvm gaacgvfapg faaklgflsa mfghaikmvv mpliflsvtv
       61 gvfragrlre rlgkvalssi gffvlmtgla aslglllnfa frpglgasmv qsgsmpaala
      121 ssidwtkflv dlipanivaa laagnslpvl vfgvifgaal aaaperaepa iavfeallsg
      181 lfkmvqwvia wsplaifaai aqllsakgft gahslvellg vaylgmaila vvltlviria
      241 gqsplavlrk vkeplilgft trsseitypl hlkklvelgv pygvastilp layifnrdga
      301 vlytalavgy ladayhlaws wplvitilil tiitidgaan vpsgaivait ivltsiglpa
      361 davllllgvd affdmgrtal nvygstaaaa vavrlsgsds iaaetvprqa sv
//
LOCUS       WP_175875691             246 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175875691
VERSION     WP_175875691.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..246
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26889
     Region          2..213
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mshdiepttt qqdtiyatlr qwvtvgrflp gerlkirnva aemgvgqmpv raalqrlaae
       61 galvnvpnag tivprltvpe fddllqmrml legeaaergc lrlepaelat lrklcqrmak
      121 alkhpadqpa rarksaggkq alkqpavslk agqatdylaa nedfhvllyk aagspllfel
      181 idtlwlkagp isnrlfdtse asavlndahe dlmdaldrrd aaaarraver difvagqflr
      241 stlkrd
//
LOCUS       WP_175875712             127 aa            linear   BCT 11-JAN-2025
DEFINITION  GtrA family protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175875712
VERSION     WP_175875712.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..127
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=13587
     Region          5..127
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mstllqaert rlvrfgvsgl cstaihvlva talfarldaa pvtanalafl catafsylan
       61 tlwsfsstvr trnairflav tlagfvetml iaraaealda sramgvvaia llippttfvl
      121 hrlwtyr
//
LOCUS       WP_175875728             175 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: flavin reductase family protein [Burkholderia].
ACCESSION   WP_175875728
VERSION     WP_175875728.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..175
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18656
     Region          12..164
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mettvtdraa ldpmqlraaf gqfptgvtvi ttcaadgrkv gltansfssl sldpplvlws
       61 lrkvapsrpd fvaathfain ilahdqidls rrfatpstdk fdgvphvase sggvpclgga
      121 sarfvcrnvg hyeggdhllf igeierfdaf gkaplvfhag qyhaiadhpd lsrei
//
LOCUS       WP_175875730             341 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Burkholderia].
ACCESSION   WP_175875730
VERSION     WP_175875730.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12168325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37757
     Region          31..203
                     /region_name="AraC_binding_2"
                     /note="AraC-binding-like domain; pfam14525"
                     /db_xref="CDD:434015"
     Region          247..334
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 maqfsetgwl adaacfnhdt lllqsndvde vrarvadvfk phrltptges ralhscmhha
       61 rwgnlslnll dygggvsiep gplehffllq iplrgdaeie cgatrfvssp gtasllsptl
      121 plkmrwgdac pqvilriere vmerhaqrhf gddrrasvef epefdlsspq gtclaqllpv
      181 lagaiatdah plrhplafeq lestllnlll yghpnsarng trsapaplap fyvrrveeyi
      241 rahldeplti erladlagvs pstlfagfrn rhgitpmgfv rqlrlqhvrd elladdtpgl
      301 asvtdialkw gfahlgrfai eykrafgesp satlrmrrvr g
//
LOCUS       WP_175875751             264 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175875751
VERSION     WP_175875751.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..264
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28632
     Region          1..255
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mtpplldarh ltlgydgerr ntvladvsls vdrgeivali gpsgtgkssl lralaglerp
       61 qsgtvsidgt tlqgphpria iafqdpcllp wlsternvaf glafehqerl treqqcervr
      121 salhavglea aaslrpaqls ggmaqraala ralarqphal lldepfsald evtraamqql
      181 lvnivattrc atvlvthdid eallladriv llgmqgrfid awhvdyphpr dafvselgrm
      241 ridilkalra gmkrphasdl hpln
//
LOCUS       WP_175875764             156 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Burkholderia].
ACCESSION   WP_175875764
VERSION     WP_175875764.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..156
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15875
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 myarifaald gsrgsrlald eaialaresg glivavcvvs daprptdvds gyierrdpag
       61 ldadkaaiav adaetafrlc gvrgtaqaid acgedvssal araaaecdad livmgthgrr
      121 gmrrallgsv aeslvriadr pvlvvregqg agaavl
//
LOCUS       WP_175875772             215 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175875772
VERSION     WP_175875772.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..215
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=23177
     Region          3..143
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
     Region          78..214
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mksdtalkqd veqalfwnpa idsrridvdv rdrivtlrgt vdswaqklea qktalhvada
       61 ralvlelnve ppqdacadhe laiaitfalg wqealrdqqi rvevdhgcvt ldgdvehafq
      121 sraaekmvsr mkgvvgvanr irvqadqtvp dvgtriaeal arraqresag iaidaddgiv
      181 tltgtvasla erraacgapa svrgvrevvd rltva
//
LOCUS       WP_175875796             701 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia sp. BCC0097].
ACCESSION   WP_175875796
VERSION     WP_175875796.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..701
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76052
     Region          22..701
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 msrrnwaaap maivvgttgm gaadaqetal ptievsaqra tapfrtrest satrseadvm
       61 eipfavssvg tkliqtvaat rgddlydwva gvsrqnnfgg lwdnyavrgf agdgntsgtd
      121 ylvngfswnr gmsvprdtvn lermevlkgp asalygrgdp ggiisyttkq pqfarantig
      181 vsagsygalr qtldstgpvt kslayrfvam nenngsfrdt vsskrylfsp sftwdigadt
      241 tlhyefesar qrapldrgvl avngqlgvip asrflgeprd gdydvrntgh qftlehrids
      301 swsinagvaq rntdlsgrss eafslqpdgr tlwrryrqva fhsndlqgrl ettgafrtgs
      361 ightlvmgvd ayrfnydqfv trstpsaaap yaidifdpvy gqpaptprta tnllerddgq
      421 giyaqdtlaf gphwkilagl rwdrfhqsid nrlkgvttsq lqtalsprig vvyemspaws
      481 fyantaysfr pnngadingr afdpekghgy eagakwagar slttvsafyv tkrnvltadp
      541 anagfsraag evrsrgvefe wsgdlghglr gianfayvda evtrdsvlap gsrlvdvprl
      601 sgsallmyet tlpfadkaga gagviyvgrr agntantqdg felpayatvq lngylqvnkh
      661 lrasvvlnnl fnrttyvssy nslwvtpgap rslfaslays f
//
LOCUS       WP_175875836             286 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia sp. BCC0097].
ACCESSION   WP_175875836
VERSION     WP_175875836.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15202679
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..286
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30624
     Region          12..132
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          168..273
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 msdlnpsrtl tyrpftetdl paahrlseav kwphriddwr fafqlgggfv aedesgvvgt
       61 algwrfddah aslgmvivsp erqgcgigre lmtrvvesfg ertvflhatp sgeplyvkfg
      121 faaigtvdqh qgaafqppli slppgerlrp lgtndgprla alasraagye rgaviealld
      181 vangialdrd gellgfalfr rfgrghvigp vvapdalraq alishwlalh egmfvrldvp
      241 gdsglsdwlq glglprvdtv vamargtppa rdpalrpfai vnqalg
//
LOCUS       WP_175875920             347 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175875920
VERSION     WP_175875920.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..347
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=37583
     Region          64..315
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mvgphdarpy vdafpardsi vnatsprtwl ppyaarggas paapavpdtr agdhsaaqae
       61 paathserll aidqvsleyr sgerivrath qvsfdvygsd rfvllgpsgc gkstllkaia
      121 gfiepvagsi aldgrpvrgp gpdrivvfqe fdqlppwktv venvafplra aaklsraear
      181 eralhyldkv glgtfadayp htlsggmkqr vaiaralamq prvllmdepf aaldaltrrk
      241 mqeellrlwd efrftllfvt hsieealvvg nrilllsphp grvraelnsh ehslenvdtg
      301 dfrdnvarih rllfdtdaph aphaphapha phaphaphaa ttegaas
//
LOCUS       WP_175875921             343 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [Burkholderia].
ACCESSION   WP_175875921
VERSION     WP_175875921.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..343
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36743
     Region          23..326
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 msfsflparr alaatltaal afagvvipqa ahaegriria eqfgvvylml nvardqqlie
       61 kegrkagldi kvdwvrlsgg aavndallsg avdiagagvg plltvwdrtr grqnvkgvas
      121 lgnfpyylvs snpnvktiad lsakdriavp avgvsvqsrv lqyaaakqwg dkqfdkldsl
      181 tqaiphpdat aailansnvi tghfgnppfq eqelagnpna hivlnsydvl ggpssatvly
      241 atekfrddnp ktyrafvaal adaarqiaad peraadtyir vngskidral llkilrnpqv
      301 qfktapqntl plaqfmhrtg airnepkswr dyffddpata ggs
//
LOCUS       WP_175875930             176 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175875930
VERSION     WP_175875930.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..176
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=19427
     Region          47..172
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mttlndylaq krdawhakqq aarndpdfka tplkatvral grsgvreiri rdfqvisdsp
       61 pdfagynlgp aspelqlgvl gsclthitli qaaerglkid aievevtgdq hplaqqpgfe
      121 hvpvfphnlr ytldivspep peairalhqa veqvcpifnl lrlpqhidge lrhtrg
//
LOCUS       WP_175875941             157 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia sp. BCC0097].
ACCESSION   WP_175875941
VERSION     WP_175875941.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 157)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..157
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17208
     Region          22..139
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04667"
                     /db_xref="CDD:467552"
ORIGIN      
        1 mmlpdpadfp vravplapla keratiichr nqrvllvarg rasrwtlpgg virrgesald
       61 aahrelreet gladlelayf fhvdgsvkrh hvfvaslprg ahacpgreia lcrwvgidav
      121 shwpasaptq riirqfaglc vasdlqprvl trlsssr
//
LOCUS       WP_175875931             252 aa            linear   BCT 11-JAN-2025
DEFINITION  YoaK family protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175875931
VERSION     WP_175875931.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..252
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=26582
     Region          11..243
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mpaqyfrnlt gkhrsatanr qlgfslafva gaanaggfla vkqytshmsg ivsaiadqta
       61 lgdvrlalag isslgsflig ascsailvnw grrqglhsqf mlpllveaal lllfgllgsh
      121 lalwetffvp vtvtllcfim glqnatitkl sgaeirtthi tgivtdlgie lgklfywnrs
      181 aidvdahavi anrsklriha tmlasffvgg lagaigfkhv gyvstvplaa vlvtlaivpv
      241 iddllallrg qr
//
LOCUS       WP_175876029             430 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NRAMP family divalent metal transporter
            [Burkholderia].
ACCESSION   WP_175876029
VERSION     WP_175876029.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..430
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45945
     Region          20..430
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 msgfdedapp aaeappdaak pwyrrlgpgl lagasdadps nvavyaqags qfgfnmlwmi
       61 vvtlpmmvav qlaaafigrr nreglvagir qhyservakt livmvvivnv vnvgadlaam
      121 gdatalvvgg rsywyaplyg iaslalqvml syeryarwlk wmtlgliayv lelgfvhvdw
      181 gdllhaivlp hiafthdyat tavavlgttl spylfvwqaa leveettaeq qngernsrre
      241 teqritfdtw tgmivtnavs fcimvigaav ffshgrhdig staqaaealr piageaaflv
      301 fafgivgcgl laipafagsa aygcaeawrf reglnepvrr apafytvlal cvivgiaicf
      361 spidpiraly wsavlngvaa vpmlvlvmll sqqrdaagqp gsgpvskvfg wlavalmaas
      421 vatmivdvlt
//
LOCUS       WP_175876068             392 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Burkholderia].
ACCESSION   WP_175876068
VERSION     WP_175876068.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 392)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..392
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42416
     Region          3..364
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtsqpyisfv gvsksydgrh avvdgldldi argefvsllg psgsgktttl mmlagfetpt
       61 dgtilldgrr lddkpphqrd igmvfqnyal fphltiaenv afplsvrkta reerkqrvqr
      121 aldmvelshl asrrpaqlsg gqqqrvalar alvfeprvvl mdeplgaldk rlretmqyei
      181 mrlhrdlslt ivyvthdqne altmsnrvav fsdgriqqaa tptelyenaq nafvanfvge
      241 nnglagrvga ldgewavlql rggitirgrr gnqveagdea mlalrperaq vlgiaetanv
      301 pagsnalaat vrdivycgdh hrvqlqldsg dtmvvkvpnt rlvalppiga tativwrpdd
      361 ckvlspsaip rvassavrlp ippvavpias ga
//
LOCUS       WP_175876042             362 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 9 protein [Burkholderia].
ACCESSION   WP_175876042
VERSION     WP_175876042.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..362
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38843
     Region          15..356
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mkldpgvdsd gsrgpkriav fralqlgdml cavpalralr rgepdaritl iglpwarefa
       61 srfsdyidsf iafpgapglg eqpepdaatr eafiaecrsr dfdlaiqlhg sgahtnaiva
      121 slgatrtagf vsadggtaal dcalvwrdde pevtrylalt rklgyadwgd ylefplggld
      181 yalwhvlcde haldpgryvi vhpgarmasr rwpverfaha arqladdgwq ivltgtrael
      241 alasafaehl grpcvnlcgr tplgalaali ararlllcnd tgvshvaaal gtpsivvacg
      301 sdtarwapld tgrhhvlany ppcrpcmfdt cpyghecata igvgdvmdra gellaeerrh
      361 vt
//
LOCUS       WP_175876107             141 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175876107
VERSION     WP_175876107.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..141
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15342
     Region          8..127
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mkpdqpdlsr hatdlgllfl rvaasvlllv vhglpkvvhy taeaaaiedp fhlgrtlsil
       61 faifaevvcp vfmivglypr laalpvmivt lvalvfvhpd wplrdaqfaw mllilfgtia
      121 iagagryvlp lplpgvmrrr a
//
LOCUS       WP_175876122             632 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia sp. BCC0097].
ACCESSION   WP_175876122
VERSION     WP_175876122.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..632
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=66998
     Region          5..543
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mlratepars adlvvfngki atqdeqrsfv ralavkdgti vatgddrdvl rharddtaci
       61 dlngrtvipg lidahlqair ggmnfnlevr wdgvpslada lellgrqvrr tpaphwarva
      121 ggwtalqfae krgpttaeln aiapdtpvfv qhladsawln aaalralgyg rdtpdppgge
      181 lrrdlhgqpt glllarpdpa vlgaalarap rldaadrvns trqfmralnr vgvtsaidag
      241 gdglaypddy aavatlarrg elttriayal garhagreld dfakwialta pgdgdaflra
      301 ngagerllfs avdlgnflep rvalpasvev elaaivrllv hhrwpfrlqa tydesigrfl
      361 dvfeavdrdt pfdglrwcfd rcetisdani arvaalgggi tvqprmafqg eafiarhgaa
      421 aatrappira mlaaglpvga gsgamgaasy npfvalywmv sgrsvggtal yparnrlgrm
      481 ealrrytvgs awfsadehrk galvpgryad favlsddyft idvrriptls svltvvdgki
      541 vhaeqefspl apppppvspa wspvaagvga gaagadarar phgaaasdac avsgsdacra
      601 rghgrrfarp ryptasaaae rcgafgrgci af
//
LOCUS       WP_175876130             301 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175876130
VERSION     WP_175876130.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32221
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdkfsalraf vevaeaggfs sagrrldlaa ssvvravdal easlgtvlln rttrqvtlsd
       61 agavyyarak rvlgeladad alvadrgdap sgplrvsvpv ayglrriaph vaafvarhpk
      121 ldldlqltde rvdlvsarid vairlgdaap tadvvarplg tfrryvvasr ayldahgtpa
      181 tpgelvdhac lrfhfgvdqq twtfvgaqrt tqvvvtgrlk snhsevlrea aldgagiall
      241 pdwlvdtdle agrlqrlfdq ydvtpgsara vitalylpnq rgskrvtafi dfveslaraq
      301 p
//
LOCUS       WP_175876218             274 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia].
ACCESSION   WP_175876218
VERSION     WP_175876218.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 274)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 274)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..274
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28448
     Region          1..274
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mldltfplrw rvalvapala vfaafwllpm aslvqvsadg affshyaall gnarymkslg
       61 etvalsagvt latlalstis glllarrefa gkrvllallt fplafpgvvv gfmvimlagr
      121 qgligmlsak ltgdkfvfay svaglfigyl yfsiprvivt viaaasklda sleeaarslg
      181 aspwrifvdi vlpalapgli aagaicfata mgafgtaftl atdlnvlpmt iyteftlnan
      241 iataaglsiv lgvvtwavla larrftghta aaaa
//
LOCUS       WP_175876219             298 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0097].
ACCESSION   WP_175876219
VERSION     WP_175876219.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..298
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31364
     Region          32..261
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mqslsgsstp spapaplhak raarhaprva garaiaalqw gvtlllcafl ivpvvmsvla
       61 gltvnyfrgl ssgltlrwle qvwqqyhgsv alslyvafat laivlavgvp agyalarsks
      121 riaraieeal vlpvalpgla salallvvyg gftafrmslw fivvghvvft lpfmvravaa
      181 vaagadlrti eegaaslgas fvtrfvtivl pnlrpgivag alavltlsig efnltwmlht
      241 pdtktlpvgl adtyaslrle vgsaytilfl lmtlpllvam qwlgvdpsgt ralkkrar
//
LOCUS       WP_175876220             343 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Burkholderia].
ACCESSION   WP_175876220
VERSION     WP_175876220.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..343
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36679
     Region          8..343
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkldstpitl tgcaktfrgt rvlepldlsi gagetlvllg psgcgktttl rliagldtpd
       61 aggtiafgdd dvtalpierr qvgmvfqnya lfpnltvrgn vgyglkirkt epralrervd
      121 ellammrlda hadkpvdqls ggqrqrvala ralavrprvl lldepltald aklrdvlrrd
      181 mnallrelgv ttvyvthdqa eamelgdriv vmgagrieqi gtpreiyyhp anrtvaqfig
      241 tlnrlagqwr dgalattggt ivtphaadew ffrpedaqla dpahaplrga vgacaflger
      301 trltiehaap dalvidvpgr ialargtavg ltiapegliv lga
//
LOCUS       WP_175876295             299 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Burkholderia].
ACCESSION   WP_175876295
VERSION     WP_175876295.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 299)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..299
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32408
     Region          30..>77
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          80..299
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          216..296
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msatrlpdsa rywrtplvpd adlltatyrd hafaphwhda ytipvildga erftyrgagh
       61 vaetgtvpvi npgevhtgsr aadegwcyrv sympvefihe lastiagrpq dapwfapdvi
      121 rdadlaarlt lahrmleags eralsshapg qpagdpaaga priydplaae tamldalstl
      181 ivrhadvrpq paplaadepr vdamrerlaa dltctvtldd vaqtvglspf haarlftrtt
      241 gmpphawrnq lrlqralapl ragvpvadva aasgfvdqsh ftrhfkrmfg vppgrwqas
//
LOCUS       WP_175876390             418 aa            linear   BCT 11-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175876390
VERSION     WP_175876390.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..418
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45287
     Region          12..395
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mlkrfgnpdv akavanlvwl glerltqigv aiaisgllar yfgpdvfgkw qyantlllvl
       61 apltwvcgae ilvptivqrp paqlgavlgs afvlriavsv aalaatwvai aagafdplvg
      121 amlaglavtm vfrepfvgvi nawlqsmtys kpqlvtsmlt alakallvwl lvraaagpar
      181 fawlwaleaa aiglalllyy rhrnggalgw tfdkplfrhf atagtvfwlg licmylflkl
      241 drlmlerhvs fadlgrysaa qqlnenwitl almlaqtiap afvyrvqdva rlrrnivrli
      301 amtaglmtag alvldaaapl ivgkvfgrgy easvdifrwa vwlsvpagie aignlivlky
      361 qakfvlltkw llalaiaalv nlftiprlgl ygalvglaag ylaaaavnfy yirfklrt
//
LOCUS       WP_175876366             222 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0097].
ACCESSION   WP_175876366
VERSION     WP_175876366.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..222
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23097
     Region          12..213
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msfppasmls dgfflslslc ldiglvnvam lsltlshgfr pgfwlgvgsc vgdlvyaala
       61 lagmavllqf epvrwivwig ggavllfltw kmarealapa kaaddnadda apprasarrs
      121 fvrgmllams spsailwfaa vggaliakag attpatasvf lsgfflggla wtlfmctlas
      181 qgrkragagl mrachiasal lfayfsysvi vggyrdlivh aa
//
LOCUS       WP_175876407             260 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia].
ACCESSION   WP_175876407
VERSION     WP_175876407.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..260
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29306
     Region          7..260
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mltlsladlk qsiaswrlwt llgwleirqr yarsrvgpfw ltismgvmit slgvvygtlf
       61 gqkmneylpf lassivlwgl fsqtvqegsm ayissgsyir qmatpkliym lqviwrnliv
      121 lahnfvivia lllifgvkdw evlpvfvpal lvfilnalwi amvagllsar frdlpqiiga
      181 llqvafyvtp iifrpnalnr fsfivdwnpi aylidvvrgp ligqmpsalt wgvtigmaii
      241 gwpiallltg rylkripywv
//
LOCUS       WP_175876431             212 aa            linear   BCT 11-JAN-2025
DEFINITION  2-hydroxychromene-2-carboxylate isomerase [Burkholderia sp.
            BCC0097].
ACCESSION   WP_175876431
VERSION     WP_175876431.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Thompson,L.C., Ladner,J.E., Codreanu,S.G., Harp,J., Gilliland,G.L.
            and Armstrong,R.N.
  TITLE     2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class
            glutathione transferase from Pseudomonas putida
  JOURNAL   Biochemistry 46 (23), 6710-6722 (2007)
   PUBMED   17508726
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122490
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..212
                     /product="2-hydroxychromene-2-carboxylate isomerase"
                     /EC_number="5.99.1.4"
                     /GO_function="GO:0018845 - 2-hydroxychromene-2-carboxylate
                     isomerase activity [Evidence IEA]"
                     /GO_function="GO:0043295 - glutathione binding [Evidence
                     IEA]"
                     /GO_process="GO:1901170 - naphthalene catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24070
     Region          12..191
                     /region_name="DsbA_HCCA_Iso"
                     /note="DsbA family, 2-hydroxychromene-2-carboxylate (HCCA)
                     isomerase subfamily; HCCA isomerase is a glutathione (GSH)
                     dependent enzyme involved in the naphthalene catabolic
                     pathway. It converts HCCA, a hemiketal formed
                     spontaneously after ring cleavage of 1; cd03022"
                     /db_xref="CDD:239320"
     Site            18
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239320"
ORIGIN      
        1 mttgldtaqp awffdfvspf syllleqhdk wpdvpfepva vslsdlqrhw gqratadvpa
       61 krvftyrhal fraeqlgirf kmppahpfds dkvlrlaial radiatvlem frfiwregnd
      121 pstpegfaal cervgvshgd eliefeetaa qltrnttdai algvfgvptf wmnqqlfwge
      181 dalpmvlyca rmpnwlesre vkristlpkg ra
//
LOCUS       WP_175876432             314 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0097].
ACCESSION   WP_175876432
VERSION     WP_175876432.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..314
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34934
     Region          23..69
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          101..302
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(116..117,119..120,123,127,129..135,228..233,
                     239..240,242..243)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 meddrtasld iwlvrvlrtl llersvtqaa lrlnqtqpai stalrklret lndpilvrgk
       61 sgmvpteyga slleaasral revdfiatph gdfdpssarr tfrvaapdyl ndffmptlie
      121 rfrdaaphah leidslnpal dhagalesga ldlvignwpn pdpqfarqdl fsdtivclmr
      181 dahplarapl treayasaah vaptpytgdk rnaieiglar arltrrivtt lpyfgivpqv
      241 llqsdliftt trrfathyaq llplvvvtpp vpfpriksyl lthphpdrpt diawlcalmq
      301 svsdeltvar trkr
//
LOCUS       WP_175876481             152 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175876481
VERSION     WP_175876481.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 152)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..152
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15831
     Region          23..106
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(45,48)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mvpagvdpaa fdafdmqald agtfdaaidg agdalavvff wgvdcfncei akkamlaqpd
       61 airalglkwf hcnvyehhel grrfglhgvp twfffhrgkr lgratgwhgl aqfqaavaaa
      121 rgkiaaaada aaaaapager tagqhdplag gd
//
LOCUS       WP_175876561             403 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: type II secretion system F family protein
            [Burkholderia].
ACCESSION   WP_175876561
VERSION     WP_175876561.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..403
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=42469
     Region          10..403
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 msmrtppret rfawrgrrrd gsprrgivia fdaaaaratl ardgiavlsl dvrgparppa
       61 aaarditrft rqlasllqag lplapsleml ahtrtrdgvp riaaglarei vggrrfadal
      121 arypsqfgtl yrqlievgea sgslgivltr vaehrerada qwrklraala ypaavilfal
      181 aisaalmvwv vptfrqifdg fgaalpaptr allalssals awggvllaga atmglaaqha
      241 lrrsaalrha larrllrapl agsalerfaa arwcrslatl lgagvplada fatlertagh
      301 pvfahatahi aarvlrgvrl adamhsagcf pddvvqpiav aeetgaldtm ladiaalcer
      361 qldarldtla algepliviv lgalvgglvi amylpilqlg nvv
//
LOCUS       WP_175876592             434 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0097].
ACCESSION   WP_175876592
VERSION     WP_175876592.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45619
     Region          7..406
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mtspsssrra wtyenrllli lfmtfgfvff drlalsflfp fmsaelhltn tqlgmvssal
       61 altwalsgaa tgawsdargt rkpllvaavl gfsvcsalsg lvggfaslla fralmgiaeg
      121 pvlplsqslm vesstpsrrg lnmgllqgsa agllgamigp pvvigiatay gwreafyvsc
      181 ipgfliafci wrwvreappg gvrhvqadta avpaasgael srwallkern illcvliscf
      241 fltwfvviis fapvflvesr hlapsdmgvv mtclgaawvf wgfavpaisd rigrkptmig
      301 faliasmcpv vlihvgsvwa lgalvfvtyt glgcftlfma tipaetvppr aiasalglim
      361 gageliggfv aptvagfaad ryglqfamwt sttgallacv lsfglvetap avlrkrapag
      421 aaagrldthn lggr
//
LOCUS       WP_175876614             244 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: polysaccharide deacetylase family protein
            [Burkholderia].
ACCESSION   WP_175876614
VERSION     WP_175876614.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..244
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26887
     Region          71..225
                     /region_name="CE4_NodB_like_5s_6s"
                     /note="Putative catalytic NodB homology domain of PgaB,
                     IcaB, and similar proteins which consist of a deformed
                     (beta/alpha)8 barrel fold with 5- or 6-strands; cd10918"
                     /db_xref="CDD:213023"
     Site            order(74..75,140,144,180..182)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213023"
ORIGIN      
        1 mlartprypi lmyhqirplp pptdrlrsls vapdafrrqm tlfrqlgyrg lsvrelqpyl
       61 rgerqgkvfg isfddgflnv lthampvlda lgftatcyfv agrfggandw dagapttrsp
      121 lmtcedmlaw rdhgheigsh tldhvalsyv pvpvsafqlt eskrqlemls gqcvesfcyp
      181 ygdldarvrd qviaagygna tttrrgcaga addpfllpri pvaggvgavr lwfkcmkgrm
      241 agcq
//
LOCUS       WP_175876638             277 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: phytanoyl-CoA dioxygenase family protein
            [Burkholderia].
ACCESSION   WP_175876638
VERSION     WP_175876638.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..277
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30664
     Region          6..245
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mdamkrkaff edgavliegv lndeqlaqcr avfdwgmenp gpmattlldg teykshndna
       61 npyakerlda lvgtlpfgql fadlwgskhv wyfaeelfmk aggksarspw hqdtsylpwq
      121 gmhfgnawis fehvpkrnal eivrgshhgv rhdgttfqna edptdplhgg dvwprlpnie
      181 aerraapday dilswetkpg dvlllhpgvl hgggavdaef pdrhtlvlrf fgddavfspl
      241 pdesrsgftp agvlfveela glkagdpfra pcfrqlv
//
LOCUS       WP_175876646             223 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia sp. BCC0097].
ACCESSION   WP_175876646
VERSION     WP_175876646.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 223)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 223)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..223
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23412
     Region          31..130
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          130..222
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mkrtwmigav lviagvaaag tlygpdlvdg mryqksmaai deadkangga wpqpqetcff
       61 chgvhgqsqn awypslsgqp atyiaaqlra fatdqrrnat mgplsreldd akiaalatyf
      121 arqaparnea vpadaaldkr gmalvearsc rachgaaltg kdpaprlagq gqlyleaqla
      181 afrsgerhdp tgamnalaat lsgddtrava hylaglspdr aak
//
LOCUS       WP_175876689             402 aa            linear   BCT 11-JAN-2025
DEFINITION  benzoate/H(+) symporter BenE family transporter [Burkholderia sp.
            BCC0097].
ACCESSION   WP_175876689
VERSION     WP_175876689.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..402
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41719
     Region          11..399
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mqpntppgai rtigndwsvs aitagflavl isyagplaif fqasqaahas ndmvsswvwa
       61 isigagvsgl faswklkvpv vtawsapgta llvglfpqlt lnqavgaylt agliilaigv
      121 sgyfdrlvrh iprgiacgmm agillpfgmh afsaataqpv lgfgmiaayv ifrrllprys
      181 ivlvlltgaa latllgmthl gnvspslarp ifiapewtvg ttlslalplv vvsltgqflp
      241 gmtilrvsgy htparpiita tsvmslvvac fggitivvaa itaalctgkd ahedpdrryv
      301 aglangvfyl igglfagtiv tvffalpkaf vailaglali gaisanvhgi fedenhreas
      361 mitflatasg mtwlglgsaf wgivigsvay gvlnrvrgrr gd
//
LOCUS       WP_175876656             327 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175876656
VERSION     WP_175876656.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..327
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34952
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,146,160,162,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,220,
                     222..225,232..233,236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdmlenmrtf vrvvqagsfs avakqtdvat aqvsravasl eayaqirlln rttrkialtd
       61 sgrryferlq silgdvdqan aearnalvrp ygrlrvhtmp glgqshvtal avayrarfpe
      121 vaiemtysqr mpnlveegyd vsvvtaaslp dsaciahscg tsfsvlvasp aylarhgvps
      181 apadlarhtc lrldtpaean dewllhgpgg qtashavtaa pfhanapeal sialraglgi
      241 gslaiysaid dlrsgrlvrv lpdyrltmld vyamyasrrf ldakvrtfve hlrlglspal
      301 kadaraldal vapcgregar aaagvta
//
LOCUS       WP_175876696             456 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia sp. BCC0097].
ACCESSION   WP_175876696
VERSION     WP_175876696.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..456
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47690
     Region          <65..455
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          233..411
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mrsdlrfrva reqgqpascg vhrfpigraf lrgivaaacv agaqgvaaqa fhdaapaasa
       61 aaentdlddv pffnsarttw gslhapsvpl dvayashaln vsagierddp varfgacvay
      121 rvlcdtarga vergyasrfd yglasalpat garpafapgp vdlasaepft laqpdrgtra
      181 gaivgslhas laradlpagv aaqivrmlag rvdpkqrgah gdtfrvafep dhdatrpgrv
      241 rvtaldvrfr gqqvaavwfa aqagsrgayy dldgmplaga rfampvaatr isskfgarvh
      301 pvsgarhvhs gvdlaapagr avhasergvv tfigteprgy gkyvvirhdg gyasyyahls
      361 afeptlrtga rvmrgqrvga vgstgtatgp hlhfevrrha rlvdpielvh aaraaklkga
      421 qrvafnrvar darvqlasaa faqpvalskv vgreag
//
LOCUS       WP_175876715             293 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0097].
ACCESSION   WP_175876715
VERSION     WP_175876715.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..293
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31351
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mlldnlalfl rivekgglaa agrevglspa tvserltale rhygaalltr ttraisltde
       61 grtlvdgarr llaeadeles rvrlgvqtls gpvrlsapad lgrervvpvv daflaehpgv
      121 tvdlhlgdgy vdlvgqgldf airrgmlads slrsrslgra rrvvcaspay laahgtpahp
      181 dalashdciv mrfgqelyae wpfsidgvlk rvvvrgrrva ndgalvrawc iaghgvalks
      241 lvdverdlas gllveilrdf spgevdlqiv ypgsvaqprr vralidrlae ala
//
LOCUS       WP_175876722             210 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Burkholderia].
ACCESSION   WP_175876722
VERSION     WP_175876722.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22117
     Region          2..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 midlstlalf sgaclaltit pgpdmllias rsvsqgrrag fatlagiqag tychalaaaf
       61 glsqlfvavp laydvvrfag aayllylawk tfrsdatals pvasqrrrst atifrqgltt
      121 nllnpkmalf vlalfpqfvr peqgsitvqi lvlatvlnli glvangavil sasrlsqrig
      181 arrrpskvpq yllgsvfvgl aarlavagrn
//
LOCUS       WP_175876777             496 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175876777
VERSION     WP_175876777.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..496
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53497
     Region          72..450
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mttlaispri gaaaialafl agcttfskdg gfdavssaas erigkdavvv rtdadreavd
       61 qrtkellgkp lsmddavqva llnnrglqas yaelglsead lvqagrlpnp rfafsrtrag
      121 ageltlgrtf sanvfalltm platkierrr feqtkletad amlkvaadar rayveavaae
      181 qaahyaqqvr daasaaaela lrmrqagnfs rldyareqaf hadavaqhak arqqavaare
      241 kltramglwg ertryalper lpdlpkarpn lpdlerfamg nrldvqaakl qtqgvasslg
      301 lskatrfvna velgyvndye tgkghehgye isieiplfdw ggakvaraea iymqsanrla
      361 ktaidarsev resyaayvts ydvathyrde vvplrkrisd elllryngml asvfelltda
      421 reqvgsvngy idalkdywla etdlqmavgg rlpspgaths aesasesipd adaapqpasi
      481 peapsapatq phpegh
//
LOCUS       WP_175876802             177 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: methylated-DNA--[protein]-cysteine
            S-methyltransferase [Burkholderia].
ACCESSION   WP_175876802
VERSION     WP_175876802.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..177
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18798
     Region          1..165
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtpahlipsp lgdiavried daltglyfvg qkyfpslaim readalarsp varrvaeeia
       61 eyftgardtf svpihlrgta fqrrvwqell aipfgelvsy gditervglp msgaravgga
      121 vgrnpvsiiv pchrvvgasg sltgyaggid rkrallsleg agfsrgayqp tqqalaf
//
LOCUS       WP_175876825             380 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175876825
VERSION     WP_175876825.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..380
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40980
     Region          7..351
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msspypdesy rgfaaelrer lqacllpeae gaearghlpr aiwpalaaeg wldlplageg
       61 fvrsavflee lgrlgyagvr aaigvhafma asylawfgdd aqrerylarm rdgtavaala
      121 itedqagsdl sglqcsaaas ddgwrvngtk rfvsngsqat livalvrsna qrhalggcsl
      181 lvvdaeapgi trtplnllgw rsadvcdirf edvavprent lgkpdkafty lmrcldferm
      241 vagmlalgga gcsirlmnrf vrqrvvrgap lsanqtirhe lveliaelrl lrhfayqlvq
      301 qyvggklgsg dasilklrst elakraahlc aqfhgargyl sesdvarlyr datagtiaag
      361 aselvreiif dsvdsealld
//
LOCUS       WP_175876827             254 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: thioesterase II family protein [Burkholderia].
ACCESSION   WP_175876827
VERSION     WP_175876827.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..254
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=28030
     Region          19..254
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mtqaqagaaq arwclvprpv aaprlrlicf ayaggsadlf rnwvehlapd velvavrlpg
       61 rgmrlreply gewpalvedc asalapylge phalfghsfg grlayeiaqr mrpvlppgtc
      121 rglfiggcrs pdspqarpyl helpepafra alrtmggtpt evlederlmn lmlpimradm
      181 rlaelwgnwh rtpldvplhv yyghadpids easvagwrgf ttsgcelvgf dgahffldsh
      241 relllahmat rlrs
//
LOCUS       WP_175876891             304 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Burkholderia].
ACCESSION   WP_175876891
VERSION     WP_175876891.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..304
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32020
     Region          5..298
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhsrhevivi ggsfaglsaa mqlararrrv lvidagrprn rfaehahgff gqdgkppari
       61 vaeaaaqlaa yptvqriege artaerdahg rfhvtladgs rasadrlila tgirdelpal
      121 pglaerwgvt vlhcpychgy evsgqrlgvl athplsvhqa ilipdwgptt wftqgvvean
      181 eeeaallaar gvriehspvv eilgdaprid alrladgqvv pidalfigar tdmasdlarq
      241 lgcafdegpl gtairvdtwk qtsvagvyaa gdasslmtna tfasasgvaa gvgahrslif
      301 glda
//
LOCUS       WP_175876914             374 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: amidase [Burkholderia].
ACCESSION   WP_175876914
VERSION     WP_175876914.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..374
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37474
     Region          17..364
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mtgfidtftl ggpgptiaik dtidiaghpt raasralada ppaehhadvv rllldagwqi
       61 agkanmhela fgmtgindyt gtpvnpqdaa ripggsssgs aslvglgavd aalgtdtggs
      121 irgpaaccgv aglkptfgrv srrgvapaet tldcvgpfar eirtlvavma aiapgfdrar
      181 aaasaagctv aqltveadpa iaaaldaavr asglrshdvv lddmpaafaa glsvinaets
      241 rafghlvatg rlgadldarl rmaatttpaa laeaeavrar ftaqvdaale hadvlvlptl
      301 pvlpitlqqa rdgvsviams slirpfnlsg hpalslplpl agsplkaglq vvgrkgadeq
      361 vcaiaahfea alaa
//
LOCUS       WP_175876937             300 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175876937
VERSION     WP_175876937.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32758
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdrlqtmqiy vqivergnft qaadalqlhr pavtkavqql eqelgvrlln rstrrvsvta
       61 egeafharcv qllasiddaf asfpkqravp kgrlridial alaktivipa lpdfqqrypq
      121 ielvlgasdq padligegid cvvrvgtlkd ssmvartvga vsmatcaspa yiarhglprt
      181 lddlrthrav nfftgrnrrv lewtfrphge tvavklassl ltdnsealls cglaglgivh
      241 alrpalqpsi dsgqliellp gvpavpkpvs vlypnrahlp dkvrafidwl telfarrypa
//
LOCUS       WP_175876956             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0097].
ACCESSION   WP_175876956
VERSION     WP_175876956.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33004
     Region          9..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..294
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,229,246,273)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,193,
                     223..227,234..235,238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 madlrdvnln rlaifvavvd agsltaaaer lglaktvvst hmqrlesevg anllvrttrr
       61 lsvtdagrvf ydacrdivra teaaldavss dagplrgtlr vsvpidygal vvapavvalr
      121 drhpalavel vandrvvdlv adnldvairi grladsnyra vqlgtyekwl vaspafvarh
      181 glprapdala alpfvmlssl prphtleldd arggrasvrc vapvvsntat acraivlagg
      241 gfglltdfst addvaagrlv rllpgwrtap agihavypst rlpspkvraf ieamkgklge
      301 aptapttkrs wsk
//
LOCUS       WP_175876975             208 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0097].
ACCESSION   WP_175876975
VERSION     WP_175876975.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..208
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22187
     Region          12..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mfdlttlttf tavvlglfli pgpavllvls rtvqggrktg iltglgvasg dfvhtlfaav
       61 glsallmtsa lafnvvklvg aayliylgvr allekpsdps lpqvspvtpl kaylqaipae
      121 vlnpktalff lafmpqfvhp ergstfvqfa vlglifvvls slyttliacs irplgrivkr
      181 ltwltrwqgk iigsilialg lrvavqqr
//
LOCUS       WP_175876995             416 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia sp.
            BCC0097].
ACCESSION   WP_175876995
VERSION     WP_175876995.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..416
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=45628
     Region          8..>119
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mnrqqswtrt aapgeiiyse gfagepvlfl itdgkvelst rcddkrviva tlgrgeffge
       61 sallaaepra htakalsfcq ltvvpagvld eeiervsall rhivrtmirr vkrkddqlat
      121 ythadfmpgv lsyahvlslm agadareagd twarramqah aaetsvplae virkcraiag
      181 hsrphvlaml rrmeklnlvt ieaaqtdgag gvtdyaassd arqvvtfdaa rvidraqqva
      241 dhdldlsins elelieladl esligvdktl llnklsngei aeevfafrks kvlnyveqkg
      301 vayfsrrnar rggdvraled lvwvdqrtlf dvisafdtyd laklianldd ravadklfsv
      361 mtearrnevs wvmrrelkld pveiedieqr vleavraaka paagvtavas asasna
//
LOCUS       WP_175877014             850 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: type VI secretion system Vgr family protein
            [Burkholderia].
ACCESSION   WP_175877014
VERSION     WP_175877014.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 850)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 850)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..850
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..850
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=92939
     Region          14..800
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mgrlpnslml dagieqtnra lvletplgak vllpqramge srvgrdfdlt vdvvsreral
       61 hlkklmaqpv tlwvrqades ylpwhgyvha trrlgadggl tyyqlsfssw mrflqyrkda
      121 rifqdlttad iltkvfsghs qarghfrldv kdpgavrsyc tqyetdhnfv hrlmesegwf
      181 tyvehaedgk shtivvtddl fnckalatqr vpfyrgdrdg qagtlvewsg erttqsvgya
      241 fstadykrpa rtlqradrst vdqgdipqel evyeyaghys fpvtgesydr geramrirle
      301 emasrskrff gvgsvpcmda grwftledhp ehdadkpedr efailgvrwa iqnnlplgns
      361 rpfpgslqrr lsrlraeykd rqaafvskdp lgnesfvlae ievqrrsvpf rspfehrkpv
      421 mhmqtativg pageevytde lnrvkaqmhw drlgsnnets scwmrvilph agkgfggvfv
      481 prigqevavn yldgdcdrpv vsgvlfhsvn tphwhsngll sgfksqeysg qgfnqlvfdd
      541 stsqnraqlf sstansylhi gylidhsgnt rgnylgtgfe lkteasgalr agrglyvsty
      601 arggtssqpl dvkeatqhli dssgviqhrs laaadgqaet lddaqdaikn faattqsdaq
      661 gsmaggrtag ggtgsanafs qpvmllaspa dmglstqksl haaatqhvnl vsgestyvsv
      721 arswiasige klsffvqnag iklfagkgkv evqaqsdnie ltadktvkvv stsdsvnvta
      781 qkeitltagg asiriaegki fihapglvev kgsplifdgp agdsasaqla pskscaqqfa
      841 aaaqagsalv
//
LOCUS       WP_175877079             496 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sigma-54 dependent transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175877079
VERSION     WP_175877079.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..496
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=53169
     Region          18..139
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <157..464
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mvarspdang paapemtdvs vtapeagrkl fvimrtpdep llaqlrglgw eitvaktaga
       61 aqnmtcgvsv aaglvdftgf tsrdypalkm clsqpaigwi siaqagitig aavrelirsy
      121 cfdyvtlplp yewishvlgh argmaaldrv dgaayaasig ehgmigncea mqqlfstirk
      181 vaktdasvfi sgesgtgkel talaihersg rgkgpfvain cgaiphhllq selfgyerga
      241 ftganqrrag riesanggtl fldeigdmpv esqasllrfl qegkierlgg qesiavdvri
      301 isathvdldg aveagrfrad lyhrlcvlri hepplrargk didilahyvl qkfkadsgrk
      361 isgftsaald amrryewpgn vrelinrvrr aivmaesrll tphdlgldtp getepvtleq
      421 aralaertai enallrndhr inkaaaelgi srvtlyrmmi ehglndhdnn ggnggngdsg
      481 ghdgapsgda ghqrvg
//
LOCUS       WP_175877080             128 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GtrA family protein [Burkholderia].
ACCESSION   WP_175877080
VERSION     WP_175877080.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..128
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=13582
     Region          11..128
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mirtfhaaer arlirfgvsg lgstalhali aaamfalfda tpvianataf vgstafsyla
       61 ntlwsfsspv twgnfvrfla vamaglavtm llahgtdalg larawsivav vlcvppvtfv
      121 lhrlwtyr
//
LOCUS       WP_175877160             695 aa            linear   BCT 11-JAN-2025
DEFINITION  M3 family metallopeptidase [Burkholderia sp. BCC0097].
ACCESSION   WP_175877160
VERSION     WP_175877160.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..695
                     /product="M3 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=76857
     Region          4..693
                     /region_name="Dcp"
                     /note="Zn-dependent oligopeptidase, M3 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0339"
                     /db_xref="CDD:440108"
ORIGIN      
        1 msasantnpl ldfsglprfg eirpehvtpa ldtlldaasr avetasasdt pstwaavvet
       61 veqateplgr awgivghlna vadtpelraa ygenlprvte fwssvgqnla lyekykaiaa
      121 saeyatlsae rkkildnalr dfrlsgaelp edqkprfael qeqqaalska fsdhvldatn
      181 ayayfvtdea elaglpgdai eaareaaqkd gkegwkftlh fpsyfpvlqy adnralretl
      241 yrayatrase lgpqygdgkv ewdntaivid alklrreeaq mlgyrnfaev slapkmaesp
      301 qqviafledl atrarphadk dwdelrtfaa kelglaelap wdvayaaekl rqqryafsen
      361 evkqyfpepa alkglftvte tlfgvkikpd dapvwhkdvr ffrvenrdgs lvaqfyldly
      421 aregkrggaw mddararakr gstvqtpvay ltcnfsapvg gkpacfthde vitlfhefgh
      481 glhhmltrvd elgvsgingv ewdavelpsq fmenfcwewd vlssmsshvd tgaslprelf
      541 dkmiaaknfq sglgtlrqiv fsmfdmllhv dfdpagatgv tafareiner yhvipqaafs
      601 rwpntfshif aggyaagyys ykwaevlsad ayaafeeaaa asgsvldaat gtryrreile
      661 vggsrpames fkafrgrepq idallrhngm aasah
//
LOCUS       WP_175877240             323 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ankyrin repeat domain-containing protein
            [Burkholderiaceae].
ACCESSION   WP_175877240
VERSION     WP_175877240.1
KEYWORDS    RefSeq.
SOURCE      Burkholderiaceae
  ORGANISM  Burkholderiaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderiaceae"
                     /db_xref="taxon:119060"
     Protein         1..323
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=33420
     Region          39..323
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          89..119
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(90,94..95,98..100,102..103,107,110,119,121,123,127,
                     128..130,132..133,137,140,149,151,153,157..158,161..163,
                     165..166,170,173)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          121..149
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          151..180
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          226..257
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          259..284
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mskksknprk aaghakkqgk airnrynqsl gafgetwqvd apidagagpf alatalrnrd
       61 akavaaaldl phlnklkmac ytgsgpvggl salhvaayfd dlasvevlln agfdadartt
      121 tgtvplhhtg dpriikalva aganvnaven tgmsalmiat aadsldavha llaagadpdv
      181 iggvmqesal svaqltgnha ieqvlahvtt vqapclrqsp yetvgrgftm lhnaaamgsd
      241 alvnqclemg aspdvttesg mtpllvalln ghgstarilw dhkaqklnpt lspitdeefa
      301 aisaelrhvl eslnyqlapm ada
//
LOCUS       WP_175877283             255 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix domain-containing protein
            [Burkholderiaceae].
ACCESSION   WP_175877283
VERSION     WP_175877283.1
KEYWORDS    RefSeq.
SOURCE      Burkholderiaceae
  ORGANISM  Burkholderiaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
REFERENCE   5  (residues 1 to 255)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10249011
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderiaceae"
                     /db_xref="taxon:119060"
     Protein         1..255
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=27621
     Region          77..118
                     /region_name="HTH_MerR-SF"
                     /note="Helix-Turn-Helix DNA binding domain of
                     transcription regulators from the MerR superfamily;
                     cl02600"
                     /db_xref="CDD:470628"
     Region          198..247
                     /region_name="HTH_17"
                     /note="Helix-turn-helix domain; pfam12728"
                     /db_xref="CDD:463684"
ORIGIN      
        1 mtaratpttv ngkpclglad atvhlglaas skaavwrkiq vghlhglqda rgawfvpvae
       61 ldrhkaraad tarvgareaa allevatttv rdwaqrgvla galddggrws farksiaaha
      121 ktlavqregl tasqaarycs lgqvnsplrh lntlndavkr geltafvdan grrrfhqvel
      181 drflaerakq drhvpgtlsa keaaevlgva drstiawfae rgqldrvrig rywrypaksv
      241 qalkrkrdka aqakg
//
LOCUS       WP_175877325             540 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Burkholderia].
ACCESSION   WP_175877325
VERSION     WP_175877325.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 540)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..540
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58967
     Region          10..537
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msestvstqh epllslehlh vrfgdtvavd dvtlaigrge rvalvgesgs gksvtalsil
       61 rllrdaevgg aicfagqdla akseremrgl rgsdiamifq epmtalnply tigvqigeti
      121 vlhdgvsave arkraialla rtgiaeperr vdsyphqlsg gqrqramiam alacrprlll
      181 adepttaldv tiraqivdll lelqrdeaek rgmaillith dlnlvrhfaq rvavmehgrl
      241 vesgpveqif aapehpytqr llnsrpqrtv tpvmpiapvv ldarhvsvqf arkrpgfagw
      301 fgtvpvtava dvsvsvrqge tlgivgesgs gkstlamall glqktaagei efqgralsty
      361 rgreqtalrs nmqvvfqdpf sslsprhtie rivgeglelh rpdmtpdarr akslavlrev
      421 gldrtvlhry phefsggqrq riaiaralvl eprilildep tsaldvsiqq qvlkllanlq
      481 qkynlgyvfi shdlevigam ahrvavmqdg avvesgevsd iftrpshpyt qkllkavwka
//
LOCUS       WP_175877326             224 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: C40 family peptidase [Burkholderia].
ACCESSION   WP_175877326
VERSION     WP_175877326.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..224
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=23949
     Region          15..196
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mqhrsltqac artiaglfig alfaaapgaf adevssfnqn vtnstqigsg sslqqtsaqp
       61 ssggaksffa gmagkagdvv vgalnmigvr yrwggnspds gldcsgfvry vfqdtlgmsl
      121 prraeemsrv gekvsmsnlk pgdlvffntm rrtfshvgiy igdnkfvhsp stgstvrvdd
      181 ldsgywekrf tgarriesef ppmkpedlrr vratigddsa ngnn
//
LOCUS       WP_175877375             234 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175877375
VERSION     WP_175877375.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..234
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25334
     Region          4..224
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mqimnepdst psgaagpeai aerirtaile hrlapgaklt eaqlcdvfgv krgtirqala
       61 qlatdklvdl epnrgafvas ptlqevhevf emrriielav verlatgpga rrlkgvaali
      121 dkerkaferh dfaawirlsg efhtalatlm gnatlsecle glvarstlms alyeshgrsp
      181 cscddhdeil aaleagdpkq avtlmarhlq hvelkmldrp aqgqvdlrev fgga
//
LOCUS       WP_175877478             544 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Burkholderia].
ACCESSION   WP_175877478
VERSION     WP_175877478.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 544)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..544
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58955
     Region          1..534
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 manallqidg fsarfgakaa vqdlslsvgr gervalvges gsgksvtals ilrlaqqatl
       61 sgrmlfdged llakterqmr girgadiamv fqepmtalnp lytigkqiae slrlheglrp
      121 gdarergial lrrtgipepe rridsfphql sggqrqrami amalacrprl lladepttal
      181 dvtvrqqivd llielqeqea aargmavlli thdlnlvrrf aqrvavmeqg vlvetnatda
      241 lfsapqhayt rrlldsapqr dvepvaagaq tildvqdlav dyrvaakgwr avlgkttfra
      301 vhdvklnlrr getlgivges gsgkstlaat vlglqrpaag sieidgmpld alrttggrra
      361 lygrmqvvfq dpfgslsprm tveqivgegl avhrpqvaga arrarvaall qevglpaeam
      421 lryphefsgg qrqriaiara lavepellvl deptsaldvs iqkqvlnllt nlqkkyklsy
      481 lfithdlavm ramahrvvvm kagrvveegd tldvlhapsh pytrallass mlapvrgtqe
      541 rtdd
//
LOCUS       WP_175877485             299 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [Burkholderia].
ACCESSION   WP_175877485
VERSION     WP_175877485.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..299
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31150
     Region          73..279
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mtkrslaala asllmsvaai dglvapqlay aqasgtaats dastqaaapt sataepappp
       61 apaateaven pyglgalwkn gdfvarfvli llvimsmgsw yimitkfveq lranrrakla
      121 daqlwsapsl aegaklldea spfrfiaeta ieagehhdea lleavdrntw idvsversit
      181 nvsnrmqdgl aflatvgsta pfvglfgtvw giyhaltaig iagqasidkv agpvgealim
      241 taiglavavp avlgynflvr rnksvmervr nfgaqlhtvl lagskrsarv pspaaslvn
//
LOCUS       WP_175877496             330 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sugar kinase [Burkholderia].
ACCESSION   WP_175877496
VERSION     WP_175877496.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..330
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34857
     Region          6..301
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(37..38,41,93,108,110,139,172,261,264,300)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(230,235,251,261..263,266,288,292)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mkaaldvvty geamamfvat epghlahagq fakriagadl nvaiglsrlg frvgwmsrvg
       61 rdsfgryvld tlaregidas cvtvdprypt gfqlksrndd gsdptveyfr kgsaashlsc
      121 ddyvadyvlg arhlhltgva paisatscel afrlaremra agktisfdpn lrptlwpsad
      181 vmaktlnala tladwvlpgl aegrqltghd tpadiagfyl argargvvik lgeqgayfrt
      241 adgragtvag ervekvvdtv gagdgfavgv vsallegrsv eqavargnri galaiqvigd
      301 seglptrdal drlekvsnha drleetvtaq
//
LOCUS       WP_175877502            1048 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia sp. BCC0097].
ACCESSION   WP_175877502
VERSION     WP_175877502.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..1048
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114632
     Region          11..1027
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msvsheegrf nlsawalrhq alvvyliala tlagilaytr laqsedppft frvmvirtfw
       61 pgasarqvqe qvtdrigrkl qetpaidflr sysrpgesli fftmkdsapv kdvpetwyqi
      121 rkkvgdigyt lppgvqgpff ndefgdvytn iwtlegdgft paqlhdyadq lrtvllrvpg
      181 vgkvdyfgdp dqrifievnn aqltrlgisp qqlgqainaq ndissagvlt taddrvfvrp
      241 sgqfdnvdai antliringr tfrlgdlatv krgyddpqvt qmrtnghavl gigvtmqpgg
      301 dvirlgkald aeskdlqaql paglkltevs smphavshsv ddfleavaea vaivlvvslv
      361 slglrtgmvv visipvvlav talfmylfdi glhkvslgtl vlalgllvdd aiiavemmav
      421 kleqgytrar aaafaytsta fpmltgtlvt vsgflpiala ksstgeytrs ifevsaiali
      481 aswfaavvli pllgyhmlpe rkrhaheahl pddheheiyd trfyrrlrgw idwcierrfv
      541 vllitgalfv vammgfslvp qqffpssdrp ellvdlrlpe gasfaatlre terlekviak
      601 rpeidhavnf vgsgaprfyl pldqqlqlpn faqfvitaks vedreklatw lettlrdtfp
      661 avrwrlsrle ngppvgypvq frvsgdsiat vrsiaekvaa tmrgdartvn vqfdwdepae
      721 rsvrfeldqk karelnvtsq dvssflamtl sgttvtqyre rdkliavdlr apradrvdpa
      781 klaglalptp ngpvplgslg rftptleygv vwerdrqpti tvqsdvhaga qgidvthavd
      841 aklnalraql pvgyqinigg sveesakaqk sinaqmplma iavftllmiq lqsfsrvlmv
      901 vltaplglig vvatlllfgq pfgfvamlgv iamfgiimrn svilvdqieq diaaghgrid
      961 aiigatvrrf rpitltaaaa vlalipllrs nffgpmatal mggitsatvl tlfylpalya
     1021 twfrvkrder dpqdgpppgg tpaapsga
//
LOCUS       WP_175877504             342 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia sp. BCC0097].
ACCESSION   WP_175877504
VERSION     WP_175877504.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10859374
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..342
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38615
     Region          3..98
                     /region_name="HTH_NolA-AlbR"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators NolA and AlbR; cd04788"
                     /db_xref="CDD:133415"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133415"
     Site            order(51,54,58..59,68,80,84,90,94,97..98)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133415"
     Region          <259..>305
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 mrlkvgdlak rsgltvrtlh hyhaiglltp saradngyrl ydrddiarlh qiqalrrfgl
       61 slaeigdyln qpgtplvdlv arqivsldrq laqtaqlrer laslhaqlaa gtepeladwl
      121 ttlelmtvyd kyfseeelar lpmyqksqag daewialvde vralhdagvp aedervrala
      181 arwmallvrd tnndprllak lnlmheheps mqskigista lrdyvlrasa etkmrlfeky
      241 lapdeirfmr ahygersmew pqlmadvrda idagtqpdsp qgralaqrwl elfcsyaghd
      301 pathakfrha lmnepaltkd swtddtllgf vreamaqlap ar
//
LOCUS       WP_175877525             316 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175877525
VERSION     WP_175877525.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..316
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33905
     Region          21..78
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          107..301
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(117,121,160,174,176,235,252,280)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(118..119,123..124,126..127,130,134,136..142,203,
                     229..233,240..241,244)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mtsdpgsdpi papdkpldll dvalfvraal lanvtaagre fgvsaavasa riaqlerqlg
       61 arllhrttrr isltqdgeif mvradallaa adaarasvgr grsepygrlk vsmsssfgrq
      121 hvapvipafl rrypsvsldl rlsdeivdlv ddgydvairl galkdstlva rklatnrrvl
      181 ccspaylaer gtprhpadlt qhecvilgdq rdwsfttpqg pltvrvggrl vasngeaire
      241 alvdgfgiai kstwdvgpll asgalvsvld dypfaddvai wavypsrahv plktlafitf
      301 laehfgdppy wdrasg
//
LOCUS       WP_175877570             250 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: HesA/MoeB/ThiF family protein [Burkholderia].
ACCESSION   WP_175877570
VERSION     WP_175877570.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..250
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26437
     Region          2..248
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mnddqllrys rhilvdeigi eaqqrfldah aivvgagglg spaamylaas gvgtltlvda
       61 dtvdltnlqr qilhvtasvg rskvesgrda laqlnpevtv navaervdga wldahvphas
      121 vvldctdnfa trhainracv ahgvplvsga alrfdgqist fdfrdaaapc yacvfpedqp
      181 feevacstmg vfaptvgiig amqaaealrv iggigktlng rlmmldslrm ewttmkiarq
      241 adcpvcggrh
//
LOCUS       WP_175877580             381 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175877580
VERSION     WP_175877580.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..381
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40639
     Region          1..376
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfqhtedrr mladtlnrfi aeqyafpvre riaqsaegcd ramwrrfael gtvgalfsea
       61 dggfggagfd iavvfeclgr glvvepflga llagralala ggdahrerla alidgsasaa
      121 fahdepgshy elttvrtrae rtaegwvltg akgvvdqaaq aaffvvsarv sgsdddaagi
      181 glfvvpadap gvslrdyrki dggraaevrf ervalppdaa lgapdaldge agaellervl
      241 gygllalsae algamdvake htldylrtrk qfglpigsfq alqhrmadll leveqarsav
      301 inaaaqldap ravreralaa akysigrigt lvaeesiqlh ggigmtwelp lshyakrlvm
      361 idhqlgdedh hlaryialsk q
//
LOCUS       WP_175877614             307 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175877614
VERSION     WP_175877614.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..307
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=31517
     Region          167..306
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mavsglasag cvladtrapv vvlsgnidtg rdaplgaeia rftwnttdft fgtrctpgtv
       61 tlantvtpnm gpgvgnlypt sikgvsvrig lndtsvngdm ifpnsytlka gpgspifpgv
      121 simwrnltvf yslvktgpid ggaitrlpda amaldgktyl varavgnvtl kaascttpdv
      181 svslgrhsma efpgvgatsk piafdlkidn cpdglksigy rfeapagtld aaggvialna
      241 ssttkgfgvk lmdgagkaid lrrsyeiapr pglrsysvpl qgalyrtamn asggradavl
      301 tvtmsyl
//
LOCUS       WP_175877620             423 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175877620
VERSION     WP_175877620.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..423
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45084
     Region          67..298
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mafskvlvgw maacalsaaq agtlpsantg agasgslaha ehfdyadanl pqvaadlneq
       61 ilripadasg aitleatlfk pngpgpfplv vfnhgkntgd lhlqprsrpl afarefvrrg
      121 yaviapnrqg fagsdgtyrq egcnvgkngl aqaadvdatv rymahqpyvd asrivvagts
      181 hgglvsvayg teaaagvrgi infsgglrqd lcdgwqrnlv dafdqygaht avrslwlygd
      241 ndsvwtpalv aqmhdaylsh gtqaqfidfg rykddahrli vdrdgvpvww pavhaflael
      301 nlptavryav anphepkatg yasidavnav pyvdeagreg yrrflnqhps rafavssega
      361 wswaeggddp malaldncak qgagacrlya vndrvvwnds ttqtadngdt ptrdtdtral
      421 asr
//
LOCUS       WP_175877638             741 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia sp. BCC0097].
ACCESSION   WP_175877638
VERSION     WP_175877638.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..741
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=78027
     Region          6..741
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mntltgqpld rvdgvlkvtg gahyaaefsd arlahavlvt stiasgries idaararamp
       61 gvlivithen amrlpnggrp plsppagrrl tllqddtvry snepvavvva etleqatdaa
      121 havqvryras eavvdfaqak rgarvppkqq gramdtqrgd veaglregav gidatyttpm
      181 qhhnpiepha tmarwdgptl tlhdatqgvs gastavaavf giapehvrvi spflgggfgc
      241 kgsswshvsl camaakqvgr pvrlaltrpq mfgpvggrpf teqrivlaar qdgtltamrh
      301 dtiattstfe dwtetcgmls rimyavpnqa tthrivslnv gtptfmrapg easgsfales
      361 amdelawrlg mdpvalrlan yaevdpqdgk pwssnklrec yeagarrfgw srrtgaprtm
      421 rdgdtliglg maaatypanr seasararil pdgtaevasg tqdigtgtyt vmtqvaadal
      481 gfapqnvrfs lgdsslprap vsggsqsaas vapavreaal qarakliala iadpgsplhg
      541 aaaddvtvdn gwvvhrgeps rrdpaaavia raggqpidaq atakpgdeks ryashsfgav
      601 faevhvdael gtirvprivg vysvgrllna ktarsqligg mvwglgtale egshldvrhg
      661 rftnanlaey hvpvnadige ldvsfvdend thfnplgirg igeigitgvp aaianavyha
      721 tgvrvrdlpi tldkvatpir a
//
LOCUS       WP_175877640             252 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175877640
VERSION     WP_175877640.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..252
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=25985
     Region          <5..87
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          85..240
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mssdrsdsps aepardaaps plgpgrsaaa pplphdtpss aarrrflqsa aaaatvsaas
       61 hvhpqppyaa stpaaprrdt vpaqpvrldi ngraytlqle prvtlldalr eyagltgtkk
      121 gcdrgqcgac tvlvdgrrin acltlavmhe garittvegl arggelspvq rafvecdafq
      181 cgyctsgqlc satalldefa agagsaatdd vrrrpanlsd deisermsgn lcrcgaypni
      241 vaavraahaa hg
//
LOCUS       WP_175877650             358 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia sp. BCC0097].
ACCESSION   WP_175877650
VERSION     WP_175877650.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..358
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=38221
     Region          31..358
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkafarrasr tsvkliaaaa cvvaaapvha qssvslygqv dewvgatkfp ggdrawnvsg
       61 ggmstsywgl hgaedlgdgy kaiftlesff raqngqygrf qgdtffarna yvgisspygt
      121 vtagrltthl flstilfnpf ydsytfspmv yhvflglgtf ptypsdqgav gdsgwnnavg
      181 ytspsfggln fgamyalgnq agdnrskkws aqfnyangpf aatavyqyvn fnngpqdlsa
      241 lvtgmksqgi alvgatydlk lvklfgqymy tkndqvagsw hvntaqggvs vpigvgnama
      301 syaysrdagg ldqtrqtwav gydyplskrt dvyaaymndh isglstgntf gagirakf
//
LOCUS       WP_175877647             163 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia sp.
            BCC0097].
ACCESSION   WP_175877647
VERSION     WP_175877647.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..163
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17761
     Region          13..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mlkrlsppav asldatdrai vaaladdari atselarqig lsapatadrv rrleaqgvia
       61 aftveldpra lgytlqaivr vkplpgqlhl vegllrripe fvecdkvtgd dcficrlylr
      121 tiehlddils kvteraetst aivkstpvpr rlpplveddh ahr
//
LOCUS       WP_175877750             349 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175877750
VERSION     WP_175877750.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..349
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38465
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdhlqsmrvf vkvadlgsfa raasamdisn avatrhvadl egrlgtrlln rttrslslte
       61 sgqvylerar qildeledve qmvvarnhep vgtlrivapv vfglhnlapv lqsytenfpk
      121 vvpdltlvdr qvdlveegfd vgivvtrqmr sasivtrrlt tgcmtvcatp sylekhgvpt
      181 hpeqlaehpa lslpteywgd ervftgpdge vrvrptnviv anntamlrqf allgmgvail
      241 psyligsdia rgalvrllpd frlpqveini aypsrrhlpa kvrtfidhlv ehfshstdat
      301 mgeqwaaqsa tlppigvemr aeqpestdpn lqpriarspr trvampspl
//
LOCUS       WP_175877734             347 aa            linear   BCT 11-JAN-2025
DEFINITION  M48 family metallopeptidase [Burkholderia sp. BCC0097].
ACCESSION   WP_175877734
VERSION     WP_175877734.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Lew,R.A.
  TITLE     The zinc metallopeptidase family: new faces, new functions
  JOURNAL   Protein Pept Lett 11 (5), 407-414 (2004)
   PUBMED   15544561
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..347
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36777
     Region          132..315
                     /region_name="M48C_Oma1_like"
                     /note="Peptidase M48C, integral membrane endopeptidase;
                     cd07331"
                     /db_xref="CDD:320690"
     Site            order(198..199,202,255,259,299)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320690"
     Site            order(198,202,255,299)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320690"
ORIGIN      
        1 mrgnrlhrla rvtaalsvga aalaatsaya tdigataags apaaappapa tsaapvppsa
       61 aegaqptgaa vpakaytptp pqvrygnaia frtlipspll eqltaneyaq ivqtaadsnr
      121 llsanqprvk rlraivakla pysvkwndrv kswawdvnai rsrdirltcl pggkvlvygg
      181 mldrvrlndd elgvllahgi ahalrehars nfsvssqtsl raaalpplfg vgdplpqaln
      241 lgerlqslhy dptdeteadv iggdiaarag fdpraaitlw dklavatran kasgfiythp
      301 ysaarrqdll nrlpdlmply akatgkrves lpdyagisaq rrkitrr
//
LOCUS       WP_175877834             324 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175877834
VERSION     WP_175877834.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..324
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35912
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdriqamevf trvvdansft raadtlampr asvttiiqnl eallgvrlmh rttrrlsltp
       61 egaayyehcm kiiaeiaead asfqagnrkp sgvlrvhmpn slgrrvvlps lsifrqrypd
      121 itlelglsdr yvdpveegid cmirvgpled ssmvarrigm lkrvtcaspd ylarhgepne
      181 iadlvehhav nfrsshgara ipwvfmidgk pfevrmnasv tvndsdayvt cglegfgmiq
      241 ptlfmvlphl ldgslvevlp dcnpkpkpis ivyphnrhls qkvrvfadwi aevfestpal
      301 eggenwrgkl raetpdaqrg vvva
//
LOCUS       WP_175877835             552 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175877835
VERSION     WP_175877835.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..552
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58928
     Region          18..538
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(31..32,35..36,39,77,135..136,138..140,143,163,
                     166..167,170,256,259..260,263..265,268,296,300,464..465,
                     469,473,489,492..493,496..497,500)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 matlggqish spmtgeekkv ifasslgtvf ewydfylags laayisksff sgvnptaafi
       61 ftllgfaagf avrpfgaivf grlgdlvgrk htflvtivim gistfvvgfl pgyasigiaa
      121 pvifiamrll qglalggeyg gaatyvaeha panrrgfyta wiqttatlgl flsllvilgv
      181 rtfigeeafg nwgwrvpfva silllgvsvw irlqlnespv flrikaegkt skaplteafg
      241 qwknlkivil aligltagqa vvwytgqfya lffltqtlkv dgasanilia ialligtpff
      301 lffgslsdki grkpiilagc liaaltyfpl fkalthyanp qlelatqkap itvvadpatc
      361 sfqfnpvgts kftsscdiak salakaglny envaapagtq aeikvgdtvi qtydgkaada
      421 kaqgaafdkt lastlkgagy pakadpaqln wpmtivilti lvifvtmvyg piaamlvemf
      481 ptrirytsms lpyhigngwf ggflpatafa ivaakgniys glwypivial atfvigllfv
      541 ketkdsdiya qd
//
LOCUS       WP_175877870             318 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sugar kinase [Burkholderia].
ACCESSION   WP_175877870
VERSION     WP_175877870.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..318
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32948
     Region          3..296
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(36..37,40,91,105,107,136,168,256,259,295)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(227,232,247,256..258,261,283,287)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 maeivvagel laefvaaerg qgfdtpglfe gpfpsgapai fadqaarlga rvayagcvgr
       61 dafgdaivar lardgvdvar irrvarptgt afvayrddgs rsfvftlsts aaacvdasdv
      121 dttmfdgcry fhvmgsslts esaiaavqrg vieaaragak vsfdpnvrpe mlsfrpmraa
      181 ldemlaachl flpseadlpf fcgpqpaera iagllathpl lervvlkrga qgsvafdrah
      241 raeapafpvd evdptgagdc fggtlvaslv agaavdvalr ranaagaiav trrgpmegns
      301 saaeidrflt ergiacpa
//
LOCUS       WP_175877842             895 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: type VI secretion system Vgr family protein
            [Burkholderia].
ACCESSION   WP_175877842
VERSION     WP_175877842.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 895)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 895)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..895
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..895
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=97880
     Region          15..827
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnsqalrsal lagpvqherl ikldtplgpd vllpqrvtgr srlgrhfeft vdtvsvsddl
       61 elkkliaqpv tlwiqqsdqs yaphhgyvha arrlgsdsgv thhqivfasf lhflkfrrdq
      121 riwqdrsadd iiadvlnqhp qakgrftfkl yqplpsrsfc mqyeddwnfv hrlmesegly
      181 gfweqdddgk ahrlvivdri dalpalsprt vrfhhagtgd eadtlvqfsg trtlrsvart
      241 trtfdykqpp tasnpkatht ptianqgdlp qqlevyeytg aytypeqsrg dhlskiwmee
      301 qeshakrfhg vggvrrmdag rvfefaehpe hdkddagqre favietawvi vnnlpvadep
      361 avfphslqae igsimqatdt grsrvrhpdg segffqvrie aqrttvpfrs pfehakppmh
      421 lqsaivvapq geevhtdeln rvkvrfhwdr lndgdekasc wlratasdsg ngygavhphr
      481 sgeevlvdfl ggdcdrpiiv gkvyngatsp qwhsngilsg yrskeyagag ynqlvlddat
      541 aqnrvhlyss qanthlhlgy lidhtgnnrg sylgsgfdlr sdaygavran rglyvsthpk
      601 qaasqpldvd etreqlvraq glidamsqvs aqhqgesldp ghtalkqfsd atrnsvsgsa
      661 sggrtagggt gnanafkepv mlfgspagig mstqqsaqfs adqhinlvsg qsthvaagks
      721 liasvldris lfaqnagmkl fagkgkvevq aqadnielta qkalkliavt qsiegaaake
      781 illtsggayi riadgnievh apgkidikga qhafsgpthl sqtmptlpns sgnydqafia
      841 hwagtdipva ntryqmfsng kllsegvtna agetgltqsh vphdvvvkfl gksng
//
LOCUS       WP_175877932             238 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: pseudouridine synthase [Burkholderia].
ACCESSION   WP_175877932
VERSION     WP_175877932.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..238
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=25574
     Region          6..224
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mdlesilytq gfgsrrqcrg lietgrvtva gaaatdpdap fdtdglvfsv ddtawpfhar
       61 aylalnkpag yecsrdpqhh asvfsllpap lvargvqcvg rldqdttgll llsddgqfvh
      121 aytspkrkvp ktyvatvrhp lddaqlhalr tgvqlhgepk piaavaadar dthalaltvl
      181 egkyhqvkrm vaaasnrvel lhresiggfa lpadlapgaw rwldaadlaa lrnsvktl
//
LOCUS       WP_175877901             235 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia sp.
            BCC0097].
ACCESSION   WP_175877901
VERSION     WP_175877901.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..235
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25086
     Region          18..228
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mpsslapylp qieanpwfag lppalradli aratlrrlps ghalfrrgdp pcglyavlag
       61 sltigavdpq gkealltvae pvtwfgeial fdgqprthda ialddalllh vpqaallail
      121 dttpqywrqf allmaqklrl sfltvesmsv mpaaqrlaar llmiaegygg isagrthirl
      181 sqetlasmls ltrqttnqll kalqadgavr lhvgeielvd idalrrasgl gdgas
//
LOCUS       WP_175878007             234 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: pirin family protein [Burkholderia].
ACCESSION   WP_175878007
VERSION     WP_175878007.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..234
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25042
     Region          10..234
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mfkilraedr chthhgwles shsfssvcrd ghapvrppvg alcvlsedli aptrgfgmqp
       61 rrdveivtyv ldgelahrds lgcgaivrtg giqrmsagtg lvhsetnasr drplhlvqiw
      121 lqpaerggrp gyeerrfadd ekrgrlrlva apdgsdgals mradarifag lidgdettaf
      181 evpagrsvyv hvargevevn gralaagdga riggvdavaf argrsaevll fdva
//
LOCUS       WP_175878016             207 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0097].
ACCESSION   WP_175878016
VERSION     WP_175878016.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22128
     Region          6..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maergrprsf dkeaaldram evfwrlgyeg asmtdltaam giaspslyaa fgsketlfrq
       61 alehyrateg qeiwggvera asaydavqsy lmdtarvftr rskpagcliv lsalhpaers
      121 dmvrqtliam regtvdalrg rlaqgvatge isahaeldai aryyvtvqqg msiqardgas
      181 rrdleavaqa alaawpalvg tgsaagv
//
LOCUS       WP_175878092             519 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [Burkholderia].
ACCESSION   WP_175878092
VERSION     WP_175878092.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..519
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56066
     Region          34..454
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msagpaglth dvpaapfern atmsdsvakp vdatfdqfgl apdilkaive qgyttptpiq
       61 aqaipvvlag rdvmgaaqtg tgktasfslp iiqrllpqan tsasparhpv raliltptre
      121 ladqvaanvh ayakhtplrs avvfggvdmn pqsaelrrgv eiliatpgrl ldhvqqktan
      181 lgqvqilvld eadrmldmgf lpdlqrilnl lpkerqtllf satfsgeikk lastylrnpq
      241 tievarsnst nanvtqivyd vaegdkqaav vqllrdrglk qvivfcnski gasrlarnle
      301 rdgvvasaih gdktqiermq aldafkrgei ealvatdvaa rgldiaelpa vinfdlpfsa
      361 edyvhrigrt gragatgdal slcspnerkq ladieklikr pldvqtltid kparqrhder
      421 ggernsergg erggerggrr erdehrgaag rrtgspersg hhrrheapvd dfflkpyeps
      481 asakqpddaq paqqpekkgp krqvaallgg fgmprkpsa
//
LOCUS       WP_175878096             392 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 9 protein [Burkholderia].
ACCESSION   WP_175878096
VERSION     WP_175878096.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..392
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43055
     Region          8..369
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 malfssarpp rtilvaaprr igdvllttpl vrslkarwpd aqidmlvfrg tegvlehnpd
       61 vrrvivvaqr agfgerlrda lsmwrrydla caalssdrpr fyswfagrkr vglvdpnrvt
      121 wltrmmlngi ainhhesaht vvstlalapv lgiepvsevv apgigddpar rarfdawlae
      181 spavragkpl vvlhpypmfr ykqwrldgwv emigwlreqg favalsggpa drereyaeqv
      241 ateaggdvln lvgrltfges aelvrrarlf igpdtgathv aaatgtdtia lfgpsdpvrw
      301 gpwpqhwpat enpwalrgsg rhanvwllqg egdcvpcrhe gcerhvdsrs dclvhldaqr
      361 vkaaaaemlg lnppgpadvi vdtsrlrrag sd
//
LOCUS       WP_175878119             871 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia].
ACCESSION   WP_175878119
VERSION     WP_175878119.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 871)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 871)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 871)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 871)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 871)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 871)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 871)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..871
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..871
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=91650
     Region          35..871
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mkgpqhaaqp pagqpghdgr ahagrfglrd lihqaarmta rdwrageltl lvlalvlava
       61 altsvgflad rlrqglerda rqmlgadfvv radrpvdpsf drqaralglr tattaifpsm
      121 iaaaaggqaa daapsrlaav kavspgyplr gaveilpaga atarkaaaip apgtvwadpa
      181 lldalhlkag dtvrvglrtf tvaaaitrel drgfsfvnfs prlmmradel aatgltgygs
      241 rvtyrllvag dapaiarfet yahqrvdggk lrgvgleslq egqpqvrqtl drarhfltlv
      301 alltallaav aiamaaqrym rrhldgcatm rclgvsrrtl galfalefvg lgivsgaaga
      361 vlgygghwal laalgslidv vlppptlwpa ligmgaalvl llgfalpplv pltrvppvrv
      421 lrrewgdasr tawaayaigv vlfaglliva agnlklgliv aggfagalvg faliarlvlf
      481 aaaravrnar vaagvgwrya laslhrrgta salqitalal glmcllliai trndlvagwr
      541 qstppdapnq flidiqpdqr advaaylaah gvrdavpapm vrgrlvaing kpvnpdayps
      601 eearrlvdre fnlsyttelp sdnrivegdw fgtaatpqis ieaglaktln vkpgdtlrfd
      661 vtgltvdapi tsvrkldwgs frvnffvlmp ppvlkdfpav yltsfhlpas naalldplia
      721 rypnltaidv apilaqlqrm mlqvvgavqf lfaftlaagv lvlytalags rdervreaal
      781 lralgasraq vgavqraefv vvgalagtla sagaiavgwv lasrvfdfql avdpwlvpag
      841 iaagvvcaga agwlslhnvl rrpalqslrd a
//
LOCUS       WP_175878120             243 aa            linear   BCT 11-JAN-2025
DEFINITION  alanyl-tRNA editing protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175878120
VERSION     WP_175878120.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V.
  TITLE     Evolution of aminoacyl-tRNA synthetases--analysis of unique domain
            architectures and phylogenetic trees reveals a complex history of
            horizontal gene transfer events
  JOURNAL   Genome Res 9 (8), 689-710 (1999)
   PUBMED   10447505
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Cusack,S., Hartlein,M. and Leberman,R.
  TITLE     Sequence, structural and evolutionary relationships between class 2
            aminoacyl-tRNA synthetases
  JOURNAL   Nucleic Acids Res 19 (13), 3489-3498 (1991)
   PUBMED   1852601
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Schimmel,P.
  TITLE     Classes of aminoacyl-tRNA synthetases and the establishment of the
            genetic code
  JOURNAL   Trends Biochem Sci 16 (1), 1-3 (1991)
   PUBMED   2053131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..243
                     /product="alanyl-tRNA editing protein"
                     /GO_function="GO:0002161 - aminoacyl-tRNA editing activity
                     [Evidence IEA]"
                     /GO_function="GO:0002196 - Ser-tRNA(Ala) hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004813 - alanine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006419 - alanyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=26323
     Region          3..243
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
ORIGIN      
        1 mttqalfred ayltqceaiv qavgddgirl drtvfyplgg gqagdtgtlt lpdgstiaia
       61 dtrkakfdga tpddavhvpa pgqeasvatl apgtrvvaei dwlrryrhmr lhtaahlmca
      121 vlpyavdgcs vtadyvrldf atsdaidrdd verrlagfvv gahpvtaewi tddemaerpe
      181 lvrtmsvkpp mglgrvrllr ienvdlqpcg gthvrntsei gglrvaklek ksartrrlvl
      241 efa
//
LOCUS       WP_175878134             339 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)H-quinone oxidoreductase [Burkholderia].
ACCESSION   WP_175878134
VERSION     WP_175878134.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..339
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=35545
     Region          1..333
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(40..41,127,131,134,157,160..162,181..182,186,201,
                     225..226,247..248,250,272..274,322,327)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mkaieitefg apdvlklaer prpepkrgev likvaasgvn rpdvfqrkga yapppgasdl
       61 pglevageiv ggdlsdaaln pfglklgdrv callagggya eyavaplpqc lpvpdgltdi
      121 eaaslpetff tvwsnvfdra qlgageggeq etllvqggss gigvtaiqia halgfrvfat
      181 agtadkcrac ealgaeraid yktedfvevv kslthdrgvd vildmvagsy vprelsalad
      241 ggrlvliall ggakaevnls eilrrrltvt gstlrprpve fkariaaqlk arvwplladg
      301 rikpviyrvl paadaaqaha lmessehtgk ivldwgsna
//
LOCUS       WP_175878142             377 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Burkholderia].
ACCESSION   WP_175878142
VERSION     WP_175878142.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..377
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40466
     Region          1..365
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfsftdeqq qfadalrryl geqygfearq aivrsdagvs daqwraftel gltalpvpda
       61 qggfgggpvd mlvvmqelgr alviepywat avgvealria gsgagddaal leavaqgqkr
      121 vavafhepra rydlyeldth aheqggtyrl tgtksvvqhg aqahvwivpa rvdgggiglf
      181 vverdagntk vvdyrtidgq raatitfddt parvltggar daaaleqiad yatfllcaea
      241 vgaldelnra tveytktreq fgmpiarfqa lqhrmvdmli haeqarslty laavryangd
      301 adarrkavsa akarvgsaar fvgqqavqlh ggmgvtneva aahlfkrlsi iettlgdtdh
      361 hlaritalpd faqtdva
//
LOCUS       WP_175878165             362 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 9 protein [Burkholderia].
ACCESSION   WP_175878165
VERSION     WP_175878165.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..362
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40213
     Region          5..333
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mangnptqri lviridflgd mlcttaflra lkarwpgael hvvanrynaa alagnpdvht
       61 ihtyvysrqc erndrpgrmr affdrlrlvr rlrrlrfdlv ivpnggmhrs smqfarqlra
      121 kdcrwhdaet efddrkpehv aqrpmcheal sgfrlvpelg caeldrlels vhpdrarqea
      181 whrllgartk prvglfvsnk averrwpadr wrdlgerlap vadvivfrdp aigqaiedeg
      241 wrdvnarhva pssvadlvaa aslldaivsa dsapvhlasa lgvpvaalfe drpekylrwh
      301 pigvphvilr agrtvdaigv daveravrhl lsqagqrdea paatarvqpa aatapaiati
      361 as
//
LOCUS       WP_175878186             123 aa            linear   BCT 11-JAN-2025
DEFINITION  type II toxin-antitoxin system VapC family toxin [Burkholderia sp.
            BCC0097].
ACCESSION   WP_175878186
VERSION     WP_175878186.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003923
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..123
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /calculated_mol_wt=13402
     Region          2..118
                     /region_name="VapC"
                     /note="Ribonuclease/mRNA interferase VapC, contains PIN
                     domain [Defense mechanisms]; COG1487"
                     /db_xref="CDD:441096"
ORIGIN      
        1 milvdtsvwi dhlrggdatl talleaervl ihpfivgela lgsmrnretv ldalrdlpaa
       61 tlatddevqr midavplhgl sigyvdahll asarltsdsr lwtrdrrlla aaerlqlvah
      121 pah
//
LOCUS       WP_175878196             393 aa            linear   BCT 11-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Burkholderia sp.
            BCC0097].
ACCESSION   WP_175878196
VERSION     WP_175878196.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 393)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..393
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41035
     Region          39..391
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mtqlfdtlgf ieasavraga gadaaayeea vtpvggaavs leqvgkvfat prgqaaalrd
       61 vtldvrrgev fgiigrsgag kstllrllng lerpssgrvr vqgvdvgald edglvalrrr
      121 tgmvfqhfnl lsaktvfenv alplkiagvp kaervrkvea llelvglaak rdaypaslsg
      181 gqkqrvgiar alvhdpevll cdeatsaldp ettqsilall adinrrlglt ivlithemev
      241 iravcdtvav ieqgevvetg pvwrvfgdpr hgatrallst lqhdlpaela arvrplpeqa
      301 alpdgaqivl dvrytgesgg epdvgalaaa lggsvrflhg giesiqghaq grlviaatpr
      361 addgpsaarg gavaallera rrhanhaevl gyv
//
LOCUS       WP_175878234             313 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [Burkholderia].
ACCESSION   WP_175878234
VERSION     WP_175878234.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..313
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34527
     Region          44..299
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mfyltspdvr eadvftrmpe kfrkpdarte waranrggmv tdsflegpvw dpdgylfvtd
       61 iphgrifris psgdwdlvve ydgepngmkr fdashliitd yrnglmlldi ergeirpyle
      121 rrnterfrgv ndltfdsagn lyftdqgqtg lhdptgrvyr lspngkldml lgtcpspngl
      181 vlsrdekvlf vamtrgnavw rmplqadgsv tkvsqfftsy gpsgpdgltv dlegrlfvan
      241 pglgrvwvln hcaepveilt gpkgasltsv cfggpdmktl fitestsgsv lkadmsiagp
      301 lpkqaakrav kqd
//
LOCUS       WP_175878237             236 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175878237
VERSION     WP_175878237.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..236
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25281
     Region          4..226
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mgndgvvave kalslldcfk pgaesqslam lsqasgmhkt tvyrlmnsle rmgyvvraqs
       61 gnyslghrvl ylgklyeqsf hlstvvepal halaaltkes asyyvhdngq rlclfrveps
      121 eglretrlag tmlplddtai shvirfwglg epiydkppal plftagardv htaafavpif
      181 gagdkfmaal tlsgpasrls vahesgeldr pqldaaadls rklgasvalc enlygt
//
LOCUS       WP_175878246             371 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alkene reductase [Burkholderia].
ACCESSION   WP_175878246
VERSION     WP_175878246.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..371
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39413
     Region          5..349
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,236,303,323,325..327)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,103,110,183,186,188,236,243,303,323,
                     325..326)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(27,103,183,186,188,326)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mtqdplfqpl rlgaltlpnr ivmppmtrsr asqpgdeane lmaayyaqra saglivsegt
       61 yiaplgkgya wtpgihtpsq vagwrkvtdt vhaahgrifa qlwhvgrlsh tsllggqqpv
      121 sssplqakgv nvfiagedgs tpgfvqasep ralsideire ivdqyraaar haieagfdgv
      181 elhgangylv nqfidsnant rtdayggsle nrlrflrevt qaliegagda srvgirlapl
      241 ttlngcvddd pettylaaak llgelgvgyl hiaeadwdda plmpvafkqq lraafpgvli
      301 yagaytaera reaiaagwad lvafgrpfva npdlperlrt gaalaphdrn tlfgggahgl
      361 tdyptlaqaa a
//
LOCUS       WP_175878255             268 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MetQ/NlpA family ABC transporter substrate-binding
            protein [Burkholderia].
ACCESSION   WP_175878255
VERSION     WP_175878255.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 268)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..268
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28459
     Region          25..268
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mrrsiltglg alaaalafaa pgahadsqtl kvgtmsgpda qiwtevtkva areglaikvi
       61 efndyvqpna aldagdldan gfqhqpflds qikqrgykiv nvgltytapm gfyskkiksl
      121 kdlpvgakvg iqndpsngnr allllqkygv iklkpgvgan gvnatpldia enpkkikive
      181 ldsaqlpral pdvdaasint dyavkagltp vkdaiaiedl rgpyanliav raqdkdkpwv
      241 kklvaayesd dvrkfidqkf ggaivpaf
//
LOCUS       WP_175878277             195 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175878277
VERSION     WP_175878277.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..195
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20179
     Region          5..157
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgvsrqqaae nrhaivaaae rlfrlrgvda vgltelmkea gftqggfynh fkskdaliae
       61 vmdkamqdra dspnagsvak qvtaylsgah rdnveggcpl sgfagdaprl tdaaracytr
      121 gvaaylerle rlvategsaa aaarddaiav lsqmvgalvl sravagtdpa ladeildaar
      181 rtlvgqpddp aavpa
//
LOCUS       WP_175878288             212 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: 2-hydroxychromene-2-carboxylate isomerase
            [Burkholderia].
ACCESSION   WP_175878288
VERSION     WP_175878288.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Thompson,L.C., Ladner,J.E., Codreanu,S.G., Harp,J., Gilliland,G.L.
            and Armstrong,R.N.
  TITLE     2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class
            glutathione transferase from Pseudomonas putida
  JOURNAL   Biochemistry 46 (23), 6710-6722 (2007)
   PUBMED   17508726
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122490
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..212
                     /product="2-hydroxychromene-2-carboxylate isomerase"
                     /EC_number="5.99.1.4"
                     /GO_function="GO:0018845 - 2-hydroxychromene-2-carboxylate
                     isomerase activity [Evidence IEA]"
                     /GO_function="GO:0043295 - glutathione binding [Evidence
                     IEA]"
                     /GO_process="GO:1901170 - naphthalene catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23363
     Region          8..188
                     /region_name="DsbA_HCCA_Iso"
                     /note="DsbA family, 2-hydroxychromene-2-carboxylate (HCCA)
                     isomerase subfamily; HCCA isomerase is a glutathione (GSH)
                     dependent enzyme involved in the naphthalene catabolic
                     pathway. It converts HCCA, a hemiketal formed
                     spontaneously after ring cleavage of 1; cd03022"
                     /db_xref="CDD:239320"
     Site            15
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239320"
ORIGIN      
        1 mnaahsatwy fdfvspfayl qqeqfdrlpp aaafeprpiv lgallahwgq kapaeiaakr
       61 vftyrhaqyr adklgiafrm ppahpfnpik plrlaiamgg sldairrifr hiwrdgqdvs
      121 tpegfaalce avgfpegvta veaqpvkdal rantdraiae nvfgvptfvl dgdlfwgeda
      181 tdmfvdcats rawldspevr risalpegvr rg
//
LOCUS       WP_175878319             350 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: porin [Burkholderia].
ACCESSION   WP_175878319
VERSION     WP_175878319.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..350
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=36918
     Region          4..350
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mqrkaflvga cvlcttsaha ssvtlygivd syvefdrigs lstlrqsggg sstsrvgltg
       61 ienlgggtst kfvlesgfsp adgsfqggtl fyrqayvslq ntrygdlrlg rqytpafyvv
      121 ydgdpfglne rmsplallat stdtitsntt ppiprfnqaa sylspdwngl rvmatygfpt
      181 pnalstqagr nygaglqyri gglyvgagfq gdtsagnlap vvspsttrhy vfaanyafar
      241 vklyaaflyg vgtaarlpaf stasvgasin vgaldrvlvs vvrrdvkgsa ndatalgvgy
      301 dhplskrtsl yarylymkng gdarntvvag lqpqpggteq vfalgiahrf
//
LOCUS       WP_175878337             330 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Burkholderia].
ACCESSION   WP_175878337
VERSION     WP_175878337.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..330
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35259
     Region          4..321
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 maallevenl gvrftrkdap pidavngvsf sleagktlgi vgesgsgksq tvmallglla
       61 gngtttgaar yrgdnllemd tralnavrgd riamifqdpm tslnpfltie rqmtetlqlh
      121 rklsrkeaik raiealesvr ipdaarrirm yphefsggmr qrvmiamall sepeiliade
      181 pttaldvtvq aqiidllrel nrergtaivl ithdmgvvag laddvmvmya grtveyapad
      241 sifaapshpy tigllnalpr ltdaddaplv aipgnppmpg tapagcafak rctyaeercg
      301 aerpaletyg aagavrachr pladltgglr
//
LOCUS       WP_175878358             234 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MOSC domain-containing protein [Burkholderia].
ACCESSION   WP_175878358
VERSION     WP_175878358.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12233312
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..234
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25857
     Region          30..183
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
     Region          180..219
                     /region_name="3-alpha"
                     /note="3-alpha domain; pfam03475"
                     /db_xref="CDD:460938"
ORIGIN      
        1 msddarpais vaigavriga srplagtpha saidkqpvga rlwlgalgfa gdehadarhh
       61 ggpdkavhhy aydhypwwaa qigardvlar pgafgenlst rgitehdvcl gdvftlggam
      121 lqvsqsrqpc wklnarfdhp rmaalvqrsg rpgwhyrvlq egwveagdml alharhypew
      181 rlstvldvly rrtldmaald alcdvpllpp gwrtmlekrr tgrqvedwtk rleg
//
LOCUS       WP_175878389             385 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Burkholderia].
ACCESSION   WP_175878389
VERSION     WP_175878389.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 385)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..385
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41337
     Region          1..373
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masismrrvq kaygehapvi rdvdleigah efcvflgpsg cgkstllrmi agledlsage
       61 lsidgrrvdd vpaaergvam vfqsyalfph mtvyenmafg lklarvpkae idrkvrdaar
      121 ilqldmller kpkalsggqr qrvaigraiv repgvflfde plsnldaalr gqtrieiarl
      181 hrqferasvv yvthdqteam tladkivllh agadtarhgs iaqvgapldl yhhpasrfva
      241 gfigsprmnf lpavvtacda rrttvtlvps getftlprdg salsagaavt lgirpehltl
      301 gaapdattla rdvalverlg eqtyvhldps gqpsatplia kvpgdapvrp gervhvhapa
      361 aachlftedg ravparadlp vhhya
//
LOCUS       WP_175878438             541 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia sp. BCC0097].
ACCESSION   WP_175878438
VERSION     WP_175878438.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..541
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57631
     Region          20..463
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpgqgnahps vplsrsahpd aghgkfkkql sltdltfigl gaifgsgwlf aashvstiag
       61 pagifswllg gfavlllgiv ycelgaalpr aggvvrypvf shgpllgylm gfitliafss
      121 liaievvaar qyaaawfpgl tvegssdptt vgwlvqaall cfffylnyss vktfakanni
      181 isvfkfivpl avigvlftff kpanltvhgf apfgmpgiem avsaggiifa ylgltpivsv
      241 asevrnpqrt ipialilsil lstliyvllq lafigsipta mlaagwhdvs kafslpyrdi
      301 alalgvgwla vmvvadamis psgcgniymn atprvvygwa ktgtffkvft rvdeasgipr
      361 aglwltfgla ifwtlpfpsw ealinivsaa lvlsyavapv svaalrrtap dlprpfrasa
      421 fgltgpasfv iaalivywsg wstvswllgl qivmfviyla crrwvptahl slaeqvrssa
      481 wliafyaami vlsylggfgg tgrlahpydt vvvaavalvi yywgantgvr adklqlddde
      541 d
//
LOCUS       WP_175878442             232 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: fumarylacetoacetate hydrolase family protein
            [Burkholderia].
ACCESSION   WP_175878442
VERSION     WP_175878442.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..232
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25211
     Region          25..232
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mtfvfppeap valpvagsda rfavrrvycv grnyaahare mgfdpdrepp fffckpadsi
       61 vpvaygdtle laypsqtrny hyeaelvavi gkggadiple raldhvwgya vgldmtrrdl
      121 qmkmremgrp weigkafdrs apigpvhpas dvghveqggl wltvngatkq ksdvshliws
      181 vaetvadlsk ffrlepgdvi ftgtpegvga vvagdvmkvg verlgeltvr vv
//
LOCUS       WP_175878513             366 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [Burkholderia].
ACCESSION   WP_175878513
VERSION     WP_175878513.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Saurin,W. and Dassa,E.
  TITLE     Sequence relationships between integral inner membrane proteins of
            binding protein-dependent transport systems: evolution by recurrent
            gene duplications
  JOURNAL   Protein Sci 3 (2), 325-344 (1994)
   PUBMED   8003968
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004772
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..366
                     /product="ABC transporter substrate-binding protein"
                     /calculated_mol_wt=39889
     Region          62..364
                     /region_name="AfuA"
                     /note="ABC-type Fe3+ transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG1840"
                     /db_xref="CDD:441445"
ORIGIN      
        1 mpfapkhlaa alaivlgtaa gsavaqvpag ypgnyqgvid aakkegkliv ysttdtglvr
       61 plikdfesly gvkveyndmn stelynryis enaasstsad vlwssamdlq vklvndglma
      121 sydspespnv pqwaqyqkqa ygttfeplai vynkrlipen evpttradli kllttqadkf
      181 kgkvttydie ksgvgfnylt qdahvnekvt welvkaigat gpklqsstga mmerissgen
      241 ligyniigsy ayakakkdks igyvfpkdyt qvvsrlatvs kkaknpnaak lwvdyllsrr
      301 gqtlianqan lyairadvtg etsaasltke lgdslkpiqi gtgllvyldq skrlaflkqw
      361 qqaikr
//
LOCUS       WP_175878520             273 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175878520
VERSION     WP_175878520.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..273
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29221
     Region          23..268
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mvsaavleps aatvaapavt pprgaridir rvshafdgpg galpvlddvs lsvaagefva
       61 llgpsgcgks tllrlvagld aarqgtiaqd gvpierpdps rivvfqdptl ypwrrvhanv
      121 algleargva rtaqhrvdda larvglqefa nvfphqlsgg maqrvalara lvndprllil
      181 deplgkldsl trltmqaelt alwqrdgfsa llvthdveea lflaqrvivf gprpativae
      241 lrvdlpyprh rgdprlaelr hhalrhlgld asw
//
LOCUS       WP_175878532             545 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glycoside hydrolase family 32 protein [Burkholderia].
ACCESSION   WP_175878532
VERSION     WP_175878532.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 545)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..545
                     /product="glycoside hydrolase family 32 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=59153
     Region          37..533
                     /region_name="SacC"
                     /note="Sucrose-6-phosphate hydrolase SacC, GH32 family
                     [Carbohydrate transport and metabolism]; COG1621"
                     /db_xref="CDD:441228"
ORIGIN      
        1 mnstsfrcsv rlvrllfacl actqavaapc happdndtpq wrpalhytpq rnwmndpngl
       61 vyangryhlf yqynplgndw gnmswghats tdlvhwreqp vamranatke ifsgsivadt
      121 lntsglgtpg htplvalyts vyktgsghap giqaqslays ldqgttwqpy ahnpvltldp
      181 eskefrdpkv swyaaggywl mttvvadahv vklyrsddli hwsflsdftl pdvphagalw
      241 empdliplpl dgdprrikwv mivnvnpwsi aggsgamyfv gnfdgrtfvp drvapagsdp
      301 aqfrwvdhga dfyaagtfsg apgarpvaia wmsnwdyaak vpttpwrgat tlprelalkt
      361 idgeptliva paaafdawad grpavhegdl tvdsatrals aatrgvvqri tvtispqraa
      421 raglivrrsa dgsigtrivy dtakrtltld rsqsgeanfa gtfsrehivd lplehgqlrl
      481 eivvdrgsve vfanggrval tdlifpplda drvavfaeqg ratfagltvt qlktgddtrg
      541 acasr
//
LOCUS       WP_175878539             281 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC0097].
ACCESSION   WP_175878539
VERSION     WP_175878539.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..281
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30747
     Region          <39..96
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <78..281
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msrtanrsav pspfwrdtal pfieartvdd graicyakht hdtfsvgaiv ggtstyvnga
       61 tnahvgrgvl viidpeqvha cnpygpdawa yrmvyvdvpw larlqhalgr dpnrdfhgfs
      121 pkltergdlf arfggfyrtl vspgidalgk esaaveffta lhgaldrepp darpgddnak
      181 laraadyiaa hcreavslda icaaadlsps ylirafnary gmtphaflid rrvqygrtel
      241 rrgrpiaeva ldagfadqah fqrafrriaa atpgqyrsam r
//
LOCUS       WP_175878551             247 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175878551
VERSION     WP_175878551.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..247
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=26984
     Region          34..242
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mhdhpqaaaq padmppepgp laplatlfgq cawfrtlape hqarvlaesh vaqceagdvi
       61 ahrlapseyw igvhqgllkl aifnvsgrgc tfsgvpsggw fgegsvikre lrkyevvaiq
      121 rstvlfvpvd tfhalldtsl pftrfvihql nnrmgefias iqnsrlldvd arvaqalaql
      181 fnpalypdtg pslsisqeel gmlvgvsrqr inqalqqlek lgalrlaynq ievvdldala
      241 rfgmeql
//
LOCUS       WP_175878569             266 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175878569
VERSION     WP_175878569.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..266
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29068
     Region          78..258
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          202..256
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mdrlfseiam hqalgraidh lgqprfwrfl vlllnemapf dnalataigh dgvplvldey
       61 dtggtdtasp vplylnglyl ldpflqaahd gladgcyrle evapdlfrqs eyflsyfrda
      121 vgddeiqilv rpnadtllsl slgastrfdv eplgkltaam pwvlaairqh wrlvgdaara
      181 apdadlgarv eqalarfgag vltdremsia rmvlrgnssk aiaerlaisp etvkvhrrhl
      241 yaklgissqp elfsrfiqal gedaag
//
LOCUS       WP_175878579             263 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175878579
VERSION     WP_175878579.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..263
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28793
     Region          13..260
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 metssdqand llfnqslekg lnvlrafsak rrtmtlaeva daagmtkssa qrmvytlekl
       61 gyirkhpvtr ryqltphvmr igfnylaadt lidvanpfls eltnltgett nltepdedem
      121 vyvarfvstk fvpihmpigs ripmyctgsg raflsalppd hararldgma rtphtprtvt
      181 alddlvalld garregyatn qeelfigdms iaapvlgsqg qpvaavhvva ptsrwtfdda
      241 rrklapavid cargisnsir tle
//
LOCUS       WP_175878572             727 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Burkholderia].
ACCESSION   WP_175878572
VERSION     WP_175878572.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..727
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79165
     Region          39..722
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mkpqpaiarp sieparwrrw ldplgnaard waatdgliwl hlaktvlaal lamgiamrle
       61 msqprtamtt vfvlmqplsg mvfaksfyrv lgtaaglvga lalgglfaqq pelymagitl
      121 wiggcialav rnrhfrwygf vlagytaali glpavmtpqt lfqsaltraa evalgiacsg
      181 avsalilpls sakalmrsls arhatfaaft agalagdvar gdferrfadf vddivgfean
      241 rafasfedph irarsrrlar lnsefmnact rlhalhqlvk rlranqsdav ldalaphvda
      301 lalrfaalrd erqrgiapat gallelrrfh galpkaaras rrtiedhaag glldfdtaie
      361 llyrfigeyl gyvdtyasld qddhafersv thyavktnaf fvgfaflrtv vavgamsafw
      421 iasewpsgsl aviataiaca lsstsprapk fvaqmgvgaa fatavgylfl cyvypnidgf
      481 pllcaalapv lglgaflamr pglsgygigf avffcllagp dntiaytpev linnglavvv
      541 amlacslvfa vvlpthmpwl tgriahdlrr qvtlacegap dglaqrfqss thdlmaqlrt
      601 llvrrtrqhr dalrwmlstl evghavidlr delhafrask ppqtlrwtgs idavlnelpr
      661 ffddptpsrh artlksvnla iraaqhtlqa wyavpdarrs mqrivgclhf mrsalldkda
      721 pfnrhrh
//
LOCUS       WP_175878584             473 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cytochrome-c peroxidase [Burkholderia].
ACCESSION   WP_175878584
VERSION     WP_175878584.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..473
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=50927
     Region          83..468
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mtarpafpsp dasgtpapra psrllrraay vlgaavigyg afaiafpaqv paaigtvvad
       61 wtganphpvv lqrpaaqpls avaqlgralf hdpslsasgk qscaschspd haygppnald
      121 vqpgglamtq qgyrpppslm ylyrqpnfsi gpdagendaa psvaqqataa agvvkaqkva
      181 gtsaapqlvp qggmfwdgra dtlqqqafgp llnpvemana siddvarkla qsshraqfeq
      241 lfgarvfstp qlavseamfa iaryqvedps fhpydskydr wlegrarltq aelrglrlfn
      301 dpdkancagc hlskpgkdgl ppmftdyqye algaprnral aqnrnpafyd lgvcgpfrdd
      361 lkdqtqycgm fltptlrnaa trhvffhngv fhtldqvmaf ynersispqk fyargadgkv
      421 deyddippky ranvdvtdap fdrkpgdkpa mtaqdikdie aflgtltdap aqh
//
LOCUS       WP_175878594             858 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: penicillin-binding protein 1A [Burkholderia].
ACCESSION   WP_175878594
VERSION     WP_175878594.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 858)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 858)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..858
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..858
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=92877
     Region          60..712
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mqpfqpsptr vnrrnvssvr alcarwvara qsaaaaavar akplaatawh hvrhptrrgv
       61 lltvaavpal favyvvvlip ftpgigdirk arvdqpaqvl sadgkllaef kpsnrewvpl
      121 kqisprmvda liatedhrfy ehhgldwkrt asaalhtfsg srqggstitq qlarnlypde
      181 igraptltrk vkeaitalki eavyskdqil etylntvpfl ynaygvemaa rtyfdksade
      241 ldvldsatlv gmlkgnsyyn pvlnperalq rrntvlgqmv kygklsaaqf aqlqrrplri
      301 dferqkeppg paphfaqqlr kwliawadrn dyniysdgli vrttidsrlq qmatqaltlq
      361 gnqlqgiann awsgrdgcgt dnevfrtfmr espeykaaqd agkddaaamk mlaadrgflr
      421 alckaktdvq agflaidprd gqirawvgsr dftrepfdhv aqarrqpgst fkpfvygaaf
      481 asgmkpedtf idqpveialk ggeiwrpndd vpptgkpmtl rdavalsrnr itaqvmekvg
      541 pgavarlard mgvrespler vpslalgtsp vtlkemvasy atiangglyv epqmvtrien
      601 rqgevlaeya papperalda etdktlldvm rdvvtrgtgg sirtrfgirg dvagktgttq
      661 dnadgwfilm qpglvagawv gfddgrvtlr sdywgqgahs alpivgdffq raqrarivdt
      721 kakfdtepsp gwfgslrerv tdlfdtwfpp eakkapapvr tqrierpaet degaasaasa
      781 pdaasggive ewvpasevaa saaalssgas qppqfapppa gasatsassa gigvapsavp
      841 apppasvpat pdatgasq
//
LOCUS       WP_175878597             311 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Burkholderia].
ACCESSION   WP_175878597
VERSION     WP_175878597.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..311
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=33165
     Region          12..155
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          168..307
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mqpaqsiptl arialavdpt pesltaaryv rtllrpgmrl riicaidnpr lvlpdiprid
       61 alltsaredm mreaqatcer iaalfadvgi dveqavvdts vtggsvadal vndtstwhad
      121 vlviganphh gllrlvegam sdtltkrarc allivpgtya rptdgalqrl mfavdgseps
      181 lhavrvglgf aapgtllyaa yvidravrlt dvvpvraled ayraegedal akigplfhat
      241 gnptkrgive thptsddvah almrdavhwr aellvvgthg rrgiaawlig svarrvahla
      301 qvpvllvrga e
//
LOCUS       WP_175878610             221 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cation diffusion facilitator family transporter
            [Burkholderia].
ACCESSION   WP_175878610
VERSION     WP_175878610.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..221
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22856
     Region          17..>202
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mqrpsratsh vyaatsrala vslainllll avetaaawsa hssglladva haaidlaada
       61 lilvacrlda rlpparrpty eplalaglga llavtgaqmi whaltrfdtp pvvqpgatal
      121 alvavtlagk avlsywmlrk aretgsalle asgwhvrtda lssllaalam saalvgfgrl
      181 ddlaalaiga lvirtgvgfi rrgcvqwpal aewanrstrg s
//
LOCUS       WP_175878632             472 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175878632
VERSION     WP_175878632.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..472
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47952
     Region          23..450
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,277,280..281,284..286,289,317,321,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mseiaspaga hepavnwram savllavala tldtaianta lpaiaadlha spaasvwiin
       61 ayqlamvatl lpfaslgdiv ghkrvyvagl avftlaslgc slastlpmlt aarivqgfga
      121 saimsvnval irglfpahrl grgvgfnalv vgvsfavgpt iaslilsvaa wpwlfavnvp
      181 lgvfalavai pslpqtargk hafdpvaalf nvitfaslif algefaqrgp lpvvlaaaav
      241 afvfgwllir rqaghpapml pvdlfrrpvf tlsaltavca faaqglafvs lpfyfetvlh
      301 rsavetgflm tpwsaivala apiagrlsdr yppgllgaig lallsagmvs laalpvspgv
      361 vdigwrmmlc gagfgffqsp nlkalmssap persggasgi iatarligqa tgaalvalsf
      421 giagrhgptl almlgagfag aasvasglrl fapshragap vvsepvkepa te
//
LOCUS       WP_175878681             302 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0097].
ACCESSION   WP_175878681
VERSION     WP_175878681.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32791
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdllatmriy vrvvergtms gaardldmgq pavseriekl ekhlgtrllm rsartlacte
       61 egrifyersk alleaaelav asvskaenal dgtirlaapq cfgevvlpav lmrirtaypk
      121 lhidlvlnde ivdpvtegvd isirvgqlgd ggfvayalga vgrvlvaaps ylerhgpidt
      181 kadlanhpfi rvkgvfaneq vplrrddgav eyarirtvmt ashwrpmfdt iaagggvgvv
      241 qhpacadala hgrlvrllph ydvpdfalnv lvhaqrplpp rvravvdllk selpplltqg
      301 qr
//
LOCUS       WP_175878688             365 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175878688
VERSION     WP_175878688.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..365
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40559
     Region          12..194
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(15,17,102)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(49,101..102)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            100..102
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 msrhtlkplv slvvpfhdea eaidaffatt vpileaigta rfeivcvndg srdgtldkli
       61 dvavadtrvr ivdltrrfgk eaaltagide aagaavilid adlqdppali pamlerwhag
      121 aevvaakrtd rrcdpmmqrv aaalyyrvhn qlsevempen vgdfrlmdrq vvdalralpe
      181 rrrfmkglfa wvgyrteiie ytraarsggr skfsgwrrwn falegitsfs tvplrvwtyi
      241 glafaalsfv ygayivmrtl lfgnpvhgya slisvmlfvg giqligigvi geylgriyhe
      301 skqrpvylvr rryradtqag qqparhaapa dgskllqfpv rriamarrrq tivagaqasr
      361 nlsvk
//
LOCUS       WP_175878695             760 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia sp. BCC0097].
ACCESSION   WP_175878695
VERSION     WP_175878695.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 760)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..760
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..760
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81026
     Region          <34..>162
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          176..745
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mnrsellart gcltvirppa ppvkpapgqp gslssyvpal pevfvaildd grilafnghv
       61 dlgtgirtsl aqivaeeldv paarvtmvlg dtaatpnqgp tiasatiqis atplrcaaaq
      121 arhallalaa erfgvdverl giddgtisad gqvvtfaalv aaqrialtld lntrtkdpah
      181 yrivgraspr vdlpakatgq ltfvhdmrvp gmlhgrvvrp pyaghdsgpf vgtslvdvdr
      241 asvadvpglv avvalgdfvg vvaereehai raarqlrvtw rplpalppld apaaaiaaap
      301 atrrvlldeg dvdavrtepd tltlsrtyaw pfqmhgsigp scaladyrap gdgritvwsg
      361 tqnpvslryd latlvardea didvvrmeaa gcygrngadd vcgdalllsr avgrpvrvql
      421 sradehlwep kgagqsmqvt gtvtrdgrll gydfttryps ndapllaall tgaiapeprv
      481 femgdrtavs pyasphrrfv cedlaplvra swlrgvsalp nsfahdafvd ecaaltgvdp
      541 lafrlrhlqd traiellqav aeragwtprv prpldkhder dearlvrgrg iayaryvhsr
      601 fpgfgaawsa wvvdlsvdrv sgeiriervt vgqdtgtmin pdgvrhqihg nviqvlsrtl
      661 kervrfadgk vasrewasyp iltfaevpdv dvvlmprqge pplgagesas vpgpaavana
      721 lfdatgvrfy appftpetvr aglheagrlm sadaaapvtt
//
LOCUS       WP_175878720             227 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Burkholderia].
ACCESSION   WP_175878720
VERSION     WP_175878720.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..227
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23876
     Region          23..225
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mtatlplttd pdsglqyrvr paagrpaarl lllhgvggne tnllnvadai dprieiaflr
       61 gpltfgpsqh awfpvrfgpn gpeidaerad esrvqlitll halrkqdgaa palptviagf
      121 sqggimsasv gltspgdvsa favlcgrilp eidpliaprd allplhaliv hgrfddklpv
      181 awadkadakl talgvahdtr lyaaghelta emagdfgrwv geragln
//
LOCUS       WP_175878770             301 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SH3 domain-containing protein [Burkholderia].
ACCESSION   WP_175878770
VERSION     WP_175878770.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..301
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30366
     Region          7..96
                     /region_name="YraI"
                     /note="Uncharacterized conserved protein YraI [Function
                     unknown]; COG4991"
                     /db_xref="CDD:444015"
     Region          <130..298
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
ORIGIN      
        1 mrntivrslc vvlaslaaap gvadaqssay tnspaelfag papdypvvaq vppgtaldvf
       61 gclsdytwcd valpgvrgwi daqlldypyq gnyvplleyg aiigvpvtgf aigaywdryy
      121 rhrpwypdrd rwahraeprl gpggmppaqg rpqpgapmqv apggpppvhd trpsatrggw
      181 nganrvappa apaptpmpgg tgnarpaspp tpmpggmgnv rpaspaaptp mpggagntrp
      241 agpppaglrp ppapggevrt mpqparqggg ggggyarpqg ggngggnhgg gggggpdelr
      301 h
//
LOCUS       WP_175878784             203 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ankyrin repeat domain-containing protein
            [Burkholderia].
ACCESSION   WP_175878784
VERSION     WP_175878784.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..203
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=21520
     Region          <49..203
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(77,79,83..84,87..89,91..92,96,99,108,110,112,
                     116..117,120..122,124..125,129,132,141,143,145,149..150,
                     153..155,157..158,162,165,174)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          77..108
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          110..141
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          143..174
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          176..201
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mrserfprti raavaglala tlagcahlpd qptygkadpa alrrydgdwf daarvgrvdi
       61 lralhdagyp vdatdshgyt avilasydgq paaldyllsv gadacagdrh gntalmgalf
      121 rnepdiarrl igtrcpidqt ngagetalgf atlfnrfeli pllvarganp nhvdrrgqsl
      181 lqlalthdnt yaadalrdag akp
//
LOCUS       WP_175878798             111 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: putative quinol monooxygenase [Burkholderia].
ACCESSION   WP_175878798
VERSION     WP_175878798.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..111
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12357
     Region          8..96
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mnepylqvia hyfakpgngd rvvellaela patrtepknl dyayfrspen pdhivilery
       61 sdadgldahr etphfqrigv gaimplldrr dvirymvqpd tgtatppggt r
//
LOCUS       WP_175878829             415 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ROK family protein [Burkholderia].
ACCESSION   WP_175878829
VERSION     WP_175878829.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..415
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=43927
     Region          82..375
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 mrsphfgqgs nsanvrryne rlllktlrra gsaskadlar lanmtgtavg siigsladak
       61 liefagrteg qrgqpaslir vdprgafgig vhldrmriet alvnfagdvl grrshdtllp
      121 ppadvleivr hdidamqall pdherarltg vgvaqpynlg awmrelglap dtfrawedid
      181 faadlgrtls lpvfgendgn aaaiaelfyg ygrqcddfvy lfigpaiggg iaidgdclrg
      241 vtgnagdiav ipvppsrlas appprgpwdi llaraslhal vrhlrhhget venradleac
      301 iarglpavde widdcvdala palravlcvi dapvvvldad tdaglldavt trlraalvat
      361 apeargtpvl vrgtfgadag aigaatlpmf fnfspragil kgartdlqev hhvaf
//
LOCUS       WP_175878834             328 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Burkholderia].
ACCESSION   WP_175878834
VERSION     WP_175878834.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..328
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34760
     Region          7..236
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mndndhrpvr fgivgagsia rrfaqslahv pgatlagvwa rradaaaafc etyggtpaas
       61 ldallaseid aiyiatlhds haqytlaala agkavlcekp aalnaaqldt vlhaarnarl
      121 lfmeamkppf fplyrqlrah lrddpigeir lvragcasss vpedhsvyrl draggalldi
      181 giyeaflavd wlgaardvqt lgrvgatgvd lfaslnsvha nggiaqlfcg ldvmgrgdal
      241 iaaagghvti hekwwnpara tiryadgrtv eleapaeggg lnyetahfcd llragrtesp
      301 imthdhsrqm iamtdaarav lgvrysge
//
LOCUS       WP_175878887             159 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DUF2280 domain-containing protein [unclassified
            Burkholderia].
ACCESSION   WP_175878887
VERSION     WP_175878887.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009432
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..159
                     /product="DUF2280 domain-containing protein"
                     /calculated_mol_wt=17735
     Region          1..149
                     /region_name="COG5556"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:444299"
ORIGIN      
        1 maalpdaikv fivqslacfd tisrtakavr eefgvevspq qcerydptkr agatlskkyr
       61 eifertreef lndtsrigvs hravrlrald ravaeaerrn nlplmaqlle qaakesgday
      121 tnrrrlehtg enggpienrt vvvdesqvaa avakledey
//
LOCUS       WP_175878937             165 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Burkholderia].
ACCESSION   WP_175878937
VERSION     WP_175878937.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..165
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18005
     Region          4..141
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 masynkillc ydgtlegrka lryganlamd lkaethllsv vdmrssiaqs aglltdvacg
       61 rfeetareil qegvnwlrer gvqaeghfaf gypideianl aselkvdlvv vghrcrsgls
      121 rwwmgsgntq lldrvncsil vacssaeeqk aeiarereaa mangq
//
LOCUS       WP_175878969             754 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [Burkholderia].
ACCESSION   WP_175878969
VERSION     WP_175878969.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 754)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..754
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81584
     Region          61..754
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mkkveqkkme watgtrlrai aaaasvafgt aaaghayaqt apavnagaaa sassaqngat
       61 attstsaqng tlpaitvnaa sagdgtvglv akrsttgtkt dtplneipqt invvtaqqie
      121 mtgatdvnaa lryvpgfssy gsdnrsdwya alrgftptay vnglqvpnti nlaswrvdpy
      181 midsisvlrg ptsvlygagd pgaiidvhtk ladgervrea gvqignyark qfmidvgdkl
      241 dpdgkyayrf vgvardgnal tgpnndqrva lapsfrwrpd adtsltlsat ylqdwgdiss
      301 nflpaqgtvl pnpngqinkd vyegdgnfny yrkkqwsvgy qfernltpaw tfrqntrlmh
      361 lsldngsvfg ngfvdgsttd vsrwagvfqm nysrfdidnn legrfatgpl qhtlllgfqy
      421 nrqtatdsew laaapplniy npvyqpvtta vftpdatfrt ntyttmntfg lyaqdqvkwn
      481 rwtltlggre dwvnmrmddr aggtstkadv taftgrvglt yqgdyglspy vsyatsfnpl
      541 igvnlvgggl pqptrgkqie aglrwqppgk nlmlnaaiyq inqtnvltsa lpsqddtgtk
      601 svqtgevrsr gielsatgkv trnlsviasy vyqdvknvqa ndvslnnwpv diprprqmas
      661 lwtdwtwytg plagfglggg iryqsasaga adnsltvssv tlfdaglhyd trnwrfavng
      721 tnlfnrhyis gcqsanvcvf gtdrtviata kynw
//
LOCUS       WP_175878989             140 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [Burkholderia].
ACCESSION   WP_175878989
VERSION     WP_175878989.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 140)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..140
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15287
     Region          13..127
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04667"
                     /db_xref="CDD:467552"
ORIGIN      
        1 mstgpdtlav ikerativcr qrssvllvar aaarwslpgg tirrgetple aaqrelaeet
       61 rleglaldya vqfggltklh hvfvadvpah ltprasneia rckwftvdrl dtlrasvptr
      121 kiiellrldg fsafvsgplr
//
LOCUS       WP_175879020             293 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0097].
ACCESSION   WP_175879020
VERSION     WP_175879020.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 293)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 293)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 293)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..293
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30961
     Region          11..291
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mstlatggat rdakawlvap alafiaalfi ypfayglvls fqptnatngg galanyvqff
       61 tdtamwptvl vtlklavpat llnvgiavpv afalrrnspy qkfvttllvi pvtlgtvlva
      121 dgmltyfgpn gwfpqalqgl hlytdevrlt hnywgvllsl ivsgfpfafl lmlsyisgid
      181 ptlaraaatl ganpwqqfrq iylpllvpgl tmaaclsfvq afsvfpsavl lgapagptrv
      241 isiaaaeaaf esydyslasa iaivmgfvql lvvasmlgar rffytgavtg gkg
//
LOCUS       WP_175879040             123 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GFA family protein [Burkholderia].
ACCESSION   WP_175879040
VERSION     WP_175879040.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..123
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13120
     Region          4..109
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 msatrfkgsc hcgavkfevt aaiapavrcn cslcrrrgal mspmfaaanl tivegegalt
       61 cyrfnthtar hyfcsrcgvy pfhqtrkdpa cwrvnlgcld gvdptaldat vldgaslsvv
      121 eda
//
LOCUS       WP_175879041             238 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Burkholderia].
ACCESSION   WP_175879041
VERSION     WP_175879041.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..238
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25397
     Region          152..233
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mpdamtgnat tdahvldrvv wnaltgrqrr falgdgralr fptaiapfaa iddtspasfd
       61 alcglitthg paalvtpdei eppaalsvir ratllqmtwq gtldttheae pvplgeadvp
      121 dmlaltaaaq pgpfgprtfe lghyigvrse grlaamagqr mqvdgyteis avcvdaafrr
      181 rglaarlirs liatigarae tpflhvlttn rvaierylal gfvvrremhl lvlgdaha
//
LOCUS       WP_175879097             316 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: OmpA family protein [Burkholderia].
ACCESSION   WP_175879097
VERSION     WP_175879097.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..316
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32613
     Region          32..314
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          211..314
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(216..217,250..251,254,258..259,262,304,308)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mhrtiqvrra rlsaavspal aalfaaglva sgaafaqntg atvtpvgngt vattalpqan
       61 pnaggasgtv vhgtagtiap ppanatpgqv vvggkvpdea tkaavlqklr dtygaanvvd
      121 qvevgdvatp pnwsanvqkl lgaqlkqisk gqlkingtqi emkgevhnea qrqqlasdma
      181 ntlnptytik nglrvsaseq gvldqtlanr tiefetgsat ltpqgklild qmaaalakmq
      241 nrtvdiight dnsgnrtsni alsqaradav kgylitknip pqqmtttgvg pdqpiapndt
      301 adgrarnrri efrvgq
//
LOCUS       WP_175879117             191 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: recombinase family protein [Burkholderia].
ACCESSION   WP_175879117
VERSION     WP_175879117.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..191
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=20512
     Region          4..135
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(9,11,72..73,76)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            11
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(71,116..117,119..120,124)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(77,82..83,112,115..116,119..120,123,126)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(101..103,112..113,116..117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(101,117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(125,131..132)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          147..188
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
     Site            order(148..150,182..183,185..187)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 msrtfayarv stsdqttanq lreieaagfs vdrrrvvses isgsvsadqr pgfaqllvkm
       61 eegdvlivtk ldrlgrnamd vratveglae rgirvhclal ggvdltsaag rmtmqvlnav
      121 aeferdllie rthagiarak aegkamgrps alsneqradv lreldagasv aalarrfgts
      181 rqtimrvrda v
//
LOCUS       WP_175879132             308 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Burkholderia].
ACCESSION   WP_175879132
VERSION     WP_175879132.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..308
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34055
     Region          4..237
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msaieirhvk krykslqalk gvslsveege ffgllgpnga gkttlisila glaradegsi
       61 svrghdvvqd frsarralgv vpqelvfdpf ftvretlriq sgyfglrrnd dwidevmanl
      121 dltekadanm ralsggmkrr vlvaqalvhr ppvivldept agvdvelrqt lwkfisrlnr
      181 eghtivltth yleeaeslcd riamlrrgev valdrtdall rrfaglqlyl rlatgalpae
      241 lrgletdpaa rapgehllrl asydeveril aqcrvagctf deievrkadl edvfvqvmng
      301 aeviegla
//
LOCUS       WP_175879160             797 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia sp. BCC0097].
ACCESSION   WP_175879160
VERSION     WP_175879160.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..797
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=87214
     Region          25..745
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mpmqsttpts pppapepkkr pwwqkvllgf aamcvalvva gglvlgyalv vawpnmpsld
       61 altdyrpkvp lriytsdhvl igefgeerrd vvhfkdvpds lkkailaied arfydhggvd
      121 ltgiiragfv altnghasqg astitmqvar nfflssekty trkiyemlla yrieraltkd
      181 qilevymnqi ylgqraygfa saarvyfgkd lkditlaeaa mlaglpkaps aynpvvnpkr
      241 akvrqeyilq rmlelnfitr eqydeaaaqp lvvkgpgrdf svhaeyvaem vrqmmyaqyr
      301 eetytrgfnv vttidsadqq vaytalrkgi mdyerrhgyr gpegfielpa gtddreqaid
      361 dallehpdng eliaavvtaa sprqitvafi dgstatiegd nlrfasgals anaqpnrrir
      421 pgaivrvvkn dagkwsitql pqvegaflsi vpqdgairsl vggfdynknk fnhvtqawrq
      481 pgssfkpfiy sasldkglgp atvindgply fsaaetggqp wepknygggf egpmsmrtal
      541 qrsrnlvsir ilnnigtkya qqyitrfgfd adrhpaylpm algagqvtpl qmagaysvfa
      601 nggyrvnpyl iaevtdpnga ivaraqplva eqnapraida rnayvmnsll qsvaqrgtga
      661 rtnvlkrtdl agktgttnds hdawfagyqh tlaaiawigy dnprslgdre tggglslpvw
      721 idymgaalkg vpefkptvpd gvesiggely fteftpghgf vstvgvpqap aaqnvdeavp
      781 hvdeqekqdi mnlfrgh
//
LOCUS       WP_175879168             367 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase, partial
            [Burkholderia sp. BCC0097].
ACCESSION   WP_175879168
VERSION     WP_175879168.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         <1..367
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
     Region          <1..194
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          263..365
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 ytlfaegcrg hlgrqliskf kldanadpqa ygigikelwe idpakhkpgl vihtagwplk
       61 sdtyggsfly hmdnnqvvvg fvvglgytnp ylspfeefqr ykthpsiraf leggkrvsyg
      121 araitaggll slpktvfpgg aligddagfl nasrikgsha aiktgmlaad aafdavqagr
      181 qsdelnaypd afkqswlyte lyrarnfkqw makglylgtl mvgleqkvmg gnvpwtlhhq
      241 hadhemlkpa sqcepieypk pdgkltfdrl ssvfisntnh eenqpahltl kdasvpvnvn
      301 lrtyagpear fcpaavyefv knddggerlv inaqncvhck tcdikdptqn ivwvtpeggg
      361 gpnypnm
//
LOCUS       WP_175879196             293 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: pirin family protein [Burkholderia].
ACCESSION   WP_175879196
VERSION     WP_175879196.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..293
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31239
     Region          12..270
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 msasiktllt presdignlv vrrvlparaa rlvgpfiffd emgpavlpag rgidvlphph
       61 iglatvtylf dgslmhhdsl gfrqkivpgd vnwmtagrgi vhserspded rpreqpvhgi
      121 qtwvalpveh edttpafvhh aadtlpsftr dgvtvrviag tafglvspva vfsptlyava
      181 efaaggtlal daeheergvy lvdgdlsvdg tslapatmav lepgasvala sahgarvmll
      241 ggahlpgerf iewnfvsser akidaaraaw adqtfgkvpg eenewtrqpa rka
//
LOCUS       WP_175879226             774 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: xanthine dehydrogenase family protein
            molybdopterin-binding subunit [Burkholderia].
ACCESSION   WP_175879226
VERSION     WP_175879226.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..774
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81673
     Region          <68..>194
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          203..764
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msapdlsvhn asrralllgf asgglllafg vpslaqaaap vqppvsanpq yggagmphgl
       61 rddpnlfvai apdgtvtvtc irsemgqgvr tsvalvvade lgadwarvkv aqavgdepry
      121 gnqntdgsrs lrqsfaalrr agaaartmle qaaaatwgvd vrqvkatvhe vvdtktgrkf
      181 gfgelatkaa alpvpdtksv alkapaefry igkgktalid grdivggraq ygidtrldgm
      241 lyavvarppv ygdtvasfda saaeklpgvv kvvqltstpl psgfqplggv aviahdtwta
      301 iqaraqlkid wkhgpnagyd saeyrkalea aaaqpgdvir ndgdaaaala gaakrvraty
      361 yiphlahatm eppaavarva dgrcevwtct qapqttrdei akalglpter vtvnvtllgg
      421 gfgrkskpdy vveaallska agapvkltft reddiahdyf havsleafda gidasgkvva
      481 wqhrtvapsi qstfrpgvvh eqpgelaqgi adlpfaipnv rienpaaqah trigwfrsvy
      541 niphafgiqs fvselahaag rdpkdflldl igparrfeph itvknvnyge dpalypvdtg
      601 rlrrvvetva reagwgrklp kghglgiaah rsfvsytaav cevqveadgk isvprvdiai
      661 dcgpqvnper vrsqlegavv mglgialhge itfkdgrpeq snfngfqvlr mneapreirv
      721 hlvapddyat plggvgepgl ppvapaltna ifaatgtrir slpvadqlak sqag
//
LOCUS       WP_175879247             421 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia sp. BCC0097].
ACCESSION   WP_175879247
VERSION     WP_175879247.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..421
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=43778
     Region          205..412
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(212,252,290,393,396)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(212,393,396)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(212,252,290)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 msfrssfaaa vlgaavlvap lavsaapagw vaawatalqp ipdlaapppl yrapdvagrt
       61 vrqivyptvs graarirvsn aygraplvve aaslaragdg aaladgaamp vrfggkasvt
      121 lapgqelesd pvaigvtaar pyaislqmga dqrmtvwhrv snqfnyvsap gdhvgdpgta
      181 afrtrftqya wvtelaveag parasvaaig dsitdglrss mnrnrrwpda larrltasgv
      241 dsigvvnlgi sgnrllsdsa cygtslasrf erdalsrsgv kaaivligin dinfaamppr
      301 agldcdhpht qvtaaslidg yrrlteaahr qgvkvfgatl tpaalpagre airlevnrwi
      361 rsgggfdgvv dfdavlrdpa rpsvlqrryd sgdgihpsda gytamadavp verlqaavgg
      421 k
//
LOCUS       WP_175879265             384 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia].
ACCESSION   WP_175879265
VERSION     WP_175879265.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..384
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41315
     Region          18..184
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          128..382
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mfvlkliarn amrhrlrtll tvlgltiavl afgllhtvvd awyagaaaas sgrlvtrnai
       61 slvfplpvsy enrirgvdgv tavvrsnwfg giyrdpknff asfavsdnyl dlypefilpa
      121 qqradydrdr rgclvgrqla tqfgfkvgdv iplkgtiypg twdfvvrgil dgrddstitr
      181 qlvfhwdyln etvrkrtpkq adqvgvfvlg vahpddgasi arnvdavfkn slaetltete
      241 qafqlgfvam snqiiaairl vsyvviliim avmanamams arertaeyat lkalgfgpgf
      301 lalivfgesv viavaggglg ilatppaasl fkqaaggifp vfkvstetvm lqaacsvavg
      361 faaaivpawq aarvrvvegl raig
//
LOCUS       WP_175879270             325 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0097].
ACCESSION   WP_175879270
VERSION     WP_175879270.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0097
  ORGANISM  Burkholderia sp. BCC0097
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia sp. BCC0097"
                     /db_xref="taxon:2676289"
     Protein         1..325
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34342
     Region          23..>193
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          113..307
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(123,127,168,182,184,242,259,286)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(124..125,129..130,132..133,136,140,142..148,211,
                     236..240,247..248,251)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mandgavaak ietrrfsmwt lemnlndlyl fvqaveagsm saaarrldlp kstvskrvae
       61 lertlgarlv hrtsrsfrlt pvgaeffeha raavieansa rdavlrqaae pagvvritss
      121 vpvaqhilap clpalaiahp klllqihasd rlvdiaqegf diavrshfap lpdsalvqrp
      181 laaspivvva apaylaragt pdtpadlaqh dglhpgpqpw rlqragdavd vtprlrlqad
      241 estlllqaat aglglaclpd wiagaalasg alvrvlpgwc agtvtttllm phrrgqlpgv
      301 raaveflaqh varhhgggst iepha
//
LOCUS       WP_175879283             230 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: dienelactone hydrolase family protein [Burkholderia].
ACCESSION   WP_175879283
VERSION     WP_175879283.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..230
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24257
     Region          1..227
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mtaqwidipt gndsfggyla lpkrgkgpav iiiqeifgvn ahiravadqy aadgfvalap
       61 dvfwrtqprv eltyegadrd kgielmkktd vglavadiga aadalrarpe vagklaaigy
      121 cfggqlayra aatgkldaav syygggiqna hdlagqvtqp ilfhyaendh gipltavdqv
      181 kaafaghgha sfhvypgaeh gfnctdrasy nqraaalahg rtltflaehl
//
LOCUS       WP_175879366             302 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175879366
VERSION     WP_175879366.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33028
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,219..224,
                     230..231,233..234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mklsfealea ldaidrtgtf adaaelvhrv psaltyliqk lesdldvalf drsgrraklt
       61 ragrvvveeg rrllhaaeql erkaqraeqg wetevrvcia eilpfdmmwp yvhafydlem
      121 dtrlrlstev lggtwdalis rradlivgaa geppelpdiv aqpigtlrhv favapthpla
      181 alpeplsmas iveyrgavis dtsrelqpqs vavdagqpyl avptlaakla aqceglavgt
      241 lpdciaapai aqgrlvarev tgmrdtthcy iawrtdeagh alrwwveqlg hpdlvdrfta
      301 lv
//
LOCUS       WP_175879376             786 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LPS-assembly protein LptD [Burkholderia].
ACCESSION   WP_175879376
VERSION     WP_175879376.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..786
                     /product="LPS-assembly protein LptD"
                     /GO_process="GO:0015920 - lipopolysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86791
     Region          76..757
                     /region_name="LptD"
                     /note="LPS assembly outer membrane protein LptD (organic
                     solvent tolerance protein OstA) [Cell
                     wall/membrane/envelope biogenesis]; COG1452"
                     /db_xref="CDD:441061"
ORIGIN      
        1 mppkplfpnv fpgdgaprkr rlalallavp glvpavsyaq lsgaaaqpqp ldspwdlrla
       61 pqledhplkd gakpaafvia dhtsgtaeqd laakgsaelr rgdavvkada ihydqdtdma
      121 daygqvkvin ggtsfagpea hlkieanqgf mtapkyhfnv tggsgsaerv dmvdnersvf
      181 vngtytacqc stnpawyikg srfdfdtgad egtarngvlf fqgvpifasp wmtfplsger
      241 rsgllpptfs mnssngfels lpyyfniapn rdltltprii srrgvmteat frylspsysg
      301 tftanylpdd rlahrnryai ywqhqqnfgg gfggyvyynk vsdntypedl gsanqfvngt
      361 qtlyqqeagl tynngpwsvl aryqhwqtlp psiapysrep qlnvkytkyn vggfdfgaea
      421 dysrfritta dategdrivf npyisygvyg pgyfvvpkvq yhfasydlny lssttpnspk
      481 rftesiptvt fdtglifdrs vrlfgqdfiq tleprlyyvy tpyrdqsnap lfdtaesdfg
      541 laeiyqpntf vgndriadan ritagltsrf idprtgdera rfviaqqyyf adqrvtlnpg
      601 qaavlarhsd livgaalklg sgfmsetafq ynqnnnqlvk ssvgfgyspg errvinvgyr
      661 ytranttldn qpinqflvsa qwpltrrlya igrfnydlag drvvdglvgl qydadcwalg
      721 vgvqraangi nssgqqnsst rfmmqltlkg lstvdnglvs afragvpgyt plppppppms
      781 rfsnye
//
LOCUS       WP_175879398             531 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MDR family MFS transporter [Burkholderia].
ACCESSION   WP_175879398
VERSION     WP_175879398.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..531
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56866
     Region          33..425
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(34..35,38..39,42,73,123..124,126..128,131,152,
                     155..156,159,285,288..289,292..294,297,325,329,382..383,
                     387,391,407,410..411,414..415,418)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mavhtaahhs sgqvlpfres llamigisfv tmlvaldqtv vgtalptiva elrgfdlyaw
       61 vatsyllssv itvpifgrlg dyygrkpfvi asivvftgas vlcgmandml ylvlarglqg
      121 igggmlvgta facipdlfpd svvrlrwqvl mssafgiana vgpslggvlt qsfgwrsvfy
      181 vnlpigilsl ffvwrylphl rhvehdrkmr ldwpgallia lslgalqlfv ewlpkygvas
      241 waslllvvav aagiglwhwe krcaqpilpf dmfgnralsa lfvlailagf smfsllfyap
      301 llfqggfgms preaglvitp lvvfitigsi mngrvvtrir hpntmlhvgf vlfaiacagi
      361 vvsthttptw mlmalmvagg iglgfvlpnl tvfaqqtagr ehlgiatall qslrmvggml
      421 gtaltgtlvn qmysggvrna lstdhamqwh arladpqili draaqgglva eltraghnga
      481 llleaaresl vgaihlgvam aavvavvsvw qcrrvppial rrkiephvaa d
//
LOCUS       WP_175879399             320 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Burkholderia].
ACCESSION   WP_175879399
VERSION     WP_175879399.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..320
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34893
     Region          81..282
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mswqskfacw llrwqfrpet trevldpara rrftdlrmfv prrppsgyrl rqcygaddap
       61 lrgewlertd agagrgpgrt llyfhgggyy fcstkthrpl vfgltkragv rsfsldyrla
      121 penrfpaald dalaayrqll algtppesiv fggdsagggl alatlvalrd rgeplpagai
      181 lfspwtdlag tggtmrsndg rdpmfaaaal pkaatlylgd epatnpyasp fyadftglpp
      241 lyiqvgstev llddsrrvae kakaagvqve ievwpdmphv wqlyapmvpe ardaldgaaa
      301 flrrvavera vqrageasia
//
LOCUS       WP_175879453             125 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: BON domain-containing protein [Burkholderia].
ACCESSION   WP_175879453
VERSION     WP_175879453.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..125
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=12819
     Region          58..>125
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mmnrisvlaf avalvfvgts alaqttqvds atqtasgvqa vssagnarka ararsrklak
       61 dvrhafsrtp glnqthigvl vkpgevtltg tvpdaaqida aekaaesvpg vmkisnrltv
      121 hengq
//
LOCUS       WP_175879354             424 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NupC/NupG family nucleoside CNT transporter
            [Burkholderia].
ACCESSION   WP_175879354
VERSION     WP_175879354.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Hirschi,M., Johnson,Z.L. and Lee,S.Y.
  TITLE     Visualizing multistep elevator-like transitions of a nucleoside
            transporter
  JOURNAL   Nature 545 (7652), 66-70 (2017)
   PUBMED   28424521
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Johnson,Z.L., Lee,J.H., Lee,K., Lee,M., Kwon,D.Y., Hong,J. and
            Lee,S.Y.
  TITLE     Structural basis of nucleoside and nucleoside drug selectivity by
            concentrative nucleoside transporters
  JOURNAL   Elife 3, e03604 (2014)
   PUBMED   25082345
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Munch-Petersen,A., Mygind,B., Nicolaisen,A. and Pihl,N.J.
  TITLE     Nucleoside transport in cells and membrane vesicles from
            Escherichia coli K12
  JOURNAL   J Biol Chem 254 (10), 3730-3737 (1979)
   PUBMED   374403
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..424
                     /product="NupC/NupG family nucleoside CNT transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005337 - nucleoside transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:1901642 - nucleoside transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=43830
     Region          1..422
                     /region_name="NupC"
                     /note="Nucleoside permease NupC [Nucleotide transport and
                     metabolism]; COG1972"
                     /db_xref="CDD:441575"
ORIGIN      
        1 mdilrsllgm lflllvayll snnrravsar tmiaalltqf aigalvlfvp sgraalagaa
       61 ngvnrvldmg nhgiafvfgg lvdarmfqlf gdggfvfglr vlpmiifvta lisvlyyigv
      121 mkwivailga glakvlgvsr ieacsavati flgqsempal vkpfvrnmts aeiftvmasg
      181 masvagsvlv gyaglgvkme yllaasfmav pggllfgkll fptvepsrvv vdgldfddkr
      241 aanvieaaas gasvglriai nvgamliafv glialmnliv gsaaafagfp qltlvgiigh
      301 lfaplawiig vpwhdaalag nfigeklifn efvaygdlsp ylkggahaaa aglqvldpkt
      361 laivsfalcg fanfssiail aggfsavape rrsdvarlgl raltaatlsn lmsaaiaglf
      421 fslh
//
LOCUS       WP_175879458             304 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Burkholderia].
ACCESSION   WP_175879458
VERSION     WP_175879458.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..304
                     /product="VOC family protein"
                     /calculated_mol_wt=32555
     Region          <217..303
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 mksvrsvlla amlagglava pvtfakppap pgavptvavg pqydtthvcv apedfdrftd
       61 sfvatfggkk skqgvfqvtp tpsqtmsqlv ltpvgtisvf gfktpipypf caertgylvt
      121 dmdvavksar ehgadvivdt fpdpigrdai itwaggvnmq lywhtqaphy dalqtvpenr
      181 vyvspqsvrk fvhdfvkfsk gkvvsdnlka pgieigrpdd tyrririesg fgkmtvlvtd
      241 ghlpypfgre mtgyevadla atlkqaeaag vtvlvppfks dgrdaalvqf pggyvaeiha
      301 saar
//
LOCUS       WP_175879516             159 aa            linear   BCT 11-JAN-2025
DEFINITION  cation:proton antiporter, partial [Bacillus cereus].
ACCESSION   WP_175879516
VERSION     WP_175879516.1
KEYWORDS    RefSeq.
SOURCE      Bacillus cereus
  ORGANISM  Bacillus cereus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus; Bacillus cereus group.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 159)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Bacillus cereus"
                     /db_xref="taxon:1396"
     Protein         1..>159
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
     Region          1..>159
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mefefffqia lillstklag dlsvrlgqps vlgklivgiv igpavlgwie nselltqlsn
       61 vgvillmfma gletdleeln anrnsslava lggiilpfvg gyvsglvmgm eqgnavflgl
      121 llcatsvsis vqtlrdlgkm ktresttmlg aavfddilv
//
LOCUS       WP_175879604             706 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Klebsiella aerogenes].
ACCESSION   WP_175879604
VERSION     WP_175879604.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella aerogenes
  ORGANISM  Klebsiella aerogenes
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Klebsiella aerogenes"
                     /db_xref="taxon:548"
     Protein         1..706
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77269
     Region          3..706
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 missvyfkrs alvcalaaaf platqaedtl ivtakpddsa saqtqgysak tstgatktdq
       61 plittaqsvs vitrqqiadq gantvsqalq ytpgvyssfg ggatrfdtis lrgyhggdvd
      121 nlfldgmrlm sdggshnvlq idpwfiervd virgpssaly gqsvpggvvn ltskrpqfsq
      181 qghfrltggt qntkgaafdy tdaindqwaw rligmtrssd tqydhtreer yaispsllwq
      241 pdsdtslllr aylqkdpsgg yhgslpldgt ryahngrkls pstnegdpgd gyqrreqiys
      301 yefnhqfsdv wsaysagsyt htnvsldqvy qvgwvgdsdm lsrgysgsrg sldawstdnr
      361 lradfatgel thtlilgaey hrfrndlwtg agnaaplnpf tgytpqtght itysdnnnrr
      421 yyqtglylqd emvwnrwhld vsgrydrivs qqvsdtsgts nrrsddhisg rasllyaldn
      481 glspylsysq aitpamlpga dgtllkptta eqveaglkfq ppgssdlysi aiydlmqkdv
      541 atrdpniata tyipagkvhs qgveleahnq itpqlstias ytwnrlrfqd tkdgtdsntp
      601 qlspdqmasf waryqlpagi tvgagvryig kqwaddante rlpsvtlida maradlgaws
      661 tamkgayiqv nannigdrey lsgcygtgnc ywgaersvta tvgydf
//
LOCUS       WP_175879784             243 aa            linear   BCT 11-JAN-2025
DEFINITION  sirohydrochlorin chelatase [Mycobacterium sp. IS-2888].
ACCESSION   WP_175879784
VERSION     WP_175879784.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium sp. IS-2888
  ORGANISM  Mycobacterium sp. IS-2888
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Mycobacterium sp. IS-2888"
                     /db_xref="taxon:1834159"
     Protein         1..243
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=25733
     Region          8..231
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mwvarlvttl vltahgsrdp rsaasarava drvarlrpgl dvrlafceln spslpdvlsd
       61 crdavvtpll lanayharvd ipgqiaqsgv dvaqadvlge dprlisvlrq rvtdlgvsrh
      121 ddgvgvlvaa igssdamana rtrrvatyll agtswagatt afvtrpepsl aeaagrlrrq
      181 garriivapw flapgrlpdr vrsfadnagm elakplgahr lvaetvlnrf dearksglqg
      241 iaa
//
LOCUS       WP_175879860             200 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Mycobacterium sp.
            IS-2888].
ACCESSION   WP_175879860
VERSION     WP_175879860.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium sp. IS-2888
  ORGANISM  Mycobacterium sp. IS-2888
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Mycobacterium sp. IS-2888"
                     /db_xref="taxon:1834159"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22307
     Region          2..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mesrrqrtrq allhaamkrf vadgvhqtsv adiardvgvt ertfyrhfps khavifadyd
       61 igfewfaral alrphgepit asvrkavdaf pfdfamvrea atirsrdldq diitthirrm
      121 rdqvadeiar fihersapta dgamiadiaa hslatavfva leawmakdeh diddlgrltd
      181 malsaledgl thtlrkagld
//
LOCUS       WP_175879938             392 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Streptococcus thalassemiae].
ACCESSION   WP_175879938
VERSION     WP_175879938.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..392
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43304
     Region          17..376
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(19..20,23,56,110..111,113..115,118,138,141..142,145,
                     224,227..228,231..233,236,258,262,312..313,317,321,337,
                     340..341,344..345,348)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mnryavqlis rgavnkignm lydygnsvwl asmgtigqtv lgmyqiselv tsilvnpfgg
       61 visdrfsrrk ilmttdlvcg ilclaisfir ndswmigali vanivqaiaf afsrtankai
      121 itevvekdei viynsrlelv lqvvgvsspv lsflvlqfas lhmtllldsl tffiafvlva
      181 flpkeeakvq ekkaftgrdi fvdikdglhy iwhqqeiffl llvassvnff faafefllpf
      241 snqlygsega yasiltmgai gsiigallas kikanvynll illaltgvgv fmmglplpnl
      301 lsfsgnlvce lfmtifnihf ftqvqtkver eflgrvlsti ftlailfmpi akgfmtvlps
      361 vhlssfliig sgviilscis fiyvrthfek li
//
LOCUS       WP_175880008             334 aa            linear   BCT 11-JAN-2025
DEFINITION  PhoH family protein [Streptococcus thalassemiae].
ACCESSION   WP_175880008
VERSION     WP_175880008.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Kazakov,A.E., Vassieva,O., Gelfand,M.S., Osterman,A. and
            Overbeek,R.
  TITLE     Bioinformatics classification and functional analysis of PhoH
            homologs
  JOURNAL   In Silico Biol 3 (1-2), 3-15 (2003)
   PUBMED   12762842
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..334
                     /product="PhoH family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=37388
     Region          1..325
                     /region_name="PhoH"
                     /note="Phosphate starvation-inducible protein PhoH,
                     predicted ATPase [Signal transduction mechanisms];
                     COG1702"
                     /db_xref="CDD:441308"
ORIGIN      
        1 mkehsidiql shpddlfhlf gsnerhlrlm eeeldvviha rteivqvlge etaceearqv
       61 iqalmvlvnr gmtvgtpdvv taismvknde idkfvalyee eiikdntgkp irvktlgqkl
      121 yvdsvkqhdv tfgigpagtg ktflavtlav talkrgqvkr iiltrpavea geslgflpgd
      181 lkekvdpylr pvydalyqil gkdqttrlme reiieiapla ymrgrtldna fvildeaqnt
      241 timqmkmflt rlgfnskmiv ngdisqidlp rnvksglida qeklknihqi dfvhfsakdv
      301 vrhpvvaqii rayepapvkk eeseeldpqp iseg
//
LOCUS       WP_175880049             274 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Streptococcus thalassemiae].
ACCESSION   WP_175880049
VERSION     WP_175880049.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..274
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31571
     Region          9..270
                     /region_name="YbbA"
                     /note="Predicted hydrolase of the alpha/beta superfamily
                     [General function prediction only]; COG2819"
                     /db_xref="CDD:442067"
ORIGIN      
        1 mnhsyfylkm kehklkvpyt gkerrvrvll pkdyekdtdr sypvvyfhdg qnvfyskesf
       61 ighswkiipa ikrnpdisrm ivvaidndgm grmneyaawk fqespipgqq fggkgveyae
      121 fvmdvvkpfi detyrtkadr qhtamigssl ggnitqfigl eyqdqigclg vfssanwlhq
      181 eafnryierq klspdqrifi yvgteeaddt dktlmagnik qsyidsslry yhdliaggvh
      241 ldnlvlkvqs gaihseipws enlpdclrff aekw
//
LOCUS       WP_175880084             752 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Streptococcus
            thalassemiae].
ACCESSION   WP_175880084
VERSION     WP_175880084.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Ingmer,H., Vogensen,F.K., Hammer,K. and Kilstrup,M.
  TITLE     Disruption and analysis of the clpB, clpC, and clpE genes in
            Lactococcus lactis: ClpE, a new Clp family in gram-positive
            bacteria
  JOURNAL   J Bacteriol 181 (7), 2075-2083 (1999)
   PUBMED   10094684
REFERENCE   4  (residues 1 to 752)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11909043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..752
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=83633
     Region          1..>80
                     /region_name="McsA"
                     /note="Protein-arginine kinase activator protein McsA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3880"
                     /db_xref="CDD:443088"
     Region          100..712
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mlcqnckind stihlytnln gkqkqidlcq ncykiiktdp nnslfkgmtd lnnrdfdpfg
       61 dffndlnnfr pssntppipp tqsgggyggn ggygsqnhgs aqtpppsqek glleefginv
      121 teiarrgdid pvigrddeii rvieilnrrt knnpvligep gvgktavveg laqkivdgdv
      181 phklqgkqvi rldvvslvqg tgirgqfeer mqklmeeirk rediilfide iheivgagsa
      241 sdgnmdagni lkpalargel qlvgattlne yriiekdaal errmqpvkvd eptvdetiti
      301 lkgiqkkyed yhhvqytdaa ieaaatlsnr yiqdrflpdk aidlldeags kmnltlnfvd
      361 pkvidqrlie aenlksqatr eedfekaayf rdqiakykem qkkkvtdqdt piisektieh
      421 iieqktnipv gdlkekeqsq lihlaedlks hvigqddavd kiakairrnr vglgtpnrpi
      481 gsflfvgptg vgktelskql aielfgsads mirfdmseym ekhsvaklvg appgyvgyde
      541 agqltekvrr npyslillde vekahpdvmh mflqvlddgr ltdgqgrtvs fkdaiiimts
      601 nagtgkaeas vgfgaaregr tnsvlgelgn ffspefmnrf dgiiefkals kdnllqivel
      661 mltdvnkrls cnnihldvtd kvkeklvdlg ydpkmgarpl rrtiqdyied aitdyylenp
      721 sekdlkavmt skgkiqiksa kkaevkaset ek
//
LOCUS       WP_175880118             185 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Streptococcus
            thalassemiae].
ACCESSION   WP_175880118
VERSION     WP_175880118.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..185
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21608
     Region          25..>123
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          101..178
                     /region_name="TetR_C_8"
                     /note="Transcriptional regulator C-terminal region;
                     pfam14278"
                     /db_xref="CDD:464123"
ORIGIN      
        1 mserriseks lenlrksnqe snlltreaie tallqllekk dltkisisel vkragvsraa
       61 fyrnydskee ilesvfkrtv hnimeqlhyy dlktdlylvw vhlfrearke arviqlaldy
      121 hlekifvqam qeflekyhgk skgvssylhs fwssaivsvl lkwikdgmkv paekiadlgl
      181 pffkk
//
LOCUS       WP_175880140             406 aa            linear   BCT 11-JAN-2025
DEFINITION  cell division protein FtsQ/DivIB [Streptococcus thalassemiae].
ACCESSION   WP_175880140
VERSION     WP_175880140.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..406
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=46394
     Region          132..345
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mskdkknegk eileefkels ewqkrnqeyl kkkaeeeaal aeekekerqa rmaskseksd
       61 atedqesesd pkdsksakee seekvespea dkeeeeiees tskedeeqdk klakkatkek
      121 pakakipgfh ilraltilfp sllllivsay llspyatmke irvegtmhtt addirqasgi
      181 qdsdytinll ldkakyekqi ksnywvesaq lvyqfptkft ikvkeydiva yyisgenhyp
      241 ilssgqlets avslvslpet ylsvlfndse qikafvsela qispelkaai qkvelapskv
      301 tsdlirltmn dsdevlvpls emskklpyys kikpqlseps vvdmeagiys ytvadklime
      361 aeekakqeak eaekkqeedr krleeeqkkq eeqnnrnqtt qrssrr
//
LOCUS       WP_175880165             261 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Streptococcus thalassemiae].
ACCESSION   WP_175880165
VERSION     WP_175880165.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007845
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..261
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30011
     Region          1..261
                     /region_name="COG3694"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:442909"
ORIGIN      
        1 mkkyqrmhli firqyikqim eykvdfvvgv lgvfltqgln llflnvifqh ipslegwsfq
       61 eiafiygfsl ipkgldhlff dnlwalgqrl vrkgefdkyl trpinplfhi lvetfqidal
      121 gellvggill gttvtsidwt lpkfliflvc ipfatliyts lkiatasiaf wtkqsgamiy
      181 ifymfndfak ypisiynsll rwlisfivpf aftayypasy flqdkdvifn igglilislv
      241 ffsislklwd rgldsyesag s
//
LOCUS       WP_175880306             235 aa            linear   BCT 11-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Streptococcus
            thalassemiae].
ACCESSION   WP_175880306
VERSION     WP_175880306.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..235
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=25674
     Region          127..221
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 meeksmwkel lnragwilvf llatilyqip lavtailtln avpllqsgli vaglsivvla
       61 lfifgarktq lasfnfsffr akdlarlgls ylviicsnil gsillqlsne tttanqsqin
      121 dmvqnsslis sffllallap iceeilcrgi vpkkifrgke nlgfvvgtiv fallhqpsnl
      181 pslliyggms tvltwtvykt qrlemsillh mivngvafcl lalvvimsrt lgisv
//
LOCUS       WP_175880344             420 aa            linear   BCT 11-JAN-2025
DEFINITION  NRAMP family divalent metal transporter [Streptococcus
            thalassemiae].
ACCESSION   WP_175880344
VERSION     WP_175880344.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..420
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45811
     Region          10..417
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 msqaislnqs twssklkamg pgilmasaav ggshivsstq aggsygwsll llvilanifk
       61 ypffrfgaey tadtgktlve gyaekgklyl wiffilnvfs amvntagvai lcsaiiasaf
      121 pmiglsitqw slilvaiiwa mllfggykll dgmvkwimsa ltiatvlavi iaavkhpeys
      181 sdfvektpwq maalpfivsl lgwmpapiei sainslwsae krktvnfnte dalfdfntgy
      241 igtailavff valgaliqyp tgqaveaasa kyisqfvgmy asvlgewsry litfiaflci
      301 fgtvitvidg ysrvnqeslr llisqkednr kslniwmtit aiigiviikf fagqvstmlr
      361 famigsfltt pffallnyal vtrenknlps wlkhlaiagl lflfgfaiff iyalaigkag
//
LOCUS       WP_175880351             231 aa            linear   BCT 11-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Streptococcus thalassemiae].
ACCESSION   WP_175880351
VERSION     WP_175880351.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 231)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 231)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 231)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..231
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24654
     Region          6..229
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mkekgfwega qaamptalgy vsiglacgii gapyvtpvem glmslfvyag saqfamlali
       61 avqapvaaia mtvflinlrl fllslhasty frhtslwqni gmssiltdet ygvlmgelah
      121 adkvnpmwmh gnnlnsyvaw fvgtvagtal ggllpnpeif gldfalvgmf igifasqfqi
      181 mqrripvrnl liilavvavs ffllltvvsq slavlfatll gctmgvvldg q
//
LOCUS       WP_175880383             426 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 125 protein [Streptococcus
            thalassemiae].
ACCESSION   WP_175880383
VERSION     WP_175880383.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Gregg,K.J., Zandberg,W.F., Hehemann,J.H., Whitworth,G.E., Deng,L.,
            Vocadlo,D.J. and Boraston,A.B.
  TITLE     Analysis of a new family of widely distributed metal-independent
            alpha-mannosidases provides unique insight into the processing of
            N-linked glycans
  JOURNAL   J Biol Chem 286 (17), 15586-15596 (2011)
   PUBMED   21388958
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007529
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..426
                     /product="glycoside hydrolase family 125 protein"
                     /EC_number="3.2.1.163"
                     /GO_function="GO:0004559 - alpha-mannosidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48973
     Region          3..426
                     /region_name="COG3538"
                     /note="Meiotically up-regulated gene 157 (Mug157) protein
                     (function unknown) [Function unknown]"
                     /db_xref="CDD:442759"
ORIGIN      
        1 miyskeivre wldevaerak dhpewvdvfe rcytdtldnt veiledgstf vltgdipamw
       61 lrdstaqlrp ylhvakrdal lrqtiaglvk rqmtlvlkdp yansfnieen wkghhetdht
      121 dlngwiwerk yevdslcypl qlayllwket getsqfdetf vaatkeilhl wtveqdhkns
      181 pyrfvrdtdr kedtlvndgf gpdfavtgmt wsafrpsddc cqysylipsn mfavvvlgyv
      241 qeifaelvla dsesiiadak rlqseiqegi enyaytsnsk gekiyafevd glgnasimdd
      301 pnvpsllaap ylgycdidde vyqatrrtil spenpyfyqg eyasglgssh tfyryiwpia
      361 lsiqglttrd kaekkflldq lvacdggtgv mhesfhvddp tlysrewfsw anmmfcelvl
      421 dyldir
//
LOCUS       WP_175880384             698 aa            linear   BCT 11-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Streptococcus thalassemiae].
ACCESSION   WP_175880384
VERSION     WP_175880384.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..698
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=79347
     Region          2..698
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mkplletidt rfgtaskhaf srgntlpytg vpfgmnyfvp qtsdqdgswf fdphlpifqg
       61 irlthqpspw igdyswllli pvtgqisgds lfhrqssydm dkasfqphyl kifslryqie
      121 tqltptcyga sirlnqkqgk alslylhvad eltveqvder tlalrqegkt etnknplilf
      181 ttlqmntdil avsqegedwr idlasshaei qlatsfispt qallnlpqvd fdnckanaqa
      241 dwenllhrfd iietgeadrt ffdhclyrlf lfpqtfyevd esgqaihidl atgtakpgvl
      301 fsnngfwdtf rttfplfalv ipehyhrfle gflnsyrdtg flpkwlapde rgmmpgtlld
      361 giiadsackd mapdleeell qamletaskf dplgingrhg laqyqelgyl stdhhesvsh
      421 tldyaysdfc iascakklgq ndiaetyrta sqnyrhlfda etgymrards qgnfrsdfsp
      481 yswgrdyaec saiqatlgvl hdipgliqlm dgkevfsnyl lkacqdaplf ettgygyeih
      541 emsematapf gqiaisnqps fhipylfrys nypnytalli ktlrqkafhp swqaypgded
      601 ngslsawyiw salgfyptcp gkssydlgip lfdhlriyla kenkwldiht eqnhshfnfv
      661 kecrldknlv stiqhqdllk aeqltftlsw llsqpsts
//
LOCUS       WP_175880398             810 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Streptococcus
            thalassemiae].
ACCESSION   WP_175880398
VERSION     WP_175880398.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..810
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=90036
     Region          2..806
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mnyskalnec iesaymvagh fgahyleswh lliamsnhsy svagatlndy pyemdrleev
       61 aleltetdys qdeiftelpf shrlqvllde aeyvasvvha kvlgtehvly ailhdgnala
      121 trileragfs yedkkdqvki aalrrnleer agwtredlka lrqrhrtvad kqnsmanmmg
      181 mpqtpsggle dythdlteqa rsgklepvig rdkeisrmiq ilsrktknnp vlvgdagvgk
      241 talalgiaqr iasgdvpaem akmrvleldl mnvvagtrfr gdfeermnni ikdieedgqv
      301 ilfidelhti mgsgsgidst ldaanilkpa largtlrtvg attqeeyqkh iekdaalsrr
      361 fakvtieeps vadsmtilqg lkatyekhhr vqitdeavet avkmahrylt srhlpdsaid
      421 lldeaaatvq nkskhvkadd sdlspadkal mdgkwkqaaq liakeeevpv ykdlvteadi
      481 lttlsrlsgi pvqkltqtda kkylnleael hkrvigqdqa vssisrairr nqsgirshkr
      541 pigsfmflgp tgvgktelak tlaevlfdde salirfdmse ymekfaasrl ngappgyvgy
      601 eeggeltekv rnkpysvllf devekahpdi fnvllqvldd gvltdskgrk vdfsntiiim
      661 tsnlgatalr ddktvgfgak dirfnqenme krmfeelkka yrpefinrid ekvvfhslss
      721 dhmqevvkim vkplvaslae kgidlklqas alkllanqgy dpemgarplr rtlqtevedk
      781 laelllkgel eagstlkigv kagqlkfdia
//
LOCUS       WP_175880458             456 aa            linear   BCT 11-JAN-2025
DEFINITION  MATE family efflux transporter [Streptococcus thalassemiae].
ACCESSION   WP_175880458
VERSION     WP_175880458.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..456
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49466
     Region          14..440
                     /region_name="MATE_yoeA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Bacillus
                     subtilis yoeA; cd13138"
                     /db_xref="CDD:240543"
ORIGIN      
        1 mnkkrtvdli hgpilpslvs fafpillsni fqqlyntadv livgrflgqd slaavgttta
       61 ifdlivgftl gvgngmgivi aryygarnft kikeavaatw ilgallsilv mllgflglyp
      121 llqyldtpve ilpqsyqyis mivtcvgvsf aynlfagllr sigdslaalg flifsalvnv
      181 vldlyfitql qlgvqsagla tiisqglsav lcfyylrksv pellpqlkhf kwdkalyadl
      241 leqglamglm ssivsigsvi lqssvntfga viisaqtaar rimafallpm taisasmttf
      301 asqnlgakrp drivqglrig srlsiswavf vciflffasp alvsflasst dsylvengsl
      361 ylqissafyp ilsllliyrn clqglgqkvl plvssfieli gkiafvvlii pwagykgvil
      421 cepliwvamt vqlyfslfrh plikegeeil atkvss
//
LOCUS       WP_175880517             285 aa            linear   BCT 11-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Streptococcus
            thalassemiae].
ACCESSION   WP_175880517
VERSION     WP_175880517.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     A novel family of ubiquitous heavy metal ion transport proteins
  JOURNAL   J Membr Biol 156 (2), 99-103 (1997)
   PUBMED   9075641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440813
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..285
                     /product="cation diffusion facilitator family transporter"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31827
     Region          7..278
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
ORIGIN      
        1 mkakytvwva fflnlsyaiv efiaggifgs savladsvhd lgdaiaigis afletisnre
       61 edshytlgyk rfsllgamvt avilmtgsvl vileniakif hpqpindegi lwlgiiaiti
      121 nvlaslvirk gqtknesils lhfledtlgw vtvilmaivl rftdwyildp llslvisffi
      181 lskalprfwr tlkifldavp egvdiqkikt dlaeldhvas inqlnlwtmd gleknaivhv
      241 clkemehmet ckesiriflk dcgfqnitie vdadleshqa hkrkv
//
LOCUS       WP_175880494             227 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Streptococcus thalassemiae].
ACCESSION   WP_175880494
VERSION     WP_175880494.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..227
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25106
     Region          1..225
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msilsiknis kfyaldgkhq eqalkninlq iakgkitaiy gpsgcgktsl lniisgldrq
       61 yegglefkge slrdlseiel tqfrkdkigf vfqnfnliph qsvldnvklp lyvkdlsdre
      121 mtmiakeqls nlgmepfvak nvkqlsggqk qrvaiaralv nqpdmivade ptgsldsqsq
      181 emvlevfknl aqtgktvliv thnpevaeya dviikmkdge vveevkk
//
LOCUS       WP_175880502             292 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Streptococcus thalassemiae].
ACCESSION   WP_175880502
VERSION     WP_175880502.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..292
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33328
     Region          3..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..288
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(106..107,109,112,116,118..124,218..223,229..230,
                     232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mnlkdlqyfy dlcqlqsyte vakqhkvsqp sisyaikrle esfncklihh dpshrsfklt
       61 pqgqillkht elilpevist rkeinrslaq ystvgfppii iqylfaalnk kdkfdflkkv
      121 rpirggsvel lnllikgdld asllgliepl nypsieshel fhkelyvvls knhpfataps
      181 lafeeladqs filldehfvh lkafetlnqk yqnkaeiffk tddiailkel lkkgiglsll
      241 adialseedd dlikiplipk dkitftvyya ylksatpsse vealfnllks ye
//
LOCUS       WP_175880637             418 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA recombination protein RmuC [Streptococcus thalassemiae].
ACCESSION   WP_175880637
VERSION     WP_175880637.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19586425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..418
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=47787
     Region          <30..123
                     /region_name="Apolipoprotein"
                     /note="Apolipoprotein A1/A4/E domain; pfam01442"
                     /db_xref="CDD:460211"
     Region          86..418
                     /region_name="RmuC"
                     /note="DNA anti-recombination protein (rearrangement
                     mutator) RmuC [Replication, recombination and repair];
                     COG1322"
                     /db_xref="CDD:440933"
ORIGIN      
        1 mesllvllli anlaglfliw qrqdkqekhl sknledqadh lsdqldyrfe qarqasqldq
       61 kdlevavsdr lqevrielhq gltqvrqemt enllqtrdkt dqrlqalqes neqrleqmrq
      121 tveeklektl qtrlqasfet vskqlesvnr glgemqtvar dvgtlnkvls gtktrgilge
      181 lqlgqiiedi mtpaqyerey atvensserv eyaiklpgqg dleyvylpid skfpladyyr
      241 leeayeagdk deiercrksl lasvkrfakd irnkyiappr ttnfgvlfvp teglyseivr
      301 npvffddlrr eeqiivagps tlsallnsls vgfktlniqk sadhisktla svktefgkfg
      361 gilvkaqkhl qhasgnidel lnrrtiaier tlrhielseg epaldllhfq eneeeyed
//
LOCUS       WP_175880615             288 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Streptococcus
            thalassemiae].
ACCESSION   WP_175880615
VERSION     WP_175880615.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..288
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33037
     Region          1..260
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mdkpditsli dlhfeemtdl eqeiahyflq tetiaddlss qqvtqklhis qaaltrfakk
       61 cgftgyrefi fqyqheaenq anqvskhspl tkrvlrsysn mreqtqnlid evqleriaql
      121 iedaeriyff gtgssglvar emklrfmrlg vvcealtdqd gfawttsimd enclvlgfsl
      181 sgttpsilds lldakemgak tvlfssvpsk dsqtytetvl vathsqpsyi qrisaqlpml
      241 ffidliyayf leinreskek ifnsywenkk lngyrrqkrv rkesgtkv
//
LOCUS       WP_175880642             257 aa            linear   BCT 11-JAN-2025
DEFINITION  TatD family hydrolase [Streptococcus thalassemiae].
ACCESSION   WP_175880642
VERSION     WP_175880642.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..257
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28716
     Region          2..254
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mifdththln veefagreae eialaaemgv tqmnivgfdk ptieralelv deydqlyati
       61 gwhpteagty teeietylld klkhpkvval geigldyhwm tapkevqeqv frrqiqlskd
      121 ldlpfvvhtr daledtyeii ksegvgprgg imhsfsgtle waekfvalgm tisfsgvvtf
      181 kkatdiqeaa kklpvdkmlv etdapylapv pkrgrenkta ytryvvdfia dlrgmtteel
      241 aaattanaer ifgldsk
//
LOCUS       WP_175880654             294 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Streptococcus thalassemiae].
ACCESSION   WP_175880654
VERSION     WP_175880654.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 294)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..294
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33273
     Region          4..225
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtvikvekls kkikdkeilr nisfeindge cvaligpnga gkttlldcll gdklvtsgqv
       61 siqglsvtss qldyirgylp qenvivqklk vkeliaffqs typnplsnqe idqllqfdqq
      121 qkeqfaekls ggqkrlfsfv ltligrpklv fldeptaamd tstrqrfwei vqdlkakgvt
      181 ilysshyiee vehtadrilv lnkgelirdt tplamrseei ekyfilplay kevveksnlv
      241 enwtlkqdsl qvvtreadaf wqllvqagcs iqeievnnrs lldtifeetq kgdd
//
LOCUS       WP_175880677             213 aa            linear   BCT 11-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Streptococcus
            thalassemiae].
ACCESSION   WP_175880677
VERSION     WP_175880677.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..213
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=23983
     Region          109..210
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mkllknfgwf llavlsflfi ygfiqglats slalgaspya vtllyvalag vyvygiykwy
       61 qkapvhieks gfnrfiwlpa lvwflslvvq fflpddpsvn qqiatdltls qplfsffavv
      121 ifaplteeli frgmlarylf pkqdnskqtl ifllvssvlf alihfpgdvq qffvyfslgf
      181 slglayisrk glvysislha lnnlvgflmi lml
//
LOCUS       WP_175880692             115 aa            linear   BCT 11-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin
            [Streptococcus thalassemiae].
ACCESSION   WP_175880692
VERSION     WP_175880692.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..115
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=13210
     Region          8..112
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mefnenaysl ivsetvqeql rgikdyisan yfseqagant vknilygler levfpevgfd
       61 adervggiiy pphktrciil gdylafyhil edrkavfvsd iihckqdyir lfkkk
//
LOCUS       WP_175880713             169 aa            linear   BCT 11-JAN-2025
DEFINITION  VanZ family protein [Streptococcus thalassemiae].
ACCESSION   WP_175880713
VERSION     WP_175880713.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008822
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..169
                     /product="VanZ family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=19223
     Region          44..130
                     /region_name="VanZ"
                     /note="Glycopeptide antibiotics resistance protein
                     [Defense mechanisms]; COG4767"
                     /db_xref="CDD:443799"
ORIGIN      
        1 mleskkttry vfyvylmllt wgilfkfetn pefiafflap ryinwipfse plivdgkivf
       61 aemlfnlisf iplgvcfpli ktnlsslkiv gtgflisllf eclqyilaig itditdlaln
      121 tlgvcvglli yqmfirvfks qtrkwvnilg mlslgfayfv llllhligv
//
LOCUS       WP_175880724             195 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Streptococcus thalassemiae].
ACCESSION   WP_175880724
VERSION     WP_175880724.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..195
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=22609
     Region          2..138
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(7,9,66..67,70)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            9
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(65,119..120,122..123,127)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(71,76..77,111,118..119,122..123,126,129)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(96..98,111..112,119..120,123,127,130,134)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(96,120,123,127,130,134)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Region          128..>193
                     /region_name="transpos_IS3"
                     /note="IS3 family transposase; NF033516"
                     /db_xref="CDD:468052"
     Site            order(128,134..135)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 mrygyvrvst keqnidrqfs alvenklske nifidyvsgk dfdrmeyqkl latlkendel
       61 viksidrlgr nydeileqwq aitkkkkvni tvldfpllnt knsndnitgk lisdivlqvl
      121 syvaqfereq ikqrqmegir eaqkkgkkfg rpklivpnnl pdviaqykkk eitlregadi
      181 lgvskstfhn wikns
//
LOCUS       WP_175880894             311 aa            linear   BCT 11-JAN-2025
DEFINITION  serine hydrolase domain-containing protein [Streptococcus
            thalassemiae].
ACCESSION   WP_175880894
VERSION     WP_175880894.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Agarwal,V., Yadav,T.C., Tiwari,A. and Varadwaj,P.
  TITLE     Detailed investigation of catalytically important residues of class
            A beta-lactamase
  JOURNAL   J Biomol Struct Dyn 41 (5), 2046-2073 (2023)
   PUBMED   34986744
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Philippon,A., Jacquier,H., Ruppe,E. and Labia,R.
  TITLE     Structure-based classification of class A beta-lactamases, an
            update
  JOURNAL   Curr Res Transl Med 67 (4), 115-122 (2019)
   PUBMED   31155436
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444642
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..311
                     /product="serine hydrolase domain-containing protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35891
     Region          6..294
                     /region_name="Beta-lactamase"
                     /note="pfam00144"
                     /db_xref="CDD:395092"
ORIGIN      
        1 mkwtkiikki eeqieagiyp gasfayfkdn qwtefylgqs dpehglqtea glvydlasvs
       61 kvvgvgtvft flwersqldi drpvtdflae sdypditirq llthatdldp fipnrdllta
      121 selkeamshl nrrsqpafly sdvhflllgf ilerifdkdl deilqeqvwn pwrmtetqfg
      181 pvelavptvr gietglvhdp karllgrhag saglfstvkd lqiflehyla ddfardlsqn
      241 fsplddkers lawnlegdwl dhtgytgtfi mwnrqnqeaa iflsnrtyek deraqwildr
      301 nqvmdlirke e
//
LOCUS       WP_175880930             409 aa            linear   BCT 11-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Streptococcus thalassemiae].
ACCESSION   WP_175880930
VERSION     WP_175880930.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18641232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..409
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=47291
     Region          5..>125
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          33..60
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          63..88
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          67..328
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          97..124
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          130..155
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          169..195
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(171..172,175..176,178,202,205,208..209,211..212,235,
                     238..239,242..243,246)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          200..229
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          234..262
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          268..294
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          269..399
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Site            order(303,306..307,310..311,313,333,336..337,340..341,
                     343..344,367,370..371,374..375,378)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          303..327
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          331..361
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mnnsqqmlqa leeqdlakae hyfakalend psdllyelat ylegigfypq akeiylkive
       61 dfpevhlnla aiasedgqie eafayleeiq adsdwyvsal alkadlyqme gltdvarekl
      121 lealtysedp llilglaeld selenyqeai qgyaqldnrs iyeqtgisty qrigfayaql
      181 gkfetatefl ekaleleydd ltafelasly fdqeeyqkav lyfkqldtis pdfegyeygy
      241 sqalhkehqv qealriakqg leknpfetrl llaasqfsye lhdasgaeny lltakvdaed
      301 teeillrlat iyleqeryed ildlqseepe npltkwmiar syqemddldt ayehyqelag
      361 dlkdnpefle hyiyllrelg yfeeakvnaq tylklvpddv qmqelyerl
//
LOCUS       WP_175880958             182 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Streptococcus thalassemiae].
ACCESSION   WP_175880958
VERSION     WP_175880958.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..182
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19692
     Region          3..165
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mskkvlfivg slrqgsfnhq maleaekala gkaevsyldy salplfsqdl evpthpavaa
       61 areavlaada iwifspvynf sipgtvknll dwlsraldls dtrgasalqd kfvtvssvan
      121 aghdqlfaiy kdllpfirtq ivgdftaarv ndsawadgkl vleetvlksi ekqaqdlina
      181 ik
//
LOCUS       WP_175880966             623 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Streptococcus thalassemiae].
ACCESSION   WP_175880966
VERSION     WP_175880966.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 623)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..623
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=70632
     Region          6..525
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          554..620
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 msdfivekln ksvgdktvfk disfiihdld rigligvngt gkttlldvls gvsgfdgdvs
       61 pfsakndyqi gyltqdpdfd dsktvldtvl ssdlkeiqli reyelimlny sedkqarler
      121 vmaemdslqa weiesqvktv lsklgiqdls tpvgelsggl rrrvqlaqvl lgnhdlllld
      181 eptnhldiat iewltlflkn skktvlfith dryfldalst rifeldragl teyqgnyqdy
      241 vrlkaeqder daallhkkeq lykqelawmr rqpqaratkq qarinrfhdl kkevsggvae
      301 tdltmnfets rigkkviefq dvsfayenkp ilqdfnllvq akdrigivgd ngvgkstlln
      361 liagslepta gqvvigetvr iayfsqqieg ldeskrviny lqevaeevkt sggsttsiae
      421 lleqflfprs thgtliekls ggekkrlyll klllekpnvl lldeptndld iatltvlenf
      481 lqgfagpvlt vshdryfldk vatkilafed gkirpffghy tdyldekafe temanqvqka
      541 ekekvvkvre dkkrmtyqek qewasiegdi ealenriaai eeemqangsd fgklatlqke
      601 ldeknealle kyeryeylsd fds
//
LOCUS       WP_175880953             466 aa            linear   BCT 11-JAN-2025
DEFINITION  bifunctional Cof-type HAD-IIB family hydrolase/peptidylprolyl
            isomerase [Streptococcus thalassemiae].
ACCESSION   WP_175880953
VERSION     WP_175880953.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 466)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   5  (residues 1 to 466)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
REFERENCE   6  (residues 1 to 466)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..466
                     /product="bifunctional Cof-type HAD-IIB family
                     hydrolase/peptidylprolyl isomerase"
                     /EC_number="3.1.3.-"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=51813
     Region          13..265
                     /region_name="HAD_HPP"
                     /note="phosphatase, similar to Bacteroides
                     thetaiotaomicron VPI-5482 BT4131 hexose phosphate
                     phosphatase; belongs to the haloacid dehalogenase-like
                     superfamily; cd07517"
                     /db_xref="CDD:319819"
     Site            order(18..22,53..55,194,216..217,220..221)
                     /site_type="active"
                     /db_xref="CDD:319819"
     Region          282..466
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mdaklrykak kikivffdid dtlrnsktgf ipssipvvfk qlrekgiltg iasgrgifgv
       61 vpeirelkpd ffvtlngayi edkkgqviyq hqieksdvee yiswakqegi eyglvgshaa
      121 klstrtdmis eainpiypdl dvdpdfheke niyqmwtfed kgddlrlpds lsdklrmvrw
      181 hehssdvvpi sgskatgvek vvehlglkpe nvmvfgdgln dlelfdyagi svamgishdn
      241 ikekadyitk tleedgifda legfgmveke lhfpqvdiet vegpiatikt nhgdlriklf
      301 pehapktvan fvalskdgyy dgvifhriik dfmiqggdpt gtgmggesiy gesfedefse
      361 elynirgals managpntng sqffivqnqh lpyskkeiar ggwpepiaei yanqggtphl
      421 drrhtvfgql adeasyavld aiasvetgam dkpvedvvie tieied
//
LOCUS       WP_175880973             168 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrofolate reductase [Streptococcus thalassemiae].
ACCESSION   WP_175880973
VERSION     WP_175880973.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11087044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..168
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19612
     Region          4..165
                     /region_name="DHFR_1"
                     /note="Dihydrofolate reductase; pfam00186"
                     /db_xref="CDD:425512"
     Site            order(8,25,30,61,100,106,119)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(10,17,47..49,68,101..104)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 mtkkivaiwa qdeegvigkd nrlpwhlpae lqhfkettln hailmgrvtf dgmgrrllpq
       61 retliltrnp eekidgvatf qdvqsvldwy qtqeknlyil ggkqifqafe syldevivth
      121 iharvegdty fpeefdlslf etvsskfyak deknpydfti qyrkrkev
//
LOCUS       WP_175880977             191 aa            linear   BCT 11-JAN-2025
DEFINITION  cysteine hydrolase family protein [Streptococcus thalassemiae].
ACCESSION   WP_175880977
VERSION     WP_175880977.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..191
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21279
     Region          4..182
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mtkalisidy tedfvadsgk ltagapaqai sdaiskvtrl afergdyiff nidaheendc
       61 fhpesklfpp hnligtsgrn lygdlgtfyq ehgsdsrvfw mdkrhysafs gtdldirlre
      121 rristviltg vltdicvlht aidaynlgyd ieivkpavas iwpenhqfal ghfkntlgak
      181 lvdenlneil e
//
LOCUS       WP_175881016             778 aa            linear   BCT 11-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Streptococcus thalassemiae].
ACCESSION   WP_175881016
VERSION     WP_175881016.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus thalassemiae
  ORGANISM  Streptococcus thalassemiae
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus; Streptococcus thalassemiae group.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 778)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 778)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 778)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11552376
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Streptococcus thalassemiae"
                     /db_xref="taxon:2736608"
     Protein         1..778
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=85322
     Region          8..667
                     /region_name="P-type_ATPase"
                     /note="uncharacterized subfamily of P-type ATPase
                     transporter, similar to uncharacterized Streptococcus
                     pneumoniae exported protein 7, Exp7; cd02609"
                     /db_xref="CDD:319795"
     Site            order(298..300,364,383..385,408,462..464,507,510,513,532,
                     535)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319795"
     Site            order(592,596..597,599..600,633,636..637)
                     /site_type="other"
                     /note="putative cation binding site [ion binding]"
                     /db_xref="CDD:319795"
ORIGIN      
        1 mdknkimglt qrevkerqae glvndftasa ststwqivkr nvftlfnaln faialalafv
       61 qawsnlvffa vicfnafsgi vtelrakhmv dklnlmtkek vktirdgqev alnpeelvlg
      121 dvirlsageq ipsdalvleg faevneamlt gesdlvqkev dalllsgsfl asgsvlaqvh
      181 hvgadnyaak lmleaktvkp insrimksld klagftgkii ipfglallle almlkglplk
      241 ssvvnsstal lgmlpkgial ltitslltav iklglkkvlv qemysvetla rvdmlcldkt
      301 gtitqgkmqv eavlpltaty geetiasilt symahsedkn ptaqairqrf vgeitypmis
      361 nlpfssdrkw gameleglgt vflgapemll dsevpearea lergsrvlvl alsqekldhh
      421 kpekpsdiqa lalleildpi regaaetldy lrsqevglki isgdnpvtvs siaqkagfad
      481 ydsyvdcski tdeelvamae etaifgrvsp hqkkliiqtl kkaghttamt gdgvndilal
      541 readcsivma egdpatrqia nlvllnsdfn dvpeilfegr rvvnniahia pifliktiys
      601 fllavicias allgrsewil ifpfipiqit midqfvegfp pfvltferni kpvepnflrr
      661 smlralpsal mvvfsvlfvk ifgasqgwye leistllyyl lgsigflsvf racmpftlcr
      721 vllivwsvgg flatalfpri qklleistlt gqtlpvygvm mlvftvifil tsryqark
//
LOCUS       WP_175881048             810 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein, partial [Burkholderia
            cepacia].
ACCESSION   WP_175881048
VERSION     WP_175881048.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..>810
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
     Region          14..789
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnmqntiaal rggllqqdrl lkldtplggn vltvqravgr srigrayeft ldvlstegdl
       61 elkkliaqpv tlwieqgnrs yrpisgyvht arrlgadggl ttyqltfadf thflkfrrdq
      121 rfwndttvdq iisdvlnqhp qakghfrfal skplpnrsyt rqhdtdwhfv hrlmedegly
      181 cawqqaddgk shtlvitdnl qafaplspet vsfyrggsas eadaftqwsg trtlqsvtrs
      241 trtfdyknpa qpsnpkgtsl ptmagqgelp dqlevyeytg aytyldqtrg dhltkvkmee
      301 wesqakrfha aggvraidag rrftltehpe hdrdsadqre favievawwi ennlpvasds
      361 adfpyslrea lvgaqegyga spvfrvphdd gstgfylvev eaqrvsvpyr spfehhkpem
      421 hletaivvgp qgeevytdsl nrirvqfvwd rmnpgdenas cwvrvvqsdt gggyggvhvp
      481 rigeevlidy vggdcdrpla vgrvynganq pqwhtdgils gyrskeysgs gynqlvmdda
      541 tgqnrvqlms ssansllhlg yiidhsansr gsylgsgfdl rsdaygavra sqglyvtthp
      601 kaansqpldv keaqqqlvtg eslveamsgv seqhqaeslk daqdtmraft datqesasgs
      661 asggrtaggg tgnanafkep vmlfgspsgi gmstqqsvhm vandhvnvas gqsvhvaagk
      721 sligsigqkl slfvqnagmk lfagkgkvei qaqsdnievt aqkavkvvsa tgqveiaadq
      781 gilltsggay irikdgnvei hapgkidikg
//
LOCUS       WP_175881058             204 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175881058
VERSION     WP_175881058.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..204
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=23123
     Region          1..>191
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mrklyygris ttdgqssasq yddarvhgvq dkdvfidegv sgyhvapder eqwrkaehdl
       61 rhggvlivrw ldrisrryde lhrtmrrlmd lgvrvectln gmafdgnttd piakatrdav
      121 lafmaaqgea dyrnraemqr rgvaiakteg kyrgrvrshd yeairewrse ngasiretae
      181 kfgvgtatvk racaestimh ldks
//
LOCUS       WP_175881059             531 aa            linear   BCT 11-JAN-2025
DEFINITION  ADP-ribosylglycohydrolase family protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175881059
VERSION     WP_175881059.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..531
                     /product="ADP-ribosylglycohydrolase family protein"
                     /calculated_mol_wt=57870
     Region          4..366
                     /region_name="DraG"
                     /note="ADP-ribosylglycohydrolase [Posttranslational
                     modification, protein turnover, chaperones]; COG1397"
                     /db_xref="CDD:441007"
ORIGIN      
        1 mvnredtiva salwaaygda vgfptelvtl aefrkrtgqh emtgpiawar kvgglfgana
       61 rfprgaysdd tqlrlctsra irgdgffdve sfakielpvw lnyalgagrg sklaagnlal
      121 rdstwsqnfy rgpksnyweg ggngaamrvq phvwaaknfd astfmppvir davcthghpr
      181 alagaaihal mlaytidtgv lpaptqwvdf aeacdmafas lteddelalv wcpnwerfae
      241 rslaaafadv klewqtscer avvlcdgard eykayrdvle alggfspaer gsglktplya
      301 aalawlfrdr speigllaaa ntfgsdtdti atmagaliga vtgeapkdev qdsgyirsea
      361 krlahigqgk reasfsypdt lswvapraqr dawisfedgf alsglgpvvp fgdtfvpekq
      421 gelewqwcrt sfnqtilakr kpnaqrgpgr nrnessaean erhaprqmtf mdeseskpes
      481 iheltnrcir egfdatlige cllalsngpd gveraiafsa iiakarlarn r
//
LOCUS       WP_175881063             209 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0044].
ACCESSION   WP_175881063
VERSION     WP_175881063.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..209
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21831
     Region          1..206
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mslsallafa lilsvgvatp gptvllamsn gsryglrham vgmlgavsad vvlvalvgfg
       61 lgvlldaset afvtlkllga awlayvgirm lmsnggaaaa qprvpatpdr rsaflksffv
      121 amsnpkyylf msallpqfvd rsqaiapqya ilaativtid aigmtgyall gvhsvrvwka
      181 agekwlnrvs gslllmlagy valyrkaah
//
LOCUS       WP_175881074             410 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0044].
ACCESSION   WP_175881074
VERSION     WP_175881074.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..410
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42674
     Region          12..394
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(22..23,26..27,30,65,112..113,115..117,120,145,
                     148..149,152,224,227..228,231..233,236,266,270,320..321,
                     325,329,345,348..349,352..353,356)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mtpieqevrr rwlpvlaggl imgaalgirh vqglflapvs ldhgwsreaf glalalqnli
       61 wgvaqpftgm vadrfgsvrv ivagmllyaa glvtmaqaat tglftvgagl vigvalsgsa
      121 fasiygalsr lfppdrrgwa lgvagaiggl gqfcmvpvaq eliggigwqh afialalvaa
      181 llaplavalr drpaqaagaa agpdqsigea vreafahrgf wllnagffac gfqlafiath
      241 lpaylldhgl parhasvala lialtnvagt yacghlggll rrkyvlsvly lvralamaaf
      301 vaaplspasv yvfaavmgft wlgtvpltng visqvfgvry iatlfgfvff ghqlgsffgv
      361 wlgalvydat hsymplwigs ialgvlaall hlpiddarva rpasghaawa
//
LOCUS       WP_175881091             470 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0044].
ACCESSION   WP_175881091
VERSION     WP_175881091.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..470
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49515
     Region          16..419
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(28..29,32..33,36,76,134..135,137..139,142,162,
                     165..166,169,251,254..255,258..259,262,290,294,346..347,
                     351,355,371,374..375,378..379,382)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msrpqsppaa qprpgraala afvgttiewy dfyiygtaaa lvfgkvffss tmdpgvatll
       61 afvtfwagfa arplggivfg hlgdrvgrkt alvitlvmmg lattgigllp gyasigvwap
      121 aglvvlrvlq giavggewgg avliasenap khrsilyaaf aqqgsptgnl lataaffals
      181 alptpsflmw gwripfllsa vlviigmvir lrleesadmq rvlarkrtvk lplrdvvrdh
      241 wvvvllaagt lpvinvtyfr stfalswatk elgyaqgtfl gilsislvvq flmqpvgawf
      301 vskvdmrram cwilipeivl mpvmfhalat rsywvavagm cistipsamf ygavggvlar
      361 vfpanirytg lslayqlsal vvgggtpvla qailnatgsi vgvaiasgly alvslacmla
      421 llnrtgyrad elstaersda aewgaestga gsaageaaqp ddrgtlkpag
//
LOCUS       WP_175881197             273 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Burkholderia sp. BCC0044].
ACCESSION   WP_175881197
VERSION     WP_175881197.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..273
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28342
     Region          2..272
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mlktrvitai vmlavllpvm lfaplngfga ligivlvfaa wewarllklg gaspvvyavv
       61 aalalaatap lgvdtassrp lfmaagvfwl lvgpfalrrk pvlaggvwrp fllaaglvvf
      121 aacwhalvaa raqgvpfvls lllvvwladi gayfagkafg krklaitisp gkswegaigg
      181 wfavmvvsgi amavhafept lfsafaaryg magawaaltl lvaysvigdl fesllkrqag
      241 vkdssgllpg hggvldrvda llpvlplaml llg
//
LOCUS       WP_175881206             144 aa            linear   BCT 11-JAN-2025
DEFINITION  NfeD family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175881206
VERSION     WP_175881206.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Green,J.B., Lower,R.P. and Young,J.P.
  TITLE     The NfeD protein family and its conserved gene neighbours
            throughout prokaryotes: functional implications for stomatin-like
            proteins
  JOURNAL   J Mol Evol 69 (6), 657-667 (2009)
   PUBMED   20012272
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Kuwahara,Y., Ohno,A., Morii,T., Yokoyama,H., Matsui,I., Tochio,H.,
            Shirakawa,M. and Hiroaki,H.
  TITLE     The solution structure of the C-terminal domain of NfeD reveals a
            novel membrane-anchored OB-fold
  JOURNAL   Protein Sci 17 (11), 1915-1924 (2008)
   PUBMED   18687870
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..144
                     /product="NfeD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=15258
     Region          3..142
                     /region_name="YbbJ"
                     /note="Membrane protein implicated in regulation of
                     membrane protease activity [Posttranslational
                     modification, protein turnover, chaperones]; COG1585"
                     /db_xref="CDD:441193"
ORIGIN      
        1 mmsghlfwwi gvgvlvvael ltgtfyllmi algflaggvl qlagfaphaq fgaaaavaiv
       61 amivlrrsgl grkqkrdtst npdvnldigs tvtvdawrdg rarvqyrgad wdvelahger
      121 ddahvyqvsa vrgnclvvva kpag
//
LOCUS       WP_175881207             311 aa            linear   BCT 11-JAN-2025
DEFINITION  SPFH domain-containing protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175881207
VERSION     WP_175881207.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..311
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33418
     Region          2..284
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 mdsliiwvvl lviaivivsk tvkivpqqha wvlerfgryh atlspglniv lpfvdriayr
       61 hvlkeipldv psqvcitrdn tqlqvdgvly fqvmdpmkas ygssnfvlai tqlsqtmlrs
      121 vigkleldkt feerdfinhs ivsalddaaa nwgvkvlrye ikdltppkei lhamqaqita
      181 erekraliaa segrkqeqin lasgareaai qksegerqaa inqaqgeaaa ilavaeanaq
      241 aiqkiasaiq sqggmdavnl kvaeqyvgaf anlakqgntl ivpsnlsdlg taissaltiv
      301 ksagvgsgak g
//
LOCUS       WP_175881249             840 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia sp. BCC0044].
ACCESSION   WP_175881249
VERSION     WP_175881249.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 840)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 840)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..840
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..840
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=91254
     Region          62..778
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mpiikrppss sdrnephytl rrspsgayyp ddddrddgrr aqqrsggggg rrrtfgsrva
       61 lwfvglfatl avvgalivgy alvvmapqlp sldalthyqp kvplrvftad hvligefgee
      121 rrslvrfqdi pdvmkkavla iedyrfyehg gvdflgilra gvadlmhgga rqgastitmq
      181 varnfflsse ktytrkiyem llaykiekal tkdqilelym nqiylgqrsy gfaaaarvyf
      241 gkdlkditla eaamlaglpk apsaynpvvn pkrakvrqey ilkrmldigy itqpqydeai
      301 keeihvrtpg nqyavhgeyv aemvrqmmye qykdetytrg ltvtttinsa dqeaayqavr
      361 rgildyerrh gyrgpeasin lpaagderde aiddaladhp dngdlqsavv lsaspnavev
      421 qfvggattti gpaglrfvsa algarannal rikpgsvvrv lkdgktgwqv vqlpqvegal
      481 vaiapqdgai rslvggfdfn kskfnhvtqa wrqpgssfkp fiysasldkg mgpatminda
      541 plyfppsvpg gtawepkddd qpdgpmtmrt glqrsknlvs irilasigtq yaqqyvtqrf
      601 gfdpaktppy lpmalgaglv tplqlatgya vfanggykvd pyliaevdda rgqplqksqp
      661 vvaggtaprt iegrnayvmn sllhsvatag tgagtnalgr ndlqgktgtt ndakdgwfag
      721 yqqslvavaw mgfdqpkslg srefgaqlal piwvnymrta lngvpeqqmp mpdglttidg
      781 elyyadrtpg ngfvanvdin paenaisand algsagaagl apppvtpqek qqimdmfenk
//
LOCUS       WP_175881293             391 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Burkholderia sp. BCC0044].
ACCESSION   WP_175881293
VERSION     WP_175881293.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 391)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..391
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41718
     Region          4..386
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 mtalktlaia nyrslreliv plaalnvvtg pngsgkssvy ralrlladta qgrvipslar
       61 egglpstlwa gperfsraml agdvpvtgtv rkgpvslklg facddfgysi dlglplpsns
      121 qfaldpvvkr eciwggallr pstllvdrqg aqirartasg dwqtipqpva sfdsmmtefa
      181 dptgapemia vrerirswrf ydhfrtdaqa parqshigth tpvladdgad laaalqtire
      241 igdaaaldaa iddafpgasi eidnpggrgr fdvlmrqpgl lrplaaaels dgtlryllla
      301 aalltprppa lmvlnepets lhpdllpalg rliaqaarrs qvlvvshaar liatlereag
      361 ceslvldkql gatalvdads rdlpawkwps r
//
LOCUS       WP_175881303             336 aa            linear   BCT 11-JAN-2025
DEFINITION  inorganic phosphate transporter [Burkholderia sp. BCC0044].
ACCESSION   WP_175881303
VERSION     WP_175881303.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..336
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=35434
     Region          6..336
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 mhsiqlalwm vatlvlvalv fdfmngfhda ansiatvvst gvlkpqqavv faaafnviay
       61 fifhlkvaqt vgkgtidpei vdhyvvfgal vgaigwnvit wyygipssss haligglvga
      121 alaksgwsal nidgllktia fifispllgf ilgslfmlgv swlyfrtaps kvdrrfrrlq
      181 llsaglyslg hggndaqkti giiwmllias gyasasadap pawvigacyl smglgtlfgg
      241 wrivrtmgqk itklkpvggf caesggaitl fiasflgipv stthtitgai vgvgatqkls
      301 avrwgvagni vwawvltlpa aalfaaggww igrqif
//
LOCUS       WP_175881309             558 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 39 protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175881309
VERSION     WP_175881309.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14304616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..558
                     /product="glycosyltransferase family 39 protein"
                     /calculated_mol_wt=62369
     Region          24..375
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
     Region          450..555
                     /region_name="Arnt_C"
                     /note="Aminoarabinose transferase C-terminal domain;
                     pfam18583"
                     /db_xref="CDD:465810"
ORIGIN      
        1 mndtpsrlpl nritlvlllv alaivwfapl glrhlipsde gryaemarem fvtgdwitpr
       61 yngykyfekp plqtwlnalt fawfglgewq arlytavasf agvllvgytg arlfnplsgf
      121 laavvlasap ywnlmghfna ldmglafwma aslcslllaq rpglrpaavr gwmwacwaam
      181 alavlskglv glilpgavlv lytliardwa lwkrlylvsg lviffaivtp wfvlvqqrnp
      241 effnfffvvq qfrryltpeq nrpgplyyfv pvllvgflpw lsvawqsirh alrmprqpng
      301 fspmlvlliw safiflffsa shsklisyvl pvapalalii gaylplmtad rfrrhllgyl
      361 vffvaaafgi iflayqgdar tpnalyrafq mwlyaglavs aaltlaaawl nrragvaaal
      421 aafgaawlaf gtiggtghde fgryssgall apavraelak lpantpfysi emldhtfpfy
      481 mghttimvqr qdelafgisv epnkwvptvg ewitrwkqdt halaimppgq ydalvkegvp
      541 mrviardnrr vivekpqs
//
LOCUS       WP_175881389             294 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia sp. BCC0044].
ACCESSION   WP_175881389
VERSION     WP_175881389.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..294
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31902
     Region          <9..294
                     /region_name="bifunc_ST_SDO"
                     /note="bifunctional sulfur transferase/dioxygenase Blh;
                     NF040641"
                     /db_xref="CDD:468609"
ORIGIN      
        1 msnapalsve gffdpathtv syllldptsr acalidsvld ydpksgrtrt asadrliarv
       61 aelgatvhwl lethvhadhl saapylkaqv ggqiaigshv rrvqhvfgtl fnagpgfaed
      121 grqfdrlvdd gdtlplgalt iralhtpght pacmtycvdd atqraafvgd tlfmpdygta
      181 rcdfpggdar tlyrsiarvl alppdtrlyl chdyqpggrd vqfvttvaeq rranvhvkdg
      241 vteddfvamr tardatldmp vlmlpsvqvn mraghlpepe nngvrylkip ldai
//
LOCUS       WP_175881402             330 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Burkholderia sp. BCC0044].
ACCESSION   WP_175881402
VERSION     WP_175881402.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..330
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34842
     Region          6..301
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(37..38,41,93,108,110,139,172,261,264,300)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(230,235,251,261..263,266,288,292)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mkaaldvvty geamamfvat epghlahagq fakriagadl nvaiglsrlg frvgwmsrvg
       61 rdsfgryvld tlaregidas cvtvdprypt gfqlksrndd gsdptveyfr kgsaashlsc
      121 ddyvadyvlg arhlhltgva paisatscel afrlaremra agktisfdpn lrptlwpsad
      181 vmantlnala aladwvlpgl aegrqltghd tpadiagfyl aqgargvvik lgeqgayfrt
      241 adgregtvag ervekvvdtv gagdgfavgv vsallegrsv eqavargnri galaiqvigd
      301 seglptrdal drlekvsnha drleetvtaq
//
LOCUS       WP_175881412             299 aa            linear   BCT 11-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175881412
VERSION     WP_175881412.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..299
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31160
     Region          73..279
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mtkrslaala asllmsvtai dglvapqlay aqasgstats dastqaaapt paaaepappp
       61 apaateaven pyglgalwkn gdfvarfvli llvimsmgsw yimitkfveq lranrrakla
      121 daqlwsapsl aegaklldea spfrfiaeta ieagehhdea lleavdrntw idvsversit
      181 nvsnrmqdgl aflatvgsta pfvglfgtvw giyhaltaig iagqasidkv agpvgealim
      241 taiglavavp avlgynflvr rnksvmervr nfgaqlhtvl lagskrparv psaaaslvn
//
LOCUS       WP_175881421             380 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175881421
VERSION     WP_175881421.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..380
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40821
     Region          1..380
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mpfdwtqeqh atlarfrdig agiaaaverd grapagfdea gwtrlghegl wdmivpetyg
       61 gdghgwwhfs aaleglassi rrpalllsvi aqagmvrale rygtaaqqdr yfgailrgel
      121 sataiaepgt gtdvrsiatt laehgdgyrl tgskfniaha plarfilvvt rietpgrrnt
      181 alvivdrdqp gmtvappdrk lglddlptga lhfddcpiar gqllgepgag lgnlidiisl
      241 grlyyglvaa qvtapylrda igycrerrsf dstidahqyv qrrlvdlqig mergtwlarg
      301 alaqlltdhp qalmtcsiak lvgaqdlvdg alglvrlygs lgyqagpvaa fasdalgfms
      361 vggteemhrk nifnqmmrag
//
LOCUS       WP_175881441             123 aa            linear   BCT 11-JAN-2025
DEFINITION  GFA family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175881441
VERSION     WP_175881441.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..123
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13145
     Region          6..109
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 msatcfkgsc hcgavkfevt aaitpavrcn cslcrrrgal mspmfaaanl tivegegvlt
       61 cyrfnthtar hyfcsrcgvy pfhqtrkdpa cwrvnlgcld gvdpyaldat vadgaslsvv
      121 eda
//
LOCUS       WP_175881449             307 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0044].
ACCESSION   WP_175881449
VERSION     WP_175881449.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..307
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33696
     Region          38..293
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 matdnhaart wppkpdapdt rpvdarkphr mksnlagraw kalvwglmaf fllnvmllia
       61 tvavnsvatr wfgtplpqgf tlhwyakawe dfqlasvlwv tvevvgavvl lsialgvpaa
      121 yalarvqfrg krfallvfll plmvppvtyg ipmatvmyki glagtlpgvi lanlvpalpf
      181 vilvmtpfie qidpnlesaa rifgantwry fryvllpllv pgmlaagllv lvrtigmfel
      241 tfftagpstq tlvvalyyav fstgvrapqs idamamiyma itlvwvvial qfvsptqlvs
      301 rvkqerq
//
LOCUS       WP_175881495             282 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175881495
VERSION     WP_175881495.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..282
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29946
     Region          7..260
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtrrtaalaa rglsvgyrdh vvidgldlsi aagrvtalcg pngcgkstll rtlaglqpvr
       61 aghvdvngkp lasfrrrala reltmlaqfn qipsgltvre lvaygryayg gflrglsrad
      121 haaidealdt sgladdaerd vgalsggerq rawiamalaq qapivlldep ttyldihhql
      181 dildalraln rtrgltivwv lhdlnqaaay sdeivlmrag rlvaqgtpda mleparlraa
      241 fgvemlklah pqtgapmcvp aygpstdgap qvagvfdrdl av
//
LOCUS       WP_175881505             420 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia sp. BCC0044].
ACCESSION   WP_175881505
VERSION     WP_175881505.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..420
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44392
     Region          184..355
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mvksvatpda vapgraqrav ralvpaavlg alaafglaaa lpavsqlpga vdsgtaalpq
       61 rvlsdtpfpt aqhfvtsela rtigernehv drslqpglfa plsahrndml gyaslfqfas
      121 perqqgmrag dieltlsdtl nrldvppevr iqlgdlvtgk vamrasaqrg dyyrvafdtn
      181 dgsprltale lrvagrtfga iwfrapgaah gayyaldgsp leaaaftmpv kwtrissffg
      241 erihplsqam afhtgvdlaa psgtpvdaaa dgvvsfvgtd pggygryviv dhadgystyy
      301 ahlsafargl ktgetvkqgq rigsvgmtga atgphlhfev rvandpvdpl vtlasaqtal
      361 sdmqltafrq eaaqwrlrla sisttpfafa qndgplwgdf atgpstlrav fdthysaers
//
LOCUS       WP_175881591             326 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175881591
VERSION     WP_175881591.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..326
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=35346
     Region          140..324
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mssatllalm falicaaagl llwrgsqvre grahaqrffd srlgqgarpt apaadtrpar
       61 spaagtanaq epeqgfarwr asafdawavl sdragldear pglvlalavv vllalwagma
      121 ggvlaaaaav vagsvlvvlw itsrisrrrl kivrqlpsfl dgivrlvtlg nsvpaafqsa
      181 lqtaemplrr clddvsqmlr sgveidraml hiahtyrire felvgavlrl svryggradv
      241 mldrmstfmr dleqaerels amsaetrlsa wvlallpiav gsfviatspr yftamwndda
      301 grqlvylafa lqaiggfwlf rlarlr
//
LOCUS       WP_175881592             448 aa            linear   BCT 11-JAN-2025
DEFINITION  CpaF family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175881592
VERSION     WP_175881592.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..448
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49188
     Region          44..412
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mahdiqfadg aapfsqtqqf hdiknaaheh lltrieelga efgrwsrqai nqfvdleids
       61 fvrlrripln esevravaea ltkelagfgp iedlladphv edilingynd iyvsrhgils
      121 klpirftdna hllrivrril apvgrrldes npmvdarlpd ggrvnvviep lsidgpvvsi
      181 rkfrkdplkp edllgngtyn eeigrlleaa vdarcnvlvs ggtssgktsl lnalafhipm
      241 aervvtiedt aelslnhphv vrlesrpggf dgsgivsird llrntlrmrp driivgevrg
      301 gevlemlqam ntghdgsmgt vhassprecl yrlemlagfa gfqgteaslr rqianaidfi
      361 vqigrlsngr rrilsitevt gmsdnivstq elyryearvt pegeeidhwe slgihphspk
      421 larfrstlva sggggfggnf grgggfnv
//
LOCUS       WP_175881623             138 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175881623
VERSION     WP_175881623.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..138
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15467
     Region          19..107
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(20..22,36,53..55)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mtttvekvvl ppipakryft igevselcgv kphvlryweq eftqlrpvkr rgnrryyqhh
       61 evllirrire llyeqgftin garnrldspg seraaaaepv esgaqavdar gavrpganvd
      121 vialrqalld vidglkhd
//
LOCUS       WP_175881638             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175881638
VERSION     WP_175881638.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34546
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdtlqnmrvf vrvvdagsft aaaqqmnstt ayasravsdl eahlrtrlln rttrrialte
       61 agerylqrce qilayvdqae aeagdaharp sgklkvhcft slgqhylvpa iaryrerypd
      121 vhveltlaqr mpdlldegyd vaivvgrdlp dsglvsqrlg esysvvcasp gyieshgvpq
      181 rpadlaqhvc lgmvapgfhf dewalagpng nevvpitapp frvnvaeala vavregmgvg
      241 glplysaigw lrsghivrvm peyrshvmni yalypsrqyl dakirtwvdf lreelpltle
      301 adeaaleqft rat
//
LOCUS       WP_175881693             293 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175881693
VERSION     WP_175881693.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..293
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31207
     Region          12..270
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 msasiktllt presdignlv vrrvlparaa rlvgpfiffd emgpavlpag rgidvlphph
       61 iglatvtylf dgslmhhdsl gfrqkivpgd vnwmtagrgi vhserspded rpheqpvhgi
      121 qtwvalpveh edtapafvhh aadtlpsftr dgvtvrviag tafglaspva vfsptlyava
      181 efaaggtlal daeheergvy lvdgdlsvdg tplapatmav lepgasvala stngarvmll
      241 ggahlpgerf iewnfvsser akidaaraaw adqtfgkvpg eegewtrqpe rra
//
LOCUS       WP_175881750             240 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175881750
VERSION     WP_175881750.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..240
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25665
     Region          2..226
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mslvtvehls ktylldsvrv tgladvsatl dagrftvlsg psgsgkttll nmigcidrpd
       61 sgrvtiagqd taslsddals dfrarhvghv fqtfnllpvl sayenveypl lmagwasarr
      121 aarvrdllda vgladkarhr psqlsggqrq rvaiaralaa epamvladep tanldsatgh
      181 aiielmraiq rerdvsiivs shdpqvvrva devirildgr ivghergrer gdaaaqeacr
//
LOCUS       WP_175881737             183 aa            linear   BCT 11-JAN-2025
DEFINITION  PadR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175881737
VERSION     WP_175881737.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 183)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..183
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20936
     Region          1..86
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          91..179
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 mslphallta laerpgsgse ladrfdrsig yfwqathqqi yrelgrledm gwieslpaes
       61 grgrkrayri lpagkkelrr wiaepedptp lrealmvrlr aeavlgpagl edeikrrial
      121 hqekldlylq ieardfsadd dsadddsrrk rlqhlvlqag ianerfwvef sqhaldtlrl
      181 pkd
//
LOCUS       WP_175881720             141 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175881720
VERSION     WP_175881720.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..141
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15668
     Region          1..141
                     /region_name="COG3565"
                     /note="Predicted dioxygenase of extradiol dioxygenase
                     family [General function prediction only]"
                     /db_xref="CDD:442786"
ORIGIN      
        1 mslspfhlai pvydlpaard fygrvfglae grssaqwvdf dfyghqlvih ehpktasqeg
       61 ahtnavdghd vpvphfgivl dwaswealae rlrgfgvtfv iepyvrfqgq vgeqatmflf
      121 dpcgnalefk afrdigqlfa k
//
LOCUS       WP_175881755             475 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175881755
VERSION     WP_175881755.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..475
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50736
     Region          61..468
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mtralaivla avacaafasp araqlldvyr trddvaatqg gsmasatacg aphvdgrpla
       61 ledailqaic shpqltrtws daraataevg vakaaywptl natagiqrdn lttdynggfs
      121 qnqrsssryg mlnlswvlfd fgkrganldr arallraana ahddtlqsvf fdaaqafyal
      181 rdaqaaleaa qaveraaqes laeatarhdg gagtlgdalq aqttyrkall drvsaegdlq
      241 naigtlattl gvdadtplri adaepspdrd dftrgvadli aeakrhhpkl iaarekldaa
      301 rdqvravraq tlptisltgs lsrnnpsyqq qpsflqiqss hgnsigiqvs iplfegfasg
      361 yrvaeakaqa daqeadvrst elkvsldvwk syqslqtdtt nldnsqhlld talhsldiar
      421 grykagvgtf tellnaqsal adarrqrvla vskwrtarlk laeslgrlgl wndas
//
LOCUS       WP_175881805             136 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175881805
VERSION     WP_175881805.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..136
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=14787
     Region          32..134
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mntnptlaer hpstvhaaaa eaarrpaitp svdivedarg vtlradlpgv prdnldvkvh
       61 dntltieast hidtpadlrv rhaeirstry arsfvlsadl dtsridanlr dgvltltipr
      121 reetrprrid vtagna
//
LOCUS       WP_175881766             712 aa            linear   BCT 11-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175881766
VERSION     WP_175881766.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..712
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=75784
     Region          378..630
                     /region_name="CE4_u2"
                     /note="Putative catalytic domain of uncharacterized
                     bacterial proteins from the carbohydrate esterase 4
                     superfamily; cd10926"
                     /db_xref="CDD:200552"
     Site            order(389..390,457,462,502..504,596)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:200552"
ORIGIN      
        1 mlaksgkflr ilfalfalaf afspggvqaa tnqllllvpd tltlpdsrvs awldsaqeeg
       61 lqitvmtdsq fmaagaslsq ypglilpdqv httasdtlvt aiqnyalngg kvmlvydfgv
      121 lnsagfyvsp ksrfssmagv dyvlydqygg nmiglgnvtg msswlrtlqv ppgksmawst
      181 tssttttasa laststsgas tnassgsaqf laaspsnpgg lanynhdawf kyttpptgsg
      241 vlnqtapklt gtvtgklkkt taytanslls tstgktantl astlatttdt legisgyvyg
      301 fltypsfvtq gtytgttilt sptfglvsgy ntygnggvlf vnlplayldg qtdgmlihgy
      361 lhyfgtqmln lpslsalpka maglvfnwhf cagdqiqpal qlknlgvwnn gpfslvitag
      421 pdeatfgdgn ginlannpta qnlvkyfltk ghrvgshggw ihdywganas etnastftqy
      481 lvmnhqavqa atgqpdveya apegntptws vnwlesngfn gyyftghtgs aptrayrnga
      541 llnpglwayp vmpfgkyatf eefqqyavpt advnnwyasl mnfvvanrts rliyahplga
      601 ssytstlsai fsqantlklt gqfkwytmsd ittfdrarln vtwsatdtgs gwtfaashpt
      661 slanmtwllp kkgfampvit qgfgsvgitd stywlvtans gtslkftsak vh
//
LOCUS       WP_175881840             455 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia sp. BCC0044].
ACCESSION   WP_175881840
VERSION     WP_175881840.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..455
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48480
     Region          2..449
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mknlqrhlsa rhirflalgs aigtglfygs asaiqlagpa vilayllgga avymvmralg
       61 emavrepvag sfghyatenl gpfagfvtgw tytlemviva iaditafgiy mgfwfpdvpq
      121 wiwvlgvvai icglnlchvk vfgelefwls iikvgaivam igggvaillt gmrfghsadv
      181 ptfanlwnhg gflpngvggl iaslsvvifa yggievigms ageakdperv iprainavpa
      241 rillfyvltm vvlmsispwt gvgsdgspfv qifsalgvks aatilnlvvi saaisainsd
      301 ifgagrmmfg marqgqaprv ltttsrhgvp wvtvlvmaga llvgvllnyl mpkdvflvva
      361 aiatfatvwv wlmillsqva mrrrlsraev aalkfkvplw pvapaltiaf mgfvivmlgw
      421 fedtrvalyv gaawlallaa vfyarirpkf aaasr
//
LOCUS       WP_175881886             288 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175881886
VERSION     WP_175881886.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..288
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30514
     Region          12..278
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mkkiqgvysa prghwvgdgf pvrsmfsyqs hgthlspfll ldyagpatfe ptsaprgvgq
       61 hphrgfetvt ivydgevahr dstgaggtig pgdvqwmtaa sgilheefhs eaftkqggal
      121 emvqlwvnlp aadkmgapgy qtllnadipv velpdgagra riiageldgr rgparthtpi
      181 dvwdvrlvag gharfpvaeg rtlavvvlsg tvlvngetva reaqfvqlgr dgsdveiean
      241 gdakllilsg epidepvvgy gpfvmnsqae irtaiedfng grfgqmpa
//
LOCUS       WP_175881978             226 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175881978
VERSION     WP_175881978.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..226
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24814
     Region          10..225
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mstvtdipre raaaspasla erayaliqrd iitmrlkpga alneadlvar tgigrtpvhq
       61 avhrlvlegl lsvmprkglm vqplslddiv avidvrrine ahcaelaarh atpddlarla
      121 allddgqacv dthdvegmme ldrafhqtia saarnavlad ilralhersl rfwfvtlsep
      181 hhladvqheh relferlsar daagaraave shidsfrstl lqhlrp
//
LOCUS       WP_175882014             372 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175882014
VERSION     WP_175882014.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 372)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..372
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40424
     Region          1..371
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 maslsirdvy ktypngvpvl kgvdieiedg qflilvggsg cgkstllnmi agletvtsge
       61 icidgkvvnn lspkdrdiam vfqsyalyps mtvrenisfg lnirkvpkse qqqivdrvss
      121 mlqiqhlldr kpgqlsggqr qrvamgrala rdpslflfde plsnldaklr iemraeikll
      181 hqrlgttivy vthdqieamt lgdriavmkd gvvqqfgapq eiydspsnlf vagfigappm
      241 nfingklveq gsgialeidt glarsalnlp fdaaklkshv grevilglrp eritdarnah
      301 ngeasnlqpi dvrvdvtept gpdthvfaqv ngkrivsrvh paanpqpgqt qsllfdvska
      361 vlfdpaseer ia
//
LOCUS       WP_175882106             262 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175882106
VERSION     WP_175882106.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..262
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26751
     Region          8..261
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mslphidlly slsglfvgil vgltgvgggs lmtpilvllf gvhpatavgt dllyaaatka
       61 tgtlvhglkg sidwritgrl aagsvpaaal tlwwlhthgm ntpgtarmiq lvlgvalllt
      121 slalifrpql tafaarnpla pspartlwst vltgavlgvl vsmtsvgaga igvtvlllly
      181 pllatarivg sdiahavplt lvagmghwll gsvdwsmlls lllgslpgiv igsllsarap
      241 erllrnllas tlvavgvrlv la
//
LOCUS       WP_175881938             419 aa            linear   BCT 11-JAN-2025
DEFINITION  M48 family metallopeptidase [Burkholderia sp. BCC0044].
ACCESSION   WP_175881938
VERSION     WP_175881938.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Bode,W., Grams,F., Reinemer,P., Gomis-Ruth,F.X., Baumann,U.,
            McKay,D.B. and Stocker,W.
  TITLE     The metzincin-superfamily of zinc-peptidases
  JOURNAL   Adv Exp Med Biol 389, 1-11 (1996)
   PUBMED   8860988
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Stocker,W. and Bode,W.
  TITLE     Structural features of a superfamily of zinc-endopeptidases: the
            metzincins
  JOURNAL   Curr Opin Struct Biol 5 (3), 383-390 (1995)
   PUBMED   7583637
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..419
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46677
     Region          8..415
                     /region_name="M48A_Zmpste24p_like"
                     /note="Peptidase M48 subfamily A, a type 1 CaaX
                     endopeptidase; cd07343"
                     /db_xref="CDD:320702"
     Site            order(279..280,283,361,365,405)
                     /site_type="active"
                     /db_xref="CDD:320702"
     Site            order(279,283,361,405)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320702"
ORIGIN      
        1 mspfsftllf aiavlamvvt klwlasrqir fvaahrngvp aqfsatiplt ahqraadytv
       61 ertrltmlei vvsaavlvgl tllggvgald tlltgwlgrg ygqqvalvaa vlvitgvidv
      121 pfeyyrqfgi eqrfgfnrmt krlfftdmlk ntllgavlgl pllfvvlwlm nqagslwwlw
      181 twivwvafqm lvlliyptfi apifnkfepl kdealrsrie slmkrcgfaa kglfvmdgsr
      241 rsahgnayft gfgaskrivf fdtllarlsg qeieavlahe lghfkrrhvm krmlvsfvls
      301 lvllallgwl aqrtwfytgl gvtpsldtsn agaalilffl aipvflffat pfssltsrkh
      361 efeadafaas qtdaqdlvsa lvklyednas tltpdpvyta fyyshppasq ridrllqha
//
LOCUS       WP_175882110             212 aa            linear   BCT 11-JAN-2025
DEFINITION  2-hydroxychromene-2-carboxylate isomerase [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175882110
VERSION     WP_175882110.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Thompson,L.C., Ladner,J.E., Codreanu,S.G., Harp,J., Gilliland,G.L.
            and Armstrong,R.N.
  TITLE     2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class
            glutathione transferase from Pseudomonas putida
  JOURNAL   Biochemistry 46 (23), 6710-6722 (2007)
   PUBMED   17508726
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122490
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..212
                     /product="2-hydroxychromene-2-carboxylate isomerase"
                     /EC_number="5.99.1.4"
                     /GO_function="GO:0018845 - 2-hydroxychromene-2-carboxylate
                     isomerase activity [Evidence IEA]"
                     /GO_function="GO:0043295 - glutathione binding [Evidence
                     IEA]"
                     /GO_process="GO:1901170 - naphthalene catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24002
     Region          12..191
                     /region_name="DsbA_HCCA_Iso"
                     /note="DsbA family, 2-hydroxychromene-2-carboxylate (HCCA)
                     isomerase subfamily; HCCA isomerase is a glutathione (GSH)
                     dependent enzyme involved in the naphthalene catabolic
                     pathway. It converts HCCA, a hemiketal formed
                     spontaneously after ring cleavage of 1; cd03022"
                     /db_xref="CDD:239320"
     Site            18
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239320"
ORIGIN      
        1 mttgldtaqp awffdfvspf syllleqhdk wpdvpfvpvp aslsdlqrhw gqrptadvpa
       61 krvftyrhal fraeqlgirf kmppahpfds dkvlrlaial radivtvlem frfiwregnd
      121 pstpegfaal cervgvshgd eliefeetaa qlarntadai algvfgvptf wmnqqlfwge
      181 dalpmvlyca rtpnwlesre vkristlpkg ra
//
LOCUS       WP_175882201             319 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: hydrogen peroxide-inducible genes activator
            [Burkholderia].
ACCESSION   WP_175882201
VERSION     WP_175882201.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Jo,I., Chung,I.Y., Bae,H.W., Kim,J.S., Song,S., Cho,Y.H. and
            Ha,N.C.
  TITLE     Structural details of the OxyR peroxide-sensing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 112 (20), 6443-6448 (2015)
   PUBMED   25931525
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444038
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..319
                     /product="hydrogen peroxide-inducible genes activator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35216
     Region          3..61
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..301
                     /region_name="PBP2_OxyR"
                     /note="The C-terminal substrate-binding domain of the
                     LysR-type transcriptional regulator OxyR, a member of the
                     type 2 periplasmic binding fold protein superfamily;
                     cd08411"
                     /db_xref="CDD:176103"
     Site            order(103,106..107,110,114,122..126,225,228..229,232,
                     235..236,238..239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176103"
ORIGIN      
        1 mtltelkyiv avarerhfgr aaeacfvsqp tlsvaikkle delnvqifer gasevsvtpi
       61 gdqivtqaqr vleqtfaike iakqgkdplv gpfrlgviyt igpyllptlv kqmiqrvpqm
      121 plmlqenytl kllellkqge idaaimalpf petglmvrpl ydepfvvalp aghpwekrde
      181 idaedlkqet mlllgnghcf rdhvlgvcpe lmrfsqtadg iqktfegssl etirhmvasg
      241 vgitvlprms vaevgprang pdaellsyvp fnepvpdrrv vlvwrksftr mpaidaisda
      301 itacelpgva kldmpatmn
//
LOCUS       WP_175882155             215 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175882155
VERSION     WP_175882155.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..215
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24309
     Region          1..213
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 mielddvrky ystrngqrlv ldgvnltinp gerigilgrn gagkstiirl isgselpssg
       61 risrsmsvsw plafsggfqg sltgldnlrf vcriyqasfe nalpfveefs elgeylrepv
      121 kkyssgmrar lafaismave fdcflidevi avgdrrfhek ckyelferrk dramilvshd
      181 aitvkeycdr acvleggrlh hfddvedayd fynhi
//
LOCUS       WP_175882219             134 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175882219
VERSION     WP_175882219.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..134
                     /product="VOC family protein"
                     /calculated_mol_wt=14183
     Region          13..132
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 mtsatatatp eraiawfdip sldfdrairf yetvlqttlq raviggvpma tfdrdasstg
       61 gsivfdpqqi kpsangvlvy lnagesvvaa lervkraggv vqgsvvelpn nygyvgylid
      121 tegnrvglha pkch
//
LOCUS       WP_175882246             215 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175882246
VERSION     WP_175882246.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..215
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22646
     Region          14..129
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          80..209
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mkdkpaqgpr gldkdaivaa alalledvge aafsvrklaq svgcdpmsvl yhfkskdgls
       61 raianalsrs lvpvdpslpw rerlrdlarq yralalrypa afallqrhms tgpadlahie
      121 avhraltdag ipraalpsvc vgwyasvigl aaaeaggltr aandvelaem halsdaahpl
      181 vksaaplyaq ldpavvhdtm ldvlldgiaq rahta
//
LOCUS       WP_175882277             299 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175882277
VERSION     WP_175882277.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..299
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32141
     Region          41..290
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mtkmpdsltl darrampadt sltdsigats tpldlaaqqa gtqtllrgla ileaiangar
       61 dmraigaalg ttrstthrlv sslvqarylr qvqggyllgp klielgtial eqmpltavar
      121 phlealaeat ldtihlgvrd gddvlyidki pgtrglemrs rvghrmplas tgigkammld
      181 ldpdlwrslf eaarralagv nfkpdnrpet saflqrmahy aaggytfdle eneasircva
      241 apirdasgai vaavsvasti pymphdrmde liplvqrear aisaelgwsp pqgtrrikr
//
LOCUS       WP_175882339             338 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia sp. BCC0044].
ACCESSION   WP_175882339
VERSION     WP_175882339.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..338
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37733
     Region          171..316
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mqdtltkpag aadavegeva valdgaahgq aaavvehald awrpddapda llatfvalfn
       61 tdtrydaati tvplggadat avasyvarav regvidgaqv agdtlrltvs rttfwqnprp
      121 wlkapasggm plrytitngh rhpvrppspa geiyarampq vgmtfslrtv didahadlfs
      181 gwmnldrvah fwdqrgtrde haaylaerla dphmhpmigy fddtpfgyfe fywakedrla
      241 pfydahdydr glhlligdsr fqsagklhaw wsgvlhymfv deprtqrlvg eprvdhvrhi
      301 aymhrlgfyt lkefdfphkr aaltvierdt ffdtfrlp
//
LOCUS       WP_175882358             274 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia].
ACCESSION   WP_175882358
VERSION     WP_175882358.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 274)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 274)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..274
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30612
     Region          13..274
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mqsfslsprs laaslvknrr lmldlarrda vgrykgsflg ifwslltplm mlsvytfvfs
       61 evfksrwnda shaaskgefa vvlfagmivf nlfsecinra pgqilshsnf vkkivfplei
      121 lpcvtllsal fhlsvsvcil lvaewfivgs vpltallfpv vlaplcvfim gvswilsatg
      181 vylrdigqtv givitammfl spvffpvssl peqfrgfvyl npmtypieqg rdvliwghmi
      241 dwsrwsvysl mavavawigf awfqktrrgf advi
//
LOCUS       WP_175882373             677 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Burkholderia sp. BCC0044].
ACCESSION   WP_175882373
VERSION     WP_175882373.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 677)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 677)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..677
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=72939
     Region          2..663
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mrddveqaag sraahpagwp apaiqkaher setfglqvsa rpdydvlpss alvlkreqsr
       61 vlcvhampvm etlheqivnt qsmivltdae glilhsigdd dflrraekva lrpganwaen
      121 rqgtnaigta laelcpmvvh gdqhflaanr fltcssvpil dpygdaigvl dvtgdhrsyh
      181 qhtmalakms vqmienhlft ttfqetlqvs fhgrpeflgt lmegivafta dgrflsanrs
      241 aqfqlgmpla alrahtlssl fdvtsaqlid rmrastdrhl mlnlgngavv carvhfrrat
      301 laegsrptdv hdagapaara navpapaagt saglsrlnyl dtgdaqvacv iakvrkvigk
      361 dipilitget gtgkellaqa ihndsprrda pfvavncasi petlieself gyeegaftga
      421 rrkgaigkll qanggtlfld eigdmpyplq vrllrvlqer lvnplgstkt iavdiaiica
      481 thrdlrdmia qnrfredlyy rlnglvvrlp plrdrtdlav vvqkmlqrea fagpgrppls
      541 vapdvmelfv rctwpgnfrq lgnllrtaaa mvdddgeirr ehlpddffdd lrrgdaqatq
      601 vmpdsaasag agpgvadall padarlqdva asaiaaalar hggnvsaaar algvsrntiy
      661 rkmpaadaar hpssded
//
LOCUS       WP_175882384              98 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175882384
VERSION     WP_175882384.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 98)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002085
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..98
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10297
     Region          1..98
                     /region_name="ManC"
                     /note="Mannose-6-phosphate isomerase, cupin superfamily
                     [Carbohydrate transport and metabolism]; COG0662"
                     /db_xref="CDD:440426"
ORIGIN      
        1 mslidfksva naqaiawkst ivgevgpari kvlrmdaqpy eaevhdyneg llvldgtlml
       61 evdaetvvvg agqmylahag trhavlpgsh gtlaiidv
//
LOCUS       WP_175882462             706 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175882462
VERSION     WP_175882462.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..706
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=77107
     Region          86..>677
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msfapnggip sglgggalgs lsalgglagp vassvagslg plaglaghvd tvqramqlaq
       61 tgfslmdktp gaiaeainga anparltqln ryvtldtplg pdvllvsaav vdecvnrlpe
      121 ihldllshrh dlrpedligq qvkirfdqqa rlstlervva sgtgdndryf dgyvasfdra
      181 gnpgnvtqyh ltavpwfwfl trstdcrifq nktaqdilte ifqehgfsdf tfdirtsqkp
      241 leyvvmyqes yynfcarlme qeglvwthry ekdkhflvig dtnllfrpid glasvpfaat
      301 easedsgidq lhegrrfgvg kvtfrdfnhq npssplmlve agpqnlkhar ldaterfehq
      361 slydhgddgn ryarfameae eaqahrytgg gyawrmttag avavanhpvl ennqeyvilh
      421 vrheavndyt qhsaklpyrn sfsllpkkip yrapratpkp vihgtqsaiv vgpkgeeiyt
      481 ngsavkvhfp wdrrgkkdgs dsmwvrvsqp wagdgwgaaa iprikqevlv afnqgdpdnp
      541 vivgrvfnge qgnpyhgaag qtmgiksqth kgqgsnellm sdvagaqmly mhaqkdmhtv
      601 vedaqwtqvl kgdrtvevgk gnhttavavg nlsdvvvqgn tlhqtpqgvh tveakelwik
      661 iggdggtrih mtadsidiyk gdsvihldds niniqaartd inpkng
//
LOCUS       WP_175882482             249 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia sp. BCC0044].
ACCESSION   WP_175882482
VERSION     WP_175882482.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..249
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25953
     Region          2..236
                     /region_name="17beta-HSD-like_SDR_c"
                     /note="17beta hydroxysteroid dehydrogenase-like, classical
                     (c) SDRs; cd05374"
                     /db_xref="CDD:187632"
     Site            order(8,10..13,33,51..53,75..78,98,125..127,140,144,173,
                     176..178)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187632"
     Site            order(99,127,140,144)
                     /site_type="active"
                     /db_xref="CDD:187632"
     Site            order(127..129,134,140,171..172,179,194,197)
                     /site_type="other"
                     /note="steroid binding site"
                     /db_xref="CDD:187632"
ORIGIN      
        1 mktvlitgcs sgfgleiary flardwqvva tmrkstddvl ppsarlrvlp ldvtdadsir
       61 aaidaagpid vlvnnagfga aapaeltpld tvralfdtnt igtiavtqav lpqfrargag
      121 vvvnvtssvt lkalplvsay raskaavnay tesmaaelep fgvrahlvlp grapdtrfad
      181 nargnmhgfe heayadfvgk avarmldasg pithaqdvae avwraatdps spmripagad
      241 aqawaaeag
//
LOCUS       WP_175882481             325 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175882481
VERSION     WP_175882481.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 325)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 325)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..325
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35202
     Region          23..198
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          232..314
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 magavfatid nplffcespa midpltevvt llqpgaryak yvrgaspwai nrtvagepfy
       61 cavldggcri aidghapiel lagdfmlipa aygvamssle ppppgvdtap pvmlehgeyr
      121 igdpanpvdt rmmagncsfg spdaallvsl lprfvhvrge prlttlvqlv rdesraqrpa
      181 reivlarlle vllieamrft tgthaspglv rgladsrlaa alrrmherpa hpwtivelak
      241 eaalsrstff erfsravgva pmeylltwrm alakdllrrn egriaeiaar vgyssastfs
      301 vafarhvgrp paqyardeqa tvses
//
LOCUS       WP_175882494             631 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Burkholderia sp. BCC0044].
ACCESSION   WP_175882494
VERSION     WP_175882494.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..631
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=67401
     Region          8..631
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mpqpfvlpat agrtdllaqa harstavglr aherpdfapl srvalralld tnhtlfshar
       61 pvmedlhaqi aetqslvllt dadgvilhsi gdadfiekan rvalcngvsw aegargtnai
      121 gtalasgqav vvhgsehflr anhiltcaca pivdpfgrtl gtldvsgdpr gasphtlalv
      181 rmsaqlienh lfanqcgeal rlrfhahedc vdslfaglva fgpdggliaa nrsaqfqlga
      241 sfdalqhqas dalfgmrfgq laqqaarapg atfrltlstg vrvlarcefp eaqkttvavt
      301 ppapaarvra pdpdaitfat ldtgdarmaa vlervakirg rdlpllilgq tgtgkewlar
      361 alhqasprad gpfvavncaa lpdslieael fgyedgaftg arkrgspgki aqadggtlfl
      421 deigdmplaq qvrlmrvlqe ravmplggar avpvdvrvvc athrdlrami aegtfredlf
      481 yringlavtl palaartdlp alverilarl arsepmprrl aadvldafar hrwpgnlrqm
      541 tnvlrtagml aedeaeitla hlpddfwldc ddapampeaa tpagkregtt lqshqaamid
      601 avlarhggnv saaarelgla rntvyrylrr h
//
LOCUS       WP_175882511             512 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0044].
ACCESSION   WP_175882511
VERSION     WP_175882511.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..512
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52270
     Region          16..438
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,142,
                     145..146,149,273,276..277,280..282,285,313,317,371..372,
                     376,380,396,399..400,403..404,407)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtlsdsrrna valaavclts lmfgleissv pvilptlehv lhgdfngmqw imnaytiact
       61 tvlmaagtla drfgrkrvyv igtvlfgats llcglapnvp vlvagrllqg asggamlicq
      121 iavlshqfre grergrafgi wgmvfgiglg fgpivggaiv alaswpwvfl vhaplaaval
      181 vliggavqes rdphagtldv agivtlslav lglafyitqs aelgltsaag lgvlgatvla
      241 vigfviaera sarpmfdfsv friraftgai fgsmgmnfsf wpfmiylpiw fqvalgydsv
      301 taglallayt lptliappfg erlalrygpg vvipsglfti aagfvlmrlg saadpaswlt
      361 mlpgcviagv glgltntpvt ntttgavpsa ragmasgidm sarmislaln iatmgfvlva
      421 givaslkggp agaigdaalr rlaqeiasgr tdglqalapa laqadpsgaa lhaalvhgfg
      481 wvmvygaagv avlatasava faparrgatv ce
//
LOCUS       WP_175882550             245 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175882550
VERSION     WP_175882550.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..245
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=24917
     Region          1..245
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mlaliivagl waglqnalag ggsfvtlpal ivsgmsplaa nitstvalfp gqvttgwasr
       61 nmvsgvgrlp fralfaisva ggalggllll ktpssifshl vpwlvlfata vfawgsffrk
      121 pgagaqhlgp vaagvsqfli aiyggyfggg igflmmaalt maglpprham stknalagvm
      181 nasavllfvt sphlhwreai algggaivgg llgawalhrv nervlriaiv cigalltigl
      241 fvkpi
//
LOCUS       WP_175882519             467 aa            linear   BCT 11-JAN-2025
DEFINITION  HdeD family acid-resistance protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175882519
VERSION     WP_175882519.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..467
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=51439
     Region          10..185
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mvrlvllllg ieylrtrwrg ltvlgwlwvv agvgifvdal dgalhfpiel fawlfliegl
       61 atlavagsgv ggqrilryvk giavvvaagl vfaghhhghf llsmifgtlf lvdgllqcts
      121 awmvryrrwh vafawgvvei llaifffqpy pthyvgtvpy clglllmfgg mhmlslaarv
      181 rrltrnpafa tspapalapd lddapdlpqf tqsewdgppa dgeraltvhv wtptgtskae
      241 aqryplidry iaavdvngvi stghaalesp egiyislypg veidrspdef trilratren
      301 dvpglfqpdy atestawcps tvrvrirnyd pakldafwss yrqnttynlt hrncsstvsn
      361 aleaaldgav wrlkgaragw gafvrllltp elwvaaqirk ravtmawtpg ltldyarals
      421 mladprpfaw wkvarsavsa imasrrawre qdsaalspgg seaasmk
//
LOCUS       WP_175882558             405 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175882558
VERSION     WP_175882558.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..405
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43645
     Region          8..404
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(103..105,129,179,211,240,242..243,251)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(106,139,204,249..251,280,283)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            243
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 msapidtlnr flaaarpsat yqvmdrvaar rasgaavisl sagepdfdtp ehvreagiaa
       61 iraghtrytq vaglralrda iadkfrreng ldvdwrdtlv csggkqvifn alaatlnegd
      121 evivpapywv sypeivqlcg grsvtvpcga tsgfkltpea lqaaitprtr wlilnspsnp
      181 tgavysrael ralaevllay phvlvlsddi yehlifdgie fftiaqvepr lrervltmng
      241 vskayamtgw rigfgtgprw lidameklqg qqtsgastis qhaalaaltg pqdfiahsrv
      301 afqrrrdrvv aqlnqarglr cevpqgafya fascerligr ttragvrlas dedvvnalld
      361 eagvatvhgs afglgpfiri ayalddasll racmaiqdfc gtlta
//
LOCUS       WP_175882573             481 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar porter family MFS transporter [Burkholderia sp. BCC0044].
ACCESSION   WP_175882573
VERSION     WP_175882573.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024203
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..481
                     /product="sugar porter family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51536
     Region          30..457
                     /region_name="MFS_XylE_like"
                     /note="D-xylose-proton symporter and similar transporters
                     of the Major Facilitator Superfamily; cd17359"
                     /db_xref="CDD:340917"
     Site            order(42,160,163,167,282..283,287..288,291..292,381,
                     385..386,390,413..414,417)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340917"
ORIGIN      
        1 mqevyetlts vehsqsvaae paqahrsmrf iaiiatlggl lfgydtgvin galaymtedl
       61 gltplteglv tsslllgavl gsvtsglvad rygrrmsimm lavlflggal sctfaptvsm
      121 liasrfvlgi avggasicvp tylaelapvh rrgqiitqne lmivsgqmia fivnammgsl
      181 wgsehgiwrw mlavatlpav glwfgmlamp esprwlaskg klhaawkvlq qvrdmqaalq
      241 efdsirhagh rnahparrtg pglsapwvrh vfwvgigiai vmqatgvnsi mfygtqilts
      301 sgfgretali gnvangvisv vatlvgiqvl gkigrrpmfl iglsgttlsl lmiglfsefl
      361 pvsflragli lasmacflgf mqaliapvcw vllaelfplh irgfavgvag cvlwmvnfvl
      421 glsfpslvay vgisstffvf faigvisiaf iwrnlpetkg rsleeieahf rslyggaeqa
      481 r
//
LOCUS       WP_175882578             339 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175882578
VERSION     WP_175882578.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..339
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36318
     Region          2..327
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mskklriavv gaglmgsdhv eriarrivga evsavvdida araravadka pgavavagie
       61 qvladrlada vviatpgflh eatllqvlse glpilcekpl tpdaqsswrv veaevklgrk
      121 liqvgfmrrf daeyrqlrel iatrrlgdtl mlhfshrnaa tpasftsqml vndsvvhefd
      181 girfltgdei asvqvrlgrp trhahpgqhd pqqvlietas gvladveifv narfgyqvat
      241 qavfedgivn igndggpyvr sagqwggsvt ptfverfsaa fdlevqtwvd aarngtingp
      301 sawdgyataa cceagveaqr sgekvavvln dkpalyrda
//
LOCUS       WP_175882614             548 aa            linear   BCT 11-JAN-2025
DEFINITION  NRAMP family divalent metal transporter [Burkholderia sp. BCC0044].
ACCESSION   WP_175882614
VERSION     WP_175882614.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..548
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=58644
     Region          48..452
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 mstpsnvspp iaversavld eahlgdirga lgtishhdtg argtwwarlr tllaiigpgl
       61 ivmvgdndag afgtytqagq nygttllwtl lllvpvlyvn qemvlrlgav tgvgharlif
      121 erfgkfwgaf svidlfllna ltivtefigi tfvldffglp kvagvcvaaa ltmaavstgd
      181 frrferfaig lcvlslllvp vlvsihppva qmtrdffvpn wpahaklsdv mllvigvvgt
      241 tvapwqlffq qsyvidkrit prfmkyekad lwigiafvlv gavamigfss alfsghpeag
      301 nftdaggvia glekyagrts atlfavalld aciigaaavs lstayaigdv fkirhslhrg
      361 vtdakgfylv yfgivaaaat lvlipgsplg llteavqtla gvllpsatvf llvlcndrqv
      421 lgpwvnstkl nvftgaviwv lvllsiilta svmypdisge aivdvlvggt vlaiagylat
      481 vlvrrnkrvv epgidrslrd twrmppldtl epqnmtlatr iwmavlrgyl viavglvivk
      541 vvqmtllk
//
LOCUS       WP_175882674             486 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0044].
ACCESSION   WP_175882674
VERSION     WP_175882674.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..486
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50554
     Region          31..475
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,156,
                     159..160,163,226,229..230,233,301..302,305,333,337,
                     390..391,395,399,415,418..419,422..423,426)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtnntlapca pacaaaaatp rshhgwalvv llvgailppl dyfivnlalp airdgigarq
       61 aelqlvvsay acanavvqit ggrlgdlygr rrmfmvgmag fvlastlcgl adngtvlvgg
      121 rvlqglfaai lapqvlatir svfspqeqvr vmgfygfafg laavigqlgg galislhpfg
      181 lgwraiflvn lpigilalig swrfipenra prgqridvpg tvlmslfllm lvyplthgre
      241 agwplwmiac gigalpmlga lltvearrla rghdplldvr lfrnpivalg lllaflfytl
      301 safflsygiy lqgclnwspl asgfailplg lgflaspllt trlvarfggy rvltlgfail
      361 atgvaiaaal ardgapgpgf yagiaaigig qglvlpsvvr ivlaevdtar agvasgmvsa
      421 mlqigaavga atiggvffar lgvhpaaldy vqgfrasmft lttvlvgcva lsmalgplhr
      481 rlhada
//
LOCUS       WP_175882706             442 aa            linear   BCT 11-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175882706
VERSION     WP_175882706.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..442
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=46920
     Region          3..408
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mnkrmsaagw illamaagil tgyliytqlp dkqsaaeiag yislvsdvfl rlikmvigpl
       61 vfstlvvgia hmgdassvgr vfvkalgwfv taslislllg llmanllrpg enlglplpdi
      121 gasahlatsk ftlkdfvghm vpksiaeama nneilqivvf smffgvalaa lgergkilva
      181 aidqlahvml kitgyvmkla plavmaamas tvavnglsil lkfavfmgdf yvslvllwat
      241 lvaagllflg rrvfkllvli keafmlsfat asseaaypki ldaldrfgvk rkissfvmpm
      301 gysfnldgsm myctfaslfi aqaynihlsl gtqitmllil mltskgmagv praslvviaa
      361 tlhqfdipea glllilgvdt fldmgrsatn avgnsiasav vakwegalms eseanahaah
      421 ldaelerqsr epaygagqtt st
//
LOCUS       WP_175882728             514 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175882728
VERSION     WP_175882728.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..514
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52002
     Region          90..493
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrppeppaas iaaaalatav alagcatssi dlapeasdrp wqpqtsaage ivaapprasa
       61 qgahdytlpa spalasvspp aaldaahayt lpelidlaes anpltriawn darnaalavg
      121 laksaylprl satamgayqa nhgststilg dsssnttahg tisalslqwl lfdfggraar
      181 veaaeqasia snvaftavhq qvihdvtvsy yryeaarsra lsaqqgltna dailaasrar
      241 lkhgvgtvve laqatqnraq anlalvqang aesdsylalv salgisplsk ptiaalpkrp
      301 lppalgssvd aivsdaiarr pdlqgafave kanrakikaa eaafmpkvfl sastsyasgg
      361 tsisalpaig dqaptvnlng srygggvflg vtiplydggl rsavlmqarn daesasarlt
      421 rtkeeavrqv vaaqnavqts lashdaakal veaaqtsyda altayrngvg svtdatiaqs
      481 qllaarnaev dsyagalsaa aalalatgti gsaq
//
LOCUS       WP_175882749             414 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia sp. BCC0044].
ACCESSION   WP_175882749
VERSION     WP_175882749.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..414
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43937
     Region          14..414
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mneadtqeqp apgtvvvigg gqaagwvlkt lraegfagrl vmiadephlp yerpplskav
       61 lagdadietv rvvrpdefda lnveawqper aasidrarrv vktesgreie ydrlviatgg
      121 tsrrlpdalv ntpnlhylrt ldeaaalgek lrasrrvlvi gggwigleva atarklgvea
      181 vvvegaprlc grsvpqivsd flldlhrsng vdvrlgaala slaaqpddas kvratladgt
      241 tidadfavag iglalnasla sdaglavddg ivvdeygats dpaifacgdv anhhngwlkr
      301 rvrleswana qnqaiaaaka vlgvrapyae ipwfwsdqyd vnlqilgdlp adaqlvvrgd
      361 laarratlff vgdghvrgvv avnnarelkl arkwmnqgra vntealadtt qala
//
LOCUS       WP_175882750             466 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0044].
ACCESSION   WP_175882750
VERSION     WP_175882750.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..466
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49471
     Region          42..449
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(51..52,55..56,59,91,141..142,144..146,149,169,
                     172..173,176,284,287..288,291..293,296,324,328,379..380,
                     384,388,404,407..408,411..412,415)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mstfdnvvag ratmeaaast pgaiiarler lpanamqira rvligtatff dgfdvitiaa
       61 tlpllihkwg lsptqigmli asgaigqlig aflfpalaek hgrvkaiaws savigitsia
      121 cgfaptfeif vllrilqglg lggelpvaat yineitrahg rgrfvllyei vfpigllvsm
      181 algawlvprf gweimyfvgg lpvilslvla rlvpesprwl asrgrlaeag ravgvfegsv
      241 rgelppvtqa aafdemvrqh pkrrmsdlfs aayrkrtlav atlwatcgfi qyglstwlpt
      301 iyknfyhapl qlalnlavig svmgvlgsla sallvdklgr kpvivwsfvl calslafagi
      361 yhassvyvva ifcslslglm asgfitayvy tpeqyptsir asgcglgsaw lkiasfaapm
      421 ivphaiiggn lapafyligv vpliaaatvh fvgietkgkv lealea
//
LOCUS       WP_175882755             144 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175882755
VERSION     WP_175882755.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..144
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15757
     Region          1..143
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mlkllvpvgh ssrslqavrh atflyrerca sevvlinvqp plestrleay hplsrlraie
       61 tqfatddlam aerilrdadv kfsvvmkvgp vadtiaaaat etgcdeivva aprrdplhal
      121 msvfrrsvma rlvrisnvpv tavq
//
LOCUS       WP_175882803             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175882803
VERSION     WP_175882803.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33329
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrltslgvf vaaveegsla aaarrfglsp amagkhvsai eaqlnarllq rttrrlsltd
       61 igqtyyarsk qileafedan reahdsqrta rgvlriaapv tfgamhlgev taryledhpq
      121 vnvevllgdr yvdlleagid vairigklqg nalvtsriap crmvicaspa yierhgmprk
      181 psdlrhaqrl vfseavsagd wtlfdaknra hviegpcria anntqmllsa alagagvayg
      241 ptfvfgehvr rgelvallpn yrateltiqa vypsarripl kvrrfvdylt atfgneppwd
      301 rsmkg
//
LOCUS       WP_175882807             466 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0044].
ACCESSION   WP_175882807
VERSION     WP_175882807.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..466
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48632
     Region          17..413
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,142,
                     145..146,149,273,276..277,280..282,285,313,317,369..370,
                     374,378,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mpspskhhal lvqvaaclgf vvvlvdvsvv nvaldtlrtv fgadvtdlqw vvnayalvfa
       61 slllfagalg drlgakhvfi agyavftlss igcgltrtmq aliewrlvqg vgaallvpns
      121 lavlrlafqd ttarsraigw wgagggiala agplvggllv agigwrsifl invpvgvagi
      181 wltwrfapdt kaqrgrsldl pgqltgafal alltfastev salgwtspiv lgafalcigl
      241 sivfirlear npaamlpaal wqdrtvrsat vigmianlvf ygivftlsll fqsvwhmtpv
      301 rsgvallpmm gilmlmniva grlasrfgaq alatvgllis aagylamwpa iaaesfwlla
      361 vpmllagsgi altiptitaa tltavssahs gvasgllnaa rqvggvmgva ifgffvrqta
      421 wvpfmhgmqr alvvsvlllv vgaatawrnl dhtpalarrq nghsps
//
LOCUS       WP_175882833             305 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175882833
VERSION     WP_175882833.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..305
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32679
     Region          15..285
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 msinstaapa aplceidglk igfrghdgvv tdavrdlslt lapgerlgiv gesgsgkslt
       61 grallgllpd aarwsartmr faghdllams prerrrlcgs qmgmilqdpk yslnpvmtva
      121 kqmgeafrrh epglrgralr erivdalaav qirdparvad ayphelsggm gqrvmiammv
      181 stgprlliad eptsaldvav smqvlavlda miarhdtglm fishdlplvm sfcdrvavmy
      241 agrvvetcaa rdlrdashpy trgllaanpp lanppdelpv lrrdpawlda appaaaradr
      301 qetar
//
LOCUS       WP_175882852             187 aa            linear   BCT 11-JAN-2025
DEFINITION  cysteine hydrolase family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175882852
VERSION     WP_175882852.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..187
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19542
     Region          11..171
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 msatrldtnt alvvidlqkg ivalptahpv apviaharel ldafrsrglp vvlvnvagga
       61 pgrteqsppv aqlpadwtel vpelnrqpsd hvvtkrtwga ftgtgldahl kaagvtqivl
      121 tgvatsigve starqahelg ynvtlavdam tdlnadahan sierlfprlg etgttqdiva
      181 lldrrga
//
LOCUS       WP_175882900             288 aa            linear   BCT 11-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175882900
VERSION     WP_175882900.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..288
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=29962
     Region          194..>258
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mslsllpcat iwlalfaaaa fawhrplhgl siglavlgya galafgqiap itlapfalli
       61 aagwgvlper plavriaahl vfaalaials lhlipgfhnp rvigpirftp daapftmyln
      121 fdkplvglwl lwalpwvapd vapsralrtg vvaavataaa clagalafgm igwapkwpps
      181 gwlwlannll lvtlaeealf rgyvqggltr vlrayswgpw valaagavlf gaahaaggsq
      241 wivlgtvagv gyglawrrgg llaaalahag lnvvhfglft ypmlaaar
//
LOCUS       WP_175882961             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0044].
ACCESSION   WP_175882961
VERSION     WP_175882961.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21468
     Region          2..205
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mlfiksvvmg lsiavpvgpi gmlciqrsls rgfragfatg igaacadaiy gllgalgvag
       61 ivtafpmltv glkigggafl vwlawtiarq alaapagqre lprttvlrdf lttfgltlsn
      121 pmtivsfvgi faalgplpga regamwatva wmvagvfvgs atwwlclssa taalraklsf
      181 afmhglsrvs aavvavfgai qlvagvrali
//
LOCUS       WP_175882964             190 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175882964
VERSION     WP_175882964.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Cuthbertson,L. and Nodwell,J.R.
  TITLE     The TetR family of regulators
  JOURNAL   Microbiol Mol Biol Rev 77 (3), 440-475 (2013)
   PUBMED   24006471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..190
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=20088
     Region          1..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          82..179
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam13305"
                     /db_xref="CDD:463838"
ORIGIN      
        1 maragltldk lveagaqlad etgfeqltga alarhfdvkl aslyshipsf ddlksrialf
       61 alqelaaraa dalagrtgrd alaalanvyr dyarahpgrf aaarhpvsae raaasaggql
      121 vrmtsavlrs ydlpdtehth airllggffm gyvtlesagg fshsapdada swsrsldald
      181 vmlrhwpsaa
//
LOCUS       WP_175882992             959 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia sp. BCC0044].
ACCESSION   WP_175882992
VERSION     WP_175882992.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 959)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..959
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=104171
     Region          42..958
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mknhglsrrg flkasvlagv avyvapigsr afaalfeekl ltpvkwdsvt gipqfridgi
       61 akvtgskvfa rdvraadmph wpqqqshali lrvtqadrty egfdlsllgd elkpdrvvta
      121 ddlardgvaf pafygddmll pagktpaylg havailiyhd farfrfakna lkfrddviry
      181 gavtgplerd pwgtfryvrv ggktaydddv ysslkdapif psmmrkhlpv wpdgkehgkl
      241 deqgmflagq iaseldhpsa dwlvfdreyn tqsvdtaale pdnancwyda atqslhlvvp
      301 tqsplevsen aaamvakcrf pvkklfvhpc ytvgygskdh fnvpfyglvc alyadgrpvr
      361 fandryeqfq tslkrhafkm hyriavdrnt gllqsfkgdf eangggrsnf spsvamvgat
      421 aaqsiyyfpk sdlaavaias raidagsarg ygtlqsmaat emavdeiaaq lnidpidfrl
      481 rnalrsgmkn tqgaipagal rvdevlerak qhplwtrraa rkaefeaahp grrygvgfac
      541 vqkdfgtgae asfakvefda hgkvslqhta aeigtgmsts qavavakwlg rpatevrval
      601 tewpdlpvet sgdpylmsqa dqdrlsanpr wspgyaspss atnsayyfth streaaravf
      661 ryglwpaams iwtrglgggq aapytiried arwvdgklta dglepltfeq lakqahalgl
      721 ptgavvhvfn rwqwtdaefe vggmierlpi dglslrvgap ktgaddgplp gtaapagata
      781 lhgtlpptan gyrvldrkrv fipptsrnna avtyytavgt lvelavheat gkvellthhs
      841 imecgnqisp qlvsgqlqgg lamgighalh eylplyedgp gngtwnfnry plprasdvav
      901 wtqtgdvlpp lsetdppkgv aevvmipvvg aivngiahai ghrftdlpvt pqkiqevla
//
LOCUS       WP_175883011             221 aa            linear   BCT 11-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175883011
VERSION     WP_175883011.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..221
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22940
     Region          17..>202
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mqrpsratph vyaatfrala vslainllll avetaaawsa hssglladva haaidlaada
       61 lilvacrfda rlpperrpty eplalaglga llvvtgaqmi whaltrfdtp pvvqpgatal
      121 alaavtlagk avlshwmlrk asetgsalle asgwhvrtda lssllaafam saalvgfgrl
      181 ddlaalaiga lvirtgigfi rrgcaqwpal adwtnrsthg s
//
LOCUS       WP_175883045             861 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia sp. BCC0044].
ACCESSION   WP_175883045
VERSION     WP_175883045.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 861)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 861)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..861
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..861
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=93050
     Region          60..712
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mqpfqpsstr vnrrnvssvr afcarwvara qpvaaaavar lkplaatawh hvrhptrrgv
       61 llaaaavpvl faayvvvlvp ftpgigdirk arvdqpaqvl sadgkllaef kpsnrewval
      121 kqisphmvda liatedhrfy ehhgldwkrt asaalhtfsg srqggstitq qlarnlypdd
      181 igraptltrk vkeaitalki eavyskdqil etylntvpfl ynaygvemaa rtyfdksade
      241 ldvldsatlv gmlkgnsyyn pvlnperalq rrntvlgqmv kygklspaqf aqlqrrplri
      301 dferqkeppg paphfaqqlr kwliawadrn dyniysdgli vrttidsrlq qmatqaltlq
      361 gnqlqgiann awsgrdgcgt dnevfrtfmr espeykaaqd agkddaaamk mlaadrgflh
      421 alckaktdvq agflaidprd gqirawvgsr dftrepfdhv aqarrqpgst fkpfvygaaf
      481 asgmkpedtf idqpveialk ggeiwrpndd vpptgkpmtl rdavalsrnr itaqvmekvg
      541 pgavarlard mgvrespler vpslalgtsp vtlkemvasy atiangglyv epqmvtrien
      601 rqgevlaeya papperalda etdktlldvm rdvvtrgtgg sirtrfgirg dvagktgttq
      661 dnadgwfilm qpglvagawv gfddgrvtlr sdywgqgahs alpivgdffq raqrarivdt
      721 kakfdtepsp gwfgslrerv tdlfdtwfpp epkkasapvr tqrierpaea degaaseasa
      781 asapdaasgg iveewvpase vaasaaalsa gasqqpqpaq ppagasttgg ssagagaaps
      841 avpapppvpv paapdatgas q
//
LOCUS       WP_175883057             157 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175883057
VERSION     WP_175883057.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..157
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17365
     Region          6..144
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mpepvldrid rhllsvlqen grasnldlak avglspaqtl rrhrrleeig airryetrlc
       61 adtlgfgvta fvhvtmergh irdlskfqkl vsdlaqiqec fsvtgdidyv lkvvahdlkg
      121 lsrflletlm ripgvsgvhs svcldeikct sampves
//
LOCUS       WP_175883063             251 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175883063
VERSION     WP_175883063.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..251
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27646
     Region          1..239
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 miridsihkr fhqhavlkgv sldvqqgevv cligpsgsgk stvlrcingf etydegsiti
       61 dgvkvdahsk rihelrmrvg mvfqrfnlfa hrtalenvme gpvhvrrmpa aqareqaral
      121 ldkvglshrm naypselsgg qqqrvaiara lamepqailf deptsaldpe lvgevlgvmr
      181 glardgmtmv vvthemafar evadrvcflh dgticesgpa rdvltqpthp rtqeflrrll
      241 asdgadhpdr t
//
LOCUS       WP_175883070             442 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0044].
ACCESSION   WP_175883070
VERSION     WP_175883070.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..442
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46493
     Region          28..407
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(39..40,43..44,47,79,129..130,132..134,137,157,
                     160..161,164,262,265..266,269..271,274,302,306,355..356,
                     360,364,380,383..384,387..388,391)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 msthhaqals saagdanasl nrllfrklmp lliaayvisf ldrtniafak hsmgvdlgis
       61 saayglgagl ffltyalfei psnlimhrvg arfwitrimi twgalsvama fvrgetsfyv
      121 mrlllgvaea glfpgvmlyl tywfgreera ratgyfllgv cianivggpl agalieldgt
      181 lgfhgwqwlf vvegipaill afvvwtrlpd rpsaapwlap etgralerkl aaeqdagvaa
      241 hgghafgaal rdpqiwlaif vyfchqltiy tvifflpgii gasgrlspva vglltslpwl
      301 aaalgagtlp rfaresrhsr rmlcaglvvm aagmigaaha splagllcvc vaasmffvvq
      361 sivftfpasr lagsalaggl glvntcgllg gfvgptvvga ieqatgnakn gltllaaalv
      421 vaafaslalr hgheradgrs rg
//
LOCUS       WP_175883075             315 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175883075
VERSION     WP_175883075.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..315
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34487
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdtlqnmrvf srvvetgsft aaaqslnstt gamsravsel earlrtrlmn rstrrlalts
       61 agesylrrcr qiladvdrae eeascaherp agvlrmhsfa svghhyvlpa ltryhaqfpd
      121 vsielslsqr mpdlfdgtsd mavvtasslp dselvshllg stfnilcasp dyvkrhgvpa
      181 rpqdlaahac ltlctpafpt hewvlegpeg veqihvagpm qtntaeslal airdgigigm
      241 lplysaidal rdgslvrvlp ahilqkmnvy alypsrrfvd akvrtwveml raqvpamiar
      301 dvemlnaidr epqaa
//
LOCUS       WP_175883091             319 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175883091
VERSION     WP_175883091.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..319
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35025
     Region          2..313
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhrigflisd gfqimalaaq svfeyanmgm dapfyamdsy svdggdvrss lglpvatral
       61 rgrigvdtwi vagvndplaa papagvvayl rrangqarri agictgafvl aeagllaqrr
      121 atthwafgrd mqrhypeirv eddrifivdg piwtsagmta gldlalamve kdlgadaars
      181 vahklvmhqr raggqsqhse mlelapksdr iqnalnyarr nlgraltved laeavhlspr
      241 qfsrvftlet gqspakaier lrlesarlmi eqsrhpldvi akengfrdrr hmrdafvrgf
      301 gvppqalrrd araderemg
//
LOCUS       WP_175883140             288 aa            linear   BCT 11-JAN-2025
DEFINITION  MOSC domain-containing protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175883140
VERSION     WP_175883140.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..288
                     /product="MOSC domain-containing protein"
                     /EC_number="1.7.-.-"
                     /GO_function="GO:0016661 - oxidoreductase activity, acting
                     on other nitrogenous compounds as donors [Evidence IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=31216
     Region          1..281
                     /region_name="YcbX"
                     /note="N-hydroxylaminopurine reductase subunit YcbX,
                     contains MOSC domain [Nucleotide transport and metabolism,
                     Defense mechanisms]; COG3217"
                     /db_xref="CDD:442450"
ORIGIN      
        1 mpaitelfvy pikscagial traqlletgl aydrhwlitd pdgqmltqrt hprlalirpt
       61 ldgdalvlna pgmpeirtpl dgdatpatpk maatvwrdtv daidtgadta awltefvgvp
      121 tklarfgpda rrdcnrtwtg didthtqfsd aypllvigqs slddlnarla akgapaipmn
      181 rfrpnivvsd ldayeedfve hldtngdtpv rlrlvklctr cpmptidqat gapdpawphe
      241 ptdtmqtyra npnydgaltf ginaivvega gawlevgqpi eaeigfgd
//
LOCUS       WP_175883242             231 aa            linear   BCT 11-JAN-2025
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Burkholderia
            sp. BCC0044].
ACCESSION   WP_175883242
VERSION     WP_175883242.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Sciara,G., Clarke,O.B., Tomasek,D., Kloss,B., Tabuso,S.,
            Byfield,R., Cohn,R., Banerjee,S., Rajashankar,K.R., Slavkovic,V.,
            Graziano,J.H., Shapiro,L. and Mancia,F.
  TITLE     Structural basis for catalysis in a CDP-alcohol phosphotransferase
  JOURNAL   Nat Commun 5, 4068 (2014)
   PUBMED   24923293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Koga,Y.
  TITLE     From promiscuity to the lipid divide: on the evolution of distinct
            membranes in Archaea and Bacteria
  JOURNAL   J Mol Evol 78 (3-4), 234-242 (2014)
   PUBMED   24573438
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Koga,Y.
  TITLE     Early evolution of membrane lipids: how did the lipid divide occur?
  JOURNAL   J Mol Evol 72 (3), 274-282 (2011)
   PUBMED   21259003
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..231
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=24431
     Region          37..212
                     /region_name="PgsA"
                     /note="Phosphatidylglycerophosphate synthase [Lipid
                     transport and metabolism]; COG0558"
                     /db_xref="CDD:440324"
ORIGIN      
        1 mdqrktatrp epplprtwda rlarslvrpl vdtpvtpnhl ttlrlligla gawclahggf
       61 gwsnagafli vlsnfvdhtd gelarisgks skighfydla adalvtialf vsmgvgivaq
      121 ggqmaaspvl lgavagaava lifflrmrie siagkagtkq afaggfeted vlyllpivtl
      181 vdgvepflla asigaplfaa wvvidwwriv rrgnlpqnpa aqnpteiqas k
//
LOCUS       WP_175883133             451 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175883133
VERSION     WP_175883133.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..451
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47754
     Region          38..408
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msaslaassp spqpalrlmp adaaeaatda adettdaria allerlapel aadaarndvd
       61 grfphenfar lhragliaqv vprehggaga tlarasriva avgradpata lvltmtylqh
      121 ralgradnrw paqvrravfh savahgalin alrvepalgs psrgglpati arrdgdgwrl
      181 sghklystgi palrwlavwa rtdepaprvg vflvprdpat dgdrirvies wnhlglrasg
      241 shevvfddvp lpadhavdvr apdawvvsaa thadadaqad qqawmvallg slydavaras
      301 rdwlvefatt rapsglgapl atlprvqeav geiegwlhtn rvllddhiar tdagnapsvt
      361 tsglvkrtvt ehairtveqa lklsgnhgls rgnplerhyr dvlcsrvhtp qddaiavaag
      421 raaldaatrg qthaaadats rngiergrrd a
//
LOCUS       WP_175883294             227 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia sp. BCC0044].
ACCESSION   WP_175883294
VERSION     WP_175883294.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..227
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23850
     Region          23..225
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mtdvlpltte pesglryllr patgrpaarl lllhgvggne tnllnvadvi dprieiaflr
       61 gpltfgpnqh awfpvrfgpn gpeidaarad esrvqlltll halraqdgaa palptviagf
      121 sqggimsasv gltspgdvsa favlcgrilp eidpliaphd alstlhalvm hgrfddklpv
      181 awadtadakl talgvahdtr lygaghelta qmagdfgrwv geragln
//
LOCUS       WP_175883364             371 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia sp. BCC0044].
ACCESSION   WP_175883364
VERSION     WP_175883364.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..371
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40419
     Region          3..348
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,57,99,231,302,322,324..326)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,57,99,101,108,179,182,184,231,238,302,322,
                     324..325)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,101,179,182,184,325)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            184
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 msklfsrtrv ghfdlqhrvv lapltrmrte pgnvpgnlmv eyytqratdg gllisdatav
       61 sqlgiayvda pgiytgeqvd gwarvidavh akgariflqm whagrqahpa ntggitpvap
      121 salrslehaa irdengrite aelivprple treipaiveq frrgaelakr agfdgvelhg
      181 angylfeqfl ldgtnhrtde yggsienrar flfdtldavv svwgpgrvav rlspsgtygt
      241 msdsdphatf gyvaerlnsy dlayvhviep rvrgtmeqat tdadvsskdi rriyrgtiia
      301 aggftgetae rivvdghadl vafgrlfisn pdlpqrlrtg aplnrydrtt fyggdargyt
      361 dygsisadia a
//
LOCUS       WP_175883363             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175883363
VERSION     WP_175883363.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13300132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32347
     Region          13..>125
                     /region_name="PRK11242"
                     /note="DNA-binding transcriptional regulator CynR;
                     Provisional"
                     /db_xref="CDD:183051"
     Region          92..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrlaamety vsvveagsfs aaakrmnlgq paisksiaql eerlgarlll rstrgltptd
       61 agqrfyehak rvireadeae hivrdasssl sgklrisaav sftclhvlpr ldtflsrhpd
      121 leidlvlddr nidlleegtd valrmgtlid ssmiarriar sprlvvgtpa yferagvpna
      181 paelarhqai vysqrgggea wsfsrngtev avavsgrlrv saaegmrtav lsgmglavas
      241 rwmfspelas gavqavltdw elppvdlwav fpagrlvtar arafvefveq vlagqdaapa
      301 a
//
LOCUS       WP_175883312             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0044].
ACCESSION   WP_175883312
VERSION     WP_175883312.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46881
     Region          28..433
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(39..40,43..44,47,86,144..145,147..149,152,172,
                     175..176,179,261,264..265,268..270,273,301,305,358..359,
                     363,367,383,386..387,390..391,394)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mqtrstldeh asiatpaper takhyllagw asmagttiew ydfflygtaa alvfnriffp
       61 sldpvvgtla afgtfavgfi grpmggivfg hfgdrigrks mlmitlllmg vpsmiiglip
      121 sydsigywaa alliamrflq gmavggewgg avlmavehap kgrkglfgsl pqtgvglgli
      181 lssvamaava alpeadmlsw gwrvpflasi alvglgwfir akvpespdfe kvrkqgkaek
      241 spvtaalrrh prevltivga raaentwfym vvtfalayat qqlhlpkaem lhaitagaal
      301 slvtmplcgh lsdrigqrrm faiglvlmca faapffmmlg tqqtsyawwa ivlglgvvfp
      361 ilyapesllf aqqfpaeiry sgislsvqla gvigggfapm iatsllkagg gqphyviayl
      421 vgfgvfalvc talmrpara
//
LOCUS       WP_175883365             137 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175883365
VERSION     WP_175883365.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..137
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14343
     Region          6..130
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mdrykflpll griligapfl msglsklgah dgtvayiaav glpapslafi vavlveaggg
       61 lllmsgyrar ivalamavfc vvtavffhhn fadqnqmihf lknvmmaggl lqiayfgaga
      121 fsldaraera tsravta
//
LOCUS       WP_175883368             446 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia sp. BCC0044].
ACCESSION   WP_175883368
VERSION     WP_175883368.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..446
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47631
     Region          5..435
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mqassssepv rlkrtlglps vllfglayma plivygtygv lakasddtaa layllaliai
       61 aftalsygkl arlypaagsa ytytrrtfnp hlgfmigwat lldyfflpmv iwligaayln
      121 aafphvptwi wivafivlts glnivgiela arfnivlmvv qlaivamfva lcwhyasaaa
      181 gpggiamaep ffkphvpfga tmagaaiaay sylgfdavst lteetidpkk nmpraillia
      241 liggaifvia aytmqlahpg vefkdtdsaa fevakmiggd lfvtvflagl ilaqfasgis
      301 aqasvgrlly amgrdeilpk rifgfihprf ktpainiala gvvglialkl dvatstsfin
      361 fgaflaftav nlcvirlyls gnhgerrigv fgglvfpaig avsdiwllvs lekaalvlgv
      421 awfvlglvyl cwitrlfrqa ppevai
//
LOCUS       WP_175883418             278 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175883418
VERSION     WP_175883418.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..278
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31180
     Region          1..204
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkfslimatl grsdeiermf dslllqayad levivvdqnp ddrverivdr yrdrltivhl
       61 rsakgksrat nvglkavtgd vvgfpdddcw yrpgmlhava arlsadrtid gvtgmsidaa
      121 grpsqgrwat aaqtvnrfnv wvcatsytif lrrtavtaag qfdvdlgvga tsrwgageev
      181 dflvralrag cridydphlr vhhpeplavl dehayargrr ynrgfghvlr inryplayvl
      241 ymiarpvagc vlscvrrnpr rakyywiaas hrllgwmd
//
LOCUS       WP_175883439             157 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175883439
VERSION     WP_175883439.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..157
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17047
     Region          3..153
                     /region_name="COG3865"
                     /note="Glyoxalase superfamily enzyme, possible
                     3-demethylubiquinone-9 3-methyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:443074"
ORIGIN      
        1 mtiqkitpfl wystqaeeaa afyagifpds rivrvtavpg tdstrmvefe lfgqpflams
       61 hprteafnht isllvscadq aeldrywsal ldnggtadgc gwlrdrygvs wqivpealip
      121 mmadrdavka grvaaammqm tkfddaalka afagtag
//
LOCUS       WP_175883499             203 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175883499
VERSION     WP_175883499.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..203
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=21468
     Region          <33..203
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(77,79,83..84,87..89,91..92,96,99,108,110,112,
                     116..117,120..122,124..125,129,132,141,143,145,149..150,
                     153..155,157..158,162,165,174)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          77..108
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          110..141
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          143..174
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          176..201
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mrserfthai raaaaalala alagcahlpd qpaygkadpa alrrydddwf daarigrvdi
       61 lralhdagyp vdatdshgyt avilasydgq paaldyllsa gadacvgdrh gntalmgalf
      121 rnepaiarrl idtrcpidqt ngagetalgf atlfnrfeli pllvahganp nhvdrrgqsl
      181 lqlalthdnt yaadalrdag akp
//
LOCUS       WP_175883506             216 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175883506
VERSION     WP_175883506.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10583942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..216
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23294
     Region          25..168
                     /region_name="Pyridox_ox_2"
                     /note="Pyridoxamine 5'-phosphate oxidase; pfam12900"
                     /db_xref="CDD:432864"
ORIGIN      
        1 mndqttlsst prttirrlpe lashdrtmly rivddayvch iafgdgqhph ciptahwrig
       61 dalyihgsng srmikalsag aqacvamtll dglvlarsaf nhsmnyrsav iygqfdmieg
      121 saeklaalda lmdkiapgrk hearpgnske inatrvlris laeaavkvsd slpsdkeedl
      181 glavwtgilp lktthgapvh adgnvavpdy vlnwad
//
LOCUS       WP_175883551             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0044].
ACCESSION   WP_175883551
VERSION     WP_175883551.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46426
     Region          23..427
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(35..36,39..40,43,82,140..141,143..145,148,168,
                     171..172,175,258,261..262,265..267,270,298,302,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mpatmstlaq paahtprrvr nsrlatasmi gtslewydft iyntlaalvf nhlffpsvdp
       61 lagtilafst yavgyvsrpl ggfvfgnlgd rigrravlml tlvlmgvtta lmgalptyaq
      121 agilspillv alrfvqgval ggewagavll svehgdqkrr glsaswtqig psfgtllgtg
      181 cialvtlstt sdtflswgwr vpfaasallv afgfwvrrgv detpqfeqla eshataevpv
      241 advlkyhwkr lliaggsrig sdvlyalivv ftltyvttvl hlsrpvalta vmigtacnal
      301 avpffgalsd rfgrrpvyla galagivwaf vfftlldsar pvaivaavai glvihavmyg
      361 pqgafvteqf ptrvryagss laytlagivg ggfaplviaa lfrqtgttta vslyvtaalv
      421 vtsialvaar etahrpled
//
LOCUS       WP_175883560             252 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia sp. BCC0044].
ACCESSION   WP_175883560
VERSION     WP_175883560.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..252
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26311
     Region          1..245
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 msvskkfaav tgagsgigra aalalaqagf tvallgrtea slretqdair aagsdaevfp
       61 vdvtdeasvd hafaqiaqrf grldvlfnna grnapvmsld eyeldvwnsv vatnltgvfl
      121 caraawrlmk tqtpqggrii nngsisahap rpdtiaytat khavtgitks laldgrrhni
      181 acgqidigna atsltermtq gvpqadgsla peprmdvahv anaivqmanl pldtnilnmt
      241 imatampfvg rg
//
LOCUS       WP_175883571             345 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175883571
VERSION     WP_175883571.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..345
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37525
     Region          6..334
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 maivriwvyd gilasgvagp vdvfsaanqf hmrkatpagt psapllawrv esldgrpvta
       61 asgqtiqvdg kidprkrada vlltapffsn idefigrreq lnaltsalrr qrkagavlaa
      121 yctanyllae aglldgraat thwakaadfa rryprvevra qelmiaqdgi isggsvtsyl
      181 nlavqlvetl agealatmta kallidmnrt sqasfatlvd ehghtdtlva raqrqmeatl
      241 qqgfrlsela aslavsertl nrrfkeavgl apltylqnlr ievakrllet rpiglealsq
      301 rvgygdistf rqlfkrktgl spseyqvrfs raaaknrdde prskg
//
LOCUS       WP_175883664             138 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175883664
VERSION     WP_175883664.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..138
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14888
     Region          1..125
                     /region_name="COG3607"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]"
                     /db_xref="CDD:442825"
ORIGIN      
        1 mhkmvfinlp vadlpraktf yqalgfevvp aytneqaaci risdtifaml lvrpffqtft
       61 dktiidpath iqvlsclscd sraevdaiva kalaaggaap qapreypnmy ghgftdpdgh
      121 twelmampld asaqgqas
//
LOCUS       WP_175883676             133 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175883676
VERSION     WP_175883676.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..133
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=14487
     Region          17..133
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mslihaaavl dadaadyvvq lqagthaltg deapreggqd rgpapyefvl aglaqctaat
       61 lrmymqrktw paariavrte lhadregaqy vrrvvtldgp lddaqrqrla eicektpvtq
      121 fikrgtriet tln
//
LOCUS       WP_175883687             558 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175883687
VERSION     WP_175883687.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..558
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=60449
     Region          27..556
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 matvtpratn eslhptigag rltlgnrill sfgvlfvlml vtagvsyerl rainaeavsi
       61 erdslpgvyl asslrgsvne sftllqrgif vetepdiaqr dlakiadalk eveslsadyq
      121 nttfrdddrq rftafrgayd hyvpllneav qksrashdea vaayakalpa wtevvrnanv
      181 lvqenrkfae qsakmiresv qdtevvlata lafmllsala lgyllyrsvt vpmarlvevh
      241 dvmrtgnlth rldlrrsdef gtletgfnrm adeltelvsr aqqsslqvtt svaeiaatsr
      301 eqqataneta attteigats reifatsrdl lrtmnevagv aeqsatlagv sqsgltrmge
      361 tmrsvmdaag svnaklailn ekalninqvv atitkvadqt nllslnaaie aekageygrg
      421 favvateirr ladqtavaty dieqtvkeiq savsagvmgm dkfseevrrg mldvqqvggq
      481 lsqiiaevqt laprfqmvne gmqtqangae qitqalsqls eaaqqtaesl rqssqaiddl
      541 tlvanqlrts vsrfkvda
//
LOCUS       WP_175883702             259 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Burkholderia sp. BCC0044].
ACCESSION   WP_175883702
VERSION     WP_175883702.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..259
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=28908
     Region          2..220
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mnvlivyahp eprslngalr dfavahleaa ghavqvsdly amnwkavfda ndvidrepda
       61 rfdptldskr afaegtqsed iareqdklkw adavilqfpl wwfsmpaimk gwfervyayg
      121 faygvgehsd thwgdrygeg slagkramiv vttggwephy sprgingpid dllfpiqhgv
      181 lyypgfdvlp pfviyrtgkm naarfdetra algqrlddlw ttppipfrrq nagdyeipal
      241 tlkeeiapgk vgfavhlaa
//
LOCUS       WP_175883725             220 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175883725
VERSION     WP_175883725.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122607
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..220
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24815
     Region          8..79
                     /region_name="GST_N_1"
                     /note="GST_N family, unknown subfamily 1; composed of
                     uncharacterized proteins, predominantly from bacteria,
                     with similarity to GSTs. GSTs are cytosolic dimeric
                     proteins involved in cellular detoxification by catalyzing
                     the conjugation of glutathione (GSH) with...; cd03043"
                     /db_xref="CDD:239341"
     Site            order(19,21..22,24..25,28..29,72,75..76)
                     /site_type="other"
                     /note="putative C-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(19,57..59,70..71)
                     /site_type="other"
                     /note="putative GSH binding site (G-site) [chemical
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(57,69..70,72..73,76)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239341"
     Region          92..204
                     /region_name="GST_C_3"
                     /note="C-terminal, alpha helical domain of an unknown
                     subfamily 3 of Glutathione S-transferases; cd03194"
                     /db_xref="CDD:198303"
     Site            order(95,102,163,166..167,170,174)
                     /site_type="other"
                     /note="putative N-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:198303"
     Site            order(95..96,99..100,103,139)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:198303"
     Site            order(102,106..107,110..111,171,174)
                     /site_type="other"
                     /note="putative substrate binding pocket (H-site)
                     [chemical binding]"
                     /db_xref="CDD:198303"
ORIGIN      
        1 mestvqttlt issrnyssws mrgwllakls glsfetisvp idatsraell llspsilvpc
       61 lthdgnavwd tlaiaeylne ihpqarllpd drrarahcrs icgemhsgfs alrsalpmnl
      121 rghfpgfriw sraqhdieri vtiwreclme yggpwlfgae igiadamyap vvtrfltydv
      181 klesdvaeyc mrvlahpfva ewietakaeh edideldmef
//
LOCUS       WP_175883744             356 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175883744
VERSION     WP_175883744.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..356
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38477
     Region          26..265
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mtaplptrlp plvrhalrpl ldpyrryrha klihaarval ailvsialst glnvphgews
       61 titvlivvgg lqhhgnirkk aaeralgtsi galaglglil lysflhapfa iyllmavgcg
      121 vcayhaigka gyiallsait mvivaghgdn eivdglwrav nvlvgiaial afsfalplya
      181 tyswryklad alracaavha rlagdrhvsn dahlkemaal stllvqlrsl mpsvskecet
      241 smtqleaiqr slrlcigyle ilssalpaad dvaareymrv emkgvnrrir dtlvgasral
      301 kfgtpsrlap rrrpvdpphd apppqlsgyv sitaklagev dqlrerlldt arswni
//
LOCUS       WP_175883769             439 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175883769
VERSION     WP_175883769.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..439
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45750
     Region          55..435
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mlklnlvaai vfvmaataha qpspspspgp ataaigsatp igappsntlp essltlsdal
       61 avaarnnpal rgaradvdas agalmqagar pnpevsflqe gfsraertst alinqtielg
      121 gkrrarldva sygreaanas ldeqgaavra dviaafygll aaqrqlqvte esaaiaarsa
      181 dlagrraqag kvspveatka qvaaagvqie vvtargrvev areklnavmg earndrlavr
      241 gdletvppve plsaltvqld daplarvara emlrsnaavs lerarripdv tvsagvkrvt
      301 tggvpdnqav vgvsipiplf ntnkgallea thkaeranad ldrertrlrl eltqayanfe
      361 aaeqeaqrlk sdilpaarla ldamsrgyel gkfsfldvld aqrtlfqgqs qyvralagah
      421 aaradigrlv gtplaavaq
//
LOCUS       WP_175883770             396 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175883770
VERSION     WP_175883770.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..396
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43522
     Region          68..371
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 msfplepdgp lsrdvappqf gvdgeqaerd wplithdeva gvlaridgag epvrltwhsp
       61 rqfaaavlvr madgrglfvk rhhaslrdva gleeehrfia hlrargmpvv dvladrdgat
      121 afasgewtye vhvlapgvdp yrgvmswqpf thpshayaag ralaelhras agydaparpv
      181 rtllssfrvl ssadladale rwvdaqpllv ralgsrdwrg dvadaigpyh arlvpllpal
      241 pplwthgdwh asnllwtaae pgaqvrtvld fglsdrtcav mdlalaiern tvdwmapada
      301 rrveygqida lldgyeslep lsddayaalv allpivhtef alsevayfgc iidapaivdi
      361 aydgyligha rwfgerdgrq lidwlvqrrr gkqrit
//
LOCUS       WP_175883772             743 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia sp. BCC0044].
ACCESSION   WP_175883772
VERSION     WP_175883772.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..743
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79485
     Region          40..743
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mtvnrtttap arrrrvkvgl gvglgvtlfa aqaaaaqgdt papgadatgn atlpaitvng
       61 ergqplrare asvaglddap lrdtpasvnv itraliddqq akrlsdvvrn dasvvndyap
      121 vgyfegfair gfpvdlasai ridgltvsge qnvplenker veilkglagi dsgvvapggv
      181 infvtkraan vasvtggvds rgstsaavdl grrfgpgnqf gfrinaaken mhsyidgtng
      241 rrtfgsiaad wdispraslq lnaefqqwiq rsapgyqllg gtvvpsvktt skalgtqpwa
      301 kpvttdalnl narfdyqfnd dwkayiaagr srtmiddnsa faygcsyaas caagatspff
      361 fgangdydvy dfrspgeyrr nddlravttg kfatgplrhe ltlgvsvqrr vvhmatavyd
      421 yvgseniygp dvafapspnt pgpsypqlds wqygvfgldr islgehwqvl aggkevllrq
      481 rswssldgda thtdrsvflp qvalvykpvn alslyasysk alslgdqapv ratnayaflp
      541 pveshqievg akydwldrls ltaavfsisk pfqfadpdas gtsytfvqrg tqrhqgielg
      601 aagrvterlg ltasvaaira ravdsgspay eghqiinvpa lraslyadya vpgvaglnvl
      661 ggveysaarn aneegtarvp swfvfnlgar yttkigghrt vlrvsvdnlf nkfywrdage
      721 qqgdaylfpg aprtarvslt ydf
//
LOCUS       WP_175883775             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175883775
VERSION     WP_175883775.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33076
     Region          9..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..294
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,229,246,273)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,193,
                     223..227,234..235,238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 madlrdvnln rlaifvavvd agsltaaaer lglaktvvst hmqrlesevg anllvrttrr
       61 lsvtdagrvf ydacrdivra teaaldavss dagplrgtlr vsvpidygal vvapavvalr
      121 drhpaldvel vandrvvdlv adnldvairi grladsnyra vqlgtyekwl vaspafvary
      181 glprdpdala glpfvmlssl prphtleldd arggrasvrc vapvvsntat acraivlagg
      241 gfglltdfst addvaagrlv rllpgwrtap agihavypst rlpspkvraf ieamkgrlge
      301 aaatpttkrs rsk
//
LOCUS       WP_175883802             300 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175883802
VERSION     WP_175883802.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..300
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31752
     Region          32..278
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mqephspgts paarmphpde davpadsada agapgtgmlq rafailrala gmqqdgvrvt
       61 hlakavgltq gtahrilqsl iaegmveqde qsklyrlsvd ffalaalagn pssmrtlcrp
      121 allrlcaslg etifllvksg fdavcldlce gpfpirsftg diggrialgv gqgslailaf
      181 lpeaereevi rfnvprirgy gvldevylrt eiervrqlgy agrnsgvldg magvavpild
      241 rtgypvgals vgtlasrlgd drmpmvvell rrqadaigpr tnpfdaalrr pmhglsgktg
//
LOCUS       WP_175883787             190 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Burkholderia sp. BCC0044].
ACCESSION   WP_175883787
VERSION     WP_175883787.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..190
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19913
     Region          15..169
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mvnetrtdse rpldivalcg slraqsynaa lldaaarvap hgmritrfdr lgefplfnpd
       61 aeypapaavr dlidrlnaad gvliaspeya hgvtgvmkna ldwivgceav vykpvavlna
      121 sprathadaa lretlsvmsa rivedasitl pilgsqldaa giaahppfas alvealhalr
      181 taiddpaagr
//
LOCUS       WP_175883803             360 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175883803
VERSION     WP_175883803.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..360
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39436
     Region          1..358
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msfltltdlt ktfgeltava dvnlsveqge fvsllgpsgc gktttlqmia gfvdvtrgri
       61 aldgqdithl kpnrrglgiv fqsyalfphm svaenvgfgl dmrgvdkaer veriraalal
      121 vrldalahrf prelsggqrq rvaiaravvi eppvllldep msnldaklre emqfelraiq
      181 rkigtttimv thdqsealsi sdrvvvmeag ritqtdtpyr ayerpenhfv sqfigkanll
      241 pgtivahdgd airidlghdl aetgrtahlp arerdmrigd avsvcirpek lrlcapdagr
      301 faatvtsrff lgsqwlyrvd salgevlvcc qnegaeplae gapvgidwhs davrvmrrea
//
LOCUS       WP_175883804             328 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0044].
ACCESSION   WP_175883804
VERSION     WP_175883804.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 328)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..328
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34714
     Region          40..321
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mgqpsrplss dgapaglaps gatatadams pravggnalr aswrahaplw lmcapafalf
       61 aalvlvplam tfvltfyrfd patgpiaafq fgnyaevlgs syfhtifart fgiaalttai
      121 cvaigtpeay vlskmrdpwr slfllailap llvsvvvraf gwsmllntsg lvnqalglvg
      181 lgpykleytt faivialvhv mlpfmvipvw talqrldpqt ehaalslgas pfttlrrivv
      241 pqlmpgvlsg slmvfglsas afaipgllgg rrlkvaatav ydeflgslnw plgatiavll
      301 laanlvvmlt yyrvlerrya rslggasr
//
LOCUS       WP_175883815             395 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175883815
VERSION     WP_175883815.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..395
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42918
     Region          8..390
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mfdhlqrpef valraavlrf vddelrpier elqldsedvw prdvlrrvwr rsaalgfyta
       61 slpveiggqg lsiaevcalk adlaasgaal aphvlgelgg pprignmlky atpaqleryf
      121 kpvmrgekst cfaltephsg sdamsirtta vedgdalvin gtkhyisgap fadfaivmcv
      181 tdatatppqi tavlvdldlp gvridheyvp msgqyidadi cftdvrvpre nvfggigngf
      241 klgmsrisvn rllhcptmlg lamsayraal dyartrqqfg gpiarfqaiq hmladmatel
      301 wacesmiaht aaladagadl rmmssacklf vsercfevad kavqihgnvg vtrghpveqt
      361 frklrmfrvl tgtseiqrnt iakailepag agrda
//
LOCUS       WP_175883818             445 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0044].
ACCESSION   WP_175883818
VERSION     WP_175883818.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..445
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47249
     Region          22..426
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(35..36,39..40,43,83,141..142,144..146,149,169,
                     172..173,176,258,261..262,265..267,270,297,301,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 myptdtvqsp savrpladrq lrriviasva gnamewydff vygtaaalvf ghvffppgas
       61 plagslaafa afalgfvarp lggivfghvg drygrkaslv wtllimgast faigllptya
      121 qvglwapaal vvlrllqgia sggewgggvl misenappeq rgyyaawsql gvgggfvlss
      181 aaflaaqalp ddafrtwgwr lpflasiaif aigiyirrhl pesrdfeqag krgahthlpi
      241 vecirrhpke illamglrva enggayifla fslvygkylg ipngtmltgv miamivemga
      301 mlawgrlsdr igrkpvylig alslvacafp ffwlldtrvt plvwlaltvg tavshgamig
      361 tlpalvgelf stevrysgva lghevasifa ggmspliata llaryhaswp vslflialgl
      421 vtvatlcvmr etrtppadgs rgdpa
//
LOCUS       WP_175883881             240 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD family hydrolase [Burkholderia sp. BCC0044].
ACCESSION   WP_175883881
VERSION     WP_175883881.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..240
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26191
     Region          6..233
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mrlakvsals fdlddtlwpf gpsvvraeat lrawliehap ntasvlptqq alsalreeye
       61 rlcpdlasdy ramrigsirl aleranedvs ltdraydvfy aarnrvefye dalpalawls
      121 arfpliavtn gnadlrltgg geffrttlsa rafgfakpep eifhaaadal gvrpaellhv
      181 gddfhldivg alnaglqaaw vvreprvdge qapqhavtph lmlrdlamlc ralggpdtvs
//
LOCUS       WP_175883882             205 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175883882
VERSION     WP_175883882.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..205
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23161
     Region          1..192
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mklygfagtr sqralwglke ldadfefvsv nllegahkrp eflrlnpagk vpvlvdgdlv
       61 ipesaaivly ladkypekal lpvdpalrae ayrwimfavt eleqplwrit rhtflyppek
      121 rspadielar edfatmavil dkhlegrefi vgdsltvadc vtaylidwas echliepfpq
      181 lraylerlya rpkapqriad arkaa
//
LOCUS       WP_175883891             349 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175883891
VERSION     WP_175883891.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 349)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..349
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37226
     Region          29..225
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          257..340
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtynpllliv rpnlamsepl lppipdahdl vselllgmrl sgvqyrriqv arpfglsfgh
       61 gtgraqfhfi vrgpvllrda sgetmrleag daillphggm halvsdpdvp creingfeia
      121 kicdtvasva sagvspatca ttepgagdal ifsacmeldl ggmqplvgtm pafmhvgtll
      181 arypeirpml damereacta ragfagilar ladvvaafiv rgwvecgcgd atgwvqalre
      241 pklgraival hrdpgrnwsv aelateagvs rsvfaerfla atgmtpvryl telrmrlaaq
      301 wiardretie avayrlgygs laafsrafkr vvgkppgavr adgdvpaea
//
LOCUS       WP_175883886             185 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175883886
VERSION     WP_175883886.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..185
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19145
     Region          40..178
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msayplhtid sapaaskpvl qqlqqafgvv pniaaamaas pvlingfigl fervhasslt
       61 epqiqilllt navtnasewp vafhtalalk qgvlsadvda irrgglpada klaalsatar
      121 alidargrls dtdrqafvda gftaeqllev iavvaastit nyvgsvarpa leapfdafaw
      181 hahaa
//
LOCUS       WP_175883915             348 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175883915
VERSION     WP_175883915.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 348)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..348
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38345
     Region          2..325
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mttlaaqata cdalwytrcp vptalgiavh rgwfdeefgp dgialhslqe tldadkresh
       61 fdhslphsfr qggnipalwa rargadtrvi glswtnefqa ivtlpergir tardlrgrrl
      121 glprhpisid fwraaalkgf lsaleleglg ygdaewvdlp dtrerrtgpa sftrgpheyg
      181 leiaalvrgd vdavfvkgva gletvhlida qvvidlgahp dplvrigngt prtltvdral
      241 idarpdlvsr flsvvvgagd waarhpaetv ayigretras dewvryayga dvhrhletgl
      301 aptsidglva fkdflvewgf lehdfdaraw idpapftqid rhrhawva
//
LOCUS       WP_175883917             358 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175883917
VERSION     WP_175883917.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..358
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38618
     Region          <72..335
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mtdrpdsssd kqqtfwyars pvptplgiav hlgwlngets adgvairsrr gatrhdvssi
       61 sdhtlaqsfr qggsipamwa rsndantrvi glswvdesql ilarpesgir svkalrgrri
      121 aipsrpddri difrasalrg fvnalsldgl tlgdvervdv rartlqavgp araaslfasp
      181 qgfssralya aeagallrge vdaiyvkgst gleiaqliga hvvidigfhp ersirnnngt
      241 prpltvnadv lanhpdivag flklvvaage wagthpdeta hyvagetass idwvraaygn
      301 qlhrhlgvnl ddesvaalde fktflhdhgf leadfdvadw idprpladvl rpslqkra
//
LOCUS       WP_175883935             425 aa            linear   BCT 11-JAN-2025
DEFINITION  epoxide hydrolase family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175883935
VERSION     WP_175883935.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..425
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46703
     Region          39..143
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          110..>251
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 msstpfspmr rhllatsvaa gvsamlptal haatgasgir pftahipdea vadlrrriaa
       61 trwpgretva desqgvrlar mqallrywgt dydwrkgear lngfpmfite idgldihfih
      121 vrsrhenamp mimthgwpgs ifellkaigp ltdptahgas addafhvvvp slpgfgfsgr
      181 ptktgwgsdh iarawgelma rlgytrfvsq ggdcgsvish rmamqrvqgl agihvnmpat
      241 vppdiatlla tdapapasls pkekaayekl atfyrdncgy sammvtrpqt vgyaladsps
      301 gqaawmydki sqwtysggvp ersiprdeil ddislywltn tatssaqiyw edhsnnfnav
      361 dislpaaitv fpgeiyqapr swaersyhnl iyfnevdkgg hfaaweepel farevragfr
      421 plrra
//
LOCUS       WP_175883961             315 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175883961
VERSION     WP_175883961.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..315
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34821
     Region          11..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrkfkipnmg alvafeaaar hesfthaake lfltesavsr qiatleaslg vrlfarvkqr
       61 vvltragkly gtqvrrales ldrdtlsiia hgsgggylel avlptfashw lipriksfyd
      121 rtpdvrvnmg srtdlfsfed thfeaaihyg kptwpgtssd ylfgeevvpi cspallngpv
      181 ervedllayp llhsttrpga waqwfethgv edirtmqgvr yelhtmlisa aaaglgvalv
      241 pkffveeqlq qlglvvpcda atvgdsayyl vyptefshsk plesfrswll eqasayaape
      301 laennadeed dedve
//
LOCUS       WP_175884008             336 aa            linear   BCT 11-JAN-2025
DEFINITION  sodium:calcium antiporter [Burkholderia sp. BCC0044].
ACCESSION   WP_175884008
VERSION     WP_175884008.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schnetkamp,P.P.
  TITLE     The SLC24 gene family of Na/Ca(2)-K exchangers: from sight and
            smell to memory consolidation and skin pigmentation
  JOURNAL   Mol Aspects Med 34 (2-3), 455-464 (2013)
   PUBMED   23506883
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Besserer,G.M., Nicoll,D.A., Abramson,J. and Philipson,K.D.
  TITLE     Characterization and purification of a Na+/Ca2+ exchanger from an
            archaebacterium
  JOURNAL   J Biol Chem 287 (11), 8652-8659 (2012)
   PUBMED   22287543
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..336
                     /product="sodium:calcium antiporter"
                     /GO_function="GO:0008273 - calcium, potassium:sodium
                     antiporter activity [Evidence IEA]"
                     /GO_process="GO:0006874 - intracellular calcium ion
                     homeostasis [Evidence IEA]"
                     /calculated_mol_wt=35277
     Region          19..332
                     /region_name="ECM27"
                     /note="Ca2+/Na+ antiporter [Inorganic ion transport and
                     metabolism]; COG0530"
                     /db_xref="CDD:440296"
ORIGIN      
        1 mtfmfvelaf mlivilvaae iftnalehlg erlkisegvt gslfaavgta lpetmvplla
       61 laggtssqav neeigvgail gaplmlatlt tflmalavir srglrgtiap ertgfvrdmn
      121 tflaafslat vamfvphhnw avrallaaml vglyvmyvvl tfrastglvd aghgteapha
      181 mllsriglpt nlativlqll igvallvgga kgfihgvegv shvlgvsall lsliivpiat
      241 elpekvnsvl wirrkkdtla fgnitgamvf qgtllpaigi mltpweprpe vltgviitla
      301 aaawlrvnar trglaiwall angagyagyl altltr
//
LOCUS       WP_175884018             294 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175884018
VERSION     WP_175884018.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..294
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32041
     Region          111..271
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mllnvnsfhr dddrfnvsfk algelietvg tphfvprltq llndivpldv ahversrvdg
       61 tmptgyrcew igssgigaas teisdvmtly yerfldsdpl faglrgktgt mlvvrdiaai
      121 ppgefrqrlf ddvhighecv largtrysqh sialergrdr ppftlaemnr frsisdmlfp
      181 llelhastta arriahatpd vhplaqfdar laadgvklsk reyetckhll sgktvpetag
      241 ilgvrvasae syvkrafakl gvrtkrelaa wgsataalpa agspdggapp aipr
//
LOCUS       WP_175884042             335 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175884042
VERSION     WP_175884042.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..335
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=36057
     Region          172..335
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mknfvpllrh igvgmllamg lhgtaqaick wsspngahst sytvmpsrsi tlqrvpvgqr
       61 maimklapnl lpadkyyicd ndfvnyrldt snlapsgypn vwktsipgig vtlamqrydn
      121 aaieylpfsf qsgpnsehsn fpnlslvfvr igvgvvsgeq eisfkaslda pglpkvtlnv
      181 gparvnivnd vyfescsvvd kavtvqmgqe qierikrgta tehpfgfdvr clglkpnaag
      241 gsvrvyfegn avsdgllrls stgtnaatgm gialvndsgv klpfskaral plkwnrsepe
      301 gemyrfsgta kyaptsgtik pgeadavmnf vieyn
//
LOCUS       WP_175884096             214 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator transcription factor [Burkholderia sp. BCC0044].
ACCESSION   WP_175884096
VERSION     WP_175884096.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..214
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22903
     Region          15..208
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mndslqsasm raasvvaivd ddeavrdgla lllrtvgvpt rcyadasafl adaddaalgc
       61 vlldirmpgm sgldaldelr arrdlpvivm tghgnvdacr rafkrgaldf lrkpvdddel
      121 idtvqqalrr qaaqrgqdda dqtraarlat lstrerevld givrggsnke iaralglspr
      181 tvetyranvf dklraaslve lvrdyaalag gspp
//
LOCUS       WP_175884089             288 aa            linear   BCT 11-JAN-2025
DEFINITION  ion transporter [Burkholderia sp. BCC0044].
ACCESSION   WP_175884089
VERSION     WP_175884089.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11997982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..288
                     /product="ion transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0034702 - monoatomic ion channel complex
                     [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30952
     Region          29..234
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
ORIGIN      
        1 misliqssfd tareavthva rrpsflrkld iavlalivas vlvvmadsvq elhqqyghal
       61 yaaewaftll fsaeyllrlc tarkpaayar sffgivdlvs vlptylafff pglhalidvr
      121 llrllrvfri lglsiyleeg qmliraltra rrkifvfigg mfvlvvilgt viflvegpeh
      181 gitsipvgvy waavtmsttg ygdltpvtpl grlitscail lgygiiafpt gimgaelvas
      241 alernranar padgdgpccp hcggalpveg gadthahgsa lakgrdar
//
LOCUS       WP_175884097             482 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Burkholderia sp. BCC0044].
ACCESSION   WP_175884097
VERSION     WP_175884097.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 482)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 482)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..482
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=52202
     Region          <250..478
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mkpsfriaal aawlalslag tafvisravs daygrffqds sitirllaqk aaqheailat
       61 lgasslaapp ahmldnlrer mpqldglayw rpgvgwqtdg gpapdalpqq rpgkpftlaf
      121 dgpaaywlia gtgwavrvdp rrmlqpgdws taissaalel rdrrvellqr msgdatplwt
      181 mhlekhlpaq pqafvlrttr tltaadlpwl pialwnavaa llaagalgaw rlrearrred
      241 ararldrfgr ldtfgemaag lahelnqplt aivshtraae rlldqpaerd svrralqtsv
      301 aqakraaail ermrdavtta hggerrpldp daimntllfl yrddcarehi algwhnaaar
      361 erpfaepiav eqilhnliqn ardalagagv gvgtsrgeir isgarvgrly rfsvtdngpg
      421 vpedalprlf epffttrarg lglglplcdt laqrqdgtlt vrnlpsggve aalllplage
      481 aa
//
LOCUS       WP_175884103             236 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175884103
VERSION     WP_175884103.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..236
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24873
     Region          132..233
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(135..136,169..170,173,177..178,181,223,227)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mtmktlllra asigaiamal gacttqsgvt ydiravsipg kpdnvfrvsc dgllgsanac
       61 araaeefcqg kgftplemid nvysrapkkd preitfmcgk pqpapvaapv aqpqpqpvpv
      121 pqrqvllqgd anfaldsavl tpqarsnldr fievnrgvef rrvtvtgftd stgsathnla
      181 lsasrarnam nylsanglka qsfvsqgqga aepvasnata egraqnrrve vridaq
//
LOCUS       WP_175884196             429 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175884196
VERSION     WP_175884196.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..429
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46458
     Region          22..415
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mirlnksaal pvvgltgfet plseeesaiq htvhrfardv lrpigreldr mtaedviapg
       61 spywaaives aklgldpqli aqfppetavr iesligeelg wgdaglavsi gaatmplmma
      121 htvgnaelve mctgkvgcwm ntqpdrgsda ailyrqelag ngrqpvgnvt akvgadeivi
      181 ngqssawisn gsvaqvalay maadygdgfy gegersaftn giamilpldl pgvsrgkpld
      241 kigqrslpqg eiyfdnvkvp krfavalkdd ylgnlastws yagthmcqmf vgaaraafel
      301 alaycherkq ggallmdhqm thlrigemlr rlemaraiar rslafsrmsp qshpyataqa
      361 kvsvteeamk iaheafqlfg gngttrefpi eklfrdvrsa liedgenyvl asrlgvlagq
      421 lyengwtre
//
LOCUS       WP_175884202             223 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia sp. BCC0044].
ACCESSION   WP_175884202
VERSION     WP_175884202.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 223)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 223)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..223
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23295
     Region          <57..130
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          130..222
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mkrtwmigaa lviagvaaag tlygpdlvdg mhyqkamaai geadktsgga wpqpqetcff
       61 chgahgqsqn awypslsgqp aryiaaqlra fatdqrrnay mgplsreldd akiaalatyf
      121 arqaparnea vptdaaldkr glalvearsc rachgaaltg kdpaprlagq gqlyleaqla
      181 afrsgerhdp tgamnalaat lsgddtrava hylaglspdg aak
//
LOCUS       WP_175884285             205 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0044].
ACCESSION   WP_175884285
VERSION     WP_175884285.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..205
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22235
     Region          4..194
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mefltlsalp agmlfalvts itpgpnntml lasgvnfgfr rtmphlfgis igvailmlcv
       61 gfglgeafkr lpllytilea asvayllyla wrigtsgevk ahgakprpmt fieaaafqwv
      121 npkawmmvlt aattirlsad yglnaawmsv vfiligfpci clwaafglgl rrflsnpral
      181 rlfnvtmavl lilslyplva hllpq
//
LOCUS       WP_175884294             155 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175884294
VERSION     WP_175884294.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..155
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16274
     Region          1..144
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mykrilvavd gsdtsrhafd aalalakahg aelqpfyvve naaiyynvpg ydpsvlrdql
       61 vaqgntlaqd fasrmqaagv kgetrlneat slndvsslil dgakafgadl lvlgthgrrg
      121 frrlvlgsia eqcvrhatlp vllipaaasa depaa
//
LOCUS       WP_175884353             663 aa            linear   BCT 11-JAN-2025
DEFINITION  beta-galactosidase [Burkholderia sp. BCC0044].
ACCESSION   WP_175884353
VERSION     WP_175884353.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 663)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 663)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 663)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448998
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..663
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=74083
     Region          1..622
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
ORIGIN      
        1 mrlgvcyype hwpesmwadd arrmkalgid qvriaefaws riepspgeyd wgwldravdv
       61 lgaagleivm ctptatppkw lvdrhpdila igadglprkf gsrrhydfss ptyleasrqi
      121 ctavaerygr hpavrywqtd nelgchqtvv syspaalvrf rewlkarygt idalnrawgt
      181 vfwsmeyrhf devdapvgtv teahpshrld yrrfasdela ryhrmqvdvi rahspgrpva
      241 hnfmqlftef dhyevardld latwdsyplg aleelwfapd vkarwlrtgh pdfasfnhdl
      301 yrgmsklpfw vmeqqpgpvn wahwnpaplp gmvrlwswea fahgagcvsy frwrqapfaq
      361 eqmhaglntp dnqldeggre aqrvaqeiaa vldadadada ngsvrapval vfdyeakwlf
      421 evqpqgadfh yprfafeyys alrslgldvd ivsahaqldg yrlvvvpplp ivpddfasrl
      481 aasgahvvfg prtgsktadl qippalppgp lasilpvrvw rveslrpnvt eridgtlrdg
      541 splagearhw rdlvelndda ssvvrarfad ghpacvshga lhywaalfdd attarlfadi
      601 aaeaglaptp lgdavrvsrr ggltyvfnya saphtvdavp psafvvgaaq vepqgvavyr
      661 srs
//
LOCUS       WP_175884354             382 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175884354
VERSION     WP_175884354.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..382
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41014
     Region          1..370
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masismrrvq kaygehapvi rdvdleigah efcvflgpsg cgkstllrmi agledlsage
       61 lsidgrrvdd vpaaergvam vfqsyalfph mtvyenmafg lklarvpkae idrkvrdaar
      121 ilqldtller kpkalsggqr qrvaigraiv repgvflfde plsnldaalr gqtrveiakl
      181 hrqferasvv yvthdqteam tladkivllh agadtaqhgs iaqvgapldl yhhpasrfva
      241 gfigsprmnf lpavvtacda rrttvtlvps getfvlprdg salsagaavt lgirpehlml
      301 gaapdattla rdvalverlg eqtyvhldqp ggtpliakvp gdaqvrtger vhvhapaaac
      361 hlftedgrav paradlpvhh ya
//
LOCUS       WP_175884356             235 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175884356
VERSION     WP_175884356.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..235
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25284
     Region          25..210
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mkktvktgaa tasgtararr qtqaershat rerviaaais llhkegysga ttlairread
       61 vsmgalqhqf ptkaelmaav qerltgdrfa qferasrsat tpleridrml dvagaligtp
      121 lfaasmeiql arradkelde avtrilqpfd egfrtlmrev vagfdratal kitqlqllgg
      181 smirgltidv vtggdpaaar aafalwrdia lgqitdvtqs paqaptktgk rrasr
//
LOCUS       WP_175884364             309 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175884364
VERSION     WP_175884364.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..309
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33316
     Region          2..256
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msnpvslgvv gigkiardqh lpaiaaepgf altacasrha evngvrnypd lnallaaepe
       61 ldavslcapp qvryaqaraa leagkhvmle kppgatlgev aaldalarer gltlfatwhs
      121 rcasavepar awlatrtira vqvrwkedvr rwhpgqqwiw epgglgvfdp ginalsivtr
      181 ilprelvlre atlivpsdaq mpiaaeldca dtdgvpvrae fdwrhgpveq weiavdtadg
      241 vlaisrggaq lsiagepvei gpereypaly ahfhaliarg esdvdvrplr lvadaflfgr
      301 rvqtdafgr
//
LOCUS       WP_175884395             234 aa            linear   BCT 11-JAN-2025
DEFINITION  MOSC domain-containing protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175884395
VERSION     WP_175884395.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12233312
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..234
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25809
     Region          30..183
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
     Region          180..219
                     /region_name="3-alpha"
                     /note="3-alpha domain; pfam03475"
                     /db_xref="CDD:460938"
ORIGIN      
        1 msddtrpaia aavdavrigt srplagtpha saidkqpada rlwlgalgfa gdeqadarhh
       61 ggadkavhhy ahdhypwwag qigardvlar pgafgenlst rgitehdvcl gdvftlggav
      121 lqvsqsrqpc wklnarfdhp rmaalvqdsg rtgwyyrvlq egwvaagdvl alharrypqw
      181 plstvldvly rrtldmaald alcdvpllpp gwrkmlekrr ierqvedwtk rleg
//
LOCUS       WP_175884402             251 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia sp. BCC0044].
ACCESSION   WP_175884402
VERSION     WP_175884402.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 251)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..251
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26278
     Region          2..202
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mkivviggtg ligskvvrnl iarghdavaa apstgvdtit gagldhalag aevvvdlans
       61 psfeeaavra ffeasgrnlf aaeraagvrh hvalsvvgtd rlqqsayfrg kiiqenlire
      121 agvpytivrs tqffefvgai aqagaqgdtv rlttahfqpi asddvaaavt dfaldaprng
      181 iaeiggperv riadlverfl sathdarkvt rdagadyfga vlqddtlvpa pgarlgtttf
      241 dawfrqnala r
//
LOCUS       WP_175884403             334 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175884403
VERSION     WP_175884403.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13300132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..334
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37333
     Region          29..>163
                     /region_name="PRK11242"
                     /note="DNA-binding transcriptional regulator CynR;
                     Provisional"
                     /db_xref="CDD:183051"
     Region          112..309
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(122,126,165,179,181,244,261,288)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(123..124,128..129,131..132,135,139,141..147,208,
                     238..242,249..250,253)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mpdtsirrpd addpfarsfs tcyagvvtfl avvtegsfar aadrlgvgrs svsrhvqrle
       61 drldarlfqr ttrsmsltre gelfyencrp giehlaqale dmrelrsgpp sghlrigstp
      121 gfgrkviapl lrdfharypd itldlllndr padfsadrid vafrdgrmed saivarrlip
      181 mqmivcasps yahrhglprh vddlaqhrci nlctasgrvt ewefridgvt qqrqlaahht
      241 fndidlvvra aldglgiaql payqvcdlla dgrlvsclgq hapddgghyl cylsrkhlpt
      301 rirvfidymi eqtrardlqc lttmttlapl eavd
//
LOCUS       WP_175884444             350 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia sp. BCC0044].
ACCESSION   WP_175884444
VERSION     WP_175884444.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..350
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=36905
     Region          4..350
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mqrkaflvga cvlcttsaha ssvtlygivd syvefdrigs lstlrqsggg sstsrvgltg
       61 vedlgggtst kfvlesgfsp adgsfqggtl fyrqayvslq ntrygdlrlg rqytpafyvv
      121 ydgdpfglne rmsplallat stdtitsntt ppiprfnqaa sylspdwngl rvmatygfpt
      181 pnalstqagr nygaglqyri gglyvgagfq gdtsagnlap vvspsttrhy vfaanyafar
      241 vklyaaflyg vgtaarlpaf stasvgasin vgaldrvlvs vvrrdvkgsa ndatalgvgy
      301 dhplskrtsl yarylymkng gdarntvvag lqpqpggteq vfalgiahrf
//
LOCUS       WP_175884448             254 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175884448
VERSION     WP_175884448.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..254
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27337
     Region          6..247
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 msgnvvksaa rvfevlelfs alqrplsvre iatrcgypgs saaalltsmk tlgylaydds
       61 thayaptarl vnlgealvds aagsrrhwha vakrlaarth eavviavqsd lyvqyidave
      121 gshsipvqfy apigtrreic msglgwalls lqpdstirrl vsrsirrigk sgrtidedvv
      181 ldkveqtrrl gysysahtvt qgaamismvi adgwnglpla mgvagpveri dphrdaivra
      241 mraalaerag dgpr
//
LOCUS       WP_175884459             558 aa            linear   BCT 11-JAN-2025
DEFINITION  alkaline phosphatase family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175884459
VERSION     WP_175884459.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 558)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..558
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=58258
     Region          43..536
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 misrfvkqrn mavmvagala lasagvhaaq qdgnaqgegn grasrvvkhv lllsidglhe
       61 qdlarcigan tcpnlavlak sgvtyanayt pglsdsfpgl aalvtggspk taglfydvsy
      121 drnlyapsdt tcsgkqgwnv vfdettgida qnggallhld gggafnpqai phakvngqcv
      181 pvyphnyvkt ntvfeavkag vpnahtawad khawgydwln gpsgtgvddl mrteinsidp
      241 atntdytdvy shtarfdnlh vqalihqigg rdssgtktap vptlfganfq tlsvaqkapv
      301 akgggyldad ftpngqvana ityvddaigh vvaalkqanl ytstavivta khgqspsdht
      361 klvkngdtlt klleandfld pngnfgqnnt ttgnlndgsg lvgtgfvqtd dvgliwlrdr
      421 sqrtavvqtl kanlgcnapg icadgpqayv lygaaladrf gdpangrtpd ivvqpnpgvi
      481 ytsstkkdee hggnapddsh lgllvsypgi hrartvndlv gtkqvaptil allgadprll
      541 qavvaentrv lpglgigr
//
LOCUS       WP_175884466             219 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175884466
VERSION     WP_175884466.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..219
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24786
     Region          2..207
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mmptlyahpf ssycqkvlta lyengtpfey rvlahddpkp mqeltalwpl krfpvlvdag
       61 rtvieasiii eylglthpgp vrllpddpra alevrtmdrf fdnyvatpqq kvvfdalrpe
      121 aerdargvad aramldtsya wldktmadre waagdrfsla dcgaapflfy adwthridpa
      181 fanviayrqr llarpsfara vdearpyrsf fplgapdrd
//
LOCUS       WP_175884498             203 aa            linear   BCT 11-JAN-2025
DEFINITION  trimeric intracellular cation channel family protein [Burkholderia
            sp. BCC0044].
ACCESSION   WP_175884498
VERSION     WP_175884498.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..203
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=21061
     Region          1..196
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mhtlyliaiv aeamsgalmg mrrgmdrfgl alvgavtalg ggtvrdvllg hyplgwiahp
       61 eylvitlvaa tvaswaarhv armktlfvtv daiglaafti igcdvgastg tapiivvlag
      121 aitgvcggml rdllcnempl ilreelyasv afvtgglyvg mqhvgidagf atlaalaagf
      181 smrmlavrlg wkmrtfgaad veh
//
LOCUS       WP_175884509             315 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175884509
VERSION     WP_175884509.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..315
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33719
     Region          2..315
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhtvavlalp dvvpfdlgva cdtfarvrap dvaqayrvrv cseqprvggd lfelrppfrl
       61 aaladadtim vpgtsvplap tsrrvldalr aaaargcria sicsgafvla eaglldglra
      121 tthwlaaael arrypnvdvd pnvlfvdngr iltsagaaag ldlclhmiqa dygaavavda
      181 arsavaprvr eggqaqfiap ewpaggdglh dlmdwlhanl rqpltldaia rkastsvrtl
      241 trrfqeqtgt spgqwlqtar vrhaqqllev telsiehvat eagfgsvtaf rerfarivgt
      301 spqryrqafr arada
//
LOCUS       WP_175884516             371 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia sp. BCC0044].
ACCESSION   WP_175884516
VERSION     WP_175884516.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..371
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39430
     Region          5..349
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,236,303,323,325..327)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,103,110,183,186,188,236,243,303,323,
                     325..326)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(27,103,183,186,188,326)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mtqdplfqpl rlgaltlpnr ivmppmtrsr asqpgdeane lmaayyaqra saglivsegt
       61 yiaplgkgya wtpgihtpsq vagwrkvtda vhaahgrifa qlwhvgrlsh tsllggqqpv
      121 sssplqakgv nvfvagedgs tpgfvqasep ralsideire ivdqyraaar haieagfdgv
      181 elhgangylv nqfidsnant rtdayggsle nrlrflrevt qaliegtgda srvgirlapl
      241 ttlngcvddd pettylaaak llgelgvgyl hiaeadwdda plmpvafkqq lraafpgvli
      301 yagaytaera reaiaagwad lvafgrpfva npdlperlrt gaaltphdrn tlfgggahgl
      361 tdyptlaeaa a
//
LOCUS       WP_175884573             208 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0044].
ACCESSION   WP_175884573
VERSION     WP_175884573.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..208
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21696
     Region          1..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mphvawlpfm atslliiltp gqdmilvmsr tlsggtragi vtaagvsvgl lvhtmlatlg
       61 lgallqasew lftalkviga lyllylgitl lrssgeltla asgaapasrl rtfaqgalsn
      121 vsnpkvalfy laflpqfvpa gaphpmlslf vlgatfaglt flvkgpvalf agllsasirr
      181 npriltrmhr vsgvvllalg vklalerr
//
LOCUS       WP_175884592             130 aa            linear   BCT 11-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175884592
VERSION     WP_175884592.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10577308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..130
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=13838
     Region          15..>74
                     /region_name="SnoaL_2"
                     /note="SnoaL-like domain; pfam12680"
                     /db_xref="CDD:432716"
ORIGIN      
        1 mntaqtassv hadlidryfd awnepdaarr ralidatyas daayrdplma gdghagidtm
       61 iaavqqrfpa frfrrttdvd afgqhlrfsw alvspdgaai vkgsdfgtvd asgrlasvtg
      121 fidempaaaa
//
LOCUS       WP_175884611             236 aa            linear   BCT 11-JAN-2025
DEFINITION  chemotaxis protein CheW [Burkholderia sp. BCC0044].
ACCESSION   WP_175884611
VERSION     WP_175884611.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..236
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=25106
     Region          79..230
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mnraaatdda tldvddcwnr igtrgdrsce rlndclrcln cpvyashaak llerpldvae
       61 madvtrrmsa lgtaragddd gdtrhaalaf rvadewlalp isvlreiagt rpihslpyrr
      121 hsavrgvvni rgtlriaisi gallgldagk agngggggdg rftrllvaah qgepvvfpvd
      181 evegvlrfga sdwvpvpatv grasaglsrg vlswrgksvg lldddrlfda vtrsmr
//
LOCUS       WP_175884628             233 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175884628
VERSION     WP_175884628.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..233
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25296
     Region          15..175
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mnaphcvtep nilyfgtpvv lvstlnengt anlapissaf wlgwrgvigi aassqttrnl
       61 lrtgecvlnl pssaqadavd riarttgtyp vpdgkrakgy ifepdkfgta gfteaasqtv
      121 appralecpv hmeavvatth gigddmpdlr grirvfevri qrvhahpdll mdgqpdridp
      181 dkwsplimsf qkfyglaprq vhasrladip ehayrspdie rsreagvmig tgr
//
LOCUS       WP_175884677             237 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175884677
VERSION     WP_175884677.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..237
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25971
     Region          6..229
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 msqtsgstit frrpdgqelq gylatparte gapavvviqe wwglndqirg vadrlarcgy
       61 falvpdlyrg kstveeeeah hlmtgldfgd aasqdipgav aylktlaprv avtgycmgga
      121 ltllslqyae adagvtwygf ppldyidpak lkvplmghwa tqdafftidq vdalekkltd
      181 akvgfefhry lahhafanet avgpgriagt qfdpvwseta wdrtltffgr tlwteha
//
LOCUS       WP_175884699             707 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175884699
VERSION     WP_175884699.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..707
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77166
     Region          9..691
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mtypslrdwl fsgktfaasm lalylglyfq lprpywamas vyivsnpfvg atrskalyra
       61 lgtalgaaaa iffvppfvet pllfsiivat wcgtllylai sdrtarsyvf mlagytmpli
      121 alptvtdpst vfdvaiarte eivlgivcas vvgsavfpnr laptliertd awfkdaafyg
      181 retlsghlag kalsacrqrl aatitglefl lsqlgydhah prilaraqal agrmqlflpl
      241 mssladplia lmrdlhvrpp aldvlladaa kwfdaplptv ktgtdgdmah dpvadnlrer
      301 iaalqppdsa laswdgalls nalwrlrqvv diwqdcrslr alianesgvw qpryrhwrlg
      361 gterffdrgm mlfstltvvf aivfacwlwi ssgwhdgaaa vtlvavscsf faaldepapl
      421 vfkfflstaa svvfaglylf vvlphvhdfa mlvlmfagpf iligtllprp qfnmvtmlva
      481 vntatfisiq sayeadffvf lnsnlagvag llfayvwtra trpfgaelav rrllrsgwed
      541 varsastqpl ddqrnhasrm ldrvtqllpr lgasddhrhp siesfrdlri alnaldlrrs
      601 rrrlsgdvpd aidrvlagvt dhyarcaaan arqpvppall atiddalrrv agrnlpgatq
      661 adgvsapavp athrrlrdtl halvglrlsl ypaaaaqapq apdgaha
//
LOCUS       WP_175884737             374 aa            linear   BCT 11-JAN-2025
DEFINITION  Fic family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175884737
VERSION     WP_175884737.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..374
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40994
     Region          23..367
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mmsgdctfiw eaadwpawrf dlpalatpla dvsraqgmlv grladvglal rdeaslaalt
       61 ddvvktsaie genlnvasvr ssiarrlgvd igalapvdrh vegvvdmvld atthsgapvt
      121 darlfgwhaa lfptgysgls ritvggwrtd argpmqvvsg pigrqrvhfe appaprlphe
      181 iarflawlna ppaepllira glahlwfvtl hpfddgngri aralgdlvla radrspqrfy
      241 slsaqiqrer nayydvlert qrgsldvtew lawflntlgr aidhahttld avlikarfwq
      301 rcagvamner qvkvmnrlld gfegkltttk waalakcsqd talrditelv eqrmlrrsas
      361 ggrstsyelv pfdg
//
LOCUS       WP_175884762             238 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0044].
ACCESSION   WP_175884762
VERSION     WP_175884762.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 238)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 238)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 238)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..238
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24660
     Region          29..235
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mtrrtvqlvg slvaiiaagw alargigadt fhqrsddlay yagqhmllva ysmtlaiavg
       61 vpagvllnrp rfqhqaerfm qvfnigntip slavlaialg ifgigdvpai valflasllp
      121 vtrnayegmk nvpaalreaa kgigmtgwqs lvrvelpnal piivggvrta lainvgtapl
      181 ayligadslg slifpgiyld nqpllllgas ltailalald gvvaagsrhw larhggaa
//
LOCUS       WP_175884794             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175884794
VERSION     WP_175884794.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32919
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..295
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,190,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mqnldallif arvaemasft haaeslgiqk grvstviral erdmgvallh rttrrvqlte
       61 dgrafyarat dllaevqelq smfsgrgtsl rgrlrvdmpt elarsvvvpa lpqlmaahpd
      121 lelelsstdr rvdlvregfd cvirlgpiad etliarplgk lrmtnaaspd ylarhgvpht
      181 ladlhsqghr mihytltlga rhpgweypdg dgyawlplps amqvnsvqty haaglagigl
      241 iqagysalah hiesgalvev lpdlrpepla aslvvahrrn lsprvrafmd wiggvlepyl
      301 d
//
LOCUS       WP_175884802             210 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia sp. BCC0044].
ACCESSION   WP_175884802
VERSION     WP_175884802.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..210
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23145
     Region          1..210
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mtrvlyiegs ankaysasie vceafldayr qahpdheirk idiwdlplpe fdgaalaaky
       61 aglggtaltp eqaaawrqie rlaapfhead kflfgvplwn fsiryklkhl idvisqedvl
      121 ftfdaagftg klvgkkaavv yarglayqsp gsftpaaefd lqrpymetwl kfvgvtditg
      181 ivvertlfgp dgkvdrsrai dearaiaptf
//
LOCUS       WP_175884813             185 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter small permease [Burkholderia sp. BCC0044].
ACCESSION   WP_175884813
VERSION     WP_175884813.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 185)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..185
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=19636
     Region          26..180
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mthrtsldsa saaapdgtpp arphaapllr rvndvlfrvl aviasaclav ltvlvfyavv
       61 mryvfenapd fvepialllv iviamfgaam kvrdgghigl dslvrrlspk artvviaiqh
      121 lsliafaimi migcgsmaae tmgdripiig lpegvrylit mpaavaiilf slehllalrr
      181 sssgq
//
LOCUS       WP_175884819             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0044].
ACCESSION   WP_175884819
VERSION     WP_175884819.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..359
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38027
     Region          159..356
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mtkvflilvr nellgylrsr sslfwtlvfp vfllsvmlfa fggsgslgta diafdvpgga
       61 tpynqackaq ivaslshsdt vkatfggrga padrvtvvlg adertpatir ydfngslavk
      121 aasrvveial arcaaqrlgl paaqarfena aptrrpfdyg affatgilvm afmaiglnst
      181 ttaiaalrer ntfklyvcfp vsrgvflaal ivarmammal salvlltvar vafgialpia
      241 tpdglralpi vllgaamvls igvllasrtr slaaaelacn vtyypllffs dltipmhdap
      301 awlkaglafl ptnqfavalr gvlvdgapya qlapqllgmt vctalflfaa arlfrwhda
//
LOCUS       WP_175884843             410 aa            linear   BCT 11-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175884843
VERSION     WP_175884843.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..410
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43326
     Region          5..363
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 minprdsivs lagvvvgqva lfvcifvigr rfgpeslghf nyllalasfa gtllafryel
       61 acvddapges fnalvnvtal svlvaaaggm liaiagrtdf ypvavyalas fvqlaagayl
      121 nslrrygwma lsrivvngaf liglvlslac sacgkvdvfa lyawvtaavs avmagaivln
      181 gyragysfrl spgffvrnrr falyilpstl casvltyala iaiphwfdaq sagyfaaayr
      241 lgffpvslia qsvggvfrrd aigamarpda gsavhlvyrt yaralaglav vylagglllf
      301 aplvdlffga swrgsvgfyh slmplfalql iyvplsqifl atraqrvdfl fqltcgtclv
      361 galgiarltn lsaptsvmif sltgaalmaa gialtyrvld anlsrsaela
//
LOCUS       WP_175884859             201 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia sp. BCC0044].
ACCESSION   WP_175884859
VERSION     WP_175884859.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..201
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20724
     Region          1..190
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mkllhidssi lgqgsvsrel saeivanfra rdpgltvtrl dlaatpighl taghlaaaqg
       61 apvddalkad vetgqralda flaadivvig apmynfgias qlkawidris vagktfryde
      121 ngpvglcggk klvvassrgg vysagspvas fdhqetylrd afgflgitdi tfiraegvam
      181 gpdkrsdaia sakeavaala a
//
LOCUS       WP_175884862             347 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0044].
ACCESSION   WP_175884862
VERSION     WP_175884862.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..347
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34815
     Region          13..301
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtglrtlfrh slawpvltla llfaldvahr pgflsialld ghlfgapidi lnraaplviv
       61 slgmtlviat rgidisvgai vaiagaaaat vleadpsqvg talaaalgvg llagawngll
      121 vafvgmqpii atlilmvagr gvaqlltggq iipigapgyl algggylatv pcavwialat
      181 igatallvnr talglfirai gvnpvatrlv glrsgaivfg vylcsgvmsa lagilassnv
      241 rsadgnnagl lleldailav tlggtsllgg rfslagsvlg aliiqtltyt tysigvppea
      301 tlvvkavvvi vvtliqsdaa rallvrhvsr llpsarsrat ttgatpr
//
LOCUS       WP_175884936             130 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175884936
VERSION     WP_175884936.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..130
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14378
     Region          8..115
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 msatkayleh vaiwvkdihw hirffedvlg mtlrevdgtl daprqywtlg glqfihapeh
       61 egpegrlahl gvmcedleaa laaaqrfdvt empqgrnwir lpdglaveli qarpascvaq
      121 alainpraea
//
LOCUS       WP_175884937             316 aa            linear   BCT 11-JAN-2025
DEFINITION  ketopantoate reductase family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175884937
VERSION     WP_175884937.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..316
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32547
     Region          1..307
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkiailgaga lgcaigatlt qgghetwlid rspahvdtmr rdglrvddag gtrqvrvhat
       61 tqaaevgtad vvvvlvksfh tdaairgals lvgpdtvvls lqnglghedi lsdavgrerv
      121 lagktyvggv lrgpghiesg vigkytyige ldgritprvq aiadafntag lattisdniv
      181 gtmwdkllvn vatgaltglt gltygqlyde pllkatslaa vaeaiaaaqa agvklsmtdp
      241 eqawtlaaeg lpaafktsml qslekgsite idfingsvvr agqrygvptp vnatlvacik
      301 gleramadrq rgeaaa
//
LOCUS       WP_175884938             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175884938
VERSION     WP_175884938.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33999
     Region          <27..72
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          104..302
                     /region_name="PBP2_DntR_NahR_LinR_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators that are involved in
                     the catabolism of dinitrotoluene, naphthalene and
                     gamma-hexachlorohexane; contains the type 2 periplasmic
                     binding fold; cd08459"
                     /db_xref="CDD:176148"
     Site            order(110,112..113,117,174,210,277)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176148"
     Site            order(111,114..115,118..119,122..123,125..126,129..130,
                     132..136,138,200,227..231,234..235,238..239,242,256)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 mdnnatmpad lpdlkllqlf dllydvrsvt rvaeqlgqsq ptvsiwlghl rehlhdplfi
       61 rtpggmaptp qadaligpcr eileslrrft aweiafdpat aqrrfricmt dashvtllpr
      121 llahvraqap gvrleaarid gnteralesg eadlaigyvp wlgggiyqqk lydqdwiclv
      181 nrhhprirgr lgakqyrseg hvaitagtga qlleqalrqa rierdvvlel pgflglgaiv
      241 qttdlittlp rhigetlaqa sdlavhacpi pvegfavrqh wharyhheag nrwlrgvvsr
      301 lfgnsy
//
LOCUS       WP_175884952             347 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175884952
VERSION     WP_175884952.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..347
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38958
     Region          12..194
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(15,17,102)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(49,101..102)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            100..102
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mresiytplv slvvpfyneg eaverffdvv iplmtsidai rfeivcvndg srddtlerlv
       61 rigaaerrvr vidltrnfgk eaaltaglde aagdavipld adlqdppsli pvliehwrdg
      121 aevvaakrsn racdsftkrt aaaiyyrvhn llsdvklpen vgdfrlmdrk vvnalrnlpe
      181 rhrfmkglfa wvgyktvive yqrdprsagh skfsgwklwn falegitsfs tvplrswtyi
      241 gvgiaalafl ygsfiilrtl lfgnpvlgya slisitlfig gieligigvv geyvgriyde
      301 skqrpvylir rryqahgkvi elpvahdtrr qlarrraqpv rarigar
//
LOCUS       WP_175884973             175 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175884973
VERSION     WP_175884973.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..175
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18778
     Region          12..164
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mettvterta ldpmqlraaf gqfptgvtvi ttcaadgrkv gltansfssl sldpplvlws
       61 lrklapsrpd fvaathfain ilahdqidls rrfatpsadk fdgvlhmdse nggvpcldga
      121 sarfvcrnvg hyeggdhllf igeieqfdaf gkaplvfhag qyraiadhpd lsrap
//
LOCUS       WP_175884978             831 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia sp. BCC0044].
ACCESSION   WP_175884978
VERSION     WP_175884978.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 831)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..831
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..831
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=86679
     Region          <55..>200
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          207..751
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mrirtagrpa stdtphsdas pvagtgsprl grrgflkltm aasgclalgi aptraaaeag
       61 kalpssppqa fliiapdntv tvavnrtesg qgvstalpma ladeldadwr nvrtvlapag
      121 epykdpvtgi qmtagstsvn hsfaqyrelg asaramlvaa aaqrwnvdpa tcrtangvvt
      181 sgsyratyge lapaamampv pqrvplkspd qfriigkptp rvdaramldg tlkygmdwrl
      241 pdtmvavvar pprfggkvas ydaaaaravk gvvevveipt drggtgvavi angywpaklg
      301 rdalkitwqd agstvtsaeq mhaykqlagt pgtvvrtada gsappaatri ekdyefpyla
      361 haameplsct vdvgpancac gikiwggssl qttdraavak algvapekvq iftltsggdy
      421 grrstptsdy vveaarvsaa ylaaghlgpv ktiwtreddl rggyyrpmvl hrvdigvdgs
      481 gavrdwqhvv vgqsvlkgsp lerttmlkrg tdpsltegva nspygfpmqv svhqtdadvp
      541 vqswrsgght htafvmetlv delahaarqd pvayrmarla gpehaphrqa lalavdksgy
      601 gtrtlpagha wgvamhetag svvayvtdvs idaqqprvhr vtagvyagri vnptgaeaqi
      661 qggalfglat tkpgfaidvd hgavrnagfa dyppvrmqda ppvdvffvps daqptglsda
      721 gvppiapava ngafvltger lhalpfapml vasaapampa apaaaadedp ygdlpaggcr
      781 iphkvkraal kpktdqshag vgqapavpkf lrpkrragip ciedlkkgtv t
//
LOCUS       WP_175884990             724 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia sp. BCC0044].
ACCESSION   WP_175884990
VERSION     WP_175884990.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..724
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78098
     Region          37..724
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mwmetgtgrr araiaaggaw cvaaaggaha qasapgaava vlpaidvrgp adaspvglvg
       61 rrtatgtktd tpideipqti nlvtaqqidm tgaadlnqal ryvpgfatfg adsrtdwyaa
      121 lrgftptlyv dglpapntav ianwrvdpyt idsiavlrgp tsvlygagep gaivdahtkl
      181 adgervreag vqigndarkq tmldvgdrld pdgrtayrfv gvardgnavt gpngdrrval
      241 apsfrwrpna dtsltvsatf lqdsgdissn flpasgtvlp npngrlsqdl ymgdpsfndy
      301 rkkqwslgya lehrvnaiwt lhqdvrwshl slddatvfgn glvprsttnm mrfaglfqln
      361 ysrldidnha qarfgtgple htllfgvqfd rqtttnsvwl alapslnlyh pvyrpvtaai
      421 fsgptslghv dqytamntvg vyaqdqirwq rwtltlggre dvvnarfddr tagthaqqdv
      481 safsgrvglt yrgdagwspy vsystsfdpv igvrmfgggl pkptrgaqte aglrweppgr
      541 nlmlnaavyq idqtnvvtpt pinldptgtt svqtgkvrsr gielsavgkv trelsivasy
      601 ayqdvknvqa ndvslnhwpv svplprqmas mwadwtwrtg alaglgvggg vryqsasaga
      661 pdnsltvpsa tlydlaihye lprwhfavnv anlfdrryvs gcqsyavcvf gnertvlasa
      721 kynw
//
LOCUS       WP_175884986             656 aa            linear   BCT 11-JAN-2025
DEFINITION  beta-galactosidase [Burkholderia sp. BCC0044].
ACCESSION   WP_175884986
VERSION     WP_175884986.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 656)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448998
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..656
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73139
     Region          1..606
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
ORIGIN      
        1 mhlgvcyype hwpreqwdrd arrmaelglt rvriaefaws rmepepgryd wawldeaidt
       61 larqqlkivl gtptaappkw lvdrhpemlp vgadgavwqf gsrrhydias pvyrehcvri
      121 adamarryga hpaviawqtd nelgchntlp sytraalegf rawlavrygd igalnrawgn
      181 vfwsmeyrgf deielprhtp tdanpahlld frryqsdeva rfhavqvdai rphapgrdvl
      241 hnfmgfytef dhyafarggl dvaawdsypv prtevlplde adkqrwartg hpdvsafshd
      301 lyrgvgngrm wvmeqqagpv nwgpynpvph agavrlwtwe afahgaelvs yfrwrqypha
      361 qeqlhsglna pddrlspggh evarvareia aldpalvage rgtarvallf dyeadwmiri
      421 qphgadfdyq qhaldwyral relgldvdiv aagadvsrya lvvaptlpvv tdriveqaas
      481 ghahwlfgpr tgsrtaefai apglapgtlr dvlpvrigqv eslrpslapr vsfdgvdgha
      541 lkwrdhvdmd aapgvdvlaa cddgvpalvr rgpvtmatac fdrtllraii arcardaglq
      601 vcalpdgvrl rrrgrvtfaf nyggtpcmlp apagtrfvlg srdlgavdva awvaad
//
LOCUS       WP_175885010             371 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175885010
VERSION     WP_175885010.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..371
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38748
     Region          18..>224
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mgtpdtgrlt apaldaslad wldanatqld tsaalkadiv prlaaaglfr tgvpaslgga
       61 ggtiadaiag iaavaehslt aafvlwgqrs fieyllqspn nalrerwlpa lldgrsagas
      121 glsnamkyls gieslqidat phaeraddwr mtgrmawvtn lraerfvvaa avafddgrps
      181 aivaipddap gltrstdldl ialrgsntaa lhldrvpsda awlihpdaqt flpavrpafl
      241 glqcglsigl arralaearr aaettrgilg pevetcaael aaacahlssg ladgslrlhp
      301 nrlfelrial athvatavnl eleasggrgy lrdaglgfer rwreaafipi vtpsvvqlka
      361 qlaaqarsia a
//
LOCUS       WP_175885016             144 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175885016
VERSION     WP_175885016.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..144
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=15731
     Region          42..144
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mthltrydpf siepvsdlfq glfrplrgma ttdepdlasm kidvtesdda ykvnaelpgv
       61 akedidvqvt grtvtinakv ersnerkdge rvirrerysg aigrsfslsg eiddanatat
      121 yqdgvlsltl pkkapvgqkk ltis
//
LOCUS       WP_175885048             403 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar ABC transporter permease [Burkholderia sp. BCC0044].
ACCESSION   WP_175885048
VERSION     WP_175885048.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..403
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42316
     Region          26..403
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mnselssstp aapdadarrp dgrtprlalr hvftrykvla llfavvaiwa ffsvltdgaf
       61 vtprnvsnll rqmsitgmla cgmvfviiag eidlsvgsll gllggvaail dvnrhwpvaa
      121 tvpavlalgv liglfngwws tyrrvpsfiv glggmlafrg illgvtggst iapvsdgfvf
      181 igqgylprla gdglavllfv vatllvvrqr gtrrryrlav aplwqdvaki vgagavlfaf
      241 vatldryggi pvpvllllvl lgvfswiatq tvfgrriyav gsnleatrls gvdtdrvklv
      301 ifalmgamca faglvntarl aagspsagsm geldaiaacf iggtsmrggs gtvygaliga
      361 lvmasldngm smldvdaywq mivkgavlvl avwidvvsrs nrr
//
LOCUS       WP_175885079             448 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0044].
ACCESSION   WP_175885079
VERSION     WP_175885079.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..448
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48387
     Region          27..437
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(40..41,44..45,48,80,139..140,142..144,147,167,
                     170..171,174,268,271..272,275..277,280,308,312,363..364,
                     368,372,388,391..392,395..396,399)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mpsitqaaaa paaadsseda lyrkvmrril pllllcyvva yldrvnvgfa klqmlddlsl
       61 sdgvyalgas iffwgyflfe mpsnlllhry garfwiarim itwgivsssm afivplaqff
      121 hvqtttmfyt lrfllglcea gffpgvilym nywfparrqs vamsgflvai plsltlgsvl
      181 sgwlmeqthg lsgmsgwqwm llleglpsiv vafivlaclg dgpqsakwls adekavlsrn
      241 leseaahksh sigaalrspr vwlltfillt fntgfyglaf wlpsiirasg vhsplhigvl
      301 taipyltaif amvwnashsr ktgerrlhaa ipaliggvfl ilsaafahnv aisivfltia
      361 tcgilalmpi ywtfpgqils gtaaaagial insvgnlsgf tgsmitgvak qmtgninngt
      421 yalgacllvs cvliaaiprd ilrppvgr
//
LOCUS       WP_175885103             287 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia sp. BCC0044].
ACCESSION   WP_175885103
VERSION     WP_175885103.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..287
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=31003
     Region          2..213
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mtilvtgatg rigrqlvrql vdrgadvrvl vrdpakadfp aavtvaqgdm ldvdalraaf
       61 sgvrtlflln gvagdeftqa lialnlarea gvervvylsv lhadrfvnvp hfavksgaer
      121 mieqtgfsat ilrasyfmdn damvkdvivg hgvypipigg kgvamidvrd iaevaaieli
      181 rrndapatlp vdtinlvgpd tltgaqlasi wsdtlgrpva yggddptpfe dnfakfmpkw
      241 mayemrlmae ryvsdgmvpe agdverltai lgrplrtyrd fvaalvr
//
LOCUS       WP_175885121             295 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            sp. BCC0044].
ACCESSION   WP_175885121
VERSION     WP_175885121.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..295
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30465
     Region          2..294
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mssfvihllt vgclyatmal glnlqagyag lvnfgfiafs glgayaagia sqlgwplpsa
       61 lalalaaaga laivvarlgr qlsadywgia tlaiaeilrt ialneswltg gaqgiggiap
      121 lfpglrapwa dlaflavtag claltyatyr rltasrfgra lkvmreepal avcfgydpla
      181 lktraciaga lpaalagala awyigyvgpd amiasetfal wtvvmvgglg shlgvlvgtl
      241 ivqavyalap flkdwldvgs dltgavrlgl vglmllacvl wrphglvper levrp
//
LOCUS       WP_175885122             297 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            sp. BCC0044].
ACCESSION   WP_175885122
VERSION     WP_175885122.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 297)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..297
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30508
     Region          1..296
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mlsfivdvli rtadlllvsv glstlyslir fpniahvqya mlgafatlwl eraglpfala
       61 tvvscalvgt aatllnlfvf arllrsgsav amigslaism lavalvlgla gsrpqqyaqd
      121 vhppmviagv alsvpqlssi acgagalaif aallyrtglg ramralasnr alalatgida
      181 trvtnvitfa sgvlaalggt mlgatesvhv nlgygllipv fsaailgglg nplgaaagal
      241 liavaetval nvdfgglvdr pmqffpveyv gavsfaillv alifrpygif drevrrv
//
LOCUS       WP_175885136             123 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175885136
VERSION     WP_175885136.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..123
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=12790
     Region          3..>123
                     /region_name="PRK10568"
                     /note="molecular chaperone OsmY"
                     /db_xref="CDD:182556"
     Region          56..>115
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mklrsmiasa gvvalmsvtc yaqsdtpdtq takppttssr sakkaerlen rkfakrvrqa
       61 ivkapgigna qvtvfakakt gevtlagmit deaqnkaave aarqvpgvts vtsklglrme
      121 ggq
//
LOCUS       WP_175885174             353 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0044].
ACCESSION   WP_175885174
VERSION     WP_175885174.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..353
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36119
     Region          18..348
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mkpvtsssav hqaasverss rpvparirda lertgillvl ailvvvfalk epaflnvdnl
       61 fsilqavsiv allgigvtit laaggfdlsv gsvaataqma asyvlvvwhg sawaavlacv
      121 vlgvaaglfn gllitrlrvp dqlatlgtlf llaglqlipt ggrslatgsv lpdgtdatgv
      181 fpdaflalgr lrvfdvvplp vlllaavtvl acvtmeatrw grviyaiggn etaarlagap
      241 aaryriaayv vsgaiaslgg vliaarvgrg dvsaghslll davaaaligy avwgakrpnv
      301 fgtvvgavfv gvllngltml napyymqdfi kgvllvlala ftfgigrrtd ara
//
LOCUS       WP_175885200             157 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia sp. BCC0044].
ACCESSION   WP_175885200
VERSION     WP_175885200.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 157)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..157
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=16993
     Region          22..139
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04667"
                     /db_xref="CDD:467552"
ORIGIN      
        1 mtlpdpsdfp vravplapla kerativclr nrrvllvarg rssrwtlpgg virrgesald
       61 aahrelleet gladlelayf fyvdgsvkrh hvfvaslprg ahacpgreia lcrwvgidav
      121 phwpasaptq riirqfaglc aasdlppgav trlsssr
//
LOCUS       WP_175885213             205 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175885213
VERSION     WP_175885213.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22919
     Region          18..172
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkkidpspap argpadhdvr dqivaaateh fsrygyektt vsdlakaigf skayiykffe
       61 skqaigemic anclreietd vraavtaael pteklrrmfr vsteaslrlf fhdrklydia
      121 asaatenwqs vqgyearvqt llrdvlqegr qngeferktp ldetataiyl vmrpylnpll
      181 lqynldttda apaqlsslvl rslap
//
LOCUS       WP_175885303             949 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175885303
VERSION     WP_175885303.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 949)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 949)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 949)
  AUTHORS   Ingmer,H., Vogensen,F.K., Hammer,K. and Kilstrup,M.
  TITLE     Disruption and analysis of the clpB, clpC, and clpE genes in
            Lactococcus lactis: ClpE, a new Clp family in gram-positive
            bacteria
  JOURNAL   J Bacteriol 181 (7), 2075-2083 (1999)
   PUBMED   10094684
REFERENCE   4  (residues 1 to 949)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11909043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..949
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..949
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103579
     Region          4..>54
                     /region_name="McsA"
                     /note="Protein-arginine kinase activator protein McsA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3880"
                     /db_xref="CDD:443088"
     Region          83..877
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mpalcdicha rpavaratvm qdgerktisi cdyhfrqlmr hqsmlnpfds llggggpssl
       61 fgglgddspl aaeipresvd ptdafseqtl ellqraaeka helrrselds ehllyaladt
      121 dvcaallkel klspediksy idahahtgta dpdapldkls isprvkkavq yafqasrdlg
      181 hsyigpehll iglasvpdsv agtllkkygv tpealrqkvv kvvgkgaedg rvdaptgtpn
      241 ldkfgrdlta iarqgkldpv lgraqeiest ievlarrkkn npvligepgv gktaivegla
      301 qrivngdvpe vlrdkrlvev ninsmvagak yrgefeerak qlidevtakq delilfidel
      361 htivgagqgg geggldianv lkpalargel sligattlne yqkyiekdaa lerrfqpvfv
      421 pepsveqtiv ilrglrdsle ahhqvtfadd afvaaaefad ryitsrflpd kaidlidqaa
      481 arvrigatsr pvdiqegeaq iaqlkreqdy atsrkrfdea kqfeeqinak qtavdemmea
      541 wqrktgsetl evtvesvaev vsrltgipvs eltqeerqkl lkmeeqlrer vvgqsdavva
      601 vsdavrlsra glgqthrpia tflflgptgv gktelakala etvfgdeqai iridmseyme
      661 rhavarliga ppgyvgydeg gqltervrrr pysvilldei ekahpdvynv llqvfddgrl
      721 tdgkgrvvdf sntiiiatsn lgaaiimdnl tqpeaarktd kaireelmqv lkghfrpefl
      781 nridevivfh alskenirai vqiqldrvvr taaaqditlv mgdslvahlt eagyqpefga
      841 relkrqirqt ietrlakeil adrlksgdkc evdydkdsde vtfntlaape akeakdtkda
      901 kdadgkakpn gkaakaaada ksddapadap ppaakpsgkk ssgakkdah
//
LOCUS       WP_175885309             145 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175885309
VERSION     WP_175885309.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..145
                     /product="RidA family protein"
                     /calculated_mol_wt=16112
     Region          28..137
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 msqpthtrir mfntkdtypn qtldndlcqa vragntvyvr gqvgtdfdgn liglgdpraq
       61 aeqamknvkq lleeagsdit hivktttyli dpryrepvyq evgkwlkgvy pistglvvsa
      121 lgqpqwlmei dviavipdnr qpnra
//
LOCUS       WP_175885324             466 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Burkholderia sp. BCC0044].
ACCESSION   WP_175885324
VERSION     WP_175885324.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..466
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51713
     Region          4..440
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 meifdafhla rlqfaftvsf hivfpaisig masflavlew rylvtgdaay ksmfqfwski
       61 faigfgmgvv sgvvmayefg tnwsgfsrva gnitgpllty evltafflea gflgvmlfgw
      121 qrvsprahff atlmvavgtl istfwilasn sfmqtpqgyk ienglvvpvd wfkivfnpsf
      181 pyrlvhmtia afivagfiva acgawhllkg rrdepvkrsf smalwmllvl apiqivvgda
      241 hglntreyqp akiaaieglw etekggtaln lvglpdmqae ttryaiqvph lgslilthsw
      301 dgeirglkef apqdrpyspi ifwtfrimag lgmlmlltal lglllrkggr lyetrwfqwf
      361 vvamgpsgiv allagwitte vgrqpwtvyg vlrtidsvsp ltaqqvgvsl lvfvvvyflv
      421 fgtgiyymmk lmkrgpaaqa gyielhrhpg lrksalstpl nvteae
//
LOCUS       WP_175885328             243 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175885328
VERSION     WP_175885328.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..243
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27007
     Region          1..241
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mnrphfaeia rdltegiasg rfpvgsylpt elelrdlykt srhtvraalh elqqlgfvsr
       61 rknagtrves aqpkndfrps lasiedlvqf gsenlrvvqs ieelaaegal akvlkceega
      121 rwlrisslrv erdatrppig wtdvyidpgy leiaetarhe pdtlisalie arygrcvaei
      181 qqnvqavnvs pemaarlrip agtaaleivr ryldstgvaf eisisihpae rfsvsmrlkr
      241 ses
//
LOCUS       WP_175885369             370 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia sp. BCC0044].
ACCESSION   WP_175885369
VERSION     WP_175885369.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..370
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39149
     Region          4..344
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,233,300,320,322..324)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,181,184,186,233,240,300,320,
                     322..323)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,181,184,186,323)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            186
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mssllsaydl rglalpnrvv mgpmtrsrap srglptelma eyyaqrasag livteatnvs
       61 pasaafeltp glvddaqaaa wkivtdavha nggrifaqlw hggrvssltl lggaaplsps
      121 gvnddleqlq vwaqlqngyy tkihatpsra mttdevvaav defrqaaara maagfdgvei
      181 haangylphq flsstlnrrd dryggsvanr arfledivda vggvmplnrv gvrispyaky
      241 nnvrdadpda tlayvgrmld aagiaylhaa dtngwsgepd lpriveharr sfhgtlivng
      301 gispeaanal idagdadlva farayianpd lveriaarap laepkaagwy ggdragyvdy
      361 arhdaaqspa
//
LOCUS       WP_175885371             636 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia sp. BCC0044].
ACCESSION   WP_175885371
VERSION     WP_175885371.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..636
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=67569
     Region          5..543
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mlratepars adlvvfngki atqdeqrsfv ralavkdgti vatgddrdvl rhahdhttri
       61 dlngrtvipg lidahlqair ggmnfnlevr wdgvpslada ldllgrqvrr tpapqwarva
      121 ggwtalqfae krgptaaeln aiapdtpvfi qhladsawln aaalralgyg rdtpdppgge
      181 lrrdrhgrpt glllarpdpa vlvaalarap gldaadrvns trqfmralnr vgvtsaidag
      241 gdglaypddy aavatlarrg elttriayal garhagreld dfakwialta pgrgdaflra
      301 sgagerllfs avdlgnflep rvdlpasida elaaivrllv rhrwpfrlha tydesigrfl
      361 dvfeavdrdt pfdglrwcfd rcetisdani arvaalgggi tvqprmafqg eafiarhgaa
      421 aamrappira mlaaglpvga gsgataaasy npfvalywmv sgrsvggtal yparnrlgrm
      481 ealrrytvgs awfsadehrk galvpgryad favlsddyft vdarripals svltvvdgkv
      541 vhaeqefspl apppspvspa wspvaagvdd asgvggpgtd ardsahasaa gdacaapgid
      601 acrarghgrr farpryptat aaaerceafg rccvaf
//
LOCUS       WP_175885375             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175885375
VERSION     WP_175885375.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32160
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdkfsalraf vevaeaggfs sagrrldlaa ssvvravdal easlgtvlln rttrqvtlsd
       61 agavyyarak rvlgeladad alvadrgdap sgplrvsvpv ayglrriaph vaafvarhpk
      121 ldldlqltde rvdlvsarid vairlgdaap tadvvarplg tfrryvvasr ayldahgtpa
      181 tpgelvdhac lrfhfgvdqq twtfagaqrt tqvvvtgrlk snhsevlrea aldgagiall
      241 pdwlvdadle agrlqrlfdp ydvtpgsara vitalylpnq rgskrvtafi dfveslarar
      301 p
//
LOCUS       WP_175885377             317 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175885377
VERSION     WP_175885377.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..317
                     /product="VOC family protein"
                     /calculated_mol_wt=33943
     Region          <241..301
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 msslklrnll rmtaassaml aallagtpaf adethlddia spaaaarspa iavgpqydtt
       61 hvcvapedfd rftdsfvatf ggkkskqgvf qvtptpsqtm sqlvltpvgt isvfgfktpi
      121 pypfceertg ylvtdmdvav ksarahgadi vvttfpdpig rdaivrwpgg vnmqlywhtq
      181 apnydalqtv penrvyvspe sagklarnfa afshgkivsd vrhapgieig rpndtyrrir
      241 iesgfgkmtv latdghlpyp fgremtgyev adlaatlkqa eaagvtvlvp pfksdgrdaa
      301 lvqfpggyva eiharsk
//
LOCUS       WP_175885381             245 aa            linear   BCT 11-JAN-2025
DEFINITION  YoaK family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175885381
VERSION     WP_175885381.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..245
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24955
     Region          22..>176
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mqpaqvtaag aaapdhlrge dvflasiagy vdtlgfvalf glftahvtgn filigsglag
       61 vgqgltikwl afpafiagiv aarlldhrmr vrghgpracs lyalqtilla gfmlagvaas
      121 pignadapat ivcgllgaaa mgvqnahgrl taravvantv mtgnvtqavi dafdwlvpia
      181 apaereaara rlrrtlppvv gfalgagaga taylyagfwa lalplaalgf ltwrsgrtse
      241 psasr
//
LOCUS       WP_175885412             323 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia sp. BCC0044].
ACCESSION   WP_175885412
VERSION     WP_175885412.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..323
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34110
     Region          13..224
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(54..55,57,71..73,79,81..82,123,223)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(54,56..57)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(79,82,85,92)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(115,119..122,124)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(120..121,144..146,197..198)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          239..323
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 miendllaar viarervacd vislrlvsda pgfslpafea gahidlhlrd gltrkyslcn
       61 dpvergvyei aikrepassg gsahvhdair vgdvlrigap lnyfplapdd spavllaagi
      121 gvtpllamah slvragrpla fhyfvrsada aaygatlasr ladvatlhtg ltpdatrdai
      181 ativgamdsr shlyfcgpap fmaavdtiar palgdarlhh eyfsapaaqp adgeadafri
      241 elarsqrvll vppgqsitdv lyehgiavat sceagvcgac rttvlegtpd hrdaflsaad
      301 karndcmmpc vsrcrgerlv ldl
//
LOCUS       WP_175885392            1082 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia sp. BCC0044].
ACCESSION   WP_175885392
VERSION     WP_175885392.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..1082
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114246
     Region          1..1057
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mwivrlalrr pytfvvlall ifiagplall rtptdifpni dipvvsivws yngfsaedma
       61 kritsnyera ltsdvddieh iesqslngvs vvkiffhpga dinraiaeaa snsasilril
      121 ppgtlppnii tynastvpil qlglssdtla eqqlydlgns firtqlatvq gaavplpfgg
      181 kirqivvdld tralqakgla pidvvnaina qnlilpggta kigtheynvq mngstqtvaa
      241 lndlpvktig gnvvyvrdva hvrdgyapqt nivrvdgkra alltvektgs tstltiidqv
      301 kamlpkiaag lpkalhiapl ddqsvfvkaa vqgvvreali aacltalmil lflgswratl
      361 iiaitiplav ltsllalsvl gqtinimtlg glalavgilv ddatvaieni thhlelgapl
      421 eeailtgsge iavptfvstl sicivfvpmf llsgvarylf vplaeavifa miasyffsrt
      481 lvptlamalm rakgsgrppr gvlaplvhla rfqaafehrf eavrlryral lsaaiarrrr
      541 faaafllacv astglyafag qdffpsvdtg eirlhlrapt gtrieetarl tdeveakirn
      601 vipanelagv ldnigvpvsg inltydssdp igsgdadvlv tlkpnhasta ayvaklrnvl
      661 aqafpgvtfa flpadivsqi lnfglpapid iqivgnkldq nravanalla klrgvrglvd
      721 ariqqpgdep ainvnvdrtk aiqagldqrd vaqnllials gssqttpnfw ldprngvsyp
      781 vlvqtpqytv nslqslanvp lpagtarppq tpaggpaaga paqnllgalg sfsratqqav
      841 vshynvqpvl difasvqgrd lggvtadvtk lvdaaraqlp pgssivlrgq vqamhesfag
      901 llgglalais lvyllmvvnf qswldplviv gglpaslagi awmlfvtrtt lsvpaltgti
      961 lcigiatans ilvvnaarel laageppwqa aldagfsrfr pvvmtalaml igmlpmalgl
     1021 gdggeqnapl gravigglaf gtvstllfvp vlfgfvhawl arrrdaaapr haqhapdtpa
     1081 lr
//
LOCUS       WP_175885436             557 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Burkholderia sp. BCC0044].
ACCESSION   WP_175885436
VERSION     WP_175885436.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60599
     Region          25..384
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          453..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mttqdllaqy gpresmeydv vivgggpagl saairlkqla aekgteigvc vlekgseiga
       61 hilsgavmdp raitelfpdw kergapldve vsedrflfls eksavttpnw alpdnfknhg
      121 nyvislgnvt rwlgqqaeal gveifpgfpa aeilynddgs vkgvatgnmg vgkdgepten
      181 fqlgmelhak ytlfaegcrg hlgrqliskf kldanadpqa ygigikelwe idpakhkpgl
      241 vihtagwplk sdtyggsfly hmdnnqvvvg fvvglgytnp ylspfeefqr ykthpsiraf
      301 leggkrvsyg araitaggll slpktvfpgg aligddagfl nasrikgsha aiktgmlaad
      361 aafdavqagr qsdelnaypd afkqswlyte lyrarnfkqw makglylgtl mvgleqkvmg
      421 gnvpwtlhhq hadhemlkpa sqcepieypk pdgkltfdrl ssvfisntnh eenqpahltl
      481 kdanvpvnvn lrtyagpear fcpaavyefv knddggerlv inaqncvhck tcdikdptqn
      541 ivwvtpeggg gpnypnm
//
LOCUS       WP_175885517             383 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175885517
VERSION     WP_175885517.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..383
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40547
     Region          1..375
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnfeatpdqr aaaatyraia lrhfapsprr gfdwatwral seaglwrlla adrdagadss
       61 sngfiaafea ivtatrsvgf amalanqatv iralqrhgtp aqrdrflpal msgavaatai
      121 sekgtgteir alqtrvapdg qafrldghky nishapdaal ilvaasvthe srsgtalvll
      181 dpqragvtrs apqetlgvad lpigdmtfdg vsvgtddllc spkdglrilm diasmnralf
      241 gllcadvvgp flddalayvr ergalgvtld hhqhvqrrlv dihvgsersr wmalaaldql
      301 ragdpsalas csiaklggar dltqaalhll aiygsdgyrr gpiaafvada lamgtaggte
      361 emharnifnq mqrratashm haa
//
LOCUS       WP_175885495             396 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175885495
VERSION     WP_175885495.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..396
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=42478
     Region          13..396
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 mstqafdvql lvdgriveri ahgideadvr aqlgpsagiv vtinrragfg krtkrpafal
       61 alflqelstl ldaglvllea lqalrdktgd drasksvldr ivavmvegqp lsvalarqpd
      121 vfpallvtti esaegsgqlp hvlkrylqye trianirkrv vgalvypalv igigcaillf
      181 maffviprfa tvfetmntlp ataramlaws nllknhggai cialaaavtf gfvairggal
      241 krlgrmllwr lprvrdvaal faltrfyrtv gllagggtpa ltalelagra lpeqyclrld
      301 aalvelragr tvsavlaqha lttpvaerll rvgeqsgdla gmcehiaqfh daeidraiem
      361 iskvfepvlm lavgaivgtv vvllympvfe ladsig
//
LOCUS       WP_175885609             531 aa            linear   BCT 11-JAN-2025
DEFINITION  MDR family MFS transporter [Burkholderia sp. BCC0044].
ACCESSION   WP_175885609
VERSION     WP_175885609.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..531
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56628
     Region          33..425
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(34..35,38..39,42,73,123..124,126..128,131,152,
                     155..156,159,285,288..289,292..294,297,325,329,382..383,
                     387,391,407,410..411,414..415,418)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mavhtaahhs sgqvlpfres llamigisfv tmlvaldqtv vgtalptiva elrgfdlyaw
       61 vatsyllssv itvpifgrlg dyygrkpfvi asivvftgas vlcgmandml tlvlarglqg
      121 igggmlvgta facipdlfpd svvrlrwqvl mssafgiana vgpslggvlt qsfgwrsvfy
      181 vnlpvgllsl lfvwrylphl rhvehdrkmr ldwpgallia lslgalqlfv ewlpkygias
      241 waslllvvav gagiglwhre krcaqpilpf dmfgnralsa lfvlailagf smfsllfyap
      301 llfqggfgms pkeaglvitp lvvfitigsi mngrvvtrir npnamlhvgf vlfaiacagi
      361 vvathttptw mlmalmvagg iglgfvlpnl tvfaqqtagr ehlgiatall qslrmvggml
      421 gtaltgtlvn qmyssgvrna lsadhamqwh arladpqili draaqgglva eltraghnga
      481 llleaaresl vgaihlgvam aavvavvsvw qcrrvppial rrkiephvaa d
//
LOCUS       WP_175885714             309 aa            linear   BCT 11-JAN-2025
DEFINITION  MlaD family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175885714
VERSION     WP_175885714.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..309
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=32723
     Region          1..289
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 menkshafwa glftialtla iagtvfwfnv drtvrvpydl lartnvtglf pdaavrfrgl
       61 dvgkvqsigf drthpgqiri rilvdhdapi tqstygslgf qgvtgiafvq ledtgrdlap
      121 lpsspktiaq ipmrpslfdq iqergdvllr qlelaaksan almspemreq lrataeslqh
      181 aadgaatltk qlgpavtalp etmhevnram asantllqpn gplvsnlnka gtaaeqigva
      241 lnglnarvqy dtlprfnala dsvgdasrql kdvagelgrn prsllfgspg aapgpgeagf
      301 vwpgatagk
//
LOCUS       WP_175885715             304 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175885715
VERSION     WP_175885715.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..304
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32411
     Region          29..270
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 mnasnetaah aaaigagsvg arpdaaadag dlvievrnlt krygrnivhq kldfdvrrge
       61 ivsivggsgs gkttlvrqil glerptsgti kvfgedtati ddasarmmrt rsgmlfqhga
      121 lfssmtvfdn vaqplrelgr vppdllhdiv mlklemvglp ckhaskmpaa lsggmvkrvg
      181 iaraialepe llfldeptag ldpqasdefv eliatlhrtl gltvvmvthd ldtmvalstr
      241 vavladrkvl vaapveeaan vdhpfiheyf lglrgrralq alpperrakl pkaalepals
      301 svel
//
LOCUS       WP_175885726             288 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175885726
VERSION     WP_175885726.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..288
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30881
     Region          29..283
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mpasplpddd ladsdtddat sgehgekvrs giqsievgfr lldvltsepr ammlrdlaqr
       61 agmspakahr ylvsfsrlgv vsqdpvsgry elggfalqmg larlarvdgv klarialtef
      121 rdrldqtvgi avwgnqgpti vhwmesshpa kaslklgdvm pllgsatgll faaylprskt
      181 aamlerelad trrsphhggp rtldevdavl advrrhqaar vegmllptih afcmpvfdav
      241 gelalaival gqegsfdiaw ggeidtalra caqklsyelg yspdarda
//
LOCUS       WP_175885739             423 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175885739
VERSION     WP_175885739.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..423
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45062
     Region          67..298
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mayskvlvgw maacalsaaq agtlpsantg agasgslaha ehfdyadanl pqvaadlneq
       61 ilripadasg avtleatlfk pngpgpfplv vfnhgkntgd lhqqprsrpl afarefvrrg
      121 yaviapnrqg fagsdgtyqq egcnvgkngl aqaadvdatv rymsrqpyvd asrivvagts
      181 hgglasvayg teaaagvrgi infsgglrqd lcdgwqrnlv dafdhygaht avrslwlygd
      241 ndsvwtpalv aqmhdayvsh gtqarfidfg rykddahrli vdrdgvpvww pavhaflael
      301 nlptavryav adphepkasg yasidavnav pyvdeagreg yrrflnqhps rafavssega
      361 wswaeggddp malaldncak qgagacrlya vndrvvwndn ttqtasnggd ntrdtdtral
      421 asr
//
LOCUS       WP_175885751             204 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175885751
VERSION     WP_175885751.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..204
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22389
     Region          1..199
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mklyywpktr afralwmlee iggvyelvpi dlrsheqgsd afvqvnpmak lpalddgsap
       61 faesgavlly ladrcpgagl giapddplrg rflqwmfftp tclepamaek ftgasgnpva
      121 fgwgnivrvq ralaqalahn rwlvgerfta adlllastlk iafdahllph egvlgdyvar
      181 aedrdafrra vaieqreaar llha
//
LOCUS       WP_175885791             261 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia sp. BCC0044].
ACCESSION   WP_175885791
VERSION     WP_175885791.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..261
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=27181
     Region          9..242
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 merkplvgit adltqigaha shtvgdkyva aivdgahala mvlpalgerq stadvldavd
       61 gllftgsysn vephryggep sepgtkhdpa rdattlpllr aaivagvpvl avcrgfqeln
      121 vvcggtlhqr vhdvpgfadh redddapmdt qygpahvvrl tpggklhala ggrdevhvns
      181 lhkqgvaqlg sglaveavap dglieavsvv dapafalavq whpewrhaqd plssaifraf
      241 gdacrarraa rtrataaaal a
//
LOCUS       WP_175885837             271 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: endonuclease/exonuclease/phosphatase family protein
            [Burkholderia].
ACCESSION   WP_175885837
VERSION     WP_175885837.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..271
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29919
     Region          13..268
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 msadalslpf aephaapdei tavswnlhkg rsplgftawn amrdwmqsth advyflqeam
       61 arrmprpmla agfgapmddt vddvwhcqat eiaqaldwqi algpnvfkps wrhgnailsp
      121 hpldlggrwd isahrferrg llvaratlag arpvtllcah laltraarlr qmhwiahwiv
      181 rnagdgplml agdfndwrnd svalfgeigl sevatllges grtfpafspa laldkmfvrg
      241 ltplewraps geaawlsdhl pyiarlrldp q
//
LOCUS       WP_175885878             279 aa            linear   BCT 11-JAN-2025
DEFINITION  polyphosphate kinase 2 family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175885878
VERSION     WP_175885878.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Motomura,K., Hirota,R., Okada,M., Ikeda,T., Ishida,T. and Kuroda,A.
  TITLE     A new subfamily of polyphosphate kinase 2 (class III PPK2)
            catalyzes both nucleoside monophosphate phosphorylation and
            nucleoside diphosphate phosphorylation
  JOURNAL   Appl Environ Microbiol 80 (8), 2602-2608 (2014)
   PUBMED   24532069
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Sureka,K., Sanyal,S., Basu,J. and Kundu,M.
  TITLE     Polyphosphate kinase 2: a modulator of nucleoside diphosphate
            kinase activity in mycobacteria
  JOURNAL   Mol Microbiol 74 (5), 1187-1197 (2009)
   PUBMED   19843229
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Nocek,B., Kochinyan,S., Proudfoot,M., Brown,G., Evdokimova,E.,
            Osipiuk,J., Edwards,A.M., Savchenko,A., Joachimiak,A. and
            Yakunin,A.F.
  TITLE     Polyphosphate-dependent synthesis of ATP and ADP by the family-2
            polyphosphate kinases in bacteria
  JOURNAL   Proc Natl Acad Sci U S A 105 (46), 17730-17735 (2008)
   PUBMED   19001261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..279
                     /product="polyphosphate kinase 2 family protein"
                     /EC_number="2.7.4.-"
                     /GO_function="GO:0008976 - polyphosphate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016776 - phosphotransferase activity,
                     phosphate group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006797 - polyphosphate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31730
     Region          7..277
                     /region_name="PPK2_rel_1"
                     /note="polyphosphate:nucleotide phosphotransferase, PPK2
                     family; TIGR03709"
                     /db_xref="CDD:274737"
ORIGIN      
        1 makqpslddf rvpystrdke aaafkldafd paakpfssgs keadrerlsv vsteldvqqe
       61 rlhtqqkkrv llvlqgmdts gkdgtvravf revdplglri vpfkaptpie aahdflwrvh
      121 aqvpaagela ifnrshyedv lvprvlgaig dkecerryrq irdfetmlse ngttiikcfl
      181 hiskdeqrar lqariddptk hwkfdisdld arkhwdayqs ayrdalaats aehapwyvip
      241 anskthrnvm iaelllrtmt dmklefpppk pelegvkir
//
LOCUS       WP_175885876             351 aa            linear   BCT 11-JAN-2025
DEFINITION  M48 family metallopeptidase [Burkholderia sp. BCC0044].
ACCESSION   WP_175885876
VERSION     WP_175885876.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Lew,R.A.
  TITLE     The zinc metallopeptidase family: new faces, new functions
  JOURNAL   Protein Pept Lett 11 (5), 407-414 (2004)
   PUBMED   15544561
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..351
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36986
     Region          136..319
                     /region_name="M48C_Oma1_like"
                     /note="Peptidase M48C, integral membrane endopeptidase;
                     cd07331"
                     /db_xref="CDD:320690"
     Site            order(202..203,206,259,263,303)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320690"
     Site            order(202,206,259,303)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320690"
ORIGIN      
        1 mrgnrlhrla haaaalsvga aaalaatgah atdtgatapg sapaaaqaap paaatsaapv
       61 ppsaaegaqp tgaaapakay tptpqqvryg naiafrtlip splleqltan eyaqivqtaa
      121 dsnrllsanq prvkrlraiv aklapysvkw ndrvkswawd vnvirsrdir ltclpggkvl
      181 vyggmldrvr lnddelgvll ahgiahalre harsnfgvts qtslraaalp plfgvgdplp
      241 qalnlgerlq slhydptdet eadviggdia aragfdpraa itlwdklava trankasgfi
      301 ythpysaarr qdllnrlpdl mplyakatgk rveslpdyag isaqrrkivr r
//
LOCUS       WP_175885894             349 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175885894
VERSION     WP_175885894.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..349
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38461
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdhlqsmrvf vkvadlgsfa raasamdisn avatrhvadl egrlgtrlln rttrslslte
       61 sgqvylerar qildeledve qmvvarnhep vgtlrivapv vfglhnlapv lqsytenfpk
      121 vvpdltlvdr qvdlveegfd vgivvtrqmr sasivtrrlt tgcmtvcatp sylekhgvpi
      181 hpeqlaehpa lslpteywgd ervftgpdge vrvrptnviv anntamlrqf allgmgvail
      241 psyligsdia rgalvrllpe frlpqveini aypsrrhlpa kvrtfidhlv ehfshstdat
      301 mgeqwaaqaa tmppigvemr aeqpestdpn lqpriarspr trvavpspl
//
LOCUS       WP_175885897             204 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CGNR zinc finger domain-containing protein
            [Burkholderia].
ACCESSION   WP_175885897
VERSION     WP_175885897.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..204
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22529
     Region          12..204
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mvtrsdptrh ghewcaadfv gghpaldfln tvadtgktrd eeklvdwpav rawaakagll
       61 apddlarllr hprqdgpdel aalrrfrdda yvaiahltae gggsagaraa drlavtirea
      121 igrsafdavg grfawrldar gasrwidaaa lgfehlmrsd dfarvrqcgr ctwffvdrgr
      181 gvgrrwcdmr tcgnrakvea frer
//
LOCUS       WP_175885956             339 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-quinone oxidoreductase [Burkholderia sp. BCC0044].
ACCESSION   WP_175885956
VERSION     WP_175885956.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..339
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=35549
     Region          1..333
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(40..41,127,131,134,157,160..162,181..182,186,201,
                     225..226,247..248,250,272..274,322,327)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mkaieitefg apdvlklaer prpepkrgev likvaasgvn rpdvfqrkga yapppgasdl
       61 pglevageiv ggdlsdaaln pfglklgdrv callagggya eyavaplpqc lpvpdgltdi
      121 eaaslpetff tvwsnvfdra qlgageggeq etllvqggss gigvtaiqia halgfrvfat
      181 agtadkcrac ealgaeraid yktedfvevv kslthdrgvd vildmvagpy vprelsalad
      241 ggrlvliall ggakaevnln eilrrrltvt gstlrprpve fkariaaqlk arvwpllaeg
      301 rikpviyrvl pageaaqaha lmesgehigk ivldwgata
//
LOCUS       WP_175886003             519 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia sp. BCC0044].
ACCESSION   WP_175886003
VERSION     WP_175886003.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..519
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56091
     Region          34..454
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msagpaglth dvpaapfern atmsdsvakp vdatfdqfgl apdilkaive qgyttptpiq
       61 aqaipvvlag rdvmgaaqtg tgktasfslp iiqrllpqan tsasparhpv raliltptre
      121 ladqvaanvh ayakhtplrs avvfggvdmn pqsaelrrgv eiliatpgrl ldhvqqktan
      181 lgqvqilvld eadrmldmgf lpdlqrilnl lpkerqtllf satfsgeikk lastylrnpq
      241 tievarsnst nanvtqivyd vaegdkqaav vqllrdrglk qvivfcnski gasrlarnle
      301 rdgvvasaih gdktqlermq aldafkrgei ealvatdvaa rgldiaelpa vinfdlpfsa
      361 edyvhrigrt gragatgdal slcspnerkq ladieklikr pldvqtltid kparqrhder
      421 ggernsergg ersgerggrr erdehrgaag rrsgspersg hhrrheapvd dfflkpyeps
      481 asakqpddaq paqhpekkgp krqvaallgg fgmprkpsa
//
LOCUS       WP_175886022             107 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175886022
VERSION     WP_175886022.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..107
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11648
     Region          1..103
                     /region_name="COG5606"
                     /note="Predicted DNA-binding protein, XRE-type HTH domain
                     [General function prediction only]"
                     /db_xref="CDD:444337"
ORIGIN      
        1 mieieqgsgn vyadlgmhda gemrvkaqla akigeiikar kwtqqhaarl lgmtqpklsn
       61 mlrgqfrgvs eakmldclak lgrdvqiivg pdrhpeaegh ievvfta
//
LOCUS       WP_175886052             193 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Burkholderia sp. BCC0044].
ACCESSION   WP_175886052
VERSION     WP_175886052.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..193
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22073
     Region          21..186
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 meppptsqtm tdpdrditat vmrertrlgn firrrirdpd daedvlqdvl hefvqayrlp
       61 apieqasawl frtarnriid rfrkkkeqpl adlldaddea dseyrldlal pshdagpeal
      121 yartlllkal qdaldelpan qrevfiahel dgqsfkemaa qsgvtlntll arkryavlhl
      181 rarlqpiyde ldi
//
LOCUS       WP_175886084             269 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175886084
VERSION     WP_175886084.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..269
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29437
     Region          19..98
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(44,69)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(51..52,63,66,70..71)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          117..267
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 msqpssapvp pldatparal gefirahrer lspqaiglpp gprrrtpglr reevaqlcgv
       61 sptwytwieq grpvsasada lariavalql skaeraylfe laaqrdpaep dvaagdlppt
      121 laatvaaiat payvldrqwn alawnapaaa lfsgwldgeh drnllrftfm spaartlivd
      181 wetrarrlaa efradsirhl adaptralid altagsdafa qywasqdvfe regglrefdh
      241 padgrlvyqq itlkpahred lklvvlvrd
//
LOCUS       WP_175886105             271 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175886105
VERSION     WP_175886105.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..271
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29106
     Region          16..265
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtgpalnaaa gdmyytavdl tlkagartll dcftqafrpg eiwcvagpng agkttllatl
       61 aglqppaggh veidgrplaa wrperlaqrr almpqqlhda fsatvfdtvl lnrfpylggw
      121 gwerdgdraa ardalatfdl splasrdvms lsggerqrva laatlcqdap lmlldeplah
      181 ldlhhqidcl talaawlaag prtvlfschd lnlarrfath allldgrgha wagpvhdvlt
      241 perasdafgy plvlirengr dallpawpar q
//
LOCUS       WP_175886110             108 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia sp. BCC0044].
ACCESSION   WP_175886110
VERSION     WP_175886110.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..108
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11175
     Region          28..106
                     /region_name="CytC552"
                     /note="Cytochrome c551/c552 [Energy production and
                     conversion]; COG4654"
                     /db_xref="CDD:443692"
ORIGIN      
        1 mkqtilrvll atlltgsaaa aradqadgla laqrkncmac haigkplmgp sfhdiagkya
       61 argdaadyla qsivkgsvgv wgsvpmpant qltsieartl aqwvlsvr
//
LOCUS       WP_175886122             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175886122
VERSION     WP_175886122.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32735
     Region          13..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..295
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(106,110,149,163,165,230,247,274)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(107..108,112..113,115..116,119,123,125..131,193,
                     224..228,235..236,239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mgfdsrllsg igvlsaviea gtfarageam gltqpavsra varleervgi rifnrtarai
       61 tltdegrrfy eavapllagi eeaaldagqs karvrgrlrv nvdgtfghyv laprmaefld
      121 rfpdlsveis vrdrmgdlva dgfdvavrfg ipepssyrar llletrvltc asaayvarhg
      181 eprhprdlad ghrcvlirdp vtgrpyewef hrgkevvpid aagrltvndt ggllgacvgg
      241 vgiaqllely ardvlaegrl vlllpewtde tfplyayhha snlvaakvrv fldfvrelma
//
LOCUS       WP_175886127             309 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175886127
VERSION     WP_175886127.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33849
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..294
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdkldqvrif lqvaemgsfi kaahaldvpr atvsaavqql etalgtrllh rttrqvqlta
       61 dgalllergr rllaeadeld rlfrrrdrdv vgrlnvdvps riarrvvapa lpslfrrhpk
      121 lqlslgstdr tidlvqegvd cairvgrlad sslvvrplgq ftlincaspd ylrecgvpeh
      181 pdalahghwa igyaspttgr elgweycang qrhtlalpsr vivnnaetyi agcvagmgli
      241 qiprfdvehl lasgalvdvm pghraepmdv savyphrrhr srrlnafiew fgalmaealn
      301 dagasdsgd
//
LOCUS       WP_175886153             459 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia sp. BCC0044].
ACCESSION   WP_175886153
VERSION     WP_175886153.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..459
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48989
     Region          7..457
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mtqqqrsfda ivareqglrh altsgqmami aiggaigtgl flgsgfaigl agpsvlvsya
       61 igalialllm galaemtvah ptagsfgaya ehyvgplagf lvryaywfav vfaigteisa
      121 iavfmkywfp avpgwywvig fsalliavnl asvalygtve yafsllkiaa iivfivlgay
      181 lvwsapaasg igfanytahg gfmpkgpwgt wvavivaifs ymsieavaia ageardpqha
      241 vtrafrstvf rlvlfylltl almlaivpwt qagtdespfv kvmaathvpy aagvinfvll
      301 iaalsamnsq lyvttrmmfs lsrarlapav fgrlgangvp raalwistsg vavaavlval
      361 apdtaftvmm aiamfgalft wlmifvthlr fraryrgpal afrmwghpfg sllgaglvaa
      421 illttaftre frmtmvvgvv fvvlltlaya lhyrhqhar
//
LOCUS       WP_175886216             404 aa            linear   BCT 11-JAN-2025
DEFINITION  cation:proton antiporter [Burkholderia sp. BCC0044].
ACCESSION   WP_175886216
VERSION     WP_175886216.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..404
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43610
     Region          13..390
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mksafsflpn wplvpdavfw aglalfaagl cgelcyrawr lpritgyavi gliagsfgfg
       61 vidtstdets rllmdvalgl llfelgsrld lrwirrnpwl vasslaeatl tfvlvlfvml
      121 algvsgmval vlsaiaiats psmviqlkte lraegqvsqr litltalnsv yaivltklvt
      181 swlhqeaygn vfatilqply llagsfivay lvaracnylf rhmtatmrde hsfvalfglv
      241 mlaiavaqal klstlltlll agiivknlea rpqlwpehfg tagwlltvvl fvltltsftw
      301 gdialgglla ivlivtrlaa klagvvafak psglgmkqgv algialtpms alsyllvddt
      361 yqlypnfdph lraivmcsiv ilqlvspfvv yrclsavger sdgn
//
LOCUS       WP_175886224             561 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia sp. BCC0044].
ACCESSION   WP_175886224
VERSION     WP_175886224.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..561
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=61061
     Region          10..539
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mstertlege fdyvivgagt agcvlanrlt edpdisvlll eaggkddyhw ihipvgylyc
       61 ignprtdwly ktqpeaalng ralsyprgrv lggcssingm iymrgqredy dnwaqetgda
      121 gwswdsvlpi fkrsedhhag asdahgsggy wrvekqrlrw eilesfaqaa qqtgipatdd
      181 fnrgdnagvg yfevnqkrgv rwntskaflr pamarpnltv itgahaqrvt fdgrravgve
      241 yhgggtdyva raraevllts gavnspqlle lsgvgdgrrl qalgidvvqd lpgvgenlqd
      301 hlqlrmafrv dgvrtlntls arwwgklmig aeyallqrgp msmapsqlga faksdpddpa
      361 ltrpdlqyhv qplslerfge plhgfnafta svchlrpssr gsvhiaspda gvapaiapny
      421 lstdhdrhva analrltrri asapalaryr peeilpgtry qteaelidaa gvvgttifhp
      481 vgtcrmgrad deravvdsrl rvrgiaglri vdasvmpfit sgntnsptlm iaerasdmir
      541 adrraareat pvrteaavtv a
//
LOCUS       WP_175886283             200 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA-3-methyladenine glycosylase I [Burkholderia sp. BCC0044].
ACCESSION   WP_175886283
VERSION     WP_175886283.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..200
                     /product="DNA-3-methyladenine glycosylase I"
                     /EC_number="3.2.2.20"
                     /GO_function="GO:0008725 - DNA-3-methyladenine glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=22022
     Region          3..187
                     /region_name="Tag"
                     /note="3-methyladenine DNA glycosylase Tag [Replication,
                     recombination and repair]; COG2818"
                     /db_xref="CDD:442066"
ORIGIN      
        1 msqrcnwvkt eadahyhdte wgvpshddrh lfemlilega qaglswstil nkragyreaf
       61 adfdvdavar ftpkriekll enpgivrnra kvesavanar avqrireehg slaaflwsfv
      121 gdtpvqnawq syrdapaste qsdalskalk aydckfvgst icyalmqatg mvndheagcp
      181 chaqcaalgg kqparrrkag
//
LOCUS       WP_175886307             405 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0044].
ACCESSION   WP_175886307
VERSION     WP_175886307.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..405
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40499
     Region          32..399
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(42..43,46..47,50,82,132..133,135..137,140,159,
                     162..163,166,234,237..238,241..243,246,274,278,327..328,
                     332,336,352,355..356,359..360,363)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 msessspess spfaappdah rvlplparqr artasmalff vagmmyaswg vhvptvrdkf
       61 alspgllsia lfavaggsia amltiarwia rvgsrtacva gglvmsacaa lilvvpdywm
      121 llavlalfgf smatldvamn aeasaveial gkpimsslhg mfslggmgga aaggallsag
      181 mapaahlala aaasaavlva aspavlphvp hheqahgggn rwrspalwml ggialialia
      241 egamydwatv ymrdvvaasp alasaayaaf sggmavarfa gdavrarfga pqlvlasasl
      301 acagmigall lpkpvavltg ftlmglglan mmpvlfaaaa rvkgihaaeg lahvaglayf
      361 gllfgpvvig avaqaanltv glsvvalcaa lvalvapkvl ahlki
//
LOCUS       WP_175886299             168 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175886299
VERSION     WP_175886299.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..168
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18171
     Region          5..164
                     /region_name="COG3865"
                     /note="Glyoxalase superfamily enzyme, possible
                     3-demethylubiquinone-9 3-methyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:443074"
ORIGIN      
        1 mnshiqritp flwfdrdaea aagfyvsvfd narivhvary gkagaqasgn aegavmtvaf
       61 eldgqafval nggpmfqmtp avsfvvncrd qaeidhywar lseggdaraq qcgwlrdrfg
      121 vswqvvpvqm aelmtgdpar aervmaqvmt mkkldlgalq raaagesa
//
LOCUS       WP_175886315             115 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia sp. BCC0044].
ACCESSION   WP_175886315
VERSION     WP_175886315.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..115
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11810
     Region          26..113
                     /region_name="CytC552"
                     /note="Cytochrome c551/c552 [Energy production and
                     conversion]; COG4654"
                     /db_xref="CDD:443692"
ORIGIN      
        1 mkqmkrwmvq gaaaaalaag tlgaahadvg dglkvarsna cmgchavdrk lvgpsfkdia
       61 aryqsdpqav tklskkvkdg gsgvwgaipm pahprmsdad vrsvvewvla gapsk
//
LOCUS       WP_175886346             421 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175886346
VERSION     WP_175886346.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..421
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=43712
     Region          205..413
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(212,252,290,393,396)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(212,393,396)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(212,252,290)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 msfrssfaaa vlgaavfvsp faasappagw vaawatalqp ipdlaapppl yrapdvagrt
       61 vrqivyptvs graarlrvsn aygraplvve aaslarageg aalaggaaap vrfggkasvt
      121 lapgqelesd pvaidvtaaq pyaislqmgp nqrmtvwhrv snqfnyvstp gdhvsdsgaa
      181 afrtrftqya wvtelaveag sahasvaaig dsitdglrss vnrnrrwpda larrlmasga
      241 dsigvvnlgi sgnrllsdsa cygtslasrf erdalsrsgv kaaivligin dinfaampph
      301 agldcdhpht qvtaaslidg yrrlidaahr qgvkvfgatl tpaalpagre airlevnrwi
      361 rsgggfdgvv dfdaalrdsa rpsvlqrryd sgdgihpsda gytamadvvp veqlqaavgg
      421 k
//
LOCUS       WP_175886354             492 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Burkholderia sp. BCC0044].
ACCESSION   WP_175886354
VERSION     WP_175886354.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..492
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51852
     Region          3..487
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mhsdylahda iglaalvrdr hasprellda aigqaeavng ainaivlqdy eaararaaaa
       61 pepgadapfa gvpylvkdlg aavaglplsm gsrhyryfvp addspviars raaglnvfgk
      121 tntseigqmp ytepelfgac rnpwnldhtp ggssggaaaa vaagivplah asdgggsiri
      181 pasccglfgl kpsrnpvlvd lpsngelvvq havsrsvrds allldvttgq tlppgapgtf
      241 lgaldtppgp lriglvvdpm lapaladdtr aalddaaall eslghhvepa tlpidyaraa
      301 etfltlwati aeemvlgara ltgrtprrge feaatwamav vgrrlartrl pdvlewqrql
      361 tvqvaglvsr ydailcasla gppvkigelq ptpfesaqmk lvsalpvkpl lkemlaksse
      421 kafawagcte lfnltgqpam svplywnarg lpigvqfaar hadealllrl arqleqarpw
      481 fdrrpplmqa qr
//
LOCUS       WP_175886363             116 aa            linear   BCT 11-JAN-2025
DEFINITION  FmdB family zinc ribbon protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175886363
VERSION     WP_175886363.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..116
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11026
     Region          1..73
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 mpiyayrcea cgfakdvlqk msdaplsqcp ecgkdafrkq vtaagfqlkg sgwyvtdfrg
       61 gsggasapat asgdaapaap aaeapaaaap aaassagstt ttsaapapaa tpaags
//
LOCUS       WP_175886388             310 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0044].
ACCESSION   WP_175886388
VERSION     WP_175886388.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34458
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrlgdirlf veaaelgslt aagrklnltp aaasarlakl eakiatrlfe rstrqlrltd
       61 egklylnccr qalqalddad amlqegrnvv sgkvrlssts dfgrhqlldw lhefttlhpg
      121 vtfsltasds ssnlwqdeid lairfaappd galiarrlat nrrvlcaaps fverhglpad
      181 phdlarfpcn vitiasgpmn twhftrgdev qihtvpvsta fetndggltr ewtlrghgia
      241 lkslwdiadd vragrlrvll pdwrhqdapl haiyhskrym aprvrvlldf laerfareea
      301 alddllnacr
//
LOCUS       WP_175886404             486 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia sp. BCC0044].
ACCESSION   WP_175886404
VERSION     WP_175886404.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..486
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52215
     Region          1..388
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfeslglae plvkavnelg ytsptpiqqq aipavlgggd llagaqtgtg ktagftlpil
       61 qrlhtfyaeh rgakravral iltptrelaa qveesvrays kylklrstvm fggvsinpqi
      121 dalkrgvdiv vatpgrlldh mqqktidlsd ldilvldead rmldmgfihd ikrvlaklpp
      181 qrqnllfsat fsdeikalad slldspalie varrnttaes vaqkihpvdr drkrellthl
      241 irehnwfqvl vftrtkhgan rlaeqltkdg isamaihgnk sqsartrala efknstlqvl
      301 vatdiaargi didqlphvvn fdlpnvpedy vhrigrtgra gatgeavslv cvdekqllrd
      361 ierlikreip qeviagfepd pnakpepiqq rrgqqqprsg gggggnrqpr gggsgqpaak
      421 rdgnaqpkas qpkaaqqkaa kprtqggagg ngggrpaggg ngarpasgna ahpnrnrssr
      481 sgqrgh
//
LOCUS       WP_175886430             234 aa            linear   BCT 11-JAN-2025
DEFINITION  TerC family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175886430
VERSION     WP_175886430.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..234
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24609
     Region          24..191
                     /region_name="R_switched_YjbE"
                     /note="integral membrane protein, YjbE family; TIGR03717"
                     /db_xref="CDD:163429"
ORIGIN      
        1 mlefltslhw gailqiiiid illggdnavv ialacrnlpa nqrlrgvvwg tagaillrva
       61 litfavalld vpflklgggl lllwigiklm apaadahddi kpadrlwdav ktiviadavm
      121 sldnviaiag aaeqadpshr ialvifglvv svpiivwgst lvlklldrfp vvvafgagll
      181 gwiagglivn dpvgdrwpvl dtpqvvygas ivgalfvvai gyalrkrrsv phap
//
LOCUS       WP_175886462             318 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Burkholderia sp. BCC0044].
ACCESSION   WP_175886462
VERSION     WP_175886462.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..318
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33015
     Region          3..296
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(36..37,40,91,105,107,136,168,256,259,295)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(227,232,247,256..258,261,283,287)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 maeivvagel laefvaaerg qgfdtpglfe gpfpsgapai fadqaarlga rvayagcvgr
       61 dafgdaivar lerdgvdvar irrvarptgt afvayrddgs rsfvfslsts aaacvdasdv
      121 dtamfdgcry fhvmgsslts esaiaavqrg vieaaragak vsfdpnvrpe mlsfrpmraa
      181 ldemlaachl flpseadlpf fcgpqpaera iagllathpl lervvlkrga qgsvafdras
      241 rvdaqaypvd evdptgagdc fggtlvaslv aglavdvalr ranaagaiav trrgpmegns
      301 saaeidrflt ergiacpa
//
LOCUS       WP_175886455             458 aa            linear   BCT 11-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175886455
VERSION     WP_175886455.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..458
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47694
     Region          22..430
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mqsntvhpcd evlptgklvt lglqhvlvmy agavavpliv ggalklpkdq iaflisadlf
       61 scgiatliqt lglwifgirl pvimgctfaa vgpmiaigtn pglgildifg stiaagiigi
      121 vlaptigkll rffppvvvgt viaviglslm evginwaagg vgnpeygspv ylglsllvlt
      181 lillinkfgr gfianisvll givagfviaf aigrvntegv slapwvgfvm pfhfgwphfd
      241 plsiatmvtv mfvtfiestg mflavgdmvd rpvnqerlvr glrvdglgtl iggifnsfph
      301 tsfsqnvgli gvtgvksrfv catggvilvl lglfpkmaqv vasvppfvlg gagivmfgmv
      361 aangikvlsk vdfvnnshnl fivavsvgmg lvpvvsphff sklppalapi lhsgillasa
      421 savilnivfn gvkgekdarc eirraghdfd grpadvhh
//
LOCUS       WP_175886493             156 aa            linear   BCT 11-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Burkholderia sp. BCC0044].
ACCESSION   WP_175886493
VERSION     WP_175886493.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..156
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=16899
     Region          1..153
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mfnavidapf gkvgirtdaa vvreivylpe smqsvdpdsa lakraveqie ryferasarf
       61 dlpladvgsa fqhrvwdvis dippgtvlty gqvakrigsa pravgqacga nyfplvipch
      121 rvvaagglgg fanhddngyy qkvkrwllah egvpyq
//
LOCUS       WP_175886468             369 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175886468
VERSION     WP_175886468.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..369
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39649
     Region          1..358
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masvllrnia kryddtevlr nvnldiadge fvvfvgpsgc gkstlmrmia gledisngdl
       61 lidgakvndv psakrgiamv fqsyalyphm tlydnmafgl klagakkpei dqavkqaaki
      121 lhidhlldrk pkqlsggqrq rvaigraitr kpkvflfdep lsnldaalrv kmrlefarlh
      181 delkttmiyv thdqveamtl adkivvlsgg avqqvgtpne lyhapsnqfv agfigspkmn
      241 flkgtvesad aggvlvrfds getqrvavda aglqrgaavt vgvrpehllv daaaagvaar
      301 tmaveslgda aylyaesava pdgliaripp ldtyrtgdal rvhaqaehch lfdengqafr
      361 rlsvhakaa
//
LOCUS       WP_175886546             532 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia sp. BCC0044].
ACCESSION   WP_175886546
VERSION     WP_175886546.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..532
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58021
     Region          1..449
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mkssiqrnig pfalmltglg siigsgwlfg awkaakiagp aaicawiiga vvilaialty
       61 aelgamfpes ggmvryarys hgslvgfisa wanwiaivsv ipieaeasiq ymstwpypwa
      121 halfvngelq tlglllsavl vviyfmlnyw gvkafarant aitifkflip gltilglmlt
      181 sfhsenlgva snasfapygw savltavats givfafngfq spvnlagear npsrsvpfav
      241 itsillalvi yvllqmayig svnpadvakg wahfnfsspf aelaialnln wlaillyvda
      301 fispsgtgtt ymatttrmiy amernntmpk mfgnvhpiyg vprqamwfnl lvsfvflfff
      361 rgwsslaavi svatvisylt gpislmalrr satdierpls iplmkliapf afvcaslily
      421 wakwpltgei illmivalpv yfyfqaksgw tgwgadlkaa wwlvaylptm avlsligske
      481 fgghgylpyg wdmlivaais lvfyfwgvnt gyrtqylder eshdeilegi ga
//
LOCUS       WP_175886502             235 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia sp.
            BCC0044].
ACCESSION   WP_175886502
VERSION     WP_175886502.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..235
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25248
     Region          18..228
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mpaslapylp qieanpwfaa lppalrveli aratlrrlpa ghalfrrgdp pcglyavlag
       61 sltigavdpq gkealltvae pvtwfgeial fdgqprthda ialddtlllh vpqaallail
      121 dttpqywrqf allmaqklrl sfltvesmsv mpaaqrlaar llmiaegygg isagrthirl
      181 sqetlasmls ltrqttnqll kalqadgvvr lhvgeielvd idalrrasgl gdgth
//
LOCUS       WP_175886576             252 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome c1 [Burkholderia sp. BCC0044].
ACCESSION   WP_175886576
VERSION     WP_175886576.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 252)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..252
                     /product="cytochrome c1"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28229
     Region          18..252
                     /region_name="CYT1"
                     /note="Cytochrome c1 [Energy production and conversion];
                     COG2857"
                     /db_xref="CDD:442105"
ORIGIN      
        1 mkkllstlal igatacalla apavraegnf pldrapdnte nlvslqhgaq lfvnyclnch
       61 sanlmrynrl tdlgisqkei etnllfttdk vgntmsvamr pddaknwlgt tppdlsveer
      121 argrdwlyty lrsfyrddtr ptgwnnavfe nvgmphvlwq lqgqraakfe dktdeetgek
      181 ahvlvgfqqv tpgtlsspdy daavadlvay mtwmsepaqq trkrlgvwvl iflgvltfla
      241 wrlnaaywkd ik
//
LOCUS       WP_175886631             392 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0044].
ACCESSION   WP_175886631
VERSION     WP_175886631.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 392)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..392
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39787
     Region          168..370
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mtqraaasar rvtldkvgil igiltivavf glsfavlrpn riaagtglsv faalppmqga
       61 alaalwtvga lwamtasrpa wrlvagcagl atlayavgaa aahavapddm larvspdagv
      121 wlllfawavl iadalarlaf gpwrrlaala vaiaavsvpl atgwwdglsv mreyavrsdd
      181 fwreairhvs laggsvaaal vagvplgiac ariatvrtva mpvlnivqtv psiamyglmm
      241 aplgllaahv plaaalgirg igvapavlal flysllpias svvvgleqvp phvteaaram
      301 gmtrtqrllr vdlvlalpvi lsgvrivlvq nigltavaal iggggfgtfi fqgigqsaad
      361 lvllgaipti alalaaavvf eaatslakgr ag
//
LOCUS       WP_175886633             255 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0044].
ACCESSION   WP_175886633
VERSION     WP_175886633.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 255)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 255)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..255
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25835
     Region          55..239
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mttrgnvqpk rsslpayvar aaalalllvl llrpawlqgl fapfadngap viydraslld
       61 ltlahlgtva lssligtvva vaagiavtrp fgadflpvar svvdigqtfp pvavlalavp
      121 avgfglkpvl ialvlygllp vfestiagle dvprdvvdaa rgmgmsgwqq lvsvelplaf
      181 pvivngirla vvinlgtati gstvaarglg dviiaglqts ntafvlqggv ivgllavlvs
      241 daigaiaraa sarra
//
LOCUS       WP_175886638             146 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydroneopterin aldolase [Burkholderia sp. BCC0044].
ACCESSION   WP_175886638
VERSION     WP_175886638.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Illarionova,V., Eisenreich,W., Fischer,M., Haussmann,C.,
            Romisch,W., Richter,G. and Bacher,A.
  TITLE     Biosynthesis of tetrahydrofolate. Stereochemistry of
            dihydroneopterin aldolase
  JOURNAL   J Biol Chem 277 (32), 28841-28847 (2002)
   PUBMED   12039964
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..146
                     /product="dihydroneopterin aldolase"
                     /EC_number="4.1.2.25"
                     /GO_function="GO:0004150 - dihydroneopterin aldolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0046656 - folic acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16379
     Region          23..133
                     /region_name="FolB"
                     /note="Dihydroneopterin aldolase [Coenzyme transport and
                     metabolism]; COG1539"
                     /db_xref="CDD:441148"
ORIGIN      
        1 mkpfdepfva idaprlrgrg wsvfvdelkv parigihahe heapqpivid arlgyrceps
       61 eqgewidydg ycarvaafla hkphtrllet lvadvavmsf rewpaleslt lsvykpkirp
      121 gtkrvgvsld wtrgdylrwt gaagql
//
LOCUS       WP_175886657             208 aa            linear   BCT 11-JAN-2025
DEFINITION  trimeric intracellular cation channel family protein [Burkholderia
            sp. BCC0044].
ACCESSION   WP_175886657
VERSION     WP_175886657.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..208
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=21008
     Region          6..204
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mkrieqvvla adlagtavfa ieganaaiga gldlfgvmvl slvvalgggv irdlligarp
       61 psavsdwryp alafaaglfa fvfharvasf spsllttlda aglalfavag avkalefrvh
      121 pfiatlmgav tgcgggvvrd vllaripvvl vtdiyasaal lgavvvvvcr rlgcppvvaa
      181 vlggvacfal rmaavrfdwq lpkiatga
//
LOCUS       WP_175886662             216 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Burkholderia sp. BCC0044].
ACCESSION   WP_175886662
VERSION     WP_175886662.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..216
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22805
     Region          12..176
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mtafdqhrrp fvvgiggttr aassterals falrgaqaag artrlfdgpf lhtlphyape
       61 hktltdaqre lidavrqada iiiatpgyhg gvsglvknal dtleelrade rpyldgravg
      121 livtaygwqa agtvltslrs ivhalrgwpt pfgatvntle trfesadscs dpkvvaqlet
      181 vgtqaaefal afashraash aasvdalapv lkvanh
//
LOCUS       WP_175886700             449 aa            linear   BCT 11-JAN-2025
DEFINITION  NCS2 family permease [Burkholderia sp. BCC0044].
ACCESSION   WP_175886700
VERSION     WP_175886700.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..449
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46085
     Region          14..443
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 msatdtmpar tpanwlerrf alaargtsvr tetiagvtsf laaayllvvi psllatggmd
       61 rgaattativ vfvlfttlmg lyanlpflvg pgiggsviig vtlattehvg wqtglgiacv
      121 sgvlffllti lgargvvvrl ipvqiklglg asiglfvtml glrnagmvva naktnafalg
      181 dfsrpgalva liglavaivl qarkvpgaim iailvaaaag vplgvthlpa sfmslphsia
      241 piafkldigs alslaaapyl faffaaeffs tlgtalavga kanlldehgn lpninrpflv
      301 dslaatlgpv fgipaltali esaagveagg rsglsslaaa vlfaamllfv pvalaipkea
      361 tapaliligl smfatirhth fddftdalpv msmvlltlms nsfgtgiagg llcyvlvkll
      421 agrwrdvswg lvvlalplgy yfwtvvkph
//
LOCUS       WP_175886729             278 aa            linear   BCT 11-JAN-2025
DEFINITION  thioesterase II family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175886729
VERSION     WP_175886729.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..278
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=31106
     Region          42..278
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mrlrctssar rpgsdrgrda srlplsigmp vkitpwfilh rpqpaathrl fcfpyagags
       61 llyrrwaldl pswievvave lpgrqtrfse apptsldamt dalataasgl ldkpfgtfgy
      121 sfgsvvgiew lkeldrrrlp rpihafcaah raphvaprpl sihrlpepdl inwlktmggt
      181 pdallsepdw lrhflralra dlalaegyct dtpfalrcgl tvfgglhdph vdmdalrewr
      241 rysdgpfslh rfdgdhffih arerelqdhv vatlaaha
//
LOCUS       WP_175886788             290 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia sp. BCC0044].
ACCESSION   WP_175886788
VERSION     WP_175886788.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..290
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31330
     Region          15..280
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mttarsldrt ypalrttegg gfvvhrpfpt rllmdfdpfl lldemgpvdy apgeavgapd
       61 hphrgfetvt yaldgrfrhr dssghagtlg pgdvqwmtag agvvhsempd pafaqaggrs
      121 hgfqlwvnlp rrdkmiapry qeipaaript atspdgrasv rviageafgv qaaietrtpi
      181 lyqhftlepg atvtqpvpag yrvfaypidg tglygpdrqa vdarhmivyg ddgdavtfaa
      241 gdtsldllli ggvplnepiv rygpfvmnte eeirqavvdy qtgrmgriea
//
LOCUS       WP_175886791             243 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Burkholderia sp. BCC0044].
ACCESSION   WP_175886791
VERSION     WP_175886791.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0044
  ORGANISM  Burkholderia sp. BCC0044
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia sp. BCC0044"
                     /db_xref="taxon:2676295"
     Protein         1..243
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25093
     Region          163..241
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mqashlapag ampaaprmnp rvivvavgvl aahaimltaa wlhrnapppa kqvevqsita
       61 qlippaptaq piavqsaaqq ptppkpvprv kpkiepkpvq kaiptpqpva qapsptpapa
      121 avdptpapaa papaapaaap gparetmqvs apknvsaltc nfvkpdypsm skrrgetgta
      181 yvhfiigvtg kiesvqlqks sgyprldeaa leatrastcp pyiengqair aahtlpfnft
      241 lnd
//
LOCUS       WP_175886828             355 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia contaminans].
ACCESSION   WP_175886828
VERSION     WP_175886828.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..355
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38412
     Region          1..340
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfvfdedqe aladsvkrll mtemtpelir elwatptgrs ddlwalfasq gltavsvpda
       61 hgglglteae wallaqaygy fgspeplldt alvsagvlar lpasdwrdal lrdiaegrar
      121 valvhpvnpy aadvhvaqml lcehrgelhr vdpaqcawra vnsvdpsrrl ftldwepsag
      181 triagadaaa pllnraldhg afavaaqllg ltqrvldvai dysaqrkqfg kaigsyqalk
      241 hlladvairy efarpvvara aqaiaddhpq ravfvshakl aataaaqlaa rhtmqvhgai
      301 gytweldlqi fmkriwalsg swgdsafhka rvadailgda lpigpaqtfd feetn
//
LOCUS       WP_175886831             412 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia contaminans].
ACCESSION   WP_175886831
VERSION     WP_175886831.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..412
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42410
     Region          1..386
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdlaltdeqa mirdaaadvl aersasadvr ralehsagrd dalwaalage lgwnalalpe
       61 asgglelgav eqtvlmeqlg rriacvpyfs taclaatala gcadtppanr wlakiaegac
      121 satlalpfdl pagarqlpvv aeeaagghal sgtveqvidg ahadlllvpa rianegqsig
      181 lfaidvatas gldvtpldtl datrpiariv ldevrvnrdg lfacgnaaaq vlertawfaa
      241 lalaaeqlgg aqqcldltld ytsqrvqfgr aiasfqavkh rcaqmmvlie sarsavlgaa
      301 hawdaeaggv apsdalradi aaaksaanda yafgaqeaiq lhggvgftwe ydphlyfkra
      361 qasgaqfgst pqllewiash aidggasard eafaspaapa srpsaaraga lq
//
LOCUS       WP_175886836             249 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Burkholderia contaminans].
ACCESSION   WP_175886836
VERSION     WP_175886836.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26308
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkvlvavkrv vdanvkvgvk sdrtgadian vkmsmnpfde iaveeavrlk eagvvtevia
       61 vsvgvvqaqe tlrtalaiga drailveshd gveplgvaki lkalvdkeqp qlvilgkqai
      121 dddsnqtgqm laalaglpqa tfaskvtvad gratvarevd ggaetlslql pavittdlrl
      181 nepryvtlpn imkakkkpld tvkpedlgvd vkprlkvlkv aeppkraagv kvpdvktlve
      241 klkteakvl
//
LOCUS       WP_175886851             481 aa            linear   BCT 11-JAN-2025
DEFINITION  sialidase family protein [Burkholderia contaminans].
ACCESSION   WP_175886851
VERSION     WP_175886851.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 481)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 481)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 481)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..481
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51061
     Region          144..428
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Region          177..238
                     /region_name="Sialidase propeller 2"
                     /note="Sialidase propeller 2 [structural motif]"
                     /db_xref="CDD:271234"
     Region          243..296
                     /region_name="Sialidase propeller 3"
                     /note="Sialidase propeller 3 [structural motif]"
                     /db_xref="CDD:271234"
     Region          305..364
                     /region_name="Sialidase propeller 4"
                     /note="Sialidase propeller 4 [structural motif]"
                     /db_xref="CDD:271234"
     Region          375..428
                     /region_name="Sialidase propeller 5"
                     /note="Sialidase propeller 5 [structural motif]"
                     /db_xref="CDD:271234"
ORIGIN      
        1 mrrmivshsl vtrlsaamam aaaaaahaep vvvsgpspfv actiggpgtn yvnaevepwl
       61 svnpanpmnm igvwqqdrws nggahglvag ytfdggatwa rtpqpfsaca pgglkyeras
      121 dpwvsfgpdg taysvsisfn qsnnsnavaa svssdggqtw sspavliand epttqffndk
      181 esvtanpvka gtayavwdrl elpngnpyan lhtkafrgpt lfskttdggk twsapkvivn
      241 vpsrqqtign qivvdprsgt lydffdliqp pfskaagkva fikstddgat wtkpqviagl
      301 qtvgvtdpvt gepvrtgdii pepaidpasg llyvvwqdsr fnggtydeia vstskdggat
      361 wsapqqlntp tgrpafnpsv rvdntgavmv tyydfrdlqa gntttlptgf wrkishdggt
      421 tfaderrvgg pfdmklapna egffigdyqg ldvlpsssfh pffvqtnagn ltnrtdvffa
      481 p
//
LOCUS       WP_175886872             340 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA-binding protein [Burkholderia contaminans].
ACCESSION   WP_175886872
VERSION     WP_175886872.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13774834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..340
                     /product="DNA-binding protein"
                     /calculated_mol_wt=37330
     Region          26..144
                     /region_name="KfrA_N"
                     /note="Plasmid replication region DNA-binding N-term;
                     pfam11740"
                     /db_xref="CDD:432038"
     Region          <116..>337
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
ORIGIN      
        1 msdlaadesr ltaeierlka dfpktrelyr eacallffrf gitptanrly qlvrkgsmst
       61 ptavlgefwa elreksrvri ehpdlpadlq aaagelvaal wnrssadaag aldalraeve
      121 aervaakaev aalqaelart etaleqrtaa llaaqvriqe leqaraadda srqaleaeie
      181 rltadnaegd ralaqaradf ttqldrlred agraeerlra sekralqeid rerlaaarlq
      241 keldaaalra eerdaqqrke vaalqaqlgd amhrcgvlqg qldgaqatda argkeldalr
      301 remtalsrrs alrgakaapa aqrderrart rkradeappr
//
LOCUS       WP_175886859             302 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia contaminans].
ACCESSION   WP_175886859
VERSION     WP_175886859.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..302
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=33579
     Region          26..276
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mhnpqavpdy lmqsdavrer farlkardvi ldvrhvgkrf atpqgectal ddisfrtyrr
       61 efvcvigpsg cgkstliril agldaqtsge vlldgkpveg pgadrgmvfq gytlfpwltv
      121 kknvmfglrm ngsssgqaer ealqwldlvg ltrfadvyph qlsggmkqrv aiaralanrp
      181 rillmdepfg aldaqtrarm qthlldiwrn idvtilfith dldeaiflad rilvlkanpg
      241 avqelievpv prprdysqvn tpefvatkar lealihpkea vaiddgvrph mvrmtdvsdn
      301 ve
//
LOCUS       WP_175886879             460 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia contaminans].
ACCESSION   WP_175886879
VERSION     WP_175886879.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..460
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49569
     Region          3..451
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mkqpedqlhr gleerhinlm algatigvgl flgsatairv agpailltyl aggiaiflim
       61 ralgemaian pvagafsrya rdylgplagy ltgwtywfvw ivtcmaeita vgvymhmwfp
      121 gvpnwiwala almamgsvnf iavklygefe fwfalikivt ivlmiigggl miafgigngg
      181 vaiglsnlwa hggfmpngin gvvaalpivm faylgvemlg ltagearnpe ksltkavnsv
      241 fwrvlifyig alfvimslyp wdqigtqgsp fvmtfsrlgi paaagiinfv vltaalsscn
      301 sglfstarml ynlaqqgqap sklgqvnrng vpvygvivsv allligvlln ylapqhvftw
      361 ltsvstfgai wtwcviliaq mrfrrtlsad kiarlpirvp fyplgsfval gflvlvvvlm
      421 aftpdtrval vigpvwivll gityalfyan rpaasvptks
//
LOCUS       WP_175886881             293 aa            linear   BCT 11-JAN-2025
DEFINITION  PilZ domain-containing protein [Burkholderia contaminans].
ACCESSION   WP_175886881
VERSION     WP_175886881.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..293
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30633
     Region          175..280
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mrlstdyvpl trddlaagvp lgfdlydadg aallpagttl hdaaqhaflf dhfrpvrrrd
       61 daeaaaeprm pdavphslrm glspgasigi rrrvgttrgl qrcrligiaa sgvlfvepqp
      121 vaaldfargd dieavaigra avsrfgatve svqatgaaqy lvlsppgfvd rlrsraeprv
      181 pvriaaccag gsegaegigm vrdvsvsgls iavdrpiaai geplrvqlpy avgdrvella
      241 ldgtvravha dpaapaltlh haafgetgad dlirlkallf drlmassdtg rrg
//
LOCUS       WP_175886943             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia contaminans].
ACCESSION   WP_175886943
VERSION     WP_175886943.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46929
     Region          28..433
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(39..40,43..44,47,86,144..145,147..149,152,172,
                     175..176,179,261,264..265,268..270,273,301,305,358..359,
                     363,367,383,386..387,390..391,394)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mqtrstldeh atiatpaper takhyllagw asmagttiew ydfflygtaa alvfnriffp
       61 sldpvvgtla afgafavgfi grpmggivfg hfgdrigrks mlmitlllmg vpsmiiglip
      121 sydsigywaa alliamrflq gmavggewgg avlmavehap kgrkglfgsl pqtgvglgli
      181 lssvamaava alpeadmlsw gwrvpflasi alvglgwfir akvpespdfe kmqrqgkaek
      241 spvtaalrrh prevltivga raaentwfym vvtfalayat qqlhlpkaem lhaitagaal
      301 slvtmplcgh lsdrigqrrm faiglvlmca faapffmmlg tqqtsyawwa ivlglgvvfp
      361 ilyapesllf aqqfpaeiry sgislsvqla gvigggfapm iatsllkagg gqphyviayl
      421 vgfgvfalmc talmrpara
//
LOCUS       WP_175886979             304 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia contaminans].
ACCESSION   WP_175886979
VERSION     WP_175886979.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..304
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33679
     Region          1..300
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mtrhdiefqs egatlrgwyy epaqriadta typaivmahg fsgvkeqyld ryaevfaagg
       61 fgvllydhrn fgasdgyprq eidpvqqrrg yrdaisyllt rpdvdaerig iwgtsysggh
      121 vlevaaidrr vkcvvsqvpt isgyqsalrr trsdlvpaal arfdedrrqr fagaapamlt
      181 avsadpatac amagadayrf ftesaaqfap nwknevtlrs aelscenepg qyvdrisptp
      241 llmivadqdl ltptdlclna wgsalepkrl lmikgghftp yiehfeatsq aavewftlhl
      301 rstr
//
LOCUS       WP_175887010             374 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Burkholderia contaminans].
ACCESSION   WP_175887010
VERSION     WP_175887010.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..374
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37724
     Region          17..373
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mtgfidtftl ggpgptiaik dtidiagypt raasralada ppamqhadvv rllldagwqi
       61 agkanmhela fgmtgindyt gtpvnpqdat ripggsssgs aslvglgmvd aalgtdtggs
      121 irgpaaccsv aglkptfgrv srrgvapvet tldcvgpfar dirtlvavma aiapgfdraq
      181 asasaagrtv ahvtvdadpa iataldaavr asglhahavv ldempasfva gltvinaets
      241 rafghlvetg klgadldarl raaattapaa lkeaeavrar ftaqvdaale hadvlvlptl
      301 palpitlqqa rdgvsviams slirpfnlsg hpalslplpl agsplkaglq iigrkgadeh
      361 vcaiaahfet alas
//
LOCUS       WP_175887011             521 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Burkholderia contaminans].
ACCESSION   WP_175887011
VERSION     WP_175887011.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 521)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 521)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 521)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..521
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=56891
     Region          <55..>204
                     /region_name="PRK13560"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:106506"
     Region          148..513
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mraaragaml gfrprdaarp hpmpimsfpd eddfhrllda lttcvllhda htkaivwanr
       61 aacialgfsv eellplkapd mtrpepkyqr eiavsawdra lvdgpqvyew cyrsrtgvdm
      121 lseatatyvp lrgrdvvmvq frdisaeeav rqqlrryear lrefmqdlde giavvtphgg
      181 vqfisesgrr vlglapdeal gevldycsea drdrlvaqlr dapsaypsap qryrivrrdg
      241 spcwlrilcr qveieddldg llvqfrdvsd evaieearra earmlehagr ynamgemasv
      301 iahelsqpla avrnfiegav qrlngrgaid daiwglrsad rqaehaalii ksvrefivkr
      361 epvvaladlr diladvayfi elrakeagvt vtivqagepl pihcervlig qvilnlafna
      421 ieafagcerv prtltlgtan vgghaelrai dngpgiaada hdrlfdgfss skaggngigl
      481 slcksivtrh ggriaaspad gggldcrvtl plagmeanas a
//
LOCUS       WP_175887015             374 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD/NADP-dependent octopine/nopaline dehydrogenase family protein
            [Burkholderia contaminans].
ACCESSION   WP_175887015
VERSION     WP_175887015.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13367875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..374
                     /product="NAD/NADP-dependent octopine/nopaline
                     dehydrogenase family protein"
                     /calculated_mol_wt=39667
     Region          1..>107
                     /region_name="GpsA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0240"
                     /db_xref="CDD:440010"
     Region          187..333
                     /region_name="Octopine_DH"
                     /note="NAD/NADP octopine/nopaline dehydrogenase,
                     alpha-helical domain; pfam02317"
                     /db_xref="CDD:426715"
ORIGIN      
        1 mkvcvlgggh gchaaaidll ekghdvtwwr rdrepharlr elgvlnvtdy rgkravplgd
       61 apgairltgd laaalrgaql vvvplpatsh dalaaqvapl ledgqvvflp pgtfgsfvfa
      121 qaaagagnrs rvafaetgtl pylvrkhgdn dvvisayatr lptgvlpana agwafdvlra
      181 gypsvepved alsgalmnag pvihpplilm nagplehfda wdihnegtqp sirrvtnald
      241 aeriavreal gyraphfpla dhyategdew mygrgahgkl tdsgdwreki dlrthrymle
      301 dtrlglsfiv scgrwagvpt pvaqgllsia savaerdlya egrtlerlgi aalskaamra
      361 lldagmtgva gvsa
//
LOCUS       WP_175887054             144 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia contaminans].
ACCESSION   WP_175887054
VERSION     WP_175887054.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..144
                     /product="cupin domain-containing protein"
                     /calculated_mol_wt=15641
     Region          23..126
                     /region_name="cupin_bxe_c0505"
                     /note="uncharacterized protein bxe_c0505, cupin domain;
                     cd06980"
                     /db_xref="CDD:380385"
     Site            order(28..34,43,45,47,49,67,69,71,73,91,93,95,112,114,116)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380385"
ORIGIN      
        1 mstptptafs hlkpqdtayr geglrdffly rdlgiaaatn gkvvaqlvra nhapeagtgw
       61 hrheaefhiv imlkgwarfm ygdretlvsa gdcvhqapgi vhylfdyspd meyleivgpa
      121 dftsidvegp cavppptpwg eaga
//
LOCUS       WP_175887057             221 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia
            contaminans].
ACCESSION   WP_175887057
VERSION     WP_175887057.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122607
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..221
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24808
     Region          9..80
                     /region_name="GST_N_1"
                     /note="GST_N family, unknown subfamily 1; composed of
                     uncharacterized proteins, predominantly from bacteria,
                     with similarity to GSTs. GSTs are cytosolic dimeric
                     proteins involved in cellular detoxification by catalyzing
                     the conjugation of glutathione (GSH) with...; cd03043"
                     /db_xref="CDD:239341"
     Site            order(20,22..23,25..26,29..30,73,76..77)
                     /site_type="other"
                     /note="putative C-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(20,58..60,71..72)
                     /site_type="other"
                     /note="putative GSH binding site (G-site) [chemical
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(58,70..71,73..74,77)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239341"
     Region          93..206
                     /region_name="GST_C_3"
                     /note="C-terminal, alpha helical domain of an unknown
                     subfamily 3 of Glutathione S-transferases; cd03194"
                     /db_xref="CDD:198303"
     Site            order(96,103,164,167..168,171,175)
                     /site_type="other"
                     /note="putative N-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:198303"
     Site            order(96..97,100..101,104,140)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:198303"
     Site            order(103,107..108,111..112,172,175)
                     /site_type="other"
                     /note="putative substrate binding pocket (H-site)
                     [chemical binding]"
                     /db_xref="CDD:198303"
ORIGIN      
        1 mevtgrqttl tissrnyssw smrgwllakl sgltfetvsv pidaasrael lllspsilvp
       61 clthdgntvw dtlaiaeyln eirpqarllp edrrarahcr svcgemhsgf salrsalpmn
      121 lrahfpgfri wsraqhdier ivtiwrecla ayggpwlfga eigiadamya pvvtrfltyd
      181 vklepdiaey cmqvlahpfv aewidaakae hedideldme f
//
LOCUS       WP_175887075             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175887075
VERSION     WP_175887075.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33689
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdyidklrif rsvvemrsft raadmhglar pvvsravadl earfgsrllh rttrqvslte
       61 taeriyerca avldeldsle aeaqaptrep egllrlvaht taalnrlvpl iagfkaahpk
      121 vrldvtlter pvdlvgegyd igivvpymlt nestvvrmie riplvivatp aylrahshpv
      181 apadladhpf vpmspslrrp tlsfrvdgdl ltvpfrfdis snspvfnrem vmhdfgigvv
      241 pktlvqaela sgalvqllad adlvdqfvei klayanrall pakvkafidy taaycdregw
      301 ivpaaa
//
LOCUS       WP_175887206             154 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia contaminans].
ACCESSION   WP_175887206
VERSION     WP_175887206.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..154
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17111
     Region          <39..128
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mtsqdvrfti cavraeetyp lraailmagd eegsalpgdl aptsmhfavh dndgivavas
       61 vcqeghagvl naeawrlrgm avhpsvrgmg fgrllvnlsi ryvreqhgll lwctaresay
      121 pfyemlgfnr dpkpismqrr ddmrfflmqr riag
//
LOCUS       WP_175887141             188 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            contaminans].
ACCESSION   WP_175887141
VERSION     WP_175887141.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..188
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20745
     Region          1..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 metkptvreq ildhaitlmm lrgyngfsyr dlselvgvkt ssihyyfpsk ddlvleavsv
       61 ysddvlsavr tidpalpadv klslytkmfg rtlgdgnmic lcgmlaadie slpenvrqav
      121 qvffkanesw laellaqgak egtlqfsgkp etaartlyaa fqgsvlasrl fhtrarledv
      181 eavwktrs
//
LOCUS       WP_175887240             607 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Burkholderia contaminans].
ACCESSION   WP_175887240
VERSION     WP_175887240.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..607
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=65900
     Region          36..595
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 msvlplafgq pavnrpdnas lielreqfvt dpintdlstl rpviarswqr smqsnvstgk
       61 rvldamaepe ldehflraae palndlerlf aeangclslc dprgtlavyr gthsmvkvad
      121 rlfptlggrm sesllgtnsd gtaieegcav qvwggehfne afqdacctsv lirdplhqgv
      181 rgvlsltlpe rfvrgldprt vmfilqgaas eitgalaari apgeqamlga ylrevrkrga
      241 eavvvmddht tiasraatql leqsdyavls afareakqyn rpsehqvvcg pdrvlqlqva
      301 pvhagnpkag siikvrkfdt sdtriavscp avrgsrfgal vgesfairra vesaaaaveq
      361 gigayvsgep gtgkkfiaqm iaqqlrthve sfdlgrrgda ealarhldde lsddsralli
      421 hrvdlasdtv lerlvavlag vdrspvvltv rqitdrllal faaakgvdir mpplrtrred
      481 ipllaqsfaq ssqggrrvsa rlldvlasae wadnvrelre viegaalrst gaeirvddlt
      541 evhkralars rlsplqqael qqirdalvea ggnrqraaai lriarstlyr kidsyesrgf
      601 dlgiamh
//
LOCUS       WP_175887253             252 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia contaminans].
ACCESSION   WP_175887253
VERSION     WP_175887253.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..252
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26156
     Region          1..245
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mqtgkkiaav tgagtgigqt aavalaqagf svallgrrid pllatqeiie rvggvaaaip
       61 tdvsdeasvd asfaqiahtf grldvlfnna grnagavpid dytvqfwndv vatnltgvfl
      121 caraawcqmk rqtpqggrii nngsisahtp rpntiaytat khavlgitrs laldgrpfni
      181 acgqidigna atsltermdr gvlqadgria peprvdvahv asaivqmanl pleanilnmt
      241 imasampfvg rg
//
LOCUS       WP_175887308             373 aa            linear   BCT 11-JAN-2025
DEFINITION  AI-2E family transporter [Burkholderia contaminans].
ACCESSION   WP_175887308
VERSION     WP_175887308.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..373
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40310
     Region          7..344
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mkpqtgrqtv lalllvglis lgivvlrpfv ipstwafiva yltwpiyerm crisgnrrst
       61 aallmtgllt lllvvpmlll tmplrresia fghevatwfs dgphtlprqv ssipwlgawl
      121 qaslddimye psawraqlaq wgnrwigmaa llaggvgrna vklgfalltl ffvyrdgkal
      181 leqvrlgmep ylgtrfeiyl aaigdvcrsv vygivlsaia qgalagigyw vagvaaplll
      241 ailtalaall pfgtplvwvp asiallinge iwvgaglllw gvlvissidn iirplvisgr
      301 ahmpflfvii sivggitafg lvglfigpfv vatllavwre wqtelvadkd kshenshdga
      361 egansreest akh
//
LOCUS       WP_175887315             246 aa            linear   BCT 11-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Burkholderia
            contaminans].
ACCESSION   WP_175887315
VERSION     WP_175887315.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..246
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=27389
     Region          139..225
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mattitepsc psphganpfa knwrwallfg ffvywgyrll elvlfgvvve qfgltseaqs
       61 ytilfayvpa lvflggmfyv hrrlvfpdiq figairrrdv vtgislvtlv yllgyglawl
      121 thqprepima glfqsktslq ivvmigamll lppvveelaf rhfllsllpf raswrvaava
      181 vcatalffsy vhayqywttn ltiflvgvvf avarirsngm vlpmmlhaya valalaldql
      241 mattvg
//
LOCUS       WP_175887331             258 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Burkholderia
            contaminans].
ACCESSION   WP_175887331
VERSION     WP_175887331.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..258
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=27335
     Region          4..255
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mqtidvtiqs niatltlnrp dkrnavsdam rtelidalds larapevrav ivtgngkgfc
       61 aggdiagmaq rmeapadeva fngwsrqqrv hhavsllhtm pkptiaavng aaaglgadma
      121 lscdfviase aatfvwsyik rglvpdgggl yflprrvgla aakdlifsgr kvdarearel
      181 giadrvsapd tlladatawa qelikgspta lalgktllnq syelsaaqml aqgsqaqavc
      241 ytsrehrsav refldntr
//
LOCUS       WP_175887350             237 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia
            contaminans].
ACCESSION   WP_175887350
VERSION     WP_175887350.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..237
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26577
     Region          90..237
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          181..234
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mnlsasditp eelrlfgdiv arleelgpvv dvrtvvlpai tqllradfaa sfdcdvhtgl
       61 wrngfsynvd pfqiaryeaw fqhidpvtsq lrarrvatcv devvsrcele rtefyndflc
      121 rdgmhhginv yafdgathvg dlriwrakgr pdfterdkll lngiepffrr allrrrhact
      181 glteresdva rlvaagypdk dvartlgigv ptvrthlrrv makkgvanra slaaala
//
LOCUS       WP_175887363             940 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Burkholderia
            contaminans].
ACCESSION   WP_175887363
VERSION     WP_175887363.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 940)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 940)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 940)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..940
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..940
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=102813
     Region          83..877
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mpalcdicha rpavaratvm qdgerktisi cdyhfrqlmr hqsmlnpfds llggggsssl
       61 fgglddespl aaeipresvd ptdafseqtl ellqraaeka helrrselds ehllyaladt
      121 dvcaallkel klspqdirsy idehahtgta aadapldkls isprvkkavq yafqasrdlg
      181 hsyigpehll iglasvpdsv agtllkkygv tpealrqkvv kvvgkgaedg rvdaptgtpn
      241 ldkfgrdlta iarqgkldpv lgraqeiest ievlarrkkn npvligepgv gktaivegla
      301 qrivngdvpe vlrdkrlvev ninsmvagak yrgefeerak qlidevtakq delilfidel
      361 htivgagqgg geggldianv lkpalargel sligattlne yqkyiekdaa lerrfqpvfv
      421 pepsveqtiv ilrglrdsle ahhqvtfadd afvaaaefad ryitsrflpd kaidlidqaa
      481 arvrigatsr pvdiqegeaq iaqlkreqdy atsrkrfdea kqfeeqinak qksvdekmea
      541 wqrktgsetl evtvesvaev vsrltgipvs eltqeerqkl lkmeeqlrer vvgqsdavva
      601 vsdavrlsra glgqthrpia tflflgptgv gktelakala etvfgdeqai iridmseyme
      661 rhavarliga ppgyvgydeg gqltervrrr pysvilldei ekahpdvynv llqvfddgrl
      721 tdgkgrvvdf sntiiiatsn lgaaiimdnl tqpeaarktd kaireqlmqv lkghfrpefl
      781 nridevivfh alskedirai vqiqldrvvr taaaqditlv mgdslvahlt eagyqpefga
      841 relkrqirqt ietrlakeil adrlksgdkc evdydkdsde vkfnklaape akdtkdangk
      901 akpngkaaka aadanaddtp papaakssgk kssgakkdah
//
LOCUS       WP_175887383             370 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia contaminans].
ACCESSION   WP_175887383
VERSION     WP_175887383.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..370
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39118
     Region          4..344
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,233,300,320,322..324)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,181,184,186,233,240,300,320,
                     322..323)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,181,184,186,323)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            186
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mssllsaydl rglalpnrvv mgpmtrsrap srglptelma eyyaqrasag livteatnvs
       61 rasaafeltp glvddaqaag wkivtdavha nggrifaqlw hggrvssltl lggaaplsps
      121 gvnddleqlq vwaqlqngyy tkihatpsra mttdevvaav defrqaatra maagfdgvei
      181 haangylphq flsstlnrrd dryggslanr arflaeiida vggvmplgrv gvrispyaky
      241 nnvrdadpda tlayvgrmld dagvaylhaa dtngwsgepd lpriveharr sfggtlivng
      301 gispdaanal idagdadlva farsyianpd lverlaarvp laepktvgwy ggdragyvdy
      361 arhdaagspa
//
LOCUS       WP_175887386             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175887386
VERSION     WP_175887386.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32160
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdkfsalraf vevaeaggfs sagrrldlaa ssvvravdal easlgtvlln rttrqvtlsd
       61 agavyyarak rvleeladad alvadrgdep sgplrvsvpv ayglrriaph vaafvarhpk
      121 ldvdlqltde rvdlvsarid vairlgdaap sadvvarplg tfrryvvasp ayldahgtpa
      181 tpgelvdhac lrfhfgadqq awtfadargt tpvivagrlk snhsevlrea aldgagiall
      241 pdwmvgpdid agrlrrlfer yevtpgsars vitalylpnq rgskrvtafi dfveslaraq
      301 p
//
LOCUS       WP_175887408             542 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia contaminans].
ACCESSION   WP_175887408
VERSION     WP_175887408.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..542
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=59179
     Region          1..529
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mknsfdylvv gggsagsvla srltedpdvt lclfeaggtg dgwpvnvpaa lvlmipsrln
       61 nwafetvpqk glqgrrgyqp rgkalggssa inamvytrgh hadyddwaal gnegwgwndv
      121 fpyfkrsehn erlgnewhgr ggplwvsdlr tdnpfqarwl daarecglpv tddfngaeqe
      181 gvgiyqvtqk ngerwsaara ylfphmktrg nltvetgaqv rrivfdgkra vgvevarggn
      241 vetvwakkev ilsagafqsp qllmlsgvgp kdelerhgie vvadlpgvge nlqdhpdfvl
      301 syktnsldal gvsvrgaikt lgdirqyrns rtgtlttnfa eggaflktrp eldrpdvqmh
      361 fvvgpvsdhg rkvrlghgls chvcllrpks rgsvklrsad pldaplidpa fldheddlev
      421 lvegykltrr lmaapamarf vtedmfasrs rsdddirall rertdtvyhp vgtcrmgnda
      481 lavvdsqlrv rgteglrvvd asimptlvga ntnaptimig ekasdlirri srfpsampet
      541 av
//
LOCUS       WP_175887389             317 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia contaminans].
ACCESSION   WP_175887389
VERSION     WP_175887389.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..317
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34243
     Region          <227..315
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mislnlrhvl rmttastaml aallaaapsh adethlddta rqpaaarfpa vavgpqydtt
       61 hvcvapedfd rftdsfvatf ggkkskqgvf qvtptpsqtm sqlvltpvgt isvfgfktpi
      121 pypfceertg ylvtdmdmav ksarahgadv vvatfpdpig rdaiirwpgg vnmqlywhtq
      181 apnydplqtv penrvyvspe rasklahdfv afshgkivsd vrkapgieig rpndtyrrir
      241 iesgfgkmtv latdghlpyp fgremtgyev adlaatleka kaagvtvlvp pftadgrdaa
      301 lvqfpggyva eiharsk
//
LOCUS       WP_175887415             320 aa            linear   BCT 11-JAN-2025
DEFINITION  1-phosphofructokinase family hexose kinase [Burkholderia
            contaminans].
ACCESSION   WP_175887415
VERSION     WP_175887415.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..320
                     /product="1-phosphofructokinase family hexose kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008443 - phosphofructokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32765
     Region          4..306
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 mteivtvtln pavdvstsve hivdthklrc arprrdpggg ginvartvhr lggdcvalyl
       61 aggptgdvlt llldaehvpa vrlriagetr envcvtetat greyrflmpg psvtaaewrd
      121 caariaalqp aprylvlsgs lppgapddly atlartaaan gtrvvvdaag palraaldag
      181 vhlvkpslde lsalagepld easacgkaae lvaqgradiv altlgargaw vvtreralrl
      241 pgrpatvcst vgagdsfvgg mvwalargap fddacryala asaasvehpg talctradve
      301 rihaelvaqa sgaaiargta
//
LOCUS       WP_175887449             200 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            contaminans].
ACCESSION   WP_175887449
VERSION     WP_175887449.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22083
     Region          1..157
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mraskrqqvv dkagelfslh gfhpvgidri iaeadvarmt lyhhfaskdd likavleqry
       61 tfimesmaak lgpmphaaar lkgifdwygt wfsspefagc lferalaefg atcpkvtdva
      121 vryrddllal meqllaeivp rrrasqlagv yvmllsgata daraigdpra aarawqaaem
      181 llneskvaae smrkarsrra
//
LOCUS       WP_175887451             191 aa            linear   BCT 11-JAN-2025
DEFINITION  YbhB/YbcL family Raf kinase inhibitor-like protein [Burkholderia
            contaminans].
ACCESSION   WP_175887451
VERSION     WP_175887451.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..191
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=20424
     Region          29..186
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mrfdtflrsg icatvlfaiv pavafadplt vtvddldhdg rfsnaqvyng fgcrgdnvsp
       61 rvswahvppg trsivvtmyd pdaptgglgw thwevvnipp setsirkgas gdarrmpvga
      121 letltdfges ryggpcppqg eshryvvtvs alsiarvdvk stsspavvay qmhgnilgqa
      181 ryvatyhrss n
//
LOCUS       WP_175887463             296 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia contaminans].
ACCESSION   WP_175887463
VERSION     WP_175887463.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13484798
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..296
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=33734
     Region          2..>193
                     /region_name="PRK12678"
                     /note="transcription termination factor Rho; Provisional"
                     /db_xref="CDD:237171"
     Region          178..>253
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mqrrypgrhr erggppdwqe rnerayrgag ergipddpar wpeagdesay rrfasedvgp
       61 edwgsewter aarpvgqrrg apdagwqgdf qreparepep gygerdrraq grdwrespyg
      121 esqyrgvppe frgqhrmggy dsgrargdpr dypryggdap dpsrfgsdae rdalrnrrgp
      181 kgytrsderi redvcerlah afdidvsdvt vqvqdgrvel dgtvparwmk hgiedladgc
      241 mcvrdvenrv rvrregehep gmvlhpdqrt vtptqpavld pepgtvghdr erkphh
//
LOCUS       WP_175887518             339 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Burkholderia contaminans].
ACCESSION   WP_175887518
VERSION     WP_175887518.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..339
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=37871
     Region          60..332
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mscqlfrvgk fwhyrfqing hrvqrstkct tyadaqsiar nayrsayasc ghhsrlvipt
       61 ladltqawld ahamiaspsh lagvdafrrl hlyhlgnipi dclttaavee arnhhlqsha
      121 astvnhwsri vrllgnwavh rgiidrvpfk vkmlklqrrp ratlpvdlsg qwlaaidaia
      181 sapvriairl mlgvglrese aatarwewld lvrqtytpgr tkgreadpvp vpawltdylr
      241 plrqstglmv vrpdgrpfar gftrasikva narigigeit phrlrgtfat llsengapvq
      301 viqrvmrhks plttigylea dltraaraqa rigeqygfq
//
LOCUS       WP_175887537             108 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia contaminans].
ACCESSION   WP_175887537
VERSION     WP_175887537.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..108
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11245
     Region          23..106
                     /region_name="CytC552"
                     /note="Cytochrome c551/c552 [Energy production and
                     conversion]; COG4654"
                     /db_xref="CDD:443692"
ORIGIN      
        1 mkhstlrvll amlligsgaa aradqadgla laqrkncmac haigkplmgp sfrdiagkya
       61 argdavdyla qsivkgsvgv wssvpmpant qltnseahtl aqwvlsvr
//
LOCUS       WP_175887641             136 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Burkholderia contaminans].
ACCESSION   WP_175887641
VERSION     WP_175887641.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..136
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=14879
     Region          32..134
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mntnptlaer qtntvhpaaa eaarrpaitp avdivenhlg vtlradlpgv prenldvkvh
       61 dntltieadt hldtpadlrv rhaeiratry arsfvlspdl dtsridanlr dgvltltipr
      121 reetrprrid vtggna
//
LOCUS       WP_175887668             134 aa            linear   BCT 11-JAN-2025
DEFINITION  PaaI family thioesterase [Burkholderia contaminans].
ACCESSION   WP_175887668
VERSION     WP_175887668.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..134
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14429
     Region          15..134
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mdenavrell drllapwfrs lglvpvsigd dsvtlrlpfs gefrhsggii cgqvftaaad
       61 tamvvaisaa lgefrpmttv slntnfmrpv rkgdvlvtar vlrmgrnlvf gevelfdedg
      121 kmavhatsty alvs
//
LOCUS       WP_175887682             548 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Burkholderia contaminans].
ACCESSION   WP_175887682
VERSION     WP_175887682.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..548
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58364
     Region          13..529
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 maaatptgal valhhvsfrf ddgftlfdsl dlsidrtptg ivgrngigks qlaqliagcy
       61 apsagtierh tsvvyvaqqh ddgdvsagpr tvaqiaaldg plgalarlad graephdfdl
      121 igdrwdlaer lrtaldaagl hdvradtpaq alsggqlarv aligallsga gllvldeptn
      181 hldapgrawl raaldgwrgg vvivshdral lagvqrivel tpqgvrsygg nyalyraqrd
      241 aeqdaaqsal dnaraergrv rrrleqehdt iqhhaaaslr daksanlssm akqsrkgaar
      301 simgtvrrhq nefkatlder vqeaaarvea dapvlvslpg tevsarrqlf tlerahlpwh
      361 iagaadaitw sasgparial tgpngcgkst llrmlagele prsgactthv saayldqrla
      421 lldpdrsive qlglldtpla egdlrsrlar lqldavratq parqlsgger lkaalacalw
      481 rgtpaqllll deptnhldle svraieaala gfpgaivvas hdpaflaald pthtmqwhrd
      541 gwryepva
//
LOCUS       WP_175887700             386 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF4382 domain-containing protein [Burkholderia contaminans].
ACCESSION   WP_175887700
VERSION     WP_175887700.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10626736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..386
                     /product="DUF4382 domain-containing protein"
                     /calculated_mol_wt=38903
     Region          33..184
                     /region_name="DUF4382"
                     /note="Domain of unknown function (DUF4382); pfam14321"
                     /db_xref="CDD:433865"
ORIGIN      
        1 mnniiksalc aafvpfvlag cgggddggsa tqtgtlhvam tdapscgfdh ayitvsqvrv
       61 nananaadnd agwstitlat pqkmdllslt ngvladlgqt alpagqyqqv rlvltqnqgn
      121 nlansvvptg gteqalatps atqsgykiih pftvqpntlv dlvldfnack sivqrgngty
      181 alkpvvtaip tvvsgaisgy vasaeagatv yaeqggkvvr gtvadstgkf vlspliqsst
      241 qgnydvvivq nnfasgivrs vpvivnttta vsastapitl pasttstvsg tvtasanafm
      301 ralqtvdana yeitainanm dtgayalnvp taapivgtys gslpvalaaa ptaagqytie
      361 adaasgatqs tnvnattsqs nvnftf
//
LOCUS       WP_175887718             155 aa            linear   BCT 11-JAN-2025
DEFINITION  inorganic phosphate transporter, partial [Burkholderia
            contaminans].
ACCESSION   WP_175887718
VERSION     WP_175887718.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..>155
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
     Region          21..>155
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 mhsiqlalwm vaalvlvalv fdfmngfhda ansiatvvst gvlkpqqavv faaafnviay
       61 fifhlkvaqt vgkgtidpei vdhyvifgal vgaigwnvit wyygipssss haligglvga
      121 alaksgwssl nidgllktia fifispllgf ilgsl
//
LOCUS       WP_175887721             155 aa            linear   BCT 11-JAN-2025
DEFINITION  inorganic phosphate transporter, partial [Burkholderia
            contaminans].
ACCESSION   WP_175887721
VERSION     WP_175887721.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..>155
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
     Region          6..>155
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 mhsiqlalwm vatlvlvalv fdfmngfhda ansiatvvst gvlkprqavv faaafnviay
       61 fifhlkvaqt vgkgtidpgi vdhyvvfgal vgaigwnvit wyygipssss haligglvga
      121 alaksgwssl nidgllktia fifispllgf ilgsl
//
LOCUS       WP_175887777             515 aa            linear   BCT 11-JAN-2025
DEFINITION  FGGY-family carbohydrate kinase [Burkholderia contaminans].
ACCESSION   WP_175887777
VERSION     WP_175887777.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..515
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=55256
     Region          3..448
                     /region_name="ASKHA_NBD_FGGY_RrXK-like"
                     /note="nucleotide-binding domain (NBD) of Rhodospirillum
                     rubrum xylulose kinase (RrXK) and similar proteins;
                     cd07804"
                     /db_xref="CDD:466806"
ORIGIN      
        1 meyvigvdig tqstkallvd rhgrivarrs agyqpdtprp lwaeqwpqvw fdavlaciag
       61 cvsdaraqgv psdairavcv gslyggsgip vdiymrplhp cliwmdrrat aevdwvnanv
      121 nverlrvitg ngvdsyygft kmlwlrdqrp dvwanvryfl ppnayviyll tgevavdhss
      181 agniggvydv arrewsddal dmlgipatmm perlvestdi vggllsqwte qlglpagtpv
      241 vaggvdaava tfaagathag qhvamigtsm cwgyvsqhvd arhglvsmph vfngqrdlyv
      301 fggaitagas vawfrdqfch aeidaarllp hgdphvllee aaesvppgad gvlflpylmg
      361 erspvwdaka sgafvglsla htrthlyrav legvafalrh nieagrqgaa alddrlivvg
      421 gaahsalwmq iiadvtgfpv wtieqdveaa mgaallagvg aglvshddaq ggwvtlvera
      481 rpdverakay aarfalytal ypalkpimhg lhtps
//
LOCUS       WP_175887838             204 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia contaminans].
ACCESSION   WP_175887838
VERSION     WP_175887838.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..204
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21636
     Region          1..192
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mnnllfvdas phgshslgar iaheaiaqwr aarpdarvvs rslgqpglps lsadyaravv
       61 arqpdsdpal tyseqliaev ehsdgvlist pmhnftvpaa lklwidfvlr igrtftatpe
      121 gkfglladrp vlvlvrsggv ctgaaarqpd fltpylkqvl aviglstvdf iyleglapsd
      181 taidavraql aastllarrt teta
//
LOCUS       WP_175887835             244 aa            linear   BCT 11-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Burkholderia
            contaminans].
ACCESSION   WP_175887835
VERSION     WP_175887835.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..244
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27364
     Region          71..225
                     /region_name="CE4_NodB_like_5s_6s"
                     /note="Putative catalytic NodB homology domain of PgaB,
                     IcaB, and similar proteins which consist of a deformed
                     (beta/alpha)8 barrel fold with 5- or 6-strands; cd10918"
                     /db_xref="CDD:213023"
     Site            order(74..75,140,144,180..182)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213023"
ORIGIN      
        1 mllpasrypi ltyhqvrtlp pptdrlrsls vapdafrrqm mlfrrlgyrg vsvrelqpyl
       61 rgersgkvfg itfddgflnv lthampvlda lgftatcyfv agrfgrendw dagadtnrsp
      121 lmtfadmlaw rdhgheigsh tldhvalsqv pahvsevqii eskrrleafs gqpvesfcyp
      181 ygdldprvrd qvaaagyrna tttrrgcada yddrfllpri tvaggvgamr lwfkcakarv
      241 qrrg
//
LOCUS       WP_175887843             305 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia
            contaminans].
ACCESSION   WP_175887843
VERSION     WP_175887843.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Grant Pearce,F., Hudson,A.O., Loomes,K. and Dobson,R.C.J.
  TITLE     Dihydrodipicolinate Synthase: Structure, Dynamics, Function, and
            Evolution
  JOURNAL   Subcell Biochem 83, 271-289 (2017)
   PUBMED   28271480
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Laber,B., Gomis-Ruth,F.X., Romao,M.J. and Huber,R.
  TITLE     Escherichia coli dihydrodipicolinate synthase. Identification of
            the active site and crystallization
  JOURNAL   Biochem J 288 (Pt 2) (Pt 2), 691-695 (1992)
   PUBMED   1463470
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..305
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0009436 - glyoxylate catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=32863
     Region          8..292
                     /region_name="DHDPS-like"
                     /note="Dihydrodipicolinate synthase family; cd00408"
                     /db_xref="CDD:188630"
     Site            order(11,43,46..48,139,167)
                     /site_type="inhibition"
                     /note="inhibitor site"
                     /db_xref="CDD:188630"
     Site            order(43,46..48,139,167,210)
                     /site_type="active"
                     /db_xref="CDD:188630"
     Site            order(47,52..53,84..85,109..110,120,124,276..277)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:188630"
     Site            167
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188630"
ORIGIN      
        1 mnaryqgvfp vvptifdatg aldldgqrrc lefmidagsq glcihanyse qfalgdderd
       61 litrvtlehv agrvpvivtt shfsaricaa rnrraqalga amvmvmppyh gatfrvpeaq
      121 vraffreaad gldiplmiqd apasgvalpa pflaslarei davsyfkiet agaasklrel
      181 ialggdaieg pwdgeegitl ladldagatg amtgggypdg irritdayfa grrdeaveqy
      241 arwlplinye nrqsgfltak almreggvia cdtprapwpe lpppvragll daarrldplv
      301 lrwgr
//
LOCUS       WP_175887856             454 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia contaminans].
ACCESSION   WP_175887856
VERSION     WP_175887856.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..454
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47755
     Region          228..409
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mrldlrfrla reqgqpaqrg vhgfpmhral lrgviaaacv agapgmvaha shdaapfepv
       61 tadlvdvpff naarttwggl hastagpldv tyashalsvp tagerddpva rfgacvayrv
      121 lcdaargave rayasrfdyg lasalpitge qavferrpvd laaaepfvla qaergargga
      181 ivgslqasla raelpagvaa qitrmlagrv dlkqrgalgd tfrvayepdd satlpggvrv
      241 talelrlrgq rvaavwfaae agspgayydl dgmpfagsrf ampvnakris shfgarvhpv
      301 tgarhvhsgv dlaapagrav hasergvvtf igteprgygk yvvirhdggy asyyahlsaf
      361 eptlragtrv argqrvgavg stgtatgphl hfevrrharl vdpvalvqag kaaklkgerr
      421 vafnrvvlda rtrlasvewv qpvamskpag prag
//
LOCUS       WP_175887894            1068 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia contaminans].
ACCESSION   WP_175887894
VERSION     WP_175887894.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..1068
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=114674
     Region          1..1043
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 miahiirwsv hnrflvllat vliaawgvhs lrqtpldalp dlsdtqvivk asypgkapqi
       61 vedqvtyplt ttllgvpgak tvrayssfgd afvyvlfddr tdpywarsrv leylsqvqsr
      121 lpagatvslg pdatgvgwvy eyalvdrtgr hdlgqlraln dwflkfelka vpdvsevasi
      181 ggmvqqyqvv ldpdklrayg itqaevatal gnanqasggs vvelaeseym vrstgylrtl
      241 ddfrhvvlrt ndagtpvllg dvariqvgpa mrrgiaelng qgevtggvvv mrsgknaltt
      301 idavkaklad lkrslppgve ivttydrsql ieravgnlkd klieefvivg lvcavflfhl
      361 rsafvailsl plgvlaafiv mryqgvnanl mslggiaiai gamidaaivm ienahkhlea
      421 ydhahpgepi tparrwelva tsaaevgpal ffslliitls fipvfslegq egklfaplaf
      481 tktytiaaaa glsvtlvpvl mgylvrgrip hehanpinrv lirayrplle atlrrpwvai
      541 giavvalvlt avpvsrlgge fmppldegdl lymptalpgi sadkasellq qtdrliktvp
      601 evdtvfgksg radtatdpap lemfettirf kprsawrpgm tpeklvdeld rtvkvpglsn
      661 vwvppirnrl dmlstgiktp vgvkisgpdl agidaiakqv eaavkpvpgv tsalaerlng
      721 gryidvdidr laaaryglsv advqsvvsta vggddvgevi agrerfpini ryprevrdsv
      781 enlrqlpvvt argaqirlgd varitiadgp pmirsenarl sgyvyvdlrg tdlqsavram
      841 qqavarqval ppgysiawsg qfeyleraaa klrtvvpvtl vvifvllflt fgsaadalll
      901 mstvpfalvg gfwlvwalgh avsvatsvgf ialagvaaef gvvmllylkg alqrrldage
      961 pltdalllda iregavlrvr pkamtvavvl aglvpimvgh gagsevmqri aapmvggmvt
     1021 apllsmfvip aawlllqrrr aqsmgharhs eavphgtnvp siptgesr
//
LOCUS       WP_175887908            1048 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia contaminans].
ACCESSION   WP_175887908
VERSION     WP_175887908.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..1048
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114722
     Region          11..1027
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msvsyeegrf nlsawalrhq alvvyliala tlagilaytr laqsedppft frvmvirtfw
       61 pgatarqvqe qvtdrigrkl qetpaidflr sysrpgesli fftmkdsapv kdvpetwyqi
      121 rkkvgdigyt lppgvqgpff ndefgdvytn iwtlegdgft paqlhdyadq lrtvllrvpg
      181 vgkvdyfgdp gerifievdn aqltrlgisp qqlgqainaq ndissagtlt taddrvfvrp
      241 sgqfdnvdai agtliringr tfrlgdlatv krgyddpqvt qmrangkavl gigvtmqpgg
      301 dvirlgksld aeskdlqaql paglkltlvs smphavahsv ddfleavaea iaivlvvslv
      361 slglrtgmvv visipvvlav talfmylfdi glhkvslgtl vlalgllvdd aiiavemmav
      421 kleqgytrar aaafaytsta fpmltgtlvt vsgflpiala ksstgeytrs ifevsaiali
      481 aswfaavvli pllgfhllpe rkrqaheahl pddhehdiyd trfyrrlrgw idwcierrfv
      541 vllitgalfv valmgftlvp qqffpssdrp ellvdlrlpe gasfaatlre terlekvidk
      601 rpeidhsvnf vgsgaprfyl pldqqlqlpn faqfvitaks vkdreklatw lettlreqfp
      661 avrsrlsrle ngppvgypvq frvsgdsiat vrsiaekvaa tmrgdartvn vqfdwdepae
      721 rsvrfeidqk karelnvtsq dvssflamtl sgttvtqyre rdkliavdlr apradrvdpg
      781 klaglalptp ngpvplgslg rfkptleygv vwerdrqpti tvqsdvraga qgidvthavd
      841 aklndlraql pvgyqinigg sveesakaqk sinaqmplma iavftllmiq lqsfsrvlmv
      901 vltaplglig vvatlllfgq pfgfvamlgv iamfgiimrn svilvdqieq diavghrrid
      961 aiigatvrrf rpitltaaaa vlalipllrs nffgpmatal mggitsatvl tlfylpalya
     1021 twfrvkrder dpqdgpppgg traapsga
//
LOCUS       WP_175887911             330 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Burkholderia contaminans].
ACCESSION   WP_175887911
VERSION     WP_175887911.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..330
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34866
     Region          6..301
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(37..38,41,93,108,110,139,172,261,264,300)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(230,235,251,261..263,266,288,292)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mkaaldvvty geamamfvat epghlahatq ftkrvagadl nvaiglsrlg frvgwmsrvg
       61 rdsfggyvld tlaregidas cvtvdprypt gfqlksrndd gsdptveyfr kgsaashlsc
      121 ddyvadyvlg arhlhltgva paisatscel afklaremra vgktisfdpn lrptlwpsad
      181 vmaktlnala sladwvlpgi aegrqltghd tpadiagfyl aqgargvvik lgaegayyrt
      241 adgrdgtvtg ervqnvvdtv gagdgfavgv vsallegkti eqavargnri galaiqvigd
      301 seglptraal drfenvsnrt drleetftaq
//
LOCUS       WP_175887914             303 aa            linear   BCT 11-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Burkholderia
            contaminans].
ACCESSION   WP_175887914
VERSION     WP_175887914.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..303
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31469
     Region          76..282
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mtkrslaala asilmsvaai dgfvapqlah aqasgaagts aqaaapsaap apvpaaaepa
       61 pppapattea venpyglgal wkngdfvarf vlillvimsm gswyimitkf veqlrtnrra
      121 kladaqlwsa pslaegarll deaspfrfia etaieagehh dealleavdr ntwidvsver
      181 sitnvsnrmq dglaflatvg stapfvglfg tvwgiyhalt aigiagqasi dkvagpvgea
      241 limtaiglav avpavlgynf lvrrnksvme rvrnfgaqlh tvllagnrrp vrasspaaas
      301 lan
//
LOCUS       WP_175887951             307 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia contaminans].
ACCESSION   WP_175887951
VERSION     WP_175887951.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..307
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33781
     Region          38..293
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 matdnraart wppkhdrhda hrvdarkpqk mtgnlagraw kalvwglmaf fllnvmllia
       61 tvavnsiatr wfgtplpqgf tlhwyakawe dfqlasvlwv tvevvgavvl lsialgvpaa
      121 yalarvqfrg krfallvfll plmvppvtyg ipmatvmykv glagtlpgvi lanlvpalpf
      181 vilvmtpfie qidpnleaaa rifgantwry fryvllpllv pgmlaagllv lvrtigmfel
      241 tfftagpstq tlvvalyyav fstgvrapqs idamamiyma itlvwvvial qfvsptqlvs
      301 rvkqerq
//
LOCUS       WP_175887992             382 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia contaminans].
ACCESSION   WP_175887992
VERSION     WP_175887992.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..382
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40956
     Region          1..370
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masismrrvq kaygdhapvi rdvdleigah efcvflgpsg cgkstllrmi agledlsage
       61 lsidgrrvdd vpaaergvam vfqsyalfph mtvyenmafg lklarvpkae idrkvrdaar
      121 ilqldtlldr kpkalsggqr qrvaigraiv repgvflfde plsnldaalr gqtrieiakl
      181 hrqferasvv yvthdqteam tladkivllh agadtaqhgs iaqvgapldl yhhpssrfva
      241 gfigsprmnf lpavvtacda hrttvtltps getfvlprdg salgagatva lgirpehltl
      301 gtahdatsla rdvalverlg eqtyvhldqp gghsliakvp gdaqvrsger vlvhapaaac
      361 hlftedgrav pacadvhvhh ya
//
LOCUS       WP_175887999             282 aa            linear   BCT 11-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Burkholderia
            contaminans].
ACCESSION   WP_175887999
VERSION     WP_175887999.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..282
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31485
     Region          11..263
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mtsiqdrvaq avtsellaaf redgavcikg ifspdevaal ragidanlaq pserakvasr
       61 pddpgwffed fcnwqhnday rdfivrspap svaaalmgtd nvrlhhdhll vkepgtrqrt
      121 pwhqdqpyyn iegddnvsmw ipvdpvples tlefvagshl gpwlmprtfm dkeakwfpeg
      181 sladlpdieg draafpirrw alepgdmvcf rmltlhasgg tqnrrrafsi rfvgddirha
      241 prrwktspdf pglaeqlpdg apldhplfpv vwsrgagqvr ai
//
LOCUS       WP_175888014             350 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia contaminans].
ACCESSION   WP_175888014
VERSION     WP_175888014.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..350
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=37086
     Region          4..350
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mqrkaflvga cvlyatsaha ssvtlygivd syvefdrvgs lssvrqsggg sstsrfgltg
       61 vedlgggtst kfvlesgfsp adgsfqggtl fyrqayvalh strygdlrlg rqytpsfyvv
      121 ydgdpfglne rlsplallat stdtitpntt ppiprfnqav sylspdwngl rvmatygfpt
      181 pnalstqagr nygaglqyri gglyvgagfq gdtsagnlsp vvspsttrhy vfatnyafah
      241 vklyaaflyg vstarnlpaf stasagasid vgaldrvlvs vvrrdvkgsa ndatalglgy
      301 dhplskrtsl yarylymkng gdarntvvvg lqpqpggteq vfalglvhrf
//
LOCUS       WP_175888051             517 aa            linear   BCT 11-JAN-2025
DEFINITION  S41 family peptidase [Burkholderia contaminans].
ACCESSION   WP_175888051
VERSION     WP_175888051.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..517
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55217
     Region          69..433
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mmpstrvvlr laicaavtat llpcvssvga qqpasappas aasapaaspa kaqppspcpp
       61 dwepqicelk aavellkkqh ltdidigall datthagikt lpyarffdak eeqerrdder
      121 rardgtpgig ivfetrpdgl hivdvtpdap aekagvrpdd lvvamndtsv vgidaadlak
      181 lakgdagvpl kltvqrgpsh avlsfapvrt ilkphpatak rldgdilytr lssfpepavg
      241 dyvdavqaar ragppvkgvi ldlringgga lnaaigital fagrdrtamv tvergdanrr
      301 ryttnwpdye lpvmhgqdpl aplqaddwwr tvplvvlvdg qsasaaeata aalkdlgrak
      361 llgmptygkg laqtgvdlid gtrlnftyar nlrpngcpmd gygvvpdwlv pprrdsdvdg
      421 vllwyreadl arapyadrla pdpfakvrke rqklreqral akidtaksaa lpqrefgtat
      481 dwqldqalaa lagrpvrtve arpqlmpaqp vceragn
//
LOCUS       WP_175888100             244 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia
            contaminans].
ACCESSION   WP_175888100
VERSION     WP_175888100.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..244
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=27371
     Region          <1..152
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(42..44,46..47,51,54,63,65,68..69,72..74,76..77,81,
                     84,93,95,98..99,102..104,106..107,111,114,123)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          65..93
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          95..123
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          125..152
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          154..181
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mdwshelwha ayngdfdrvk eaikqgadir aidagalgfs aekghleivk clvewgvdih
       61 amddwalrda akkghleivk ylveqgadih trddwplrya aeeghldivk ylveqgadih
      121 aydysflias arghleiakh ltelgadiha dnewalrias rngqyqvcqy lvsqgcdlqk
      181 vvddkessqe skqwavdfvk ardlsnkltn elaekpskad llvssineda pppqkqtrst
      241 rqki
//
LOCUS       WP_175888126             109 aa            linear   BCT 11-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Burkholderia
            contaminans].
ACCESSION   WP_175888126
VERSION     WP_175888126.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 109)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 109)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..109
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=12850
     Region          4..101
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mshkvhilaf akddyreirs yvkrqfgnnv wkeveadykk vigqiaempe tgsipeevsa
       61 lgitdyrqrl vrqtrvlyqi kdneiyvhmf ldtnrdfqtm llkrlmkia
//
LOCUS       WP_175888116             182 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia
            contaminans].
ACCESSION   WP_175888116
VERSION     WP_175888116.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..182
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=19792
     Region          12..>147
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(44,47..49,51..52,56,59,68,70,73..74,77..79,81..82,
                     86,89,98,100,103..104,107..109,111..112,116,119,128)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          70..98
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          100..128
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mskntgkhnk elmraaedge ldevkkalsn ganihsdngr vlgiasgngq ldtvkylier
       61 gariradndf afisavendq leivklliek gadihadndm alsrasqagn lelakflveq
      121 gahihadnnr avrwatengh nevrdylgsq lnkpskaekl vasidhdaea ptkkskshkh
      181 qi
//
LOCUS       WP_175888215             310 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia
            contaminans].
ACCESSION   WP_175888215
VERSION     WP_175888215.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..310
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=34316
     Region          53..288
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          75..101
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          103..131
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          134..160
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(136..137,140..142,144..145,149,152,160,162,166..167,
                     170..172,174..175,179,182,190,192,196..197,200..202,
                     204..205,209,212)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          162..188
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          190..220
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          223..253
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mkslieavid niktntvpyn daaeeisqyl hgvfppdeet reqwvedyrt ltdedidavt
       61 qafentygig siarliymck tgnldavmnc iqngadihan ndlalrmasg eghlevvkyl
      121 veqgadihgf dnqaliwasg eghlqvvqyl ieqgadihad ddgalksasi nghldvvqcl
      181 vengadihsd hdlafrhaae nghlevvqyf vdqgadihae ceiydtalem aaryenfqvc
      241 dylvslgcdp qkvidnesie nkewaydfve ardfankltn dlgkadklvs sinhdaeapa
      301 kqsrstrqki
//
LOCUS       WP_175888217             130 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia
            contaminans].
ACCESSION   WP_175888217
VERSION     WP_175888217.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Kane,E.I. and Spratt,D.E.
  TITLE     Structural Insights into Ankyrin Repeat-Containing Proteins and
            Their Influence in Ubiquitylation
  JOURNAL   Int J Mol Sci 22 (2), 609 (2021)
   PUBMED   33435370
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Mosavi,L.K., Cammett,T.J., Desrosiers,D.C. and Peng,Z.Y.
  TITLE     The ankyrin repeat as molecular architecture for protein
            recognition
  JOURNAL   Protein Sci 13 (6), 1435-1448 (2004)
   PUBMED   15152081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12150541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..130
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=14322
     Region          12..58
                     /region_name="Ank_4"
                     /note="Ankyrin repeats (many copies); pfam13637"
                     /db_xref="CDD:372654"
ORIGIN      
        1 mndnqtelnl nllkaaedgd veavkksise gadvrvandi alrmaslhgn fqacdhlvyl
       61 gcdpqvvvdd knikeenkqw avdfvnkrnf ankltndlae psskaerlls tinedaeapv
      121 kqsrstrqki
//
LOCUS       WP_175888370             475 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia contaminans].
ACCESSION   WP_175888370
VERSION     WP_175888370.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..475
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51346
     Region          42..460
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(52..53,56..57,60,100,150..151,153..155,158,178,
                     181..182,185,296,299..300,303..305,308,335,339,388..389,
                     393,397,413,416..417,420..421,424)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mastqpdpla aaaatrvgti dpgsisarld rlpptrtvwk lvvllslgff felydllysg
       61 yvapglvksg ilsatthglf gttgvasfia alfsglfigt iacgfladrf grraiftwsl
      121 lwytaanvvm afqdtaagln fwrfvvglgl gvemvtigty iselvpkqir grafaceqav
      181 gfvavpvvaf layllvphap fgldgwrwvv ligahgalfv wwirrelpes prwlaqqgrv
      241 eeadrimral eakveaeygr plplpapaep vpprgsfrdm wvqpyrsrti mmtifnvfqt
      301 vgfygfanwv ptllikqgit itsslmyssv ialaapigpl iglliadrfe rksvivamaa
      361 aivvcgllfs qttvgafliv lgigltlasn imsysfhayq aelfptsira ravgfvysws
      421 rfsaifssfv iaavlkgfgt fgvfafiaga mvivmaaigf mgprtkgval etisk
//
LOCUS       WP_175888345            1084 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia contaminans].
ACCESSION   WP_175888345
VERSION     WP_175888345.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..1084
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115227
     Region          3..1062
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mlkivrlalt rpytfvvlal liliagplaa vrtpidifpd iripvisvvw nysglqpddm
       61 sgrivtyyer tlgttvndiq hiesqsfrsf givkiffqpt vdirtataqv tsisqtvlkq
      121 mppgttppqi lnynastvpv lqialtsntl deqkledyae nfirpqllsv pgvaiptpyg
      181 gkarevqidl dpqalqskgl saqdvahala qqnqiipagt qkigrfeyni klnnsplald
      241 alndlpiksv dgttitirdv ahvrdgfppq snivrvdghr avlmsilkng sastldiiag
      301 vkaklplieq tlppglklvt mgdqstfvng avsgvaregi iaaaltslmi llflgswrst
      361 liiaasipla vlsaiallaa tgetlnvmtl gglalavgil vddatvtien vnwhleqgkd
      421 trtaivdgak qivmpalvsl lcicivfvpm lmldgisrfl fvpmakavif smmssfvlsr
      481 tfvpmlaqyl lkphasagha sgelaaimds haghagahda ppsrnplvhf qraferrfea
      541 vrasyrillg laltrrkpfv vaflcvvaas fllapwlgrn ffpaidsgei slhvrapvgt
      601 rveetaaefd rientirgvi ppaqlgevid niglpksgin ltynnsgtlg pqdgdilisl
      661 skdhaptagy vrqlrerlpr aypgttfsfl padivsqiln fgapapvdlq vagpnqqanl
      721 ayarelyrkl rliagvadpr iqqastypqf tvavdrtrad qlgiteqdvt nsvvatlagt
      781 sqvaptywln prngvsypiv aqtpqykmtt lsalqnlpvt gasgqsqllg glatitrgvg
      841 navvshynie plfdiyattq grdlgavaad iggivkatak dlpkgstvtl rgqvqtmnga
      901 faglllglvg aialiylliv vnfhswadaf vivsalpaal agivwmlftt htplsvpalt
      961 gailcmgvat ansilvvsfa rerlaetgna lasaleagft rfrpvlmtal amiigmapma
     1021 lglgdggeqn aplgravigg lacatiatlf fvpvvfslvh rrdglkhdas rasspsasga
     1081 shvh
//
LOCUS       WP_175888421             225 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Burkholderia contaminans].
ACCESSION   WP_175888421
VERSION     WP_175888421.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..225
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=22898
     Region          147..223
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 msvlhagvfv llarepavrs vpvqrqvmva tlippepaqe vsmvataatr pkaashttrg
       61 anaaarssas salqpagpva pvrarqrvgd alapprpvpf aaaierreap hvdaasgvtp
      121 tqaaspappa paiprfvahp ecalvtpdyp pqslragehg talveletda agrvvaariv
      181 agsgsprlda aardavlasr caphvengaa lpmrarapit fnlde
//
LOCUS       WP_175888438             558 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 39 protein [Burkholderia contaminans].
ACCESSION   WP_175888438
VERSION     WP_175888438.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14304616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..558
                     /product="glycosyltransferase family 39 protein"
                     /calculated_mol_wt=62711
     Region          9..375
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
     Region          450..555
                     /region_name="Arnt_C"
                     /note="Aminoarabinose transferase C-terminal domain;
                     pfam18583"
                     /db_xref="CDD:465810"
ORIGIN      
        1 mndtpsrlpl nritlvllfv alaivwfapl glrhlipsde gryaemarem fvtgdwitpr
       61 yngykyfekp plqtwlnalt fawfgigewq arlytavasf agillvgytg arlfnplsgf
      121 laavvlassp ywnlmghfna ldmglafwms lslcslllaq rpglrpaaar gwmwacwaam
      181 afavlskglv glilpgavlv lytliardwa lwkrlylvsg lviffaivtp wfvlvqqrnp
      241 effnfffivq qfrryltpeq nrpgplyyfv pvllvgflpw lsvawqsirh alrmprqpng
      301 fspmlvlliw safiflffsa shsklisyvl pvapalalii gaylplmsad rfrrhllgyl
      361 vflvvaafgi iflayqgdar tpntlyrafq mwlyaglava avltlaaawl nrrtgvaaal
      421 aafgaawlaf gtiggtghde fgryssgall aptvraelak lpadtpfysi emldhtfpfy
      481 mghttimvqr qdelafgism epnkwiptvd ewiarwkqet halaimppgq ydtlvkqgvp
      541 mrviardnrr vivekpqs
//
LOCUS       WP_175888440             638 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Burkholderia contaminans].
ACCESSION   WP_175888440
VERSION     WP_175888440.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..638
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=69489
     Region          6..631
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mpyavpqaqh adrvlgalag rlpapadstr lvsswqrsle ryrldpassi gprvltaael
       61 revrdkeeaf lrasgqcltr lhdmirvady cvmltdahgv tidyridrer rndfrhaglh
      121 igscwsesee gtcgvanvlt dlapitvhkt dhfraafttl tcsaapifsp ageligvlda
      181 savhspdgrd sqrlvyqlvr qsaaliedgy fvhstaqhwi lfghpnrhyv eaqpewliaf
      241 decgnivaan rqardalpal reprhideif datemplrda arldaivalr lratgaplya
      301 rlraplrrtg repgtasrrp gsaqrhvgal tpflqssdah iaqqaelalr vaskrlpilv
      361 lgetgagkev faraihdaga rrtrpfvavn cgalpealie selfgyaaga ftgarkhgar
      421 gkialadggt lfldeigdmp ltlqtrllrv ladgevvplg sdtpvrvdld vicathrdla
      481 rmvadgtfre dlyyrlsgat felpplrgra dvrdviaavf aeeahatghv ltldatlaeq
      541 laaypwpgnv rqlrnvlrya cavcdaarvt rrdlpadiat qlggtspgtl pddergriva
      601 altahrwrpd aaaqalgisr atlyrriakh rivaphra
//
LOCUS       WP_175888487             300 aa            linear   BCT 11-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Staphylococcus
            aureus].
ACCESSION   WP_175888487
VERSION     WP_175888487.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     Protein         1..300
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33012
     Region          87..299
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mkfltfkynd ktsygvkvkr edavwdltqv fadfaegdfh pktllsglqq nhtldfqeqv
       61 rkavvaaeds gkaedykisf ndieflppvt ppnnviafgr nykdhaneln heveklyvft
      121 kaassltgdn atipnhkdit dqldyegelg ivigksgeki pkalaldyvy gytiinditd
      181 rkaqseqdqa flsksltggc pmgpyivtkd elplpenvni vtkvnneirq dgntgemilk
      241 idelieeisk yvalhpgdii atgtpagvga gmqppkflqp gdevkvtidn igtlttyiak
//
LOCUS       WP_175888471             458 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Staphylococcus aureus].
ACCESSION   WP_175888471
VERSION     WP_175888471.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     Protein         1..458
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48871
     Region          16..452
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,141,
                     144..145,148,273,276..277,280,281,284,312,316,370..371,
                     375,379,395,398..399,402..403,406)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mnntqssprs niiiaimlsa ltywlfaqsf inigplvgqt yqtspavlnl sisltsfatg
       61 ifmvaagdia dkigqlrmty mgliismfas llliisdita lliigrilqg lsaaillpst
      121 vgvlnnqfkg dhlrraisyl mistvggigl agviggliat nfgwqtnfii siviafiail
      181 llkgtpekvs qhshrhpfdy kgmsifavmi gsftllltqg feqgwfstfs ficlsiiiit
      241 tlifiiierr hevpfidfsv lrnrpfigaf lnnfvlnsgl gvtvvffiya qthlglsaaq
      301 sglvtlpyai vavamirlge katlcfggkl mliigplfpv igitiismts lqpsqyiiav
      361 vigfvicaig nglvatpglt iaifsmpnek vglatglykm sgtlggafgi alsttvfsml
      421 qlnyapsvaa titfivsivl milgslsaym iipktvks
//
LOCUS       WP_175888498             344 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Staphylococcus aureus].
ACCESSION   WP_175888498
VERSION     WP_175888498.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus aureus
  ORGANISM  Staphylococcus aureus
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Staphylococcus aureus"
                     /db_xref="taxon:1280"
     Protein         1..344
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38089
     Region          3..316
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mkdvtiiggg psglyasfya glrdmsvrli dvqselggkm riypekiiwd iggiapkpch
       61 eilkdtikqg lyfkpevhln ervvdirkks erhfevetea geiytskavi iaigagiinp
      121 kqldvkgver yqltnlhyvv qsyrrfkdkd vlisgggnta ldwahdiaki aksvtvvyrk
      181 edvsgheamk tlvtdlnvkl cpktrikylv gnddethise vvlehvesgd thtvkfddvi
      241 ishgfdrcnt llsetsskld mhddcrvkgf gntttsipsi yacgdivyhd akshliasaf
      301 sdganaanla ktyiqpdana egyvsshhev fkeanktivn khly
//
LOCUS       WP_175888525             205 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease signature motif containing protein, partial
            [Mycobacterium canetti].
ACCESSION   WP_175888525
VERSION     WP_175888525.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium canetti
  ORGANISM  Mycobacterium canetti
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Mycobacterium canetti"
                     /db_xref="taxon:78331"
     Protein         <1..205
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
     Region          <1..113
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          105..158
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(129,131..133,135,146..147,151..152,155)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 daaaidrdtr sqaqrnhdgl laglralias gklgqhnglp vsivvtttlt dlqtgagkgf
       61 tgggsllpma dvirmashah hylaifdhgt plalyhtkrl aspaqrimlf ardrgctkpg
      121 cdapayhsqa hhvqgwastr rtditdltla cgpdnrlaek gwitrknthg dtewlppphl
      181 dhgqprtntf hhpekllhdd ddepd
//
LOCUS       WP_175888534             230 aa            linear   BCT 11-JAN-2025
DEFINITION  PE family protein, partial [Mycobacterium canetti].
ACCESSION   WP_175888534
VERSION     WP_175888534.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium canetti
  ORGANISM  Mycobacterium canetti
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Qian,J., Chen,R., Wang,H. and Zhang,X.
  TITLE     Role of the PE/PPE Family in Host-Pathogen Interactions and
            Prospects for Anti-Tuberculosis Vaccine and Diagnostic Tool Design
  JOURNAL   Front Cell Infect Microbiol 10, 594288 (2020)
   PUBMED   33324577
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Chen,X., Cheng,H.F., Zhou,J., Chan,C.Y., Lau,K.F., Tsui,S.K. and
            Au,S.W.
  TITLE     Structural basis of the PE-PPE protein interaction in Mycobacterium
            tuberculosis
  JOURNAL   J Biol Chem 292 (41), 16880-16890 (2017)
   PUBMED   28842489
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Yeruva,V.C., Kulkarni,A., Khandelwal,R., Sharma,Y. and
            Raghunand,T.R.
  TITLE     The PE_PGRS Proteins of Mycobacterium tuberculosis Are Ca(2+)
            Binding Mediators of Host-Pathogen Interaction
  JOURNAL   Biochemistry 55 (33), 4675-4687 (2016)
   PUBMED   27483162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10469594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Mycobacterium canetti"
                     /db_xref="taxon:78331"
     Protein         1..>230
                     /product="PE family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_component="GO:0009986 - cell surface [Evidence IEA]"
     Region          16..82
                     /region_name="PE"
                     /note="PE family; pfam00934"
                     /db_xref="CDD:425952"
ORIGIN      
        1 msfviaapei iaaaatdlas lessiaaana aaatnttall aagadevsta vaalfgahgq
       61 ayqalsaqaq afhaqftqal tsgggayaaa eaaavsplld pinefflant grpligngan
      121 gapgtganga pggwligngg aggsgtagvd ggaggnggag gllgnggagg aggsaitgtg
      181 gaggaggsal lfgaggagga gggangaggi ggagtnlaig ghggnggnag
//
LOCUS       WP_175888539            1419 aa            linear   BCT 11-JAN-2025
DEFINITION  PPE family protein, partial [Mycobacterium canetti].
ACCESSION   WP_175888539
VERSION     WP_175888539.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium canetti
  ORGANISM  Mycobacterium canetti
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12841089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..1419
                     /organism="Mycobacterium canetti"
                     /db_xref="taxon:78331"
     Protein         1..>1419
                     /product="PPE family protein"
     Region          1..387
                     /region_name="PPE"
                     /note="PPE-repeat protein [Function unknown]; COG5651"
                     /db_xref="CDD:444372"
     Region          5..157
                     /region_name="PPE"
                     /note="PPE family; pfam00823"
                     /db_xref="CDD:425887"
     Region          <173..1083
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
ORIGIN      
        1 msfvvmppei nslliyggag pgpllvaaaa wdelaaelgs aaaafgsvts glvggiwqgp
       61 ssvamaaaaa pyagwlsaaa asaesaagqa ravvgvfeaa laatvdpfvi aanrsrlvsl
      121 alsnlfgqnt paiaaaefdy elmwaqdvaa mlgyhtgasa aaaalapfas plgslaaaae
      181 pakslavnlg manvglfnag ngnigsynvg agnvgsynag ggniggnnvg lgnvgfgnvg
      241 lansgvaagl mglgnigfgn agsynvglan mgvgnigfan tgsgnigigl sgdnltgfgg
      301 fntgsgnvgl fnsgtgnvgf fnsgtgnwgv fnsgshnsgi gnsgiastgl fnagdfntgl
      361 vnagsyntgs fnagqantgg fnpgsvntgw lntgdtntgv ansgdvntga fisgnysngv
      421 lwrgdyqgll gfssgvnvlp iiplslding gvgaitiepi hilpdipini netlylgplv
      481 vppinvpais lgvgipnisi gpikinpitl wpaqnfnqti tlawpvssit ipqiqqvals
      541 pspipttlig pihintgfsi pvtfsystpa ltlfpvglsi ptggpltltl gvtagteaft
      601 ipgfsipeqp lplainvigh inalstpait idniplnlha iggvgpvdiv ggnvpaspgf
      661 gnsttapssg ffntgaggvs gfgnvgahts gwfnqstqam qalpgtvsgy fnagtlmsgi
      721 gnvgtqlsgm lsggalggnn fglgnigfdn vgfgnagssn fglanmgign igfantgngn
      781 igiglsgdnl tgfggfnsgs envglfnsgt gnvgffnsgt gnlgvfnsgs hdtgffltgn
      841 ninvlapftp gtlftiseip idlqviggig pihvqpidip afdlqitggf igireftlpe
      901 itipaipihv tgtvglegfh vnpafvlfgq tamaeitanp vvlpdpfiti dhygpplgpp
      961 gakfpsgafy lsisdliing piigsyggpg tipgpfgatf nlstsslalf pagltvpdqt
     1021 pvtvnltggl dsitlfpggl afpenpvvsl tnfsvgtggf tvfpqgftvd ripvdlhttl
     1081 sigpfpfrwd yipptpangp ipavpggfgl tsglfpfhft lnggigaisi ptttvvdaln
     1141 plltvtgnle vgpftvpeip ipainfgldg nvnvsfnapa ttllsglgit gsidiagiqi
     1201 tniqtqpgql fmsvgqtlfl fdfrdgieln pivipgssip itmaglsipl ptvsesipln
     1261 fsfgspastv ksmilheilp idvsinleda vfipatvlpa iplnvdvtip vgpinipiit
     1321 epgsgnsttt tsdpfsglav pglgvgllgl fdgsiannli sgfnsavgiv gpnvglsnlg
     1381 ggnvglgnvg dfnlgagnvg dfnvgggnig gnnvglgnv
//
LOCUS       WP_175888669             363 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia cepacia].
ACCESSION   WP_175888669
VERSION     WP_175888669.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..363
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=38669
     Region          17..363
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mksraersir tvvltgsata aciaasvaha qssvtmygim dagieytnha apeggssvkl
       61 ksgnkntsrw glrgvedlgg glkavfrles gidlangald dgpdsifarr atvglkskwg
      121 eltlgrnytv tydymlpfdp mgyaqnyswa sastatggrk dgmftrssna vrydgefsgf
      181 kfgalygfgn vpgsvktssk ydfavgyekg pfaavvtfdr qngaadsvtp adtvnyiqgi
      241 haglsydfgn lktmagyrny krtfrttaan qlsdtywlgg syqftpafsl iaavyhqnik
      301 ggsdadptlv slranyalsk rtvlyaagaf aiakhdqkvg vsrdfvgygt tqvgvtagiq
      361 qrf
//
LOCUS       WP_175888677             464 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia cepacia].
ACCESSION   WP_175888677
VERSION     WP_175888677.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..464
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=48981
     Region          40..419
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msaslaassp spqppalrll ptadaddarv aallerlape laadaarndv dgrfphenfa
       61 rlhragliaq vvprehggag atlaqasriv aavaradpat alvltmtylq hralgradnr
      121 wpaqvrravf dsavthgali nalrvepalg spsrgglpet varrdgdgwr msghklystg
      181 ipalrwlavw artdepaprv gvflvprdrd ahgdrirvie swnhlglras gshevvfddv
      241 plpadhavdv rapdawavsa athadadaqa dqqawmvall gslydavara srdwvvefat
      301 trapsglgap latlprvqea vgeiegwlha nrvllddhia rtdaghappv ttsglvkrtv
      361 tehairaveq alklsgnhgl sranplerhy rdvlcsrvht pqddaiavaa grvvldaasr
      421 veakgevtve akgeskgkas gkaggetetg gasvdaterg rsda
//
LOCUS       WP_175888675             275 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175888675
VERSION     WP_175888675.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..275
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29296
     Region          23..270
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mvsaavless asaspaaspa vtaprgarid irrvshafdg pggplpvldd vtlsvaagef
       61 vallgpsgcg kstllrlvag ldaarqggia qdgvpieqpd psrivvfqdp tlypwrrvra
      121 nvalglearg varasqhrvd dalarvglqe fsnvfphqls ggmaqrvala ralvndprll
      181 ildeplgkld sltrltmqae ltalwqrdgf sallvthdve ealflaqrvi vfgprpariv
      241 aelsvdlpyp rhrgdprlae lrhdalrhlg ldasw
//
LOCUS       WP_175888694            1055 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cepacia].
ACCESSION   WP_175888694
VERSION     WP_175888694.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1055
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113119
     Region          1..1038
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mwivnlalrr pytfivmaim ivlatplalm rtpvdvlpai nipvisviwn ysgfsatemt
       61 nritsvheri ltttvnniqh vestslpgia vvkvflqpga nvqtaiaqtv ssaqaivrqm
      121 pqgatpplvi tysassipvi qlglssktls eqsladialn flrpqlitvp gvqipfpygg
      181 rtrvvaidld pqallakglt padivnavna qnlvlptgta kmgqteyrid tnasadtvad
      241 innlpvqtvn gattylreva svrdgfapqt nvvrqngqrg vlisilksgd astlkvvsdl
      301 kallpkvipt lpegltitpl fdqsvfvdaa vqgviheali aavltammil lflgnwrstl
      361 iiaisiplsi ftslialsal getinimtlg glalavgilv ddatvtieni erhlhlgtnl
      421 hdailegage iavpafvstl cicivfvpmf fltgvarflf vplaeavvfa mlasyvlsrt
      481 lvptlamllf rpqqasagpn rstsrfarlh hafneaferl rawyivllsi llvrrrfyat
      541 cflgfcvlst glvfalgrdf fpnadsgnir lhmraptgyr ieetarladq verviretvp
      601 pdelgaivdn lglpvsginl sysnagtigt ldgellialk pghratqhyv qalrkvlper
      661 fpgvefffqp sdiitqilnf gqpaaidlqv lgndlasnmt iasslmkkfr qipgavdvhv
      721 lqrndeptll admdrtrmqq lnlsaqnvaq nmlislsgss qttpsfwinp rtgvqyplqi
      781 qtpqynissv ddllgtpisa sgrtgmplql lgnlvqvrst anpavithyn irpaidvyvs
      841 vegrdlgava geidrivsda ratlprgtel tmrgqietmr tsylglgagv amaivlvyll
      901 ivvnfqswld pliiisampa alagivwmlf itgthlsvpa ltgaimtvgv atansilvvs
      961 farqrleaga ppltaaleag atrirpvlmt alamiigmvp malglgegae qnaplgravi
     1021 ggllfatvst llfvplvfgg vharlarrra rqagh
//
LOCUS       WP_175888696             549 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175888696
VERSION     WP_175888696.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..549
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=55902
     Region          15..268
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
     Region          297..546
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mqnhevsadd appkaqrgiq svevggrlld alarrrkplg lselaaaadl staqahtylv
       61 sltrlalvkr daltgnyepg plslrlglms ierqpayrat lphaarlaea vglsvalsvp
      121 galgptivri ehggyplhvn lhvgsvmsld ttatgrvfra fgapaqlram aasqagaadt
      181 laggeqpvpd tgvpqaelda irargiergv dlpspgvsam cvpvfdaaga lqlaltvigs
      241 tgsidvawdg piaaalrdaa rqasaslgaa hdapppapga apaaarvppa laddakaqrg
      301 inaldstgel llalvsagra lplrdlaaaa gmpaakafph lvslqkigll srddagcfgg
      361 gplgqalgli amqrvsptrd aeaeivalag atdmsvaaat lgplgptvir leesarpqhv
      421 slqvgtvmsl vntaigrifa agmsddvlad lladepvrla griappadda frarlatira
      481 daldfafdap vpgigtvaap vfdhtgsirl viaiigssrg fprgpdsdla qallaatrrl
      541 swrfgwigr
//
LOCUS       WP_175888698             455 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175888698
VERSION     WP_175888698.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..455
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48888
     Region          32..426
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(44..45,48..49,52,84,134..135,137..139,142,162,
                     165..166,169,276,279..280,283..285,288,316,320,371..372,
                     376,380,396,399..400,403..404,407)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 msaplqadaa ravasgaaap dddalyrrig mrivpflfic yivsildrsn igfaqlqmrq
       61 dlgltdamys lgavlffvgy vlfevpsnal lrrfgarrtf arimclwgav svamitvdsa
      121 khfyvlrfll glfeagffpg vvfyltywyp arrrasvlsi fyagvavagm vggllsgwlm
      181 rgmsgvlglh gwqwmfaieg apaillgvia wfwlcdrpeq arwlsdadrq rlaadlaadr
      241 agvagaadat gadtpaphsl rqvlaeprty lfafiyfslt tallmllfwm plmirefgih
      301 dvvqisllsv vpnaigaagl iaiarrsdrk rerrrhfaac afggavalal ltlhlpsiva
      361 mmallsvavm lifaahpvfw avpsayfsga gaaggialis sigvssgmit pwlvglirtr
      421 tgsmdpamlm iaallaacav amllgvravp raeaa
//
LOCUS       WP_175888703             310 aa            linear   BCT 11-JAN-2025
DEFINITION  AEC family transporter [Burkholderia cepacia].
ACCESSION   WP_175888703
VERSION     WP_175888703.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..310
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31363
     Region          18..305
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 migsillala pvallvacgh glrrtgfiad afwpqaerlc yyvllpalfa dglanarlqa
       61 lpvlplaaal vgstalaaal lllvrpfvrv dgagftsvfq gavrfnnyvg talaaglfga
      121 kgialaavcv aaivptvnlm cvlvfarygs trlgaaalvr qilsnplvva calgiamqag
      181 gvtfpaavep avralgvasm plgllcvgaa lkfdaarawl qpvcvasafk fmamplitla
      241 agrlfglgda altvallfqa lptssasyim arqlggdapl magitafqti aaalampvvl
      301 ttlasapafr
//
LOCUS       WP_175888713             251 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Burkholderia
            cepacia].
ACCESSION   WP_175888713
VERSION     WP_175888713.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..251
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27622
     Region          1..239
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 miridsihkr fqqhavlkgv sldvqqgevv cligpsgsgk stvlrcingf etydegsiti
       61 dgvkvnahsk rihelrmrvg mvfqrfnlfa hrtalenvme gpvhvrrmpa aqareqaral
      121 ldkvglshrm naypselsgg qqqrvaiara lamepqailf deptsaldpe lvgevlgvmr
      181 glardgmtmv vvthemafar evadrvcflh dgticesgpa rdvltqpthp rtqeflrrll
      241 asdgadhpdr s
//
LOCUS       WP_175888716             472 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia cepacia].
ACCESSION   WP_175888716
VERSION     WP_175888716.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..472
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=50856
     Region          83..470
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mtarpafpsp dasgttapra psrllrraaf vigaavlgyg afaiafpaqv paaigtvvad
       61 wtganphpva lqrpaaqpls avaqlgralf adpslsasgk qscaschspd haygppnald
      121 vqpgglamtq qgyrpppslm ylyrqpnfsi gpdagendaa psvaqqaasa agvvkaqkva
      181 gtsaapqlvp qggmfwdgra dtlqqqafgp llnpvemana svddvarkla qsshraqfek
      241 lfgarvfdsp qlavseamfa iaryqvedps fhpynskydr wlegrarlsq aelrglrlfn
      301 dpekancagc hlskpgkdgl ppmftdyqye algaprnrql aqnrnpafyd lgvcgpfrdd
      361 lkdqtqycgm fltptlrnsa trhvffhngv fhtldqvmaf ynersispqk fysrgadgkv
      421 deyddippky ranvdvtdap fdrkpgdkpa mtaqdikdie aflgtlndep ar
//
LOCUS       WP_175888719             862 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia cepacia].
ACCESSION   WP_175888719
VERSION     WP_175888719.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 862)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..862
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=93175
     Region          59..712
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mhpfqpsstr vnrrnvssvr dfcarwvara qpvaaaavar vkplaavawh hlrhptrrgv
       61 llagaavpal fvayvvvlip ftpgigdirk arvdqpaqvl sadgkllaef kpsnrewvpl
      121 tqisphmvda liatedhrfy ehhgldwkrt asaalhtfsg srqggstitq qlarnlypde
      181 igraptltrk vkeaitalki eavyskdqil etylntvpfl ynaygvemaa rtyfdksade
      241 ldvldsatlv gmlkgnsyyn pvlnperalq rrntvlgqmv kygklspaqf aqlqrrplri
      301 dferqkeppg paphfaqqlr kwliawadrn dyniyadgli vrttidsrlq qmatqaltlq
      361 gnqlqgiann awsgrdgcgt dnevfrtfmr espeykaaqd agkddaaamk llaadrgfmr
      421 alcktktdvq agflaidprn gqirawvgsr dftsepfdhv aqarrqpgst fkpfvygvaf
      481 angmkpddtf idqpveiplk ggeiwrpndd vpptgkpmtl rdavalsrnr itaqvmekvg
      541 pasvarlard mgvrespler vpslalgtsp vtlkemvasy atvangglyv epqmvtrien
      601 rqgdvlaeya papperalda etdktllsvm rdvvtrgtgg sirtrfgirg dvagktgttq
      661 dnadgwfilm qpglvagawv gfddgrvtlr sdywgqgahs alpivgdffq raqrarivdt
      721 kakfdtepsp gwfaslrerv tdlfdtwfpp kpekapapar tqrverapea dtgtestasa
      781 asapeaasgg iveewvpase vaasaaalsa gasqpqpaqp pagastpggg ssglgtapaa
      841 apsaapaqpp vpaapdasga sq
//
LOCUS       WP_175888728             766 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Burkholderia cepacia].
ACCESSION   WP_175888728
VERSION     WP_175888728.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..766
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=83868
     Region          178..765
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 msyvvavram ceftarrgdl dlrftpapta legiaghgav tsnrgsryet eialtgtwgt
       61 ltvrgradgy dpvanrleei ktfrgsldam panhralhwa qakvyahlmc dardlpeidv
      121 alvyfdivse retvltqtlg aaelaaffae qcacfvgwae retahraard aalralafph
      181 gqfrsgqrel avavyraard drclmaqapt gigktlgtvf pllkacgege ldhvyfltak
      241 tpgralalea aatlgagtpa lplrvlelva rdkacehpds achgescpla kgfydrlpaa
      301 rdaaieagll drdtvraaal ahdvcpyyls qelarwsdmv igdynyyydg samlhtlaqq
      361 nqwrvgvlvd eahnlldrar kmysasldpf afaaareaap aalrkafdrl arawgtvnra
      421 qaeryaaype ipgpivsalq nlvaavgehl adaprangda llrfhfeaiq fgvlaeafds
      481 asifdatlhg epmprqpald gvasagrrrr vqstlcvrnv ipagflapry eaacatvlfs
      541 gtlspfhfyr dtlglpgdtg wldvdgpfra eqltvrvash vstrwrdrdr slepivdlia
      601 aqyatrpgny lgflssfdyl grvvalmqar hpdvpvwaqa pgmtegerda flarfdaggr
      661 gvgfavlgga fsegvdlvge rligafiatl glpqvndvne qmrramdarf gngydymyly
      721 pglqkvvqaa grvirtehde gvvhliddry rrrevrdllp rwwrik
//
LOCUS       WP_175888735             744 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia cepacia].
ACCESSION   WP_175888735
VERSION     WP_175888735.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..744
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=78436
     Region          75..>209
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          215..737
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msrglieagk vagqaagagv srrsflklgm slgaaagggl llgfslpaag ddarrsvigg
       61 dgdetaragv fapnafvqid ragkvtlvmp kvemgqgvyt alpmliaeel evplssvtld
      121 happneklfl dpllggqltg gstsiryawe plrragatar tllvaaaakq wnvdpascra
      181 vngevqhpps grrtsygqla daaaklpvpk dvalkkpadf kligtpakrl dspekvdgta
      241 qfgldvrlpg mlyavivnsp vfggtvasid dtaakkipgv rqvvradnav avvgdhtwaa
      301 krgasalvvk wnegagakvs tkdivadlaq aaangkgava rkdgdvgkgf adaktrvdav
      361 yeqpllahat mepvnctvhv radgceiwvg tqvptravdt vqqltsfppe kivvhnhllg
      421 ggfgrrletd migqavkiak qvnapvkviw treediqhdm yrpyyydris agldangkpi
      481 awqhrivgss ilarfappaf qhgvdpdave vatdlpydlp nqlidyvrqe prhvptafwr
      541 gvgptrstfv vesfidelaa qtktdpvqyr rallgktpra lnvldvatka agwgpslptg
      601 qgrgvsvmha fgsffsivid vavdngevhv krvvcavdcg msvnpntiea qvqggiifgi
      661 tgalygeiti edgrvvqsnf tdyrmlrine tppievhlvk sgeapggige pgtaataaal
      721 snaifaatgk rlrklpvgdq lkta
//
LOCUS       WP_175888818             281 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia cepacia].
ACCESSION   WP_175888818
VERSION     WP_175888818.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20139405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..281
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30299
     Region          <41..120
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
     Region          153..274
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 mdqhedfivr tmsadevams iewaaaegwn pglhdpscfr eadpagffvg vwrgepvacl
       61 aavayderfg figlyivkpg frgkgfgiri wqhgmrylad rnigldgvva qqanyrksgf
      121 alayrniryq grvdgigcaq vtaaadvpfe qllaydrqcf paararfvsa wiaqpdaval
      181 vavdagriag ygvvrrckag ckvgplfadd agvatglfra laarmpgevi vldvpetnpa
      241 avalaerhgm tsvfetarmy tqdappiaid rvfgvtsfel g
//
LOCUS       WP_175888819             331 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cepacia].
ACCESSION   WP_175888819
VERSION     WP_175888819.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..331
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34994
     Region          130..304
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mkdqpdgvvl ptrvvpfpas iseearaalq rlvgsdgvpl nalhvmpapd dfdawmrvka
       61 aadahyaaav eqlgghlrss vetiragaad vhvatpeava sgecayidlh ggalvlggga
      121 acragaqmqa drlgircygv dyrlppehpy paplddciaa yayvleryap envviggrsa
      181 ggnlaaamvl rardeglplp aalvllspev dltesgdsfe tnrlvdvvlp tslmpnnlly
      241 angadlahpy lsplfgdfaa gfpptfiqsg trdlflsnav rlhralrraq vptelhlfeg
      301 mphggfmgap edmelgqeia rfvrahlpal n
//
LOCUS       WP_175888900             246 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia cepacia].
ACCESSION   WP_175888900
VERSION     WP_175888900.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..246
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25426
     Region          10..239
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; pfam01925"
                     /db_xref="CDD:460386"
ORIGIN      
        1 mhihtltiva vvfllagavk gmiglglpti amglltlamp psaaaslllv psfitnvwql
       61 wlgpsfgpll rrlwpllagl tigtltgglp alaagstwth aalgvvlvly glwglaaarl
      121 papgrhekwl savvgyltgv vtaatgvfvv pavpylqalr lpkddliqal glsftastiv
      181 lglqlrvtga letvdldvsa lalvpalagm aggqyarrvm sekafkrcff vglialgaym
      241 aasgwr
//
LOCUS       WP_175888919             504 aa            linear   BCT 11-JAN-2025
DEFINITION  MDR family MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175888919
VERSION     WP_175888919.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..504
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52978
     Region          38..422
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(39..40,43,74,124..125,127..129,132,152,155..156,159,
                     284,287..288,291..293,296,324,328,381..382,386,390,406,
                     409..410,413..414,417)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mttntlltpp aaetarrdap tglivaalll vmllsaldqt ivstalptiv gelggldqls
       61 wvvtayllss tvvlplygkl gdlygrkivl qaaivlflag salcgvaqdm tqlivlralq
      121 glgggglmvv tmaaigdlvp pdrraryqgm fggvyglati vgpllggflv ehlswrwift
      181 inlplgflal avigvafrph tahvkhridy mgaaflatal tcvilftseg gsllpwtspq
      241 lwmtlvlgvv aiggfiyeer laaepimple lfrhrtfvlv sligfvvgia lfgsvtfipl
      301 ylqvvkgstp sqagmqllpm mggmlvtsvv sgrlisrlgs yrmfpilgtl aggvamalls
      361 tltldtplht myaymallgi glgmvmpvlt lavqntvefr hmgvatsgat lfrsiggslg
      421 vaafgalfsh glqsrvmaal pagtelppal gpaavhqlpd avrdaylhaf agslhvvyla
      481 aatviaiafv lawfvedapl rkhn
//
LOCUS       WP_175888922             339 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175888922
VERSION     WP_175888922.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12168323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36731
     Region          27..201
                     /region_name="AraC_binding_2"
                     /note="AraC-binding-like domain; pfam14525"
                     /db_xref="CDD:434015"
     Region          255..335
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mpltpnadal salyrncvfr sglrtdaheq vslelaehal rwkqgvpdaa lfkgqlnhls
       61 vyalqygaev evaprpfdgf slvhtslagg aeiecdghvm gvsegrtavl aptsrvrlrw
      121 rtgtrqlivk vpdslmravc grrpddaapg lapgfllpta lasqwdliaq sllnvlavad
      181 dggiraewre hfeqslalfl lvhcppspaa vqagpalqar gapaqagsrg dirqmdalhe
      241 fiharlcapi sledlaraag vslrtlnvlc rryhgatpme llrnirldaa rvqlltdpaa
      301 sitdtaltfg fghlgrfsay yfarfdelpr dtqkkrapn
//
LOCUS       WP_175888538             549 aa            linear   BCT 11-JAN-2025
DEFINITION  PE family protein, partial [Mycobacterium canetti].
ACCESSION   WP_175888538
VERSION     WP_175888538.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium canetti
  ORGANISM  Mycobacterium canetti
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Qian,J., Chen,R., Wang,H. and Zhang,X.
  TITLE     Role of the PE/PPE Family in Host-Pathogen Interactions and
            Prospects for Anti-Tuberculosis Vaccine and Diagnostic Tool Design
  JOURNAL   Front Cell Infect Microbiol 10, 594288 (2020)
   PUBMED   33324577
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Chen,X., Cheng,H.F., Zhou,J., Chan,C.Y., Lau,K.F., Tsui,S.K. and
            Au,S.W.
  TITLE     Structural basis of the PE-PPE protein interaction in Mycobacterium
            tuberculosis
  JOURNAL   J Biol Chem 292 (41), 16880-16890 (2017)
   PUBMED   28842489
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Yeruva,V.C., Kulkarni,A., Khandelwal,R., Sharma,Y. and
            Raghunand,T.R.
  TITLE     The PE_PGRS Proteins of Mycobacterium tuberculosis Are Ca(2+)
            Binding Mediators of Host-Pathogen Interaction
  JOURNAL   Biochemistry 55 (33), 4675-4687 (2016)
   PUBMED   27483162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10469594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Mycobacterium canetti"
                     /db_xref="taxon:78331"
     Protein         1..>549
                     /product="PE family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_component="GO:0009986 - cell surface [Evidence IEA]"
     Region          4..94
                     /region_name="PE"
                     /note="PE family; pfam00934"
                     /db_xref="CDD:425952"
ORIGIN      
        1 msfvlispev vsaaagdlan lgstisaank aaaaattqvl aagadevsar iaalfgmygl
       61 eyqaisaqva ayhqqfvqtl rtgaasymla eatnveqnll nlinaptqtl lgrpligdga
      121 nattpggagg dggllfgsgg ngapgapgqa ggaggsagll gnggsggagg tgapggnggn
      181 agwlygrggv ggaggigggt ggagghawlf ghggtggigg gpggnggwll gngghggagg
      241 igggsggagg nggwllgngg tggaggtdgg aggtggnaaw llggggtgga ggigggkggh
      301 ggnggwllgn ggngglggng dggtggghgg nggnpgwllg taggggngga gstgtagggs
      361 ggtggdggtg grggllmgag agghggtgga ggagvdggga ggtggaggng gaggqaallf
      421 grggtggagg yggdgggggd gfdgtmaglg gtggsggtgg dggapgngga ggagqllshs
      481 gvagatgkgg aggtggngga gsagadapag sgamgstgfa ggaggdggng ggtggqqgng
      541 gnggnggtg
//
LOCUS       WP_175889029            1074 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cepacia].
ACCESSION   WP_175889029
VERSION     WP_175889029.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1074
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=115189
     Region          1..1040
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mferlirfai ahrwlvmlai aavaalgvfs yqklpidavp ditnvqvqin taapgysple
       61 aeqritypve tvmaglpgle qtrsisrygl sqvtvifkdg tdiyfarqlv neriqeakdk
      121 lppgiapamg ptstglgeiy lwtveadaaa rkpdgtryta adlrelqdwv vrpqlrnvrg
      181 vtevnsiggy vkeyrvapnp aklmsygltl advvralern ndnvgagyie krgeqylvrv
      241 pgqartvddi anivltnvgg vpvrmkdvgv vdigrelrtg aatsngeevv lgtvfmlmge
      301 nsrtvakava akmadvnrtl psgvkaipvy drtvlvekav atvkknlleg ailviavlfl
      361 flgnmraali talviplsml mtftgmvnak vsanlmslga ldfgiivdga vvivencvrr
      421 lahaqaaagr pltrderfae vfgasqearr alifgqliim vvylpifalt gvegkmfhpm
      481 aitvvmalaa amvltvtfip aavalfiger ieekenrlmg warrayepvl aafmtrpvrv
      541 mlgagaivlv tlglatrlgs efipslnegd lavaalripg tslsqsvemq ksiektlkar
      601 fpeiervfar tgtaeiaadp mppnlsdgyi mlkpadrwpd pkkprdqlvr eieealaelp
      661 gnayefsqpi qlrfnelisg vrsdvavkif gddmavlnqt geqiaaalqk vpgasevkve
      721 qttglpvltv nldrdklary gvsvadlqdt vaaavggqka gtlfqgdrrf divvrlpdel
      781 rsdieaikrl pialpapaag asaplaaapy vplaelatid vapgpnqisr edgkrrvvvs
      841 anvrgrdvgs fvadareqlq qdvrvpagyw vswggqfeql qsaserlklv vplalfmvfv
      901 llfvmfnnvk dgllvftgip falsggvvsl wlrgiplsit aavgfialsg vavlnglvmi
      961 sfirnlrdeg tpleaavreg altrlrpvlm talvaslgfl pmafatgtga evqrplatvv
     1021 iggilsstal tllvlpvlyr vshavswraa laggfgggfv sgalrrlgff kgna
//
LOCUS       WP_175889032             743 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cepacia].
ACCESSION   WP_175889032
VERSION     WP_175889032.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..743
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79459
     Region          40..743
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mtvnkttasp arrrrakvgl gvgvgitlfa aqaaaaqgdt papdagaags atlptitvsg
       61 ergnalrart asvaglddap lrdtpasvsv vtraqlddqq akrlsdvvrn dasvvndyap
      121 vgyfegfair gfpvdlasai ridgltvsge qnvplenker veilkglagi dsgvvapggv
      181 infvtkrsan vasvtggvds rgstsaavdl grrfgpdnqf gfrinaaken mhsyidgtng
      241 rrtfgsiaad wdispraslq lnaefqqwiq rsapgyqllg gtvvpsvktt skalgtqpwa
      301 kpvttdalnl narfdyqfnd dwkayiaagr srtmiddnsa faygcsyaas ctagatspff
      361 fgangdydvy dfrspgeyrr nddlravttg kfatgplrhe ltlgvsvqrr vvhmatavyd
      421 yvgseniygp dvsfasspnt pgpsypqlds wqygvfgldr isigehwqvl aggkevllrq
      481 rswssldgda thtdrsvflp qvalvykpvn vlslyasysk alslgdqapv ratnayaflp
      541 pveshqfevg akydwldrls ltaavfsisk pfqfadpdas gttytfvqrg tqrhqgielg
      601 aagrvterlg ltasvaaira raydsgspay eghqvinvpa lraslyadya vpgvaglnvl
      661 ggveysaarn aneegtaqvp awfvfnlgar yttkigghrt vlrvsvdnlf nkfywrdage
      721 qqgdaylfpg aprtarvslt ydf
//
LOCUS       WP_175888974             128 aa            linear   BCT 11-JAN-2025
DEFINITION  GtrA family protein [Burkholderia cepacia].
ACCESSION   WP_175888974
VERSION     WP_175888974.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..128
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=13678
     Region          11..128
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mirtlyiaer arlirfsvsg lgstalhali aaamfalfda tpvtanavaf acstafsyla
       61 ntlwsfsspv twgnfmrfla vamvglvvtm llahgavalg larawsvvav vlcvppvtfv
      121 lhrlwtyr
//
LOCUS       WP_175889090             819 aa            linear   BCT 11-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Burkholderia cepacia].
ACCESSION   WP_175889090
VERSION     WP_175889090.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..819
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=85081
     Region          60..810
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 msrnwglgaa llalsvglas cggdgdspsa aasnlsaaaq sqgnedgngg ngngndngna
       61 aakknadirv vqyvnpligt dyatdqpadp vgsglgggtf pgptvpfgmm qwspmtptaq
      121 ydsrkgdgsg fsggywygdt sinafsilhl sgtgcwangg ylnvmpqlap gdagtpasfs
      181 hanetvqagy ygvtlgngik aeltttlrtg farftypala qgqqatiaid ptvlnnraqg
      241 stgdtisqvg dralsgtiag ggfcwaghav pvyyyaefsq pfaakpalsn dspvaltfnv
      301 drkhpdvmmk lgisfvsean akanllaenp gtdaqgnrnw rfdkvrsaas aawnarlnai
      361 qvtggsdadk tkfytalyha slhpnvfndv ngqypdfyas ngasaaptrq veqgrtmyan
      421 fsgwdidrsf mqlqalldpv rtsdivqslv ldakacgafp rwayfnteta vmpgdagsii
      481 vanahafgat nfdtqaalsi mkrstapgag cagtpvmgsr adydrlgyvp ssgpgdnqta
      541 sntleyavrd favsrfatal gdtaaagtll kssgnwqnlf drnaiqpkta agawvtdgtg
      601 fmegnseqyt wyvphdlggv vaqaggaasv vkrldtffth lnigtvqpyf yvgnevtmav
      661 pwvyawagap shtqrvlhas lanafgtgaa glpgnddlga isgwyvwaal glypvvpgvs
      721 gvalsspqfe kivvrvgqqd gsyrllhiva pgagsgdaas fyvkslklng apyptawlpf
      781 ehiakggkls ysmtadasaa twgtdasamp sfpqaasap
//
LOCUS       WP_175889089             881 aa            linear   BCT 11-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Burkholderia cepacia].
ACCESSION   WP_175889089
VERSION     WP_175889089.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..881
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..881
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=93821
     Region          55..864
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mklrhvvgig clavlsgcgg dqastdasvl aqmsnaqgnr ndqsnqndqg enggagkrsv
       61 lrsvdpmigt anldinadwg sgvrghghvy pgatvpfgmv qlgpdttgga htlpwnwdrt
      121 sgyqyddpli tgfththlsg tgigsggevr flptlapvdt atlakvaada sitynasfsh
      181 ddetaspgyy rvkmapvgsg ntpwnvkgak ilaemtatah agvhrytyfp saaaqkrsmi
      241 vsidnpiggs tasgkiqvid aqtiagweit nnwannkpty fvarfskpfd tkhvafstdg
      301 fkayltfadg ndsgavtvkv gispssiada qanlaaevga ksfdqvrgaa ervwadalgr
      361 irikggsadq rtmfytslyr tmlaptvynn adgsyvgtds tndgttsppt tskhanpgfd
      421 ysstfslwdt fraesplmtl vqpervdgwv kslltqfrqn gkgelpvwpl aqtetftmag
      481 hpsipliada ylkhltsagi ddiwaalttt qgasahgfdq yrqrgyvvag dnasvsttqd
      541 yafddwataa vgkaagksta dyrpylqrsq nyrnvfnptl nngwkfsqpk daqgnwvagf
      601 dptaaektdf sesnawidtw nifhdfpglv allggksqfi aqldrtfdpa npltfldnqg
      661 fpdltgrsgq ffagnepanh lpylydvagm psktqdrvrt vmddmysltl tagdrallsg
      721 dslkaaladp rrvrdsaipg nddcgqlsaw yvlsalgiys lnpvggvfyl gtplfeeati
      781 dipialgggd ggalkfgksr rftvtahtag ggapssvnry vqsvslngvp lhrpyityde
      841 mkaggtldfv mgatpndgwv sqwngqdpns alapslalaa k
//
LOCUS       WP_175889096             269 aa            linear   BCT 11-JAN-2025
DEFINITION  TlpA disulfide reductase family protein [Burkholderia cepacia].
ACCESSION   WP_175889096
VERSION     WP_175889096.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..269
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28982
     Region          <53..>123
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
     Region          136..265
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mlsigpfsir vvavavaall awlvarfiqr rppdgqhkta sslildtlll gliaarigyv
       61 aqwwheyaaa praivalgdg gfdwriglaa givfagwrvr rvpalrrpvm agmlaglaaw
      121 giaqgtlatl qhgapplaal rlealdatpv pvqrfagkpv vvnlwatwcp pcqrempila
      181 qaqqdhpgmt vlmvnqgeda qavrafleqk glrfdhvlld rtlhamqayg srglpttlff
      241 dakgnlvesh mgeitaarlk davadrfgq
//
LOCUS       WP_175889114             452 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175889114
VERSION     WP_175889114.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..452
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=48433
     Region          17..434
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mdnttpnlat draprlpriv ivgggagglh latrlgetvg rrgqaevvlv drypthfwkp
       61 llheaasghr dpashtieya aqakrhgfrf vqgalqrvdr aartatiaav qdadgteilp
      121 qreldyddlv lavgsvtnff nvpgaarhal plenldqaed frrkflaact kanhlaeqqp
      181 arraapicin vigagatgve laaalrhaiq qlttyrfkal vsardvhirl ieggprilpa
      241 ldarlsgkmh aqlralnvdv ltdtrvaevg adavttatge rlasditiwa agvagpamlr
      301 eigdialnra nqvivtdtlq tpddphvyaf gdcaacptag asgflppraq vayqqavylv
      361 nafarrvagk pvagftfrda gtvvslghag avyqadlgvr srslivdgla aiglykflyr
      421 khlfsvvgvk ralfqslshw lqsrnqpsik lh
//
LOCUS       WP_175889138             312 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cepacia].
ACCESSION   WP_175889138
VERSION     WP_175889138.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..312
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33244
     Region          80..286
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mpidtdiasl lerlamteap asldalrqat dttlrgwhgp leavdhtetf avptrdgqqi
       61 rvraywpava sesaarrpal vyahgggwcl gtlelydnpc ralanatqcv vlsvdyrlap
      121 ehrfpvpled fcdaldwvvr eaaglgldpa riavggdsag gnlaaaaclv arerggpsia
      181 hqlllyppld asmsttsyrt cgqgyyltqd vmrycfdmyl tdpadggspc vsplqaasle
      241 glppatllac eydpvrddah ayaerlreag vaadfvvlpg mihacihlag vtsaarqvfd
      301 vagaqmrgaf qr
//
LOCUS       WP_175889165             441 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175889165
VERSION     WP_175889165.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..441
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=47945
     Region          8..423
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mnsahqkphr ivivgggagg lelatrlgrk ygrggaaeit lvdrhrthvw kpklheiasg
       61 smdtsthevd ylahshrhsf ryrigemvgl drerreiqva pfiddegrnv tqarvfgydt
      121 liiaigsrtn dfgtpgvqah tvrlesqsda krfharmvna cirahtqaap lrpeqlhvai
      181 igagatgvel aaelhrttre vvaygldrid pdkdikvsli eaadrvlpal pprlsqater
      241 lldklgvevh tnarvaevsg dcvsladgrm laaelvvwaa gvkapdflsn lagletnrin
      301 qlvvgatlqt trdpdifafg dcaacpcggt dgnvppraqa ahqqaahlvt qmklklagkp
      361 lrdyryrdfg slvslgkfst vgnmmggpmg gslmiegmla rimyeslykm helalhgwpk
      421 vivdtlarll trrggqhvkl h
//
LOCUS       WP_175889182             434 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175889182
VERSION     WP_175889182.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45371
     Region          7..406
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mtspsssrpa wtyenrllli lfmtfgfvff drlalsflfp fmsaelhltn aqlgmvssal
       61 altwalsgaa tgawsdargt rkplliaavi gfsvcsalsg lvggfaslia fralmgiaeg
      121 pvlplsqslm vesstpsrrg lnmgllqgsa agllgamigp pvvigiatah gwrhaffvsc
      181 ipgfliafci wrwvrevppg garhaqadtv gapaaggaai srwallkern illcvliscf
      241 fltwfvviis fapvflvdsr hlspadmgvv mtclgaawvf wgfavpaisd rigrkptmvv
      301 faliaaacpv amihanslwa lcalvlatyt glgcftlfma tipaetvppr aiasalglim
      361 gageliggfv aptvagfaad kyglqfamwt satgailacv lsfglvetap avlrkralag
      421 taanrldtqn lggr
//
LOCUS       WP_175889209             507 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175889209
VERSION     WP_175889209.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..507
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52689
     Region          14..487
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(20..21,24..25,28,60,110..111,113..115,118,139,
                     142..143,146,270,273..274,277..279,282,310,314,366..367,
                     371,375,391,394..395,398..399,402)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mpryrcaalv laaclgtfla tldisivnva lptlqtaldt digglqwvvn ayalalsafm
       61 lsagplgdry ghkrvwlasv vlftagsvvc acasrlepll igraiqglag allipgampi
      121 lthafpdare raraiggwsa fsalalilgp lvggllvehg gwqdiflvnv pigvvtvllg
      181 awgiperrhp qhaafdplgq alsvvwlgll tygligigea gashmkvlap lagaavafvv
      241 fvrvetrier pllpvwlfrd rrlvranlas fvlgfsgyss lfflslflqq aqgrtpvaag
      301 wqlmpqfvmt aitsmlfgri aariplhalm vagyglvgam lavmagfgag tpyvpvgial
      361 avlgvgmgla vpatgmtvme lapaeragma satmnalrqt gmsmgiavlg smmsvgalhr
      421 mtaamqaags aqadtlarqa vmehvfaagq pallgayrda mahgfsiavl csgilsvgva
      481 vmlmmrretk kqsgraaaac vtssrpe
//
LOCUS       WP_175889190             231 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175889190
VERSION     WP_175889190.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 231)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..231
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=24479
     Region          5..230
                     /region_name="ArtM"
                     /note="ABC-type arginine/histidine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4160"
                     /db_xref="CDD:443325"
ORIGIN      
        1 mndflslvvq sgpdiargiw itlellvlsc tlafalavpl avartsarpw lstpsrlfms
       61 vfrgtpllvq ifvlyyglaq fsvvrasplw llvggsfsca lcaltlnlaa ymaedirggi
      121 agvpagekea alafgmsrfm ltwfvivpra igivaptlgn eivlqlksta lastitvldl
      181 tgvarhisie tyttdalmla givyvgitav lstvlkrveg llnrhlgsar a
//
LOCUS       WP_175889218             382 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175889218
VERSION     WP_175889218.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..382
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40979
     Region          1..370
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masismrrvq kaygdhapvi rdvdleigah efcvflgpsg cgkstllrmi agledlsage
       61 lsidgrrvdd vpaaergvam vfqsyalfph mtvyenmafg lklarvpkae idrkvrdaar
      121 ilqldtller kpkalsggqr qrvaigraiv repgvflfde plsnldaalr gqtrieiarl
      181 hrqferasvv yvthdqteam tladkivllh agadtaqhgs iaqvgapldl yhhpasrfva
      241 gfigsprmnf lpavvtacda rrttvtltps getftlprdg salgagaavt lgirpehltl
      301 gaahdattla rdvalverlg eqtyvhldqp gghaliakvp gdaqvrtger vhvhapaaac
      361 hlfaedgrav pacadvhvhh ya
//
LOCUS       WP_175889240             282 aa            linear   BCT 11-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Burkholderia cepacia].
ACCESSION   WP_175889240
VERSION     WP_175889240.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..282
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31408
     Region          11..263
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mtsiedrvaq avtpeliaaf reegavcikg ifspdevaal ragidanlaq psprakvasr
       61 pddpgwffed fcnwqqnday rdfivrspap svaaalmgte nvrlhhdhll vkepgtrqrt
      121 pwhqdqpyyn iegddnvsmw ipvdpvples tlefvagshr gpwlmprtfm dkeakwfpeg
      181 sladlpdieg draafpirhw alepgdmvcf rmltlhasgg tqnrrrafsi rfvgddirha
      241 prrwktspdf pglaeqlpdg apldhplfpv vwsrgagqag vl
//
LOCUS       WP_175889251             506 aa            linear   BCT 11-JAN-2025
DEFINITION  peptide MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175889251
VERSION     WP_175889251.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..506
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55279
     Region          7..462
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mmqppvsqtr sfttvfliem werfgyygma allvlfmvdr lgftdshanl twgaftalvy
       61 aapsiggwig dkvlgarrtm iigasvlcag ylmlsvpndq ltymyaslgv ivvgnglfka
      121 naanlvrriy egddaridsa ftiyymavni gstvsmlatp wikdhwgwht afavccggml
      181 lailnfmlmh rtlahvgslp ddqpirwkrl gavalggvgl alvtlyvlqh kqlavasvwa
      241 aafailaifa ymiakserse ragliaalvl igqvilffif yvqmstsltl falrnvdprf
      301 mlfgttlftw saaqfqalnp iwimllspvl vwvynavakg grdlpvaaky algfgavaag
      361 ylvftisgrf avdgrvsswf mvwgyglysl gellvsglgl amiaryvpar msgfmmgayf
      421 vatgvsqylg svvanfaqmp shelpatesl plylslfekl gwlaaigmll allllplmnr
      481 lsrqhqrcte erreeslqaq gaataq
//
LOCUS       WP_175889262             266 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Burkholderia
            cepacia].
ACCESSION   WP_175889262
VERSION     WP_175889262.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..266
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28500
     Region          18..260
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mttpgafssl tgddapsilr ndddgiawlt ihrphvanal sadairrlcd elvtlddnpa
       61 iraivirgag erafsagidl gdpdmrgmrp mrglarnvhe lvlelrkpti aaingfavgg
      121 gfeialacdl riaadhatfa lpearvgmga nfasvllprl lpraiamell ftgrrfdade
      181 aqrigllnrv vpaaalddtv relaqtisen apltirrike tatrsqglpv aaalrldvgp
      241 dvyasedrie garaflekrk pafkgr
//
LOCUS       WP_175889267            1028 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Burkholderia cepacia].
ACCESSION   WP_175889267
VERSION     WP_175889267.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 1028)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 1028)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11534155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1028
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=104602
     Region          12..77
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          118..180
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(124..126,129)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          203..265
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(209..211,214)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          283..1026
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mteplasaal htielsvdgm hcggctgrvq ralaavpgvv daavdldaha atvtaqetvd
       61 aarlieavga agygasvrap vletaaaaha hpveaspapm aaaastaghp lpanstield
      121 idgmtcascv srvekalakv pgvtrasvnl ateratvdvt advsaaqlve tvkqagygat
      181 ptmtdagfta lapsspaapa sieldidgmt cascvsrvek alakvpgvtr asvnlatera
      241 tvdvtadvsa arlaeavkqa gygatpvaga aippaasttp adleldidgm tcascvgrve
      301 kalaavpgva rvsvnlater asvhgagald aatliaavtt agyraslada ssagatagad
      361 tqpasaaqdp etrkrleair erdlviwsav lsapliapml vapfgihlmp ngwvqlvlas
      421 ivqfgfgarf yraawhavka rtgnmdllva lgtsaaygls lwmllrgtgh sghlyfeasa
      481 vivtlvrfgk wlesrakrqt tdairalnal rpdrarvveh gverdvplaq vrvgtrvsir
      541 pgervpvdgr ivsgrshvde slitgeslpv pkddgdpvta gsingegalv vettaigaet
      601 tlariirlve saqaekapiq rlvdrvsevf vpailgiavl tlagwliaga gtetailnav
      661 svlviacpca lglatpaaim agtgvaarrg vlikdaqale laqrttviaf dktgtltegk
      721 psvtafeavg vphdealala aavqrqsdhp laravvaahd advaargsav ppasaadara
      781 vagrgvearv ggqllalgst rwrdelgiav ppaldaraae leragntisw lmradapral
      841 laliafgdtv kpgardaiaa lsargvasvl vtgdnrgsaa avaaslgige vhaqvlpddk
      901 arvvaelkrt hggivamvgd gindapalaa advgiamatg tdvamhtagi tlmrgdpalv
      961 adaidisrrt yrkiqqnlfw afvynlvgvp laalgwlnpv iagaamafss vsvvtnalll
     1021 rrwkgrah
//
LOCUS       WP_175889283             207 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia cepacia].
ACCESSION   WP_175889283
VERSION     WP_175889283.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..207
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23101
     Region          1..200
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mlhilgkips invrkvlwlc telnlpfeqe dwgagfrttn dpaylalnpn alvpvikddd
       61 fvlwesntii rylanryggd alypaepqar arvdqwidwq gtdlnrswvg aflglvrksp
      121 dhqdpagiaq siagwtkhmq vlnaqlektg ayvagdtftl adipiglsvn rwfgtpfehp
      181 elpavsryie rlatregfkq yagspnp
//
LOCUS       WP_175889287             706 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia cepacia].
ACCESSION   WP_175889287
VERSION     WP_175889287.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..706
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=76201
     Region          36..639
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mtdhtasppp ppvppprrrr awrtlagall gltlacagig awtihriwtq lpsvehlavy
       61 rpalplrifs rdgdllaeyg verrefvple ripplmrhal laaedakfyq hgavdvggla
      121 ratfanvvtg qpgqggstit mqvarnfylt rdkvlsrkla eilmaakler eyskdkllel
      181 ymneiylger aygfaaaanv yfgkpldaln ageaavlagl pkapsafnpv vnparatarr
      241 nyvlgrmhal gqlddatyra avdapialat tpppgivaap yvaerarrmm verfhddayt
      301 lgldvtttis mrdqraaeaa lqrqlsrqpg akrdarngle galvsldaat gdmlalvggv
      361 dfnrnvfdha lqayrqpgss fkpfvysaal ekgyfpgvlv ddtqrtlthe etgarpwrpr
      421 nfgnryegfi pvrrglvrsk nlvavslmqa tdaryvqqha vhfgfdaqrn paslplalga
      481 gavtplelas aysvfanggt rmeprlilsv kqrhggamye attpegarvv sarnaflmds
      541 mlrdvvkagt argvlalrrd daagktgtsn gskdvwfagy ssgivavawl gydtprpmgr
      601 atgatlalpv wldymktavd grtpidatpp qdvalvdgdf vyaeytrgtc tadvppyirs
      661 rfacggamaq dasdapagsg kpdapmpaav daaerervld lfrtdd
//
LOCUS       WP_175889288             127 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia cepacia].
ACCESSION   WP_175889288
VERSION     WP_175889288.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..127
                     /product="VOC family protein"
                     /calculated_mol_wt=14072
     Region          1..126
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 mplpmtriil yvqdvtllka fyqrhfdlpv ieeidgewav ldagaielal hlagpafrha
       61 aapsnappat nnvklvfrid adieahrdrl aragvtvrdv krfdgfpyrl ldgidpegnv
      121 fqvmqpd
//
LOCUS       WP_175889303             411 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175889303
VERSION     WP_175889303.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..411
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42771
     Region          22..399
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(32..33,36..37,40,72,127..128,130..132,135,156,
                     159..160,163,235,238..239,242..244,247,271,275,328..329,
                     333,337,353,356..357,360..361,364)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mnvatqagwv srlfpalsea slrrylsgqv asvlgswtqn vtlnlliyhl sgsaailall
       61 nfllygpqli vapvagsrig sanarrvtlc vlttsllltc slftlsllgl lgvklilaha
      121 laigvssave tparqvlllt slqdathtsn avamntmvyn vgrmvgptia gfvyptlgpr
      181 tsfaiyalal cfmaacvrsi raatvdrpsr aesglrdavg yvlsdafsar ylpilacigl
      241 fagsyqtlvp lladqgfhda arftgvffac agagslsaav llssafgpra shrfiayapw
      301 tavgalavla attdaagsip afyalgfslt faatstnati qrqcpdhvrg glvgmygmay
      361 ngtmpfgyll vgsasealgv rhtfaamaav lasgviavia wqrftrsqir a
//
LOCUS       WP_175889356             748 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Burkholderia cepacia].
ACCESSION   WP_175889356
VERSION     WP_175889356.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 748)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..748
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..748
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=81284
     Region          43..743
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mnspleatpd arrdessagr arapegtfel srkrvdeldt ifgeggllar aldgyrprts
       61 qiemaravas ameasarrmp epeifetrkr parrlgdgdk aaepgadaaa aepdsdagdn
      121 tliveagtgt gktyaylvpa mlwggkvivs tgtkhlqdql fqrdiptvrn alavpvsvam
      181 lkgranylch yylqrtadng rlpsrqdtay lqeivrfaki tksgdkaela svpetapvws
      241 mvtstrdncl gqecphykec fvmqarreaq qadvvvvnhh lffadimlrd tgmaellpna
      301 ntvifdeahq lpetatlffg etlsttqile lardtvaegl shardavewv klggdleraa
      361 rdlrlafand qivrmslaql gddhpmfgal daleaaldal asalasqaer aeslgaclrr
      421 arelqdllag waapgateaa akadaaaagd kaasdgdpne kvrwvevfah tvqlhetpls
      481 vapifakqra gvprawvfts atlsvrgdft hyaaqmglss rrsmtlaspf dyqsqgllyv
      541 prnlpqpssp aftdavfdaa lpaieasggg vfmlcttlra vdriasklrd viesrgwntp
      601 llvqgdasrt elldrfrayg nailvgsqsf wegvdvrgda lslvvidklp fappddpvla
      661 arldaltkkg lspfavhqlp qavitlkqga grliraetdr gvlmicdtrl vdkpygrriw
      721 qslppfkrtr eiavvqdffd ehrsakrt
//
LOCUS       WP_175889379             236 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175889379
VERSION     WP_175889379.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..236
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=24370
     Region          7..216
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          69..98
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          101..130
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(102,106..107,110..112,114..115,119,122,132,136..137,
                     140..142,144..145,149,152,161,163,165,169..170,173..175,
                     177..178,182,185,194)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          131..161
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          163..194
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mtkptnhlpk ralvaaafva sglfaaagah aesldaivka vkfddiadig kqlksgkldp
       61 ntiapngdpl iviaareksd kvaaalaatp nvdlekedka getalmlasl ngdlglakll
      121 vdkgaevskk gwaplhyaat ngqdavvkll ldhdayidta spngttplmm aargnhastv
      181 tllldqgadp qvknqlgita lefakhynap daieilskrt trigastpad aqksak
//
LOCUS       WP_175889423             287 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia cepacia].
ACCESSION   WP_175889423
VERSION     WP_175889423.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..287
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32061
     Region          10..147
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mnqslplrlr gvdhtarptw klretvefyr dilglplvht isargwgpet hpdflhfffd
       61 sgngstiaff yylgepqpad rppmpptpnd hvfdathtaw laesedellt wkaaleakgv
      121 qvssttqhev iesiyfrdpn gyfieitvkl rplekldeqd aartlqaain aehvaqqsag
      181 dvreidtvwq ekgrllgnef giasdapgmf vpalaefasv vdaarqnaey rvsqpssdyf
      241 lieaqsalef drralgmkpa vwyglftggl rgrieafdkd rvrviaa
//
LOCUS       WP_175889473             240 aa            linear   BCT 11-JAN-2025
DEFINITION  (Fe-S)-binding protein [Burkholderia cepacia].
ACCESSION   WP_175889473
VERSION     WP_175889473.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..240
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25860
     Region          <2..237
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mrvglfvtcl vdlmrpeigf salklirdag yevivppaqt ccgqpaynsg dralardlae
       61 ktlrefeqfd yvvapsgscg gmirahygdl frddpelmgr ytrfqrkvye ltdflanvak
      121 vslapgeftg pvtyhdscsg lrelgvkaqp rallaqrgia vtemkdcehc cgfggtfavk
      181 ygdisaaiad ekcanvrasg agavvlgdlg cmlniegrlr rtgdrdtrvl hvaqvlagdv
//
LOCUS       WP_175889489             308 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Burkholderia cepacia].
ACCESSION   WP_175889489
VERSION     WP_175889489.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..308
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32344
     Region          7..272
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(34..35,38,90,103,105,134,167,253,256)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 matafpeila lgeamiefnq sqpgrpeflq gfggdtsnfc iaaarqgast gfvsaigddp
       61 fgrlladmwr aervdttyvr idrtaptgvy fvthgadghq fdylragsaa sryaagdlpl
      121 dalaaakavh lsgislaist aacdaafaai dharrngakv sfdtnlrlkl wplpraravm
      181 realrqtdic lpswddvtai tgandrdaiv damlehgpqv valklgkega yvatpnerrv
      241 vpgfaveavd atgagdcfgg afvarivagd dpfaaaryan aaaalsttgy gavapipqre
      301 averlmqr
//
LOCUS       WP_175889570             749 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cepacia].
ACCESSION   WP_175889570
VERSION     WP_175889570.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 749)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..749
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81069
     Region          66..749
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mkkveqrkme watgtrlrai aaaasvafga aagqayaqta pavnagaaas assaqggaaa
       61 sastgtlpti nvnaasegdg tvglvakrsr tgtktdtpin eipqtinvvt aqqiemtgat
      121 dvnaalryvp gfssygsdnr sdwyaalrgf tptayvnglq vpntinlasw rvdpymidsi
      181 tvlrgptsvl ygagdpgaii dvqtkladge rvreagvqig nyarkqfmid vgdkldpdgk
      241 yayrfvgvar dgnaltgpnn dqrvalapsf rwrpnadtsl tlsatylqdw gdissnflpa
      301 qgtvlpnpsg qinkdvyegd pnfnyyrkkq wsvgyqfeqn ltsawkfrqn vrlmhlsldn
      361 gsvfgngfvd gsttdvsrwa gvfqmnysrf didnnvegrf atgplqhtll lgfqynrqta
      421 tdsewlaaap plniynpvyl pvtkavfdpa stfrtntytt lntfglyaqd qikwnrwtlt
      481 lggredwvnm rmddraggts tkadvtaftg rvgltyqgdy glspyisyat sfnpligvnl
      541 lggglpqptr gkqieaglrw qppgknlmln aaiyqinqtn vltpalpdqd ptgtksvqtg
      601 evrsrgiels atgkvtrnls liasyvyqdv knvkandvsl nnwpvdiprp rqmaslwadw
      661 twhtgplsgl glgggvryqs asagaadnsl tvssvtlfda gvhydtrnwr favnatnlan
      721 rhyisgcqsm nvcvfgtdrt viatakynw
//
LOCUS       WP_175889622             817 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia cepacia].
ACCESSION   WP_175889622
VERSION     WP_175889622.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 817)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 817)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 817)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..817
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=87240
     Region          1..803
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mlvvgsqsha tefnssflni dgsnnvdlsq fsqadftlpg eymldvqvnd lfyglqaief
       61 iavdasgagk pclrpelvaq fglkpslakd lprfqggrcv dlgaiegatv rylksdgrlk
      121 itipqaalef sdttylpper wsegipgaml dyrviantnr nfgtgggqtn siqaygtvga
      181 nwdawrfrgd yqaqsnvgnt ayadrtfrfs rlyafralps iqstvtfgdd yltsdifdtf
      241 altgasirsd drmlppslrg yaplisgvar tnatvtvsqa grvlyvtrvs pgafalqnin
      301 tsvqgtldva veeedgsvqr fqvttaavpf laragqlryk aavgkprlfg gagitpffgf
      361 geiayglpfd vtayggfiaa sgytsialgv grdfgafgal sadvtharar lwwngttrng
      421 nsyrinyskh fdgldadvrf fgyrfserey tnfaqfsgdp tayglanskq rysatlskrf
      481 gdtstyfsyd qttywerane qrvgltltra fsigtlrnln vsvsafrtqs agasgnqvsv
      541 tatlpiggrh tvtsnlttgs gstsvnagyi yddpdgrtyq vnagatdgra sanasyrqrs
      601 sayqltaqas tlanayaaas levdgsfvat qygvaahang nagdtrllvs tdgvpdvpls
      661 gtlshtdsrg ytvldgispy nvydatvnve klplevqvsn piqrmvltdg aigfvkfsaa
      721 rgsnlyltlt dpvgkplpfg asvqdmangk elgivgegga afltqvqpks tlavragert
      781 lctidtlpnq lqlegtpipv tcqtpgesha aaarver
//
LOCUS       WP_175889753             385 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF4382 domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175889753
VERSION     WP_175889753.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10626736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..385
                     /product="DUF4382 domain-containing protein"
                     /calculated_mol_wt=38696
     Region          32..182
                     /region_name="DUF4382"
                     /note="Domain of unknown function (DUF4382); pfam14321"
                     /db_xref="CDD:433865"
ORIGIN      
        1 mnniikgalc aafvpfilag cgggddgsgt qtgtlhvamt dapscgfdhv yitvsqvrvn
       61 ananaadnda gwstvslatp qkidllsltn gvladlgqta lpagqyqqvr lvlaqnqgnn
      121 lansvvptgg teqalatpsa tqsgykiiqp ftvqpntlvd lvldfnacks ivqrgngsya
      181 lkpvvtavpt vvsgaisgyv asaeagatvy aeqggkvvrg tvadstgkfv lspliqsstq
      241 gnydvvivqn nfasgivrsv pvvvntttav sastapitlp astmstvsga vtasanafvr
      301 alqtidanay eitsinanld tgayalnvpt aapivgtysg slpvalaasp aaaaqytiea
      361 daasgatqst nvnattsqsn vnftf
//
LOCUS       WP_175889663             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175889663
VERSION     WP_175889663.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46126
     Region          13..417
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(25..26,29..30,33,72,130..131,133..135,138,158,
                     161..162,165,247,250..251,254..256,259,287,291,343..344,
                     348,352,368,371..372,375..376,379)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mtqslpsarq pgraataafi gtmiewydfy iyataaalvf gelyfpshdr fvstmasfat
       61 favgffarpl ggvifghlgd rigrkkalmt tlmmmgvatv cvgllpdyst vgllapvllv
      121 alrvvqgiav ggewggavlm agehapqgrr tffasfaqlg spaglilsli afravtsmdk
      181 adflawgwrl pflassvllv vgilirlgvn espefarvke tnrtvklpva evfrsasglv
      241 flcigantig iagvyftntf miayttqyvg vsrslildsl favaiiqffa qpvaawiaeh
      301 iggarflkla allamlspyp mfmlvqggts asliagiala vvcmagfysv iagfvsdvfp
      361 ahvrysaisl ayqicgaiag gltplvgtwl ahrfagqwwp lavfytclag vsllsivaid
      421 arraarpaaa ealgsq
//
LOCUS       WP_175889783             787 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia cepacia].
ACCESSION   WP_175889783
VERSION     WP_175889783.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 787)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 787)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..787
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..787
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85879
     Region          69..769
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msssfaarps rgrlalacaa afawpvahaa stddtrvdta rrgverpaet vapasatatv
       61 spvpagstlt avsvtaqrqp vdpdtpavvt sitreqiesh tnvttedalk yapnlmvrkr
      121 yigdrnsvfa grdfnelqsa rglvyadgvl lsnllgssya ypprwslipp ddiarvdvly
      181 gpfsalypgn sigstvlltt rrpekleasl stqfftqryh dgygfadsfg gnhqtarian
      241 rvgrfwfals ldrlenngqp mqyaspnsay npklgaaapv sgaaidigpn gkprtivgaq
      301 tierteqlne tirmgyaftd hvdatltlgh wenhyrqhge tflrdaagnp vyggnvsigg
      361 rnmtvapnaf apqrgdqenw lyalglngrl dsgwrlsgvv saydvsrdvq rsastvqgga
      421 gtlfqgdgtg wrtfdlkaea pevkghtftf gyhydnyfls nvtyntadwl agpttslast
      481 yrgdtrtqal fgqdawrfap gwlatlglry erwdayggal gnasgtlgya drsanalspk
      541 valqwdatdv wrfrlsfatg tryptvgelf qgtisnnaiv nnnpnlrpek aidwdftaer
      601 dvgvgvvras vfqsdlrdsi ytqttvsgat tvtnisnvdr vrvrgvelaf sgenvglrgl
      661 gldanvsasn aqiladaanp ayvgsrfpri prmranllas yrfdehwlas vgvrysgrqf
      721 ntldnsdvnp evyggtssft iidlkaryrf drhwtasvgi dnltdrryyv fhpypgrtfy
      781 gelkwsl
//
LOCUS       WP_175889888             198 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175889888
VERSION     WP_175889888.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21377
     Region          7..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrkidperve akrrqildaa idcfardgfh atstaaicka agmspgnlfh yfptkasiie
       61 avaqddqrem aelfarhaaa adalaaieei altlmelssd pvyaricvet aaeatrnpdv
      121 aalfaaneaq vkgrmvalik rgvaqgkidp slkpdlvatw llalaegavg rvvfepgfkp
      181 rahramlrti iqrmlkpq
//
LOCUS       WP_175889866             520 aa            linear   BCT 11-JAN-2025
DEFINITION  S41 family peptidase [Burkholderia cepacia].
ACCESSION   WP_175889866
VERSION     WP_175889866.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..520
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55389
     Region          72..418
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mmpskravlr lavcaavtaa flpcaspvga qqpapappas apaasssspa spatarppsp
       61 cppdwepqic elkaavevlk rqhltdvdig alldatthag irtlpyarff dakeeqerse
      121 derrardgtp gigivfetrp dglhivdvip dapaeqagvr pddlvvamnd tsvvgidaad
      181 ltklakgdag vplkltvqrg pshamlsfap vrtilkphpa takrlagdil ytrlssfpep
      241 avgayidavq aarragppvk gvildlring ggalnaaigi talyagrdrt amvtvergda
      301 nrrryttnwp dymlpvmhgq dplaplqadd wwrtvplvvl vdgqsasaae ataaalkdlg
      361 rakllgmpty gkglaqtgvd lidgtrlnft farnlrpngc pmdgygvvpd wlvpprrdsd
      421 vdgvllwyre adlprapyad rlapdpfakv rkerqklreq ralakidsak saalpqrefg
      481 tasdwqlgqa laalagrpvr tvdarpqlmp aqpvceragd
//
LOCUS       WP_175889902             241 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia cepacia].
ACCESSION   WP_175889902
VERSION     WP_175889902.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..241
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26294
     Region          10..235
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 midiraanqr graehgwlss rhtfsfanyy dpkqvgfsdl lvinddrvap grgfgthphr
       61 dmeilsyvld galehkdsmg tgsvivpgdv qlmsagtgvr hsefnhspel pvhflqiwvg
      121 paekgaepry qqtnvtaddk rgklalvvsp ngdagslkir qdtriyaglf dgteratlel
      181 apdrfayvhv argsvsvngv tlgegdgvri rdertltfad gkdaevlvfd lrpvevtaew
      241 a
//
LOCUS       WP_175889963             472 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175889963
VERSION     WP_175889963.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..472
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=48575
     Region          6..466
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 msalpdraaq rhalaatlgd gwldgasaea cepyatdvtr hgglalgvar pastadtsal
       61 arvavahrva lvaqgartgl vgaavpdrsg tqcvvsfdrm ravrafdaan rsitveagar
      121 lsdinrvaad aglclpidlg sdpaagglvg anaggsrlik ygdvrrnvlg vevvladaag
      181 tvidalaplr krnagfdvtq cfigangahg lvtavsfala plersscaaf vafasydaal
      241 agllaferaf gemlsafefm saaavgcvaa afpalripfe adaaacyalv eiatgmpgld
      301 glleeraiat ldtlagervv ldaacapaer fwrirdalpv avaqhgipls fdvsfprgal
      361 aafvddaeqw iaaahpslrc hafghfgdgg chlvvsipha daerygplqq valrgalyer
      421 vvraggcfsa ehgvgpvnva yyrkhvpaaq relaaavqha vdplgligrv ry
//
LOCUS       WP_175889946             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175889946
VERSION     WP_175889946.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33910
     Region          23..80
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          109..303
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(124..125,127..128,131,135,137..143,233..238,
                     244..245,247..248)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 misdqngeld sqpmsanlps lmalrcfeaa arhenfsraa delclthgav sravrlledd
       61 lgvalfqrrs rrvfltdagr klaqavhdgl glmrhaaqel rteaararrw vlsceptllm
      121 rwliprwpdf qarhagvdvh laaaggpfsf dsgidmairr ndfawpagyh aerlfaervg
      181 pvcrpdkvda wfsarrgsrs lktdvpqlht rtrpdawkew avaahqpvvr grgqvfdhfy
      241 fslqaavagl gvaigpwhlv rddiesgvlv apmgfvddgs hyclltpepv vagraqadvl
      301 awlrava
//
LOCUS       WP_175890004             701 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cepacia].
ACCESSION   WP_175890004
VERSION     WP_175890004.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..701
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75654
     Region          7..701
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 msrrnwaaap maivvgatgv gaadaqeatl ptieisgqra sapfrtrdst satrgeadvm
       61 eipfavssvd aklvrtvaat rgedlydwva gvarqnnfgg lwdnyavrgf agdgntsgtd
      121 ylvngfswnr gmsvprdtvn lermevlkgp asalygrgdp gglisyttkq pqfarantig
      181 vsagsygalr etldstgpvt kslayrfvam nenngsfrdt vsskrylfap sftwdigadt
      241 tlhyefesar qrapldrgvv avggqlgaip asrflgeprd gdydvrntgh qftlehrvda
      301 nwsinagfaq rttdlsgrss eafalqpdgr tlwrryrqva fhsndlqgri etagkfstgg
      361 ightlvlgvd ayrfnydqfv arstptaaap yaidifdpvy gqpaptprta tnllerddgq
      421 glyaqdtlaf gphwkilagl rwdrfhqsve nrlkgttssq vqtalsprig ivyemspals
      481 lyantaysfr pnngadvdgr afdpekghgy eagakwagar wlatvaafyv nkrnvltadp
      541 anagfsraag evrsrgvefe wngdlghgvr glvnlayvda evthdavltp garlvdiprl
      601 sgsalllyet avpfadkaga gagliyvgrr agntantqdg felpayatvq lngyvqvnkh
      661 lrasvvlnnl fnrttyvssy nslwvtpgap rslfaslayt f
//
LOCUS       WP_175890022             239 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia cepacia].
ACCESSION   WP_175890022
VERSION     WP_175890022.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..239
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26550
     Region          1..206
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mkiisgplsm fgakveiaah ekgidfelvm apfsqrrgyd pkhpdvvrin pkrqvpvlid
       61 gdlelfdstq ifeyfedlkp apalwpahpa araiarqleh gsdeiyfphv vrlmgleatp
      121 ddpaaraard eaaryyrrme reladrefla gaysyadiaf ymaqlfgark gapmtdetpr
      181 llawrermta rpavrkvaga magylasige avpdflrghd slpsgadrrg etafgddcr
//
LOCUS       WP_175890047             221 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175890047
VERSION     WP_175890047.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..221
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24247
     Region          36..191
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mkdesaqknl nqdvsiepqa agpkrvltgr grntvarila saieifaaeg ygglsmrkva
       61 tsaglalsnl qhyfptredl faaiitetia eysgnyesir idaslspeqr leklvrllie
      121 dgkqprtqsl fvnfwalaqm qefarksmed aylfqrrmis gfvaavnpql spnvlarraa
      181 liagqiegll vlipqrnrfp sdikgiedea vkaiitvasm p
//
LOCUS       WP_175890069             337 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175890069
VERSION     WP_175890069.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..337
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34330
     Region          23..337
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mnlpdsssps sptlaaaagn gdapppramw aqlrrstlfy plvglivvci ammiaspsfl
       61 saanlenvlr qvsinaiiav gmtcviltgg idlsvgsvma lsgtlaaglm vagvnavaal
      121 aigiavglgf gflngvfvaf agmppiivtl ammgiargla liytggypid glpdwvaffg
      181 sgkvfgiqap vlimlvvyai awllldrmpf gryvyaiggn eqatrltgvr varvklivyt
      241 lagltsalaa ivltgrlmsg qpnagvgfel daiaavvmgg tsisggrgai lgtlvgalll
      301 gvlnnglnmi gvnpyvqnvi kggiillaiy isrersr
//
LOCUS       WP_175890113             430 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175890113
VERSION     WP_175890113.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..430
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=46931
     Region          4..412
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 matptriviv gggiaglqla trlgerlgrs graqvtvvdr spthiwkpml htiaagtrdv
       61 qqqqviflah ardhgytyqp gelkgldrar rrvqlgeirs qdgelvldar eleydvlila
      121 lgsqandfgt pgvrehcyfi dsqpqaetfn ealrmrifrs iardepfrva ivgagatgve
      181 laaelsrlle vaqaygdetv rdrlqltlle sgprilaafp pkisasaqqr leqigfhvlt
      241 strvtsadan gfhygdgsfa eadlmvwaag vkapdfmqal ggldtnranq ivvgptlqat
      301 gdehvfaigd casllpdgqe rplpptaqva tqqaehlakh lpawldgkpm ppfafhdfga
      361 lvsiseydaf gtlgqfgffr ggfiqgrlaq fshlmlyrrh qqalhgfska sllwiaerin
      421 gcarprirls
//
LOCUS       WP_175890101             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175890101
VERSION     WP_175890101.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33807
     Region          15..74
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          103..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(113,154,168,170,232,249,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(114..115,117..118,120..121,124,128,130..136,197,
                     226..230,237..238,241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mefgyhrsms gtidlnqivv fvrviqagsl seaarrlnlp kstvsrkisd lenrigerli
       61 qrttrklslt eagrvlferv spamsdieda esavagmret prgvlrvaap msfsplrpii
      121 aeylvrhpdv aielvctdrl vdlvderfdv airagalvds tlvarrlgta qfmlvatpey
      181 cerhgvpmtp aeltshacis lggkatshvw pleargkrte vhitprlmvn diemvrvavl
      241 agvgiawlpk alcaddldgk rllhllvdws wgeipvyaly ptkrhlspkv vafidllaeq
      301 irlhda
//
LOCUS       WP_175890115            1057 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cepacia].
ACCESSION   WP_175890115
VERSION     WP_175890115.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1057
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113180
     Region          1..1038
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mdfsrffidr pifavvlsiv ifaiglisip mlpageypev vppsvvvrat ypganpkeia
       61 esvaepleea ingvegimym ksvagsdgsl qvvvtflqgv dpdtaavrvq nrvsqalsrl
      121 pdevrqygvt tqkqsptplm yvslyspdns rdslylrnyl tlhvkdelsr ltgvgdvgls
      181 gsgdyamrlw ldpnrlasrg ltasdviaav reqnvqvsag qlgaeptpkk ndfllsinvr
      241 grlrtaqefg divlrngddg qvvklsdvar velgagdytl rsyfndkqsa vvgiflspga
      301 nalevakavy akfdelskrf ppgvayrpvw dptvfvrdsi ravqhtliea vvlvvlvvil
      361 flqtwrasii plvavpvsvv gtfawlyllg ysintltlfg lvlaigivvd daivvvenve
      421 rniaqglspr daahqamrev sgpivaialv lcavfvpmaf msgvtgqfyr qfavtiaist
      481 visainsltl spalaakllr phgapkdalt rgldrafgwl frpfnrffdr ssdryhgvvs
      541 rtlkrrgvvf avyaallgat alllnavpgg fipvqdklyl fagaklpega slartsevte
      601 qmtkialgtd gvemvpafag lnalqgvntp nitnsyvilk pfdqrhrsaa qinadlnarf
      661 aaigggitya lmpppiqglg ngsgyslyle drgglgygal qnaltafqaa vaktpgmsyp
      721 vssyqanipq levkvdrlka kaqgvaltdl fstlqvylgs myvndfnlfg rvyrvmaqad
      781 aghrqtaadi anlrtrnakg emvpigsmvt vapaygpdpv vryngypaas ligdadpkvm
      841 sssqaieklq qiakdvlppg ivlewtdlsy qqvtqsnaai vvfplavmlv flvlaslyes
      901 wtlplavili vpvcicaalf gvwlsggdnn vfvqvglvvl mglacknail ivefarelei
      961 qgkgvieaal eacklrlrpi vmtsvafiag svplliggga gsevraatgi tvfagmlgvt
     1021 lfglfltpvf yvairklagg tpavwsehhg tlegenr
//
LOCUS       WP_175890136             296 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia cepacia].
ACCESSION   WP_175890136
VERSION     WP_175890136.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..296
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31939
     Region          27..245
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mtksptgsen tqshlmheqr srdivhrarg mgngsitrlv spsdlgrlik pfvfldlfes
       61 dgsharplef gwhphsgiat vtvvldgavq yaettgnagv lpsggvewmq agggvwhtgt
      121 fdtaplrgfq lwvalppdle naptrsqyvm peqvpsagpv rvilgtydgm tspvdappmt
      181 ylvvtlkdge hwafvpppgq diawvsvmdg alrassritr geiaiferae taielvaegd
      241 trfvlgaatq hpyelvlghy svhtsvealq rgeagihrig rqlraegkqs yalqsm
//
LOCUS       WP_175890152             631 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia cepacia].
ACCESSION   WP_175890152
VERSION     WP_175890152.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 631)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..631
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=66589
     Region          <3..612
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mantyvqrdl saltarvrig dantsgelfd tfafrglqla tddrmwpdsq rgyapvvrgi
       61 antsarvkir qngaviydta vppgpfvidd lfptgyggnl vvtvteadgs ertfsvpyaa
      121 vaqslrpgrs rfgfvagtvr nvdlsytprv vqatysrgvn nlltlyggvl anehyrnvla
      181 ggafntplga laldvsgaft saygqrtrgs svrvtyskti datnsnlsva ayrfsssgyl
      241 dfgnalafvd nakrnltgaa arpawrarnr vsvtaaqpfg erwgqlyvsg ytqnywtrsg
      301 tdtqfqisys nryrqfdytv svnrslasgg nadtqamlsv svplgasars prlsvyaard
      361 slngftstat atgsvgaaye gnysvsaarn adatyagtvs gqyrtpvaal qgmlgkgndy
      421 gsaslgvsgt vvahpggvta vpytadtmav vaapaaggat vagysgirld rrgyavvpyl
      481 spyrvnqvei dprglpadve lqttsqqvap rqgaivmlry ptvtgrplli haaapagtel
      541 pfgapvfdgr gnnvgivsqg gqvyarlsep ndtltvkwgh adawrctirv alpppeqraa
      601 pigierieap ckldnpsada pevrrapage s
//
LOCUS       WP_175890170             222 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175890170
VERSION     WP_175890170.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..222
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23690
     Region          29..187
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpprhvqvpa ppgqpaaqpa palrrrprqs raqassdalq qafvqlller gyakatirei
       61 aavagvsigt fyeyfgdkqs laalcihrhv qaladrlrda varlrgapra elaaalvdlq
      121 vdaigadaal wgalfvlerq vsplaayrrh ydayvalwrd alahaadppp aarldgiarm
      181 ahtlcyggls qalltlgpaf diaalrdelr avllaylaaa gr
//
LOCUS       WP_175890204             423 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia cepacia].
ACCESSION   WP_175890204
VERSION     WP_175890204.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..423
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=43871
     Region          207..414
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(214,254,292,395,398)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(214,395,398)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(214,254,292)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 msfrssiaaa vlgaaafasp lvasasaapa gwvaawatal qpipdlaapp plyrapdvag
       61 rtvrqivypt vsgraarirv snaygrsplv veaaslarag egaalsgdaa vpvrfggkvs
      121 vtlgpgqele sdpvgidvra gqpyaislqm gpnqrmtvwh rvsnqfnyvs vpgehvsdpg
      181 aaafrtrftq fawvtelave tgsarasvaa igdsitdglr ssvnrnrrwp dalarrlaas
      241 gtesigvanl gisgnrllsd sacygtslas rferdalsra gvkaaivlig indinfaamp
      301 pragldcdhp htqvtaasli dgyrrlidaa hrqgvkvfga tltpaglpag reairlevnr
      361 wirsgggfdg vvdfdavlrd parpsvlqrr fdsgdgihps dagytamada vpveplqaav
      421 ggk
//
LOCUS       WP_175890122             430 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Burkholderia cepacia].
ACCESSION   WP_175890122
VERSION     WP_175890122.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Yang,W. and Mizuuchi,K.
  TITLE     Site-specific recombination in plane view
  JOURNAL   Structure 5 (11), 1401-1406 (1997)
   PUBMED   9384556
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..430
                     /product="tyrosine-type recombinase/integrase"
                     /EC_number="2.7.7.-"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=48527
     Region          4..419
                     /region_name="FimB"
                     /note="Integrase/recombinase, includes phage integrase
                     [Replication, recombination and repair, Mobilome:
                     prophages, transposons]; COG0582"
                     /db_xref="CDD:440347"
ORIGIN      
        1 mrfdarvaak lpsgehltfe gfpglrlqas tsrkswtyry kspvdgrmrq vklgewpama
       61 faaaiaawek srverdsgte lsalrrkrdk aiarpspady svgqvcrdyl egyvevnrkt
      121 kgavevarif kamlgpiadv saaaitraqa fdlldsyrst pmlaarlrme lgcawhyald
      181 agrlpentpn wwrevlrgrl kskgrkvegk ytgtqkrvls pdelgtlirw mpnfsltvad
      241 altlylwtgt rggeivamer teiteeddgf wwtipkektk glhneratdl rvpligraev
      301 vvrrrldqak gaflfessrg ssmdqtvvqh gvyyhqpyck iapkherlrl pvthwsahdl
      361 rrttrtllat lgcpndiaev vlghvqpgii giynrhtydk errewltqls hrleaiaaty
      421 pakkqiagaa
//
LOCUS       WP_175890222             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175890222
VERSION     WP_175890222.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33669
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..291
                     /region_name="PBP2_CrgA_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08475"
                     /db_xref="CDD:176164"
     Site            order(103,107,146,161,163,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176164"
     Site            order(104..105,109..110,112..113,116,120,122..128,190,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176164"
ORIGIN      
        1 mtdrldgvtt fvqvvesgsf alaaerldmt rsavgkaiar lekrlgarll qrttrsqslt
       61 ddgqayydrc vralaeleaa eadldcgrhe argklrlsvp lafghhcvtp ivldlarnyp
      121 hlridvsitd rfvdlveegi dvavrigtla dstslavrrl gtqygslgaa psylarygmp
      181 ktlddlkhhr tiaysrsgvv qpwdlrapdg stvridiphq lsfddvqaia aagaagfgia
      241 wvpswlldhy vkrgemvvvl drcfvcegdi haiwpktryl prktrcvida laqavppmie
      301 rpdear
//
LOCUS       WP_175890260             318 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cepacia].
ACCESSION   WP_175890260
VERSION     WP_175890260.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..318
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33508
     Region          80..293
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mlepeiaafv aavdawypad aaerapaeqr rlydrfaaew tpaalpagiv qqdavwqapd
       61 graialrryt saqgaprgtv lflhgggfvv gsldshalit aqlaadtgld viavdyrlap
      121 ehrapaaled clavtraard arwpfgpcah pltlagdsag gmlaaavata lrdtgeggvd
      181 gialvypmlg fepqsparet eahapmltld dvhryralyw ngdlsdalgd gnpllrasvp
      241 laaarfdglp pvlaigaehd plrddarvyv eriraaggaa hywmgeglvh gcwralgtsp
      301 qaarmhrtvg gfllapha
//
LOCUS       WP_175890223             509 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Burkholderia cepacia].
ACCESSION   WP_175890223
VERSION     WP_175890223.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..509
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53818
     Region          16..492
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(73,75,79,82,86,119,122..123,132..139,144,147,150,
                     243,247,250,253,255,428,430..431,433..434,437,440..441,
                     443,445..448,457,461,463,477,484..489,491..492)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(159..162,170,185,188,218,235..238,241,259..261,293,
                     393,395,421)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(162,259,290,293)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnanptprtg qdvptvklli dgafvesatk ewrdivnpat qqvlarvpfa tveevdaavq
       61 aahaayatwk ntpiaarmri mlkfqdlvrt nqqriaktlt aeqgktipda egdifrglev
      121 vehacsigsl qlgefaenva ggvdtytlrq plgvcagitp fnfpamiplw mfpmaivcgn
      181 tfvlkpseqd pmstmelvel aleagvpkgv lnvvhggkev vdaicthplv kaisfvgsta
      241 vgthvynlgs ahgkrvqsmm gaknhavvlp danreqtina lvgagfgaag qrcmatsvav
      301 lvgeardwlp dlvakakllk vnagaeagtd vgpvvskaak arilslieag vsegakleld
      361 grdvkvagye sgnfigptif scvktdmsiy theifgpvlv vleadtldda ialvnanpfg
      421 ngvglftqsg aaarkfqsei digqvginip ipvpvpffsf tgsrgsklgd lgpygkqvvq
      481 fytqtktvta rwfdddttag pvnttirlh
//
LOCUS       WP_175890317             548 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Burkholderia cepacia].
ACCESSION   WP_175890317
VERSION     WP_175890317.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..548
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58403
     Region          13..529
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mavatptgal valhhvsfrf ddgvtlfdsl dlsidrtptg ivgrngigks qlaqliagrc
       61 apstgtierh tpvvyvaqqh ddgnaaanpr tvsqvaalda plgalarlad graephdfdl
      121 igdrwdlaer lraaldaagl hdvradtpah alsggqrarv aligallsga gllvldeptn
      181 hldapgrawl raaldgwrgg lvivshdral ladvqrivel tpqgvrsygg nyafyraqrd
      241 adqdaaqaal dnaraergra rrrleqehdt iqrhaaaslr daktanlssg akqsrkgaar
      301 nimgqvrrhq ndfkatlder vqqaaarvea dapvlvslpg tevsarrqlf tlerarlpwg
      361 iagtadaitw sasgpvrial tgpngcgkst llrmlagelt prsgactthv saayldqrla
      421 lldpersive qlglldtpla egelrsrlal lqldaaratq parqlsgger lkaalacalw
      481 rgtpaqllll deptnhldle svraieaala gfpgaivvas hdtaflaald pthtmqwhrd
      541 gwryepva
//
LOCUS       WP_175890336             376 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA cytosine methyltransferase [Burkholderia cepacia].
ACCESSION   WP_175890336
VERSION     WP_175890336.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..376
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=41424
     Region          1..346
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 msrptaidlf sgagglalgl kksgfdlraa veadkwaart yrknlgshll evdihklava
       61 dllefaqlap gecdllaggp pcqgfsvqrr gadedprndl vleflrcveg vkpriflmen
      121 vsglmskrgr pfleavvska relgyvvhqa kleaadygvp qlrkrvilvg emprdgesyf
      181 qfpdpnvsee gyktvreaia dlpspppdga lhaeianhar earlsalnre rlqhippggg
      241 redlpehlql pchinnpshr hvdvygrlew drpsgtitar fdsftrgrfa hpvehrsltl
      301 regarlqtfp ddfhfegnre evakqignav ppllaealgk almrtlpker pkkakssprt
      361 gklgvsdnql slalhd
//
LOCUS       WP_175890362             512 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175890362
VERSION     WP_175890362.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 512)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 512)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 512)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 512)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418077
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..512
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56053
     Region          27..492
                     /region_name="HerA"
                     /note="Archaeal DNA helicase HerA or a related bacterial
                     ATPase, contains HAS-barrel and ATPase domains
                     [Replication, recombination and repair]; COG0433"
                     /db_xref="CDD:440202"
ORIGIN      
        1 meadlfaqgl wnaesnvldy srgvdtyplp lqsvylttad eletlfvaae hvnendvasp
       61 lvalgeyvga ngatcranid klfgqhcail gstgsgksgt vaavihsvle hraldgrqir
      121 privlidphg eyaaafrera vvyraydaaa peaaqanalq lpywlmsgde lrglivgkge
      181 seatsqnniv fkalkharmv aagivqplpa dgvvgdrada lcegktvqdi aafdrdrpik
      241 fsltefrrhv devqgrktak tdnlstsdrk sldslldkld vlvadprlrf lmdeheeasv
      301 esvlaqligv adgqptvrii disglrneva gplaaaisrl lfsykvwqtr aerdrdpvll
      361 vceeahryvp drgeaqyrea qdairriare grkyglglml vsqrpsdves tvlsqcnswv
      421 vlrlsngsdq ehvgrflpds lagltrilss lsrreaifvg eaaalparir irelesnqvp
      481 dsadirfsag waaqplemgd iqrivarwtk ie
//
LOCUS       WP_175890429             174 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia cepacia].
ACCESSION   WP_175890429
VERSION     WP_175890429.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..174
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=17970
     Region          15..161
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 mtntvdiaqq lkqamrgvaa tvtivttggd gaaaapcalt assftsvald pptvlvcinr
       61 rasihasitg rrrfcvnalr schvplalac sttgsdtrfa hdawrtdaat glpylenaqt
      121 sffcdtleqv evgshsilvg rvtrvamsad vnplmyvnga faavrslpsd asgg
//
LOCUS       WP_175890431             700 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia cepacia].
ACCESSION   WP_175890431
VERSION     WP_175890431.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..700
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73451
     Region          38..689
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mheaadqtra vaapprrltr aaaaliarid iftprgayva rsviaaalal gvayllelet
       61 pysaastvll vinpvqgavi gkgvwrvvgt iagmvvafvl mgcfaqqpll filgfafwlg
      121 vcvagmtllr hfrasgtvva gytiglatyg amqhpeltfe hvigrgstva igvlclslvs
      181 mllgtrdvha kldalvtrit advarviaaq rnglaaapad dkrhalfagi ygiddllalg
      241 kaesedlaqr aaavrhgmas lfgalaggmp plpadspgar avaslqprla aawqaaadal
      301 gdgpggatha rallgdarer lrdaldgial gdprdkaall iagerlieqi ddyraaldgl
      361 velqrprpgy rparvrfhrd tgaalrngvr aacaivisga fwlatgwnqg dmmllvvapy
      421 callatagnp aagaqafikg tvlavpaafv cafgilprie gfpllvvala lfwmpgiyat
      481 svpktalagl aylvafntlt gatnpfrpdv alflnqsvaw vlatfltllt frlilpgnla
      541 tdatrlrrti rddtlalvag rrvtaagwqq rqqhriaqlg allagqpaam tqasiealaa
      601 lhvgkellri rrgaardglp drarrcvrag laglarhaaa ppraarharr aahvlaglaa
      661 aqpgntelkw lmaafadvhv llhtyaayft avperardaq
//
LOCUS       WP_175890482             418 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175890482
VERSION     WP_175890482.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..418
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44064
     Region          6..411
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtssqkaplv ivgasyagth laaaarelgf dgpivligde phapyqrppl skglltgktg
       61 mgqlalrspd fyteqcidlr vgqrataldl aarrvrladg ehleygwlal atgarcrplp
      121 vpgaelqgvh qlrtlddala vqrrlgrcss acivgggfig levaaalssa gtrvtvvesq
      181 trllarafpa fmsdyvahah rrrgvslelg rsvrallgrq gsveavqfdd grtldcdlvv
      241 tgigvlpnte ladaagiacd dgilvdalgr tsvrnvlavg dvanmaqppf pgsparmrfe
      301 siqaasdgar aaasvlvsrp qplsavpwfw seqhdlrfqm aglpssgdqv vlrgapasdr
      361 ftvfylhdga maaahsvnrp sdhvlarkli aqrsripaat ladptvdlrs midagqvn
//
LOCUS       WP_175890506             424 aa            linear   BCT 11-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Burkholderia cepacia].
ACCESSION   WP_175890506
VERSION     WP_175890506.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..424
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44530
     Region          1..407
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mknrltlsia igmvlgvaag yachtsiadp gtlktvagyf sivtdiflrl ikmiiaplvf
       61 vtlvsglagm dsgedvgrig lrsvawfvca slvslglglv manalqpgag lnlteaagea
      121 nlglntaaln ardvithafp tslldamarn dilqilvfsv flgialsalk hdprvgivir
      181 sidgmvpvml rltnyvmraa plgvfgaias svalrgldvi ytygkligaf ylgllvlwti
      241 ligvgylflg rrvgallrav repaliafst asseaayprl teqlekfgvd kkvvgftlpl
      301 gyafnldgsm myqafaalfi aqafgvhmpl sqqvfmllil mlsskgmasv prgsvvvvaa
      361 vapmfhlpaa gvamilaidq vldmgrtmtn vignsvatav iakwegaraa qpdsaafdpr
      421 elna
//
LOCUS       WP_175890516             311 aa            linear   BCT 11-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Burkholderia
            cepacia].
ACCESSION   WP_175890516
VERSION     WP_175890516.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..311
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31970
     Region          78..284
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mnkrfraava aslmisagig gtliapqavl aqqaaasasq atsgvaltsa apaassaadr
       61 avpppepats atvenpyglg alwangdfva rfvlgllvvm slgswyvmvt kfieqarang
      121 raksadeqvw naptlaegaa qlddaspfrf iaenaieage hhdtalldsv drntwielni
      181 ersitsvsnr lqdglaflgt vgstapfvgl fgtvwgiyha ltaigiagqa sidkvagpvg
      241 ealimtaigl avavpavlgy nflvrrnksv mervrdfgaq lhtvllaggr raagriatpa
      301 aqspqalavq s
//
LOCUS       WP_175890549             341 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175890549
VERSION     WP_175890549.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12168325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37727
     Region          31..203
                     /region_name="AraC_binding_2"
                     /note="AraC-binding-like domain; pfam14525"
                     /db_xref="CDD:434015"
     Region          247..334
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 maqfsgtgwl ddtacfnhdn lllqsndvde vrarvadvfk phrltptges raldscmhha
       61 rwgnlslnll dygggvsiep gplehffllq iplrgdaeie cgsarfvssp gtaslisptl
      121 plkmrwgdac pqvilriere vmerhaqrhf gddrrapvef epafslsssq gaclaqllpv
      181 lagaiatdah plrhplafep lestllnlll hghpnsarng trhlpvalap fyvrrvedyi
      241 rahldeplti erlaelagvs pstlfagfrh rhgitpmgfv rqlrlqrvre elladespgl
      301 asvtdialkw gfahlgrfai eykrafgesp satlrmrrvr a
//
LOCUS       WP_175890609             425 aa            linear   BCT 11-JAN-2025
DEFINITION  epoxide hydrolase family protein [Burkholderia cepacia].
ACCESSION   WP_175890609
VERSION     WP_175890609.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..425
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46752
     Region          39..143
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          110..>251
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 msstpfspmr rhllatsvaa gvsamlptal haatgasgir pftahipdea vadlrrriaa
       61 trwpgretva desqgvrlar mqallrywgt dydwrkgear lngfpmfite idgldihfih
      121 vrsrhehamp mimthgwpgs ifellkaigp ltdptahgas addafhvvvp slpgfgfsgr
      181 ptqtgwgsdh iarawgelma rlgytrfvsq ggdcgsvish rmamqrvqgl agihvnmpat
      241 vppdiatlla tdapaptsls pkekaayekl atfyrdncgy sammvtrpqt vgyaladsps
      301 gqaawmydki sqwtysggvp ersiprdeil ddislywltn tatsaaqiyw edhsnnfnav
      361 dialpaaitv fpgeiyqapr swaersyhnl iyfnevdkgg hfaaweepel farevragfr
      421 plrrv
//
LOCUS       WP_175890627             352 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175890627
VERSION     WP_175890627.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 352)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 352)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..352
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37444
     Region          29..228
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          260..343
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtynplllid rpnlamsepl sspasdvhdl vselllgmrl sgvqyrriqv arpfglsfgd
       61 apgraqfhfv grgpvllrda ngetmrleag daillphggm halvsdpdap creingfeva
      121 kicdtvasva svasagaspa scattepgag dalifsacme ldlggmqplv gtmpefmhvg
      181 tllarypeir pmldameres csaragfagi larladvvaa fivrgwvecg cgdatgwvqa
      241 lrepklgrai valhrdpgrn wsvaelatea gvsrsvfaer flaatgmtpv ryltelrmrl
      301 aaqwitrdhe tieavayrlg ygslaafsra fkrvvgkppg avradgearv da
//
LOCUS       WP_175890666             466 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Burkholderia cepacia].
ACCESSION   WP_175890666
VERSION     WP_175890666.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..466
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51753
     Region          4..440
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 meifdafhla rlqfaftvsf hivfpaisig masflavlew rylvtgdaay ksmfqfwski
       61 faigfgmgvv sgvvmayefg tnwagfsrva gnitgpllty evltafflea gflgvmlfgw
      121 qrvsprahff atlmvavgtl istfwilasn sfmqtpqgyk ienglvvpvd wfkvvfnpsf
      181 pyrlvhmtia afivagfiva acgawhllkg rrdepvkrsf smalwmllvl apiqivvgda
      241 hglntreyqp akiaaieglw enekggtaln lvglpdmqae ttryaiqvph lgslilthsw
      301 dgeirglkef ppqdrpyspi ifwtfrimag lgmlmlltal lglllrkggr lyetrwfqwf
      361 vvcmgpsgiv allagwitte vgrqpwtvyg vlrtvdsvsp lnaqqvgvsl lvfvvvyflv
      421 fgtgiyymmk lmkrgpaaqa gyielhrhpg lrksalstpl nvteae
//
LOCUS       WP_175890658             310 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175890658
VERSION     WP_175890658.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..310
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33160
     Region          3..309
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mthrvamlvy pgfqvldaag pvsafemady artpyyavri vaaqpglvrs ssgvswhaep
       61 lpdaadldtl lvaggdgvdv amadaatcaf vrrcaargir vasvcsgsll laaagvldgr
      121 latthwgcge rfarafpqvr laldriyvnd gpfwtsagit agidltlali gedrgerlar
      181 avakrlvvyy rrpggqsqfs alieldsaqg rfkplldhir rnlgarlrvs dlaeqacmsp
      241 rqfarafqte tgltpakave klrveaaraa lesgasslqr vanecgfgdt enmrrsfhrw
      301 lgvapsalrs
//
LOCUS       WP_175890688             432 aa            linear   BCT 11-JAN-2025
DEFINITION  NRAMP family divalent metal transporter [Burkholderia cepacia].
ACCESSION   WP_175890688
VERSION     WP_175890688.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..432
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45435
     Region          22..432
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 msapdegapp aanaapagat akpwykrlgp gllagasdad psniavyaqa gsqfgfnmlw
       61 mivvalpmmv avqlaaafvg rrnreglvag irthfsdrla ktlivmvviv nvanvgadla
      121 amgdatalva ggrsywyapl ygiaslvlqv tlsyeryarw lkwmtlglia yvlelgfvhv
      181 dwrgvlhala lpqialthay attavavlgt tlspylfvwq aaleveettt eqqhatpsar
      241 geterrvtfd twagmivtna vsfcimviga avffahgrhd igttaqaaea lrpiageaaf
      301 vvfafgivgc gllaipafag saaygcaeaw rfreglnepv rrapafyavl alcvivgiai
      361 cigpidpika lywsavlngi aavpmlvlvm llarqreaag qpgsgtvsmv fgwlavglma
      421 asvvtmivdl lt
//
LOCUS       WP_175890754             215 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cepacia].
ACCESSION   WP_175890754
VERSION     WP_175890754.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..215
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22941
     Region          3..215
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtylpillqi avvylvaait pgpnffmisq lslagrrslg aasalgvgta svvwaslaml
       61 glaavlhqve wlyeairigg avylvyfgfk llrsgvrrda apadapdera plaaphardy
      121 lrayrsglft cltnpkscaf wtsvfaamlp ahvplwfnga vlvtigvlsa gwyscvaylf
      181 aspraqrgyr rvrrpldalc gvalvglgak laaer
//
LOCUS       WP_175890756             369 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175890756
VERSION     WP_175890756.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..369
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38947
     Region          1..367
                     /region_name="LhgO"
                     /note="L-2-hydroxyglutarate oxidase LhgO [Carbohydrate
                     transport and metabolism]; COG0579"
                     /db_xref="CDD:440344"
ORIGIN      
        1 meqmdcvvig agvvglaiar elaargretl vleaadaigt gtssrnsevi haglyyprgs
       61 lkatscvhgr dllyefceth hvphrrtgkl lvatsvaqvk qlkaiaaraa engvldlmpl
      121 traeaqalep alecvealfs pstgivdshq lmlallgdae rdgavcalks pvesidvlrg
      181 grfvvrtggd apaeieaacv insaglgaqa larrtrgldp rwvpplylar gnyfslsgra
      241 pfshliypmp draglgvhlt ldlggqarfg pdvewcdslr yevdparata fyasirafwp
      301 glpddalqpa yagirpklag pgeppadfiv qgaaqhgvrg lvnlfgiesp gltaslalaq
      361 rvgdmaayr
//
LOCUS       WP_175890786             402 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175890786
VERSION     WP_175890786.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..402
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=42218
     Region          4..355
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 msqkilivga gfagvwgalg aarvldaagv tssdveitlv spkpelqirp rlyesgpqhm
       61 aapllpllda vgvkflegsv eeidvrektv gvacadgekr qiaydrlllt sgsklsrppv
      121 pglaehafsv dciedavald ahfatlaklp esparntvav vgcgftgiev atelpkrlre
      181 wfgpdaksrv vvigaqddig pdlgpnprpy vaeafdslgv eavlgsrvvs iaadgvrtas
      241 gthieamtvi waggmraspl aaqvsshlda lgrvavtadl rvadaphvfv agdvararcd
      301 ddghdalmsc qhaivmgqfg ghnvaadlig vptltyrqpf yatcvdlgew gavysegwdr
      361 qiklthaegk arkqmintqw iyppapnrtd alaagnplas fg
//
LOCUS       WP_175890798             370 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia cepacia].
ACCESSION   WP_175890798
VERSION     WP_175890798.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..370
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39167
     Region          4..334
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,233,300,320,322..324)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,181,184,186,233,240,300,320,
                     322..323)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,181,184,186,323)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            186
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mssllshydl rglplpnrvv mgpmtrsrap srgqptelma eyyaqrasag livteatnvs
       61 pasasfeltp glvtdeqaag wkqvtdavha nggrtfaqlw hggrvssltl lggaaplsps
      121 gvnddleqlq vwaqlqngyy tkihatpsra mttdevadtv defrdaavra maagfdgvei
      181 haangylphq flsstlnrrd dryggsvanr arfleeivda vgavmplsrv gvrispyaky
      241 nnvrdadpdt tyayvgrmld eagvayvhaa dtngwsgepd lprivanark hfggtlivng
      301 giapdaanal idagdadlva farayianpd lverlaanap laapkavgwy ggdragyvdy
      361 arhdaagvsa
//
LOCUS       WP_175890807             119 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF485 domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175890807
VERSION     WP_175890807.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..119
                     /product="DUF485 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=12784
     Region          27..114
                     /region_name="YjcH"
                     /note="Uncharacterized membrane protein, DUF485 family
                     [Function unknown]; COG3162"
                     /db_xref="CDD:442396"
ORIGIN      
        1 mnhplpatag tapepaapsy athpllrdar frehvrsrrl fawsltfvml alyfafiltl
       61 afsptllgap ivpgrptpwg ipvgfgmfva tfalvalyvf ranavhdtvv aalrhgdas
//
LOCUS       WP_175890823             159 aa            linear   BCT 11-JAN-2025
DEFINITION  SMI1/KNR4 family protein [Burkholderia cepacia].
ACCESSION   WP_175890823
VERSION     WP_175890823.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..159
                     /product="SMI1/KNR4 family protein"
                     /GO_process="GO:0042546 - cell wall biogenesis [Evidence
                     IEA]"
                     /calculated_mol_wt=17742
     Region          17..152
                     /region_name="SUKH_6"
                     /note="SMI1-KNR4 cell-wall; pfam14568"
                     /db_xref="CDD:434043"
ORIGIN      
        1 mkilhesflg rpstasissv erayrikfpm eyllfletcn gvvpedfcve idgkqrlvvr
       61 flailddpas egeagwydvs vvlaqigarl aeekdrdeig lklipfavlf ggdylcidfr
      121 ekfanpsvay wdhsspdfrp itsqvapsfg efckrlgit
//
LOCUS       WP_175890915             254 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175890915
VERSION     WP_175890915.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..254
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26804
     Region          1..254
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mtqgahivan gvtlrygsrs vlngvdlsva pgelvallgp sgcgkssllr aiagltrtas
       61 gtirvdgepv dgprpevala fqdpcllpwl tvernvgfgl tftrqphltr adrkervtna
      121 laavgldhar halpsqlsgg maqraalarc larapralll depfgaldev tradmqqlli
      181 aavrntgasa llvthdidea llvadrivll gkrgtlvgrw tvelpqprht qvrslgelri
      241 silqalqnli saaa
//
LOCUS       WP_175890957             331 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175890957
VERSION     WP_175890957.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..331
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35070
     Region          6..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..302
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 medidlnlvt aldvllsegs vtgaarrlgl stsamsrtlt rlrvstgdql lvragrklvp
       61 tphaaalrdr vhaiatdara vlrpatadvd lathastfti raaasfmeml sgpvvaalge
      121 iapqvrirfv pkpdrdpqal rdgavdleig krgddapelh trmlfhdwhv avaraahplf
      181 asgritpary aacrhviasq lgdfggpadd paggagqgdt vrvvvpgypd amrvaastdl
      241 ialvprsslg nafspgltda lglrsfeipv rlpgilvsal whprmhgdpv hrrlrdavia
      301 vcqraypdsr tphtshtsrp parrtgpraa g
//
LOCUS       WP_175890961             323 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175890961
VERSION     WP_175890961.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..323
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35002
     Region          6..321
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpaaprsilv lafpraqlld vsgplqvfas vnelalergq papyaprvva aeagpvetss
       61 glvvmaeslc saarhpdtli vaggkgvhaa srdarlvrwv rqqaartrrv asvctgafll
      121 aeaglldgrr avthwarcde faarypnvrv esdpifireg alwtsagvta gidlalalve
      181 edlgratald varelvvflk rpggqaqfst mlsmqrtddr fgelhawmae hltadlsvpa
      241 laerasmser sfvrhyragt grtparaveq lrveaaqrll getawpvkri aarcgfgsee
      301 tlrrcfvrvl gvspqgyrer fvr
//
LOCUS       WP_175890993             260 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Burkholderia cepacia].
ACCESSION   WP_175890993
VERSION     WP_175890993.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..260
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28395
     Region          12..193
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(15,17,98)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(42,97..98)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            96..98
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mskqhassth lvlipsynpg tkvdttvrna raqwnpvwvv vdgstdgsae rlqamaerdp
       61 glrvivlpen rgkgaavlag ldaaaasgft hvltmdsdgq hpadlipafm aasqaapdam
      121 vlgvpkfdas apqlrvqgrr lsnawadlet lwagigdsly gfrvypvapl aaimrrqpwm
      181 rgfdfdpeaa vrlcwagvrp iridapvryf grheggvshf hygrdnalla wmhlrlftgf
      241 vtrlpmlvar rlarrhdqta
//
LOCUS       WP_175891020             454 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175891020
VERSION     WP_175891020.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..454
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48143
     Region          22..426
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(35..36,39..40,43,83,141..142,144..146,149,169,
                     172..173,176,258,261..262,265..267,270,297,301,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 myptdtvqsp saarpladrq lrriviasva gnamewydff vygtaaalvf ghvffppgas
       61 plagslaafa afalgfvarp lggivfghvg drygrkaslv wtllimgast faigllptya
      121 qvglwapaal vvlrllqgia sggewgggvl misenappeq rgyyaawsql gvgggfvlss
      181 aaflaaqalp ddmfrtwgwr lpflasiaif aigiyirrhl pesrdfeqag rrgahthmpi
      241 vecirrhpke illamglrva enggayifla fslvygkyvg ipngvmltgv miamivemga
      301 mlawgrlsdr igrkpvylig alslvacafp ffwlldtrat plvwlaltvg tavshgamig
      361 tlpalvgelf stevrysgva lghevasifa ggmspliata llaryhaswp vslflvalgl
      421 vtvatlcmmr etrivstapa apavpatdtr gdta
//
LOCUS       WP_175891039             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175891039
VERSION     WP_175891039.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47193
     Region          23..422
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,154,
                     157..158,161,256,259..260,263..265,268,295,299,349..350,
                     354,358,374,377..378,381..382,385)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnatdtldpa saeeqrimsk marrllpilv vmfliafidr qnvgfaklqm vhslgmteaa
       61 fglasslffi gyllfevpst lalhrygarv wlarimltwg litvlmgftt smpafcalrf
      121 vlgiaeagfy pgviyyltlw fpqsyrakvl giftlgsala nmlgslvggv llslngvwgl
      181 agwqwvfvat gipavivaiv vfrvlpasvr darflddrek qvveaalere kparaehgqp
      241 wkalldprvm lfaatymlms tslygvtywl ptlvksfgvs sttngflsml pwalavlllv
      301 wlpgklrrak silrtiaiva algalgflls lvlpstplrf ialvlggaci pllypcfwsm
      361 ppryftgara aasvaainsi gnlggffsqn lmpfagkvtg tafgpmivpi vclallgiga
      421 lvawtrserg mvavra
//
LOCUS       WP_175891099             397 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Burkholderia
            cepacia].
ACCESSION   WP_175891099
VERSION     WP_175891099.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..397
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=42484
     Region          1..386
                     /region_name="AspB"
                     /note="Aspartate/methionine/tyrosine aminotransferase
                     [Amino acid transport and metabolism]; COG0436"
                     /db_xref="CDD:440205"
ORIGIN      
        1 mnysklvdrl qgkrttawdi hyaaqqavaa gepaiilsvg dpdfatpdvi veravsalrg
       61 gdthysevrg raelraaiar ehaavsgqav gpehvivtag aqnalfamam clceagdevi
      121 vpepmyltye asvrasgatl vpvpvdasrg fhldfdalea avtprtkaif fatpcnptgv
      181 vmpradleri arlacerdlw vvsdevyaal tferemvsia slpgmaertv tlgslsksha
      241 mpgwrvgwai gpteliehae rlalcmlygl pgfiqqaavt aldnraaiva dmrelyrrrr
      301 dlayarlrdv pglrcllpea gmfmmvdvrg tgldahaftw glfrakqval ldasafgdta
      361 sgfvrfgfvv ddarlidace riaafvaslg ggsgass
//
LOCUS       WP_175891201             318 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Burkholderia cepacia].
ACCESSION   WP_175891201
VERSION     WP_175891201.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..318
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33077
     Region          3..296
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(36..37,40,91,105,107,136,168,256,259,295)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(227,232,247,256..258,261,283,287)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 maeivvagel laefvaaerg qgfdspglfa gpfpsgapai fadqaarlga rvayagcvgr
       61 dafgdaivar lerdgvdvar irrvarptgt afvayrddgs rsfvyslsts aaacveasdv
      121 dtamfngcry fhvmgsslts esaiaavqrg vieaartgak vsfdpnvrpe mlsfrpmraa
      181 letmlaachl fmpseadlpf fcgpqpaera iagllathpl lervvlkrga qgsvafdran
      241 rveapafqvd eidptgagdc fggtivasfv agvpidaalr ranaagaiav trrgpmegns
      301 saaeidrflt ergiacpa
//
LOCUS       WP_175891239             299 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175891239
VERSION     WP_175891239.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..299
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32721
     Region          112..271
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mllnvnpfhr dndrfnvsfk algelietvg tphfvprltq llnevvpldv ahversrvdg
       61 smptgyrcew igssgigaas advsdvmtly yerfldsdpl faglrgktgt mlvvrdiaai
      121 ppgefrqrlf ddvqighecv largtrysqh sialergrdr ppftlaemnr frsisdvlfp
      181 llelhastsa arriahptpe vhplaqfdar iaadgvklsk reyetckhll sgktvpetae
      241 ilgvrvasae syvkrafakl gvrtkrelaa wgsattafps sgphdgaapp alsrrpdpa
//
LOCUS       WP_175891242             574 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia cepacia].
ACCESSION   WP_175891242
VERSION     WP_175891242.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..574
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62675
     Region          7..560
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mqmqpthaat tpadfvltha nvytvdphkp waqavavrdg rivyvgdtaa vqafvgaqtk
       61 vvdaagrlvl pgfveshwhf ettafafqaf vnyedpqkvl galrayvesh pdepaitgmg
      121 wvqatippal lrketldaic adrpvcllst dfhtmwvnsk aleiagidas tppvqegasw
      181 fekdaatgep tglivdgaay sllmqrisaa gllptgidly lksippwqkk lcaagvttvf
      241 dagffdasgd qsllyetlqt meragdlklr vvgsvavige iddpvgtlvr yreqydsplv
      301 karalklfld gteanhtayl lepyadrpdt cgaptmpadt fnrylveadr ananvmvhcv
      361 gdaavrmald gfdavnrtnp prdrrhvith aflthpddip rfrragvman tqlqwgvvda
      421 yteqlrdhyg herwssmykf rtfldegvtv sigmdglacq crcqhkpleh iesghtrqla
      481 gepdapvfpd iaerlsipql iaaytihgay qlgmehevgs ltpgkradlv vlendlfevg
      541 qydigridvg ltmmggrith vgddfgartg mqas
//
LOCUS       WP_175891293             573 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent helicase [Burkholderia cepacia].
ACCESSION   WP_175891293
VERSION     WP_175891293.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..573
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63275
     Region          1..564
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mldelnpqqr evallrrhcl aiacpgagkt kmsatkaafl lkdptavvga vtfskdaave
       61 lrerilalap pdakrrliag tfhslaykql qrpgrgrpdi asegdrlgml grvlaelgfd
      121 wkveeavpiv eriktnfgra degsaeatly aayqdalern gkidfqdmlr lavertqsed
      181 ikpyrftdll vdefqdtdpl qfrwvelhar agthvtvvgd ddqsiygfra algfrgmesf
      241 astfaaqrvv lgsnyrcrae ilaaadrviq nnvdrmpkvl hadrgaggvv tarrfddeyg
      301 davaavemlq prlaagasca ilartnrild piesvcrshg vpyyrasggs vlnkpqaalm
      361 cnllqvvegh kqngidavlg ymgmssydlg alhkrmgaaf vqmqkqelvg lglreetata
      421 yrafmkrlge wqalcgrsfh slalegvyew mmtyakgdva iraiqciydv vsrlngsfte
      481 rieflkrdnn kpgtgvlvlt tmhsskgley dhvwisrsee gvvpdekspe seerrlfyva
      541 mtrardslti ssikknpvsr fviesgieqn saa
//
LOCUS       WP_175891247             336 aa            linear   BCT 11-JAN-2025
DEFINITION  sodium:calcium antiporter [Burkholderia cepacia].
ACCESSION   WP_175891247
VERSION     WP_175891247.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schnetkamp,P.P.
  TITLE     The SLC24 gene family of Na/Ca(2)-K exchangers: from sight and
            smell to memory consolidation and skin pigmentation
  JOURNAL   Mol Aspects Med 34 (2-3), 455-464 (2013)
   PUBMED   23506883
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Besserer,G.M., Nicoll,D.A., Abramson,J. and Philipson,K.D.
  TITLE     Characterization and purification of a Na+/Ca2+ exchanger from an
            archaebacterium
  JOURNAL   J Biol Chem 287 (11), 8652-8659 (2012)
   PUBMED   22287543
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..336
                     /product="sodium:calcium antiporter"
                     /GO_function="GO:0008273 - calcium, potassium:sodium
                     antiporter activity [Evidence IEA]"
                     /GO_process="GO:0006874 - intracellular calcium ion
                     homeostasis [Evidence IEA]"
                     /calculated_mol_wt=35286
     Region          19..332
                     /region_name="ECM27"
                     /note="Ca2+/Na+ antiporter [Inorganic ion transport and
                     metabolism]; COG0530"
                     /db_xref="CDD:440296"
ORIGIN      
        1 mtfmfvelav mlivilvaae vftnalehlg erlkisegvt gslfaavgta lpetmvplla
       61 laggtanpav neeigvgail gaplmlatlt tflmtlavir srgprgtiap ertgfvrdmn
      121 yflaafslat aamfvphhns avrallaaml vgiyvmyvvm tfrasnqlvd aghgteaphk
      181 mflsrvglpt nlatialqll igvallvgga kgfihgvegv shvlgvsall lsliivpiat
      241 elpekvnsvl wirrgkdtla fgnitgamvf qgtllpaigi mltpweprle vltgvivtla
      301 aaawlrvnar trglaiwall angagyaayl fltlar
//
LOCUS       WP_175891367             482 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia cepacia].
ACCESSION   WP_175891367
VERSION     WP_175891367.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..482
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50526
     Region          25..478
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mshpaspaqa lpaqhavpla gglrrnylsl peliaqsigl vgvsggigvl ipavfatagn
       61 gtwlaylfai vallfaswsi svfardsasp galyayvsag igpvwgaicg wslliayava
      121 aagilqgtin tflvlgretg llggatplga vlgltvvtaf aawyiafrdi rlstrftlfv
      181 elatllliav vvigtiafgg hpvdraqltl egvkptqlql gmvlaffsft gfesatvlga
      241 eardpfraip ravlisvvgp ailfvigayg mvsafhgqtp pldrvdgpla vlahrlgagw
      301 vgvlidagva lsffaaffss inaaarivyt fgrqgvlhas tghahernat phvavaliav
      361 lalvtalvft argtalldsy gylssiatyg wllayvlvai gaplylrrqr rlrarhvais
      421 viavvllaip lagsvypvpe gvyawlpyvf vallaiglgw flvlrvrfpe rlreleaell
      481 tk
//
LOCUS       WP_175891372             710 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia cepacia].
ACCESSION   WP_175891372
VERSION     WP_175891372.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..710
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77288
     Region          9..699
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mtypslrdwl fsgktfaasm lalylglyfq lprpywamas vyivsnpfvg atrskalyra
       61 lgtalgaaaa iffvppfvet pllfaiivaa wcgtllylai sdrtarsyvf mlagytmplv
      121 alptvtdpst vfdvaiarte eivlgivcas vvgsaifpnr laptliertd awfkdaafyg
      181 retlsghiag kalsacrqrl aatitglefl lsqlsydhah prilaraqal agrmqlflpl
      241 mssladplia lmrdlhirpa glddlladaa kwfdaplpav kagndgdmtd dpvaerlrer
      301 iaalqpadda laswdgalls nalwrlrqvi diwqdcrslr alignesgvw qpryrhwrlg
      361 gterffdrgm mlfstltvaa aivfaswlwi asgwhdgaaa vtlvavscsf faaldepapl
      421 vfkfflatta svvfaglylf vvlphvhdfa mlvvmfagpf iligtllprp qfnmvtmlva
      481 vntatfisiq gaydadffvf lnsnlagvag llfayvwtra trpfgaelav rrllrsgwed
      541 vvrsastqpl ddqrnhasrm ldrvtqllpr lgasddhrhp siesfrdlri alnaldlrrs
      601 rrrlsgdvpd aidrvlagvt dhyarcaaan arqpappall atiddalqrv agrnlpgatp
      661 aehgaapaap atpathrrlr dtlhtlvslr lslypaaagq ppqapdgara
//
LOCUS       WP_175891392             410 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175891392
VERSION     WP_175891392.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..410
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42829
     Region          12..394
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(22..23,26..27,30,65,112..113,115..117,120,145,
                     148..149,152,224,227..228,231..233,236,266,270,320..321,
                     325,329,345,348..349,352..353,356)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mtpiehevrq rwlpvlaggl imgaalgirh vqglflapvs ldhgwsreaf glalalqnli
       61 wgvaqpftgm vadrfgslrv ivagmllyaa glvtmahaat tgmftvgagl vigialsgsa
      121 fasiygalsr lfppdrrgwa lgvagaiggl gqfcmvpvaq eliggigwrh afvalalvta
      181 vlaplavllr drpaqvagaa agpdqsigea vreafahrgf wllnagffac gfqlafiath
      241 lpaylldhgl parhasvala lialtnvagt yacghlggll rrkyvlsvly lvraltmavf
      301 vaaplspasv yvfaavmgft wlgtvpltng visqvfgvry iatlfgfvff ghqlgsffgv
      361 wlgalvydat hsymplwigs ialgvlaall hlpindarva rpaagnaawa
//
LOCUS       WP_175891408             468 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Burkholderia cepacia].
ACCESSION   WP_175891408
VERSION     WP_175891408.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..468
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=50389
     Region          <14..267
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mnffgigrgh rssralvgdi aeqagklgie icdvsghvee vaarvarqae vchtlresaa
       61 vtlrgnhria eaaqqvravs anasnavrqs qqtieaslad ihglvegvts ignqmgalrd
      121 aldhvravse eisviarqth llalnaaiea aragdsgrsf avvaaevknl saktgqataq
      181 iettlarlae qtehliaegt dnaarahrvr egtrtigevv hatghaitel ageaeqiasl
      241 tddietqchr ldeqvgemas gvedssdnfs qakdrlgnll svsetlielt aatgiespdt
      301 rlidtarhta aaiskrfeea vgrgeialda lfdanyvpip gtdpqqfmtr ftdftdrvlp
      361 aiqepvlgid arivycasfd rqcylpthnr kfslpqrada awnaancrnr riytdrtart
      421 svshtkpfll qtyrrdmgng nfalmkdvsa pivvggrqwg vlrigysv
//
LOCUS       WP_175891468             207 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ImmA/IrrE family metallo-endopeptidase
            [Burkholderia].
ACCESSION   WP_175891468
VERSION     WP_175891468.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..207
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=22941
     Region          108..186
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mttlgtatqg artpsgmkva ptsyeklera akdlrpllpt lsrtgrssma idcvrvleqt
       61 lpragynymi eavddlkdca aftiperniv vlredvyegl fddspfsrst vihelahivl
      121 rhhvtlhrga ilgqhqfced sewqakalta avmmsieacr earsahelaq acgtsdqaag
      181 yrienlvkrr viepkrqqgl fdfpfgk
//
LOCUS       WP_175891464             306 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cepacia].
ACCESSION   WP_175891464
VERSION     WP_175891464.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..306
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32017
     Region          50..287
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
ORIGIN      
        1 mtatttpaaa patagpapss ppaptmgrlr tadglelasy rwpagdgteq pratialvhg
       61 laehagryaa lagrlnaagi evlavdlrgh gqspgkrawv erfdgylnda dalvaeaarg
      121 nsplflmghs mggavaalya ierapargha laglvlsspa lapgrdvprw mlavsrvisr
      181 iwptfpairi daallsrdpa ivaanradpl vhhgavpart gaeildamar iesgrgalrv
      241 pvlvyhgted kltepdgsra fgahvgspdr tltlyeggfh etmndlerdr vidaliawih
      301 arvpar
//
LOCUS       WP_175891771             141 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator, partial [Burkholderia cepacia].
ACCESSION   WP_175891771
VERSION     WP_175891771.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         <1..>141
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
     Region          <1..141
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 valgvgalla ampplfvalk lagaaylili gsrqwreggr paaganaaap geavpaavpv
       61 srlrlfresi lvagsnpktm iflsafmpqf idhqcslplq faqmyltial lvlvvhtiys
      121 tgvrhlhgrl ragravaamr r
//
LOCUS       WP_175891844             266 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175891844
VERSION     WP_175891844.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..266
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29059
     Region          78..258
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          202..256
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mdrlfseiam hqalgraidh lgqprfwrfl vlllnemvpf dnalataigp dgvplvleey
       61 dtggtdaasp vplylngvyl ldpflqaahd gladgcyrle evapdlfrqs eyflsyfrda
      121 vgddeiqilv rpsadmllsl slgagtrfdv eplgkltaam pwvlaairqh wrlvgdaara
      181 tpdadlgarv eqalarfgag vltdremsia rmvlrgnssk aiaerlaisp etvkvhrrhl
      241 yaklgissqp elfsrfiqal gedatg
//
LOCUS       WP_175891843             276 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175891843
VERSION     WP_175891843.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..276
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=30243
     Region          11..247
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mnpsspaerk gvalyarias llrgrihqge wkrgdqlppi pelcafyrag titvrqalae
       61 lsaeglvssa rgrgtfvtad vlsppdnpal raaindplql apgqslrvll reavtalpaa
      121 lqtgqpmraa ymrirtlqlh dgapygvmds yiaretydrf pkgsdarrkv gylvrqynrl
      181 plakarqeit aayadqetad llasdgadfs madmlirmrr wwtdgdgciv haglylyrad
      241 rfvldithdl dgndrsadli pspragtrkg trkpaa
//
LOCUS       WP_175891853             472 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia cepacia].
ACCESSION   WP_175891853
VERSION     WP_175891853.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..472
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=50900
     Region          83..470
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mtarpafpsp dasgttapra psrllrraaf vigaavlgyg afaiafpaqv paaigtvvad
       61 wtganphpvv lqrpaaqpls avaqlgralf adpslsasgk qscaschspd haygppnald
      121 vqpgglamtq qgyrpppslm ylyrqpnfsi gpdagendaa psvaqqaasa agvvkaqkva
      181 gtsaapqlvp qggmfwdgra dtlqqqafgp llnpvemana svddvarkla qsshraqfek
      241 lfgarvfdsp qlavseamfa iaryqvedps fhpynskydr wlegrarlsq aelrglrlfn
      301 dpdkancagc hlskpgkdgl ppmftdyqye algaprnrql aqnrnpafyd lgvcgpfrdd
      361 lkdqtqycgm fltptlrnsa trhvffhngv fhtldqvmtf ynersispqk fysrgadgkv
      421 deyddippky ranvdvtdap fdrkpgdkpa mtaqdikdie aflgtlndep ar
//
LOCUS       WP_175891857             862 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia cepacia].
ACCESSION   WP_175891857
VERSION     WP_175891857.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 862)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..862
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=93230
     Region          59..712
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mhpfqpsstr vnrrnvssvr dfcarwvara qpvaaaavar akplaavawh hlrhptrrgv
       61 llagaavpal fvayvvvlip ftpgigdirk arvdqpaqvl sadgkllaef kpsnrewvpl
      121 rqisphmvda liatedhrfy ehhgldwkrt asaalhtfsg srqggstitq qlarnlypde
      181 igraptltrk vkeaitalki eavyskdqil etylntvpfl ynaygvemaa rtyfdksade
      241 ldvldsatlv gmlkgnsyyn pvlnperalq rrntvlgqmv kygklspaqf aqlqrrplri
      301 dferqkeppg paphfaqqlr kwliawadrn dyniysdgli vrttidsrlq qmatqaltlq
      361 gnqlqgiann awsgrdgcgt dnevfrtfmr espeykaaqd agkddaaamk llaadrgfmr
      421 alcktktdvq agflaidprn gqirawvgsr dftsepfdhv aqarrqpgst fkpfvygvaf
      481 angmkpddtf idqpveiplk ggeiwrpndd vpptgkpmtl rdavalsrnr itaqvmekvg
      541 pasvarlard mgvrespler vpslalgtsp vtlkemvasy atiangglyv epqmvtrien
      601 rqgdvlaeya papperalda etdktllsvm rdvvtrgtgg sirtrfgirg dvagktgttq
      661 dnadgwfilm qpglvagawv gfddgrvtlr sdywgqgahs alpivgdffq raqrarivdt
      721 kakfdtepsp gwfaslrerv tdlfdtwfpp kpekapapvr tqrverapea dtgtesaasa
      781 asapeaasgg iveewvpase vaasaaalsa gasqpqpaqp pagastpggg ssglgtapaa
      841 apsaapaqpp vpaapdasga sq
//
LOCUS       WP_175891877             744 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia cepacia].
ACCESSION   WP_175891877
VERSION     WP_175891877.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..744
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=78441
     Region          75..>209
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          215..737
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msrglieagk vagqaagagv srrsflklgm slgaaagggl llgfslpaag ddarrsvigg
       61 dgdetaragv fapnafvqid ragkvtlvmp kvemgqgvyt alpmliaeel evplssvtld
      121 happneklfl dpllggqltg gstsiryawe plrragatar tllvaaaakq wnvdpascra
      181 vngevqhpps grrtsygqla daaaklpvpk dvalkkpadf kligtpakrl dspekvdgta
      241 qfgldvrlpg mlyavivnsp vfggtvasid dtaakkipgv rqvvradnav avvgdhtwaa
      301 krgasalvvk wnegagakvs tkdivadlaq aaangkgava rkdgdvgkgf adaktridav
      361 yeqpllahat mepvnctvhv radgceiwvg tqvptravdt vqqltsfppe kivvhnhllg
      421 ggfgrrletd migqavkiak qvnapvkviw treediqhdm yrpyyydris agldangkpi
      481 awqhrivgss ilarfappaf qhgvdpdave vatdlpydlp nqlidyvrqe prhvptafwr
      541 gvgptrstfv vesfidelaa qtktdpvqyr rallgktpra lnvldvatka agwgpslptg
      601 qgrgvsvmha fgsffsivid vavdngevqv krvvcavdcg msvnpntiea qvqggiifgi
      661 tgalygeiti edgrvvqsnf tdyrmlrine tppievhlvk sgeapggige pgtaataaal
      721 snaifaatgk rlrklpvgdq lkta
//
LOCUS       WP_175891907             495 aa            linear   BCT 11-JAN-2025
DEFINITION  sialidase family protein [Burkholderia cepacia].
ACCESSION   WP_175891907
VERSION     WP_175891907.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 495)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..495
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52404
     Region          158..442
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Region          191..252
                     /region_name="Sialidase propeller 2"
                     /note="Sialidase propeller 2 [structural motif]"
                     /db_xref="CDD:271234"
     Region          257..310
                     /region_name="Sialidase propeller 3"
                     /note="Sialidase propeller 3 [structural motif]"
                     /db_xref="CDD:271234"
     Region          325..378
                     /region_name="Sialidase propeller 4"
                     /note="Sialidase propeller 4 [structural motif]"
                     /db_xref="CDD:271234"
     Region          389..442
                     /region_name="Sialidase propeller 5"
                     /note="Sialidase propeller 5 [structural motif]"
                     /db_xref="CDD:271234"
ORIGIN      
        1 mrrstvshpl vtglprltrl trlsaaaava avamaaaaaa hadpvavsgp spfaactigg
       61 pgtnyvnaev epwlsvnpan pmnmigvwqq drwsnggahg lvagytfdag atwartpqpf
      121 sacapgglky erasdpwvsf gpdgtaysvs isfnqsnnan avaasvstdg gqtwsspavl
      181 iandepttqf fndkesvtan pvkagtayav wdrlelpngn pyanlhthay rgptlfsktt
      241 dggktwstpk vivnvpsrqq tignqivvdp ksgtlydffd liqppfskaa gkvafikstd
      301 dgatwtkpqv iagletvgvt dpntgepvrt gdiipepaid pasgqlyvvw qdsrfnggty
      361 deiavstskd ggatwstpqq lntptgrpaf npsvrvdntg avmvtyydfr dlqagntttl
      421 ptgfwrkish dggttfader rvggpfdlkl apnaegffig dyqgldvmps ssfhpffvqt
      481 nagnltnrtd vffap
//
LOCUS       WP_175891918             278 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175891918
VERSION     WP_175891918.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..278
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30647
     Region          95..248
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mspsgsafrp ppqsghreag gkfesigair rrvsmrykir stnlnirfrc iergrcgwya
       61 aghslmgqqe dflkraaldn ervltergkn tvnkimasai eifvvegygg ltmrkvaaka
      121 glalsnlqhy fptredifea ilsatmeaya ntydsvsadt sltaegrlek vvrllledgk
      181 qprtqslfvn fwalaqtqef arkmleegyg fqrrviagfi eavnpalsha alarraalvt
      241 aqieglivli pqrnrfpsdi kgieddavma vlalakap
//
LOCUS       WP_175891940             443 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia cepacia].
ACCESSION   WP_175891940
VERSION     WP_175891940.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..443
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45495
     Region          1..393
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdlaltdeqa mirdaaadvl aersasadvr raleqsagrd dalwaalage lgwnalalpe
       61 aagglglgav eqtvlmeqlg rriacvpyfs taclaatalg gcdtslatgw lakiaegacs
      121 atlalpfdwl fgepggarvg rpygrpgana fgasfgdsfd epasarplpf iaeetaagfa
      181 lsgvaaqvld garadlllvp arianegqsv glfaidmttg aagvavtpld tldstrplar
      241 ialddvrvsr daliagrdaa qvleraawfa alalaaeqlg gaqqcldltl dytsqrvqfg
      301 raiasfqavk hrcaqmmvli esarsavlga ahawdaeags vgpgnalrad iaaaksaand
      361 ayafcaqeai qlhggvgftw eydphlyfkr aqasgaqfgs tpqllewiac haieggasqr
      421 geafeppaaa asrpsaarag alq
//
LOCUS       WP_175891953             397 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Burkholderia cepacia].
ACCESSION   WP_175891953
VERSION     WP_175891953.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..397
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44483
     Region          48..393
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mtspvpsdta lrplpidalt vpaaldgrtg tnrstgthpq iaatndldav rawlarfvdt
       61 pttfqnyrke aerlllwali acgkplsslt hedlivyrqf llapapaelw canggrkhpr
      121 ddprwrpfyg plsaasqrqa lvilnvmfsw lvqagylagn plalsrqrqr rpaprvtrhl
      181 gqplwqsvke aiaamprdda rasfhadrar wlftllylgg lriteaadtt mgqffcrrda
      241 dgrdrwwldv tgkggrqrlv patdemmael sryrrahglp alpsdgestp lvlpvgqahk
      301 pltraalhri vkqvfrhaad rlrangeage qqarvleqas ahwlrhsags hmadgrvdlr
      361 lvrdnlghvs ltttsqylha dddwrhrete ekhrigw
//
LOCUS       WP_175891991             551 aa            linear   BCT 11-JAN-2025
DEFINITION  S8 family peptidase [Burkholderia cepacia].
ACCESSION   WP_175891991
VERSION     WP_175891991.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..551
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55117
     Region          239..518
                     /region_name="Peptidases_S8_13"
                     /note="Peptidase S8 family domain, uncharacterized
                     subfamily 13; cd07496"
                     /db_xref="CDD:173820"
     Site            order(246,314,318,385..387,413,415..416,486)
                     /site_type="active"
                     /db_xref="CDD:173820"
     Site            order(246,314,486)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173820"
ORIGIN      
        1 mrtkrfnlal arsaharmla gmlsaaallp lagcgggggg dgsnpsssna apapaptptp
       61 apgtpttppa sagsnacatq qaavqmaaqa apaeapidhl ivklktltat ramaaidngt
      121 rldaviqrsm trwtapvags arayastvgq apvnvqvert isngaavlsl gqrmaatdaa
      181 alaqafaads dvdyaepdhp mqirdtpsdp lynqqwylsd ptagidlppa wnvtkgsptv
      241 vtavldtgyr phadlmgnll sgysfisnvn tsnngltrnp datdpgdwvt qqeldnangp
      301 yyhcasqpsd sswhgtrvmg vigatanngt giagvswlgq ilpvrvlgkc ggvtsdiadg
      361 mrwaagiavn gvptnprpak vinlslggvg acsttfqqai ddvtakgvtv vvaagndgls
      421 tgldqpancr gvisvgatda tgrrasfsnf gadvslsapg vnilstsntg tttpgsdtyg
      481 langtslatp qvsgvaalml svngnltpaq iqqklqggar ttklaagtsc tampagsgiv
      541 dagaaiaaag q
//
LOCUS       WP_175891997             199 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cepacia].
ACCESSION   WP_175891997
VERSION     WP_175891997.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..199
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20554
     Region          1..198
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mpfrdylplm lfvivstvtp ggattlatas gahfgyrrsl pmmagiaagl asmaaaaaag
       61 lggvllalpa lqlvmkavgs vylvwlavri grggkprlda evhrpqgfls gvwmlwhnpk
      121 gwamtlgaaa sfaalasgpa plgillglaf gvaamaslsl wcvagllfar vlrterqwhc
      181 lnaalgvllv isivpmwlp
//
LOCUS       WP_175892004             304 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175892004
VERSION     WP_175892004.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..304
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32687
     Region          14..284
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mpmntatapa plceidglki gfrghdgtvt davrdlsltl apgerlgivg esgsgksltg
       61 rallgllpda arwtartmrf aghdllamsp rerrrlcgsq mgmilqdpky slnpvmtvak
      121 qmgeafrlhe pglrgralre rivdaleavq irdparvada yphelsggmg qrvmiammvs
      181 tgprlliade ptsaldvavs mqvlavldam iarhdtglmf ishdlplvms fcdrvavmya
      241 grvvetcaar dlrnashpyt rgllaanppl anppdelpvl rrdpawlepa phagtpadrq
      301 eaar
//
LOCUS       WP_175892034             261 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Burkholderia cepacia].
ACCESSION   WP_175892034
VERSION     WP_175892034.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..261
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=28986
     Region          61..256
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mfarffmpcr irtriynsgg aghparrdcr phskrpkmss mtprflpsdd rdarsttvva
       61 lerlqrdngr faaffrqvns rfarqarrly pwsrdadied alqsallslf eptsafsldd
      121 aarmddatfd arvagyvtga atkqlitrlr klgvesvrlt sleqwleneh aldallsdlg
      181 elapspeaaa ilartraave rclsklteta retfmlalgg hkdveiqqmt kagspvsvrr
      241 rvseakarvi acvqdqtget a
//
LOCUS       WP_175892059             550 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia cepacia].
ACCESSION   WP_175892059
VERSION     WP_175892059.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..550
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=59758
     Region          52..530
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mpprvdrksr erwrlkcrcl agvvlaggmg lapgvhaqea apaakaapaa pqsfdvnafv
       61 vrgnttlptl eiekavypfe gpgrtladvn aardalqkay qdrgyqsvvv elpqqqvkng
      121 villqvteak vgrlrvdgak ynspqnirda vpalaegrvp dfnqaqqqlt dlnrsadrqv
      181 ipvlkpgalp qtvdvdlkvd dhsplhgsle lnndnspgts tlrttaslsy snlwqlghvi
      241 sgtyviapqh pndarvyafs ylapirdsrw sflatvvhsd snvasvgntn vlgkgttygf
      301 taiyslpate tyahsvsiei drkhydedvs lpgqggsmap ltyvpvtlsy ngqlslknsq
      361 tsfsaslttn irglgsdwga wdnkrynatp dfvygkfdvn htqrfandmq anahvnaqis
      421 nsplvsseqf aaggvnsvrg ymqaedtads gviaslelrs pslakwlgga vgsrvnewrf
      481 haffdaahlw llsplpeqta rfnlmsvgvg trvqimkyas adfeagwplk agvytrqysp
      541 rfdffvrlgf
//
LOCUS       WP_175892088             296 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia cepacia].
ACCESSION   WP_175892088
VERSION     WP_175892088.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..296
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31981
     Region          27..245
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mtksptgsen tqshlmheqr srdivhrarg mgngsitrlv spsdlgrlik pfvfldlfes
       61 dgsharplef gwhphsgiat vtvvldgavq yaettgnagv lpsggvewmq agggvwhtgt
      121 fdtaplrgfq lwvalppdle naptrsqyvm peqvpsagpv rvilgtydgm tspvdappmt
      181 ylvvtlkdge hwafvpppgq dvawvsvmdg alrassritr geiaiferae taielvaegd
      241 trfvlgaatq hpyelvlghf svhtsvealq rgeaeihrig rqlraegkqs yalqsm
//
LOCUS       WP_175892181             180 aa            linear   BCT 11-JAN-2025
DEFINITION  SMI1/KNR4 family protein [Burkholderia cepacia].
ACCESSION   WP_175892181
VERSION     WP_175892181.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10558574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..180
                     /product="SMI1/KNR4 family protein"
                     /GO_process="GO:0042546 - cell wall biogenesis [Evidence
                     IEA]"
                     /calculated_mol_wt=19513
     Region          24..160
                     /region_name="SMI1_KNR4"
                     /note="SMI1 / KNR4 family (SUKH-1); pfam09346"
                     /db_xref="CDD:430545"
ORIGIN      
        1 mldklsqlga tptklssetk mrllasveae vgplpddygn lllhfggdie fnslikfrsd
       61 epspwaaqdg tdslellygl sskygstilk rvetykgrip adwipigeap ggnqvclrih
      121 psgvrsvefw dhesevgpgl pprgtgltki tdtlqefvsr ltpedppana pravkvdlqf
//
LOCUS       WP_175892171             441 aa            linear   BCT 11-JAN-2025
DEFINITION  leucine-rich repeat-containing protein kinase family protein
            [Burkholderia cepacia].
ACCESSION   WP_175892171
VERSION     WP_175892171.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Shen,K., Hines,A.C., Schwarzer,D., Pickin,K.A. and Cole,P.A.
  TITLE     Protein kinase structure and function analysis with chemical tools
  JOURNAL   Biochim Biophys Acta 1754 (1-2), 65-78 (2005)
   PUBMED   16213197
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
REFERENCE   7  (residues 1 to 441)
  AUTHORS   Hanks,S.K. and Hunter,T.
  TITLE     Protein kinases 6. The eukaryotic protein kinase superfamily:
            kinase (catalytic) domain structure and classification
  JOURNAL   FASEB J 9 (8), 576-596 (1995)
   PUBMED   7768349
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..441
                     /product="leucine-rich repeat-containing protein kinase
                     family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=46990
     Region          <2..>186
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          39..61
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          62..81
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          82..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..175
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          214..432
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(214..217,220,222,238,240,269,287..290,345,349..350,
                     352,362..363)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
ORIGIN      
        1 mthtleqlqa gqlagarqlk lacgltafpr eifdladtle vldltgnalt alpddlprlh
       61 rlrilfasgn rftafpsvlg acerldmigf kanriqtvpr gslphalrwl iltdnaidel
      121 padigdcsrl qklmlagnrl rtlpaglaac ralelvrlsa nrldelpdwl lrlprlawla
      181 aagnpfgaap eaaasaepdi advdwaslac eqklgegasg viyraqwaae nrapravavk
      241 lfkgavtsdg lpdcemaacl hagrhpnmip vigkvrghpd gthglvmelv dpaltnlagp
      301 psfatctrdv yadgtgfepa aalriahgia svaghlherg imhgdlyahn ilhdgsggal
      361 lgdfgaasly dvsdrmrgar ferlevrafg yllgelldrc gqqawagrra ldalasacln
      421 edvdarpsfv eitaalaaqt r
//
LOCUS       WP_175892268             257 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175892268
VERSION     WP_175892268.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..257
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27987
     Region          1..>240
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mnllelddlc laydtphgrr tvvdglslal prgdigcllg asgcgkttvl raiagfepvr
       61 mgrivldgap vaapsldvpp errrigmmfq dyalfphlsa adnvafglrr mpkserrmrv
      121 aemldlvgla dsgsayphel sggqqqrval aralapspel llldepfsnl dvdtrerlaf
      181 elrdilkrtg htailvthnq aeafaiadri gvmkdgqlaq wdtpyalhhh paspfvadfv
      241 rrdaladera ralargr
//
LOCUS       WP_175892252             465 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54 dependent transcriptional regulator [Burkholderia
            cepacia].
ACCESSION   WP_175892252
VERSION     WP_175892252.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..465
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51365
     Region          1..118
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <139..438
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mgvdqrhviy ysrepndalr ghfdecgwrv dlaetvrdvr rvvqhgvata glldfspgfk
       61 psdlrelesc lsiqhigwia atrrgqlqda tlrhlirdyc fdyvtmpyet arivetvgha
      121 hgmvalteta appvgtgrse gemvgtcdam lglfrtirrv aatdapvfis gesgtgkelt
      181 avaiherssr ahapfiainc gaipstllqa elfgyergaf tganqrkigr veaanggtlf
      241 ldeigdlple sqasllrflq egkierlgah vsvlvdvrvi cathvdmdaa lregrfredl
      301 fhrlcvlkie epplrargkd ieilarhmle rfkgdahrrl rgfspdavas lygyswpgnv
      361 relinrvrra ivmsegrmit aadlelsefa tlapvsllea reaaerqaie qallrhrgrf
      421 adaarelgvs rvtlyrlmca hgmrdrgdtl agfsaplqel prhac
//
LOCUS       WP_175892379             333 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia cepacia].
ACCESSION   WP_175892379
VERSION     WP_175892379.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..333
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=36232
     Region          146..331
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mysamvwvla iamlcvaaam mlwrhaetrr vrtdakrfid srlepgarag agaqaarpsa
       61 agaaravpaq rgaarspssd tfwkhwyata seyltnlesr agiedargkt lvalvvlvai
      121 aafagnrgga lascaalacg ssilgvwlas riqrrrlkiv rqipsfldgi vrlvtlgnsv
      181 paafqsallt teeplrgcld hvsrmlrsgv eidramvhia kiyrteefel vgsvlrlsvk
      241 yggradvmle rmavfmrdle qaereltams aetrlsafvl vmlpigigsf iivsnpkylh
      301 gmwndpggqt llmlafllql agsvwlyrma rlr
//
LOCUS       WP_175892170             209 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cepacia].
ACCESSION   WP_175892170
VERSION     WP_175892170.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..209
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21962
     Region          1..207
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mplqtwmlfa aaylattlsp gpnvllvirn tvrygthgta atiagnlvaq gvvvvlvalg
       61 vgavlaampp lfvamkvaga aylmvlgvrq lrgerkagas tgaaevaapd rgklfrealf
      121 vsgsnpktmi flsafmpqfi vydrplalqf vvmyatiact vvvvhsvysa gvrrfhrgfg
      181 msravralkr asgllfvglg iklltarqa
//
LOCUS       WP_175892452             282 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175892452
VERSION     WP_175892452.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..282
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29807
     Region          7..260
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtrstaalaa rglsvgyrdh vvidgldlsi aagrvtalcg pngcgkstll rtlaglqpar
       61 aghvevngqp lasfrrrala reltmlaqfn qipsgltvre lvaygryayg gflrglsrad
      121 haaidealdt sglasdaerd vgalsggerq rawiamalaq qapivlldep ttyldihhql
      181 dildalrtln rtrgltivwv lhdlnqaaay sdeivlmrag rlvaqgtpda mldparlraa
      241 fgvemlklah pqtgapmcvp aygpatdgap qaagvfdrdl av
//
LOCUS       WP_175892323             141 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia cepacia].
ACCESSION   WP_175892323
VERSION     WP_175892323.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..141
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15700
     Region          1..141
                     /region_name="COG3565"
                     /note="Predicted dioxygenase of extradiol dioxygenase
                     family [General function prediction only]"
                     /db_xref="CDD:442786"
ORIGIN      
        1 mslspfhlai pvydlaaard fygrvfglae grssarwvdf dfyghqlvih ehpktasqeg
       61 ahtnavdghd vpvphfgivl dwaswealae rlrsfgvtfv iepyvrfqgq vgeqatmflf
      121 dpcgnalefk afrdigqlfa k
//
LOCUS       WP_175892447             423 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia cepacia].
ACCESSION   WP_175892447
VERSION     WP_175892447.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..423
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44931
     Region          164..353
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mvksaatpda fapgraqrvv ralvpaavlg alaalglaal pavsqlpgav dsgtaalpqr
       61 vlsdtpfpta qhfvtselar tigernehvd rnndrslqpg lfaplsahrn dmlgyaslfq
      121 lappehqqgm ragdieltls dtlnrldvpp evriqlgdlv sgkvalrasa qrgdyyrvaf
      181 dtndgtprlt alelrvagrt fgaiwfrapg aehgayyald gspleaaaft mpvkwtriss
      241 ffgerihpls qamafhtgvd laapsgtpvd aaadgvvsfv gtdpggygry vivdhadgys
      301 tyyahlsaya rglkvgetvk qgqrigsvgm tgaatgphlh fevrvandpv dplvtlanaq
      361 tglsdmqlta frqeaaqwrf rlasinktpf afaqndgplw gdfatgpstl ravfdthyaa
      421 ers
//
LOCUS       WP_175892469             388 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia cepacia].
ACCESSION   WP_175892469
VERSION     WP_175892469.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..388
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42127
     Region          1..386
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mqfdltddqr aiesaiekic arfgddywle rdraggfpad fhaalaeagw lgiamdpahg
       61 gaglgmteaa lmmrtisasg aglsgasavh mnifglnpvq vfgndaqkar flppliagrd
      121 kacfavtepd agldtthlst qarrdgdhyv lsgrkiwist aqvankmlii arttpldrva
      181 kptdglslfy tdldrsrvev reiekmgrka vdsnmlfidn lrvpegdlig negdgfryll
      241 hglnperili aaeaiglgqa alrratqyac ervvfgrpig qnqsiqhpla qtwmqleaaw
      301 lmvmkaatry dagqpcgaea naakylgaea afqacqtava thggmgyake yhverylrec
      361 miprlapvsp qlilcyiaek vlglpksy
//
LOCUS       WP_175892487             290 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175892487
VERSION     WP_175892487.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 290)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..290
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30898
     Region          1..288
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mstlpargtp rdakawlvtp alafivalfi ypfayglvls fqpmngggal anyvqfftdt
       61 amwptvlvtl klavpatlln vgvavpvafa lrrnspyqkf vttllvipvt lgtvlvadgm
      121 ltyfgpngwf pqalqglhly tdevrlthny wgvllslivs gfpfafllml syisgidptl
      181 araaatlgan pwqqfrriyl pllvpgltma aclsfvqafs vfpsavllga pagptrvisi
      241 aaaeaafesy dyslasaiai vmgfvqllvv asmlgarrff ytgavtggkg
//
LOCUS       WP_175892570             451 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175892570
VERSION     WP_175892570.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..451
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48293
     Region          24..443
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mptqpstpaa slalqdeala ahasqhsraq rylqllllvi aagaiypmly lrqvyqptml
       61 qffhiddvql gylysslgti flvsylpsgw ladrlsprwl icfsllatga lglayatgps
      121 fdtlvlifgg wglttgltfw aavikrvnmi agpdeqgrff glldggrglv eallatiait
      181 lfayvtqahg gtdaagfrlv vhlyaffcia lgvllalvkd pagtsdraaa akrrtgsdrq
      241 gnvltdlktl aaipelwlva aivfcgyqvf watysfsayl hegnfglsat aagfittlkl
      301 wmrpiggigg gflgdrvskv svlfwallla alslvgliaa pahspqamlv vlvlfigilt
      361 yairglywsl lddckvpthc aglaiglisv lgyspdvfvp lingyvtqtw pgahgyqlyf
      421 gyiaaialcg agaaaflkyr ltrihriqes a
//
LOCUS       WP_175892522            1054 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cepacia].
ACCESSION   WP_175892522
VERSION     WP_175892522.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1054
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115087
     Region          11..1032
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mstpheegrf nlsawalrhq alvvyliala tlagilaytr laqsedppft frvmvirtfw
       61 pgatarqvqe qvtdrigrkl qetpaidflr sysrpgesli fftmkdsapv kdvpetwyqi
      121 rkkvgdigyt lppgvqgpff ndefgdvytn iwtlegdgft paqlhdyadq lrtvllrvpg
      181 vgkvdyfgdp dqrifievnn aqltrlgisp qqlgqainaq ndissagvlt taddrvfvrp
      241 sgqfdnvnai adtliringr tfrlgdlatv krgyddpvvt qmraagpgsa gkavlgigvt
      301 mqpggdvirl gkaldaeskd lqaqlpaglk lvevssmpha vahsvddfle avaeavaivl
      361 vvslvslglr tgmvvvisip vvlavtalfm ylfdiglhkv slgtlvlalg llvddaiiav
      421 emmavkleqg ytraraaafa ytstafpmlt gtlvtvsgfl pialaksstg eytrsifevs
      481 aialiaswfa avvlipllgy hmlperkrqa heahlpddhe hdiydtrfyr rlrgwidwci
      541 errfvvllit galfvvammg fslvpqqffp ssdrpellvd lrlpegasfa atlreterle
      601 kvidkrpeid hsvsfvgsga prfylpldqq lqlpnfaqfv itaksvkdre klatwlettl
      661 reqfpavrwr lsrlengppv gypvqfrvsg dsiatvrsia ekvaatmrgd trtvnvqfdw
      721 depaersvrf eidqkkarel nvtsqdvssf lamtlsgttv tqyrerdkli avdlrapkad
      781 rvdpaklagl alptpngpvp lgslgrfkpt leygvvwerd rqptitvqsd vragaqgidv
      841 thavdaklna lraqlpvgyq iniggsvees akaqksinaq mplmaiavft llmiqlqsfs
      901 rvlmvvltap lgligvvatl lmfgqpfgfv amlgviamfg iimrnsvilv dqieqdiaag
      961 hgrvdaiiga tvrrfrpitl taaaavlali pllrsnffgp matalmggit satvltlfyl
     1021 palyatwfrv krderdpqng pppggstpaa psga
//
LOCUS       WP_175892621             881 aa            linear   BCT 11-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Burkholderia cepacia].
ACCESSION   WP_175892621
VERSION     WP_175892621.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..881
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..881
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=93678
     Region          55..876
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mklrhvvgig clavlsgcgg dqastdasvl aqmsnaqgnq ndqgdqndpg esggagkrsv
       61 lrsvdpmigt anldinadwg sgvrghghvy pgatvpfgmv qlgpdttgga htlpwnwdrt
      121 sgyqyddpli tgfththlsg tgigsggevr flptlapvdt atlakvaada sitynasfsh
      181 ddetaspgyy rvkmapvgsg ntpwnvkgak ilaemtatah agvhrytyfp saaaqkrsmi
      241 vsidnpiggs tasgkiqvid aqtiagweit nnwannkpty fvarfskpfd tkhvafsadg
      301 fkayltfadg ndsgavtvkv gispssiada qanlaaevga ksfdqvrgaa ervwadvlgr
      361 irikggsadq rtmfytslyr tmlaptvynn adgsyvgtds tndgttsppt tskhanpgfd
      421 ysstfslwdt fraesplmtl vqpervdgwv kslltqfrqn gkgelpvwpl aqtetftmag
      481 hpsipliada ylkhltnagi ddiwaalttt qgasahgfdq yrqrgyvvag dnasvsttqd
      541 yafddwataa vgkaagksta dyrpylqrsq nyrnvfnptl nngwkfsqpk daqgnwvagf
      601 dptaaektdf sesnawidtw ntfhdfpglv allggksqfi aqldrtfdpa npltfldnqg
      661 fpdltgrsgq ffagnepanh lpylydvagm psktqdrvrt vmddmysltl tagdrallsg
      721 dslkaaladp rrvrdsaipg nddcgqlsaw yvlsalgiys lnpvggvfyl gtplfeeati
      781 dipiasgggd ggalkfgksr rftvtahtag ggapssvnry vqsvslngvp lhrpyityde
      841 mkaggtldfv mgatpndgwv sqwngqdpns alapslalag k
//
LOCUS       WP_175892667             100 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175892667
VERSION     WP_175892667.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..100
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10823
     Region          1..94
                     /region_name="COG5606"
                     /note="Predicted DNA-binding protein, XRE-type HTH domain
                     [General function prediction only]"
                     /db_xref="CDD:444337"
ORIGIN      
        1 mnydtsnqhs dnvpddfdyy dvgelaaksv lvlklnalmv shglteegaa alaemarpvv
       61 tpeqrerlrn vtldqlmltl asfgqhveiv vrpagitvsv
//
LOCUS       WP_175892699             713 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia cepacia].
ACCESSION   WP_175892699
VERSION     WP_175892699.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 713)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..713
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=80297
     Region          9..686
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mqsdlcftqs dlrftftggi esfevveftl heglsetfll qvelasanpa idfgevldrs
       61 gvltiwqggq pvryvygais sfvqrdtgfr rtrysavvep rlarlklssd wrifqtlsvp
      121 eiatavlkah nqtldyeqri taehlareyc vqagdtdydf ierilreegf fyafqhkadg
      181 hrlihcdrlf iygrqqgepv lynptpggdq papclrkfay tenvrtarqv qrdytfkspr
      241 ypheypregt dldhqgrgya rydypgrykh essgkaftqd llrghrrdar manvsgddar
      301 lqpgvafdlt ghpredmnrg wrpvsivhhg vqytsqaeeg adaqqgthyr yeavlvpdda
      361 ewraeplprp ridgpqpatv vgpegeeiyt daygrvkvqf pwdregkyde hsscwiqvaq
      421 nwagatwghm aiprigqevi vvnldgdpdq pliigraynr lqlppyelpr hktrmtiksq
      481 thkgegynel rfedekdqee iyvhaqkdqn ihvnhdettf vgndrseqve hdetiaignd
      541 rketvghdeq vtigqdrrhd igqddflsvg rnhtihtgkd rteevgnhrr dktaanhtvd
      601 igghlkqrva graeleagqa irhrtkvyei raagvlevkg pggtvridng gitlegvair
      661 tkgpmtqqsg gasnpfaitg apasgkpldr rcgrrpdgtc pladctclgg rak
//
LOCUS       WP_175892714             291 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia pseudomultivorans].
ACCESSION   WP_175892714
VERSION     WP_175892714.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 291)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..291
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31489
     Region          37..260
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mntlsspvag aapaarakad rywllvvpll avlivlyvyp lvrvlwlgft vpepglqnya
       61 rlvanhgvhr vlwttlrvca vttvcsvalg ygiayamahv gprqrmalmf gllvpfwasv
      121 lvrafswlfl lgeqglvntl lmriglidap lplmrnevgv vigmihfmip yavlplyanm
      181 kgidpqlara sqglgarafv tfrkvyfpqt rpgivgaail vfifslgfyv tpvilgggrt
      241 vmiaeyistq ilqlvnwgsg aalaslllas ilaalallar fvdlrelfga r
//
LOCUS       WP_175892729             375 aa            linear   BCT 11-JAN-2025
DEFINITION  J domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175892729
VERSION     WP_175892729.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10644999
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..375
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=42685
     Region          <210..250
                     /region_name="DnaJ"
                     /note="DnaJ molecular chaperone homology domain;
                     smart00271"
                     /db_xref="CDD:197617"
     Site            order(226..228,237,243..244,247..248)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
ORIGIN      
        1 mtarrgaavv iapghetasl skaqktfntl vqqiearrer lgawdavtpa fhkkfvdgll
       61 pleqaatalr isllnrldda flqkglskae qrtlsdvian mardlldvsd daqlkilynr
      121 hrasgdddrt aadrarpkqa pepapapaqe ddldtlspde laermqaeld eqfrrdmaeh
      181 eareaqrakr kkaprqsaaq arreaeqaks sksirdvyrk lasvlhpdre tdpkeqerkt
      241 vlmqrvnhay akgnllqlle lqleieqidr raidglgedr lmryngilee qvreldqeir
      301 hvethfrrty giassvkiap dtvmriltrd iagmqrsnqd ltiavrefdd pdnvrewlkd
      361 mkrrpassrf dddsy
//
LOCUS       WP_175892743            1012 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding and (Fe-S)-binding domain-containing protein
            [Burkholderia cepacia].
ACCESSION   WP_175892743
VERSION     WP_175892743.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1012
                     /product="FAD-binding and (Fe-S)-binding domain-containing
                     protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=110292
     Region          24..539
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
     Region          492..1011
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mtsavspslv rpvhlvpsqg aalsplferl rremrgdvya drasrgryat dasiyqimpl
       61 gvvvprdqdd lrialdiard rkipvlarga gtsqcgqtvg ealvvdnskw lnrivafdaq
      121 artvtvepgi vldhlnawlk phglwfpvdv staaqctigg magnnscgsr sieygnmvhn
      181 vlaidailad gsecrfgsla qpvtdrrtld llhgveriak rerdeiverv pkvlrrvagy
      241 nldlfdcqnp raytddghan lahllvgseg tlahsrqitl klaplpahkt lgvvnfptfy
      301 qamdtaqhiv klkpvavelv drtmidlsme npafrpvier alvgrpqail lvefagesrd
      361 aqhaqldrla elmadlglpg svvkmtdaga qkalwevrka glnimmsmrg dgkpvsfied
      421 cavplehlae ytrrltdvfh khetegtwya hasvgtlhvr pildmrrdga trmreiaeea
      481 aalvreykga ysgehgdglc rgewvawqyg prlnaafaei kklfdpdnrf npdkivnppk
      541 mdarehfrfa pgyaalplrp aldwsawnvt rnpltgeeta pgsgtdvthg lasavemcnn
      601 nghcrkfdag tmcpsyrvtr deqhvtrgra ntlrlavtgq lgadglagdd vkaaldlcvs
      661 ckgckrdcpt gvdmarfkie arhawnrkhg ttlrerlvay lpryapwaar mrgaiafvng
      721 vpvvassikr wiglapqral pgfarpflad tgagagastp tqtgsaprev llfvdtfnny
      781 qepdnaraaq avleaagytv hfnvragarp lccgrtflaa glvdeaksea rrtldalrpy
      841 lergiaivgl epscllsmrd eflaygygde atrlashafl feeflvrehe agrltlplha
      901 idanealvhg hchqkafgaf tpvqtvlrwi pglkvspves sccgmagsfg yeaehyaasq
      961 amaelsllpa vraraegaiv vadgtscrhq iqdgaqaqav hvakvlaral rs
//
LOCUS       WP_175892827             256 aa            linear   BCT 11-JAN-2025
DEFINITION  TniQ family protein [Burkholderia cepacia].
ACCESSION   WP_175892827
VERSION     WP_175892827.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Li,Z., Zhang,H., Xiao,R. and Chang,L.
  TITLE     Cryo-EM structure of a type I-F CRISPR RNA guided surveillance
            complex bound to transposition protein TniQ
  JOURNAL   Cell Res 30 (2), 179-181 (2020)
   PUBMED   31900425
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Kholodii,G.Y., Mindlin,S.Z., Bass,I.A., Yurieva,O.V.,
            Minakhina,S.V. and Nikiforov,V.G.
  TITLE     Four genes, two ends, and a res region are involved in
            transposition of Tn5053: a paradigm for a novel family of
            transposons carrying either a mer operon or an integron
  JOURNAL   Mol Microbiol 17 (6), 1189-1200 (1995)
   PUBMED   8594337
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10534787
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..256
                     /product="TniQ family protein"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=28099
     Region          23..153
                     /region_name="TniQ"
                     /note="pfam06527"
                     /db_xref="CDD:461938"
ORIGIN      
        1 mknqswmscs vrpansmlrl plalrvepyp deslssvlmr lvdanglrsv gallrdagcv
       61 afgpfvsaei aelsrvcrig qstmrsmcpv eiggrargta fsyavgrhvi earhllvrer
      121 ericplclld seimlaahrl twmtacpvha vqlhdvcpqc akpiavtrpg mtrcrcgfil
      181 sqispvacgs eeietarhlh qcwrfltstg velsaglaav ekrmdntrai rakggrdlvd
      241 lrgiplhqir nelgyi
//
LOCUS       WP_175892934             126 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175892934
VERSION     WP_175892934.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..126
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=13686
     Region          37..117
                     /region_name="COG5606"
                     /note="Predicted DNA-binding protein, XRE-type HTH domain
                     [General function prediction only]"
                     /db_xref="CDD:444337"
ORIGIN      
        1 mptshqnqrs rstntrrrrr phateadngn avndeilsgd dfdadsakma lasklnallg
       61 errlsqsaaa qllgmsqprv sairnyklhg islerllqal lamgqqveiv vkphhetgdp
      121 airvta
//
LOCUS       WP_175892942             393 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA-binding protein [Burkholderia cepacia].
ACCESSION   WP_175892942
VERSION     WP_175892942.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13774834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..393
                     /product="DNA-binding protein"
                     /calculated_mol_wt=43262
     Region          25..143
                     /region_name="KfrA_N"
                     /note="Plasmid replication region DNA-binding N-term;
                     pfam11740"
                     /db_xref="CDD:432038"
     Region          <102..>343
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
ORIGIN      
        1 mtldeirqti rdeleslrak garrqelslh ackrlffdlg irpsaanvrd ltqtgsasdi
       61 pkdidhfwer irsaskvrld gaaipkavee kagallgaly eealkaards ldvdreqvra
      121 dvadaeqrlr daivrqetle galargeakn eqlqarvtel evqlasqtth gsaseatllt
      181 tvarlekela aavgrveaeq aqnatlrdri dalqaelqqr tehyaqqikd avaeaerrvk
      241 pmlveldslr stastyqngl rdvqrkefdf lqqlsaakar adrleeqlrs qgdeleratr
      301 dvsllrasrg tnpeiaalir rladagqlda eafaaigtsl dqetpvpahc phcdgepels
      361 hgkegfevac pecehasgaw psrleavarf vrt
//
LOCUS       WP_175892971             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175892971
VERSION     WP_175892971.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33881
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdyidklrif rsvvelrsft raadmhglar pvvsravadl earfggrllh rttrqvslte
       61 taerlyerca avldeldale leaqtqtrep egllrlvvht taalnqlvpl iagfksahpk
      121 lrldvtlter pvdlvgegyd igivvpymlt settvvrlia ripfvivatp aylrahprpa
      181 mpadladhpf vplspslrrp alsfrvdgdt ltvpfrfdis snspvfnrem vmhdfgigvv
      241 pktlvsaela sgalvplled aelldafvei klayanrall pakvkafidy ttrycerenw
      301 itslaa
//
LOCUS       WP_175892992             325 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia pseudomultivorans].
ACCESSION   WP_175892992
VERSION     WP_175892992.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..325
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33041
     Region          12..322
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mnlanlisep daprrlsrrs lfalardhsv ylafvalvvf nlivtpgfsn plaarsllfq
       61 aapivlialg qnlaiatrgi dlsvgsvmal asamiavclp ygtgaafaaa vaiglavglf
      121 ngalvarldi dplisglall vaarglaqal lggsrvslpp sdafdfigig tfaglpvvml
      181 valacaaivf fvvrnttfgr htilvgasrd aahlagvpvr rtllavyaas galaglaglf
      241 atarlgagdp nyvgvnfeld aiaasviggt plsggrvsiv gtvfgvlllq lldasfimnn
      301 isytyaqilk aafilgalyl qrsga
//
LOCUS       WP_175893005             216 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175893005
VERSION     WP_175893005.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..216
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23834
     Region          12..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpnptddpgr rarkriqmla hladtaarlf dahgydavtm eqiaakadva krtlynhfat
       61 keavlahwle helardlahl qrdvarrksf asrvgcvlda saawceqhpv hllaylrhrf
      121 lsigaaapdg dhahgndial vwqqlivagq qagelnrslp aeqlatwfhh lylaamlrwl
      181 tvpglslkke fqsvarlfve gaqaktpapp rgasra
//
LOCUS       WP_175893040             384 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia cepacia].
ACCESSION   WP_175893040
VERSION     WP_175893040.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..384
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41921
     Region          1..384
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnfdlelehg mirdlvarfv qdelipleaa vmareadgqr fglldeerah ldersrqlgl
       61 wgldapldad gsdlpavamv gvneaigttv tpyilppdsp nlrmlcdvad aaqrarylep
      121 yargitraam aisepgagsd pgalsttavr dgdswvlngr kiwishapea dwtivmaltd
      181 rskgkrggms afivdrgtpg fiierripmi gglstyeivl ddcripaaql lgqegagfap
      241 mqarlanrrl emaawcigra eravamlcdh akqrktfgvp laerqaiqww vadaltqiha
      301 crlmtyeaaa rvdagqdart qismvkvfat emassvidha mqalgamgmt kemplqqmas
      361 earlmrifeg ptevhrwvia rsal
//
LOCUS       WP_175893064             212 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia pseudomultivorans].
ACCESSION   WP_175893064
VERSION     WP_175893064.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..212
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22534
     Region          5..205
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtasaavfai laalwlgami pgpsfvlvar nsiglsrrdg latalgmgig givfggvala
       61 glytllqave wlyvglklag gayliymask iwrgadrpia mddpkaagag rasrsfwtgl
      121 ttqlsnpkta iwygsifaal lpqhpplwcy lalpplvfgv efgwytival cfstrrprel
      181 ylrakkwvdr iaagaitllg lrlilnapka gi
//
LOCUS       WP_175893044             350 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia cepacia].
ACCESSION   WP_175893044
VERSION     WP_175893044.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..350
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=36733
     Region          4..350
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mqrkalliga cvlsatpaha ssvtlygivd syvefdrigs lsslrqsggg sstsrigltg
       61 vedlgggtst kfvlesgfsp adgsfqggtl fyrqayvslq ntrygdlrlg rqytpafyiv
      121 ydgdpfglne rlsplallat stdtitsntt ppiprfnqaa sylspdwngl rvmatygfpt
      181 pnalstqagr nygaglqyri gglylgagfq gdtsagnlap vvspsttrhy vfaanyafar
      241 vklyaaflyg vgtaphlpaf stasagasin vgaldrvlvs vvrrdvkgsa ndatalgvgy
      301 dhplskrtsl yarylyvkng gdarntvavg lqpqpggtgq vfalgiahrf
//
LOCUS       WP_175893021             431 aa            linear   BCT 11-JAN-2025
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Burkholderia pseudomultivorans].
ACCESSION   WP_175893021
VERSION     WP_175893021.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..431
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=46312
     Region          1..431
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 mteqasskwr letlavhggy rpdpttrava vpiyqtvaya fddtqhgadl fdlkvqgniy
       61 trimnpttdv leqriaaleg gigalalasg qaavtyaiqt iaeagdnivs asslyggtyn
      121 lfahtlpqyg ittrfadprd pasfeplida rtkaifaesv gnplgnitdi aaladiahrh
      181 giplivdntv pspyllrpfe hgadivvhsl tkylgghgts lggaivdsgk fpwaehadrf
      241 krlnepdvsy hgvvyteafg paayigrarv vplrnmgaai spfnafqilq gietlalrid
      301 risdnalkia qhlarheqve wvnyaglpdh pdhplvaryl sgrapgiltf gvkggregga
      361 kfqdalklft rlvnigdtks lathpastth rqlspaelak agvkeetvrl sigiehiddl
      421 ladldqalaq v
//
LOCUS       WP_175893090             116 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia cepacia].
ACCESSION   WP_175893090
VERSION     WP_175893090.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..116
                     /product="VOC family protein"
                     /calculated_mol_wt=13097
     Region          1..112
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 mklrtvylkv sdmetsasfw erllgytplk rsgkwtefmi gtnrlgllln dfgdeikrsg
       61 svpvfefeek alhefvkrat engasivmdg lkiesmksiv lsspdghefe lcmcrd
//
LOCUS       WP_175893109             418 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia pseudomultivorans].
ACCESSION   WP_175893109
VERSION     WP_175893109.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 418)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 418)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..418
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45077
     Region          <195..412
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mtiassapss aalkrelkaa earkrtmall lvaplalfvl lifvvpigtl ltravqnpei
       61 aaalpdtvaa lahwdrkapp sdaayaalaa dmtkvadsda mgalarrlnt eipgyrslva
      121 ktaramplkg dhdatltpaq mrdklvelds rwgdvaywqa iakngstysp fyllaaldhk
      181 qdgfghivpa dpdqsiylai fgrtlvigva vtlfalllgy playwistls erranlvmil
      241 vlipfwtsvl vrvaawivll qseglinkal lgtglishpl tllfnrvgvy ismthillpf
      301 milplysvmk sipptyqraa vslgshpfaa fwrvyvpqty pgvgagallv filaigyyit
      361 pallggpndq mvsyyvayft nvtinwgmac algglllaat lvlyavygrf trtnvslg
//
LOCUS       WP_175893115             711 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia cepacia].
ACCESSION   WP_175893115
VERSION     WP_175893115.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 711)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..711
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76338
     Region          46..691
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mlnatiaaav avaapdvfat egkqaqstte spdsgtsass aestvlepvt vtarktterl
       61 qdvpesitvl qaktlkespf dpgvaiagha pnvqwvsrat gsqwfsirgv sslgtpanya
      121 dgtiafnvdg vpnsmmsasn mlldvdhiev lrgpqgtlwg tnalggainv vtkqpdgtrd
      181 vhvttevgeh gyrmgeavlg gnivpgqldg rmairyghen gdirslytdk lgkrdigafr
      241 gglrftgldd tlitvtanyl hdqansplyv lrsasqfpts giltepdlkt tqagatvtve
      301 hffknfqlts issyqhnkle seldlvdklv ydaigfpass nvghstdqen ifsqeirlns
      361 legapvrwvv gasamrtngi rwcsstqcap ppysgsvamk snldttnlgl fgdvsipfan
      421 rwefsiggrv shdniemkqd nslglasltg snstsqtypt grvalsfkwt ndiqsyvsva
      481 rghasrvypl fsypvdgivg npypaalgwt yeagvkadll shrlqidasv yhndikngvm
      541 syldpslgdf rttyqdykts gfelqaralv aeglsfsggv gyihselgan gaavntvtgn
      601 pvpntpkwta taglqyetsa kaihlpgkls adlqyqytgk rtadidksyy ldayslvnaq
      661 igwknkdlev ylfgrnlfdk ryetfgslya gmqlvsvgrg rtlgvgltks f
//
LOCUS       WP_175893136             271 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175893136
VERSION     WP_175893136.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..271
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29267
     Region          16..265
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mstsvtspal keresspdei talarglavl rriaaadapv snreltgipk ptvsritatl
       61 vsagflfqlp dserfvltas vlelshgflr nfdirarsrp fmielaerts lsvhlavrdr
      121 ldmvaidvir prsavlvtrl eigsrmdiar tavgraylaa ledderrali dalraaagdd
      181 wphvharlnp alddamregy aiaigewreg lnavaagfvg psgqrysvnc ggasnqcppe
      241 wlhehvvpal heciakitre iggaparrta v
//
LOCUS       WP_175893142             286 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cepacia].
ACCESSION   WP_175893142
VERSION     WP_175893142.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..286
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30632
     Region          54..257
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mdasefskfl kavlpaqata gaaltvaeve ipgyaqdivl rlyrrpdktg lpvvlyfhgg
       61 gfvrgsleda dfaarflaer lpalvvsvdy slapafpfpa apedayraav waatrarafg
      121 gnpkrigvag hdaggqlanc lafiardrge vsiaaqalfg pmldpsmtri gdaerlasdi
      181 tarecaacyr aylpqaaqrm hpyaaplesv rlaglpptlv vtaqndvlhv eaekyagcli
      241 ssgvltqvir ypdithaala theaafeeav rffqcrfqar qpnrse
//
LOCUS       WP_175893156             393 aa            linear   BCT 11-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Burkholderia
            cepacia].
ACCESSION   WP_175893156
VERSION     WP_175893156.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 393)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..393
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40783
     Region          38..391
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mtqlfdtlgf vdasvaraga aagphdaaaa aaaggaavsl eqvgkvfatp rgqaaalrdv
       61 tldvrrgevf giigrsgagk stllrlvngl erpssgrvrv qgvdvgalde dglvalrrrt
      121 gmvfqhfnll saktvfenva lplkiagvpk aervrkveal lelvglaakr daypaslsgg
      181 qkqrvgiara lvhdpevllc deatsaldpe ttqsilalla dinrrlglti vlithemevi
      241 ravcdtvavi eqgevvetgp vwrvfgdprh gatrallstl vhdlpaelaa rvqplpeqaa
      301 lpdgahvvld vrytgesgge pdvgalaaal ggsvrflhgg ieriqghaqg rlviaaapra
      361 ddagqpaarg gavaallera rrhanhaevl gyv
//
LOCUS       WP_175893202             209 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175893202
VERSION     WP_175893202.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..209
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23000
     Region          1..206
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mkligmldsp fvrrvaisak lldlpfehep lsvfrhfdrf rtvnpvvkap tlvtddgaml
       61 ldsslivdyl dhrvaperrl lpdapdarlr alvpvgfala aaektvqvvy eqmlrptdkq
      121 hepwlervlg qleaaygale plvaaangwf ggarllqpdv ttavawrftq fmaadfppla
      181 ridparypal aahsaraeal aafietpld
//
LOCUS       WP_175893243             326 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH:quinone oxidoreductase family protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175893243
VERSION     WP_175893243.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Shimomura,Y., Kakuta,Y. and Fukuyama,K.
  TITLE     Crystal structures of the quinone oxidoreductase from Thermus
            thermophilus HB8 and its complex with NADPH: implication for NADPH
            and substrate recognition
  JOURNAL   J Bacteriol 185 (14), 4211-4218 (2003)
   PUBMED   12837796
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..326
                     /product="NADPH:quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=33617
     Region          1..322
                     /region_name="QOR1"
                     /note="Quinone oxidoreductase (QOR); cd08241"
                     /db_xref="CDD:176203"
     Site            order(40..41,122,126,147,150..152,171..172,176,191,215,
                     237..238,240..241,262..264,314,316,318)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176203"
ORIGIN      
        1 mkallctafg pidslriddv aapepaagqv rirvkaasln fpdalivqgl yqvkpalpfs
       61 pgaelagvid avgdgvtawk pgdavvaftg hggfaeqcva dlhqvaalpp gmtfeqgaal
      121 vlaygtslha lqqrarlqag etllvlgaag gvglaaieia kalgarviaa assadklalc
      181 raagadetid yatedlrrrv deltggrgad vvydpvggay seaalrataw hgrflvvgfa
      241 ageipkialn lallrerdil gvfwgdamrr dpaqhaanlr qlaawfasgk vrpaitervp
      301 lagaadaiar masrqikgkv vilpda
//
LOCUS       WP_175893272             463 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatase PAP2/dual specificity phosphatase family protein
            [Burkholderia pseudomultivorans].
ACCESSION   WP_175893272
VERSION     WP_175893272.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Pulido,R. and Lang,R.
  TITLE     Dual Specificity Phosphatases: From Molecular Mechanisms to
            Biological Function
  JOURNAL   Int J Mol Sci 20 (18), 4372 (2019)
   PUBMED   31489884
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Patterson,K.I., Brummer,T., O'Brien,P.M. and Daly,R.J.
  TITLE     Dual-specificity phosphatases: critical regulators with diverse
            cellular targets
  JOURNAL   Biochem J 418 (3), 475-489 (2009)
   PUBMED   19228121
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   5  (residues 1 to 463)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12932297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..463
                     /product="phosphatase PAP2/dual specificity phosphatase
                     family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=49584
     Region          38..212
                     /region_name="PAP2_Aur1_like"
                     /note="PAP2_like proteins, Aur1_like subfamily. Yeast
                     Aur1p or Ipc1p is necessary for the addition of inositol
                     phosphate to ceramide, an essential step in yeast
                     sphingolipid synthesis, and is the target of several
                     antifungal compounds such as aureobasidin; cd03386"
                     /db_xref="CDD:239481"
     Site            order(113,121,147..149,184,190,194)
                     /site_type="active"
                     /db_xref="CDD:239481"
     Region          316..453
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
ORIGIN      
        1 mselggdarg laapapdasl alrvgwlaam gavffstygf anwlaarrat vptfafgweh
       61 aipfvpwtiv pywsidllya lsflfwtrrd dlldhvkrll tvqlvsvacf iawplrfgfe
      121 rpdaggvaga lftllmgfdk pynqapslhi gllvvlwavy aqhlrgtlar gvlhlwfaai
      181 gvsvlttyqh haidvptgaa vgclalflfp lrdaagrlpd aaaapgaagr rlarryagaa
      241 alvaivalyc vprapggalv agwialalgc vawiyrrgap gafqkdaqgr fpvpvrwlla
      301 ptiagafvns rlwtfrqpap vridervsig rtpttrelrr hgftalvdlt aemprwaaad
      361 aslayaavpq ldlvapsaaq laravaaler lhaegrdvlv ccalgygrsv lcaaawlaar
      421 rglgdardal aavravrpha vwsddgvavl qdwidrrraa ggv
//
LOCUS       WP_175893292             231 aa            linear   BCT 11-JAN-2025
DEFINITION  YoaK family protein [Burkholderia pseudomultivorans].
ACCESSION   WP_175893292
VERSION     WP_175893292.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..231
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=23257
     Region          6..219
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mkhedtilaa vagfvdtlsf valfglftah vtgnfvliga gvagfgqgvl lklsvfpafv
       61 cgvvasslia rslsarpawq garalhavqa vlllgfclag vwatpvtqsd slpvlvagiv
      121 gtfamgiqna hprvipragv pntvmtgnvt qaildvvdll sagtadaara tartrfgkml
      181 paivafalga mggalgfrqv gfwallvpag alaalavcag afappvtqer a
//
LOCUS       WP_175893324             216 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cepacia].
ACCESSION   WP_175893324
VERSION     WP_175893324.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..216
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22439
     Region          7..202
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 malhypllfa ylaaivllia tpgpvvmlvv gtvarrgfrq gmltavgana aslvmiagam
       61 lmvfgvvlvs drlltglhva gcvfiallav rtllgewrag rtrdangaap gepasqtwrl
      121 pgvvrgflvg ianpkdllff vaffpqfvgi tpdsrvslai lavlwiavdf timtgymaai
      181 nhplihrkqr witassagal lvialaglgg aiagga
//
LOCUS       WP_175893337             729 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia pseudomultivorans].
ACCESSION   WP_175893337
VERSION     WP_175893337.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..729
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79487
     Region          44..716
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 msssstaspp aggtlstrya afsdwartdg vawlylakal laafislgvs mrldlpapkt
       61 amttvfivmq pqsgavlaks fyrvagtifg liatltfvsl fpqqpqlfll aialwialct
      121 agaarnrnfr sygfllagyt taliglpasq hpdgafmsam trvsevivgi vsagvvsalv
      181 fpqytgeqmr ttvrkrfgsf vdyvaaalsg qldrahieti htrfvadvvg feaarsmavf
      241 edpgtrmrgg rlarlnsefm sassrfhalh qlmnrlraag aqaaidaiep yfreiapllt
      301 rngepvrsst daahaaeqll awrdalprri ratraeceaq pdfplldfdt aaellyrfit
      361 dlheyaatya slasethere rwiehyeprt nltaaviagi rtatvilllg wfwietawpn
      421 gvtlvltaaa tcalasstpr ptamsaqmgm gtalavctgm llmfgiypri dgfvllcval
      481 apllaigiym tmkpklagyg mgyliffcfl agpdsithyd pssfmndala lvlsmlvsai
      541 afavmfppta pwlkkrlfad lrhqavaach arlaglrtrf esgardlmyq ahtlsadqpd
      601 vqrdalrwmf avleagnaai dlrqelstlp adpryaptmp wrraietmrt alsalfakpd
      661 aarfattlaa vnaaidatrp mpdafassre drhrlqrils hlhfvrtall dpesplepln
      721 rnrtqgtls
//
LOCUS       WP_175893367             948 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Burkholderia
            cepacia].
ACCESSION   WP_175893367
VERSION     WP_175893367.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 948)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 948)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 948)
  AUTHORS   Ingmer,H., Vogensen,F.K., Hammer,K. and Kilstrup,M.
  TITLE     Disruption and analysis of the clpB, clpC, and clpE genes in
            Lactococcus lactis: ClpE, a new Clp family in gram-positive
            bacteria
  JOURNAL   J Bacteriol 181 (7), 2075-2083 (1999)
   PUBMED   10094684
REFERENCE   4  (residues 1 to 948)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11909043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..948
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103807
     Region          4..>54
                     /region_name="McsA"
                     /note="Protein-arginine kinase activator protein McsA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3880"
                     /db_xref="CDD:443088"
     Region          83..877
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mpalcdicha rpavaratvm qdgerktisi cdyhfrqlmr hqsmlnpfds llggggpssl
       61 fgglgdespl aaeipresvd ptdafseqtl ellqraaeka helrrselds ehllyaladt
      121 dvcaallkel klspediksy idahahtgta dpdapldrls isprvkkavq yafqasrdlg
      181 hsyigpehll iglasvpdsv agtllkkygv tpealrqkvv kvvgkgaedg rvdaptgtpn
      241 ldkfgrdlta iarqgkldpv lgraqeiest ievlarrkkn npvligepgv gktaivegla
      301 qrivngdvpe vlrdkrlvev ninsmvagak yrgefeerak qlidevtakq delilfidel
      361 htivgagqgg geggldianv lkpalargel sligattlne yqkyiekdaa lerrfqpvfv
      421 pepsveqtiv ilrglrdsle ahhqvtfadd afvaaaefad ryitsrflpd kaidlidqaa
      481 arvrigatsr pvdiqegeaq iaqlkreqdy atsrkrfdea kqfeeqinak qksvdemmea
      541 wqrktgsetl evtvesvaev vsrltgipvs eltqeerqkl lkmeeqlrer vvgqsdavva
      601 vsdavrlsra glgqthrpia tflflgptgv gktelakala etvfgdeqai iridmseyme
      661 rhavarliga ppgyvgydeg gqltervrrr pysvilldei ekahpdvynv llqvfddgrl
      721 tdgkgrvvdf sntiiiatsn lgaaiimdnl tqpeaarktd kaireelmqv lkghfrpefl
      781 nridevivfh alskenirsi vqiqldrvir taaaqditlv mgdslvehlt eagyqpefga
      841 relkrqirqt ietrlakeil adrlksgdkc evdydkdsde vkfnklaapg akeakeaket
      901 keadgkakpn graakaaadv kphdtpadap ppaakpgkks sgakkdah
//
LOCUS       WP_175893407             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175893407
VERSION     WP_175893407.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33060
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          90..273
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(105..106,108..109,112,116,118..124,216..221,
                     227..228,230..231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdlaalaifr avvrengvtr aaaklnrvqs nvttrikqle eelgaalfvr dgrrlvltpa
       61 gqtllpyaer llaladeard avredtprgr lrlgtmesta asrlptvlar yhhawpdvsl
      121 elvtgttgwl idkvrdfevd aalfarppap dmlpdtfetv pvfredlvll tprghppvrt
      181 prdvilptlv afergcsyrk yveqwyaahg mkparvlelg syhaivacva agagiavapr
      241 svldrqpevg slaqheiael hgidtllawr hgyasaalaa lrdalaeaar qaddaaakpp
      301 vampa
//
LOCUS       WP_175893457             558 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 39 protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175893457
VERSION     WP_175893457.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14304616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..558
                     /product="glycosyltransferase family 39 protein"
                     /calculated_mol_wt=62585
     Region          9..377
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
     Region          450..555
                     /region_name="Arnt_C"
                     /note="Aminoarabinose transferase C-terminal domain;
                     pfam18583"
                     /db_xref="CDD:465810"
ORIGIN      
        1 mndtpprlpl nrialvllli afaviwfapl glrhlipsde gryaemarem fvtgdwitpr
       61 yngykyfekp plqtwlnalt fawfgvgewq arlytalasf agvllvgftg arlfnplsgf
      121 laavvlacsp ywnlmghfna ldmglafwma lslcalllaq rpglrpaavr gwmwtcwaam
      181 afavlskglv glilpgavlv lytliardwa lwkrlylvsg lviffaiatp wfvlvqqrnp
      241 effnfffivq qfrryltpeq nrpgpfyyfv pvllvgflpw lsvawqsirh alrmprqpng
      301 fspmlvlliw safiflffsa shsklisyvl pvapalalmi gaylplmtae rfrrhllgyl
      361 vffvvaafgi vflarlgdar tpnalyrafq vwlyaglava aaltlaaawl nrragvaaai
      421 amfgaawlaf gtiggtghde fgryssgali apavraelak lppdtpfysv emldhtfpfy
      481 vghttimvqr qdelafgisv epnkwiptvd ewiarwkqdt halaimapgq ydtlvkqgvp
      541 mrviardnrr vivekpqs
//
LOCUS       WP_175893465             357 aa            linear   BCT 11-JAN-2025
DEFINITION  C40 family peptidase [Burkholderia pseudomultivorans].
ACCESSION   WP_175893465
VERSION     WP_175893465.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..357
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36538
     Region          <6..175
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mlriwvpvav vsllaacssv ppqtasrssg mtittprafp ppanfpkfvd hsvgqeeisi
       61 qamslvgvpy rwggntptsg fdcsglvryv igraadvnlp rttadmssrg vsidpdqiap
      121 gdliffnttg rphshvgiyv gklrfvnaps tggtvrldyl tnpywakrfd girrvappra
      181 kptpfdapty earrdesrtp aaaapapvvt aaapqppaya aaqrvsaasp apvvaaappa
      241 sataaptdpy eppparlsaa rqqavsaggd aiaatsnats naapagvpev gtqipttalt
      301 aaeaaafdae lpaaaapsrn tepaavqvlr astqsapvga rtgttddpia rfangsy
//
LOCUS       WP_175893468             402 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175893468
VERSION     WP_175893468.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..402
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=42182
     Region          4..355
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 msqkilivga gfagvwgalg aarvldaagv tssdveitlv spkpelqirp rlyesgpqhm
       61 aapllpllda vgvkflegsv eeidvrektv gvacadgekr qiaydrlllt sgsklsrppv
      121 sglaehafsv dciedavald ahfatlaklp esparntvav vgcgftgiev atelpkrlre
      181 wfgpdaksrv vvigaqddig pdlgpnprph vaeafdslgv eavlgsrvvs iaadgvrtas
      241 gthieamtvi waggmraspl aaqvsshlda lgrvavtadl rvadaphvfv agdvararcd
      301 ddghdalmsc qhaivmgqfg ghnvaadlig vptltyrqpf yatcvdlgew gavysegwdr
      361 qiklthaegk arkqmintqw iyppapnrtd alaagnplas fg
//
LOCUS       WP_175893486             630 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia cepacia].
ACCESSION   WP_175893486
VERSION     WP_175893486.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..630
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=67693
     Region          12..543
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mlratasaaa adlivcngki atqddrqsfv talavkdgri latgsghdvm chahagtqci
       61 dlngrtvipg lndshlhmir gglnfnlelr wdgvptlada lamlrrqvlr tpaphwvrvv
      121 ggwtefqfae krgptaaeln aiapdtpvfi mhlgdsalln aaalraigyg rdtsnppgge
      181 iqrdrlgrpt glliarpdma vlhealerap klghddqmns mrhfmrelnr lgvtsaidag
      241 gdfqafpddy gailalarrg emtvrvaysl fvqhagreld dyarwvtlak pgdgdaflrm
      301 ngagellvys aadfgnflep rpdlpaalea elaavvrllv rhrwpfrlha tydesigrfl
      361 nvleavnret pfdglrwffd hcetitdani ariaalgggv tvqhrmafqg eyfiarygaq
      421 aamrtppira mlaaglpvga gtdatriasy npfvslywmv sgrtvggtal ypernrlgrm
      481 ealrcytvgs awfsgeddck galvpghyad favltddyft idearitsls svltvvggri
      541 vhaddefasl appppavspa wspvaefgga grrrsaesas lraaagaaga gplaasaarg
      601 lgrafmqrlh aatmetaeqc easgypgfay
//
LOCUS       WP_175893487             370 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia cepacia].
ACCESSION   WP_175893487
VERSION     WP_175893487.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..370
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39205
     Region          4..334
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,233,300,320,322..324)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,181,184,186,233,240,300,320,
                     322..323)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,181,184,186,323)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            186
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mssllshydl rglplpnrvv mgpmtrsrap srgqptelma eyyaqrasag livteatnvs
       61 pasasfeltp glvtdeqaag wkqvtdavha nggrifaqlw hggrvssltl lggaaplsps
      121 gvnddleqlq vwaqlqngyy tkihatpsra mttdevadav defrdaavra maagfdgvei
      181 haangylphq flsstlnrrd dryggsvanr arfleeiida vgavmplsrv gvrispyaky
      241 nnvrdadpdt tyayvgrmld eavvayvhaa dtngwsgepd lprivanark hfggtlivng
      301 giapdaanal idagdadlva farayianpd lverlaanap laapkavgwy ggdragyvdy
      361 arhdaagvsa
//
LOCUS       WP_175893503             148 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia cepacia].
ACCESSION   WP_175893503
VERSION     WP_175893503.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..148
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15577
     Region          18..137
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 msmttgrysp awirallaqp wigalvrlal vsafliggvn kamhfdaaia eqahfglhpp
       61 alwaalavvv eiggslcivf rrftwlgagg lgmltlvama vandfwnqtg aahfmalnsf
      121 fehlgliaal vlvtmlgdvr sgegdgrs
//
LOCUS       WP_175893511             567 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175893511
VERSION     WP_175893511.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..567
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=62260
     Region          17..552
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 msageinear ltqsvgefdy ivvgagtagc avanrlsedd dvsvllieag gkdnyhwihi
       61 pvgylycign artdwryktr deaglngral syprgrvlgg cssingmiym rgqredydgw
      121 armtgdsswr wdsvletfkk sedyhggasd ahgaggpwrv ekqrlkwdil etfaqaaeqt
      181 gipatddfnr gdntgvgyfd vnqkhgirwn askgylrpva krgnltiltn aqtrrllfen
      241 krctgiefrh ggesriakgk revilcagav nspqllelsg ignadrltkl gievvedlrg
      301 vgenlqdhlq lrmafkvegv rtlntlsahw wgklmigley glfrsgpmam apsqlgvfak
      361 sdpndktlsr pdvqyhvqpl slerfgeplh pfdaftasvc qlrpssrgsv hitsndplma
      421 psiapnylst eedrhvaana lrltrrivaa palerfrpqe ilpgiqfqte eelqyaagnv
      481 gttifhpvgt crmgraddpg svvdsrlrvr gvsglrvvda svmptitsgn tnsptlmiae
      541 rasemiradr kregrsaeti rggvlst
//
LOCUS       WP_175893550             726 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cepacia].
ACCESSION   WP_175893550
VERSION     WP_175893550.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 726)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..726
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78079
     Region          38..726
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mvtgtgaakr amaiaagsal yvaaagaaha qasgaavapp tavlpeidvt gkgdrsssgl
       61 vglrttagtk tdtpvaevpq tinivtaqqi emtgatdlnq alryvpgfat fgadsrtdsy
      121 aalrgftptl yvdgvaapht aviadwrvdp ytidsiavlr gptsvlygag epgaivdaht
      181 kladgervre agvqigndar kqfmvdvgdt ldpdgryayr fvgvardgna etgpngdrrv
      241 alapsfrwrp nadtsltlsa tflqdsgdis snflpasgtv lpnpngrlsq diymgdpgfn
      301 dyrkkqwslg yalehrvnai wslhqdvrws hlslddatvf gngfaprstt nmmrtaglfq
      361 lnysrldidn haqarfgtgp lehtlllgvq ydrqtttnsv wlaiapslnl yhpvyrpvtd
      421 aifagptslg hvdqytamnt fgvyaqdqir wkrwtltlgg redfvnarfd drtagkqarq
      481 dvsafsgrvg ltyrgdagls pyvshstsfd pvigvrlygg glpkptrgtq teaglrwqpp
      541 grnlmlsaal yqidqtnvat ptpvnldptg ttsvqtgkvr srgielsavg kvtrelsiva
      601 syvhqdvknv qandaslnhw pvavplprqm asmwadwtwr tgvlsglgfg ggvryqsasa
      661 gapdnsltvp svtlvdlalh yemphwrfal nvanlfdrry vsgcqsynvc vfgnertvla
      721 sakynw
//
LOCUS       WP_175893552             341 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175893552
VERSION     WP_175893552.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12168325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..341
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37778
     Region          31..203
                     /region_name="AraC_binding_2"
                     /note="AraC-binding-like domain; pfam14525"
                     /db_xref="CDD:434015"
     Region          247..334
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 maqfsgtgwl ddtacfnhdd lllqsndvde vrarvadvfk phrltptges ralhscmhha
       61 rwgnlslnll dygggvsiep gplehffllq iplrgdaeie cgsarfvssp gtaslisptl
      121 plkmrwgdac pqvilriere vmerhaqrhf gddrrapvef epafslsssq gaclaqllpv
      181 lagaiatdah plrhplafep lestllnlll hghpnsarng trhlpvalap fyvrrvedyi
      241 rahldeplti erlaelagvs pstlfagfrh rhgitpmgfv rqlrlqrvre ellvdespgl
      301 asvtdialkw gfahlgrfai eykrafgesp satlrmrrvr a
//
LOCUS       WP_175893569             838 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia pseudomultivorans].
ACCESSION   WP_175893569
VERSION     WP_175893569.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 838)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..838
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=90951
     Region          60..776
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mpiikrpssp pdrtephytl rrspsgayys ddddgdqrra srsdgggrgr rsfgsrvalw
       61 fvglfatlai vgalivgyal vvmapqlpsl daltnyqpkv plrvftadhv ligefgeerr
      121 slvrfqdipd vmkkavlaie dyrfyehggv dfvgilragv adlmhggarq gastitmqva
      181 rnfflssekt ytrkiyemll aykiekaltk dqilelymnq iylgqrsygf aaaarvyfgk
      241 dlkditlaea amlaglpkap saynpvvnpk rakvrqeyil krmleigyit qpqydeavke
      301 eihvrtpgnq yavhgeyvae mvrqmmyqqy kdetytrglt vtttinsadq eaayqavrrg
      361 ildyerrhgy rgpegaiklp aagddrdeai ddaladhpdn gdlqsavvls aapsavevqf
      421 vggatttigp aglrfvsaal sarandtlri kpgsivrvlk dgktgwqivq lpqvegalva
      481 iapqdgairs lvggfdfnks kfnhvtqawr qpgssfkpfi ysasldkglg patiindapl
      541 yfppsvpggt awepkdddqp dgpmtmrtgl qrsknlvsir ilasigtqya qeyvtqrfgf
      601 dpkktppylp malgaglvtp lqlatgyavf anggykvdpy liaevddarg qplqksqpai
      661 agstaprtie grnayvmnsl lhtvatagtg agtnvlgrgd lqgktgttnd akdgwfagyq
      721 qslvavawmg fdqpkslgsr efgaqlalpi wvnymrtaln gvpeeqmpmp dgltsidgel
      781 yyadrtpgng fvasvdinpa anaisandal gsagaegltp ppvtpqekqq imdmfesk
//
LOCUS       WP_175893579             490 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175893579
VERSION     WP_175893579.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..490
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51946
     Region          26..449
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(36..37,40..41,44,84,134..135,137..139,142,162,
                     165..166,169,285,288..289,292..294,297,324,328,379..380,
                     384,402,405..406,409..410,413)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mshshaasia aridrlpata tiwtlvlfls vggffevydl fqmtylppgl irdgifhags
       61 hgvlgmsdqg algaatfagl fvgemfvsrl adrfgrralf tgalllytaa slamcvqtha
      121 lgilvcrfia gcgigaelit igafltelvp kavrgrafal cfavgylamp vlalvswlwv
      181 phdplgmsgw rwvvllggsg avfvwwlqsr lpesprwlah tgreaeaeav lqrleqaver
      241 esgrplpavp tpvaaatvka taaqrapsmw darhrgrttm liafnaflsi gffgfsqwlp
      301 tllaaqgasv tkslwyafvi afaypvspfv aglladrver kwlivasafg valfgtafam
      361 saqapfviaf gllvtlsntv lasngtayqs evfpteirgr algfvhsigr ltgiassfiv
      421 allleragvp avfvliggsm livmvsigvf gprtnnrald eiadgagnaa alrglaeapt
      481 ghvdgrrklg
//
LOCUS       WP_175893597             281 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia cepacia].
ACCESSION   WP_175893597
VERSION     WP_175893597.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..281
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30367
     Region          10..257
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(24,105,107,109..110,138,189,210,213,226,228,257)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 matltfprqq vgdftitais dgyltasldf lsnidpadas nmqrdagqka peavhincyv
       61 vrgagrtvli dagaggfrqw ggqlgtnlal agiepaaidt illthahpdh vgglvngage
      121 iafpnaelvv hrrevgfwqd dvnlsraser argnfavarr vfdaygdrlr lfddgqvlpg
      181 idalpipght dghtgylles rdqgllvwgd vvhfphiqiq rpevsiafdh daslaaatrs
      241 rlldqvsseg lliagmhlge rgfariertn ggyrlryere e
//
LOCUS       WP_175893591             254 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF899 domain-containing protein [Burkholderia pseudomultivorans].
ACCESSION   WP_175893591
VERSION     WP_175893591.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..254
                     /product="DUF899 domain-containing protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28280
     Region          1..251
                     /region_name="COG4312"
                     /note="Predicted dithiol-disulfide oxidoreductase, DUF899
                     family [General function prediction only]"
                     /db_xref="CDD:443453"
ORIGIN      
        1 mtthptgtrd ewlaarisll daekaltrqs delarrrqal pwvrvdktyr fdtadgpatl
       61 aglflgrsql lvyhfmfgpd yragcpscsa ladgfdgfav hlanhdvtla avsraplakl
      121 layrqrmgwr fpwassvgsd fnfdfnvsft etqqragdve ynyaragham dmdppppava
      181 qfaatcgtda atysldrpgm safvcedgvv yhtystyarg ldglwgmyqw ldraprgrne
      241 tgvwwrrhde yalg
//
LOCUS       WP_175893616             308 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175893616
VERSION     WP_175893616.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..308
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=32053
     Region          43..294
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mssprlsrrh ftiacasasl aactsfggks rpdnasgaaq phekpvkigi algggaargf
       61 shigvlkale argisieiva gtsagsvvga lyasgmnalq inkialdmdq asisdwalpf
      121 rsrgllqgva lqnflnktln nrpiekmakp lgivatdlqn gqpilfqqgn tglavrascs
      181 vpsvfepvki gnreyvdggl vspvpasfar kmgasfviav disarpdgaa tnnpiemllq
      241 tftimgqtik tyeldkyadv virpnlnamg gsdfnqrnaa ilageeavar impelqrkla
      301 aargvaaa
//
LOCUS       WP_175893619             452 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175893619
VERSION     WP_175893619.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..452
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48230
     Region          17..411
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(24..25,28..29,32,64,114..115,117..119,122,142,
                     145..146,149,268,271..272,275..277,280,308,312,364..365,
                     369,373,389,392..393,396..397,400)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtnssskvrk yvgltgicia sflgcidltv vntilpaigr dfsipiqttq witsifmval
       61 safmvpvatl adnlgrkkll ivglvifgaa sllagiahqf wllvgfrflq gigcailytv
      121 sgaivsytfd eneqgkalgi lfgangvgla lgpiigglfa galdwhdafl inipfiaisl
      181 alcawaipef kaqarkridv tgclllvvgl ttlvsylsvd gsglnlwllp vslvalalfv
      241 whelrtrdpi vefhffrepr flsallatff laffycivll tlpiffstql hksditigly
      301 llpatitfsi asswiggrse rlgpsrvivt glslfvvasv llsivagqpd aawfvvplll
      361 fgigwgailg pstlvalgal prekaavamg tswtvhnvgg asgiafaifl mrqvddfrhg
      421 yqtlmlalaa iilaagalyh vlsresvava id
//
LOCUS       WP_175893670             265 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease signature motif containing protein [Burkholderia
            cepacia].
ACCESSION   WP_175893670
VERSION     WP_175893670.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10052677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..265
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30677
     Region          13..61
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(33,35..37,39,48..49,53..54,57,61)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 mvrvtipeev aaevmfladr tccicrdprr kveihhidgd pshndinnls aickdchsda
       61 httqafarnl tpalirkyne swreivriri mpggeeaeal eyraqillei yliphhwlnr
      121 lldlfeggvs dedaagpnrw eylervvkpt yskgawehyr plfehasdsl skdlerivmi
      181 ygdalkprik lqvqrttrcl rmeragylfl pklirqepdi pidrffqlrf sssifslstl
      241 stmadrerei lepnksgqnp maldf
//
LOCUS       WP_175893690             701 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cepacia].
ACCESSION   WP_175893690
VERSION     WP_175893690.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..701
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75729
     Region          7..701
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 msrrnwaaap maivvgatgv gaadaqeatl ptieisgqra sapfrtrdst satrgeadvm
       61 eipfavssvd akliqtvaat rgddlydwva gvsrqnnfgg lwdnyavrgf agdgntsgtd
      121 ylvngfswnr gmsvprdtvn lermevlkgp asalygrgdp gglisyttkq pqfarantig
      181 vsagsygalr etldstgpvt kslayrfvam nenngsfrdt vsskrylfap sftwdigadt
      241 tlhyefesar qrapldrgvl avngqlgaip asrflgeprd gdydvrntgh qftlehrvda
      301 nwsvnagfaq rttdlsgrss eafalqpdgr tlwrryrqva fhsndlqgri etagkfstgg
      361 ightlvlgvd ayrfnydqfv arstptaaap yaidifdpvy gqpaptprta tnllerddgq
      421 glyaqdtlaf gphwkilagl rwdrfhqsve nrlkgttssq vqtalsprig ivyemspals
      481 lyantaysfr pnngadvdgr afdpekghgy eagakwagar wlatvaafyv nkrnvltadp
      541 antgfsraag evrsrgvefe wngdlghgvr glvnlayvda evthdavltp garlvdiprl
      601 sgsalllyet avpfadkaga gagliyvgrr agntantqdg felpayatvq lngyvqvnkh
      661 lrasvvlnnl fnrttyvssy nslwvtpgap rslfaslayt f
//
LOCUS       WP_175893691             203 aa            linear   BCT 11-JAN-2025
DEFINITION  cysteine hydrolase family protein [Burkholderia pseudomultivorans].
ACCESSION   WP_175893691
VERSION     WP_175893691.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..203
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21038
     Region          24..192
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mqhptirtla gataptsida artallvidf qneyfsgrlp ipdgaralgn aqrviafadr
       61 agipvfhvqh vgpadsplfa dgsdafrfha dlqpaphhtv vqktsvsvfp ttdidarlka
      121 agidtlivtg lmthacvaga ardavplgya vivvddacat rdldvaaggt vphdalhrat
      181 laaltdvfgd vltteqvlal hva
//
LOCUS       WP_175893740             587 aa            linear   BCT 11-JAN-2025
DEFINITION  fatty acyl-AMP ligase [Burkholderia cepacia].
ACCESSION   WP_175893740
VERSION     WP_175893740.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10148874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..587
                     /product="fatty acyl-AMP ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=62470
     Region          18..567
                     /region_name="FAAL"
                     /note="Fatty acyl-AMP ligase (FAAL); cd05931"
                     /db_xref="CDD:341254"
     Site            order(168,171..176,178..179)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341254"
     Site            order(195,217..219,292,295..298,323..327,332,385,445,456,
                     459)
                     /site_type="active"
                     /db_xref="CDD:341254"
ORIGIN      
        1 mtkcastihr liesledvag athrmtfvde agneagityr rfaeavfhqa galreldvre
       61 ndlvmlalpa svehavamma cvmtgalpct vpvparrata grqvvdvace lyrprlviaa
      121 daqaaawrdd afpaastrvv dldtlssaad agaralisak sgrdphhvql tsgstshpka
      181 avlshenvia nvlgiggsvr fdiaagdgta swlplyhdmg lltllsnlhy rapllmmqpn
      241 sfirnplgwl kriasaratt tsvptfalry cvrrfnaaam egvdlsacrn ifiggervdd
      301 atlrdfaatf apyglaasal qpcygmaest lavsmhrawh egtvdgapyv iadtldrral
      361 ierrdaqpaa andgadaete tvlamgtpid gmafrilddg dhalanravg evairgtsvm
      421 lgylnpddgs iaapltadgw frtgdigyva dgqlhilgrk keviiirgsn yfphdieeal
      481 ashrtlrknt ciafglpdpe tgterlvvai earpadatpq traecqqlla srigfaaqdl
      541 cfvepgslpr ttsgklqrlk crdlyangal pvihaaaave agqgaya
//
LOCUS       WP_175893742             405 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175893742
VERSION     WP_175893742.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 405)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..405
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42487
     Region          18..230
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          144..>322
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnwstfawrn lwrnkrrtvl tmamigvaaf asslalgyvi atfdavregs idsgvghvqv
       61 lhhgyldlig erplqyglta deqataarav aalqgvatta rgidfdglis ngdlsygfvg
      121 egiepnrepp gffdyhtvls grylsptnag tevvvgaela rklgvhvgsv vqlmastahg
      181 ginatdaqiv gvmstgnkdv derivnvtfa aaqallrtdr asriavflsd tahtpaaaat
      241 lraalpaldv ktwdqlvsly hqvvalyknq fsvfgailcv tillsmsnwi lmsiverrre
      301 istlralgvp aatvrgvliq etaflgllga aagiaaallt mvalnhaqih lpappgrvkp
      361 illeftvspa avaavegafv vlgvaaalla tlglakrnil eglap
//
LOCUS       WP_175893776             515 aa            linear   BCT 11-JAN-2025
DEFINITION  FGGY-family carbohydrate kinase [Burkholderia pseudomultivorans].
ACCESSION   WP_175893776
VERSION     WP_175893776.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..515
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=55218
     Region          3..448
                     /region_name="ASKHA_NBD_FGGY_RrXK-like"
                     /note="nucleotide-binding domain (NBD) of Rhodospirillum
                     rubrum xylulose kinase (RrXK) and similar proteins;
                     cd07804"
                     /db_xref="CDD:466806"
ORIGIN      
        1 meyvigvdig tqstkallvd rhgtivarrs agyrpdtprp lwaeqwpqvw fdavldciag
       61 cvddaraqgv padairavcv sslyggsgvp vdsemrpihp cliwmdrrat aevdwvngnv
      121 nvgrlraitg ngvdsyygft kmlwlreqrp eawanvryfl ppnayviyll tgevavdhss
      181 agnlggvydv arrewsddal dmlgipatmm perlvdstei vggllsqwte rlgllagtpi
      241 vaggvdaava tfaagatrtg qhvamigtsm cwgyvsqhvd arhglvsmph vfdgqrdlyv
      301 fggaitagas vawfrdqfcr aeidaaralp hgdphvllee aaarvpagad gvlflpylmg
      361 erspvwdaka sgafvglsla htrahlyrav legvafalrh nieagrrgaa vlddrlivvg
      421 gaahsalwmq iiadvtgfpv wtieedveaa mgaallaavg aglvsrqdaq ggwvtlvera
      481 rpdparagly aarfelytss ypalrpimhg lqaps
//
LOCUS       WP_175893790             210 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia cepacia].
ACCESSION   WP_175893790
VERSION     WP_175893790.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..210
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23082
     Region          1..210
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mtcvlyiegs pnkaysasid vcnafldayr hahpdheirk ldvwdlampe fdedalaaky
       61 aglsgtaltp sqavawqrie qlaapfhaad kflfgvplwn fsipyklkhl idaisqkdvl
      121 ftfddvgftg klagkkaavv yarglgyqsp gsftpaaefd lqrpymetwl rfvgvtdvtg
      181 ivvertlfga dgkvdrsrai dearsiargf
//
LOCUS       WP_175893796             225 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175893796
VERSION     WP_175893796.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..225
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24451
     Region          13..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mssdedadag qkayhhgdlr raiietaldt lqeqqgwqft lreiarranv shsapyrhfp
       61 dkaallhela ligfdrlrde laasidpaas apdvllalay ahlafgqrnp dlyrlmfaad
      121 agepsdihld prvqapfllv vnilehgqra gtirarpalg qatacwahlh gltmlaidrr
      181 lvrekvgdha iedalttlld glvlpaspar aaktktktka ktkgs
//
LOCUS       WP_175893798             239 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia cepacia].
ACCESSION   WP_175893798
VERSION     WP_175893798.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..239
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26600
     Region          1..206
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mkiisgplsm fgakveiaah ekgidfelvm apfsqrrgyd pkhpdvvrin pkrqvpvlmd
       61 gdlelfdstq ifeyfedlkp dpalwpahpa araiarqleh gsdeiyfphv vrlmgleatp
      121 ddpaaraard eaaryyrrme reladrefla gaysyadiaf ymaqlfgark gapmtdetpr
      181 llawrermta rpavrkvaga magylasige avpdflrgvd llpsgadrrg etafgddcr
//
LOCUS       WP_175893799             736 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia pseudomultivorans].
ACCESSION   WP_175893799
VERSION     WP_175893799.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..736
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=77371
     Region          57..>192
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          200..728
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mtieldnrgs vqpsrrtflk aagaaaavsl tigfewaglg rralaatapa agfapnaflr
       61 itpdgtvtvi akhvelgqga ytgiativae eldadwssvr vesapadakr yanlafgtmq
      121 gtggssamsn swqqlreagg karamlvsaa aarwkvpase lttangvvth aksgntaayg
      181 tlvadasklp vpdkvvlkqp adfklighri prvdasaksn gtahftldtt fpgmrvallq
      241 rpprfgatvk sfdataakav pgvvsvvqvp ggiavvgtgf waakqgrdal kvewdetnae
      301 krgsdeimre yrqlaakpga sarkdgdada aiagaarkis atyefpylah apmepldavv
      361 rltkdsceiw agdqfqtvdq gnaakvaglk peqvqihtly aggsfgrran awsdyvveav
      421 siakalgadg kpvklqwtre ddiqggfyrp myfhkldagl tadgrlvgwr hrivgqsila
      481 gtpfeafmvk ngidatsveg aanlpyavpn vsveltttkv glpvlwwrvv gsshtayave
      541 afideaahaa gkdpylfrrd llakeprmra vlelaaqkag wdpakplpeg rgrgiavaea
      601 fksyvaqvae vsvdadgkvk vervvcavdc giainpdiva aqmeggigfg lgaamhsait
      661 lkdgrveqrn fdgyhvlria empkvdvhiv psaeaptgvg epgvapigpa vanaifaatg
      721 krhyvlpfds gdsaka
//
LOCUS       WP_175893811             339 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Burkholderia cepacia].
ACCESSION   WP_175893811
VERSION     WP_175893811.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..339
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36963
     Region          13..323
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(16..18,48,53,79,142..143,183..184,207,236..242,278,
                     295..298,303,306..307)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(48,53,79,142)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 msledklpgn kilgfgtapl gnmfrnipda eaaatveaaw qhgiryfdsa pfygaglaei
       61 rlgdalanhp rdeyvlstkv grvildeied vsardlgekg glfehgrpnr ivndytadat
      121 lrsiedslkr lrtdrldivw vhdiaqdfyg dewlaqfeva rkgafrvlsk lreegviraw
      181 glgvnrvepi elvldlaepq pdgmllagry tlldheralq rvmpaaaaqn vgivvggpys
      241 sgvlaggthf eyqkaspeil akverikaia trydvpikaa alqfsmshpa tvavipgasr
      301 periaedqaa lnvvipadfw remreqglia anaplpagr
//
LOCUS       WP_175893857             245 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175893857
VERSION     WP_175893857.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..245
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=24996
     Region          1..245
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mlalviiagl waglqntlag ggsfvtlpal ivsgmsplsa nitstvalfp aqittgwasr
       61 hmvqgagrls fralfaisvv ggalggllll ktpssifsrl vpwlvlfati vfawgsffrr
      121 pgdaaahlgp vpaaisqfli aiyggyfggg igflmmaalt maglsprham stknalagvm
      181 nasavvlfvt sphlhwgaal algggaiagg llgtwalhrv nervlrigiv cigvaltvgl
      241 fvrpi
//
LOCUS       WP_175893888             379 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175893888
VERSION     WP_175893888.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..379
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41887
     Region          26..362
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 mstpvtshda yaehapevlf rvvnrvalit lnrpaalnal syamigelaa lfercrhddq
       61 ivavvlrgag ekgfcaggdv rqlyrmvaqr etwlpffvde yrldhaihtf pkpvvalmdg
      121 vtmgggmgla qgaalrvate rskiampetr iglvpdvgat hflarmpvel elyvgltgat
      181 lsgadaltak ladlcvpssw ldtfetries vkwdsdalpa lrrvfeppcn vvphaaldgq
      241 mawivrhfdk rstverivat lkqdlardel srehrqwlqa tldaltghsp tmlavtreal
      301 lrgrqmtlae sfrmelgiva raieegdfce gvrahlvdkd rkprwapasl velraervrh
      361 fltspwklfa hplaylgta
//
LOCUS       WP_175893889             509 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Burkholderia pseudomultivorans].
ACCESSION   WP_175893889
VERSION     WP_175893889.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..509
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53629
     Region          16..492
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(73,75,79,82,86,119,122..123,132..139,144,147,150,
                     243,247,250,253,255,428,430..431,433..434,437,440..441,
                     443,445..448,457,461,463,477,484..489,491..492)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(159..162,170,185,188,218,235..238,241,259..261,293,
                     393,395,421)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(162,259,290,293)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 msanptprtg qdvptvklli dgafvesats ewrdivnpat qqvlarvpfa tvaevdaavq
       61 aahaayatwk ntpiaarmri mlkfqdlvrt nlpriaktlt aeqgktipda egdifrglev
      121 vehacsvgtl qlgefaenva ggvdtytlrq plgvcagitp fnfpamiplw mfpmaivcgn
      181 tfvlkpseqd pmttmelval aleagvpkgv lnvvhggkev vdaicthplv kaisfvgsta
      241 vgthvynlgs angkrvqsmm gaknhaivlp danreqavna lvgaafgaag qrcmatsvav
      301 lvgaardwlp divekaktlk vnagaeagtd vgpvvsrgak arilslieag vkegaklvld
      361 grdvqvpgye ngnfigptif sgvktdmsiy theifgpvlv vmevdtldda ialvnanpfg
      421 ngvglftqsg aaarkfqsei digqvginip ipvpvpffsf tgsrgsklgd lgpygkqvvq
      481 fytqtktvta rwfdddttag pvnttirlh
//
LOCUS       WP_175893910             433 aa            linear   BCT 11-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175893910
VERSION     WP_175893910.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..433
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46403
     Region          5..431
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 mslnddatfw rnarqhliry ggtfepmive raqgsfvyda dgraildfts gqmsavlghc
       61 hpeiaavige yagrldhlfs gmlsrpvvdl atrlacltpd gldralllst gaesneaair
      121 maklvtgkye ivgfaqswhg mtgaaasaty sagrkgvgpa svgsfaipap fmyrprferd
      181 gtydplaeld yafdlidrqs sgslaafiae pilssggiie lppgymaalk rkceqrgmll
      241 ildeaqtgig rtgtmfacqh dgvtpdiltl sktlgaglpl aavvtsaqie erahelgylf
      301 ytthvsdplp aavglrvldv vqrdglvara hamgdrlrrg lldlmerfdc igdvrgrgll
      361 lgveivkdrr tkepadglga qitrecmklg lsmnivqlpg mggvfriapp ltvseaeidl
      421 glslleqaie ral
//
LOCUS       WP_175893895             196 aa            linear   BCT 11-JAN-2025
DEFINITION  flavodoxin family protein [Burkholderia cepacia].
ACCESSION   WP_175893895
VERSION     WP_175893895.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..196
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=20767
     Region          11..189
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mtphsapvnt vvvfhsgygh termasavae garavlvaid segnipadaw etlagadail
       61 fgsptymggp swqfkkfada sskvwfeggw rnkifggftn sasingdkln tleyffllag
      121 qhggiwvsmd ikpanvkasm rddlnrmgay igpmaqtpad aspgemspgd letarrhgmr
      181 vatiagqfrs gtlrgn
//
LOCUS       WP_175893911             294 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia cepacia].
ACCESSION   WP_175893911
VERSION     WP_175893911.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..294
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=30907
     Region          9..270
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mtsdptssta fvfagggslg aievgmlrel vasgerpdcv vgasagaina ayfagqpded
       61 gvamlaalwc rirrqdimpf smrslvamll rnrphlvead alrlllernl pyrrieqaal
      121 plhivatdvl ngrevvlsag pvvdavqasa aipgvfpsvs iggvelvdgg vanntpisva
      181 ialgvkrivv lpagfacalr vpprsaiaha thaltlviar qlvrdlelyg araqihvvpp
      241 lcpldvssyd ysqcaqlidk aaertrawid sgglaqceip gqlrehdhaa vlsh
//
LOCUS       WP_175893925             430 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia cepacia].
ACCESSION   WP_175893925
VERSION     WP_175893925.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..430
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46538
     Region          38..419
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 msfhpgtpla rrarrrapml waallvagaa haqqppftld aalqsatdhs asmqaaqasv
       61 rasseaavka gqlpdpmlka gidnlpvngg qrftvgqdfm tmrrigieqe wvsgdkrrlr
      121 salaneqvgr eragylaqla svrqqtataw lnavyakqal alqqalldhm nhefdatkas
      181 yrgakasaad vvqaramlaq tqdqwlkarq vyqtalials rwtavpasdv tgtppapesf
      241 vsslppdelr vsqpalitaa ddiavaeadt avanserrpn wtwevayqqr ggaysnmvsv
      301 gvtiplplnr rnrqnrdvae kaelatkarl vyedtlrqvq adirtqsetl asgrerianl
      361 sasllpaadq rvqlanaayr agtgsladtf aarraqldaq lqvldlrrdv sqtwaqleyq
      421 vvpstmaaaq
//
LOCUS       WP_175893966             484 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia pseudomultivorans].
ACCESSION   WP_175893966
VERSION     WP_175893966.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..484
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51924
     Region          1..421
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfeslglae plvkavnelg ytsptpiqqq aipavlgggd llagaqtgtg ktagftlpil
       61 qrlhtfyadh rgakravral iltptrelaa qveesvrays kylklrstvm fggvsinpqi
      121 dalkrgvdiv vatpgrlldh mqqktidlsd ldilvldead rmldmgfihd ikrvlaklpp
      181 rrqnllfsat fsdeikalad slldspalie varrnttaes vaqkihpvdr drkrellthl
      241 irehnwfqvl vftrtkhgan rlaeqltkdg isamaihgnk sqsartrals efksstlqvl
      301 vatdiaargi didqlphvvn fdlpnvpedy vhrigrtgra gatgeavslv cvdekqllrd
      361 ierlikreip qeviagfepd pnakpepiqq rrgqqprggg gggggnrapr aggsaqpaak
      421 rdgnakregt qqpkaakpra sggnggnsgn ggrpagggng araangnaah pnrnrssrsg
      481 qrgh
//
LOCUS       WP_175894031             228 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175894031
VERSION     WP_175894031.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..228
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24368
     Region          5..>55
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkvsktqvae nrlailqaaa rlyrergftg vgvaditrea glthgglyrh feskdalaae
       61 aaeyafewkl seletpdada nadadgflrt gvanylspqh rdsvgqgcpv aalaadaare
      121 tgaiadafaq gigrymtlfa qrrpdgteaa qiepedrvra ismlstmvgg lilaratarg
      181 lpelsdeila tlrdhlaatw gldeanvdgr dwksiaegan ppephrvr
//
LOCUS       WP_175894058             310 aa            linear   BCT 11-JAN-2025
DEFINITION  ketopantoate reductase family protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175894058
VERSION     WP_175894058.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 310)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..310
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32424
     Region          1..310
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mriailgaga mgslfgglla esgedvtlid vndahldair rdglridddr gerridtlqa
       61 lrpdaanasa gtpfellivf tkslhtrsal dgvralltph thvltlqngl gnvetlnafv
      121 plerilvgvt twpadlagpa hvhshgagti rmmtadgaas pfaaavadal sraglactld
      181 advwaaiwek vafnaalntl cavtrctvdq lgehhdgprl aqaivaetaa varakgiavd
      241 aariarnveh airehrghrp smlqdvlagr rteidaisgk vvaaarevgl avphtetmlg
      301 lvrlidaqag
//
LOCUS       WP_175894100             205 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia cepacia].
ACCESSION   WP_175894100
VERSION     WP_175894100.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..205
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23139
     Region          1..192
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mklygfagtr sqralwglke ldadfefvsv nllqgehkrp eflrlnpagk vpvlvdgdlv
       61 ipesaaivly ladkypekal lpvdpalraq ayrwvmfavt eleqplwrit rhsflyppek
      121 rspadielar ddfrttaail dkhlegrefi vgdtltvadc vtaylidwag ecnliesfpq
      181 lraylerlya rpnapqriad arkaa
//
LOCUS       WP_175894140             374 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Burkholderia cepacia].
ACCESSION   WP_175894140
VERSION     WP_175894140.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..374
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37442
     Region          17..364
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mtgfidtftl ggpgptiaik dtidiaghpt raasralada ppaaqhadvv rllldagwqi
       61 agkanmhela fgmtgindyt gtpvnpqdat ripggsssgs aslvglgtvd aalgtdtggs
      121 irgpaaccgv aglkptfgrv srrgvapadt tldcvgpfar dirtlaavma aiapgfdraq
      181 aaasvagcti aqirveadpa iaaaldaavr asglrshalv ldempasfaa gltvinaets
      241 rafghlvdtg klgadldarl rtaatttpaa laeaeavrar ftaqvdaale ladalvlptl
      301 palpitlqqa rdgvsviams slirpfnlsg hpalslplpl agsplkaglq ivgrkgader
      361 vcaiaahfea alaa
//
LOCUS       WP_175894148             344 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175894148
VERSION     WP_175894148.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..344
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=38001
     Region          34..93
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          124..324
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(139..140,142..143,146,150,152..158,250..255,
                     261..262,264..265)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mthaatgrsa aptrvesaph dsdlselrvq dldlnllktf ravyeerhvg raalrlgvtq
       61 psvshalgrl rlmfrdalfv rtgtgveptp raqrlaisvd kalailqdvl degsrftpds
      121 tqrvfrlhms dfaasaflpt llaafdrrap gavietlhvd ecqlnvales gridfalghf
      181 adasshfqrt allhercvll mprrtaqrva lpddyvldgd apetlrfvav tshpqsmqll
      241 erhglmprvr aalpdfmvvp allrdgdyal ilpetiaitf aarqpcalye iagagewavn
      301 aywhrrfdad pghrwlrall lelfnigela pfdawlapqp paca
//
LOCUS       WP_175894151             368 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD/NADP-dependent octopine/nopaline dehydrogenase family protein
            [Burkholderia cepacia].
ACCESSION   WP_175894151
VERSION     WP_175894151.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13367875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..368
                     /product="NAD/NADP-dependent octopine/nopaline
                     dehydrogenase family protein"
                     /calculated_mol_wt=39406
     Region          1..>107
                     /region_name="GpsA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0240"
                     /db_xref="CDD:440010"
     Region          187..333
                     /region_name="Octopine_DH"
                     /note="NAD/NADP octopine/nopaline dehydrogenase,
                     alpha-helical domain; pfam02317"
                     /db_xref="CDD:426715"
ORIGIN      
        1 mkvcvlgggh gchaaaidlf ekghdvtwwr rdrepharlr elrvlnvtdy rgkrtvplgd
       61 apgairlsgd laaalrgarl vvvplpatsh dalaaqvapl ledgqvvflp pgtfgsvvfa
      121 raaadagnrs rvafaetgtl pylvrrhgdn dvvisayatr lptgvfpana sgwafdvlra
      181 gypsvepved alsgalmnag pvihpplilm nagplehfda wdihnegtqp sirrvtnald
      241 aeriavreal gypaphfpla dhyatdgdew mygrgahgkl tdsgdwreki dlrthrymle
      301 dtrlglsfiv scgrragvpt pvaqgllsia savavrdlya egrtlerlgl aalsmdamra
      361 lldagyaa
//
LOCUS       WP_175894161             360 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175894161
VERSION     WP_175894161.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..360
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39468
     Region          1..358
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msfltltdlt ktfgeltava dvnlsveqge fvsllgpsgc gktttlqmia gfvdvtrgri
       61 sldgqdithl kpnrrglgiv fqsyalfphm svaenvgfgl dmrgvdkaer aeriraalal
      121 vrldalahrf prelsggqrq rvaiaravvi eppvllldep msnldaklre dmqfelraiq
      181 rkigtttimv thdqsealsi ndrvvvmeag ritqtdtpyr ayerpenrfv sqfigkanll
      241 pgtivahdgd airidlghdl aetgrlahlp arerdmrigd avsvcirpek lrlcapdagr
      301 faatvtsrff lgsqwlyrvd salgevlvcc qnegaeplae gapvgidwhs davrvmrrea
//
LOCUS       WP_175894171             390 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia pseudomultivorans].
ACCESSION   WP_175894171
VERSION     WP_175894171.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..390
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44402
     Region          7..390
                     /region_name="COG3146"
                     /note="Predicted N-acyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:442380"
ORIGIN      
        1 mkheridyrt gilsspaeva adewnallar daqptpflrh efldalhvar cavdetgwsp
       61 hfvtltdart grlaaaapvy akqhsygeyv fdwawadayq rndlpyypkl lcavpftpvq
      121 gtrllaadad arrrlaatll afaeqsdvss lhvlfptgge arllesmgmm lregvqfhwi
      181 ndgyrhfddf lgtleqkkrk niraerrkvh dagvrfrrlt gdrigdadwr ffsrcyrqty
      241 rehfsspyln ldffrtigat mpenlllvia eadgrpiasa lavyrrgehg ggtlygrywg
      301 aieqvpclhf etayyqllef cieagldtfe ggaqgehkla rgflptvths ahwlahpafs
      361 davarflere tehihayvde lrehdpfrra
//
LOCUS       WP_175894191             743 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cepacia].
ACCESSION   WP_175894191
VERSION     WP_175894191.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..743
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79545
     Region          40..743
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mtvnrttasp arrrrakvgl gvgvgitlfa aqaaaaqgdt papdagaags atlptitvsg
       61 ergnalrart asvaglddap lrdtpasvsv vtraqlddqq akrlsdvvrn dasvvndyap
      121 vgyfegfair gfpvdlasai ridgltvsge qnvplenker veilkglagi dsgvvapggv
      181 infvtkrsan vasvtggvds rgstsaavdl grrfgpdnqf gfrinaaken mhsyidgtng
      241 rrtfgsiaad wdispraslq fnaefqqwiq rsapgyqllg gtvvpsiktt skalgtqpwa
      301 kpvttdalnl narfdyqfnd dwkayiaagr srtmiddnsa faygcsyaas ctagatspff
      361 fgangdydvy dfrspgeyrr nddlravttg kfatgplrhe ltlgvsvqrr vvhmatavyd
      421 yvgseniygp dvtfapspnt pgpsypqlds wqygvfgldr isvgehwqvl aggkevllrq
      481 rswssldgda thtdrsvflp qvalvykpvn vlslyasysk alslgdqapv ratnayaflp
      541 pveshqfevg akydwldrls ltaavfsisk pfqfadpdas gttytfvqrg tqrhqgielg
      601 aagrvterlg ltasvaaira raydsgspay eghqvinvpa lraslyadya vpgvaglnvl
      661 ggveysaarn aneegtaqvp awfvfnlgar yttkigghrt vlrvsvdnlf nkfywrdage
      721 qqgdaylfpg aprtarvslt ydf
//
LOCUS       WP_175894198             443 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia cepacia].
ACCESSION   WP_175894198
VERSION     WP_175894198.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..443
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46067
     Region          112..433
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mlklnlavav vfamavtaha qpslspgpap aasgsaapig apppdarpst sltladalaa
       61 aarnnpalrg aradvdasag almqagarpn pevsflqesf rraertstvl lnqtielggk
      121 rgarldvasy greaanasld eqgavvradv iaafygllaa qrqlqvtees aaiaarsadl
      181 asrraqagkv spveatkahv aaagvqievv targhvevar eklnavmgea rdgrlavlgd
      241 leavppvesl paltaqldda plariaraem lrsnaavsle rarripdvti sagvkrvttg
      301 gvpdnqavvg vsipiplfnt nkgalleath kaaranadld rertrlrlel tqayanfeaa
      361 aqeaqrlkdd ilpaarvald amsrgyelgk fsfldvldaq rtlfqgqsqy vraladahta
      421 radigrlvgt plaplvplvp vtq
//
LOCUS       WP_175894213             222 aa            linear   BCT 11-JAN-2025
DEFINITION  O-methyltransferase [Burkholderia cepacia].
ACCESSION   WP_175894213
VERSION     WP_175894213.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..222
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23018
     Region          43..220
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mnqehwnqvd ayfsatlvps ddaldaalaa sdaaglpain vapnqgkllq llatirgarr
       61 ilevgtlggy stiwlaralp pggtlvtlel npehakvatr niaragfaev vtvvvgsakd
      121 slarlvdage apfdfifida dkdnnpvyld aalklsrpgt vivvdnvvrg grvadpgnre
      181 pdvagvrdgf arlaaapnvt ttavqtvgqk gwdgfsisiv gv
//
LOCUS       WP_175894268             185 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175894268
VERSION     WP_175894268.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..185
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19378
     Region          40..178
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msrypvhtpe sapaqsrpvl arlrqtfgti pniaatmags pvlingfigl feqvhssslt
       61 epqiqtlllt navtnasewp aafhtalalt agvsradvda irhgalpgda qlsalsalar
      121 tliekrgrva eadrnrfada gfsaeqilev vavvaastit nytagvtrpp leapfdafaw
      181 hapta
//
LOCUS       WP_175894276             437 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pseudomultivorans].
ACCESSION   WP_175894276
VERSION     WP_175894276.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..437
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46274
     Region          24..429
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,156,
                     159..160,163,254,257..258,261..263,266,294,298,356..357,
                     360,364,380,383..384,387..388,391)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mhledsagpr qtahattaap tavrwrifwl llllssinyi draslsvalp iistefslsp
       61 amegvllsaf fwtyalmqip sgllvdrfka rtivglatig wgacqavaaa cfswvplllt
      121 rlglgiaesp impagaklag awltpsergr gaalldggap lgsacgaiii taliaglgsw
      181 rlafvvagvg timvgiaaww yirnhpseha gvnaaelehv tahaaaartg epkasvpfre
      241 llrdrsvlcm faswacynsv fyglmtwmps ylhkahgfdl kqmggatfii fmcgfvgelf
      301 ggwladkwra aggapnrvmr smfsvagfva aaailsvsfa kglvsvvvll sialffirwc
      361 gmfwgvpatl ggqsraglla gamnfsgniv gvivpiligl ivqftgtyfl almffvvaaf
      421 glavcaslid yrdrgld
//
LOCUS       WP_175894283             482 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175894283
VERSION     WP_175894283.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..482
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48653
     Region          21..421
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(28..29,32..33,36,68,118..119,121..123,126,148,
                     151..152,155,287,290..291,294..296,299,327,331,383..384,
                     388,392,408,411..412,415..416,419)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mdtplpssaf ppalarvvat vstgfvvtql dvtivniala hlagdlrlpv aglqwvvday
       61 tlafavlmls ggalgdrfga rrlyiaglvl falaslacga asapamliaa ralqgvgaaa
      121 mlpnslalln dacrhdprlr aravgwwtaa gsisiaagpv vgglliaawg wrgiflvnlp
      181 lcaaglaaaf awiparraaa tpaapsrsvr aldlrgqfia iamltaltga viewrplgft
      241 hpvvaggfal atlaalafva vetrtatpml plslfrhrtf saavlfgisv nltyygtvfv
      301 lalylqrarg esalqaglaf lpltggflls nlasgrvvar hgprapmlag alvaalgygs
      361 lhfidastpl avllvpflli psgmgfavpa mttavlasva peragiasav lntarqagga
      421 mgvaafgala ggggaaqvvd glrietavsv allaaaalla tlvrpdahrg assvrqavpa
      481 ad
//
LOCUS       WP_175894356             254 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175894356
VERSION     WP_175894356.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..254
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26727
     Region          1..254
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mthgahivan gvtlrygsrs vlngvdlsva pgelvallgp sgcgkssllr aiagltrtas
       61 gtirvdgepv dgprpvvala fqdpcllpwl tvernvgfgl tfarqphltr adrkervtna
      121 laavgldhar halpsqlsgg maqraalarc larapralll depfgaldev tradmqqlli
      181 aavrntgasa llvthdidea llvadrivll gkrgtlvgrw tvelpqprht qvrslgelri
      241 silqalqnsi saaa
//
LOCUS       WP_175894211             241 aa            linear   BCT 11-JAN-2025
DEFINITION  ZIP family metal transporter [Burkholderia cepacia].
ACCESSION   WP_175894211
VERSION     WP_175894211.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Dempski,R.E.
  TITLE     The cation selectivity of the ZIP transporters
  JOURNAL   Curr Top Membr 69, 221-245 (2012)
   PUBMED   23046653
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Guerinot,M.L.
  TITLE     The ZIP family of metal transporters
  JOURNAL   Biochim Biophys Acta 1465 (1-2), 190-198 (2000)
   PUBMED   10748254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..241
                     /product="ZIP family metal transporter"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24338
     Region          27..235
                     /region_name="ZupT"
                     /note="Zinc transporter ZupT [Inorganic ion transport and
                     metabolism]; COG0428"
                     /db_xref="CDD:440197"
ORIGIN      
        1 mtptaklall tlppvlaacf galaaawrap gpatssviqh ftggivfaaa alellpqdra
       61 halfpvivgf vlgialmlai ralsgaietr fedarllvsl vivtaidlvi dglvlgiafs
      121 astesgiilt ialtlevlfl alsvsaalaa agigrmlsiv vpvglaalls iaavagnaaf
      181 aglpaniyaa llglgtvall ylvteellve ahevpetpfa taaffigfiv ffliegsvka
      241 g
//
LOCUS       WP_175894361             546 aa            linear   BCT 11-JAN-2025
DEFINITION  S8 family peptidase [Burkholderia pseudomultivorans].
ACCESSION   WP_175894361
VERSION     WP_175894361.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..546
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=54714
     Region          235..513
                     /region_name="Peptidases_S8_13"
                     /note="Peptidase S8 family domain, uncharacterized
                     subfamily 13; cd07496"
                     /db_xref="CDD:173820"
     Site            order(241,309,313,380..382,408,410..411,481)
                     /site_type="active"
                     /db_xref="CDD:173820"
     Site            order(241,309,481)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173820"
ORIGIN      
        1 msakrfnfas ararhahmla gvlsaavllp lagcgggggd gsspsssnas paptpapttp
       61 ttppassssn acatqqaavq maaqtvapte ppidhlivrl ktstathama avdtasrfda
      121 viqrsmtrws aptataraya sgvapaalnv qvertvsnga avlslgqria atdatalaqa
      181 faadadvdya epdhpmkvrd tpsdpdysqq wylsdptagi dmppawnvtk gspavvtavl
      241 dtgyrphadl kdnllpgysf issastsnng ltrgpdasdp gdwvtqqeid nasgpfyhca
      301 aepnastwhg trvmgvvgan anngigiagv swlgrilpvr vlgkcggtts diadamrwaa
      361 gipvngvpnn ptpakvinls lggvgacstt fqqaiddvta kgvtvvvaag ndglstgqdq
      421 pancrgvisv gatdatgrra sfsnfgtdvs lsapgvnils tsnagtttpg adtydtdngt
      481 sfatpqvagv aalmltvngn ltpaqiqqkl qggtraakla agtactalpa gsgildagsa
      541 vasasq
//
LOCUS       WP_175894404             224 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175894404
VERSION     WP_175894404.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..224
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25218
     Region          21..222
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mkshdtptte twhmddatag twiraahlgr rrkyhkgati yrqgelgftf yfllsgrvqv
       61 sifqndgaef ilevmgrwsm fgespaidgh priataiave daellefdir iiegaipshp
      121 elamsllrvi alkqrilasr iqylalpkpe mrisellvrl sdlygekhdd htlitialth
      181 eqiaamtgat rvtvtralkr ladigaieir qrrirvidps rlld
//
LOCUS       WP_175894420             418 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175894420
VERSION     WP_175894420.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 418)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 418)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..418
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44920
     Region          <195..412
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mtiassspst aalkrelkaa earkrtmall lvaplaifll lifvvpigtl ltravqnpei
       61 atalpntvaa lsgwdrkapp sdaayvalaa dmtkvadsea mgalarrlnt eipgyrslva
      121 ktaramplkg dsdaaltpaq traklidlda rwgdvaywqs iakngstvsp fyllaaldhk
      181 qdgfghivqa dpdqsiylai fgrtfvigva vtlfalllgy playwistls erranlvmil
      241 vlipfwtsvl vrvaawivll qseglvntal igsglishpl tllfnrvgvy ismthillpf
      301 milplysvmk sipptyqraa vslgshpfaa fwrvyvpqty pgvgagallv filaigyyit
      361 pallggpndq mvsyyvayft nvtinwgmac algglllaat lvlyavygrf trtnvslg
//
LOCUS       WP_175894426             164 aa            linear   BCT 11-JAN-2025
DEFINITION  arsenate reductase ArsC [Burkholderia pseudomultivorans].
ACCESSION   WP_175894426
VERSION     WP_175894426.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Messens,J. and Silver,S.
  TITLE     Arsenate reduction: thiol cascade chemistry with convergent
            evolution
  JOURNAL   J Mol Biol 362 (1), 1-17 (2006)
   PUBMED   16905151
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Mukhopadhyay,R. and Rosen,B.P.
  TITLE     Arsenate reductases in prokaryotes and eukaryotes
  JOURNAL   Environ Health Perspect 110 Suppl 5 (Suppl 5), 745-748 (2002)
   PUBMED   12426124
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Messens,J., Martins,J.C., Van Belle,K., Brosens,E., Desmyter,A., De
            Gieter,M., Wieruszeski,J.M., Willem,R., Wyns,L. and Zegers,I.
  TITLE     All intermediates of the arsenate reductase mechanism, including an
            intramolecular dynamic disulfide cascade
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8506-8511 (2002)
   PUBMED   12072565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..164
                     /product="arsenate reductase ArsC"
                     /EC_number="1.20.4.4"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030612 - arsenate reductase
                     (thioredoxin) activity [Evidence IEA]"
                     /GO_process="GO:0046685 - response to arsenic-containing
                     substance [Evidence IEA]"
                     /calculated_mol_wt=17660
     Region          4..143
                     /region_name="LMWP_ArsC"
                     /note="Arsenate reductase of the LMWP family; cd16345"
                     /db_xref="CDD:319973"
     Site            order(9,11..16,112,114)
                     /site_type="active"
                     /db_xref="CDD:319973"
ORIGIN      
        1 mttrvlilct hnsarsvlae gmlnhwaakl gkdvraysag sapsgrlnpf alealtragv
       61 dvggyrsksw defvgdrape mrivitvcds aaaetcpywp gspvnvhwgy adpsnapggd
      121 dgkrlafelt rqaiayrmlq llalpldrmd naelqaaltd isrn
//
LOCUS       WP_175894451             144 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia pseudomultivorans].
ACCESSION   WP_175894451
VERSION     WP_175894451.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..144
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15704
     Region          1..143
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mlkllvpvgh sprslqavrh atflyrerca seivlinvqa plestrleay hplsrlrsie
       61 ekfacddlat aerilqeagv eysvvkkvgp vadtiaaaaa eigcdeivva aprhdplhal
      121 lsmfrrgvmd rlvrisnvpv tavq
//
LOCUS       WP_175894507             325 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175894507
VERSION     WP_175894507.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..325
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=36306
     Region          149..322
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mnsifygfvi ltfvavvlai egayqwwsar hgtaarries riramsaggq vqqerlsilk
       61 krmldeskpl drlllrvprv ksidlllqqs gldwsvakli alsamlppla wlvlsftalp
      121 lpavlllalp saclptlrvl rrraarmrkl qrqlpdvcdm iaralrsgha ftgalgmvge
      181 efpepmggef ritfdeinyg vslhdalmnl atrvpvqdlr yfviavliqr etggnlaell
      241 dsiaglirer fklfdkvrvl saegrlsawi lgllpfgtaa lmallnrdfl svlwedpagv
      301 rmtgtmlvsm vfglfwmrri irirv
//
LOCUS       WP_175894560             386 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175894560
VERSION     WP_175894560.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..386
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39940
     Region          12..359
                     /region_name="MFS_YcaD_like"
                     /note="YcaD and similar transporters of the Major
                     Facilitator Superfamily; cd17477"
                     /db_xref="CDD:341030"
     Site            order(19..20,23..24,27,59,109..110,112..114,117,137,
                     140..141,144,214,217..218,221..223,226,250,254,304..305,
                     309,313,329,332..333,336..337,340)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341030"
ORIGIN      
        1 mkailnrdfl alilsvavvg lgtgatlplt alalteaghg tnvvgmltaa qalgglaivp
       61 fvtalarhig srraivvsvv llaaatalmq ftsnlilwga lrvlcgaalm llftigeawv
      121 nqladdstrg rvvaiyatnf tlfqmagpvl vsqiagatsi rfalcgalfl lalptlatir
      181 raplagddah yeahgrwldv lprmpaliig tgffalfdtl alsllplyam dhgvasatav
      241 llasimlfgd tamqfpigwl adklgrervh lgagwivlag lpllplvian pwlcwpllfv
      301 lgaaagsiyt lslvacgerf rgaalvtass lvsaswsaas fggplvagal meqlgsnalv
      361 gvlvvcvaaf vaaalwerra alqrav
//
LOCUS       WP_175894580             391 aa            linear   BCT 11-JAN-2025
DEFINITION  zinc-dependent alcohol dehydrogenase [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175894580
VERSION     WP_175894580.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..391
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41362
     Region          1..389
                     /region_name="FDH_like_1"
                     /note="Glutathione-dependent formaldehyde dehydrogenase
                     related proteins, child 1; cd08283"
                     /db_xref="CDD:176243"
     Site            order(38..40,43,86,169,173,192..193,195..197,216..218,222,
                     236,260..262,291,308..310,333..335,375)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176243"
     Site            order(38,40,60,169)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
     Site            order(90..91,93,96,104)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
ORIGIN      
        1 mmalcwhgkr avhyervddp aiahprdaiv kvalcaigga dlhlydavlp glkdgavlgr
       61 efmgevvevg senrhlrvgd rvvvpfaiac gtcdacrrgn ysvcetsnpn rafvqrvygq
      121 gtgglfgcgh laggypggqa eyvrvpfadv gpiripdeid deralplgdt lptgwqaavq
      181 caiqpndvva vwgagpvgly avlaarllga gdviaidcvp erldcaralg atpldftkls
      241 vadtlaeqtr gkgpdkcida vgleahavda vdatldrfke ttvpgvdqph vlreaiyacr
      301 pggvvsiagl ygglvdnlpi gaivnkgltl raaqtyvqrw sddllkrivd gqidpsfvvt
      361 hrarlsdgpd lyelsrtrgd gcikavmrpg d
//
LOCUS       WP_175894605             249 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia pseudomultivorans].
ACCESSION   WP_175894605
VERSION     WP_175894605.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..249
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26161
     Region          13..244
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mngthdpaqa llagrtalvt gggrglgeai cdelarhgan vvvadldgdr aaavaqrlar
       61 hggkavgrpl dvrdetsvlq avhdarealg dldvivnnaa idvtapiddv svdawqqvlm
      121 tnlfgpylmc havvpmmkar ggghivnias taskrawpna sayhatkwgl lglshalhae
      181 lrpagvrvsa ivaggmrtpf lldrfpdide dtlqppehva aavrfvltqp pgtvvpelmv
      241 lpmketswp
//
LOCUS       WP_175894611             284 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia pseudomultivorans].
ACCESSION   WP_175894611
VERSION     WP_175894611.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13484798
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..284
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=31738
     Region          6..>184
                     /region_name="PRK12678"
                     /note="transcription termination factor Rho; Provisional"
                     /db_xref="CDD:237171"
     Region          171..>239
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mqrrypgrps errgppdwqe rnerayrgag ergmpdddsl lpeergdeaa yryasedvgp
       61 edwgsewner sarpeaeqgr rsaraewrgg pggpggprqa ayeaergygq pgrradegrq
      121 gddrpdfrgh frlgryggar gdddprggya pdlsrfgsda erealrrrrg pkgytrsder
      181 iredvcerla haleidvsdv svqvqegcvt ldgtvpvrwm khgiedladd cfgvrdvdnr
      241 vrvrrederd tgmvlhpaqr tvtptqpaas dpepgattgs esrh
//
LOCUS       WP_175894619             401 aa            linear   BCT 11-JAN-2025
DEFINITION  zinc-dependent alcohol dehydrogenase [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175894619
VERSION     WP_175894619.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..401
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42183
     Region          1..401
                     /region_name="FDH_like_1"
                     /note="Glutathione-dependent formaldehyde dehydrogenase
                     related proteins, child 1; cd08283"
                     /db_xref="CDD:176243"
     Site            order(38..40,43,86,162,166,185..186,188..190,209..211,215,
                     229,253..255,303,320..322,345..347,387)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176243"
     Site            order(38,40,60,162)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
     Site            order(90..91,93,96,104)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
ORIGIN      
        1 mkavvfhgig diridtvpdp evaevtdavv rltasaicgt dlhmvrgtlg gmkpgtilgh
       61 egvglveavg rdvrnlrrgd rvlipstiac ghcvycragy taqcdvanpg gpragtaffg
      121 gpadtgpfdg lqaeyartpl anaslirlpd eidddrailm sdifptgyfg aqlaevkpgd
      181 tvavfgagpv gqfaiasakl mgagrviavd riasrlemac aqgaesvdfs eddpvdtvlr
      241 ltggigvdra idavgvdamr athgpaaadr daarafdaev daiaprrkpd grywvpgdgp
      301 sqvlqwavra vakagtvavi gvyppqarvf pigeamnrnl tikmgncnhr tiipplvelv
      361 rsgafdplsv ltrrepltna idayrafdvr epgwmkvkle p
//
LOCUS       WP_175894626             278 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia pseudomultivorans].
ACCESSION   WP_175894626
VERSION     WP_175894626.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 278)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..278
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29611
     Region          37..276
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mklarplfap hmsfverawy valrvlvvlt llylilpvla ivplsfssst flvypipgfs
       61 trwyenlias dewrmaakns fivapsatvv atvlgtlaai gltkadfrgk gllmavllsp
      121 mivpvvvvgv gmylffaplg lantytglia ahaalgvpfv vttvaatlqg fnhnlvrasl
      181 slganpvttf frvtlpviap gvmsgalfaf atsfdevvvt lflagadqtt lprqmftgir
      241 enisptiaal atilivfstg lllalewlrg rnarravs
//
LOCUS       WP_175894632             442 aa            linear   BCT 11-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175894632
VERSION     WP_175894632.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..442
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=47492
     Region          23..441
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 mrsdpamlna fnpaqaarld eharalverr arvlgpayrl fyetplhivr gegvwlydsa
       61 grayldaynn vasvghcrpe vveaiarqaa tlnshtrylh dgildyaerl lrtlpdalsq
      121 amftctgsea ndlalriakq ytggtgvivt rlayhgvtaa vseispslgr qvplglhvrt
      181 vappdtyldg edgvgarfar dvqraiddlt rhgirpaali vdtifssdgv fadpcgflqd
      241 avaairhagg ifiadevqag fartgskmwg ferhgvtpdl vtmgkpmgng hpiaglaarp
      301 dvlerfgret ryfntfggnp vscaaasatl dvieqdglqa naarigaylr qgfrtlarkh
      361 aligdvrgdg lflgvelvrd rttktaadde aqrvvdlmre hgvlisstgi rgnvlkirpl
      421 lpftqahadl llgaadtald al
//
LOCUS       WP_175894690             261 aa            linear   BCT 11-JAN-2025
DEFINITION  peptidylprolyl isomerase [Burkholderia pseudomultivorans].
ACCESSION   WP_175894690
VERSION     WP_175894690.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..261
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=28014
     Region          100..247
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mndmlhqapa tlringvaid ddaiaaeaah hgdtrdpfda arrslavrel lrqravslal
       61 ldadaalgda avdallerel thlpepdrad ceryyvqhpa rfrrndivya shllfavtdr
      121 vplaplrqra eaaladvvaa pdtfeavara ssncpsaqlg gslgqllrgd tvpefeaalf
      181 dsdgigvlpk lvntrfgfhi vrierrvpgd avpfdeaaaq iaahlsarvr eramrqyvai
      241 laggariegv sfdgahgplv q
//
LOCUS       WP_175894715             269 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175894715
VERSION     WP_175894715.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..269
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29841
     Region          85..268
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mrtwrieran laaqldvsra trlvaaiggn epnafaaeil klfddalsit qctifayefg
       61 nrprtmsvad hrggrylrdl adtyarhfya ldgnqqivst ahlgtrrhdl llhqqagdei
      121 dheayraacy rgpdvsdrla llmqpgdatw lsinlyrahr sgafqpreia aiealaplia
      181 qaarhhyala gaaqigipqr mlarlrhacp dlskreldvl rgvldgqtar eigetigvka
      241 ssvvtyqkra yrrlgistqr elfalcmqp
//
LOCUS       WP_175894792             189 aa            linear   BCT 11-JAN-2025
DEFINITION  group III truncated hemoglobin [Burkholderia cepacia].
ACCESSION   WP_175894792
VERSION     WP_175894792.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Keppner,A., Maric,D., Correia,M., Koay,T.W., Orlando,I.M.C.,
            Vinogradov,S.N. and Hoogewijs,D.
  TITLE     Lessons from the post-genomic era: Globin diversity beyond oxygen
            binding and transport
  JOURNAL   Redox Biol 37, 101687 (2020)
   PUBMED   32863222
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Bustamante,J.P., Radusky,L., Boechi,L., Estrin,D.A., Ten Have,A.
            and Marti,M.A.
  TITLE     Evolutionary and Functional Relationships in the Truncated
            Hemoglobin Family
  JOURNAL   PLoS Comput Biol 12 (1), e1004701 (2016)
   PUBMED   26788940
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Wajcman,H., Kiger,L. and Marden,M.C.
  TITLE     Structure and function evolution in the superfamily of globins
  JOURNAL   C R Biol 332 (2-3), 273-282 (2009)
   PUBMED   19281958
REFERENCE   4  (residues 1 to 189)
  AUTHORS   Vinogradov,S.N., Hoogewijs,D., Bailly,X., Arredondo-Peter,R.,
            Guertin,M., Gough,J., Dewilde,S., Moens,L. and Vanfleteren,J.R.
  TITLE     Three globin lineages belonging to two structural classes in
            genomes from the three kingdoms of life
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11385-11389 (2005)
   PUBMED   16061809
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Wittenberg,J.B., Bolognesi,M., Wittenberg,B.A. and Guertin,M.
  TITLE     Truncated hemoglobins: a new family of hemoglobins widely
            distributed in bacteria, unicellular eukaryotes, and plants
  JOURNAL   J Biol Chem 277 (2), 871-874 (2002)
   PUBMED   11696555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..189
                     /product="group III truncated hemoglobin"
                     /GO_function="GO:0005344 - oxygen carrier activity
                     [Evidence IEA]"
                     /GO_function="GO:0019825 - oxygen binding [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20933
     Region          21..130
                     /region_name="TrHb3_P"
                     /note="Truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 3 (P); cd08916"
                     /db_xref="CDD:381257"
     Site            order(33,46,49..50,57,60..61,64..65,75,77..79,82..83,86,
                     89,93..94,97,121,124..125,128)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381257"
ORIGIN      
        1 mtvlpaspep aparsrdaep teenirdlvy afydrvrtdp llgpvfdarl agrwddhlpk
       61 mvtfwsslvl gtkgyrgnvq qahqplggie pahfsrwlsl flktvearya ppaairfmep
      121 alriaqslql srfgwdyrip peqqalldai aprrrggddg gddphalpsr argepfpaki
      181 igrstdpda
//
LOCUS       WP_175894805             530 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Burkholderia pseudomultivorans].
ACCESSION   WP_175894805
VERSION     WP_175894805.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 530)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..530
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=55862
     Region          44..150
                     /region_name="SoxW"
                     /note="Thioredoxin-related protein SoxW [Posttranslational
                     modification, protein turnover, chaperones]; COG2143"
                     /db_xref="CDD:441746"
ORIGIN      
        1 mktvlrnlta aclfaasgaa fataapqgva aslspqrahl ppgiawqqgd vddafalakr
       61 tgkplllywg avwcpscnqv kstifsqqaf ktrsslfvpv yldgdtesaq klgerfkvhg
      121 yptmilfrpd gtevtrlpge adldrymqal slgmtaahpv rqtlasalkd gasltpdewr
      181 lladyswdtd galpvpadrv aqtlqtlsqr araagakaea arfalkaava aasddppqag
      241 aldksalada wrtvladral sradsdvlvv aparvvaylg gsdaqraklr gaydaalarl
      301 stdatlssid rlmalhgrvl largdartga pldapalvdt vrrqiaasvq gaanpyerqa
      361 lvsegadtlt daglfdesda llkaelprss tpyyfmsgla anakargdna aaldwyrkay
      421 dtatgpatkl rwgatyfana vqlapddsar iegiaasvla qagktrdafy ganlraltkv
      481 vaqlnrwrsg gahdaavrtv vrqfdevcgk lpagdpqaaa cakliqpvka
//
LOCUS       WP_175894834             557 aa            linear   BCT 11-JAN-2025
DEFINITION  alkaline phosphatase family protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175894834
VERSION     WP_175894834.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 557)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 557)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..557
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=58285
     Region          47..535
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 mmsffvkqrk tavmvagala lasmgayaqq dgnsqgsdaa hgrrvvkhvl lisidglheq
       61 dlarcigant cpnlavlaqs gvtytnaytp glsdsfpgla alvtggspkt aglfydvsyd
      121 rnlyapsdtt csgkqgwnvv fdettgidae nggalvhldg ggafnpqaip hakvngqcvp
      181 vyphnyvktn tvfeavkagi pnahtawadk hawgydwlng psgtgvddla rteinsidpa
      241 tgtnytdiys htarfdnlhv qalinqiggr dstgtksapv ptlfgadfqt lsvaqkapva
      301 tgggyldanf tpngqvanai tyvdnsighi vaalkqanly sstavivtsk hgqsptdhtk
      361 lvkngdtltk lleannyldp ngnfgqnntt tgnlndgsgl vgtgfvqtdd vgliwlrdrn
      421 qrtavvqtlk anlgcnapgi cadgsqayil ygaaladrfg dpangrtpdi vvqpnpgviy
      481 tsstkkdeeh ggnapddshl gllvsypglh rartvtdlvg tkqvaptilg llgadprllh
      541 avvaentrvl pglgidr
//
LOCUS       WP_175894859             705 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia pseudomultivorans].
ACCESSION   WP_175894859
VERSION     WP_175894859.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 705)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 705)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..705
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=75976
     Region          37..634
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mtdptasppp ppaaprrrrv wrtlagallg ltlactgiga wtihriwtql psvehlavyr
       61 palplrifar dgellaeygv errefvpler ipplmrqall aaedaqfyqh gavdpgglar
      121 atfanlvtrq pgqggstitm qvarnfyltr dkvlsrklae ilmayklere yskdkllely
      181 mneiylgera ygfaaaahvy fgkpldalsa geaavlaglp kapsafnpvv nparatarrn
      241 yvlgrmhalg qlddatyraa vgaplalstt pppgivaapy vaerarrmmv erfhddaytl
      301 gldvtttvsm rdqraaeaal drtlrrqpak rdrlegalvs ldvatgdmla lvggadfsrn
      361 vfdhalqayr qpgssfkpfv ysaalekgyf pgvlvddaqr tltpaetgar pwrprnfgnh
      421 yegfiavrrg lvrsknlvav slmqaadary vqqhamrfgf daprnpaslp lalgagavtp
      481 lelasaygvf anggvrtepr lilsvkqrhg gvlydapapd gtrvvsarna fvmdsmlrdv
      541 vragtargal alrrddaagk tgtsngskdv wfagyssgvv avawlgydtp rsmgratgat
      601 lalpvwldym ktavdgrtpi dttppqdval adgdfvyaey lhgtctadvp pfirsrfacg
      661 gapvaaasda aatygnrgaq pgepmpaavd aaerervldl frted
//
LOCUS       WP_175894875             334 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Burkholderia pseudomultivorans].
ACCESSION   WP_175894875
VERSION     WP_175894875.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..334
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36265
     Region          7..317
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(12..14,44,49,75,138..139,179..180,201,230..236,272,
                     289..292,297,300..301)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(44,49,75,138)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 mrialpsrlg fgtaplgnmy rdipneeala tvdaawesgi ryfdaaplyg aglaelrlge
       61 alagrprdey slgtkvgrlv ldehedasqr dlgekgglfq hglpnkivyd ytedgtlrsi
      121 easlkrlrtd rldtvwihdp aidfhgerwr dvfdvamsga akaltrlrde kviqgwglgv
      181 nriepcelal ersdpdgfll agrytlldha dalerlmpes aarglgiivg gpynsgvlag
      241 gthfeyqpat qdmldrvaqi rriserlgvd vravalqfsl ahpavaaaip gasrperiae
      301 nlrlasapip aelwnalkae rliaehaptp igaa
//
LOCUS       WP_175894711             277 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia pseudomultivorans].
ACCESSION   WP_175894711
VERSION     WP_175894711.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5), 4725 (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10084616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..277
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=30309
     Region          2..122
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          153..275
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mtyktllvhi ddsarssari dlaldlarrw dahliglyiv cqdlfeplrr pdeplklavh
       61 erlceerrre aetafleaae lagrsvewra pagpatdaai lharhadlli lgqcaphdrs
      121 tfvarhfved llmaggrpai vvpyagqfhs cgdnvlvawd ggreaarala dalpllrrar
      181 fvtvetvehr rpdpdqtpag vdvaaylerh gvrasfsttp haattgvgvt llnrasdlha
      241 dllvmgaysh trvhervlgg atrtlletmt vpvlmsh
//
LOCUS       WP_175894922             308 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175894922
VERSION     WP_175894922.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32713
     Region          3..61
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          90..287
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(105..106,108..109,112,116,118..124,217..222,
                     228..229,231..232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 melrqlryfl svvehgsmgk aalelglvts alsqqisrle gelstrllqr tsagvvptda
       61 glafwrqaql alrhvdaaal aarsarlsgh vsvgmapsta svlgvafmqa mrtrypdvrl
      121 hlveslsgyl asmlsarqid lavlfraepa qrwsvmslld erlfvigagd lkgmptsasv
      181 rlknlgklpl ilpsgthglr sllssaftra ayepnivaev dglallmdav rqgigatiqp
      241 gaalarvena rlksvpvaeq yatrpnmias isddelspag laarvvladv arqlvsegrw
      301 pgarlhap
//
LOCUS       WP_175894849             331 aa            linear   BCT 11-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175894849
VERSION     WP_175894849.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..331
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=34893
     Region          <14..324
                     /region_name="FAD_binding_2"
                     /note="FAD binding domain; cl46878"
                     /db_xref="CDD:481218"
     Region          48..74
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          79..109
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          113..136
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          174..199
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          208..232
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(224..225,228,231..232,255..256,259,262..263,266,
                     286..287,290,293..294,297,317..318,321,324..325)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          301..325
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mtafsstasl pgthdpdraa lalrlaapda svrrialiel adleesdlvp sfvaalcddp
       61 sadvrseaar vlgaweqpdv vdalcgalld pdegvrataa qslselkdaa sgtvlcrwad
      121 rpesfvrrav lrglrelrdp gafapalral daehaavrae avavlgwlrd pralpplari
      181 attdaaadvr raavgaigfa apddaatida llaalrdhew qvreeaattl gklrvaaard
      241 plaaaldddy wqvrlraara lgqlhdaaaa pavaallsha isnlrkeaal algelrdrat
      301 laalthaled hdpevrkavr iairqideas r
//
LOCUS       WP_175894966             208 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: superoxide dismutase [Burkholderia cepacia complex].
ACCESSION   WP_175894966
VERSION     WP_175894966.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..208
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22721
     Region          5..201
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mpyvlpalpy pvdalephid trtmeihhak hhqtyvnnln aalegthygd lpvetlvsqi
       61 eslpdalrpa vrnnggghan hslfwtvmsp qgggepdgpl rqaidaelgg fdafkdaftk
      121 aaltrfgsgw awlsvdaqgk lvvestanqd splmaglmsg ntpvlgldvw ehayylkyqn
      181 rrpeyiaafy nvvnwpevar ryaaalgk
//
LOCUS       WP_175894998             388 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175894998
VERSION     WP_175894998.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..388
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41107
     Region          19..217
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          143..387
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 maiplnyiar nlwtrrltta ltaggmalvi fvfatvqmld agltktlvst gepdnavvir
       61 kgaeteiqss idhqqanale mhpavapgpd grplvskeav vlislvktst gkpsnvvirg
      121 vspaglalrp hvtlaagrtf apgsseiivg saiakgfsgt qlgdslhfaq rdwtivgifd
      181 aggsgfdsei wgdvdqlmqs frrtsyssmv lripgadgfa rfkadidvdp rltdeakreq
      241 tfygdqskal skfinilgit lstifsiaam igamitmyas vanrvaeigt lralgfkrtn
      301 vlaaflleal llgfvggvag lacaslmqfa sfsttnfqtf adlsfrfvlt paivvktllf
      361 slvmglvggf lpamraarlk ivdalraq
//
LOCUS       WP_175895076             707 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cepacia].
ACCESSION   WP_175895076
VERSION     WP_175895076.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..707
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76909
     Region          29..707
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mtvslvrppv rprrvaaala cvaaslahad dspggatvlp avnvtaahds pqhltdtvst
       61 galgtrrqld tpfsttivts eelearqpyk lgdvfandas vsdnsgaysa wasymtvrgm
      121 qldwqngyki dglpfvtygi tmpyeqldrv ellkglggfl ygfvtpggvv nyvtkqpgae
      181 pvrsidvgyr stnvwtehvd lgqrfgpdgr fgarlnathe egktyndgni rrdsvslalq
      241 anltrdlsvn vgalyqdrrt tgqtpsiftg sypggvlpat isggttnlgg kdqylntnlq
      301 lytaglqyql apdwqldvay syskatrrrn estlylqdaa gnytdsryvg medhrfsqwr
      361 amvegkvrtg pfshqiviga swqkqandys ansvfvplga gnlyapnpyr ydsphgfiqy
      421 rtseivqksl fasdtvqlte rwsvlagvry mnyeqrsfqa sgaedpgyrq ngvvtptfav
      481 mfrlapttta yasyaeslep gsrvndvyan agqvlkplrs kqyelgikse harwsataal
      541 friersaeya naanvyvqdg esviqgiefg arakfgahwn agvdamllda wyangignng
      601 nrvagaprfv lagdigyavp gvpgltlgvd akftgatplr aaggldapgf lvvnagaryl
      661 trigrhdvml rasidnvlnr ryweyqyady vkpgdprtvs lsakldf
//
LOCUS       WP_175895036             134 aa            linear   BCT 11-JAN-2025
DEFINITION  PaaI family thioesterase [Burkholderia pseudomultivorans].
ACCESSION   WP_175895036
VERSION     WP_175895036.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..134
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14453
     Region          15..133
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mdenavrell drllapwvrs lnlvpvsidd dsvtlrlpfs gefrhsgggi cgqvftaaad
       61 tamvvaisaa lgefrpmttv slntnfmrpv rkgdvlvtar vlrmgrnlvf gevelfdedg
      121 nmavhatsty alvn
//
LOCUS       WP_175895153             418 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175895153
VERSION     WP_175895153.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..418
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44024
     Region          6..411
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtssqkaplv ivgasyagtq laaaarelgf dgpivligde phapyqrppl skglltgktg
       61 mgqlalrspd fyteqcidlr vgqrataldl aarrvrladg ghleysrlal atgarcrplp
      121 vpgaelqgvh qlrtlddala vqrrlgrcss acivgggfig levaaalisa gtrvtvvesq
      181 trllarafpv fmsdyvahah rrrgvslelg rsvrallgrq gsveavqfdd grtldcdlvv
      241 tgigvlpnte ladaagiacd dgilvdalgr tsvrnvlavg dvanmtqppf pgsparmrfe
      301 siqaasdgar aaasvlvgrp qplsaipwfw seqhdlrfqm aglpssgdqv vlrgapasdr
      361 ftvfylhdga maaahsvnrp sdhvlarkli aqrsripaat ladptadlrs midagqvn
//
LOCUS       WP_175895154             338 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175895154
VERSION     WP_175895154.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..338
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38057
     Region          25..335
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 msknafvppa psrsreaihd lrvvrygfll vdnfslials aaidplrian mvvgrrvydy
       61 rliapgddvv rssdgirvvp dvsmsdseaf dvvfvvgpnp vprrrtgaiv dwlrrqarsg
      121 talggldtgs yflaraglln gyrctihwed qdvlmeqfpk ltvstrlyev drdrytcsgg
      181 vapldlmvhl laaapgsral aarvlellva eprsreyrqq tslrqyigae hekldealql
      241 mesnveetls vpeiaehlhv sqrqlqrwfq drlgkspaqa yleirllrar qllyrtaasl
      301 edvcartgft stthfatryk eqfqispiad rrryqnal
//
LOCUS       WP_175895166             333 aa            linear   BCT 11-JAN-2025
DEFINITION  transketolase family protein [Burkholderia pseudomultivorans].
ACCESSION   WP_175895166
VERSION     WP_175895166.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..333
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35724
     Region          22..332
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 msavadkkpr lttsamiasi aaegqktrpa pfghalvaea ekrrnivgmt adlskytdlh
       61 vfnqafperh fqmgmaeqll mgaaggmake gfipfattya vfatrraydf ihqviaeenl
      121 nvkicaalpg lttgygpshq atedlalmra ipgmtvidpc daldteqava aiaaydgpvy
      181 mrllrgkvpa vlddydyrfe lgkakllrdg advlvissgl mtmraleaaq alddgsasva
      241 vlhvptikpl deativeqcr kpgrlvivae nhsvigglgd avasalvrhr vmpefrqial
      301 pdrfldagal ptlhdrygis tasivanikt wlk
//
LOCUS       WP_175895169             185 aa            linear   BCT 11-JAN-2025
DEFINITION  ester cyclase [Burkholderia cepacia].
ACCESSION   WP_175895169
VERSION     WP_175895169.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Sultana,A., Kallio,P., Jansson,A., Wang,J.S., Niemi,J., Mantsala,P.
            and Schneider,G.
  TITLE     Structure of the polyketide cyclase SnoaL reveals a novel mechanism
            for enzymatic aldol condensation
  JOURNAL   EMBO J 23 (9), 1911-1921 (2004)
   PUBMED   15071504
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..185
                     /product="ester cyclase"
                     /EC_number="5.5.1.-"
                     /GO_process="GO:0030638 - polyketide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=19654
     Region          57..184
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
ORIGIN      
        1 mktstvvsvv srialaaata aaalpavsat ddnlvqpktl iidkslskhq aeqqiraarl
       61 fdtfwstgde aqarealaad ftdrtlpagr pqgiagplaa skgfhgavpd vhaeveqmiv
      121 agdrvithlh ftghftgsfn gvqgkgqavd fiatdiyrvr dgkitdnwhl ednltflqql
      181 gvvar
//
LOCUS       WP_175895215             263 aa            linear   BCT 11-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Burkholderia cepacia].
ACCESSION   WP_175895215
VERSION     WP_175895215.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..263
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29225
     Region          91..245
                     /region_name="CE4_NodB_like_5s_6s"
                     /note="Putative catalytic NodB homology domain of PgaB,
                     IcaB, and similar proteins which consist of a deformed
                     (beta/alpha)8 barrel fold with 5- or 6-strands; cd10918"
                     /db_xref="CDD:213023"
     Site            order(97..98,153,157,201..203)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213023"
ORIGIN      
        1 mslraivcll llsclprmas agagtvvpvs qrvlilvyhr fatqrldsmt vrtgtfieql
       61 haieasgyri vpladvvrwh dgqtdalpar avaitvddgh rsvydvlrpl laahpvpvtl
      121 fiypsaisna ryamtwdqlr algrsggydi eshtywhpnf aterarrtea dyqrfvsfql
      181 grsrerlese tgrpirllaw pfgvhdaqtd rlaaregyva aftidgrpvr ptdppmalpr
      241 ylmtdacgtr cmngllqtag ehp
//
LOCUS       WP_175895231             429 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pseudomultivorans].
ACCESSION   WP_175895231
VERSION     WP_175895231.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..429
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46413
     Region          14..417
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(27..28,31..32,35,67,117..118,120..122,125,145,
                     148..149,152,252,255..256,259..261,264,291,295,345..346,
                     350,354,370,373..374,377..378,381)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mhsleqvtma rvfrrlvpff mlcyfisfld rvnvgfaslq mndaigltpa qyglgsglff
       61 llyflfevps nlllvrvgtr iwiarilitw glisgatafv tgpwnfyavr lllglaeagf
      121 fpgvaycitl wfpsayrarv mgyllvaapl ssvigspisg mllglrgldg lgglqgwqwm
      181 flieaapavi lgfvtlrylk gaprdahwlq pderawlaer mtsednrrrd ehdipvahvf
      241 sdrrvwmlaa mafgffltiy gigfflpqiv ksfgltnvqt gfvtaipyvi gsaslvfwar
      301 radrtgerrw niaipaliaa aalvgaglid apvlklgcfc vlafgvfgal pafwaintdl
      361 lsgaaaaasi awigavgnlg gfagpyllgv tkartggyta alllmavvav iaagialsvg
      421 rqrrtyhpa
//
LOCUS       WP_175895246             498 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175895246
VERSION     WP_175895246.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 498)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..498
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=53573
     Region          5..498
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mterihelld rwlaeapgrp fihlpdrsls yadvgalada lerelrddgv rrgdrvlvva
       61 encaehaall iacsrvgaws cgvnarmapg evdafagkad arvlyftpgv spaagahaar
      121 hdarpscvng larsavqvaa rvepeplasd vaaviftsgt tgapkgvmmt hrgvlhfarv
      181 saesralgpd drvyayapmt hifglgtvll aslhagaale mrpqfepael fdalahrrvs
      241 qvqgppmlfs rllrhcaehg ivrpeapclr ylyagagpld lalkrqveal fgqtlhhgyg
      301 lseyagslha trlgetrgdt sagyafpgaa lrivdpasgr tlpagargei wlrgtglmpg
      361 yfrdpqatad vmrdggwyas gdlgelhddg alfivgrlke miirsgfnvy pgeveqalnr
      421 fpgilnsavv gqkdadgnea vvafveldaa raldetalrr ylreqlapyk hparivpidk
      481 lpfnsngklm rrqllerl
//
LOCUS       WP_175895269             244 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia pseudomultivorans].
ACCESSION   WP_175895269
VERSION     WP_175895269.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 244)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..244
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25437
     Region          7..238
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mtltdlngki avitgassgi geaaarvlva egmkvvltar rkerivqlaa elgdaalava
       61 tdvsdagqva tlfdtvrerf ggldllfnna gmgiagafeh srpddwrtqi danlygvlhc
      121 thaaiplmkg ragamistvs svggkagaps wavycatkfa vsgfceglrq elagdgirvs
      181 liypgavhte wghnvpaeam rerrdaigal lpedvanala ysfaqpagvl vneleirpsl
      241 qlvl
//
LOCUS       WP_175895270             700 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia cepacia].
ACCESSION   WP_175895270
VERSION     WP_175895270.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..700
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73493
     Region          38..634
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mheaadqtra vaapprrltr aaaaliarid iftprgayva rsviaaalal gvayllelet
       61 pysaastvll vinpvqgavi gkgvwrvvgt iagmvvafvl mgcfaqqpll filgfafwlg
      121 vcvagmtllr hfrasgtvva gytiglatyg amqhpeltfe hvigrgstva igvlclslvs
      181 mllgtrdvha kldalvtrit advarviaaq rnglaaapad dkrhalfagi ygiddllalg
      241 kaesedlaqr aaavrhgmas lfgalaggmp plpadspgar avaslqprla aawqaaadal
      301 gdgpggatha rallgdarer lrdaldgivl gdprdeaall iagerlieqi ddyraaldgl
      361 velqrprpgy rparvrfhrd tgaalrngvr aacaivisga fwlatgwnqg dmmllvvapy
      421 callatagnp pagaqafikg tvlavpaafv cafgilprie gfpllvvalg lfwmpgiyat
      481 svpktalagl aylvafntlt gatnpfrpdv elflnqsvaw vlatfltllt frlilpgnla
      541 tdatrlrrti rddtlalvag rrvtaagwqq rqqhriaqlg allagqpaam tqasiealaa
      601 lhvgkellri rrgaardglp dparrcvrag laglarhaaa ppraarharr aahalaglaa
      661 tqpgntelkw lmaafadvhv llhtyaayft avperardaq
//
LOCUS       WP_175895272             174 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia cepacia].
ACCESSION   WP_175895272
VERSION     WP_175895272.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..174
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=17954
     Region          15..161
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 mtntvdiaqq lkqamrgvaa tvtivttggd gaaaapcalt assftsvald pptvlvcinr
       61 rasihasitg rrrfcvnalr schvplalac sttgsdtrfa hdawrtdaat glpylenaqt
      121 sffcdtleqv evgshsilvg rvtrvamsad vnplmyvnga faavrtlpsd aggg
//
LOCUS       WP_175895277             305 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia pseudomultivorans].
ACCESSION   WP_175895277
VERSION     WP_175895277.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..305
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32767
     Region          1..304
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mekvsfknln gqgittaavi nfpagfdask kyaavvvshp gggvkeqtag lyarklaeqg
       61 fvtiafdrsy qgestgeprq lenpyisted vsavidyltt lpyvdqanig amgicagagy
      121 sanaaindrr ikalgtvsav nigqmfrngw entvkdadav gllqagsqtr thdanqggya
      181 tiplaplkke dapnaelaea weyyhtprce hpnapgfala rdltqivtyd aynkaeaflt
      241 qpiltvvgnv agskwmsddl laraasqdkq mhiveganhm slydvpkyvd eavsvlapff
      301 rrtlk
//
LOCUS       WP_175895313             314 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia pseudomultivorans].
ACCESSION   WP_175895313
VERSION     WP_175895313.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..314
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33620
     Region          76..283
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 maldpeiaav lrslestppm eslsvdalra glayplldrr tmvgevvdle iplagrslaa
       61 rlyrprpear qcdgvivffh gggfvignld thdhvcrdlc egsgaavial dyrlapehrf
      121 paavddcfda vgwiaqhaet lsldasrivv agdsaggnla avtalrirde ggpslcaqvl
      181 vypvtdyhtp ptrsyienqs gyaltraami rfwhdyvane rdafhphacp lrakslaglp
      241 ralvvtagfd plrdegdaya nrlfdagvpv tsrhyegmih gffrmglaca aakealmeaa
      301 awiggamarr gvaa
//
LOCUS       WP_175895345             190 aa            linear   BCT 11-JAN-2025
DEFINITION  YbhB/YbcL family Raf kinase inhibitor-like protein [Burkholderia
            cepacia].
ACCESSION   WP_175895345
VERSION     WP_175895345.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..190
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=20022
     Region          50..186
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mrslpmprka vcacalfatl pgvataetfa lkvadldhgr frneqvfsgf gchgenvsph
       61 vtwsnapagt rsiavtihdp daptsglgwt hwavvnipps qtslqkgasg nvnllppgat
      121 etltdfgqsk yggpcppqgk phryivtaya ldvphidvsp asspalvafq mhgkiiarar
      181 yvaiyqraan
//
LOCUS       WP_175895405             468 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia pseudomultivorans].
ACCESSION   WP_175895405
VERSION     WP_175895405.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 468)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..468
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49487
     Region          <229..467
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mhtlmlalrn lqrnrrrslt tllamivgvs aillfggfsr ditlglqtdf vqrsghlqiq
       61 rqgyylygtg dpaaygirry aalidllrrd pqlapllqvv tptlqfggia gnfaagvsrt
      121 vmgfgeipdd qyrmqqwnay gfplrprafa lrgsaddaav vglgvarvlh lcgplhvpdc
      181 rdappgpaap aaagpdanap advlalaqge agsqpagdga thievltasa ggapnvgrfs
      241 vvtaeqqgvk elddvylavr lsqaqrlvyg gaepratale iqlartadlp aararieqll
      301 rggfdgqpld vvdfatlnpf ydqtnrmfsv ifgfvfvlis aivlfvisnt mstaiiertv
      361 eigtlramgm rrggiqalfv cegallgvag aslgvlaala iaaavnhsgl awtpparida
      421 valtvrvwge wrtiavtftg lacvaglsaw lpsrhaarls ivdalrhv
//
LOCUS       WP_175895406             137 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia cepacia].
ACCESSION   WP_175895406
VERSION     WP_175895406.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..137
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14259
     Region          4..130
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mnpnrlndfa atllrvglgv lylahvaqkv fvftlpgtaq ffasiglpgw laylttfvel
       61 agglallagf rvrvaalvll pfmlgataah lpngwsfasp nggweypafw avtlavqall
      121 gggafalgar easvqra
//
LOCUS       WP_175895419             401 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175895419
VERSION     WP_175895419.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..401
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=42249
     Region          8..401
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 mstppretrf awrgrrrdgt prrgtviafd aaaaraalar dgiavlslda rgparapsah
       61 arditrftrq lasllqaglp lapsldmlar trtrdglpri aaglareigg gqrfaaalar
      121 yphqfgtlyr qlievgeasg algavltrva ehreradaqw rklraaltyp aavilfalai
      181 saalmvwvvp tfrqifdgfg talpaptral lalssalstw ggalaaltaa aglalqqatr
      241 hrpslryala rymlaapfig dtlarfaaar wcrslatllg agvpladafa tlertaghpv
      301 feratahiaa rvlrgarlad amqaagcfpd dvvqpiavae etgalhtmla diaalgerql
      361 darldtlaal geplivivlg alvgglviam ylpilqlgnv v
//
LOCUS       WP_175895463             392 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia cepacia].
ACCESSION   WP_175895463
VERSION     WP_175895463.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..392
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42921
     Region          8..369
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 malfssarpp rtilvaaprr igdvllttpl vrslkarwpd aqidmlvfrg tegvlehnpd
       61 vrhvivvaqr agfrerlrda lsmwrrydla caalssdrpr fyswfagrkr vglvdpnrvt
      121 wltrmmlngi ainhhesaht vvstlalapv igiepvsevv apgigddpar rarfdawlae
      181 spairagkpl vvlhpypmfr ykqwrldgwv emigwlrehg yavalsggpa dsereyaeqv
      241 aaeaggdvln lvgrltfges aelvrrarlf igpdtgathv aaatgtdtia lfgpsdpvrw
      301 gpwpqhwpat enpwplrgsg rhgnvwllqg egdcvpcrhe gcerkvdsrs dclvnlgaqr
      361 vkaaaaemlg lnppgpaavt vntsrlhrag sd
//
LOCUS       WP_175895517             275 aa            linear   BCT 11-JAN-2025
DEFINITION  carbon-nitrogen hydrolase family protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175895517
VERSION     WP_175895517.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10166075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..275
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30409
     Region          12..272
                     /region_name="nit"
                     /note="Nit1, Nit 2, and related proteins, and the
                     Nit1-like domain of NitFhit (class 10 nitrilases);
                     cd07572"
                     /db_xref="CDD:143596"
     Site            order(50,106,123,127,138,163..164,166..167,186)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143596"
     Site            order(50,123,163)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143596"
     Site            order(124..125,144..146,164,167..171,173..174,194..195,
                     198..199,201..203,205..206,236,266..267,270..271)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143596"
ORIGIN      
        1 mtdsslsatp frvaalqmvs tpdvarnlae agrliaeaae egaqlvllpe yfcfmghrdt
       61 dklalaetyr dgpiqqflad tarrhrvwvi ggtlplkape pdrvlnttlv fdpdgreaar
      121 ydkihlfnfa kgdesfdear tirpgdtvva fdapfgrvgl svcydlrfpe lyrrmgdcal
      181 ivvpsaftyt tgrahwetll raravenqcy vlaaaqggkh engrrtwghs mlidpwgeiv
      241 avrdegasvv sgaldpqria dvrqslpawr hrvlt
//
LOCUS       WP_175895526             306 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia cepacia].
ACCESSION   WP_175895526
VERSION     WP_175895526.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maindola,P., Raina,R., Goyal,P., Atmakuri,K., Ojha,A., Gupta,S.,
            Christie,P.J., Iyer,L.M., Aravind,L. and Arockiasamy,A.
  TITLE     Multiple enzymatic activities of ParB/Srx superfamily mediate
            sexual conflict among conjugative plasmids
  JOURNAL   Nat Commun 5, 5322 (2014)
   PUBMED   25358815
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445158
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..306
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=34794
     Region          13..215
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
     Region          21..110
                     /region_name="ParB_N_Srx"
                     /note="ParB N-terminal domain and sulfiredoxin
                     protein-related families; cl28891"
                     /db_xref="CDD:452888"
     Site            order(35,37,73,76..77)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:319246"
ORIGIN      
        1 mngnqehepv plsssekisl ipadrlrvln prtrnplffs qlveniavvg lkrpisvalg
       61 gkdkdgdwye vlcgqgrlea lkhlgetmip ccifdapevd rflislteni arrrhtteel
      121 lsgiqvlrsk gysseqiark inldadyiss ilhllnngeq rlvravekrv vpiwlaveis
      181 rassedvqka lleayeqgtl kgeqllrvrk liskrealgk ayypkpssgr ddkptpqkll
      241 riyktevrrq qlniqkariq eerlllitsa mrhflsdehf rtllraeqis dipeviarri
      301 ptemlp
//
LOCUS       WP_175895602             429 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175895602
VERSION     WP_175895602.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..429
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=47143
     Region          27..84
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          116..318
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(131..132,134..135,138,142,144..150,244..249,
                     255..256,258..259)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrdtlepdal prrasdaaga ldvldarlmr illvlltert vsraavrlnm sqpatsaalk
       61 rlrtllgdpl lvrsrygmvp tefgarliep lrnalrvidf iriqqptfda rtsvrtyrig
      121 cpdylnvlfv pklvalfrer apnaqlvfhp lgdgfddera ladgeldvvi dnrparssrf
      181 rqddlfddrv vclmrathpl arhgamtaad fadapqlcpt pswleasgai drqlervglq
      241 rrivvtlphf elaahalvrt dmlltttyrl arhyakllpl aavalpvepp divyrmtwne
      301 sgacvdgvrw lrgliaeatr awldaeamlp avaavpagav adignsvpaa admsdmsdms
      361 dmsdmsdmsd tadptdptdt satsdtspta dapepvrrtr rrqathcras hpprvahaar
      421 ihrhatksh
//
LOCUS       WP_175895611             353 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175895611
VERSION     WP_175895611.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..353
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=39373
     Region          82..314
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mkpsqfakgf qarpdittse krtaldrlna idgivksetp astptksskk dnpqppapev
       61 vldastdesa qyrawrlenr yapgqvielp lkaikhspfn prhfylkssi aelavnlakq
      121 gqqqaihvip dydnpgtyfv sdggrrvral keankesvka ividvpigiq syklgydlnv
      181 qrdsqtvfdn avvwrrfldd qhfqsqkela ehlgldestv avalsigklp eaimqemvar
      241 pdrfgsnmay qvgryhsarg teatlrlink ivsddlstrq vsdivkgrva aqetpkpasr
      301 qryaqrleik lggksvgdlk sygedrielr lrglpkdkrd aileqlerml lsd
//
LOCUS       WP_175895629             227 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cepacia].
ACCESSION   WP_175895629
VERSION     WP_175895629.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..227
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24068
     Region          23..225
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mtdvlplttd pesglqyrlr paagrpvarl lllhgvggne tnllnlagii dprieiaflr
       61 apltfgpgqh awfpvrfgpn gpeidaaran esriqlitll rafrardgaa salptviagf
      121 sqggimsagv gltspddvaa favlcgrilp eidpliaprd alrplhaliv hgrlddklpv
      181 awadtadakl tslgvahdtr lydaghelte emagdfsrwv geragln
//
LOCUS       WP_175895652             309 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175895652
VERSION     WP_175895652.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..309
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33642
     Region          8..301
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mtssrtpryr gifpvvpttf tetgeldlas qqravdfmid agsdglcila nfseqfalad
       61 derdlltrti lehvagrvpv ivttshysth tciarsvraq qlgaamvmvm ppyhgatfrv
      121 peaqihafya rlsdalsipi miqdapasgt vlsapflaql areieqvayf kietpgaank
      181 lrelirlggd aiegpwdgee aitlladlha gatgamtgga ypdgirpile ayregrhdda
      241 faryqawlpl inhenrqsgi ltakalmreg gviaceaprh pmpalhpdtr aelvaiarrl
      301 dplvlrwar
//
LOCUS       WP_175895860             358 aa            linear   BCT 11-JAN-2025
DEFINITION  M48 family metallopeptidase [Burkholderia cepacia].
ACCESSION   WP_175895860
VERSION     WP_175895860.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Lew,R.A.
  TITLE     The zinc metallopeptidase family: new faces, new functions
  JOURNAL   Protein Pept Lett 11 (5), 407-414 (2004)
   PUBMED   15544561
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..358
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37746
     Region          139..322
                     /region_name="M48C_Oma1_like"
                     /note="Peptidase M48C, integral membrane endopeptidase;
                     cd07331"
                     /db_xref="CDD:320690"
     Site            order(205..206,209,262,266,306)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320690"
     Site            order(205,209,262,306)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320690"
ORIGIN      
        1 mrsnrlhrla rvaaswsvga aalaagfaah asdtgataat aagsapaaap asppatstsa
       61 apaqpataep aqptggaast kvytptpqqv rygnaiafrt lipsplleql taseyaqivq
      121 aaadsnrllp anqprvkrlr aivtklapys vkwndrvknw awdvnvirsr dirltclpgg
      181 kvlvygglle rvrlnddelg vlaahgiaha lreharsnfs aasqtslraa alpplfgvgd
      241 plpqalnlge rlqslhydpt deteadvigg diaaragfdp raaitlwdkl aaatrankat
      301 gfiythpyst arrqdllnrl pdlmplyaka igkrvdslpd yagisaqrrk vvrrgatg
//
LOCUS       WP_175895867             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175895867
VERSION     WP_175895867.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32474
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdkfsalraf vevaeaggfs sagrrlelaa ssvvravdal easlgtvlln rttrqvtlsd
       61 agavyyarak qlleelaead alvadrgdep sgplrvsvpv aygvrriaph vaaflarypk
      121 ldldlqltde rvdlvtgrid vairlgeaap saevvarplg afhryvvash dyldahgtpa
      181 tpgelvdhec lrfhfggdqq awafadahgt trvlvtgrlk snhsevlrea aldsagiall
      241 pdwlidadvq sgrlrrlfeq ydvtpdtars vvtalylpnq rgskrvaafi dfvetlaraq
      301 h
//
LOCUS       WP_175895868             279 aa            linear   BCT 11-JAN-2025
DEFINITION  polyphosphate kinase 2 family protein [Burkholderia cepacia].
ACCESSION   WP_175895868
VERSION     WP_175895868.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Motomura,K., Hirota,R., Okada,M., Ikeda,T., Ishida,T. and Kuroda,A.
  TITLE     A new subfamily of polyphosphate kinase 2 (class III PPK2)
            catalyzes both nucleoside monophosphate phosphorylation and
            nucleoside diphosphate phosphorylation
  JOURNAL   Appl Environ Microbiol 80 (8), 2602-2608 (2014)
   PUBMED   24532069
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Sureka,K., Sanyal,S., Basu,J. and Kundu,M.
  TITLE     Polyphosphate kinase 2: a modulator of nucleoside diphosphate
            kinase activity in mycobacteria
  JOURNAL   Mol Microbiol 74 (5), 1187-1197 (2009)
   PUBMED   19843229
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Nocek,B., Kochinyan,S., Proudfoot,M., Brown,G., Evdokimova,E.,
            Osipiuk,J., Edwards,A.M., Savchenko,A., Joachimiak,A. and
            Yakunin,A.F.
  TITLE     Polyphosphate-dependent synthesis of ATP and ADP by the family-2
            polyphosphate kinases in bacteria
  JOURNAL   Proc Natl Acad Sci U S A 105 (46), 17730-17735 (2008)
   PUBMED   19001261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..279
                     /product="polyphosphate kinase 2 family protein"
                     /EC_number="2.7.4.-"
                     /GO_function="GO:0008976 - polyphosphate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016776 - phosphotransferase activity,
                     phosphate group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006797 - polyphosphate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31933
     Region          7..277
                     /region_name="PPK2_rel_1"
                     /note="polyphosphate:nucleotide phosphotransferase, PPK2
                     family; TIGR03709"
                     /db_xref="CDD:274737"
ORIGIN      
        1 makqpalddf rvpyftreke aaafkldafd paakpfssgs kdddrerlsa vsteldvqqe
       61 rlhtqqkkrv llvlqgmdts gkdgtvravf revdplglrv vpfkaptpie aahdflwrvh
      121 aqvpaagela ifnrshyedv lvprvldlid akecerryrq irdfetmlve ngttiikcfl
      181 hiskdeqrar lqariddptk hwkfdisdld arkhwdayqs ayrdaltats aehapwyvip
      241 anskthrnvm iaelllrtmt dmklefpppk pelegvkir
//
LOCUS       WP_175895885             218 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175895885
VERSION     WP_175895885.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..218
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24650
     Region          1..210
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mltvwgrrna fnvqkvmwlv gelglahrhv paggpfggld apaflamnph grvpviddgg
       61 tvvweshsil rylaarygrp rfwsddpglq shadrwldws qttlqpaflt gvfrayfrtp
      121 peqrdnarve qsiaqcaryf rllddvltdq pflagdaitl adiaagthly ryfeldiarp
      181 plpnveawya rlkarpayrt hvmipfddlr gqlddpvr
//
LOCUS       WP_175895887             204 aa            linear   BCT 11-JAN-2025
DEFINITION  CGNR zinc finger domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175895887
VERSION     WP_175895887.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..204
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22452
     Region          11..204
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mvtrhepvrh ahewgavdfv gghpaldfln tvadtgktrd adkfvdwpav hawaersgll
       61 apadlarlrr harqddadal valhrfreea ysaiahltag gggtagaraa grlavairea
      121 igrsafdavd grfawrpdar vasrwvdaaa lgfehllrsd dfarvrqcgr ctwffvdrgr
      181 gvgrrwcdmr tcgnrakvea frar
//
LOCUS       WP_175895897             830 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia pseudomultivorans].
ACCESSION   WP_175895897
VERSION     WP_175895897.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 830)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..830
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..830
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=86786
     Region          <56..>201
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          208..747
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mrirtagrpa stdapdapda tpvtgartpg ldrrgflklt maasgclalg lastragaqt
       61 gsaartqapq afliiapdnt vtvavnrtes gqgvstalpm aladeldadw rnvrtvlapa
      121 gepykdpvtg iqmtvgstsv shsftqyrel gasaramlva aaaqrwnvdp atcrtahgvv
      181 tsgshsatyg elapdamamp vpqhvplksp dqfriigkpt prvdsravld gtlqygmdwr
      241 lpdmmvavva rpprfggqva synaaaarav kgvvevveip tdrggtgvav iangywaarl
      301 grdalqitwk dsgstvtsae qmqtykqlag tpgtvvrtaa agnappaatr irkdyefpyl
      361 ahapmeplsc tvdvgpanca cgikiwggss lqttdraava ralgvapakv qiftmmsggd
      421 ygrrstptsd yvveaarvsa aylaaghlgp vktiwtredd lrggyyrpmv lhrvdigvdd
      481 sgavrdwqhv vvgqsvlkgs plerttalrs gtdpdltdgv anspygfpvr vsvhqpevdv
      541 pvqswrsagh thtafvmetl vdelahaarq dpvayrmarl sgpeharhrq alalaveksg
      601 ygtralpagh awgvamheta gtvvayvtev siaaqqprvh rvtagvyagr ivnptgaeaq
      661 iqggalfgla ttkpgfaidv ehgavrnagf adyppvrmhe appvdvffvp sdahpsglse
      721 agvppiapav angafvltge rvhalpfapm lvaaaapalp aapaaeddpy adlpagdcri
      781 phkarpaalk pktaqsqagv gqpgavpkfl rprrragipc iedlkkgvtt
//
LOCUS       WP_175895905             482 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia pseudomultivorans].
ACCESSION   WP_175895905
VERSION     WP_175895905.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..482
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50111
     Region          25..478
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mshpatsapa paaqratpha gglrrnylsl peliaqsigl vgvsggigvl ipavfatagn
       61 gtwlaylfai vallfsswsi avfardsasp galyayvsag igpvwgaicg wslliayava
      121 asgilqgtvn tflvlgretg llgsatplgt vlgltvvtal aawyiafrdi rlstrftllv
      181 elatllliai vvigtiafgg hpvdhaqltl egvkptqlql gmvlaffsft gfesatvlga
      241 eardpfraip ravlisvigp ailfvigayg mvgafhgqtp sldrvdgpla vlahrlgagw
      301 igvlidagvs lsffaaffss inaaarivya fgrqgvlhas tgrahetnat phvavgliav
      361 lalvvalalt argtalldsy gylssiatyg wllayvlvai gaplylrrqg rlkaahvais
      421 vvavvllaip lagsvypvpd gvyawlpyvf aallaiglaw fvvlrvwfpq rlreleaell
      481 tk
//
LOCUS       WP_175895930             259 aa            linear   BCT 11-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Burkholderia
            cepacia].
ACCESSION   WP_175895930
VERSION     WP_175895930.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..259
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28713
     Region          10..259
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mtrdprltln arqqellewv qrdgfvtvdd laahfavtpq tirrdvnwla dlnllrryhg
       61 gaslptssen vsytarqrmf hdekrriaal aashipdqas lfinlgttte evaralnrhh
      121 glhvitnnln vasmmsgypd cevlitggiv rpwdkgivge laidfirqfk vdyaiigtsa
      181 ieadgtlrdf dtrevrvaea imqhartvyl vadhskvgrp alvrqghlsq vhalftdkpl
      241 ppemtdavat agtqvyvae
//
LOCUS       WP_175895939             710 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia pseudomultivorans].
ACCESSION   WP_175895939
VERSION     WP_175895939.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..710
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77192
     Region          9..699
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mtypslrdwl fsvktfaasm lalylglyfq lprpywamas vyivsnpfvg atrskalyra
       61 lgtalgaaaa vffvppfvea pilfsiivat wcgtllylai sdrtarsyvf mlagytmpmi
      121 alptvtdpgs vfdvaiarte eivlgivcas vvgstifpnr laptliertd awfkdaafyg
      181 retlsghiag kalsacrqrl astitglefl lsqlsydhah prvlaraqal agrmqlflpl
      241 mssladplia lmrdlqvrpp aldalladaa kwfdaplpav kagtdgdmtd dpvadrlrag
      301 iaalqpadga ltswegalls nalwrlhqvv diwqdcrslr alianesgvw qpryrhwrlg
      361 gterffdrgm mlfstltvvg aivfacwlwi ssgwhdgaga vtlvavacsf faaldepapl
      421 vfkfflstaa svvfaglylf valphvhdfp mlvlmfagpf iligtllprp qfnmvtmlva
      481 vntatfisiq gaydadffvf lnsnlagvag llfaylwtra trpfgaelav rrllrsgwed
      541 varsastqpl edqrnhasrm ldrvtqllpr lgasddhrhp siesfrdlri alnaldlrrs
      601 rrklsgdvpd aidrvlagvt dhytrcaaan arqpappall esiddalrrv adrnlpaapa
      661 taadaapaap tpaamhrwlr dslhalvglr lslypasaar apqapdgaqa
//
LOCUS       WP_175895951             375 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia pseudomultivorans].
ACCESSION   WP_175895951
VERSION     WP_175895951.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..375
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41920
     Region          88..328
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 masslvfihr vlgltaarrg rtqhadgspq hdgarfrnva prpveglgkv lgiawnmlvn
       61 kprdtapaga lpvdvltreq ldnapdrsly rlghstlllk lrgefwltdp vfaeraspfr
      121 hfgpkrfhap pialddlppl rgvilshdhy dhldrdtvla laattgvfvt tlgvgdrlie
      181 wgidankvrq ldwwqsidvd gltltatpaq hfsgrslfdg nstlwaswvi vdddlrvffs
      241 gdtgyfdgfk tigerlgpfd vtfietgayd aqwpyvhmqp eetvqahidl rgrrlmpihn
      301 gtfdlamhrw qepfervtal altrgvalst prmgerldln qphrgeawwr paeapakapt
      361 tksrrwqlca sqatk
//
LOCUS       WP_175895953             342 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175895953
VERSION     WP_175895953.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..342
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37341
     Region          67..270
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 makdtskekk ptgnlhlaag llrglaqena aletrlpepl aatpaaaeps pvaapaaatp
       61 vdaldlgapq kvavkdcipn pfnprvfyse sslhelaltl kregqiepik vtrlpefpgk
      121 lvvidgqrrl ratsingdet inatfrtdht peqlytiayr anhdherqti fddavawkrl
      181 ldekvfpdqn tlaekigkdk asisktlsln alpntllerm agandvvglq aayflklife
      241 rlgeptadrl ltavierkks vrdlenflra qsdgskkagr trysvrhdfa lesraigqlk
      301 typdgrldlq lkgvdaaqqe aladklktvi dayvaelaaa qk
//
LOCUS       WP_175895973             318 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Burkholderia cepacia].
ACCESSION   WP_175895973
VERSION     WP_175895973.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..318
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33018
     Region          3..296
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(36..37,40,91,105,107,136,168,256,259,295)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(227,232,247,256..258,261,283,287)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 maeivvagel laefvaaerg qgfdspglfa gpfpsgapai fadqaarlga rvayagcvgr
       61 dafgdaivar lerdgvdvar irrvarptgt afvayrddgs rsfvyslsts aaacveasdv
      121 dtamfdgcry fhvmgsslts esaiaavqrg vieaaragak vsfdpnvrpe mlsfrpmraa
      181 letmlaachl fmpseadlpf fcgpqpaera iagllathpl lervvlkrga qgsvafdran
      241 rveapafqvd eidptgagdc fggtlvasfv agvpidaalr ranaagaiav trrgpmegns
      301 gaaeidrflt ergiacpa
//
LOCUS       WP_175895989             487 aa            linear   BCT 11-JAN-2025
DEFINITION  catalase [Burkholderia pseudomultivorans].
ACCESSION   WP_175895989
VERSION     WP_175895989.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..487
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54915
     Region          3..479
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 msdqsndrkl thangapvgd nvniqtagpr gpallqdvwl ieklahfdre viperrmhak
       61 gagaqgtftv thditrytka klfsaigkrt pmfarfstva gergaadaer dirgfalkfy
      121 teegnwdlvg nntpvfffrd plrfpdlnha ikrdprtgmr saesnwdfws llpealhqvt
      181 ivmsergipr sfrhmhgfgs htysllnaan ertwvkfhfr tqqgienltd aqaealiakd
      241 rethqrdlfd siergdfprw tlfiqvmtda qakafrfnpf dltkvwpkae fplievgcfe
      301 ldrnpdnffa eteqaaftpa nvvpgigfsp dkmlqarlfs ygdaqryrlg vnfnhlpvna
      361 pqcpfhsyhr dgvmrtdgnl ggtpsywpns kgvwtdqpql neppleldga aahwdhrvdd
      421 dhyrqpgdlf rnmnaaqrqt lfdntarqia gvskeiqqrh iancakadpa ygagivaala
      481 rlavqrg
//
LOCUS       WP_175896040             439 aa            linear   BCT 11-JAN-2025
DEFINITION  replication-associated recombination protein A [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175896040
VERSION     WP_175896040.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..439
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=47449
     Region          1..430
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 msdlfspepr rpladalrpa slddvigqth llgagmplrr afesgkphsm ifwgppgvgk
       61 ttlarltaqa fdcafvalsa vlggvkdira aaaraqqafd eagrrtivfv deihrfndtq
      121 qaallpsvas gavifigatt enpsfevnra llsrarvyvl kplsedelrs lfdrvrgial
      181 gklsfdddar dtlvahadgd arrflnlleq vrtaaesagl ttldagfiar tttsgarrfd
      241 kggehfydqi salhksvrgs npdaalywlc rmldggtdrr ylarrivaia yddigladpa
      301 alriandaar tsdrlgapdg dlalaqavly lacaaksnag gmalmqaraf vrqdrprevp
      361 ahlrdvpdel tpalgrayrn phdaphgyaa gesylpdgmq apywyrptsr gveagiaerl
      421 dalrrldrda vsgafsrtr
//
LOCUS       WP_175896075             163 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175896075
VERSION     WP_175896075.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..163
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17727
     Region          13..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mpkrlslpav asldatdrai laaladdari atselarqig lsapatadrv rrleaqgvia
       61 aftveldpra lgytlqaivr vkplpgqlhl veemlrripe fvecdkvtgd dcficrlylr
      121 tiahlddils kvteraetst aivkstpvpr rlpplveddg ahr
//
LOCUS       WP_175896094             338 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia pseudomultivorans].
ACCESSION   WP_175896094
VERSION     WP_175896094.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..338
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37848
     Region          171..316
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 medtltkpad aahavegeva aaldgaahgq vapeavhrld awrpddppaa llaafvalfn
       61 tdtrrdaati slplagtdpa avasyvarav rdgvidgaqa vgdrlhvtas ratfwqnpqp
      121 wlkapasggm plrytitngh rhpvrpptpa geiyardmpq vgmtfslrtv dvdahadlfs
      181 gwmnldrvah fwdqrgtrde haaylaerla dphmhpmigy fddtpfgyfe fywakedrla
      241 pfydahdydr glhlligdsr fqsagklhaw wsgvlhymfv deprtqrlvg eprvdhvrhi
      301 aymhrlgfyt lkefdfphkr aaltvierdt ffdtfrlp
//
LOCUS       WP_175896100             337 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia pseudomultivorans].
ACCESSION   WP_175896100
VERSION     WP_175896100.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..337
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37031
     Region          180..316
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mlaevrpdgf tmpdtcrlaf adglfaardg aeirvaqgdg igaqllraql addgtlrvva
       61 ynhraapadq rrallaalsa afsddakraa irvdlaawpa valdalrasg vlgdggrcmr
      121 egwaqqadlw lvdarplcat lqtlsdgrrh prrppaprgd iyardlpalg vrftlrgwqp
      181 dedaarvarw fdeprvrdgw tgaqpgthda dphltplvgc fdgepfayfd afwlkedpla
      241 phvaardydr glrmlvgepr wrgphcvagw lpcvvhylfl ddprteavgc avpagharla
      301 dylarhgfar qrrlaladaq plwmrtlret ffagrhv
//
LOCUS       WP_175896102             194 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175896102
VERSION     WP_175896102.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..194
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21223
     Region          1..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 metkptvrdq ildhaitlmm qrgyngfsyr dlsdlvgvkt ssihyyfpsk ddlvleavaa
       61 ysdevlaavr aidpalpadv klslytkmfg rtlgdgnlic lcgmlaadie tlpenvrqav
      121 qaffkanesw laellkqgaq egtlqfsgep dtaartlyaa fqgsvlasrl fhtrarledv
      181 eavwksgpdg armq
//
LOCUS       WP_175896114             282 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175896114
VERSION     WP_175896114.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..282
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29610
     Region          7..260
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtrstaalaa rgltvgyrdh vvidgldlsi aagrvtalcg pngcgkstll rtlaglqpar
       61 aghvevngrp lasfrrrala reltmlaqfn qipsgltvre lvaygryayg sflrglsrad
      121 haaidealat sgladdagrd vgalsggerq rawiamalaq qapivlldep ttyldihhql
      181 dildalrtln rtrgltivwv lhdlnqaaay sdeivlmrag rlvaqgvpda mldparlraa
      241 fgvemlklah pqtgapmcvp aygpsaagta qaagafdgdl at
//
LOCUS       WP_175896120             379 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175896120
VERSION     WP_175896120.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 379)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..379
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41437
     Region          18..379
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mihtlpaasv aagmcrdada fvrienvvkk fgdstavdnv nltiaknelf allgssgcgk
       61 stllrmlagl etatsgkifv dgedlaslpp yrrpvnmmfq syalfphmtv esnvafglkq
      121 egtpkneire rvadalalvq mskyakrkph qlsggqqqrv alarslvkrp klllldepms
      181 aldkkirqkt qlelvniiek vdvtcvmvth dqeeamtmas rlavmsegki vqigspgevy
      241 eypnsrfsae figstnlfeg rvvedesdhi fvesddlear myvshgvtgp lgmpvgisvr
      301 pervhvsrek pgskhnwarg vvtdiaymgs yslyhvrlps gktvvsnlss shlmndnapa
      361 wnddvfvsws pasgvvltq
//
LOCUS       WP_175896145             352 aa            linear   BCT 11-JAN-2025
DEFINITION  permease [Burkholderia pseudomultivorans].
ACCESSION   WP_175896145
VERSION     WP_175896145.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..352
                     /product="permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=36895
     Region          61..346
                     /region_name="YraQ"
                     /note="Uncharacterized membrane protein YraQ, UPF0718
                     family [Function unknown]; COG0701"
                     /db_xref="CDD:440465"
ORIGIN      
        1 mtttrtqpsp algwmtflli avaglfyvkw fpyynkafva aehhsigqsi lmgtsatape
       61 pslkaaldya waygkaiwqa mvlglllgsa vqallpahwv arvlgrtgfg svaaggllsl
      121 pgmmctccaa pvvaglrarh aspggavafw lgntvlnpaa lvfmgfvlgw hwsalrlvlg
      181 vamvfgigyl lnriarpedr siddaqlaal aadqaaagnp fvrwikllar mavrlvpeyi
      241 vlvlllgaar awlfphigpd ignhlgwiva favagmlfvi ptagevpiiq amlslgmgvg
      301 paaallmtlp pisvpsiaml arsfkpymla ivavlvvafg iasgllavaf gf
//
LOCUS       WP_175896150             338 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175896150
VERSION     WP_175896150.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37679
     Region          60..210
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <223..319
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhpapaqysp gqqvdtapla afnrvpprst rqsresdlrl tlaervarwt dgvdhlttvi
       61 pnlslhrret ptqpmgcmve psfglvvqgt kriiqsgdvy lcdanrflit sldlpgstqv
      121 ieasretpfl giglkldfra maelmaqvap dhedtpagrg lvvgdmtepl ydavnrllal
      181 lddpnaiavl apyvereiyy rlltsdqggr lrqiasagsq gnrvsraiqw lrthydeslr
      241 vddlatqvqm ssstfhhhfr qltgmsplqy qkwirlnear rlmlserlda tsasfrvgya
      301 sptqfnreys rlfgnsprrd idnlrsgtdv vpsvaaty
//
LOCUS       WP_175896217             826 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 2 protein [Burkholderia cepacia].
ACCESSION   WP_175896217
VERSION     WP_175896217.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 826)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 826)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 826)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 826)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..826
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..826
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90229
     Region          10..>626
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mtrtraqpaw smlataagaa reprdlpaag ngwipaavpg tvaqslalag rldeavslde
       61 rdhwyrielr ghgprvlrfh glatlaqawl ddtpilhsds mfvahdvpvs ldgshrltlc
      121 fralaphlrd araprrarwr trlaepaalr tirtslfghm pgwfpphvpt gpwrpvdvld
      181 padgpvladc nlhariegdt gwldadltfa aplpdalaar lscgqhhatl eragpdrlra
      241 svavpnvcrw wphthgepvl ydialhigde rrplgatgfr tievdpgadg kgfglrvngv
      301 pvfargacws saaplalhad datyarllgl ardagfnmir vggtmtyead afhawcdrlg
      361 llvwqdfmfa nfdyalddpa faanvdrear qflsrhgasp slavlcggse iaqqaamsgl
      421 gpkqrflelt adrlaghaaa crpdvpyvpd spdggvlpfm prervshyyg vgaylrpldd
      481 arradvrfas eclafsnvpc datlaelgwp gvheprwkaa vprdpgtswd fedirdhylq
      541 tlydvvpdrl rredparyfe lsravvadlm retfsewrrt gsrcagaliw qfqdvmpgag
      601 wgvidaahrp ksawhalrqv lqpvqvllvd eglngldvhv vnerpaplsa alelvalrdg
      661 rtavaragcp vriaahdtvr igsaellgrf fdwtyayrfg pcehdtvvat lrgddgtlls
      721 qafhfpsrth pavlarrelg leacvsrtgd twhvdidtrh varhvqidap gfvprddwfh
      781 lapgtparvv lvplgtagkn gaadeppave iravnaarav ramqag
//
LOCUS       WP_175896174             817 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175896174
VERSION     WP_175896174.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 817)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 817)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 817)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..817
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=86929
     Region          1..803
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mlvvgsqsha tefnssflsi dgasnvdlsq fsqadftlpg eymldvqvnd lfyglqsief
       61 valdasgagk pclrpelvaq fglkpslmkg lprfqggrcv dlgaiegatv rylkgdgrlk
      121 itipqaalef tdstylppdr wsegipgaml dyrviantnr nfgaaggqtn svqaygtvga
      181 nwdawrfrgd yqaqsnvgnt vyadrtfrfs rlyafralps iqstvtfgdd ylssdifdtf
      241 altgaslrsd drmlppslrg yaplisgvar tnatvtvsqa grvlyvtrvs pgafalqnin
      301 tsvqgtldva veeedgsvqr fqvttaavpf lartgqlryk aavgkprlfg gagitpffgf
      361 geaayglpfd vtvyggfiaa sgytsialgv grdfgtfgal sadvtharar lwwngatrng
      421 nsyrvnyskh fdgldadvrf fgyrfserey tnfaqfsgdp tayglanskq rysatlskrf
      481 gdtstyfsyd qttywqrtse qrigltltra fsigalrnln vsmsafrtqs agasgnqfsv
      541 tatlpiggrh ivssnlttgn gstsvnagyl yddadgrsyq inagatdgra sanasfrqrt
      601 sayqltaqas tvanayaaas levdgsfvat qygvaahang nagdtrllvs tdgvpavpls
      661 gtlahtdsrg yavldgispy nvydaavnve klplevqvsn piqrmvltdg aigfvkfsaa
      721 rgsnlyltlt dpagkplpfg asvqdaangk elgivgegga ayltqvqpks slavragert
      781 lctigvlpnq lqlegtpipv tcqtpgesha aaarder
//
LOCUS       WP_175896252             709 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia cepacia].
ACCESSION   WP_175896252
VERSION     WP_175896252.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 709)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..709
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=77550
     Region          26..>212
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mnavtteipa lahdagvppa ppeahrtade lrdiplkrlv aspynvrrvp ptgikelaln
       61 iwkvgqlqnl ivhpmkvgar kaqtfgaaag errrlaliyl lehdyisadh pvrcrvvpve
      121 davllsaten emrepmhpad acdayrilve sgrsieeiad lygvhpktvq rrlklarvsp
      181 klvdlfrtge ikldqmqala lsdshaeqea awfdaepynr dahairrrfv rdeqsfvsnr
      241 vakfvgveaf eaaggavrrd lfsaaedawy rdhalmlrla teqlealgas vlaegwawvk
      301 amperdhatr sqfrpvlprr teptdevake laaidqrlae iaaqweaddm ddeaaerlel
      361 eegalsmrqd eiegsllvyh pddmaqagal lsldangepv ierglvarep vavattesge
      421 ngddddddss agqparvdap avkpakgphs erltlrlnah rtaavaaala qqphvalaal
      481 vhrllageyg hstegsaldv tfrdhshtlt khapeldddl aftmrreqrr vwggvipnds
      541 dallrwlieq tderlllila qyvaasvdsv rpderphain alipalglnl adawqptkag
      601 yfdhvskdri vdvvsaavsp sdamrvaklk kgdaateaer liagrgwlpe hfamaevvrv
      661 klwdvpakas dteasadeae adepalvasa ddvrddtava egegmpard
//
LOCUS       WP_175896280             146 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydroneopterin aldolase [Burkholderia pseudomultivorans].
ACCESSION   WP_175896280
VERSION     WP_175896280.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Illarionova,V., Eisenreich,W., Fischer,M., Haussmann,C.,
            Romisch,W., Richter,G. and Bacher,A.
  TITLE     Biosynthesis of tetrahydrofolate. Stereochemistry of
            dihydroneopterin aldolase
  JOURNAL   J Biol Chem 277 (32), 28841-28847 (2002)
   PUBMED   12039964
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..146
                     /product="dihydroneopterin aldolase"
                     /EC_number="4.1.2.25"
                     /GO_function="GO:0004150 - dihydroneopterin aldolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0046656 - folic acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16409
     Region          23..133
                     /region_name="FolB"
                     /note="Dihydroneopterin aldolase [Coenzyme transport and
                     metabolism]; COG1539"
                     /db_xref="CDD:441148"
ORIGIN      
        1 mkpfdepfaa idaprlrgrg wsvfvdelkv parigihahe heapqpivid arleyrceps
       61 eqgewidydg ycarvasfla hkphtrllet lvadlavlsf rewpaleslt lsvhkpkirp
      121 gtkrvgvsld wtrgdylrwt gaagqi
//
LOCUS       WP_175896301             421 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175896301
VERSION     WP_175896301.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..421
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=44063
     Region          205..412
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(212,252,290,393,396)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(212,393,396)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(212,252,290)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 msfrssfaaa vlgasvflsp vaawaapagw vaawatalqp ipelaapppl yrapdvagrt
       61 vrqivyptvs graarirvsn aygraplvve aasfarageg aaladaapvl vrfggrasvt
      121 lapgqelesd pvaievsagr pyavslhlga nqrmtvwhrv snqlnyvstp gdhvndsgaa
      181 afrtrftqya wvselavetg sarasvaaig dsitdglrss ldrnrrwpda larrltaaga
      241 dsigvvnlgi sgnrllsnsp cygtslasrf erdalsragv kaaivligin dinfaampph
      301 agldcdypht qvtaaslidg yrrlieaahr qgvkvfgatl tpaglpaare airlevnrwi
      361 rsgggfdgvv dfdavlrdpa rpsvlqrryd sgdgihpsda gysamadavp verlqavavg
      421 k
//
LOCUS       WP_175896363             222 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175896363
VERSION     WP_175896363.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..222
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23706
     Region          29..187
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpprhvqvpa ppgqpaaqps palrrrprqs raqassealq qafvqllrer gyakatirei
       61 aavagvsvgt fyeyfgdkqs laalcihrrv lamadrlraa aqalrgtpra elaaalvdlq
      121 idvigadapl wsalfalerq vsplaayrrh ydayvalwrd alahaadppp aarldglarm
      181 aqtvcyggis qalltlgpal dfaalrgelq avlraylaai dg
//
LOCUS       WP_175896419             378 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175896419
VERSION     WP_175896419.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..378
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40355
     Region          1..355
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfqhtedrr mladtlnrfi aeqypfavrd riaqsadgfd ramwqrfael gaigalfpea
       61 dggfggagfd iavvfeclgr glvvepflga llagralala ggdahrakla alidgsasaa
      121 fahdepgshy elttvrtrae rsgdgwvltg akgvveqaaq aaffvvsarv agadddaagi
      181 glfvvpadap gvslrdyrki dggraaelrf ervalpadaa lvdphgeqga arleqvlgfg
      241 llalsaqalg amdvakeytl dylrtrkqfg mpigsfqalq hrmadlllev eqarsavina
      301 aaqldaprlv reralaaaky tigrigtlva eesiqlhggi gmtwelplsh yakrlvmidh
      361 qvgdedhhla ryialskq
//
LOCUS       WP_175896424             177 aa            linear   BCT 11-JAN-2025
DEFINITION  TlpA disulfide reductase family protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175896424
VERSION     WP_175896424.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..177
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=18928
     Region          41..157
                     /region_name="TlpA_like_family"
                     /note="TlpA-like family; composed of TlpA, ResA, DsbE and
                     similar proteins. TlpA, ResA and DsbE are bacterial
                     protein disulfide reductases with important roles in
                     cytochrome maturation. They are membrane-anchored proteins
                     with a soluble TRX domain containing a...; cd02966"
                     /db_xref="CDD:239264"
     Site            order(72,75)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239264"
ORIGIN      
        1 mnttppvqgr spvryiaaav ivaaiavagf fafngkssvp datftllsgq kvstagdlkg
       61 kvylvnfwat scatcmqemp qmvetynrfk gqgldfvava mnydppmyva nyaqtrqlpf
      121 kvalddgsva kqfgnvqltp ttfvvdkdgk ilkryvgapq faeldallkk aldgnaa
//
LOCUS       WP_175896444             271 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Burkholderia pseudomultivorans].
ACCESSION   WP_175896444
VERSION     WP_175896444.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 271)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..271
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29013
     Region          1..271
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkrrsllkvf svlatgaalt lsagahaedk vikvgtvagp daevwqvvqk vakekeglnv
       61 kviefndyvq pnaaldagdl dansfqhqpy ldsqvkqrgy klvsagltyi spmgvyskkf
      121 kslkdlpqga klavpndpsn enrallllqa qgaiklkaga gtggnnatvl diadnpkklk
      181 iseldaaqlp rvlsdvdaav intnyalaan lqptkdaial esltspyanl iavrakdkdq
      241 pwvkklvkay qspevkefik kqfkgsmvas f
//
LOCUS       WP_175896437             284 aa            linear   BCT 11-JAN-2025
DEFINITION  ComF family protein [Burkholderia pseudomultivorans].
ACCESSION   WP_175896437
VERSION     WP_175896437.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..284
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=29698
     Region          109..254
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mvrrslprpv rvvlsqvral aarmatvalp nrcalcgnls havictacda aywnearlrc
       61 dmcavplgig aprrrdghtg cghtgfghtg fghtgsgrtg aaraaayrck acrtapppfd
      121 atlaladyra pldglarglk fharlalgae faarlarlvd dtrgaggfdv vapvplshrr
      181 lvargynqaw aiarplarrl gvradatlla rvaetapqsr ldrrarrdnv aaafavagdv
      241 agrhvalvdd vmtsgatlaa aahalkaaga arvtnlvalr tard
//
LOCUS       WP_175896461             379 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter, partial [Burkholderia cepacia].
ACCESSION   WP_175896461
VERSION     WP_175896461.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         <1..379
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          6..373
                     /region_name="MFS_YajR_like"
                     /note="Escherichia coli inner membrane transport protein
                     YajR and similar multidrug-efflux transporters of the
                     Major Facilitator Superfamily; cd17472"
                     /db_xref="CDD:341025"
     Site            order(13..14,17..18,21,55,105..106,108..110,113,135,
                     138..139,142,205,208..209,212..214,217,244,248,292..293,
                     297,301,324,327..328,331..332,335)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341025"
ORIGIN      
        1 rattslaaif alrmlglfmi mpvfsvyakt ipggdnvllv gialgaygvt qslfyifygw
       61 asdkfgrkpv iatglvifai gsfvaafahd itwiivgrvi qgmgavssav lafiadltse
      121 qnrtkamamv ggsigvsfav aivgapivfh wvgmsglfai vgvlsilaig vvlwivpdaa
      181 kpvhvpapfa evlhnvellr lnfgvlvlha tqtalflvvp rllvdgglpv aahwkvylpv
      241 mglafvmmvp aiivaekrgk mkpvllggil ailigqlllg saphtiliva ailfvyflgf
      301 nileasqpsl vsklapgsrk gaatgvyntt qsiglalggi vggwllkhgg antvfytcsg
      361 lvaawliiaa smkapprka
//
LOCUS       WP_175896503             228 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia cepacia].
ACCESSION   WP_175896503
VERSION     WP_175896503.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 228)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 228)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 228)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..228
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22730
     Region          27..123
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          140..213
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mndtvhtprr rfaplllaaa tllagharad daalgktlat kgsttgaaac igchgsqgeg
       61 naaagfprla gtsaaylsaq laafadgsrq npvmqplskl ltpherdavs ayfaslpapa
      121 givaaddtsi dpantgawla trgrwsqglp acaqchgpgg lgvgsafppl agqpaayiag
      181 qlngwkhgtr ppgpmalmpa iagklsdadi davaayyarg gaaqgdkr
//
LOCUS       WP_175896505             312 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia cepacia].
ACCESSION   WP_175896505
VERSION     WP_175896505.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..312
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32746
     Region          90..290
                     /region_name="TsdA"
                     /note="Thiosulfate dehydrogenase TsdA, contains C-terminal
                     cytochrome c domain [Inorganic ion transport and
                     metabolism]; COG3258"
                     /db_xref="CDD:442489"
ORIGIN      
        1 midrttlirr traallgaaw mpalafaaap qdappangsa sapsavaaaa gpfappaesa
       61 ipadefgktv klgeqiflht pefagkyvgn kltcaschld agrrpdsspm waayllypay
      121 rsknghvntf aerlqgcfry smngkappag dpilvalety sywlakgapv gtklpgqgfl
      181 klpppaqkad yargaavytq hcalchgadg qgqssggkav fpalwgarsf nwgagmgdir
      241 naagfikanm plglggtltd qeawdvatfm dsherpqdpr ftgsvhdtra kfhdspdsmy
      301 glsvngrvlg ap
//
LOCUS       WP_175896518             415 aa            linear   BCT 11-JAN-2025
DEFINITION  lactonase family protein [Burkholderia pseudomultivorans].
ACCESSION   WP_175896518
VERSION     WP_175896518.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..415
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44012
     Region          52..411
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 mpnrlrehda rastrgfplr fahwmkgfai vlslsathaf aqqspapadg vynllvgtyt
       61 gggsdgiyvy rfdtktgsva pvssaktvnp syllpsrdgq tvyavnelpg dngpadqrgg
      121 vsafrfdakt galtfidrvs segndpcyla lspdgkylvt anysvaadpg gsfavfpign
      181 ggavgpavlt vhhegtgpvk grqdgahvhs tvfspdgryl fvqdlgtdki ygyrytvdgs
      241 rglisptdtr ytpvkagsgp rhmvfsadgr fayvtselna svevfgyhdg kltpvetvsm
      301 tapgfkgkvg ggaihlspdg rflyasnrgd andiviyavn radgrlktvg rqsslgrtpr
      361 eflidptgkw livgnqdsdt fyvfsrdvdt gllganpqkv svgkpvdfkl vavpq
//
LOCUS       WP_175896519             743 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia cepacia].
ACCESSION   WP_175896519
VERSION     WP_175896519.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..743
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=81883
     Region          48..715
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mnrfvpllrd awlrcrarva plaaasrari ralcagawhr lrhptrrgva ltlaaipmag
       61 llvllafvpf tpsigdirka ridrparvls adgqviaefr pvnrewvplk qisphmvdal
      121 iatedhrfya hhgidwrrtl aaglhtfsgs rqggstitqq larnlypdev graptltrkv
      181 kelitafkie tvyskdeile tylntvpfly naygvemaar tyfgksadql divesatlvg
      241 mlkgnsyynp vlnperavqr rnivlarmaa mgmlsprqla qlqrrplrvd fepqtaqpgp
      301 aphfavqlrk wliawadrnn ydlysdglvv rttldaqlqd mamqaltqqt drlqavadsa
      361 wrgpsgcglr ndlfrgfirq tpdyrdaraa gladvaalkq lganrafmha lcerktqvqa
      421 gfvaidprng airawvgspd fgsepfdhvv qarrqpgstf kpfvygaafa dgmrpgdtfv
      481 drpvaipigt havwrptdae pptdapmtlr dalalsrnri taqvmqrega arvaqlaram
      541 gvrespldav pslalgtspv tlkemvsayg tianrgvyva pqmitriedr dgkvlaafns
      601 apperalpva aaqtlvdvmr gvvdygtged irsrygirvd vagktgttqd ntdgwfilmh
      661 pqlvagawvg fddgnvtlrs dywgagahsa lpivgafyda alrtraidpr aqfspdfrpr
      721 sapapapkrr phpglfdwlr ffr
//
LOCUS       WP_175896525             449 aa            linear   BCT 11-JAN-2025
DEFINITION  NCS2 family permease [Burkholderia cepacia].
ACCESSION   WP_175896525
VERSION     WP_175896525.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..449
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45913
     Region          14..443
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 msatdtmpar apaswlerrf alaargtsvr aetiagvtsf laaayllvvi psllatggme
       61 rgaattativ vfvlfttlmg lyanlpflvg pgiggsviig vtlattehvg wqtglgiacv
      121 sgilffllti lgargvvmkl ipvqiklglg asiglfvtml glrnagmvva naktnafalg
      181 dfsrpgalva liglavaivl qarkvpgail iailvaaaag vplgvthlpa sfvslphsia
      241 piafkldigs alslaaapyl faffaaeffs tlgtalavga kanlldeqgn lpninrpflv
      301 dslaatigpv fgipaltali esaagveagg rsglsslaaa alfaamllfv pvalaipkea
      361 tapaliligl smfatirhth fddftdalpv msmvlltlms nsfgtgiagg llcyvlvkll
      421 agrrrdvswg lvvlalplgy yfwtvvkph
//
LOCUS       WP_175896583             321 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia pseudomultivorans].
ACCESSION   WP_175896583
VERSION     WP_175896583.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..321
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34651
     Region          12..227
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(56..57,59,73..75,81,83..84,125,226)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(56,58..59)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(81,84,87,94)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(117,121..124,126)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(122..123,147..149,199..200)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          237..321
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 mnaresifvd vvavetltpl ikrftlalpd gaplppfsgg ahvlvsmqng dqwhhnaysl
       61 lssphdtrqy qiavrreeas rggsafmheh vaagtrlaig tpanlfelar narrhvfiag
      121 gigitpflaq laehapggdv elelhyayrs pehgafvdel kagphaanvh tyvdslgqrl
      181 dlmqlfkslp adahvyvcgp qglndavyan aallgwpksq lhseqfaatd tagqaftvvl
      241 arsgielevp edttilqaie ragvkidslc regvcgtcev ailegeadhr dqyldddeka
      301 aqktillcvs rartprlvid l
//
LOCUS       WP_175896635             535 aa            linear   BCT 11-JAN-2025
DEFINITION  multicopper oxidase family protein [Burkholderia cepacia].
ACCESSION   WP_175896635
VERSION     WP_175896635.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..535
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=57882
     Region          88..535
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mirrtflsra igvaaaslfa raawaqhagh agmagmesmd dmpsmssmsg maghgqhgks
       61 apaalaaada lpagaplaal rtlanesrep gtfratlvaq pvarpmlqga gpttfwqfga
      121 gtqgpvvgpl idvregdtve ikfvnklpqp stihwhglpv ppdqdgnpsd pvapgasrvy
      181 rftlpkgsag tywyhphphm mtaeqvfrgl agpfvvraad dplagwpern lfvsdlklar
      241 dgtiapndmm dwmngregqf vlvngarrpr idvagderwr vwnacsaryl riafddgraf
      301 ehagtdgglf daprrvtsll iapgeraell vragdrasra vlqaaeydrr kmsmshddgh
      361 gslpadpala ladvafapat arvlpttlra vpplgepvah ktvafgeemd mdammkgpah
      421 grlagmrfti ngetyaahra tltsrrgdve rweirnttdm dhpfhlhgtq fqvierasgg
      481 srtsepfraw rdtvnvrsge tvtilvtqdm rgermfhchi lehedlgmmg tlkvv
//
LOCUS       WP_175896656             200 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Burkholderia cepacia].
ACCESSION   WP_175896656
VERSION     WP_175896656.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18951323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..200
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=21342
     Region          15..139
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(20,22,77..78,81)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            22
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(76,120..121,123..124,128)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(82,87..88,116,119..120,123..124,127,130)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(105..107,116..117,120..121,124,128,131,135)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(105,121,124,128,131,135)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(129,135..136)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          151..193
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
     Site            order(152..154,187..188,190..192)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 mtttkkrtrn lpghvigyar vstadqdaam qrealtvaga arvfedvasg sradrpglaa
       61 alaylregdt lavwkldrlg rslphlvqtv adleqrgigf rsltenidtt tpngrlvfhl
      121 faaladferd lirertragl aaakargstp grrpvvtpsk lararelidt kgltvreaaa
      181 rvkvgktaly kalgatadas
//
LOCUS       WP_175896669             555 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia pseudomultivorans].
ACCESSION   WP_175896669
VERSION     WP_175896669.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..555
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59828
     Region          5..550
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mqavanplaa vtiftarril tmnpaqpsat hvavregril avgdaadaaa wraqhgactt
       61 ddtlrdkvlm pglveghchl megamwdavy vgyydrrgpd gtlwpglrsl davldrlaaa
      121 eramnddgpl lawgfdpiff gtarltvrel drvsarrpia ilhasvhlmn vngamlarag
      181 idedtdvdgi trdadgrptg elqefaamfp vyqtiggkla isasekphai rnfgrvaqla
      241 gvttatdlvn dlspdgnrtl rdvtddpdfp vrivpafapq rnpargadsv laaigrntdk
      301 lrfgpvkfiv dgsiqgftar vrwpgyaggq pnglwlippa qlvdafepfh caglqlhvht
      361 ngdeatevvl damttllarh prpdhrhtlq hcqmadaaql ariralglcv nffanhlyyw
      421 gdahysqtig pdranrmnpa gsarrlgvpf alhsdapitp lnplftawca vrretasgrv
      481 lgegerigvd dalraitlga aytlkmdhlv gsievgkfad favldddpsa caperlntlt
      541 isgtvlggrv frspr
//
LOCUS       WP_175896672             294 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175896672
VERSION     WP_175896672.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..294
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31648
     Region          1..>157
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          91..286
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,221,238,265)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     215..219,226..227,230)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 melndlrifv atvdagsfta aadqlmlskq fvsrrtmale aslgvrllhr ntrnlavtes
       61 gqefyaraqr ilaevadaeq amsvrstelh gslkisapls fgithlspli aeflsahpav
      121 rlnldltdrr vdligegfdl vlrigsleds tliarplgaw rmiacaspay lkrhgtpatp
      181 aelanhtcll ygrerrvgwe frvdgaartf dvqgplvann gevvrdaaia glgiallphf
      241 ivggaldgga lvpvldayap apitlnavfp qhregfvtlr tfigflaerf grsa
//
LOCUS       WP_175896679             188 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175896679
VERSION     WP_175896679.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..188
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20668
     Region          1..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 metkttvreq ildhaitlmm lrgyngfsyr dlsdlvgvkt ssihyyfpsk ddlvleavsv
       61 ysddvltamr aidpalpada klsrytklfg rtlgdgdric lcgmlaadie slpdtvrqav
      121 qaffranenw laellaqgak egtlvfsgpp etaartlyaa fqgsvlasrl fhtrarledv
      181 eavwkara
//
LOCUS       WP_175896685             146 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia pseudomultivorans].
ACCESSION   WP_175896685
VERSION     WP_175896685.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..146
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15185
     Region          17..135
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mgpgtgnpaw irallsqpwv lpvarlalvs ayligglgka ldfdgavaeq arfglhpaal
       61 wavlaiavei vgslcvvlrr ftwlgagglg mltlvamtva ndfwnqagaa rfmvlnsffe
      121 hlgliaalvf vtvlgdvqrg eagsra
//
LOCUS       WP_175896718            1050 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175896718
VERSION     WP_175896718.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..1050
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114636
     Region          11..1026
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mspsheegrf nlsawalrhq alvvyliala tlagilaytr laqsedppft frvmvirtfw
       61 pgatarqvqe qvtdrigrkl qetpaidflr sysrpgesli fftmkdsapv kdvpetwyqi
      121 rkkvgdigyt lppgvqgpff ndefgdvytn iwtlegdgfs paqlhdyadq lrtvllrvpg
      181 vakvdyfgdp dqrifievnn aqltrlgisp qqlgqainaq ndissagtlt taddrvfvrp
      241 sgqfdnvaai adtliringr tfrlgdlatv trgyddppvt qmrangkavl gigvtmqpgg
      301 dvirlgkald aeskdlqarl paglklaevs smphavshsv ddfleavaea vaivlivslv
      361 slglrtgmvv visipvvlav talfmylfdi glhkvslgtl vlalgllvdd aiiavemmav
      421 kleqgysrar aaafaytsta fpmltgtlvt vsgflpiala ksstgeytrs ifevsaiali
      481 aswfaavvli pllgyhllpe rkkhaheahl pddhehdiyd trfytrlrgw irwcierrfv
      541 vllitgalfv vsllgfslvp qqffpssdrp ellvdlrlpe gasfaatlre terlekvldk
      601 rpeidhsvnf vgsgaprfyl pldqqlqlpn faqfvitaks vddreklasw lettlrdrfp
      661 aarwrlsrle ngppvgypvq frvsgddiat vrsiaekvaa tmrgdaravn vqfdwdepae
      721 rsvrfeldqk karelnvtsq dvssflamtl sgttvtqyre rdkliavdlr apqadrvnpa
      781 klaglalptp ngavplgslg rftptleygv vwerdrqpti tvqsdvraga qgidvthaid
      841 gklnalraql pvgyrieigg sveesakaqt sinaqmplma iavftllmiq lqsfsrvlmv
      901 vltaplglig vvgtlllfgq pfgfvamlgv iamfgiimrn svilvdqieq diaaghgrfd
      961 aivgatvrrf rpitltaaaa vlalipllrs nffgpmatal mggitsatvl tlfylpalya
     1021 twfrvksger dpqdgpphdd gtppaapsga
//
LOCUS       WP_175896733             308 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Burkholderia pseudomultivorans].
ACCESSION   WP_175896733
VERSION     WP_175896733.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..308
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31957
     Region          7..272
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(34..35,38,90,103,105,134,167,253,256)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 maaafpeila lgeamiefnq sqpgraeflq gfggdtsnfc iaasrqgast gfvsavgddp
       61 fgrllgdlwr aegvdttfvr idrtaptgvy fvthgadghq fdylragsaa sryaaadlpl
      121 dalaaakavh lsgislaist sacdaafaai dharsrgakv sfdtnlrlkl wplpraravm
      181 realrqtdic lpswddvtal tgaddrdaiv damlehgpqv valklgkega yvatpherrv
      241 vpgfaveavd atgagdcfgg afvarivagd dpfaaaryan aaaalsttgy gavapiprsd
      301 avarlmqg
//
LOCUS       WP_175896740             360 aa            linear   BCT 11-JAN-2025
DEFINITION  AI-2E family transporter [Burkholderia pseudomultivorans].
ACCESSION   WP_175896740
VERSION     WP_175896740.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..360
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39419
     Region          85..351
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mekqqesrda qnrephlrsv rltsdfslpk msaieigsya faivamwlvi elkllgglla
       61 gllvyqliht iapaierhtt smrarwvavv lvaiaivggl tglsigiveh fehtvpnlqs
      121 lldqlmqive qtrartpawi anllpvdveq mktkaavlmh thmdqlqqgg knvargfghv
      181 lfgmvigami aigvehgkar rplstalvtr vsrfadafrr ivfaqikisa inaaftgiyl
      241 lvalpifhqr lplsktlvlv tfivgllpvi gnlisntliv avslsvsmgt aiaslaflvi
      301 ihkleyflna kiiggqiesr awelllamli meaafglpgv iaapifyayl krelymlrli
//
LOCUS       WP_175896761             495 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA recombination protein RmuC [Burkholderia pseudomultivorans].
ACCESSION   WP_175896761
VERSION     WP_175896761.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19586425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..495
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=54056
     Region          71..229
                     /region_name="Apolipoprotein"
                     /note="Apolipoprotein A1/A4/E domain; pfam01442"
                     /db_xref="CDD:460211"
     Region          154..471
                     /region_name="RmuC"
                     /note="DNA anti-recombination protein (rearrangement
                     mutator) RmuC [Replication, recombination and repair];
                     COG1322"
                     /db_xref="CDD:440933"
ORIGIN      
        1 mtitlllaal vvlavalava ivalvrgggr hddtamlgdq iedaahaqar averlerelr
       61 geivenargs rtelagsfaq lqqtlaaqlt svatvqnnqi egfaqqlgkl vagnaqqfda
      121 mresvqrhaq qareeqtaal rlfgdtlnrq ltqlteandr rigevratle qrlkeietnn
      181 aakleemrrt vdeklhatle qrlgesfklv sdrleqvhrg lgemqtlaag vgdlkkvltn
      241 vktrgtwgev qlealleqml tpdqyaknva tvpksserve fairlpgrda gardaapvwl
      301 pidakfpred yerlidaqer adaaavedaa ralearvrle artiaekyva pphttdfall
      361 flpteglyae ilrrpgltdl lqrdyrvtva gpttltalln slqmgfrtla iekrssevwq
      421 vlgavktefg kfgdvlartk sqletvtrsi eaaeqrtrvm nrklkqveal pgdaavgllg
      481 aaaadgaega dadea
//
LOCUS       WP_175896824             177 aa            linear   BCT 11-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Burkholderia pseudomultivorans].
ACCESSION   WP_175896824
VERSION     WP_175896824.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..177
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18732
     Region          1..161
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtpahlipsp lgdiavried daltglffvg qkyfpplaia dqanvraapp ivrkvaeeia
       61 eyfggtretf svpihlrgte fqrlvwkell aipfgellsy gditarvglp msgaravgga
      121 vgrnpvsiiv pchrvigasg sltgyaggie rkrallaleg agyadgrhnp aqhvlaw
//
LOCUS       WP_175896829             211 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia pseudomultivorans].
ACCESSION   WP_175896829
VERSION     WP_175896829.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..211
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21737
     Region          8..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtnhtfftan lllaytayfv gtaspgpsnl aimsvaahhg rkaalafalg visgsmcwat
       61 iatlgvsaal lawskllvai klfgglyllw lafksartam aapasssagt aaseprlarf
      121 yargamlhlt npkailvwvs ivalssngag ashgavvpgc vvigcavfgg yalvfsmdra
      181 rrlyvrcrra meaclavvfg vagirllasn v
//
LOCUS       WP_175896840             264 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Burkholderia pseudomultivorans].
ACCESSION   WP_175896840
VERSION     WP_175896840.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13469656
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..264
                     /product="energy transducer TonB"
                     /calculated_mol_wt=27220
     Region          67..263
                     /region_name="PRK10819"
                     /note="transport protein TonB; Provisional"
                     /db_xref="CDD:236768"
     Region          185..263
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mtgltiryga lharryaara vraapplaar pplplppapa dtrrasnngw rdavaaalav
       61 aalhagvall aarapatpav qpprplpmtv eltrppeplp qaahpppvvp pkplkqaptp
      121 kphvaqprpp vaqaaapqpv heappaaatp laaapatpap apaptpaapv retapigdaa
      181 ylrnpapdyp afaqdqgweg rvvlrvhvla ngspdsvevk tssgrrvldn aalaavrrwt
      241 fvpakrgdea vdgwvnvpid fklg
//
LOCUS       WP_175896845             649 aa            linear   BCT 11-JAN-2025
DEFINITION  arylsulfatase [Burkholderia pseudomultivorans].
ACCESSION   WP_175896845
VERSION     WP_175896845.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..649
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=69268
     Region          47..615
                     /region_name="PAS_like"
                     /note="Bacterial Arylsulfatase of Pseudomonas aeruginosa
                     and related proteins; cd16025"
                     /db_xref="CDD:293749"
     Site            order(57..58,95,156,158,263,406..407,466)
                     /site_type="active"
                     /db_xref="CDD:293749"
     Site            order(57..58,95,156,158,263,407,466)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293749"
ORIGIN      
        1 mslsasrlvp frlrvvgaia agalslascg gvgestppqa datpaakhpn ilyimaddlg
       61 ysdihafgge idtpnldalv asgrilsnhh tgtvcaitra mlisgtdhhl vgegtmgvpt
      121 derrglpgye gylndralsv aqllkdagyh tyiagkwhig sgivgsatgs gqtpdqwgfe
      181 rsyvllggaa tnhfahepag ssnytedgry vqpgqpgqpg gaggspavfy stnfytqkli
      241 eyidsnrqdg kpffayaayt sphwplqvpd pwlhkyagvy dagydairna riarqkalgl
      301 ipadfkpfdg lpetttaspa tandgtanak ylsavhsaad gysdygagkv dkrwaslspa
      361 erkaqaryme iyagmvenld yniglliqhl kdigeydntf imfqsdngae gwpidsgadp
      421 tatdtanaqe ptysalgtdn gkqnaqrlqy glrwaevsat pfrltkgysa eggvstptiv
      481 hlpgqaqqlp tlrafthvtd ntatflavag vtppsqpapp lvntltgvdq nkgkvvynnr
      541 yvypvtgqsl lpvltgsaag evhttpfgde aygraylrsa dgrwkalwte pplgpldghw
      601 qlydlasdrg ettdvsaqnp sviqtlvaqw ktymsnvggv eplrprgyy
//
LOCUS       WP_175896878             739 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia pseudomultivorans].
ACCESSION   WP_175896878
VERSION     WP_175896878.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..739
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=77935
     Region          60..>204
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          210..732
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msrglieagr agagvsrrsf lrlgvslgaa aggglllgfs lpaagddarr sviggdaaep
       61 aptgvfapna fvqidrtgkv tlvmpkvemg qgvytalpml iaeelevpls svtldhappn
      121 eklfldpllg gqltggstsv ryaweplrra gatartllva aaakqwnvdp ascraengev
      181 qhppsgrras ygqladaaak lpvptdvalk rpadfklvgt pakrldspek vdgtaqfgld
      241 vrlpgmlyav ivnspvfggt vasvddtaak ripgvrqvvr vddavavvgd htwaakrgas
      301 alvvkwnega gakvstkdlf adlaqaaang kgavarkdgd vakafadakt rvdavyeqpl
      361 lahatmepvn ctvhvrgdgc eiwvgtqvpt ravdtvqrlt glspdrivvh nhllgggfgr
      421 rletdmigqa vkigkqvgap vkvvwtreed vqhdmyrpcy ydrisaglda ngkpiawqhr
      481 ivgssimarf appafkdgvd pdavevaael pydlpnqlvd yvrqeprhvp tafwrgvgpt
      541 rgtfvvesfi delaaqtktd pvqyrralld ktprarnvld vaakaagwgs alpkgqgrgv
      601 svmhafgsff sivvdvavdd gevqvkrvvc avdcgmfvnp ntieaqvqgg iifgitgaly
      661 geitiengrv mqsnftdyrm lrinetppid vhivksgeap ggigepgtaa taaavsnaif
      721 aatgkrlrkl pvgnqlkta
//
LOCUS       WP_175896866             103 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia pseudomultivorans].
ACCESSION   WP_175896866
VERSION     WP_175896866.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 103)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 103)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 103)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..103
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11244
     Region          18..103
                     /region_name="CytC552"
                     /note="Cytochrome c551/c552 [Energy production and
                     conversion]; COG4654"
                     /db_xref="CDD:443692"
ORIGIN      
        1 mavalvcvar paaaeriaep telvdrqhcm fchtpdrafl apafhdiagr yrdvpgaram
       61 lvdklrhggt ahwgdqempl aperggplsd edaqrlvdwv msq
//
LOCUS       WP_175896906             360 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Burkholderia
            cepacia complex].
ACCESSION   WP_175896906
VERSION     WP_175896906.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..360
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38694
     Region          16..331
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mpfresvvag pvpvswaldd dqqglvaaar efarerlepl lggapdstrw tetvqlaatl
       61 dlatmilpeq mggmgisrhd lalvveqfaa gpleraaelt lssvalmtlr eydaldrlpd
      121 pniqhyldgt tsiapaipdv aasgfwvlrq hassqvlmvq mdgehpqlal atlparrvep
      181 ycavvtlpga lsigryttap pgdtpwlvlp dggradgnav rqwlvdvatw laallsgavr
      241 qgvnfalays afrqtfrrpi aahqlvaarl admlisahti hlflrsvaaq etqvqigsvr
      301 smahhvatea ldvarelvql cgghgyvqgl ppaarfqtvh wfamllmkve aalraftvtg
//
LOCUS       WP_175896984             213 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia pseudomultivorans].
ACCESSION   WP_175896984
VERSION     WP_175896984.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..213
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22984
     Region          1..210
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msfrlylsfl aasavlvyap gpvnlltmnh alragwrral pcvwggtlav llqlaltalc
       61 lnsllhvder altalrwaga aylvwlgckq wlsrapagas aqapagtvpa etdteralfw
      121 rgvatsglnp ktllffpsff pqfisphaew slnqqyllla tsfallfagg vasmalfshr
      181 lsrtlqrpar mramnrvtgg llvgmgaimv gwn
//
LOCUS       WP_175896987             163 aa            linear   BCT 11-JAN-2025
DEFINITION  2,4'-dihydroxyacetophenone dioxygenase family protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175896987
VERSION     WP_175896987.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14449000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..163
                     /product="2,4'-dihydroxyacetophenone dioxygenase family
                     protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17579
     Region          24..143
                     /region_name="cupin_DAD"
                     /note="2,4'-Dihydroxyacetophenone dioxygenase (DAD), cupin
                     domain; cd20302"
                     /db_xref="CDD:380436"
     Site            order(40..41,44,50,52,69,71,73,75,88,91..95,97..99,117,
                     123,125,133,136,139)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:380436"
     Site            order(64,66,81,102,118)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380436"
ORIGIN      
        1 mtqppaplpt dlppisclpg dalpwlpmsa dlpglaikyl hidaaedtlt allkmpaggt
       61 lprhrhdgrv fvhtlqgawr yreydwiaqa gstvlepags vhtpetlgap gedvitlnvm
      121 rgdlvllddd gretarencr vallrqrkha rtapgdaapf vtr
//
LOCUS       WP_175896990             505 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Burkholderia pseudomultivorans].
ACCESSION   WP_175896990
VERSION     WP_175896990.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..505
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53856
     Region          11..488
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(67,69,73,76,80,113,116..117,126..133,138,141,144,
                     237,241,244,247,249,424,426..427,429..430,433,436..437,
                     439,441..444,453,457,459,473,480..485,487..488)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(153..156,164,179,182,212,229..232,235,253..255,287,
                     389,391,417)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(156,253,284,287)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mkhdsnvtst lghlidgkrv dggsrvqpvf dpatgasnks valadkqtve aaiasaqaaf
       61 pawrntpplk rarvmsrfkt lleehadelc alitaehgkv ladamgelqr gienveyaty
      121 vpellkgehs knvgpaidsw sefqalgvvs gitpfnfpvm vplwmwpmav acgntfvlkp
      181 sertpsstlr maelaleagl ppgvlnvvng dkeavdtilt dprvkavsfv gstpiaeyiy
      241 stgcahgkrv qalggaknfa vvmpdadign avnalmgaay gscgercmai plvvaigdet
      301 gdkvvaglka eidkmkvgpg tgegvdmgpl vtkqhfekvt sfveagveag aslvvdgrsv
      361 kvdghedgyy lgpclfdhvk pgmpiyqhei fgpvlgvirl ksldeamali daheygngtc
      421 lftrdgeaar yfsdniqigm vginvplpvp vayhsfggwk rslfgdlhay gpdavrfytk
      481 rktitqrwps agvregtvfs fpsnr
//
LOCUS       WP_175896992             727 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia pseudomultivorans].
ACCESSION   WP_175896992
VERSION     WP_175896992.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..727
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79567
     Region          39..722
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mkppsaiers sieparwrtw ldplgdaard waasdgliwl hlaktvfaal lamgiamrle
       61 msqprtamtt vfvlmqplsg mvfaksfyrv lgtaaglvaa lalgglfaqq pelymagitl
      121 wigccialav rnrhfrwygf vlagytaali glpavmspqt lfqsaltraa evalgiacsg
      181 avsalilpls sakalmrsls arhanfaafa tgalagdlar gdferrfadf vdeivgfean
      241 rafasfedph irarsrrlar lnsefmnact rlhalhqlvk rlragradav ldalaphvda
      301 lsqrlaalrd erqrgiastt gallelrrfh galpkaaras rreleahaag gvldfdtaie
      361 lmyrfigeyl gyadtyasld qddhafersv thykvktnaf fvgftflrti vavgamscfw
      421 iasewpsgsl aviaaaiaca lsstsprapk fvaqmavgaa fatavgylyl cyvypnidgf
      481 pllcatlapv lgfgaflamr pgmsgygigf avffcllagp dnviaytpev linnglavvv
      541 amlvcaivfa vvfpthmpwl tgriahdlrr qvtlacedap eglaqrfqss thdlmaqlrt
      601 llvrrtrqhr dalrwmlatl evghavidlr delhafseak ppqtlrwses idavlhelpr
      661 ffddptptrh artlksvnla iraaqhalqa wyavpdarrr mqrivgclhf vrsalldkda
      721 pfnrhrr
//
LOCUS       WP_175897010             354 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia pseudomultivorans].
ACCESSION   WP_175897010
VERSION     WP_175897010.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..354
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=36769
     Region          203..354
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mrknlvqtlg ylslvvvlag frpavaacqg dwtaasgvvg fspitlagpa davqhgtlik
       61 pgatarvsgw ryffseptqm adclklkgrf eslgtvvpgi ryvsngqvsd vwesgvpgig
      121 yalvmrsefg peigvkeggi dviydkepvr ssstsiavvv alvatgrlas gtytiparqv
      181 gkytitdgsg taksasipma sarvtvnaqg ckvisgdgnn vmlpkaityd fkevgatsav
      241 sssfavglkc dttlavhatl tdasdrants nvlslapgst atgfglqifr dksttplafg
      301 pesstkgnln qwlvgtanay dtmlipftvr yvktnetvgp gsvnaralit fsyq
//
LOCUS       WP_175897011             872 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175897011
VERSION     WP_175897011.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 872)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 872)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 872)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 872)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..872
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..872
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=93440
     Region          9..852
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mdwelrhqpr lkpiralllt iiagwqaear agkpdevfqv vqtefaqvef esgflsggaa
       61 idvsryergn vvrpgaytpd lyvdgrwvgr vevkfeaapg tpdaqpcfdr plldrigvdr
      121 arlpqdiras lepegacmri gqiipeasvg fefgdqrldl sipqiamlrn prgyvspdqw
      181 tagvpvamlg ynvntyhsqa rggygttqgy vgldagfnvq rwhfrhngsf swddrgerry
      241 qniatyvqrd vaawssqlvv gdsytsgdlf dstsfrgvrl ytddrmlpes qrgyapvvrg
      301 vansnakvti tqngmrlyet tvapgafiid dlyptgyggd lhvtvteadg svhsfavpfa
      361 aiplslrpgq nrysftagav rnldntsppf mqatwqhgft ntltgyggvt aaqgylsaml
      421 ggvlntswga igadvtqatt qipgerrysg qsfrvsyakt iaatgtniai aayrystngf
      481 fgltdamrar dqaavhidsa rlyrqrnras ltlsqqfgnk wgsvsatasa atywnrggsd
      541 ldytvgynnt frkvsygisa trqrnafags sttvyvglsv pfgrarpall stnvnhdsrg
      601 saqwqtnlsg svgadgnlay gvnvmrgmga gnsqtsgsan vtyrgartel sgsvgasndy
      661 qqysvalrga vvahpggvtl sqpvgetfai vsapnaagal vtnatgvrvd rngyavvpyl
      721 spfainditi dpkglstdie lletrqrvap lagavpmlrf ktvygrsavi rarqpdgspl
      781 pfgatvkdrn gadvgmvgqg gkifarglad hgelsvtwga adaasachls yalpvrkrsa
      841 gyqqpqsldl pcvaapgvdy apklssraap rv
//
LOCUS       WP_175897117             522 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA cytosine methyltransferase [Burkholderia pseudomultivorans].
ACCESSION   WP_175897117
VERSION     WP_175897117.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..522
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=58652
     Region          5..502
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 msvpvidlfa gpgglgegfs avsdtkgrri fdirvsiekd avahrtltlr amfralsehg
       61 vpdayydyvr gdidratlmn dptvasvmks vnqeahclel ggapesqidd lirdgingns
      121 ewvliggppc qayslagrsr rknvdpsfeq dpkhflyrey lriirdfqpa vfvmenvkgm
      181 lssthdgqri ferilgdlse papgvhydir sfttasrpeg lrpadflira edfgvpqmrh
      241 rvillgirsd hasrnhella ripenvtvrs vladlpalrs klsrqpdshe awlkilnsap
      301 ntlsgwrcea rdhiehwmee airlarhinr tggqflesdv pffpglptel atwyrddrlg
      361 gvcqhetrsh masdlhrylf assfarqqry spkldtfppk llpahgnvgd enipfddrfr
      421 vqiadspstt ivshiakdgh yyihpdpsqc rsltvreaar lqtfpdnyff egnrtqqyhq
      481 vgnavppfla kqlgesvarf lkipvyvdnq irpsegsvvt gs
//
LOCUS       WP_175897188             260 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia pseudomultivorans].
ACCESSION   WP_175897188
VERSION     WP_175897188.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..260
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29451
     Region          7..260
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mltlsladlk qsiaswrlwt llgwleirqr yarsrvgpfw ltismgvmit slgvvygtlf
       61 gqkmneylpf lassivlwgl fsqtiqegsi ayinsgsyir qvptpkliyi lqvvwrnliv
      121 lahnfvivig llvifgvksw etlpmfipgl llyvlnalwi amvagllsar frdlpqiiga
      181 mlqiafyvtp iifrpdalnr fsfivewnpl aylidivrgp ligqmpsvlt wevtigmavv
      241 gwpiallmtg rylkripywi
//
LOCUS       WP_175896911              92 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl carrier protein [Burkholderia cepacia complex].
ACCESSION   WP_175896911
VERSION     WP_175896911.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Moretto,L., Heylen,R., Holroyd,N., Vance,S. and Broadhurst,R.W.
  TITLE     Modular type I polyketide synthase acyl carrier protein domains
            share a common N-terminally extended fold
  JOURNAL   Sci Rep 9 (1), 2325 (2019)
   PUBMED   30787330
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   4  (residues 1 to 92)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10455525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..92
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10067
     Region          15..70
                     /region_name="PP-binding"
                     /note="Phosphopantetheine attachment site; pfam00550"
                     /db_xref="CDD:425746"
ORIGIN      
        1 mthdthsprr eeiaatirsc lvsaigsama adliaddtnl fdvgvdsmnm tdlllqleeh
       61 fgftlapedl sadlfmrfsn lvdfveshvp rd
//
LOCUS       WP_175897256             321 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia pseudomultivorans].
ACCESSION   WP_175897256
VERSION     WP_175897256.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..321
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34396
     Region          11..224
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(52..53,55,69..71,77,79..80,121,223)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(52,54..55)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(77,80,83,90)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(113,117..120,122)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(118..119,142..144,196..197)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          237..321
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 msdasltikv arkwqeardi cgfefvsddg splpgftaga hidvhlpggl vrqyslcnhp
       61 aqadryqiav lldaegrggs raihdavrqg dtvristprn hfplaagaah hlllaggigv
      121 tpilsmaerl sssgepfamh ycarsterma fveriaasaf rdrvrlhvdd gepaqrfdla
      181 avlaaapegt hlyvcgprgf mdavlneara rnwaeerlhy effggavets aadrpfqvri
      241 assgrvidvp aectvvaala angvdvltsc eqgvcgtclt rvldgepehr dsyltddeka
      301 agdqflpccs rsrsavlvld l
//
LOCUS       WP_175897258             237 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175897258
VERSION     WP_175897258.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..237
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26050
     Region          19..176
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtaiakadrp dtsrapagrk sqqrvldilr agrevfaekg yesattaeia qrvgvseatv
       61 fsyfrgkrel carviadwyd enitafedgm pldapvrqqf afvvrthlrl mlvsgtglca
      121 lvlsegrakq halsdeltal qrrytaplmd vlargqaagq vradmplsll rsmvfgpveh
      181 vlwdailgrr kldteataaq lidmlwaavq ppapeqaalv rfrnevmeaa rrlegst
//
LOCUS       WP_175897321             163 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia
            pseudomultivorans].
ACCESSION   WP_175897321
VERSION     WP_175897321.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..163
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17729
     Region          13..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mpkrlsppav asldatdrai laaladdari atselarqig lsapatadrv rrleaqgvia
       61 gftveldprs lgytlqaivr vkplpgqlhl vedvlrripe fvecdkvtgd dcficrlylr
      121 tiehlddils kvteraetst aivkstpvpr rlpplaedda arr
//
LOCUS       WP_175897369             178 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein, partial [Burkholderia pseudomultivorans].
ACCESSION   WP_175897369
VERSION     WP_175897369.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         <1..178
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
     Region          75..176
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(78..79,112..113,116,120..121,124,166,170)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 gllsgpqtcm kaarkicgdq pvrvvdaara lrdgsdpatl vfqcgaapma qtaapapeks
       61 tpapvehvnl agdalfatgq aaltpaaras ldkllskrdd raysqvtvtg htdsvggeay
      121 nralsqhrae avaaylqehg lragawlvtg rgkadpvasn ttaegrasnr rveislqr
//
LOCUS       WP_175897364             592 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia pseudomultivorans].
ACCESSION   WP_175897364
VERSION     WP_175897364.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pseudomultivorans
  ORGANISM  Burkholderia pseudomultivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Burkholderia pseudomultivorans"
                     /db_xref="taxon:1207504"
     Protein         1..592
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=65075
     Region          4..584
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mtkamkpvdv vviglgwtgs ilsmeladeg ldvvalergh nrdtlpdyty pkaidelkyg
       61 irgelfrrls letvtvrhkp gdlavpyrqy nafllpdnvg gagvhwngql yrpspedlkf
      121 rshsvaryga rflapdmtiq dydvtyddle pyfdrfeyln gtsgragnlk gqlqpggnpf
      181 egprsraypt ppvadtypak lfaeaarqlg hhpfpqpsan tsepytnfyg vrlgpcnlcg
      241 fcerfgcfly skgspqttil palfrkpnfe lrtqshvvki nvdssgkrat gvtyidgagn
      301 evfqpaelvi lssfqvnnvr lmllsgigkp ydpatgrgvi gknfayqims stsvffgqdv
      361 pinpfiaags ggsqivdefn sdhfdhgphg flgggyiigg qtggrpiqql avphgtpawg
      421 aqwkraakdh ylhttnvvth gsvmsyrday ldldptykds lgnpllrmtf dwhdnefkkt
      481 afltdralei vakmnpkshs tmlrkpgdhf nvreyqttht tggvitgadp qssalnrylq
      541 swdvpnlfvm gasafpqnig ynptglvgal ayfaanairt qylkhpgplv ha
//
LOCUS       WP_175897411            1141 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175897411
VERSION     WP_175897411.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1141)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1141)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 1141)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 1141)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 1141)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 1141)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 1141)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10025428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1141
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1141
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=128542
     Region          199..>343
                     /region_name="RecD"
                     /note="ATPase/5#-3# helicase helicase subunit RecD of the
                     DNA repair enzyme RecBCD (exonuclease V) [Replication,
                     recombination and repair]; COG0507"
                     /db_xref="CDD:440273"
     Region          303..435
                     /region_name="AAA"
                     /note="The AAA+ (ATPases Associated with a wide variety of
                     cellular Activities) superfamily represents an ancient
                     group of ATPases belonging to the ASCE (for additional
                     strand, catalytic E) division of the P-loop NTPase fold.
                     The ASCE division also includes ABC; cd00009"
                     /db_xref="CDD:99707"
     Region          315..1027
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
     Site            318..325
                     /site_type="other"
                     /note="Walker A motif"
                     /db_xref="CDD:99707"
     Site            order(319..326,385,422)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:99707"
     Site            381..386
                     /site_type="other"
                     /note="Walker B motif"
                     /db_xref="CDD:99707"
ORIGIN      
        1 mtknvappks tsgggflfed kvcawfvvqm lcgeaplepi lgaatridfq trpdgwfldd
       61 vllttkgqng shrfawsiks ntqfstvsap sdfvetvwaq ylhegfsifd rlrdymglvt
      121 tpldvefras lefvlttana tssdllpgry aqegwasdar rslfgsfhcp vdlanrngit
      181 gadtgsllsr lrflqfdfda lasesekrai eacrqilrsg ryedaqamwh silgitadyr
      241 ttaggidrqt llqrlparfg iielpdyrdd wnrlrsltka nmalirdtig kkiqlqdadl
      301 rcalrealdd yggavltggs gvgksaavkv faetlegsge pvlwfnpssf dkpdfaafqs
      361 dlglahtlee lfrsvssqtr livfdgfdrl yvpavmrlva tlvrfvqgde gatswktiit
      421 cqthdwprlr isltdaglpv sdwpcinvet wsadalrpvw daipgtarlk skvklqplwg
      481 nlkildllat risagnnvet sgwvgeadva awywdsyvrs gdnpharerf ammlaekean
      541 elrssfplda fevaeltpye alrldgvcqt taegrvrfah dlfgdwgrlr ilvshaddfp
      601 rfietrinsp lwhrairlyg tylleninnv drwrsvrrvl naqdntiasd llleaavfsa
      661 npseildrlk adlleengad lrrllgrflt sstvpdvrye tdgqplnprl asrlrlptwa
      721 dwppmlgflf rnrndvvaca adevakiadl wfvhtpedfl frkemasigl llgevahrgw
      781 rdrtvhfskr kllyrtalag aahypdevar falkaamrdg heedrdgeeh emlpfditfd
      841 prydpaavpe epwpdgpygh vdddfreail degaliplmr irpavareii lavmlkkrrr
      901 fdwhnhvhhs hdldlhsgdd wsiplftqgp flsllqhdfs eglgtiarlv dfaserwmyy
      961 tqlaaeeyra qpagadlgam safledatrp pgktaltlan etrfllgddr vygwsgknpp
     1021 saigpalmal ekyfydelda ehpiaeklda vlqrtrsvav lkvlcdvgkl eqslfgtvlr
     1081 pllsvpelyl wdrrhgfhgr qhlfmfafrq prwfieaare fhslphrkid skrvpstvst
     1141 g
//
LOCUS       WP_175897432             441 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175897432
VERSION     WP_175897432.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47634
     Region          33..435
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(46..47,50..51,54,86,136..137,139..141,144,164,
                     167..168,171,267,270..271,274..276,279,307,311,361..362,
                     366,370,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mrakypassv qpemlqrdda qtfeaatyak varrlipflm lcylgayldr vnvgfaklqm
       61 lsdlrfsetv ygmgagiffl gyflfevpsn lilhrvgarr wlarimltwa visasfvfvk
      121 spaafyvlrf llgvaeagfa pgvilyltyw fpsarrakal slffmaipla giiggplsga
      181 imhslhgams magwkwlfll ealpsfvlgf aillyldddi agakwltdae kallarnvsa
      241 daehttahls irafvadrrl wlmaaiyfcv vlgqygltfw lptiirkagv adplwvglft
      301 aipyacaiva lpligmsadr rrerrfhlav pmliaaagfa tlpmlgsvsa aivclsiasa
      361 gilasssqfw slptallggm saaagiaavn cfanlagffs paivgwlndl tgkstaglif
      421 isvaitfgal lvflvprsvn r
//
LOCUS       WP_175897443             421 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: dienelactone hydrolase family protein [Burkholderia].
ACCESSION   WP_175897443
VERSION     WP_175897443.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..421
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45970
     Region          1..225
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
     Region          237..373
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
ORIGIN      
        1 mtkhirivrg dtafdaylal peagrgpviv llqeifgvna eirevadlya aegyvviapd
       61 lfhpfgsnie lgygeadhak afdyytrfdv agavddirat vahartlpes tgrvgvlgfc
      121 lggklawlaa aqgdvdcavg yygvgieqsl elaeriacpl alhfgaddpl nppetvtair
      181 aaldgkpnak lyvyegagha fsrngptfvk aaamsahtrs lavfrkvlgp dydlgaladh
      241 hfhlefaard peetmrtmvp epyvnhvptm tggtgytelk rfythhfvhn npadmamapi
      301 srvvgvdrmv defiltfthd reidwllpgv aptgkrveip mvvvvafrgp klynehiywd
      361 qasvlvqlgl ldprglpvag vdvarklrde tlpsntlmar wreskparsg ydivlgkkrp
      421 v
//
LOCUS       WP_175897447             258 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175897447
VERSION     WP_175897447.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..258
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=28322
     Region          21..221
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mihqadnvie lphalganqf laaldgisra elaprlmlsn lktgqvlcda genleavyfp
       61 vtagislqyt igskttlgvt eigregivcd dvigsttqrr vvvyhggfay rlyarrfada
      121 cdaspairrq vfvrmqlvla qasqvmfcsr hhvmrhqvsr wlliayersr sieipvthgm
      181 lgqmlgvrre titdtarqlh elgvihqhrg aivltdlarl agqgcdchrv irdetcrila
      241 idagteagag lsrrvrtt
//
LOCUS       WP_175897538             416 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia cepacia].
ACCESSION   WP_175897538
VERSION     WP_175897538.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..416
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45480
     Region          69..387
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mtlneswfap lvgilillaa agaitavvhf llfrvvarla rlsatrvdda lfefgafkwl
       61 nrivpfvvik lglgvvpgip dtaaqvadkv lfalivflvt mtvsatlsal ehahrtyqrd
      121 qprlslkgam qlvklvmfit aalvvigdat gkqiglllsg igamsavlml ifkdtllglv
      181 agvqlssndm lrigdwitmp sagadgtvid itlntvkvan fdhtiitvpt wklitesyqn
      241 wrgmteaggr rikralfvda tsvrflsnde ierlerltll kdyledkvda ieqwngtlga
      301 agdcpanrrq ltnlgtfray vanylkghpr irrdmtcmar qlpltaegip lelycftdtt
      361 twvdyeaiqs dlfdhliavl pefglrvyqh psgfdmrqma gvvqagqagl qaphag
//
LOCUS       WP_175897547             246 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia cepacia].
ACCESSION   WP_175897547
VERSION     WP_175897547.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..246
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25384
     Region          10..239
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; pfam01925"
                     /db_xref="CDD:460386"
ORIGIN      
        1 mhihtltiva vvfllagavk gmiglgppti amglltlamp psaaaslllv psfitnvwql
       61 wlgpsfgpll rrlwpllagl tigtltgglp alaagstwth aalgvvlily glwglaaarl
      121 papgrhekwl savvgyltgv vtaatgvfvv pavpylqalr lskddliqal glsftastiv
      181 lglqlrvtga letvdlgvsa lalvpalagm aggqyarrvm sekafkrcff vglialgaym
      241 avsgwr
//
LOCUS       WP_175897552             256 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia].
ACCESSION   WP_175897552
VERSION     WP_175897552.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..256
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=27778
     Region          3..235
                     /region_name="ArtM"
                     /note="ABC-type arginine/histidine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4160"
                     /db_xref="CDD:443325"
ORIGIN      
        1 mifslpflld tvmpkllaav pttlaltlfs gvasvllgvp lalaagarha plrwsargwi
       61 mlirgtpllv qlyllyygfg qivprewmrd swaspllrda fwyaivalsv nesayvatil
      121 rgaiagvpag eieaghaygm traqvlrriv gprawrlalp alvgeailll kstvlastvt
      181 vfdvmgtant lrfetlhvye plagaaivyv vlvallivpa grfeqhvnry ltrapdertp
      241 arrrrrassg awaapn
//
LOCUS       WP_175897591             541 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: amidohydrolase [Burkholderia].
ACCESSION   WP_175897591
VERSION     WP_175897591.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..541
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59265
     Region          2..537
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mqyadtayln gllytgdaqr rfaqalatrd gkivavgrdd dirpligpat rtvdlagrlm
       61 lpglidghvh pleghqilgd fdlsgindpd tilqriraca datpnepwvy lgganlaafg
      121 ayptrelldr ivpdrpllvv gfdvhsgcln tkgleaagih adtpdpaggv yerdasgapn
      181 gvvheaafyr vcplipqlsp agypkslaka hamahgygit gwfdarveea elkayadaqr
      241 agtlkvymsa glyanprrdp reqierfaaw rrayecdnlr lhtvkifvdg vpesktaall
      301 epyagtddcg lalwsqdaln eiclladsag fdlhfhtlad havrmtldal eyvrirngmr
      361 drraqlahlq lvdpadmsrf nrlgaiasvq tlwtaareeq qqlyrdllga ertarnypfr
      421 slrnagamla agsdwsvstm dpmqiiqtgv thllidqpds ppwnpherld lltmleaytv
      481 ntayalrfdd ctgsleagkd asfaildrnp fahpvetfaq traietcfrg evvyaapgwa
      541 d
//
LOCUS       WP_175897627             736 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: xanthine dehydrogenase family protein
            molybdopterin-binding subunit [Burkholderia].
ACCESSION   WP_175897627
VERSION     WP_175897627.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..736
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=77434
     Region          28..>192
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          200..728
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mtieldntgs vrpsrrtflk aagaaaavsl tigfewtglg rralaatapa adfapnaflr
       61 itpdgavtvi akhvemgqga ytgiativae eldadwstvr vesapadakr yanlafgtmq
      121 gtggssaman swqqlreagg karamlvsaa aarwkvpage lttangvvth aksgkkaayg
      181 tlvadasklp vpdkvvlkqp adfkligqri prvdaspksn gtahftldtt fpgmrvallq
      241 rpprfgatvk sfdataakav pgvvsvvqvp ggvavvgtgf waakqgrdal kvewdeahae
      301 krssdeimre yrqladkpgt sarkdgdada aisgaarkig atyefpylah apmepldavv
      361 kltadsceiw agdqfqtvdq anaartaglk peqvqihtly aggsfgrran awsdyvveav
      421 siakalgadg kpvklqwtre ddiqggfyrp myfhkldagl tadgklvgwr hrivgqsila
      481 gtpfeafmvk ngidatsveg aanlpyavpn vsveltttkv glpvlwwrvv gsshtayave
      541 afideaahta gkdpyafrrd llakeprmra vldlaaqkag wdpakplpkg rgrgiavaea
      601 fksyvaqvae vsvdadgkvk vervvcavdc giainpdiva aqmeggigfg lgavmhsait
      661 lkdgqveqrn fdgyhvlria empkvevhiv psaeaptgvg epgvapvgpa vanaifaatg
      721 krhyvlpfds adsaka
//
LOCUS       WP_175897648             512 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175897648
VERSION     WP_175897648.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..512
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52245
     Region          16..438
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,142,
                     145..146,149,273,276..277,280..282,285,313,317,371..372,
                     376,380,396,399..400,403..404,407)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtlsdsrrna valaavclts lmfgleissv pvilptlehv lhgdfngmqw imnaytiact
       61 tvlmaagtla drfgrkrvyv tgtvlfgats llcglapnvp vlvagrllqg asggamlicq
      121 iavlshqfre grergrafgi wgivfgiglg fgpivggaiv alaswpwvfl vhaplaaval
      181 aliggavqes rdphagsldv agivtlslav lglafyitqs aelgltsaag lgvlgatvla
      241 magfflaera sarpmfdfsv friraftgai fgsmgmnfsf wpfmiylpiw fqvalgydsv
      301 taglallayt lptlvappfg erlalrygpg vvipgglfti aagfalmrig saadhaswvt
      361 mlpgcviagi glgltntpvt ntttgavpsa ragmasgidm sarmislaln iaamgfvlva
      421 givaslkggv agtigdgalr rlaqeiasgr tdglhaiapa laqadptgav lhaalvhgfg
      481 wvmvygaagv amlatasava faparrgaav ce
//
LOCUS       WP_175897720             468 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175897720
VERSION     WP_175897720.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 468)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..468
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49373
     Region          <229..467
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mhtlmlalrn lqrnrrrslt tllamivgvs aillfggfsr ditlglqtdf vqrsghlqiq
       61 rqgyylygtg dpaaygirry aaligllrrd pqlapmlqvv tptlqfggia gnfaagvsrt
      121 vmgfgaipdd qyrmqqwnay gfplrprafa lrgsaddaav vglgvarvlh lcgplhvadc
      181 rdappgpaap aatgpdasap advlalaqge agsqpagdga thievltasa ggapnvgrfs
      241 vvkaeqqgvk elddvylavr lpqaqrlvyg gaepratale iqlartadlp aararieqll
      301 rggfdgqpld vvdfatlnpf ydqtnrmfsv ifgfvfvlis aivlfvisnt mstaiiertv
      361 eigtlramgm rrggiqalfv cegallgvag aslgvlaala iaaavnhsgl awtpparida
      421 valtvrvwge wrtiavtfag lacvaglsaw lpsrhaarls ivdalrhv
//
LOCUS       WP_175897741             255 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Burkholderia].
ACCESSION   WP_175897741
VERSION     WP_175897741.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..255
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27693
     Region          1..251
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mldiervsws pggaiavlds vtlsvadgef vglvgpngsg ktsllrcvfr yarpdagrva
       61 ldaqdvwrir pravaqriav lqqetpddfg ltvdelvgmg rtphkrpfda etaddrrive
      121 salhdvglve rraqrfasls ggekqralla ralaqqpell lldeptnhld lrhqlellar
      181 vrrlgiatla tihdlnlaaa ycdrlhvlah grvvasgapa dvlteallrd vfgvvalvdr
      241 hpvtgrprit plhpe
//
LOCUS       WP_175897860             787 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor [Burkholderia].
ACCESSION   WP_175897860
VERSION     WP_175897860.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 787)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 787)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..787
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..787
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85982
     Region          69..769
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msssfaarps rgrlalacaa afawpvahaa ptddtrvdta rrgverpadt vapastaaav
       61 spvptgstlt tvsvtaqrqp vdpdmpavvt sitreqiesh tnvttedalk yapnlmvrkr
      121 yigdrnsvfa grdfnelqsa rglvyadgvl lsnllgssya ypprwslipp ddiarvdvly
      181 gpfsalypgn sigstvlltt rrpekleasl stqfftqryh dgygfadslg gnhqtarian
      241 rvgrfwfals ldrlenngqp mqyaspnsay npklgaavpv sgaatdigpn gkprtivgaq
      301 tierteqlne tirigyaftd hvdatltlgh wenhyrqhge tflrdaagnp vyggnvsigg
      361 qnmtvapnaf apqrgdqenw lyalglngrl dsgwrlsgvv saydvsrdvq rsasivqgga
      421 gtlfqgdgtg wrtldlraea pevkghtftf gyhydnyflr nvtyntadwl agpttslast
      481 yrgdtrtqal fgqdawrfap gwlatlglry erwdayggal gnasgtlgya drsanalspk
      541 valqwdatdv wrfrlsfatg tryptvgelf qgtisnnaiv nnnpnlrpek aidwdftaer
      601 dvgvgvvras vfqsdlrdsi ysqttvsgat tvtnisnvdr vrvrgvelaf sgenvglrgl
      661 sldanvsatn aqifadaanp ayvgsrfpri prmranllas yrfdehwlas vgvrysgrqf
      721 ntldnsdvnp dvyggtssft ivdlkaryrf drhwtasvgi dnltdrryyv fhpypgrtfy
      781 gelkwsl
//
LOCUS       WP_175897905             275 aa            linear   BCT 11-JAN-2025
DEFINITION  carbon-nitrogen hydrolase family protein [Burkholderia cepacia].
ACCESSION   WP_175897905
VERSION     WP_175897905.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10166075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..275
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30524
     Region          13..272
                     /region_name="nit"
                     /note="Nit1, Nit 2, and related proteins, and the
                     Nit1-like domain of NitFhit (class 10 nitrilases);
                     cd07572"
                     /db_xref="CDD:143596"
     Site            order(50,106,123,127,138,163..164,166..167,186)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143596"
     Site            order(50,123,163)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143596"
     Site            order(124..125,144..146,164,167..171,173..174,194..195,
                     198..199,201..203,205..206,236,266..267,270..271)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143596"
ORIGIN      
        1 mtdhtrsatp fqvaalqmvs tpdvarnlae arrliaeaag egaqlvllpe yfcfmghrdt
       61 dklalaepyr dgpiqhflad aarrhgiwvi ggtlplkape pdrvlnttlv fdpsgneaar
      121 ydkihlfnfe kddesfdear tiragdtvvt fdapfgrvgl svcydlrfpe lyrrmgdcal
      181 ivvpsaftyt tgrahwetll raravenqcy vlaaaqggkh engrrtwghs mlidpwgeiv
      241 avrdvgasvv rgtldpqria dvrqslpawr hrvlt
//
LOCUS       WP_175897909             520 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: S41 family peptidase [Burkholderia].
ACCESSION   WP_175897909
VERSION     WP_175897909.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..520
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55348
     Region          72..418
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mmpstravlr lavcaaataa flpcaspvga qqpaparpas apaasssssa spatarppsp
       61 cppdwepqic elkaavevlk rqhltdvdig alldatthag irtlpyarff dakeeqerre
      121 derrardgtp gigivfetrp dglhivdvip dapaeqagvr pddlvvamnd tsvvgidaad
      181 ltklakgdag vplkltvqrg pshamlsfap vrtilkphpa takrlagdvl ytrlssfpep
      241 avgayidavq aarragppvq gvildlring ggalnaaigi talyagrdrt amvtvergda
      301 nrrryttnwp dyalpvmhgq dplaplqadd wwrtvplvvl vdgqsasaae ataaalkdlg
      361 rakllgmpty gkglaqtgvd lidgtrlnft farnlrpngc pmdgygvvpd wlvpprrdsd
      421 vdgvllwyre adlprapyad rlapdpfakv rkerqklreq ralakidsak saalpqrefg
      481 tasdwqlgqa laalagrpvr tvdakpqlmp aqpvceragn
//
LOCUS       WP_175897963             140 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175897963
VERSION     WP_175897963.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..140
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=14488
     Region          18..66
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mafpvqtltq lrpilvgfrk sagltqaqla arlgvtqqsy aqleanpsav sierlfkvln
       61 ilgvrmtlap gtqdasaasa dpapdaapav rqpaaskrkp daargttaak nparpaagaa
      121 rkrpatatpg kprvskredw
//
LOCUS       WP_175897961             312 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Burkholderia].
ACCESSION   WP_175897961
VERSION     WP_175897961.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..312
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32292
     Region          78..282
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mpldpqaqal lavfaqapai dfaqltvpay raslaaggaf apgdavaaee dwqipasgrq
       61 lsarlyrpaa dgplpltvff hgggfvacgi dshanlcrsl aarartlvls vdyrlapear
      121 fpaaahdacd avrwaaasar dlcaragala vagdsaggnl aavaalqlrg sgiaiahqll
      181 lypvvdcate hpsyeslgng yfltadmmrw fkrhyfddga drasplaspl aapdvagaap
      241 ativsaefdp lrdeaeayal rlaqagtpvt vvrwpgqlhg fasmlgaida adrvltfgad
      301 alrrafdate ap
//
LOCUS       WP_175897973             950 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: type VI secretion system Vgr family protein
            [Burkholderia].
ACCESSION   WP_175897973
VERSION     WP_175897973.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 950)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 950)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..950
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..950
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=104445
     Region          24..826
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 malrppvigd lknrdlyeav hrgllqrdrl lmldtplgkn altplrargs sgiggdyhwt
       61 vdvaslrddt allslmhqpv tlwiqqrtal yadsvyrpvh gfvhqvgylg gdgsvstyql
      121 efssalifls ktrndegwle kdareiisdv fnrypqlqgr frfdltrepa vrswcrqses
      181 dlhfvyrlle degmyfrwvh eptkegeppk ttlvivdrvs slpeaklaey yrgntdhead
      241 gftqwavmqt mqslrymsra fdykhptshf qtesalqstt yemdggrqse srsipvapmt
      301 iyqptaygyp dsnsgegrar rrveewdsra rryfgvgglr wldagsrftl dnhprhpdsd
      361 pkkreflvve arwfiennvs igqlateypr slratlaeqq aahgarfktp ehpqdgtagf
      421 fvieveaqea sveyrsplah skpnmtieha ivvtqqgsea wtnernqvrv hfawdrknpd
      481 gtfassplls tmqadtgngy gsvhvprage wvliaywand cdkpfilgrv nggttpsqwh
      541 snvllsgfqs qgfggtgafn sfvhddatnq sgtrlvsytg ssyasiaqgy liqqsgntrg
      601 rylgsglllh adhyasvrgs rgvsisahpv srdsdqldvd eareqltrsk dllgsisdas
      661 eqhqaeslkl gvdalttftd atkqsasgea tggrtagggt gnanafaapl lllgspagig
      721 lsthqslhas adqqanwisg qdsyfaaggs mhaaaidhls lfarnqgika vagkgkveiq
      781 aqdgdlemia qqlvkllsva grmeiaadqe lvlycggati rikggnvsih apgnvdfkga
      841 sfsfagpasq syampqfkps yqaqyvlkse ndgtpmirha yemklpsgrt vlghtndlge
      901 tvpvftpsaq svslkafeqe kqdvepwkya gggepdiwad ylkvdpdert
//
LOCUS       WP_175897988             382 aa            linear   BCT 11-JAN-2025
DEFINITION  epoxide hydrolase family protein [Burkholderia cepacia].
ACCESSION   WP_175897988
VERSION     WP_175897988.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..382
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42173
     Region          5..108
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          73..381
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mhtapfdiai pdhalddlrr rlratraptl tpaepwqqgv dgawlrelta ywaerfdwra
       61 aeralnrlpq fvadaggqrv hfihrrgvgp kpyplvithg wpgsvfefda lidrlcdpaa
      121 fggdpddafd vvvpslpgfl fspapaapgm safqvadrwa almsglgyrr fgaqggdlga
      181 gvsialgarh advvdgihln flpgsyeppt daalpltdee rafvtqrgew aaleggyahv
      241 httkpqtlav alndspagla awiaekfraw sdcdgdlarr fshdtlltgi slywftgcig
      301 ssmqmywenr lqpmrfaagq rvavpvgfar fpkeigrppr swlervfdvv qwtdmpsggh
      361 faameepdll addvrrffrr lr
//
LOCUS       WP_175897989             323 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175897989
VERSION     WP_175897989.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..323
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35465
     Region          2..317
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhrigflisd gfqimalaaq svfeyanmgm sepfyvmgny sveggdvrss lglsvathal
       61 rgqlavdtwi vagvndpvas pappgvvafl rranararri agictgafvl aeagllsqrr
      121 atthwafgrd lqrdypeirv eedriyivdg piwtsagmta gldlalamve kdlgadvars
      181 vahklvmhqr raggqsqhse mldlapksdr iqnalnyarq hlgraltved laeavhlspr
      241 qfsrvftlet gqspakaier lrlesarlmi eqsrhsldvi akengfrdrr hmreafvrgf
      301 gvppqavrrd aradersdgr evg
//
LOCUS       WP_175897992            1082 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cepacia].
ACCESSION   WP_175897992
VERSION     WP_175897992.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1082
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115788
     Region          1..1065
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mwivnlalrr pytfivmaim ivlatplalm rtpvdvlpai nipvisviwn ysgfsatemt
       61 nritsvheri ltttvnniqh vestslpgia vvkvflqpga nvqtaiaqtv ssaqaivrqm
      121 pqgatpplvi tysassipvi qlglssktls eqsladialn flrpqlitvp gvqipfpygg
      181 rtrvvavdld pqallakglt padivnavna qnlvlptgta kmgqteyrid tnasadtvad
      241 innlpvqtvn gattylreva svrdgfapqt nvvrqngqrg vlisilksgd astlkvvsdl
      301 kallpkvipt lpegltitpl fdqsvfvdaa vqgviheali aavltammil lflgnwrstl
      361 iiaisiplsi ftslialsal getinimtlg glalavgilv ddatvtieni erhlhlgtrr
      421 aapsvpsapl ggqrpegawg ssfstnlhda ilegageiav pafvstlcic ivfvpmfflt
      481 gvarflfvpl aeavvfamla syvlsrtlvp tlamllfrpq qasagpdrst srfarihhaf
      541 neaferlraw yivllsillv rrrfyatcfl gfcvlstglv fvlgrdffpn adsgnirlhm
      601 raptgyriee tarladqver viratvppde lgaivdnlgl pvsginlsys nagtigtldg
      661 ellialkpgh ratqhyvqal rtvlperfpg vefffqpsdi itqilnfgqp aaidlqvlgn
      721 dlasnmtias slmkkfrqip gavdvhvlqr ndeptlladm drtrmqqlnl saqnvaqnml
      781 islsgssqtt psfwinprtg vqyplqiqtp qynissvddl lgtpisasgr tgmplqllgn
      841 lvqvrstanp avithynirp aidvyvsveg rdlgavagei drivsdarat lprgteltmr
      901 gqietmrtsy lglgagvama ivlvyllivv nfqswldpli iisampaala givwmlfitg
      961 thlsvpaltg aimtvgvata nsilvvsfar qrleagappl taaleagatr irpvlmtala
     1021 miigmvpmal glgegaeqna plgraviggl lfatvstllf vplvfggvha rlarrrarqt
     1081 gh
//
LOCUS       WP_175898067             359 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Burkholderia].
ACCESSION   WP_175898067
VERSION     WP_175898067.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..359
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37953
     Region          8..321
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mtapassdaf dawleanada ldvdpsraad ilpqlvrsrt vavgvpevmg gtggtiadai
       61 dtvaavaqrs ltaafvlwgh rtfveyvlqs dndalrarwl tplldgevag atglsnamky
      121 lsdieplqmh aarsgnafvl ngslpwitnl rregfiaaaa fdhddgtpps vfaiphdarg
      181 versddldli glrasntaal rvsdtvldes yrlaadapaw larvrpaflg lqcgmsigla
      241 rrallatlda sepsrasiga eirelettla dqaaqlkrgv ldgtflhapa amfelrialv
      301 etvsqavsle vqatggrgyl rgqsgsarrv reasfipivt pslvqlksql arhrraaaa
//
LOCUS       WP_175898121             232 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175898121
VERSION     WP_175898121.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..232
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26112
     Region          21..179
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnakstvarp rgrrpsvddf dlrdhmldva mqlfaergia attvaqiaaa agvtsamvhy
       61 yftnrerlld aiveerlaqa iafvwrptep ridddpfalv gelvdrffdv thrmpwlpsi
      121 wlreivhegg llrermvrri pldhvgrfae rirgaqqagt lnpalepafl fhsivalvml
      181 plataklwqs argmppidre vlhrhvrall gsgmqppapa rrtrarsprw ps
//
LOCUS       WP_175898137             397 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia cepacia].
ACCESSION   WP_175898137
VERSION     WP_175898137.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..397
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=41965
     Region          18..382
                     /region_name="MidA"
                     /note="SAM-dependent methyltransferase, MidA family
                     [General function prediction only]; COG1565"
                     /db_xref="CDD:441173"
ORIGIN      
        1 mnpkahepas lpapgpdala qsetlaaqlr geiaaaggwl pfdrfmeral yapglgyysg
       61 garkfgrrad dgsdfvtape lsplfaqtla qpvaealaas gtrcvmefga gtgklaagll
      121 aaldalgagl deylivdlsg elrerqrdti taaapalaak vrwldalper fdgvvvgnev
      181 ldampvrlfa kaggawqerg valdarqafv fedrpaapag lpavlgglde agdgyvteth
      241 eaalaftrtv ctmlgrgavl lvdygfpahe yyhpqrdrgt lmchyrhhah ddpflypglq
      301 ditahveftg iydaaiatga dllgytsqar fllnagitda laaidpsdir eflpaanavq
      361 kliseaemge lfkviafsrg idgtldafar gdrshal
//
LOCUS       WP_175898172             531 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MDR family MFS transporter [Burkholderia].
ACCESSION   WP_175898172
VERSION     WP_175898172.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..531
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56719
     Region          33..425
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(34..35,38..39,42,73,123..124,126..128,131,152,
                     155..156,159,285,288..289,292..294,297,325,329,382..383,
                     387,391,407,410..411,414..415,418)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mavhtaahhs sgqvlpfres llamigisfv tmlvaldqtv vgtalptiva elrgfdlyaw
       61 vatsyllssv itvpifgrlg dyygrkpfvi vsivvftgas vlcgmandml mlvlarglqg
      121 igggmlvgta facipdlfpd svvrlrwqvl mssafgiana vgpslggvlt qsfgwrsvfy
      181 vnlpigllsl lfvwrylphl rhvehdrkmr ldwpgallia lslgalqlfv ewlpkygvas
      241 waslllvvav aagfglwhwe krcaqpilpf dmfgnralsa lfvlailagf smfsllfyap
      301 llfqggfgms pkeaglvitp lvvfitigsi mngrvvtrir npnamlhvgf vlfaitcagv
      361 vvsthttpkw llmalmvagg iglgfvlpnl tvfaqqtagr ehlgiatall qslrmvggmi
      421 gtaltgtlvn qmysggvrda lsadhamqwh aqladpqili draaqgglva eltraghnga
      481 plleaaresl vgaihvgvam aavvavvsvw qcrrvppial rrkiephvaa d
//
LOCUS       WP_175898213             535 aa            linear   BCT 11-JAN-2025
DEFINITION  multicopper oxidase family protein [Burkholderia cepacia].
ACCESSION   WP_175898213
VERSION     WP_175898213.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..535
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=57765
     Region          88..535
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mirrtflsra igiaaaslfa raawaqhagh agmagmdsmd dmpgmsdmsg maghgqhgks
       61 apaalaaada lpagaplaal rtlanesrdp gtfratlvaq pvarpmlhga rpttfwqfgg
      121 gtqgpvvgpl idvregdsve ikfvnklpqp stihwhglpv ppdqdgnpsd pvapgasrvy
      181 rftlpkgsag tywyhphphm mtaeqvfrgl agpfvvraad dplagwpern lfvsdlklar
      241 dgtiapndmm dwmngregqf vlvngarrpr idvagderwr vwnacsaryl rvafddgraf
      301 ehagtdgglf daprrvtsll iapgeraell vragdrasra vlqaaeydrr kmsmshddgh
      361 gslpadpala ladvafspat arvlpttlra vpslgepvah kevafgeemd mdammkggah
      421 grpagmrfti ngdtyaphra tltsragdve rwtirngtdm dhpfhlhgtq fqvierasgg
      481 srtsepfraw rdtvnvrsge tvtilvtqdm rgermfhchi lehedlgmmg tlkvv
//
LOCUS       WP_175898299             377 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Burkholderia].
ACCESSION   WP_175898299
VERSION     WP_175898299.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..377
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40261
     Region          1..366
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfsftdeqq qfadalrryl geqygfearq aivrsdagvs ntqwsafael gltalpvpda
       61 qggfgggpvd mlvvmqelgr alviepywat avgvealria gsgagedaal leavaqgqkr
      121 vavafhepha rydlfeldth areqggtyrl tgtksvvqhg aqahawivpa rvddggiglf
      181 vverdaanak vadyrtidgq raatigfnet parlltggar daaaleqvad yatfllcaea
      241 vgaldelnra tveytktreq fgmpiarfqa lqhrmvdmli haeqarslty laavryassd
      301 adarrkavsa akarvgaaar fvgqqavqlh ggmgvtneva aahlfkrlti iettlgdtdh
      361 hlariaalpd faqadaa
//
LOCUS       WP_175898333             386 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175898333
VERSION     WP_175898333.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..386
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41338
     Region          1..386
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfqhtedrr mladtlnrfi aeqyafpvrd riaqspqgcd ramwrrfael gavgalfpea
       61 dggfggagfd iavvfeclgr glvvepflga llagralllg gggggaqrer laqlidgrac
      121 aafahdepgs hyelttvrtr aersgdgwvl tgakgvveqa aqasffvvsa rtagrdddah
      181 giglfvvpad apgvswrdyr kidggraaev rfervalpge aalvdthdap agddgqgaal
      241 lervlgygll alsaealgam dvakeatldy lrtrqqfgmp igsfqalqhr madllleveq
      301 arsavinaaa qldaprtvre ralaaakysi grigtlvaee siqlhggigm twelplshya
      361 krlvmidhql gdedhhlary ialskr
//
LOCUS       WP_175898374             371 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alkene reductase [Burkholderia].
ACCESSION   WP_175898374
VERSION     WP_175898374.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..371
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39469
     Region          5..349
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,236,303,323,325..327)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,103,110,183,186,188,236,243,303,323,
                     325..326)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(27,103,183,186,188,326)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mtqdplfqpl qfgaltlpnr ivmppmtrsr asqpgdeane lmaayyaqra saglivsegt
       61 yiaplgkgya wtpgihtpsq vagwlkvtda vhaahgrifa qlwhvgrlsh tsllggaqpv
      121 sssplqakgv nvfiagedgs tpgfvqasep ralsvdeire ivdqyraaar haieagfdgv
      181 elhgangylv nqfidsnant rtdqyggsle nrlrflrevt qaliegtgda srvgirlapl
      241 ttlngcvddd pettylaaak llgelgvgyl hiaeadwdda plmplefkqq lraaypgvli
      301 yagaytaera reaiaagwad lvafgrpfva npdlperlrt gaalaphdrn tlfgggargl
      361 tdyptlaqaa a
//
LOCUS       WP_175898378             315 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [Burkholderia].
ACCESSION   WP_175898378
VERSION     WP_175898378.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..315
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33809
     Region          2..315
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhtvavlalp dvvpfdlgva cdtfvrvrsp dvapayhvrv cseqprvtgd lfelrppfrl
       61 dalagadtim vpgtseplap tsprvlaalr aaaargcria sicsgafvla eaglldglra
      121 tthwlaatel arrypdvdvd pnvlfvdngr iltsagaaag ldlclhmiqa dygaavavda
      181 arsavaprvr eggqaqfiap ewpaggdglh dlmdwlqanl rkpltldema rkastsvrtl
      241 trrfqeqtgt sprqwlqtar vrhaqqllev talsiehvat eagfgsvtaf rerfvrivgt
      301 spqryrqtfr araga
//
LOCUS       WP_175898405             194 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175898405
VERSION     WP_175898405.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..194
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20174
     Region          5..157
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgvsrqqaae nrsaivaaae rlfrvrgvda vgltelmkea gftqggfynh fkskdalvae
       61 vmekamqdra dspnagslda qvasylsaah rdnveagcpl sgfagdaprl tdaaracyah
      121 glatyldrle rmvaveggtp aqtrrdaiav fnqmvgalvl sraiagtepa ladeilaagr
      181 daltagrddp vapa
//
LOCUS       WP_175898444             181 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia vietnamiensis].
ACCESSION   WP_175898444
VERSION     WP_175898444.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 181)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10632273
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..181
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20385
     Region          2..33
                     /region_name="Nudix_N_2"
                     /note="Nudix N-terminal; pfam14803"
                     /db_xref="CDD:464323"
     Region          37..159
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04511"
                     /db_xref="CDD:467545"
ORIGIN      
        1 mkfcsvcghe viaripqgdn rerfvcdhcg tihyqnprnv vgtvpvwgdq vllcrraiep
       61 rygfwtlpag fmemgettae aaaretleea garveiqnlf tllnvphvhq vhlfylarli
      121 dpdyeagees levklfdead ipwdeiafpt vsqtlrfffa draagdygvh tgdifrslrt
      181 a
//
LOCUS       WP_175898458             235 aa            linear   BCT 11-JAN-2025
DEFINITION  MOSC domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175898458
VERSION     WP_175898458.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12233312
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..235
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25655
     Region          30..183
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
     Region          180..223
                     /region_name="3-alpha"
                     /note="3-alpha domain; pfam03475"
                     /db_xref="CDD:460938"
ORIGIN      
        1 msdaarpais apvgavrigt srplagtpha saidkqpvgs rlwlgalgfa gdeqadarhh
       61 ggpdkavhhy ahdhyawwaa qigargvlaq pgafgenlst hgvtehdvcl gdeftlggav
      121 lqvsqsrqpc wklnarfdhp rmaalvqqsg rtgwyyrvlq agwvapgdvl alhrraypqw
      181 tlsavldvly rrtldmaald algevpilpa gwrrmldkrr aerqvedwtk rlegr
//
LOCUS       WP_175898460             298 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia cepacia].
ACCESSION   WP_175898460
VERSION     WP_175898460.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..298
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=31063
     Region          5..292
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 msillkgiia ypvtpfsadg gvdltaldal ierliadgvh aiaplgstge saylsdaewe
       61 avatasirav rrrvptvvgi sdlttagavr rarfaeqaga davmvlpvsy wklghdeiva
      121 hyraigaaig ipimlynnpa tsgvdmspdl iaticrtvdn vtmvkestgd igrmhrlaql
      181 sdgaipfyng snpmalaala agaagwctaa pnlnaalpla lfdamragdl araravfqaq
      241 lpllqfivng glpvtvkagl rlcgfdagep rkplmplgda rtrelerlla alrdgvtt
//
LOCUS       WP_175898465             557 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Burkholderia vietnamiensis].
ACCESSION   WP_175898465
VERSION     WP_175898465.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60555
     Region          25..384
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          453..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mtpaslieqy gpresmeydv vivgggpagl saairlkqla aekgaeigvc vlekgseiga
       61 hilsgavmdp raitelfpdw kergapltve vtedrflfls eqsavttpnw alpdnfknhg
      121 nyvislgnvt rwlgtqaeal gveifpgfpa aeilynddgs vkgvatgnmg vgkdgepten
      181 fqlgmelhak ytlfaegcrg hlgrqliskf kldanadpqa ygigikelwe idpakhkpgl
      241 vihtagwplk sdtyggsfly hmdknqvmvg fvvglgytnp ylspfeefqr ykthpsiraf
      301 leggkrvsyg araitaggll slpktvfpgg aligddagfl nasrikgsha aiktgmlaad
      361 aafdavqagr qsdelhaypd afrqswlyte lyrarnfkqw makglylgtl mvgieqkvmg
      421 gnvpwtlhhk hadhemlkpa sqctpieypk pdgkltfdrl ssvfisntnh eenqpahltl
      481 kdasvpvnvn lrtyagpegr fcpaavyefv knddgsdrlv inaqncvhck tcdikdptqn
      541 ivwvtpeggg gpnypnm
//
LOCUS       WP_175898485             441 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            vietnamiensis].
ACCESSION   WP_175898485
VERSION     WP_175898485.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 441)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..441
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=44595
     Region          32..310
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 manrmpngal rwtlfaacla lpawlwpqga vlgylaqtaa lvvlalsynl qlgttgllsf
       61 ghaavagvga faaahwfnrv gaplpllplv ggvagaafgc vagllatrra gtvfamitlg
      121 igecvaaaaw svpawfggvg gvpidraggt pwggwqfgap thayaliaaw cigsalamya
      181 ltrtplarla navrdnparv aalgtepchv rlamvtcasf fagvagtltl idveiatpds
      241 vsmarsatvl iaaviggtgt ffgpalgavv ltalsvvvag vsrawalylg vlfvavvvaa
      301 prgiagvaqa cahawrrgap averwrmlcg vgagafwaia ivcaaelgya wrfaqddggg
      361 safgvwrida dapagwavaa saagigmllw gwrarlagra hdvpdvpdvp dapdapdapd
      421 apdapdapda pdapdaredg r
//
LOCUS       WP_175898492             663 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: beta-galactosidase [Burkholderia].
ACCESSION   WP_175898492
VERSION     WP_175898492.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 663)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 663)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 663)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448998
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..663
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=74162
     Region          1..622
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
ORIGIN      
        1 mrlgvcyype hwpesmwadd arrmkalgie qvriaefaws riepspgeyd wgwldravdv
       61 lgaagleivm ctptatppkw lvdrhpdila igadgrpraf gsrrhydfss ptyleasrqi
      121 ctavaerygr hpavrywqtd nelgchqtvv syspaalvrf rawlkarygt idalnhawgt
      181 vfwsmeyrhf devdapvgtv teahpshrld yrrfasdeva ryhrmqvdvi rahspgrpva
      241 hnfmqlftef dhyevardld vatwdsyplg aleeqwfapd vkarwlrtgh pdfasfnhdl
      301 yrgmsklpfw vmeqqpgpvn waqwnpaplp gmvrlwswea fahgagcvsy frwrqapfaq
      361 eqmhaglntp dnrldeggre aqrvareiaa irdagadadp ngavrapval vfdyeakwlf
      421 evqpqgadfh yprfafeyya alrslgldvd ivsahapldg yrlvvvpplp vvpddfaarv
      481 aasgahavfg prtgsktvdl qipptlppgp lasilpvrvw rveslrpnvt epidgtlydg
      541 tplagharhw rdfvelhddt rgvvrarfad ghpacvshgt lhywaalfdd attarlfadv
      601 aaeagltptp lgdgvrvsrr ggltyvfnyg dtphtidavp psafvlgsaq vgpqdvaayr
      661 srs
//
LOCUS       WP_175898539             316 aa            linear   BCT 11-JAN-2025
DEFINITION  ketopantoate reductase family protein [Burkholderia cepacia].
ACCESSION   WP_175898539
VERSION     WP_175898539.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..316
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32625
     Region          1..307
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkiailgaga lgcaigatlt qgghetwlid rspahvdams rdglrvddag gtrhvrvhat
       61 traadvgvad lvvvlvksfh tdaairgaqs lvgpdtavls lqnglghedi lidvvgrerv
      121 lagktyvggv lrgaghiesg vigkytyige ldgritprve aiaaafnaag lattisdniv
      181 gtmwdkllvn vatgaltglt gltygqlyde pplkatslaa vaeaiaaaqa agvklsmtdp
      241 eqawtlaaeg lpatfktsml qslekgsite idfingsvvr wgqrygvptp vnatlvacik
      301 gleramadrq rqeaaa
//
LOCUS       WP_175898610             454 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: M23 family metallopeptidase [Burkholderia].
ACCESSION   WP_175898610
VERSION     WP_175898610.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..454
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47661
     Region          228..409
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mrldlrfrla reqglsalrg acgfpmrral lrgvvaaacv agspgasahv shdtapfspv
       61 tadlvdvpff daarttwggl hassaapldv ayalpastvp svherdgava rfgacvayrv
      121 lcdaargave rayasrfdyg lasalpamge qaayerrpvd laaaepfvle eaergargga
      181 ivgslrasla radlpagvae qvirmlagri dlkqhgalgd tfrvayepdd samqpggtrv
      241 talelrfrgq yvagvwfapa dgasggyydf dgvplagsrf ampvnatris shfgarvhpv
      301 tgarhvhsgv dlaapagrav hasergvvtf igtepsgygk yvvirheggy asyyahlsaf
      361 eptlrtgmrv argqrvgavg stgtatgphl hfevrrhdrl vdpvalvqag daaklkgerr
      421 vafnqvalda rtqlasadwl rsvamstlsp shdg
//
LOCUS       WP_175898621             822 aa            linear   BCT 11-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Burkholderia cepacia].
ACCESSION   WP_175898621
VERSION     WP_175898621.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..822
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=85724
     Region          63..813
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 msrnwglraa llalcvglas cggdgdspsa aasnlsaaaq sqgnedgngg nsgngngndn
       61 dnaaskknad irvvqyvnpl igtdyatdqp adpvgsglgg gtfpgptvpf gmmqwspmtp
      121 taqydsrkgd gsgfsggywy gdtsinafsi lhlsgtgcwa nggylnvmpq lapgdagtpa
      181 sfshanetaq agyygvtlgn gikaeltttl rtgfarftyp alaqgqqati aidptvlnnr
      241 aqgstgdtis qagdralsgt iagggfcwag havpvyyyae fsqpfavkpa lsndspvalt
      301 fnvdrkhpdv mmklgisfvs eanakanlla enpgtdaqgn rnwrfdkvrr aasaawnarl
      361 naiqvtggsd adktkfytal yhaslhpnvf ndvngqypdf yasngvsaap trqveqgrtm
      421 yanfsgwdid rsfmqlqall dpvrtsdivq slvldakacg afprwayfnt etavmpgdag
      481 siivanahaf gatnfdtqaa lsimkrsttp gaacagtpvm gsradydrlg yvpssgpgdn
      541 qtasntleya vrdfavsrfa talgdtatag tllkssgnwq nlfdrnaiqp ktaagawvtd
      601 gtgfmegnse qytwyvphdl ggvvaqagga apvvkrldtf fshlnigtvq pyfyvgnevt
      661 mavpwvyawa gapshtqrvl haslanefgt gaaglpgndd lgaisgwyvw aalglypvvp
      721 gvsgvalssp qfekivvrvg qqdgsyrllh ivapgagsgd vasfyvkslk lngapyptaw
      781 lpfehiakgg klsysmtada saatwgtdas ampsfpqaag ap
//
LOCUS       WP_175898623             881 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GH92 family glycosyl hydrolase [Burkholderia].
ACCESSION   WP_175898623
VERSION     WP_175898623.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..881
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..881
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=93714
     Region          55..877
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mklrhvvgig clavlsgcgg dqtstdasvl aqmsnaqgnr ndqgdqndqg enggagkrsl
       61 lrsvdpmigt anldinadws sgvrghghvy pgatvpfgmv qlgpdttgga htlpwnwdrt
      121 sgyqyddpli tgfththlsg tgigsggevr flptlapvdt atlakvaada sitynasfsh
      181 ddetaspgyy rvkmapvgsg stpwnvkgak ilaemtatah agvhrytyfp saaaqkrsmi
      241 vsidnpiggs tasgkirvvd aqtiagweit nnwannkpty fvarfskpfd tkhvafsadg
      301 fkaylsfadg ndsgavtvkv gispssiada qanlaaevga ksfdqvrgaa ervwadalgr
      361 irikggsadq rtmfytslyr tmlaptvynn adgsyvgtds tndgttsppt tskhanpgfd
      421 ysstfslwdt fraesplmtl vqpervdgwv kslltqfrqn gkgelpvwpl aqtetftmag
      481 hpsipliada ylkhltsagi ddiwtalttt qgasahgfdq yrqrgyvvag dnasvsttqd
      541 yafddwataa vgkaagksta dyrpylqrsr nyrnvfnptl nngwkfsqpk daqgnwvagf
      601 dptaaektdf sesnawidtw nifhdfpglv allggksqfi aqldrtfdpa npltflgnqg
      661 fpdltgrsgq ffagnepanh lpylydvagm psktqdrvrt vmddmysltl tagdrallsg
      721 dslkaaladp rrvrdsaipg nddcgqlsaw yvlsalgtys lnpvggvfyl gtplfaeatl
      781 dipvasgggd ggalkfgksr rftvtahtag ggapssvnry vqsvslngvp lhrpyityde
      841 mkaggtldfv mgatpndgwv sqwngqdpns alapsltlag k
//
LOCUS       WP_175898628             420 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175898628
VERSION     WP_175898628.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..420
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=43768
     Region          204..412
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(211,251,289,392,395)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(211,392,395)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(211,251,289)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 msfrsgfvaa lvgasvflsp vaasaapggw vaawatalqp ipdlaapppl yrapdvagrt
       61 vrqivyptvs graarirvsn tyghaplqid aaslapagag aalaggaaav rfggraavtl
      121 apgqelesdp vtidvtsgrp yaislqmgar qrmtvwhrvs nqvnyvsspg dhvtdadarv
      181 frtrftqyaw vtelavedgs arasvaaigd sitdglrssl nrnhrwpdal arrlaaagsd
      241 svgvvnlgis gnrllsdsac ygtslaarye rdalsrsgvk aaivligind infaampara
      301 gldcdsphtq vtaaslidgy rrlidaahrr gvkvfgatlt paalpaarea trlevnrwir
      361 sgggfdgvvd fdaalrdpar psvlqrryds gdgihpsdag ytamadavpl eqlrvavrgn
//
LOCUS       WP_175898632             190 aa            linear   BCT 11-JAN-2025
DEFINITION  flavodoxin family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175898632
VERSION     WP_175898632.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..190
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=19827
     Region          3..185
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 msnivivyhs gyghtqklae avhagaqdag atarliavge lddagwaald aadaivfgap
       61 tymggpsaqf kqfadatskp wftqkwkdkl aagftnsatm ngdkfstiqy fvtlamqhgm
      121 vwvgtgmmpa nskaatrndi nyvggftgll aqspadatpd eaplpgdlet aklfglrvaq
      181 aavrwtaggr
//
LOCUS       WP_175898635             881 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia cepacia].
ACCESSION   WP_175898635
VERSION     WP_175898635.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 881)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 881)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 881)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 881)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..881
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..881
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=94381
     Region          53..860
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 miekrqprmq aetepklkpv callltiiag wqthayaaqt dsgelqiart efaqvefegg
       61 flnngsgaid vsryerrnvv ragmykpdvy vdgdwigrie lqfksapntv daqpcfdkaq
      121 leligvdfsk lpqdvratld edgaclrigq aiqeasvsyd fneqrldlsi pqismrrqar
      181 gyvspdqwse gipvgmldyn asvyhartdg qgestqgyvg vnggvnvgrw hfrhngsfnw
      241 ddrgrrkyen vatylqrdlt awssqlivgd aytsgdlfds tsfrgvrlyt ddrmlpesqr
      301 gyapvvrgva nthakvtvtq ngatlyettv apgafviddl yptgyggdlk vnvteadgsv
      361 hsftvpyaav plslrpgqnr ysfttgvvrn lpnttpyfaq atwqrgvtnl ltgyggvtfa
      421 qgylsamaga vlntslgavg vdvthattsi pgerrysgqs frisyakava atgtnvaiaa
      481 yrystngffa lndamqardq aqlgagaasv srqrnraslt vsqslgargg slnatasast
      541 ywnrsgsdvn ftvgysntfr dvaysvsatr qrdawgksst myyanlsipl gktrpmtlat
      601 slsrdtrgst qaqtslsgal gvdnnvsygl nvnhgnssgt sqtnggasiq yrgpiaelsg
      661 svsagadyqq fsagargaiv ahrggvtlsq plsetfaiie apnaegarvt ntsgvridrr
      721 gyavvpyltp famndigidp kglstdvelk etsqriapla gavpmltfkt aygrsavira
      781 rqadgspvpf gatvtdadgk dvgtvgqggk llarglvdqg elkvqweadr gksvcalsys
      841 lpvrkraaty qslqslelpc vasevtnyap avsnrvvsar r
//
LOCUS       WP_175898695             480 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FAD-binding oxidoreductase [Burkholderia].
ACCESSION   WP_175898695
VERSION     WP_175898695.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..480
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49766
     Region          40..480
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mqslpaagvp dgpgvppqad dalaaalaaa lgdalddglv trsadiepry ftaynepagv
       61 rpralvrprs vdevsrtlal ctrlaqpvvp qggltglarg avalggeivl smerfagvea
      121 idaaagtmtv ragtplqtvq eaadaagftf gvdlgargsc qiggmlatna ggtrairygm
      181 mreqvlglea vladgtvvss mnrmlknnag ydlkqlfigs egtlgvvtra vlrlhpklae
      241 patalcrvqg ydavlelwnr lralpelvsf eamwpafydy varhtpgvva pfagdggfav
      301 liecatsapg gdaraaleaa ladaldaglv ddavlatsar qardvwtlre glaidalphl
      361 mnfdvslptg elgafavrce aalrgrwpdi vclffghvgd gnvhvgvsla grrdadaeai
      421 ddcvyavvrd mggsvsaehg igvlkrgyla htrseaeial mrrlkaaldp agvlnpgkvl
//
LOCUS       WP_175898715             300 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175898715
VERSION     WP_175898715.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33159
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 melrqlryfv avaeelhfgr aakrlfisqp alsfdirkfe dalgvqlfsr tnktvaltna
       61 gevllgearr lllqaaeaer ltvrsasgla grlrigfvhs mlyrglpdav rrfeadypgv
      121 evvlsemntq aqvqaiqrgq idlgyahwgh fppevesvpv yaepfvcclp aahplarrrq
      181 valaalaaep filfpreaap hyhdliiaqc vnagfsplir hearlwqtil smiefemgva
      241 lvprvlqqak sdrlafrplk daslesrtla lkrsgtaepv alrfadyvra sidalpalag
//
LOCUS       WP_175898723             731 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia vietnamiensis].
ACCESSION   WP_175898723
VERSION     WP_175898723.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..731
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=80721
     Region          58..692
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mnrfvpslrn lwlrcrdrar alcagawqrl rhptrrgvvl tlaalpllgl lvllafvpft
       61 psigdirrar idrparvlsa dgqliaefrp vnrewvplrq isphmvdali atedhrfyah
      121 hgidlrrtia aglhtfsgsr qggstitqql arnlypdeig raptltrkvk elitafkiet
      181 vyskdeilet ylntvpflyn aygvemaart yfgksadqld ivesatlvgm lkgnsyynpv
      241 lnperavqrr nlvlarmaal hmlspqqlaq lqrrplrvdf epqtaqpgpa phfavqlrkw
      301 liawadrnny dlysdglvvr ttldaqlqqm atralaqqte rlqavadgaw rgasgcglrn
      361 dlfrgfirqs adyraardag ladavalkql ganrafmral cerktrvqag fvaldprdga
      421 irawvgspdf dsepfdhvaq arrqpgstfk pfvygaafad gmrpddtfvd rpvaipigah
      481 aqwrptdaep ptdapmtlrd alalsrnrit aqvmqregaa rvaqlaramg vrdspldavp
      541 slalgtspvt lkemvsaygt ianrgvyvap qmitriedrd gkvlatfgsa pperalpvaa
      601 aqtlidvmrg vvdygtgadi rarygiridv agktgttqdn tdgwfilmhp qlvagawvgf
      661 ddgsvtlrsd ywgagahsal pivgtffdaa lraraidprv qfspdfrprs apapkrraph
      721 sglfdwlkff r
//
LOCUS       WP_175898795             452 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia vietnamiensis].
ACCESSION   WP_175898795
VERSION     WP_175898795.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..452
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48496
     Region          31..434
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(45..46,49..50,53,85,135..136,138..140,143,163,
                     166..167,170,267,270..271,274..276,279,306,310,360..361,
                     365,369,385,388..389,392..393,396)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mttqytpahp aaeqsdspaa vderqltrll trklvpflal iyvvayvdrt vvgfaklhmn
       61 aavgigdaay glgaglffig yflcevpsnl algrfgarvw farilatwgv itmamalvqg
      121 ptsfyvlrfl lgaaeaglyp gilyfltqwf pmrdrarvig llvlaqplag ivtgplagwl
      181 lsthglfgls dwqtlfvvsg lpavlltwst lrllpespah arwlndverr wianqlaadr
      241 dtyrpdshrn plaalrdrrv lllaalflpf plciyglslw lptiihafga gdaatgllsa
      301 vpylfavlgl livprhsdrk reryghivvv saaaaltmaa sawvrqpalq laficltafs
      361 lysiqavvwa lpgeflsgts aavgiaains lanlggyagp ygiglikaat gslaaglyfl
      421 aatllfavlm tfvvraalrt pepaacafar es
//
LOCUS       WP_175898775             367 aa            linear   BCT 11-JAN-2025
DEFINITION  J domain-containing protein [Burkholderia vietnamiensis].
ACCESSION   WP_175898775
VERSION     WP_175898775.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10644999
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..367
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=41081
     Region          <203..243
                     /region_name="DnaJ"
                     /note="DnaJ molecular chaperone homology domain;
                     smart00271"
                     /db_xref="CDD:197617"
     Site            order(219..221,230,236..237,240..241)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
ORIGIN      
        1 mtarrgaaia iapghetarl sdaqktfntl veridkrrer laawdavtpa fqkkfvdall
       61 pleresaalr trlihlldda flrsglskae qrtlsdliad mardvldaad daalqrvydr
      121 hhasgpagsa aadpqpapga daaddldals pdelaqrlqa eldaqferdm aahaareaqr
      181 akrrktpkqt aaqaraeaeq aessksirei yrklasalhp dratdphdqe rktalmqrvn
      241 hayakrnllq llelqleieq idrhaiaglg earltryngi ldeqlreldr eiehvendfr
      301 rtygiapsvk iapdtvvrll ardiagmqrs iqdltvtlre fedpdnvrrw lkemkrrpas
      361 agfdddr
//
LOCUS       WP_175898871             532 aa            linear   BCT 11-JAN-2025
DEFINITION  multicopper oxidase family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175898871
VERSION     WP_175898871.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..532
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=57325
     Region          86..532
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mirrtflsha igvaaaslfa rsawaqhaah agmagmepmd dmpgmagmad haqhakpapa
       61 alaavdalpa gaplallrtl anesgeagtf ratlvaqpva rpmlqhahpt tfwqfgagta
      121 gpvvgplidv regdtveirf vnklpqpsti hwhglpvppe qdgnpsdpva pgasrvyrft
      181 lpkgsagtyw yhphphmmta eqafrglagp fivraaddpl agwperhlfv sdlklasdgs
      241 ippndmmdwm ngregqfalv ngarrpridv agderwrvwn acsaryvcva fddgrafehv
      301 gtdgglfetp rrvtslllap geraellvra gdrasravlq aaeydrhkma mshdggrgsl
      361 ppdpalplad vtfapaaara lpatlravpa pgepvadkdv algeamdmna mmsgpahgrp
      421 agmrfminga tyaphratlt srrgelerwt irnttdmdhp fhlhgtqfqv terasggtrt
      481 aepfrawrdt vnvrsgetvt llvkqdmpge rmfhchileh edlgmmgtlk vv
//
LOCUS       WP_175898912             308 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia vietnamiensis].
ACCESSION   WP_175898912
VERSION     WP_175898912.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33870
     Region          16..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          101..300
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(116..117,119..120,123,127,129..135,229..234,
                     240..241,243..244)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mmhpdlrrld lnlllafdal yrhrsvaaaa helamspsal shalarlrda igdalfvrlg
       61 nemqptvrad diagwaaeal dtmskglara rrfdpaesdr tfvlaasdyt afavlpalla
      121 riervaphlr frivhsdrki atdelaagri dfalgyhees saaapgiddf dwfsddyvvi
      181 asathpdlrs rltldqylaa rhvvvtpwne prgvvdyvld rlglarqvam qlpsvlaapf
      241 viagstllmt vpnraaqvlq haapiriyaa pfdiprytvk iyshakhart dahrwlraql
      301 laarpapg
//
LOCUS       WP_175898958             495 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease [Burkholderia cepacia].
ACCESSION   WP_175898958
VERSION     WP_175898958.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..495
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54353
     Region          69..131
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 maslfkrptg ltvfdhdepy edlydpaehe alpvevppvq vepgslqdll fsqlveglra
       61 smrhteswmv ryladqqsgv caycgltlsv tgnrvdgapr amadllvpla lggtaleenr
      121 vlccaecqna kggrdwlafg ratdpvklla rrrealldga nhvlplsvkg tddamhalrq
      181 rwafprfrvl aqafgevgyf gwdlrglpne rggavrlrlr fefgardvsq srfalfevpl
      241 drwyeaawal veenavlvrp smtdrertaf ppfapsslal qererlapgg whehyerwhi
      301 llsgerwvqe arrvarwsmq akpgqravee qrrralrekp lndalaglaq rledvrtgra
      361 epvasgagrs vrspgesapl rrplnpglaq rqtavvarha afldalregk plpvrehevv
      421 pvapdaveps raplpldvqd rlaalrerll nptsqatatg rtgdavgrpg gvvddaggar
      481 ddalvtegpa wggaa
//
LOCUS       WP_175899015             323 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia vietnamiensis].
ACCESSION   WP_175899015
VERSION     WP_175899015.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..323
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33872
     Region          9..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..294
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,229,246,273)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,193,
                     223..227,234..235,238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 madlrdvnln rlaifvavvd agsltaaaer lglaktvvst hmqrlesevg anllvrttrr
       61 lsvtdagraf ydacrdivra aeaaldaass dagplrgtlr vsvpidygal vvapaivalr
      121 dahpaldvel iandrvvdlv adnldvairi grladsnyra vqlgeyekwl vaspafvarc
      181 glprdpdala alpfvmlstl prphtleldh argahasvrc vapvvsntat acraialagg
      241 gfglltdfsi addvaagrlv rllpawrsar agihavypst rmpsrkvraf vdamkacigt
      301 arptaparat askraarrap gaa
//
LOCUS       WP_175899024             360 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia vietnamiensis].
ACCESSION   WP_175899024
VERSION     WP_175899024.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..360
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39435
     Region          1..357
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msfltltdlt ktygeltava dvnlsveqge fvsllgpsgc gktttlqmia gfvdvtrgri
       61 aldgrdithm kpnrrglgiv fqsyalfphm sveqnvgfgl dmrgvdkaer aeriraalsl
      121 vrldalaqrf prelsggqrq rvaiaravvi eppvllldep msnldaklre dmqfelraiq
      181 rkigtttimv thdqsealsi sdrvvvmeag ritqtdtpyr ayerpenrfv sqfigkanll
      241 pgtvvahdgd airidlghdl aetgrtahlp mherdvrvgd avsvcirpek lrlcvpgagr
      301 faatvtsrff lgsqwlyrvd salgevlvcc qnegaeplee gapvgvdwhs davrvmrgea
//
LOCUS       WP_175899025             264 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia vietnamiensis].
ACCESSION   WP_175899025
VERSION     WP_175899025.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..264
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28220
     Region          1..253
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mrnngpvala fhtlvilfvl aplaivvlva ftpdetltlp thglslrwfr aildypdfit
       61 afansvklaf asatlslalg lpaglaigra tfpgrafvng lllsplvipg lvlgiallrl
      121 faligatgsf awlvlahtiv itpfvmrlvl asvagldrsi eqaacslgad pwtifrritl
      181 pmivpgitgg wllafinsfd eltmsifvts pqtvtlpvrm ymyatesidp mmasvsalvi
      241 fitagamlll drvyclnril igqh
//
LOCUS       WP_175899031             144 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Burkholderia].
ACCESSION   WP_175899031
VERSION     WP_175899031.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..144
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15515
     Region          1..142
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mfrhilvptd gselsqkaid gaidlaravg arvtayaclp qypyspfsev iieppadfra
       61 rserearthl devesaakaa gvdcdtwtsv hpspylgiie aaehggcdvi fmashgrrgl
      121 gslligsetq rvlthtkipv ivyr
//
LOCUS       WP_175899037             575 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Burkholderia cepacia].
ACCESSION   WP_175899037
VERSION     WP_175899037.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..575
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=63206
     Region          327..570
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mrtkltvknp kpasptrapv rsgslvarka vrpaappagd kparpkkaap aaagersfkp
       61 rgapgaerpg adrapakrap rdggaergtr apyrdnaage gakrsfgdrr pssdrpprrd
      121 ddarprragg dddkrssyrd kaagegakrn fgdrrpssdr pprrdddarp rraggdddkr
      181 ssyrdkaage gakrnfgdrr pssdrpprrd ddarprraga ddgkrpsyrd ktagegakrs
      241 fgdrrpssdr pprrdddarp rragaddgkr psyrdktage gakrsfgdrp arpardgerr
      301 sfgavktaqp vkraaadvdy gdetglmrls krmselgmcs rreadewiek gwvlvdgeri
      361 dtlgtkvrad qkieideras aaqaaqvtil lhkpvgyvsg qaedgyepaa vlitranrws
      421 gdhspvrfsp qhlhalapag rldidstgll vltqngviak qligeqsdid keylvrvrfg
      481 erlididqhf paeslaklrh gleldgvalk pamvswqnge qlrfvlregk krqirrmcel
      541 vgldviglkr vrmgrvtlga lpqgqwryls adetf
//
LOCUS       WP_175899076             331 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia vietnamiensis].
ACCESSION   WP_175899076
VERSION     WP_175899076.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..331
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=35373
     Region          67..316
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mvgpcatppy vddlparvsi vnatspsigl ppyamrgaaa savhpvtdar dasapqaaaa
       61 gasserllai ervsleyrag arivrathqv sfdvyggdrf vllgpsgcgk stllkaiagf
      121 iepvsgsial dgrpvhgpgp drivvfqefd qlppwktvve nvafplraaa klsraearer
      181 alhyldkvgl aafadaypht lsggmkqrva iaralamqpr vllmdepfaa ldaltrrkmq
      241 eellrlwdef rftllfvths ieealvvgnr illlsphpgr vraelnsdeh sfdsvgsgdf
      301 rasvarihhl lfdadalget raastteata s
//
LOCUS       WP_175899084             366 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: C40 family peptidase [Burkholderia].
ACCESSION   WP_175899084
VERSION     WP_175899084.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..366
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37560
     Region          <7..176
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
     Region          <177..>360
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
ORIGIN      
        1 mlriwvpvav vsllaacssv ppqsasrpas gmkittpraf papanfpkfv dhsvgqeeis
       61 iqamslvgvp yrwggntpts gfdcsglvry vigraadvnl prttadmsgr gvsvepdqia
      121 pgdliffntt grphshvgiy vgklrfvnap stggtvrldy ltnpywakrf dgirrvappr
      181 gaptpfdapt yeakrdeprs apvvapapvv vtaaaprqpa ytqsqaaatr apapvmpaaq
      241 avstaavapa aasadpyepp pprmqtaqqq atsvsdgtgt aaatltanaa pagpaevgtq
      301 ipttaltaaq aaafdaeppp avaatsprgt epapvqvlra stqstpvspr tataddpiar
      361 fangsy
//
LOCUS       WP_175899097             637 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sigma-54-dependent Fis family transcriptional
            regulator [Burkholderia].
ACCESSION   WP_175899097
VERSION     WP_175899097.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 637)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 637)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..637
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=69376
     Region          6..630
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mpyavpqaqh adrvlgalag rlpapaestr lvsswqrsle ryrldpassi gprvltaael
       61 revrdkeeaf lrasgqcltr lhdmirvady cvmltdahgv tidyridrer rndfrhaglh
      121 igscwsesee gtcgvanvlt dlapitvhkt dhfraafttl tcsaapifsp ggeligvlda
      181 savqspdgrd sqrlvyqlvr qsaaliedgy fvhstaqhwi lfghpnrhyv eaqpewliaf
      241 decgnivaan rqardalpal reprhideif datemplrda arldaivalr lratgaplya
      301 rlraplrrtg repgtasrrp gttqrhvgal tpflhssdah iaqqaelalr vaskrlpilv
      361 lgetgagkev faraihdaga rrarpfvavn cgalpealie selfgyaaga ftgarkhgar
      421 gkialadggt lfldeigdmp lalqtrllrv ladgevvplg sdtpvrvdld vicathrdla
      481 hmvadgtfre dlyyrlsgat felpplrera dvrdviatvf aeeaqatghv ltldatlaeq
      541 laaypwpgnv rqlrnvlrya cavcdaarvt rqdlpadlaa qlggastalp ddergrivaa
      601 ltahrwrpda aaqalgisra tlyrriakhr ivaphra
//
LOCUS       WP_175899114             330 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: phosphotransferase enzyme family protein
            [Burkholderia].
ACCESSION   WP_175899114
VERSION     WP_175899114.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..330
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=36513
     Region          6..285
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mgplaatfde ileacalgrs gpprqvserv whlptddggv avklyaaghq araareaavl
       61 ahfethgdtr fhvqalkrta agaplwtgan ahamltrwet gqfrtydtfs paewealgas
      121 laalhlsler lqlpsldtir arliaidada vrrslldaln harsnenaan lrryvdlalr
      181 mldryypgsi dafpaddpqh pihndynqfn ylftgtlppl ildweatiga preyelvrcl
      241 nhlpleapql aeafvraylr vrpvdparia wavdaaclqh alklwivqgw lddpsrfash
      301 lsgavtmasa mvdardrlvd ffsrcieagr
//
LOCUS       WP_175899118             291 aa            linear   BCT 11-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175899118
VERSION     WP_175899118.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..291
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32171
     Region          1..239
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mltnqqlafy aehgylviek lfdtdevvrs laaidtllsp anpekpyefe pedgatvrri
       61 wsptqkhpaf kdmataprll dciegligkn vlfhysklnm kgpkvgsvve whqdfsyyph
      121 tnadlvtali flddaseang clrvvpgshr rgllshevdg ffrgkvhdvd earavsievp
      181 agsvlflhcl tlhasarnvs qlprrtflpa yraadafpiy fgphaahnep gvellrgqrs
      241 kvarvdqgth llplaerefg slyevqegsh lrkalttmkt sgyavkaasg r
//
LOCUS       WP_175899131             472 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia vietnamiensis].
ACCESSION   WP_175899131
VERSION     WP_175899131.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..472
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=51137
     Region          83..468
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mtarpaypsp dtpgaaasrs pirvlrraaf vlaaavlgyg afavafpart paaigevvan
       61 wtganphpvv lhrppvqpls avaqlgralf fdpslsasgk qscaschspd raygppnald
      121 vqpggltmtq qgyrpppslm ylyrqpnfsi gpdagendaa psvaqqaasa agvvkaqkva
      181 gtaaapqlvp qggmfwdgra dtlqqqafgp llnpvemana siddvarkla qsphrarfeq
      241 lfgprvfasp qlvvseamfa iaryqvedrs fhpydskydr wlegrarltq telrglrlfn
      301 dpakancagc hlsqpgkdgl ppmftdyqye algvprnral aanrnpafhd lgvcgpfrdd
      361 lkdqtqycgm fltptlrnaa trqvffhngv fhtldqvmaf ynersiapqk fyprgadgkv
      421 deyddippqy ranvdvtdap fdrkpgdrpa mteqdikdie aflgtltdap qk
//
LOCUS       WP_175899141             547 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia vietnamiensis].
ACCESSION   WP_175899141
VERSION     WP_175899141.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..547
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=56521
     Region          15..274
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
     Region          296..544
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mqnhevsadd appkaqrgiq svevggrlld alarrrkplg lselaaaagl ssaqahtylv
       61 sltrlalvkr daltgnyepg plslrlglms ierqpayraa lphaarlaet vglsvalsvp
      121 gvlgptivri ehggyplhmn lhvgsvmsld atatgrvfra fgdpaqldam tashaagada
      181 heythadaha rpdahpsrae ldairargie rsvdrpspgv samcvpvlda hgrlqlaltv
      241 igpsgsidvg wdgpiatalr daarqatasl daapdvrpdt pavprippal gddakaqrgi
      301 naldstgell lalvsagrgl plrdlaaaag mpaakafphl vslqkiglls rddagcfdgg
      361 plglalglia mqrvsptrda epeivalaaa tdmsvaaatl gplgptvirl eesarpqhvs
      421 lqvgtvmslv ntaigrvfas gmsddvlagl ladepvrlag gatqvddafr arlatirmdq
      481 ldfafdapvp gigtiaapvf dhtgsirlvi aiigssrgvp rgtdselaht lraaarrlsw
      541 rfgwigg
//
LOCUS       WP_175899143             356 aa            linear   BCT 11-JAN-2025
DEFINITION  AI-2E family transporter [Burkholderia vietnamiensis].
ACCESSION   WP_175899143
VERSION     WP_175899143.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..356
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37753
     Region          35..355
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mtarvppsnd iaarpraqqi arvvlyaall vlalwvirdf lpaiawacvi aialwpllkr
       61 fesnrwfrdr ptliatvvta gvsllvvlpv aialgqaiaq ahdlriwlhs iqdngialpd
      121 vvsrlpygst qiadwwqanl ghplhagtam hgangekvia fgrqfgtkla halfefgfml
      181 vtlfvimrag hqlsgalllg arrafgrgga aliermvaav ygtvtglvvv glgegailgv
      241 ayalaglpha allgfvtava amlpfcapiv fcgsalwlfv qgatawaivv lalgivvvfv
      301 aehfvrpvli gnstrlpfll vlfgilggae tfgliglfvg palmtvltml wsewva
//
LOCUS       WP_175899147             232 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: energy transducer TonB [Burkholderia].
ACCESSION   WP_175899147
VERSION     WP_175899147.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..232
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24600
     Region          162..231
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mkveeslvts nsgvatlgrp refgkkqqnp vrrfggvgiv lvlhavliya llnglatkvv
       61 qviqhpietr iiepvkpppp ppmpvvklpp pkfapppppf vpppevpvqa ppqatithqs
      121 apvpsapavq apvvappapa kpvshdvgvv cpnsdalras iqypkeaqen nitgdvtief
      181 vvdaegnitn ervaqsadpv ldraayntvk rfkcvaqgqs vrvqvpfsfn ln
//
LOCUS       WP_175899153             547 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175899153
VERSION     WP_175899153.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 547)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..547
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59557
     Region          1..531
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtrpllqidg fsahfganaa vqdlslsigr gervalvges gsgksvtals ilrlaqqatl
       61 sgrmlfdged llakteqqmr girgadiamv fqepmtalnp lytigkqiae slrlheglrp
      121 gearergial lrrtgipepe rridsfphql sggqrqrami amalacrprl lladepttal
      181 dvtvrqqivd llielqerea aergmavlli thdlnlvrrf aqrvavmekg vlvetgttag
      241 lfaapqhpyt rrlldsapqr avepvaagaq tildvwqlav dyriaakgwr svlgkttfra
      301 vhdvqlslkr getlgivges gsgkstlasa vlglqrpasg gieidgmpla slrttqgrrt
      361 lygrmqvvfq dpfgslsprm tveqivgegl gvhrpqvtgd arrariaall qevglpaeam
      421 lryphefsgg qrqriaiara lavepellvl deptsaldvs iqkqvlnllt nlqkkyklsy
      481 lfithdlavm ramahrvivm kagrvveege tldvlhapsh pytrallass mpapargpqq
      541 rqeridd
//
LOCUS       WP_175899174             316 aa            linear   BCT 11-JAN-2025
DEFINITION  ketopantoate reductase family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175899174
VERSION     WP_175899174.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..316
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32785
     Region          1..307
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkiailgaga lgcaigaalt eggnevwlln rsaahveamr rdglrvddrn vsrhvkvhat
       61 traaeagvvd lvivlvksfd tdaamrgave ligpetlvls lqnglghedv ladivgrerv
      121 lagktyvggv mrnpghiesg vagkathige ldgritpran aiadtfnasg ldttvsaniv
      181 gtmwdkllvn vatgaltgat gltygqlyde pllkatalsa vaeamavaha agvtlstddp
      241 erawtlageg lspgfktsml qslekgsite idfingavvr wgrrhgvptp vnatlvacik
      301 giergmadrk kqetta
//
LOCUS       WP_175899198             430 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia cepacia].
ACCESSION   WP_175899198
VERSION     WP_175899198.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..430
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46581
     Region          38..419
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 msfhfgtpla rrarrrapml waallvagaa haqqppftld aalqsatdhs asmqaaqasv
       61 rasseaavka gqlpdpmlka gidnlpvngg qrftvgqdfm tmrrigieqe wvsgdkrrlr
      121 salaneqvgr eragylaqla svrqqtataw lnavyakqal alqqalldhm nheldatkas
      181 yrgakasaad vvqaramlaq tqdqwlkarq vyqtalials rwtavsasdv tgtppapesf
      241 vsslppdelr vsqpalitaa ddiavaeadt avanserrpn wtwevayqqr ggaysnmvsv
      301 gvtiplplnr rnrqnrdvae kaelatkarl myedtlrqvq adirtqsetl asgrerianl
      361 stsllpaagq rvqladaayr agtgsladtf aarraqldaq lqmldlrrdv sqtwaqleyq
      421 vvpstmaaaq
//
LOCUS       WP_175899207             336 aa            linear   BCT 11-JAN-2025
DEFINITION  sodium:calcium antiporter [Burkholderia cepacia].
ACCESSION   WP_175899207
VERSION     WP_175899207.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schnetkamp,P.P.
  TITLE     The SLC24 gene family of Na/Ca(2)-K exchangers: from sight and
            smell to memory consolidation and skin pigmentation
  JOURNAL   Mol Aspects Med 34 (2-3), 455-464 (2013)
   PUBMED   23506883
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Besserer,G.M., Nicoll,D.A., Abramson,J. and Philipson,K.D.
  TITLE     Characterization and purification of a Na+/Ca2+ exchanger from an
            archaebacterium
  JOURNAL   J Biol Chem 287 (11), 8652-8659 (2012)
   PUBMED   22287543
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..336
                     /product="sodium:calcium antiporter"
                     /GO_function="GO:0008273 - calcium, potassium:sodium
                     antiporter activity [Evidence IEA]"
                     /GO_process="GO:0006874 - intracellular calcium ion
                     homeostasis [Evidence IEA]"
                     /calculated_mol_wt=35319
     Region          19..332
                     /region_name="ECM27"
                     /note="Ca2+/Na+ antiporter [Inorganic ion transport and
                     metabolism]; COG0530"
                     /db_xref="CDD:440296"
ORIGIN      
        1 mtfmfvelav mlivilvaae vftnalehlg erlkisegvt gslfaavgta lpetmvplla
       61 laggtanpav neeigvgail gaplmlatlt tflmtltvir srglrgtiap ertgfvrdln
      121 yflaafslat aamfvphhns avrallaaml vgiyvmyvvm tfrasnqlvd aghgteaphk
      181 mflsrvgvpt nlatialqll igvallvgga kgfihgvegv srvlgvsall lsliivpiat
      241 elpekvnsvl wirrgkdtla fgnitgamvf qgtllpaigi mltpweprle vltgvivtla
      301 aaawlrvnar trglaiwall angagyaayl fltlar
//
LOCUS       WP_175899213             498 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia cepacia].
ACCESSION   WP_175899213
VERSION     WP_175899213.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..498
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53586
     Region          72..450
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mtrlsispri gaaaavlafl agcttfskdg gfdavssvas erigkdavvv rtdadreavd
       61 trtkellakp lsiddavqva llnnrglqas yaelglsead lvqagrlpnp rfafsrtrag
      121 dgeltlgrtf sanvfalltl platnierrr feqtkletad amlkvaadar rayveavaae
      181 qaanyagqvr daasaaaela qrmrqagnfs rldyareqaf hadavaqhak arqqavaare
      241 kltramglwg ertqyalper lpdlpkarpn lpdlerfamr nrldiqaakl qtqgvasslg
      301 lskatrfvna vdlgyvndye tgkghehgfe isveiplfdw ggakvaraea vymqsanrla
      361 ktaidarsev resyaaymts ydvathyrde vvplrktisd elllryngml asvfellada
      421 reqvgavngy idalkdywla etdlqmavgg rlptpgdvph atpsappesa snadaapqpa
      481 stsaaqsapa tqthpegh
//
LOCUS       WP_175899229             263 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175899229
VERSION     WP_175899229.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..263
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29448
     Region          32..87
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(33,58)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(40..41,52,55,59..60)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          104..263
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mtvttrtpfg dflrsrrkkl rpdavglhgg prrrtpglrr eevaelagig vdwyvrleqg
       61 rdvspsdatl dalaralrld kaeaahlrtl arrdearafv pervppaiar lvahlrqpay
      121 vtgrrwdila wnaaaaellg fdrlaeadrn ilvymfveph aralfaaswa dearrmialf
      181 ranhdlyase pafvalverl ragsvefaqw wdehdvrsgv sgekvlvhaq rgaqryeyat
      241 fqanddpalk laiytpmdgd egt
//
LOCUS       WP_175899243             496 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: phenylacetate--CoA ligase family protein
            [Burkholderia].
ACCESSION   WP_175899243
VERSION     WP_175899243.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Luengo,J.M., Garcia,J.L. and Olivera,E.R.
  TITLE     The phenylacetyl-CoA catabolon: a complex catabolic unit with broad
            biotechnological applications
  JOURNAL   Mol Microbiol 39 (6), 1434-1442 (2001)
   PUBMED   11260461
REFERENCE   2  (residues 1 to 496)
  AUTHORS   El-Said Mohamed,M.
  TITLE     Biochemical and molecular characterization of
            phenylacetate-coenzyme A ligase, an enzyme catalyzing the first
            step in aerobic metabolism of phenylacetic acid in Azoarcus evansii
  JOURNAL   J Bacteriol 182 (2), 286-294 (2000)
   PUBMED   10629172
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Ferrandez,A., Minambres,B., Garcia,B., Olivera,E.R., Luengo,J.M.,
            Garcia,J.L. and Diaz,E.
  TITLE     Catabolism of phenylacetic acid in Escherichia coli.
            Characterization of a new aerobic hybrid pathway
  JOURNAL   J Biol Chem 273 (40), 25974-25986 (1998)
   PUBMED   9748275
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..496
                     /product="phenylacetate--CoA ligase family protein"
                     /EC_number="6.2.1.30"
                     /GO_function="GO:0047475 - phenylacetate-CoA ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0010124 - phenylacetate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55726
     Region          49..490
                     /region_name="PaaK"
                     /note="Phenylacetate-coenzyme A ligase PaaK,
                     adenylate-forming domain family [Coenzyme transport and
                     metabolism]; COG1541"
                     /db_xref="CDD:441150"
ORIGIN      
        1 mntlirlfle avlwtlwflr rvisvdgrly vflnapifqp ylayvgrmra rvaflkasts
       61 cpayieflka egykaggkwr ladlpamtke nyikrysiel rcyggaipks gvvidessgs
      121 tgqpnnwvrs aaersdvkri lqlnyqlvfr dsgkmllncf algpwatgmn vsmslvdvgi
      181 mksigpdkak lintlklfgp kyqylifgyp pfirsvvdec dldlsayhid fivggeglse
      241 alrdhllrka stvissygas dleinigvet pttiglrral ltrpelcrel fgrdtppmif
      301 qynaldyvie tnddgellvt igrqsgaapk irynirdsgg tyrfrelnrr lsahgmrlqd
      361 faartshfpf lfvygrndss vpfygakvfp sdieqvlsas pvlhdaistf qlattedaql
      421 tsflhlhler algsapmpld daalhgemve gmkrvnqdfr evsrlfdpkq vvvhlhehdt
      481 gpfqgrdiri knryia
//
LOCUS       WP_175899284             304 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cepacia].
ACCESSION   WP_175899284
VERSION     WP_175899284.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..304
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33650
     Region          1..300
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mtrhdiefls eaatlrgwyy epaqriagte aypaivmahg fsgvkeqyld ryaevfaagg
       61 fgvllydhrn fgasdgyprq eidpvqqkrg yrdaisyllt rpdvdaarig iwgtsysggh
      121 vlevaaidrr vkcvvsqvpt isgyqsalrr trsdlvpaal arfdedrrqr faggvpamlp
      181 avsadpatac amagadayrf ftesaarcap nwknevtlrs aemsrenepg qfvdrisptp
      241 llmivanddl ltptdlclka wenalepkrl lqikgghftp ylehfdetsr aavewftlhl
      301 sgar
//
LOCUS       WP_175899314             273 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: energy transducer TonB [Burkholderia].
ACCESSION   WP_175899314
VERSION     WP_175899314.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..273
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27732
     Region          194..272
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mtgltieygv pparrhaara aprtgagvaa avaaawppsa spaarpdara akpgqwrvtg
       61 avalavaalh agvallaara pvaspvqppr plpmtveltr ppeplpqaah ppppvvpkpq
      121 pplkqaptpp kpraavahpa papaatqpvm reaapaptap avaaqattap apaapaapvr
      181 etapigdaay lrnpapdypa faqdqgwegr vvlrvhvlan gtpdavdvrt ssgrrmldna
      241 avaavkrwtf vpakrgdeav dgwvnvpidf klg
//
LOCUS       WP_175899285             285 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia
            vietnamiensis].
ACCESSION   WP_175899285
VERSION     WP_175899285.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..285
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30896
     Region          28..267
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 msdakaapds taarvalwra lhveldapph vladeiglrl lapapgwqqr gdmdpkftrp
       61 frasivarar fiedlvveqa aqgvsqyvil gagldsfvqr rpemasrvtv fevdppapqa
      121 wkrrrlvelg fgvpdwlrfv pvdfeakqsw rdalvragfd agkpavvvst gvsmyltrea
      181 naaalrevas lapdttfamt fllplehadp dvrpglemae qgarasgtpf isffmpdeir
      241 alataagfar aehvsadala rryfagradg lrppnnaeel lvatv
//
LOCUS       WP_175899438             843 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175899438
VERSION     WP_175899438.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 843)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 843)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..843
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=92363
     Region          14..811
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mghtalyktl rlgdaqynrl vkldtplgvd wllplyvkgt arlgrdyefe idavsprgsq
       61 ielsallakp vtlwiqqtdg sylpihgyvh rfsrlgadgp ltfyklafss wlyflrlrrd
      121 mrdwqeqnge qilvdvfneh sqargafrid lhkplpsysn rvqweydlnf vyrsmeevgv
      181 fpyfeqaeng rshtmvvtdd vyfvpqlkqp vvefgpteis geldgfaqwk eqlqidsaql
      241 tsrsfdykrp dlprqvqgvt dvngelptdg eiydypgaym wsdreqgerl aqirleerks
      301 rmkrfhgigg lrcampgrrf elrghpvhda gsqpdrefvl lgvdwlicnn lpgldeadqf
      361 pdglaaevaq akagatvrha dgsegffqvv veaqprnvpf rspfehkkpv mqlqnaivag
      421 psgeevytds lnrvkvwfhw nrrngqdera scwvrptfld agsnrggiqp lrkgdevvvg
      481 fmegdcdrpv iiarmyggat qpvwhtngll sgqrsreygg tgynqlvmdd stqqnrvhly
      541 sssyqshlhl gyliqqtdnt rgaflgsgfd lksdaygair agqglfvsth ptatnqplnv
      601 taaseqlasa etvidltsqa sssnqaeslq egqdalkkft dathysvsgg agsggrtggg
      661 gtgnangfst pimlmaspag lglstqdsaq ltanqqvniv sgksthvaag ksliasvmek
      721 islfaqnagi klfaakgkve iqaqsdemkl aalndvtits sngrvvisae keiwigaggs
      781 yikitpdlie ngtsgqilek csswdkpgas smrlpspias vpkgcawkta saaadsassv
      841 vle
//
LOCUS       WP_175899451             414 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175899451
VERSION     WP_175899451.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..414
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=45495
     Region          8..>119
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mnrqqswtrt aapgeiiyse gfagepvifl itdgkvelst rcddkrvvva tlgrgeffge
       61 sallaaepra htakalsfcq ltvvpagmld eeiervsall rhivrtmilr vkrkddqlat
      121 ythadfmpgv lsyahvlalm agadareagd awtrrpmqah aaetsvplae virkcraiag
      181 hsrphvlaml rrmeklnlvt ieaaqadhag gaadyaassd arqvvtfdaa rvidraqqva
      241 dhdldlsins elelieladl esligvektm llnklsngei adevfafrks kvlsyveqkg
      301 vayfsrrnar rggdvraled lvwidqrtlf dvisafdtyd laklianldd ravadklfsv
      361 mtearrnevs wvmrrelkld pveiedierr vldavraaka paagttpvas asda
//
LOCUS       WP_175899480             207 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: BON domain-containing protein [Burkholderia].
ACCESSION   WP_175899480
VERSION     WP_175899480.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..207
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=20740
     Region          34..199
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mkgilsshts irtaliavgl vaglgigaac laagessmsk tassvgtaid dtaittkvka
       61 rlmgeeglgk sdisvttvdg vvtldgtvss lhaksvaesa arsvdgvqrv sdnlavpmda
      121 gkpakpgava kteravsdsw ittkvkskil sdsvskgfdv svmtthgvvt lkgslasqha
      181 idhvrniars vkgvrhvntg glvvagk
//
LOCUS       WP_175899507             239 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175899507
VERSION     WP_175899507.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..239
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25226
     Region          4..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mstdrsnpdv rtrlieatir llatngpsev karsvaneag lstigvynyf ggvpellrav
       61 adeglrrlva afeqvpktdd pladlcamal ahrdaarcna hlydlmfgls ihsrygpara
      121 ganavpsvhs safkaafall vdtcarlvet gcvrqtdpvh iglqlwgavh gfvtlelagh
      181 fadvadppse ilvpmcnnlv vglgatrasv eaatsrvvgv rastqevest aptrkrrgt
//
LOCUS       WP_175899547            1085 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia
            vietnamiensis].
ACCESSION   WP_175899547
VERSION     WP_175899547.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..1085
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114506
     Region          1..1058
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mwivrlalrr pytfvvlall ifiagplall rmptdifpni dipvvsivws yngfsaedma
       61 kritsnyera ltsdvddieh iesqslngvs vvkvffhpga dinraiaeaa snaasilril
      121 ppgtlppnii tynastvpil qlglssdtla eqqlydlgns firtqlatvq gaavplpygg
      181 kirqivvdld tralqakgla pidvvnaina qnlilpggta kigtheydvq lngstqtvaa
      241 lndlpvktig gsvvyvrdva hvrdgyapqt nivradgkra alltvektgs astltiidqv
      301 kamlpkiaag lpkalhiaal ddqsvfvksa iqgvvreali aacltalmil lflgswratl
      361 iiavsiplav ltsllalgal gqtinimtlg glalavgilv ddatvaieni thhlergepl
      421 edailtgage iavptfvstl sicivfvpmf lltgvarylf vpmaeavifa mvasyffsrt
      481 lvptlamvlm rtkgqgrppr gvfariaglq aaferrfdai rlgyrallaa aiahrrrfaa
      541 afvlacvast glfafagqdf fpaidtgeir lhlraptgtr ieqtarltde veakvrsvip
      601 arelagmldn igvpvsginl tydssdpigt edadvmitlk pghaptaayv arlrnllaqs
      661 fpgvtfaflp adivsqilnf glpapvdiqi vgnkldqnra vanallaklr gvrglvdari
      721 qqpgdepaid vnvdrtkaie aglqqrdvaq nllialsgss qttpnfwldp rngvsypvlv
      781 qtpqytidsl qalanvplpt sgapspqrpa ggpaagapaq nllgtlgsfs rttqqavvsh
      841 ynvqpvldif asvqgrdlga vtadvtklvd dvraqlppgs sivlrgqvqa mhesfagllg
      901 glalaialvy llmvvnfqsw ldplvivggl paslagiawm lfvtrttlsv paltgtilci
      961 giatansilv vnaarellag gaspwqaald agfsrfrpvv mtalamligm lpmalglgdg
     1021 geqnaplgra vigglafgtl stllfvpvvf gfvhawlerr rdaarargap dmpnapaapd
     1081 tpalr
//
LOCUS       WP_175899571             783 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175899571
VERSION     WP_175899571.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 783)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..783
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=87366
     Region          1..754
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msmilpsqay elklaphpap tsvlrftgrd avselyhydi eftspvagip mdqvvgrpak
       61 fivspvdpnm nylrrmfgen aeqfsalpta ytihgiitef defgtsndqt hyrvrlepkl
      121 adlnrgvtsr lfqkqsvdei vtdtlrhygy ragvdfqfql rdqykrreyv tqyhettfaf
      181 irricteegi wfrweqkkdh avlvfgddld aysrkqrtla yrrdagless gadaiktldk
      241 rtrrvpeavr lndynhrqag vsllveenaa rddkttsgid yrwgehyetp eegkrvarrr
      301 heeflaaqit fkgtgnpfwl eagevmrlep npsdakhgif vtsveshggr dqsywvtfeg
      361 ipsdrvwrta masisrpavd gilparitsp gnykyaylte qgwyviklpf dldewspggt
      421 srpvrfakpy sgdnyghhfp lidgaevaiv ftdghpdrpv iigamhdslh pdlvnnlnht
      481 rnvvrtaaqn elrmedkenv ehihlttpfq tselnlghmv detrkergqg aelrtdghla
      541 araskgmlls teaqsdangk qldmskatgq leeafslmqn ltanaeaara hlaeldeqrq
      601 fleqrlnglq ravilasapd gialtsgehl qfaarnnlav taggsadigv fkkftvaage
      661 aismfaqklg mklfaargki eiqaqtdeme isalkdlkic svdgklilaa tkevwigagg
      721 syikitpngi engtpgdile kcaswdkpsa vsdkipmpel pqgvckecrm haaqsrsalt
      781 pra
//
LOCUS       WP_175899584             784 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175899584
VERSION     WP_175899584.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 784)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 784)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..784
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=86402
     Region          19..753
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mqtiqdvlah psaivtqplh leiatlqspv svfsfvltee mnapfvadit vtskdkhidg
       61 aavvgrpaif tieehasvps lselinpfqr aartvhgivt qwtriktsrd eatyqvllkp
      121 rlalleqvhd savfldrsfr elltdtiidr elfqsydvef eldgldakld qtvmyeetva
      181 nfidrhcrra gvfyyfkhak kedgpqrdtl vfsntargym reievpllpn sglvswheai
      241 lelnvtrslv pqtvrewdhn yrqpddplqv esavaekadr svygsinrsi ehfhtaeegq
      301 aladarrdgl itrqtriagk snvmgmmpgm vvrvmndvtp eaphgfvitk lvttgsrkes
      361 vtnqfeaips hltyrpdyvp erhwrwvaga ligivesgdd qpyawmdeyg gyrvrllftr
      421 htgkrgansm slrllrtsas yqgglhvpll pntevrviat qgncdrllia gathdyarrd
      481 lvhgkegwys ravfrspllg nklrfedlkd hegirlatvf gqsslnmgyl vdreknkrge
      541 gyelttqgwg vvraakglfw sadpvnrtap hlemqvaikq lqaaiqrvta lanatgqara
      601 tsadkatqsn lmdvldqlkd agllasapag mafvtpksiq qaagenvivt agqhadvsvv
      661 krftvaagel islcahklgl kvfathgkve iqsqsdamdl vaakqlklas adedvlvvar
      721 kkivlasgga alkiedgtfe figpgafkik agsfvfqgpg nvnpplpvlp ksnlnspddy
      781 plsh
//
LOCUS       WP_175899613             286 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Burkholderia].
ACCESSION   WP_175899613
VERSION     WP_175899613.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15202679
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..286
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30746
     Region          12..132
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          168..269
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 msdlnpsrtl iyrrfaetdl paahrlseav kwphrlddwr fvlqlgdgfv aedetgivgt
       61 algwrfgeah aslgmvivsp ehqgrgigre lltrvvdsfg trtiflhatp ageplyakfg
      121 fevidtidqh qgaafqppli slppgerlrp igandgprla alasraagyr rdevieallg
      181 vangialdrd gellgfalfr rfgrghaigp vvapdaqraq alishwlalh egkfvrldvp
      241 gdsglsdwlq glglprvdtv vamargatpa rapalrafai vnqalg
//
LOCUS       WP_175899701             928 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175899701
VERSION     WP_175899701.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 928)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 928)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..928
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..928
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=101249
     Region          25..840
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mdirssalgd lklrelyeai sngvlqqgrl lmldtplgkn alvplrargs arigrdysyt
       61 idvastrddt allslmhqpv tlqiqqvtap faipvyrpvh gfvhrvaylg gngglstyqi
      121 efssalvfle kthneegwle kdareiisdv ldrypqlrgq yrfsllsdpa krswcrqses
      181 dlhfvnrlae aegwyfywih envaegdapk talvivdhvs tlpdakavef irandsnesd
      241 gfahwtgvqt mqstryisra fdykrpasdf qaesglaats yvteerrqkv ersvpdvpmt
      301 vyestaygys ssdtgearar rlvevwdara sryfgvggvr wldagsrfvl nghprheggd
      361 akkreflvie arwfiennvp igqqtaefpq slratlaeqq aihrerfktp ghaadgsagf
      421 fvieveaqpt tveyrspldh pkpimsieha lvvtpdgaea wtndrnqirv hfawdrknpp
      481 daftssplls slqsdtgngy gavhvprare wvivgywngd cdkpfvlgri nggatpspwh
      541 snallsgfks egfgktgayn sfvhddstnq ggtrlvsytg ksyaaltqgy likhegntrg
      601 kylgagfilh adefgavras kglsisahsk syddeqmgvd earsqlqqag mlveslssas
      661 ttaqaeslqt gqdalkalsk diqhpvsgdt sggvtagggt gsangfsqpn ilvstpkdia
      721 lvadnsthiv aekeinvvsn entymatgks lvvaaaekvs ffaqklgaff vtakgpikls
      781 antddvnvna gkdvtvkakr ivldadeiii kaggsytrwv aagiedgtqg prtiksasls
      841 rqgpssiaqh mnslpqakfn dpyvlrdris gevlknhpye lvrgdgtrik gmtnelghva
      901 eqknedietl klhalrpelp assgngse
//
LOCUS       WP_175899733             187 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: shikimate kinase [Burkholderia].
ACCESSION   WP_175899733
VERSION     WP_175899733.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Herrmann,K.M.
  TITLE     The shikimate pathway as an entry to aromatic secondary metabolism
  JOURNAL   Plant Physiol 107 (1), 7-12 (1995)
   PUBMED   7870841
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Bentley,R.
  TITLE     The shikimate pathway--a metabolic tree with many branches
  JOURNAL   Crit Rev Biochem Mol Biol 25 (5), 307-384 (1990)
   PUBMED   2279393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..187
                     /product="shikimate kinase"
                     /EC_number="2.7.1.71"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004765 - shikimate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=20174
     Region          18..179
                     /region_name="AroK"
                     /note="Shikimate kinase [Amino acid transport and
                     metabolism]; COG0703"
                     /db_xref="CDD:440467"
ORIGIN      
        1 msavttavda ralpdraflv gmmgagkstl gralaaslgw tfadsddeia rrtgrsvael
       61 fdrvgeggfr lletqivdel tqrpnvvvat gggavlnprs rarlsergcv iylhadpdal
      121 wrrtrddtrr pllqvadprq tlaalyrmrd plyrecahal vdttaqdvac atadvltvll
      181 aridapd
//
LOCUS       WP_175899793             159 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia seminalis].
ACCESSION   WP_175899793
VERSION     WP_175899793.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..159
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17248
     Region          14..132
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mtsrdtlfti apidaaqthp lraaillngd lnacelagdh apttlhvgvr drsgivavas
       61 lceeprdddp aqpawrlrgm avhpavrgmg fgrvlvqvcv rhaeergaal vwctareaay
      121 rfyeklgfaa dgalmtmpgr tdtvfhvmrr yigrhsrsa
//
LOCUS       WP_175899803             236 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: thioesterase II family protein [Burkholderia].
ACCESSION   WP_175899803
VERSION     WP_175899803.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..236
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=25572
     Region          1..230
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mrlicfpyag gsaavyrple allpgidvyr helagrgsrl sepaardmst lidtllrdlr
       61 dcfdrpfsll ghsmgaaiaa elalrlpadv rpnlrhlfvs graapgnarp grrmqalddh
      121 afidalhemg gtpkpvlend elmallmpal radfalieny rpepgcqlav ditafagrad
      181 thapvdsvag wraatagnfd fhviegdhff lrsemrtmag iiaarlrhah ciasna
//
LOCUS       WP_175899849             857 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175899849
VERSION     WP_175899849.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 857)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 857)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..857
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..857
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=94003
     Region          26..752
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 madlfddarr fvsnltevsg rqayflevpg adsaaalsiv sveatekmga ptevrivlth
       61 plaleradyl nrdaafsivs vdgmprrfsg fiagfstlqt tadftkyevv lkshfarlka
      121 vstsriyqhq ttpqiidavl rshgleghqf afrlrreypk hlfrfqykld dlsyvqmlmq
      181 kagiysyive tehgdqvvfa ddidhylwdp hltvpyreva gleatgmeav talrthsvvv
      241 pqsfvvadyn peqawerfrd danvapqdpt tygqtyvygt hhldqdgakw eaqlrheaai
      301 awqvvyeges nvlalqagrv lnldtvlpda pdgqvvievt hrgardrayt nsykaipanr
      361 rfrlqledam wpkiagtlsa rvtspdkyky ayltaagyyt vrfdvdfadw paggesvplr
      421 lakpfagklq tgfhfpaqdn deaviafrda dpdkpeiigf hhhsqardlv tsdrrwlsrn
      481 virtqsnnkl rmedwagqeg iklstehsgt shmdlgylvd eklerrgegf elrtsghgve
      541 ragkglhlta ydrpgasgkq ldmqetiaql eqalalaksl gdaartakam padtdaqqqm
      601 kdefdglkqp gllasapasi gvvagggvqm aakesisava gknadfsvmk rftaaageav
      661 slfaqklgik ifaakgpvei qaqsdamslv ankdvtvasv ngtvrisark eltlncggaf
      721 iqlkdgditl ggpldlflkv itiqkkgkes lapsfvvlps gkvgdlphfl einhhyadie
      781 pvrnapykvq lsdgviltgt ldakgfahld gvepgkatie lgedarhwrg eakrpnsdad
      841 aapdrqsain larkfls
//
LOCUS       WP_175899854             469 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia seminalis].
ACCESSION   WP_175899854
VERSION     WP_175899854.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..469
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47245
     Region          31..430
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,157,
                     160..161,164,288,291..292,295..297,300,328,332,385..386,
                     390,394,410,413..414,417..418,421)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msdcnsvpvs vplpaasrpt areqrftlal vaigmfmavl dstivnvalp amraslgatv
       61 aelawivday tlsfaalila ggalsdrfga khaylaglal fvaasaacgv apsvailvaa
      121 rfvqgigaal flpaslavvr gtfdvpaera raiavwagia svavavgpvl ggilvddfgw
      181 rsaflinvpt gavafagaam lvrasggrha hpfdwagqgi gaaalgalcf avielptrgp
      241 gagevrcall aaalaaallv vverrtrhpm vplawfrnrv fvamnlmgsl vyvgyfgllf
      301 vlslylhgsf gmsarqtgmt llpfalslsl gnllsgklhg rvrpvtlmas glgtaalaip
      361 aiavalalra pwpvvwtama afgtgtassv apmiatvleq vpaeaagvas gflnaarqag
      421 slfgvavaga atillpdltd alwaiaalgc vayavaalaa raagmtkgt
//
LOCUS       WP_175899862             147 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Burkholderia].
ACCESSION   WP_175899862
VERSION     WP_175899862.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..147
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15547
     Region          27..147
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mtvvkrpnvs skialtggah miaslgilvp veddrfravv dfyrlalalp vhyegvsaag
       61 npwhrfvmgg atltvhtgsg grfpypefrp tghgialave vahvsevvar lescrvgiln
      121 ewdygdgtva isvadpagnv ceiwgrp
//
LOCUS       WP_175899896             324 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175899896
VERSION     WP_175899896.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..324
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35663
     Region          13..72
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          101..301
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(111,115,154,168,170,232,249,280)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(112..113,117..118,120..121,124,128,130..136,197,
                     226..230,237..238,241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mkkgaretgv dhlgamrafv rvvetgsfsa vakemhvsts tvarkvtaie dalgvallhr
       61 sthsvtltea ghiyleravt liadlddtlr vvaelnaqps gplkltapva fgrrhlaplv
      121 apflarypti qldvrltdnh ndlvaggydl dihegenyld nlvvhrlsrn dsilcatpgy
      181 ldrcgrpasp ddlkhhnclr yvhpegdprw dfvngdvrhs vlpagnlvtd hsellleatc
      241 aglgiaefei wlvrdllasg rleavlpryr lqnrltgeyi yiaylanrrs saklrvlkdf
      301 laehlaqige lserelakir gara
//
LOCUS       WP_175899903             421 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia vietnamiensis].
ACCESSION   WP_175899903
VERSION     WP_175899903.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..421
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45440
     Region          91..415
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnqphhirii gmprsrdaya irdflqrrmv aydwceltsd adctrelgia plrdvrlpvv
       61 ifpdgsrlyq ptlaeiaarl gwvaqprfve ydvliygagp aglsaavyaa seglravlie
      121 raavggqagt sslienymgf pdgipgaela erareqatkf gvelltmreg vharfvdgki
      181 hvdladgsvl varsnicatg ieyrslglpe epaflnaglf ygagsseapm csgehvfivg
      241 ggnsagqaam nfsrharevt mlvrgaslad tlsrylidri ertpnitvry rsavdalygd
      301 gwldaigirt ddgpservpa trlfvcigga pntewakdta iirnpggylv tgtdlydcpa
      361 fervwplerr pyyletsvpg sfaagdvrsg svkrvasavg egamavtfvh rflgedahrl
      421 a
//
LOCUS       WP_175899956             159 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF2280 domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175899956
VERSION     WP_175899956.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009432
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..159
                     /product="DUF2280 domain-containing protein"
                     /calculated_mol_wt=17650
     Region          1..149
                     /region_name="COG5556"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:444299"
ORIGIN      
        1 maalpepikv fvtqalacfd tpsraakavr eefgvevspq qcerydptkr agsalskkyr
       61 eifertreef lkdtsrigva hravrlrkld ravgvaeerg niplmaqlle qaakesgdaf
      121 tnkhrlehtg kdgapidqrt vvvdekqvad avakledey
//
LOCUS       WP_175900021             325 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175900021
VERSION     WP_175900021.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..325
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34257
     Region          6..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..302
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mgdidlnlvt aldallsess vtgaarrlgl stsamsrtlt rlriatgdpl lvragrrlvp
       61 tphaaalrdr vhaiasdara vlrpatadvd matlaatfti raaasfmeml sgpvvaalge
      121 iaphvrirfv skpdrdpqgl rdgtvdleig krgddapelh trmlfhdwhv avaraghplf
      181 asaritpary aacrhvisaq lgdfggpagd saartgsgsp vhvvvpgypd amrvaastdl
      241 ialvprsslg nafspgltea lglrsfeipv rlpailvsal whprmhgdpl hrrlrdavia
      301 vcqraypdsr apratargag trkvg
//
LOCUS       WP_175900070             430 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia vietnamiensis].
ACCESSION   WP_175900070
VERSION     WP_175900070.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..430
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=46990
     Region          16..345
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mnemksnsvd vaiigagpsg avaaallrna grsvlvlerq hfprfsiges llpqsmryld
       61 eagmlqavve agfqfkngay fvhrdrmssf dfrdkfsdgw gtayqveraa fddllircae
      121 kqgaqvrfgh tvrafhagat prldvvdeag heysvqasfv ldasgfgrvl prllgleapt
      181 glptraaifs hvedrlsags tdrdkiciav hperrdvwyw mipltngrss vgcvadaafl
      241 dvpeaeqeal lrellqtept lsrlvgskpf vmpvrricgy asnveslhgh gyallgnage
      301 fldpifssgv tialrsahla vatlerqlrg etvdwardyd valrkgidtf rafverwysg
      361 alqdivfhed kasdvkrmvc silagyawde tnpfvrepar gldilaqlcc ptgasgnaaq
      421 aatpdgarrr
//
LOCUS       WP_175900049             328 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Burkholderia].
ACCESSION   WP_175900049
VERSION     WP_175900049.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..328
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34326
     Region          7..324
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mndndhrpvr fgiigagsia rrfaqslahv pgatlagawa rradataafc gahggspaas
       61 leallasdid avyiatlhds haqytlaala agkavlcekp atlnaaqldt vlqaardagq
      121 lfmeamkppf fplyrqlrah lqddpigeir lvragcasss vpgdhsvyrl draggalldi
      181 giyeaflavd wlgaaldvqt lgrvgatgvd lfaslnsvha hggiaqlfcg ldvmgrgdal
      241 iaaagghvti hekwwnpvra tisyadgrtv eldapaeggg lnyetahfcd llragktesp
      301 imthdhsrqm iamtdaaraa lgvrysge
//
LOCUS       WP_175900116             733 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Burkholderia].
ACCESSION   WP_175900116
VERSION     WP_175900116.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 733)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..733
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..733
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79992
     Region          33..716
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 msassplspt aggpfaawya afgdwartdg aawlylfkal laafialgvs mrldlpapkt
       61 amttvfivmq pqsgavlaks fyrvagtifg liatltfvgl fpqqpqlfll aialwialct
      121 agaarnrnfr sygfllagyt taliglpasq hpdgafmsam trvseviigi vsagvvsalv
      181 fprytgeqmr ttvrkrfgsf vdyvasalsg qldrahieti htrfvadvvg feaarsmavf
      241 edpdtrmrsg rlarlnsefm sassrfhalh qlmnrlhaag aqaaidaiep yfreiapllt
      301 rdgepvrtsi daahsaeqll awrdalprri ratraeletq pdfplldfdt aaellyrfit
      361 dlqeyaatya slatathere rwieryeprt nktaatiagi rtatvilalg wfwietawps
      421 gvmlvlnaaa tcalassapr ptamaaqmgm gtalavctgf lltfgiypri dgfvllcaal
      481 apllaigiym slkpklagyg agyliffcfl agpdsithyd ptsfmndala lllsmlvsai
      541 afavlfppta pwlkkrllad lrhqavaach arlaglrtrf esgardlmyq ahtlsadqpd
      601 vqrdalrwmf avletgnaai dlrhelatlp sdpryapttp wrraietmra alsslfarpd
      661 aerfdatlaa vndaidatrq tldaftptre erhrlqrils hlhfvrtall dpesplaaln
      721 rnrpvrpqpg ass
//
LOCUS       WP_175900192             477 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia seminalis].
ACCESSION   WP_175900192
VERSION     WP_175900192.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..477
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48542
     Region          23..450
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,277,280..281,284..286,289,317,321,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msefaspaga hepavnwram savllavala tldtaianta lpaiaadlqa spaasvwiin
       61 ayqlamvatl lpfaslgdiv ghkrvyiagl avftlaslgc slastlpmlt aarivqgfga
      121 saimsvnval irglfpahrl grgvgfnalv vgvsfavgpt iaslilsvaa wpwlfavnvp
      181 lgvialavai pslpqtargk hvfdpvaalf nvitfaslif algefaqrgp lsivfasaav
      241 alafgwllir rqaghpapml pvdlfrrpvf tlsaltavca faaqglafvs lpfyfetvlh
      301 rsavetgflm tpwsaivafa apiagrlsdr yppgllgaig lallsagmvs laalptspsv
      361 vdigwrmmlc gagfgffqsp nlkalmssap persggasgi iatarligqa tgaalvalsf
      421 giagrhgptl almlgagfag aasvasglrl fapshragvp aapervneqa aeqgtgq
//
LOCUS       WP_175900195             524 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia vietnamiensis].
ACCESSION   WP_175900195
VERSION     WP_175900195.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..524
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52667
     Region          37..515
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,157,
                     160..161,164,288,291..292,295..297,300,328,332,384..385,
                     389,393,409,412..413,416..417,420)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mpqpspvspm ssvsrsggga gapaaatlav asatcslivl dtnvvavslp siargfhasf
       61 aeiewvvsay mtafaacllp aggladrfgr krmlaaglal falaslgcgv apsaawliaa
      121 ravkgggaam lltaalavia nrfpdgrera rawaiwgmcm giatalapli ggaitqwigw
      181 rwvfllnlpa callaagvra aiaesrdpha trvdapgsll fgaalacaia aligapshgw
      241 ltgatlgrlg laaalstafv averrharpm vdlalfgqpr fvgavvamfg yaacaqvmmt
      301 flplylqnaf gmsaidaglg mlpfalamiv gpslgaklaa rmssggvlag glaligvgnl
      361 atalltagad yrlvalgicv tgcgagimng dtqkaiiacv prnrtgmasg istttrfsai
      421 vtavgvlgav lagsthaqlv rrlsampdvr afvdarfmss llagdltqal arlpptaarv
      481 lhdvapaafa agfstaltvs gvlalvgaav aywllvqpmr dvgv
//
LOCUS       WP_175900212             184 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175900212
VERSION     WP_175900212.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..184
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19978
     Region          42..177
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtdrlppfdp asasdeqkav laeilggprg nlngpfvgwi aspelaqhaq rlgafcryrt
       61 glplrlsela iletaarwrs qaewyihhpi aleagvpaat adairrgvkp afesdddali
      121 hafatelydt qrvsdatfar ararfghetv vnlvallgyy alvamtlntf gmradgqtdl
      181 pfse
//
LOCUS       WP_175900234             528 aa            linear   BCT 11-JAN-2025
DEFINITION  MDR family MFS transporter [Burkholderia seminalis].
ACCESSION   WP_175900234
VERSION     WP_175900234.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..528
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56474
     Region          37..516
                     /region_name="MFS_LmrB_MDR_like"
                     /note="Bacillus subtilis lincomycin resistance protein
                     (LmrB) and similar multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17503"
                     /db_xref="CDD:341046"
     Site            order(39..40,43,75,125..126,128..130,133,153,156..157,160,
                     287,290..291,294..296,299,327,331,383..384,388,392,408,
                     411..412,415..416,419)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341046"
ORIGIN      
        1 madtsatmpa pphegrasvt dwiavaagal galmatldis itnsalpqiq geigatgteg
       61 twistgylms eivmiplaaw ltrvfglrnf lltnaalfia fsmmcgwshs lpmmiagrig
      121 qgftggalip taqtiirtrl plsqlpvgmt lfglivllgp lfgpvlggwl aenvswswcf
      181 flnlpvclll mallvfglps drphwsaffn adwlgifgla iglssltvvl eegqrerwfe
      241 sqmivtlsiv slagmilial sqrfatrpiv rlslmrnpry asvivivsav gaglygvsyl
      301 lpqflaivag ynaeqagaim llsglpaflv mpilprllgk vdfrilvisg lllfclscml
      361 disltaqsvg hdfvwsqlir gvaqmlammp lnqasmaava redsgdaagl ynmarnlggs
      421 iglaiigtvi drrttyhtav lresvtansl igqdrlsaya anwfshtgdl aysnlralgq
      481 laqqiqiqav vmtysetfyl lglallacvp lalllrtprg pqpmssgh
//
LOCUS       WP_175900260             388 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia vietnamiensis].
ACCESSION   WP_175900260
VERSION     WP_175900260.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..388
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=42353
     Region          27..84
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          116..318
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(131..132,134..135,138,142,144..150,244..249,
                     255..256,258..259)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrnppakhga iadtrdagga ldlldarlmr illvlltert vsraavrlnm sqpatsaalk
       61 rlrtllgdpl lvrsrygmvp tefgaqlidp lrnalrvidf irnqqprfaa rtsvrtyrig
      121 cpdylnvlfv pklvalfrer apdaqlvfhp lgdgfdaqra ladgaldvvi dnrpahpsrl
      181 rhdalfddri vcvmrathpl arrgamtaee faqapqlcpt pswleasgai drqlervglr
      241 rrivvtlphf elaahalvrs dlvltttyrl ashyakllpl gtvalpaqpp dityrpawde
      301 tgacadavrw lrgliveatr awldaeaalp avtavaarvp tstaaplaga aaesarrgrr
      361 qqptqcdatp qpsaaratra hriamkar
//
LOCUS       WP_175900266             341 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-binding protein [Burkholderia vietnamiensis].
ACCESSION   WP_175900266
VERSION     WP_175900266.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 341)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10025428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..341
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36908
     Region          14..161
                     /region_name="AAA"
                     /note="The AAA+ (ATPases Associated with a wide variety of
                     cellular Activities) superfamily represents an ancient
                     group of ATPases belonging to the ASCE (for additional
                     strand, catalytic E) division of the P-loop NTPase fold.
                     The ASCE division also includes ABC; cd00009"
                     /db_xref="CDD:99707"
     Site            26..33
                     /site_type="other"
                     /note="Walker A motif"
                     /db_xref="CDD:99707"
     Site            order(27..34,96,134)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:99707"
     Site            92..97
                     /site_type="other"
                     /note="Walker B motif"
                     /db_xref="CDD:99707"
     Site            152
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:99707"
ORIGIN      
        1 mklspaqlie llgiyipqrf pvlisgrpgi gksdiveaaa aatdhellis hpvvedptds
       61 kglpfpsadg erarflpfgd leralntrrp llwflddlgq stpavqaakm qlllarrige
      121 hklpdhvtfv aatnrrgdna gvtgildpvi srfaavvele ptindwtawa vnhgvppeli
      181 aflrfrpdll svvktnrdie aspsprswgf vakvllsvpa hllthavsga vgegaaaefv
      241 sflgifralp svdaivmnpd lgpipeepsv lyalttalac haddgnferv lryaerlvda
      301 qhrefvavlv rdavlrkpel qshnafiraq ggeigkilrg d
//
LOCUS       WP_175900305             359 aa            linear   BCT 11-JAN-2025
DEFINITION  C40 family peptidase [Burkholderia vietnamiensis].
ACCESSION   WP_175900305
VERSION     WP_175900305.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..359
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36811
     Region          <6..175
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mlriwvpvav vsllaacssv ppqsasrsag mkittprafp apanfpnfvd hsvgqeeisi
       61 qamslvgvpy rwggntptsg fdcsglvryv lgraadvnlp rttadmssrg asidpdqiap
      121 gdliffnttg rphshvgiyv gklrfvnaps tggtvrldyl tnpywakrfd girrvapprg
      181 tptpfdapiy darrdapaaa tapvvaaaav rrpayasspa rataqaavpa vstttavtta
      241 aaaaaspapy epaprmsapv ssaggdtmam tpvlppagps eevgtqiptt altaaqaaaf
      301 daeppsampa psspgsaepv qvqvqvqvqv lrastqsapv sprtstaddp iarfangsy
//
LOCUS       WP_175900311             236 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175900311
VERSION     WP_175900311.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..236
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=24326
     Region          25..216
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          66..98
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          101..130
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(102,106..107,110..112,114..115,119,122,132,136..137,
                     140..142,144..145,149,152,161,163,165,169..170,173..175,
                     177..178,182,185,194)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          131..161
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          163..194
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mtksttylpk ralaaavlaa sglmaaagah aesldaivka ikfddiadig kqlkagkldp
       61 ntlapngdpl lviaareksd kvaaalaatp nvdlekedka genalmlasl ngdaglvkll
      121 idkgaevskk gwaplhyaat nghddvvkil ldhdayidta spngttplmm aargnhastv
      181 nllldqgadp qvknqlgita lefakhynap daieilskrt vrvgasapad aqksak
//
LOCUS       WP_175900318             444 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia seminalis].
ACCESSION   WP_175900318
VERSION     WP_175900318.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..444
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=47963
     Region          14..426
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mhriiivggg agglelatrl gdrygargnr paralvtlvd rnpthiwkpl lhevaagsmd
       61 pftqeleyaa qarwhgfefq qgeltgldra akrvtlspln dsdgaellpa releydtlvi
      121 aigstthffg vqgapenaia ldtvgeaerf rkrliaacmr aehqapapta pgdaaepriq
      181 vvivgggatg velsaelrnt aqvlsvyglh kldprhdvgi vliesgpril palqervsta
      241 taelleklgv rlmlgervte vapgfvhtas gkavradltv waagikapsv lshldglqvn
      301 klgqldvrrt lqtftddnvf algdcaacvw pgnernvppr aqaahqqasf llkaigcrle
      361 grplpeftyk dfgslvslgh fsavgnlmgg liggnmlieg lfarfmymsl yrlhiaalhg
      421 yprmildtva hwlrrttlpr vklh
//
LOCUS       WP_175900338             298 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175900338
VERSION     WP_175900338.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..298
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32061
     Region          27..>204
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mndmtelvag nrevirsvat grpdaymipl givriregfn darkadpdyp ahvreiadsm
       61 kangwlrhkp lvgvitpegl avpsdghsry eaallanseg agieqipfmp ehkgtneddr
      121 ifglilnnng krltpmgeai vikqligrgi aekeiarrlg ysittvqkal tliaaptpir
      181 dmvlagevsa ttaikaikeh gaqavgqlqe aketaaaagk tritgkhlge pkpkkphvdt
      241 vrldflietg arvekvsdep qyavvdkngn ptfqagnprn aidaaieytn qsnkdate
//
LOCUS       WP_175900379             476 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FAD-binding oxidoreductase [Burkholderia].
ACCESSION   WP_175900379
VERSION     WP_175900379.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..476
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49667
     Region          21..476
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mqnrnttaag gepagtplsg daleavlvae lgdalvtraa didpryftay nepagarpra
       61 lvrprsvddv srtlalcarl gqtvvpqggl tglargaval ggevvlsmer fagvealdaa
      121 agtmtvragt plqtvqeaae aagftfgvdl gargscqigg mlatnaggtr airygmmreq
      181 vlgleavlad gtvvssmnrm lknnagydlk qlfigsegtl gvvtravlrl hpllaapata
      241 lcrvrdydav ialwnrvrtl pevvsfeamw pafydyvarr tpgvsapfvg ddgfavliec
      301 atsaprgdah qaletglaag ieaglvedav latserqard lwtlreglai dalphlvnfd
      361 vslptgelgv faerceaalr mqwpdavclf fghvgdgnvh igvslagmsd adadaldhcv
      421 yavvrdmggs vsaehgigvl krpylahtrs daeiglmrrl kaaldpggil npgkvl
//
LOCUS       WP_175900345             232 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Burkholderia seminalis].
ACCESSION   WP_175900345
VERSION     WP_175900345.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17575897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..232
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=24402
     Region          1..149
                     /region_name="PgpB"
                     /note="Membrane-associated phospholipid phosphatase [Lipid
                     transport and metabolism]; COG0671"
                     /db_xref="CDD:440435"
     Region          <78..148
                     /region_name="PAP2_like"
                     /note="PAP2_like proteins, a super-family of histidine
                     phosphatases and vanadium haloperoxidases, includes type 2
                     phosphatidic acid phosphatase or lipid phosphate
                     phosphatase (LPP), Glucose-6-phosphatase,
                     Phosphatidylglycerophosphatase B and bacterial acid...;
                     cd01610"
                     /db_xref="CDD:238813"
ORIGIN      
        1 mfdlsshlwi mitafggagl tlplaitiav wlglgyswrr aaawlgvlga aigvvaltki
       61 aflgwgigir awdftgfsgh amlstsvypv aiflalirtr tpvrmagial glaagvavgv
      121 srvaldahsp sesitgcivg aiaalafiag swravphrws vpavvaslai vtvalhgitv
      181 pshrwvtkva lqlsgherpf vrarwkanpn yhpasqpssl qrtesstral rt
//
LOCUS       WP_175900383             493 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54 dependent transcriptional regulator [Burkholderia
            seminalis].
ACCESSION   WP_175900383
VERSION     WP_175900383.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..493
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=52855
     Region          18..139
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <157..464
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mvarspdang qaapemtdva vtapeagrkl faimrtpdep llaqlrglgw evavaktaga
       61 aqnmtsgvsv aaglvdftgf tsrdypalka clsqpaigwi siaqagvtig pavrelirsy
      121 cfdyvtlplp yewishvlgh argmaaldrv dgaayaasig ehgmigncea mqqlfstirk
      181 vaktdasvfi sgesgtgkel talaihersg rgkgpfvain cgaiphhllq selfgyerga
      241 ftganqrrag riesanggtl fldeigdmpv esqasllrfl qegkierlgg qesiavdvri
      301 isathvdldg aveagrfrad lyhrlcvlri hepplrargk didilahyvl qkfksdsgrk
      361 isgftsaald amrryewpgn vrelinrvrr aivmaesrll tphdlgldap getepvtleq
      421 aralaertai enallrndhr inkaaaelgi srvtlyrmmi ehglndhdnh ggngdngghd
      481 gapsgdaghq rvg
//
LOCUS       WP_175900464             133 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Burkholderia seminalis].
ACCESSION   WP_175900464
VERSION     WP_175900464.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..133
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=14586
     Region          16..133
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mslihaaavl dadapdyvvq lqagthaltg deapreggqd rgpapyefvl aglaqctaat
       61 lrmymqrktw pavriavrte lhtdrdgvqy vrrvvtldgp lddaqrqrla eicektpvtq
      121 fikrgtriet tln
//
LOCUS       WP_175900513             306 aa            linear   BCT 11-JAN-2025
DEFINITION  bestrophin family protein [Burkholderia cepacia].
ACCESSION   WP_175900513
VERSION     WP_175900513.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..306
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33933
     Region          1..299
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 mivrprqnwl rmlfvwngsv lqsiipqlvf maivstlavf tngrifgeki plntapftlf
       61 glalaiflaf rnnasferfk earhlwgnll iaaraltsql nrylpdsvdd ternrladll
      121 iaftyalkhq lrhtdptqdl qrilgaerta alagkcfkpv aildelrgsi vralgrapgs
      181 datcwmfeaq ldelgksvgg cerilstpip fsysvllhrt vyaycvllpf glvdstefft
      241 plicvfiayt lialeaiane vaepfglapn alaldamart iersvlelgd rplpeefvpa
      301 styqit
//
LOCUS       WP_175900523             828 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175900523
VERSION     WP_175900523.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 828)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 828)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..828
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87731
     Region          510..796
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mrhfllgwll aavvsiahaa apasapaaas aasgavpalt pqqaqqalsv lqnprereqv
       61 ettlraiaav gvlstpalpa saaapasaas aaapaalttn glasmlvrqg shwageigga
      121 lneslrslld vasvgnwwhe rlvraderad llhalltiva vlvpalgaew larrllrrtl
      181 ralgarraes srradaapse teppestelp esiapaastp laagtpsass vsstsatpet
      241 qsrgharrht tllhrmpral vslvvravpl lvfagvaslt msvldgdgtp tdtalgslid
      301 iyvicrlvti vsrlffqpda rqlrllhisd awaayaqrai ariaivvgic taaielaasf
      361 glseaghval lkavalvghl misalilrcr qpvaarirat gdehrafamf shaladawap
      421 vavfavmalw fmwaldvhng yrvlialggr siavmigmri vsivvfgala rlfqrrdddr
      481 tlvhlhayry ypllrrivst viaivtvvll lqiwgvpifh afktgtighr lasalmtiai
      541 aalvalfvwe aaniaierrl qqwtregnlv raarlrtllp mlrslllimi alvvvltgls
      601 qigvnigpll agasifgval gfgsqklvqd fitgifllme namqvgdwvt lagvsgtvey
      661 lsirtvrlrg gdgslytipf ssvttvnntn rglgnaavkv siaygqdidp aiatlkeiga
      721 alrddpnykd gilsdfsywg vdqvdgatvt lagqiqckds arwgvqrefn rriavlfrer
      781 girianpqrs vvaydagaqh ggaegaegpd taaapsaavn ppprpapq
//
LOCUS       WP_175900535             259 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Burkholderia seminalis].
ACCESSION   WP_175900535
VERSION     WP_175900535.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..259
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=28855
     Region          2..220
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mnvlivyahp eprslngalr dfavghleaa ghavqvsdly amnwkavfda ndvtdrapga
       61 rfdpsldskr afeagtqsdd iareqeklkw adavilqfpl wwfsmpaimk gwfervyayg
      121 laygvgehsd thwgdrygeg rmagkramvv vttggweshy sprgingpid dvlfpiqhgv
      181 lyypgfdvlp pfviyrtgkm ndarfdetra algrrlddlw ttppipfrrq nagdyeipal
      241 tlkdeiapgq egfavhlaa
//
LOCUS       WP_175900564             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia vietnamiensis].
ACCESSION   WP_175900564
VERSION     WP_175900564.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45735
     Region          21..426
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(34..35,38..39,42,81,139..140,142..144,147,167,
                     170..171,174,257,260..261,264..266,269,297,301,353..354,
                     358,362,378,381..382,385..386,389)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msafppavar atgsagavsh rrivfasfig taiefydfyv yataaalvig pmffphgsat
       61 aqalsafvtf giafiarpig sflfghfgdr igrkstlvas llvmgistta igfvpgydti
      121 gtlapvllcv lrfgqgiglg gewggaalla tehappgkrg wfgmfpqlgp svgflmsngl
      181 ffalalslsd eqfrswgwri pflvsavlva vglyvrlkia etpafqaale rdervrvpva
      241 tlisqhwqpt llgalamvvc ytlfyistvf slsygvsalh iprqsflgll cfavvfmgla
      301 tplsawaadr fgrkpvlaag aiaallsgfa mepllgsgsm plvalfltle lflmgvtfap
      361 mgallpelfp tnvrytgagv aynlggilga siapyiaqll aargglswvg gyvsvaaals
      421 ligvllmret rdaslv
//
LOCUS       WP_175900581             416 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175900581
VERSION     WP_175900581.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..416
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=45632
     Region          8..>119
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mnrqqswtrt aapgeiiyse gfagepvifl itdgkvelst rcddkrviva tlgrgeffge
       61 sallaaepra htakalsfcq ltvvpagmld deiervsall rhivrtmirr vkrkddqlat
      121 ythadfmpgv lsyahvlslm agadtrdagd twarrpmqah aaeasvplae virkcraiag
      181 hsrphvlaml rrmeklnlvt ieaaqsdgag gaadyaassd arqvvtfdaa riidraqqva
      241 dhdldlsins elelieladl esligvdktl llnklsngei adevfafrks kvlsyveqkg
      301 vayfsrrnar rggdvraled lvwvdqrtlf dvisafdtyd laklianldd ravadklfsv
      361 mtearrnevs wvmrreikld pieveeieqr vldavraaka paasvapvas tsssda
//
LOCUS       WP_175900589             144 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia seminalis].
ACCESSION   WP_175900589
VERSION     WP_175900589.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..144
                     /product="cupin domain-containing protein"
                     /calculated_mol_wt=15547
     Region          23..126
                     /region_name="cupin_bxe_c0505"
                     /note="uncharacterized protein bxe_c0505, cupin domain;
                     cd06980"
                     /db_xref="CDD:380385"
     Site            order(28..34,43,45,47,49,67,69,71,73,91,93,95,112,114,116)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380385"
ORIGIN      
        1 mseqtttafs hvkpqdtayq geglrdffly rdlgiaaatn gkvvaqlvra nhapaagtgw
       61 hrheaefhiv imlkgwarfm ygeqetlvaa gdcvhqapgi vhylfdyspd meyleivgpa
      121 dfksidvdgp cavpaptpwg daga
//
LOCUS       WP_175900608             877 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175900608
VERSION     WP_175900608.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 877)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 877)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 877)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 877)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..877
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..877
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=92708
     Region          53..860
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mekkysgpha eiaprikpic alvfsivasw qtdalavade harpqqiaqm efaqvefegg
       61 flnngagsid vsrysrgnvv ragtyspdvy vsgrwagrfe vpfksvadsp daqpcfdkal
      121 lerigvelta lsqeirtlle qqggcvrigq aipeatvgfd fndlrldlgi pqvslsrtar
      181 gyvspdrwsa gvpvamlgyn anvyhaqasg ahgstqgyvg vdsgfnvqrw hfrhsgsfnw
      241 ddrgrrryqn vatyvqrdla swssqfvagd tytsgdlfds tsfrgvriss ddrmlpdsqr
      301 gyapvvrgva ntnakvtisq ngvklyettv apggfviddl yptgyggdln vvvteadgst
      361 htfsvpyaav pmslrpgqnr ysftagavrn lsnttplftq atwqhgftnm ltgyggataa
      421 qgylaamvga vlntgwgaig vdvahattrv qndrtysgqs frvsyaktva atgtnvaiaa
      481 yhystngyfg lndamtardr sasggplrqv yrqrnraslv asqqlgdkgg slsvtastst
      541 ywnragsdvd ftvgysnafr svaynvsatr qrdawgqtst lvylglsipl gstrpatlst
      601 sfnhdtrgst qiatslsgsa gvdsnvsygv nvnrssgpgg aqtsgganvs yrgaraelsa
      661 svgasadyqq ysigargavv ahrggvtlsq plsetfaive akhaegarvt nasgvrvdan
      721 gyaivpyltp fsmndvsldp kglstdvelk etsqrvapla gavpllvfkt dygrsavirl
      781 rqadgspvpf gavvtdqagk digvvgqagk llarglaeqg elnvgwesda grsgcrlsya
      841 lpanprgagq ralrsldlpc vaagaeqyap teaqpaa
//
LOCUS       WP_175900640             349 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175900640
VERSION     WP_175900640.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..349
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37070
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..294
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(103,107,146,160,162,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(104..105,109..110,112..113,116,120,122..128,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdnpiramri ftrivemnsf traaqalgis ratatrtvqe leaalgtpll vrttralrtt
       61 segdayyrrc vsitadvdel easmrgaarh pggplrvevp asvagaivlp aldafharhp
      121 dlvlmlgvag ragdrdadav dcgirlgalp dsslvarrlg tlervtcasp ayldrfgvpr
      181 tfdaltthra vggarvpgqr saeldfvadd gvrkvrldsi vsvddeqayl acgvhglgli
      241 qptriaaqpl idagrlrevl pcwqpepvav savyvkrphv spgvrafvdw iaerfvqaah
      301 eheglaaaga agwrareaav trepvassvr aapattridl ehvalvaas
//
LOCUS       WP_175900665             222 aa            linear   BCT 11-JAN-2025
DEFINITION  O-methyltransferase [Burkholderia seminalis].
ACCESSION   WP_175900665
VERSION     WP_175900665.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..222
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23033
     Region          43..220
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mdqdrwnqvd ayfsatlvps ddaldaalaa sdaaglpain vapnqgkllq llatirgarr
       61 ilevgtlggy stiwlaralp pggtlvtlel npahakvatq niaragfasv vsvmvgsakd
      121 slarlvdage apfdfvfida dkdnnavyld aalklsrpgt vivvdnvvrg grvadpdnre
      181 pdvigvrdgf arlvaepalm ttavqtvgqk gwdgfsisiv ga
//
LOCUS       WP_175900671             270 aa            linear   BCT 11-JAN-2025
DEFINITION  creatininase family protein [Burkholderia cepacia].
ACCESSION   WP_175900671
VERSION     WP_175900671.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Yoshimoto,T., Tanaka,N., Kanada,N., Inoue,T., Nakajima,Y.,
            Haratake,M., Nakamura,K.T., Xu,Y. and Ito,K.
  TITLE     Crystal structures of creatininase reveal the substrate binding
            site and provide an insight into the catalytic mechanism
  JOURNAL   J Mol Biol 337 (2), 399-416 (2004)
   PUBMED   15003455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..270
                     /product="creatininase family protein"
                     /EC_number="3.5.2.10"
                     /calculated_mol_wt=28348
     Region          29..265
                     /region_name="ArfB"
                     /note="Creatinine amidohydrolase/Fe(II)-dependent FAPy
                     formamide hydrolase (riboflavin and F420 biosynthesis)
                     [Coenzyme transport and metabolism]; COG1402"
                     /db_xref="CDD:441012"
ORIGIN      
        1 mkclpraafa alaftvaqaa faqapatvrl edmtwtelrd siragkttil ipvgateqsg
       61 pyialgkhna rvavlseria qglgnaivap viayvpeggy apptshmrfp gtitvpddvf
      121 ektlesaans frvhgftniv flgdhggyqn dirqsvarln kswagtgara fvpaeyygts
      181 sdgydrilre havpaadigt hagladtsll lavapgmvrv dklrnaakpg aadgvyggdp
      241 rhasvelgrl gtdaivsrtv dairkdtagr
//
LOCUS       WP_175900711             627 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia cepacia].
ACCESSION   WP_175900711
VERSION     WP_175900711.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..627
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=67529
     Region          12..543
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mlratasaaa adlivcngki atqddrqsfv talavkdgri laagsghdvm rhahagtqci
       61 dlngrtvipg lndshlhmir gglnfnlelr wdgvptlada lamlrrqvlr tpaphwvrvv
      121 ggwtefqfae krgptaaeln eiapdtpvfi mhlgdsalln aaalraigyg rdtsnppgge
      181 iqrdrlgrpt glliarpdma vlhealerap klghddqmns mrhfmrelnr lgvtsaidag
      241 gdfqafpddy gailalarrg emtvrvaysl fvqhagreld dyarwvtlak pgdgdaflrm
      301 ngagellvys aadfgnflep rpdlpaalea elaavvrllv rhrwpfrlha tydesigrfl
      361 nvleavnret pfdglrwffd hcetitdtni ariaalgggv tvqhrmafqg eyfiarygaq
      421 aamrtppira mlaaglpvga gtdatriasy npfvslywmv sgrtvggtal ypernrlgrm
      481 ealrcytvgs awfsgeddck galvpghyad favltddyft idearitsls svltvvggri
      541 vhaddefasl appppavspa wspvaefgga grrrsaesas lraasgaglp aagaarglgr
      601 afvqrlhaaa metaeqceas gypgfay
//
LOCUS       WP_175900751             212 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia seminalis].
ACCESSION   WP_175900751
VERSION     WP_175900751.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..212
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22478
     Region          5..205
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtasaavlai latlflgami pgpsfvlvar nsiglsrrdg latalgmgig givfggvala
       61 glytllqave wlyvglkvag gayliymask iwrgadrpia mddpqamagg sarksfltgl
      121 ttqlsnpkta iwygsifaal lpqhpplwcy lvlpplvfav efgwytlval cfstrrprel
      181 ylrakkwvdr iaagaitllg lrlilnapka gi
//
LOCUS       WP_175900760             258 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia vietnamiensis].
ACCESSION   WP_175900760
VERSION     WP_175900760.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 258)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 258)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..258
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28959
     Region          4..258
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mkefvsaakl wrvwlhmglq diksrfrssa lgpgwilvnl aavvgavgli ygrlfhqpmn
       61 eflpfltlgv viwtfitssl vegamafvva egyikqfpfp kpiylyralv pyavvfsigl
      121 ivyfivvafy hrhvgwgalw vipglvlfla inffhvviva hvgvrfrdlp hllgslmqia
      181 fyltpviftv gmlrdrglsf vyafnplyyl ieilryplln saaappevly valgycvvvg
      241 ilamvvvkkm skrivyvl
//
LOCUS       WP_175900827             358 aa            linear   BCT 11-JAN-2025
DEFINITION  M48 family metallopeptidase [Burkholderia cepacia].
ACCESSION   WP_175900827
VERSION     WP_175900827.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Lew,R.A.
  TITLE     The zinc metallopeptidase family: new faces, new functions
  JOURNAL   Protein Pept Lett 11 (5), 407-414 (2004)
   PUBMED   15544561
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..358
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37704
     Region          139..322
                     /region_name="M48C_Oma1_like"
                     /note="Peptidase M48C, integral membrane endopeptidase;
                     cd07331"
                     /db_xref="CDD:320690"
     Site            order(205..206,209,262,266,306)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320690"
     Site            order(205,209,262,306)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320690"
ORIGIN      
        1 mrsdrlhrla rvaaslsvga aalaagfaah asdtgataat aagsapaaap asppatstsa
       61 apaqpataep aqptgaaast kaytptpqqv rygnaiafrt lipsplleql taseytqivq
      121 aaadsnrllp anqprvkrlr aivtklapys vkwndrvknw awdvnvirsr dirltclpgg
      181 kvlvygglle rlrlnddelg vlaahgiaha lreharsnfs aasqtslraa alpplfgvgd
      241 plpqalnlge rlqslhydpt deteadvigg diaaragfdp raaitlwdkl aaatrankat
      301 gfiythpyst arrqdllnrl pdlmplyaka igkrvdslpd yagisaqrrk vvrrgatg
//
LOCUS       WP_175900799             264 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia seminalis].
ACCESSION   WP_175900799
VERSION     WP_175900799.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..264
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28343
     Region          1..253
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mrkngpvala fhtlvilfvl aplvivvlva ftpdetltlp trglslrwfr aildypdfvt
       61 aflnsvklaf asatlslaia lpaglaigra tfpgraflng lllsplvipg lvlgiallrf
      121 faligatgsf awlvlahmiv itpfvmrlvl asvagldrsi eqaacslgad pwttfrritl
      181 pmivpgitgg wllafinsfd eltmsifvts pqtvtlpvrm ymyatesidp mmasvsalvi
      241 fitagamlll drvyglnril igqh
//
LOCUS       WP_175900815             445 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia seminalis].
ACCESSION   WP_175900815
VERSION     WP_175900815.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..445
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47265
     Region          22..426
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(35..36,39..40,43,83,141..142,144..146,149,169,
                     172..173,176,258,261..262,265..267,270,297,301,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 myptdtvqsp saarpladrq lrriviasva gnamewydff vygtaaalvf ghvffppgas
       61 plagslaafa afalgfvarp lggivfghvg drygrkaslv wtllimgast faigllptya
      121 qiglwapaal vvlrllqgia sggewgggvl misenappeq rgyyaawsql gvgggfvlss
      181 aaflaaqtlp ddlfrtwgwr lpflasivif aigvyirrhl pesrdfeqag krgarthlpi
      241 vecirrhpke illamglrva enggayifla fslvygkyvg ipngvmltgv miamivemga
      301 mlawgrlsdr igrkpvylig alslvacafp ffwlldtrvt plvwlaltvg tavshgamig
      361 tlpalvgelf stevrysgva lghevasifa ggmspliata llaryhaswp vslflvalgl
      421 vtvatlcamr etraphadgs rgnaa
//
LOCUS       WP_175900832             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175900832
VERSION     WP_175900832.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34073
     Region          9..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          99..299
                     /region_name="PBP2_DntR_NahR_LinR_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators that are involved in
                     the catabolism of dinitrotoluene, naphthalene and
                     gamma-hexachlorohexane; contains the type 2 periplasmic
                     binding fold; cd08459"
                     /db_xref="CDD:176148"
     Site            order(105,107..108,112,170,208,275)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176148"
     Site            order(106,109..110,113..114,117..118,120..121,124..125,
                     127..131,133,197,225..229,232..233,236..237,240,254)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 mtsvdhldln llrvfqaive ersltkager lalsqpavsy slgrlrtlfd dplfvrtrsg
       61 mqptpvalel agivgkaldm vrvalryaer fdpatstrtf rlslsdagem aylpaicqal
      121 reraprvtls vqplpveeie ealrasrldf aignlpelmp rtrhqvlfee tyvcmtgrrr
      181 glpagaalgl epfvraahvn vksvehshha lddalraqgv grnialevph fvalpsvlsv
      241 tdlyatlprr laqilnrdna frlydlpvtl ppapvtmhwh ehfhedegna wmrallaeiv
      301 erfdda
//
LOCUS       WP_175900763             285 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia
            seminalis].
ACCESSION   WP_175900763
VERSION     WP_175900763.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..285
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31284
     Region          9..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(32,57)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(39..40,51,54,58..59)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          105..270
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 madapdnllg aylrdrrekl dpaalglpat rrrtpglrre evaqrahvsa awytwleqgr
       61 ggapsadvld rlaralmlne aerehlflig vghppevryh apasvtprlq hvldsldasp
      121 aivrsatwdv vawndaaaat ltdyatlppa arnilrlifv dtvvrhaqpn wervarfavg
      181 afradvargg atqavqafvd emratsaefd amwrdhdiht hdegtkeirh pqagrialey
      241 safsvtgrpd lslviftpvt padrarirel vaareraral pvsaa
//
LOCUS       WP_175900860             178 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia vietnamiensis].
ACCESSION   WP_175900860
VERSION     WP_175900860.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..178
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=19230
     Region          16..168
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mskmsdtimr hgkaqrialt lngrersgyc eprellsdfi rhelgatgth vgcehgvcga
       61 ctvqvdgvaa rsclmlavqa dgrhidtveg lapeqtlgdl qqafqrhhal qcgfctagil
      121 mscadylrrv pdpseeqvre mlsghicrct gytpivaavl dvaarrraea stkeveha
//
LOCUS       WP_175900888             572 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia seminalis].
ACCESSION   WP_175900888
VERSION     WP_175900888.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..572
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=62390
     Region          22..534
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 msktfdyivv gggsggcvva grltedpavt vcvleaggrg dgalvnvptg avammstrln
       61 nwafdtvpqp glggrigyqp rgralggssa inamvyirgh rvdydgwaal gnegwgyddv
      121 lpyfrlsehn erfddawhgr dgplwvsdlr tgnpfharyl eaarqaglpl tddfngarqe
      181 gigiyqvtqk hgerwsaara yllphlgrrd nltvethaqv lrilfdgtra igvevrqhge
      241 vrtlrarrev vlaagalqtp qllmlsgvgp gralqqfgia vqadlpgvgr nlqdhpdfif
      301 gyrtrsvdtm gvsargglrm lrefarfrre rrgmltsnfa egggflktrt dlaapdiqlh
      361 fvvalvddha rklhaghgls chvcllrprs rgsvtlnsad plaapridpa ffddprdvdd
      421 mvagfritrr lmeapalasw itrdlftanv ttddeirdvl rrrtdtvyhp vgtcrmghda
      481 lavvdpqlrv rglqglrivd asvmptligg ntnaptimia ekavdlmrgv rrvpdrphag
      541 etvrtatdcd saraaraahd viqpeetrha va
//
LOCUS       WP_175900910             579 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia vietnamiensis].
ACCESSION   WP_175900910
VERSION     WP_175900910.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..579
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=62293
     Region          1..564
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mkrfdyvivg ggsagcvlah rlsalpslrv alieagadtp pgavpeaild sypmpvfcgd
       61 tyiwpdlkak atkdaasrvy eqgrvmgggs svnvqsanrg lprdyddwaa tgadgwawrd
      121 vlpyfrkler dldfpsgelh ggdgpvpirr impkdwpafc hafakglraq gvaelqdqng
      181 efgngffpga fsnedekrvs taiayldeat rkrpnltvys klrveqilme gaaargviav
      241 aengervrfd agevvlsaga lqspalllra gigdarelaa lgiacavdlp gvgrnlqdhp
      301 sltfchflep rfrmpltrrr asmmaarlss gvagcdesdl ylssatraaw helgnrlglf
      361 flwcnrpysr grvqlvcada aaaprvdlnl ldderdlqrl aagvrmlari veasglgrdg
      421 rdffpaafsp rvkalsrvge gnalltsalg alldtpapmr rllierfftr glkmdallad
      481 draladfira nvfgvwhasg tcrmggandr davtdtegrv rgtqglrvvd aslmpklpsa
      541 ntniptimia ekiadvmvaa rragvdrsvs grpplaaah
//
LOCUS       WP_175900925             603 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia seminalis].
ACCESSION   WP_175900925
VERSION     WP_175900925.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 603)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12379621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..603
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62791
     Region          1..284
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
     Region          329..603
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 maswldytln glivgniyal lavglalifg vshlinfahg svymvgafig wlcltrfglp
       61 lpvalaavvv gcgalgiaie riglrplrha ariapllati gisfildqla qlafgadpra
      121 vptplpdwhv riagatlgsl dlliagigia aaallygflr ftrlgwavra taqdrdaalq
      181 mgvdvdrvnq tvfaiacalg gvsgllvgmy ynsidpamgf qatlkgvval ligglgnvpg
      241 aiagslllgl vesygvalfg tsyrdlfafg llivflvwrp nglfsanral ppepmtgtfl
      301 aaakavrvpr pvlvaliala avlpwlgasp yvlqtltnaw lygllalslt lvagtvgqis
      361 lghaallvig ayasallssd lgwspavtip cagvitavlg tllvypafrl rghyvsiatl
      421 gigevvslvi lnwdgltrgp lgitgiaplp wastaraayw ftfavlvafa lvqvrllrsh
      481 lgrtlravre ddvaarahgi apnrykaiaf avggvaagvs ggiaahlysy inhqtfdsqv
      541 silaltmvil gglgnvlggi agaialiglp elfrwaadyr mliyglvlll lvrfrpqgll
      601 gtv
//
LOCUS       WP_175900941             499 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Burkholderia cepacia].
ACCESSION   WP_175900941
VERSION     WP_175900941.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..499
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=56724
     Region          2..402
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mstehqqyst enqldvirvf aetrdlevvr vyadegksgl rldgrdslka llrdaesgsa
       61 dfsvvlvydv srwgrfqdpd esasyeirck hagvkvlyca eqfendgspv ssiiksvkrt
      121 mageysrels vkvhagqsrl ircgnrqggp agyglrrmlv dhareikgtl ergqqksiqt
      181 drvilspgpa eevdtvrgiy safvedgrte teiaaslnae glrtdrgtlw trgtvhqili
      241 nekyvghnvw nrtsfklkqq rvknppeqwv radnafkpiv spllfeaarq iimarsyrms
      301 daemlerlrq lllkngylsg ivideavgcp sssaymhrfg sllrtydlig ylpsrdyryv
      361 einrqlrrlh pqivaqaiha mteagadvvr dersdllwvn defrislvls rcrptaigsn
      421 rwvirfdnal lpditvaarm efdaksirdy fllpavelrv nmvrlqdynd fgfeayrfdd
      481 ldvlcqlgrr aplkgveye
//
LOCUS       WP_175900864             374 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Burkholderia seminalis].
ACCESSION   WP_175900864
VERSION     WP_175900864.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..374
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37393
     Region          17..364
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mtgfidtftl ggpgptiaik dtidiaghpt raasralada ppaahhadvv rllldagwri
       61 agkanmhela fgmtgindyt gtpvnpqdat ripggsssgs aslvglgavd aalgtdtggs
      121 irgpaaccgv aglkptfgrv srrgvapadt tldcvgpfar dirtlaavma aiapgfdraq
      181 aaasvagrtv ahvtveadpa iaaaldaavr aaglpshavv lddmpasfaa gltvinaets
      241 rafghlvatg rlgadldarl rmaatttpaa laeaetvrar ftaqvdaale hadvlvlptl
      301 palpitlqqa rdgvsviams slirpfnlsg hpalslplpl agsplkaglq ivgrkgadeq
      361 vcaiaahfea alaa
//
LOCUS       WP_175900964             529 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxylesterase/lipase family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175900964
VERSION     WP_175900964.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..529
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=57563
     Region          13..515
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mneqthisei dhrhagsdcv ltlahgrlrg srshgvarfl gipygmpatg srrfappvap
       61 lawdgtrdcr aygdacpqvn ddlpawrfdg dhsanclnln vwtpaaampg drlpvmvwlh
      121 ggaylsgsan lplydgrtla deqqvvvvsi nhrlnafgyl ylsdrdehga qaanvgqqdi
      181 vlalewiaan iaafggdagn vtlfgesggg gkicaltmmp sadglfhkai iqsgtfvtml
      241 sraqarertd allsllgada rslaaiddar llgaarrlid rygytafwpv ddgnvvdasr
      301 rraasvpmli gttrheaayf lppqllarsp ldstdyrdal eegmrplcig addvraaaat
      361 aarlhalgpr slgrdltdvm frmpalalae rnaehadtfv yrfdwafpcc ggryaihgae
      421 ipfvfgtldy alpawdsadl prdryrddph gdrfrlaarv rrawagfarc gdpsagdasi
      481 wrrytrdqpa trifdrvcri esdpdgprrh alfaadsnaf ssstlidke
//
LOCUS       WP_175900965             240 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD family hydrolase [Burkholderia seminalis].
ACCESSION   WP_175900965
VERSION     WP_175900965.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..240
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26153
     Region          6..233
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mrlakvsals fdlddtlwpf gpsvvraeam lrawliehap gtasvlpthq alselreeye
       61 rlrpdlagdf ramrigsirl alaranedva ltdaaydvfy aarnrvefyd dalpalawls
      121 arfpliavtn gnadlrltgg geffrttlsa rafgfakpep eifhaaadal dvrpaellhv
      181 gddfhldvvg alnaglqaaw vvrdprpeed htprqaatph ltlrdlsmlc ralggpddgs
//
LOCUS       WP_175900989             299 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175900989
VERSION     WP_175900989.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..299
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32709
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..296
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(103,107,146,160,164,231,248,275)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(104..105,109..110,112..113,116,120,122..128,191,
                     222..225,229,236..237,240)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mqtdlgdlna fmavaraggf rdaarmtgls asglseavrr learlgvrll hrttrsvvpt
       61 eagerllarl gpaltevaaa lddidefrdr pagtlklnvp vsasrlvlpa ivprfldayp
      121 dirleviade sfvdvlaagc dagiryderl eqdmiavpig priqrfataa apgyldrhgr
      181 prhprdlldh kclrgrfasg amlpweferd gevvrvepaa gpllvqigga sellvdaala
      241 gtgilhlfee wvrphfdsga lervlepwwr pfpgpflyyp grrlvppalr afidfikas
//
LOCUS       WP_175901026             652 aa            linear   BCT 11-JAN-2025
DEFINITION  arylsulfatase [Burkholderia seminalis].
ACCESSION   WP_175901026
VERSION     WP_175901026.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..652
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..652
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=69796
     Region          50..618
                     /region_name="PAS_like"
                     /note="Bacterial Arylsulfatase of Pseudomonas aeruginosa
                     and related proteins; cd16025"
                     /db_xref="CDD:293749"
     Site            order(60..61,98,159,161,266,409..410,469)
                     /site_type="active"
                     /db_xref="CDD:293749"
     Site            order(60..61,98,159,161,266,410,469)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293749"
ORIGIN      
        1 mkksasplhv frfrvvcaai agavslascg gvdsdspppq anttppqaak rpnilyimad
       61 dlgysdihaf ggeintpnld alvasgrils nhhtgtvcai tramlvsgtd hhlvgegtmg
      121 vptderrglp gyegylndra lsfaqllkda gyhtyiagkw higsgivgsa tgsgqtpdqw
      181 gfersyvllg gaatnhfahe pagssnyted gryvqpgqpg qpggtggspa vfystdfytq
      241 klisyidsnq rdgkpffaya aytsphwplq vpepwlhkya gvydagydai rnariarqka
      301 lglipadfkp fdglpettaa spatanngaa nakyisavhs aadgysdygp gkvdklwssl
      361 spaerkaqar ymeiyagmve nldyniglli qhlkdigeyd ntfimfqsdn gaegwpidsg
      421 adptatdtan aqepvysalg tdngkqnaqr lqyglrwaev saapyrltkg ysaeggvstp
      481 tivrlpgqsq qlptlrafth vtdntatfla iagvtppsqp applvntltg vdqnkgkviy
      541 nnryvypvtg qsllpvltgs atgevhtapf gdeaygrayl rsadgrwkal wtepplgpld
      601 ghwqlydlas drgettdvsa qnpsvistlv dqwktymsnv ggveplrprg yy
//
LOCUS       WP_175901015             153 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175901015
VERSION     WP_175901015.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..153
                     /product="RidA family protein"
                     /calculated_mol_wt=16942
     Region          28..137
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 msqpthtrir mfntkdtypn qtldndlcqa vragntvyvr gqigtdfdgn lvglgdpraq
       61 aeqamrnvkq lleeagsdlt hivktttyli dpryrepvyr evgkwlkgvy pistglvvsa
      121 lgqpqwlmei dviavipdnw qpaqasgsvr eaq
//
LOCUS       WP_175901048             431 aa            linear   BCT 11-JAN-2025
DEFINITION  multicopper oxidase family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175901048
VERSION     WP_175901048.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..431
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=47515
     Region          64..327
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mvsrrkflsg sgaalmgaam vskagaaslp eaptmakatt qpplvppngr pytpvttlng
       61 wtlpwrmkng wkefhltaep vvremapgmk anlwgyngqs pgptieaveg dkvrifvtnk
      121 lpehttvhwh gmllpcgmdg vggltqphip pgktfvyefq lekhgtfmyh phademtqma
      181 mgmmglfivh pkdrsvmpvd rdfvfllaay didpgsytpr vnemtdfnmw tfnsrvfpgi
      241 dplpvraddr vrirfgnltm tnhpihlhgy hfevagtdgg wippaarwpe vtadvavgqm
      301 raieftanrp gdwafhchks hhtmnamghq vpnligvpqk dlakrinklv pdymamgstg
      361 gamgemempl pdntlpmmtg tgpfgplemg gmftvvkvre glgrndyrdp gwfkhpkgtv
      421 ayeytgelpd s
//
LOCUS       WP_175901130             450 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter large permease [Burkholderia vietnamiensis].
ACCESSION   WP_175901130
VERSION     WP_175901130.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..450
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47488
     Region          1..446
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 melailsvsf liflvlgvpv sfalgiacvl tylveglpia tamqsmisgm nafsflavpf
       61 fifsgelmlh ggiadrilrf aqatvghfrg glgmanvvac tlfggvsgsp tadtsamggv
      121 viplmkregy saayavnvtt haslagalmp tstnmiiyaf aaqgitgmlh gqqvsgvsig
      181 dllfsgllpv lwvmgfvlaa aywqavrhgy prredgssal pafpgwyavl rsfvgavpgl
      241 mvisiilvcv akgiatatea aaiavvyslv ltalvyrtlt veklrralsh aarttgvvll
      301 liavsnmlrf qmsyleipda iegllkqsta apwlmllyin viqvflgtfv dmaahilitt
      361 plflpiamac gvgpvqfgim lllncslglv hppigsvqfv gcaignvsig ettkmawpyy
      421 laifsainiv tympffstwl pslisghavf
//
LOCUS       WP_175900968             205 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia seminalis].
ACCESSION   WP_175900968
VERSION     WP_175900968.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..205
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23137
     Region          1..192
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mklygfagtr sqralwglke ldadfefvsv nllqgehkrp dflrlnpagk vpvlvdgnlv
       61 ipesaaivly ladkypekgl lpadpalraq ayrwvmfavt eleqplwrit rhsflyppek
      121 rspadielar ddfttmaall dkhlegrefi vgdaltvadc vtvylidwas ecrliepfpq
      181 lrayldrlya rpkapqriad arkaa
//
LOCUS       WP_175901165             343 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175901165
VERSION     WP_175901165.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..343
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37595
     Region          70..269
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 makdtskekk ptgnlhlaag llrglaqena aletrlpeps aasntavdaa laipptvttp
       61 adtpdlgapq kvavkdcipn pfnprvfyse sslhelaltl kregqiepik vtrlpefpgk
      121 lvvidgqrrl ratsingdet inatfrtdht peqlytiayr anhdherqti fddavawkrl
      181 ldekvfpdqn tlaekigkdk asisktlsln alpntllerm asandvvglq aayflklife
      241 rvgeaaadrl ltavmerkks vrdlenflrt qgdgnkktgr trysvrhdfa lesravgqlk
      301 typdgrldlq lkgvdtshqe aladqlkavi dayvaelava aqk
//
LOCUS       WP_175901192             163 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175901192
VERSION     WP_175901192.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..163
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17899
     Region          4..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 magitlddld lrilailqed asvsnlqlae ralsspptcm rrvrrlteag virrqvavld
       61 pvaigtavta lieisldrqt aedydafety vcaepavtqc yrvspgpdfv vvadladvae
      121 ydefarrlft gasnvrnvrt ffsthrakfe anarvahamr kra
//
LOCUS       WP_175901235             208 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent F420 reductase [Burkholderia cepacia].
ACCESSION   WP_175901235
VERSION     WP_175901235.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..208
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21262
     Region          18..201
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mkiaflgggn fggnlaellv aaghdvvvgl rnpararpga ryriasleea athgdvviia
       61 vlyqacaevl pslahrlagk ivvdatnalk ddwsplplga dgsaaeaigh llpgarlvkc
      121 fntvfadimt pdridrggha vtafiagndv qanttvagia esagfapivt gplnnaryle
      181 amahlniqia vgrgggtnag fvyhrala
//
LOCUS       WP_175901237             336 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175901237
VERSION     WP_175901237.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..336
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35720
     Region          9..330
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 msqstcsarn vvvvgfegvq slditgpmev favanrhlpd havpyrltla sqhgddivth
       61 aglrlagaaa lsalpgridt iivaggheaa lrhaaseagv lpwlrtriad trriasictg
      121 afvlaaggwl dgkratthwn qcsalqalcp garidpdaiy vsdppfhtsa gvtagidlcl
      181 alveadcgap talavarelv lfmhrpggqa qfsvgldiqa ratprmrsll vdiaddpagd
      241 lgvaalaarm hmsertfarn flketgvspa qyvlaarier akalleradw pleriaersg
      301 fgsvdalqra fakrvgtspr dyrarfgprr dkprte
//
LOCUS       WP_175901246             214 aa            linear   BCT 11-JAN-2025
DEFINITION  HD domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175901246
VERSION     WP_175901246.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..214
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23215
     Region          23..214
                     /region_name="RnaY"
                     /note="HD superfamily phosphodieaserase, includes HD
                     domain of RNase Y [Translation, ribosomal structure and
                     biogenesis, General function prediction only]; COG1418"
                     /db_xref="CDD:441028"
ORIGIN      
        1 mtlpafapfq dlakallahw sgadgdgshd tshlqrvwkn aaaihakegg daevlfaatl
       61 lhdcvavekd splraqasrl saqkarqvlk sldwpdakid avahaveahs fsacvapttl
      121 eakvlqdadr ldaigmvgva rcfyvagrmg salydpadph aserelddtr faidhfhtkl
      181 lrlstgfqta tgtrmaivrr drlqrfldef adei
//
LOCUS       WP_175901265             430 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia seminalis].
ACCESSION   WP_175901265
VERSION     WP_175901265.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..430
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46334
     Region          38..419
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 msfdfstprt rracrrapvl wvallaasav haqqspvtld aalqsatdhs asmqaaqasv
       61 larseaavra gqlpdpmlka gidnlpvngg qrftvgqdfm tmrrigieqe wvsgdkrrlr
      121 talaneqvgr eragylaqla ivrrqtataw ldavyakqal alqqallghm nheldatqas
      181 yrgakagagd vvqaramlaq tqdqmlkaqq ayrtalvvla rwtavpvadv tgappapesf
      241 vsslppdelr lsqpalvaaa ddiavaeadt avanserspn wtweiayqqr ggaysnmvsv
      301 gvsiplplnr knrqnrdvae kaaletrarl myedtlrqvq adirtqseal asgrerianl
      361 saallpaadq rvqlaiaayr agtgsladtf aarraqldaq lqvldlrrdv srtwaqleyq
      421 vvpsalaaaq
//
LOCUS       WP_175901308              97 aa            linear   BCT 11-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Burkholderia
            vietnamiensis].
ACCESSION   WP_175901308
VERSION     WP_175901308.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 97)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 97)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 97)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..97
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=11086
     Region          1..93
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mivewrakar eerhsifdyi aadnpvaale lddeierktd alpdhpelyr agrvrgtrem
       61 vlgpnyvlvy rvlkqagiie ivrivgarqd ypkgkrk
//
LOCUS       WP_175901316             463 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia cepacia].
ACCESSION   WP_175901316
VERSION     WP_175901316.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..463
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49889
     Region          25..451
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mdndspgrya saaatqdfaa hafrsdaddr rkphllglat lvifglayml pmtvfttygl
       61 vtsetnghlt aayavtlvam lftarsyghm arlmpsagsa ytfasrnfgt sagfmvgwal
      121 lmdylfipmi sylaigiymk qifpmvpasv wivgsialit glnivgirlv nrvnlilias
      181 qlvfiaifvi asarvaageg lsmavalpss gdaraifags ailclsflgf davttlseet
      241 repkrtvpra illctlasgv lfmliayvgq vvfpdwhafk dldsaslelm rrigggtlsa
      301 ffvavyvagc fasamagqas vtrvlfamgr drvlpervfg hlharlrtpv retlavgvvs
      361 lsalfvtldl astmisfgal vafaivnlcv mrsylcraeh rrfagwitfd vvpalgfamn
      421 vwlwsglsrq tfyvgigwlv lglcqlawlt rgftrpaptl smn
//
LOCUS       WP_175901375             710 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Burkholderia].
ACCESSION   WP_175901375
VERSION     WP_175901375.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..710
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77278
     Region          9..699
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mtypslrdwl fsgktfaasm lalylglyfq lprpywamas vyivsnpfvg atrskalyra
       61 lgtalgaaaa iffvppfvet pllfaiivat wcgtllylai sdrtarsyvf mlagytmplv
      121 alptvtdpst vfdvaiarte eivlgivcas vvgsaifpnr laptliertd awfkdaafyg
      181 retlsghiag kalsacrqrl aatitglefl lsqlsydhah prilaraqal agrmqlflpl
      241 mssladplia lmrdlhirpa glddlladaa kwfdaplpav kagndgdmtd dpvaerlrer
      301 iaalqpadda laswdgalls nalwrlrqvi diwqdcrslr alignesgvw qpryrhwrlg
      361 gterffdrgm mlfstltvaa aivfaswlwi asgwhdgaaa vtlvavscsf faaldepapl
      421 vfkfflatta svvfaglylf vvlphvhdfa mlvvmfagpf iligtllprp qfnmvtmlva
      481 vntatfisiq gaydadffvf lnsnlagvag llfayvwtra trpfgaelav rrllrsgwed
      541 varsastqpl ddqrnhasrm ldrvtqllpr lgasddhrhp siesfrdlri alnaldlrrs
      601 rrrlsgdvpd aidrvlagvt dhyarcaaan arqpappall atiddalqrv agrnlpgatp
      661 aehdaapaas atpathrrlr dtlhalvglr lslypaaagq ppqapdgara
//
LOCUS       WP_175901419             108 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Burkholderia seminalis].
ACCESSION   WP_175901419
VERSION     WP_175901419.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..108
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11288
     Region          21..101
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(33,36)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mdteqrytan aptraevdal ggatviefga nwcgicasaq paitasfsah pavrhlkied
       61 gpgrplgrsf gvklwptlvf lrdgvevarv vrpadakqie adgfaala
//
LOCUS       WP_175901389             453 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: uracil-xanthine permease family protein
            [Burkholderia].
ACCESSION   WP_175901389
VERSION     WP_175901389.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..453
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46052
     Region          9..423
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mshdpiptpv darlpawqla lfglqhvlsm aaspitavfl iakvlalpad ltvqligatf
       61 facgigtllq slgagpigar mpfvmvpgga ptmlfagiaa qsglptaaga allasafywv
      121 llpvftrclr lfprivvgam lllvsinlir iyativvgqp gsadfaqpra lglalativa
      181 tvivagafrg tlgrlavlig lmagatlgwa ldampaladv wrgplfthpv wlpfgmprfd
      241 vlaalpllif taismaeata qtvavgetcg kpislsrdvp ktirgdglas lagalfgtpl
      301 ivtsaenigv vqttgvrsry vtaaagaili vialfaplar layaipaavv ggtalvvfam
      361 igvmgirlla gvdlharanq ytlaaalvvg lapilvpnly rhfgspvqiv lgngmaagtl
      421 aaiatqlafa afarlsgqas atpvaassps rdg
//
LOCUS       WP_175901427             190 aa            linear   BCT 11-JAN-2025
DEFINITION  YbhB/YbcL family Raf kinase inhibitor-like protein [Burkholderia
            seminalis].
ACCESSION   WP_175901427
VERSION     WP_175901427.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..190
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=19894
     Region          29..186
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mkfsffprst lctamllsiv ptiavagafs vkvddlnhgq faneqvyggf gchgdnvspr
       61 iswshlprgt ksvvvtihdp daptgglgwt hwgvvnipas dasiekgasg npermpagai
      121 etltdfgaak yggpcppqge shryivtasa lsvpgidvna asspalvayq mhgkviarar
      181 yvamyrraae
//
LOCUS       WP_175901429             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia seminalis].
ACCESSION   WP_175901429
VERSION     WP_175901429.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21929
     Region          2..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 midlstlalf sgaclaltat pgpdmllias rsvsqgrrag fatlagiqag tychalaaal
       61 glsqlfvavp laydavrfag aayllylawk tyrsdatals pvasprrhst atifrqgltt
      121 nllnpkmalf vlalfpqfvr pehgsiaaqi lvlatvlnli glvvngavil sasrlsrrig
      181 arrgpsklpr yllgsvfvgl aarlavagrn
//
LOCUS       WP_175901432             700 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia cepacia].
ACCESSION   WP_175901432
VERSION     WP_175901432.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..700
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73377
     Region          38..634
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mhdaadqtra vaapprrltr aaaaliarid iftprgayva rsviaaalal gvayllelet
       61 pysaastvll vinpvqgavi gkgvwrvvgt iagmvvafvl mgcfaqqpll filgfafwlg
      121 vcvagmtllr hfrasgtvva gytiglatyg amqhpeltfe hvigrgstva igvlclslvs
      181 mllgtrdvha kldalvtrvt advarviaaq rnglaaapad dkrhalfagi ygiddllalg
      241 kaesedlaqr aaavrhgmas lfgalaggmp plpadspgar avaslqprla aawqaaadal
      301 gdgpggatha rallgdarer lrdaldgial gdprddaall iagerlieqi ddyraaldgl
      361 velqrprpgy rparvrfhrd tgaalrngvr aacaivisga fwlatgwnqg dmmllvvapy
      421 callatagnp aagaqafikg tvlavpaafv cafgilprie gfpllvvala lfwmpgiyat
      481 svpktalagl aylvafntlt gatnpfrpdv alflnqsvaw vlatfltllt frlilpgnla
      541 tdatrlrrti rddtlalvag rrvtaagwqq rqqhriaqlg allagqpvam tqasiealaa
      601 lhvgkellri rrgaardglp dparrcvrag laglarhaaa ppraarharr aahalaglaa
      661 aqpgntelkw lmaafadvyv llhtyaayft avperardaq
//
LOCUS       WP_175901436             152 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175901436
VERSION     WP_175901436.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..152
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16917
     Region          1..139
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mkldaidrri lsalqrdgrm qnvelahevg lspspclrrv rlleeagvie kyvavlnpak
       61 vgkgltiftr vwlkgqdaes vnrfseavqq mpevvechlm agdcdfllrv vaadiddyrr
      121 fqmetltrip gvlsvktdip mqkvkltsal pt
//
LOCUS       WP_175901457             187 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Burkholderia seminalis].
ACCESSION   WP_175901457
VERSION     WP_175901457.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..187
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=20991
     Region          84..186
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mntdpkkwnp fkflrgaark sdgdgpenpp aseswqaswp diprlfsrep wravetflhd
       61 pfagrgaler wfgdfsssrf qpridvvdeg pvlrvtaelp gmaredlkvs vedgaivlrg
      121 ekkqdvrsee ngcyrlerah gsfvrtipmp enadpdhtla kfdngvltlt vpkseparil
      181 srtieih
//
LOCUS       WP_175901481             164 aa            linear   BCT 11-JAN-2025
DEFINITION  arsenate reductase ArsC [Burkholderia seminalis].
ACCESSION   WP_175901481
VERSION     WP_175901481.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Messens,J. and Silver,S.
  TITLE     Arsenate reduction: thiol cascade chemistry with convergent
            evolution
  JOURNAL   J Mol Biol 362 (1), 1-17 (2006)
   PUBMED   16905151
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Mukhopadhyay,R. and Rosen,B.P.
  TITLE     Arsenate reductases in prokaryotes and eukaryotes
  JOURNAL   Environ Health Perspect 110 Suppl 5 (Suppl 5), 745-748 (2002)
   PUBMED   12426124
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Messens,J., Martins,J.C., Van Belle,K., Brosens,E., Desmyter,A., De
            Gieter,M., Wieruszeski,J.M., Willem,R., Wyns,L. and Zegers,I.
  TITLE     All intermediates of the arsenate reductase mechanism, including an
            intramolecular dynamic disulfide cascade
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8506-8511 (2002)
   PUBMED   12072565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..164
                     /product="arsenate reductase ArsC"
                     /EC_number="1.20.4.4"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030612 - arsenate reductase
                     (thioredoxin) activity [Evidence IEA]"
                     /GO_process="GO:0046685 - response to arsenic-containing
                     substance [Evidence IEA]"
                     /calculated_mol_wt=17340
     Region          4..143
                     /region_name="LMWP_ArsC"
                     /note="Arsenate reductase of the LMWP family; cd16345"
                     /db_xref="CDD:319973"
     Site            order(9,11..16,112,114)
                     /site_type="active"
                     /db_xref="CDD:319973"
ORIGIN      
        1 mttnvlilct hnsarsvlae gmlnhwaakl gkdvraysag sapsgrlnpf alaaltnagv
       61 dvdgyrsknw defvgggapr mrvvitvcds aasepcpywp gspvkihwgy adpsnatggd
      121 egkrlafelt rqaigyrmlq llalpldrig daelqaalvg isqn
//
LOCUS       WP_175901508             418 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia seminalis].
ACCESSION   WP_175901508
VERSION     WP_175901508.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 418)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 418)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..418
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45140
     Region          <195..412
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mtiapsspst aalkrelkaa earkrtmall lvaplaifll lifvvpigtl ltravqnpei
       61 atalpntvaa lsgwdrkapp adaayvalat dmtkvadsea mgalarrlnt eipgyrslva
      121 ktaramplkg dndaaltpaq trekfvdlds rwgdvaywqa iakngsqvsp fyllaaldhk
      181 qdgfgrivqa dpdqsiylai fgrtfvigia vtlfalllgy playwistls erranlvmil
      241 vlipfwtsvl vrvaawivll qseglinkal igsglishpl tllfnrvgvy ismthillpf
      301 milplysvmk sipstyqraa vslgshpfaa fwrvyvpqty pgvgagallv filaigyyit
      361 pallggpndq mvsyyvayft nvtinwgmac algglllaat lvlyavygrf trtnvslg
//
LOCUS       WP_175901509             308 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175901509
VERSION     WP_175901509.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33095
     Region          6..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..293
                     /region_name="PBP2_DntR_like_1"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     similar to DntR, which is involved in the catabolism of
                     dinitrotoluene; contains the type 2 periplasmic binding
                     fold; cd08460"
                     /db_xref="CDD:176149"
     Site            order(102,104..105,109,166,203,268)
                     /site_type="other"
                     /note="putative substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:176149"
     Site            order(103,106..107,110..111,114..115,117..118,121..122,
                     124..128,130,192,220..224,227..228,231..232,235,249)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176149"
ORIGIN      
        1 mnapdlnlli vldallsens varaaetlgl spsalsrsla rlrattgdpl lvragrdlvp
       61 tphalelrvq vralvegaqa vlcpcknadl gglertftir anegfvdtfa aellalvmet
      121 apnvrlrfap kpdksvealr mgavdleigv vghtgpelrv qalfrdrfig vvraghplar
      181 eevtpqryas fghisvsrrg qlsgpidnvl dtlglqrtva aivsgfpaal slardsdlia
      241 nvperqtaks rggmfsfplp vltatltvsq iwhprfdndp ahrwlrsclr rvcatrassl
      301 ydvgapep
//
LOCUS       WP_175901521             185 aa            linear   BCT 11-JAN-2025
DEFINITION  ester cyclase [Burkholderia cepacia].
ACCESSION   WP_175901521
VERSION     WP_175901521.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Sultana,A., Kallio,P., Jansson,A., Wang,J.S., Niemi,J., Mantsala,P.
            and Schneider,G.
  TITLE     Structure of the polyketide cyclase SnoaL reveals a novel mechanism
            for enzymatic aldol condensation
  JOURNAL   EMBO J 23 (9), 1911-1921 (2004)
   PUBMED   15071504
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..185
                     /product="ester cyclase"
                     /EC_number="5.5.1.-"
                     /GO_process="GO:0030638 - polyketide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=19686
     Region          57..184
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
ORIGIN      
        1 mktstvvsvv srialaaata aaalpavsat ddnlvqlktl ivdkslskhq aeqqiraarl
       61 ydtfwstgde aqarealaad ftdrtlpagr pqgiagplaa skgfhgavpd vhadveqmiv
      121 agdrvithlh ftghftgsfn gvqgkgqvvd fiatdiyrvr dgkitdnwhl ednltflqql
      181 gvvar
//
LOCUS       WP_175901563             468 aa            linear   BCT 11-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Burkholderia seminalis].
ACCESSION   WP_175901563
VERSION     WP_175901563.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..468
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=47995
     Region          2..458
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mtmlslgeaa rlipgatvhg dagvtfdrvs tdsrtagpgd lfvalkgerf dahdflgdva
       61 argaaaalva hvpagvtmpa ivggetraal galahgwrmr fplplvavtg sngkttvkem
      121 iasifaaavg adarlatagn lnndvglplt llrlsaahrl avieigmnhp getevlarlt
      181 aptvalvnna qrehqefmst veavalehaa vihalppdgv avfpaddaya siwrvaatgn
      241 rildfalhda erqndaqvvg rlhggelaid tpagavtvrl ralgehnarn alaataaalg
      301 agvslsairq glesfepvkg rlqvkqaiag slagatvvdd tynanpdsmr aaidvlaahp
      361 aprvlvigdm gevgeegpaf hreigayard rgidalfalg dasrdactay gdaarhfdda
      421 galvsallaa gygaratvlv kgsrymkmer vvdaltnqpa agtapaah
//
LOCUS       WP_175901659             310 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [Burkholderia].
ACCESSION   WP_175901659
VERSION     WP_175901659.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..310
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33178
     Region          4..309
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mtdrvamlvy pgfqvldaag pvsafemady arepyyavri vaaqpglvrs ssgvswhaep
       61 lpdavdldtl lvaggdgvda amadaatcaf vrrcaargir vasvcsgsll laaagvldgr
      121 latthwgcge rfarafpqvr laldriyvnd gpfwtsagit agidltlali gedrgerlar
      181 avakrlvvyy rrpggqsqfs alieldsaqg rfkplldhir rnlgarlrvs dlaeqacmsp
      241 rqfarafqte tgltpakave klrveaaraa lesgaaslqr vanecgfgdt enmrrsfhrw
      301 lgvapsvlrs
//
LOCUS       WP_175901697             410 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175901697
VERSION     WP_175901697.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..410
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42917
     Region          12..394
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(22..23,26..27,30,65,112..113,115..117,120,145,
                     148..149,152,224,227..228,231..233,236,266,270,320..321,
                     325,329,345,348..349,352..353,356)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mtpieqevrr rwlpvlaggl imgaalgirh vqglflapvs ldhgwsreaf glalalqnli
       61 wgvaqpftgm iadrfgslrv ivagmllyaa glvtmahaat tgmftvgagl vigialsgsa
      121 fasiygalsr lfppdrrgwa lgvagaiggl gqfcmvpvaq eliggigwrh afialalvav
      181 vlaplavllr drpaqvagaa agpdqsigea vreafahrgf wllnagffac gfqlafiath
      241 lpaylldhgl parhasvala lialtnvagt yacghlggll rrkyvlsvly lvraltmavf
      301 vaaplspasv yvfaavmgft wlgtvpltng visqvfgvry iatlfgfvff ghqlgsffgv
      361 wlgarvydat hsymplwigs ialgvlaall hlpindarva rpaagnaawa
//
LOCUS       WP_175901729             204 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia seminalis].
ACCESSION   WP_175901729
VERSION     WP_175901729.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..204
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22697
     Region          1..204
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mmkligslgs pyvrkarivl aekkidykle lenvwapdtn ihasnplgkv pclvmedgaa
       61 vfdsrvicey vdtlspvgkl ippsgrerve vrcwealgdg vldaavairv ehtmrddaqr
      121 saswiarqqr kiddglvams qglggktwcv gnhytladia lgcalgyldf rmpelnwrdr
      181 hpnldkhfvk lqqrqsfadt lpqn
//
LOCUS       WP_175901750             205 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175901750
VERSION     WP_175901750.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22896
     Region          18..172
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnkptpsasp srgpsdhevr aqivdaatey fsrygyektt vsdlakeigf skayiykffd
       61 skqaigqvic anrlaamita vrenidgvhs atekfrrmfk tllssgself fqdrklydia
      121 avsaaspwps vqgyedqirq lvaeilrlgr etgeferktp qdeavnaifl vmkpyfnpll
      181 lqynlegaee attqlenlvl rslap
//
LOCUS       WP_175901821             442 aa            linear   BCT 11-JAN-2025
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Burkholderia seminalis].
ACCESSION   WP_175901821
VERSION     WP_175901821.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..442
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=47386
     Region          71..440
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 malgehlrqq laakalkrql eratdaaaap gvpgtpaaqt asarsrfesm pqyqqvrimr
       61 emgeklrvds pffrvhdgva gattqiggre ylnfanynyl glagdpdvsa rakaaidryg
      121 tsasasrmva gerpvqrdle ralaafyetd dcvafvsgha tnvtvigalf gpgdlvvhda
      181 lahnsivqga qlsgakrlsf phndwqalde llsrvrreyr hvliaiegly smdgdfpdlq
      241 rfvdvktrhg afllvdeahs lgvlgatgkg irehcgvapd qvdmwmgtms ktlagcggfi
      301 agcqplvdml rhlapgflys vgiaptlaea slaalerlqa eparvaqlqa rgrqfltear
      361 aaglntgtsa gyavvpvitg sslkaaqwan amfdeginvq pifypaveek aarlrffics
      421 thepeqisrt vgvlsrlagr sa
//
LOCUS       WP_175901862             243 aa            linear   BCT 11-JAN-2025
DEFINITION  DsbA family oxidoreductase [Burkholderia seminalis].
ACCESSION   WP_175901862
VERSION     WP_175901862.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..243
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26012
     Region          15..214
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(23,26)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 mttapaptar ptltveiwsd licpwcwigk rrfdealaaf ahadrvdvvl rayrlmpgqp
       61 vepvegmlag kyrmspaqvd qmlrqvtdaa asvglrydlp gtlvgdtldg hrlvklaeat
      121 grahalterl yrayfcehgs lfdhaaltef avetgleraa veavlrsday rdeveadiar
      181 aaqiggrgvp lfvfggryav sgaqpadafa qaldqawrdg iveldgtdaa acgpdgcalp
      241 ara
//
LOCUS       WP_175901888             271 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia seminalis].
ACCESSION   WP_175901888
VERSION     WP_175901888.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10549394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..271
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30344
     Region          79..163
                     /region_name="Methyltransf_11"
                     /note="Methyltransferase domain; pfam08241"
                     /db_xref="CDD:462406"
ORIGIN      
        1 meptqivrgy chvcgswtif ksyepvdfpc krnsflcdrc gssarnrhla ksildlwlrg
       61 dthtslrkfa rkfrgtvyia stagavaesl aplgdrlvas eyidgtasge crngvlcedi
      121 qatsfddssf dlvitedvle hvpcpemafa eirrilkpgg yhvstipvkw hlaksesrai
      181 iengtilhlq epefhldptr vegilaftdy gqdilarycs iigksemlaa hgdtdmerty
      241 aiynnwvfls qregisslpa sawtrfvsrw r
//
LOCUS       WP_175901901             418 aa            linear   BCT 11-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Burkholderia seminalis].
ACCESSION   WP_175901901
VERSION     WP_175901901.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..418
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45293
     Region          12..395
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mlkrfgnpdv akavanlvwl glerltqigv aiaisgllar yfgpdvfgkw qyantlllvl
       61 apltwvcgae ilvptivqrp paqlgavlgs afalrigvsv aalvatwiai aagafdplvg
      121 amltglavtm vfrepfvgvi nawlqsmtys kpqlvtsmvt alakallvwl lvraaagpar
      181 fawlwaleaa aigfalllyy rhrnggalgw tfdkplfrhf atagtvfwlg licmylflkl
      241 drlmlerhvs fadlgrysaa qqlnenwitl almlaqtiap afvyrvqdva rlrrnivrli
      301 amtaalmtag alvldaaapl ivgkvfgrgy easvdifrwa vwlsvpagie aignlivlky
      361 qakfvllskw llalaiaavv nlfaiprlgl ygalvglaag ylaaaavnfy yirfklrt
//
LOCUS       WP_175901982             390 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia seminalis].
ACCESSION   WP_175901982
VERSION     WP_175901982.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..390
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=41678
     Region          156..387
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 msehtpspag lpgtssassd slrpepaktp dapaaqaaaq nvaadgaspv ttasepgapg
       61 aadgavappk pgapppgfga ppdfetsrpp pasaqnappa ylkqsdtpws vfgrivaara
      121 rrlfdragqr itqrtlrigv sarifhpepg akglrgktlq yleesiahwv msrdvlvfmi
      181 ptvghqgmih psnirlrdya khldglllqg gadvspqtya asdvrpewpg drvrdmyele
      241 llhefvesgk pvlgvcrgcq linvafggsl yqdiatdvpt anahvsehyd qhrhairfpd
      301 tstlasmfpg rseaivnsih hqairdlgrd lnieavsagd giiegirhrr spfvvgvqwh
      361 pefhraggae lldctpllda flraaretrl
//
LOCUS       WP_175901970             779 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia seminalis].
ACCESSION   WP_175901970
VERSION     WP_175901970.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 779)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 779)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..779
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..779
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84578
     Region          61..761
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msfthvarlp rgrlalacaa afawpaahaa spvdapadss sggvarpaga avppapsggt
       61 ltavsvtaqr qpvdpdtpav vtsitreqie shtnvtteda lkyapnlmvr kryigdrnsv
      121 fagrdfnelq sarglvyadg vllsnllgss yaypprwsli ppddiarvdv lygpfsalyp
      181 gnsigstvll ttrrpdklea slstqfftqr yhdgygfads fggnhqtari adrvgrfwfa
      241 lsldrlendg qpmqyaspns aynpklgaav pvtgaatdig pngkprtivg aqtierteql
      301 netvrmgyaf tdrvdatltl ghwenhyrqh getflrdtag npvyggnvsi ggrnmtvapn
      361 afapqrgdqe nwlyalglng rldsgwrlsg vvsaydvsrd vlraastvqg gagtlfqgdg
      421 tgwrtldlka eapavkghtf tfgyhydnyf lrnvtyntad wlagpttsla svyrgdtrtq
      481 alfgqdawrf apgwlatlgv ryerwdaygg algnaggtlg yadrganals pklalqwdat
      541 dvwrfrlsfa tgtrfptvge lfqgtisnna ivnnnpnlrp ekaidwdfta erdvgvgvvr
      601 asvfqsdlrd siysqttvsg attvtnvsnv drvrvrgvel afggenvglk glaidanvsa
      661 snaqiladaa npayvgsrfp riprmranll asyrfdehwl asvgvrysgr qfntldnsdv
      721 npdvyggtss ftvvdlkary rldrhwsasl gidnlmdrry yvfhpypgrt fygelkwsl
//
LOCUS       WP_175902049             299 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175902049
VERSION     WP_175902049.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 299)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..299
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32361
     Region          18..144
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          216..296
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msaprlpdaa rywrtpllpd adlltatyrd hafaphwhda ytipvilega erftyrgngy
       61 vaetgtvpvi npgevhtgsr atdegwcyrv sylpvefirg lasaiagrpq dapwfasdvi
      121 rdadlaarlt lahrmmeags asalssnphg hpagepaada priydplaae tamldalstl
      181 ivrhadarpr paplaadepr vdamrerlaa dltctvtldd vaqaaglspf haarlftrtt
      241 gmpphawrnq lrlqralapl ragvpvadva aasgfvdqsh ftrhfkrmfg vppgrwqas
//
LOCUS       WP_175902088             290 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia seminalis].
ACCESSION   WP_175902088
VERSION     WP_175902088.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..290
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30753
     Region          12..280
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mkkiqgvysa prghwvgdgf pvrsmfsyqs hgahlspfll ldyagpatfe pgsvsaprgv
       61 gqhphrgfet vtivydgeva hrdstgaggt igpgdvqwmt aasgilheef hseaftkrgg
      121 plemvqlwvn lpaadkmgap gyqtllnadi pvvelpdgag rariiageld grrgpartht
      181 pidvwdvrlv aggharfpva egrtlavvvl sgtvqvnget vareaqfvql grdgsdveie
      241 angdakllil sgepidepvv gygpfvmnsq aeirtaiedf nngrfgqmpa
//
LOCUS       WP_175902162             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175902162
VERSION     WP_175902162.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32324
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(103,107,146,160,162,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(104..105,109..110,112..113,116,120,122..128,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mnrfealrif cvaaestnfr aaavrlgvsp qvitrviral eaefreplfh rstrgvrlth
       61 fgaalasrsa aaiegidrvf ahatagtpge ltgivkiaap ialgrriitp glasvlahhp
      121 gllvdlrlsd vladvvdeqi digvrigpmr dtshvarevs saslvivgsp elvgrcgapv
      181 drnaleqapl tllidrntgr pwpwllqdga sfvpanpvfv tddpeaecea vlagmgfgql
      241 pahlaapyln rnmlvpvaee lnppatvmyv yrphrtpvpg rvrvvfdalc allkdcedrr
      301 i
//
LOCUS       WP_175902202             343 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia seminalis].
ACCESSION   WP_175902202
VERSION     WP_175902202.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..343
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36706
     Region          23..326
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 msfsflparr alaatltaal afagavipqa aqaegriria eqfgvvylml nvardqqlie
       61 kegrkagldi kvdwvrlsgg aavndallsg avdiagagvg plltvwdrtr grqnvkgvas
      121 lgnfpyylvs snpnvktiad lsakdriavp avgvsvqsrv lqyaaakqwg dkqfdkldsl
      181 tqaiphpdat aailansnvi tghfgnppfq eqelagnpna hivlnsydvl ggpssatvly
      241 atekfrddnp ktyrafvaal adaarqiaad peraadtyir vngskidral llkilrnpqv
      301 qfktapqntl plaqfmhrtg airnepkswr dyffddpata ggs
//
LOCUS       WP_175902203             329 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia seminalis].
ACCESSION   WP_175902203
VERSION     WP_175902203.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..329
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=35633
     Region          64..320
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mvgprdarpy vdvfpardsi vnatsprtwl ppyaarggas pvafaapdtg aagqpagnaa
       61 qagahserll aidqvsleyr sgarivrath qvsfdvygsd rfvllgpsgc gkstllkaia
      121 gfiepvsgsi aldgrpvrgp gpdrvvvfqe fdqlppwktv venvafplrv aaklsraear
      181 eravhyldkv glgafadayp htlsggmkqr vaiaralamq prvllmdepf aaldaltrrk
      241 mqeellrlwd efrftllfvt hsieealvvg nrilllsphp grvraelnsh ehsldnvdtg
      301 dfrdnvarih rllfdtdaph vpttedaas
//
LOCUS       WP_175902250             151 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia
            seminalis].
ACCESSION   WP_175902250
VERSION     WP_175902250.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..151
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16919
     Region          13..141
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mperisfgql parlldvvln veeyanhtgh dfklvelvra rvsqlngcay cldrhikegi
       61 hagddplryn llplwhetpa lyspkeqaal rwaealtlls ehaiddalva atrehfdrde
      121 latltlivaq intwnrlakp fawqagvfqa g
//
LOCUS       WP_175902319             294 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia seminalis].
ACCESSION   WP_175902319
VERSION     WP_175902319.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..294
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31472
     Region          12..270
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 msasiktllt presdignlv vrrvlparaa rlvgpfiffd emgpavlpag rgidvlphph
       61 iglatvtylf dgslmhhdsl gfrqkivpgd vnwmtagrgi vhserspded rpreqpvhgi
      121 qtwvalpveh edtapafvhh paatlpsftr dganvrviag tafglaspva vfsptlyaya
      181 eftpggrlal daeheergvy lvdgdltvdg tplaaatmav lepgatvala sangarvmll
      241 ggahlpgerf iewnfvsser akidaaraaw adqtfgkvpg eehewtrqpa rhaq
//
LOCUS       WP_175902330             466 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatase PAP2/dual specificity phosphatase family protein
            [Burkholderia seminalis].
ACCESSION   WP_175902330
VERSION     WP_175902330.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Pulido,R. and Lang,R.
  TITLE     Dual Specificity Phosphatases: From Molecular Mechanisms to
            Biological Function
  JOURNAL   Int J Mol Sci 20 (18), 4372 (2019)
   PUBMED   31489884
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Patterson,K.I., Brummer,T., O'Brien,P.M. and Daly,R.J.
  TITLE     Dual-specificity phosphatases: critical regulators with diverse
            cellular targets
  JOURNAL   Biochem J 418 (3), 475-489 (2009)
   PUBMED   19228121
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   4  (residues 1 to 466)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   5  (residues 1 to 466)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12932297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..466
                     /product="phosphatase PAP2/dual specificity phosphatase
                     family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=50016
     Region          41..215
                     /region_name="PAP2_Aur1_like"
                     /note="PAP2_like proteins, Aur1_like subfamily. Yeast
                     Aur1p or Ipc1p is necessary for the addition of inositol
                     phosphate to ceramide, an essential step in yeast
                     sphingolipid synthesis, and is the target of several
                     antifungal compounds such as aureobasidin; cd03386"
                     /db_xref="CDD:239481"
     Site            order(116,124,150..152,187,193,197)
                     /site_type="active"
                     /db_xref="CDD:239481"
     Region          319..456
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
ORIGIN      
        1 msalgggagg laepaagard asfalrvgwl aamgavffst ygfanwlaar raavptfafg
       61 wehaipfvpw sivpywsidl lyaasfffwt rradlldhvk rlltvqlvsv acfiawplrf
      121 gferpdaggv agalftllmg fdkpfnqaps lhigllvvlw avyarhlrgt iaravlhpwf
      181 aaigvsvltt yqhhaidvpt gaavgclalf lfplrdatgr lpgadaspsa agrafarrya
      241 igaallawaa lwcvprapgw alaagwvala lacvawayrr gapgafqkda ngrfpvfira
      301 llaptiagaf vnsrlwtwrq papvriderv sigrtpttrd vrrqgftalv dltaemprwa
      361 addaslayac vpqldlvapt aaqlaqavaa lerlhgegrd vlvccalgyg rsvlcaaawl
      421 aarrglgdar dalaavravr pravwsnega avlqqwidrr rgterv
//
LOCUS       WP_175902332             201 aa            linear   BCT 11-JAN-2025
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Burkholderia
            seminalis].
ACCESSION   WP_175902332
VERSION     WP_175902332.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Sciara,G., Clarke,O.B., Tomasek,D., Kloss,B., Tabuso,S.,
            Byfield,R., Cohn,R., Banerjee,S., Rajashankar,K.R., Slavkovic,V.,
            Graziano,J.H., Shapiro,L. and Mancia,F.
  TITLE     Structural basis for catalysis in a CDP-alcohol phosphotransferase
  JOURNAL   Nat Commun 5, 4068 (2014)
   PUBMED   24923293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Koga,Y.
  TITLE     From promiscuity to the lipid divide: on the evolution of distinct
            membranes in Archaea and Bacteria
  JOURNAL   J Mol Evol 78 (3-4), 234-242 (2014)
   PUBMED   24573438
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Koga,Y.
  TITLE     Early evolution of membrane lipids: how did the lipid divide occur?
  JOURNAL   J Mol Evol 72 (3), 274-282 (2011)
   PUBMED   21259003
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..201
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20988
     Region          28..196
                     /region_name="PgsA"
                     /note="Phosphatidylglycerophosphate synthase [Lipid
                     transport and metabolism]; COG0558"
                     /db_xref="CDD:440324"
ORIGIN      
        1 mslyalkpkf qnrlrpfads laargvtanq vtlfaaggsi vvgalaglgv faralflltp
       61 lwlfarmaln aidgmlareh gqkstlgayl nelgdivsdv alvlpflaip vfapadvwlf
      121 altaviveca gligplvgat rrydgpfgks dralavgafa lwiglgfpvg gvaawlwrll
      181 ivlsimtavr rvragiaeag g
//
LOCUS       WP_175902387             539 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA synthetase [Burkholderia seminalis].
ACCESSION   WP_175902387
VERSION     WP_175902387.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..539
                     /product="acyl-CoA synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016405 - CoA-ligase activity [Evidence
                     IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57825
     Region          48..538
                     /region_name="MACS_like_3"
                     /note="Uncharacterized subfamily of medium-chain acyl-CoA
                     synthetase (MACS); cd05971"
                     /db_xref="CDD:341275"
     Site            order(111,241..243,267,287,289,293,314..317,336..341,
                     344..345,361,421,433,436,442,444..447,476,505,510..511,
                     513,515)
                     /site_type="active"
                     /db_xref="CDD:341275"
     Site            order(192,195..200,202..203)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341275"
     Site            order(237,289..290,293,314,444..446,505,511)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341275"
     Site            order(314..317,336..341,361,421,433,436,442,447)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341275"
ORIGIN      
        1 mlpaadrydd llsrfrwdip arynigvdvc dkwadgsgrl aliyetaqgd vfrmtfddlk
       61 nasnrfansl araglqrgdr igiflaqgpe tavahlaayk lgaiavplft lfgvdaleyr
      121 lanseaaalv tdavgyakia slrarlpalh tvycvgddap daprvlryda alaaetpefv
      181 padtaaddpa viiytsgttg kpkgalhahr vllghlpgve msqqgfprda rlfwtpadwa
      241 wigglldvll pswhhgvpvl arrfekfdgd aafalmarhg vthaflppta lklmrtvaap
      301 rerhalslks vasggeslgt eltawgrdal gvtinefygq tecnmvlssc aalfdarpga
      361 igkavpghav aivdadgtpl ppgvegriav rrpdpvmfle ywrnpdatrd kfagdylltg
      421 dtgmldadgf vrfvgrdddv itsagyrigp gpiedcllth pavrmaavvg vpdatrteiv
      481 kafvvlnpgh vgddtlvlal qahvrtrlaa heypraiafv dslpmtatgk ivrralrda
//
LOCUS       WP_175902426             136 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Burkholderia seminalis].
ACCESSION   WP_175902426
VERSION     WP_175902426.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..136
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=14960
     Region          32..134
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mhtnptlaeh qtkpvhpaaa eaarrpaitp nvdivenprg vtlradlpgv prenldvkvh
       61 dntltieadt qidtpadlrv rhaevratry arsfvlspdl dtsridanlr dgvltltipr
      121 reetrprrid vttgna
//
LOCUS       WP_175902454             343 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia seminalis].
ACCESSION   WP_175902454
VERSION     WP_175902454.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..343
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36690
     Region          8..343
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkldstpitl thcaktfrgt rvlepldlsi gagetlvllg psgcgktttl rliagldtpd
       61 aggtiafgnd dvtalpierr qvgmvfqnya lfpnltvrgn vgyglkirkt epralrervd
      121 ellammrlda hadkpvdqls ggqrqrvala ralavrprvl lldepltald aklrdvlrre
      181 mnallrelgv ttvyvthdqa eamelgdriv vmgagrieqi gtprniyyqp anrtvaqfig
      241 tlnrlagqwr dgalvttgga iatphaadew ffrpedaqla dpahaplrga vgacaflger
      301 trltiehaap dalvidvpgr ialargtavg ltiapeglia lga
//
LOCUS       WP_175902482             496 aa            linear   BCT 11-JAN-2025
DEFINITION  HDOD domain-containing protein [Burkholderia seminalis].
ACCESSION   WP_175902482
VERSION     WP_175902482.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..496
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=54642
     Region          18..235
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 msitehlprt alldklwarm sergdfplls eslratmaam knddldftal vrvvlsdfal
       61 tqkvlrlans amymafggni ttvtralmvl gmdavghlvv glklvdhfhh stprridakl
      121 elnrallsgc varklterad lrageeavvc tlmrqvgkll vvcyldsewd kirrraaemh
      181 gdesaacvev lgvgfdeigl eaaarwrlpd mirdgiaddh hhvnrvdafg relaadedmi
      241 ervnwlravs rcstdvasal ampdgpqrda hiaalaqhya saldtepdal veiasrlane
      301 easdtvmrei velranadai araqaepeac leagladlra lpsehvltpv lalaseslla
      361 slaftrtvmf vrhddgtfaa rlgfgpgvda alyrlrfher fepdvfhlai tnsvgifieq
      421 aqepkmlkrl pawyldvfdd trafvllpvr vdtatvally gdwagaqpar kisqqemsil
      481 nelahelgrf fpaqhg
//
LOCUS       WP_175902472             213 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia seminalis].
ACCESSION   WP_175902472
VERSION     WP_175902472.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..213
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=21827
     Region          7..213
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mtqrslkial fgatgmigsr iaaeavrrgh rvtalsrhpg aagdgitaqa adlfdaasia
       61 aalpghdvva saygpkqdda akvvgaaqal vagtrqaglk rlvvvggags levapgkqlv
      121 dtegfpdayk avalahrdaf dylktvtdld wtflapaali apgertgtfr tgvgklivda
      181 qghskisaed yavafvdale qdsfvreiat vay
//
LOCUS       WP_175902498             341 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia seminalis].
ACCESSION   WP_175902498
VERSION     WP_175902498.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..341
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35612
     Region          10..341
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mgnlnpvada qtitlksrht kwppelsifl vlvgislffe ivgwivvgqs flfnaerlei
       61 ivlqmavigi iavgvnlvii tsgidlssgs vvaaaavvsa slaqvsdfpr avfphltdlp
      121 iiwpvlagvc vgllvgllng tliamtgipp fiatlgtmva argfakwftn gmpvsmltdq
      181 faaigaganp viifvviaai fhvvlrytrf gkytyaigan rhaavvsgin vtrhlvfvya
      241 iagllsgiag tvtaaraisg qsgmgvmyel daiaavvigg tslsgglgrv tgtvigvlil
      301 gvmtsgftfi ridayyqemv kgaiivaavi adqyrnkkkr r
//
LOCUS       WP_175902506             199 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia seminalis].
ACCESSION   WP_175902506
VERSION     WP_175902506.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..199
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20302
     Region          1..180
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msetlfsliv fvivatitpg gattlatasg tqfgfrrsvp llggialgla slaaiaaagl
       61 agllhavpal qlimkvlgsa yllwlawkia ssgapknhan asqtptsfig galllwlnpk
      121 gwtmalgaaa sfaaltpdpg rlavilgtaf gvaaifslvl wctvgvllgr tlrtnrhwri
      181 anaalgllla lsivpiwld
//
LOCUS       WP_175902576             238 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia seminalis].
ACCESSION   WP_175902576
VERSION     WP_175902576.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..238
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25749
     Region          146..223
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 msgsepvgld hpvwsalttk qahlgqgdal arryhpdvap faalaaetta ayralqallr
       61 preqlallsv eplgpvdglq tehvglihqm vaspldagrm dneavvrlgg adandmldla
      121 rrtrpgpfgk rtvamgnyig irergrlvam agermhidgy veisavcvdd ahrgnghagr
      181 lvnilrheig qrgetpflhv fsdnvsairl yerlgfqlrr tfhlnrigqa hadsvaal
//
LOCUS       WP_175902582             193 aa            linear   BCT 11-JAN-2025
DEFINITION  flavodoxin family protein [Burkholderia seminalis].
ACCESSION   WP_175902582
VERSION     WP_175902582.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..193
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=20472
     Region          11..189
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mtqhvspart avvyhsgygh trrlaeavad gagavlvaid adgnltedaw dtlagadail
       61 fgsptymggp swqfkkfada sskawfdgaw rdkifggftn sasingdkln tleyfvllag
      121 qhggiwvsmd ikpanlkasa rddlnrmgsy lapmaqtpad aspdemspgd letarrygar
      181 vatiagrfra gqr
//
LOCUS       WP_175902595             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175902595
VERSION     WP_175902595.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33060
     Region          7..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..292
                     /region_name="PBP2_LTTR_like_4"
                     /note="TThe C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08440"
                     /db_xref="CDD:176131"
     Site            order(111..112,114..115,118,122,124..130,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176131"
ORIGIN      
        1 mainfdltdl qafravvetg sfrkaadavs isqpalsrri dkleealgvr lferttrsvs
       61 lttvgrvfaq saeqllddld aallgirdvs ssrlghvtia cvpsvayyfl paviaryhqr
      121 fprirvklld asanevlgav isgeadfgvs figsqeaeie fkvllqerfv aacrrdhpla
      181 rkkrvtwsel yahdyvsvdk tsgnrllldq alaavappap svcetrhvtt llglieaglg
      241 vaavpsmamp ghdhpiltsv plvepvvkrr vgivkrrgrp ltpaaeafhq mvlearrggi
      301 agsgapa
//
LOCUS       WP_175902609            1056 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia seminalis].
ACCESSION   WP_175902609
VERSION     WP_175902609.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..1056
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114713
     Region          29..1033
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnapehrsst dgalgaqavs asrddgrfnl sawalkhqql vifliglati fgmigytrla
       61 qsedppftfr tmviqtywpg atarevqeqv tdrigrqlqa apyvdniksy srpgesmiff
      121 amkdsapvdq vpetwyqvrk kvgdiratlp kgtvgpffnd efgdvytniy alegdgyspa
      181 qlhdyadklr tvllrvpgva kvdyfgdpaq hvfveisnaq ltrlaitpqq laqaidaqna
      241 vapvgtitta ddrvfvrpng afkdtqalad mlvtvngrtf rlgdvakvtr gyndppvtqm
      301 rtnghavlgi gvtmqkggdv idlgkaldak aaelraglpa glkltavssm phavkhsvdd
      361 fveavgeava ivlvvslvsl glrtgmvvvi tipivlavta lcmhvfgigl dkvslgtlvl
      421 algllvddai iavemmavkl eqgwsraraa afaytstafp mltgtlvtvs gflpialaks
      481 stgeytrsif evsaislivs wfaavvlvpl lgyhmlpeqq hhdahahgqd vyetgfyrrl
      541 sgwisacier rwvvlgvtav lfaiamaaft rvpqqffpns erpellvdlr lpegasfdat
      601 lreatrlekv ldgrpeidhv vdfvgtgapr fylpldqqlq qpnfaqfvit akdvesrdrl
      661 shwlestlas rfptvrtrva rlengppvgf pikfrvsgdd iatvrgiaek vadkmradar
      721 trnvqfdwde paersvsfei dqlkarqlgv tsedvssfla mtlsgytvtq yrerdklidv
      781 dlrapkreri dpsqlaglai ptphgpvplg tighvrdtle ygviwerdrq ptvtvqadvr
      841 geapsigvtr aidgtlatlr atlptgyrie iggaaeesmk gqtsinaqmp lmiiavltll
      901 miqlkrfsrt fivvltaplg ligvvaalll fgkpfgfval lgviamfgii mrnsvilvdq
      961 idqdiaagqp rftaivgatv rrfrpimlta aaavlalipl lrsgffgpma talmggitia
     1021 tvltifflpa lyatcfkvrs dereshamdv assetc
//
LOCUS       WP_175902630             339 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA-binding protein [Burkholderia seminalis].
ACCESSION   WP_175902630
VERSION     WP_175902630.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13774834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..339
                     /product="DNA-binding protein"
                     /calculated_mol_wt=37495
     Region          26..144
                     /region_name="KfrA_N"
                     /note="Plasmid replication region DNA-binding N-term;
                     pfam11740"
                     /db_xref="CDD:432038"
     Region          <118..>338
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
ORIGIN      
        1 msdlaadepr ltaeierlka nfpktrelyr eacallffrf gitptanrly qlvrkgsmst
       61 ptavlgefwa elreksrvri ehpdlpadlq aaagelvaal wnrsstdaaa aldalraeve
      121 aervaaqaev atlqaelart etaleqrtaa llaaqvriqe leqaraadea srqalqadie
      181 rlkadntead ralaqaradf ttqldrlrdd agraeerlra aekralqeid rerlaaarlq
      241 keldatasrm eqrdarhrkd vadlqtqlgd alhrcgvlqg qldgaqatda arvkeldalr
      301 reiamlarra plrgvktapa aqreerkart rkrtdeaag
//
LOCUS       WP_175902660             854 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia seminalis].
ACCESSION   WP_175902660
VERSION     WP_175902660.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 854)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 854)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..854
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..854
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=92654
     Region          59..712
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mqpfqpsstr vnrrnvssvr afcarwvara qpvaaaavar vkplaatawh hvrhptrrgv
       61 lltgaavpal faayvvvlip ftpgigdirk arvdqpaqvl sadgkllaef kpsnrewvpl
      121 kqisphmvda liatedhrfy ahhgldwkrt asaalhtfsg srqggstitq qlarnlypde
      181 igraptltrk vkeaitalki eavyskdqil etylntvpfl ynaygvemaa rtyfdksade
      241 ldvldsatlv gmlkgnsyyn pvlnperalq rrntvlgqmv kygklspaqf aqlqrrplri
      301 dferqkeppg paphfaqqlr kwliawadrn dyniysdgli vrttidsrlq qmatqaltlq
      361 gnqlqgiang awsgrdgcgt dnevfrtfmr espeykaaqd dgkddaaamk llatdrgfmr
      421 alckaktdvq agflaidprd gqirawvgsr dftrepfdhv aqarrqpgst fkpfvygvaf
      481 akgmkpddtf idqpveiplk ggeiwrpndd vpptgkpmtl rdavalsrnr itaqvmeqvg
      541 paavarlard mgvrdspler vpslalgtsp vtlkemvasy atiangglyv epqmvtrien
      601 rqgevlaeya papperalda etdktllgvm rdvvtrgtgg sirtrfgirg dvagktgttq
      661 dnadgwfilm qpglvagawv gfddgrvtlr sdywgqgahs alpivgdffq raqrarlvdt
      721 kakfdtepsp gwfaslrerv tdlfdtwfpp epkktsapvr tqrierppev dedaasdasa
      781 asapdaasgg iveewvpase vaasaaalsa spsqpqpaqp pasasatggs gaspgaaplp
      841 ppapsapdat gasq
//
LOCUS       WP_175902679             263 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175902679
VERSION     WP_175902679.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..263
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28778
     Region          13..260
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 metspdqsnd llfnqslekg lnvlrafsak rrtmtlaeva daagmtkssa qrmvytlekl
       61 gyirkhpvtr ryqltphvmr igfnylaadt lidvanpfls eltnltgett nltepdenem
      121 vyvarfvstk fvpihmpigs ripmyctgcg raflsalppg dararldama rpphtprtvt
      181 aldelvalld garregyatn qeelfigdms iaapvlgsqg qpvaavhvva ptsrwtfdda
      241 rrklapavid cargisnsir tle
//
LOCUS       WP_175902693             276 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175902693
VERSION     WP_175902693.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..276
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=30183
     Region          11..247
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mnpssnlerk gvalyaqias llrgrihqge wkrgdqlppi pelcafyrag titvrqalae
       61 lsaeglvssa rgrgtfvtad ivspadnpal raaindplql apgqtlrvll reavtalpaa
      121 lqtgqperaa ymrirtlhlh dgtpygvmds yvaretydrf pkgsdarhkv gylvrqynrl
      181 plararqeit aayadqatag llasngadcs madmlirmrr wwtdgdgciv haglylyrad
      241 rfvldithdl dgddrsadli pssraatrkg prkstt
//
LOCUS       WP_175902697             418 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia seminalis].
ACCESSION   WP_175902697
VERSION     WP_175902697.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..418
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44448
     Region          17..395
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(27..28,31..32,35,69,124..125,127..129,132,152,
                     155..156,159,234,237..238,241..243,246,270,274,325..326,
                     330,334,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 msvpaagvfr slrsfnyrvw aigslvsnig twvqrtaqdw lvltqlthhd asavgtvmal
       61 qfgpqllllp wtgyaadrfd qrkllmttqa lmgvlalalg mltvtgaarl ehvyvfaflf
      121 gcasafdapv rqtfvaelvg drelanaval nstsfnaarm igpaaagfmi asvgtgwafi
      181 anglsffavl asllllrede lranlragrs rgglldgfry vwhredlkai lvmlfligtf
      241 glnfqlfist maasvfhvda rgfgflssmm avgtvsgall aarreqprfg hlwfgaalfg
      301 lgctfaalap gywlfaaalv ltgvaaitfm nstnslmqls tepamrgrvm alrlavalgg
      361 tpigapvagw vanhlgprwa lgvgaasgfa aalvathfvk rnrgtlragr aveqrdaa
//
LOCUS       WP_175902702             319 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175902702
VERSION     WP_175902702.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..319
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35351
     Region          2..312
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhrigflisd gfqimalaaq svfeyanmgt repfyvmdsy svdggdvrss lgltvatral
       61 rgridvdtwi vagvndplvs papagvvtyl rranararri agictgafvl aeagllaqrr
      121 atthwafgrd mqrhypeirv eedriyivdg piwtsagmta gldlalamve kdlgadaars
      181 vahklvmnqr raggqsqhse mldlapksdr iqnalnyarr nlgraltvee laeavhlspr
      241 qfsrvftlet gqspakaier lrlesarlmi eqsrhpldvi akengfrdrr hmreafvrgf
      301 gvppqamrrd arlderetg
//
LOCUS       WP_175902705             453 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia seminalis].
ACCESSION   WP_175902705
VERSION     WP_175902705.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..453
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48788
     Region          34..420
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(47..48,51..52,55,87,137..138,140..142,145,165,
                     168..169,172,270,273..274,277..279,282,310,314,365..366,
                     370,374,390,393..394,397..398,401)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 msaplqahaa paaapaagst daagddalyr riglrivpfl ficyivsild rsnigfaqlq
       61 mrqdlgltda myslgavlff vgyvlfevps nallrrfgar rtfarimclw gavsvamitv
      121 dsarhfyvlr fllglfeagf fpgvvfylty wyparrrasv lsifyagvav agmvggllsg
      181 wlmrgmsgvm glhgwqwmfa iegapaillg viawfwlcdr peharwlsda ererlaadla
      241 adrartgtpa phslrqalae prtylfafiy fslttallml lfwmplmire fgihdvvqis
      301 llsvvpnaig aagliaiarr sdrnrerrrh faacafggaa alalltlhlp sivammalls
      361 iaamlifaah pvfwavpsay fsgagaaggi alissigvss gmitpwlvgl irtrtgsmdp
      421 amlmiaalla acaiamllgv rpgeagartd avh
//
LOCUS       WP_175902729             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175902729
VERSION     WP_175902729.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33319
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..288
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mlsedelall dairatgsls raaarlgkap stvshaarql etrfdallfd rrgyrlqltp
       61 agqvladeaa rlaldvarlt qrvrqiasgw edrlwivsde vlefdtllpv vrafdalesg
      121 vslrfthevl ggtwealrdg radlvvgatn eppaipgfkw felgamewvf avsprhplas
      181 aggvltrdai gahravvvad ssrraagray gllggqpvla vpsmrakila qrdalgvgwv
      241 prrrvtslla rgelvekqta dprepnllyv awhgerdgra lqwwleqlre prlaqrlldg
      301 idvvg
//
LOCUS       WP_175902752             366 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia seminalis].
ACCESSION   WP_175902752
VERSION     WP_175902752.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Saurin,W. and Dassa,E.
  TITLE     Sequence relationships between integral inner membrane proteins of
            binding protein-dependent transport systems: evolution by recurrent
            gene duplications
  JOURNAL   Protein Sci 3 (2), 325-344 (1994)
   PUBMED   8003968
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004772
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..366
                     /product="ABC transporter substrate-binding protein"
                     /calculated_mol_wt=39790
     Region          62..364
                     /region_name="AfuA"
                     /note="ABC-type Fe3+ transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG1840"
                     /db_xref="CDD:441445"
ORIGIN      
        1 msfapkrvaa alaivlgtaa ggavaqvpag ypgnyqgvid aakkegkliv ysttdtglvr
       61 plikdfesly gvkveyndmn stelynryis enaasstsad vlwssamdlq vklvndglma
      121 sydspespnv pqwaqyqkqa ygttfeplai vynkrlipen evpktraeli kllasqpdkf
      181 kgklttydve ksgvgfnalt qdahlnekvt welvkaigat gpklqsstga mmerissgen
      241 ligyniigsy ayakakkdks igyvfpkdyt qivsrlatis kkaknpnaar lwvdyllskr
      301 gqtmianqan lfairtdvtg etsaasltke lgdslkpiqi gtgllvyldq skrlaflkqw
      361 qqaiks
//
LOCUS       WP_175902779             260 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175902779
VERSION     WP_175902779.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..260
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=28412
     Region          28..233
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mtlqaqdava yangmielsh sfdanrflaa idrdelatla phlqlvhlns gqvlcepgem
       61 ltavylpvtt aislqyvssg gmtlevaeig sesvvcddvi ggsgrmpcra vacrdgfvyr
      121 ldrrvfaaaf daspvirhlv fvcvrllmaq vsqitfcsrh hvlkhqlcrw fllaydrtrs
      181 ieiqvthsml aqmlgvrret vtdaageiqk lglirqyrss ieladlagle kmscgcraiv
      241 rdemkrilsa dsgvpaasra
//
LOCUS       WP_175902794             809 aa            linear   BCT 11-JAN-2025
DEFINITION  right-handed parallel beta-helix repeat-containing protein
            [Burkholderia seminalis].
ACCESSION   WP_175902794
VERSION     WP_175902794.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 809)
  AUTHORS   Burnim,A.A., Dufault-Thompson,K. and Jiang,X.
  TITLE     The three-sided right-handed beta-helix is a versatile fold for
            glycan interactions
  JOURNAL   Glycobiology 34 (7) (2024)
   PUBMED   38767844
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12131601
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..809
                     /product="right-handed parallel beta-helix
                     repeat-containing protein"
                     /calculated_mol_wt=82600
     Region          <32..>88
                     /region_name="GH55-like"
                     /note="glycoside hydrolase family 55 (GH55) family domains
                     and similar proteins; cl49631"
                     /db_xref="CDD:483971"
     Region          100..281
                     /region_name="Beta_helix"
                     /note="Right handed beta helix region; pfam13229"
                     /db_xref="CDD:463811"
     Region          185..>611
                     /region_name="AidA"
                     /note="Autotransporter adhesin AidA [Cell
                     wall/membrane/envelope biogenesis, Intracellular
                     trafficking, secretion, and vesicular transport]; COG3468"
                     /db_xref="CDD:442691"
ORIGIN      
        1 mtaefpatyl vgsstgliar tllqelvdlp tsvrrfgvmg dgvtddtaal qvalnagipl
       61 yfppgtylys ntltatasii gagwnsilqc ttpqgqnsvi ywrnasnlki qnlqffskna
      121 tayypdenag sinlqdcsqf eisgckfnns agggalmrsc vngkvfdntl ldiwhdgihv
      181 tkasaditit nnevinggdd afavvgyfne gvrprritis nnrvvgtkya rgiaivgaqe
      241 itvtdnqiyk pmaagiyvas eltsvyqsyg ndnvtvanni ldtcgvqsni gaivnssngp
      301 igyaalavta tagfnnsnit ivnntiknsa gtpiglwqqa gsnihvnisq nsisnawdpn
      361 nkngfpltti satsssatln fannpgvavg mtawyfngst svqigtvlsa sgaavtlnkt
      421 atvpsggtvi fsgvglfgat iattaaalsa atsltfaatt gvtyndnygf gspgdettgv
      481 sigqgvsgtn iapgtfvtgv tansvtlskp tigavasgts ivftpmvcmt sqtittsaas
      541 aagtntltft pypsargcav gqgvsgtnip vgtyvtsvsg ngngptvtls nnftgsgias
      601 gasitftgtg glsavsgitl ystrgcivsk nqlsgiskdg iyvdgsctsf teisgnagen
      661 igccngfarl itvgtltaga llklrgnyma qpvnypraid slissasway tswsednlaq
      721 ngfvglgvql gpvtqtvsas pwtfangyps avsmsvsggt vlsinvsrng qqsyatgltn
      781 gmidlkpgda mtvtysaaps iamiprlgq
//
LOCUS       WP_175902817             314 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Burkholderia
            seminalis].
ACCESSION   WP_175902817
VERSION     WP_175902817.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..314
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33122
     Region          16..294
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mtplvppdai hdepaiaeri asamplmtpi hrrmgefvla npfraatmri delaqavnas
       61 iatanrfaka lgfdgypamr aalvrgfeat lgpverlrsa qeqepgvrga vwidavfdqa
      121 vanigstraq ldaadveaav eaivgarrvl ilgagssafl aglmehglsv chdsvqslal
      181 lggpshaarr lytadsrdlv ialafpryvk dtielarraa argarvlgis dgpqsplapi
      241 aslnlyvkae rrfaatseaa vltmiealid avalrthrsa ksaaemtefl lpwlmqpqaa
      301 lpavnpsspg pkks
//
LOCUS       WP_175902802             424 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia seminalis].
ACCESSION   WP_175902802
VERSION     WP_175902802.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..424
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41831
     Region          5..>331
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msshadspaa rhagsltifq gaalyigavl gtgvialpal aaevagpasl lawaalvvls
       61 gplaatfaal garypdsggv styarrafgp kaaaivgwcf yfavpagapa aamfggayva
      121 avtggghtti ivtaaaliat vsaanafgvt vsgrmqlvls allvtlllva vlasaphart
      181 anlqpfaphg wvavgqaaal lvwsfagwea ithlaaefrr pahdmprsag iavvvvgfly
      241 lsvaaasvmv lgpsagasga plaeliaggi gghaqvlaaa aallltlgtm nayfagaakl
      301 gaalgrdgal pawlaqgsqv ggvprrslgv iallaavala attlsdvgpk plvlvtsgcf
      361 vmvyglgaaa alkllprggi ayrcawvslv avaglflttg wyflcpllva gaallylqvt
      421 asrk
//
LOCUS       WP_175902823             282 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia seminalis].
ACCESSION   WP_175902823
VERSION     WP_175902823.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..282
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30239
     Region          52..146
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 metsrpneaq salwngpsgr awvdvqetid rmfepfetll adaeavssas nvldvgcgtg
       61 avtlaiarrl ganahctgid isarmidaar araersgvqa rfvradvqth afepagvdli
      121 vsrlgvmffd dpvrafanlr qaarpdarmr fvawrgaadn pfmttaeraa apllpnlpvr
      181 qpgvpgqfaf gdrqrivsvl adsgwadvei epvdracalp apaldeyiar lgpvglalle
      241 adeatrrrvv dtvcaafery vhgaevrfda acwlvtarap sa
//
LOCUS       WP_175902997             286 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia seminalis].
ACCESSION   WP_175902997
VERSION     WP_175902997.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..286
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30671
     Region          54..257
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mdasefskfl kaalpapala gaaltvaeve ipgyaqdivl rlyrrpdktg lpvvlyfhgg
       61 gfvrgsleda dfaarflaer lpalvvsvey slapafpfpa apedayraav waatrarafg
      121 gnpkkigvag hdaggqlanc lafiardrge vsivaqalfg pmldpsmtri gdaerlssdi
      181 tprecaacyr aylpqaaqrm hpyaaplesv rlaglpptlv vtaqndvlhv eaekyascli
      241 ssgvltqvir ypdithaala theaafeeav rffqcrfqar qpnrse
//
LOCUS       WP_175902873             376 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia seminalis].
ACCESSION   WP_175902873
VERSION     WP_175902873.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..376
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40902
     Region          183..376
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 msgfsvsrww smvtkellqi rrdrvtlgmi avlpivqlal fgfainsdpr hlptivladd
       61 tsefsrslva gmrntgyfdv qgglfseraa rdalqkgivq fvvsvphdfs rrlvrnehpe
      121 ilveadatdp aatgnaiaal ntmtqtvlnk dltgalvrta ppqafsarvh riynpagitq
      181 yniipglmgv ilsmtmvmmt slaitrerer gtienilasp atsievicgk ivpyvligll
      241 qctiillaar fvfsvpfegn pvtvycvasl livanlmvgi aissvarnql qamqmtffyf
      301 lpsvllsgfm fpfagmpgwa rllgnglplt yfnrairgvl lkgsgwneiw pdaaamvvfa
      361 lvamtvglla yrttld
//
LOCUS       WP_175903071             219 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia seminalis].
ACCESSION   WP_175903071
VERSION     WP_175903071.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..219
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24910
     Region          2..207
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mmptlyahpf ssycqkvlta lyengtpfey rllahddpkp mqeltalwpl krfpvlveag
       61 rtvieasiii eyldlnhpgp vrllpddpha alevrmmdrf fdnyvstpqq kvvhdalrre
      121 gerdargvad aramldtsya wldnkmadre waagdhfsla dcgaapflfy adwthridpa
      181 fanviayrkr llarpsfara vdearpfraf fplgapdrd
//
LOCUS       WP_175903026             462 aa            linear   BCT 11-JAN-2025
DEFINITION  NCS2 family permease [Burkholderia seminalis].
ACCESSION   WP_175903026
VERSION     WP_175903026.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..462
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46818
     Region          23..457
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 msdtpvqptv dvgaaktdfg tpgvidryfg iasrgstqrr eiiagvttfl amvysvfvvp
       61 gmfgkagfdt savfvavclt tafgsllmgl waklpiaigc aisltaftaf glvlgkglhp
      121 tvalgavflm glvftgisvt gvrswilrnl pagvahgtgi giglflllia sndvglvikn
      181 pgaglpvslg qitalpvims ivglaaifgl ekrrvpggil lvviaisifg lvfdpavkyh
      241 gifalpslsa pghesligam dikgalsmav lpsvlalvmt avfdatgtir avagqagqld
      301 engriinggr altadsissi fsgflggapa aayiessvgv aagaktglaa avvgllflvv
      361 mffsplaglv psyatapalm yvgllmlgsv sklhmddmvd amsglvcavf ivltanivtg
      421 imlgfstlvi grvasgefrk lnvgtvliaa vlvafylggw ai
//
LOCUS       WP_175903076             470 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Burkholderia seminalis].
ACCESSION   WP_175903076
VERSION     WP_175903076.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..470
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51901
     Region          5..446
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mdtalsaldl arlqfaftvs fhivfpalsi glasfiavle yrwlktgkqy yktlclfwsk
       61 ifavafgmgv vsgvvmsyqf gtnwsgfssf agavtgpllm yevmtaffle agflgimlfg
      121 wnrvsprahf gatlmvaigt listfwilas nswmqtpqgf eivdgrvvpt dwfaiifnps
      181 fpyrlfhmai aafivaalvv aatgawhllk grrdkgvkkm fsmalwlllv laplqavigd
      241 qhgintlkhq pakiaaiegl wetekggtal nlfgipdmka ettryavqvp hlgslilths
      301 wdgeirglka fppedrpnst vvfwsfrimv glgfamigla alawflrrrg rlyeskgfqr
      361 falvmgptgf vsllagwvtt eagrqpwvvy gvmrtaqavs plsvqqvsls mmtfvivyfl
      421 vfgtgvyyml klmkagpalp dvqhddtpdt rpdhtarrpm savdelietv
//
LOCUS       WP_175903098             255 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175903098
VERSION     WP_175903098.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..255
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27374
     Region          6..244
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 msgnvvksaa rvfevlelfs alqrplsvre iatrcgypgs saaalltsmr algylaydda
       61 thayaptarl vnlgealids aagsrrhwha vakrlaarth eavviavqsd lyvqyidave
      121 gahsipvqfy apigtrreic msglgwalls lqpdsairrl vsrsirrigk sgrtidedvv
      181 ldkveqtrrl gysysantvt qgaamismvi adgwnglpla mgvagpveri darrdaivra
      241 mrdtldaqrp daaag
//
LOCUS       WP_175903102             350 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia seminalis].
ACCESSION   WP_175903102
VERSION     WP_175903102.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..350
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=36916
     Region          4..350
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mqrkalviga cvlcatsaha ssvtlygivd syvefdrigs lssmrqsggg sstsrfgltg
       61 vedlgggast kfvlesgfsp adgsfqggtl fyrqayvslq htrygdlrlg rqytpafyvv
      121 ydgdpfglne rlsplallat stdtitsntt ppiprfnqaa sylspdwngl rvmatygfpt
      181 pnalstqagr nygaglqyrl gglylgagfq gdtsagnpap vvspsttrhy vfaanyafar
      241 vklyaaflyg vgtaphlpaf stasagasin vgaldrllvs vvrrdvkgss ndatalgvgy
      301 dhplskrtsl yarylymkng gdarntvvvg llpqpggteq vfalgivhrf
//
LOCUS       WP_175903120             536 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Burkholderia seminalis].
ACCESSION   WP_175903120
VERSION     WP_175903120.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 536)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..536
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=55965
     Region          46..152
                     /region_name="SoxW"
                     /note="Thioredoxin-related protein SoxW [Posttranslational
                     modification, protein turnover, chaperones]; COG2143"
                     /db_xref="CDD:441746"
ORIGIN      
        1 mktalrnlta aclfaaaaga afaaatpsga paasvspdga hlppgiawqh gdvdaafala
       61 krtgkpllly wgavwcpscn qvkstifsqq afktrssffv pvyldgdtes aqklgerfkv
      121 hgyptmilfr pdgtevtrlp geadldrymq alslgmtaah pvrqtlatal kngasltpde
      181 wrlladyswd tdgalpvpad rvaetlqsla qraraagaka eaarfalksa vvaasddpaq
      241 agaldkaala dslrtvlhdp alsradsdvl vaaparvvay lgsgsgggda qraklrgayd
      301 talarlstdt tlssidrlma lhgrvllarg darkgaplda paladtarkq iaasvqgaan
      361 ayerqalvse gadtltdagl ydesdallka elprsstpyy fmsglaanak argdkaaald
      421 wyrkaydaas gpatklrwga tyfanavela pddsariegi aanvlaqadk trdafyganl
      481 raltkivtql nrwraggahd asvrsvvkqf dgvcgklpag dpqatacakl iqpvka
//
LOCUS       WP_175903174             158 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Burkholderia seminalis].
ACCESSION   WP_175903174
VERSION     WP_175903174.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..158
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=17025
     Region          5..153
                     /region_name="OsmC"
                     /note="Organic hydroperoxide reductase OsmC/OhrA [Defense
                     mechanisms]; COG1764"
                     /db_xref="CDD:441370"
ORIGIN      
        1 maagehkyrv avewtgnrgt gtsgyreygr dhviragskp dipgssdpaf rgdasrwnpe
       61 dlllgsasac hklwylhlcs eagirvlaya dnaegtmldg agegrfteiv lrphvtirag
      121 ddrelaghlh hdahakcyia nsvnfpirce pviafaaa
//
LOCUS       WP_175903175             213 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175903175
VERSION     WP_175903175.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..213
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23847
     Region          7..213
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 meakldstad avaaslrdmi ingelsager lverdlaerf gisripmrea iqrleregll
       61 difrnrgavv rmlsasdvqe iydlrvlleg daiyrsvkrl ddetlarael vhrllgdasv
      121 prrqgelnre fhallyagcg narqlksiae lrsqveryer lqttlladtp sfqveheail
      181 racrerdara aravtvahle sarsivmrlv ega
//
LOCUS       WP_175903236             249 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Burkholderia
            seminalis].
ACCESSION   WP_175903236
VERSION     WP_175903236.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..249
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27326
     Region          3..241
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mplvetrgle knfgthhvlk gidfsvergq vvsivgrsgs gkstllrtln glesidagti
       61 svdgervdar hadlralrlk vgmvfqqynl fphlsagqnv mlaqsvvkka hrqqaraiae
      121 lmlervglgd kfdafpeqls ggqqqrvaia ralamkpsvl lcdeitsald pelvgevlgv
      181 veqlaredmt limvthemnf aravsdrivf mhqgrvwetg taeeiferpq tveltrflgs
      241 vrnteavar
//
LOCUS       WP_175903243             216 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia seminalis].
ACCESSION   WP_175903243
VERSION     WP_175903243.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..216
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22789
     Region          7..195
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mslhypllfa ylaaiallia tpgpvvmlvt gtvarrgfrq gmltavgana aslvmiagam
       61 lmvfgvvlvs drlldglhvt gcvfiavlai rsllgewraa rrrggdgnvr aepvlqprgl
      121 pgfvrgflvg ianpkdllff vaffpqfvai tpdsrvslai laalwiavdf tiltgymaai
      181 nhplfhrkqr witagsafal laialaglag tiarva
//
LOCUS       WP_175903069             212 aa            linear   BCT 11-JAN-2025
DEFINITION  2-hydroxychromene-2-carboxylate isomerase [Burkholderia seminalis].
ACCESSION   WP_175903069
VERSION     WP_175903069.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Thompson,L.C., Ladner,J.E., Codreanu,S.G., Harp,J., Gilliland,G.L.
            and Armstrong,R.N.
  TITLE     2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class
            glutathione transferase from Pseudomonas putida
  JOURNAL   Biochemistry 46 (23), 6710-6722 (2007)
   PUBMED   17508726
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122490
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..212
                     /product="2-hydroxychromene-2-carboxylate isomerase"
                     /EC_number="5.99.1.4"
                     /GO_function="GO:0018845 - 2-hydroxychromene-2-carboxylate
                     isomerase activity [Evidence IEA]"
                     /GO_function="GO:0043295 - glutathione binding [Evidence
                     IEA]"
                     /GO_process="GO:1901170 - naphthalene catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23418
     Region          9..188
                     /region_name="DsbA_HCCA_Iso"
                     /note="DsbA family, 2-hydroxychromene-2-carboxylate (HCCA)
                     isomerase subfamily; HCCA isomerase is a glutathione (GSH)
                     dependent enzyme involved in the naphthalene catabolic
                     pathway. It converts HCCA, a hemiketal formed
                     spontaneously after ring cleavage of 1; cd03022"
                     /db_xref="CDD:239320"
     Site            15
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239320"
ORIGIN      
        1 msaarpaawy fdfvspfayl qqeqfdrlpp aaafeprpiv lgallthwgq kapaeiaakr
       61 iftyrhaqyr adklgiafrm ppahpfnpir plrlaiamgs srdairrifr hiwrdghdvs
      121 tpdgfaalce avgfpegvta veaqpvkdal rantdralad gvfgvptfvl dgdlfwgeda
      181 tdmfvdcats rawldspevr risalpegir rg
//
LOCUS       WP_175903263             401 aa            linear   BCT 11-JAN-2025
DEFINITION  zinc-dependent alcohol dehydrogenase [Burkholderia seminalis].
ACCESSION   WP_175903263
VERSION     WP_175903263.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..401
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41813
     Region          1..401
                     /region_name="FDH_like_1"
                     /note="Glutathione-dependent formaldehyde dehydrogenase
                     related proteins, child 1; cd08283"
                     /db_xref="CDD:176243"
     Site            order(38..40,43,86,162,166,185..186,188..190,209..211,215,
                     229,253..255,303,320..322,345..347,387)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176243"
     Site            order(38,40,60,162)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
     Site            order(90..91,93,96,104)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
ORIGIN      
        1 mkavvfhgig diridtvpdp evsaatdavv rltasaicgt dlhmvrgtlg gmkpgtilgh
       61 egvgiveavg rdvrnlrhgd rvlipskiac gscaycragy taqcdvanpg gpragtaffg
      121 gpadtgafdg lqaeyartpl ahaslirlpd aidddrailm sdifptgyfg aqlaevkpgd
      181 tvavfgagpv gqfaiasakl mgagrviavd riasrlemac aqgaeivdfs eddpvdtvlr
      241 ltggigvdrv idavgvdamr athgpaaadr daarafdaev eaiaphrhpd grnwvpgdgp
      301 sqvlqwavra vakagtiavi gvyppaarvf pvgdamnrnl tikmgncnhr tvtpplvelv
      361 rsgafdplsv ltrcepltna idayrafdvr epgwmkvklt p
//
LOCUS       WP_175903271             400 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia seminalis].
ACCESSION   WP_175903271
VERSION     WP_175903271.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..400
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43073
     Region          5..345
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mnaawhrarr ilcvrldslg dvlmttpalr alkeggsgrr ltlltsrtga alaphlpmvd
       61 dvwcydapwv rhpdvrgdpv adldmidrll agrfdaavif tvysqnplpa ammcwlagip
      121 lrlahcrenp yelltdrvpe tepdahvrhe varqlalvra vgattsdwrm afepgdaarr
      181 avharlraal qriggprrpe agrgrwlvvh pgasaasrrw paerfgeaaa avaplfdgia
      241 vtgsageral idavceragp ravplagalp lgelgaliet adlllsnnsg pvhlaaalgt
      301 pvvdlyaltn pqhtpwrvph rvlnvdvpcr ncyrstcnqp ghpcllgvrv ddvvaavhtl
      361 lrdrarhaqr taaraaarga epvampasnv ipfahvitrn
//
LOCUS       WP_175903274             362 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia seminalis].
ACCESSION   WP_175903274
VERSION     WP_175903274.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..362
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38617
     Region          15..356
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mmldhgfdag sargprriav fralqlgdml cavpalralr hgepdaritl iglpwarefa
       61 srfsdyidgf iafpgapgla eqpepdaaar eafvaecrsr dfdlaiqlhg sgahtnaiva
      121 slgamrtagf vpadggttal dcalawrdde pevtrylalt rmlgyadrgd hlefplggld
      181 halwqvlsde haldpgryvi vhpgarmasr rwpverfala arrladdgwq vvltgtraem
      241 alagafaerl arpcvnlcgr tplgalaali ararlllcnd tgvshiaaal gtpsvvvacg
      301 sdtarwapld garhrvlany pacrpcmfdt cpyghecata igvgdvigqa gdllaeerrh
      361 vt
//
LOCUS       WP_175903358             277 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175903358
VERSION     WP_175903358.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033773
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..277
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30911
     Region          21..>124
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          192..267
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 magkaavtss dwmmrakple gverieawfh dkayalhrhd tyaigrtlag vqsfnyrrsq
       61 raslpgntiv lhpdeahdgq agtsegfryr miyvepalfq evlggralpf ieggvttdpr
      121 laaatetllq hvgytleple qsdalaelar aladvarvpr ipekgdyvaa rrardylhan
      181 ctrvvtleev eaetgrdrws lshdfrtfyg tspyryltmr rldtvrrmll agislataaa
      241 dagfadqshm trhflktfgl tpgrwlqiad rtatiqf
//
LOCUS       WP_175903372             475 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia seminalis].
ACCESSION   WP_175903372
VERSION     WP_175903372.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..475
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50764
     Region          61..468
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mmkrsvavvl tavalaaalp asaqmldvyr trddvaatpa gsmasatacg alrlddrpla
       61 ledaillaic shpqlrrtwa daraataevg vskaaylptl natagiqrdn vnttytggfs
      121 gdqrstsryg mlnlswvlfd fgkrganldr arallraana ahddalqsvf fdaaqafyal
      181 rdaqaaleaa qavehaaqes laeasarhdg gagtlgdalq aqttyrkall drvsaegdlq
      241 naigtlattl gadadtplri adaepspdrd dftrgvanli aeakrdhpkl iaarerleaa
      301 rdqiravraq slptisltgs lsrnnpsyqq qpslfqlqss hsnsigiqis iplfegfasg
      361 yriaeakaqa daqeadvrnt elkvsldvwk syqslqtdtt nldnsqhlld talhsldiar
      421 grykagvgtf tellnaqsal adarrqrvla vsrwrtarlk laeslgrlgl wndas
//
LOCUS       WP_175903383             258 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175903383
VERSION     WP_175903383.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..258
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=28330
     Region          21..221
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mihqadnvie lphalganqf lsaldaisra elaphlmlsn lktgqvlcea genleavyfp
       61 vtagislqyt tggkttlgvt etgregivcd dvigstmqrr vvvyhggfay rlhahrfada
      121 cdasaairrq vfvqmqlvla qasqvmfcsr hhvmrhqvgr wlliayersr sieipvthgt
      181 lgqmlgvrre titdtvrqlh elglihqhrg aivltdlarl egqgcdchrv irdetrrila
      241 idagtqagag lsrrlrtt
//
LOCUS       WP_175903388             323 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175903388
VERSION     WP_175903388.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..323
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34620
     Region          13..80
                     /region_name="HTH_MlrA-CarA"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators MlrA and CarA; cd01104"
                     /db_xref="CDD:133379"
     Site            order(14..16,30,47..49)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133379"
ORIGIN      
        1 msprkdretp hryrsgeaar larmpaatlr iwerrygvva ppktpsgqrl ysdddvqrir
       61 llkalvnqgh aigsiaglsr eelealsltn trsaalpene vslavigalp vsasalermg
      121 iriaariasi ddasehvsts aealiastts lheevvaqia aaaqkldara vavvyafgta
      181 eaielarlsg felfrstesq tnpasimskl araavtarqs neadrglwlr trrrfdeatl
      241 aslsglsttv kcecprhlse limqlsafer ysdecvsrsp adallhrhlg daanraaell
      301 esalavilre eglggptpdp gap
//
LOCUS       WP_175903417             198 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia seminalis].
ACCESSION   WP_175903417
VERSION     WP_175903417.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14388723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..198
                     /product="cupin domain-containing protein"
                     /calculated_mol_wt=20728
     Region          39..176
                     /region_name="cupin_BLL6423-like"
                     /note="Bradyrhizobium japonicum BLL6423 and related
                     proteins, cupin domain; cd02231"
                     /db_xref="CDD:380359"
ORIGIN      
        1 mnfpvirrvv tghdadgrav vasdgplptv veiaaipgtv fhevwstsss parvdngadp
       61 tlaalmlppp khgtrmrfvd ippdtpefla hgavkmhhaf sqigdaaast vkagsphplm
      121 hrtesidygv viegemslil ddaevalapg svviqrgtnh awanrsgrpc rmlfvlidga
      181 ydpaiaavld tpahggar
//
LOCUS       WP_175903424             264 aa            linear   BCT 11-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Burkholderia seminalis].
ACCESSION   WP_175903424
VERSION     WP_175903424.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..264
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29227
     Region          91..246
                     /region_name="CE4_NodB_like_5s_6s"
                     /note="Putative catalytic NodB homology domain of PgaB,
                     IcaB, and similar proteins which consist of a deformed
                     (beta/alpha)8 barrel fold with 5- or 6-strands; cd10918"
                     /db_xref="CDD:213023"
     Site            order(97..98,153,157,201..203)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213023"
ORIGIN      
        1 mavrpiacll llscvsavss tdvatvdsps prvlilvyhr faatrvdsmt vrtdtfrhql
       61 qaidangyri vpladvvrwh ggqadavpar avaitvddgh rsvydvlrpl laarpmpvtl
      121 fiypsaisna syamtwdqlr tlgqaagfdi eshtywhpnf hterarltpd dyrrfvsfql
      181 srsrdrlese tgkpvrllaw pfgvhdaqtd qlaaregyva aftldarpvr vadpamalpr
      241 ylmtddcdtr cmngllrtag gsrd
//
LOCUS       WP_175903445             277 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia seminalis].
ACCESSION   WP_175903445
VERSION     WP_175903445.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..277
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30387
     Region          3..142
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          153..275
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 msyktllvhl ddsercatrv dlaldlagrw nahliglyvv cqdlleplrr pdeplklavy
       61 erlcdqrrkd aeerfltaae ragrsvewqa pageptaaai lharhadllv lgqedpddrm
      121 tyvarhfved vvmgsgrpal vvpyagdvrt lgenvligwd ggreaarvma dalpllarar
      181 fvnvetvvrg qpdpdrtpag vdvaaylerh gvrasfsttp rdrsvgvgat llnrvtdlha
      241 dllvmglysh trahervlgg atrtilqtmt vpvllsh
//
LOCUS       WP_175903458             157 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia seminalis].
ACCESSION   WP_175903458
VERSION     WP_175903458.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..157
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16746
     Region          1..144
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 myttimvatd gsptanqald aglrmakvcg arlfavfvvd ksallacrgr iepeamldei
       61 rrhgaailhd adrtiaraav ngetdlvetd fgqdvaerlq ryvvdhsidl avvgthgrrg
      121 vrrlvlgsva erflrasrcp vllvrgedaa hatvaaa
//
LOCUS       WP_175903469             295 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            seminalis].
ACCESSION   WP_175903469
VERSION     WP_175903469.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..295
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30294
     Region          2..290
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mssfivhllt vtclyatmal glnlqagyag lvnfgfvafa glgayaagia sqlgwplpaa
       61 lalaagtasv lavaiarlgr hlsadywgia tlaiaeilrt falnegwltg gaqgiggiap
      121 lfprlrapwa dlaflavaag glavayaacr llttgrfgra lkvmreepal avcfgydpva
      181 lktwasvaga lpaafagall twyisyvgpd amvasetfal wtivmvgglg shagvlagal
      241 ivqavyafap flkdwlgvgs dlagavrlgl vglmllacvl wrprglvper levhp
//
LOCUS       WP_175903479             272 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia seminalis].
ACCESSION   WP_175903479
VERSION     WP_175903479.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..272
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28911
     Region          17..262
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 msttasaasa rtaahidtpl ldlritrkqy gdrtiladia lqvargeivc vvgpsgcgks
       61 tllrivagld thfrgnaqld gvalagpsar vgvifqeprl lpwlsiadnv gfasgphggr
      121 dpsvtrllde vglagvarql patlsggmaq raaiarglfg epdlllldep fsavdaitrm
      181 rlqtllldvv hrhrmaaivv thdldealyl gdrvlmlapn pgrvddeirv dlarprdrrd
      241 pslaalrarl lgafqrfhdh addagsgtir gl
//
LOCUS       WP_175903483             729 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia seminalis].
ACCESSION   WP_175903483
VERSION     WP_175903483.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..729
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78242
     Region          18..729
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mrtqtgairr tmtivaggtl caavaggaha qasgtaaaka daatavlpai dvqgaadaas
       61 aglvgqrtta gtktdtpvae ipqtvnivta rqiemtgaad lnqvlryvpg fstfgadsrt
      121 dwyaalrgft ptlyvdgaaa pntavianwr vdpytidsia ilrgptsvly gagepgaivd
      181 ahtkradger vreagvqign darkqvmldv gdaldpdgky ayrfvgvgrd gngvtgpnge
      241 rrvalapsfr wrpdadtslt vaatflqdsg dissnflpas gtvlpnpngr lsqdiymgdp
      301 sfndyrkkqw slgytlehrv naiwtlhqdv rwshlsldda tvfgngfapr sttsmmrfag
      361 lfqlnysrld vdhhaqarfg tgplehtllf glqfdrqttt nsvwlalaps ldlyhpvyrp
      421 vtaaifagpt slghvdqyta mnalgvyaqd qirwrrwtlt lggredvvna rfddrtagtq
      481 arqdvsafsg rvgltyqgda glspyvsyst sfdpvvgvrm fggglpkptr gaqteaglrw
      541 qspgrnlmls aavyridqtn vvtptpvnld ptgttsvqtg kvrsrgiels avgkvtrels
      601 ivasyayqdv knvqandasl nhwpvsvplp rqmasmwadw twrtgalsgl gigggvryqs
      661 asagapdnsl tvpsatlydl alhydlphwr falnvanlfd rryvsgcqsy avcvfgnert
      721 vlasakydw
//
LOCUS       WP_175903485             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175903485
VERSION     WP_175903485.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33444
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,219..224,
                     230..231,233..234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mklsfealea ldaidrtgtf aeaaellhrv pssltylvqk lesdlgvvlf drsgrraklt
       61 hagrivveeg rrllraaeql eikaqraqqg wetevrvcid eilpfdalwp yvhrfyalgm
      121 dtrlrlstev lggawdalis rradlvvgaa gdppelpgiv arpigslrhv favapthpla
      181 alpeplpmgs vvqyrgavis dtsrelqpqs vaidagqpyl avptlaakld aqceglavgt
      241 lpeciaarai adgrlvarqv tgmrdtthcy lawrgdeagr alhwwveqld rpdlverfta
      301 pdkspr
//
LOCUS       WP_175903488             137 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia seminalis].
ACCESSION   WP_175903488
VERSION     WP_175903488.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..137
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14874
     Region          8..137
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mkpahsdlsr ptvdlgllfl rvaasllliv vhglpkvihy taeaaaiedp fhlgrtlsil
       61 faifaevvcp vfmivgvwtr laalpvlivt lvalvfvhpd wslrdgqfaw mllilfgtia
      121 iagagryalp avvrrqr
//
LOCUS       WP_175903502             370 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia seminalis].
ACCESSION   WP_175903502
VERSION     WP_175903502.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..370
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39090
     Region          4..344
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,233,300,320,322..324)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,181,184,186,233,240,300,320,
                     322..323)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,181,184,186,323)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            186
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mssllapydl rglalpnrvv mgpmtrsrap srglptelma eyyaqrasag livteatnvs
       61 aasaafeltp glvddaqaag wkkitdavha nggrifaqlw hggrvssltl lggaaplsps
      121 gvnddleqlq vwaqlqngyy tkihatpsra mttaevvdav defrraaara meagfdgvei
      181 haangylphq flsstlnrrd dryggsvanr arfleeivaa vggvmplarv gvrvspyaky
      241 nnvrdadpda tlayvgrmld eagvaylhaa dtngwsgepd lpriveharr sfggtlivng
      301 giapdaaqal idagdadlva farayianpd lveriaarap laepksagwy ggdragyvdy
      361 arydaagaha
//
LOCUS       WP_175903509             317 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia seminalis].
ACCESSION   WP_175903509
VERSION     WP_175903509.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..317
                     /product="VOC family protein"
                     /calculated_mol_wt=34144
     Region          <241..301
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 mnalnlrqvl rmtaastavl aallaaapsr adethlddta rqtaaarspn vsvgpqydtt
       61 hvcvapedfd rftdsfvatf ggkkskqgvf qvtptpsqtm sqlvltpvgt isvfgfktpi
      121 pypfcaertg ylvtdldvam ksarahgadv vvdtfpdpig rdaivrwpgg vnmqlywhne
      181 pphydalqtv penrvyvspq sasklahdfv afshgkivsd vrrapgieig rpndtyrrir
      241 iesgfgkmtv latdghlpyp fgremtgyev adlaatlkqa eaagvtvlvp pftsdgrdaa
      301 lvqfpggyva eiharsk
//
LOCUS       WP_175903560             304 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175903560
VERSION     WP_175903560.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32813
     Region          15..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..293
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(113..114,116..117,120,124,126..132,226..231,
                     237..238,240..241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 maafpterlk givpfvcaad aggftaaaer lnltssavsk svarlerrlg valferttrs
       61 laltdagraf hetctrilae laeaeavlaa qkreptgtvr ialpasfgrl cvvpvlsrfs
      121 aqypdvrphl lfadrfvdla eegvdlavri ggpqdlpssl grrflgrerl ifcaapayie
      181 ksgmpqtidd lhehacvvyg rpdgtqspwl yaradgqvgq cvvrprivag daeaqlafvr
      241 aglgiaqlat wlveddlkag rlvnildeaa tdglllsllw pvarqltpkv hvlaqmleah
      301 lyir
//
LOCUS       WP_175903592             197 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia seminalis].
ACCESSION   WP_175903592
VERSION     WP_175903592.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..197
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=19251
     Region          1..197
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mkkiammmsa aglafaamna ahaadgtinf tgeivaascd itggngtsvt ggkgaqsidv
       61 klgkvstdtl sstagggiaa gtainlvldc gstakglttv kvrfdpaggs gvdssnnkll
      121 kttgtatgvg igifntagtl lnlnanetfd aplvkggtea vptytanlal ragyvkngve
      181 iiagtangtl pftltye
//
LOCUS       WP_175903594             835 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia
            seminalis].
ACCESSION   WP_175903594
VERSION     WP_175903594.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 835)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 835)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..835
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=90183
     Region          20..825
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 menvrkevdi wtaahigapc laliglvlpa hghavefnes flrkgegpve lsyfekgsav
       61 spgrydvdvy lnhtlakrqg vtfragadgt vkpmvtlgll rtagvniarl ekdgriaaga
      121 ddetivdlpa vadgasvefe sntlslnisf pqfyvsrtsr gyvdqslwdd gipalytdyq
      181 anysrndggg ygnesyfvgl rsgfnaggwr frnestftgt kgtkgrftsn rtyverdirr
      241 lrskvaagel ytsgdifdsv rfvgaqvgtd lgmlpdsevg fapvvrgiae snavvevrqn
      301 gyviystpvp pgafeitdiy psgsngdlei riteadgrvr rftqpysylp vmvrrgslry
      361 afsagqyrvq gqsspkftqg tlvygmsdnf tgyggiiaae nyvaaalgig vntriggmsl
      421 dvttsrsrts sgarqgqslr flysktlhst nttftmvgyr ystdgyrtls qhvedtdrsy
      481 gpriarqksr ldvnvnqplg sgsmfagvgd ttywngeghs rrlqvgysns yknisysvsa
      541 shiqesgpfg rpdtqfnvsv siplgkasss hrlyanavss trgefnmqag asgylndsnt
      601 vnygvqtgys rsgggsggvs agwdtpnakl tgnftqdrsg rhfdagasgs vvvhgggitl
      661 gqplgetfav vevpkvrdvt fggtstvrtd rrgyavvpyl qpyrqnwlni dpssigthte
      721 itdnaksvvp trgaivrtrf eaesgrrvqf elgqegggkv pfgaqaydak gkllgmvdnq
      781 srllvfgied kgsidvrwge nnckvsyqlp tqnkelayer qaamcmragt vvglk
//
LOCUS       WP_175903596             346 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia seminalis].
ACCESSION   WP_175903596
VERSION     WP_175903596.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..346
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=36425
     Region          194..346
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 maylrkklrw lqaaivagsl iwsgtalgyc lnngdwagrt fnvtfpatmn vaaapvggvl
       61 araevtytna atgwstacwd sqaklsitvp dgqlvpgykg vyktsvegig vrfvfvavgn
      121 engdippmty psgstitggg apvvhpphmv rvelvrtakn vgpggtvsla fnalfdadkd
      181 lsgnilrryi ngkgttqvtn niyfggcqtt tpvtnvrmgk eiieriksgr aaehpfslev
      241 acgtnkpgnp lpvkvyfegd neaegllrls grgtpgvasg igialtsdkg vklpfikana
      301 ltmdwnrssp egevyrftgk aryapttgai tvgsgnatln fvieyn
//
LOCUS       WP_175903609             203 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            seminalis].
ACCESSION   WP_175903609
VERSION     WP_175903609.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..203
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22146
     Region          13..177
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msptspgsrd rgrprefdtd evidaaarvf waqgyhatsi dtlceatgvf rgslyrtfgd
       61 khgllvaafd ryaegaiarl kerlaadlpp rqalrqallh yteigvrlse rrgclitnsa
      121 vellpgddvl rpyiestllr igtqlslava rgqqsgdfdr nldpeevgrf llcliqgmrv
      181 lgkssaseae lasivdiamr alt
//
LOCUS       WP_175903646             309 aa            linear   BCT 11-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Burkholderia
            seminalis].
ACCESSION   WP_175903646
VERSION     WP_175903646.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..309
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33967
     Region          44..299
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mfyltspdvr eaevftrmpe kfrkpdvrte waranrggmv tdsflegpvw dpagylfvtd
       61 iphgrifris psgdwdlvae yggepngmkr fdashliitd yrnglmlldi ergevrpyle
      121 rrnterfkgv ndltfdsagn lyftdqgqtg lhdptgrvyr lspdgkldml ldtcpspngl
      181 vlsrdekvlf vamtrgnavw rmplqadgsv tkvsqfftsy gpsgpdgltv dldghlfvan
      241 pglgrvwvln hcaepveilt gpkgasltsv cfggpdmktl fiteatsgsi lkadmtvagp
      301 lpkqaaqqd
//
LOCUS       WP_175903652             440 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia seminalis].
ACCESSION   WP_175903652
VERSION     WP_175903652.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..440
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47775
     Region          21..424
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,152,
                     155..156,159,256,259..260,263..265,268,295,299,349..350,
                     354,358,374,377..378,381..382,386)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mqtgfmetse ierrtirkvv wrlipflmic yllafidrgn vgmaslqmnh dlgmsatvfg
       61 fgsslffisy fffevpsnla lqkygariwi arimitwgia saatalvhna ttfyvlrfll
      121 gaaeagffpg vllylsywip aqyrarivat fmvaipaasf igspisalll qmdgvwglrg
      181 whwlfilegi ptvllgfacl fmltnkpena kwlddderaw lsgalaaghk trkkvpslpl
      241 tqlfrnryvl clalvdtcas aagstlsvwq pqllksfglt vmqtgllnsv pyavasvlmv
      301 ywgrrsdrvg errwhtavpm lligvglfat slsgsllptv cmlcavlvga ysfkgpfwal
      361 atdmlsnstv aaglatvnai anllggglmv nvygwvkaat gsyalalmpl ailtlvsvat
      421 lllltrnhaa gklvgktgti
//
LOCUS       WP_175903663             249 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia seminalis].
ACCESSION   WP_175903663
VERSION     WP_175903663.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..249
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26022
     Region          2..234
                     /region_name="17beta-HSD-like_SDR_c"
                     /note="17beta hydroxysteroid dehydrogenase-like, classical
                     (c) SDRs; cd05374"
                     /db_xref="CDD:187632"
     Site            order(8,10..13,33,51..53,75..78,98,125..127,140,144,173,
                     175..177)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187632"
     Site            order(99,127,140,144)
                     /site_type="active"
                     /db_xref="CDD:187632"
     Site            order(127..129,134,140,171..172,178,194,197)
                     /site_type="other"
                     /note="steroid binding site"
                     /db_xref="CDD:187632"
ORIGIN      
        1 mktvlitgcs sgfgleiarh flardwrvva tmrtpredvl ppsanlrvlp ldvtdavsir
       61 gaidaagpid vlvnnagfga aapaeltpld tvralfetnt igtialtqav lpqfrergag
      121 vvvnvtssvt lkalplvsay raskaavnaf tesmavelap fgvrthlvlp grapdtrfgd
      181 naranmhgfe heayaefvgk avarmldatg pithaqdvae avwraatdps splhmpagad
      241 ahawaaqag
//
LOCUS       WP_175903672             437 aa            linear   BCT 11-JAN-2025
DEFINITION  leucine-rich repeat-containing protein kinase family protein
            [Burkholderia seminalis].
ACCESSION   WP_175903672
VERSION     WP_175903672.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Shen,K., Hines,A.C., Schwarzer,D., Pickin,K.A. and Cole,P.A.
  TITLE     Protein kinase structure and function analysis with chemical tools
  JOURNAL   Biochim Biophys Acta 1754 (1-2), 65-78 (2005)
   PUBMED   16213197
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   5  (residues 1 to 437)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   6  (residues 1 to 437)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
REFERENCE   7  (residues 1 to 437)
  AUTHORS   Hanks,S.K. and Hunter,T.
  TITLE     Protein kinases 6. The eukaryotic protein kinase superfamily:
            kinase (catalytic) domain structure and classification
  JOURNAL   FASEB J 9 (8), 576-596 (1995)
   PUBMED   7768349
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..437
                     /product="leucine-rich repeat-containing protein kinase
                     family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=46393
     Region          <2..>186
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          39..61
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          62..84
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          85..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..175
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          211..>379
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(214..217,220,222,238,240,269,287..290,345,349..350,
                     352,362..363)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Region          <323..437
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
ORIGIN      
        1 mthtleqlqa gqlsgarqlk lacgltefpr eifdladtle vldltgnals alpddlprlh
       61 rlrilfasgn rftafpdvlg acgqldmigf kanrirtvpr galpralrwl iltdnaidal
      121 padigdcsrl qklmlagnrl ralpadmaac ralelvrlsa nrlealpdwl lrlprlawla
      181 tagnpfgaap eaaasagpdv aeidwaslsc erklgegasg viyraqwrve ghparavavk
      241 lfkgavtsdg lpdcemaacl hagrhpdlip vigkvsghpd gthglvmelv dpalanlagp
      301 psfasctrdv yaadarfala eavriahgia svaghlharg imhgdlyahn ilhdgaggal
      361 lgdfgaasly dvndrtragr ferievrafg yllgellerc gsrsdaldal aaaclneevd
      421 arpsfgeiaa vlaafmr
//
LOCUS       WP_175903720             286 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Burkholderia
            seminalis].
ACCESSION   WP_175903720
VERSION     WP_175903720.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..286
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30544
     Region          4..283
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 maanfdelas riraqfsels pqfqagaafl ldhpdevats smrkvaqraq vqpaslvrla
       61 qqfgfpgwne lrdlcvarvr trpepltqra rslvrpdaka slahdllaaq qhnlsataaq
      121 nehaladaar lirkashvhv agfrscypva fgfvygyrlf rptvsllngv agslemelrt
      181 iakqsvtvvv sfapysaeat rvaqaakeqg skivaitdsa vapialhada qlifthdsps
      241 ffpslvaaha maealvaqll alegsdaiaa lerteaalha kgayvv
//
LOCUS       WP_175903722             555 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia seminalis].
ACCESSION   WP_175903722
VERSION     WP_175903722.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Kane,E.I. and Spratt,D.E.
  TITLE     Structural Insights into Ankyrin Repeat-Containing Proteins and
            Their Influence in Ubiquitylation
  JOURNAL   Int J Mol Sci 22 (2), 609 (2021)
   PUBMED   33435370
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Mosavi,L.K., Cammett,T.J., Desrosiers,D.C. and Peng,Z.Y.
  TITLE     The ankyrin repeat as molecular architecture for protein
            recognition
  JOURNAL   Protein Sci 13 (6), 1435-1448 (2004)
   PUBMED   15152081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19763717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..555
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=57946
     Region          139..399
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          412..466
                     /region_name="Ank_4"
                     /note="Ankyrin repeats (many copies); pfam13637"
                     /db_xref="CDD:372654"
ORIGIN      
        1 mnklppnahp dhlkkqakal lrlyrqgdad avarfvrslp aaanrthdet ralglrlhda
       61 qsciareygf aswadlgafv ethaltrqpr pvlvrrwldl ayggdvtggv aaprprvaah
      121 llldhpdlvs adpaiacaag dldavkaala adpgwierag galklpplva vthsrlgqip
      181 afavrlraca rhlldagadp nqrignrfpp aslaepdesa plsalygaag vnrdpaltam
      241 lleagadpnd geslyhslen pactrvlleh gaqvggtnal rrafdmrdaa alelllahgg
      301 daneppgagl aqtwgapllr aigvrcsarh vaallaagad practpagvs ayrlamqagl
      361 tdvaallraa gaeealgpdd afvaacarad adtarrirar hpelpgaltg drlrqlpdaa
      421 awgsrdavkv mvelgwpiav rggdwdasal nhavfrgdad llafllahga swreqhgfgs
      481 dalgtlswas vnepegvdvp dweacarvli ahgvpqavrd pshpdavlid grtmrfseav
      541 advllgidgg paast
//
LOCUS       WP_175903758             209 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            seminalis].
ACCESSION   WP_175903758
VERSION     WP_175903758.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..209
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22277
     Region          18..172
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msgtssrtal sprkaprqrr saatvdaive aaarilerdg fdgyttnava alagvsigsl
       61 yqyfpnrdal taalveresa hllddvdraa alsscddvlr tlvrgavahq mrrpvlarli
      121 dfeearlplg araarvadri hatllhalgl rdaprviapd vvahdllaiv kgivdaagar
      181 getdaaalet rawravrgyl resreskla
//
LOCUS       WP_175903795             319 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175903795
VERSION     WP_175903795.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18598969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..319
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35407
     Region          1..283
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          15..97
                     /region_name="cupin_MtlR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to MtlR, N-terminal cupin domain; cd06976"
                     /db_xref="CDD:380381"
ORIGIN      
        1 mmhpdlevvd vrrdesfkvw shgypyrtir whfhpefelh livathgkyf vgdhigsfgp
       61 ghlvllgpnl phnwvsdmae getverrnlv iqfdpafvrr cmdafpecrd aqallddarr
      121 gvgfdaatsa aiaplfdall aargmrrial fmtilerlcg aaertllasp aydqtdvtpt
      181 rlshalsyig knlaselres dlaqltgqsv safsrafhrq tgmpfvqyvn rlriesacqm
      241 lladdanitd icfqagfnnv snfnrqfrav kgmapsefra lqrlnarsrd lalhaaptgn
      301 pmpprvltpg apelapqpg
//
LOCUS       WP_175903821             140 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Burkholderia seminalis].
ACCESSION   WP_175903821
VERSION     WP_175903821.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..140
                     /product="RidA family protein"
                     /calculated_mol_wt=15146
     Region          1..115
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 maeavnppev wapfgafsma viqgdgrivh lkgqvaldrd gqvvgagdmr aqvrqtldni
       61 rdvlaplggq mrdvislvhy atdieafmqa gdirstyfaa pypvtttvqv erlyrpdlli
      121 eiaaiaeipa arfrrpetaa
//
LOCUS       WP_175903844             203 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia seminalis].
ACCESSION   WP_175903844
VERSION     WP_175903844.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..203
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21528
     Region          1..187
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtlstltvfa fallvtagtp gpsvaalvar vltngirdvl pflmamwlge alwltlavag
       61 lsafartfat glfvlkllgv ayllflawkm wiaptdtgad dlprgqspwr mfvagmlvtl
      121 gnpkimvfyl allptivdla hvsvaawael vgtmlavlil adcfwsllas rarafltstr
      181 akrianrtsa tamasaalai atr
//
LOCUS       WP_175903854             302 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175903854
VERSION     WP_175903854.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31896
     Region          13..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..294
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(106,110,149,163,165,229,246,273)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(107..108,112..113,115..116,119,123,125..131,192,
                     223..227,234..235,238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mgidgrilan vgvlaaives gsfaraadal glspsgvsra vgrlearvgv rlldrttrsv
       61 tltdegrrly eeigpllagi gdavtlaags aaavrgrlrv nvdayfsrrm laphlpafla
      121 rhpdlslela areqlgdlva dgfdvavrfg eppssslvar klletravtv aspayvkrhg
      181 rpvvpadlag haciqmrntl tgqplewvyr lgrkrvpvkt agrllvndag tmlgaclagv
      241 gvarfkasgv aalieqgrlv elladwrges fplfayypsr hlppakvraf vdfvaeivaa
      301 gp
//
LOCUS       WP_175903905             232 aa            linear   BCT 11-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Burkholderia
            seminalis].
ACCESSION   WP_175903905
VERSION     WP_175903905.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..232
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24549
     Region          23..229
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 msayvidaae rpsvevdqss arfpvrrvfc vgrnyadhar emgadpdrep pffftkpada
       61 ivpasgtvay ppltndlhhe ielvvaigkd grsidpadal shvwgygvgv dltrrdlqad
      121 akklsrpwdw akgfdasgpv talraasatg hpatgriwla vngdtrqqgd ladmiwavpd
      181 viayvsrsve lkagdliftg tpagvgalqp gdrvtggvdg vatfefvvga kp
//
LOCUS       WP_175903948             549 aa            linear   BCT 11-JAN-2025
DEFINITION  S8 family peptidase [Burkholderia seminalis].
ACCESSION   WP_175903948
VERSION     WP_175903948.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..549
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=54917
     Region          237..516
                     /region_name="Peptidases_S8_13"
                     /note="Peptidase S8 family domain, uncharacterized
                     subfamily 13; cd07496"
                     /db_xref="CDD:173820"
     Site            order(244,312,316,383..385,411,413..414,484)
                     /site_type="active"
                     /db_xref="CDD:173820"
     Site            order(244,312,484)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173820"
ORIGIN      
        1 mrakrfnsal arsaharmla gmlsaaallp lagcgggggg dgsnpsssna apaptptpap
       61 tppttppass ggnacatqqa avqmaaqaap veppvdhliv klktltatra maaidngtrl
      121 daviqrsmtr wtapvtgsar ayastvaqap vnvqvertis ngaavlslgq rmaatdaaal
      181 aqafaadsdv dyaepdhpmq vrdtpsdply nqqwylsdat agidlppawn vtkgsptvvt
      241 avldtgyrph adlvgnllsg ysfisnvnts nngmtrgpda sdpgdwvtqq eldnangpyy
      301 hcasqpsdss whgtrvmgvi gatanngtgi agvswlgqil pvrvlgkcgg vtsdiadgmr
      361 waagiavngv ptnprpakvi nlslggvgac sttfqqaidd vtakgvtvvv aagndglstg
      421 ldqpancrgv itvgatdatg rrasfsnfga dvslsapgvn ilstsntgtt tpgadtygpa
      481 ngtslatpqv sgvaalmlsv ngnltpaqiq qklqggtraa klaagtscta mpagsgilda
      541 gaaiasanq
//
LOCUS       WP_175903959             403 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia
            seminalis].
ACCESSION   WP_175903959
VERSION     WP_175903959.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..403
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44292
     Region          69..387
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mtlneswltp lvgilillat agaltaavhf llfrvvarla rlsatridda lfefgafkwl
       61 nrivpfvvvk lglgavpgip ervsqvadkv lfalivflvt mtisatlsal ehthrthqrd
      121 qprlslkgam qlvklvmfit aalvvigdat gkqiglllsg igamsavlml ifkdtllglv
      181 agvqlssndm lrigdwitmp sagadgtvid itlntvkvan fdhtiitvpt wklitesyqn
      241 wrgmteaggr rikralfvda tsvrflsnde iarlerltll kdyledkida iaqwngtlgt
      301 agdcpanrrq ltnlgtfray vanylkghpr irrdmtcmar qlpltaegip lelycftdtt
      361 twvdyeaiqa dlfdhliavl pefglrvyqh psgfdmrqmi gaa
//
LOCUS       WP_175903992             252 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia seminalis].
ACCESSION   WP_175903992
VERSION     WP_175903992.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..252
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26178
     Region          1..245
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 msvskkfaav tgagsgigra aaialaqagf tvallgrtea slretqdtir aaggdahafp
       61 advtdeasvd rafariaqqf grldvlfnna grnapvvsld eydldvwnsv vatnltgvfl
      121 caraawrvmk aqtpqggrii nngsisahap rpdtiaytat khavtgitks laldgrryni
      181 acgqidigna atsltermtq gvpqadgsla pearmdvahv anavvqmanl pldtnilnmt
      241 imatampfvg rg
//
LOCUS       WP_175903995             452 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TldD/PmbA family protein [Burkholderia cepacia
            complex].
ACCESSION   WP_175903995
VERSION     WP_175903995.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..452
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47628
     Region          19..451
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 mqssstqlqt vaaelassae rviafarqag aegtrveiea aessavtvtn rvqtersfcg
       61 tlemtvtvlr dgkrafakss dlsddglkki vraaiertaa tepdpaagfa dssqlardfp
      121 dldlhhpldw slddigahaq raedaafaha psikaskgvt vrtmsgtsll atsagfhata
      181 pwsvhsiaca pvafgagekq igfwgdasra fddlakpeev galaarraid algatqvptq
      241 qcpvlfepsa slgllaelvs sasgdalyrs gsflkddida plfpphvqld edpfvrrgma
      301 srcfdsdgip ggrrkvvedg rlrglflgly aarrlnltpt gngygphnld mrstrtgpgd
      361 dfaamlrklh rgllvtemvg ggvnrltgdf srgakgfwve ggeirfpvsg itiasnlrrm
      421 fgglqaigsd altrgwatsg swlidamkig ga
//
LOCUS       WP_175904038             144 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia seminalis].
ACCESSION   WP_175904038
VERSION     WP_175904038.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..144
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15761
     Region          1..143
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mlkllvpvgh sprslqavrh aaflyrerca seivlinvqa plestrleay yplsrlrsie
       61 eqfasddlak aerilreagv kytvvmkvgp vadtiataaa etgcdeivvt aprhdplhal
      121 msvfrrsvmg rlvrisnvpv tavq
//
LOCUS       WP_175904075             310 aa            linear   BCT 11-JAN-2025
DEFINITION  AEC family transporter [Burkholderia cepacia].
ACCESSION   WP_175904075
VERSION     WP_175904075.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..310
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31430
     Region          18..305
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 migpillala pvallvacgh glrrtgfiad afwpqaerlc yyvllpalfa dglanarlqs
       61 lpvlplaaal vgstalaaal lllvrpfvqv dgagftsvfq gavrfnnyvg talaaglfga
      121 kgialaavcv aaivptvnlm cvlvfarygs trlgaaalvr qilsnplvva calgiamqag
      181 gvtfpaavep avralgvasm plgllcvgaa lkfdaarawl qpvcvasafk fmamplitla
      241 agrlfrlgda altvallfqa lptssasyim arqlggdapl magitafqti aaalampvvl
      301 talasapafr
//
LOCUS       WP_175904096             550 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia cepacia].
ACCESSION   WP_175904096
VERSION     WP_175904096.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..550
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=59734
     Region          52..530
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mpprvdrksr erwrlncrcl agvvlaggmg lapgvhaqea apaakaapaa pqsfdvnafv
       61 vrgnttlptl eiekavypfe gpgrtladvn aardalqkay qdrgyqsvvv elpqqqvkng
      121 villqvteak vgrlrvdgak ynslqnirda vpalaegqvp dfnqaqqqlt dlnrsadrqv
      181 ipvlkpgalp qtvdvdlkvd dhsplhgsle lnndnspgts tlrttaslsy snlwqlghvi
      241 sgtyviapqh pndarvyafs ylapirdsrw sflatvvhsd snvasvgntn vlgkgttygf
      301 taiyslpate tyahsvsiei drkhydedvs lpgqggstap ltyvpvtlsy ngqlslknsq
      361 tsfsaslttn irglgsdwga wdnkrynatp dfvygkfdvn htqrfandmq anahvnaqis
      421 nsplvsseqf aaggmnsvrg ymqaedtads gviaslelrs pslakwlgga vgsrvnewrf
      481 haffdaahlw llsplpeqta rfnlmsvgvg trvqimkyas adfeagwplk agvytrqysp
      541 rfdffvrlgf
//
LOCUS       WP_175904152             352 aa            linear   BCT 11-JAN-2025
DEFINITION  LLM class flavin-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175904152
VERSION     WP_175904152.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..352
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38596
     Region          43..341
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 mtkdtkvsnv ridhiafltp gnyagedaaa gfeqtlelfs agealgydsa wvrqrhlera
       61 vssaatflaa asqrttrigl gaaviqmgye npfrlaedla tvdvlsrgrl nvglsagapn
      121 hgallgerlf dtdpdlvdfs harvarlrrn lagdwlgddd tfvesaagrv rprvspfapg
      181 ltgrlwyggg srrsiewaar ngfnlligni ttgegtdshi daqlrqldly rdhwhdahap
      241 rialgrvivp tdgasakere ryrafadarh artlapqger rtlfapdlvg ssdeiverll
      301 adpvvgqvre lrlelpydlp fenyrqildd fitriapalg wqpvdrrepa aa
//
LOCUS       WP_175904143             514 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia seminalis].
ACCESSION   WP_175904143
VERSION     WP_175904143.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..514
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52063
     Region          90..493
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrrpeppaas iavaalatav alagcatssi dlapeasdrp wqpqtsaagd ivpgpprasa
       61 pgahdytlpa spalasvspp avldaahpyt lpelidlaes anpltriawn darnaalavg
      121 lakaaylprl satamgayqt shgststilg dsssdttvhg tisalslqwl lfdfggraar
      181 veaaeqasia snvaftavhq qvihdvtvsy yryeaarsra vsaqqglana dailaasrar
      241 lkhgvgtvve laqatqnraq anlalvqang aesdsylalv salgisplsk ptiaalpkrp
      301 lppalgssvd aivsdaiarr pdlqgafale kanrakikaa eaafmpkifl sastsyasgg
      361 taisalpaig dqaptvnlng srygggvflg vtiplydggl rsavlmqarn daesasarlt
      421 rtkeeavrqv vaaqnavqts lashnaakal vdaaqtsyda altayrngvg svtdatiaqs
      481 qllaarnaev dsyagalsaa aalalatgti gaaq
//
LOCUS       WP_175904164             355 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175904164
VERSION     WP_175904164.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..355
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38446
     Region          29..336
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mqtvsnhssa glsvnrgrgp gtghqrasvi vlllegfsim qmgklaavfe lanqlgradg
       61 vfadhyelrl ysihggpvrs ssgvgiwtda trmleastvh amfvlsgegg idaldeqlia
      121 wlrhahqrar vvrgsgggrk lltqihlaqk evekvlpvad dgvashagrd dvecsddedd
      181 gpfsdalsiv rvdmgyeiaq eivacmvsga nrkltdvlfg arvarastli rraahhlrvn
      241 senrisiade aqaaamsern flrrfkneig vtptefvlri rlekacrmli etdlpadkva
      301 rrtglgsgdr maklfrqhlq tspteyraaa rkggdasaem lyasdlsswm nntas
//
LOCUS       WP_175904270             154 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia seminalis].
ACCESSION   WP_175904270
VERSION     WP_175904270.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..154
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17515
     Region          48..138
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 mldptdlrll yqlrpaepgd fpfaealthg nmggyykrhg lvwrsdlfya swresenfil
       61 eadgerigvl rvteegdslh irdlqiaagh rgqgagtyml dmshrwarar glhelqlrvf
      121 vdnpaarlyq rmgyrvagpr lsqlgsirhm vrpv
//
LOCUS       WP_175904293             144 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia seminalis].
ACCESSION   WP_175904293
VERSION     WP_175904293.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..144
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15500
     Region          1..142
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mfrhilvptd gselsqkaid gaidlaravg arvtayaclp qypyspfsev iieppadfra
       61 rserearahl deveaaaraa gvvcdtwtsv hpspylgiie aaerggcdvi fmashgrrgl
      121 gslligsetq rvlthtkipv ivyr
//
LOCUS       WP_175904287             171 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF485 domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175904287
VERSION     WP_175904287.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..171
                     /product="DUF485 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=18360
     Region          67..171
                     /region_name="YjcH"
                     /note="Uncharacterized membrane protein, DUF485 family
                     [Function unknown]; COG3162"
                     /db_xref="CDD:442396"
ORIGIN      
        1 msaptpptcg gcyspmaeis svvlaivlag pagqgsepyl mddesidgmt dsqgdpdsqn
       61 wrwrrhmtln asavsrireh akfrelvder arlgrvsmvi vlgayfglia lvalrpdllr
      121 saawagsvtt vgvifaiavi vagwgltwly vrvandrfer ltgellgevg q
//
LOCUS       WP_175904338             155 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein, partial [Burkholderia
            cepacia].
ACCESSION   WP_175904338
VERSION     WP_175904338.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 155)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         <1..>155
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
     Region          <1..126
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            32..34
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 vrivdltrrf gkeaaltagi deaagtavil idadlqdppa lipamverwl agaevvaakr
       61 tdrmcdplmq rvaaalyyrv hnrlsevemp envgdfrlmd rqvvdalral perrrfmkgl
      121 fawvgyrtei ieytraprsg grskfsgwrr wnfal
//
LOCUS       WP_175904354             620 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Burkholderia seminalis].
ACCESSION   WP_175904354
VERSION     WP_175904354.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..620
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..620
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=68310
     Region          372..615
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mrtkltvknp kpasptrapv rsgslvarka vrpaappagd kparpkkaap aaagersfkp
       61 rgaagaerpg tdrapakrap rdggaergtg apyrdnaagd gakrsfgerr tssdrpprrd
      121 ddarprragg dddkrpsyrd kaagegakrs fgerrtssdr pprrdddtrp rrasgdddkr
      181 psyrdkaage gakrsfgdrr tssdrpprrd ddtrprragg dddkrpsyrd kaagegakrs
      241 fgdrrtssdr pprrdddarp rraggdddkr psyrdkaage gakrsfgdrr tssdrpprrd
      301 ddgrprragg nddkrpsyrd kaagdgvkrs fgdrparpar dgerrsfgav ktaqpvkraa
      361 advdygdetg lmrlskrmse lgmcsrread ewiekgwvlv dgeridtlgt kvradqkiei
      421 derasaaqaa qvtillhkpv gyvsgqaedg yepaavlitr anrwsgdhsp vrfspqhlha
      481 lapagrldid stgllvltqn gviakqlige qsdidkeylv rvrfgerlid idqhfpaesl
      541 aklrhgleld gvalkpamvs wqngeqlrfv lregkkrqir rmcelvgldv iglkrvrmgr
      601 vmlgalpqgq wrylsadetf
//
LOCUS       WP_175904369             254 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF899 domain-containing protein [Burkholderia seminalis].
ACCESSION   WP_175904369
VERSION     WP_175904369.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..254
                     /product="DUF899 domain-containing protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28703
     Region          1..254
                     /region_name="COG4312"
                     /note="Predicted dithiol-disulfide oxidoreductase, DUF899
                     family [General function prediction only]"
                     /db_xref="CDD:443453"
ORIGIN      
        1 mtthltgtrd ewlaerrall daekaltrqs delarrrqal pwvridkayr fdtedgqatl
       61 ddlfrgrsql lvyhfmfgpd ykagcpscsa ladgfdgfav hlahhdvtla avsraplakl
      121 layrermgwa fpwassvgsd fnfdfnvsft etqrragdve ynyaraaham dmdpppapva
      181 qfattcgtda rtysldrpgm safvredgav yhtystyarg ldglwgmyqw ldraprgrne
      241 agpwwrrhde yarg
//
LOCUS       WP_175904377             145 aa            linear   BCT 11-JAN-2025
DEFINITION  ester cyclase [Burkholderia seminalis].
ACCESSION   WP_175904377
VERSION     WP_175904377.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Sultana,A., Kallio,P., Jansson,A., Wang,J.S., Niemi,J., Mantsala,P.
            and Schneider,G.
  TITLE     Structure of the polyketide cyclase SnoaL reveals a novel mechanism
            for enzymatic aldol condensation
  JOURNAL   EMBO J 23 (9), 1911-1921 (2004)
   PUBMED   15071504
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..145
                     /product="ester cyclase"
                     /EC_number="5.5.1.-"
                     /GO_process="GO:0030638 - polyketide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=15920
     Region          15..140
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
ORIGIN      
        1 mtsatspdlt rlgylfaeim snhdvsrlde ikapnyvnhn afaepgregs kkvlgaiiag
       61 vpdlkvtaed vfvsadgsrv vgryryegth tgnllgypat grpfvmrsid iwrvehgrfv
      121 ehwdelntle vfiqigavqp pkqpa
//
LOCUS       WP_175904385             256 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175904385
VERSION     WP_175904385.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..256
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28517
     Region          10..245
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mtasnvvpls aaplyvqikd mlrarildgt yaphsrmpse helcamfdvs ritvrqalgd
       61 lqkegllfkl hgkgtfvskp kafqnvtslq gfaeamssmg yeivnqlrsl rtvkadrhla
      121 tklnvpegap lveihrvrll nrepvsleqt wvpealgkrl agadlatrdi flvlendcgi
      181 plghadvsid ailaddeivd alhvedgspv lrierlthda sgapidyeyl yfrgdafqyr
      241 lridrqkprk parkqr
//
LOCUS       WP_175904425             381 aa            linear   BCT 11-JAN-2025
DEFINITION  glycerate kinase [Burkholderia seminalis].
ACCESSION   WP_175904425
VERSION     WP_175904425.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..381
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38404
     Region          10..376
                     /region_name="GlxK"
                     /note="Glycerate kinase [Carbohydrate transport and
                     metabolism]; COG1929"
                     /db_xref="CDD:441532"
ORIGIN      
        1 mpqhpsapvv viapdsfkgs lsaeqvadai atgirrarpd avvrccpmad ggegtldaml
       61 agggtrrtlr vagaslaard aavgvidart aivetaeivg itdavgmsvp vdarstrgmg
      121 eairallddg vrrffvalgg sstndagagl laglglqcfd aggqpvepvp srladiarid
      181 asaldprlkd tefvgmsdvd npltgahgat avfgpqkgat pgqvatldaa larfadllea
      241 aldrrgrdlp gagaagglgf alhmlgaqfe agaevvarqv gldaalagad wlitgegrsd
      301 vqtlhgkapf iacrharavg vpasllsgav dpaalprlse hfsgcfspap gpitldvair
      361 daanllanea eqltrlkyga h
//
LOCUS       WP_175904440             466 aa            linear   BCT 11-JAN-2025
DEFINITION  GGDEF domain-containing protein [Burkholderia seminalis].
ACCESSION   WP_175904440
VERSION     WP_175904440.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 466)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 466)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 466)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..466
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51638
     Region          202..464
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 msttyaagep prvvsaaarl yakcllvgfa llpayliayl wffsdphvgf enhafheiai
       61 aaatlegafv tyvtwvcyrs sgepllrwlt lgflgfamiy alhgaftgma hhniwlflly
      121 gpasrlvmsi llltgllsys rppdrierrt sartwlpwiv ffvivdvvva ylayspiaga
      181 lgtrlsmegg alvfsllnvc mllarrirsp lmviygvsim afalsslafi lgkpwnhmww
      241 lahaifaggf fllsygvvqa lqttrsfsai ysqedlmsrl sesmartesa lqelrrtnqk
      301 leymaatdpm tgasnrrqfi aqveremvra erdgtpfcll aldldnfkni ndayghqigd
      361 evlrgvvrqc leairpaggl arvggeefma llpdmplega rmtaervrss iasspfgldf
      421 krvqvtvsvg vaqygvdgst vdallrvvde rlyqakregr nrvvsr
//
LOCUS       WP_175904451             391 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Burkholderia seminalis].
ACCESSION   WP_175904451
VERSION     WP_175904451.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 391)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..391
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41710
     Region          4..386
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 mtalktlaia nyrslreliv plaalnvvtg pngsgkssvy ralrlladta qgrvipslar
       61 egglpstlwa gperfsraml agdapvtgtv rkgpvslklg facddfgysi dlglpvpsds
      121 qfaldpvvkr eciwggalpr pstllvdrqg aqirartasg dwwtipqpva sfdsmmtefa
      181 dptgapemia vrerirswrf ydhfrtdaqa parqsqigth tpvladdgad laaalqtire
      241 igdaaaldaa iddafpgasv eidnpggrgr fdvlmrqpgl lrplaaaels dgtlryllla
      301 aalltprppa lmvlnepets lhpdllpalg rliaqaarrs qvlvvshaar liatlereag
      361 ceslvldkql gatalvdadt rdlpawkwps r
//
LOCUS       WP_175904459             336 aa            linear   BCT 11-JAN-2025
DEFINITION  inorganic phosphate transporter [Burkholderia seminalis].
ACCESSION   WP_175904459
VERSION     WP_175904459.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..336
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=35403
     Region          21..336
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 mhsiqlalwm vaalvlvalv fdfmngfhda ansiatvvst gvlkpqqavv faaafnviay
       61 fifhlkvaqt vgkgtidpei vdhyvifgal vgaigwnvit wyygipssss haligglvga
      121 alaksgwgsl nidgllktva fifispllgf ilgslfmlgv swlyfrtaps kvdrrfrrlq
      181 llsaglyslg hggndaqkti giiwmllias gyasasadap pawvigacyl smglgtlfgg
      241 wrivrtmgqk itklkpvggf caetggamtl flasflgipv stthtitgai vgvgatqkls
      301 avrwgvagni vwawvltlpa aalfaaggww lghqif
//
LOCUS       WP_175904460             355 aa            linear   BCT 11-JAN-2025
DEFINITION  C40 family peptidase [Burkholderia seminalis].
ACCESSION   WP_175904460
VERSION     WP_175904460.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..355
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36871
     Region          <7..176
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mlriwvpvav vsllaacssv ppqsasrsas gmkittprpf papanfpkfv dhsvgqeeis
       61 iqamslvgip yrwggntpts gfdcsglvry vmgraadvnl prttadmsgr gvsiepdeia
      121 pgdliffntt grphshvgiy vgklrfvnap stggtvrldy ltnpywakrf dgirrvappr
      181 taptpfdapt yeakrdeprt ppvaaaapav vtaaaarqpa yapqqarvtq apapvvtaaa
      241 apaapaadpy epppprmqga qqqatsmndg mtamtanaap avpaesgtqi pttaltaaqa
      301 aafddepppa aasasprsie papvqvwras tqsapvsprt gtsddpiarf angsy
//
LOCUS       WP_175904479             638 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Burkholderia seminalis].
ACCESSION   WP_175904479
VERSION     WP_175904479.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..638
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=69249
     Region          6..631
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mpyavpqaqh adrvlgalag rlpapadsar lvsswqrsle ryrldpassi gprvltaael
       61 revrdkeeaf lrasgqcltr lhdmirvady cvmltdahgv tidyridrer rndfrhaglh
      121 igscwsesee gtcgvasvlt dlapitvhkt dhfraafttl tcsaapifsp ggeligvlda
      181 savhspdgrd sqclvyqlvr qsaaliedgy fvhstaqhwi lfghpnrhyv eaqpewmiaf
      241 decgnivaan rqardalpal reprhideif datemplrda arldtivalr lratgaplya
      301 rlraplrrag repgavsrra gtaprnvgal tpflhssdah iaqqaelalr vaskrlpilv
      361 lgetgagkev faraihdaga rrarpfvavn cgalpdalie selfgyaaga ftgarkhgar
      421 gkialadggt lfldeigdmp lalqtrllrv ladgevvplg sdtpvrvdld vicathrdls
      481 rmvadgtfre dlyyrlsgat felpplrara dvrdviaavf aeeaqatghv ltldptlaeq
      541 laayawpgnv rqlrnvlrya cavcdaarvt rrdlpaelaa qlggappgal pddergriva
      601 altahrwrpd aaaqalgmsr atlyrriaky rivaphra
//
LOCUS       WP_175904482             327 aa            linear   BCT 11-JAN-2025
DEFINITION  thiamine pyrophosphate-dependent dehydrogenase E1 component subunit
            alpha [Burkholderia seminalis].
ACCESSION   WP_175904482
VERSION     WP_175904482.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..327
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=34546
     Region          6..327
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 mtastqlsrd tlldayrlmr tirefeerlh vefatgeipg fvhlyageea savgtmlhlg
       61 ladyvatthr ghghciakgv dvhgmmaeiy gkktgvchgk ggsmhiadls mgmlgangiv
      121 gaggplvcga alaakhkktg gvgvcffgdg asnqgvifes mnlasvwrlp aifvaenngy
      181 aeatsstwsv atdniadran gfgmpgvivd gfdffavhea lgeaverarn gggptlvevk
      241 ftryfghfeg daqtyrapge vqklrdekdc lkhfetrvvr aealttadlr avdaqvkali
      301 ddavaqakaa pvpdaadlla dvyvsyp
//
LOCUS       WP_175904477             153 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175904477
VERSION     WP_175904477.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..153
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16460
     Region          14..126
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(15..17,31,48..50)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(62,65,69..70,79,97,101,107,111,114..115)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 msktvsrsss agpltigqva eltgvsthtl ryyeqagllr aisrtaaghr lyapadlagl
       61 afvmrlkatg mpiaqiqafa vlreqgestf garrdllvah rdavrahiae lqanldaigd
      121 kiayyeaqer etqrrakpsl slseqdghdg ttr
//
LOCUS       WP_175904525             259 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Burkholderia seminalis].
ACCESSION   WP_175904525
VERSION     WP_175904525.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..259
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26813
     Region          4..236
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mplkilvpvk rvvdpnvrvr vgaagsiett glkmsinpfd ecaletalrl reaghaaqvs
       61 vvtcglpvcq dvlrtglamg addailidtg datasldslg varllhaylg tspydlvlcg
      121 kqaidddtgg vapmlagllg wpqgldatal apdgdgwrvt cgddsgtatw rlagravvsa
      181 dlrlaeprrv tlpsivkakq kplaivpaar favdlapssr avrldeptvq rsghrvadid
      241 aliaalaahn vfahtgvra
//
LOCUS       WP_175904548             123 aa            linear   BCT 11-JAN-2025
DEFINITION  GFA family protein [Burkholderia seminalis].
ACCESSION   WP_175904548
VERSION     WP_175904548.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..123
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13334
     Region          6..109
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 msatwfkgsc hcgavkfevr aamtpavrcn cslcrrrgal mspmfaaasl nivegedvlt
       61 cyrfntrtar hyfcsrcgiy pfhqtrkdpa cwrvnlgcld gvdpyaldat vadgaslsvv
      121 eaa
//
LOCUS       WP_175904550             238 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia seminalis].
ACCESSION   WP_175904550
VERSION     WP_175904550.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..238
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25351
     Region          152..236
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mrdattgtpt gdthvldrvv wnaltgkqrp lalgngrawr fpsaiapfaa iadtsaasfd
       61 alrelvaahg paalvtpdei epptgwpvvr ratllqmvcq raadpadese hvtlgeadvp
      121 dmlaltaaaq pgpfgprtve lgryigvrsa grlaamager mrvdgyteis avcvdaefrr
      181 qglaarlirs liasigarse tpflhvlttn qvaieryval gfvvrremrl lvlgdpha
//
LOCUS       WP_175904585             206 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            seminalis].
ACCESSION   WP_175904585
VERSION     WP_175904585.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23259
     Region          9..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkpqrltreq srdqtrerll kaahriflkk gyvaasvedi aaaagytrga fysnfrsksd
       61 lllellernh aevradfeai fegggsreqm esmslayyrt lfrddeysll wgeaklqaar
      121 dakfrvrfnq flhgkrvqma efierfaers gtplllpadt lafglmclcd gvqsyytadp
      181 qhvsadvaes vlagffarvv lgrtpd
//
LOCUS       WP_175904587            1049 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia seminalis].
ACCESSION   WP_175904587
VERSION     WP_175904587.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..1049
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114536
     Region          11..1027
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mstpheegrf nlsawalrhq alvvyliala tlagilaytr laqsedppft frvmvirtfw
       61 pgasarqvqe qvtdrigrkl qetpaidflr sysrpgesli fftmkdsapv kdvpetwyqi
      121 rkkvgdigyt lppgaqgpff ndefgdvytn iwtlegdgft paqlhdyadq lrtvllrvpg
      181 vgkvdyfgdp dqrifievnn aqltrlgisp qqlgqainaq ndisstgvlt taddrvfvrp
      241 sgqfdnvdai adtviringr tfrlgdlatv krgyddpavt qmrangkavl gigvtmqpgg
      301 dvirlgkald aeskdlqaql paglkltevs smphavshsv ddfleavaea vaivlvvslv
      361 slglrtgmvv visipvvlav talfmylfdi glhkvslgtl vlalgllvdd aiiavemmav
      421 kleqgysrar aaafaytsta fpmltgtlvt vsgflpiala ksstgeytrs ifevsaiali
      481 aswfaavvli pllgyhllpe rkrqaheahl pddhehdiyd trfyrrlrgw iawcierrlv
      541 vllitgalfv vslmgfslvp qqffpssdrp ellvdlrlpe gasfaatlre terlekaidk
      601 rpeidhsvnf vgsgaprfyl pldqqlqlpn faqfvitaks vedreklatw lettlrdrfp
      661 avrwrlsrle ngppvgypvq frvsgdsiat vrsiaeqvaa tmrgdartvn vqfdwdepae
      721 rsvrfeidqk karelnvtsq dvssflamtl sgttvtqyre rdkliavdlr apkadrvdpa
      781 rlaglalptp ngpvplgslg rftptleygv vwerdrqpti tvqsdvraga qgidvthavd
      841 aklnalraql pvgyqinigg sveesakaqa sinaqmplma iavftllmiq lqsfsrvlmv
      901 vltaplglig vvatlllfgq pfgfvamlgv iamfgiimrn svilvdqieq diavghgrid
      961 aiigatvrrf rpitltaaaa vlalipllrs nffgpmatal mggitsatvl tlfylpalya
     1021 twfrvkrder dpqdgpppgg sapaapsga
//
LOCUS       WP_175904607             330 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Burkholderia seminalis].
ACCESSION   WP_175904607
VERSION     WP_175904607.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..330
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=36780
     Region          13..286
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mgplaatfde ireayalgrg paprrvserv whlpadggdm avklyasehh araakeaail
       61 ahlethgdtr fhvqtlkrtt dgeplwtgqh shamltrwea gqfrtydtfs paewdalgas
      121 laalhlgler lhllsldtir arlaaidada vrrslldaln rsrsndnaan lrryvdlalr
      181 vldryypgsl dafpaddpqy pihndynqfn ylftgrlppl ildweasiga preyelvrcl
      241 nhlpleapqr aeafvrayqr vrpvnparia wavdaaclqh alklwvvqgw lddparfash
      301 lsgavtmaaa mvdarghlvd ffsrcveagn
//
LOCUS       WP_175904640             361 aa            linear   BCT 11-JAN-2025
DEFINITION  AI-2E family transporter [Burkholderia seminalis].
ACCESSION   WP_175904640
VERSION     WP_175904640.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..361
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39613
     Region          86..352
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mekqpdssrd vhnrephlrs vrltsdfslp klsaleigsy afailamwlv ielkllggll
       61 agllvyqlih tiapaierht tsmrarwvav vllsiaivga ltgltigiie hfertvpnlq
      121 slldqlmqiv eqtrartpaw ianllpvdve qmktkaavlm hshmdqlqqs gksvargfgh
      181 vlfgmiigam iaigvehgkv rrplstalvt rvsrfadafr rivfaqikis ainavftgiy
      241 llvalpifhq rlplsktlvl vtfivgllpv ignlisntli vavslsvsmg taiaslaflv
      301 vihkleyfln akiiggqies rawelllaml imeaafglpg viaapifyay lkrelyllrl
      361 i
//
LOCUS       WP_175904618             267 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia seminalis].
ACCESSION   WP_175904618
VERSION     WP_175904618.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10508417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..267
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28362
     Region          10..251
                     /region_name="UPF0014"
                     /note="Uncharacterized protein family (UPF0014);
                     pfam03649"
                     /db_xref="CDD:427424"
ORIGIN      
        1 mspalqdlsl vdvgiaaalv avngaisaal slglgrklal aavrtvvqll aigyvlgrvf
       61 ghphwyvvlp ltalmtliag fagagrgkrt yrgqridsia siwfsswfva avglfvviri
      121 hpwyapqyai pilgmilgnt ltgvslgver mmeeltarrd rvetalalga trweaaqdaa
      181 rqavragmlp tlnqmavvgv vslpgmmtgq vlagqsplqa vryqivimfl iaaasalgtv
      241 gavlmtyrrl fsadhrflas rleerap
//
LOCUS       WP_175904678             287 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Burkholderia
            seminalis].
ACCESSION   WP_175904678
VERSION     WP_175904678.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 287)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..287
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31619
     Region          23..269
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mnvltdiaas sahalpasda aplievrelg krfgevevlc gvdleirkse vaciigpsgs
       61 gkstllrcla aletydrgev riegellgys nrngrreras laeinrvrrn vgmvfqqfnl
      121 wphmtalgnv tealqrvrgl srdesrrrgm amletvglah kadahpskls ggqqqrvaia
      181 ralamephim lfdeptsald pelvgevlqv mkqlaregmt mvvvthemgf aaqvankvvf
      241 idqgriavqg spdevfhdtt qprlrqflqn yfdrnafwtq nndkdsa
//
LOCUS       WP_175904684             311 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Burkholderia seminalis].
ACCESSION   WP_175904684
VERSION     WP_175904684.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..311
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31524
     Region          2..310
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtilviaehd nasikaatln tvaaaakigg dihvlvaghn aqaaadaaak iagvskvlla
       61 dapqlaegla enveatalni akdyshilap ataygkniap riaakldvaq isditavdsa
      121 dtferpiyag naiatvqssd pikvitvrat gfdpvaaegg saavekidaa adagksqfvs
      181 revtkldrpe ltsasiivsg grglgsgeny tkvlepladk lsaalgasra avdagyvpnd
      241 yqvgqtgkiv apqlyiavgi sgaiqhlagm kdskvivain kdpeapifsv adyglvgdlf
      301 tsvpdlieql p
//
LOCUS       WP_175904687             298 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia seminalis].
ACCESSION   WP_175904687
VERSION     WP_175904687.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..298
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31081
     Region          1..294
                     /region_name="COG4120"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443296"
ORIGIN      
        1 mslfsflgal eiglifslva lgvlisfril dfpdltvdgs fplggavaat lisagydpft
       61 stllaivaga lagfvtgwln vrlkimdlla silmmialys vnlrimgrpn vpliteptlf
      121 tvlqpdwmpd yvlrpallai vvvvaklgld wffssqlgla mratganprm araqgiatgr
      181 atlagmalsn alvalagalf aqtqggsdis mgigtivigl aaviigetll parrlvlttl
      241 avvlgaivyr ffialalnse figlkaqdln lvtaalvtla lvlpatrkkl farkngga
//
LOCUS       WP_175904690             271 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Burkholderia seminalis].
ACCESSION   WP_175904690
VERSION     WP_175904690.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 271)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..271
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29098
     Region          1..271
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkrrsllkvf svlaagaalt lsagahaddk vikvgtvagp daevwqvvqk vakekeglnv
       61 kviefndyvq pnaaldagdl dansfqhqpy ldsqvkqrgy kivsagltyi spigvyskky
      121 kslkdlpqga klavpndpsn enrallllqt qgviklkaga gtggnnatvl diaenpkklk
      181 iseldaaqlp rvlsdvdaav intnyalaan lqptkdaial esltspyanl iavrakdkdq
      241 pwvkklvkay qsqevrefik kqfkgsmvas f
//
LOCUS       WP_175904701             140 aa            linear   BCT 11-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Burkholderia seminalis].
ACCESSION   WP_175904701
VERSION     WP_175904701.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..140
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=14443
     Region          35..135
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mtfftdytnl aliailvvsg gllawpalrr grgglsaaea tqlinrrnav vidlraasdf
       61 aaghlpsarq vaageigaki aqiaknkstp vllvcqngqq sqkaarevea agyaevhvle
      121 ggvaawqqag mpvvkqgvak
//
LOCUS       WP_175904702             515 aa            linear   BCT 11-JAN-2025
DEFINITION  S41 family peptidase [Burkholderia seminalis].
ACCESSION   WP_175904702
VERSION     WP_175904702.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..515
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=56205
     Region          43..393
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mrmklknigl iaaglatgvf atlqvsasae qtataplpld qlrlfaevfg qikreyvepv
       61 ddkklltaai kgmvssldph ssfldktdyd elqeqtkgrf aglgieisqe dglvkvispi
      121 edtpafragi rpgdlitrin dkpvrgmtld kavkqmrgep gtkvtltifr ksddrtfpvt
      181 vtraiikvqs vkmkildpgy ayiritsfqe rttpdlaqkl qdiarqqpnl kglvldlrnn
      241 gggllqsavg vagaflppds vvvstngqip dskqvyrdty dnyrlpsfdg dplknlppif
      301 ktvpmivltn aysasaseiv agalqdskra qimgkttfgk gsvqtvrpmt adtalrltta
      361 yyytpsgrsi qnkgitpdvp vdqyadgdpd dvlvtrevdy tnhlantqdp nekkeqedre
      421 qrrmdqlrvl eeqndkktpe qrqkdrdrkp iefgsaddfm mqqalnkleg kpvqesksll
      481 aestknpagk aaaaskasga sakpasapkp asapk
//
LOCUS       WP_175904734             304 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia seminalis].
ACCESSION   WP_175904734
VERSION     WP_175904734.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..304
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32386
     Region          29..270
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 mnasnettah aaavgagsvg prpagaadag dlvievrnlt krygrnivhq kldfdvrrge
       61 ivsivggsgs gkttlvrqil glerptsgti kvfgedtati ddasarmmrt rsgmlfqqga
      121 lfssmtvfdn vaqplrelgr vppdllhdiv mlklemvglp ckhaskmpaa lsggmvkrvg
      181 iaraialepe llfldeptag ldpqasdefv eliatlhrtl gltvvmvthd ldtmvalstr
      241 vavladrkvl vaapveeaan vdhpfiheyf lglrgrralq alpperrakl pkaalepals
      301 svel
//
LOCUS       WP_175904780             120 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia seminalis].
ACCESSION   WP_175904780
VERSION     WP_175904780.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 120)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 120)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..120
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12305
     Region          31..118
                     /region_name="CytC552"
                     /note="Cytochrome c551/c552 [Energy production and
                     conversion]; COG4654"
                     /db_xref="CDD:443692"
ORIGIN      
        1 mkgarmkqvk qwmvqgaaga alvvgtlgaa hadvgdglkv arsnacmgch avdrklvgps
       61 fkdiaaryks dpqavaklsk kvkdggsgvw gaipmpahpr msdadvrsvv ewvlagapsk
//
LOCUS       WP_175904775             445 aa            linear   BCT 11-JAN-2025
DEFINITION  carotenoid oxygenase family protein [Burkholderia seminalis].
ACCESSION   WP_175904775
VERSION     WP_175904775.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Poliakov,E., Uppal,S., Rogozin,I.B., Gentleman,S. and Redmond,T.M.
  TITLE     Evolutionary aspects and enzymology of metazoan carotenoid cleavage
            oxygenases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1865 (11), 158665 (2020)
   PUBMED   32061750
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Sui,X., Kiser,P.D., Lintig,Jv. and Palczewski,K.
  TITLE     Structural basis of carotenoid cleavage: from bacteria to mammals
  JOURNAL   Arch Biochem Biophys 539 (2), 203-213 (2013)
   PUBMED   23827316
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Kloer,D.P. and Schulz,G.E.
  TITLE     Structural and biological aspects of carotenoid cleavage
  JOURNAL   Cell Mol Life Sci 63 (19-20), 2291-2303 (2006)
   PUBMED   16909205
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Wyss,A.
  TITLE     Carotene oxygenases: a new family of double bond cleavage enzymes
  JOURNAL   J Nutr 134 (1), 246S-250S (2004)
   PUBMED   14704328
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..445
                     /product="carotenoid oxygenase family protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006720 - isoprenoid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48962
     Region          10..439
                     /region_name="COG3670"
                     /note="Carotenoid cleavage dioxygenase or a related enzyme
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]"
                     /db_xref="CDD:442887"
ORIGIN      
        1 mtafdlnhga iapvadevdv vdlrvtgaip reldgtllrn gpnppggrfe gndmlswwpe
       61 aamlhaiafd rgratgyrnr wartqrwaav hapgqvphlp dtnpnvnvlq hagellalae
      121 ggaplaitpa ldslgvaarh agfgggmtah pkvdpvtgel itfradwrap wlrygvidah
      181 gvqrvdveid lnapsmmhdl aitetrslll dlnvgydfsl lkqghrmplr whderparig
      241 vmprhggavr wfgvepcfiq hvvnaydcda scivldavry psflrldart grfadnpvge
      301 lwryvidtan glvdegplad ggielprind srtgrryryl yaveqpnhae mrgvmrfdha
      361 hgttthyavp pgdqnsepvf vprpggtded dgwllvmvyr aatdtsdvvi ldaraiddep
      421 vatvhlprrv pagfhgawvp rerrt
//
LOCUS       WP_175904772             232 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia seminalis].
ACCESSION   WP_175904772
VERSION     WP_175904772.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 232)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..232
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24878
     Region          6..228
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mndappplve ishvaksyrr gnqivpvltd itldigagdf valmgpsgsg kstllnlvag
       61 idrpdsgelr vggldisqla eaqlaewraa nvgfifqfyn lmpvltafen velplmltql
      121 srrerrerve lvldmvnlgd rtshypsels ggqqqrvaia ralitdpvli vadeptgdld
      181 rasatdvlam lqrmnaelgk tiimvthdah aagaarslvh lekgelidgh ag
//
LOCUS       WP_175904792             230 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia seminalis].
ACCESSION   WP_175904792
VERSION     WP_175904792.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..230
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24280
     Region          1..227
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mtaqwidipt gndsfggyla lpkrgkgpav iiiqeifgvn ahiravadqy asdgfvalap
       61 dvfwrtqprv eltyegadrd kgielmkktd vglavadiga aadalrarpe vagkvaaigy
      121 cfggqlayrt aatgkldaav syygggiqna ldlagqvtqp ilfhyaendh aipltavdav
      181 kaafaghdha sfhvypgaeh gfnctdrasy nqraaalahg rtltflaehl
//
LOCUS       WP_175904845             143 aa            linear   BCT 11-JAN-2025
DEFINITION  phage tail protein [Burkholderia seminalis].
ACCESSION   WP_175904845
VERSION     WP_175904845.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10536982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..143
                     /product="phage tail protein"
                     /calculated_mol_wt=15320
     Region          7..126
                     /region_name="Phage_P2_GpU"
                     /note="Phage P2 GpU; pfam06995"
                     /db_xref="CDD:429236"
ORIGIN      
        1 mmmsldqfvf slattpyqel qrqrnwkhrt ssrigvrdas qftgagddti tltgivapdn
       61 gigeiasiea larmgdagda yvlvdgngnv ygayvidsln etatyhtkeg mprkiaftlt
      121 lkrvddgvla easqddesga aeq
//
LOCUS       WP_175904854             235 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia seminalis].
ACCESSION   WP_175904854
VERSION     WP_175904854.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Upton,C. and Buckley,J.T.
  TITLE     A new family of lipolytic enzymes?
  JOURNAL   Trends Biochem Sci 20 (5), 178-179 (1995)
   PUBMED   7610479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..235
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=24527
     Region          43..214
                     /region_name="FeeA_FeeB_like"
                     /note="SGNH_hydrolase subfamily, FeeA, FeeB and similar
                     esterases/lipases. FeeA and FeeB are part of a
                     biosynthetic gene cluster and may participate in the
                     biosynthesis of long-chain N-acyltyrosines by providing
                     saturated and unsaturated fatty acids, which it...;
                     cd01836"
                     /db_xref="CDD:238874"
     Site            order(53,90,118,209,212)
                     /site_type="active"
                     /db_xref="CDD:238874"
     Site            order(53,209,212)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238874"
     Site            order(53,74,118)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238874"
ORIGIN      
        1 mgypfataal gpllfaqgry vrrvtprlpe aagprdgvag dgpplrvlvv gdsaaagvgv
       61 atqrdalagq lahalaathr vswkllartg lttgelvewl aaepaepfdv avtslgvndv
      121 tggvtparwl aqqaelvrll aarfrvghai lsavppmerf ralpqplawy lglrakrlna
      181 alagwaaalp hctflrvdlp lerhlmaadg fhpgeaacaa waaqvaaavr qraaa
//
LOCUS       WP_175904866             537 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia seminalis].
ACCESSION   WP_175904866
VERSION     WP_175904866.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..537
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53662
     Region          23..500
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,279,282..283,286..288,291,319,323,375..376,
                     380,384,400,403..404,407..408,411)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mdhpvsavsa qsarrrawvl aavcmaaval plsfsggava tpaigrdlhg spvamnwitn
       61 afmlafgsfl masgaladqf grkrlfaigv ggftlmsval afapsmlavd llraaqglaa
      121 aaalaggtas laqefdgaar trafsllgtt fgiglafgpv lagglighyg wraifvtsav
      181 agvvslvfgl prmhesrdph atgldwpgta aftaaltlft fgvieaparg wssalviall
      241 agaalgaaaf vaietrvarp mldlslfria rfvgvqvlpv stcccyivll vvlplrfigi
      301 dgfseidagw lmlaisapml vvpfvaatlt rwlsagvisg lgllvaaagl vwlgialrgg
      361 agpaaiapml aigvgagmpw glmdglsvsv vpkeragmat gifsttrvag egialaivga
      421 vlaalartgl tqaagaagtp datlraaarl atgdlagaaa alpgvghaal iasyahafdr
      481 llaalavvtv lcaavvfvfl ggrvavaeap etpeagegag asargriepa caethgr
//
LOCUS       WP_175904877             221 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            seminalis].
ACCESSION   WP_175904877
VERSION     WP_175904877.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..221
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23693
     Region          29..187
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpprhvqvpa ppgqpaaqpa palrrrprqs raqassdalq qafvqlller gyakatirei
       61 aavagvsigt fyeyfgdkqs laalcihrrv qaladrlrda aerlrgapra elaaalvdlq
      121 vdaiaadaal wgalfvlerq vsplaayrrh ydayvalwrd alaqaadppp aarldglarm
      181 aqticyggls qalltlgpal dfaaqrrelr avllaylaad a
//
LOCUS       WP_175904959             364 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia seminalis].
ACCESSION   WP_175904959
VERSION     WP_175904959.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..364
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38586
     Region          86..311
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mtvdtytapp gavlshqdal acpgtllapd gtlvapydle sgnlradghv paaptlgllh
       61 aahrpfrldy gdarhvhain amgvtlgdsv igltavaalr aahpglrftl yrparapryv
      121 ealyalaadv vapsrplpyp adalpadapc idvgnhlywp afarlpmidf fldalgvdpa
      181 avpaaakrnr wlarlplpal paawqrpyvl fcpnastavr svppalraaf verlvqrygl
      241 pvagfgpvah pdyvdvsgda tdtarfiawv kgasllfapd taalhladgf dvptlacftt
      301 igpalrvrdy phcvpvelel paelhglhrs erpddlaave aayrkidwdg lpwpaprdaa
      361 aatg
//
LOCUS       WP_175904999             164 aa            linear   BCT 11-JAN-2025
DEFINITION  TadE/TadG family type IV pilus assembly protein [Burkholderia
            seminalis].
ACCESSION   WP_175904999
VERSION     WP_175904999.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..164
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=17169
     Region          2..138
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mtfsrlasgi rrrergatai efalmlpvff lilyaiityg mifaaqqnlt laategaraa
       61 lnyqqvgaaa svpaaqqaal aaraqaacta atnlttwlkg atctptqqgs csydttmlcv
      121 qitltypysq nplvppfpll gsllpvpsal igtamvqisp vnil
//
LOCUS       WP_175905021             187 aa            linear   BCT 11-JAN-2025
DEFINITION  flavodoxin family protein [Burkholderia seminalis].
ACCESSION   WP_175905021
VERSION     WP_175905021.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..187
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=19668
     Region          4..185
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mseiaivfhs gyghaaviad avargvekvd gasvklipvd aidehwtyle rdadaiifgs
       61 ptymgsasaq fkgfmdassk ywgkwrdkla agftvsasqs gdklstlqql avfaaqhqml
      121 wvslglmpgn nsstgsvndl nrlgsflgam aqanadqggd ailesdrkta evlgervaia
      181 akrwsga
//
LOCUS       WP_175904996             561 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia seminalis].
ACCESSION   WP_175904996
VERSION     WP_175904996.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..561
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=60479
     Region          7..560
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mksrldrwmm llaitaasta haqsrvggnp ldslpqinap ktgpnvtvqv apqapqlqel
       61 lsrhltpstf qvegvksvpf eeisrrftpl vgkditigdl ietangvtkl yqergyalsf
      121 afvpaqtfen gvvritvveg yvsdvkvtgk pgamepkira iaahitddrp lrratferyv
      181 ntfgllpglt vkanvpppqt tdgattlela vdrkpfnvst gidfnhpgvq glitatengl
      241 trfgeqlsis alappgrdkq tyfafsgavp vgssglitrl dastyrgkpt dnpglpstvq
      301 rtvkneklgl sasypillnn qrsllgtvsg yaahnedhyq nqingntldn rsqvrvlqlq
      361 ldytsvepkq vrklsvnvak afdilgasks qtglvngvgv tyadptsltf vrtgatvtqt
      421 newpfrigts vsltgqyspd slptseqisf gstryalgyq pgeasgdsgw gmsleinrgf
      481 tpgwtylksi tpyvaydmar vylhsgtpsp nrmssvgigv rftdsrfysl dlnvakpigd
      541 apvesasrsp rinaafsyql n
//
LOCUS       WP_175904906             176 aa            linear   BCT 11-JAN-2025
DEFINITION  SET domain-containing protein [Burkholderia seminalis].
ACCESSION   WP_175904906
VERSION     WP_175904906.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Qian,C. and Zhou,M.M.
  TITLE     SET domain protein lysine methyltransferases: Structure,
            specificity and catalysis
  JOURNAL   Cell Mol Life Sci 63 (23), 2755-2763 (2006)
   PUBMED   17013555
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Dillon,S.C., Zhang,X., Trievel,R.C. and Cheng,X.
  TITLE     The SET-domain protein superfamily: protein lysine
            methyltransferases
  JOURNAL   Genome Biol 6 (8), 227 (2005)
   PUBMED   16086857
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Yeates,T.O.
  TITLE     Structures of SET domain proteins: protein lysine
            methyltransferases make their mark
  JOURNAL   Cell 111 (1), 5-7 (2002)
   PUBMED   12372294
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459262
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..176
                     /product="SET domain-containing protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19537
     Region          1..143
                     /region_name="SET"
                     /note="SET domain-containing protein (function unknown)
                     [General function prediction only]; COG2940"
                     /db_xref="CDD:442183"
ORIGIN      
        1 mssrriavrr sgvhgkgvfa vapikagerv veykgerisw kealrrhphd psepnhtfyf
       61 aldeggvidg kidgnsarwi nhscapncea eevkgrvfih alrdigpeee lfydyglvid
      121 akltkklkre yachcgaatc rgtllatsde ggkkkkkkdr kdgksesksk dkkskk
//
LOCUS       WP_175905058             352 aa            linear   BCT 11-JAN-2025
DEFINITION  permease [Burkholderia seminalis].
ACCESSION   WP_175905058
VERSION     WP_175905058.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..352
                     /product="permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=36745
     Region          61..346
                     /region_name="YraQ"
                     /note="Uncharacterized membrane protein YraQ, UPF0718
                     family [Function unknown]; COG0701"
                     /db_xref="CDD:440465"
ORIGIN      
        1 mtttrtqpnp algwitflli avaglfyvkw fpyynkafva aehhsigqsi lmgtsasape
       61 pslkaaldya waygkaiwqa mvlglllgsa vqallpahwv arvlgrtgfg svaaggllsl
      121 pgmmctccaa pvvaglrarh aspggavafw lgntvlnpaa lvfmgfvlgw hwsalrlvlg
      181 iamvfgigyl lnriarpedg slddaqlaal aagqaaagnp fvrwvkslar mavrlvpeyi
      241 vlvlllgaar awlfphigpd ignhlgwiva favagmlfvi ptagevpiiq amlslgmgvg
      301 paaallmtlp pisvpslaml arsfkpymla ivatlvvvfg ivsgllaial gf
//
LOCUS       WP_175905082             194 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia seminalis].
ACCESSION   WP_175905082
VERSION     WP_175905082.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..194
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=19681
     Region          1..193
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mkmnllrgcv aagiasvalv psvshafdge lafygsisdv tcningvapg agnrkevqlg
       61 dninpskfdk igatstpvpf nlvlggnagc vdgtkvvief dpfsvnvnpv tgnlklvgtk
      121 paegveiqis dagngktgki vlgkpqnlad aqvatigknt atlaysaayv staepaaikt
      181 gsgnsfiryt layh
//
LOCUS       WP_175905100             282 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia seminalis].
ACCESSION   WP_175905100
VERSION     WP_175905100.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..282
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29951
     Region          7..260
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtrstaalaa rglsvgyrdh vvidgldlsi aagrvtalcg pngcgkstll rtlaglqpar
       61 aghvevngrp lasfrrrala reltmlaqfn qipsgltvre lvaygryayg gflrglsrad
      121 haaidealdt sgladdaerd vgalsggerq rawiamalaq qapivlldep ttyldihhql
      181 dildalrtln rtrgltivwv lhdlnqaaay sdeivlmrag rlvaqgtpda mldparlraa
      241 fgvdmlklah prtgapmcvp aygpttdgap raagvydrdl av
//
LOCUS       WP_175905143             326 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia seminalis].
ACCESSION   WP_175905143
VERSION     WP_175905143.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..326
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=35649
     Region          130..324
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mssatllalm falicaaagl llwrgsqvre grahtqrffd srvgqgarte lpagdartmr
       61 taaagmvnaq aseqgfarwr slvfdawtvl sdragldevr aglvlglaii allalwagma
      121 ggmlaaaaaf iaggvlvvlw itsrisrrrl kivrqlpsfl dgivrlvtlg nsvpaafqsa
      181 lqtaemplrr clddvsqmlr sgveidraml hiahtyrire felvgavlrl svryggradv
      241 mldrmstfmr dleqaerels amsaetrlsa wvlallpiav gsfvistspr yftamwndds
      301 grqliylafa lqaiggfwly rlarlr
//
LOCUS       WP_175905182             126 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Burkholderia seminalis].
ACCESSION   WP_175905182
VERSION     WP_175905182.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 126)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..126
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=13629
     Region          23..>80
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(33,36)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mpalnldtda driaerladp gtllvaclca ewcgtcrdyr tafdqladah pdacfawidi
       61 ethadrlddl dvenfptili edantarffg tvlphaaive rmlsdlsavp gaphapklrd
      121 vlavea
//
LOCUS       WP_175905291             320 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175905291
VERSION     WP_175905291.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..320
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34522
     Region          9..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,161,163,225,242,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,190,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdtlvsmnvf ryvvevgsfv gaaermqmsa amaskhvmhl eqqlgarllh rttrrvapte
       61 agreyyerlv qalseldeag qavgaasvvp qgrlrvtsls afglrhvmqa vtdyagrfpd
      121 vtvdmtlsdr vvdlieegyd vavraapngl kssslvarqi atahillvas paylekhgtp
      181 qtiadlahhn ylrrdsnstm ldslvidaaa asrvnlngnl ivnhleglra avlagagial
      241 lgtevvgddi esgrlvpvll dsvppheapi yavyasrrhv sakvrsfvdf laarfegqsl
      301 cpsiesrlrv lpiarmkrvv
//
LOCUS       WP_175905234             369 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia seminalis].
ACCESSION   WP_175905234
VERSION     WP_175905234.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..369
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38882
     Region          1..365
                     /region_name="LhgO"
                     /note="L-2-hydroxyglutarate oxidase LhgO [Carbohydrate
                     transport and metabolism]; COG0579"
                     /db_xref="CDD:440344"
ORIGIN      
        1 meqmdcvvig agvvglaiar elaargreti vleaadaigt gtssrnsevi haglyyargs
       61 lkatscvhgr dmlyefceth hvphrragkl lvatsaaqvk qlkaiaaraa engvldllpl
      121 traeaqtlep alecvealfs pstgivdshq lmlallgdaq rdgamcalks pvdsidvlrg
      181 grfvvrtggd apteieaacv insaglgaqa larrtrgldp rwvpplylar gnyfslsgra
      241 pfshliypmp draglgvhlt ldlggqarfg pdvewcdslr yevdparaga fyasirafwp
      301 glpdgalqpa yagirpklag pgeppadfiv qgaaqhgvrg lvnlfgiesp gltaslalaq
      361 rvgemtayr
//
LOCUS       WP_175905205             404 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent rRNA methyltransferase [Burkholderia
            seminalis].
ACCESSION   WP_175905205
VERSION     WP_175905205.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..404
                     /product="class I SAM-dependent rRNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=43389
     Region          3..403
                     /region_name="RlmK"
                     /note="23S rRNA G2069 N7-methylase RlmK or C1962
                     C5-methylase RlmI [Translation, ribosomal structure and
                     biogenesis]; COG1092"
                     /db_xref="CDD:440709"
ORIGIN      
        1 mqtvtlkpsk eksllrrhpw vyanaidrvd gkpapgatvl vrahdgrfla rgayspqsqi
       61 rvrvwsfdeq epidhaffkr rvqravahrt tmvsgtgavr lvfgeadglp glvvdyyvad
      121 taeagaaprg qlvcqfmaag veawkdaiva altgatgcpn vyersdvsir dkeglaqttg
      181 vlagdappat lisnengvry hvdvpnghkt gfyvdqrdnr alvaqyaagr dvlncfcytg
      241 gfslaalkgg atrvvsidss gdalalaqqn vvangfdaer atwldadafk tlrrlvdege
      301 rfdlivldpp kfaptrdsvd raaraykdin lsgfkllrpg gllftyscsg aidmdlfqki
      361 vagaaadakv darilkrlga gvdhpllaaf pegeylkgll lqiv
//
LOCUS       WP_175905304             212 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia seminalis].
ACCESSION   WP_175905304
VERSION     WP_175905304.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..212
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22784
     Region          4..195
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mnayrlylsp gacslavhia leetgapfdi eivsvqkqen laapylaina karvpvlaip
       61 geprvltetp ailtylarry pdaqllplgd plrearchew lawlvgwvhg vgygalwrpg
      121 rfigdpalhg avsahsrgti eaanasieaa ladgrtwaep aahsivdpfl lvlyrwgaai
      181 gldmaqhaaw tahaqreaer paarralare ag
//
LOCUS       WP_175905283             396 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia seminalis].
ACCESSION   WP_175905283
VERSION     WP_175905283.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..396
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=42098
     Region          18..381
                     /region_name="MidA"
                     /note="SAM-dependent methyltransferase, MidA family
                     [General function prediction only]; COG1565"
                     /db_xref="CDD:441173"
ORIGIN      
        1 mnpkahepas lpapgpdala qsetlaaqlr deiaaaggwl pfdrfmeral yapglgyysg
       61 garkfgrrad dgsdfvtape lsplfaqtla qpvaqalaas dtrrvmefga gtgklaagll
      121 aaldaqdvel deylivdlsg elrerqrdti aaaapalaak vrwldalpgr fegvvvgnev
      181 ldampvrlfa kaggawherg valdarqafv fddrpadaag lppalagldv gdgyvtethe
      241 aalaftrtvc tmlargavll ldygfpahey yhpqrdrgtl mchyrhhahd dpflypglqd
      301 itahveftgi ydaavatgad llgytsqarf llnagitdal aaidpsdira flpaanavqk
      361 liseaemgel fkviafsrgi dgtldafarg drshal
//
LOCUS       WP_175905328             548 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Burkholderia seminalis].
ACCESSION   WP_175905328
VERSION     WP_175905328.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..548
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58404
     Region          13..529
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 maaatptgal valhhvsfrf ddgvtlfdsl dltidrtptg ivgrngvgks llaqliagrr
       61 apsagaierh tpavyvaqqh ddgnaaanpr tvsqvaalda plgalarlah graeprdfdl
      121 igdrwdlaer lrtaldaagl hdarpdtpah alsggqrarv aligallsga gllvldeptn
      181 hldapgrawl raaldgwrgg lvivshdral ladvqrivel tpqgvrsygg nyafyraqrn
      241 adqdaaqaal dnaraergra rrrleqehdt iqrhaaaslr daktanlssg akqsrkgaar
      301 nimgqvrrhq ndfkatlder vqqaaarvea dapvlvslpg tevsarrqlf tlerarlpwd
      361 iagaadaitw sasgpvrial tgpngcgkst llrmlagela prsgtctthv saayldqrlt
      421 lldperstve qlglldtpla egelrsrlal lqldatratq parqlsgger lkaalacalw
      481 rgapaqllll deptnhldle svraieaala gfpgaivvas hdaaflaale pthtmqwhrd
      541 gwhyepva
//
LOCUS       WP_175905414             344 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia seminalis].
ACCESSION   WP_175905414
VERSION     WP_175905414.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..344
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36277
     Region          109..316
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mkivkpllia aavaatlsta paafaagadt irpdtktsaf laalngqkgp gletlspaka
       61 rqvlvdaqng vkvdlsgidv snrtieqdgv svpvtivrpq gatgtlpvfm fihgggwvlg
      121 dfptherlvr dlvvqsgava vfvnytpspe ahypvainqa yaatkwvaah gaeigvdgsr
      181 lavvgnsvgg nmtavvalma kdkggpairf qglmwpvtdh nfntgsynay qqghfltrpl
      241 mkwfwdaytk deaqrneiya splrastaql kglppaliqv aqfdvlrdeg eaygrkldaa
      301 gvdatttryd gtihdfglln aladdaptka atkamaneia trlk
//
LOCUS       WP_175905418             241 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia seminalis].
ACCESSION   WP_175905418
VERSION     WP_175905418.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..241
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26079
     Region          10..235
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mieiraanqr graehgwlss rhtfsfanyy dpkqvgfsdl lvinddrvap grgfgthphr
       61 dmeilsyvld galehkdsmg tgsvivpgdv qlmsagtgvr hsefnhspdt pvhflqiwvg
      121 paekgaepry qqtnvaaddk rgklalvvsp ngdagslkir qdtriyaglf dgdesttlel
      181 dpsrfayvhv argsvtvngv tlgegdgari rgeqaltiad gqdaevlvfd lrpvevtaew
      241 a
//
LOCUS       WP_175905455             136 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia seminalis].
ACCESSION   WP_175905455
VERSION     WP_175905455.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..136
                     /product="VOC family protein"
                     /calculated_mol_wt=14896
     Region          10..119
                     /region_name="VOC_like"
                     /note="uncharacterized subfamily of vicinal oxygen chelate
                     (VOC) family; cd07246"
                     /db_xref="CDD:319910"
     Site            order(10..15,17,32,48..49,51..53,64..66,68..73,79,100,105,
                     113..116)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:319910"
ORIGIN      
        1 matfqpdgwh tvtprivvpd penliafvrt vfdargeyra glpadirigd svvmisggdg
       61 lrdpmpafly vyvedtdaih rravaahais leapadmpyg drramvkdpw gnlwqiathq
      121 rdlsadeira rlagge
//
LOCUS       WP_175905464             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175905464
VERSION     WP_175905464.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33716
     Region          23..80
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          109..303
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(124..125,127..128,131,135,137..143,233..238,
                     244..245,247..248)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 misdddrefd shsiranlps lmalrcfeaa arhenfsraa delyvthgav sravrvleed
       61 lgvllflrrs rrvfltdagr klaqavhdgl glmrratlel rseaararrw vlsceptllm
      121 rwliprwpdf qarhpgvdih lvaaggpfsf dsgidmairr ndfawpagyh aeplfaeqvg
      181 pvcrpdraga wfaarrgqra lkpdapllha rtrpdawktw avaagqpaas rrgqtfdhfy
      241 fslqaavagl gvaigpwhlv rddiengvlv apmgfvedgs hyclltpapv vdgsasaals
      301 gwlkava
//
LOCUS       WP_175905470             350 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia seminalis].
ACCESSION   WP_175905470
VERSION     WP_175905470.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..350
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=37412
     Region          <54..>169
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(72,74,78..79,82..84,86..87,90,93,102,104,106,
                     110..111,114..116,118..119,123,126,135,137,139,143..144,
                     147..148,153,155..156,160,166)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          72..102
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          104..135
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          137..169
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mskakkkllp kdfdalldeg dlaklmavfd tcdvnarggp skrtalsfdr cpdelarwlv
       61 aqgadigaad aygntalhvr arsrrsrfdv llelgadvhd dgapigtalh aaadarhaes
      121 arlllahgar vdalnrdght pleralrtcg naglvhmval agvlldagaa ktpsmrtsva
      181 eigerfefmr erfnpeavda asaalarlya lfdvppvprr rlhdgrspiv vadgpwqaqh
      241 qalwaqlvpg tghaatvqge lvriagriah eldhngggnw dadfremada fasivrtgts
      301 lpaadlsdvd avvqdvkrqa gdpaqlcrla vawvrlnpdp velappsyrr
//
LOCUS       WP_175905490             190 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter small permease [Burkholderia seminalis].
ACCESSION   WP_175905490
VERSION     WP_175905490.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..190
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=19806
     Region          37..185
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mtrrtslnga aaggssaaap dgagparpha apflrcvndv lfrvlavias aclavltvlv
       61 fyavvmryvf enapdfvepi alllviviam fgaamkvrdg ghigldslvr rlspkardvv
      121 vgiqhlslia favmimvgcg smaaetmgdr ipiiglpegv ryliampaav aiilfslehl
      181 lalrrsssgq
//
LOCUS       WP_175905495             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia seminalis].
ACCESSION   WP_175905495
VERSION     WP_175905495.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..359
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38044
     Region          159..356
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mtkvflilvr nellgylrsr sslfwtlvfp vfllsvmlfa fggsgslgta diafdvpggp
       61 tpysraceag iveslthsdt vkatfggrga padrvtvvlg adertpttir ydfngslavk
      121 aasrvveial arcaaqrlgl paaqarfena aparrpfdyg affatgilvm afmaiglnst
      181 ttaiaslrer ntfklyvcfp vsrgvflaal ivarmvmmal salvlltvar vafgialpia
      241 tpdglralpv vllgaamvls igvllasrtr slaaaelacn vtyypllffs dltipmhdap
      301 awlkaalafl ptnqfavalr galvdgapya qlapqllgmt actalflfaa arlfrwhda
//
LOCUS       WP_175905505             327 aa            linear   BCT 11-JAN-2025
DEFINITION  ferritin-like domain-containing protein [Burkholderia seminalis].
ACCESSION   WP_175905505
VERSION     WP_175905505.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10090058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..327
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36625
     Region          98..228
                     /region_name="Ferritin_like"
                     /note="Ferritin-like superfamily of diiron-containing
                     four-helix-bundle proteins; cd00657"
                     /db_xref="CDD:153097"
     Site            order(107,137,140,187,217,220)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 mtdtltvmqd tadirwsmpv dalmsndyal reealnrlye kakaaqwdva tdvdwrhdld
       61 panplgmpdp tlliygtelw aklsdadkre vrhhaqgwll sqilhgeqaa licasklasa
      121 eeglsarlca aaqmmdearh veayaklvne kldvsypmsr slkgllhdti tssaldmtnl
      181 gmqvlvegia lsifqsvvay stdpfikdlf lriqrdesrh favgritlcr vyaemsatel
      241 rereqfvceg aavlyehlca ddiwepmgls krecsamvre spvsssirrs ifrrlvptir
      301 emglltptvq atfekldvld yaampln
//
LOCUS       WP_175905547             162 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175905547
VERSION     WP_175905547.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 162)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..162
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18121
     Region          8..148
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 msknrasvel dgvdramlrl lqedgalsna tlgeklslsv tpcwrrrkrl edervitgyq
       61 anldrralgm nvfafvqvtf nmhsdqdpdh feevmrrhde vtschkitga adyllqvvaa
      121 dldayaefve rvlrkqagvs siqsslalre vkfssrvpvp da
//
LOCUS       WP_175905577             374 aa            linear   BCT 11-JAN-2025
DEFINITION  J domain-containing protein [Burkholderia seminalis].
ACCESSION   WP_175905577
VERSION     WP_175905577.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10644999
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..374
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=42439
     Region          <209..249
                     /region_name="DnaJ"
                     /note="DnaJ molecular chaperone homology domain;
                     smart00271"
                     /db_xref="CDD:197617"
     Site            order(225..227,236,242..243,246..247)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
ORIGIN      
        1 mtarrgaavv iapghetasl skaqktfntl vkqieqrrer lgawdavmpa fqkkfvdgll
       61 pleqastalr irllnlldda flqkglskae qhtlsaliad marnlldfsd daqlkviynr
      121 haksdddrpa anrapakqha eptpdvapad dldtlspdel aermqaelde qfardmaahe
      181 areaqrakrr kaprqsaaaa rreaeqaess ksireiyrkl asalhpdret dpqeqarktv
      241 lmqrvnhaya kgnllqllel qleieqidrr aidglsedrl tryngileeq ireldqeirh
      301 vendfrrtyg iapsvklapd tvmrtltrdi aamqrsnhdl tvalrefddl envrdwlkdm
      361 krrpassrfd ddsf
//
LOCUS       WP_175905596             432 aa            linear   BCT 11-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Burkholderia seminalis].
ACCESSION   WP_175905596
VERSION     WP_175905596.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..432
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=45675
     Region          3..412
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mkkkhnitky iviammlgia vgyachsafp dpkmakevag yvsllsdvfl rlikmiiapl
       61 vfatltvgia qmgdgsavgr vgikafgwff iasftslllg lltatilqpg shlslplpps
      121 daalnlktga ftlkdfvvhl vpksiaeama nneilqivvf siffgtalsa lgdagkrltg
      181 viedlaqvml kvtgavmgfa pvavfaalas titteglgil ltfakfmasf ylalallwgv
      241 ltlagvtflg kraftlirli repfllsfat asseaaypkl ldaldrfgvn rkissfvlpi
      301 gysfnldgsm myctfavlfi aqvygihlpl gtqitmllml mvtskgmagv praslvviaa
      361 tlnqfnlpea glllimgvdm fldmgrsatn avgnsiaaav vakwegqlge prddndsggg
      421 tvtevkvret sa
//
LOCUS       WP_175905591             342 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175905591
VERSION     WP_175905591.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..342
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35878
     Region          11..109
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(55,58,62..63,72,91,95,101,105,108..109)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mntstrrlna saaaaqlgvs tkalrlyeqh glvmpertpa gyraygpddl araadiaalr
       61 klglslaqva dvldgdarsl daalaaheaa ldrgvqdlvr kmdrvraira glargrmpag
      121 geltrlldds gtgvafslpw pwggewfecr dirplnyiig slgsgktrla lrladalpga
      181 vfvgldrldd dcaaasnalr adpelksrvd raaallaakg atlspaltal lvsleaqgpr
      241 aqivdmieqg ldratqlali ahlregaaag mrplslfllt rssaildlaa vgpdetillc
      301 panhspparv apypgapgye avatclaape vreriarrpm ta
//
LOCUS       WP_175905597             244 aa            linear   BCT 11-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Burkholderia seminalis].
ACCESSION   WP_175905597
VERSION     WP_175905597.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..244
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27078
     Region          71..225
                     /region_name="CE4_NodB_like_5s_6s"
                     /note="Putative catalytic NodB homology domain of PgaB,
                     IcaB, and similar proteins which consist of a deformed
                     (beta/alpha)8 barrel fold with 5- or 6-strands; cd10918"
                     /db_xref="CDD:213023"
     Site            order(74..75,140,144,180..182)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213023"
ORIGIN      
        1 mlartprypi lmyhqirplp ppadrlrgls vapdafrrqm tlfkrlgyrg lsvrelrpyl
       61 rgersgkvfg isfddgflnv lthampvlda lgftatcyfv agrfggqndw daaddtarsp
      121 lmtcedmlvw rdhghevgsh tldhvalsqv pafesdhqvs eskrrleals gqrvesfcyp
      181 ygdldarvrd qvadarydna tttrrgcaga addpfllpri pvaggvgaar lwlkcvkarv
      241 marg
//
LOCUS       WP_175905620             177 aa            linear   BCT 11-JAN-2025
DEFINITION  2,4'-dihydroxyacetophenone dioxygenase family protein [Burkholderia
            seminalis].
ACCESSION   WP_175905620
VERSION     WP_175905620.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14449000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..177
                     /product="2,4'-dihydroxyacetophenone dioxygenase family
                     protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20083
     Region          37..160
                     /region_name="cupin_DAD"
                     /note="2,4'-Dihydroxyacetophenone dioxygenase (DAD), cupin
                     domain; cd20302"
                     /db_xref="CDD:380436"
     Site            order(53..54,57,63,65,82,84,86,88,101,104..108,110..112,
                     129,135,137,145,148,151)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:380436"
     Site            order(77,79,94,115,130)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380436"
ORIGIN      
        1 mvdqavsefw qntpaianpf kpdalpeayi pnaatddery yvpftetvss rplwispsqn
       61 kwcdilmake aglvnrhyhp hevfaytlsg kwgylehewt atkgdfvyet pgeghtlvaf
      121 dhpepmraff ivkgpliwld degnpdgyfd vhsyiamcka hyekvglgaq aveklfr
//
LOCUS       WP_175905621             434 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia seminalis].
ACCESSION   WP_175905621
VERSION     WP_175905621.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45427
     Region          7..406
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mtssspsrsa wtyenrllli lfmtfgfvff drlalsflfp fmsaelhltn tqlgmvssal
       61 altwalsgaa tgawsdargt rkplliaavl gfsvcsalsg lvggfaslia fralmgiaeg
      121 pvlplsqslm vesstpsrrg lnmgllqgsa agllgamigp pvvigiatay gwreafyvsc
      181 ipgfliafci wrwvrevppg garhvqadga gapaasgaai nrwallkern illcvliscf
      241 fltwfvviis fapvflvesr hlspsdmgvv mtclgaawvf wgfavpaisd rigrkptmia
      301 faliaavcpm vmihvgsvwa lgalvfvtyt glgcftlfma tipaetvppr aiasalglim
      361 gageliggfv aptvagfaad kyglqfamwt satgailacv lsfglvetap avlrkralag
      421 aaasrldtpn lggr
//
LOCUS       WP_175905635             273 aa            linear   BCT 11-JAN-2025
DEFINITION  siderophore-interacting protein [Burkholderia seminalis].
ACCESSION   WP_175905635
VERSION     WP_175905635.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..273
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=29728
     Region          5..266
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mqnpsertvt rvrhtlkfrl lqvlrvqavt phllrvtlgg pdladfesas fddhvkvffp
       61 ppgaerpamp tlgangpefp egepkpvard ftprrfdraa celdlefvln hpgpasqwaa
      121 qarigqwlgi ggprgsfvvp tgfdwhllig ddtalpavar rleelpagar aavvlevadr
      181 aaqisfdtra dvhevwrfra etdaadgdal lnavrdlplp ssgdgyvwaa gealsmravr
      241 qhltgergid ksriraaayw krgaaavhet led
//
LOCUS       WP_175905646             290 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia seminalis].
ACCESSION   WP_175905646
VERSION     WP_175905646.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..290
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31454
     Region          15..280
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mttarsldrt ypalrttegg gfvvhrpfpt rllmdfdpfl lldemgpvdy apgeavgapd
       61 hphrgfetvt yaldgrfrhr dssghagtlg pgdvqwmtag agvvhsempd pafaqaggra
      121 hgfqlwvnlp rrdkmiapry qeipaeript atspdgrarv rviageafgv qaaietrtpi
      181 lyqhftlepg atvtqpvpag yrvfaypidg tglygpdrqa vdaqhmivyg ddgdtvtfaa
      241 gdtpldllli ggvplnepiv rygpfvmnte eeirqavvdy qtgrmgriea
//
LOCUS       WP_175905673             410 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia seminalis].
ACCESSION   WP_175905673
VERSION     WP_175905673.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..410
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42724
     Region          12..394
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(22..23,26..27,30,65,112..113,115..117,120,145,
                     148..149,152,224,227..228,231..233,236,266,270,320..321,
                     325,329,345,348..349,352..353,356)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mtpieqevrr rwlpvlaggl imgaalgirh vqglflapvs ldhgwsreaf glalalqnli
       61 wgvaqpftgm iadrfgsarv ivagmllyag glvtmahaat tglftvgagl vigialsgsa
      121 fasiygalsr lfppdrrgwa lgvagaiggl gqfcmvpvaq tlisgigwrd afialalvaa
      181 llaplavllr drpvqaadaa agpgqsigea vreafahrgf wllnagffac gfqlafiath
      241 lpaylldhgl parhasvala lialtnvagt yacghlggll rrkyvlsvly lvralamaaf
      301 vaaplspasv yvfaavmgft wlgtvpltng visqvfgvry iatlfgfvff ghqlgsffgv
      361 wlgavvydat hsymplwigs ialgvlaall hlpindarva rpasanaawa
//
LOCUS       WP_175905714             234 aa            linear   BCT 11-JAN-2025
DEFINITION  TerC family protein [Burkholderia seminalis].
ACCESSION   WP_175905714
VERSION     WP_175905714.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..234
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24537
     Region          12..191
                     /region_name="R_switched_YjbE"
                     /note="integral membrane protein, YjbE family; TIGR03717"
                     /db_xref="CDD:163429"
ORIGIN      
        1 mlefltslhw gailqiivid illggdnavv ialacrnlpa nqrlrgvvwg tagaillrva
       61 litfavalld vpflklgggl lllwigiklm apaadahddi kpasrlwdav ktiviadavm
      121 sldnviaiag aaeqadpshr ialvifgliv svpiivwgst lvlklldrfp ivvafgagll
      181 gwiagglivn dpvgdrwavl dtqpvlygas iagalfvvai gyalrkrhga phar
//
LOCUS       WP_175905765             520 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Burkholderia
            seminalis].
ACCESSION   WP_175905765
VERSION     WP_175905765.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..520
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54420
     Region          24..520
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mpspirsses ldvdallaal prriadvpar waaqapahpa liedarrlsy gelaqavdaa
       61 aarlaslgvq ggdrvmivae ncvaqivllf aaarldawal vsnarlsage ldaiaahaqp
      121 klvafttdas pdarahaarl gatpagalpv digawsyrvg agtpaepvaa dgaaqcaali
      181 yttgttgtpk gvmlshrnll fiaatssalr rvspddvvyt vlpvshvygl asvclgslya
      241 gatlrlaprf speavrvala degvtifqgv pamhaklleh lhthghawha prlrfaysgg
      301 spldanlkar verqygvplh ngygmtessp titqtpldap radssvgvpi pgvelrivap
      361 dgtdvppgev geirvrgpnv mlgyyrnada traavspdgw lstgdlarqe adgavtiagr
      421 skeliirsgf nvypveveqv lnahpdvvqa avigravegn eevlafvelv pgasadetvl
      481 hawcaerltp ykrparirvl dalpaastgk vlkhrlrdla
//
LOCUS       WP_175905822             337 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175905822
VERSION     WP_175905822.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..337
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35872
     Region          32..327
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mrpagrpagr ppdpnriaiv skssekldla traawlyyva gdtqneiaek lqvsrpvaqr
       61 lvafaveknl irvrvdhrla dcldlgaqls kryglamcev vpvdadapda idrklavaga
      121 qvmerylnet rpmviavssg rtlkaavaqi aqidrpqhrl vsmvgaiaad gssnrydvaq
      181 yisektgskh fllpaplfad sdaeraqwcn hrlyriveal sgqadvafvg ignigphcpl
      241 yedgfiteqe rdemtalgav aellgvpida hgtqitvsts arvtsvalat ppklptiafa
      301 ggpkkhdavi aalrggwlsg lvtdetcara alaakaa
//
LOCUS       WP_175905847             403 aa            linear   BCT 11-JAN-2025
DEFINITION  benzoate/H(+) symporter BenE family transporter [Burkholderia
            seminalis].
ACCESSION   WP_175905847
VERSION     WP_175905847.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..403
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41371
     Region          15..403
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mnpsptasag rvggrrffad tsvsalvagf vammtgytss lvlmfqagra ahltdaqiss
       61 wiwalsigma lttiglslrf rapvvvawst pgaallvasl pgvpyaeaig afvvcalllt
      121 avgvsglfdt lmrripagia aallagilfe igieifraaq fqtalvlamf ftylivkrla
      181 pryaivttli vgtavagglg lldfsrfhia laqpvftmpa fsiasivsig iplfvvamas
      241 qnvpgiavlr adgyptpssp liattglasl llapfgshgv nlaaitaaic tgpeahedha
      301 krytaavwcg tfylvagvfg atiaalfaal pkalvvsvaa lalfgsimsg lanamqdvkq
      361 reaalvtfmv tasgltllsi gsafwglvag ivtqvilnar rpa
//
LOCUS       WP_175905919             361 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia seminalis].
ACCESSION   WP_175905919
VERSION     WP_175905919.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..361
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40070
     Region          5..333
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mangnptqri lviridflgd mlcttaflga lkarwpgael hvvanrynaa vlagnpdvha
       61 vhtyvysrqc erndrpgrmr affdrlrlvr rlrrlrfdlv vvpnggmhrs smqfarrlra
      121 kdcrwhdadt efddrkpehv aqrqmcheal sgfrlvpelg radldrlela vhpdrtlqdt
      181 whrllgartk prvglfvsnk averrwpadr wrdlglrlap cadvivfrdp aigkcdvdda
      241 wrdvsarhvt pvsvaelmaa aslldvivsa dsapvhlasa lgvpvaalfe drpekylrwh
      301 plgvphmilr agatvdaigv daveravrhl lpqaghrdep vaaagheqpa aaapaiasta
      361 s
//
LOCUS       WP_175906001             402 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Burkholderia].
ACCESSION   WP_175906001
VERSION     WP_175906001.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..402
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44506
     Region          119..379
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mkmselpave rhvklsqlge fakrlsvmtd elrdqilapr prktapvfti geltdmcgid
       61 rqkinylatk eggslppgea hgtgrsrift laeartwvqq vsnvhqtalv tgqghhrgrv
      121 litanfkggs ckttttmcia qglslrgrrv lvidldpqas lselcglyae kdvtwedtvl
      181 pfiydpaieg glgakvqtty wdgldvipsh nylhdaefhl ptaqkedpey efwsvlrrgi
      241 eplrahydyi ildtapslsy mtlnglmaad amvmplvpes ldfissvsfw slfsevaagf
      301 vehevdktyd fisvllskvd ygttssapvv rswaqraygd wlatteipas svmsngalaf
      361 stvfdlsrsd gvaktlarvk qplmdyckwi ddqyvaqwra ea
//
LOCUS       WP_175906035             312 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Burkholderia
            seminalis].
ACCESSION   WP_175906035
VERSION     WP_175906035.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..312
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32859
     Region          26..303
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mntpaspsap faaeprpapa aapvldivar iaecapelrd aerkvaafil adlaraahas
       61 igalardaev svatvtrfak avgcrdvrel kvlvaqaaav gqrflvpsgd apaedtspas
      121 mvydeirval ahnhqllrnt sfdaaadlla gakmtyvygq gggstalade lrfrlvrfgr
      181 pvasyqdsvl qrmvaatlsr dtvivalsvs grvpellesc rlakrygatl iaitapaspl
      241 akladhlipv vafetdfiyk pstsryammm aidvlvtgva lrlgdagres lrrikhalda
      301 hrgggdrqpv gd
//
LOCUS       WP_175906052             131 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA thioesterase [Burkholderia seminalis].
ACCESSION   WP_175906052
VERSION     WP_175906052.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..131
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14079
     Region          7..131
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mtdstlelpq kqpalrvvpq phdanvhgdv fggwimsqvd iagsipasqr angrvatvav
       61 nsfvfkqpvf vgdllsfyat itrtgntsit vdvevfaqrm rlmgevvkvt eatltyvatg
      121 adrkprqlpp l
//
LOCUS       WP_175906078             246 aa            linear   BCT 11-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Klebsiella pneumoniae].
ACCESSION   WP_175906078
VERSION     WP_175906078.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 246)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 246)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..246
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26247
     Region          6..229
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mnkkvifrga saimplcigd fpfsfivgal svsagmsvwq stvwsaivia gsaqmlalnm
       61 lktgatlgvi ifttliinlr hvlysasisg tvreasffkk cfmsyaltde vyattvkeme
      121 gnkkekylfy gsamitfwai wvladflgal vgasfphiek ygldfamvaa fiaivvpqik
      181 sqactvaavv aavsgvllvv lpyslgivva svlgvlaglc vdlaeerkqm aktesdmplv
      241 eamene
//
LOCUS       WP_175906113             323 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175906113
VERSION     WP_175906113.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..323
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35119
     Region          6..321
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpavprsilv lafpraqlld vsgplqvfas vnelalergr papyaprvva veagpvetss
       61 glvvmaeslr saarhpdtli vaggkgvhaa skdarlvrwv rqqagrarrv asvctgafll
      121 aeaglldgrr avthwarcde faarypnvrv esdpifireg alwtsagvta gidlalalve
      181 edlgratald varelvvflk rpggqaqfsa mlsmqrtddr fgelhawmae hltadlsvpa
      241 laervrmser sfvrhyragt grtparaveq irveaaqrll getawpvkri aarcgfgsee
      301 tlrrsfvrvl gvspqgyrer fvr
//
LOCUS       WP_175906149             311 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175906149
VERSION     WP_175906149.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..311
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34122
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..294
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdkldqvrif lqvaemgsfi kaahaldvpr atvsaavqql etglgtrllh rttrqvqlta
       61 dgalllergr rllaeadeld rlfrrrdrdv vgrlnvdvps riarrvvapa lpslfrrypk
      121 lqlslgstdr sidlvqegvd cairvgrlad sslvvrplgq ftlincaspd ylrecgvpeh
      181 pdalahghwa igyaspttgr elgweycadg qthlltlpsr vivnnaetyi asciagmgli
      241 qiprfdvehl lesgalvdvm pghraepmdv savyphrrhr srrlnafvew fgelmtdalt
      301 gtaagpgteg d
//
LOCUS       WP_175906171             271 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia seminalis].
ACCESSION   WP_175906171
VERSION     WP_175906171.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..271
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29003
     Region          16..265
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtdaapharg gelyctavdl tlkagartll dgftqafrpg eiwcvagpng agkttllatl
       61 aglqppaggr veidgrplaa wrpgplaqrr almpqqlhda fsatvldtvl lnrfpyldgw
      121 gwerdgdraa aydalatfdl talasrdvls lsggerqrva laatlcqdap lmlldeplah
      181 ldlhhqidcl taltawldrg grtvlfschd lnlarrfath allldgrgra sagpvhdvlt
      241 perasdafgy plvlirengr dallpawpar p
//
LOCUS       WP_175906222             455 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia seminalis].
ACCESSION   WP_175906222
VERSION     WP_175906222.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..455
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47079
     Region          19..447
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(26..27,30..31,34,66,116..117,119..121,124,144,
                     147..148,151,273,276..277,280..282,285,313,317,369..370,
                     374,378,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mnadtglplp qrywaivcva lgitlavldg aianvalpti ardlrasdaa siwivnayql
       61 avtitllpla slgerigyrr iyiaglalft aaslgcalag slpmlavmrv iqgfgaagim
      121 svnaalvrmi ypssmlgrgl sinamvvals saigptvasa ilsfaswpwl favnvpigia
      181 avlgslralp anplhdapyd fpsalmnacv fgllitavdg lghgerhayv aaelavafvv
      241 gyffvkrqls qpapllpvdl mripmfalsv ytsmasftsq mlafvalpfw lqnslgfsqv
      301 etglymtpwp lvivfaapla gvlsdrysag ilggiglalf aagllslati gahpgtvdiv
      361 wrmalcgagf glfqspnnra mlssaprers ggaggmlsta rltgqtlgaa lvalifglsp
      421 drgptialyv atafaavaav vsmlritspr pdtat
//
LOCUS       WP_175906232             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175906232
VERSION     WP_175906232.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33257
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 melrqlryfv avaeelhfgr aakrlfisqp alsfdirkfe dtlgvqlfsr tnktvaltna
       61 gevllgearr lllqaaeaer ltvrsasgla grlrigfvhs mlyrglpdav rrfeadypgv
      121 evvlsemnth aqvqaiqrgq idlgyahwgh fppevesmpv yaepfvcclp aahplarrrq
      181 valaalatep filfpreaap hyhdliiaqc vnagfsplir hearlwqtil smiefgmgva
      241 lvprvlqqak sdrlafrplk daslesrtla lkrtgaaepv alrfadyvra sidrlpalag
//
LOCUS       WP_175906324             333 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175906324
VERSION     WP_175906324.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35702
     Region          17..197
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          230..312
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mlysaiylrd stmmsddpfs dilrlanaes latggfsagg awairfpapd kikffavvkg
       61 tcwvcideee tpirfgsgdv glltakrsfv lasdpgvppv damtlfsgag ksavklgdgd
      121 dfahigghvl ldpvtghlls dvlppwihvp atapqavkvr wlleqlmeer aadlpgaqlv
      181 saqlshllfi qilrahlnts aplagwlral snpriapalr lmhgdparaw hldelaaaca
      241 msrttfaahf rasagvaplt ylgqwrmrva errlrdesip vallaqslgy ssesafsnaf
      301 krmsghspta yrhiartaae nigserggvr ges
//
LOCUS       WP_175906336             351 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia seminalis].
ACCESSION   WP_175906336
VERSION     WP_175906336.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..351
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35822
     Region          16..346
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mktvtssakh dappverpra apapirdale rtgillvlvl lvigfalrep aflnvdnlfs
       61 ilqsvsival lgigvtitla aggfdlsvgs vaataqmaas yvlvvwhggt laaviacvtl
      121 gmaaglfngv litrlrvpdq latlgtlflm aglqliptgg rslatgsvlp dgtdatgvfp
      181 daflalgrlr vfdvvplpvl llaaitavac vameatrwgr viyaiggnet aarlagapaa
      241 ryrvaayvvs gaiaslggvl iaarvgrgdv saghslllda vaasligyav wgakrpnvfg
      301 tvvgavfvgv llngltmlna pyymqdfikg allvlalaft fgigrrtdar a
//
LOCUS       WP_175906345             358 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175906345
VERSION     WP_175906345.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..358
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39734
     Region          12..194
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(15,17,102)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(49,101..102)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            100..102
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mstharkpli slvvpfhdee etidaffaet lpvlesvagv rfeivcindg srdrtldrlv
       61 avaardprvh vvdltrrfgk eaaltaglde aagaavilid adlqdppali pamiehwrgg
      121 aevvaakrtd rmcdpylqra aaalyyrvhn alsevempen vgdfrlmdre vvdalralpe
      181 rrrfmkglfa wvgfrtaive ytraprsggr skfsgwrrwn falegitsfs tvplrvwtyv
      241 gitfamlslv ygafivvrtl lfgnpvhgyp slisvvlfvg giqligigvi geylgriyhe
      301 skqrpvylvr rryraerdaa gqpaskllqf plkranaarr rtalpaatgv aarkasfk
//
LOCUS       WP_175906346             320 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175906346
VERSION     WP_175906346.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..320
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34617
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,161,163,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,190,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdtltslrvf cavaelesft aaasrlglsp amtskhvqhl edrlgirlln rtsrrvslte
       61 agalylvqar qaldgldeve aalshvavap rgtlkvsapv wiattrivam ladyhrrype
      121 vrldldlsgr lvnlvdegfd lalrattper ldpgliarpl gridfwlvaa psyiegagri
      181 ariadlndhs lllysgvsig pdlvfngaeg aetvrfrvvm rsgnetllhl aalegmgfai
      241 lpvwmvladi aqgrlqailp gvatvsttly avypsrkyls akvrtfidhl asqdspctwy
      301 ripemaippd avgkgsapar
//
LOCUS       WP_175906352             189 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia seminalis].
ACCESSION   WP_175906352
VERSION     WP_175906352.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008168
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..189
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20494
     Region          3..187
                     /region_name="COG3981"
                     /note="Predicted acetyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:443180"
ORIGIN      
        1 msaiellrpt tallpsyisa leagwspdnv rkeiaareql daididaerf vdglddpaas
       61 gspiplpdgs ivarlpsivr wiwdgdfsga igfrwqvgta elpsyvlghi gfsvvpwkrg
      121 ngyakqalnl mlgeakgkgl pyveltvdpe niasqrviaa cngvlierfr kpaaygfaet
      181 lryrieldd
//
LOCUS       WP_175906386             135 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DUF427 domain-containing protein [unclassified
            Burkholderia].
ACCESSION   WP_175906386
VERSION     WP_175906386.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Lupas,A.N., Zhu,H. and Korycinski,M.
  TITLE     The thalidomide-binding domain of cereblon defines the CULT domain
            family and is a new member of the beta-tent fold
  JOURNAL   PLoS Comput Biol 11 (1), e1004023 (2015)
   PUBMED   25569776
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..135
                     /product="DUF427 domain-containing protein"
                     /calculated_mol_wt=14631
     Region          <41..129
                     /region_name="COG2343"
                     /note="Uncharacterized conserved protein, DUF427 family
                     [Function unknown]"
                     /db_xref="CDD:441912"
ORIGIN      
        1 msispdtpsr pvkspgpdhp itiephpsrv vvkvagkvva dtrhalalre asypavlyvp
       61 redadiallq rtdhatycpy kgdcayysip aggeratnav wtyehpnpav esirahlafy
      121 pdrvdsiees plgtd
//
LOCUS       WP_175906412             157 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175906412
VERSION     WP_175906412.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..157
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17049
     Region          3..153
                     /region_name="COG3865"
                     /note="Glyoxalase superfamily enzyme, possible
                     3-demethylubiquinone-9 3-methyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:443074"
ORIGIN      
        1 mtiqkitpfl wyateaeeaa afyagifpns rvvrvtavpg tsgtrmvefe lfgqpfiams
       61 hprtetfnha islmiscadq aeldrywsal ldnggtadgc gwlrdrfgvs wqivpdalip
      121 mmadrdevka arvasammqm tkfdvaalka ayagtag
//
LOCUS       WP_175906465             346 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia seminalis].
ACCESSION   WP_175906465
VERSION     WP_175906465.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..346
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34821
     Region          31..301
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtrlrmlfrh plawpvltlv lllaldvayr pgflsialld ghlfgapidi lnraaplvlv
       61 slgmtlviat rgidisvgai vaiagaaaai vldadpsrvg lalaaalgvg llagawngll
      121 vafvgmqpii atlilmvagr gvaqlltggq iipigapgyl algggylatv pcavwiaaat
      181 iaatallvnr talglfirai gvnpvatrlv glrsgavvfg vylcsgvmsa lagilassnv
      241 rsadgnnagl lleldailav tlggtsllgg rfslagsvlg aliiqtltyt tysigvppea
      301 tlvvkavvvi vvtliqsdaa ralvvrfasr llpaarsrat tgatpr
//
LOCUS       WP_175906504             289 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfurtransferase [Burkholderia sp. BCC1640].
ACCESSION   WP_175906504
VERSION     WP_175906504.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..289
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30465
     Region          15..284
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mphthyttli saanlaerlt aapgsvavfd crfdlvdpga geaayatghi pgahylhldr
       61 dlsgrktgtn grhplptrda fatliasrgv kqgqqviayd aqggayaarl wwllrwlghd
      121 svavldgglq aweaagqplt advphpaagd frattplest vdaaavlanv tsakrvvida
      181 rapdryrgen etidrvgghi pgarnrffkd nlaadgrfkt ghelretftt llagtepnsv
      241 ilqcgsgvta chnalaleia glhgaslypg swsewsadps rpiatgpnp
//
LOCUS       WP_175906510             310 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175906510
VERSION     WP_175906510.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33933
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrlkaltvf vrvaaagsis agarelgitp qaaskqiaal eallsvrlfq rstrrivltv
       61 egerlfsqcr gavgelesal rmldddraqa vgtirvaapy slarrflapl lgefcdrqpg
      121 itaelivsdd madvveqrid lavrtgnlpd sglvarrvad lqlivcaapa ylcrhgepqt
      181 idalsehrct aflyprtgkp fpweffvdgs vhtrqmnpfi atndidaeld tvlsgaaigq
      241 ffgysvhahv regrlvpllt rhatsrygly lcmpqrthlp rrnrllmdfl adrlrahpdl
      301 aplpladaaa
//
LOCUS       WP_175906547             296 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175906547
VERSION     WP_175906547.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..296
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32330
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..272
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrfhelnaf iavveaggfs aaarrtgdsq sgiskaigtl esrlgvrlfn rstrsvtltd
       61 dgqryydrtk plleelddad selassthda sglirisasa tfgrlhvlpl ipdllasnpg
      121 lqvdlvlsdf vrdmvedrid lairvgavhd pdavvrrvas tplvcvgsrr yfeqhgiprt
      181 paelvnhncl lygglteavn wpftgpqgrf svavrgnlss nsvetiragv lagvgiglfa
      241 risladelrh pdvmtvldey vsevrdisvv wpkrrfvpvr vrrateffat alprrv
//
LOCUS       WP_175906550             490 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sigma-54 dependent transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175906550
VERSION     WP_175906550.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..490
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=52960
     Region          21..139
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <157..465
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mvarspdasg ttasempfvs vtapeagrkl fvimrspdep llaqlrelgw disvaktaga
       61 aqnmtsgvnv aaglvdfsgf tsrdypalka clsqpaigwi svaqagitig vavrelirsy
      121 cfdyvtlplp yewishvlgh argmaaldrv dgaayaasig ehgmigncea mqqlfstirk
      181 vaktdasvfi sgesgtgkel talaihersv rgkgpfvain cgaiphhllq selfgyerga
      241 ftganqrrag riesanggtl fldeigdmpv esqasllrfl qegkierlgg qesipvdvri
      301 isathvdldg aveagrfrad lyhrlcvlri hepplrargk didilahyvl qkykadsgrk
      361 isgftsaald amrryewpgn vrelinrvrr aivmaesrll tphdlgldvp getepvtleq
      421 arslaertai enallrndhr inkaaaelgi srvtlyrmmi ehglndhdnn gdnggkdgap
      481 pddadhqrvg
//
LOCUS       WP_175906635             207 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD family hydrolase [Burkholderia seminalis].
ACCESSION   WP_175906635
VERSION     WP_175906635.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..207
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23209
     Region          3..191
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mtikavvfdf ggvlidwspe ylyrelipde aerrwflthv camdwvirqd ggqtieegta
       61 elvakfpehe alirafyarw hemiggvlee gaalvdrlda qgmplfgltn wsaqtfpyaw
      121 dnfpvlrrfr divvsgrvkl vkpdpaiyre mharivphlp giaphelvfi ddnaknaqaa
      181 talgwhgihh tsaaatearl relgala
//
LOCUS       WP_175906661             427 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia seminalis].
ACCESSION   WP_175906661
VERSION     WP_175906661.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..427
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45286
     Region          15..415
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(26..27,30..31,34,69,116..117,119..121,124,148,
                     151..152,155,243,246..247,250..252,255,286,290,341..342,
                     346,350,366,369..370,373..374,377)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mnwavtrigg rfhygwlaaa vvflillaaa gtratpsvlm vplerelgws raaislaisv
       61 nialygltgp faaaamqrfg lrptiltalv tmsagvalss mmtqswqmvv iwglmvgcst
      121 gvvaltlsat fvtrwfharr glvmgiltas tatgqlvflp mlaaiaqrhg wrpvvlvvav
      181 aaaiviplva fllperpadv klrpygepad apaapdatke nplavafrtl lmasrsrdfw
      241 llffsfficg astngyvgth liamcsdygm tevqgaslla amgvfdlfgt tlsgwlsdry
      301 dnrvllfwyy glrglsliyl phafgidffg lplfamfygl dwiatvpptv rlatdvfgka
      361 aapvvfgwiv aghqlgaafa algagllras lgtytvasmi sgglciagal ivlrinrgps
      421 raaaqaa
//
LOCUS       WP_175906684             434 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175906684
VERSION     WP_175906684.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..434
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45070
     Region          50..430
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mlkltlavav vfataataha qslqvaapal astasavapp sdaafspslt lsdalaaaar
       61 nnpalrgara dvdasagalm qagarpnpev sflqegfsra ertstalinq tielggkrra
      121 rldvasygre aanasldeqg aavradviaa fygllavqrq lqvteesaai aarsadlagr
      181 raqagkvspv eatkaqvaaa gvqievatar grvdvarekl navmgeargd rrvalgdlet
      241 vpaveplsal taqlddapla rvaraqmlrs naavslerar ripdvtvsag mkrvttggvp
      301 dnqavvgvsi piplfdtnrg alleathkag ranadldrer trlrleltqa yanfdaaaqe
      361 arrlksdilp garlaldams rgyelgkfsf ldvldaqrtl fqgqsqyvra ladahaarad
      421 igrlvgtpla avaq
//
LOCUS       WP_175906698             316 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia seminalis].
ACCESSION   WP_175906698
VERSION     WP_175906698.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..316
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32779
     Region          24..314
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          211..314
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(216..217,250..251,254,258..259,262,304,308)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mhrtiharra rlsaalspal valfaaglva sgaafaqntg atvtpvgngt vatttlpssn
       61 psagaasgtv vrgtagtitp ppanatpgqv vvggkvpdea tkaavlqklr dtygatnvvd
      121 qievgdvatp pnwsanvqkl lgaqlkqisk gqlkingtqi emkgevhnea qrqqlasdma
      181 ntlnptytik nglrvsaseq glldqtlanr tiefetgsat ltpqgrlild qmaaalskmq
      241 nrtvdiight dnsgnrtsni alsqaradav kgylitknip pqqmtttgvg pdqpiapndt
      301 adgrarnrri efrvgq
//
LOCUS       WP_175906747             240 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: HAD family hydrolase [unclassified Burkholderia].
ACCESSION   WP_175906747
VERSION     WP_175906747.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..240
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25951
     Region          6..233
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mrlsrisais fdlddtlwpf gpsveraeas lhawliahap dtanvvptsq algqlrneye
       61 rsrpdlvsdf ralrigsirl aleranedvt ltdraydvfy sarnrveffd dalpalawls
      121 arfpliavtn gnadlqltgg geffrdtlsa rafgfakpep eifhaaaakl gvpaaellhv
      181 gddfhldvvg alnaglqaaw vvrhegpeae haahrapsph ltvrdlsalc ralggpveas
//
LOCUS       WP_175906792             425 aa            linear   BCT 11-JAN-2025
DEFINITION  epoxide hydrolase family protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175906792
VERSION     WP_175906792.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..425
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46697
     Region          39..143
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          110..>233
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 msstqfspmr rhllatsvaa gvsamlptal haatggdgir pftahipdea ladlrrriaa
       61 trwpgretva desqgvrlar mqallrywgt dydwrkgear lngfpmfite idgldihfih
      121 vrsrhanamp mimthgwpgs ifellkaigp ltdptahgas addafhvvvp slpgfgfsgr
      181 paktgwgsdh iarawgelma rlgytrfvsq ggdcgsvish rmamqhvqgl agihvnmpat
      241 vppdiatllq tdapapasls pkekaayekl atfyrdncgy sammvtrpqt vgyaladsps
      301 gqaawmydki sqwtysggvp ersiprdeil ddislywltd tatsaaqiyw edhsnnfnav
      361 dislpaaitv fpgeiyqapr swaersyhnl iyfnevdkgg hfaaweepel farevragfr
      421 plrra
//
LOCUS       WP_175906797             508 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia seminalis].
ACCESSION   WP_175906797
VERSION     WP_175906797.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..508
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=54675
     Region          11..497
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mllnavdshv ydyvivgagp agciiadrls rdsssnvlll eaggdlstse dvltpnrwpt
       61 lidsehdway rtepqsalgn rsvawprgrm vggsaamham vyvrghpndf alwadevgps
      121 wgwenlqrff hefehgsget vsverptslh afcevfldva ralglpcrem vdvcaqpglg
      181 rylvmqrdgq rsfpaqtcla ralgrpnfkm ltlcqveqlk fdgrnvrevl vecadgvrsi
      241 rverevilca gtigspslll rsgvgpaeml raadipiaha legvgrnlhd haqvalsvrs
      301 lhkvpvahts nlgevggfln tpasteqsss qfvfapiigl shggdigsgf slgpsvglps
      361 srgrvgirrv agrlqididp gyltderdla vlaegvavcr divrhprfst itgstsgdfn
      421 rlegrdairr fcrehahtqf hpvgtckagr gdnavvgpdf kviglnnvrv vdgsvipsit
      481 rantcapima lamaaadslt qerstfnh
//
LOCUS       WP_175906885             228 aa            linear   BCT 11-JAN-2025
DEFINITION  lytic transglycosylase domain-containing protein [Burkholderia
            seminalis].
ACCESSION   WP_175906885
VERSION     WP_175906885.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..228
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - lytic transglycosylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=23874
     Region          2..187
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 mrrrffwliv lslgiaqqas aeqtpavpas apdvlasapt vasaplanan dqpneanrri
       61 tsyltkkfgv arekaaklad ivsvtatkys lppalvyaii siesrfqeka rgqhgatglm
      121 qvvpsahrgm lrnvkdltep nanveagsri lsgyvkaagg nvqaglksys ggssayaakv
      181 mqrvdsfrfv lepdddaqaa ntandgkarm vpvsdpsgpa paanrnak
//
LOCUS       WP_175906863             331 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175906863
VERSION     WP_175906863.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..331
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34892
     Region          6..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..302
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 medidlnlva aldvlltegs vtgaarrlgl stsamsrtlt rlrtttgdpl lvragrrlvp
       61 tphasalrdr vhaiasdara vlrpasadvd matlsstfti raaasfmdml agpvvatigd
      121 iatgvrvrfv arldrdpgpl rdgtvdleig krgddapelh trelfhdghv avaraghplf
      181 aaaritpary aacrhviasq lgdfggpand padtlapahi vqvvvpgypd amrvaagtdl
      241 ialvprsslg naftpglvda lglrsfaipv rlpeilisal whprmqrdpv hrrlreavid
      301 vckraypaar aprapkrghc napdgaggpf g
//
LOCUS       WP_175906893             392 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia seminalis].
ACCESSION   WP_175906893
VERSION     WP_175906893.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 392)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..392
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39743
     Region          168..370
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mtdraaasar rvtldkvgil igvltivavf glsfavlrpn riaagtglsv faalpamqga
       61 alaalwtvga lwamtasrpa wrlaagcagl atlayavgaa arhvvapddm larvspdagv
      121 wlllfawavl vadalarlaf gpwrrlvala vaiaaisvpl asgwwdglsv mreyavrsdd
      181 fwreairhvs laggsvaaal vaglplgiac arvpsvrtva mpvlnvvqti psiamyglmm
      241 aplgllaahv plaaalgirg igvapavlal flysllpias svvvglgqvp phvteaaram
      301 gmtraqrllr vdlvlalpvi lsgvrivlvq nigltavaal iggggfgtfi fqgigqsaad
      361 lvllgaipti alalaaavvf eaatslakgr ag
//
LOCUS       WP_175906971             312 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia sp. BCC1640].
ACCESSION   WP_175906971
VERSION     WP_175906971.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..312
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32322
     Region          78..282
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mpldpqaqal laalaqapai dfdqltvpay raslaggsaf apgdaiaaee dwqipapgrq
       61 lsarlyrpda dgplpltvff hgggfvacgi dshanlcrsl agrartlvls vdyrlapeah
      121 fpaaaqdacd avrwaaasar dlgaragaia vagdsaggnl aavaalqlrg sgiaiahqll
      181 lypvvdcate hpsyeslgeg yfltadamrw fkrqyfddda drasplaspl avadlsgaap
      241 ativsaefdp lrdeaeayal rlaqagtpvs lvrwpgqlhg fasmlgavda adraltfgad
      301 alrrafdate vq
//
LOCUS       WP_175906992             460 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: amino acid permease [unclassified Burkholderia].
ACCESSION   WP_175906992
VERSION     WP_175906992.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..460
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49338
     Region          3..452
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mkqpedqlhr gleerhinlm algatigvgl flgsatairt agpailltyl lggiaiflim
       61 ralgemaisn pvagafsrya rdylgplagy ltgwtywfvw ivtcmaeita vgvymhmwfp
      121 gvpnwiwala altamgavnf vavklygefe fwfalikivt ivlmiigggl miafgigngg
      181 vatgisnlwa hggfmpngid gvigalpivm faylgvemlg ltagearnpe ksltkavnsv
      241 fwrvlifyig alfvimslyp wdqigtqgsp fvmtfsrlgi paaagiinfv vltaalsscn
      301 sglfstarml ynlaqqgqap aslgrvnrng vpvygvavsv allligvlln ylapqqvftw
      361 ltsvstfgai wtwcviliaq mrfrrtlsad riarlpirvp fyplgsfval gflalvvvlm
      421 aftpdtrval vigpawivll giayavfyan ragapastks
//
LOCUS       WP_175906994             168 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175906994
VERSION     WP_175906994.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..168
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18245
     Region          1..141
                     /region_name="CFF1"
                     /note="Predicted sugar epimerase, cupin superfamily
                     [General function prediction only]; COG3542"
                     /db_xref="CDD:442763"
ORIGIN      
        1 mpisaadlih qfdlqphpeg gyfretyraa dtvvrpadga praastaiyy llcdgayssw
       61 hrirsdevwh fyagdplevw vlderdglti hrlgnplthp gtvfqavvpa grwfgarcas
      121 pehvalvgct vapgfefaef eladatalaa afpeyaeyvg alaqrpda
//
LOCUS       WP_175907000             854 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia sp. BCC1640].
ACCESSION   WP_175907000
VERSION     WP_175907000.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 854)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 854)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..854
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..854
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=91895
     Region          48..697
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mssvrdlcak wvaraqpvaa aaavpvkrvl asawhhlrhp trrgvlraaa avpvlfvlyv
       61 lalipftpgi gdirkarvdq paqvlsadgk vlaefkpsnr ewvslkqisp hmvdaliate
      121 dhrfyehhgl dwkrtasaal htfsgsrqgg stitqqlarn lypdeigrap tltrkvkeai
      181 talkieavys kdqiletyln tvpflynayg vemaartyfd ksadeldvld satlvgmlkg
      241 nsyynpvlnp eralqrrntv lgqmvkygkl spaqfaqlqr rplridferq keppgpaphf
      301 aqqlrkwlig wadrndyniy sdglivrtti dsrlqqmatq altlqanqlq giannawsgr
      361 dgcgtdnevf rafmrespey kaaqdagknd avamkqlaad rgfmralcka ktdvqagfva
      421 idprdgqira wvgsrdftne pfdhvaqarr qpgstfkpfv ygvafangmk pddtfvdqav
      481 eiplkggeiw rpnddappsg kpmtlrdava lsrnritaqv mekvgpaava rlardmgvre
      541 splervpsla lgtspvtlke mvasyatian gglyvepqmv trienrqgdv laeyapappe
      601 raldvetdkt llgvmrdvvt rgtgssirtr fgirgdvagk tgttqdnadg wfilmqpglv
      661 agawvgfddg rvtlrsdywg qgahsalpiv gdffqraqra rivdtklkfd tepspgwfss
      721 vrervtdlfd gwfgpepkqv papvrtqrie rqpeadaaaa saasaasape aasggiveew
      781 vpasevaasa aalsagasqp qaaqppatgg satpagntgg gglgsapaap savpapsaal
      841 apapvspgat sgse
//
LOCUS       WP_175907009             472 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia sp. BCC1640].
ACCESSION   WP_175907009
VERSION     WP_175907009.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..472
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=50630
     Region          83..468
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mtarpafpsp dasgaaaprs paravrraaf algaavlgyg afaiafpart paaigdvvad
       61 wtganphpvv lqrpaaqpls avaqlgralf adpslsasgk qscaschspd haygppngld
      121 vqpgglamtq qgyrpppslm ylyrqpnfsi gpdagendaa psvaqqaasa agvvkaqkva
      181 gasaapqlvp qggmfwdgra dtlqqqafgp llnpvemana giddvarkla qsshraqfeq
      241 lfgarvfssp qllvseamfa iaryqvedps fhpydskydr wlegrarltq aelrglrlfn
      301 dpdkancagc hlskpgkdgl ppmftdyqye algaprnmal eqnrnpafhd lgvcgpfred
      361 lkdqtqycam fltptlrnaa trhvffhngv fhtldqvmaf ynersispqk fysrgadgkv
      421 deyddippky ranvdvtdap fdrkpgdkpa mtaqdikdie aflgtltdap ar
//
LOCUS       WP_175907031             475 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia seminalis].
ACCESSION   WP_175907031
VERSION     WP_175907031.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..475
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51391
     Region          42..460
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(52..53,56..57,60,100,150..151,153..155,158,178,
                     181..182,185,296,299..300,303..305,308,335,339,388..389,
                     393,397,413,416..417,420..421,424)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mastqpdplt aagtarpaai dpgsisarld rlpptrsvwk lvvllslgff felydllysg
       61 yvapglvksg ilsatthglf gttgvasfia alfsglfigt iacgfladrf grraiftwsl
      121 lwytaanvvm afqdtaagln fwrfvvglgl gvemvtigty iselvpkqir grafaceqav
      181 gfvavpvvaf layllvphap lgldgwrwvv ligahgalfv wwirrelpes prwlaqqgrv
      241 deadrimral eakveaeygr plpppapaep vpprgsfrdm wvqpyrrrti mmtifnvfqt
      301 vgfygfanwv ptllikqgit itsslmyssv ialaapigpl iglviadrfe rksvivvmaa
      361 aivvcgllfs qttvgafliv lgigltlasn imsysfhayq aelfptsira ravgfvysws
      421 rfsaifssfv iaavlkgfgt fgvfafiaga mvivmvaigf mgprtkgial etisk
//
LOCUS       WP_175907038             505 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CoA-acylating methylmalonate-semialdehyde
            dehydrogenase [unclassified Burkholderia].
ACCESSION   WP_175907038
VERSION     WP_175907038.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..505
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53649
     Region          11..488
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(67,69,73,76,80,113,116..117,126..133,138,141,144,
                     237,241,244,247,249,424,426..427,429..430,433,436..437,
                     439,441..444,453,457,459,473,480..485,487..488)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(153..156,164,179,182,212,229..232,235,253..255,287,
                     389,391,417)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(156,253,284,287)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mkhdsnvtst vghlidgkrv dggsrvqpvf dpatgeshks valadkltve aaiasaqaaf
       61 pawrntpplk rarvmsrfkt lleehadelc alitaehgkv ladamgelqr gienveyaty
      121 vpellkgehs knvgpaidsw sefqalgvaa gitpfnfpvm vplwmwpmav acgntfvlkp
      181 sertpsstlr maelaleagl ppgvlnvvng dkeavdtilt dprvkavsfv gstpiaeyiy
      241 atgcahgkrv qalggaknfa vvmpdadign avnalmgaay gscgercmai plvvaigdet
      301 gdkvidglka eiakmkvgpg dgagvdmgpl vtkqhfekvt gfvdagveag atlvvdgrgv
      361 kvdghdggyy lgpclfdnvk pgmpvyqhei fgpvlgvirl ksldeamali daheygngtc
      421 lftrdgeaar yfsdniqigm vginvplpvp vayhsfggwk rslfgdlhay gpdavrfytk
      481 rktitqrwps agvregtvfs fpsnr
//
LOCUS       WP_175907037             310 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AEC family transporter [unclassified Burkholderia].
ACCESSION   WP_175907037
VERSION     WP_175907037.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..310
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31669
     Region          19..305
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 migpillala pvallvalgh glrrtgfigd afwphaerlc yyvllpalfa nslanarlqa
       61 lpvlplaaal vgstvlvaal lllvrrfvsv dgagftsvfq gavrfnnyvg talaaglfga
      121 hgialaavcv aaivptvnlm cvlvfarygd trlgawalvr qilsnplvvg calgiamqva
      181 giafpaavep avralgaasm plgllcvgaa lkfdaarewm qpmciasafk fmamplatla
      241 agrlfglgda altiallfqa lptssssyim arqlggdapl magitafqti aaalampavl
      301 talasapvfr
//
LOCUS       WP_175907068             282 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC1640].
ACCESSION   WP_175907068
VERSION     WP_175907068.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 282)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..282
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30958
     Region          23..158
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          197..278
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msrsakplav pspfwrdaal pfieartvdd grticyakht hdtfslgaiv ggtstylnga
       61 tkehvgrgvl viidpeqvha cnpygpdawa yrmvyvdvpw larlqhalgr dpnsdyhgfs
      121 pklterrdlf aqfggfyrtl vapgvdplgk esaavefftr lhgaldreap vdtrrgtdna
      181 klaraadyia ahcrqavtld aicaaadlsp sylirafnar ygmtphaflv drrvqygrte
      241 lrrgrpiaev aldagfadqa hfqrafrria aatpgqyrsa an
//
LOCUS       WP_175907069             722 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia seminalis].
ACCESSION   WP_175907069
VERSION     WP_175907069.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..722
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78098
     Region          26..722
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mpsrrtprra rtqrpwrtrl palitlcvas gahaaianpv tpastpatpt ehelpaisvs
       61 asatadptvg yqprttrlag gedrslkeip qsvavvsssv mqdqqarsld dvlgnisgvt
      121 qtntlggtrd afikrgfgsn ndgsvlvdgv rtpvlhsyla tidrvevlkg pasllygmqd
      181 pggvinlvtr kpedtfggsi sasrtshrgs saqfdltgpl gkpgqvaggt lafrltgeyd
      241 tsrywrsfgr ernaliapal swhdantsvd vsyqyvdytt pfdrgtvlvn gqlddtlryr
      301 ryeeawsqss giqetlrtri ehrfsdawrv ratygwgrdr ydqyitrata fnsrtgaltr
      361 ssdanlgrnd sdqiatlgll gnvtlagmnh alylggeyer qrsfrgdtir gkattgfnly
      421 dpvygllapg gtpnakqsds rsvvhaysti vqdtvkitdr ltavgglrwe nwqqesgmgr
      481 pfvfadrsrg svwlpqlgla yaltpeltay anvsrsfkpn vasnvaapla peygrvleag
      541 lkfslkpait gtlavyqidk rnvavtvgdl tstigtarsr gieldvagqi trhlsvigsy
      601 aytnandrdg ntplvnvarh tgslfavydt aianlpgrwr fgggarvvga rpgdtansft
      661 lpgyvtvdaf aayetmigkf ptrfqlnvkn lldktyypss nnnlivavge prlvtltttv
      721 sf
//
LOCUS       WP_175907080             551 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 32 protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175907080
VERSION     WP_175907080.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..551
                     /product="glycoside hydrolase family 32 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=59912
     Region          41..536
                     /region_name="SacC"
                     /note="Sucrose-6-phosphate hydrolase SacC, GH32 family
                     [Carbohydrate transport and metabolism]; COG1621"
                     /db_xref="CDD:441228"
ORIGIN      
        1 mrstflrfpl litrlllaca asaacthaaa apcdappehg tpqwrpavhy tpqrnwmndp
       61 nglvyengry hlfyqynplg hdwgnmswgh atstdlvhwr eqpvamrana teeifsgsiv
      121 adtrntsglg apgetplval ytsvykdgsg hapgtqaqsl aysldhgatw rpyahnpvlt
      181 ldpeskqfrd pkvswyapgg ywlmttvvad aqvvklyrsd dlihwsflsd ftlpdvphag
      241 vlwempdlvp lpvdddprhi kwvmivnvnp wsiaggsgam yfvgdfdgrt ftpdqvapag
      301 sdparfrwvd hgadfyaagt fsgapgarpv aiawmsnwdy aakvptapwr gattlprefa
      361 lktidgeptl vvtpaaafda wadgrpavhe gnlnvesatr alseatrgvv qritvtiapr
      421 haaragvivr gsadgsigtr ivydtakrtl tldrsragst dfagtfsreh ivdlpldhgq
      481 lrleivvdrg svevfanggr valtdlifpp ldadrvavfa ehgsatfsgl tvtqlhgrdr
      541 adevrdacts r
//
LOCUS       WP_175907106             439 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175907106
VERSION     WP_175907106.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..439
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=46806
     Region          25..397
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msaslaassp lppqsslrhl paddarvaal lerlapelaa daarndvdgr fphenfarlh
       61 ragliaqvvp rehggagatl aqasrivaav aradpatalv ltmtylqhra lgradnrwpa
      121 rvrravfdsa vaegalinal rvepalgsps rgglpetiar rdgdgwrlsg hklystgipa
      181 lrwlavwart depeprvgvf lvrrerdved dagirviesw nhlglrasgs hevvfddvrl
      241 padhavdvra pdawavsaas hadvdaqadq qawmvallgs lydavarasr dwllafattr
      301 apsglgapla tlpriqeavg eiegwlhtnr vlldehiart dagdaptvtt sglvkrtvte
      361 qairtvehal klsgnhglsr hnplerhyrd vlcsrvhtpq ddaiavaagr aaldaaarsa
      421 naetggtsrd apasgrrda
//
LOCUS       WP_175907107             220 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia seminalis].
ACCESSION   WP_175907107
VERSION     WP_175907107.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..220
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22843
     Region          117..218
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(120..121,154..155,158,162..163,166,208,212)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mnklalalal satalaacst asgptfsase lqprdgvrtf qvdchgllsg pqtcmkaark
       61 icgeepvrav dsaralrdks dpatlvfqcg aapaeaapaa apaaavveqv nlsgdalfat
      121 dhatlaptar esldrllner kdhtytqvtv tgftdsvgsd dynlalskrr aesvaaylka
      181 hglkadsmtv sgrgkadpva snatpegras nrrveirlqh
//
LOCUS       WP_175907120             366 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia sp.
            BCC1640].
ACCESSION   WP_175907120
VERSION     WP_175907120.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Saurin,W. and Dassa,E.
  TITLE     Sequence relationships between integral inner membrane proteins of
            binding protein-dependent transport systems: evolution by recurrent
            gene duplications
  JOURNAL   Protein Sci 3 (2), 325-344 (1994)
   PUBMED   8003968
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004772
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..366
                     /product="ABC transporter substrate-binding protein"
                     /calculated_mol_wt=39817
     Region          62..364
                     /region_name="AfuA"
                     /note="ABC-type Fe3+ transport system, periplasmic
                     component [Inorganic ion transport and metabolism];
                     COG1840"
                     /db_xref="CDD:441445"
ORIGIN      
        1 mpfapkqlaa alaivlgtta gaavaqvpvg ypgnyqgvvd aakkegkliv ysttdtglvr
       61 plikdfesly gvkveyndmn stelynryis enaasstsad vlwssamdlq vklvndglmt
      121 sydspesanv pqwaqyqkqa ygttfeplai vynkrlipen evpktradli klltsqpdkf
      181 kgklttydve ksgvgfnalt qdahlnekvt welvkaigat gpklqsstga mmerissgen
      241 ligyniigsy ayakakkdks igyvfpkdyt qvvsrlatis kkaknpnaak lwvdyllskr
      301 gqtlianqan lyairtdvtg etsvasltke lgdslkpipi gtgllvyldq skrlaflkqw
      361 qqaiks
//
LOCUS       WP_175907132             398 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia seminalis].
ACCESSION   WP_175907132
VERSION     WP_175907132.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..398
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41545
     Region          1..379
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mviflavlfg ivgldrlviv ylfpvllpel nlnntqagai asvlaltwav stwvlgslsd
       61 rhgrrkillg ssiffsvmts ftgvaksfhg mllvrgllgv geggvfsasv atideistps
      121 rrglnlgihq sffpllgigl gpiiatqlvm hmrwewvffv lgipgllltf ligrtmrkte
      181 agrdkqarsa sggpltvlry kniwlttvig slfqtglfvf stfvalyltk vvglglgtvg
      241 liisgwgfgg figmiavpai sdrlgrrivl vvsaacygvl mlafvlchas pivmfanlfa
      301 agicgfgiap lflavipces vpstltgsav gvptavseli ggvlmpvvag gladtfglgy
      361 pmlivgsvsl vsalvgmfld etvpaatsqh avstidaa
//
LOCUS       WP_175907210             215 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia seminalis].
ACCESSION   WP_175907210
VERSION     WP_175907210.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..215
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23432
     Region          9..203
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mtsthslafy tadtpnghki aiyleeagla ydrvhvnlsa geqrspayla inpngkipai
       61 vdrdtglavf esgailgyla aktgylhpet laertavqqw lhfqiggigp mlgqlwwflr
      121 asktanaeai dryrkeamrl yrvvngrlse saylasprys iadiaafpwl rtaaeldldv
      181 sgfphverwl adiaarpavq rgliacrapa avaar
//
LOCUS       WP_175907161             450 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia seminalis].
ACCESSION   WP_175907161
VERSION     WP_175907161.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..450
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47344
     Region          5..407
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(20..21,24..25,28,60,110..111,113..115,118,138,
                     141..142,145,232,235..236,239..241,244,272,276,334..335,
                     339,343,358,361..362,365..366,369)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnhlrwkiva flvapltfvm tldraamava apaiqgelgl sivemsmilt iyfwayaigq
       61 ipagraaerf gsrrvlfgts tlwslmmivt plggsfawlf gcrlvlggaq sadwsssvva
      121 lkrwfpager akgnavllag lylgpivsap ltawtivhfg whavfhgfga lglllgaiww
      181 fgyrdapash plitpaeady iaagqppght avsgslarcl rlgrfwifgi qyfllvliqs
      241 fyttwlptyl mrarglslka mglyaslpwv avfaavfvag tvsdrllrrt gsiywartpv
      301 aiagfvvsal alvaasraqa maaviallcl sfaavgfvqv vvwsaaqdlg rpfagvmsgw
      361 tnvwgalsnv agpmalalvv kitgswgsgm vvigaaavcg avlwlfvhpe rpllavtagg
      421 lppsaaggna prgdagatra dagrvsepad
//
LOCUS       WP_175907218             541 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia seminalis].
ACCESSION   WP_175907218
VERSION     WP_175907218.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..541
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59477
     Region          2..535
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mqhadtvyln gllytgdaqr rfaqalatrd gkivavgrdd dirplagpat rrvdlagrlm
       61 lpglidghvh pleghqilgd fdlsgindpd tilqriraca datpnepwvy lgganlaafg
      121 typtrelldr ivsdrpllvv gfdvhsgcln tkgleaagir adtpdpsggv ierdasgapn
      181 gvvheaafyr vcplipqlsp agypkslaka hamahgygit gwfdarvdea elqayadaqr
      241 agtlkvymsa glyanprrdp reqierfaaw rreyerdnlr lhtvkifvdg vpesktaall
      301 epyagtddcg lalwsqdaln eiclladtag fdlhfhtlad ravrmtldal ehvqrrngmr
      361 drraqlahlq lvdpadmsrf nrlgaiasvq tlwtaareeq qqlyrdllga ertarnypfr
      421 slrnagamla agsdwsvstm dpmqiiqtgv thrlidqpds ppwnpherld lltmleaytv
      481 ntayalrfdd ctgsleagkd asfaildrnp fahpvetfaq trvletcfrg evvhavpgwa
      541 d
//
LOCUS       WP_175907252             673 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: BCCT family transporter [unclassified Burkholderia].
ACCESSION   WP_175907252
VERSION     WP_175907252.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..673
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73248
     Region          3..514
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mpdsrssprt tfkpqvvlpa lavigallvv callpteaga lfssgqqwvv arfdwfyvla
       61 vttflvflvl iaasdfgnir lgpddaepef sflswtamlf aagmgiglmy fgvgepmqhf
      121 lkpptvdpgt paaareamlm tffhwgfhaw aiyglmglvl ayfgfrynlp ltlrsglypv
      181 lrervngwig htvdafalvg tvagiattlg ygvmqlsagl htvagwdtsg nafriglvvi
      241 vvilagasaa sgldkgvrrl selnlllafl llafvvvagp tsfllralgd nigqylsnlv
      301 dlsfrtyaya ppreegwfgg wtilywawwv swspfvgmfi arisrgrtir qfvigvllvp
      361 tafnlvwmtv fgnsaiwldt hgaagalaqt agsvdallfr ffdflplpql lsivaivlia
      421 vffvtsadsg afvidqiatr gtahspvwqr lfwaallgvt aavllvaggl galqamtlia
      481 alpvalimla lcyglwrgla adrahysqdv apatsfwtgq hwrhrlthil rqttesdarq
      541 fvaetvepal rkvadelrsg gvdahvqrds ddavrltvpt aehrdfvyga rvtaksaaaf
      601 lvreaaepea erphvygivt ffedgrlgyd veylrgdeli advlrqyery vslaadqrth
      661 llsrapghat eae
//
LOCUS       WP_175907273             267 aa            linear   BCT 11-JAN-2025
DEFINITION  SH3 domain-containing protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175907273
VERSION     WP_175907273.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..267
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27755
     Region          7..96
                     /region_name="YraI"
                     /note="Uncharacterized conserved protein YraI [Function
                     unknown]; COG4991"
                     /db_xref="CDD:444015"
ORIGIN      
        1 msntiirslc vvlfgiaavp giadaqssay tnspaeiyag papdypvvaq vppgtaldvf
       61 gclsdyswcd valpgvrgwv daeqldypyq gnyvplleyg aiigvpvtgf aigaywdryy
      121 rhrpwfhdrd rwerraeprv gpggmppayg hpqpggpnqr apgggaperh darpsatrgg
      181 wngpnrapap qqaapapapm pgarqpqqpa qqpapnggaa rmmapptyqg gggygarpqg
      241 ggnsggnrgg gnhggggggw gtdefrh
//
LOCUS       WP_175907306             894 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AAA family ATPase [Burkholderia].
ACCESSION   WP_175907306
VERSION     WP_175907306.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 894)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 894)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 894)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 894)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 894)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 894)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 894)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18409402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..894
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..894
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=96636
     Region          2..>88
                     /region_name="SbcC"
                     /note="DNA repair exonuclease SbcCD ATPase subunit
                     [Replication, recombination and repair]; COG0419"
                     /db_xref="CDD:440188"
     Region          180..871
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
ORIGIN      
        1 mklkrlrien fkrfraplel gnfadglnlf vapneagkst vaeairaaff eryksnsvsg
       61 lrpwsdssat psveiefelg gkparlsksf lgkkrcqlsi dgkvldgtea edhlgemlgf
      121 sfagrggssp ehmgipgllw ikqgtshela kavgfasdhl rnalgdslge lastsgddvi
      181 kavesernql ltpsteaprg tyaealkrrs aleetlevlr aeidayridv drlatlrrdh
      241 grddearpwl avreqlaqaq aklndatgla drrtaqevll kqamaqvvav rqqlqlmerd
      301 eealtlrevn leaaqsklik aqgllqawep rhaeaaltst karerlvvar qvaawqaqek
      361 svidlttqaq alqrslheaq lkqeeltrlk aealslalps velkrlregt drlrtaqakl
      421 davstaldfe lepgakvrva gaevmgtkrl tvvartgidi egvgritvlp ggedlqslig
      481 drdrqrdelt vllqslgvan laeaesrerl haqrvaegka ttsvlaahap nglaaleadv
      541 aalstkltaa kqtletlala vgaetasvpv sqaesdessa rtalddasaq lneaklavse
      601 analvsaard elaaaratls dplradkkaa ashaltdala rettaqadvd alaeqlrsln
      661 msvlqqdver fersakqlea ahalrageii rleadleakg algleevaad kqreldqvgr
      721 rcaelerran alshllkllt ekrsalarrl raplqrhlsh ylqilfpgss ievgedlspg
      781 ritrvgtnga etgefeelsv gareqmgvva rlayadllqe agkstllild dalvhtdkdr
      841 ldqmkrvlyd aasrhqilvf schpqtwqdl gvaarelsqe snpvagsvgg aasq
//
LOCUS       WP_175907375             301 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175907375
VERSION     WP_175907375.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..301
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32660
     Region          19..>115
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          <146..301
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 msaprllpds arywrtpllp dadlltatyr dhtfaphwhd aytipvileg aerytcrgsg
       61 hvaetgtvpv inpgevhtgs ratdegwcyr vsyvpvdyir alasaiagrp qdapwfpsdv
      121 irdadlaarl alahrmmeag secmppfhph eqpaadvpaa aapcaydpla aetamldals
      181 tliarhadar lqpaalaade prvdamrerl aadltctvtl ddvaqaagls pfhaarlftr
      241 tigmpphawr nqlrlqrala plragvsiad vaaasgfvdq shfsrhfkrm fgvppgrwqa
      301 r
//
LOCUS       WP_175907496              99 aa            linear   BCT 11-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Burkholderia
            seminalis].
ACCESSION   WP_175907496
VERSION     WP_175907496.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..99
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=11584
     Region          8..99
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mpvnarvvrl tplaetdled iwsytferws peqaehyvge lsaaferlar rewigrpsra
       61 gegywrylvg shvvfyreta etldvirvlh qrmdvephl
//
LOCUS       WP_175907630             386 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Burkholderia].
ACCESSION   WP_175907630
VERSION     WP_175907630.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..386
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39958
     Region          12..360
                     /region_name="MFS_YcaD_like"
                     /note="YcaD and similar transporters of the Major
                     Facilitator Superfamily; cd17477"
                     /db_xref="CDD:341030"
     Site            order(19..20,23..24,27,59,109..110,112..114,117,137,
                     140..141,144,214,217..218,221..223,226,250,254,304..305,
                     309,313,329,332..333,336..337,340)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341030"
ORIGIN      
        1 mkailnrdfl alilsvavvg lgtgatmplt alalteaghg tnvvgmltaa qalgglaivp
       61 fvtalarrig srraivvsvv llaaatalmq ftsnlivwgv lrvlcgaalm llftigeawv
      121 nqladdstrg rvvaiyatnf tlfqmagpvl vsqiagatsi rfalcgalfl lalptlatir
      181 raplagddah haahdswlav lprmpaliig tgffalfdtl alsllplyam dhgvasatav
      241 llasimlfgd tamqfpigwl adklgrervh lgagwivlag lpllpfvivn pwlcwpllfv
      301 lgaaagsiyt lslvacgerf rgaalvtass lvsaswsaas fggplvagal meqlgsnali
      361 gvlvvcvaaf vaaalwerra tlqrav
//
LOCUS       WP_175907654             443 aa            linear   BCT 11-JAN-2025
DEFINITION  phenylacetate--CoA ligase family protein [Burkholderia seminalis].
ACCESSION   WP_175907654
VERSION     WP_175907654.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Luengo,J.M., Garcia,J.L. and Olivera,E.R.
  TITLE     The phenylacetyl-CoA catabolon: a complex catabolic unit with broad
            biotechnological applications
  JOURNAL   Mol Microbiol 39 (6), 1434-1442 (2001)
   PUBMED   11260461
REFERENCE   2  (residues 1 to 443)
  AUTHORS   El-Said Mohamed,M.
  TITLE     Biochemical and molecular characterization of
            phenylacetate-coenzyme A ligase, an enzyme catalyzing the first
            step in aerobic metabolism of phenylacetic acid in Azoarcus evansii
  JOURNAL   J Bacteriol 182 (2), 286-294 (2000)
   PUBMED   10629172
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Ferrandez,A., Minambres,B., Garcia,B., Olivera,E.R., Luengo,J.M.,
            Garcia,J.L. and Diaz,E.
  TITLE     Catabolism of phenylacetic acid in Escherichia coli.
            Characterization of a new aerobic hybrid pathway
  JOURNAL   J Biol Chem 273 (40), 25974-25986 (1998)
   PUBMED   9748275
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..443
                     /product="phenylacetate--CoA ligase family protein"
                     /EC_number="6.2.1.30"
                     /GO_function="GO:0047475 - phenylacetate-CoA ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0010124 - phenylacetate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49250
     Region          14..441
                     /region_name="PaaK"
                     /note="Phenylacetate-coenzyme A ligase PaaK,
                     adenylate-forming domain family [Coenzyme transport and
                     metabolism]; COG1541"
                     /db_xref="CDD:441150"
ORIGIN      
        1 mtlhvqavpe agesrrffdp emetisreal ealqferlsk iirvaydkga lirakwdeag
       61 vtpddiqsld dfrrkvpfis kddlrawtar tgdpfggllc versalrqit gtsgttgdpt
      121 llahtritpp tgssfwnryf wesglrpgdt viicipttrg psvkiamefg lvpllvdhdp
      181 relsrlvela rvykpkamli mstplvigle kleaetdvdl raifepmkmv afggeapggr
      241 almlaqrwgm kiinllnagd ssvvldcsaq dgahpwedel liehvdpqtf mqveeggvge
      301 lvvttlentv dplvryradd lvrltrqpck cgrtharfkv lgragdevvv neqcilprdv
      361 gpmveafpet kaglyqlvkp qrvmpelwvr vgydgqpdld alrqrlathv semlglqakv
      421 elvpneellk qgpphkipri vki
//
LOCUS       WP_175907683             200 aa            linear   BCT 11-JAN-2025
DEFINITION  YbhB/YbcL family Raf kinase inhibitor-like protein [Burkholderia
            sp. BCC1640].
ACCESSION   WP_175907683
VERSION     WP_175907683.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..200
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=20862
     Region          43..199
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mrvdrritsp aspgrpspff aalpcaaacv afavlparae gpftvssndl tpggrvsaan
       61 vfdrgdckgd nrspqlswrn pppgthgyai tifdpdapgh gwwhwavagi pasvtslpad
      121 asasgflrri gasearndfg vdgyggpcpp pgkphryvit vyalkgtdlr vaqgrpapmf
      181 eheigtlaig taqltvtygq
//
LOCUS       WP_175907704             445 aa            linear   BCT 11-JAN-2025
DEFINITION  carotenoid oxygenase family protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175907704
VERSION     WP_175907704.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Poliakov,E., Uppal,S., Rogozin,I.B., Gentleman,S. and Redmond,T.M.
  TITLE     Evolutionary aspects and enzymology of metazoan carotenoid cleavage
            oxygenases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1865 (11), 158665 (2020)
   PUBMED   32061750
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Sui,X., Kiser,P.D., Lintig,Jv. and Palczewski,K.
  TITLE     Structural basis of carotenoid cleavage: from bacteria to mammals
  JOURNAL   Arch Biochem Biophys 539 (2), 203-213 (2013)
   PUBMED   23827316
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Kloer,D.P. and Schulz,G.E.
  TITLE     Structural and biological aspects of carotenoid cleavage
  JOURNAL   Cell Mol Life Sci 63 (19-20), 2291-2303 (2006)
   PUBMED   16909205
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Wyss,A.
  TITLE     Carotene oxygenases: a new family of double bond cleavage enzymes
  JOURNAL   J Nutr 134 (1), 246S-250S (2004)
   PUBMED   14704328
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..445
                     /product="carotenoid oxygenase family protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006720 - isoprenoid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49024
     Region          8..439
                     /region_name="COG3670"
                     /note="Carotenoid cleavage dioxygenase or a related enzyme
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]"
                     /db_xref="CDD:442887"
ORIGIN      
        1 mttfdlnrga iapvadevdl vdlrvtgtip peldgtllrn gpnppggrfe gndvlswwpe
       61 aamlhaiafe rgraagyrnr wartrrwadv hapeqaphlp dtnpnvnvlq hagellalae
      121 ggaplaitaa ldtlgaparh aafggamtah pkvdpvtgel ilfradwrap wlrygvadaq
      181 gvqrvdlavd vrapsmmhdl aitetrslll dlnvgydfam lkqghrmplr whddrdarig
      241 vmprhggdvr wfgiepcfiq hvvnaydcda scivldavry pwflrldart grfadnpvge
      301 lwryvidtan glidegplad ggielprine srtgrryryl yaveqpnnte mrgvmrfdhv
      361 rgtttryavp agdqngepvf vprpggaded dgwllvvvyr aatdtsdvvi ldaraidaap
      421 vatvhlprrv pagfhgawvp rerra
//
LOCUS       WP_175907709             434 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia seminalis].
ACCESSION   WP_175907709
VERSION     WP_175907709.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46465
     Region          25..417
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,156,
                     159..160,163,258,261..262,265..267,270,298,302,353..354,
                     358,362,378,381..382,385..386,389)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 metlvstvlp aagvsedaay rkvawrlmpl llfcylvsyl drvnvgfakl qmaghlglsd
       61 aayglgagif ffgyfifevp snlilhriga rvwiarimvt wgavsaltmf vttptafyam
      121 rfllgaaeag ffpgvilylt ywypahrrgr ittvfmtava lsgvvggpis gyilkafdgi
      181 ngwhgwqwly lleglpsiva gllvyalldd riaqakwlsd eerallernv naedavkshl
      241 slgavlanpr vwlmcaiyfs fviglygvgf wlptlihatg vadpltigll stvpyelavv
      301 amiaiarssd rlrerrwhla vpgamgtvgl vlavgwahqt glaiaaltla tmgiltaipl
      361 fwslptaflg gtaaaagiam insvgnlagf lgpylmgllk qltasndagl ymmagcmalg
      421 gllalslpka lvnr
//
LOCUS       WP_175907711             211 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia seminalis].
ACCESSION   WP_175907711
VERSION     WP_175907711.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..211
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23433
     Region          1..206
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mkthtlfycp ghlsfaphvi lrelgepfel alvsikdgat qsaefrqlnp kgkvpvlhtg
       61 ddvltessai llylalrfpq arlvpdtpmg laravewmnw lasvlpgtva lnfhpsrfse
      121 dpaahdgira kgragilaay aqiderlaar dwalgehysi vdpmlliffk wgnmlkldmr
      181 gfehwaahte rmlrrpavat alsveqisiw a
//
LOCUS       WP_175907729             230 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175907729
VERSION     WP_175907729.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..230
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24268
     Region          1..227
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mtaqwidipt gndsfggyla lpkrgegpav iiiqeifgvn shiravadqy aadgfvalap
       61 dvfwrtqprv eltyegadrd kgielmkktd vglaiadiga aadalrarpe aagkvaaigy
      121 cfggqlayra aaagkvdaav ayygggiqna ldlagkitqp ilfhyaendh gipldaveqv
      181 kaafagrhna sfhlypgaeh gfnctdrasy nqrasalahg rtltflaeha
//
LOCUS       WP_175907731             492 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: amidase [unclassified Burkholderia].
ACCESSION   WP_175907731
VERSION     WP_175907731.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..492
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52133
     Region          3..487
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mhsdylahda lglaalvrer kasprellda aigqaeavng ainaivlqdy ddarkraesa
       61 vdtgtdapfa gvpylvkdlg aavaglplsm gsrhyryfvp addspviars raaglnvfgk
      121 tntseigqmp ytepelfgac rnpwnldhtp ggssggaaaa vaagivplah asdgggsiri
      181 pasccglfgl kpsrnpvlvd lpsngelvvq havsrsvrds allldvttgq tlppgapgtf
      241 lgeldtppgp lriglvvdpm lapalsddtr aalddaaalv eslghhvepa tlnidyaraa
      301 etfltlwati aeemvlgara ltgrtpkrae fepatwamav vgrriararl pdvlewqrql
      361 tvqvsglvsr ydailcatla gppvkigelq ptpleaaqmk llgalpvkpl lremlakase
      421 kafawagcte lfnltgqpam svplywnarg lpigvqfvar htdealllrl arqleqarpw
      481 fdrrpplmqa qr
//
LOCUS       WP_175907764             235 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SGNH/GDSL hydrolase family protein [Burkholderia].
ACCESSION   WP_175907764
VERSION     WP_175907764.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Upton,C. and Buckley,J.T.
  TITLE     A new family of lipolytic enzymes?
  JOURNAL   Trends Biochem Sci 20 (5), 178-179 (1995)
   PUBMED   7610479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..235
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=24460
     Region          43..214
                     /region_name="FeeA_FeeB_like"
                     /note="SGNH_hydrolase subfamily, FeeA, FeeB and similar
                     esterases/lipases. FeeA and FeeB are part of a
                     biosynthetic gene cluster and may participate in the
                     biosynthesis of long-chain N-acyltyrosines by providing
                     saturated and unsaturated fatty acids, which it...;
                     cd01836"
                     /db_xref="CDD:238874"
     Site            order(53,90,118,209,212)
                     /site_type="active"
                     /db_xref="CDD:238874"
     Site            order(53,209,212)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238874"
     Site            order(53,74,118)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238874"
ORIGIN      
        1 mgyplataal gplllmqgrr vrrvtprlae aagprdgtag dgpplrvlvl gdsaaagvgv
       61 asqrdalsgq laralaashr vswkllartg ltaeelvdwl aaepaqpfdv avtslgvndv
      121 tggvsparwr aaqaalvell aarfgvahvi lsavppierf palpqplawy lglrakrlna
      181 tlaewaathp rctflrvalp lephlmaadg fhpgaaacaa waaqaadalr qrlra
//
LOCUS       WP_175907772             264 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: enoyl-CoA hydratase/isomerase family protein
            [Burkholderia].
ACCESSION   WP_175907772
VERSION     WP_175907772.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..264
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=27205
     Region          12..258
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mttsaapvgl viangvarir fqrpevlnai dvrtalclrd avytatrdaa vrvivlsgeg
       61 rafvaggdla yfrdagtdap saaveliapm heaievlasa aqpvlaslhg pvagagmsia
      121 laadlavaad nvvmnlayar vgatpdcsas wtlprlvglr kameiallad sinaqealrl
      181 glvnrvvpld vleaqttsma qrlaaaapla lagikrllrd sfnqslsaql aaeqaafaag
      241 agtqdfheal naffgkrapv frgr
//
LOCUS       WP_175907794             222 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175907794
VERSION     WP_175907794.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..222
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23400
     Region          29..187
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpprhvqvpa ppgqpaaqpa palrrrprqs raqatsealq qafvqlller gyakatirei
       61 aavagvsvgt fyeyfgdkqs laalcihrrv laladrlrea ahglrgvpra alaaalvdlq
      121 vdaiaadaap wsaffalerq vsplaayrrh ydayvalwhd alaqcsdppp aarldgiarm
      181 ahavcyggvs qalltlgpal dfaalrgelq avlgaylaaa ga
//
LOCUS       WP_175907799             131 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Zn-ribbon domain-containing OB-fold protein
            [Burkholderia].
ACCESSION   WP_175907799
VERSION     WP_175907799.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 131)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..131
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14415
     Region          17..127
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 measiqnrsl iqpdqefeqf lregrfmlqr stssgayvfy prvaapgagt ldlqwvlvsg
       61 cgtvyattvv rpkppqaayn valvdldegp rmmsrvesvp peavhigmrv qariatpneq
      121 apciifyplf e
//
LOCUS       WP_175907818             173 aa            linear   BCT 11-JAN-2025
DEFINITION  SET domain-containing protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175907818
VERSION     WP_175907818.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Qian,C. and Zhou,M.M.
  TITLE     SET domain protein lysine methyltransferases: Structure,
            specificity and catalysis
  JOURNAL   Cell Mol Life Sci 63 (23), 2755-2763 (2006)
   PUBMED   17013555
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Dillon,S.C., Zhang,X., Trievel,R.C. and Cheng,X.
  TITLE     The SET-domain protein superfamily: protein lysine
            methyltransferases
  JOURNAL   Genome Biol 6 (8), 227 (2005)
   PUBMED   16086857
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Yeates,T.O.
  TITLE     Structures of SET domain proteins: protein lysine
            methyltransferases make their mark
  JOURNAL   Cell 111 (1), 5-7 (2002)
   PUBMED   12372294
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459262
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..173
                     /product="SET domain-containing protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19432
     Region          12..143
                     /region_name="SET"
                     /note="SET domain-containing protein (function unknown)
                     [General function prediction only]; COG2940"
                     /db_xref="CDD:442183"
ORIGIN      
        1 mssrrisvrr sgvhgkgvfa vepikagerv veykgerisw kealrrhphd pnepnhtfyf
       61 aleeggvidg kidgnsarwi nhscapncea eeikgrvfih alrdigpeee lfydyglvid
      121 ekltkklkre yachcgtaac rgtllatpdd dgkkkkkkdr ksesgakdkk kkk
//
LOCUS       WP_175907823             190 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: recombinase family protein [Burkholderia].
ACCESSION   WP_175907823
VERSION     WP_175907823.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 190)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18951323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..190
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=20899
     Region          2..127
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(7,9,65..66,69)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            9
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(64,108..109,111..112,116)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(70,75..76,104,107..108,111..112,115,118)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(93..95,104..105,108..109,112,116,119,123)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(93,109,112,116,119,123)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(117,123..124)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          139..177
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
     Site            order(140..142,173..174,176..177)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 mkigyarvst deqnldlqkd alrragcevi fadqgisgat fqrpgleral hrlknggvlv
       61 vwrldrlgrs lgklvdlvsy leqqdvkfes lsenistdss ggvllfhmma amaqfertli
      121 sertkagiqa akargkrhgr kpalsatqqe qalalmktes itsvanlfgv nprtlvrmra
      181 rfaneqsltq
//
LOCUS       WP_175907901             435 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Burkholderia].
ACCESSION   WP_175907901
VERSION     WP_175907901.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..435
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=46765
     Region          7..414
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 merelqrrki vivgggvagl eiatslgrrw rrdphalsvm lvdrdsahvw kpmlhtiaag
       61 trdlsqqqtp yiaqacnagf eyqpgemcgl nraareirla plhapdgrll vparrvgyda
      121 lviaigsean dfgtpgvqeh cfridsrrqa dafnqevrir mlqclarere lsiaivggga
      181 tgvelaaelv hlteaavayg akglgsriri tiiesgprll aafpqdisaa tcarlgtlgi
      241 evmtdtrvta atangfelgd ggrveaslkv waagvkapgf lagldglett rgnqlvvqps
      301 lqttrdpaiy avgdcahytp agagralapt aqaahqqaqh mirhlpgavl hgqpipafay
      361 rdmgalvsla dydafgslgk fglfsgtsir grlaqfsham lyrshqarly gfwrgglvwl
      421 vdrlnmrlrs sirld
//
LOCUS       WP_175907903             219 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            seminalis].
ACCESSION   WP_175907903
VERSION     WP_175907903.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..219
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24186
     Region          30..179
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mteaplkvgg paseahtpep rvarqpsqlr grarvesild avsvtiaeeg lagvtmhgva
       61 rrsgtsigsl yhffpgrddl llglvrrhea aiaaingeml avprevwrrf svseavnyll
      121 apyvgytrqh pdffplmhdr syaeneatfr qvlrcivdar lpkakpaare rhaamlhtia
      181 vgvmrvaflv eperltfymn emprvmaayl vsleaeagr
//
LOCUS       WP_175907994             270 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175907994
VERSION     WP_175907994.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 270)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..270
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29001
     Region          18..264
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mthaaphaag emtyaaidlt ltagertlle gftqafrpge iwcvagpnga gkttllatla
       61 glqrpagghv eidgrplaaw ppeqlarrra lmpqqlhdaf satvfdtvll nrfpylggwg
      121 werdgdraaa rdalatfglt alasrdvlsl sggerqrval aatlcqdapl mlldeplahl
      181 dlhhqidglt alsawldagp rtvlfschdl nlarryatha llldgrghaw agpvhdvltp
      241 arasdafgyp lvlirengrd allpawperr
//
LOCUS       WP_175908052             117 aa            linear   BCT 11-JAN-2025
DEFINITION  Rieske (2Fe-2S) protein [Burkholderia seminalis].
ACCESSION   WP_175908052
VERSION     WP_175908052.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005408
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..117
                     /product="Rieske (2Fe-2S) protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=13076
     Region          3..108
                     /region_name="NirD"
                     /note="Ferredoxin subunit of nitrite reductase or a
                     ring-hydroxylating dioxygenase [Inorganic ion transport
                     and metabolism, Secondary metabolites biosynthesis,
                     transport and catabolism]; COG2146"
                     /db_xref="CDD:441749"
ORIGIN      
        1 mnterllcal ddlpdggsrg mlreglndrl cvvrqgddvf vwlndcpheh rpmeyrqdrf
       61 lsgdgrhivc yahsahfdir tgkcfagpci gqrltkvpal vangkvwipv elpsifd
//
LOCUS       WP_175907860             158 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia sp.
            BCC1640].
ACCESSION   WP_175907860
VERSION     WP_175907860.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..158
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17029
     Region          11..146
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtaklnpfaa apalmknwmt vsvaaagsle ptlielvkir asqinacanc lnmhtveare
       61 qgeteqrinl laawreapcy tdreraalgw tdaltrlseg hgaheaayaa lndhfsqeeq
      121 vkltvminvi ngwnrlavgf glwvdpaeak aaaakmva
//
LOCUS       WP_175908057             460 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia sp.
            BCC1640].
ACCESSION   WP_175908057
VERSION     WP_175908057.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..460
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=48885
     Region          157..435
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 mmqnrllshr lasvirdfnq pvmiwqaail vgalcfawva arfvhgrida rrraagrtpg
       61 agaqslkral fplfgglfvl aaqlgfdpfm stsllslalv plfgigliyv lfffarrvfa
      121 rdghthawls ivekivsviv waamvltvlg iqrdviawld svqfrvanah ltllsvisga
      181 lwvcvtlmva mwlgsvleer larattldan lkvvmsrvgr allvfaaili glslvgidvt
      241 vlgvfggavg vglgfglqki asnyvsgfii lldrslrlgd aisvgglqgv vtqirtrytv
      301 vrgldgnetl ipneklitdv vqnqssyltr gyakvavqva ytsdvelals vlaeaakdvp
      361 rvladpapta ylvsfgadgi dlelgfwied sakgtsgvrs svnrniwrlf gehgisipfp
      421 qrevrvvglp dglaatgava dgmpvaavvg gaadgrasaa
//
LOCUS       WP_175908120             418 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Burkholderia].
ACCESSION   WP_175908120
VERSION     WP_175908120.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..418
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43182
     Region          24..372
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mhvpssrfaa alagrllpag vdnsawlila srgmrgfcdg fiavllpayl lslgfsqlhv
       61 glistttlmg saiatiavgm ltsrfthrrm ltlaaglmaa tgigfaslsa lwpllviafv
      121 gtlnpssgdv slflpleqsr laeaasgdar talfaryslv gavsaacgsl vaglplwita
      181 rtgipapdam rgmfvvyait gaavcmlyrr lprpeahasr papplgpsrp ivvrlamlfs
      241 vdafagglvv nsllslwlmq rfglsiaaag qfffwaglls agsqlaaapl shrigllntm
      301 vfthipssvc ligaafapsl pltltlllmr salsqmdvpt rtayvmavvt paeraaaasf
      361 tsaprslaaa vaptlagglf slgwlgaplv acgalkiayd lsllaafrhi kldeggkp
//
LOCUS       WP_175908061             535 aa            linear   BCT 11-JAN-2025
DEFINITION  multicopper oxidase family protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175908061
VERSION     WP_175908061.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..535
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=58209
     Region          88..535
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mirrtflsha igvaaaslfa rtawaqhagh tgmagmdqmd dmpgmsgmsg madhaqhakp
       61 apaalaaada lpsgaplasl rtlanesrep gtfratlvaq pvarpmlrga rpttfwqfga
      121 gtqgpvvgpl idvregdtve irfvnklpqp stihwhglpv ppdqdgnpsd pvapgasrvy
      181 rftlpkgsag tywyhphphm mtaeqvfrgl agpfvvraad dplagwpern lfvsdlklar
      241 dgtippndmm dwmngregqf vlvngarrpr idvarderwr vwnacsaryl rvafddgraf
      301 eqvgtdgglf daprrvtsll lapgeraell vragdrasra vlqaaeydrr kmamshdggh
      361 gslppdptlp ladvtfapaa aralpatlra vpalgepvah kevafgeemd mdammnspah
      421 grpagmrfti ngatyaphra tltsrrgdve rwairnatdm dhpfhlhgtq fqvierasdg
      481 trtsepfraw rdtvnvrsge ivtmlvmqdm pgermfhchi lehedlgmmg tlkvv
//
LOCUS       WP_175908125             303 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia seminalis].
ACCESSION   WP_175908125
VERSION     WP_175908125.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32830
     Region          8..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..297
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,229..234,
                     240..241,243..244)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mpnfppdlrq wyyfvavaee rhfgraavrl smtqpplsqa iralegelgv elfartkrsv
       61 altavgeall pevlkllaaa ealpplaqsl algetgrlsl afvsiadygl lpsllrefgt
      121 ryplvrlqlt estsdvqide laaghidagl iiapvppryv aemsylplls eplvlampta
      181 vsnapedvpi hlkevatlpl vifprrlape fydgimecys aagvvprigq eaiqmqtiis
      241 lvsagigval vpqslrnlrr tgviyrplah dpfivetgla wrtgdisrvl asfinivrtl
      301 lpt
//
LOCUS       WP_175908239             314 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia seminalis].
ACCESSION   WP_175908239
VERSION     WP_175908239.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia seminalis
  ORGANISM  Burkholderia seminalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia seminalis"
                     /db_xref="taxon:488731"
     Protein         1..314
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=33910
     Region          7..218
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(47..48,50,64..66,72,74..75,115,217)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(47,49..50)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(72,75,78,84)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(107,111..114,116)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(112..113,136..138,190..191)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          230..314
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 mkviidsrtg iareichltf rstdgsdlpp ftpgshidlh lpsglvrqys lcgdprdlrq
       61 ydiavlreah srggsteaht lqpgsvieig eprnlfslas dakhsillag gigitpllsm
      121 athlstihas yelhycvrds araafldrls rqpyashtti yvdndersen adfeailarp
      181 dasthlyacg pdgfitaama tarsqgwqet nihreffava dpggsnsyfq inlarsnriv
      241 dvpadqtalv alanagveip ssceqgvcgt cltrvlagep dhrdmylses eqaandcflp
      301 ccsraksail vldl
//
LOCUS       WP_175908312             599 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Burkholderia sp. BCC1640].
ACCESSION   WP_175908312
VERSION     WP_175908312.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 599)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 599)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 599)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 599)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 599)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 599)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19843850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..599
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64085
     Region          1..>370
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          15..>153
                     /region_name="SbcC"
                     /note="DNA repair exonuclease SbcCD ATPase subunit
                     [Replication, recombination and repair]; COG0419"
                     /db_xref="CDD:440188"
ORIGIN      
        1 mkitdiyvsk vlgihtadlr lskpvalfag pngagksslq eavrmaltgn tvrvalkkey
       61 gslvtegsea gqivvacgeq ansvmlpggk ikrdlaedpr lplvldaqrf aqlddaarra
      121 flyelmgvki gaqeirarli dkltsparvi klavdtqlea itpmlragfe aaqkeaadra
      181 rgakqawrat tgetygsqka adwrpaavsf daaalrtleg ereslegeig elqrqigaae
      241 ageatarara skiaaqrdka agyakaaela qladgqvaef lpkvealrvr agtapagiec
      301 scpecgallr flngalaaaa aagardeeai aklpeyersl tvlqnaarnr rteleaadaa
      361 akqlkeiene tnadgghsss eaidatrrel gslmqrrkql dtdiaaarda erraaaaiei
      421 tgkafalyqd vaaweaiada lapsgipadl lrealtpmne rltalaelse wadvtitpdm
      481 eilangrvya llseserwrv dahiaaaish fsglkllvld radvlvgper drllywlddl
      541 ayteqidtal vfmslktppa glpdgieafw iedgqvavaa prraaygrqr erghravss
//
LOCUS       WP_175908330             159 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF2280 domain-containing protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175908330
VERSION     WP_175908330.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009432
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..159
                     /product="DUF2280 domain-containing protein"
                     /calculated_mol_wt=17609
     Region          1..149
                     /region_name="COG5556"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:444299"
ORIGIN      
        1 maalpehikl yvvqslacfd tvsrvakavr eefgvevspq qcerydptkr agstlskkyr
       61 eifertreef lqdtsrigva hrsvrlrkld ravglaedrg nlplmaqlle qaakeagdaf
      121 tnrhrlehmg kgggpitais tvtndpqeaa kiyatlmnp
//
LOCUS       WP_175908420             305 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175908420
VERSION     WP_175908420.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33805
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..295
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,190,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdrfdamraf vrvaeagsft kaaetlhmsk ttvthlvqql earlrvrlln rttrrinvtp
       61 dgiayyervt rlladmddae tslssasavp rgrlrvdvps pfarlilipa lpaflarypd
      121 iqldlgvsdr ivdiigenvd cvvrggkpnd ksmvarrvae lplgvfaspg ylalagtpsh
      181 prelenshhr iigfswgrag slyplvmhrr getvkvqsry alavddgnay laaglaglgi
      241 lwlprymsea hpragelval fenwqldpmp lyiayppnrh vsaklrvfid wvvelmgeha
      301 pvhmq
//
LOCUS       WP_175908397             893 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC1640].
ACCESSION   WP_175908397
VERSION     WP_175908397.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 893)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 893)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..893
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=96919
     Region          14..826
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnvtelaqai rggliqqdrl lktdipslpn nalvprravt rselgrdfsv tldlvstasd
       61 velktliaqp itlwiqqadk sylpingyvh tarrlgadgs lssyqlrfas wmhflkfrsd
      121 mrywqdkpvd ailadvfdmh pqargryqfa lskplpsrsy crqsetdwnf vhrlmedegl
      181 fgfwrhgedg kshtlvitdd vhavdalspn avtfdrsgtg tetagftqwa asrtlqstlh
      241 ttrtfdyksp ssagnpngts lptkagqgdl pgqaeiyeyt gaytypgqdr gehlskirle
      301 ewesrakrff gvggvraida grrftltghp ehdrdsasdr efaaigvtry iennlpisdh
      361 eanfphslqd qlaqaraghg eaaafqvghd dgsagfylve veaqrasvsy rspfehrkpa
      421 mqletavvvg pkgeevytde lnrikvmfvw drqsegreta scwmrvvqsd tgggyggvhi
      481 prvgeevlig yiggdcdrpi vmhrvyngav kpqwhsdgil sgfrskeyag sghnemvldd
      541 atgqnrarlf sssansllhl gylieqngnt rgaylgsgfd lrtdaygamr agqglyvtth
      601 pkqansqpld vseakqqlan aqglvesmsq vsemhqaesl gaghdalkqf tdatqnsvag
      661 asagggrtag ggtgnanafk epvmlfaspa gigvasqqsv hlasdrqtni vsgqstfits
      721 gkslvasvke klslfaqnag mklfagqgav eiqaqndnve mvaqktikvl satstiegva
      781 keeilltsgg ayvrikggni eihapgkidv kggqhafsgp tsmhktfkae gkkadmriry
      841 vdadgnvphg epikfttedg tehsvaldae gkaelknidf defvasqvkr tge
//
LOCUS       WP_175908496             154 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175908496
VERSION     WP_175908496.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..154
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17656
     Region          3..141
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mpikldaidr rilralqrns nqtnaelaqq aglsptpclr rvhlleeqgv idayvallnp
       61 aavelrftaf vrvtlerqdk ttverfarem eqapevlech lmagsydyll rviardlddy
      121 qrfqmetltq iegvrnvete iplkrikqtv rlpi
//
LOCUS       WP_175908521             192 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC1640].
ACCESSION   WP_175908521
VERSION     WP_175908521.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20033
     Region          26..159
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 marprspdkh dailaaaara laedgasatt ariarlagva egtvftyfet kdallnalyl
       61 slkaemream mtgfpehapa eqamrhawng yvswgvanpd grralqqlgv sgriddahra
      121 agaegfgaig sllraqvaaa gglkaddaha fcaalftsia etamesiard paladgyrea
      181 gfralwavlh av
//
LOCUS       WP_175908537             203 aa            linear   BCT 11-JAN-2025
DEFINITION  trimeric intracellular cation channel family protein [Burkholderia
            sp. BCC1640].
ACCESSION   WP_175908537
VERSION     WP_175908537.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..203
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=21145
     Region          1..196
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mhtlyliaiv aeamsgalmg mrrgmdrfgl alvgavtalg ggtvrdvllg hyplgwiahp
       61 eylvitlvaa tvaswaarhv armktlfvtv daiglaafti igcdigaatg sapiivvlag
      121 aitgvcggml rdllcnempl ilreelyasv afftgtlyvg sqhlgidagl asmvalvagf
      181 ttrmlavrlg wkmrtfgvad veh
//
LOCUS       WP_175908555             473 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cytochrome ubiquinol oxidase subunit I
            [Burkholderia].
ACCESSION   WP_175908555
VERSION     WP_175908555.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..473
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=52185
     Region          5..446
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mdtafsaldl arlqfaftvs fhivfpalsi glasfiavle yrwlktgkqy yktlclfwsk
       61 ifavafgmgv vsgvvmsyqf gtnwsgfssf agavtgpllm yevmtaffle agflgimlfg
      121 wnrvsprahf gatlmvaigt listfwilas nswmqtpqgf eivdgrvvpt dwfaiifnps
      181 fpyrlfhmai aafivaalvv aatgawhllk grrdkgvkkm fsmalwlllv laplqavigd
      241 qhgintlkhq pakiaaiegl wetekggtal nlfgipdmka ettryavkvp hlgslilths
      301 wdgeirglkd fapedrpnst vvfwsfrimv glgfamigla alawllrrrg glyeskwfqr
      361 falvmgptgf vsllagwvtt eagrqpwvvy gvmrtaqavs plsvqqvsls mmtfvivyfl
      421 vfgtgvyyml klmkagpalp dvghdaqhge pdtrpdhtar rpmsavdeli etv
//
LOCUS       WP_175908575             312 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [unclassified Burkholderia].
ACCESSION   WP_175908575
VERSION     WP_175908575.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..312
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33485
     Region          65..311
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mdtrhlvdpd irpwldawpt vtltadnlar hrdralplpp idtvgntlqh rrvpgsggap
       61 dvpvrvylpd datrplpaiv hmhgggyvrg aakdleavhr plvktlgcal vsidyrlape
      121 tpfpgaiddc yaalawtfhh adalgidpar igvmgesagg glaaalalla rdrgeyplaf
      181 qhlmypmldd rtcvraphph agefvwhaan nrfawtsllg hapgldgvsp yaaaaraerl
      241 dglppafiav gtvdlfvden igyaqrlira gvptelhvfp ggvhgfdivp darvstaarr
      301 ighdalrrfl hg
//
LOCUS       WP_175908585             531 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: thioredoxin family protein [unclassified
            Burkholderia].
ACCESSION   WP_175908585
VERSION     WP_175908585.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..531
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=55374
     Region          45..151
                     /region_name="SoxW"
                     /note="Thioredoxin-related protein SoxW [Posttranslational
                     modification, protein turnover, chaperones]; COG2143"
                     /db_xref="CDD:441746"
ORIGIN      
        1 mktvlrnvta aclfaaagaa fattapqgaa vsspsgdgah lppgiawqqg dvdaafalak
       61 rtgkplllyw gavwcpscnq vkstifsqqa fktrssffvp vyldgdtesa qklgerfkvh
      121 gyptmilfrp dgtevtrlpg eadldrymqa lslgmtaahp vrqtlataln dgaaltpaew
      181 hlladyswdt dgalpvpadr vavtlqtlsq raraagakad aarfalksav vaasddpaqa
      241 galdkaalad alravlrepa laradsdvlv aaparvvayl ggdaaqrtkl rgaydtalar
      301 lstdttlssi drlmalhgrv llarddahag aplaapalvd tarkqiaasv qgaanayerq
      361 alvseaadtl tdaglfdesd vllkaelprs stpyyfmsgl aanakargdk aaaldwyrka
      421 ydsasgpatk lrwgatyfan avalapddsa rieaiaasvl aqagktkdaf yganlraltk
      481 vvtqlnrwrg ggahdasvrs vvkqfdgvca klpagdpqaa acakliepvk a
//
LOCUS       WP_175908581             274 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175908581
VERSION     WP_175908581.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..274
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29853
     Region          22..267
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mtqtttnplp gsdaretmga adryrapald kgldilells eqkegltrte itkelgrnas
       61 eiyrmlerlv arryvmrssg gdrytlslkl falahrhppm nrliaealpl mqrfadaaeq
      121 schltvydrg nllviaqvdg pgpwgvsvrl gsrvgladta sgrvmlsfqg aeqrahmlae
      181 hrkvkgeaam neqelahacq sirqsgyvrq dsrqaygvtd lsapilgpag haiavltcpy
      241 mrridahmap svevvvaglr dtagqlsmcr aetc
//
LOCUS       WP_175908673             240 aa            linear   BCT 11-JAN-2025
DEFINITION  (Fe-S)-binding protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175908673
VERSION     WP_175908673.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..240
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25908
     Region          <2..237
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mrvglfvtcl vdlmrpeigf salklireag yevfvppaqt ccgqpaynsg dralardlae
       61 ktlrefeqfd yvvapsgscg gmirthygdl frddpelmgr yarfqqkvye ltdflanvak
      121 vtlapgeftg pvtyhdscsg lrelgvkaqp rvllaqrgva vtemkdcehc cgfggtfavk
      181 ygdisaaiad ekcanvrasg agavvlgdlg cmlniegrlr rtgdrdtrvl hvaqvlagdv
//
LOCUS       WP_175908724             404 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: amino acid aminotransferase [unclassified
            Burkholderia].
ACCESSION   WP_175908724
VERSION     WP_175908724.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Alexander,F.W., Sandmeier,E., Mehta,P.K. and Christen,P.
  TITLE     Evolutionary relationships among pyridoxal-5'-phosphate-dependent
            enzymes. Regio-specific alpha, beta and gamma families
  JOURNAL   Eur J Biochem 219 (3), 953-960 (1994)
   PUBMED   8112347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..404
                     /product="amino acid aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43615
     Region          1..396
                     /region_name="PRK09257"
                     /note="aromatic amino acid transaminase"
                     /db_xref="CDD:181731"
     Site            order(102..104,130,183,214,243,245..246,254)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(105,140,207,252..254,290,293)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            246
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 myehipaypg dpilslfqaf qqdahphkvn lsiglyydea gripvlestr laaervreag
       61 aphtylpmeg laayrqgvqr lvfgtdcaal aqgriatlqt lggsgalrlg aefvkryfpd
      121 saiwisdptw dnhrvifaaa gldvhtypyy dearndlrvd amlaaldalp arsivllqpc
      181 chnptgldlg rdawravidv larrglipfl dmayqgfgdg ldddawavra iveaglpaiv
      241 snsfsknfsl ygervgglsi vcasageaat vlsqlqagvr rtysspplfg aqlvsavlnd
      301 dvlracwede vaevrtrikr mrgalktrld arlpasafda lvtqrgmfsy tgiaatdvdr
      361 lrashgvyll rsgrmciagl ndanvdhvan aiadvlggts rqaa
//
LOCUS       WP_175908750             255 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC1640].
ACCESSION   WP_175908750
VERSION     WP_175908750.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 255)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 255)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..255
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25874
     Region          55..254
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mttrlarspl pqrlpahvar aaafalllvl llrpawlqgv fapfadngap viydraslld
       61 ltlahlgtva lssligtvva vaagiavtrp agadflpvar svvdigqtfp pvavlalavp
      121 avgfglkpvl ialvlygllp ifestiagle dvprdvveaa rgmgmsgwqq lvsvelplaf
      181 pvivngirla vvinlgtati gstvaarglg dviiaglqts ntafvlqggv ivgllavlvs
      241 daigalarva sarra
//
LOCUS       WP_175908752             392 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC1640].
ACCESSION   WP_175908752
VERSION     WP_175908752.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 392)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..392
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39981
     Region          168..370
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mtgravpsar rvtldkvgil igvltivavf gmpfmvlrpn riaagtglsa faalpavqga
       61 alaalwvvga lwamtasrpa wrlaagctwl atlayavgaa athvvapddv larvspaaga
      121 wlllfawavl vadalarlaf gpwrrlvalv vaiaaislpl asgwwdglsm mreyavrsdd
      181 fwreairhvs laggsvaaal vaglplgiac arvapvrtvv mpvlnivqti psiamyglmm
      241 aplgllaahv plaaalgvrg igvapavlal flysllpias svvvgleqvp phvteaaram
      301 gmtraqrllr vdlvlalpvi lsgvrivlvq nigltavaal iggggfgtfi fqgigqsaad
      361 lvllgaipti alalaaavvf eaattlakgr ta
//
LOCUS       WP_175908778             424 aa            linear   BCT 11-JAN-2025
DEFINITION  serine hydroxymethyltransferase [Burkholderia sp. BCC1640].
ACCESSION   WP_175908778
VERSION     WP_175908778.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Appaji Rao,N., Ambili,M., Jala,V.R., Subramanya,H.S. and
            Savithri,H.S.
  TITLE     Structure-function relationship in serine hydroxymethyltransferase
  JOURNAL   Biochim Biophys Acta 1647 (1-2), 24-29 (2003)
   PUBMED   12686103
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Chan,V.L. and Bingham,H.L.
  TITLE     Complete sequence of the Campylobacter jejuni glyA gene encoding
            serine hydroxymethyltransferase
  JOURNAL   Gene 101 (1), 51-58 (1991)
   PUBMED   2060796
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10793727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..424
                     /product="serine hydroxymethyltransferase"
                     /EC_number="2.1.2.1"
                     /GO_function="GO:0004372 - glycine
                     hydroxymethyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019264 - glycine biosynthetic process
                     from serine [Evidence IEA]"
                     /calculated_mol_wt=45404
     Region          4..424
                     /region_name="PRK13034"
                     /note="serine hydroxymethyltransferase; Reviewed"
                     /db_xref="CDD:237280"
     Site            order(16,18,25..26,35,40,58,76..77,85,100,107,142..143,
                     268,286)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:99733"
     Site            order(39,59,69,102..103,130,180,205,208,233..234,240,366)
                     /site_type="other"
                     /note="glycine-pyridoxal phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99733"
     Site            order(39,130,234,366)
                     /site_type="active"
                     /db_xref="CDD:99733"
     Site            order(61,68,125,129,131,260,350)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:99733"
ORIGIN      
        1 msntqpffsq plaerdapvr sailkelerq qsqveliase nivsravlea qgsvltnkya
       61 egypgkryyg gcefadevea laiervkqif nagyanvqph sgaqangsvm lalakpgdtv
      121 lgmsldaggh lthgakpals gkwfnavqyg vnrdtmridy dqvealaheh kpsliiagfs
      181 aypraldfar fraiadsvga klmvdmahia gviaagrhan piehahvvts tthktlrgpr
      241 ggfvltndee iakkinsavf pglqggplmh viagkavafg evlhadfkty idnvlanaqa
      301 lgevlkaggv dlvtggtdnh lllvdlrpkg lkgapveqal eragitcnkn gipfdtekpt
      361 vtsgirlgtp agttrgfgva efreigrlil evfdalranp egdhateqrv rreifalcer
      421 fpiy
//
LOCUS       WP_175908789             314 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC1640].
ACCESSION   WP_175908789
VERSION     WP_175908789.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..314
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34919
     Region          7..314
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpedfhflll pgfsalgfms aveplrvanr frtelyrwhv isadgapvaa sngipvaaea
       61 ayadvaqvet vfvvagfdpl vcydralgdw lrrqnrhgat lggidtgsfv laeaglfdas
      121 qtltlhweal safrerypgl natqelfeid drritcaggt asidmmldli grrhgadlaa
      181 aiseqfvvsr irqrsdsqrl eiaarygvhn rklihvidtm qrhmesplgs dalaqdvsit
      241 rrqlerlfsa tlndtptrfy lnlrldrare llqqtdmsit svcvacgfes pshfsrtyra
      301 rfgvsprsdr ratr
//
LOCUS       WP_175908796             305 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175908796
VERSION     WP_175908796.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33173
     Region          7..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(105,109,148,162,164,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(106..107,111..112,114..115,118,122,124..130,191,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 marlpdfegl amfakvaeeg sfaaaaramg vsvatvsrgv arledrlggr lfnrtsrqla
       61 ltefgrtice kagevyrhae eaesaarema vqprglvrla vpmsfglrwv apllpgffra
      121 ypdvsidlhl sdasvdliad gfdaalriaa lpdsslvarr lcavtqyvva speylkregr
      181 pahpreltgr pclsyayrah sdvwrftnda gdeeavmpng plrvtnadal lptllaglai
      241 aelpefiage yladgrleai ltewsltrgg lyfvtpsara rpakvaalsd yfaehlsdps
      301 wrwpk
//
LOCUS       WP_175908922             153 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175908922
VERSION     WP_175908922.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..153
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16655
     Region          14..126
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(15..17,31,48..50)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(62,65,69..70,79,97,101,107,111,114..115)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 msktvstpsa agpltigqva eltgvsthtl ryyeqagllr aisrtaaghr lyapadldwl
       61 afvmrlkatg mpiaqmqqfa alraqgestf garrrllaeh rdavrahiae lqasldaigd
      121 kiayyetqer eterratpsh slseqdghhg ttr
//
LOCUS       WP_175908866             255 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DUF899 domain-containing protein [Burkholderia].
ACCESSION   WP_175908866
VERSION     WP_175908866.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 255)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 255)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..255
                     /product="DUF899 domain-containing protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28518
     Region          1..254
                     /region_name="COG4312"
                     /note="Predicted dithiol-disulfide oxidoreductase, DUF899
                     family [General function prediction only]"
                     /db_xref="CDD:443453"
ORIGIN      
        1 mtnhltgtra ewltarrall daekaltrqs delarrrqal pwvrvekayr fdtedgpatl
       61 ddlfggrsql lvyhfmfgpd ykagcpscsa ladgfdgfav hlanhdvtla avsraplakl
      121 layrqrmgwh fpwassdgge fnfdfnvsft etqqrtgdve ynyaragham dmdpppaava
      181 qfaatcgtda atyardrpgm safvredgvv yhtystyarg ldglwgmyqw ldraplgrne
      241 tgvwwrrhde yaarg
//
LOCUS       WP_175908527             334 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Burkholderia sp. BCC1640].
ACCESSION   WP_175908527
VERSION     WP_175908527.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..334
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36132
     Region          7..317
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(12..14,44,49,75,138..139,179..180,201,230..236,272,
                     289..292,297,300..301)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(44,49,75,138)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 mritspsrvg fgtaplgnmy rdipneeala tvdaawesgi ryfdaaplyg aglaelrlge
       61 alagrprdey slgtkvgrlv ldehedasqr dlgekgglfr hglpnkvvyd ytedgtlrsi
      121 easlerlrtd rldtvwihdp aidfhgerwl evfdiamsga akaltrlrde kvikgwglgv
      181 nriepcelal ersdpdgfll agrytlldha galerlmpes aarglgiivg gpynsgvlag
      241 gthfeyqpat qemlgrvari rqiseqfgvd vravalqfsl ahpavaavip gasrpdride
      301 nlrlasvpip aslwdalkae rliaehapap agaa
//
LOCUS       WP_175908926             327 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: thiamine pyrophosphate-dependent dehydrogenase E1
            component subunit alpha [Burkholderia].
ACCESSION   WP_175908926
VERSION     WP_175908926.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..327
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=34605
     Region          6..327
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 mtvstqlsrd tlldayrlmr tirefeerlh vefatgeipg fvhlyageea savgtmlhlg
       61 ledyvatthr ghghciakgv dvhgmmaeiy gkktgvchgk ggsmhiadls mgmlgangiv
      121 gaggplvcga alaakhkktg gvgvcffgdg asnqgvifes mnlasvwrlp aifvaenngy
      181 aeatssswsv atdniadran gfgmpgvivd gfdffavhea lgeavarars gggptlvevk
      241 ftryfghfeg daqtyrapge vqklrdekdc lkhfearvvr aealttdelr avdaqvkali
      301 ddavaqakaa plpdaadllt dvyvsyp
//
LOCUS       WP_175909004             197 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: rhomboid family intramembrane serine protease
            [unclassified Burkholderia].
ACCESSION   WP_175909004
VERSION     WP_175909004.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..197
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=21024
     Region          1..197
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mtyalilvnf avfiaeasgw pvlidlfalw pparpgapat pdfhvwqllt ysvlhaslah
       61 iafnmfglym fgrdvervlg rarflalyla svlagaitql aviralppsd aptvgasagv
      121 fgaliayavl fpkrrvvllf ppvpmpawlf atgyaltell sglsgdtsgv ahfahlggml
      181 galvclafwr tradera
//
LOCUS       WP_175909011             324 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LOG family protein [unclassified Burkholderia].
ACCESSION   WP_175909011
VERSION     WP_175909011.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Naseem,M., Bencurova,E. and Dandekar,T.
  TITLE     The Cytokinin-Activating LOG-Family Proteins Are Not Lysine
            Decarboxylases
  JOURNAL   Trends Biochem Sci 43 (4), 232-236 (2018)
   PUBMED   29525484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..324
                     /product="LOG family protein"
                     /EC_number="3.2.2.-"
                     /GO_function="GO:0016799 - hydrolase activity, hydrolyzing
                     N-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0009691 - cytokinin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36223
     Region          123..300
                     /region_name="PpnN"
                     /note="Nucleotide monophosphate nucleosidase PpnN/YdgH,
                     Lonely Guy (LOG) family [Nucleotide transport and
                     metabolism]; COG1611"
                     /db_xref="CDD:441219"
ORIGIN      
        1 mstpvkrasa gtakgaarrr papvatiaka rgkrlrarrv tqspnrapad ddaallrgsg
       61 mrgirlqfdy wkaeerlqne righavviyg strivapsva narldeanrl laerpydpsr
      121 rravtiasrl veysvyyrva refgrivaha drctrtarla ivtgggpgim eaanrgayer
      181 gapsigfnie lpreqapnpy itpdlhfrfh yfairklhll erakaavffp ggygtfdelf
      241 evltllqtrk iaplpvilvg eaywrravdl afladegmid rrdlelftyc esaaaiwhai
      301 gswyarrrer aparckepak prtv
//
LOCUS       WP_175909017             277 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [unclassified Burkholderia].
ACCESSION   WP_175909017
VERSION     WP_175909017.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..277
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30493
     Region          3..142
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          153..275
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 msyktllvhl ddsercatrv dlalelagrw nahliglyvv cqdlfeplrr pdeplklavy
       61 erlceqrrke aeekfliaae ragrsvewqa ptgnateaav lharhadllv lgqenpddrl
      121 tfvarhfved vvmgsgrpal vvpyagdvrt lgenvligwd ggreaarvma dalpllarar
      181 fvnvetvsrg qpdpdktpag vdvaaylerh girasfsttp rqrsvsvgat llnrvtdlha
      241 dllvmglysh armhervlgg atrtiletmt vpvllsh
//
LOCUS       WP_175909012             111 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: c-type cytochrome [Burkholderia].
ACCESSION   WP_175909012
VERSION     WP_175909012.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 111)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 111)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 111)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..111
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11967
     Region          30..111
                     /region_name="CytC552"
                     /note="Cytochrome c551/c552 [Energy production and
                     conversion]; COG4654"
                     /db_xref="CDD:443692"
ORIGIN      
        1 msimrcaalc aialtagtaa aqttvpepte lvnaqhcmfc htpdmtflgp sfheiaeryr
       61 gdpraaaele rklrvggrvh wgdtpmpsai drggplsrdd ahllvqwvls q
//
LOCUS       WP_175909035             263 aa            linear   BCT 11-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Burkholderia sp.
            BCC1640].
ACCESSION   WP_175909035
VERSION     WP_175909035.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..263
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29171
     Region          91..245
                     /region_name="CE4_NodB_like_5s_6s"
                     /note="Putative catalytic NodB homology domain of PgaB,
                     IcaB, and similar proteins which consist of a deformed
                     (beta/alpha)8 barrel fold with 5- or 6-strands; cd10918"
                     /db_xref="CDD:213023"
     Site            order(97..98,153,157,201..203)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213023"
ORIGIN      
        1 mafrliacll llscmppass advatvdsps qrvlilvyhr fataqldsmt vrtetfrhql
       61 qaieangyri vpladvvrwh ggqadavpar avaitvddgh rsvydvlrpl lvahpmpvtl
      121 fiypsaisna syamtwdqlr tlgqsggvdi eshtywhpnf rterarltpd dylrfvsfql
      181 srsrerlese tgqpvrmlaw pfgvhdaqtd qlaaregyva aftldarpvr vtdpamalpr
      241 ylmtdacdtr cmngllrtag gkp
//
LOCUS       WP_175909109             512 aa            linear   BCT 11-JAN-2025
DEFINITION  S41 family peptidase [Burkholderia sp. BCC1640].
ACCESSION   WP_175909109
VERSION     WP_175909109.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..512
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=54987
     Region          64..428
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mmpasrvlhr ivawstgaaa aaafvacasa araqsasaqh aaaaaaasqp spcppdwepq
       61 lcelkaavev lkkqhltdvd igalldatvh dgiktlpyar ffnakeeqer rdderrardg
      121 tpgigivfet rpdglhiidv ipdapaeqag vrpddlvvam ndrsvvsids gevvklakgd
      181 agvplkltvr rgpnpatltf apvraivrph patakrlagd ilytrlssfp epavgnyida
      241 vqaarragpp vkgvildlri ngggalnaai gitalfagrd rtammtlerd gtkrrrfttn
      301 wpdyelpvmh gqdplaplqa ddwwrtvplv vlvdgqsasa aeataaalkd lgrarllgmp
      361 tygkglaqtg vdlidgtrvn ftfarnlrpn gcpmdgygvv pdwlvpprrd sdvdgvllwy
      421 revdlarapy adrlapdpfa qvrkarqtlr earvrekidt sksaalpqre fgtdadwqlr
      481 qaldalagrs vrtvaapaql mpaqpvcerv sd
//
LOCUS       WP_175909122             430 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia metallica].
ACCESSION   WP_175909122
VERSION     WP_175909122.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..430
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46362
     Region          38..419
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 msfhlgtppa rrarrrapml waallvagav haqqpsftld aalqsatdhs asmqaaqasv
       61 rarsesavka gqlpdpmlka gidnlpvngg qrftigqdfm tmrrigieqe wvsgdkrrlr
      121 salaneqvgr eragylaqla svrqqtataw lnavyakqal alqqalldhm nheleatkas
      181 yrgakasaad vvqaramlaq tqdqrlkaqq vyqtalials rwtavpaddv tgtppgpesf
      241 vsslppdelr lsqpalitaa ddiavaeadt avanserspn wtwevayqqr ggaysnmvsv
      301 gvtiplplnr knrqdrdvae kaalatkarl myedtlrqvq adirtqsatl asgrarianl
      361 gdallpaadq rvqladaayr agtgsladtf aarraqldaq lqvldlrrev sqtwaqleyq
      421 vvpstlaaaq
//
LOCUS       WP_175909143             220 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FMN-dependent NADH-azoreductase [unclassified
            Burkholderia].
ACCESSION   WP_175909143
VERSION     WP_175909143.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..220
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24285
     Region          1..206
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mstllhiess prksrsasrd vahayleawr dahpehrvdv ldlwatplpe ldgdaldaky
       61 adlsgtplse gqqqawagfr qlaqrmhdad tllfsvplwn fsipyklkhf idavshrgll
      121 fsfderglag llngkkavvi yargldysrq sttpaesfdf qrpfleawlr figitdiesi
      181 ivektlfgpe vdhvgreaar eqavtlahaa sssasasvdg
//
LOCUS       WP_175909148             336 aa            linear   BCT 11-JAN-2025
DEFINITION  sodium:calcium antiporter [Burkholderia metallica].
ACCESSION   WP_175909148
VERSION     WP_175909148.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schnetkamp,P.P.
  TITLE     The SLC24 gene family of Na/Ca(2)-K exchangers: from sight and
            smell to memory consolidation and skin pigmentation
  JOURNAL   Mol Aspects Med 34 (2-3), 455-464 (2013)
   PUBMED   23506883
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Besserer,G.M., Nicoll,D.A., Abramson,J. and Philipson,K.D.
  TITLE     Characterization and purification of a Na+/Ca2+ exchanger from an
            archaebacterium
  JOURNAL   J Biol Chem 287 (11), 8652-8659 (2012)
   PUBMED   22287543
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..336
                     /product="sodium:calcium antiporter"
                     /GO_function="GO:0008273 - calcium, potassium:sodium
                     antiporter activity [Evidence IEA]"
                     /GO_process="GO:0006874 - intracellular calcium ion
                     homeostasis [Evidence IEA]"
                     /calculated_mol_wt=35399
     Region          19..332
                     /region_name="ECM27"
                     /note="Ca2+/Na+ antiporter [Inorganic ion transport and
                     metabolism]; COG0530"
                     /db_xref="CDD:440296"
ORIGIN      
        1 mtfmfvelaf mliviliaae vftnalehlg erlkisegvt gslfaavgta lpetmvplla
       61 laggtanpav neeigvgail gaplmlatlt tflmtlavir trglrgtiap ertgfvrdmn
      121 yflaafslat aamfvphhng avrallavml vgiyvmyvvm tfrasnqlvd aghgteapht
      181 mflsrlgvpt nlatialqll igvallvgga kgfihgmegv shalgisall lsliivpiat
      241 elpekvnsvl wirrgkdtla fgnitgamvf qgtllpaigi mltpweprpe vltgviitla
      301 aaawlrfnar trglaiwall angagyagyl fltlar
//
LOCUS       WP_175909153             271 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia].
ACCESSION   WP_175909153
VERSION     WP_175909153.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 271)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 271)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..271
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30425
     Region          14..271
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 msakvrtpfe vtvsvwramf lrealdrlfe araawlwllm epviyiaiha fgyttfrihe
       61 vggiaitmwi iagfvgfllw rrtwiqvlhg idcnyaffvy rqvkpfdaai vravlelflm
      121 vpisiiiiaa alatgrvitp dllnpillpa dpllaiasll glwlfglglg lvtsvamnfv
      181 pevdhifklf ylplyyisga lfpimsipnp yrdillinpv vhglelvrtg flpsyhtapg
      241 isltylygwa lgamllglal yrrfsnklvt r
//
LOCUS       WP_175909155             220 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175909155
VERSION     WP_175909155.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 220)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..220
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24391
     Region          1..220
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 miciedvhkr ymtehgvgkw vlrgidmtip pkqsvaligv ngagkstllr iiggvdhptk
       61 grverlcrvs wpmgaggleg tltgrqnakf vcrihgrqde lrdrlafiqd faelgeafdr
      121 pvqtyssgmr srlqfalsla fdfdvyisde vtaagdakfr kkaadafkgk tsqasvimvs
      181 hdestlrqfc qsgiwinegr aswfdeldea lraykesifa
//
LOCUS       WP_175909181             442 aa            linear   BCT 11-JAN-2025
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Burkholderia sp. BCC1640].
ACCESSION   WP_175909181
VERSION     WP_175909181.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..442
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=47356
     Region          71..440
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 malgehlrqq laakalkrql erateaaaap gvpgtpaaqa asarsrfesm pqyqqvrimr
       61 emgeklrvds pffrvhdgva gattriggre yvnfanynyl glagdptvse rakaaidryg
      121 tsasasrmva gerpvqrdle ralaafygsd dcvafvsgha tnvtvigalf gpgdlivhda
      181 lahnsivqga qlsgakrlsf ahndwqalde llsrvrreyr hvliaiegly smdgdfpdlq
      241 rfvdvktrhg afllvdeahs lgvlgatgkg irehcavapd qvdmwmgtms ktlagcggfi
      301 agcqplvdml rhlapgflys vglaptlaea slaalerlqa epervaqlqa rgrqfltear
      361 aaglntgtsa gyavvpvitg sslkaaqwan amfdeginvq pifypaveek aarlrffics
      421 thepgqisrt vdvlarlagr aa
//
LOCUS       WP_175909244             291 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia sp. BCC1640].
ACCESSION   WP_175909244
VERSION     WP_175909244.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..291
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31084
     Region          32..286
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mpasplpddd ladsdtddtg sgehgeggek vrsgiqsiev gfrlldvlts eprammlrdl
       61 aqragmspak ahrylvsfsr lgvvsqdpvs gryelggfal qmglarlarv dgvklarial
      121 telrdrvdqt vgiavwgnqg ptivhwmess hpakaslklg dvmpllgsat gllfaaylpr
      181 sktatmlere ladtrrsphh ggprtldeve avladvrahq aarvegmllp tihafcmpvf
      241 davgelalai valgqegmfd iawggemdta lracaqklsy elgyspdard a
//
LOCUS       WP_175909261             358 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia metallica].
ACCESSION   WP_175909261
VERSION     WP_175909261.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..358
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38938
     Region          12..335
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 msitassnvq siwytrcpvp tplgiaahlg wldsefagdg itvralqesr haalhhahvd
       61 hsldnafrqg gsipalwara agaetrvval twvdeaqaiv alpesglkrp kdlrgrrigl
      121 prrdgeridi fraaalrgfv salsldglgp advawidvpa snlrapvstp atrdaafshp
      181 aslssrrlya aeaaalvrge vdaiyvkgsl gletahliga qpvvdigfhp dpqirinngs
      241 prpltvnast lerhpdivsr flarvtdveg wareheqevl gylgretgsg hdwlrlayga
      301 dvhrrlrtdl deasiaaldd fkrflvewrf lpadfdvraw idrraldgia tlsldsar
//
LOCUS       WP_175909282             101 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DUF485 domain-containing protein [Burkholderia].
ACCESSION   WP_175909282
VERSION     WP_175909282.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..101
                     /product="DUF485 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=11084
     Region          3..100
                     /region_name="YjcH"
                     /note="Uncharacterized membrane protein, DUF485 family
                     [Function unknown]; COG3162"
                     /db_xref="CDD:442396"
ORIGIN      
        1 mehsviesvt arrdyqqlvr arrrfsftlt almiatyygf illvalaprv latplyrgat
       61 ttvgivagva iilvaiglta cyvlranraf drrvdailqr s
//
LOCUS       WP_175909288             185 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia
            metallica].
ACCESSION   WP_175909288
VERSION     WP_175909288.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..185
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19283
     Region          40..178
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msayplhtid sapaasrpvl qqlqqtfgvi pnvaaamaas pvlingfigl fervhasslt
       61 epqiqtlllt navanasewp vafhtalalk qgvthadvda irrgglpgda tlaalsatar
      121 rlidirgrla dadrqaffda gftaeqllev iavvaastit nyvgsvarpa leapfdafaw
      181 ranaa
//
LOCUS       WP_175909362             285 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia
            metallica].
ACCESSION   WP_175909362
VERSION     WP_175909362.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..285
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31248
     Region          9..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          105..270
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 madtrdnllg aylrdrrekl dpaalglpat rrrtpglrre evaqrahvsa awytwleqgr
       61 ggapsadvld rlaralllnd aerehlflig lghlpevryh asgqvsprvq hvldsldasp
      121 aivrsatwdv vawndaaaat ltdyatlape rrnilrlifv dprvrgaqan wervarfavg
      181 afradvargg atravqafvd emraasaefd alwrdhdirs heegtkeihh pavgrialey
      241 aafavngrpd qtlviftpet aadrarvrsl vaaraqalag qmpva
//
LOCUS       WP_175909382             442 aa            linear   BCT 11-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Burkholderia sp.
            BCC1640].
ACCESSION   WP_175909382
VERSION     WP_175909382.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..442
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=47236
     Region          3..408
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mnkrmsaavw illamaagif igymiytqfp dkqaateiag yislvsdvfl rlikmvigpl
       61 vfstlvvgia hmgdassvgr vfvkafgwfv taslislllg llmanllrpg enlglplpdi
      121 gasahlatsk ftlkdfvshm vpksiaeama nneilqivvf smffgvalsa lgergkilva
      181 aidqlahvml kitgyvmkla plavlaamaa tvavnglsvl lkfavfmgdf yvslfllwst
      241 lviagllflg rrvfkllvli keafmlsfat asseaaypki ldaldrfgvr rkissfvmpm
      301 gysfnldgsm myctfaslfi aqaynihlsl gtqitmllvl mltskgmagv praslvviaa
      361 tlhqfdipea glllilgvdt fldmgrsatn avgnsiasav vakwegelms esealahaah
      421 ldaelerqnn epaygagqat sv
//
LOCUS       WP_175909436             414 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia sp. BCC1640].
ACCESSION   WP_175909436
VERSION     WP_175909436.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..414
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43832
     Region          27..414
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mteantqapa vpgtvvvvgg gqaagwvlkt lraegfagrl vmiadephlp yerpplskav
       61 lagdadietv rvvrpdefda lnveawqper aasidrarrv vktesglvie ydrlviatgg
      121 tsrrlpdaiv rtpnlhylrt ldeaaalgek lrasqrvlvi gggwigleva atarklgvea
      181 vvvegaprlc grsvpqivsd flldlhrang vdvrlgaala sldaqpddas kvratladgt
      241 tidadfavag iglalnatla sdaglaiddg ivvdefgats dpaifacgdv anhhngwlkr
      301 rvrleswana qnqaiaaaka vlgvrapyae ipwfwsdqyd vnlqilgdlp adaqlvvrgd
      361 iaarratlff vgdghvrgvi ainnarelkl arkwmnqgra vdtealadtt kala
//
LOCUS       WP_175909462             325 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia metallica].
ACCESSION   WP_175909462
VERSION     WP_175909462.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..325
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33048
     Region          13..322
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mnlanltser ddarrtsrra lfaqardrsv ylafvalavf nlivtpgfsn plaarsllfq
       61 aapivlialg qnlaiatrgi dlsvgsvmal ssaviavclp ygtgaacaaa iaiglavglf
      121 ngglvarlgi dplisglall vaarglaqal lggsrvslpp sdafdfigig tflglpvvml
      181 ialacaaivf fvvrnttfgr ytilvgasrd aahlagvpvr rtllavyaas galaglaglf
      241 atarlgagdp nyvgvnfeld aiaasviggt plsggrvsiv gtvfgvlllq lldasfimnn
      301 isytyaqilk aafilgalyl qrsga
//
LOCUS       WP_175909464             331 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia metallica].
ACCESSION   WP_175909464
VERSION     WP_175909464.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..331
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33550
     Region          14..330
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mstapiptht aqdasrarra qfvrlvqsrg aiailvlvcl iagrvfphfl sapnlldiva
       61 aaafvaliti gqsfviilgg fdlsvgslvg lgtviaayaa pygwgaalaa pvcaglivgl
      121 vngwliarar mapfivtlaa llglkglslv lasqdmlian pgffatiang alfgvgnlvw
      181 ivliaylvaa fvlnhtryga gvfaiggnee aarmlgvnve glkivtygls galaglagal
      241 lasrldsglp gagnsyelqs iaaaviggvl ltggvgtlfg plagvlllgv ienvinqvgt
      301 lspyyqnlas gaflllavia qtlltgkrrk r
//
LOCUS       WP_175909470             413 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia metallica].
ACCESSION   WP_175909470
VERSION     WP_175909470.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..413
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=45392
     Region          8..202
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mnrqqswtrt aapgeiiyse gfagepvifl iadgkvelst rcddkrviva tlgrgeffge
       61 sallaaepra htakalsfcq ltvvpagmld eeiervsall rhivrtmirr vkrkddqlat
      121 ythadfmpgv lsyahvlalm agaeardggd awvrrpmqah aaetsvplae virkcraiag
      181 hsrphvlaml rrmeklnlvt ieaaqadhag gavdyaassd arqvvtfdaa rvidraqqva
      241 dhdldlsins elelieladl esligvertm llnklsngei adevfafrks kvlsyveqkg
      301 vayfsrrnar raevrsledl vsidqrtlfd vigtfdtydl aklianlddr avadklfsvm
      361 tearrnevsw vmrrelkldp veiedieqrv ldavraakap aagtapvasa sda
//
LOCUS       WP_175909482             252 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia sp. BCC1640].
ACCESSION   WP_175909482
VERSION     WP_175909482.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..252
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26166
     Region          1..245
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 msvskkiaav tgagsgigra aaialanagy tvaligrkea slretkeaig aahgdahvfp
       61 advtdeasve hafaqiaqqf grldvlfnna grnapavpld eydfgvwndv vatnltgvfl
      121 caraawrvmk aqtpqggrii nngsisaytp rpntiaytat khavagitks laldgrayni
      181 acgqidigna atsltdrmte gvpqadgrma pearmdvthv anavvqmasl pldtnilnmt
      241 imattmpfvg rg
//
LOCUS       WP_175909511             413 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia sp.
            BCC1640].
ACCESSION   WP_175909511
VERSION     WP_175909511.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..413
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45181
     Region          69..387
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mtlneswfap lvgilillaa agaitatahf llfrvvarla rlsatridda lfefgafkwl
       61 nrivpfvvik lglgavpgip tvaaqaadkv lfalivflvs mtisatlsal ehthrtsrrd
      121 qprlslkgam qlvklvmfit aalvvigdat gkqiglllsg igamsavlml ifkdtllglv
      181 agvqlssndm lrigdwitmp sagadgtvid itlntvkvan fdhtiitvpt wklitesyqn
      241 wrgmteaggr rikralfvda tsvrflgnde ierlerltll kdyledkvda iaqwngtlga
      301 agecqanrrq ltnlgtfray vanylkghpr irrdmtcmar qlpltaegip lelycftdtt
      361 twvdyeaiqs dlfdhliavl pefglrvyqh psgfdmrrma gaaqaelsap har
//
LOCUS       WP_175909536             539 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GMC family oxidoreductase [unclassified
            Burkholderia].
ACCESSION   WP_175909536
VERSION     WP_175909536.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..539
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=59541
     Region          22..538
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 madtdtqkad vvvvgsgvag aivahqlama gksvilleag prmprweive rfrnqpdktd
       61 fmapypsspw aphpeygppn dylvlkgehk fnsqyiravg gttwhwaasa wrfipndfkm
      121 ktvygvgrdw piqyddlehy yqraeeelgv wgpgpeedly sprkqpypmp plplsfneqt
      181 iksalnghdp tfhvvtepva rnsrpydgrp tccgnnncmp icpigamyng ivhvekaeqa
      241 gaklidsavv ykletgpdkr ivaaiykdkt gadhrvegky fvvaangiet pkillmsanr
      301 dfpngvanss dmvgrnlmdh pgtgvsfyas eklwpgrgpq emtsligfrd gpfrateaak
      361 kihlsnmsri nqetqkifka gklmksdeld aqirdrsary vqfdcfheil pqpenrivps
      421 ktatdaigip rpeityaidd yvkrgavhtr evyataaqvl ggtdvvfnde fapnnhitga
      481 timgadards vvdkdcrtfd hpnlfissss tmptvgtvnv tltiaalalr msdtlkkev
//
LOCUS       WP_175909573             133 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Burkholderia metallica].
ACCESSION   WP_175909573
VERSION     WP_175909573.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..133
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=14482
     Region          16..132
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mplihaaavl dadapdyvvr lqagthaltg deapreggqd rgpapyafvl aglaqctaat
       61 lrmymqrkaw paaridvrte lhadrdgtqy vrrvvtldgp lddaqrqrla eicektpvtq
      121 fikrgtridt tls
//
LOCUS       WP_175909587             138 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia metallica].
ACCESSION   WP_175909587
VERSION     WP_175909587.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..138
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14751
     Region          1..125
                     /region_name="COG3607"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]"
                     /db_xref="CDD:442825"
ORIGIN      
        1 mhkmvfinlp vadlprskaf yqalgfevvp aytndqaaci kigdtifaml lvrpffqtft
       61 gktivdpatq vqalsclsce sraevdaiva ralaaggsap qppreypnmy ghgfddpdgh
      121 awelmampld aaaeghap
//
LOCUS       WP_175909593             146 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175909593
VERSION     WP_175909593.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..146
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=15845
     Region          44..146
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 msgihhghdl fdefarvqrq maslfgelpt giravrpsaf palnvgatdd aieivafapg
       61 taaadfdvsi drdlmtisge rkpvpqdagd dvrtyaqerf hgafrrvvel pqnadadnvs
      121 aryengclli rvgrreaskp rainvq
//
LOCUS       WP_175909609             445 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: dihydrolipoamide acetyltransferase family protein
            [unclassified Burkholderia].
ACCESSION   WP_175909609
VERSION     WP_175909609.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..445
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47603
     Region          2..445
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mgihvikmpd igegiaevel vawhvqpgqt iaedqpladv mtdkaaveip spvagkvlel
       61 ggrigemmav gselirleve gdgnlksgak areasaevaq ppaavdvrae sssvdegset
      121 haspkatpha asrapaeprr aehavppraa lapgerplas pavrqrawdm gielryvrgt
      181 geagrilhad ldayartggg aargsqargy derndetdvp viglrraiar kmqeakrrip
      241 hftyveeidv teleslrael nlrhgdtrgr ltplpllira mvialrdfpq inaryddeag
      301 vvtrygavhm gvatqtdsgl tvpvlrhaea rdvwsisaei arladavran raqrdeltgs
      361 titisslgal ggivstpvin hpevgivgvn riverpmird gaivarkmmn lsssfdhrvv
      421 dgadaaefiq avrgvlerpa llfve
//
LOCUS       WP_175909660             503 aa            linear   BCT 11-JAN-2025
DEFINITION  HDOD domain-containing protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175909660
VERSION     WP_175909660.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..503
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=54864
     Region          18..218
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 msitahlprt alldklwarm nergdfplls eslratmaam knddldftal vrvvlsdfal
       61 tqkvlrlans amymafggni ttvtralmvl gmdtvghlvv glklvdhfhh stprridakl
      121 elnrallsgc varkltehae lrggeeavvc tlmrqvgkll vvcyldsewd rirrraaeln
      181 gdeaaacvdv lgvgfdeigl eaaaswrlpd viragmadgd ggsahaasad eddidedrqr
      241 prdacaddsp ervrwlravs rcstdvagal ampagpqrda hiavlaqhye qeldidagal
      301 veiadrlare easdtvmrei velranadai araqpepeac leagladlra lpsehvltpv
      361 lalaseslla glaftrtvmf vrredgafaa rlgfgpdvda aldrlcfder fepdvfhlai
      421 tnsvgifieq aqdpkmvkrl pawyldalpd trafvllpvr vgtktvglly gdwagaqpar
      481 kitqqemsvl nelarelgrf fpa
//
LOCUS       WP_175909722             401 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Burkholderia].
ACCESSION   WP_175909722
VERSION     WP_175909722.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..401
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42397
     Region          17..385
                     /region_name="MFS_MJ1317_like"
                     /note="MJ1317 and similar transporters of the Major
                     Facilitator Superfamily; cd17370"
                     /db_xref="CDD:340928"
     Site            order(27..28,31..32,35,68,119..120,122..124,127,147,
                     150..151,154,228,231..232,235..237,240,267,271,320..321,
                     325,329,345,348..349,352..353,356)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340928"
ORIGIN      
        1 msapsptarr paiprtvwal glvslfmdls selihallpi ylvstmgmsv aalgvlegaa
       61 eatamivkvf sgaisdwlgr rkglllvgyg laaltkplfp lastpavvva arlldrvgkg
      121 irgaardalv adiappeirg acfglrqsmd tvgaifgpml aivlmlwfgd rirtvlwfav
      181 vpafvaiali vfgvrepeqs kpdrrfrspl rwnalrefpr sywfvvaaga tftlarfsea
      241 flvlraqqtg ldaawipavm vamsvtysls awpagivsdr ldrrvllaag mvllivadll
      301 lgigtstlsm fagvavwglh mgftqgilaa mvsetspatl rgtafgvfnl vsgicmllas
      361 siagalwthf gasttflaga alvvvplclc rfmprpgash a
//
LOCUS       WP_175909760             391 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia metallica].
ACCESSION   WP_175909760
VERSION     WP_175909760.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..391
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=43136
     Region          27..84
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          116..318
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(131..132,134..135,138,142,144..150,244..249,
                     255..256,258..259)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrdpldpaal praaadaaga ldvldarlmr illvlltert vsraavrlnm sqpatsaalk
       61 rlrtllgdpl lvrsrygmvp tefgarliep lrnalrvidf iriqqptfda rtsvrtyrig
      121 cpdylnvlfv pklvalfrer apnaqlvfhp lgdgfddera ladgeldvvi dnrparasrf
      181 rqddlfddri vclmrathpl arrgaltaad faeapqlcpt pswleasgai drqlervglq
      241 rrivvtlphf elaahalvrt dmlltttyrl arhyakllpl aavalpaepp divyrmtwne
      301 agectegvrw lrgliveatr awldadamrp avaavaaaaa dadsrptapp aadtpepvrr
      361 trrrrathcr ashparvaha arihrgatkp h
//
LOCUS       WP_175909764             764 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia metallica].
ACCESSION   WP_175909764
VERSION     WP_175909764.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..764
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81201
     Region          <34..>162
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          176..742
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mnrsellard gcltvirppa ppvkpapgqp gslssyvpal pevfvaildd grilafnghv
       61 dlgtgirtsl aqivaeeldv paarvtmvlg dtaatpnqgp tiasatiqis aaplrcaaaq
      121 arhallalaa erfgadaaql hvddatisan ghtatfaalv aarrialtld lntrtkdpar
      181 yrivgrsspr vdlpakatgq ltfvhdvrvp gmlhgrvvrp pyaghdsgaf vgtslvdvdr
      241 asvadvpglv avvtigdfvg vvaereehai raarqlrvtw rplpvlppld epaaaiaaap
      301 atrrvlldeg dvdaarahad titlsrtyaw pyqmhgsigp scaladyrap gcgritvwsg
      361 tqnpvslryd latlvardea dfdvvrmeaa gcygrngadd vcgdalllsr avgrpvrvql
      421 sradehlwep kgtgqlmqvt gtvtrdgrll gydfttryps ndapllaall tgaiapgprv
      481 femgdrtavs pyasphrrfv cedlaplvra swlrgvsalp nsfahdafad ecaaltgvdp
      541 lafrlrhlqd araiellqav aeragwtprv prqdrerdgs rhvhgrgiay aryvhsrfpg
      601 fgaawsawiv dlsvdrvsge iriervtvgq dtgtminpdg vrhqihgnvi qvlsrtlker
      661 vrfadgkvas rewasypilt faevpdvdvv lmprqgeppl gagesasvpg paavanalfd
      721 atgvrfyapp ftpetvraal rdagrlmttg avdavgaqta agtv
//
LOCUS       WP_175909765             845 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC1640].
ACCESSION   WP_175909765
VERSION     WP_175909765.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 845)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 845)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..845
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..845
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=92244
     Region          1..807
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 malfdsprtl svcgaampmy gdrpiltpvk ltggeavgel feytlelktp delgfsqsia
       61 anidldklig teltvsiqle gvghfirgla gnagmaniga gtreitgivs rasilredgr
      121 sivyavtlrp wlwlatkncd crifqdmsvi eitdavlsty lfpvdkrltp prpnnvwpkr
      181 diqrqhhesd wtflqrlwee wgifyffeha dgkhrlvlcd aiaalkphge ayatiryeap
      241 nsrrvdeehi halsisnalt tgavtsvdyd ytrpradltv gredprdtgl ahqehytwad
      301 yaqpqagmgg lsgasneprt eaeyltlvqm qayrcqglra sgqgnlrglv vgqtfvlthy
      361 pqnaanreya vigckltiee vgeasgsgqr yhceadfvlq pthepfrlpr tiakpritgv
      421 eyavvtcpen qeiwtdaygr vklqflwdrl gdndersscw vrvagawhgd qfggiflprr
      481 ghevevafan gdpdlpiivg savnafnmpp falpenqtla gfrskeigar rantlafddt
      541 ngriqahlss degtsqlnlg yitriagnag rqeergrgfe latglwgvvr salgmlvtte
      601 arsdaeghvk gmgetvqrlv eardtherla qlaqqnhaqe vnsdqsevtt alnaqndair
      661 ggaksssdpf pefaephltl aspagiqatt agsthiasge hlalttgehl giatgrslfa
      721 tikeklrifv ydagikliag agsidieslk dtinlmakir irqtatkiei waeeelslrg
      781 gksfitlnns gitngtpgqw qsyaaihemp gprsasegip aaelkvcems mvkaavkhaa
      841 ivpls
//
LOCUS       WP_175909819             291 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia sp.
            BCC1640].
ACCESSION   WP_175909819
VERSION     WP_175909819.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..291
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32303
     Region          35..277
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mfldhlhper wtflwnalst lslrlcaala llvagwwlsk rignwlnrll ankervddtl
       61 rpilcdvavw girivaivga lsqlgietas vvavlgaagl aiglalqgtm qniaagimll
      121 llrpfkvgdf idggsnvagt veevglfmtr ltkpdgicey vpnsalwgsa irnytrnptr
      181 rldlevevsv hddidralda lralaeadpd vlqdpapdvm vmrfddstai anmrvwthtd
      241 kfwamrwrla rqvrktlada dcalpirtre lhivhdaeqq rraetrrvqa s
//
LOCUS       WP_175909879             289 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175909879
VERSION     WP_175909879.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..289
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31790
     Region          112..271
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mllnvnpfhr dtdrfnvsfk algelietvg tphfvprltq llndvvpldv ahversrvdg
       61 tmptgyrcew igssgigtat aeisdvmtly yerfldsdpl faglrgktgt mlvvrdiaai
      121 ppgefrqrlf ddvhighecv largtryaqh sialergrdr ppftlaemnr frsisdmlfp
      181 llelhastta arrvahpmpe vhplaqfdar iaadgvklsk reyetckhli sgktvpetad
      241 ilgvrvasae syvkrafakl gvrtkrelaa wgsaaphdgd gapppaiar
//
LOCUS       WP_175909918             424 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia metallica].
ACCESSION   WP_175909918
VERSION     WP_175909918.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..424
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41672
     Region          5..>328
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msshadspat hhagsltifq gaalyigavl gtgvialpal aaevagpasl lawaalvvls
       61 gplaatfaal garypdaggv styarrafgp naaaivgwcf yfavpagapa aamfggayva
      121 avtgggqttv ivtaaaliat vsaanafgvt vsgrmqlvls allvtlllaa vlasaphart
      181 anlhpfaphg wlavgqaaal lvwsfagwea ithlaaefrr pahdmprsag iavvvvgfly
      241 lsvaaasvtv lgpsagasga plaeliaggi gghaqvlaaa aallltlgtm nayfagaakl
      301 gaalgrdgal pawlaqgsqv ggvprrslgv iaalaavala attisdvgpk plvlvtsgcf
      361 vmvyglgaaa alkllprggi ayrcawislv avaglflttg wyilcpllla ggallylqva
      421 aprk
//
LOCUS       WP_175909939             463 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54 dependent transcriptional regulator [Burkholderia
            metallica].
ACCESSION   WP_175909939
VERSION     WP_175909939.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..463
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51185
     Region          <36..130
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <151..454
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mnmpitrdks agaesgngqr pliywtqsps vmlrkelsrr dwkvsivaqa selrdtsgei
       61 tcgildlsgg hadaigsias tcasmrdvvw valvdvgqta spnvrallrd ycfdyvtlpa
      121 shqriadtvg haygmeclfa rdrerlesee kgivgtcsam lrlfdtvrrf artdapvfvf
      181 getgtgkelt avaihrhser rngpfvavnc gaipphllqs elfgyergaf tganarkigy
      241 veaakggtll ldeigdlphe sqasllrflq eraihrlggs gpvpvdvriv sathvdlrda
      301 meegrfrpdl fhrlcvmrid qpplrargkd iellahhmle rfrgdarhrv rgfstdaita
      361 lykhdwpgnv relinrvrra vvmtegrlit aqdleleycl daaspsvadi rksiereaie
      421 tallrtrgrv aasarelgvs ratlyrwmea ygierprgtg ssd
//
LOCUS       WP_175909942             675 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia sp. BCC1640].
ACCESSION   WP_175909942
VERSION     WP_175909942.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 675)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 675)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..675
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=72545
     Region          25..664
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mlfaavahaq adtpasstpt httplapifv tanplgdtel isptvqlsgd altrrqadsl
       61 getldglpgv stttygpmvg rpiirgmdgd rirllqngva aydasslsyd havpqdplsi
      121 erveivrgpa allyggnavg gvvntidnri preaiegvtg aldaryggan smragaaqve
      181 ggngrfafhv dafdretskl ripgyarssq qraidgpdtp qpygnvpnsd grvhggalga
      241 sytwadgfag lsysgyesny gsvaeddvrl rmrqerlala sevrnlsgpf tklkfdfayt
      301 dyrhkevdng atattfrnrg yeariearhr kigpfegaig vqfgqntfsa lgdellvpst
      361 rtnsvalfgl eewqvapalk lslggrfehv kvdpdpagve kfalaqsrdf nagsvsagal
      421 fsltpvwsva anvayterap tfyelysngp hdatgqflig npnaskekav stdlslryas
      481 gpnrgsvgvf ynrfsnylte yntgrivngd gepvapgagd tldeaiyrgv raefygveld
      541 gkwrafsrrg htvdleltad ytharnvdtg qplpriaplr atlaadygyg pfgaraqvth
      601 awsqhrvpdn dfptdgytsl gvmltykfrv gathwlaylr gdnltnqeir yatsvvrgfa
      661 pqggrsvmag lrttf
//
LOCUS       WP_175909988             249 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Burkholderia sp. BCC1640].
ACCESSION   WP_175909988
VERSION     WP_175909988.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26386
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkalvavkrv vdanvkvrvk sdntgvdian vkmsmnpfde iaveeavrlk eagvvaevia
       61 vsvgvtqaqe alrtalaiga drailvesnd sveplavaki lkalvdkeqp qlvilgkqai
      121 dddsnqtgqm laalaglpqa tfaskvtiad gratvarevd ggaetlslql pavvttdlrl
      181 nepryvtlpn imkakkkple tvkpedlrvd vaprlktlkv aeppkraagv kvpdvktlve
      241 klkteakvl
//
LOCUS       WP_175910013             355 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [unclassified
            Burkholderia].
ACCESSION   WP_175910013
VERSION     WP_175910013.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..355
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38544
     Region          1..340
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfvfdedqe aladsvkrll mtemtpelir elwatptgrs dalwslfasq gltavsvpea
       61 hgglglteve wallaqtygy fgspeplldt alvsagvlar lpasdwrdal lrdiaegrar
      121 valvhpvnpy aadvhvaqal lcehrgelhr vdpaqcawra vdsvdpsrrl ftldwepsaa
      181 triasadeaa plldraldhg afavaaqllg ltqrvldvai dysaqrkqfg kaigsyqalk
      241 hlladvairy efarpvvara araiaddhpq ravlvshakl aataaaqlaa rhtmqvhgai
      301 gytweldlqi fmkriwalsg swgdnafhka rvadailgda lpigpaqtfd feeth
//
LOCUS       WP_175910016             356 aa            linear   BCT 11-JAN-2025
DEFINITION  AI-2E family transporter [Burkholderia metallica].
ACCESSION   WP_175910016
VERSION     WP_175910016.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..356
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37924
     Region          18..355
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 msahvpsshe pavrprvqqv sravlyaall vialwvirdf ipaiawacvi aiamwpmlgr
       61 feshrlfrhr ptliaivita gisllvvlpv avaatqavaq vhdlrewlrt iqdngipvpd
      121 vvarlpygaa qitewwqanl ghplhasiam hsvngekfia fgrqfgtkla hallefgfml
      181 vtlfvilrag hklsgallqg arrafgrsga eliermvaav fgtvtglvvv glgegallgi
      241 ayalagvpha allglvtava amlpfcapvv fcgaalwlfv qgatmwaivv avlgfvvvfv
      301 aehfvrpvli ggstrlpfll vlfgilggae tfgliglfvg palmtvltml waewia
//
LOCUS       WP_175910026            1055 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia metallica].
ACCESSION   WP_175910026
VERSION     WP_175910026.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..1055
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112987
     Region          1..1038
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mwivnlalrr pytfivmaim ivlatplalm rtpvdvlpai nipvisviwn ysgfsatemt
       61 nritsvheri ltttvnniqh vestslpgia vvkvflqpga nvqtaiaqtv ssaqaivrqm
      121 pqgatpplvi tysassipvi qlglssktls eqsladialn flrpqlitvp gvqipfpygg
      181 rtrvvaidld pqallakglt padivnavna qnlvlptgta kmgpteyrid tnasadtvad
      241 isnlpvqtvn gattylreva svrdgfapqt nvvrqngqrg vlisilksgd astlkvvsdl
      301 kallpkvipt lpegltvtpl fdqsvfvnaa vqgviheali aavltammil lflgnwrstl
      361 iiaisiplsi ftslialsal getinimtlg glalavgilv ddatvtieni erhlhlgtnl
      421 hdailegage iavpafvstl cicivfvpmf fltgvarflf vplaeavvfa mlasyvlsrt
      481 lvptlamllf rpqqastgpd rstsrfarlh hafnaaferl rawyivllsi llvrrrfyat
      541 cflgfcvlst glvfvlgrdf fpnadsgnir lhmraptgyr ieetarladq verviretvp
      601 sdelgaivdn lglpvsginl sysnagtigt ldgellialk pghratghyv halrtvlper
      661 fpgvefffqp sdiitqilnf gqpaaidvqv lgndlasnmt iasslmkkfr ripgavdvhv
      721 lqrndeptll admdrtrmqq lnlsaqnvaq nmlislsgss qttpsfwinp rtgvqyplqi
      781 qtpqytlssv ddllgtpisa ngrtgmplql lgnlvqvrnt anpavithyn irpaidvyvs
      841 vegrdlgava geidrivsda ratlprgtel tmrgqietmr tsyiglgagv amaivlvyll
      901 ivvnfqswld pliiisampa alagivwmlf itgthlsvpa ltgaimtvgv atansilvvs
      961 farqrlqaga ppltaaleag atrirpvlmt alamiigmvp malglgegae qnaplgravi
     1021 ggllfatvst llfvplvfgg vharlarrra rlagh
//
LOCUS       WP_175910030             550 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia metallica].
ACCESSION   WP_175910030
VERSION     WP_175910030.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..550
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=55905
     Region          15..270
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
     Region          299..547
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mqnhevsadd appkaqrgiq svevggrlld alarrrkplg lselaaaadl staqahtylv
       61 slmrlalvkr daitgnyepg plslrlglms ierqpayraa lphaarlaet vglsvalsvp
      121 gvlgptivri ehggyplhvn lhvgsvmsld ttatgrvfra fgapaqldam aasqagagas
      181 lagaeqpapd agvppadlda irargiergv dlpspgvsam cvpvfdaqgt lqlaltvigs
      241 tgsidvdwdg piaaalrdaa rqataslgaa qdaappsasg papaaarvpp aladdaktqr
      301 ginaldstge lllalvsagr alplrdlaaa agmpaakafp hlvslqkigl lsrddagcfg
      361 ggplgqalgl iamqrvsptr dadaeivala aatdmsvaaa tlgplgptvi rleesarpqh
      421 vslqvgtvms lvntaigrif aagmsddvla dlladepvrl agrtaapadd afrrrlaair
      481 adgvdfafda pvpgigtvaa pvfdhtgsir lviaiigssr gfprgpdsdl aqallaatrr
      541 lswrfgwiga
//
LOCUS       WP_175910068             210 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Burkholderia].
ACCESSION   WP_175910068
VERSION     WP_175910068.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22036
     Region          4..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mpalptliaf glvslgmvlt pgpnmiylis rsicqgrrag lvslggvalg fvfymfcaaf
       61 gitalvltvp yaydalrfsg alylsylawq alkpggrsaf qvrqlphdsg arlftmgfvt
      121 nlanpkiamm ylsllpqfis pghgsvlaqs lalgcvqiav svsvnalias magaiaafla
      181 grpvwarvqr wlmgtvlagl avrialesrg
//
LOCUS       WP_175910075             472 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia metallica].
ACCESSION   WP_175910075
VERSION     WP_175910075.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..472
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50855
     Region          9..463
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mtaavhgcqe tdlkqpedql hrgleerhin lmalgatigv glflgsatai rvagpaillt
       61 yllggiaifl imralgemai anpvagafsr yardylgpla gyltgwtywf vwivtcmaei
      121 tavgvymhmw fpgvpnwiwa laalmamgsv nfiavklyge fefwfaliki vtivlmiigg
      181 glmiafgign ggiaigisnl wahggfmpng ihgvvaalpi vmfaylgvem lgltagearn
      241 peksltkavn svfwrvlify igalfvimsl ypwdqigtqg spfvmtfsrl gipaaagiin
      301 fvvltaalss cnsglfstar mlynlaqqgh apstlgkvnr ngvpvygviv svallligvl
      361 lnylapqhvf twltsvstfg aiwtwcvili aqmrfrrtls aeriarlpir vpfyplgsfv
      421 alaflalvvv lmaftpdtrv alvigpvwiv llgiayalfy anrpaasvpt ks
//
LOCUS       WP_175910108             312 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia metallica].
ACCESSION   WP_175910108
VERSION     WP_175910108.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..312
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32305
     Region          78..282
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mpldpqaqal ltafaqapai dfaqltvpay raslaaggaf aagdavaaee dwqipasgrr
       61 laarlyrpaa dgplpltvff hgggfvscgi dshanlcrsl aarartlvls vdyrlapear
      121 fpaaahdacd avrwaaasar dlgaragava vagdsaggnl aavaalqlrg sgiaivhqll
      181 lypvvdcate hpsyetlgsg yfltaemmrw fkhhyfddga drasplaspl aapdvagaap
      241 ativsaefdp lrdeaeayal rlaqagtpvt lvrwpgqlhg fasmlgaida adrvlsfgad
      301 alrrafdate ar
//
LOCUS       WP_175910110             360 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia metallica].
ACCESSION   WP_175910110
VERSION     WP_175910110.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..360
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38396
     Region          6..341
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(25,27,58,100,228,295,315,317..319)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(25,27,58,100,102,109,176,179,181,228,235,295,315,
                     317..318)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(27,102,176,179,181,318)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            181
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 msekslfepy alggltltnr ivmapltrnr agaglvpsel aatyyaqras agliiteatq
       61 vsaqaqgyqd tpglytpeqv agwrkvtdav hakggrifvq lwhvgrisht dlqpggtapv
      121 apsairaetk tfvnngfadv sepralelae lpgivndfrq aaanaiaagf dgveihgang
      181 ylleqfikdg anhrtddygg sienrarlll evvaavvkei gaertgvris pvspangisc
      241 sdpqaqydyv aeqlsaqgiv ylhvvegatg gprdvaafdy dalrrrfrqt ylanngydle
      301 fattqlkegr adlfafgrpf ignpdlverl khgapltqfn patlygggav gyidyptisg
//
LOCUS       WP_175910166             305 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175910166
VERSION     WP_175910166.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33221
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..290
                     /region_name="PBP2_CrgA_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08475"
                     /db_xref="CDD:176164"
     Site            order(103,107,146,161,163,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176164"
     Site            order(104..105,109..110,112..113,116,120,122..128,190,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176164"
ORIGIN      
        1 mgnnlngiav fvaaaeadnf aqaaetlhit rsavgksiar learlgvvlf qrttrsqslt
       61 negalfyeyc lraveeihag eallesgkwq mkgrlrvsmp alfghlcvap iliglarehp
      121 eldldlsfsd rtidlveerv dlavrvgalp dssglvaral gehkmafcas paylercgep
      181 atvdalaqhk alaythygqv hrwqvvvdgr teelqpaarl lsddlravld aavaglgvaw
      241 lpywlvrdei rrgalrella drpgvtygih avwphrshlp lkvraavdal vnqlparlae
      301 veara
//
LOCUS       WP_175910227             156 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia metallica].
ACCESSION   WP_175910227
VERSION     WP_175910227.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..156
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15934
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 myarifaald gsrssrlald eaialvrnsg glivavcvvs daprltvvds gyidrrdpag
       61 ldadkaaiav adaetafrlc gvrgtahtid acgedvssvl araaaecdad livmgthgrc
      121 gvrravlgsv aeslvrsadr pvlivregrg acaavl
//
LOCUS       WP_175910233             248 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Burkholderia].
ACCESSION   WP_175910233
VERSION     WP_175910233.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..248
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=26951
     Region          3..231
                     /region_name="ArtM"
                     /note="ABC-type arginine/histidine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4160"
                     /db_xref="CDD:443325"
ORIGIN      
        1 msidfdflfd tlrqllaavp ttlglffasl vlggllslvi vtmrvsphwl pnrfargyil
       61 vfrgsplliq mflvyyglgq fgviresfmw pllrepyvca vlslalctag ytaeilrggl
      121 mavpvgqiea gysiglsgfa llrrvigpia lrqclpayst eavllvksta laslvtvwev
      181 tgvaqqiiqq tyrttevfac aaviyltlnf ivvrllgale wrlsghlrap kpsgasvaat
      241 rnprrvas
//
LOCUS       WP_175910235             240 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia].
ACCESSION   WP_175910235
VERSION     WP_175910235.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..240
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=25295
     Region          1..235
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 mailemlgfg tegwggvlll aalmtvaltl aalavgavig aaiaaaklsr hrsarllgdl
       61 yttvfrgvpe llviylfyfg gstlvtavgq wfgaegfigv ppfvigalav gmisgayqae
      121 vyraavlavs kgeleaarai gmpssmvlrr ilipqvlrfa lpgignvwql slkdsalisv
      181 tglaellrts qiaansthqy fvffvaggal yllmtglsnr vfnraeaivg rsfrrnfarn
//
LOCUS       WP_175910236             156 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia metallica].
ACCESSION   WP_175910236
VERSION     WP_175910236.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..156
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16493
     Region          1..144
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mytnimvavd gspssqrald eglklarshg arlfavfvvd ksliitfggr mdpdallaei
       61 rrdgasvlrq aertiahaav ngetelvdte lgesvaerlq ryvaersidl avvgthgrrg
      121 vrrlllgsva erflrgsscp vllvrgsdaa paaaaa
//
LOCUS       WP_175910239             445 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1640].
ACCESSION   WP_175910239
VERSION     WP_175910239.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..445
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48171
     Region          21..421
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(33..34,37..38,41,73,123..124,126..128,131,151,
                     154..155,158,255,258..259,262..264,267,296,300,350..351,
                     355,359,375,378..379,382..383,386)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnhdpqqsqh latavrkaai rllpfltlmy alafidranv gfaklayqad tglsdaafaf
       61 gagiffigya lfevpsnlim nrigarvwms rimvtwglvs asmmfahtpt qfytirfllg
      121 aaeagffpgi ilyltywfpa kgraralglf yfgvpiamli gnplsgfllq mhdmfglrnw
      181 qwmylveglm atvvgviaff yltsrpkdar wltddekral cdtldaeera ksrhlsatvf
      241 gvlkdrcvlt fiaayfciqi gnaplafylp skfaatmctq idgkiglllm ipwlctiaam
      301 ivatrfadrh dnhlqvatgm ltvgilafas isvintpvla llafciaipg lvacqpvfwc
      361 lptrylggtg aasgiafivs ignlggfvsp qikafadaas hdsrtgfvvv aalcfvsvll
      421 lrslrgmgha gaesapggar agshr
//
LOCUS       WP_175910240             244 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia metallica].
ACCESSION   WP_175910240
VERSION     WP_175910240.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..244
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25593
     Region          127..235
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 mtavfvlhra dgtssstafr kqafgerdpf aqhreiaweg pdamaagrig fvgeldvasf
       61 phietivvve geltleaaga aplvlgprqg avigggtalr ivaqspvqlm fcaaacatpt
      121 krgvaalhed adfkpsatlp aevllgpapq crsdnvfvdd gaaycagtwd stpyhrivrp
      181 hrvnefmfll dggvrfaapd gsvlslgagd alfvprgasi gwesgervak fyvvqtvnas
      241 terd
//
LOCUS       WP_175910268             958 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia metallica].
ACCESSION   WP_175910268
VERSION     WP_175910268.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 958)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..958
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..958
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=104099
     Region          42..957
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mknhglsrrg flkasvlagv avyvaplgsr afaalfeekl ltpvkwdsvt gipqfridgi
       61 akvtgskvfa rdvraadmph wpqqqshali lrvtqadrty egfdlsllgd elkpdrvvta
      121 ddlardgvaf ptfygddmll pagktpaylg havailiyhd farfrfakna lkfrddviry
      181 gavtgplerd pwgtfryvrv ggktaydddv ysslkdapif psmmrkhlpv wpdgkehgkl
      241 deqgmflagq ianeldhpsa dwlvfdreyn tqsvdtaale pdnancwydt atqslhlvvp
      301 tqsplevaen aaamvaktrf pvkklfvhpc ytvgygskdh fnvpfyglvc alyadgrpvr
      361 fandryeqfq tslkrhafkm hyriavdrnt gllqsfkgdf eangggrsnf spsvamvgat
      421 aaqsiyyfpk sdlaavaias raidagsarg ygtlqsmaat emavdeiaaq lnidpidfrl
      481 rnalrsgmkn tqgaipagal rvdevlerak qhplwthrva rkaeyeaanp gkrygvgfac
      541 vqkdfgtgae asfakvefde ngkvslqhta aeigtgmsts qavavakwlg rpatdvrvav
      601 tewpdlpvet sgdpylmsqa dqdrlsanpr wspgyaspss atnsayyfth streaaravf
      661 ryglwpaams iwtrglgggq aapytiried arwvdgklta dgleplsfeq lakqahalgl
      721 ptgavvhvfn rwqwtdaefe vggtverlpi dglslrvgap ktgdngpvpg taapagatam
      781 hgtlaptang yrvldrkrvf ipptsrnnaa vtyytavgtl velavheatg kvellthhsi
      841 mecgnqispq lvsgqlqggl amgighalhe ylplyedgpg ngtwnfnryq lprasdvavw
      901 tqtgdvlppl setdppkgva evvmipvvga ivngiahaig hrftdlpvtp qkiqevla
//
LOCUS       WP_175910273             241 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [unclassified Burkholderia].
ACCESSION   WP_175910273
VERSION     WP_175910273.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..241
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26485
     Region          1..239
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 misisnvskw ygqfqvladc ttevkkgevv vvcgpsgsgk stliktvngl epfqqgeilv
       61 ndqsvgdrkt nlsklrskvg mvfqhfelfp hlsitenltl aqikvlgrgk ddatekgmkl
      121 ldrvglkaha hkfpgqlsgg qqqrvaiara lsmdpiamlf deptsaldpe minevldvmv
      181 elaqegmtmm vvthemgfak kvahrvifmd kgaiveddrk ddffsnpksd rakdflakil
      241 h
//
LOCUS       WP_175910265             307 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC1640].
ACCESSION   WP_175910265
VERSION     WP_175910265.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 307)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 307)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 307)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..307
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32277
     Region          56..304
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 maslssprdt apaaapadag snaghalpgv ppwlllapil aflavlaaat ltvlrmsvgv
       61 sgdewrtftl qnyidladpy fatsmwltlr lafqsmvcav llaipvalam artesrlarr
      121 lmlagvllpl lvnlllqgyg wlvmlgpagl inrallaagv ldrplqllyr ehgvllgliq
      181 tafplavlpl ssalravsra ydeaaatlga srwqtlrhvt lplampglvs gallvfayna
      241 safavplllg grrvpmlavl vhdqvaplln wpaasasgvv lmaatlvvma vsqrlvrtlq
      301 hagevnr
//
LOCUS       WP_175910278             402 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [unclassified
            Burkholderia].
ACCESSION   WP_175910278
VERSION     WP_175910278.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..402
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=42530
     Region          4..355
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 msqkilivga gfagvwgalg aarvldgagv tsgdveitli spkpelqirp rlyesepqrm
       61 aapllpllda vgvrflegsv eeisvrektv svacgngqrr llaydrlllt sgsrlskppv
      121 pglaehafsv driedavald ehfaalaklp esparntvav vgcgftgiev atelpkrlre
      181 wfgpqttgrv vvigaqddig pdlgpnprpy vaeafaslgv eavlgsrvvs vaadgvrtas
      241 gthieamtvi waggmqaspl tsqvsshldp lgrvevapdl rvaeaphvfv agdvararsd
      301 deghyalmsc qhaivmgqfg ghnvaadlig vptleyrqpf yatcvdlgdw gavysegwdr
      361 qikltraegk arkqmintqw iyppapnrae alaagnpqas ld
//
LOCUS       WP_175910326             305 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175910326
VERSION     WP_175910326.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33323
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrlrafevf vtvvsrggfa raadalgtsp anvtryvhel eahlgtrlmn rtsrtlslte
       61 ggetlyarck tilddvaete glvssasvep rgrlrinapv sfgilylapl wpgfmqkypq
      121 ieldiglidr vvdivdegyd lairisrags ishaarklat sqnilcaspd ylarfghptv
      181 pedlirhrci gytyaatgde welidgggrt hgvrsnfhmh tnngdtaraa alagqgviwq
      241 ptfligndlr agklvqvlpg yrlpdidvla vypsrrhlsa rvrvmidfla dafggvppwd
      301 redgs
//
LOCUS       WP_175910394             120 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Burkholderia metallica].
ACCESSION   WP_175910394
VERSION     WP_175910394.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..120
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=12368
     Region          48..119
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 msnrsmlvvs aatfaafals gvahaeapyv qasevtrctr idsrdvpyps sarragqsge
       61 vtvggvvlpd gtvsdvtlle ssghaeldav vtaaftrihc sadggaqpir mkqkvtfslm
//
LOCUS       WP_175910405             282 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia metallica].
ACCESSION   WP_175910405
VERSION     WP_175910405.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..282
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28670
     Region          21..261
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mmsinptegv lvsslqglra fdlagiaial flggmakgit gigvpliamp ilsqflpirh
       61 avlllsmpii lgnipqaleg gqvlatarki aapiagtvig nivgvailla lnpghaqaas
      121 gallivaatl mlaapklnlp dawrqpvgfv lgfgaalmes iasvpgplla tylissgatg
      181 rvftkqiaii lvvsivtlit tfsgaahasg adlaisaaas lpaiagmwlv rplrdkmspr
      241 ifrivvllfv lvaasqmiwk sgvfrhggsh avqtgtahtg nn
//
LOCUS       WP_175910412             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia metallica].
ACCESSION   WP_175910412
VERSION     WP_175910412.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46406
     Region          5..412
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(19..20,23..24,27,59,109..110,112..114,117,137,
                     140..141,144,235,238..239,242..244,247,275,279,336..337,
                     341,345,362,365..366,369..370,373)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mprirwamil mcflanvinf idranlaiaa psiradlgld avgmglvlsa ffwtyaflql
       61 pagwfidkvg vrvslalavg wwsvftvatg aarglaqlvg vrlmlgvgea aaipsfakva
      121 fnwfprserg lassifdsgs rvgsalslpl vawlisivgw rgsfaitggi givwalawwf
      181 vyrdperyra iapdavdall aqrgapivaa atdgpkvswl dlfryrtvwg mmiglfclnf
      241 aiyffitwfp syllqsrgfs laslgtwgml pallaipggw lggyvsdslf rrgwsataar
      301 ktclvlgmll sssialsafv envwaclglf alayaslsfa ganvwtlvge vaptpahvas
      361 lggiqnfagn lagifittft gvmlsitkgs fvvplavaga lcvvgalsyl fvvgkveplp
      421 plrgranrqn vepsaa
//
LOCUS       WP_175910426             448 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175910426
VERSION     WP_175910426.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..448
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48261
     Region          27..437
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(40..41,44..45,48,80,139..140,142..144,147,167,
                     170..171,174,268,271..272,275..277,280,308,312,363..364,
                     368,372,388,391..392,395..396,399)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mpsltqtaaa paavgsseda lyrkvmrril pllllcyvva yldrvnvgfa klqmlddlsl
       61 sdsvyalgas vffwgyflfe mpsnlllhry garfwiarim itwgivsssm afivplaqff
      121 hvqtstmfyt lrfllglcea gffpgvilym nywfparrqs vamsgflvai plsltlgsvi
      181 sgwlmeqthg lsgmsgwqwm llleglpsiv vafivlaclg dgpqsakwls aeekavlsrn
      241 leseaahksh gvgaalrspr vwlltfillt fntgfyglaf wlpsiirasg vrspmhigll
      301 tavpyltaif amvwnaahsr ktgerrlhaa ipaliggvgl itsaacaqnv vlsilfltia
      361 tcgilalmpi ywtfpgqils gtaaaagial insvgnlsgf tgsmitgiak emtgninngt
      421 yalgacllvs cvlimliprg vlfppaak
//
LOCUS       WP_175910434             232 aa            linear   BCT 11-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Burkholderia
            metallica].
ACCESSION   WP_175910434
VERSION     WP_175910434.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..232
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24691
     Region          27..229
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 msayvidaae rpsvevdqss arfplhrvfc vgrnyadhar emgadpdrep pfffmkpada
       61 ivpargtapy ppltndlhhe ielvvaigkd grsidpadal shvwgygvgv dltrrdlqae
      121 akklsrpwdw akgfdasgpv talrpasatg hpatgriwla vngeprqqgd ladmiwavpd
      181 viayvsrsve lkagdliftg tpagvgalqp gdrvtggvdg vatfefvvga kp
//
LOCUS       WP_175910439             286 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [unclassified
            Burkholderia].
ACCESSION   WP_175910439
VERSION     WP_175910439.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15202679
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..286
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30430
     Region          12..132
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          168..273
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 madlnssstl tyrpfaetdl paahrlseav kwphrlddwr fafqlgsgfv aedeagivgt
       61 algwrfgesh aslgmvivsp erqgrgigre llarvvdslg artiflhatp sgeplyvkfg
      121 feaigtidqh qgaafqppli slppgerlrp lgtndgprla alasraagyp rdavidalld
      181 vangialdrd gellgfalfr rfgrghvigp vvapdalraq alishwlalh egmfvrldvp
      241 gdsglsdwlq glglprvdtv vamargaapa rdpslrafai vnqalg
//
LOCUS       WP_175910507             676 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia metallica].
ACCESSION   WP_175910507
VERSION     WP_175910507.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..676
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=70229
     Region          30..590
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mkfalpslpp laavrtalrd twpalppgav gfalrntaas llalyiafrm nlddpkwaas
       61 tvwivaqgsr gmglsksqyr ilgtaigavv alvltgafaq tpelflpala awiglcagva
      121 tflrnfraya avlagytaai iamdavaapl hafdiatarf lyvvvgilcg aafetvfapg
      181 spladvrtrl aryldravav gagalrrepn gaavhrlfve alaldtaaey aaagepsvrn
      241 aighlraavl gvlsaqaagq alhehaarsg gtpdpliadt aqvldgvaar gdagaalaal
      301 rarvddamra eaaepagsdp srlltldrla alvagfdaay agqvqlarpn ppasrvryaf
      361 hrdpvlawhn glrafvavli aaalwivtaw psgagfvait gvvcalfstr pnsvgatlgf
      421 lkgagcaavv galcnfvllp avsgfemlat ilgvfmigtg iamrnprtag igsgfsiffw
      481 nftspdntar igdaaflnsa latllgiafg alvfalvfpg dagtsrrrlh ravrddlari
      541 arnprawqas awlsrtadri grelgfagrl paalierdvr dllaawtigd sllalaalat
      601 repaarrava vvrgrighad farlaragha aarvllrrvt evdsddgral lrgavllrti
      661 adtaaahdgf lsgrdd
//
LOCUS       WP_175910564             144 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia metallica].
ACCESSION   WP_175910564
VERSION     WP_175910564.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..144
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15734
     Region          1..143
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mlkllvpvgh sprslqairh atflyrerca seivlinvqv plestrleay hplsrlrsie
       61 ekfasddlam aerilqeagv kysvvmkvgp vadtiasvaa etgcdeivvv aprhgplhal
      121 lsvfrrsvms rlvrisnvpv tavq
//
LOCUS       WP_175910573             396 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase [unclassified
            Burkholderia].
ACCESSION   WP_175910573
VERSION     WP_175910573.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..396
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=42082
     Region          18..381
                     /region_name="MidA"
                     /note="SAM-dependent methyltransferase, MidA family
                     [General function prediction only]; COG1565"
                     /db_xref="CDD:441173"
ORIGIN      
        1 mnpkahepas lpapgpdala qsetlaaqlr deiaaaggwl pfdrfmeral yapglgyysg
       61 garkfgrrad dgsdfvtape lsplfaqtla npvgqalaas gtrrvmefga gtgklaagll
      121 daldalgvel deylivdlsg elrerqrdti aavapalagk vrwldalper fdgvvvgnev
      181 ldampvrlfa kaggawlerg valdarhafv fddrpagaag lppvlatldv ddgyvtethe
      241 aalaftrtvc tmlgrgavll vdygfpahey yhpqrdrgtl mchyrhhahd daflypglqd
      301 itahveftgi ydagvatgad llgytsqarf llnagitdal aaidpsdihq flpaanavqk
      361 liseaemgel fkviafsrgi dgtldafarg drshal
//
LOCUS       WP_175910640             531 aa            linear   BCT 11-JAN-2025
DEFINITION  MDR family MFS transporter [Burkholderia sp. BCC1640].
ACCESSION   WP_175910640
VERSION     WP_175910640.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..531
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56749
     Region          33..425
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(34..35,38..39,42,73,123..124,126..128,131,152,
                     155..156,159,285,288..289,292..294,297,325,329,382..383,
                     387,391,407,410..411,414..415,418)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mavhtaahhs sgqvlpfres llamigisfv tmlvaldqtv vgtalptiva elkgfdlyaw
       61 vatsyllssv itvpifgrlg dyygrkpfvi vsivvftgas vlcgmandml flvlarglqg
      121 igggmlvgta facipdlfpd svvrlrwqvl mssafgiana vgpslggilt qsfgwrsvfy
      181 vnlpvgllsl ffvwrylphl rhvehdrkmr ldwpgallia lslgalqlfv ewlpkygvms
      241 waslllivav gagvglwhwe krcaqpilpf dmfgnralsa lfvlailagf smfsllfyap
      301 llfqggfgms pkeaglvitp lvvfitigsi mngrvvtrir npntmlhvgf vlfaiacagi
      361 vvsthttptw vlmalmvagg iglgfvlpnl tvfaqqtagr ehlgiatall qslrmvggmi
      421 gtaltgtlvn qmyssgvrda lsgdhalqwh aqladpqili draaqgglva eltraghnga
      481 llleaaresl vgaihlgvam aalvavvsvw qcrrvppial rhkiephvaa d
//
LOCUS       WP_175910671             302 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: M48 family metallopeptidase [Burkholderia].
ACCESSION   WP_175910671
VERSION     WP_175910671.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..302
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=33472
     Region          64..299
                     /region_name="YgjP"
                     /note="UTP pyrophosphatase, metal-dependent hydrolase
                     family [General function prediction only]; COG1451"
                     /db_xref="CDD:441060"
ORIGIN      
        1 mkkrprprpa vvaldhrqmd lplfdgptas papsapaapp sppeaatapa vptapldpgp
       61 apdrsrvrtf aldsrvleyr lkrsarrtig ftidgsglsi taprwvtlad ieaaiaekqr
      121 wifaklaewk trteqralpq idwrdgaqlp ylgktitial gagavafdad aqrlslplpa
      181 qadmqqikdr vqgwlqgeak rifgerlvvy aemlgvtysm yalssaatrw gscssdgkir
      241 lnwrlihfpm siidyvvahe lshlremnhs pafwqtvesi fpefrearht lkhhppellp
      301 sl
//
LOCUS       WP_175910684             481 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia sp. BCC1640].
ACCESSION   WP_175910684
VERSION     WP_175910684.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..481
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51505
     Region          1..392
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfeslglae plvkavnelg ytsptpiqqq aipavlgggd llagaqtgtg ktagftlpil
       61 qrlhtfyaeh rgakravral iltptrelaa qveesvrays kylklrstvm fggvsinpqi
      121 dalkrgvdiv vatpgrlldh mqqktidlsd ldilvldead rmldmgfihd ikrvlaklpp
      181 qrqnllfsat fsdeikslad slldspalie varrnttaes vaqkihpvdr drkrellthl
      241 irehnwfqvl vftrtkhgan rlaeqltkdg isamaihgnk sqsartrala efknstlqvl
      301 vatdiaargi didqlphvvn fdlpnvpedy vhrigrtgra gatgeavslv cvdekqllrd
      361 ierlikreip qeviagfepd pnakpepiqq rrgqpprggn gggggnrqpr aggagqpaak
      421 rdgnaqpkaa kaakprtagg asgnaggggg rpsggngarp angnaahanr nrssrsgqrg
      481 h
//
LOCUS       WP_175910697             322 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175910697
VERSION     WP_175910697.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..322
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34940
     Region          6..320
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 msaaprsiiv lafpraqlld vtgplqvfas vnelaqergq pvpyaprvva aeagpietss
       61 glvvmadslr sagrpdtviv aggkgvhaas rdartvrwvr qqaqrarrva svctgaflla
      121 eaglldgrra vthwarcdef aarypnvrve pdpifirega lwtsagvtag idlalalvee
      181 dlgraialda arelvvflkr pggqaqfsam lsmqrtddrf gelhawiaeh ltadlsvpal
      241 aervsmsers fvrhyragtg rtparaveqi rveaaqrllg etawpvkria trcgfgseet
      301 lrrsfvrvlg vspqgyrerf vr
//
LOCUS       WP_175910721             393 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA-binding protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175910721
VERSION     WP_175910721.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13774834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..393
                     /product="DNA-binding protein"
                     /calculated_mol_wt=43715
     Region          25..143
                     /region_name="KfrA_N"
                     /note="Plasmid replication region DNA-binding N-term;
                     pfam11740"
                     /db_xref="CDD:432038"
     Region          <86..>309
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
ORIGIN      
        1 mtldemrevi reeleslras garrqelslh ackrlffdlg irpsaanvrd ltqtgsasdi
       61 pkdidhfwer irsaskirld gaaipkavee kagallgaly eealkaares ldvdreqvra
      121 gltdaeqrlr datvrqetle galtrsetrn eqlqarvtel evqlasqsth gsaneatllt
      181 tvarlekela vmagrvdteq tqnatlrdri dtlqaelqqr tehyaqqikd avaeaerrvk
      241 pmlveldslr smastyqsgl rdvqrkefdf lqqlssakar adrleeqlrt qsdeldratr
      301 dantlrasrg mnpeisalir rladagqlda dafsaigtsl dreipvptqc phcdgepels
      361 hgddgfevsc pecehasgpw psrfeaiarf ard
//
LOCUS       WP_175910772             430 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia metallica].
ACCESSION   WP_175910772
VERSION     WP_175910772.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..430
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=47143
     Region          4..412
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mttptriviv gggiaglqla trlgerlgrs graqvtvvdr spthiwkpml htiaagtrdv
       61 qqqqviflah ardhgytyqp gelkgldrar rrvqlgeirs qdgelvlear eleydvlila
      121 lgsqandfgv pgvrehcyfi dsqqqaetfn ealrmrvfrs iardepfrva ivgagatgve
      181 laaelsrlle vaqaygdetv rerlqltlle sgprilaafp prisasaqrr leqigfhvlt
      241 strvtsadan gfhygdgsfa eadlmvwaag vkapdfmqal dgldtnranq ivvgptlqat
      301 gdehvfaigd casllpdghe rplpptaqva tqqaehlakh lpawldgqpi ppfafhdfga
      361 lvsisdydaf gtlgqfgffr ggfiqgrfaq fshlmlyrrh qqalhgfska tllwiaerin
      421 gcvqprirls
//
LOCUS       WP_175910782             158 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [unclassified Burkholderia].
ACCESSION   WP_175910782
VERSION     WP_175910782.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..158
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=17265
     Region          5..153
                     /region_name="OsmC"
                     /note="Organic hydroperoxide reductase OsmC/OhrA [Defense
                     mechanisms]; COG1764"
                     /db_xref="CDD:441370"
ORIGIN      
        1 mahgehkyrv avewtgnrgt gtsgyreygr dhviragskp dipgssdpaf rgdaarwnpe
       61 dlllasvsac hklwylhlcs dagirvlayv ddaeatmlds pepgsfteiv lhprvtilag
      121 ddrelaerlh hdahakcyva nsvnfpirce pviefaaa
//
LOCUS       WP_175910816             477 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            metallica].
ACCESSION   WP_175910816
VERSION     WP_175910816.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..477
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=52951
     Region          25..191
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
     Region          278..470
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mqnsaikeet pdhsegaksa arpssrrnre qrireiidta rqvfqedgya gfairrvadr
       61 mgithgnlqy yfrtteellr talpaylsqv medykaiasr pgmgaaqrcs alinrifqni
      121 netdlpkfmv eiwafashea yvaellrdmq aryrgifekl lselhptlss dacqvraavi
      181 vaqmdgmtif ashgdypgkd yvelirvakr avkmvmsasp qmleseaphr rprvlhdgsn
      241 tpisvfgsng dlqpglldlr ahqstqdafh yrptaqgkrr elkineivst aanllategy
      301 anftlarvar elgilpsvlq nyfpthddll rstldavgra yldhyaelgk psgksalerl
      361 cdiaadvfee vcvpevqqlw iemfalaqhs ditreivgrg yaayrvvctd lireidssat
      421 areclaratl iaalvdgviv lrfgtqnqpv nadrafelmm amtaligqgr iaandas
//
LOCUS       WP_175910842             486 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia metallica].
ACCESSION   WP_175910842
VERSION     WP_175910842.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..486
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50183
     Region          31..475
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,156,
                     159..160,163,293,296..297,300..302,305,333,337,390..391,
                     395,399,415,418..419,422..423,426)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtndtlapcv pagtaaaatp rshhgwalvv llvgailppl dyfivnlalp airdgigarp
       61 aelqlvvsay acanavvqit ggrlgdlygr krmfmigmag fvvastlcgl agsgavlvgg
      121 rvlqglfaai lapqvlatir svfspqeqvr vmgfygfvfg laavigqlgg galislhpfg
      181 lgwraiflvn lpigllalig swrfipesrp prgqridvpg mallslfllm lvypltqgrd
      241 agwplwmvac lvgalpmlga llavearrla rghdplldvr lfrhpvvalg lvlaflfytl
      301 safflsygiy lqgclnwspl asglailplg lgflsspllm prlvgrfggy rvltlgfaml
      361 aagvataaal agaaapgpgf yagiaaigig qglvlpsvvr ivlaevdtar agvasgmvta
      421 mlqigaavga atlgglffar lgahpaaldy vqgfrtsmfa ltavllvcva lsamlgplhr
      481 rlhaga
//
LOCUS       WP_175910857             377 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175910857
VERSION     WP_175910857.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..377
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40197
     Region          1..366
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfsftdeqq qfadalrryl geqygfdarq aivrsdagvs daqwsafael gltalpvpda
       61 qggfgggpvd mlvamqelgr alvvepywat avgiealrva gsgtgddaal leavaqgqkr
      121 lavafhepra rydlyeldth ardhsgtyrl tgtksvvqhg aqahawivpa rvdggsiglf
      181 vverdaagak lvdyrtidgq raatielhdt aarqltggar daaaleqiad yatfllcaea
      241 vgaldelnra tveytktreq fgvpiarfqa lqhrmvdmli haeqarslty laavryaggd
      301 adarrkavsa akarvgaaar fvgqqavqlh ggmgvtneva aahlfkrlsi iettlgdtdh
      361 hlariaalpd faqtdaa
//
LOCUS       WP_175910854             264 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia metallica].
ACCESSION   WP_175910854
VERSION     WP_175910854.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13673959
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..264
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27580
     Region          12..144
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          179..260
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mhrvthyrrt gegieaisle sdrafprhah defgvgvivs gahrswsgrg qvdalagdai
       61 mvnpgemhdg apieagtgrr wrmlylapal vagvaaeegv ggvelahpav rdarlaaavg
      121 rlharivage spplardeal vmlvagllar hanrslpaag vapairiare rldaapaapv
      181 slgeladlsg vsrfqllrgf arelgitpha yliqsrarla rallagglpi adaaaeagfa
      241 dqshltrafa rqfgitpgrf tqav
//
LOCUS       WP_175910862             515 aa            linear   BCT 11-JAN-2025
DEFINITION  FGGY-family carbohydrate kinase [Burkholderia metallica].
ACCESSION   WP_175910862
VERSION     WP_175910862.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..515
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=55132
     Region          3..448
                     /region_name="ASKHA_NBD_FGGY_RrXK-like"
                     /note="nucleotide-binding domain (NBD) of Rhodospirillum
                     rubrum xylulose kinase (RrXK) and similar proteins;
                     cd07804"
                     /db_xref="CDD:466806"
ORIGIN      
        1 mdyvigvdig tqstkallvd rhgtivarrs agyqpdtprp lwaeqwpqvw fdallaciag
       61 cvsdarargv padairavcv gslyggsgip vdsgmrplhp cliwmdrrat aevdwvnanv
      121 nverlrvitg ngvdsyygft kmlwlrgqrp dvwanvryfl ppnayviyll tgevavdhss
      181 agniggvydv arrewsddal dmlgipatmm perlvestdv vggllsqwte qlglpagtpi
      241 vaggvdaava tfaagatrtg qhvamigtsm cwgyvsrhvd arhglvgmph vfngqrdlyv
      301 fggaitagas vawfrdqfcq aeidaarllp hgdphallee aaesvppgad gvlflpylmg
      361 erspvwdaka sgafvglsla htrahlyrav legvafalrh nieagrrgat alddrlivvg
      421 gaahsalwmq iiadvtgfpv wtieqdveaa mgaallagvg aglvshddaq rgwvtlvera
      481 rpdaerakay aarfalytal ypalqpimhg lhtps
//
LOCUS       WP_175910872             213 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: carbonic anhydrase [Burkholderia].
ACCESSION   WP_175910872
VERSION     WP_175910872.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Lindskog,S.
  TITLE     Structure and mechanism of carbonic anhydrase
  JOURNAL   Pharmacol Ther 74 (1), 1-20 (1997)
   PUBMED   9336012
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10096752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..213
                     /product="carbonic anhydrase"
                     /EC_number="4.2.1.1"
                     /GO_function="GO:0004089 - carbonate dehydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23116
     Region          11..190
                     /region_name="beta_CA_cladeA"
                     /note="Carbonic anhydrases (CA) are zinc-containing
                     enzymes that catalyze the reversible hydration of carbon
                     dioxide in a two-step mechanism in which the nucleophilic
                     attack of a zinc-bound hydroxide ion on carbon dioxide is
                     followed by the regeneration of an...; cd00883"
                     /db_xref="CDD:238448"
     Site            order(33,35,42,44..46,58,61,83,88,98,101,180)
                     /site_type="active"
                     /note="active site clefts [active]"
                     /db_xref="CDD:238448"
     Site            order(42,44,98,101)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238448"
     Site            order(43..46,48,50..51,53,58..60,62,64,78..79,82..83,121,
                     180,182..183,185,187)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238448"
ORIGIN      
        1 mnrpksmlva niawarethe htpgffdala rgqnprvlwi gcadsrvpae tithcvpgel
       61 fvhrnianlf hpdddnsasv leyavrvlev dhvivcghyg cggvrasllp ppadlphvar
      121 riaplcalar rhrdtldgld dtaaadrlae lnvleqvrll raspivhgrq rpplvhgwif
      181 sltdgrlkel dsgytappae aepehaamaa alg
//
LOCUS       WP_175910873             319 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia metallica].
ACCESSION   WP_175910873
VERSION     WP_175910873.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18598969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..319
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35434
     Region          1..283
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          15..97
                     /region_name="cupin_MtlR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to MtlR, N-terminal cupin domain; cd06976"
                     /db_xref="CDD:380381"
ORIGIN      
        1 mmhpdlevvd vrrdesfkvw shgypyrtir whfhpefelh livatrgkyf vgdhigsfgp
       61 ghlvllgpnl phnwvsdmae getverrnlv iqfdpafvrr cmdafpecrd aqsllddarr
      121 gvgfdaatsa aiaplfdell targmrrial fmtilerlcg aaertllasp aydqadvtpt
      181 rlshalsyig knlasdlres elaqltgqsv safsrafhrh tgmpfvqyvn rlriesacqm
      241 lladdasitd icfqagfnnv snfnrqfral kgmapsefra lqrlnarsrd lalhaaptgn
      301 plpprvvtpg vpalapqpg
//
LOCUS       WP_175910955             144 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [unclassified Burkholderia].
ACCESSION   WP_175910955
VERSION     WP_175910955.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 144)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..144
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15982
     Region          13..126
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04667"
                     /db_xref="CDD:467552"
ORIGIN      
        1 mntgpdtvas ikerativcr qrssvllvar taarwslpgg tirrgetple aaqrelaeet
       61 rleglaldya vqfggltklh hvfvadvpkh ltprasneia rckwfdverl etlrasvptr
      121 kiiellhldr fpahahadgp frsr
//
LOCUS       WP_175911049             748 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia metallica].
ACCESSION   WP_175911049
VERSION     WP_175911049.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 748)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..748
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..748
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=80594
     Region          <42..>196
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          204..747
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mrddhafnap qvdetarrrf lkqgsallaa giavgfrmpd amaagmhasg dpqpaagefe
       61 pnawvrvlpd dtiklvvhkh dsgtgtrtal aavvaeeldv dpfkvdvitp edpffaeyih
      121 plwkvfstgg stsvameydr lrragatara mlveaaahrw rvpaaactta dgavlhaasg
      181 rratygalas aaaqlpapdk valkdpaqfr yigklrrkrg aaqkadgsfp ysidvslpgm
      241 lvavvtrapv idgrvrsvda kaalaipgvr dvlqipprpd vlggnqagva vladdywsah
      301 rgqaaltiew edslfetfds smlaarqaaw vddpaarvvp tiadgdpaka naagartida
      361 sysmphkaan plepvnltvw ahnggieywg glqvpstaie aadviggipa hrvtlhelvs
      421 ggsfgaresk ywlfeatwla vktgkpvklm nsredemral fyhaasyhra ravldahgnl
      481 aslwlravmp aspqqwepgy lertdrmdfs ttealtkwef ayaaphrdig wirmetgvpt
      541 gwyravsyip nvfavesvmd eaahaaqrdp vefrlahmrd rprhaavlre aaqragwgqp
      601 lpdgvalgva tnqaydsyva vvarvvrkdg avkvekltcv adcgiavspa gvdeqlyggl
      661 mwglghatsd ridfrhgrvq qsnfdtyrvm rmsdmpdtdi hivqgdpakp ggvgelsspa
      721 vtpaianavf rltgkrlret pfdlsala
//
LOCUS       WP_175911023             220 aa            linear   BCT 11-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175911023
VERSION     WP_175911023.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..220
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=24425
     Region          122..>216
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
ORIGIN      
        1 mhrtvtqaai ntlsmhalnt lheqvekfre waalypvhqr sveweceygh wealwdasla
       61 vvdslapaaw tatacadlly aiardqaleh issmlwtqpd allalarasi dasepnakwq
      121 laarlgglgs haaeaealll rlvddedeyv rrrallalga lksthaeala erawhtghey
      181 qriaalwvlk niqsgklvqy vklaeadgre yvvrnardvs
//
LOCUS       WP_175911101             166 aa            linear   BCT 11-JAN-2025
DEFINITION  CinA family protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175911101
VERSION     WP_175911101.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Galeazzi,L., Bocci,P., Amici,A., Brunetti,L., Ruggieri,S.,
            Romine,M., Reed,S., Osterman,A.L., Rodionov,D.A., Sorci,L. and
            Raffaelli,N.
  TITLE     Identification of nicotinamide mononucleotide deamidase of the
            bacterial pyridine nucleotide cycle reveals a novel broadly
            conserved amidohydrolase family
  JOURNAL   J Biol Chem 286 (46), 40365-40375 (2011)
   PUBMED   21953451
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Martin,B., Garcia,P., Castanie,M.P. and Claverys,J.P.
  TITLE     The recA gene of Streptococcus pneumoniae is part of a
            competence-induced operon and controls lysogenic induction
  JOURNAL   Mol Microbiol 15 (2), 367-379 (1995)
   PUBMED   7538190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..166
                     /product="CinA family protein"
                     /calculated_mol_wt=17598
     Region          10..160
                     /region_name="PncC"
                     /note="Nicotinamide mononucleotide (NMN) deamidase PncC
                     [Coenzyme transport and metabolism]; COG1546"
                     /db_xref="CDD:441155"
ORIGIN      
        1 mptdsvvhql airagnklrd ehlslaiaes ctggmiaaai tdisgssqwf ergfvtysnq
       61 akidmigvpp dliekhgavs epvaramaeg alrnsraqva lsvtgiagpa ggsekkpvgt
      121 vsfgwsnrlh tdvetlvfkg dreqirtqaa ahalrgllkl lderer
//
LOCUS       WP_175911226             293 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: pirin family protein [Burkholderia].
ACCESSION   WP_175911226
VERSION     WP_175911226.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..293
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31328
     Region          13..270
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mtdsikallk phvrdignlq vrrtlpalaa rlvgpfiffd hmgpatlpag tgldvrphph
       61 iglatvtylf dgailhrdsl gslqeivpgd vnwmtagrgi vhsertpdaq rasghtvhgi
      121 qtwvalpvah ettepsfehh aadtlpkrde ngvsltviag dafglrspvt tfsrtlyvaa
      181 efaaggrfel dasheeravy vvdgdlsidg tsvpaeqmav lapgatvtla sdggaramll
      241 ggakidgerf iewnfvassr daierakqaw tnqemgkvpg etewiplpes kpr
//
LOCUS       WP_175911221             155 aa            linear   BCT 11-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Burkholderia sp. BCC1640].
ACCESSION   WP_175911221
VERSION     WP_175911221.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..155
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=16751
     Region          1..153
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mfnavidapf gkvgirtdaa vvreivylpe svksvdpdsp latravkqie ryferasarf
       61 dlpladvgsa fqhrvwnvis dippgtvqty gqvakrigsa pravgqacga nyfplvipch
      121 rvvaagglgg fanhddngyy qkvkrwllah egvpy
//
LOCUS       WP_175911199             153 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia metallica].
ACCESSION   WP_175911199
VERSION     WP_175911199.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..153
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16615
     Region          1..132
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mddldwkvla llqdngrisy telarhvhls vpavtervkr leaagvvdgy taqvnpvaag
       61 ypvsaligit vaqpekakfl rlletipevv echhvtgads yvmrlvaism thleqligri
      121 nlygetrtsi vmstplparg larppsqhdv grd
//
LOCUS       WP_175911248             302 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia metallica].
ACCESSION   WP_175911248
VERSION     WP_175911248.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31897
     Region          13..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..294
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(106,110,149,163,165,229,246,273)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(107..108,112..113,115..116,119,123,125..131,192,
                     223..227,234..235,238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 msidgrilan vgvlaaiveg gsfaraadal gmspsgvsra vgrlearvgv rlldrttrsv
       61 tltdegrrly edigpllagi gdavtlaags aaavrgrlrv nvdayfsrrv laphlpalla
      121 rhpdlslela areqlgdlva egfdiavrfg eppssslvar klletravtv aapayvkrhg
      181 rpetpadlig hacvqmrntl tgeplewvyq lgrkrvpvkt tgrllvndag tmlgaclaga
      241 gvarfkasgv aglieqgrlv elladwrgea fplfayypsr hlppakvraf idfvaeivai
      301 gs
//
LOCUS       WP_175911160             213 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC1640].
ACCESSION   WP_175911160
VERSION     WP_175911160.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..213
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22195
     Region          2..213
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mlgithfgff vlavfllnvt pgpdtayivg rsvaqgrgag lmsalgisag ccvhalacaf
       61 gltallaasa aaftviklvg aayliylgvr milakqaaap agaeaarvta arplrqlfmq
      121 gfwtnvlnpk vvlffvsffp qfvsadsphk alaflalgsv fvvmstvwtc ivawvagsvt
      181 qrfsgkpgvr kwldrtvgsa fvglglrlaa tqr
//
LOCUS       WP_175911304             157 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175911304
VERSION     WP_175911304.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..157
                     /product="VOC family protein"
                     /calculated_mol_wt=16637
     Region          13..136
                     /region_name="VOC_like"
                     /note="uncharacterized subfamily of vicinal oxygen chelate
                     (VOC) family; cd07246"
                     /db_xref="CDD:319910"
     Site            order(13..18,20,35,49..50,57..58,60..62,81..83,85..90,96,
                     117,122,130..133)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:319910"
ORIGIN      
        1 matsvnpipe gmrtltphli cagaaaaidf ykrafnater frlptpdgrl ahaclaigds
       61 tlmlvdempe hgalgpktln gtpvclhlfv pdtdaaivqa vaagatvrmp atdmfwgdry
      121 gqvedpfghr wsiathqrdl tpeqiaeama sappcgs
//
LOCUS       WP_175911345             823 aa            linear   BCT 11-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Burkholderia metallica].
ACCESSION   WP_175911345
VERSION     WP_175911345.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..823
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..823
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=85361
     Region          64..814
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mprnwglgta llalcvavts cggdadspss aslsnmaqaq gnqdgngsgn ssngnngngn
       61 dgstapeknv dirvaqyvnp ligtdyatdq padpvgsglg ggtfpgptlp fgmmqwspmt
      121 ptaqydgrkg dgsgfsggyw ygdtsitafs vlhlsgtgcw snggylnvmp qlspgdagta
      181 aafdhaneta qagyygvtla ngikaelttt vrtglarftf palkqgqeat ialdptvqnn
      241 rsqgstndti tqqgdralsg tiagsgfcwa ghavplyyya efsrpfatkp tlaknspval
      301 tfavdrrhpa vtmklgisfv seanakknld aengggdaqg nasghfdkvr aaasdawnar
      361 lnaihvtggs dadktkfyta lyhaslhpnv fndvngeypd fyasngapaa ptrrvdkgrt
      421 myanfsgwdi drafiqlqal ldpvrtsdiv qslvldakac gafprwayfn tetavmpgda
      481 gsiivanaha fgatnfdtqa alsimkrsta pgaacagtpv mgsradydrl gyvpasgsgd
      541 nqtasntley avrdfavsrf aaalgdaata gtllkssgnw rnlfdqgair pktsagawvt
      601 dgsgfmegna eqytwyvphd lagvvaqagg aapvvkrldt ffthlnigte qpyfyvgnev
      661 tmavpwvyaw agapshtqrv lhaslanefg agaaglpgnd dlgavsgwyv waalglypvv
      721 pgvsgvavss pqfekidvrv gqhdggyrll hivapgagsa dtasfyvksl alngvswpga
      781 wlplaqiakg atlsyamtad asattwgtda sampsfpqaa gap
//
LOCUS       WP_175911439             399 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Burkholderia].
ACCESSION   WP_175911439
VERSION     WP_175911439.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..399
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43186
     Region          1..373
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkplkvgvlg vgdisdvylh nlakypivel aavagrdlek arakaaahgv pkaypdaasl
       61 iddvgidivl nlttpdvhae ltlaalragk hvysekplat tfaegkalce darrrgltlg
      121 capdtvlggr lqtcrqlide gvigivhgat afavsrgpew fhpnpaflyr rgggplhdig
      181 pyylsalvsl lgpvrqcsav agracservv esgplcgmri pvdepthvaa nlvfvsgalv
      241 tlivsydvwd selprmelyg tagtlclndi dpcdgpnlfg gdlllrtrdd yrwvelprge
      301 aarrpwkkvp ierpfietsh rensrgiglv dmamsiaegr aprasaemal hileimhgml
      361 esaannvtyp letrmerpep mwlqfqdcls heplepara
//
LOCUS       WP_175911357             283 aa            linear   BCT 11-JAN-2025
DEFINITION  ion transporter [Burkholderia metallica].
ACCESSION   WP_175911357
VERSION     WP_175911357.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11997982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..283
                     /product="ion transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0034702 - monoatomic ion channel complex
                     [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30659
     Region          27..234
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
ORIGIN      
        1 mmtqiqstfg alrdaaahca rrptflrnld iavlalivas vlvvmadsvh dlheryghal
       61 yvtewaftll ftveylvrll sapkpaayar sffgivdlvs vlptylafff pglhalidvr
      121 llrllrvfri lglsiyleeg qmlmraltra rrkifvfigg mfvlvvilgt lifliegpen
      181 gitsipvgvy waavtmsttg ygdltphtpl grlitscail lgygiiafpt gimgaelvas
      241 alertrantr paigdepccp hcgvalpvrn apdadaggeq atk
//
LOCUS       WP_175911388             302 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175911388
VERSION     WP_175911388.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33115
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,219..224,
                     230..231,233..234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mklsfealea ldaidrtgtf aeaaellhrv psaltylvqk lesdldvalf drsgrrarlt
       61 hagrvvveeg rrllhaaeql erkaqraqqg wetevricvd eilpfeamwp yvhafyglem
      121 dtrlrlstev lggtwdalis rradlvvgas geppelpdiv trpigtlrhv favapdhpla
      181 alpeplsmas vvehrgavis dtsrelqprs vavdagqpyl avptlaakla aqceglavgt
      241 lpdciaarai aqgrlvarqv tgmrdtthcy iawrgdeagr alhwwveqld rpdlvdrfta
      301 la
//
LOCUS       WP_175911491             397 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia metallica].
ACCESSION   WP_175911491
VERSION     WP_175911491.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..397
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42500
     Region          1..364
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 maritckals khydggpavl hpldleiadg efivllgpsg cgkstmlrmi agleaitgge
       61 lvigdavvnd lpsrernvam vfqnyalyph mtvydniafg lrrlkvpade idrrvrdvar
      121 ilsldalldr rpramsggqq qraaiarami ktpavflfde plsnldaklr tqlrgdikrl
      181 hqrlktttly vthdqleamt ladrvvlmrg ghieqigtpa elygqphtvf aagfvgtpam
      241 nfadgtierl ganvllecng trwplasprf aglhdgqqvk tairpnhlrl vaetdptpgp
      301 laltgtvelv ellgaealvt ldwcgqpcaa lvpapmapap gavvalrfde ealhlfdagt
      361 ernvalpdan piahaappaa asraappaat gwsmsrs
//
LOCUS       WP_175911502             435 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia metallica].
ACCESSION   WP_175911502
VERSION     WP_175911502.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46225
     Region          11..412
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(23..24,27..28,31,70,128..129,131..133,136,156,
                     159..160,163,242,245..246,249..251,254,282,286,339..340,
                     344,348,364,367..368,370..371,374)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msthkqgrav kvavasmigs avesydffiy gtaaaawfgk iffhtnepiv gimaafatla
       61 vgflmrplgg ylaghygdri grksvlfwsl iamggatvli galptyaqag vvapillill
      121 rmvqgigfga ewggavlmac ehapekrrgf fgavpqlgip lglllangaf llsgallegd
      181 wvwrtpflls fvmvaigifi rmsvsespef eavkaenkvm kqpaleviks dwrsilkiig
      241 lrmaetggyy ittsfmlsyv alahvsttrh ilwgtligsa lglashliyg alsdkigrrp
      301 vfmmgalfti vfgvpmfmli ntgavmmviv aialsllfsh dpifaveasw fseqfpanvr
      361 ssgislgyng asvvagllpi vatfmygafg wigpalmfss lgivsaccal amketapavv
      421 erksaaatte rrlaa
//
LOCUS       WP_175911554             834 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            metallica].
ACCESSION   WP_175911554
VERSION     WP_175911554.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..834
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=89625
     Region          14..788
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 madlaaftrt pfflqdkrll alsfphddap svtdsygrqr parlvaerlv aheglgidft
       61 fevtllsgea gvtladmlgk llavsmvrpd gglryftgyc tefslvrndd siaeyravlr
      121 pwshflltrv nnrlflgqsl qqqigtllad yqglapswew rvrgddpart mnvqggglge
      181 sdwnyivrhl eaagflywwe hdekglkliv gddstvqcpa idgrspqirf qthdgpmaad
      241 aisqwsavrs lsagsysata fdfkaphaan aqiptlhpsg vapqvehhey vghygfakqt
      301 ragdalarvr meeieatatr fdaagnhhgi lpgrwfqlsd hssvasgspq dheylilear
      361 heaannylqa dgkpeyrnrf vaghrrtpwr pgrgfnsepv rvlapqtatv agakgagsvd
      421 vdeygrvciv yhwdraaqis arirvaagwa ggekgmiahp rvgsevlvmc ldgnpdrpiv
      481 sgttynaerm ppwtlpdqhv ltglrsrels gdggnaaggr snhvllddtp qqlqlklrsd
      541 tdaseltlgh nvridatqgr tdqrargfel rtdahgavra akgllvtsea rydarahatd
      601 igetvarldk ahdlheslsg sahdvkaqes gdqdavhqal rtqndglrgs ggnpqqgefp
      661 efaqpflala spagilattt gsthvasdqh valtsgahts igagksmlvs aqeavrvaaf
      721 ekgirlvaaa adidiqalkd sinvlakldv kvdanritit akeevlingg tsytrwngsg
      781 ivhgtkggft ahaashtfig pdslpvpara fpgtacapcm vnaasmaspf aaka
//
LOCUS       WP_175911642             661 aa            linear   BCT 11-JAN-2025
DEFINITION  beta-galactosidase [Burkholderia metallica].
ACCESSION   WP_175911642
VERSION     WP_175911642.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 661)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 661)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 661)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 661)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 661)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448998
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..661
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..661
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73838
     Region          1..620
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
ORIGIN      
        1 mrlgvcyype hwpetmwadd arrmkalgie qvriaefaws riepspgeyd wgwldravdv
       61 lgaagleivm ctptatppkw lvdrhpdila igadgrpraf gsrrhydfss ptyleasrti
      121 ctavaerygr hpavrywqtd nelgchqtvv syspaalvrf rawlkarygt idalnrawgt
      181 vfwsmeyrhf devdapvgtv teahpshrld yrrfasdela ryhrmqvdvi rahspgrpva
      241 hnfmqlftef dhyevardld vatwdsyplg aleelwfapd vkarwlrtgh pdfasfnhdl
      301 yrgmsklpfw vmeqqpgpvn waqwnpaplp gmvrlwswea fahgagcvsy frwrqapfaq
      361 eqmhaglhtp ddkldeggrd aqrvareiaa vhdagadadg avrasvalvf dydakwllev
      421 qpqgadfhyp rvafeyysal rslgldvdiv sahapldgyr lvvvpplpvv pddfaerlaa
      481 sgaqavlgpr tgsktvdlqi pptlppgpla silpvrvwrv eslrpnvter idgtlrdgtp
      541 ltgaarhwrd fvelhddtrs vvrarfadgh pacvshgtlh ywaalfddat tarlfadvaa
      601 eaglaptplg dgvrvsrrgg ltyvfnygat phtidavpps afvlgaaqvg pqdvavyrsr
      661 p
//
LOCUS       WP_175911566             264 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175911566
VERSION     WP_175911566.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..264
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27853
     Region          12..140
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          179..260
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mhrvthyrrt degieaisle sdrtfprhah defgvgvivs gahrswsgrg qvdalagdai
       61 mvnpgemhdg mpietgtgrr wrmlylapal vagvaaeegl ggvelahpav rdarlaaafg
      121 rlharlvagd tlplardeal vtlvagllar hsnralppag vapairvare rldaapaapv
      181 slaelaglsg vsrfqllrgf arelgitpha ylmqsrtrla rallasgrpi adaaaeagfa
      241 dqshltrafa rqfgitpgrf tqag
//
LOCUS       WP_175911659             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1640].
ACCESSION   WP_175911659
VERSION     WP_175911659.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32618
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrfkqietf aavagkgsls aaahaegvap aiigrrldal eerlgvkllv rttrkltltf
       61 egsafledcq riindmqnae asvsaggvka sghlrisapa gfgrrhvapl vpefsgahpd
      121 vsvtldlsdr mvdlvnegfd cavrlgelpd sslvslklge nrrvcvaspa ylarrgtpat
      181 laelarhncl alaananqqr gwafqeddkv vsirvngtme csdgavlhew clagyglawr
      241 swwevgddia agrlvsvlda faappigiha vfpqrrhlpl rvrlfldylk htyerpgywg
      301 e
//
LOCUS       WP_175911686             235 aa            linear   BCT 11-JAN-2025
DEFINITION  MOSC domain-containing protein [Burkholderia metallica].
ACCESSION   WP_175911686
VERSION     WP_175911686.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12233312
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..235
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25989
     Region          10..183
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
     Region          180..219
                     /region_name="3-alpha"
                     /note="3-alpha domain; pfam03475"
                     /db_xref="CDD:460938"
ORIGIN      
        1 msdparaais avigavwvgk crplagtpha saidkqpvga rlwlgthgfa gdeqadarhh
       61 ggpdkavhhy ahdhyawwaa qigardvltq pgafgenlst hgmteddvcl gdvftlggav
      121 lqvsqsrqpc wklnvrfehp rmaalvqqsg rtgwyyrvlr egwvapgdgl alhercypqw
      181 plstvldvly rrtldmaald alcdvpvlpp gwrtmldkrr merqvedwtk rldgr
//
LOCUS       WP_175911731             326 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH:quinone oxidoreductase family protein [Burkholderia sp.
            BCC1640].
ACCESSION   WP_175911731
VERSION     WP_175911731.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Shimomura,Y., Kakuta,Y. and Fukuyama,K.
  TITLE     Crystal structures of the quinone oxidoreductase from Thermus
            thermophilus HB8 and its complex with NADPH: implication for NADPH
            and substrate recognition
  JOURNAL   J Bacteriol 185 (14), 4211-4218 (2003)
   PUBMED   12837796
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..326
                     /product="NADPH:quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34054
     Region          1..322
                     /region_name="QOR1"
                     /note="Quinone oxidoreductase (QOR); cd08241"
                     /db_xref="CDD:176203"
     Site            order(40..41,122,126,147,150..152,171..172,176,191,215,
                     237..238,240..241,262..264,314,316,318)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176203"
ORIGIN      
        1 mkallctafg pidrlriedv aipepaagqv rirvkaasln fpdalivqgl yqmkpalpfs
       61 pgaefagvid avgdgvsawr pgdevvaftg hggfaeqcva dvhqiaalpp gmtfeqgaal
      121 vlaygtslha lqqrarlqqg etllvlgaag gvglaaieia kalgarviaa assadklalc
      181 reagaddtid yatedlrrrv deltggrgad vvydpvggay seaalrataw rgrflvvgfa
      241 ageipkialn lallkerdil gvfwgdavrr dpaqhvanmr qlaqwfaagk vrpaitervp
      301 lagaadaiar manrqvkgkv vilpea
//
LOCUS       WP_175911745             238 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175911745
VERSION     WP_175911745.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 238)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..238
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25423
     Region          2..226
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mslvhvehls ktylldsvrv tgladvsatl dagrftvlsg psgsgkttll nligcidrpd
       61 sgrvtiaghd taslsddals dfrarhvghv fqtfnllpvl sayenveypl lmsgwaparr
      121 aarvrdllda vgladkarhr psqlsggqrq rvaiaralaa epamvladep tanldsatgh
      181 aiielmrtiq rerdvsfivs shdphvvkva davirildgr ivgheraggd tatqevcr
//
LOCUS       WP_175911784             351 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia metallica].
ACCESSION   WP_175911784
VERSION     WP_175911784.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..351
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=36942
     Region          4..351
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mqrkaflvga cvlcatsaha ssvtlygivd syvefdrigs lssarqsggg sstsrfgltg
       61 vedlgggtst kfvlesgfsp adgsfqggtl fyrqayvslq ntrygdlrlg rqytpafyvv
      121 ydgdpfglne rlsplallat stdtitsntt ppiprfnqav sylspawngl rvmatygfpt
      181 pnalsaqagr nygaglqyri gglyvgagfq gdtsagnlsp vivspsttrh yvfaanyafa
      241 hvklyaafly gvgtaanlpa fstasagasi dvgaldrvlv svvrrdvkgs andatalgig
      301 ydhplskrts lyarylymkn ggdarntivv glqpqpagte qvfalgivhr f
//
LOCUS       WP_175911824             219 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia metallica].
ACCESSION   WP_175911824
VERSION     WP_175911824.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..219
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24932
     Region          5..207
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mlpmlyahpf ssycqkvlta lyengtpfey rvlahddpkp mqeltalwpl krfpvlvdrg
       61 rtvveasiii eylglhhpgp vrllpddpra alevrlmdrf fdnyvstpqq kvvhdalrpa
      121 aerdargvvd aramletsya wldktmadre waagdhfsla dcgaapflfy adwthridpk
      181 fgnvlayrkr llarpsfara vdearpyrsf fplgapdrd
//
LOCUS       WP_175911860             732 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia sp. BCC1640].
ACCESSION   WP_175911860
VERSION     WP_175911860.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 732)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..732
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=80559
     Region          37..704
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mnrfvpflrd lwlrcrtgar vlgagawhrl rhptrrgval tlaaipvlgl lvllafvpft
       61 psigdirkar idrparvlsa dgqliaefrp vnrewvplkq isphmvdali atedhrfyah
      121 hgidwrrtla aglhtfsgsr qggstitqql arnlypdevg raptltrkvk elitafkiet
      181 vyskdeilet ylntvpflyn aygvemaart yfgksadqld ivesatlvgm lkgnsyynpv
      241 lnperaeqrr nivlarmaam gmlsprqlaq lqrrplrvdf epqtaqpgpa phfavqlrkw
      301 liawadrnny dlyadglvvr ttldaqlqdm atqaltqqtd rlqaiaddaw hnpsgcglrn
      361 dlfrgfirqt pdyraardag ladaaalkql ganrtfiral cerktqvqag fvaidprnga
      421 irawvgspdf gsepfdhvvq arrqpgstfk pfvygaafad gmrpgdtfvd rpvaipigah
      481 avwhptdaep ptdapmtlrd alalsrnrit aqvmqregaa rvaqlaramg vrdsaldavp
      541 slalgtspvt lkemvsaygt ianrgvyvap qmitriedrd gkvlaafgsa pperalpvaa
      601 aqtlvdvmrg vvdygtgadi rsrygirvdv agktgttqdn tdgwfilmhp qlvagawvgf
      661 ddgsvtlrsd ywgagahsal pivgsfydaa lraraidpra qfspdfrprs apapvpkrhp
      721 hpglfdwlki fr
//
LOCUS       WP_175911900             192 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            metallica].
ACCESSION   WP_175911900
VERSION     WP_175911900.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20220
     Region          26..159
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 marprspdkh eailaaaara laedgatatt ariarlagva egtvftyfet kdallnalyl
       61 slkagmream magfpehapv eqavrhawng yvswgvadpd grralqqlnv sgriadahra
      121 agaegfggin vllrelvaas galkpdeaya fcaalftsia etamesiard paradayrea
      181 gfralwavlh av
//
LOCUS       WP_175911891            1018 aa            linear   BCT 11-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Burkholderia sp.
            BCC1640].
ACCESSION   WP_175911891
VERSION     WP_175911891.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1018)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1018)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1018)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1018)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1018)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1018)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1018)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1018
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..1018
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=115116
     Region          1..1012
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mstvgqiekk tqervvklfr dslgyeylgn widrvgnrnv dhgllegflk qqgyddalis
       61 raihlldkaa gdqsksiydr nkavyellry gvqvkpeige qvqtvwlinw kkplsndfai
      121 aeevtvsgad akantkrpdi vlyvngialg vlelkrstvs vsegirqnld nqkkvfiqhf
      181 fstmqfvmag ndteglrygt ietpekyylt wkeespidnl ldrhltqvcs kvrflelihd
      241 fivydagtkk lcrqnqyfgv kaaqdhvkrr eggiiwhtqg sgksltmvwl tkwirenvkd
      301 arvliitdrt eldeqiekvf kgvneeiyrt ksgadliakl nattpwllcs lihkfggked
      361 seefgdvsgy veemkralpp dfrakgdvyv fvdechrtqs gelhkamkai lpnamfigft
      421 gtpllkadka tslevfgryi htykfdeavr dgvvldlrye ardvdqhits qkkidqwfes
      481 ktkeltdlak aqlkqkwgtm qrvlssqsrl ekivadilld matkvrlisg ygnamlvsgs
      541 iyqackyyel fsktdlagkc aivtsyrpat sdikgesteg lteklsqyei ynkmlncqdp
      601 eafekdvkkk fidepgqmkl livvdklltg fdapsatyly idkqmrdhgl fqaicrvnrl
      661 dgddkeygyi idykdlfksi gsavhdytsg aldgydkddv aglledrltk aredleeare
      721 aikalcepve tpkdtaaylr yfcakdsgna gqlkenepkr lalykfaaaf irayaaiasd
      781 leeagytaae ienlkdetsh fekvrnevkl asgdyidlkm yepamrhlid tyiraddsei
      841 isafddmsli qlivergvga vdalpkgirg dkdavaetie nnvrkliide qpvnpkyyek
      901 mselldalie krktdalaye eylaelvkla kqaqsptsgs typaslktae qkalydnldk
      961 denlavnvdh ailvarqddw rsntmktrki rnaiksvlge gdarvdaild lvksqhgy
//
LOCUS       WP_175911542             243 aa            linear   BCT 11-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Burkholderia metallica].
ACCESSION   WP_175911542
VERSION     WP_175911542.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..243
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26861
     Region          70..224
                     /region_name="CE4_NodB_like_5s_6s"
                     /note="Putative catalytic NodB homology domain of PgaB,
                     IcaB, and similar proteins which consist of a deformed
                     (beta/alpha)8 barrel fold with 5- or 6-strands; cd10918"
                     /db_xref="CDD:213023"
     Site            order(73..74,139,143,179..181)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213023"
ORIGIN      
        1 mlhatrypil tyhqirtlpp psdrlrglsv apdafrrqmt lfsrlgyrgl svrelqpylr
       61 gersgkvfgi sfddgflnvl thampvldal gftatcyfva grfggendwd agadtarapl
      121 mthadmlawr dhgheigsht ldhvalshvp ahvsevqive skqrlealsg ehvesfcypy
      181 gdldprvrdq vaaagygnat ttrrgcaday ddrfllprip vaggvgavrl wfkcvkgrvr
      241 krg
//
LOCUS       WP_175911935             320 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia metallica].
ACCESSION   WP_175911935
VERSION     WP_175911935.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..320
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34840
     Region          6..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..286
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(103,107,146,160,162,221,238,265)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(104..105,109..110,112..113,116,120,122..128,189,
                     215..219,226..227,230)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 msvenlngla afvraveags ftgaarllgt tpssvsrsvg rlerrlgirl frrstratvl
       61 tvegqtyyer vaplirgiee agnaltaspa avgklrisvp galarilldp ltrdlmarhp
      121 dllfdvnvsd hhvdviregf dlviragqvm dstlharklg dlplvlvasp dylsrngvpe
      181 saselgkhrh vryrlagrvv pvmfsgeasp qmegafdsds geamrlaaln glgiaqilka
      241 tvqedidagr lcrvlpelal rsvplhvlhg ygrnmplrar vmidfvekql sqwmkgrfsl
      301 adstrrcntl eaarqrgvrq
//
LOCUS       WP_175911950             276 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Burkholderia metallica].
ACCESSION   WP_175911950
VERSION     WP_175911950.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 276)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..276
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29656
     Region          14..276
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mlhsvfsarf sagrvarfiv aallgvalld gaqadtaplk vgistspqie alkvaakeak
       61 aqgldvkive ftdwntpnaa lankdidvny fqhipflena nkqggynfvs iapgtimkig
      121 lyskkvksfa elkdgakvai andpvnggrg llllqragli tlkpgadyra tthdivsnpk
      181 hlkiialeas qlarslddvd laqgypsfik lagttdpnsa llfdgtenki faiqwvvrpd
      241 svndprirkf iaiyqqspav rraldnafgs lyaiaw
//
LOCUS       WP_175911965             215 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [unclassified Burkholderia].
ACCESSION   WP_175911965
VERSION     WP_175911965.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..215
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22355
     Region          6..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mhtsgslygf lviggmlait pgpnmvyvms rsiaqgrtag lislagvmvg ylfymfgaaf
       61 gittlflsvp yagtvlgvvg aayllylawq avrpggrspf evktlpneqp lrllamgatt
      121 svlnpklaml fvsllpqfid yrqgslfgqs lflgslliaa fasanglvai cssgiakylh
      181 grpalllaqr wamgavlggl gvqmlveasr magaa
//
LOCUS       WP_175911942             200 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: lytic transglycosylase domain-containing protein
            [unclassified Burkholderia].
ACCESSION   WP_175911942
VERSION     WP_175911942.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..200
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - lytic transglycosylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=20786
     Region          <25..191
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 miavappaaa agdvmahgva mivggaqtaa apdtaarrgv vltfavagaq prtmvtayah
       61 rrmqalaplv aeiahafrld aallmaviha esagdrrais pkgatglmql mpatgaeyga
      121 tdlfdarqni vagarflgdl lqrygsrdla laafnagaga vdryggripp ydetrryvvr
      181 vnglyaryah adeawtqavq
//
LOCUS       WP_175911983             156 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175911983
VERSION     WP_175911983.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..156
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17532
     Region          2..141
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mikldrydla ilrilerdgr itksklaeav nlsispawec vrkleesgvi rgyradvdwi
       61 gtfsgsrivv evtlsrhtap dmrrfedrvs aapevaqcya tgggvdyvlh vvardidhyq
      121 rfidgllmdd lgieryftyi vtkvvkcesg gapdwh
//
LOCUS       WP_175912052             229 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [unclassified Burkholderia].
ACCESSION   WP_175912052
VERSION     WP_175912052.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..229
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24070
     Region          23..225
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mtdvlplttd sesglhyrlr paagrpvgrl lllhgvggne tnllnlagti dprieiafvr
       61 gpltfgpgqh awfpvrfgpn gpeidaarae asrvqliall ralrargtdn ehaalptvia
      121 gfsqggimsa svaltspadv vafavlcgri lpeidpliap rdalsalhal vmhgrfddkl
      181 pvawaetada kltalgvahd trlydaghel taemagdfgr wvaartgsn
//
LOCUS       WP_175912068             320 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia metallica].
ACCESSION   WP_175912068
VERSION     WP_175912068.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..320
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34652
     Region          81..282
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mswqskfacw llrwqfrpet trevldpara rrftdlrmiv prrapagyrl recygpgdap
       61 lrgewlertd agagrgpgrt llyfhgggyy fcstkthrpl vfgltkragv rafsldyrla
      121 penrfpaald dalaayrqll algtppesiv lggdsagggl alatlvalrd rgeplpagai
      181 lfspwtdlaa tgatlrtndg adpmfagaal pkaaklylgd epgtnpyasp lyadfaglpp
      241 lyiqvgstev llddsrrvae kakaagvave ievwpdmphv wqlyapmvpe ardaldraaa
      301 flrrvavera vqrageasia
//
LOCUS       WP_175912179             303 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia metallica].
ACCESSION   WP_175912179
VERSION     WP_175912179.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32930
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..295
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,224..229,
                     235..236,238..239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mtfdlrqlra fttivacgsl graadalhvt qpalsrilkr ledqvgaplf erhskgvqlt
       61 afgdallpha tllqheaeha reeldamrgf akgtikvgtv gsiaslvlpv avgrvldrwp
      121 nlrveilegv wdrlaeglnk heidlalsah gpdtddivai pecrwedrsh ivaapqhplr
      181 algraptlad tlharwaipp rgtapfdhmr atfdaqglpl pdiavetrsv ttlkslvaha
      241 gflswmaepm ygaeqragti dtlpvrevva vrtltafrrr hgilpgpagk lldelvaltr
      301 egr
//
LOCUS       WP_175912112             123 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: nuclear transport factor 2 family protein
            [unclassified Burkholderia].
ACCESSION   WP_175912112
VERSION     WP_175912112.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629346
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..123
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=13308
     Region          8..114
                     /region_name="DUF4440"
                     /note="Domain of unknown function (DUF4440); pfam14534"
                     /db_xref="CDD:434023"
ORIGIN      
        1 mdavraviep yeaalraaml andvdtldtl ldddlvftip sglviskddd lsahrakllr
       61 ldtldiqetq aktvggmilt ttkaklagrf dgnafdgmfa ytrlwrrsgs ewrvvaghas
      121 qig
//
LOCUS       WP_175912180             375 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [unclassified
            Burkholderia].
ACCESSION   WP_175912180
VERSION     WP_175912180.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..375
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42044
     Region          87..327
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 masplvflhr mlgfaaarrg rtlsgespqh ngerfsnvap rpvegfgktl giawnmlvnk
       61 prntvptgal pidsltreql daapdrslyr lghstlllkl rgefwltdpv faeraspfrr
      121 igpkrfhasp ialadlpplr gvllshdhyd hldrdtvlal aaatgvfvtt lgvgdrliew
      181 gidakkvrql dwwqsvevdg ltltatpaqh fsgrslfdgn stlwaswviv dddlrvffsg
      241 dtgyfdgfrt igerlgpfdv tlietgaydp qwpyvhmqpe etvqahidlr grtlmpihng
      301 tfdlamhrwq epfervtala mvrgvelstp rmgerlnlda phrgerwwrt vdepakasat
      361 ktrrwqqlca sqatk
//
LOCUS       WP_175912228             233 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Burkholderia metallica].
ACCESSION   WP_175912228
VERSION     WP_175912228.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..233
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=25040
     Region          6..224
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mdlesilytq gfgsrrqcrg lieagrvava gagatdpdaa fdtdglvfsv ddtawpfhar
       61 aylalnkpag yecsrdpqhh asvfsllpap lvargvqcvg rldqdttgll llsddgqfvh
      121 aytspkrkvp ktyvatvrhp lddtqlaalr tgvqlhgepk piaalaadar dthtlaltvl
      181 egkyhqvkrm vaaasnrvea lhreniggfa lpddlapgaw rwlddadlaa lrk
//
LOCUS       WP_175912237             203 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175912237
VERSION     WP_175912237.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..203
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22791
     Region          1..157
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrankrqvvv dkatelfsrh gfhpvgvdwi iddsgvarmt lyrhfpskde lirevlvqry
       61 dliigsietq lrdvhdpver vktifdwyea wfntpefagc lferalaefg tayapisdva
      121 iryrrkmvew iaellqplvl petarqlagv ymmlldgatv darafndsas agrawhaaka
      181 lleqamsaan rpatdadpat qla
//
LOCUS       WP_175912249             272 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia metallica].
ACCESSION   WP_175912249
VERSION     WP_175912249.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..272
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28861
     Region          17..266
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtraalpaaa ggptsyaavd ltlkagartl ldgfngafrp geiwcvagpn gagkttllat
       61 laglqppagg qveidgrpla awppaqlaqr ralmpqqlhd afsatvfdtv llnrfpylgg
      121 wgwerdgdra aardalaafd lsalasrdvl slsggerqrv alaatlcqda plmlldepla
      181 hldlhhqigc ltalavwldt gprtvlfsch dlnlarrfat hallldgrgh awagpvydvl
      241 tperasdafg yplvlireng rdallpawpe rq
//
LOCUS       WP_175912277             766 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia sp. BCC1640].
ACCESSION   WP_175912277
VERSION     WP_175912277.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 766)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..766
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81493
     Region          48..724
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mketdgakrr fvarragvtl cfggmlggwl tpasaqvepa gnvdaptlap ivvvgttpll
       61 gigtplsrvp anvqtirged itrqhggvlt dyfeknvssv dineaqgnpy qtdvnyrgft
      121 aspvvgtpqg lsvfvdgvrv nepfgdvvnw dlipqvaidt mqlipgsnpt yglntlggal
      181 aittkngkts pggaaqvsvg swgrktaqie qggriggnld yyvtgnvand ngwadhnasr
      241 mrqgfgklry tdadttlsis aggadnalqg sqtiprsfld nraqaytypd lnrnsaayvt
      301 vsgdhsfgdh vqlsgnvyyr hyrntntssn vnddfgsvdg sgatdavqat ndrsvittds
      361 yganvqltll gklagmdnqf gvgasadlan sgfdqssqda mftdaratvg igdftrktra
      421 ktrnasygvy fddtlaltrq wsltlagryn wsraaiedas glqplltarh tfsrfnpavg
      481 vtwnpvpgft ayatynegmr sptaielaca dpaapcslpn dfladpalkp viaktvelga
      541 rgrsgeattw saavysttld ddiqfissng gastlgyfqn vgktrrqgfe laghtqlgpv
      601 gigvsysyvd atyrstwtes sasnssanvq gnivvrsgdr ipgipsstvk lrldyaatpk
      661 wnvgtnityr sgvfargden nqdangkvpg yvlidldttw qvtkrlqlfa sitnlldkhy
      721 asfgmlgrnf fngpnhsfdg lnpvneqfvg pgaprgawvg aryawd
//
LOCUS       WP_175912285             231 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia metallica].
ACCESSION   WP_175912285
VERSION     WP_175912285.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..231
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24387
     Region          36..231
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mfqirraadr dqrshgwhef lhsfplgsdr sgpsafgalr elneeciapt rgygmrpyrd
       61 aeivtyvldg alghrdslgn gaivraggvq rmsagtgvml setnashdap lrllriwlap
      121 agaggrpgya qtrfadhekr grlrlvaapd ggdgalpvra darifaglid gdeatafdlp
      181 agrrayvhvv rgdvevngra laagdgvrig gvdavafarg raaevllldv a
//
LOCUS       WP_175912373             441 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [unclassified
            Burkholderia].
ACCESSION   WP_175912373
VERSION     WP_175912373.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..441
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=47915
     Region          8..423
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mnsahqkphr ivivgggagg lelatrlgrk ygrggaaeit lvdrhrthvw kpklheiasg
       61 smdtsahevd ylahshrhsf ryrigemvgl drerreiqva pfiddegrnv tqarvfgydt
      121 liiaigsrtn dfgtpgvqah tvrlesqsda krfharmvna cirahtqaap lrpeqlhvai
      181 igagatgvel aaelhrttre vvaygldrid pdkdikvsli eaadrvlpal pprlsqater
      241 lldklgvevh tnarvaevsg dcvsladgrm laaelvvwaa gvkapdflsn lagletnrin
      301 qlvvgatlqt trdpdifafg dcaacpcggt dgnvppraqa ahqqaahlvt qmklklagkp
      361 lrdyryrdfg slvslgkfst vgnmmggpmg gslmiegmla rimyeslykm helalhgwpk
      421 vivdtlarll trrggqhvkl h
//
LOCUS       WP_175912319             287 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC1640].
ACCESSION   WP_175912319
VERSION     WP_175912319.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..287
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32055
     Region          11..147
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mnqsvplrls gvdhtarptw klretiefyr dtlglplvht isargwgpes hpdflhfffd
       61 sgngstiaff yylgeprpqe rplmppapdd hvfdathtaw ltdsaeqlla wkemleakgv
      121 evssatqhev iesiyfrdpn gyfveitvkl relesldard aaltleaaim aeqaassheg
      181 qvrqidtvwq ekgrllsgqc giksegpgif vpalaefasv vdvarrnaey rvsqpspgyf
      241 liesnaalef nrkelglkpa vwyglftggl cgridtfdkd rvriveq
//
LOCUS       WP_175912278             434 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia metallica].
ACCESSION   WP_175912278
VERSION     WP_175912278.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46928
     Region          24..425
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,156,
                     159..160,163,258,261..262,265..267,270,298,302,353..354,
                     358,362,378,381..382,385..386,389)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 matstqslpg ssgafeeaty rkvswrlvpl lllcyvvayl drvnvgfakl qmasdlnlsd
       61 tvyglgagif ffgyflfevp sniilhkvga rvwiarimat wgvisiltmf vttpamfyvm
      121 rfllgvaeag ffpgvilylt ywypahrrgr mttffmtava lsgviggpis gfilkafdgv
      181 sgwhgwqwlf llegipsvlv gvvvflklde riakanwltd dekallsrnv eaeeatkedp
      241 plgavmaspr vwlmaliyfs fvmglygvgf wlptiikatg vtdtftigll saipyaaavv
      301 amiliarsad khrerrwhva ipaaigaigl vlsviwahqt alamlgltla tigilttlpl
      361 fwslptaflg gtaaaagiam insignlagf lspymmgwlk qatgandsgm ymlagflvlg
      421 gllalsvpkr lvdk
//
LOCUS       WP_175912408             175 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia metallica].
ACCESSION   WP_175912408
VERSION     WP_175912408.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..175
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=19261
     Region          45..173
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 mktsqkrfyy vtltvafiml cliaglpkaf gqevvskkkd ascfvmgdsi aqgiaaqlpq
       61 casdtkvgln tvqaltrfnr ipevqtvivs lgindrdylg tranleavra rihaqnviwi
      121 lppailsfgi qkkkdalyva mrnrdymkni dhtisadhih ptnngykaia qqlgi
//
LOCUS       WP_175912426             246 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia sp.
            BCC1640].
ACCESSION   WP_175912426
VERSION     WP_175912426.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..246
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27240
     Region          78..241
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          188..241
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mptspvpadh eaadwqralr acvdafdafv spsaivfyrl dlsgepadfe lfgmsesmhr
       61 tyiaryrmld plhpsrcaag aqavvtlasq lpderrdasa ywtrflrrhd vadvveiwlr
      121 ddagrtigaf sllrfgkgda gggagnstag rfapgeidal arlqpvveaa lcpllrarrg
      181 ihridceerl threeqiarl vrdgrsnkei ardlalgqpt vkthlmrmyr klgvsnrtel
      241 vgtlfl
//
LOCUS       WP_175912442             336 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC1640].
ACCESSION   WP_175912442
VERSION     WP_175912442.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..336
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35703
     Region          9..332
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 msqstgsard ivvvgfegvq slditgpmev favanrhlpg hvpryrltla sqhghdivth
       61 aglrlagpta laalperidt ivvaggseaa lrhaasnagv lpwlrtrian trriasictg
      121 afvlaaggwl dgrratthwn qcatlqalcp dvrvepdaiy vsdppfhtsa gvtagidlcl
      181 alveadcgap talavarelv lfmhrpggqa qfsvgldiqa natppmrall tsiaddptgd
      241 lgvaalaarp hmsertfarn flketglppa qfvlaarver akvlleradw plervaqrsg
      301 fgsvdalqra fakrvgitph dyrarfgpkh grqqie
//
LOCUS       WP_175912446             309 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1640].
ACCESSION   WP_175912446
VERSION     WP_175912446.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1640
  ORGANISM  Burkholderia sp. BCC1640
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia sp. BCC1640"
                     /db_xref="taxon:2676294"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34763
     Region          7..>143
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrflsieaf vrvaeassfa eaarqlgvts svvtnriqql ekfvnaplfh rstrhvrlse
       61 vgetfyreca evvgrvnelt dqmrelratp tgrlriqmlp gfaldhfgvp laefnrrypg
      121 iqldiivhdr vvdpveegfd iafqifppis eslierrlfv vrrlfcaapa yleahgapqh
      181 prellqhtta lysgypsrnr wtltrgdevv emelpgmirs nsvhllreya ltgggvvclp
      241 tlvasdalva grlvpiltdf qiaplsfaav ypatqrqalk vkalveflve yigdespwdr
      301 pllergwvr
//
LOCUS       WP_175912516             392 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia metallica].
ACCESSION   WP_175912516
VERSION     WP_175912516.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..392
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42925
     Region          8..369
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 malfssarpp ktilvaaprr igdvllttpl vrslkarwpd aqidmlvfrg tegvlehnpd
       61 vrrvivvaqr agfrerlrda lsmwrrydla caalssdrpr fyswfagrkr vglvdpnrvt
      121 wltrmmlngi ainhhesaht vvstlalapv igiepvsevv apgigddpar rarfdawlae
      181 spairdgrpl vvlhpypmfr ykqwrldgwv emigwlrghg favalsggpa dsereyaeqi
      241 aaeaggdvln lvgrltfges aelvrrarlf igpdtgathv aaatgtdtia lfgpsdpvrw
      301 gpwpqhwpat enpwplrgsg rhgnvwllqg egdcvpcrhe gcerkvdsrs dclvnlgaqr
      361 vkaaaaemlg lnppgpaeav vdtsrlhrtg sa
//
LOCUS       WP_175912532             243 aa            linear   BCT 11-JAN-2025
DEFINITION  alanyl-tRNA editing protein [Burkholderia metallica].
ACCESSION   WP_175912532
VERSION     WP_175912532.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V.
  TITLE     Evolution of aminoacyl-tRNA synthetases--analysis of unique domain
            architectures and phylogenetic trees reveals a complex history of
            horizontal gene transfer events
  JOURNAL   Genome Res 9 (8), 689-710 (1999)
   PUBMED   10447505
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Cusack,S., Hartlein,M. and Leberman,R.
  TITLE     Sequence, structural and evolutionary relationships between class 2
            aminoacyl-tRNA synthetases
  JOURNAL   Nucleic Acids Res 19 (13), 3489-3498 (1991)
   PUBMED   1852601
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Schimmel,P.
  TITLE     Classes of aminoacyl-tRNA synthetases and the establishment of the
            genetic code
  JOURNAL   Trends Biochem Sci 16 (1), 1-3 (1991)
   PUBMED   2053131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..243
                     /product="alanyl-tRNA editing protein"
                     /GO_function="GO:0002161 - aminoacyl-tRNA editing activity
                     [Evidence IEA]"
                     /GO_function="GO:0002196 - Ser-tRNA(Ala) hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004813 - alanine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006419 - alanyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=26391
     Region          3..243
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
ORIGIN      
        1 mttqalfred aylkqcdavv lavgddgirl drtvfyplgg gqagdagtlt lpdgstiaia
       61 dtrkakfdga tpddavhvpa peqeasvaal apgtrvvaqi dwlrryrhmr lhtaahlmca
      121 vlpyavdgcs vtadyvrldf atsdaidrdd verrladlva gahavttewi tddemaerpe
      181 lvrtmsvkpp mglgrvrllr idevdlqpcg gthvrntsei gelrvaklek ksartrrlvl
      241 efa
//
LOCUS       WP_175912559             235 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia metallica].
ACCESSION   WP_175912559
VERSION     WP_175912559.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..235
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25279
     Region          18..228
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mpsslapylp qieanpwfaa lppalradll araalrrlpa ghalfrrgdp pcglyavlag
       61 sltigavdpq gkealltvae pvtwfgeial fdgqprthda ialddtlllh vpqaallail
      121 datpqywrhf allmaqklrl sfltvesmsv mpaaqrlasr llmiadgygg isagrtrirl
      181 sqeklaamls ltrqttnqll kalqadgvvr lhvgeielvd vdalrrasgl pdgmr
//
LOCUS       WP_175912569             380 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [unclassified
            Burkholderia].
ACCESSION   WP_175912569
VERSION     WP_175912569.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..380
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41286
     Region          18..358
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnvsdysgsl ldsswptdri iadvtaiadk qlaevahrid hdgfyplhim aslgavgafg
       61 ahltcggdri alsidamrai srrcgstgfm twchdvcgly meqsgnpalt gellrehmmg
      121 rsfggtalsn pmkalagiek mslravavpg gyrvsgalpw vshiapghhf gamagvyrdd
      181 gslsheimfl vrctdqvhlr qcpefsgmeg tstwgvrvde lfvgddmlia dparpfiari
      241 ravfvllqvg malgvsqgsi dsmrevepvl ghvnrflhdr pndleaeyae laeqvamlaq
      301 tpydgskdyf vsvldaraqg aelalrasqs allhqgargy lssaapqrrv reahfvaivt
      361 paikhlrwem drlsreempv
//
LOCUS       WP_175912591             475 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [Burkholderia].
ACCESSION   WP_175912591
VERSION     WP_175912591.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..475
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49961
     Region          6..423
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mdrekstgql kasslgiadi vffvvaaaap lgatlgagpa vfsmggnaap glyfiascil
       61 llfavgfaam sryvvsaggf aelvsrglgk hagnaaagva llayvcmlig iyaqfaafga
      121 dtiksftgle ldwrmlafva vamtgvlgym dinlsarvlg vlmilevlil vifdgavlvk
      181 tgghandlqi fsattlkssg igtalmfafs cfvgfestti ygeearnpqr tipgatyiai
      241 gligvfytlt mwclalaysg qniqheatan pitfvftant rfvgewstqa mqvlvltsvf
      301 avllsfhnal cryffalarv nflpapltki hrrhgsphaa svvltiscta vlaafmfgka
      361 dpvqviymwm valgtlgvlv lqtlgaagvi gyfartgkrm lwqgfiapaf gglgllvvvi
      421 iavtnfgsls gtteglstql pwlvlvaavv giangffkry gneqndeils qsqsh
//
LOCUS       WP_175912593             638 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Burkholderia metallica].
ACCESSION   WP_175912593
VERSION     WP_175912593.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..638
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=69427
     Region          6..631
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mpyavpqaqh adrvlgalag rlpapaestr lvsswqrsle ryrldpassi gprvltaael
       61 revrdkeeaf lrasgqcltr lhdmirvady cvmltdahgv tidyridrer rndfrhaglh
      121 igscwsesee gtcgvanvlt dlapitvhkt dhfraafttl tcsaapifsp ggeligvlda
      181 savhspdgrd sqrlvyqlvr qsaaliedgy fvhstaqhwi lfghpnrhyv eaqpewliaf
      241 decgnivaan rqardalpal reprhideif datemplrda arldaivalr lratgaplya
      301 rlraplrrtg repgtasrrp gtaqrhvgal tlflhssdar iaqqaelalr vaskrlpilv
      361 lgetgagkev faraihdaga rrarpfvavn cgalpealie selfgyaaga ftgarkhgar
      421 gkialadggt lfldeigdmp lalqtrllrv ladgevvplg sdtpvrvdld vicathrdla
      481 rmvadgtfre dlyyrlsgat felpplrera dvrdviaavf aeeaqatghv ltldatlaeq
      541 laayawpgnv rqlrnvlrya cavcdaarvt rhdlpadiaa qlggvapgal pddergriva
      601 altahrwrpd aaaqalgisr atlyrriakh rivaphra
//
LOCUS       WP_175912597             371 aa            linear   BCT 11-JAN-2025
DEFINITION  C40 family peptidase [Burkholderia metallica].
ACCESSION   WP_175912597
VERSION     WP_175912597.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..371
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37892
     Region          <7..176
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mlriwvpvav vsllaacssv ppqsasrpas gmkittpraf papanfpnfv dhsvgqeeis
       61 iqamslvgvp yrwggntpts gfdcsglvry vigraadvnl prttadmsgr gvsvepdqia
      121 pgdliffntt grphshvgiy vgklrfvnap stggtvrldy ltnpywakrf dgirrvappr
      181 gaptpfdapt yeakrdeprs apvvapapvv vtaaaaplqp ayasppaaat rtpapvmpaa
      241 qvastaaaps aaaaadpyep ppprmqaarq qatsvndgag iatmtsnaap atsaapaapa
      301 evgtqiptta ltaaeaaafd aepppavaat sprspepapv qvlrastqsa pvsprtatad
      361 dpiarfangs y
//
LOCUS       WP_175912600             479 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [Burkholderia].
ACCESSION   WP_175912600
VERSION     WP_175912600.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..479
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50791
     Region          6..477
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mnelssrsea glsknavgls hivffvvaaa apltamvgat paafslgngp gvpgvfvlag
       61 vmylifsigy aamsrhisna gafyayiang lgrpvgvgga fvaivaynav qiaiycmfgf
      121 flnngvqqhy gidvpwwtfa lacvvavhfc garhiefsgr llgmlmigei aivmlldlai
      181 vvhgasaggf sakpfspamv ftpglgtalv fvlgsymgfe ataifseear dpkrtiprat
      241 ylavilimvf yalsswaive awgegqiaaq anrdpanlwf avsgrllgti atdamnvllv
      301 tslfaailsf hntitryfya mgrervlwrk lghtcpvhrc pdvagkvqtl ialaaiagsa
      361 afrldpfavv fswmsalati giiavqilva asviaffard hrdtslvhrl iaplvsvial
      421 gaclvlvvrn lsvlsgsdst fvamfpyfll aigalgiraa lrlkrsdpdl yrelgravq
//
LOCUS       WP_175912628             381 aa            linear   BCT 11-JAN-2025
DEFINITION  glycerate kinase [Burkholderia metallica].
ACCESSION   WP_175912628
VERSION     WP_175912628.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..381
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38506
     Region          10..376
                     /region_name="GlxK"
                     /note="Glycerate kinase [Carbohydrate transport and
                     metabolism]; COG1929"
                     /db_xref="CDD:441532"
ORIGIN      
        1 mpqhpsapvv viapdsfkgs lsaeqvadai atgirrarpd avvrccpmad ggegtldaml
       61 asggtrralr vagaslaard aavgvidart aivetaeivg itdpvgmsvp vdarstrgmg
      121 eairalldeg vrrffvalgg sstndagagl laglglqcfd aggqpvepvp srladiarid
      181 asgldarlke tefigmsdvd npltgdhgat avfgpqkgvt paqvatldaa larfadlvet
      241 aldrrgrdlp gagaagglgf alhmlgaqfe agaevvarqv gldaalagad wlitgegrsd
      301 vqtlhgkapf iacrharaag vpasllsgav dpaalprlse hfsgcfspap gpitldvair
      361 daanllanea eqltrlkyga h
//
LOCUS       WP_175912651             838 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia metallica].
ACCESSION   WP_175912651
VERSION     WP_175912651.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 838)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..838
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=90997
     Region          60..776
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mpiikrppss sdrnephytl rrspsgayyp dddgrdddhr trrsgggggr rsfgsrvalw
       61 fvglfatlai vgalivgyal vvmapqlpsl daltnyqpkv plrvftadhv ligefgeerr
      121 slvrfqeipd vmkkavlaie dyrfyehggv dfvgilragv adlmhggarq gastitmqva
      181 rnfflssekt ytrkiyemll aykiekaltk dqilelymnq iylgqrsygf aaaarvyfgk
      241 dlkditlaea amlaglpkap saynpvvnpk rakvrqeyil krmlevgyit qpqydeavke
      301 eihvrtpgnq yavhgeyvae mvrqmmyqqy kdetytrglt vtttinsadq eaayqavrrg
      361 ildyerrhgy rgpeasiklp aagddrdeai ddaladhpdn gdlqsavvls aspnavevqf
      421 vggatttigp aglrfvaaal gprandtlri kpgsvvrvlk dgktgwqvvq lpqvegalva
      481 iapqdgairs lvggfdfnks kfnhvtqawr qpgssfkpfi ysasldkglg patmindapl
      541 yfppsvpggt awepkdddqp dgpmtmrtgl qrsknlvsir ilasigtqya qqyvtqrfgf
      601 dpaktppylp malgaglvtp lqlatgyavf anggykvdpy liaevddarg qplqksqpvl
      661 agstaprtie grnayvmnsl lhsvatagtg agtnalgrsd lqgktgttnd akdgwfagyq
      721 qslvavawmg fdqpkslgsr efgaqlalpi wvnymrtaln gvpeqqmpmp dgltsidgel
      781 yyadrtpgng fvanvdinpa enaisandal gsagaaglap ppvtpqekqq imdmfenk
//
LOCUS       WP_175912675             331 aa            linear   BCT 11-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Burkholderia metallica].
ACCESSION   WP_175912675
VERSION     WP_175912675.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..331
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=34738
     Region          <13..324
                     /region_name="FAD_binding_2"
                     /note="FAD binding domain; cl46878"
                     /db_xref="CDD:481218"
     Region          48..74
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          79..109
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          114..136
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(224..225,228,231..232,255..256,259,262..263,266,
                     286..287,290,293..294,297,317..318,321,324..325)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          240..266
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          301..325
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mtvsssafpl pdvptadhaa lvarlaapda pvrrvallel adleapelvp sfiaalrddp
       61 sadvrseaar vlgaweqpdv vdalcralld pdehvraaaa qslselkdaa sgavlcgwtd
      121 rpepfvqgav lrglrelrdp dafapalral dahtaavrae avvvlgwlrd tralaplarv
      181 attdaeadvr raavgsigfa aaddaaaaaa llaalrdaaw qvreeaaatl gklriaaare
      241 plvaaldddy wqvrlraara lgqlrdaaaa pavaallsht isnlrkeaal algelrdrat
      301 lpalhaaled rdpevrkavr iairqiddap r
//
LOCUS       WP_175912685             144 aa            linear   BCT 11-JAN-2025
DEFINITION  NfeD family protein [Burkholderia metallica].
ACCESSION   WP_175912685
VERSION     WP_175912685.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Green,J.B., Lower,R.P. and Young,J.P.
  TITLE     The NfeD protein family and its conserved gene neighbours
            throughout prokaryotes: functional implications for stomatin-like
            proteins
  JOURNAL   J Mol Evol 69 (6), 657-667 (2009)
   PUBMED   20012272
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Kuwahara,Y., Ohno,A., Morii,T., Yokoyama,H., Matsui,I., Tochio,H.,
            Shirakawa,M. and Hiroaki,H.
  TITLE     The solution structure of the C-terminal domain of NfeD reveals a
            novel membrane-anchored OB-fold
  JOURNAL   Protein Sci 17 (11), 1915-1924 (2008)
   PUBMED   18687870
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..144
                     /product="NfeD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=15238
     Region          3..142
                     /region_name="YbbJ"
                     /note="Membrane protein implicated in regulation of
                     membrane protease activity [Posttranslational
                     modification, protein turnover, chaperones]; COG1585"
                     /db_xref="CDD:441193"
ORIGIN      
        1 mmsghlfwwi gggvlvvael ltgtfyllmi algffvggll qvagvaphvq fgaaaavaii
       61 amvvlrrsgl grkqkrdtst npdvnldiga tvtvdawrdg rarvqyrgad wdvelanger
      121 ddarvyqvsa vrgnclvvva kpag
//
LOCUS       WP_175912687             273 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Burkholderia metallica].
ACCESSION   WP_175912687
VERSION     WP_175912687.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..273
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28210
     Region          2..272
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mlktrvitai vmlavllpvt lfaplaafga ligvvlvfaa wewarllklg gagpvvyavv
       61 aalalaatap lgvdaaasrp lfmaagvfwl lvgpfalrrk pelaggiwrp fllaaglvvf
      121 aacwhalvsa raqgvpfvls lllvvwladi gayfagkafg krklaitisp gkswegaigg
      181 wlavmvvagi amaahafept lfsafaahyg mpgawaaltl lvvysvigdl fesllkrqag
      241 vkdssgllpg hggvldrvda llpvlplaml llg
//
LOCUS       WP_175912715             347 aa            linear   BCT 11-JAN-2025
DEFINITION  microcin C ABC transporter permease YejB [Burkholderia metallica].
ACCESSION   WP_175912715
VERSION     WP_175912715.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..347
                     /product="microcin C ABC transporter permease YejB"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042884 - microcin transport [Evidence
                     IEA]"
                     /calculated_mol_wt=38484
     Region          1..347
                     /region_name="YejB"
                     /note="ABC-type microcin C transport system, permease
                     component YejB [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4174"
                     /db_xref="CDD:443333"
ORIGIN      
        1 mwsyilkrll lmiptlvgvl tltfaviqfv pggpveqavq elrkgateqg avpfgmraht
       61 gvdaqqlaql kalygfdkpp lerywlmlkr farfdlgdsy frhqsvwslv vqklpvsisi
      121 glwtffltyl isvplgiaka vrngspfdva tslvvlvgya ipgfvlgvll lvlfgggsfw
      181 qifplrglts dnfaqlslvg kvldylwhia lpitasvvgs favvtmltkn afldeirkqy
      241 vltarargla ertvlwkhvf rnamlplivg fpaafigaff tgsllietlf sldglgllsy
      301 esvvrrdypv vlgtlylftl iglatklisd lcyvwvdpri qfdnler
//
LOCUS       WP_175912755             695 aa            linear   BCT 11-JAN-2025
DEFINITION  M3 family metallopeptidase [Burkholderia metallica].
ACCESSION   WP_175912755
VERSION     WP_175912755.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..695
                     /product="M3 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=76992
     Region          4..693
                     /region_name="Dcp"
                     /note="Zn-dependent oligopeptidase, M3 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0339"
                     /db_xref="CDD:440108"
ORIGIN      
        1 msasantnpl ldfsglprfg eirpehvtpa ldtlldaanr averasaaat patwadvvet
       61 vehateplgr awgivghlna vadtpelraa ygenlprvte fwssvgqnla lyekykaiaa
      121 saeyatlsae rkkildnalr dfrlsgaelp edrkprfael qeqqaalska fsdhvldatn
      181 ayayvvqdea elaglpgdai eaareaaqkd gkagwkftlh fpsyfpvlqy adnralretl
      241 yrayatrase lgpqygdgka ewdntkivid alklrreeaq mlgyrnfaev slapkmaesp
      301 qqviafledl atrarphadk dwdelrtfaa kelglaelap wdvayaaekl rqqryafsen
      361 evkqyfpepa alkglftvte tlfgvrikpd dapvwhkdvr ffrvenrdgs lvaqfyldly
      421 aregkrggaw mddarsrakr gssvqtpvay ltcnfsapvg gkpacfthde vitlfhefgh
      481 glhhmltrvd elgvsgingv ewdavelpsq fmenfcwewd vlssmsshvd tgaalprelf
      541 dkmiaaknfq sglgtlrqiv fsmfdmllhv dfdpagatdv tafareiner yhvipqaafs
      601 rwpntfshif aggyaagyys ykwaevlsad ayaafeeaaa asgsvldaat gtryrreile
      661 vggsrpamds fkafrgrepq idallrhngm tapah
//
LOCUS       WP_175912769             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia metallica].
ACCESSION   WP_175912769
VERSION     WP_175912769.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33210
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 melrqlryfv avaeelhfgr aakrlfisqp alsfdirkfe dalgvqlfsr anktvaltna
       61 gqvllgearr llmqaaeaer ltvrsasgla grlrigfvhs mlyrglpdav rrfeadypgv
      121 evvlsemnth aqvqaiqrgq idlgyahwgh fppdvesapv yaepfvcclp aahplvrrrq
      181 valaalaaep filfpreaap hyhdliiaqc vnagfspvir hearlwqtil smiefgmgia
      241 lvprvlqqvk serlafrplk daslesrtla lkrsgtaepv alrfadyvra sidalpalar
//
LOCUS       WP_175912777             268 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia metallica].
ACCESSION   WP_175912777
VERSION     WP_175912777.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..268
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=27976
     Region          9..247
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mharpivavt adrilrgahp nhtagekyla alvdgagvla fvlpalgarq padaivaavd
       61 gllftgsysn vephhyggta sapdtmhdpa rdatalplir aaieagvpvl aicrgmqeln
      121 vayggtlhqr lhattgfhdh rerpadpler qygpahvvqf apggllqrva rgaaqatvns
      181 lhnqgiarlg aglvveasap dglveavsvr garafalgvq whpewryaeq plsrdifaaf
      241 gaacrarmth rihaadgamp spaasdvd
//
LOCUS       WP_175912832             506 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Burkholderia metallica].
ACCESSION   WP_175912832
VERSION     WP_175912832.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..506
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53898
     Region          13..490
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(70,72,76,79,83,116,119..120,129..136,141,144,147,
                     240,244,247,250,252,426,428..429,431..432,435,438..439,
                     441,443..446,455,459,461,475,482..487,489..490)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(156..159,167,182,185,215,232..235,238,256..258,290,
                     391,393,419)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(159,256,287,290)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnpvpaytsd advghyvdga pvagrsgrfq dvlnpalgra vrrvaladds evqqavasah
       61 aafpawaetp pirrarvlhr flqlmnehrd alaaiitaeh gkvfsdaqge vargidiief
      121 acgvpqllkg dftdqvstgi dnwtmrqplg vvagitpfnf pcmvpcwmfp ialatgntfv
      181 lkpserdpsa alfiadlltq aglppgvfnv vqgdkgavda lldhpdvqav sfvgstpiaa
      241 yvqqravqsg krvqalggak nhlvvmpdan leqavdalig aaygsagerc maisvavlvg
      301 dvadkivplv aerarklvig dgmqpevemg pivtgdalkr iegyieqgvn egaqlvvdgr
      361 glrvagreag fftggtlfdh vtpemriyke eifgpvlgcv rvkdfgeavd linahefgng
      421 vscftsdggi arefarriqv gmvginvpip vpmawhgfgg wkkslfgdmh aygeegvrfy
      481 trqksvmqrw sssigkgaef amptak
//
LOCUS       WP_175912833             390 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia metallica].
ACCESSION   WP_175912833
VERSION     WP_175912833.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..390
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42768
     Region          12..282
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 midgqillgh sirwgmvggg lgsqigyshr saalrdgsfq llagafdldp ergrqfgvkl
       61 gvaaercypd yatmfdaear rpdgiravsi atpnnthfei craalnaglh vvcekplcft
      121 tdeaetlqrl sveknrivgv aygysghqmi eqaremiarg dlgeirivqm qfahgfhseg
      181 veaasaaarw rvdpkfagps yvlgdigthp lyisevmape lkirrlmcsr qsfvksrapl
      241 ednaftimey dtgavgyvws savnagsmhs qkvrvigska svewwdehpn qlryevqgqp
      301 aqvldrgmgy lhpaalredr igaghpeglf eawsnlyarf alamdaadrg daaalkniry
      361 pdvhagvegv rwvencvrsa daggvwvdyr
//
LOCUS       WP_175912839             311 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            metallica].
ACCESSION   WP_175912839
VERSION     WP_175912839.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..311
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=31546
     Region          1..309
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mhafalqafn glsyglllfm lsagltlifs vqgvlnfaha sfymlgayvg ysiaasagfw
       61 lalalaplav gllgagcera llrrvqargh tsellltfgl ayligegakl awglaplpap
      121 vpalfdgapv tvfglalpry rlfmmgmsaa mlvalgallr asrlglvvra althraavea
      181 lgydvprvmt alfgagtala alagvigapl aviepalaet vgsivfavvv igglgslgga
      241 faaslavgfa qtfaaasdts lrdltewagi alpdsvaavs vaqlaplvpy lllvavlvar
      301 prglfgerad a
//
LOCUS       WP_175912857             470 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatase PAP2/dual specificity phosphatase family protein
            [Burkholderia metallica].
ACCESSION   WP_175912857
VERSION     WP_175912857.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Pulido,R. and Lang,R.
  TITLE     Dual Specificity Phosphatases: From Molecular Mechanisms to
            Biological Function
  JOURNAL   Int J Mol Sci 20 (18), 4372 (2019)
   PUBMED   31489884
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Patterson,K.I., Brummer,T., O'Brien,P.M. and Daly,R.J.
  TITLE     Dual-specificity phosphatases: critical regulators with diverse
            cellular targets
  JOURNAL   Biochem J 418 (3), 475-489 (2009)
   PUBMED   19228121
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   4  (residues 1 to 470)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   5  (residues 1 to 470)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12932297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..470
                     /product="phosphatase PAP2/dual specificity phosphatase
                     family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=50463
     Region          45..219
                     /region_name="PAP2_Aur1_like"
                     /note="PAP2_like proteins, Aur1_like subfamily. Yeast
                     Aur1p or Ipc1p is necessary for the addition of inositol
                     phosphate to ceramide, an essential step in yeast
                     sphingolipid synthesis, and is the target of several
                     antifungal compounds such as aureobasidin; cd03386"
                     /db_xref="CDD:239481"
     Site            order(120,128,154..156,191,197,201)
                     /site_type="active"
                     /db_xref="CDD:239481"
     Region          323..460
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
ORIGIN      
        1 msalgggard laesapaaga garhasfalr vgwlavmgav ffstygfanw laarraavpt
       61 fafgwehaip fvpwtivpyw sidllyalsf ffwtrradll dhvkrlltvq lisvacfiaw
      121 plrfgferpd aggaagalft llmgfdkpfn qapslhigll vvlwavytkh vrgtlarvvl
      181 hlwfaaigvs vlttyqhhai dvptgaavgc lalflfplrd aagrlpgada spgaagrala
      241 rryalgaalm awaavwsvpr aqgwalaagw ialalacvaw ayrrgspgaf qkdaqgrfpv
      301 firwllapti agafvnsrlw tfrqpapvri dervsigrtp ttreirrhgf talvdltaem
      361 prwaaaeasl ayagvpqldl vaptaaqlaq avaalerlhg eghdvlvcca lgygrsvlca
      421 aawlamrrgl gdardalaav ravrphavws ddgvavlqhw idrrggvgrv
//
LOCUS       WP_175912953             146 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia metallica].
ACCESSION   WP_175912953
VERSION     WP_175912953.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..146
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=15366
     Region          1..146
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mrfmlngqpf dfdgdpatpl lwvirdaarl tgtkygcgig acgactvhld geaarscvlp
       61 aasvagravt tieglshdrs hpvqrawiek dvpqcgycqs gmvmaaaall arhrkptdaq
      121 idqavtnlcr catysrirga ihvaag
//
LOCUS       WP_175912948             397 aa            linear   BCT 11-JAN-2025
DEFINITION  ammonium transporter [Burkholderia metallica].
ACCESSION   WP_175912948
VERSION     WP_175912948.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..397
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41325
     Region          1..395
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mdglksgvdt lflligavmv lamhagfafl elgtvrkknq vnalvkilvd fsvstlayff
       61 igytiaygve ffddigtlsq hsgyalvrff flltfaaaip aivsggvaer akfnpqlvat
      121 liivgfiypf fegiawnerf gvqawlthaf gapfhdfags vvvhafggwv alpavlllga
      181 rhgryakdgr iaahppsnip flalgawvla vgwfgfnvms aqtldkisgl vavnslmamv
      241 ggtlaawmag rndpgftyng plaglvavca gsdvmhpiga lvtgaaagal fvamftcvqn
      301 kwriddvlgv wplhgmcgal gglaagvfgl palgglggvs flsqlvgtlg giaiataggt
      361 lvygalkatv glrldreaef dgadlsihri satpdrd
//
LOCUS       WP_175912956             497 aa            linear   BCT 11-JAN-2025
DEFINITION  HDOD domain-containing protein [Burkholderia metallica].
ACCESSION   WP_175912956
VERSION     WP_175912956.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..497
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=54384
     Region          18..216
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 msitehlprt alldklwarm nergdfplls eslratmaam knddldftal vrvvlsdfal
       61 tqkvlrlans amymafggni ttvtralmvl gmdavghlvv glklvdhfhh stprridakl
      121 elnrallsgc varklterae lrsgeeavvc tlmrqvgkll vvcyldsewd rirrraaeln
      181 gddaaacidv lgvgfdeigl eaaarwrlpd vicagmtdpd haartdafgn ddgdaghpae
      241 nepadrvrwl ravsrcstdv agalvmpasp qrdariaala qhygteldie sdalveiaer
      301 lareeasdtv mreivelran adaiaraqae peacleagla dlralpsehv ltpvlalase
      361 sllaglaftr tvmfvrhddg tfaarlgfgp gvdttlerlr fderfepdvf hlaitnsvgi
      421 fieqaqepkm lkrlpawyld afddtrafvl lpvrvgattv allygdwagp qparkitqqe
      481 msvlnalahe lgrffpa
//
LOCUS       WP_175912968             468 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia metallica].
ACCESSION   WP_175912968
VERSION     WP_175912968.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 468)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..468
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49411
     Region          <229..467
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mhtlmlalrn lqrnrrrslt tllamivgvs aillfggfsr ditlglqtdf vqrsghlqiq
       61 rqgyflygtg dpaaygirny palietlrrd pqlapllevv tptlqfggia gnfaagvsrt
      121 vmgfgavpdd qyrmqqwnay gfplrprafa lrgsaddaav vglgvarvlh lcgplhvpdc
      181 hdappgpaep aaagpdanap advlalarge agtqpagdga thvevltasa ggapnvgrfs
      241 vvkaeqqgvk elddvylavr lpqaqrlvyg gaaprataie lqlartadlp aararieqll
      301 hggfdgqpld vvdfatlnpf ydqtnrmfsv ifgfvfvlis aivlfvisnt mstaiiertv
      361 eigtlramgm rrggiqalfv cegallgvag aslgvlvala iaaavnhsgl awtpparida
      421 valtvrvwge wrtiavtfag lacvaglsaw lpsrhaarls ivdalrhv
//
LOCUS       WP_175913017             386 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia metallica].
ACCESSION   WP_175913017
VERSION     WP_175913017.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..386
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39938
     Region          12..359
                     /region_name="MFS_YcaD_like"
                     /note="YcaD and similar transporters of the Major
                     Facilitator Superfamily; cd17477"
                     /db_xref="CDD:341030"
     Site            order(19..20,23..24,27,59,109..110,112..114,117,137,
                     140..141,144,214,217..218,221..223,226,250,254,304..305,
                     309,313,329,332..333,336..337,340)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341030"
ORIGIN      
        1 mkailnrdfl alilsvavvg lgtgatlplt alalteaghg tnvvgmltaa qalgglaivp
       61 fvtalarhig arraivvsvv llaaatalmq ftsdlilwga lrvlcgaalm llftigeawv
      121 nqladdatrg rvvaiyatnf tlfqmagpvl vsqiagatgi rfalcgalfl lalptlatir
      181 raplagddah heahgrwldv lprmpaliig tgffalfdtl alsllplyam dhgvasatav
      241 llasimlfgd tamqfpigwl adrlgrervh lgagwivlag lpllpfvian pwlcwpllfv
      301 lgaaagsiyt lslvacgerf rgaalvtass lvsaswsaas fggplvagal meqlgshalv
      361 gvlvvcvaaf vaaalwerra alqrav
//
LOCUS       WP_175913046             222 aa            linear   BCT 11-JAN-2025
DEFINITION  acyltransferase [Burkholderia metallica].
ACCESSION   WP_175913046
VERSION     WP_175913046.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..222
                     /product="acyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /calculated_mol_wt=23659
     Region          99..217
                     /region_name="WbbJ"
                     /note="Acetyltransferase, isoleucine patch superfamily
                     [General function prediction only]; COG0110"
                     /db_xref="CDD:439880"
ORIGIN      
        1 mfsafkkrli drlaaavahr lgdrlapsld vladrlagpv adrlwqqpaf rgrldevera
       61 vreraavepv dddawadrla pllaqrlatt pvlfggdwsr vetgenvhlv ntllnvssgr
      121 isigeqtffg hnvslitgth dlasvmadrh dyprdgrdiv igkgvwiasn aivlgpcaig
      181 dhaviaagav vtggqlesgc lyagvpakrv ktligeesad dq
//
LOCUS       WP_175913117             264 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Burkholderia metallica].
ACCESSION   WP_175913117
VERSION     WP_175913117.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..264
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28104
     Region          25..264
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mqrrfmlkfa aalgaaalfa sahaqaetik vgvtggphaq imeavkkvaa ksgldirive
       61 fsdyvqpnaa lasgdldans yqhdpylqaq vkdrgyklik vadtvtfpmg iyskrvksla
      121 elkpgariav pndptnggra llllqkqgll klradvglka tpldivdnpr klkiveldaa
      181 qiprslgdvd aaaintnyam eaglkpkqda iaiegpngpy anilairdad rnkpwvaklv
      241 aayhsadvkq fiegkfggav iaaw
//
LOCUS       WP_175913131             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia metallica].
ACCESSION   WP_175913131
VERSION     WP_175913131.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32474
     Region          3..61
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          90..287
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(105..106,108..109,112,116,118..124,217..222,
                     228..229,231..232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 melrqlryfv svvehgsmgk aalelgivts alsqqisrle selstrllqr tstgvmptda
       61 glafwrqaql alrhiddaav aarqarlsgh vsvglapstt gvlglafmqa mrerypdvrl
      121 rmveslsgyl gamlgarqid lailfreepa qrwsvlplld erlfvigtat lpgmpersrt
      181 siaklsalpl ilpsgthglr alldaafkra gyvpsiaaev dglamlmdav rgglgatiqp
      241 gaalaraena sltsvplvda yatrpnlias vsdeelspag laarvvladv arhtvnagrw
      301 pgaklr
//
LOCUS       WP_175913147             343 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia metallica].
ACCESSION   WP_175913147
VERSION     WP_175913147.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..343
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37573
     Region          67..270
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 makdtskdkk ptgnlhlaag llrglaqena aletrlpepa aapdvvgets pttvpsaatp
       61 tasqdlgapq kvlvkdcipn pfnprvfyse sslhelaltl kregqiepik vtrlpefpgk
      121 lvvidgqrrl ratsingdet inatfrtdht peqlytiayr anhdherqti fddavawkrl
      181 ldekvfsdqn tlaekigkdk asisktlsln alpntllerm asasdvvglq aayflklife
      241 rlgeptadrl laavidrkks vrdlenflra qsdgskkagr trysvrhdfa lesraigqlk
      301 typdgrvdlq lkgvdashqe aladklktvi dayvaelatt tqq
//
LOCUS       WP_175913164             344 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia metallica].
ACCESSION   WP_175913164
VERSION     WP_175913164.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..344
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36238
     Region          109..316
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mkivkpllia aavaaalsav paafaagtea arpdtttsaf laalngqkgp gletlspaka
       61 rqvlvdaqng tkvdlsgvdv snrtieqdgv svpvtivrpq gttgtlpvfm fihgggwvlg
      121 dfptherlvr dlvvqsgava vfvnytpspe ahypvainqa yaatkwvaah gdqigvdgsr
      181 lavvgnsvgg nmaavvalma kdkggpairf qglmwpvtdh nfntgsynay qqghfltrpm
      241 mrwfwdaytk neaqrneiya splrastaql kglppaliqv aqfdvlrdeg eaygrkldaa
      301 gvdatttryd gtihdfglln alasdaptka atkamaneia trlk
//
LOCUS       WP_175913166             241 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia metallica].
ACCESSION   WP_175913166
VERSION     WP_175913166.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..241
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25982
     Region          10..235
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mievraanqr graehgwlss rhtfsfanyy dpkqvgfsdl lvinddrvap grgfgthphr
       61 dmeilsyvld galehkdsmg tgsvivpgdv qlmsagtgvr hsefnhsqet pvhflqiwvg
      121 paekgaepry qqtnvaaddk rgklalvvsp ngdagslkir qdtriyaglf dgaesatlal
      181 dpgrfayvhv argsvtvngv tlgegdgari rgeqaltfad gkdaevlvfd lrpvevtaew
      241 a
//
LOCUS       WP_175913199             302 aa            linear   BCT 11-JAN-2025
DEFINITION  S1C family serine protease [Burkholderia metallica].
ACCESSION   WP_175913199
VERSION     WP_175913199.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..302
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=32624
     Region          <215..300
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mkrvfaltav latsllaapa alaqekaspp vytwlserfp envrydspvl tvgdsglsaa
       61 qgivnaqltl iqspqgndsm lglavafhta ekqyfntvrd ygkfgtrfrq pkipvaiptl
      121 ngggyadten wspaadggkt wpvnggvfim ldrlylktye vsgtnlvlsl sdydapdnaf
      181 riripaayls rflagvpndl hlvppdmlnq pttfgvyfve mddqelaalk vpggavrieg
      241 vlpgavadra glknydllmr fgdrplkrma dlanavhatp kgtvvpltvw rdatevklqa
      301 qf
//
LOCUS       WP_175913194             258 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia metallica].
ACCESSION   WP_175913194
VERSION     WP_175913194.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10606006
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..258
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29178
     Region          90..232
                     /region_name="Methyltransf_23"
                     /note="Methyltransferase domain; pfam13489"
                     /db_xref="CDD:404385"
ORIGIN      
        1 mnhdlnrhpt vlackvcsge apicglvdfs scgadymagk kvdpyagvpv yyhacrqcgf
       61 twapmfdswt hddfaqhvyn adyvrhdpey leirpqqlad lictsfpdmr dsrvldfgsg
      121 lgllerklls rgftdvtsyd pfshpvppeg tfdtilsfev fehhpapidl fdqimryrkp
      181 ggallfqttp itqdildsgi aqwwycvprn ghisfytpqa ltllaqrhgl eygafspslh
      241 vvferaatpr wldrflkp
//
LOCUS       WP_175913232             236 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia metallica].
ACCESSION   WP_175913232
VERSION     WP_175913232.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..236
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25552
     Region          7..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mttatltpvl elrdvtrvye gagrvvavrg atisigrrdv valvgpsgsg kstllnlagf
       61 ldvpstgerw legrriddap dtlerirrer igfvfqqfnl ipvmsalenv elgcfawgtp
      121 rtrreraram ldavglaare rhrpgelsgg eqqrvalara lakepaivia deptasldst
      181 naravaelil dtnrtlgtaf liashddrlc ahlprriemr dgvpgvnrel vdvcva
//
LOCUS       WP_175913219             450 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter large permease [Burkholderia metallica].
ACCESSION   WP_175913219
VERSION     WP_175913219.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..450
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47396
     Region          1..446
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 melailsvsf liflvlgvpv sfalgiacvl tylveglpia tamqamisgm nafsflavpf
       61 fifsgelmlh ggiadrilrf aqatvghfrg glgmanvvac tlfggvsgsp tadtsamggv
      121 viplmkregy saayavnvtt haslagalmp tstnmiiyaf aaqgitgmlh gqpvsgvsig
      181 dllfsgllpv lwvmgfvlaa aywqavrhgy prredgssal pafpgwyavl rsfvgavpgl
      241 mviaiilvcv akgiatatea aaiavvyslv ltavvyrtlt aqklrralsh aarttgvvll
      301 liavsnmlrf qmsyleipda iegllkqsta apwlmllyin iiqvflgtfv dmaahilitt
      361 plflpiamac gvgpvqfgim lllncslglv hppigsvqfv gcaignvsig ettkmawpyy
      421 laifsainiv tympffstwl pslisghavf
//
LOCUS       WP_175913277             722 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia metallica].
ACCESSION   WP_175913277
VERSION     WP_175913277.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..722
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77255
     Region          39..722
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mvtgtgaarr akaiaaggal yvaatggaha qaagaaaavl paidvtvnad gassglvglr
       61 tragtktdtp vadipqtvnl vtaqqiemtg atdlnqilry vpgfatfgad srtdwyaalr
      121 gftptlyvdg vaapntavia nwrvdpytid siavlrgpts vlygagepga ivdahtklad
      181 gervreagvq lgndarkqfm vdvgdaldpd gryayrfvgv ardgnavtgp ngdrrvalap
      241 sfrwrpnadt sltlsatflq dsgdissnfl pasgtvlpnp ngrvsqdvym gapgfndyrk
      301 kqwslgyale hrvnaiwslh qdvrwshlsl ddatvfgngl aprsttdmmr vaglfqlnys
      361 rldvdnraqa rfgtgpleht lllgvqydrq tttnsvwlal apslnlyhpv yrpvtaaifs
      421 gptslghvdq ytamntigvy aqdqirwkrw tltlggredf vnarfddrta gthaqqdvsa
      481 fsgrvgltyq gdaglspyvs hstsfdpvvg vrmwgggvpk ptrgtqteag lrwqppgrnl
      541 mlsaavyqid qtnvvtpapv nldptgttsv qtgkvrsrgi elsavgkitr elsvvasfmh
      601 qdvknvqand aslnhwpvav plprqmasmw adwtwragml sglgvgggvr yqsaaagapd
      661 nsltvpsvtl vdlalhyemp hwrfalnvan lldrryvsgc tsyavcvfgn ertvlasaky
      721 nw
//
LOCUS       WP_175913283             405 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Burkholderia
            metallica].
ACCESSION   WP_175913283
VERSION     WP_175913283.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..405
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43385
     Region          38..403
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(103..105,129,179,211,240,242..243,251)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(106,139,204,249..251,280,283)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            243
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mtvsadvlnr flaearpsat ymvmdrvaar rgsgaaaisl sagepdfdtp ehireagiaa
       61 iraghtrytq vaglralrea iaakfqreng lnvewrdtlv cnggkqvifn alaatlnegd
      121 evvvpapywv sypeivqlcg aksvivpcga ergfkltada lqaaitqrtr wlilnspsnp
      181 tgavysrael lalaevllah pgvlvlsddi yehlifdgie fctlaqvepr lrdrvltmng
      241 vskayamtgw rigfgtgpgw lieameklqg qqtsgastis qhaavaaltg pqdfiqrsri
      301 afqrrrdlvi erlaeapglh cavpqgafyv fascedligk ttragvrlds detvvnalld
      361 dagvatvhgs afglgpyiri ayalddksla racaairdfc atlad
//
LOCUS       WP_175913320             481 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia metallica].
ACCESSION   WP_175913320
VERSION     WP_175913320.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..481
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50970
     Region          1..427
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfaslglie pllrnlqdln yqaptpvqak aipavlggkd vmagaqtgtg ktagfalpll
       61 qrlvqhgpav ssnrarvlvl vptrelaeqv lqsfvaygkg fdlrmlaayg gvsinpqmmk
      121 lrkgvdvlva tpgrlldlnr qnavqfdqve tlvldeadrm ldlgfareld avfaalpaqr
      181 qtllfsatfs ddiramaani lrapvnisvs ppnataskik qwvvtvdkrn kpdlfmhlva
      241 enkwthalvf vktrngvdyl aamldeagya vdtihgdkpq parlralerf kagevqmlva
      301 tdvaargldi ddlplvinvd lpivaqdyvh rigrtgraga sgvavslvca deapqlaaie
      361 alirqtlrre eepgfeaehr vpetsatgqi ikkpkkpkkp kvpqaasgam pvsgkkprpq
      421 ggenkrkgaa pragaagkga nvpggspfga qkprgkpagk paagarkpag kpaggrgkrp
      481 a
//
LOCUS       WP_175913335             253 aa            linear   BCT 11-JAN-2025
DEFINITION  O-methyltransferase [Burkholderia metallica].
ACCESSION   WP_175913335
VERSION     WP_175913335.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..253
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27672
     Region          78..238
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 maspalallq rlhdesrtei vararaqfqg snedflslad eyeaiaprlr grfletlglf
       61 tddfespags plslavspet ggflrnmvls qrparilelg sscgvstlyf adalrtlgrg
      121 tvvaterdal kcarlrehvr tagldayvdv regdvfetva aldgafdmvf idvwadtylt
      181 vfkaverllr pgsvvladnm ytaedavrpy kryldddprf stttldfesg ieftvvvsea
      241 gmasqrschs apd
//
LOCUS       WP_175913322             281 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia metallica].
ACCESSION   WP_175913322
VERSION     WP_175913322.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..281
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30158
     Region          10..257
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(24,105,107,109..110,138,189,210,213,226,228,257)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mstvtfphqq vgdftitais dgyltasldf lsnidsdnaa smqrdagqta paavhincyv
       61 vraagrtili dggaggfrqw ggrllanlal agiepaaidt illthahpdh vgglvndaaq
      121 iafpnaelva hrrevafwqd dgnlsraser argnfvkare vfdayrdrlr vfddgqvlpg
      181 ihalplpght dghtgyvves rdqgllvwgd vvhfphiqiq rpdvsiafdh daslavatra
      241 rlldqvsadg lliagmhlge pgfariertr ggyalryase t
//
LOCUS       WP_175913369             749 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia metallica].
ACCESSION   WP_175913369
VERSION     WP_175913369.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 749)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..749
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81207
     Region          55..749
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mkkveqrkme watgtrlrai aaaasvafga aaghayaqta pavnagaaap assaqngaaa
       61 gtstgtlpti nvnaasdgdg tvglvakrsr tgtktntsin eipqtinvvt aqqiemtgat
      121 dvnaalryvp gfssygsdnr sdwyaalrgf tptayvnglq vpntinlasw rvdpymidsi
      181 svlrgptsvl ygagdpgaiv dvqtkladge rvreagvqig nyarkqfmid vgdkldpdgk
      241 yayrfvgvar dgnaltgpnn dqrvalapsf rwrpdadtsl tlsatylqdw gdissnflpa
      301 vgtvlpnpng qinkdvyegd pnfnyyrkkq wsvgyqfern ltpawtfrqn trlmhlsldn
      361 gsvfgngfvd gsttdvsrwa gvfqmnysrf didnnlegrf atgplqhtll lgfqynrqta
      421 tdsewlaaap plniynpvyq pvttavftpd stfrtntytt mntfglyaqd qikwnrwtlt
      481 lggredwvnm rmddraggts tkadvtaftg rvgltyqgdy glspyvsyat sfnpligvnl
      541 lggglpqptr gkqieaglrw qppgknlmln aaiyqinqtn vltnalpdqd ptgtksvqag
      601 evrsrgiels atgkvtrnls viasyvyqdv knvkandvsl nnwpvdiprp rqmaslwtdw
      661 twhtgpltgf glgggiryqs asagaadnsl tvssvtlfda gvhydtrnwr favngtnlfn
      721 rhyisgcqsa nvcvfgtdrt viatakynw
//
LOCUS       WP_175913422             139 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia metallica].
ACCESSION   WP_175913422
VERSION     WP_175913422.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..139
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15566
     Region          19..>96
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(20..22,36,53..55)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mtttvekvvl ppipakryft igevselcgv kphvlryweq eftqlrpvkr rgnrryyqhh
       61 evllirrire llyeqgftin garnrldspg gergaaahal veheaqaada rapgksgtav
      121 dvtalrqall dvidglkrd
//
LOCUS       WP_175913427             162 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Burkholderia
            metallica].
ACCESSION   WP_175913427
VERSION     WP_175913427.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..>162
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
     Region          25..>162
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mtpaslieqy gpresmeydv vivgggpagl saairlkqla aekgteigvc vlekgseiga
       61 hilsgavmdp raitelfpdw kergapldve vtedrflfls ekgavttpnw alpanfqnhg
      121 nyvislgnvt rwlgaqaeal gveifpgfpa aeilynddgs vk
//
LOCUS       WP_175913473             687 aa            linear   BCT 11-JAN-2025
DEFINITION  YSIRK-type signal peptide-containing protein, partial
            [Streptococcus sp. 646].
ACCESSION   WP_175913473
VERSION     WP_175913473.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. 646
  ORGANISM  Streptococcus sp. 646
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Bai,Q., Ma,J., Zhang,Z., Zhong,X., Pan,Z., Zhu,Y., Zhang,Y., Wu,Z.,
            Liu,G. and Yao,H.
  TITLE     YSIRK-G/S-directed translocation is required for Streptococcus suis
            to deliver diverse cell wall anchoring effectors contributing to
            bacterial pathogenicity
  JOURNAL   Virulence 11 (1), 1539-1556 (2020)
   PUBMED   33138686
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Yu,W., Missiakas,D. and Schneewind,O.
  TITLE     Septal secretion of protein A in Staphylococcus aureus requires
            SecA and lipoteichoic acid synthesis
  JOURNAL   Elife 7, e34092 (2018)
   PUBMED   29757141
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 687)
  AUTHORS   DeDent,A., Bae,T., Missiakas,D.M. and Schneewind,O.
  TITLE     Signal peptides direct surface proteins to two distinct envelope
            locations of Staphylococcus aureus
  JOURNAL   EMBO J 27 (20), 2656-2668 (2008)
   PUBMED   18800056
REFERENCE   4  (residues 1 to 687)
  AUTHORS   Carlsson,F., Stalhammar-Carlemalm,M., Flardh,K., Sandin,C.,
            Carlemalm,E. and Lindahl,G.
  TITLE     Signal sequence directs localized secretion of bacterial surface
            proteins
  JOURNAL   Nature 442 (7105), 943-946 (2006)
   PUBMED   16929299
REFERENCE   5  (residues 1 to 687)
  AUTHORS   Bae,T. and Schneewind,O.
  TITLE     The YSIRK-G/S motif of staphylococcal protein A and its role in
            efficiency of signal peptide processing
  JOURNAL   J Bacteriol 185 (9), 2910-2919 (2003)
   PUBMED   12700270
REFERENCE   6  (residues 1 to 687)
  AUTHORS   Tettelin,H., Nelson,K.E., Paulsen,I.T., Eisen,J.A., Read,T.D.,
            Peterson,S., Heidelberg,J., DeBoy,R.T., Haft,D.H., Dodson,R.J.,
            Durkin,A.S., Gwinn,M., Kolonay,J.F., Nelson,W.C., Peterson,J.D.,
            Umayam,L.A., White,O., Salzberg,S.L., Lewis,M.R., Radune,D.,
            Holtzapple,E., Khouri,H., Wolf,A.M., Utterback,T.R., Hansen,C.L.,
            McDonald,L.A., Feldblyum,T.V., Angiuoli,S., Dickinson,T.,
            Hickey,E.K., Holt,I.E., Loftus,B.J., Yang,F., Smith,H.O.,
            Venter,J.C., Dougherty,B.A., Morrison,D.A., Hollingshead,S.K. and
            Fraser,C.M.
  TITLE     Complete genome sequence of a virulent isolate of Streptococcus
            pneumoniae
  JOURNAL   Science 293 (5529), 498-506 (2001)
   PUBMED   11463916
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01168.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Streptococcus sp. 646"
                     /db_xref="taxon:2582660"
     Protein         1..>687
                     /product="YSIRK-type signal peptide-containing protein"
                     /note="The YSIRK form of extended signal peptide directs
                     nascent proteins to the cross-wall site, while signal
                     peptides lacking YSIRK direct proteins instead to the cell
                     pole. A large fraction of YSIRK proteins are surface
                     proteins anchored by sortase-mediated processing of a
                     C-terminal LPXTG motif."
     Region          6..46
                     /region_name="YSIRK_signal"
                     /note="Gram-positive signal peptide, YSIRK family;
                     TIGR01168"
                     /db_xref="CDD:273479"
     Region          10..>153
                     /region_name="endo_SpGH101"
                     /note="SpGH101 family
                     endo-alpha-N-acetylgalactosaminidase; NF040533"
                     /db_xref="CDD:439743"
ORIGIN      
        1 mfykgnedre krlrfsirkv sfgaasvava alfmfpgngt vsateqgvtp tneetqgssl
       61 kdpdvqngty gatpvvsqld gnsgtseasa pkgqeetstp tstdasapsv esptvskeqe
      121 etsttasate eksaekntev psteansven keqarvktee tsttsaatte skktksrkkr
      181 disatpdadv atddpsanqt ytppsadasv nqlakalqdl pdkvenndkl sknmenlgas
      241 knvsagqvle idefggwkav gengkfviar ktadgvfple tinstlddtv wlteqafdrt
      301 sdytlllsks rtranmtdvv adgstyrerg egtgitknvv nfqgiekvfk aystelgtnv
      361 vvkfktgyag dsegkkanyk vevfsiagtt etkvyettfd pqknskdndk vvtkasdgtn
      421 nsriristts nsfvlgqtkt rqgfigkeaa ekkiaepgnv pkgtpgtfts rniellkgve
      481 kykvrislan qnetgmsyqa wdlkyslpit gvdftitqdt nkvaksllqr vydklketee
      541 adtkgktett inaykaqlek vknllegnlk atqdykklat dvlmekaalr tdksglttsk
      601 qtitdlidet peptsgktps svraytaake eakkaqvaaq svldkdnpss develaiskl
      661 nekiaelkla rselvtaatd dqkdels
//
LOCUS       WP_175913474             536 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia metallica].
ACCESSION   WP_175913474
VERSION     WP_175913474.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..536
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53468
     Region          31..436
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(31,34..35,38,70,120..121,123..125,128,148,151..152,
                     155,279,282..283,286..288,291,319,323,375..376,380,384,
                     400,403..404,407..408,411)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mdlpfsadsa vsarrrawvl aavclaaval plsfsggava tpaigrdlhg gtvamnwitn
       61 afmlafgsfl maagaladqf grkrlfaigv ggftlmsgal afapsmlavd llrgaqglaa
      121 aaalaggtaa laqefdgaar trafsllgtt fgiglafgpv lagalighyg wraifvtsav
      181 agvlslgvgl prmhesrdph aagldwpgta afttaltlft fgvieaparg wssalviall
      241 agaalgacaf vaietrvarp mldlslfria rfvgvqvlpv stcccyivll vvlplrfigi
      301 dgfseigagw lmlaisapml vvplvaatlt rwlsagvisg lgllvaaagl vwlgialrgg
      361 agpaaiapml aigvgagmpw glmdglsvsv vpkeragmat gifsttrvag egialaivga
      421 vlaglaragl tqaagadgtp datlraaarl atgdlagaaa alpgvghaal lasyahafdr
      481 lliglavvtv lcagvvfafl grrvadeagd dtaalahadr papgrieaaa aqthgr
//
LOCUS       WP_175913490             235 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia metallica].
ACCESSION   WP_175913490
VERSION     WP_175913490.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Upton,C. and Buckley,J.T.
  TITLE     A new family of lipolytic enzymes?
  JOURNAL   Trends Biochem Sci 20 (5), 178-179 (1995)
   PUBMED   7610479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..235
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=24821
     Region          43..215
                     /region_name="FeeA_FeeB_like"
                     /note="SGNH_hydrolase subfamily, FeeA, FeeB and similar
                     esterases/lipases. FeeA and FeeB are part of a
                     biosynthetic gene cluster and may participate in the
                     biosynthesis of long-chain N-acyltyrosines by providing
                     saturated and unsaturated fatty acids, which it...;
                     cd01836"
                     /db_xref="CDD:238874"
     Site            order(53,90,118,209,212)
                     /site_type="active"
                     /db_xref="CDD:238874"
     Site            order(53,209,212)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238874"
     Site            order(53,74,118)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238874"
ORIGIN      
        1 mgypfatatl gpllfaqgry vrrvtprlpe aagprdgvag dgpplrvlvv gdsaaagvgv
       61 atqrdalsgq lanalaathr vswkllartg lttrelvdwl aaepaepfdv avtslgvndv
      121 tggvpperwq aqqaelvrll aarfrvghti lsavppmerf palpqplawy lglrakrlnt
      181 alagwaatqp hctflrvelp lerhlmaadg fhpgatacav waaqvaaavq rrvva
//
LOCUS       WP_175913530             405 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia metallica].
ACCESSION   WP_175913530
VERSION     WP_175913530.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..405
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40599
     Region          32..399
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(42..43,46..47,50,82,132..133,135..137,140,159,
                     162..163,166,234,237..238,241..243,246,274,278,327..328,
                     332,336,352,355..356,359..360,363)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 msessspess spfaappdah rvlslparqr artasmalff vagmmyaswg vhvptvrdkf
       61 alspgllsia lfavaggsia amltiarwia rvgsrtaclv gglvmsacaa lilvvpdywm
      121 llavlalfgf smatldvamn aeasaveial gkpimsslhg mfsiggmsga aaggallsag
      181 mapaahlala aavsaavlva aspavlphvp hheqahgggn rwrspalwml ggialialia
      241 egamydwatv ymrdvvaasp alasaayaaf sggmaaarfa gdavrarfga pqlvfasasl
      301 acagmigall lpnpaavlig ftmmglglan mmpvlfaaaa rvkgihaaeg lahvaglayf
      361 gllfgpvvig avaqaanltt glsvvalcaa lvaiiapkvl ahlki
//
LOCUS       WP_175913559             422 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia metallica].
ACCESSION   WP_175913559
VERSION     WP_175913559.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..422
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=43762
     Region          206..414
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(213,253,291,394,397)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(213,394,397)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(213,253,291)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 msfrssiaaa vlgavvfvsp laasasaapa gwvaawatal qpipdlaapp plyrapdvag
       61 ravrqivypt vsgraarirv snaygraplv veaaslarag dgaalggaav pirfagktsv
      121 tlapgqeves dpvaidvaag rpyavtlqmg anqrmtvwhr vsnqfnyvss pgdhvsdpga
      181 aafrtrftqy awvtelavea gsarasvaai gdsitdglrs svnrnrrwpd alarrltvsg
      241 vesigvanlg isgnrllsds acygtslasr ferdalsrag vkaaivligi ndinfaampp
      301 ragldcdhph tqvtaaslid gyrrlidaah rqgvkifgat ltpaglpagr eairlevnrw
      361 irsgsgfdgv vdfdavlrdp arpsvlqrry dsgdgihpsd agytamadav pveqlqaaag
      421 gk
//
LOCUS       WP_175913565             240 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Streptococcus sp. 646].
ACCESSION   WP_175913565
VERSION     WP_175913565.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. 646
  ORGANISM  Streptococcus sp. 646
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Streptococcus sp. 646"
                     /db_xref="taxon:2582660"
     Protein         1..240
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26742
     Region          1..233
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mirienlsvs yketlalkni slvlqgptit giigpngagk stllkgmlgi iphqgqafld
       61 dkevkkslhr iayveqkini dynfpikvke cvslglypsi plfralkakh wkkveealei
      121 igladyaerq isqlsggqfq rvliarclvq eadyilldep fvgidsvsee iimntlrdlk
      181 kagktvlivh hdlskvphyf dqvllvnrev iafgpiketf teanlkeayg nrlffnggdl
//
LOCUS       WP_175913609             324 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia metallica].
ACCESSION   WP_175913609
VERSION     WP_175913609.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..324
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33389
     Region          40..322
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          219..322
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(224..225,258..259,262,266..267,270,312,316)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 myrtiharra rlsatlsaal saalspavaa laaaglfasg aafaqntgat vtpvgngtva
       61 ttalpssnpn agaasgtvvr gtagtitppp anatpgqvva sgkvpdeatk aavlqklrdt
      121 ygaanvvdqi evgdvatppn wsanvqkllg aqlkqiskgq lkingtqiem kgevhneaqr
      181 qqlasdmant lnptytirng lrvsaseqgv ldqtlanrti efetgsatlt pqgklildqm
      241 aaalakmqnr tvdiightdn sgnrtsnial sqaradavkg ylitknippq qmtttgvgpd
      301 qpiapndtad grarnrrief rvgq
//
LOCUS       WP_175913626             234 aa            linear   BCT 11-JAN-2025
DEFINITION  MIP/aquaporin family protein [Streptococcus sp. 646].
ACCESSION   WP_175913626
VERSION     WP_175913626.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. 646
  ORGANISM  Streptococcus sp. 646
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Streptococcus sp. 646"
                     /db_xref="taxon:2582660"
     Protein         1..234
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24171
     Region          1..234
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mmselfgefl gtlilillgn gvvagvvlpk tksnssgwiv itmgwgiava vavfvsgkls
       61 pahlnpavti gvalkgglpw asvlpyilaq fagamlgqil vwlqfkphye veenagnila
      121 tfstgpaikd tvsnliseil gtfvlvltif alglydlqag igtfavgtli vgiglslggt
      181 tgyalnpard lgprimhsil pisnkgdgdw syawipvvgp vigaalavlv fslf
//
LOCUS       WP_175913654             308 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia metallica].
ACCESSION   WP_175913654
VERSION     WP_175913654.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..308
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33963
     Region          4..223
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msaieirhvk krykslqalk gvslsveege ffgllgpnga gkttlisila glaradegsi
       61 svrghdvvkd frgarralgv vpqelvfdpf ftvretlrlq sgyfglrrnd dwidevmanl
      121 dltekadanm ralsggmkrr vlvaqalvhr ppvivldept agvdvelrqt lwkfisrlnr
      181 eghtivltth yleeaeslcd riamlrrgev valdrtdall rrfaglqlyl rfaagalpae
      241 lrglesdpaa rasgehllrl tsyddveril aqcraagcaf deievrkadl edvfvqvmng
      301 aeviegla
//
LOCUS       WP_175913709             250 aa            linear   BCT 11-JAN-2025
DEFINITION  HesA/MoeB/ThiF family protein [Burkholderia metallica].
ACCESSION   WP_175913709
VERSION     WP_175913709.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..250
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26468
     Region          2..248
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mnddqllrys rhilvdeigi eaqqrfldah aivvgagglg spaamylaas gvgtitlvda
       61 dtvdltnlqr qilhvtasvg rskvesgrdt laqlnpdvqv navaarvdda wldthvppat
      121 vvldctdnfa trhainracv ahgvplvsga alrfdgqist fdfrdaaapc yacvfpedqp
      181 feevacatmg vfaptvgiig amqaaealrv iggigktlng rlmmldslrm ewttmkiarq
      241 adcpvcggrh
//
LOCUS       WP_175913672             549 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Streptococcus sp. 646].
ACCESSION   WP_175913672
VERSION     WP_175913672.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. 646
  ORGANISM  Streptococcus sp. 646
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 549)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 549)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Streptococcus sp. 646"
                     /db_xref="taxon:2582660"
     Protein         1..549
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=63831
     Region          104..522
                     /region_name="YesM"
                     /note="Sensor histidine kinase YesM [Signal transduction
                     mechanisms]; COG2972"
                     /db_xref="CDD:442211"
ORIGIN      
        1 mshsfkkslq keilhrssia afvtslllli llfgfsyflq kqqlskdtrq ivkqvqemke
       61 annellttmn hkmilgfldg khterevfsl fyetkaklkl ssdliilsdt gellfstnrn
      121 hqesilspyy lklliqnpsq dkvtekials sdkqhytlfi kpllqnqrvk aytiafvnen
      181 dfissfpmin skyiitdsfg nmfsnntnqf trstlekfde kllhsrthwy aneplivqke
      241 kvgaifsiyt fqsffpipsl lglasvltlc ifflyfwqar riahkiathn avpieslvyq
      301 lqeipkqaek rlslqtgdef efmaekinnm lyeldqlhqk mltiekekwi ferkmleaqf
      361 nphflyntle tikitsltda altqdliqnl trilrysvtd leketticqd lkiiedylmi
      421 hkirfehfsy divcpetvdn qpipklfllp lvenaikygm qyridlhidi qitlesdslt
      481 flvkdnaggl tkqerlaild slesphtqhg ivnsykrlsn ffsdvqldlg vnrqgetwvk
      541 fitkglthv
//
LOCUS       WP_175913772             212 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia metallica].
ACCESSION   WP_175913772
VERSION     WP_175913772.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..212
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23093
     Region          4..195
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mnayrlylsp gacslaahia leetgapfdv eivsvrqqqn learylaina karvpvlaip
       61 geprvltetp ailtylarrh pdaqllplgd plrearchew lawlvgwvhg vgygalwrpg
      121 rfigdpalhg avsthgrgvi eaandtieaa ladgrmwaep gahsivdpfl fvlyrwgvai
      181 gldmtrhpaw tahaqreaer paarralare aa
//
LOCUS       WP_175913789             397 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia metallica].
ACCESSION   WP_175913789
VERSION     WP_175913789.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..397
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=42131
     Region          18..382
                     /region_name="MidA"
                     /note="SAM-dependent methyltransferase, MidA family
                     [General function prediction only]; COG1565"
                     /db_xref="CDD:441173"
ORIGIN      
        1 mnpkahepas lpapgpdala qsetlaaqlr deiaaaggwl pfdrfmeral yapglgyysg
       61 garkfgrrad dgsdfvtape lsplfaqtla qpvaqalaas gtrcvmefga gtgklaagll
      121 aaldalgvel daylivdlsg elrerqrdti aaaapalaak vrwldalper fdgvvvgnev
      181 ldampvrlfa kaggawherg valdarhafv fddrpaapas lppvlagldd ahdgyvteth
      241 eaalaftrtv ctmlgrgavl lvdygfpahe yyhpqrdrgt lmchyrhhah ddpflypglq
      301 ditahveftg iyeaavatga dllgytsqar fllnagitda laaidpsdfh aflpaanavq
      361 kliseaemge lfkviafsrg idgtldafar gdrshal
//
LOCUS       WP_175913809             402 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ATP-binding protein [Streptococcus].
ACCESSION   WP_175913809
VERSION     WP_175913809.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus
  ORGANISM  Streptococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Miller,J.M. and Enemark,E.J.
  TITLE     Fundamental Characteristics of AAA+ Protein Family Structure and
            Function
  JOURNAL   Archaea 2016, 9294307 (2016)
   PUBMED   27703410
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Streptococcus"
                     /db_xref="taxon:1301"
     Protein         1..402
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=46914
     Region          1..400
                     /region_name="COG1373"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440984"
ORIGIN      
        1 mnyikrphyl dflrrhrdrq iikvvsgvrr agksvlfqly keellatgvd edqiisinfe
       61 dlsyyelrhf qtlfayikeq ligektyyif ldeiqhvekf elvadslfil pnvdlyftgs
      121 nayfmssqla tnltgryvei evlplsfeey lsgqsltknl ntteifnnyl fsafpyllqt
      181 ssyaekidyl rgiynsilln divtrlgnpn ptiierivrt llsstgslis tnkirntlvs
      241 qnvsishntl enylttltds llfysvprfd vksrallqrl ekyypvdlgl rhlllpdhke
      301 dighilenmv ylelrrrysq vyvgnldkye vdfvvvtdlg hyayyqvset tlapetlere
      361 lrpleaikdq fpkylltmdt iqptanyngi ekkniidwll ek
//
LOCUS       WP_175913814             560 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Streptococcus sp. 646].
ACCESSION   WP_175913814
VERSION     WP_175913814.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. 646
  ORGANISM  Streptococcus sp. 646
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 560)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 560)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Streptococcus sp. 646"
                     /db_xref="taxon:2582660"
     Protein         1..560
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62714
     Region          3..527
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mkeaiiewkd fsfqyetqqe ptlqgidlti ykgekvlivg psgsgkstlg qclngiipni
       61 ykgqtygefl ikgqvafdvs iydkshlvst vlqdtdgqfi glsvaedlaf alendvtald
      121 emkgrvykwa ekldllplld qrpqdlsggq kqrvslagvl idespillfd eplanldpks
      181 gqdiielidq ihkeegtttl iiehrledvl hrpvdrivli ndgrilfngs pdqllatdll
      241 tqngireply lttlrqlgvd lvkeeqlanl dnlsiskgqv qlrtelvket pelqslfrle
      301 dvsfsyddrl ilkslhldik kgekiaivgk ngagkstlak alssfiqteg rylwegqdik
      361 gdsvaeraer vgyvlqnpnq mistnmifde valglrlrgv dekeietrvy etlkicglye
      421 frnwpisals fgqkkrvtia silvlgaeii lldeptagqd qknyteimef leelhqkght
      481 ivmithdmql mldysdrvlv mvdgeliadt vpasllsdpe llvkanlket sifnlakkld
      541 vdpldltafy kerregckln
//
LOCUS       WP_175913835             319 aa            linear   BCT 11-JAN-2025
DEFINITION  complex I NDUFA9 subunit family protein [Burkholderia metallica].
ACCESSION   WP_175913835
VERSION     WP_175913835.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Parey,K., Wirth,C., Vonck,J. and Zickermann,V.
  TITLE     Respiratory complex I - structure, mechanism and evolution
  JOURNAL   Curr Opin Struct Biol 63, 1-9 (2020)
   PUBMED   32058886
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Babot,M., Birch,A., Labarbuta,P. and Galkin,A.
  TITLE     Characterisation of the active/de-active transition of
            mitochondrial complex I
  JOURNAL   Biochim Biophys Acta 1837 (7), 1083-1092 (2014)
   PUBMED   24569053
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..319
                     /product="complex I NDUFA9 subunit family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0010257 - NADH dehydrogenase complex
                     assembly [Evidence IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=33876
     Region          5..278
                     /region_name="NDUFA9_like_SDR_a"
                     /note="NADH dehydrogenase (ubiquinone) 1 alpha subcomplex,
                     subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs;
                     cd05271"
                     /db_xref="CDD:187579"
     Site            order(10,12..15,34..36,74..76,93,116..118,129,133,
                     156..159)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187579"
     Site            order(129,133)
                     /site_type="active"
                     /db_xref="CDD:187579"
ORIGIN      
        1 mdrqtvallg gtgfigsrlv nalidagkqv riatrrrdha rhlqmlpvei veldaldtrt
       61 larfvagaha ainlvgvlhg grgtpygpgf erahvalpaa latactqvgv qrvlhmsalg
      121 adshgasmyq rskgdgeaal haiaatdsla ltifrpsvvf gpgdaflntf anlqrtvpvl
      181 plampdarfq pvfvgdvvra fvntldlaaa hgktyelggp tvytleqlvr ycgtlvgrqa
      241 rivrlpdala rvqasvfecl pgepvltrdn lasmsvpnvl sgplapelgi tpaslesiap
      301 aylghaaqrs rfdwfrsrr
//
LOCUS       WP_175913887             449 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Streptococcus sp. 646].
ACCESSION   WP_175913887
VERSION     WP_175913887.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. 646
  ORGANISM  Streptococcus sp. 646
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 449)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 449)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Streptococcus sp. 646"
                     /db_xref="taxon:2582660"
     Protein         1..449
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=51739
     Region          62..422
                     /region_name="CitA"
                     /note="Sensor histidine kinase DipB regulating
                     citrate/malate metabolism [Signal transduction
                     mechanisms]; COG3290"
                     /db_xref="CDD:442519"
ORIGIN      
        1 mniawillya lvingleivi ffkvdgiglt fdrifkafll kfllgiiftt fqflavskyl
       61 syfieplfgi glsflllrgl pkkilifygl fpmilvelfy rgvsyfvlpf lgqgivdgdg
      121 npifllimif vcfivlvflk cldydftrlr refldtgfqk sltkinwamg ayylvmqsls
      181 yleyeqgiqs ttvrhlilvf yllffmggik kldtylkekl qeelnqeqtl ryrdmerysr
      241 hieelykeir sfrhdytnll tslrlgieee dmeqikeiyd svlrdssqkl qdnkydlgrl
      301 vnirdcalks llagkfikar eknivfnvev peeiqvegms lldfltivsi lcdnaieasa
      361 easqphvsia flkngaqetf iiensikeeg idiseifsfg asskgeergv glytvmkive
      421 shpntnlntt cqnqvfrqvl tihsmsvdd
//
LOCUS       WP_175914020             361 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia metallica].
ACCESSION   WP_175914020
VERSION     WP_175914020.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..361
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38749
     Region          14..355
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mtsnpadfdl vrgprriavf ralqlgdmlc avpalralrh gepdaritli glpwarefas
       61 rfsdyidgfi afpgapglde qpvpdaaare afvaecrard fdlaiqlhgs gthtnaivas
      121 lgatrtagfm padggatpld ctlvwrdgep evaryltlmr klgyaergdf lefplggldd
      181 alwqvlcdeh alepgryviv hpgarmasrr wpverfalaa rqladedwqi vltgtraema
      241 lagafaehla rpcvnlcgrt plgalaalig rarlllcndt gvarvaaalg tpsvvvacgs
      301 dttrwappdg erhrvlanyp acrpcmfdtc phghecatai gvgdvierag ellaqearhv
      361 t
//
LOCUS       WP_175914101             662 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Streptococcus].
ACCESSION   WP_175914101
VERSION     WP_175914101.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus
  ORGANISM  Streptococcus
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 662)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 662)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 662)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10496603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Streptococcus"
                     /db_xref="taxon:1301"
     Protein         1..662
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=74362
     Region          60..182
                     /region_name="FtsX"
                     /note="FtsX-like permease family; pfam02687"
                     /db_xref="CDD:460652"
     Region          543..655
                     /region_name="FtsX"
                     /note="FtsX-like permease family; pfam02687"
                     /db_xref="CDD:460652"
ORIGIN      
        1 mfrltnklav snliknrkly ypfalavlla vtvtylfysl tfnpkiaeir ggttiqatlg
       61 fgmfvvtlas aiivlyansf vmknrskelg iygmlglekr hlismtfkel vvfgiltvga
      121 gigigalfdk lifafllklm klkvelvatf qmnvviavlv vfgliflglm flnalriarm
      181 nalqlsreka sgekrgrflp lqtilgsisl gigyylaltv tdpltalttf flavllvifg
      241 tyllfnagit vflqilkknk kyyyqpnnli svsnlifrmk knavglatia ilstmvlvtm
      301 saatsifnsa esfkkvlnph dfgvsgqnve kedldkllsq fasdkgykik ekevirytyf
      361 gvanqegnkl tlfekgqnrv qpttvfmvfd qkdyenmtgq klslsgnevg lfaknegvke
      421 qktltlndhq fsvkeefnkd fivnhvpnqf niltadynyl vvpnlqafld qfpdsaiynq
      481 fyggmnvsis eeeqlkvaee yekyldqfna qlntegsyvy gstladasaq msalfggvff
      541 igiflsiifm vgtvlviyyk qisegyedre rfiilqkvgl dqkqikqtin kqvltvfflp
      601 llfafihlaf ayhmlslilk vigvidttmm livtlsicai fliayvlifm itsrsyrkiv
      661 qm
//
LOCUS       WP_175914129             556 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia metallica].
ACCESSION   WP_175914129
VERSION     WP_175914129.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..556
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=60321
     Region          20..529
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mnqqfdyivv gggsggsvva grltedpnts vclleaggrg dgpvinipag mvamlptrln
       61 nwafktvpqr gldgrvgyqp rgkalggssa inamvyirgh rsdydtwaal gnpgwsydev
      121 lpyfrlsehn eriddawhgk dgplwvsdlr sdnpfqarfl aaarqaglpl tddfngaqqe
      181 gvgiyqvtqk egerwsaarg yllphigkra nlavetraqv rrilfdgkra vgvevlqhgt
      241 lktfrarrev vlaagalqtp qllmlsgvgp adelarvgid tlhalpgvgr nlqdhpdfil
      301 syrtrsldtm gvsvggsvrm lreilrfrre rrgmltsnfa eggaflktqp glaapdiqlh
      361 flialvddha rrmhlghgls chvcllrprs rgsvtllsrd padaplidpa flddprdled
      421 mvagfkitrg lmeapalaew itkdmftrdv hsddeirsvl rartdtvyhp vgtcrmgqda
      481 lavvdpqlrv hgldglrivd asvmptligg ntnaptimia ekavdmmrgv srvasashga
      541 aaqthpltts gietgr
//
LOCUS       WP_175914192             106 aa            linear   BCT 11-JAN-2025
DEFINITION  PadR family transcriptional regulator [Streptococcus sp. 646].
ACCESSION   WP_175914192
VERSION     WP_175914192.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. 646
  ORGANISM  Streptococcus sp. 646
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Streptococcus sp. 646"
                     /db_xref="taxon:2582660"
     Protein         1..106
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12096
     Region          3..100
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mketqllkgv legcvldmig qkerygyelv qtlreaefdt ivpgtiypll qkleknqwir
       61 gdmcpspdgp drkyfsltke geervsvfwq qwddlsqkve gikngg
//
LOCUS       WP_175914165              75 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein, partial [Streptococcus
            sp. 646].
ACCESSION   WP_175914165
VERSION     WP_175914165.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. 646
  ORGANISM  Streptococcus sp. 646
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 75)
  AUTHORS   Munoz-Lopez,M. and Garcia-Perez,J.L.
  TITLE     DNA transposons: nature and applications in genomics
  JOURNAL   Curr Genomics 11 (2), 115-128 (2010)
   PUBMED   20885819
REFERENCE   2  (residues 1 to 75)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 75)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465738
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Streptococcus sp. 646"
                     /db_xref="taxon:2582660"
     Protein         1..>75
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
     Region          4..>75
                     /region_name="Csa3"
                     /note="CRISPR-associated protein Csa3, CARF domain
                     [Defense mechanisms]; COG3415"
                     /db_xref="CDD:442641"
ORIGIN      
        1 mkstkeeiqt iktllkdsst akyhkrlqiv lfrlmgksyk eiielldcnq ttiwptvkky
       61 eefgldsllq etrgg
//
LOCUS       WP_175914222             304 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia metallica].
ACCESSION   WP_175914222
VERSION     WP_175914222.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33897
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdqfkevqlf vevaetgsis raaeavdlsi saasrylisl esrlgvqlvr rttrnlflte
       61 agaefhrrck siladlgeae lvvkdamarp sgvlkvtasl sfcmlhiapm lpeftarype
      121 itvdvvaanr yydiiengid vavrtkvlea dsnitvrrla strrvlaaap rylaangtpr
      181 fpaelgkhkl lnygladnpr dlafqrdgec vlvkvkplle sndgqilrva aldgmgilvq
      241 pkyiiyddlk agrlvpvlde wdlprltmni afqtrshmpv kvrlfidalv erfrgndfer
      301 lwte
//
LOCUS       WP_175914251             321 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia metallica].
ACCESSION   WP_175914251
VERSION     WP_175914251.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..321
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34560
     Region          11..224
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(52..53,55,69..71,77,79..80,121,223)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(52,54..55)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(77,80,83,90)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(113,117..120,122)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(118..119,142..144,196..197)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          237..321
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 msaatltvrv arkwqeardi cgfefvsddg splprfdaga hidvhlpggl vrqyslcnhp
       61 ehgdryqiav lrepdgrggs raihdeirqg dtvqigvprn qfalapdaph hlllaggigv
      121 tpilcmaerl fssgaafdmh ycarstdrma fveridaagf rdrtrlhvdd gapeqrfdva
      181 avlaaapegt hlyvcgprgf mdavlnaare rgwaddrlhy effggavass gsdrafqvri
      241 assgqvidvp aectviaala angvdvltsc eqgvcgtcvt rvlqgepdhr dayltddeka
      301 agdqfmpccs rarsdllvld l
//
LOCUS       WP_175914258             294 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Streptococcus sp. 646].
ACCESSION   WP_175914258
VERSION     WP_175914258.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. 646
  ORGANISM  Streptococcus sp. 646
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 294)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Streptococcus sp. 646"
                     /db_xref="taxon:2582660"
     Protein         1..294
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33201
     Region          4..225
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mnmikvesln knikgkailk disfevaege cvaligpnga gkttlldcll gdklvtsgqv
       61 siqdlsvtss qldyirgylp qenvivqklk vieliaffqs iypnplsnqe idqllqfdqh
      121 qkeqfaekls ggqkrlfsfv ltligrpklv fldeptaamd tstrqrfwei vqdlkakgvt
      181 ilysshyide ventadrilv lnkgelirdt tplamrseei ekhfilplay kevieqsnlv
      241 enwsqkqdal qvvtreadaf wqllvragcr iqeievnnrs lldtifeetq kgdd
//
LOCUS       WP_175914260             245 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Streptococcus sp. 646].
ACCESSION   WP_175914260
VERSION     WP_175914260.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. 646
  ORGANISM  Streptococcus sp. 646
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Streptococcus sp. 646"
                     /db_xref="taxon:2582660"
     Protein         1..245
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27237
     Region          54..238
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mkqwialnki eflltkrqlv yyllsvgmpt afylffsgmy qdtpgepanf mrdylismta
       61 fsmmstamfs fpavlhtdki nnwqktlrht pvnmvkyyls kitsmmvdyl vsilvvfsvg
      121 hlvrgvdmpl gswigaalll ivgsvafval gltltllpss qlmsvvgnll ylglavlggl
      181 wmpislfpdw mqavgkclpt yqlmellktf lnegginlsa tvyllvfsvv lfgltiylqg
      241 hkena
//
LOCUS       WP_175914275             282 aa            linear   BCT 11-JAN-2025
DEFINITION  YSIRK-type signal peptide-containing protein, partial
            [Streptococcus sp. 646].
ACCESSION   WP_175914275
VERSION     WP_175914275.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus sp. 646
  ORGANISM  Streptococcus sp. 646
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Streptococcaceae; Streptococcus.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Bai,Q., Ma,J., Zhang,Z., Zhong,X., Pan,Z., Zhu,Y., Zhang,Y., Wu,Z.,
            Liu,G. and Yao,H.
  TITLE     YSIRK-G/S-directed translocation is required for Streptococcus suis
            to deliver diverse cell wall anchoring effectors contributing to
            bacterial pathogenicity
  JOURNAL   Virulence 11 (1), 1539-1556 (2020)
   PUBMED   33138686
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Yu,W., Missiakas,D. and Schneewind,O.
  TITLE     Septal secretion of protein A in Staphylococcus aureus requires
            SecA and lipoteichoic acid synthesis
  JOURNAL   Elife 7, e34092 (2018)
   PUBMED   29757141
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 282)
  AUTHORS   DeDent,A., Bae,T., Missiakas,D.M. and Schneewind,O.
  TITLE     Signal peptides direct surface proteins to two distinct envelope
            locations of Staphylococcus aureus
  JOURNAL   EMBO J 27 (20), 2656-2668 (2008)
   PUBMED   18800056
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Carlsson,F., Stalhammar-Carlemalm,M., Flardh,K., Sandin,C.,
            Carlemalm,E. and Lindahl,G.
  TITLE     Signal sequence directs localized secretion of bacterial surface
            proteins
  JOURNAL   Nature 442 (7105), 943-946 (2006)
   PUBMED   16929299
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Bae,T. and Schneewind,O.
  TITLE     The YSIRK-G/S motif of staphylococcal protein A and its role in
            efficiency of signal peptide processing
  JOURNAL   J Bacteriol 185 (9), 2910-2919 (2003)
   PUBMED   12700270
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Tettelin,H., Nelson,K.E., Paulsen,I.T., Eisen,J.A., Read,T.D.,
            Peterson,S., Heidelberg,J., DeBoy,R.T., Haft,D.H., Dodson,R.J.,
            Durkin,A.S., Gwinn,M., Kolonay,J.F., Nelson,W.C., Peterson,J.D.,
            Umayam,L.A., White,O., Salzberg,S.L., Lewis,M.R., Radune,D.,
            Holtzapple,E., Khouri,H., Wolf,A.M., Utterback,T.R., Hansen,C.L.,
            McDonald,L.A., Feldblyum,T.V., Angiuoli,S., Dickinson,T.,
            Hickey,E.K., Holt,I.E., Loftus,B.J., Yang,F., Smith,H.O.,
            Venter,J.C., Dougherty,B.A., Morrison,D.A., Hollingshead,S.K. and
            Fraser,C.M.
  TITLE     Complete genome sequence of a virulent isolate of Streptococcus
            pneumoniae
  JOURNAL   Science 293 (5529), 498-506 (2001)
   PUBMED   11463916
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01168.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Streptococcus sp. 646"
                     /db_xref="taxon:2582660"
     Protein         1..>282
                     /product="YSIRK-type signal peptide-containing protein"
                     /note="The YSIRK form of extended signal peptide directs
                     nascent proteins to the cross-wall site, while signal
                     peptides lacking YSIRK direct proteins instead to the cell
                     pole. A large fraction of YSIRK proteins are surface
                     proteins anchored by sortase-mediated processing of a
                     C-terminal LPXTG motif."
     Region          8..42
                     /region_name="YSIRK_signal"
                     /note="Gram-positive signal peptide, YSIRK family;
                     TIGR01168"
                     /db_xref="CDD:273479"
     Region          17..85
                     /region_name="AlphaC_N"
                     /note="Alpha C protein N terminal; pfam08829"
                     /db_xref="CDD:462613"
     Region          248..268
                     /region_name="TSP3_bac"
                     /note="Bacterial TSP3 repeat; pfam18884"
                     /db_xref="CDD:465899"
ORIGIN      
        1 mlkliqnkkk ggekafrysl rkfkfgaasv lvglaflglg sqkvyahyia ddniiylgds
       61 kseanaarqt mkirteisrg gthvkytiif ndnyelwrrp glnvwlpegl reetitiktf
      121 tsagvtgggg kefrlkndln ltnfksptre llkpphrggn kanwdkfwtn vtstgsgsei
      181 atkwkdqnll sfglnswenr shnaykweie adakngvvls qlpilagmen wdngypryvl
      241 sgpdetadtd gdgfpdvvek dagsdpndkn stpdnvdtdk dg
//
LOCUS       WP_175914291             252 aa            linear   BCT 11-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Burkholderia
            metallica].
ACCESSION   WP_175914291
VERSION     WP_175914291.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..252
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26986
     Region          1..251
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlaeqrhqyi lselgrsgal svaelvrsld vsretvrrdl nalaargllv mthggalaad
       61 rrepslsere aanadakrti grraaefvpd dasvlidsgs tphavalala drhrlsiytn
      121 dwrtafvlar rngnrvtllg gelsddedat fgldtiqqla qyhvdfafig aggitpdgec
      181 tdysrlaaev rsrmiaaagt aiivadhskf grvtpvring aaaarylvte rapdkavrra
      241 ltargiellv ca
//
LOCUS       WP_175914313             403 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia metallica].
ACCESSION   WP_175914313
VERSION     WP_175914313.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..403
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=42445
     Region          10..403
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 msmrtppret rfawrgrrrd gvarrgivia fdaasarsal ardgvavlsl dvrgparppt
       61 agardvtrft rqlasllqag lplapsleml artrpydglp riaaglarei vggrrfadal
      121 arypaqfgtl yrqlievgea sgslgvvltr vaehrerada qwrklraala ypaavilfgl
      181 aisaalmvwv vptfrqifdg fgaalpaptr allalssvls awggvlvagt vaaglaahra
      241 lrrsaplrha varhllrapl agdaltrfat arwcrslatl lgagvplada fatlertagh
      301 pvferatahi aarvlhgarl adamqaagcf pddvvqpiav aeetgaldtm ladiaalcer
      361 qldarldala algepliviv lgalvgglvi amylpilqlg nvv
//
LOCUS       WP_175914314             425 aa            linear   BCT 11-JAN-2025
DEFINITION  GspE/PulE family protein [Burkholderia metallica].
ACCESSION   WP_175914314
VERSION     WP_175914314.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..425
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=44941
     Region          <36..415
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mhfpppgaqa rtqplpthsd assapapral daaqlddapa vrlltdtlha arvrdasdih
       61 iepfeagwri rlridgvlhe hvrpplhlrd alvtrikvla rmdiaerrlp qdgrlriaid
      121 ggtrgdyrvs slptlfgekl vlrrletlpp dltlarlgfd arqaatveaa iraphglvlv
      181 tgptgsgktl slycalqmld rdghnvctve dpaeiqldgi sqvgvaekag ltfatalral
      241 lrqdpdilmv geirdaetad vaikaaqtgh lvlstlhtnd apaavarlld igvapynlaa
      301 alhlvtaqrl vrrlctacra psdapepvlr eagcdpaala agwrpfvarg csachgigyr
      361 griglhqtmp vssglaeriv arasvgelaq caaaegvrsl rdaalarvhd gttsiaeala
      421 atpaa
//
LOCUS       WP_175914317             312 aa            linear   BCT 11-JAN-2025
DEFINITION  carbohydrate kinase family protein [Burkholderia metallica].
ACCESSION   WP_175914317
VERSION     WP_175914317.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..312
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33743
     Region          4..290
                     /region_name="ribokinase_group_A"
                     /note="Ribokinase-like subgroup A. Found in bacteria and
                     archaea, this subgroup is part of the ribokinase/pfkB
                     superfamily. Its oligomerization state is unknown at this
                     time; cd01942"
                     /db_xref="CDD:238917"
     Site            order(52,250,253)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238917"
     Site            order(192,220,248,251..252,255,277,280)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238917"
ORIGIN      
        1 matlicgsia ydsimtfegr frehilpdqv hlinlsflvp tmrrefggca gniayalhll
       61 ggdarmmgtv galdaqpyld rldqlglrrd hvrvlpetyt aqamittdld nnqiaafhpg
      121 ammqshlnha gdapdiklai vgpdgfdgmv qhveelarag vpfvfdpgqg lplfdgatlr
      181 rsielatyva vndyeaklvs dktgwsedei asrvdalvit rgehgatirh kqgseqipvv
      241 aaeriadptg cgdafrggll ygiehgldwa ttgrlaslmg sikiahqgpq tyvltraeid
      301 arfetafgys lk
//
LOCUS       WP_175914343             521 aa            linear   BCT 11-JAN-2025
DEFINITION  S41 family peptidase [Burkholderia metallica].
ACCESSION   WP_175914343
VERSION     WP_175914343.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..521
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55657
     Region          73..424
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mmpptravlr lavraavmaa llpgvssada qqpasappas apasapasap aapaaprpps
       61 pcpsdwepqi celkaavevl krqhltdvdi galldattha giktlpyarf fdpkeeqerr
      121 ederrardgt pgigivfetr pdglhivdvi pdapaekagv rpddlvvamn dtsvvgidaa
      181 dlarlakgda gvplkltvqr grshavlsfa pvrtilkphp atakrldgdi lytrlssfpe
      241 pavgdyidav qaarragppv kglildlrin gggalnaaig italfagrdr tamvtvergd
      301 anrrryttnw pdyalpvmhe qdplaplqad dwwrtvplvv lvdgqsasaa eataaalkdl
      361 grakllgmpt ygkglaqtgv dlidgtrlnf tfarnlrpng cpmdgygvvp dwlvpprrds
      421 didgvllwyr eadlprapya drlapdpfak vrkerqklre qralakidta ksaalpqref
      481 gtaadwqlaq alaalagrhv qtiapnpqlm parpvcerag n
//
LOCUS       WP_175914427              67 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Burkholderiaceae].
ACCESSION   WP_175914427
VERSION     WP_175914427.1
KEYWORDS    RefSeq.
SOURCE      Burkholderiaceae
  ORGANISM  Burkholderiaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Burkholderiaceae"
                     /db_xref="taxon:119060"
     Protein         1..67
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7215
     Region          1..66
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mdtgtvkwfn dskgfgfitp daggddlfah fsevrgdgfk tltenqkvsy etkrgpkgmq
       61 asnispq
//
LOCUS       WP_175914469             216 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-mobile-trio protein GmtX [Burkholderia metallica].
ACCESSION   WP_175914469
VERSION     WP_175914469.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Mahata,T., Kanarek,K., Goren,M.G., Marimuthu Ragavan,R., Bosis,E.,
            Qimron,U. and Salomon,D.
  TITLE     Gamma-Mobile-Trio systems are mobile elements rich in bacterial
            defensive and offensive tools
  JOURNAL   Nat Microbiol 9 (12), 3268-3283 (2024)
   PUBMED   39443754
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Hurley,C.C., Quirke,A., Reen,F.J. and Boyd,E.F.
  TITLE     Four genomic islands that mark post-1995 pandemic Vibrio
            parahaemolyticus isolates
  JOURNAL   BMC Genomics 7, 104 (2006)
   PUBMED   16672049
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF040692.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     gene            1..216
                     /gene="gmtX"
     Protein         1..216
                     /product="gamma-mobile-trio protein GmtX"
                     /calculated_mol_wt=23581
     Region          9..215
                     /region_name="recomb_assoc"
                     /note="gamma-mobile-trio protein GmtX; NF040692"
                     /db_xref="CDD:468656"
ORIGIN      
        1 mtidhpdavl ntllakggra hrrtnltamh eicrkqhesg srdfslptig rlaesagilk
       61 rrvlynaqsa dyrallnawa thagelppas kplasheylm rihdpairsi mqaiiverdk
      121 lkaevnllka ntqvivdrrp sgvhvsgtlt spsvmpfgnt epltpserea lqkaisaahl
      181 eelglregth geivnergrt vfdigfarai rkvlag
//
LOCUS       WP_175914553             492 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA recombination protein RmuC [Burkholderia metallica].
ACCESSION   WP_175914553
VERSION     WP_175914553.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..492
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=53950
     Region          <35..>189
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     Region          154..478
                     /region_name="RmuC"
                     /note="DNA anti-recombination protein (rearrangement
                     mutator) RmuC [Replication, recombination and repair];
                     COG1322"
                     /db_xref="CDD:440933"
ORIGIN      
        1 mtmtlllaav vvlavalava ivvlvrgggr hddtavlgdq iedaahaqar averlerelr
       61 geivesargs rtelagsfsq lqqmlaaqlt svatvqnnqi egfaqqlgkl vagnaqqfda
      121 mreslqrqaq qardeqtgal rlfgdtlhrq ltqlteandr rigevratle qrlkeietnn
      181 aakleemrrt vdeklhatle qrlgesfklv sdrleqvhrg lgemqtlaag vgdlkkvltn
      241 vktrgtwgev qlealleqml tpeqyaknva tvpksserve fairlpgrda gtrdappvwl
      301 pidakfpred yerlidaqer adavaveeaa ralearvrle artiaekyvs pphttdfall
      361 flpteglyae ilrrpgltdl lqrdyrvtva gpttltalln slqmgfrtla ieqrssevwq
      421 vlgavktefg kfgdvlartk aqletvtrsi esaeqrtrvm srklkqveal pgdtaagllg
      481 aegadgadad da
//
LOCUS       WP_175914556             299 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia metallica].
ACCESSION   WP_175914556
VERSION     WP_175914556.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 299)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..299
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32569
     Region          18..149
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          215..296
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msaarlpdsa rywrtpllpd adlltatyrd htfaphwhda ytipvilega erytyrgsah
       61 vaetgsvpvi npgevhtgsr aadegwcyrv syipvefire ltnaiadrpq dapwfapdvi
      121 rdadlaarlt lahrmmeags eralgaqahg qpandspgda priydplaae tamldalstl
      181 ivrhadalpr aaplaadepr vdamrerlaa dllcpvtlde vaqaaglspf haarlftrtt
      241 gmpphawrnq lrlqralapl ragvpvadva aasgfvdqsh ftrhfkrmfg vppgrwqas
//
LOCUS       WP_175914568             308 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Burkholderia metallica].
ACCESSION   WP_175914568
VERSION     WP_175914568.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..308
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32194
     Region          7..272
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(34..35,38,90,103,105,134,167,253,256)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 maaalpeila lgeamiefnq sqpgrpeflq gfggdtsnfc iaaarqgast gfvsaigddp
       61 fgrlladmwh aehvdtsyvr idrtaptgvy fvthgaeghq fdylragsaa sryavgdlpl
      121 dglaaakavh lsgislaist aacdaafaai dharrngakv sfdtnlrlkl wplpraravm
      181 realrqtdic lpswddvtal tgandrdaiv damlehgpri valklgkega yvatpderrv
      241 vpgfaveavd atgagdcfgg afvarivagd dpfaaaryan aaaalsttgy gavapiphrd
      301 averlmqg
//
LOCUS       WP_175914570             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia metallica].
ACCESSION   WP_175914570
VERSION     WP_175914570.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13300132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33648
     Region          39..>154
                     /region_name="PRK11242"
                     /note="DNA-binding transcriptional regulator CynR;
                     Provisional"
                     /db_xref="CDD:183051"
     Region          103..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(113,117,156,170,172,231,248,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(114..115,119..120,122..123,126,130,132..138,199,
                     225..229,236..237,240)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 masdpipapd kpldlldval fvraallanv saagrefgvs aavasariaq lerqlgarll
       61 hrttrrislt qdgevfmtha dtllsaadaa rasvghgrte pygrlkvsms ssfgrqhvap
      121 vipaflrryp svsldlrlsd eivdlvddgy dvairlgmlk dstlvarkla anrrvlccsp
      181 aylaehgtpr hpaelaqhec vilgdqrdws fatpqgpltv rvggrlvasn geairealvd
      241 gfgiaikstw dvgpllasgt lvtvlddypf addiaiwavy psrahvplkt lafiaflaeh
      301 fgdppywdra agr
//
LOCUS       WP_175914610            1048 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia metallica].
ACCESSION   WP_175914610
VERSION     WP_175914610.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..1048
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114662
     Region          11..1027
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msvsyeegrf nlsawalrhq alvvyliala tlagilaytr laqsedppft frvmvvrtfw
       61 pgasarqvqe qvtdrigrkl qetpaidflr sysrpgesli fftmkdsapv kdvpetwyqi
      121 rkkvgdigyt lppgvqgpff ndefgdvytn iwtlegdgft paqlhdyadq lrtvllrvpg
      181 vgkvdyfgdp eqrifievnn aqltrlgisp qqlgqainaq ndissagvlt saddrvfvrp
      241 sgqfdnvdai adtliringr tfrlgdlatv krgyddpavt qmranghavl gigvtmqpgg
      301 dvirlgnald aeskdlqaql paglkltlvs smphavahsv ddfleavaea vaivlvvslv
      361 slglrtgmvv visipvvlav talfmylfdi glhkvslgtl vlalgllvdd aiiavemmav
      421 kleqgytrar aaafaytsta fpmltgtlvt vsgflpiala ksstgeytrs ifevsaiali
      481 aswfaavvli pllgyhllpe rkrhaheahl pddhehdiyd trfyrrlrgw vdwcierrfv
      541 vllitgalfv valmgfslvp qqffpssdrp ellvdlrlpe gasfaatlre terlekvidk
      601 rpeidhsvnf vgsgaprfyl pldqqlqlpn faqfvitaks vkdreklatw lettlreqfp
      661 avrwrlsrle ngppvgypvq frvsgdsiat vrsiaekvaa tmrgdtrtvn vqfdwdepae
      721 rsvrfeidqk karelnvtsq dvssflamtl sgttvtqyre rdkliavdlr apradrvdpa
      781 klaglalptp ngpvplgslg rfeptleygv vwerdrqpti tvqsdvraga qgidvthavd
      841 aklnalraql pvgyqinigg sveesakaqk sinaqmplma iavftllmiq lqsfsrvlmv
      901 vltaplglig vvatlllfgq pfgfvamlgv iamfgiimrn svilvdqieq diaighgrvd
      961 aiigatvrrf rpitltaaaa vlalipllrs nffgpmatal mggitsatvl tlfylpalya
     1021 twfrvkrder dphdgpppgg tpaapsga
//
LOCUS       WP_175914653             451 aa            linear   BCT 11-JAN-2025
DEFINITION  uracil-xanthine permease family protein [Burkholderia metallica].
ACCESSION   WP_175914653
VERSION     WP_175914653.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..451
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45748
     Region          9..423
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mshdpiptpv darlpawqlv lfglqhvlsm aaspitavfl iakmlalpad ltvqligatf
       61 facgigtllq slgagpigar mpfvmvpgga ptmlfagiaa qsglptaaga allasafywv
      121 llpvftrclr lfprivigam lllvsvnlir iyativvgqp gsadfaqpra lglalativa
      181 tvavagafrg tlgrlavlig ltagatlgwa lgampaladv wrgplfthpv wlpfgmprfd
      241 vlaalpllif taismaeata qtvavgetcg kpvslsrdap ktirgdalas lagalfgtpl
      301 ivtsaenigv vqttgvrsry vtaaagaili vialfaplar layaipaavv ggtalvvfam
      361 igvmgirlla gvdlharanq ytlaaalvvg lapilvpnly rhfgtpvqil lgngmaagtl
      421 aaiatqlafa alarlsgqvg tsaaaapsrd a
//
LOCUS       WP_175914649             321 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia metallica].
ACCESSION   WP_175914649
VERSION     WP_175914649.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..321
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34483
     Region          5..320
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpkvvgifav pgvqlldvsa pldvfaqana eygkpfytlr liasesgpir sssgaqllpd
       61 wivpdiperi dtllvagapn adrialrtdv lawlraaavq skrygsictg afilaatgll
      121 kgrhltthwa aadalaeayp slavdadaly vrdgklrtga gvtagldlal alveedlgre
      181 iarrvaaqlv mffkrpggql qfsrkgearp agrsvlqevq rwiaanpgle hsvaelakha
      241 gmsprhfarl fraevgmtpa awveatrisa arqllenghd tpkqvaakcg fanvdtlrrs
      301 ftrhvgitpt eyrkrqtvpa e
//
LOCUS       WP_175914712             146 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Burkholderia metallica].
ACCESSION   WP_175914712
VERSION     WP_175914712.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..146
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=15829
     Region          43..146
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 msdfyfgadl fgefdrlqqq maqrfggfps sirasrfgaf pqinigatde sieivafapg
       61 ldaaaldvsi dkglltisge rkstqpdgga etrsyaqerf sgafrrvvel pdsadpdkvq
      121 aryengclli sigkressrp rtitvq
//
LOCUS       WP_175914758             882 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            metallica].
ACCESSION   WP_175914758
VERSION     WP_175914758.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 882)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 882)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..882
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     Protein         1..882
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=96394
     Region          1..811
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 myvptqsrvv sisgvalpgv agrsillpir lhgqeelgtl aeftlelktl hmptlpvyea
       61 rdriqpeklv gteltisief dgkgtfspgi pggaglgnlg agkreivgli teftstgedd
      121 ryayyemsvr pwlwlttlnr enrifqnknv veitesilgs slypfkyewr lgavglkgvy
      181 ptrdyvrqmw esdfeflsrl wcewgiyyfm dgstlvlcds pgshkphgnm ydtisyhapa
      241 gkrvdeehih rltvsrrlta gavslidyds tqsranlstv vdrpsdipfs naehyawgdy
      301 sqplagtmgl sgmpnscvqe arylagvrvd aercrslrak grgnlrgiat ghtfhlegcp
      361 qartnaeylv vaatidirnn deatggepyh cvtdfvlqpa ttffrsrpkr kppcgsetav
      421 vvgpadqpiw vdgyarvkvq fvwdrlgsrd ensscwmrvs spwqgsgfgf valprigqev
      481 tvsyhegdpd kpyvsdrqvn qfnqppwvlp knhalmgwcs msltgsqanq vvvddtpgkl
      541 qvqissdyaq srlvlgyntr ieggtgrqqe rgvgfemate ahgvmranrg mlvtteareg
      601 asapakdmae tvarltqare lheemahlaq rhnaqeagvs qhdatqaikt qneaikgdva
      661 dpsetlfpem srpdivlasa sgigmsaaqg vhiasqgdha vtaardvsvs sgrsligsik
      721 gaislfaakl girlvaaqgk veiqaqddam alaalkdltv tsldgkivln askeiwigvg
      781 gsfiritadg ivngttgqiq ekcakwskag aesmripfsd sfgkiyegff klhwegtnqi
      841 apyhpyritr adgsriegit nadgettlhl aeyseslkie ll
//
LOCUS       WP_175914780             142 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TadE/TadG family type IV pilus assembly protein
            [unclassified Burkholderia].
ACCESSION   WP_175914780
VERSION     WP_175914780.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..142
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=14508
     Region          8..132
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mtrgamgarr argvislefv lmlpfllmvl igiidtslll cdkavitnas reaaragvvl
       61 rvpmltttqi asvassytqn slitggtatt ptvtvtqang ttsgtaltvt vtytysglvl
      121 gsafsaltgp vtisassvml ye
//
LOCUS       WP_175914783             358 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein [Burkholderia].
ACCESSION   WP_175914783
VERSION     WP_175914783.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..358
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39764
     Region          12..194
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(15,17,102)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(49,101..102)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            100..102
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mstharkpli slvvpfhdee etidaffaet lpvlesvagv rfeivcindg srdrtldrlv
       61 avaardprvh vvdltrrfgk eaaltaglde aagaavilid adlqdppali pamiehwrgg
      121 aevvaakrtd rmcdpylqra aaalyyrvhn alsevempen vgdfrlmdre vvdalralpe
      181 rrrfmkglfa wvgfrtaive ytraprsggr skfsgwrrwn falegitsfs tvplrvwtyv
      241 gltfamlslv ygafivvrtl lfgnpvhgyp slisvvlfvg giqligigvi geylgriyhe
      301 skqrpvylvr rryrterdaa gqpaskllqf plkranaarr rtalpaatgv aarkasfk
//
LOCUS       WP_175914808             184 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: carboxymuconolactone decarboxylase family protein
            [Burkholderia].
ACCESSION   WP_175914808
VERSION     WP_175914808.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..184
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19949
     Region          42..177
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtdrlppfdp asatdeqkav ladilsgprg nlngpflgwi aspelaqhaq rlgafcryrt
       61 glplrlsela ilvtaarwrs qaewhihhpi aldagvpaat adairrgvep afesdddali
      121 hafaselydt rrvsdatfar aqarfghetv vnlvallgyy alvamtlntf gmradgqtdl
      181 pfpe
//
LOCUS       WP_175914828             273 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SH3 domain-containing protein [unclassified
            Burkholderia].
ACCESSION   WP_175914828
VERSION     WP_175914828.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..273
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28559
     Region          7..96
                     /region_name="YraI"
                     /note="Uncharacterized conserved protein YraI [Function
                     unknown]; COG4991"
                     /db_xref="CDD:444015"
     Region          <130..244
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
ORIGIN      
        1 msntiirslc vvlfgiaavp giadaqssay tnspaeiyag papdypvvaq vppgtaldvf
       61 gclsdyswcd valpgvrgwi daeqldypyq gnyvplleyg aiigvpvtgf aigaywdryy
      121 rhrpwfhdrd rwerraeprv gpggmppayg hpqpggpnqr apgggaperh darpsatrgg
      181 wngpnrapap qqaapmpgar qpqpqpqpqp qpqqpaqqpa pnggaarmma pptyqggggy
      241 garpqgggns ggnrgggnhg gggggwgtde frh
//
LOCUS       WP_175914875             463 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sigma-54 dependent transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175914875
VERSION     WP_175914875.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..463
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51320
     Region          <36..130
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <147..454
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mnmpitrdks agggrttgqr pliywtrsps vmlrkelarr dwkvtvvaha nelrdtsgei
       61 tcgildlsgg hadaigfias tcasmrdvvw valvetgqta spnvrallrd ycfdyitlpa
      121 shqriadtvg haygmeclfa rdrealesre hgivgtcsam lrlfdtvrrf artdapvfvf
      181 getgtgkelt avaihrhser rngpfvavnc gaipphllqs elfgyergaf tganarkigy
      241 veaanggtll ldeigdlphe sqasllrflq eraihrlggs dpvpvdvriv sathvdlrea
      301 meegrfradl fhrlcvmrid qpplrargkd iellahhmle rfrgdarhrv rgfstdaita
      361 lykhdwpgnv relinrvrra vvmtegrlit aqdleleycl daaspsvadi rksiereaie
      421 tallrtrgrv aasarelgvs ratlyrwmea ygierprgtg ssd
//
LOCUS       WP_175914910             323 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Burkholderia].
ACCESSION   WP_175914910
VERSION     WP_175914910.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..323
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34665
     Region          10..227
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mnappapyai dvdrlnkrfg dkhvvkdvsl rvargeifgf lgpngsgktt sirmmcgllt
       61 pdsgsgtclg ydivrdsaqi krrvgymtqr fsywedlsir enldfvarvy gmpdrraavs
      121 raldglglas radqltgals ggwkqrlala acmlhepell lldeptagvd paarrdfwee
      181 lhrlaaqgis vlvsthymde aerchklayi asgellaqgt seeivasqhl strsvtgghl
      241 aelsarlrtm pgvdqtvvfg stlhvsgrdr alldatlaqi asqadaqtdg raplqvapid
      301 tgledvfiym mgrasgppgg aat
//
LOCUS       WP_175914893             355 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Burkholderia].
ACCESSION   WP_175914893
VERSION     WP_175914893.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..355
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38955
     Region          1..353
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mdklivddlh lsyganpilk gvsfelkage vvcllgasgs gkttllrava gleqpsdgri
       61 qlddrvffdg arhvdlpveq rslglvfqsy alwphrtvad nvgyglklrr vapaeqkrrv
      121 qtaldqlglg hlaerfphql sggqqqrvai aralvynppv illdeplsnl daklreeara
      181 wlrelivslg lsalcvthdq teamamsdri lllrngrieq egtpaelyga prslytaefm
      241 gsnnridarv aavdgecvtl agdgwelqal ardtfapgqd aqavirlerv qvtdgpganr
      301 lqadlvtsmy lgdrweylfh cgemrlrafg hvpraagkhw iefptndcwa fakag
//
LOCUS       WP_175914879             260 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175914879
VERSION     WP_175914879.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..260
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=28451
     Region          28..233
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mthqaneava hasgmielsh sfdanrflaa ldreeratli anlqlvhlks gqvlcepgem
       61 ltavylpvtt aislqyvssg gmtlevaeig sesvvcddvi ggsgrmpcra vacrdgfvyr
      121 ldrrvfaaaf daspvirhlv fvcvrllmaq vsqitfcsrh hvlkhqlcrw fllaydrsrs
      181 ieiqvthsml aqmlgvrret vtdaageiqk lglirqyrss ieladlagle kmscgcraiv
      241 rdemkrilsa dssvtaaara
//
LOCUS       WP_175914932             727 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia sp. BCC1638].
ACCESSION   WP_175914932
VERSION     WP_175914932.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1638
  ORGANISM  Burkholderia sp. BCC1638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Burkholderia sp. BCC1638"
                     /db_xref="taxon:2681391"
     Protein         1..727
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79442
     Region          39..722
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mkpqpaierp sieparwrtw ldplggaard waasdgliwl hlaktvlaal lamgiamrle
       61 msqprtamtt vfvlmqplsg mvfaksfyrv lgtaaglvga lalggpfaqq pelymagitl
      121 wiggcialav rnrhfrwygf vlagytaali glpavmtpqt lfqsaltraa evalgiacsg
      181 avsalilpls sakalmrslt arhvkfaafa agalsgdlar gdferrfadf vdeivgfean
      241 rafasfedph irarsrrlar lnsefmnact rlhalhqlvk rlranrsdav ldalaphida
      301 laqrvtalrd erqrgiastt gallelrrfh gtlpkaaras rreiedhaag glldfdtaie
      361 lmyrfigeyl gyadtnasld rddhafersv thyavktnvf fvgftflrtl vavgamsafw
      421 iasewpsgsl aviataiaca lsstsprapk fvaqmgvgaa fatavgyvfl cyvypnidgf
      481 pllcaalapv lglgaflamr pglsgygigf avffcllagp dnaiaytpev linngfaivv
      541 amlacsivfa vvfpthmpwl tsriahdlrr qvtlacegtr dglaarfqss thdlmaqlrt
      601 llvkrtrqhr dalswmlstl evghavidlr delhgfcesk ppqtqhwtas idavlrelpr
      661 ffddpttghh artlksvnla iraaqhtlha wyavpderrr mqrivgclhf irsalldkda
      721 pfnrhrh
//
LOCUS       WP_175914935             472 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cytochrome-c peroxidase [unclassified Burkholderia].
ACCESSION   WP_175914935
VERSION     WP_175914935.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..472
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=50572
     Region          83..468
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mtarpafpsp dasgaaaprs paravrraaf algaavlgyg afaiafpart paaigdvvad
       61 wtganphpvv lqrpaaqpls avaqlgralf adpslsasgk qscaschspd haygppngld
      121 vqpgglamtq qgyrpppslm ylyrqpnfsi gpdagendaa psvaqqaasa agvvkaqkva
      181 gasaapqlvp qggmfwdgra dtlqqqafgp llnpvemana giddvarkla qsshraqfeq
      241 lfgarvfssp qllvseamfa iaryqvedps fhpydskydr wlegrarltq aelrglrlfn
      301 dpdkancagc hlskpgkdgl ppmftdyqye algaprnmal aqnrnpafhd lgvcgpfred
      361 lkdqtqycam fltptlrnaa trhvffhngv fhtldqvmaf ynersispqk fysrgadgkv
      421 deyddippky ranvdvtdap fdrkpgdkpa mtaqdikdie aflgtltdap ar
//
LOCUS       WP_175914467             459 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-mobile-trio recombinase GmtY [Burkholderia metallica].
ACCESSION   WP_175914467
VERSION     WP_175914467.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia metallica
  ORGANISM  Burkholderia metallica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Mahata,T., Kanarek,K., Goren,M.G., Marimuthu Ragavan,R., Bosis,E.,
            Qimron,U. and Salomon,D.
  TITLE     Gamma-Mobile-Trio systems are mobile elements rich in bacterial
            defensive and offensive tools
  JOURNAL   Nat Microbiol 9 (12), 3268-3283 (2024)
   PUBMED   39443754
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Hurley,C.C., Quirke,A., Reen,F.J. and Boyd,E.F.
  TITLE     Four genomic islands that mark post-1995 pandemic Vibrio
            parahaemolyticus isolates
  JOURNAL   BMC Genomics 7, 104 (2006)
   PUBMED   16672049
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF040693.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Burkholderia metallica"
                     /db_xref="taxon:488729"
     gene            1..459
                     /gene="gmtY"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
     Protein         1..459
                     /product="gamma-mobile-trio recombinase GmtY"
                     /calculated_mol_wt=53078
     Region          3..437
                     /region_name="recomb_GmtY"
                     /note="gamma-mobile-trio recombinase GmtY; NF040693"
                     /db_xref="CDD:468657"
ORIGIN      
        1 mfvsikvqvl tdatnvytei palltasgil eplidyflhr shdrslewmr kvtrsirlfl
       61 eylqvnpter dphrlfqnfa qrlytgtfnr etgidptglc wpprsphdaa riithltdff
      121 nwlgemrpea srvnpqyagg afdrqtdeaa yqyrrskafl ghtwasnatp rstgyrlryr
      181 rlpkvaqgep pafpedrfed llfngfrigd rydyrgilit lllhgagfre sepfhiyvqd
      241 vfpdpanprq akvlihhphy gaapsdwrde rgqprksnra eylaqhfgla prtelmdrrh
      301 agwkggmhdg pyykqahwfv peygewflel whcylkqvar fnrahpfafv nikrepfgsm
      361 ytltqynkah aaacrrigln vgkalgttph ghrhaygqrl kragieksli rrfmhhscie
      421 sqeiytqasv revrnaleva alrlqgdqsa slsrfgpfa
//
LOCUS       WP_175914940             854 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: penicillin-binding protein 1A [unclassified
            Burkholderia].
ACCESSION   WP_175914940
VERSION     WP_175914940.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 854)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 854)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..854
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..854
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=91884
     Region          48..697
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mssvrdlcak wvaraqpvaa aaavpvkrvl asawhhlrhp trrgvlraaa avpvlfvlyv
       61 lalipftpgi gdirkarvdq paqvlsadgk vlaefkpsnr ewvsltqisp hmvdaliate
      121 dhrfyehhgl dwkrtasaal htfsgsrqgg stitqqlarn lypdeigrap tltrkvkeai
      181 talkieavys kdqiletyln tvpflynayg vemaartyfd ksadeldvld satlvgmlkg
      241 nsyynpvlnp eralqrrntv lgqmvkygkl spaqfaqlqr rplridferq keppgpaphf
      301 aqqlrkwlig wadrndyniy sdglivrtti dsrlqqmatq altlqanqlq giannawsgr
      361 dgcgtdnevf rtfmrespey kaaqdagknd avamkqlaad rgfmralcka ktdvqagfva
      421 idprdgqira wvgsrdftne pfdhvaqarr qpgstfkpfv ygvafangmk pddtfidqav
      481 eiplkggeiw rpnddappsg kpmtlrdava lsrnritaqv mekvgpaava rlardmgvre
      541 splervpsla lgtspvtlke mvasyatian gglyvepqmv trienrqgdv laeyapappe
      601 raldaetdkt llgvmrdvvt rgtgssirtr fgirgdvagk tgttqdnadg wfilmqpglv
      661 agawvgfddg rvtlrsdywg qgahsalpiv gdffqraqra rivdtklkfd tepspgwfss
      721 vrervtdlfd gwfgpepkqv papvrtqrie rqpeadaaaa saasaasape aasggiveew
      781 vpasevaasa aalsagasqp qaaqppatgg satpagntgg gglgsapaap savpapsaal
      841 apapvspgat sgse
//
LOCUS       WP_175914944             226 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CDP-alcohol phosphatidyltransferase family protein
            [unclassified Burkholderia].
ACCESSION   WP_175914944
VERSION     WP_175914944.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Sciara,G., Clarke,O.B., Tomasek,D., Kloss,B., Tabuso,S.,
            Byfield,R., Cohn,R., Banerjee,S., Rajashankar,K.R., Slavkovic,V.,
            Graziano,J.H., Shapiro,L. and Mancia,F.
  TITLE     Structural basis for catalysis in a CDP-alcohol phosphotransferase
  JOURNAL   Nat Commun 5, 4068 (2014)
   PUBMED   24923293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Koga,Y.
  TITLE     From promiscuity to the lipid divide: on the evolution of distinct
            membranes in Archaea and Bacteria
  JOURNAL   J Mol Evol 78 (3-4), 234-242 (2014)
   PUBMED   24573438
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Koga,Y.
  TITLE     Early evolution of membrane lipids: how did the lipid divide occur?
  JOURNAL   J Mol Evol 72 (3), 274-282 (2011)
   PUBMED   21259003
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..226
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23873
     Region          37..215
                     /region_name="PgsA"
                     /note="Phosphatidylglycerophosphate synthase [Lipid
                     transport and metabolism]; COG0558"
                     /db_xref="CDD:440324"
ORIGIN      
        1 mdqrktatrs epplprtwda rlarslvrpl idtpitpnhl ttlrlligla gawclahggf
       61 gwsnagafli vlsnfvdhtd gelarisgks skighfydla adalvtvalf vsmgvgivaq
      121 ggqmaaspvl lgavagaava lifflrmrie siagkagtkq afaggfeted vlyllpivtl
      181 vdgvqpflla asigaplfaa wvvidwwriv rrsgapqnst eiqask
//
LOCUS       WP_175914947             442 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cytochrome-c peroxidase [unclassified Burkholderia].
ACCESSION   WP_175914947
VERSION     WP_175914947.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..442
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=47853
     Region          53..415
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mlagtafaah aappetmllp gappsrvvgt igngtpqvtd kvdaaasrfa pdptlvalgr
       61 riffdprlse prgmscagch dpgrafaptl saaslagpgv pegsrhgrfs lrnapsllyv
      121 ryvprrhfyq dddapapspf gglfsdgrad tlaeqicgpl fdpnemnnrs paallrkvdr
      181 teladdlaar fgasvrrdpe qlvralgsav eaylqsddma pftsrfdayl rtrkplaaae
      241 mrgltlfrnp dkgncmscht lsetssrper slftdfgyda iavprnralp anrdprhfdn
      301 glcdtatrlr wpeptqwcgy lrtpglrnva vkqtfmhngv fttlrdavaf yntrstdpar
      361 wyhgartfdd vpaayrgnin vnstpmnrrp gtppaltdae iddivaflgt ltdarygniv
      421 ppaapaarit gspaarpppp vr
//
LOCUS       WP_175915113             283 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Burkholderia].
ACCESSION   WP_175915113
VERSION     WP_175915113.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..283
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30011
     Region          22..249
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mhspsapala eaipirrnkr pramagrlll rafvaafgly lalpivllli gsvgqswtnt
       61 llptgitshw fvdlaanrsf trafgtslvv alaccainav lalplayalh hralagrgfa
      121 arivmlmpia vpaltlgfgy iaifsgdalp wlgtlplmia ahavltlpyl lqtllsdlrh
      181 lglvhleaca atlgatplrq fvtivlpnlr hslfsglvmv aalsigefqi snliagfryr
      241 nypivllqaf ygasgmacaa tvvllvlavl atlasvftvq rlk
//
LOCUS       WP_175915122             708 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: penicillin-binding protein 1A [unclassified
            Burkholderia].
ACCESSION   WP_175915122
VERSION     WP_175915122.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..708
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=76548
     Region          24..641
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mtdhtanppt ppapppaspr rrawrifaga lfgltlacag igawtidriw tqlpsvehla
       61 vyrpalplri fsrdgellae ygverrefvp leripplmrh allaaedakf yqhgavdigg
      121 laratfanvv tgqpgqggst itmqvarnfy ltrdkvlsrk laeilmaikl ereyskdkll
      181 elymnqiylg eraygfaaaa nvyfgkplda lsageaavla glpkapsafn pvvnparata
      241 rrnyvlgrmh algeldeaty raavdapial attpppgiia apyvaerarr mmverfhdda
      301 ytlgldvttt ismrdqraae aalqrtlnrq prarrdarsg legalvslda atgdmlalvg
      361 gadfnrnvfd halqayrqpg ssfkpfvysa alekgyfpgv lvddtqrtlt heetgarpwr
      421 prnfgnryeg fipvrrglvr sknlvavslm qatdaryvqq havhfgfdaq rnpaslplal
      481 gagavtplel asaysvfang gtrmeprlil svkqrhggam yeattpegar vvsarnafvm
      541 dsmlrdvvka gtargalalr rddaagktgt sngskdvwfa gyssgivava wlgydtprpm
      601 gratgatlal pvwldymkta vdgrtqvaat ppqdvalvdg dfvyaeytrg tctadvpsyi
      661 rsrfacggap aaeapdasge kgrpdepmpa avdaaererv ldlfrted
//
LOCUS       WP_175915131             371 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alkene reductase [Burkholderia].
ACCESSION   WP_175915131
VERSION     WP_175915131.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..371
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39502
     Region          5..349
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,236,303,323,325..327)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,103,110,183,186,188,236,243,303,323,
                     325..326)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(27,103,183,186,188,326)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mtqdplfqpl qfgsltlpnr ivmppmtrsr asqpgdeane lmaayyaqra saglivsegt
       61 yiaplgkgya wtpgihtpsq vagwrkvtda vhaahgrifa qlwhvgrlsh tsllggrqpv
      121 sssplqakgv nvfvagqdgt tpgfvqasep ralsvdeire ivdqyraaar naieagfdgv
      181 elhgangylv nqfidsnant rtdayggsle nrlrflreva qaliegtgda srvgirlapl
      241 ttlngcvddd pettylaaak llgelgvgyl hiaeadwdda plmpvefkqq lraafpgvli
      301 yagaytaera reaiaagwad lvafgrpfva npdlperlrt gaaltphdrn tlfgggargl
      361 tdyptlaqaa a
//
LOCUS       WP_175915221             782 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor [unclassified Burkholderia].
ACCESSION   WP_175915221
VERSION     WP_175915221.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 782)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..782
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85019
     Region          64..764
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msftfaarps rgrlalacva vfawpaaqaa tidgvsadpa pgspgdpagh aapvaapapt
       61 gdtltavsvi arrrpvdpdt pavvesitre qidahtnvtt edalkyapnl mvrkryigdr
      121 nsvfagrdfn elqsarglvy adglllsnll gssyaypprw sliapddiar vdvlygpfsa
      181 lypgnaigst vllttrrpda leaslstqff tqryhdgygf adsfggnhqt arianrigkf
      241 wfslsldrle nngqpmqyag pnsaynpklg aavpvtgaat digpngkprt ivgaqtiert
      301 eqlngtvrmg yaftdrvdat ltlghwenhy rqhgetflrd aagnpvyggn vsiggrnmtv
      361 apsafapqrg dqenwlyalg lngrldsgwr lsgvvsaydv srdvlraast vqggagtlfq
      421 gdgtgwrtfd lkadaqevkg haftfgyhyd nyflrnvtyn tadwlagptt svasvyrgdt
      481 rtqalfaqda wrfapgwlat lglryerwda yggalgnang mlgyadrgan alspkvalqw
      541 datdvwrfrl sfatgtrfpt vgelfqgtis nnailnnnpn lrpekaidwd ftaerdvgvg
      601 vvrasvfqsd lrdsiysqtt vsgastvtni snvdrvrvrg velafsgqsv glrgldidan
      661 vsasnaqila dtanpayvgs rfpriprmra nllasyrfde hwlasvgvry sgrqfntldn
      721 gdvnpdvygg tsiftvvdlk aryrfdrhwt aslgidnltd rryyvfhpyp grtffgelkw
      781 sl
//
LOCUS       WP_175915304             927 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: type VI secretion system Vgr family protein
            [unclassified Burkholderia].
ACCESSION   WP_175915304
VERSION     WP_175915304.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 927)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 927)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..927
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..927
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=97612
     Region          17..853
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 matskdilqa llggwtqher flqlttplgk dvlvaecldg weaidgggfr fqitalsdnp
       61 alpiarlvgg pvlvewpttd gggqrrpfha hvaaaelvgy naglarirlv lepwlamlrq
      121 rvdsynfnda svidiseqif gyytrgavvp awrwaladse rylrrsltvq agesdfefls
      181 rlwaeeglyy wfehagdaqa ktlgghtlvl adsnecflpr epervpfhqt gesdpaggir
      241 hfaparrwri grvsraswdy rrlsarpvaa yasgavvpge drdvagpyay qtaavgeqrs
      301 qqhldaqrvd aatgtgtgtr rdlrpglrft vgdhptvnas daficlrvqh haranvaadi
      361 rsaieqhlgs vpamsdtgng slgldlawdg dgseedlave ddgvyrnrfl aipadrtyrp
      421 llghghgssl havaiahgaq saivvgsgdp vhterdhrir iqhhaqrgen aasrephpha
      481 anapanrnag twtrmltpva ganwggvtip rvgqevwtel legqpdrpva vaalyngqgk
      541 vdaqhnalvg gpsrstsnaa awfagndhpa vltgfktqdl gqsqtgtggy rqfllddsag
      601 qsraqlyttd rnsgltlghi khqqdnrrla drgygielat dasgalrgga gllittatgt
      661 nqmdarapgl dlaegmqrvr dlaeaaqsqg agvgasgrep qpdqleavag lkqsrdalea
      721 trsggaatdg igggggsava wshphlvvhg adgiaavsar shiwvsgket vlsagqdvqv
      781 taegktsvia nhgmsiytqg haavgrsven sgialhaasg saslqaqngg tlaaaaqrav
      841 tlasvdadam vqakqrlllt aadaflkmeg gnivvggpgk vefkasshvm tgpqsasgda
      901 tlagsrakdc pqtmgdmias saacadl
//
LOCUS       WP_175915322             472 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia sp. BCC1638].
ACCESSION   WP_175915322
VERSION     WP_175915322.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1638
  ORGANISM  Burkholderia sp. BCC1638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia sp. BCC1638"
                     /db_xref="taxon:2681391"
     Protein         1..472
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50887
     Region          8..462
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mqpegqfqhi aareqglrrt lsarqmamia iggaigtglf lgsgfaigfa gpsvlvsyai
       61 gafislllmg claemtvahp tsgsfgayae hyvspwagfl vryaywaciv lavgtevtai
      121 alymkywfpg vpgwlwivgf sallvfvnar svdvfgavey gfsvvkiaai vgfivlgayv
      181 vfgnpalvgd gaagagfhhy tehggffpkg mwgmwvaviv sifsylsiem iavaageaed
      241 peravtrafr stivrlvlfy lvtlalmlai vpwtaagrde spfvkvmeai hlpgaaglin
      301 fvvliaalya mnsqlyittr mmfslsragh apkalgevnt rgvpfgalml stlgialatv
      361 lsvlypdasf timmsvsmfg alftwmmifv thycfrrrra alglpapafr mrgfplltll
      421 gaalmlavmv ttyftaefhm tlifgipflv alsvvyavwy rraqpvlqpe ak
//
LOCUS       WP_175915312             395 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175915312
VERSION     WP_175915312.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..395
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43235
     Region          224..390
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mrialatddt aahdgfddaa wtarelsawl glvyqglsea tpwagfleai rvrldarftt
       61 lvlrnpggsr rgliinasad gpllpgepsy seqfyalcpf ldqtpglvft adglfgaarw
      121 rahdfyrqyl qpldlrfilg anlrgecgve caffvsrahh ardfdaaera qvatllphlq
      181 ravelhaald vldaeralya gtvdrldvgt aildedgrvi khnriaerli aqqdglclrq
      241 erlhascpld errlqkalqa alehfrtgal grieattlsr pggamplnvl lrplapyrga
      301 edrqhrpava vfvrdpassp qtsrdmlhrl frltpmetei alllvdgltl deaaaatgit
      361 kntarahlrg ifaktgatrq avlvkmllns vvsma
//
LOCUS       WP_175915155             288 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: thiol-disulfide oxidoreductase DCC family protein
            [unclassified Burkholderia].
ACCESSION   WP_175915155
VERSION     WP_175915155.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..288
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31806
     Region          1..121
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mgsselvlyf dgrcplcvaa iqrlrardar qqlafvdiag pgfdpaplgv dlpalnrelh
       61 vrlpdgrmlt gvdgilaaha ltgrsrlvrl lrvpvvrsal sllyrriarn rlavsrwlgy
      121 raeapcdgva cgidraaesa adrparddvr hivlawmyga aiahllvgia vpwvagtpwf
      181 dayhsvierh fwagmapepa raqqiwwmal igatvqcasv wmlalvhlgn rlrrrevwgw
      241 llaglliwap qdmlfslqah vwghvaidaa alvamvpplv wlwrrdsv
//
LOCUS       WP_175915369             255 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DUF899 domain-containing protein [unclassified
            Burkholderia].
ACCESSION   WP_175915369
VERSION     WP_175915369.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 255)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 255)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..255
                     /product="DUF899 domain-containing protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28520
     Region          1..254
                     /region_name="COG4312"
                     /note="Predicted dithiol-disulfide oxidoreductase, DUF899
                     family [General function prediction only]"
                     /db_xref="CDD:443453"
ORIGIN      
        1 mtnhltgtrg ewltarrall daektltrqs delarrrqal pwvrvdkayr fdtedgpatl
       61 ddlfggrsql lvyhfmfgpd ykagcpscsa ladgfdgfav hlanhdvtla avsraplakl
      121 layrqrmgwh fpwassdgge fnfdfnvsft etqqrtgdve ynyaragham dmdpppaava
      181 qfaatcgtda atyardrpgm safvredgvv yhtystyarg ldglwgmyqw ldraplgrne
      241 tgvwwrrhde yaarg
//
LOCUS       WP_175915330             262 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TatD family hydrolase [unclassified Burkholderia].
ACCESSION   WP_175915330
VERSION     WP_175915330.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..262
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28574
     Region          2..247
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mwidthchld aaefdadrda vahaaraagv srivipsigr dnfttvrela qrtpgavyal
       61 gihpmytpda rdedldrlrm eieaslddpr fvaigeigld yfvpgldedr qqffyqgqlk
      121 larefdlpvl chvrksqdrv laglrrfgvr rgiahafngs fqqadaylaq glhlgfggnv
      181 tfgralqirr laaqlpldai vvetdapdia pewayksrna pdqvpriggv laelrgidah
      241 alslsttana laalprlals sa
//
LOCUS       WP_175915381             839 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia sp. BCC1638].
ACCESSION   WP_175915381
VERSION     WP_175915381.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1638
  ORGANISM  Burkholderia sp. BCC1638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 839)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 839)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..839
                     /organism="Burkholderia sp. BCC1638"
                     /db_xref="taxon:2681391"
     Protein         1..839
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=91082
     Region          57..777
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mpiikrpssp sdrnkphytl rrspsgayyp ddddrgddrr aqrrgggggd rrsfgsrval
       61 wfvglfatla ivgalivgya lvvmapqlps ldaltnyqpk vplrvftadh vligefgeer
      121 rslvrfqeip dvmkkavlai edyrfyehgg vdflgilrag vadlmhggar qgastitmqv
      181 arnfflssek tytrkiyeml laykiekalt kdqilelymn qiylgqrsyg faaaarvyfg
      241 kdlkditlae aamlaglpka psaynpvvnp krakvrqeyi lkrmleigyi tqpqydqavk
      301 eeihvrtpgn qyavhgeyva emvrqmmyqq ykdetytrgl tvtttinsad qeaayqavrr
      361 gildyerrhg yrgpegsinl paagddrdea iddaladhpd ngdlqsavvl aaspnavevq
      421 fvggatttig paglrfvsaa lspranatlr ikpgsivrvl kdgkagwqvv qlpqvegalv
      481 aiapqdgair slvggfdfnk skfnhvtqaw rqpgssfkpf iysasldkgl gpatiindap
      541 lyfppsvpgg tawepkdddq pdgpmsmrtg lqrsknlvsi rilasigtqy aqeyvtqrfg
      601 fdpaktppyl pmalgaglvt plqlatgyav fanggykvdp yliaevddar gqplqksqpv
      661 iaggtaprti egrnayvmns llhtvatagt gagtnalgrs dlqgktgttn dakdgwfagy
      721 qqslvavawm gfdqpkslgs refgaqlalp iwvnymrtal ngvpeqqmpm pdgltsidge
      781 lyyadrtpgn gfvasvdinp aanaisanda lgsagsegla pppvtqqekq qimdmfqnk
//
LOCUS       WP_175915444             282 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [unclassified Burkholderia].
ACCESSION   WP_175915444
VERSION     WP_175915444.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..282
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28655
     Region          20..261
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mthldltqgv lvsslhglal ldligiaial llggmvkgit gigvplvamp ilsqflpirh
       61 avlllsmpii lgnipqaleg gevlattrki aapiagtvlg nvvgvaills lnaghaqaas
      121 gallivaaal mlsapklnlp eawqkpvgfa lgfgaalmes iasvpgplla tylissgatg
      181 raftkqiaii lvvsivtlit tfsgaahast adlaisaaas lpaiagmwlv rplrdkmspr
      241 vfrmvvllfv lvaasqmiwk sgvfrhaasp vapvdsphan ak
//
LOCUS       WP_175915464             413 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [unclassified
            Burkholderia].
ACCESSION   WP_175915464
VERSION     WP_175915464.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..413
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42378
     Region          1..378
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdlaltdeqa mirdaaadvl aersasvdvr raleqsagrd dtlwaalage lgwnalslpe
       61 aaggmglgav eqtllmeqlg rrvacvpyfs taclaatala scsdaplaag wlaklsegac
      121 satlalpfel pagagqlpvv aeeaaggyal sgtieqvidg arvdlllipa rianegqsig
      181 lfaidvattp glsitpldtl datrpiariv lddirvsrda lfaggavaaq vleragwfaa
      241 lalaaeqlgg aqqcldltld ytgqrvqfgr aiasfqavkh rcaqmmvlie sarsavlgaa
      301 hawdaeagga apgaalradv aaakaaanda yafcaqeaiq lhggvgftwe ydphlyfkra
      361 qaslaqfgst pqllewiach aidggtspcd avlalpqasm atrpsaartg alq
//
LOCUS       WP_175915536             312 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [unclassified Burkholderia].
ACCESSION   WP_175915536
VERSION     WP_175915536.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..312
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32239
     Region          78..282
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mpldpqaqal laalaqapai dfdqltvpay raslaggsaf apgdaiaaee dwqipapgrq
       61 lsarlyrpda dgplpltvff hgggfvacgi dshanlcrsl agrartlvls vdyrlapear
      121 fpaaaqdacd avrwaaasar dlgaragaia vagdsaggnl aavaalqlrg sgiaiahqll
      181 lypvadcate hpsyealgeg yfltadamrw fkrqyfddga drasplaspl avadlsgaap
      241 ativsaefdp lrdeaeayal rlaqagtpvs lvrwpgqlhg fasmlgavda adraltfgad
      301 alrrafdate vq
//
LOCUS       WP_175915541             766 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ATP-dependent DNA helicase [unclassified
            Burkholderia].
ACCESSION   WP_175915541
VERSION     WP_175915541.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..766
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=84087
     Region          170..765
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 msyvvavram ceftarrgdl dlrftpapta legiaghgav tskrgaryet eipltgtwgt
       61 ltvrgradgy dpvanrleei ktyrgsldam panhralhwa qakvyahlmc darglaeidv
      121 alvyfdivse retvltetlg asalaaffae qcacfvgwae retahraard talraltfph
      181 gqfrsgqrel avsvyraard erclmaqapt gigktlgtvf pllkacgege ldhvffltak
      241 tpgralalea attlgagtpa lplrvlelva rdkacehpdr achgescpla qgfydrlpaa
      301 rdaaigagll drdtvreaal ahdvcpyyla qelarwsdmm igdynyyydg samlhtlalq
      361 nqwrvgvlvd eahnlldrar kmysasldpf afaaareaap talrkafdrl arawgtlnra
      421 qaeryaaype ipgpivtavq nlvaaigehl tdaprangda llrfhfeaiq fgvladafds
      481 asifdatlhg eplprqsgld gvapaarrrr iqstlcvrnv ipagflasry eaaratvlfs
      541 gtlspfhfyr dtlglpadtg wldvdgpfra eqltvrvash vstrwrdrdr slepivdlia
      601 tqyatrpgny lgflssfdyl grvvalmrtr hpdvpvwaqa pgmaeserda flarfdaggr
      661 gvgfavlgga fsegvdlvge rligafiatl glpqvndvne qmrramdarf gngydymyly
      721 pglqkvvqaa grvirtehde gvvhliddry rrrevrdllp rwwrig
//
LOCUS       WP_175915578             220 aa            linear   BCT 11-JAN-2025
DEFINITION  LemA family protein [Burkholderia sp. BCC1638].
ACCESSION   WP_175915578
VERSION     WP_175915578.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1638
  ORGANISM  Burkholderia sp. BCC1638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia sp. BCC1638"
                     /db_xref="taxon:2681391"
     Protein         1..220
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=23819
     Region          32..209
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mstnpaaisa rrslaralli aalaasllsl sgcgynaiqs edeqvkasws evlnqyqrra
       61 dlvpnlvntv kgyanqekev lvrvtearaq vgsiratpel iadpqafakf eaaqgqltss
      121 lsrllvvsen ypqlksdanf rdlqaqlegt enriavarnr yirsvqaynt tirsfpnnlt
      181 akafgylerp nfsvsneaei skpprvefgs tpasagkasn
//
LOCUS       WP_175915626             289 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sulfurtransferase [unclassified Burkholderia].
ACCESSION   WP_175915626
VERSION     WP_175915626.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..289
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30457
     Region          15..284
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mphthyttli saanlaerla aapgsvavfd crfdlvdpga geaayatghi pgaqylhldr
       61 dlsgrktgtn grhplptrda fatliasrgv kqgqqviayd aqggayaarl wwllrwlghd
      121 svavldgglq aweaagqplt advphqaagd frattplest vdaaavlanv tsakrvvida
      181 rapdryrgen etidrvgghi pgarnrffkd nlaadgrfkt ghelretftt llagtepnsv
      241 ilqcgsgvta chnalaleia glhgaslypg swsewsadps rpiatgpnp
//
LOCUS       WP_175915666             488 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: flippase [unclassified Burkholderia].
ACCESSION   WP_175915666
VERSION     WP_175915666.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..488
                     /product="flippase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52365
     Region          5..414
                     /region_name="MATE_Wzx_like"
                     /note="Wzx, a subfamily of the multidrug and toxic
                     compound extrusion (MATE)-like proteins; cd13128"
                     /db_xref="CDD:240533"
ORIGIN      
        1 mdkgilknvs infiglilpt fvslvtvpay ihalgveryg vvslvwtlig yfgildlgms
       61 maaqnhiska lasgnadesa rvfwsafwln lgtgivggll iyfgafvyta yftkvsaamq
      121 hevylalpwl alaiplanvs wvfagainga erfgvfntnq tigtflfqll plgaawwiap
      181 nlqtvlaaav larliaavml ghasikvlgi rridppqwgt akglfnfggw mliasttsmv
      241 adtldrvmlg agmgakfvty ytvpqnlvtr lnmlpnalvr tlfprlsavg rehadtlarq
      301 sleflngvft pvgivaifal apfltlwvga dlaahsapvg rvlvisvwlv gqasvtrili
      361 qsqvnparaa faglvempff vgglwfgihh fgligaavvv atralvdygv llylsairmr
      421 aivldmlahl afllaslfla qawsglgesi glcavvlvln lawsltmtpa lralvrdlfv
      481 rlnarktv
//
LOCUS       WP_175915695             425 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GspE/PulE family protein [unclassified Burkholderia].
ACCESSION   WP_175915695
VERSION     WP_175915695.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..425
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=45121
     Region          <21..424
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mhfpppgapp rtqrppasld aspaetprsl daaqlddspa vrlltdtlha arvrdasdih
       61 vepfeggwri rlridgvlhe harppahlrd alvtrikvla rmdiaerrlp qdgrlriavd
      121 ggirgdyrvs slptlfgekl vlrrlemlpp dltlarlgfd arqaaameaa iraphglvlv
      181 tgptgsgktl slycalqmld rdahnvctve dpaeiqldgi nqvgvaekag ltfatalral
      241 lrqdpdvimv geirdaetad vaikaaqtgh lvlstlhtnd aptavarlld igvapynlaa
      301 alrlvtaqrl vrrlctvcrv rsdasaralr eagcdsaale sgwrpfvarg caachgigyr
      361 griglhqtmp vspamaehiv arasvgtlaq caasegvcsl raaalahvrd gttsiaeala
      421 atpda
//
LOCUS       WP_175915694             404 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: type II secretion system F family protein
            [unclassified Burkholderia].
ACCESSION   WP_175915694
VERSION     WP_175915694.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..404
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=42311
     Region          13..404
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 miamhappne tcfawrgrrr ngtpcrgnvi afdaaaaraa lardgvavls ldvrsaarpp
       61 aagarevtrf trqlasllqa glplapslem lartrtrdgl priaaglare ivggqrfaaa
      121 larypsqfgt lyrqlievge asgalgtvlt rvaehrerad aqwrklraal aypvavivfa
      181 laisaalmvw vvptfrqifd gfgaalpapt rallalssat sawggtlvag aagaglvarh
      241 alrrssslry tvarhllnlp lvgtalirfa tarwcrslat llgagvplad afatlertag
      301 hpvfeqataq iatrvlrgar ladamhaagc fpddvvqpia vaeetgaldt mladiaalce
      361 rqldarldal aalgeplivi vlgalvgglv iamylpilql gnvv
//
LOCUS       WP_175915683             274 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175915683
VERSION     WP_175915683.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..274
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=30312
     Region          42..274
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mramtsnqan nanptgaggp gqpgaadsvp apaaspsptf splyqqiksl itqslesgew
       61 kpgeiipsev elaarykvsq gtvrkaidel aaenlvvrrq gkgtfvathn edraqfrflr
      121 lladdgaehp hvsrllecrr lrapaeiarq ldlkpadpvv qvrrllefen evtvldeiwl
      181 pgvmfrgltf erlseykgpl yamfetefgt rmiratekir avaaepavad llhvpagfpl
      241 lsvervsyty gdrpvevrrg wyvttgyyyq ndls
//
LOCUS       WP_175915700             166 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CinA family protein [unclassified Burkholderia].
ACCESSION   WP_175915700
VERSION     WP_175915700.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Galeazzi,L., Bocci,P., Amici,A., Brunetti,L., Ruggieri,S.,
            Romine,M., Reed,S., Osterman,A.L., Rodionov,D.A., Sorci,L. and
            Raffaelli,N.
  TITLE     Identification of nicotinamide mononucleotide deamidase of the
            bacterial pyridine nucleotide cycle reveals a novel broadly
            conserved amidohydrolase family
  JOURNAL   J Biol Chem 286 (46), 40365-40375 (2011)
   PUBMED   21953451
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Martin,B., Garcia,P., Castanie,M.P. and Claverys,J.P.
  TITLE     The recA gene of Streptococcus pneumoniae is part of a
            competence-induced operon and controls lysogenic induction
  JOURNAL   Mol Microbiol 15 (2), 367-379 (1995)
   PUBMED   7538190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..166
                     /product="CinA family protein"
                     /calculated_mol_wt=17586
     Region          10..160
                     /region_name="PncC"
                     /note="Nicotinamide mononucleotide (NMN) deamidase PncC
                     [Coenzyme transport and metabolism]; COG1546"
                     /db_xref="CDD:441155"
ORIGIN      
        1 mptdsvvhql airagnklrd ehlslataes ctggmiaaai tdisgssqwf ergfvtysnq
       61 akidmigvpp dliekhgavs epvaramaeg alrnsraqva lsvtgiagpa ggsekkpvgt
      121 vsfgwsnrlh tdvetlvfkg dreqirtqaa ahalrgllkl lderer
//
LOCUS       WP_175915773             315 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: dihydrodipicolinate synthase family protein
            [unclassified Burkholderia].
ACCESSION   WP_175915773
VERSION     WP_175915773.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..315
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=34399
     Region          11..>232
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mqshqqastt iegivpvmlt pfddagaidy aglerliewy lahgsdalfa vaqssemqfl
       61 slaeraelar fvvervagrv pvvasghvse dldaqvaelc aaaesgaqgv vlvtnrldpq
      121 rkgsaafldh lhkllarlpt dlplglyecp apyrrllsdd elracidtgr fvmlkdvscd
      181 letvkrrval aagspmkiln anaaiawdam kagsagfngv ftnfhpdlyr wlrtqgdsdp
      241 vladelstfl vlsavsealg ypalakiyhq rigtfgsirc raidydvrer fwaldavldk
      301 ivsgtehfrr riaar
//
LOCUS       WP_175915709             241 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [unclassified Burkholderia].
ACCESSION   WP_175915709
VERSION     WP_175915709.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..241
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26482
     Region          1..239
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 misiknvskw ygqfqvladc ttevkkgevv vvcgpsgsgk stliktvngl epfqqgeilv
       61 ngqsvgdrkt nlsklrskvg mvfqhfelfp hlsitenltl aqikvlgrgk deatekgmkl
      121 ldrvglkaha hkfpgqlsgg qqqrvaiara lsmdpiamlf deptsaldpe minevldvmv
      181 elaqegmtmm vvthemgfak kvahrvifmd kgaiveddrk ddffsnpksd rakdflakil
      241 h
//
LOCUS       WP_175915771             733 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Burkholderia].
ACCESSION   WP_175915771
VERSION     WP_175915771.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 733)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..733
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..733
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80091
     Region          33..716
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 msasspasth aagplaawsa afgdwarsdg aawlylfkal laafiatgvs mrldlpapkt
       61 amttvfivmq pqsgavlaks fyrvagtifg liatltfvgl fpqqpqlfll avalwvalct
      121 agaarnrnfr sygfllagyt taliglpasq hpdgafmsam trvaeimvgi vsagvvsalv
      181 fpqytgeqmr ttvrkrfssf vdyvaaalsg qldrahieti htrfvadvvg feaarsmavf
      241 edpdtrmrsg rlarlnsefm svssrfhalh qlmnrlraag aqaaidaiep yfreiapllt
      301 rngepvrssa daalaaeqll awrdalprri ratraaletq pdfplldfdt atellyrfit
      361 dlheyaatya slstathere rwieryeprt nvtamviaai rtatvilvlg wfwietawps
      421 gvtmtltaaa tcalasstpr ptamsaqmgm gtalavctgf lltfgiyphi dgfpllcaal
      481 apllaigifm tmkpklagyg mgyliffsfl agpdnithyd pmsfmndala lvlsmlvsai
      541 afavlfppta pwlkkrlfad lrhqvvaach arlaglrtrf esgardlmyq ahtlsadqpd
      601 vqrdalrwmf avletgnaal dlrtelatlp sdpryapttp wrraietmrt alsalfrkpd
      661 aarfdatlda vnaaidatrq tldaftpsre erhrlqrils hlhfvrtall dpesplepln
      721 rnrpvrpqqg ass
//
LOCUS       WP_175915810             352 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: permease [unclassified Burkholderia].
ACCESSION   WP_175915810
VERSION     WP_175915810.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..352
                     /product="permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=37011
     Region          61..346
                     /region_name="YraQ"
                     /note="Uncharacterized membrane protein YraQ, UPF0718
                     family [Function unknown]; COG0701"
                     /db_xref="CDD:440465"
ORIGIN      
        1 mtttrtqpsp algwmtflli avaglfyvkw fpyynkafva aehhsigqsi lmgtsasape
       61 pslkaaldya waygkaiwqa mvlglllgsa vqallpahwv arvlgrtgfg svaaggllsl
      121 pgmmctccaa pvvaglrarh aspggavafw lgntvlnpaa lvfmgfvlgw hwsalrlvlg
      181 vamvfgigyl lnriarpedr siddaqlaal vaeqaaagnp fvrwmkllar mavrlvpeyi
      241 vlvlllgaar awlfphigpd ignhlgwiia favagtlfvi ptagevpiiq amlslgmgvg
      301 paaallmtlp pisvpslaml arsfkpymlv ivtglvvvfg ivsgllaiaf gf
//
LOCUS       WP_175915778             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1638].
ACCESSION   WP_175915778
VERSION     WP_175915778.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1638
  ORGANISM  Burkholderia sp. BCC1638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia sp. BCC1638"
                     /db_xref="taxon:2681391"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32468
     Region          8..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(104,108,147,161,163,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(105..106,110..111,113..114,117,121,123..129,190,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mliddlpald tfarivsags lsaaareldl slsvvskrla hlesqlgvrl lhrttrqqtl
       61 tddgaqfhaq vlrilaevdr aetlmsdrrg tvsgvlrlta pgelgrlria plvaafqrqh
      121 pelivqlmlt dtivdllaqd idvavrigsl adstmiarel apnhrvlcas ssylavhglp
      181 ahpaelrahr civmgdqprt ewrfdgaqga vtvevtaall tndggaartl alegagialk
      241 siwdvgadle agrlvrvlpt faapaaplha vypggrhvpl rvrafvdflr dqlretwrrs
      301 a
//
LOCUS       WP_175915822             283 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Burkholderia].
ACCESSION   WP_175915822
VERSION     WP_175915822.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..283
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29915
     Region          7..260
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtrspaalaa rgltvgyrdh vvidgldlsi asgrvtalcg pngcgkstll rtlaglqpar
       61 aghidvngtp lasfrrrala reltmlaqfn qipsgltvre lvaygryayg gflrglsrad
      121 haaidealdt sglardaerd vgalsggerq rawiamalaq qapivlldep ttyldihhql
      181 dildalraln rargltivwv lhdlnqaaay sddivlmrag rlvaqgspda mleparlraa
      241 fgvdmlklah pqtgapmcvp aygppasgta gafdravqrd iav
//
LOCUS       WP_175915827             341 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia sp. BCC1638].
ACCESSION   WP_175915827
VERSION     WP_175915827.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1638
  ORGANISM  Burkholderia sp. BCC1638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia sp. BCC1638"
                     /db_xref="taxon:2681391"
     Protein         1..341
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37217
     Region          180..320
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mlaevrpdgf tmpdtcrlaf adglfaardd aeirvaqgdg igaqllraql addgtlrlva
       61 ynhraapsaq rrallaalaa afsddarraa irldpaawpa valdalrasg vladgglcmr
      121 egwaqqadlw rvgtplpcat lpmltdgrrh prrppaprgd vyardlpalg vrftlrdwqp
      181 gedaarlarw fdeprvrdgw pgtqpgvdgt apdadphvsp lvccfdgepf ayveafwlke
      241 dplaphvgar dydrglrmlv gasrwrgphc vagwlpsvvh ylflddarte avscavpagr
      301 arvvdtlarh gfarqrrlal adgqplwmrt lretffsgrh v
//
LOCUS       WP_175915846             268 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein [unclassified
            Burkholderia].
ACCESSION   WP_175915846
VERSION     WP_175915846.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..268
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29215
     Region          12..193
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(15,17,98)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(42,97..98)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            96..98
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 msklhassth lvlipsynpg ikvdttvrna raqwnpvwvv vdgstdgsae rlqamaerdp
       61 glrvivlpen rgkgaavlag ldaaaasgft hvltmdsdgq hpadlipefm aasqaapdam
      121 vlglpkfdas apqlrvqgrr lsngwadlet lwagigdsly gfrvypvapl aaimhrqpwm
      181 rgfdfdpeaa vrlcwagvrp irieapvryf gaheggvshf hygrdnvlla wmhlrlfagf
      241 vvrlpmlvar rltrrsrstf srssgrgd
//
LOCUS       WP_175915849             265 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: (Fe-S)-binding protein [unclassified Burkholderia].
ACCESSION   WP_175915849
VERSION     WP_175915849.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..265
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28359
     Region          <8..255
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mnerhypaap ahvylfatcl vdlfvpeagl davrllereg ltvhyprgqs ccgqpayssg
       61 npdearrvaa aqldlfaepw pvivpsgsca gmirhhwpal ftddpvhgpk araiaertye
      121 laeflvhvld vrldridtna gpnervvlht scaarremgt rvhgvalvda lpgvtriehe
      181 reseccgfgg tfslkhpdis gamvhdkvas acatgcdrlv sadcgcllni ghaatkagat
      241 lpvehlasfl wrrtagagsl rgdak
//
LOCUS       WP_175915883             251 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AzlC family ABC transporter permease [unclassified
            Burkholderia].
ACCESSION   WP_175915883
VERSION     WP_175915883.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 251)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 251)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..251
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27058
     Region          15..236
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mlarfsatdr faliqgardy sptlmailsw glvtgvamsk svmtlgqasa msifvyagss
       61 qlavlpllva klpiwtillt atmvnmrfvi fsaglaphfs ylplwrrlai gyfngdviyl
      121 lfqkqgfayg hapgkeayfw gmalaswasw qvsslagill asffpaswgl elagtlallp
      181 imvsavanrs tlaavavagi vsliafdlpy rlalpiavla alaagctadf fveradwrri
      241 rtetvhekei e
//
LOCUS       WP_175915901             369 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Burkholderia].
ACCESSION   WP_175915901
VERSION     WP_175915901.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..369
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39606
     Region          1..359
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masvllrnia kryddtevlr nvnldiadge fvvfvgpsgc gkstlmrmia gledissgdl
       61 lidgakvndv psakrgiamv fqsyalyphm tlydnmafgl klagakkpei dqavkqaaki
      121 lhidhlldrk pkqlsggqrq rvaigraitr kpkvflfdep lsnldaalrv kmrlefarlh
      181 delkttmiyv thdqveamtl adkivvlsgg avqqvgtpna lyhapanqfv agfigspkmn
      241 fltgtvestd atgvlvrfgs getqrvavda aglqrgaavt vgvrpehlmv aqaatgvaar
      301 tmaveslgda aylyaesava pdgliaripp ldtyrtgeal hvhaqpehch lfdehgqalr
      361 rlsphakaa
//
LOCUS       WP_175915911             155 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: methylated-DNA--[protein]-cysteine
            S-methyltransferase [unclassified Burkholderia].
ACCESSION   WP_175915911
VERSION     WP_175915911.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..155
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=16721
     Region          1..153
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mfnavidapf gkvgirtdaa vvreivylpe svksvdpdsp latravkqie ryferasarf
       61 dlpladvgsa fqhrvwnvis dippgtvqty gqvakrigga pravgqacga nyfplvipch
      121 rvvaagglgg fanhddngyy qkvkrwllah egvpy
//
LOCUS       WP_175915912             520 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: class I adenylate-forming enzyme family protein
            [unclassified Burkholderia].
ACCESSION   WP_175915912
VERSION     WP_175915912.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..520
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54690
     Region          24..520
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 msspvrssap ldvpallaal pariadvpar waaqapahpa liedarrlsy gelsravdaa
       61 aerlarlgvh ggdrvmivae nsiaqivllf aaarvdawal vsnarlsage ldaiaaharp
      121 kliafateas pdarahavrh datpadalpv digawsyrvd psapdepvaa dgaaqcaali
      181 yttgttgspk gvmlshrnll fiaatssalr rvspddlvyt vlpvshvygl asvclgslya
      241 gatlrlaprf speavrvala degvtifqgv pamhaklleh lhthahawra prlrfaysgg
      301 spldadlkar vervygvplh ngygmtessp titqtpldap radcsvgmpi pgvemrivap
      361 dgadvpqgev geirvrgpnv mlgyyrnaea traavspdgw lstgdlarqe adgsvtiagr
      421 skeliirsgf nvypveveqv lnahpdvvqa avvgravegn eevlafvelv pgatateaal
      481 qawcaerlap ykrpahirvl dalpaastgk vlkhklrela
//
LOCUS       WP_175915949             389 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: electron transfer flavoprotein subunit alpha/FixB
            family protein [unclassified Burkholderia].
ACCESSION   WP_175915949
VERSION     WP_175915949.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..389
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40030
     Region          91..369
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mntikridpr rpfiitaagl kritlgeegs adanaaqwsa hghgaaaakp rravqdpkhv
       61 mlvvahterg alddharqai aaaavladaq tevallafge lkddaavlgv dklieladfd
      121 rrafapesel qalqacaaal apkhvfvpdn atgdgdlgrr yaaaagasva thvveidakh
      181 vgayaqagra fatrglpdvi llaqnaveak lpfvgagerl aadfirpard aaqpyrdlgl
      241 eeidaaqval eeadfivsag ngvsdigafe rlagafgaai gasrvavdng hftrdkqvga
      301 tgktveasvy iafgisgavq hlqgikdcrh viavnldgsa piakranltv vgdaqatiaa
      361 lieqvqaarv srgqsptavg aresegvaa
//
LOCUS       WP_175915938             392 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Burkholderia].
ACCESSION   WP_175915938
VERSION     WP_175915938.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 392)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..392
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39949
     Region          168..370
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mtgravpsar rvtldkvgil igvltivavf gmpfmvlrpn riaagtglsa faalpavqga
       61 alaalwvvga lwamtasrpa wrlaagctwl atlayavgaa athvvapddv larvspaaga
      121 wlllfawavl vadalarlaf gpwrrlvalv vaiaaislpl asgwwdglsv mreyavrsdd
      181 fwreairhvs laggsvaaal vaglplgiac arvapvrtvv mpvlnivqti psiamyglmm
      241 aplgllaahv plaaalgirg igvapavlal flysllpias svvvgleqvp phvteaaram
      301 gmtraqrllr vdlvlalpvi lsgvrivlvq nigltavaal iggggfgtfi fqgigqsaad
      361 lvllgaipti alalaaavvf eaattlakgr tg
//
LOCUS       WP_175915972             209 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [unclassified Burkholderia].
ACCESSION   WP_175915972
VERSION     WP_175915972.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..209
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22279
     Region          1..207
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msiqtwmlfa aaylattlsp gpnvllvirn tvrygsrgta atiagnlvaq gavvmlvafg
       61 vgavlaampp lfiamkvvga aylillgirq lrgdrnarsp dgraaivepd rrklfrealf
      121 vsgsnpktmi flsafmpqfi ahgrplamqf vvmyvtiact vvvvhsvysf gvrrlhrgig
      181 vgpwvraakr asgllfvglg iklltarqa
//
LOCUS       WP_175915976             288 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [unclassified
            Burkholderia].
ACCESSION   WP_175915976
VERSION     WP_175915976.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..288
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30691
     Region          13..262
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(28,109,111,113..114,142,194,215,218,231,233,262)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 msapvprpsf prrqvgdftv taisdgtlta gldllsnidv ddaigimhra gihapsdvni
       61 ncyvirgngr tvlvdtgagg irnwggllrp slsragidar didtvlltha hpdhigglld
      121 tdgqpafpqa evfiherera fwlddgmyer aserargnfr iarrtfdvyr aqlrtieaag
      181 dvlpgivavp lpghtpghtg yrveslgerl liwgdlvhfa piqvarpdvs iafdhdpsqa
      241 sstraatlae vasdnlliag mhladtgfar iarangatgd ayvlsgad
//
LOCUS       WP_175915982             509 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CoA-acylating methylmalonate-semialdehyde
            dehydrogenase [unclassified Burkholderia].
ACCESSION   WP_175915982
VERSION     WP_175915982.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..509
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53843
     Region          16..492
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(73,75,79,82,86,119,122..123,132..139,144,147,150,
                     243,247,250,253,255,428,430..431,433..434,437,440..441,
                     443,445..448,457,461,463,477,484..489,491..492)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(159..162,170,185,188,218,235..238,241,259..261,293,
                     393,395,421)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(162,259,290,293)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnanptprtg qdvptvklli dgafvestts ewrdivnpat qqvlarvpfa tvaevdaavq
       61 aahaayatwk ntpvsarmri mlkfqdlvra nlqriaktlt aeqgktlpda egdifrglev
      121 vehacsvgtl qlgefaenva ggvdtytlrq plgvcagitp fnfpamiplw mfpmaivcgn
      181 tfvlkpseqd pmstmelvel aieagvpkgv lnvvhggkev vdaicthplv kaisfvgsta
      241 vgthvynlgs qhgkrvqsmm gaknhaillp danreqaina lvgagfgaag qrcmatsvav
      301 lvgnardwlp divakakllk vnagseagtd vgpvvsrgak arilslidtg ikegakleld
      361 grdvkvagfe egnfigptif sgvktdmtvy theifgpvlv vmevdtldda ialvnanpmg
      421 ngvgiftqsg aaarkfqsei dvgqvginip ipvpvpffsf tgsrgsklgd lgpygkqvvq
      481 fytqtktvta rwfdddttag pvnttirlh
//
LOCUS       WP_175916004             217 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175916004
VERSION     WP_175916004.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..217
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24067
     Region          29..180
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maevteraps krrtrgrpla easvgpdvil raarrtfakr gydatsvrev arelgidaal
       61 iahhfgaket lwlavveqia dlaeplfkal ralrtsslph rervrraiel cvdhefeepd
      121 igmffstaat eeggrldclq qrivrpyhda mfplladave ageirpvdpn vlffmiasav
      181 gttvsyshmm leftslptrq dafrqavldv alsilrv
//
LOCUS       WP_175916122             297 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ParB/RepB/Spo0J family partition protein
            [unclassified Burkholderia].
ACCESSION   WP_175916122
VERSION     WP_175916122.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..297
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31938
     Region          29..290
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mnavpkkkgl grgleallgg saditeavki egapntlalg klqagkyqpr trmdegslqe
       61 laasiraqgv mqpilvrpis sdkyeiiage rrfraarlag ldevpvlvkd vsdqaaaama
      121 lieniqredl npleeahgiq rlldefgfth eqaaesvgrs rsavsnllrl lnlaapvqtm
      181 llagdldmgh arallavdaa tqitlahqvv nkrmsvrete klvahttkea pavkvrakdd
      241 ggrdtrrlee elsdllastv kiklgrrgrg qvmidfgnld alegilarlr gnvatee
//
LOCUS       WP_175916133             309 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175916133
VERSION     WP_175916133.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34754
     Region          7..>143
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrflsieaf vrvaeassfa eaarqlgvts svvtnriqql ekfvnaplfh rstrhvrlse
       61 vgetfyreca evvgrvnelt dqmrelratp tgrlriqmlp gfaldhfgvp laefnrrypg
      121 iqldiivndr vvdpveegfd iafqifppis eslierrlfv vrrlfcaapa yleahgapqh
      181 prellqhtta lysgypsrnr wtltrgdevv emelpgmirs nsvhllreya ltgggvvclp
      241 tlvasdalva grlvpiltdf qiaplsfaav ypatqrqalk vkalveflve yigdetpwdr
      301 pllergwvr
//
LOCUS       WP_175916051             413 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: mechanosensitive ion channel family protein
            [unclassified Burkholderia].
ACCESSION   WP_175916051
VERSION     WP_175916051.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..413
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45151
     Region          69..387
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mtlneswfap lvgilillaa agaitatahf llfrvvarla rlsatridda lfefgafkwl
       61 nrivpfvvik lglgavpgip avaaqaadkv lfalivflvs mtisatlsal ehthrtsrrd
      121 qprlslkgam qlvklvmfit aalvvigdat gkqiglllsg igamsavlml ifkdtllglv
      181 agvqlssndm lrigdwitmp sagadgtvid itlntvkvan fdhtiitvpt wklitesyqn
      241 wrgmteaggr rikralfvda tsvrflgnde ierlerltll kdyledkvda iaqwngtlga
      301 agecqanrrq ltnlgtfray vanylkghpr irrdmtcmar qlpltaegip lelycftdtt
      361 twvdyeaiqs dlfdhliavl pefglrvyqh psgfdmrrma gaaqaelsap har
//
LOCUS       WP_175916161             317 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175916161
VERSION     WP_175916161.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..317
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34270
     Region          11..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..291
                     /region_name="PBP2_CrgA_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08475"
                     /db_xref="CDD:176164"
     Site            order(103,107,146,161,163,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176164"
     Site            order(104..105,109..110,112..113,116,120,122..128,190,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176164"
ORIGIN      
        1 mderlrgive fvdvvesgsf aaaalrlgmt rsavakivar leqrlgarll qrttrqlglt
       61 deglvyyeqc rrllaelget eaaldagrre ptgrvrvsvp vlfgrqcvap vvrrlverhp
      121 rleidvsfsd riadlvndgf diavrigtla dtsalvgrkl gvqrmgicas payldrhgrp
      181 sgldelashg giaysrggqp tpwriigadg avhdhrpagr lrfddlqaia daaaagagla
      241 wlpcwlmapy vrdgrlalvm dsdsvsgaev fvvrpasrnv pmkvrvvida lvdeiprmla
      301 sddadgervp qrivqas
//
LOCUS       WP_175916162             649 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: arylsulfatase [unclassified Burkholderia].
ACCESSION   WP_175916162
VERSION     WP_175916162.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..649
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=69480
     Region          47..615
                     /region_name="PAS_like"
                     /note="Bacterial Arylsulfatase of Pseudomonas aeruginosa
                     and related proteins; cd16025"
                     /db_xref="CDD:293749"
     Site            order(57..58,95,156,158,263,406..407,466)
                     /site_type="active"
                     /db_xref="CDD:293749"
     Site            order(57..58,95,156,158,263,407,466)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293749"
ORIGIN      
        1 mkksasplha frfrvvcaai agalslascg gvdsdpppqa natpaakrpn ilyimaddlg
       61 ysdihafgge istpnldalv asgrilsnhh tgtvcaitra mlisgtdhhl vgegtmgvpt
      121 derrglpgye gylndralsf aqllkdagyh tyiagkwhig sgivgsatgs gqtpdqwgfe
      181 rsyvllagaa tnhfahepag ssnytedgsy vqpgqpgqpg gaggspavfy stdfytqkli
      241 syidsnkrdg kpffayaayt sphwplqvpd pwlhkyagvy dagydairna riarqkalgl
      301 iptdfkpfdg lpettsasla tanngtanak yisavhsaad gysdygtgkv dklwaslspa
      361 erraqaryme iyagmvenld yniglliqhl kdigeydntf imfqsdngae gwpidsgadp
      421 tatdtangqd pvystlgtdn gkqnaqrlqy glrwaevsat pfrltkgysa eggvstptiv
      481 rlpgqtrqlp tlrafthvtd ntatflavag vtppsqpapp lvntltgvdq nkgkvvynnr
      541 yvypvtgqsl lpvltgsatg evhttpfgde aygraylrsa dgrwkalwte pplgpldghw
      601 qlydlaadrg ettdvsaqnp svistlvdqw ktymsnvggv eplrprgyy
//
LOCUS       WP_175916172             197 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175916172
VERSION     WP_175916172.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..197
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22036
     Region          11..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkkgtdtngs apdtrerilq tastlfyqeg travgvdliv aragvaktsl yrhfatkddl
       61 ieafllreda dfwahwdava aqyrrtpree ldaqlqwige rierpgyrgc pqiniaaeya
      121 dgnhparkva vahkqelrrr ltelasamri depetyalrl atvidgalss gqalhahgpv
      181 rflqefaqll mpkkark
//
LOCUS       WP_175916176             319 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1638].
ACCESSION   WP_175916176
VERSION     WP_175916176.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1638
  ORGANISM  Burkholderia sp. BCC1638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia sp. BCC1638"
                     /db_xref="taxon:2681391"
     Protein         1..319
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34962
     Region          15..74
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          103..304
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(119..120,122..123,126,130,132..138,235..240,
                     246..247,249..250)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mldnisikrh amldlddlrl vraigasrsl asaarlldlt ppavtirlqr mearlnvrla
       61 vrqpkgialt degqrlyqea vgilerveal pvnisgdhgd vqgtlrvvap fgfgrkyvar
      121 ivrdvqrahp kleislhlse spltsasgad vvihvgglks sswigyplap nerflcaspg
      181 yarrikelnh psdlarydcl clrendedvp rwrfsqtgdg kgesrrltvi rvtgalssnd
      241 gtvvtdwala glgiversew dvapllasgk lvrllpdwhl ppapvtallp srtgrsarqr
      301 vflqvatqfl dpppwrgka
//
LOCUS       WP_175916191             212 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Burkholderia].
ACCESSION   WP_175916191
VERSION     WP_175916191.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..212
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22463
     Region          19..207
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtasaavlai laalwlgami pgpsfvlvar nsiglsrrdg latalgmgvg giafggvala
       61 glytllqave wlyvglklag gayliymask iwrgadrpia mddsqavvag sarksfwtgl
      121 ttqlsnpkta iwygsifaal lpqhpplwcy lalpplvfgv efgwytlval cfstrrprel
      181 ylrakkwvdr vaagaitllg lrliltapka gi
//
LOCUS       WP_175916202             797 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: penicillin-binding protein 1A [unclassified
            Burkholderia].
ACCESSION   WP_175916202
VERSION     WP_175916202.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..797
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=87247
     Region          24..742
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mpmqstspts pppapepkkr swwlkvligl aamcvalvva gglvlgyalv vawpnmpsld
       61 altdyrpkvp lriytsdhvl igefgeerrd ivhfkdvpds lkkailaied arfydhggvd
      121 ltgiaragfv altnghasqg astitmqvar nfflssekty trkiyemlla yrieraltkd
      181 qilevymnqi ylgqraygfa saarvyfgkd lkditlaeaa mlaglpkaps aynpvvnpkr
      241 akvrqeyilq rmlelnfitr eqydeavaqp lvvkgagref svhaeyvaem vrqmmyaqyr
      301 eetytrgfnv vttidsadqq vaytalrkgi mdyerrhgyr gpegfielpa gaddreqaid
      361 dallehpdng elvaavvtaa tsrqitvafi dgssatiegd nlrfasgals asaqpnrrir
      421 pgaivrvvkn dagkwaitql pqvegafisi vpqdgairsl vggfdynknk fnhvtqawrq
      481 pgssfkpfiy sasldkglgp atvindgply fsaaetggqp wepknygggf egpmsmrtal
      541 qrsrnlvsir ilnhigtkya qqyitrfgfd adrhpaylpm algagqvtpl qmagaysvfa
      601 nggfrvnpyl iaevtdpnga ivaraqplia eqnapraida rnayvmnsll qsvaqrgtga
      661 rtnvlkrtdl agktgttnds hdawfagyqh tlaaiawigy dnprslgdre tggglslpvw
      721 idymgaalkg tpefkptmpd dvqalgsely fteftpghgf vstvgvpqap amqntdepvp
      781 hvdeqekqdi mnlfrgh
//
LOCUS       WP_175916233             731 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [unclassified
            Burkholderia].
ACCESSION   WP_175916233
VERSION     WP_175916233.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..731
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78501
     Region          18..731
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mgkatgsvrr aiaiaaggtl caaaaggvha qasdtatata ppadtaallp kidvtgaadr
       61 aslglvglrt atatrtdtpv aeipqttnlv taqqiemtga tdlnqalryv pgfatfgads
      121 rtdwyaalrg ftptlyvdgv papntavian wrvdpytids iavlrgptsv lygagepgai
      181 vdahtkladg erireagvri gndarketml dvgdtldpdg kyayrfigva rdgnaatgpn
      241 adrrvavaps frwrptadts ltvsasflqd hgdissnflp asgtvlpnpn grlsqdiymg
      301 dpafndyrkk qwslgyaleh rvdsiwtlqq dvrwsrlsld datvfgnglv pgsttnmmrt
      361 aglfqlnysr ldidnraqar fatgplehtl llglqfdrqt ttnsvwlala pslnlyhpvy
      421 lpvtaaifsg rtslgrfdqy tamntlgaya qdqirwnrwt ltlggredrv sarfddrvag
      481 tgtqqdvsaf sgrigltwqg daglapyisy stsfdpvigv rmyggglpkp trgrqteagl
      541 rwqphgrnlm ltaavyridq tnvvtpapps ldptgtssvq tgkvrsrgve lsavgkvtre
      601 lsivasyayq dvknvqanda slnnwpvsvp lprqmaslwa dwtwhggala gvgigagvry
      661 qsalagapdn sltvpsttly dlamhydlrh wrlalnvanl fdrryvsgcq syavcvfgne
      721 rtvlasakyn w
//
LOCUS       WP_175916249             167 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [unclassified Burkholderia].
ACCESSION   WP_175916249
VERSION     WP_175916249.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..167
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17567
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mysnilvald gsdtssrald aalnlasetg arltpvyvvd flvpaydtyg ydpsilidaf
       61 reeglrvted aakrmkardv agtprisnva psgedvaqhi valageikad livmgthgrr
      121 gfqrlflgsv aervlrqatc pvlmipasca akaaaettaa stekeps
//
LOCUS       WP_175916252             374 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia].
ACCESSION   WP_175916252
VERSION     WP_175916252.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13386660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..374
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40294
     Region          13..>122
                     /region_name="YhgE"
                     /note="Uncharacterized membrane protein YhgE, phage
                     infection protein (PIP) family [Function unknown];
                     COG1511"
                     /db_xref="CDD:441120"
     Region          174..370
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 msrllvifrl gvkelwslar dpillalivy tfsasiyvaa tarpetlhkv piaivdedas
       61 plsariaaaf fppqfapppi vdagaadrgl ddgdytfsld ippdfqrdvl agrhatvqln
      121 vdatrmtqaf tgggyvqqiv ageidafvrr hrgtslppvd lamrmrfnpn ldevwfgalm
      181 elinnvtmls miltgaalir erehgtiehl lvmpvtaaei mlakvwsmgl vvaaaavasl
      241 tfvvggalhv pipgsvplfv agmalhlfat tsmgiflatl vrsmpqfgml lvlvllplql
      301 lsggltpres mppvvqdiml aaptthfvel aqrilyrgag ldavwaqfaa lfaigcvlfl
      361 lsltrfrkti gqmt
//
LOCUS       WP_175916256             263 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: polysaccharide deacetylase family protein
            [unclassified Burkholderia].
ACCESSION   WP_175916256
VERSION     WP_175916256.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..263
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29140
     Region          91..245
                     /region_name="CE4_NodB_like_5s_6s"
                     /note="Putative catalytic NodB homology domain of PgaB,
                     IcaB, and similar proteins which consist of a deformed
                     (beta/alpha)8 barrel fold with 5- or 6-strands; cd10918"
                     /db_xref="CDD:213023"
     Site            order(97..98,153,157,201..203)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213023"
ORIGIN      
        1 mafrliacll llscmppass advatvdsps qrvlilvyhr faaaqldsmt vrtetfrhql
       61 qaieangyri vpladvvrwh ggqadavpar avaitvddgh rsvydvlrpl lvahpmpvtl
      121 fiypsaisna syamtwdqlr tlgqsggvdi eshtywhpnf rterarltpd dylrfvsfql
      181 srsrerlese tgqpvrmlaw pfgvhdaqtd qlaaregyva aftldarpvr vtdpamalpr
      241 ylmtdacdtr cmngllrtag gkp
//
LOCUS       WP_175916298             220 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: HEAT repeat domain-containing protein [unclassified
            Burkholderia].
ACCESSION   WP_175916298
VERSION     WP_175916298.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..220
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=24411
     Region          122..>216
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
ORIGIN      
        1 mhrtvtqaai ntlsmhalnt lheqvekfre waalypvhqr sveweceygh wealwdasla
       61 vvdslapaaw tatacadlly aiardqaleh issmlwtqpd allalarasi dasepnakwq
      121 laarlgglgs haaeaeglll rlvddedeyv rrrallalga lksthaeala erawhtghey
      181 qriaalwvlk niqsgklvqy vklaeadgre yvvrnardvs
//
LOCUS       WP_175916284             305 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [unclassified Burkholderia].
ACCESSION   WP_175916284
VERSION     WP_175916284.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5), 4725 (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10084616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..305
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=30970
     Region          1..126
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          <198..286
                     /region_name="COG3945"
                     /note="Hemerythrin domain [General function prediction
                     only]"
                     /db_xref="CDD:443145"
ORIGIN      
        1 myrhllvtvd gmpggidaig halelaravg arvtfvlsaa apdsrlsgar mpehgakvea
       61 aaraqglsha iagagrpgag daspatlage lgcdliavaa lphdadaaat aqrwvllats
      121 gvpvlvcpar rapaearvma rclaahralg eqlqaltmtm asdtpdaatr ptgdaggpla
      181 alaslaalqn arfgasaear lfaalrmrae staaeldeld rqrrrdahal dalarlaadg
      241 lpsaafdaal adyargafeq mgriegvifp aarrylgdad wneldappas gtvattpgad
      301 epdda
//
LOCUS       WP_175916306            1048 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit [unclassified
            Burkholderia].
ACCESSION   WP_175916306
VERSION     WP_175916306.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..1048
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114624
     Region          11..1027
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msgpreegrf nlsawalrhq alvvyliala tlagilaytr laqsedppft frvmvirtfw
       61 pgasarqvqe qvtdrigrkl qetpaidflr sysrpgesli fftmkdsapv kdvpetwyqi
      121 rkkvgdigyt lppgvqgpff ndefgdvytn iwtlegdgft paqlhdyadq lrtvllrvpg
      181 vgkvdyfgdp dqrifieadn tqltrlgisp qqlgqainaq ndissagvlt taddrvfvrp
      241 sgqfdnvaai adtliringr tfrlgdlatv krgyddppvt qmrtkghavl gigvtmqpgg
      301 dvirlgkald veskdlqaql paglkltlvs smphavshsv ddfleavaea vaivlvvslv
      361 slglrtgmvv visipvvlav talfmylfdi glhkvslgtl vlalgllvdd aiiavemmav
      421 kleqgysrar aaafaytsta fpmltgtlvt vsgflpiala ksstgeytrs ifevsaiali
      481 aswfaavvli pllgyhllpe rkkhaheahl pddhehdiyd trfytrlrgw idwcierrfv
      541 vllitgalfv valmgfslvp qqffpssdrp ellvdlrlpe gasfaatlre terlekvldk
      601 rpeidhsvnf vgsgaprfyl pldqqlqlpn faqfvvtaks vedreklatw lettlrdrfp
      661 avrwrlsrle ngppvgypvq frvsgddiat vrsiaekvaa tmrgdartmn vqfdwdepae
      721 rsvrfeldqk karalnvtsq dvssflamtl sgttvtqyre rdkliavdlr aprpdrvdpa
      781 klaglamptp ngpvplgslg rftpaleygv vwerdrqpti tvqsdvraga qgidvthaid
      841 gklnalraql pvgyqinigg sveesakaqt sinaqmplma iavftllmiq lqsfsrvlmv
      901 vltaplglig vvgtlllfgq pfgfvamlgv iamfgiimrn svilvdqieq diaaghgrfd
      961 aivgatvrrf rpitltaaaa vlalipllrs nffgpmatal mggitsatvl tlfylpalya
     1021 awfrvkrder dprdgpphdg spaapsga
//
LOCUS       WP_175916315             386 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Burkholderia].
ACCESSION   WP_175916315
VERSION     WP_175916315.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..386
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41894
     Region          25..386
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mnsqsgapva gapsfvpssg adaraenfvq ivdvvkkfge tevvrnvnlt vrqgelfall
       61 gssgsgkstl lrmlagletv tsgkilidge dlaqmppykr pvnmmfqsya lfphmsvesn
      121 vayglkqegt pkaelkerva aalelvqmsk yakrkphqls ggqqqrvala rslvkrpkvl
      181 lldepmsald kqirqrtqie lvnilnkvgv tcimvthdqe eamtmanrla vmsegqivqi
      241 gspnevyeyp nsrfsaefig stnlfegvtv edepdyvyie spelpsrlyv shgitgplgm
      301 svtvsvrper ialtrkppeg afnwargkit nvaymggysl yhvkldagkt vianvsslai
      361 seldtpslgd eiyvrwsata gvvlts
//
LOCUS       WP_175916322             308 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sugar kinase [unclassified Burkholderia].
ACCESSION   WP_175916322
VERSION     WP_175916322.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..308
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32037
     Region          7..272
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(34..35,38,90,103,105,134,167,253,256)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mtaafpqila lgeamiefnq sqpgrpeflq gfggdtsnfc iaaarqgast gfvsaigddp
       61 fgrlladmwa aegvdttyvr idrsaptgvy fvthgadghq fdylragsaa sryavadlpl
      121 dalavakavh lsgislaist aacdaafaai dhargngaqv sfdtnlrlkl wplpraravm
      181 realrqtdic lpswddvtal tgandrdaiv damlehgprv valklgkega yvatpnerrv
      241 vpgfaveavd atgagdcfgg afvarivagd dpfaaaryan aaaalsttgf gavapiphre
      301 averlmqg
//
LOCUS       WP_175916382             136 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: group II truncated hemoglobin [unclassified
            Burkholderia].
ACCESSION   WP_175916382
VERSION     WP_175916382.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Keppner,A., Maric,D., Correia,M., Koay,T.W., Orlando,I.M.C.,
            Vinogradov,S.N. and Hoogewijs,D.
  TITLE     Lessons from the post-genomic era: Globin diversity beyond oxygen
            binding and transport
  JOURNAL   Redox Biol 37, 101687 (2020)
   PUBMED   32863222
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Bustamante,J.P., Radusky,L., Boechi,L., Estrin,D.A., Ten Have,A.
            and Marti,M.A.
  TITLE     Evolutionary and Functional Relationships in the Truncated
            Hemoglobin Family
  JOURNAL   PLoS Comput Biol 12 (1), e1004701 (2016)
   PUBMED   26788940
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Wajcman,H., Kiger,L. and Marden,M.C.
  TITLE     Structure and function evolution in the superfamily of globins
  JOURNAL   C R Biol 332 (2-3), 273-282 (2009)
   PUBMED   19281958
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Vinogradov,S.N., Hoogewijs,D., Bailly,X., Arredondo-Peter,R.,
            Guertin,M., Gough,J., Dewilde,S., Moens,L. and Vanfleteren,J.R.
  TITLE     Three globin lineages belonging to two structural classes in
            genomes from the three kingdoms of life
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11385-11389 (2005)
   PUBMED   16061809
REFERENCE   5  (residues 1 to 136)
  AUTHORS   Wittenberg,J.B., Bolognesi,M., Wittenberg,B.A. and Guertin,M.
  TITLE     Truncated hemoglobins: a new family of hemoglobins widely
            distributed in bacteria, unicellular eukaryotes, and plants
  JOURNAL   J Biol Chem 277 (2), 871-874 (2002)
   PUBMED   11696555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10201300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..136
                     /product="group II truncated hemoglobin"
                     /GO_function="GO:0005344 - oxygen carrier activity
                     [Evidence IEA]"
                     /GO_function="GO:0019825 - oxygen binding [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15806
     Region          15..133
                     /region_name="TrHb2_PhHbO-like_O"
                     /note="Truncated hemoglobins, group 2 (O);
                     Pseudoalteromonas haloplanktis PhHbO like; cd14773"
                     /db_xref="CDD:381282"
     Site            order(47..49,55,58..59,62,73,82,85..86,89,91,95..96,99,
                     124,127..128,131)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381282"
ORIGIN      
        1 mtdvndeaps qptafelvgg etrvremvdr fydlmdlepe faeiralhpa sldgsrdklf
       61 wflcgwlggp dhyisrfghp rlrarhlpfp iasverdqwl rcmawamedi glveplrerl
      121 mhsfydtadw mrnrpg
//
LOCUS       WP_175916443             351 aa            linear   BCT 11-JAN-2025
DEFINITION  YncE family protein [Burkholderia sp. BCC1638].
ACCESSION   WP_175916443
VERSION     WP_175916443.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1638
  ORGANISM  Burkholderia sp. BCC1638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Burkholderia sp. BCC1638"
                     /db_xref="taxon:2681391"
     Protein         1..351
                     /product="YncE family protein"
                     /calculated_mol_wt=37543
     Region          48..251
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          203..>328
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mkhaghwrss lpllvalcgg fgasgpsihq afaagddtsi galplkhvad iplpgrptrl
       61 dyasldsprn rlmiahlgdd eviafdtras rviarisavs svhgvlavpe lsriyasatg
      121 sdeivaidva tlkivarmpg ghypdgmaya anmhklyvsd eygktetvid vrsnrrvati
      181 pldgeagntq ydpvsrhifv nvqtrrqlve idpatdrivd rldlpgakgn hgllieprsr
      241 lafiacednd tllvfdmrar rvvrafhigg gpdvlafdsa sdvlyvagea gvvsmfgvrg
      301 sdvvklgegr lgpnahvvav dpathrsyfp lkdvdgrpvl rvmetgraak p
//
LOCUS       WP_175916464             841 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: type VI secretion system Vgr family protein
            [unclassified Burkholderia].
ACCESSION   WP_175916464
VERSION     WP_175916464.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 841)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 841)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..841
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..841
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=91606
     Region          1..797
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 malfdsprtl svcgaampmy gdrpiltpvk ltggeavgel feytlelktp delgfsqsia
       61 anidldklig teltvsiqle gvghfirgla gnagianiga gtreitgivf rasilredgr
      121 sivyavtlrp wlwlatkncd crifqdmsvi eitdavlsty lfpvdkrltp prpnnvwpkr
      181 diqrqhhesd wtflqrlwee wgifyffeha dgkhrlvlcd aiaalkphge ayatiryeap
      241 nsrrvdeehi halsisnalt tgavtsvdyd ytrpradltv gredprdtgl ahhehytwgd
      301 yaqpqagkgg lsgasneprt eaeyltlvqm qayrcqglra sgqgnlrglv vgqtfvlshy
      361 pqnaanreya vigckltiee vgeasgsgqr yhceadfvlq pthepfrlpr tiakpritgv
      421 eyavvtcpen qeiwtdaygr vklqflwdrl gdndersscw vrvagawhgd qfggiflprr
      481 ghevevafan gdpdlpiivg savnafnmpp falpenqtla gfrskeigar rantlafddt
      541 ngriqahlss degtsqlnlg yitriagnag rkdergrgve lrtdgdgvfr aatgmlltte
      601 grpnaqghak amseairrle vaqslhvams daaqeaqaqe tdghqsdlak tidaqndqir
      661 gvesdgnpfp efsephlmid gkagveittp atvhvaaqqv altseghvgv asgrsffasv
      721 rdtislfaqr aairisaalg divlhaltss iklesaksiq lltkviqitg veklelqggk
      781 trmvlddsga qiftpgkfva fasthslpgp kdspvsltpk siciecllka arggsalvpr
      841 q
//
LOCUS       WP_175916476             291 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: mechanosensitive ion channel family protein
            [unclassified Burkholderia].
ACCESSION   WP_175916476
VERSION     WP_175916476.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..291
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32180
     Region          35..277
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mfldhlhper wtflwnalst lslrlcaala llvagwwlsk rignwlnrll ankervddtl
       61 rpilcdvavw girivaivga lsqlgietas vvavlgaagl aiglalqgtm qniaagimll
      121 llrpfkvgdf idggssvagt vdevglfmtr ltkpdgicey vpnsalwgsa irnytrnptr
      181 rldlevevsv hddidralda lralaeadpd vlqdpapdvm vmrfddstai anvrvwthpd
      241 tfwamrwrla rqvrktlada dcalpirtre lhivhdaeqq rradprrvqa s
//
LOCUS       WP_175916521             736 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: xanthine dehydrogenase family protein
            molybdopterin-binding subunit [unclassified Burkholderia].
ACCESSION   WP_175916521
VERSION     WP_175916521.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..736
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=77419
     Region          57..>192
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          200..728
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mtieldnrds vrpsrrtflk aagaaaavsl tigfewaglg rralaatapa adfapnaflr
       61 itpdgavtvi akhvemgqga ytgiativae eldadwstvr vesapadakr yanlafgtmq
      121 gtggssamsn swqqlreagg karamlvsaa aarwkvpage lttadgvvth aksgktaayg
      181 tlvadasklp vpdkvtlkqp adfklighri prvdgsaksn gtahftldtt fpgmrvallq
      241 rpprfgatvk sfdataakav pgvvsvvqvp ggvavvatgf waakqgrdal kidwdetnae
      301 krgseeimre yrqlaakpga sarkdgdada aiagaarkvs atyefpylah apmepldavv
      361 kltansceiw agdqfqtvdq gnaaraaglk peqvqihtly aggsfgrran awsdyvveav
      421 siakalgadg kpvklqwtre ddiqggfyrp myfhkldagl tadgklvgwr hrivgqsila
      481 gtpfeafmvk ngidatsveg aanlpyavpn vsveltttkv glpvlwwrvv gsshtayave
      541 afideaahaa gkdpylfrrd llekeprmra vlelaaqkag wdpakplpkg rgrgiavaea
      601 fksyvaqvae vsidadgkvk vdrvvcavdc giainpdiva aqmeggigfg lgaalhsait
      661 lkdgqveqrn fdgyhvlrma empkvevhiv psaeaptgvg epgvapvgpa vanaifaatg
      721 krhyvlpfds gdtaka
//
LOCUS       WP_175916527             473 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sigma-54 dependent transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175916527
VERSION     WP_175916527.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..473
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51878
     Region          35..147
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <171..471
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mnhccpirls gpqegerapc tppfvavrrh hgvpsrplvy lspcpdaglv dclasrgwdv
       61 wraksvadal nlvkanrlha givdfddfas pdvasfeall rdprigwval adderlrdat
      121 iarlirqccf gyardatadt tigylvghay gmlklaegdp avdaappggt migacdamrr
      181 lfatirkvan teatvfiage sgtgkeltas aihqhssrad apfvavncaa ipttllqael
      241 fghergaftg ahqrkigrie sahggtlfld eigdmpfesq asllrflqeg kierlgghts
      301 ipvdvrivsa thvdleaamq agrfradlyy rlcvlridep plrargrdim lladhilrry
      361 rgdsahrirg fmpcaieaih nyawpgnvre linrirfavv mtngplisav dlelnqytah
      421 rpptlaelrr qaerrtieet llrhrrqhad vaaelgvsra tlyrlmtahg lhg
//
LOCUS       WP_175916590             245 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [unclassified Burkholderia].
ACCESSION   WP_175916590
VERSION     WP_175916590.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..245
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25054
     Region          1..245
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mlaliiiagl waglqnalag ggsfvtlpal ivsgmsplaa nitstvalfp gqvttgwasr
       61 nmvrgagklp fralfaisvv ggalggllll ktpssifshl vpwlvlfatv vftwgsffrk
      121 pgadtqhigp vtaaisqfli aiyggyfggg igflmmaalt maglsprham stknalagvm
      181 nasavalflt sphlhwreal algggaivgg llgawalhrv nervlriaiv cigaaltvgl
      241 fakpi
//
LOCUS       WP_175916545             346 aa            linear   BCT 11-JAN-2025
DEFINITION  YncE family protein [Burkholderia sp. BCC1638].
ACCESSION   WP_175916545
VERSION     WP_175916545.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1638
  ORGANISM  Burkholderia sp. BCC1638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Burkholderia sp. BCC1638"
                     /db_xref="taxon:2681391"
     Protein         1..346
                     /product="YncE family protein"
                     /calculated_mol_wt=37061
     Region          33..251
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          203..>328
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mkhirngrfr llvlvamsia lvvtgivvqr vdaaaddlsl gslplkhvad iplpgratrl
       61 dyasldkgrn llfiahlgdg evivfdtqas rvaariadvs svhgvlavpe lsrvyasatg
      121 tdeivaidaa tlkivarmpg ghypdgmaya pamhklyvsd eygktetvid vqsnqrvatt
      181 pldgeagntq ydpasrhifv nvqtrrqlve idpatdrvvg rfdlpgakgn hgllidprer
      241 lafiacegnd kllvfdmrsk qviqsfavgg dpdvlafdpt lstlyvaged gvvslfrfka
      301 gtgdkigegr lgpnahvvav dlathrsyfp lkdvggrpvl rvaepk
//
LOCUS       WP_175916591             326 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175916591
VERSION     WP_175916591.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..326
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35486
     Region          12..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,232,249,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,195,
                     226..230,237..238,241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 medldgglvs gllvlaaiae sgsfgraasr lgrtqpavsr aiqrledrlr tklvhrtsrh
       61 vevtdaghel lskvrpllqg ieeataeasg qtslvngtlr vacdaafarl vlapelaqfm
      121 kdypalhlkl etrndvpdlv sdgfdlairf gtpsvstlvc rrlysprvlt vaapsyleqr
      181 grprspqdlv ddghecilai dpatgrpfdw efwrdnekvk vavngnltvt dagtkigacv
      241 agfgiaqlid lgidahlrag tlepiltdwr detfplyvyy psrnhvpakv rafidfvvgm
      301 mpglqskghg acqrlssaml etlhre
//
LOCUS       WP_175916633             469 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: phosphatase PAP2/dual specificity phosphatase family
            protein [unclassified Burkholderia].
ACCESSION   WP_175916633
VERSION     WP_175916633.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Pulido,R. and Lang,R.
  TITLE     Dual Specificity Phosphatases: From Molecular Mechanisms to
            Biological Function
  JOURNAL   Int J Mol Sci 20 (18), 4372 (2019)
   PUBMED   31489884
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Patterson,K.I., Brummer,T., O'Brien,P.M. and Daly,R.J.
  TITLE     Dual-specificity phosphatases: critical regulators with diverse
            cellular targets
  JOURNAL   Biochem J 418 (3), 475-489 (2009)
   PUBMED   19228121
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   5  (residues 1 to 469)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12932297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..469
                     /product="phosphatase PAP2/dual specificity phosphatase
                     family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=49927
     Region          44..218
                     /region_name="PAP2_Aur1_like"
                     /note="PAP2_like proteins, Aur1_like subfamily. Yeast
                     Aur1p or Ipc1p is necessary for the addition of inositol
                     phosphate to ceramide, an essential step in yeast
                     sphingolipid synthesis, and is the target of several
                     antifungal compounds such as aureobasidin; cd03386"
                     /db_xref="CDD:239481"
     Site            order(119,127,153..155,190,196,200)
                     /site_type="active"
                     /db_xref="CDD:239481"
     Region          322..459
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
ORIGIN      
        1 msalgggaga gdglaesaag ardasfalrv gwlaamgavf fssygfanwl aarravvptf
       61 afgwehaipf vpwtivpyws idllyalsff fwtrrddlld hvkrlltvql vsvacfvawp
      121 lrfgferpda ggvagalftl lmgfdkpfnq apslhigllv vlwavyakql rgtvarfvlh
      181 pwfaaigvsv lttyqhhaid vptgaavgcl alflfplrda agrlpgatgs psaggralar
      241 ryafgaalva lvalgcvsra pgwalaagwa alalacvawi yrrgapgafq kddagrfpvf
      301 irwllaptia gafvnsrvwt frhpaparid ervsigript trdlrrhgft alvdltaemp
      361 rwaaadasla yasvpqldlv aptaaqlaaa vaalerlhad grdvliccal gygrsvlcaa
      421 awlaarrglg dardalaavr amrpravwsd dgvavlqgwi drrrvtgaa
//
LOCUS       WP_175916729             220 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [unclassified Burkholderia].
ACCESSION   WP_175916729
VERSION     WP_175916729.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..220
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24802
     Region          1..206
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mkimtgplsm fgakveiaah ekgiafervl vpfsqqrgyd pkhpdvlrin pkrqvpvlid
       61 gdleifdstq ifeyledlkp dpalwpaqpk aravarqleh csdevyfphv irlmgleetp
      121 dhpaaraard earqyyrrme rvladrkflg gtysyadiaf ymaqlfgark gapmtaetpn
      181 llawrermta rpavrkvaga magylasidh pvpdflrglh
//
LOCUS       WP_175916739             262 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: peptidylprolyl isomerase [Burkholderia].
ACCESSION   WP_175916739
VERSION     WP_175916739.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..262
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=28010
     Region          101..248
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mndvfsevat vpltingiai ddaaiaaeaa hhgdapdpld aarhalavre llrqravsla
       61 lidagapldd aavdallere lthvpepdra dceryyaqhp arfrrndivy ashvlfavtd
      121 rvplaplrqr aeraladvva apdtfeavar assncpsaqv ggslgqllrg dtvpefeaal
      181 fdtdglgvlp klvntrfgfh ivrierrvpg dvvpfdeaag qiaaylserv rqramrqyva
      241 ilasgarveg vtfdgangpl vq
//
LOCUS       WP_175916755             413 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase, partial
            [Burkholderia sp. BCC1638].
ACCESSION   WP_175916755
VERSION     WP_175916755.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1638
  ORGANISM  Burkholderia sp. BCC1638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Burkholderia sp. BCC1638"
                     /db_xref="taxon:2681391"
     Protein         <1..413
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
     Region          <1..240
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          309..411
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 fpgfpaaeil ynddgsvkgv atgnmgvgkd geptenfqlg melhakytlf aegcrghlgr
       61 qliakfklda nadpqaygig ikelweidpa khkpglviht agwplksdty ggsflyhmdn
      121 nqvvvgfvvg lgytnpylsp feefqrykth psiraflegg krvsygarai taggllslpk
      181 tvfpggalig ddagflnasr ikgshaaikt gmlaadaafd avqagrqsde lnaypdafkq
      241 swlytelyra rnfkqwmakg lylgtlmvgl eqkvmggnvp wtlrhqhadh emlkpasqcq
      301 pieypkpdgk ltfdrlssvf isntnheenq pahltlkdas vpvdvnlrty agpegrfcpa
      361 avyefvkndd gsdrlvinaq ncvhcktcdi kdptqnivwv tpeggggpny pnm
//
LOCUS       WP_175916758             666 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acetyl/propionyl/methylcrotonyl-CoA carboxylase
            subunit alpha [unclassified Burkholderia].
ACCESSION   WP_175916758
VERSION     WP_175916758.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..666
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70872
     Region          1..460
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          598..662
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(620,629..631,638)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            630
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mfdkilianr geiacrvaat ckrlgiasva vysdadanak hvaacdeavh iggsaaadsy
       61 lrieriieaa ratgaqaihp gygflsened fahaceaagi afigppvdai aamgskaaak
      121 almhaaavpl vpgyhgddqd aanlhreade igypvllkas aggggkgmrv versedfpaa
      181 lascqreaas sfgndrvlie kyltrprhve vqvfgdthgn tvylfdrdcs vqrrhqkvle
      241 eapapglhed vrqamgeaav aaaravnyvg agtvefimtg dafyfmemnt rlqvehpvte
      301 mvtgldlvew qlrvaagepl plqqdelrvq ghaiearlya enpargflps tgtlkhlrlp
      361 egvefaigaa vrvdsgvreg daitpfydpm iaklivhgad reealgrmlr alracevvgl
      421 htnaaflqri vtcapfaiad ldtgliernh aalfapqqpp ratlalacaa llarereaaa
      481 regaspwrvl pdwrlnggyr rtlewhaper eadvtvtyld dggstriatg daaaqpfawa
      541 rgvtpldfdv tldgvrssgr vyadgdsfhv ftqgvaetfe wrnvlahagd aehgggrlta
      601 pmpgkviavl vepgqkveag tplivmeamk mehtigapga gvvaevlygv gdqvadgaql
      661 lmmaeg
//
LOCUS       WP_175916760             248 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175916760
VERSION     WP_175916760.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..248
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27266
     Region          27..184
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtaatadtmt ttakadrpep srapagrksq qrvqdilrag revfaekgye hataaeiaqr
       61 vgvseatvfs yfrgkrelca rviadwydei iaafeigmpq easvqqqfaf ivrthlrlml
      121 vngtglcalv lsegrakqha lsdeltalqr rytaplmdvl argqaagqvr sdmplsllrs
      181 mvfgpiehvl wdailghrkl dtettatqli dmlwaavqpp apeqaalvrf rnevaeavrr
      241 legeasrp
//
LOCUS       WP_175916765             728 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia sp. BCC1638].
ACCESSION   WP_175916765
VERSION     WP_175916765.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1638
  ORGANISM  Burkholderia sp. BCC1638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 728)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Burkholderia sp. BCC1638"
                     /db_xref="taxon:2681391"
     Protein         1..728
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78203
     Region          59..728
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mpsrrlprra rtlrpwrasl palitlcvas gahadaepaa taspatssps stpapperel
       61 ptisvtasaa adptvgyqpr tssvaggddr plkeipqsva vvsssvmqdq qarslddvlg
      121 nisgvtqtnt lggtrdafik rgfgsnndgs vlvdgvrtpv lhsylatidr vevlkgpasl
      181 lygmqdpggv inlvtrkpee tfggsisasr tshggssaqf dltgplgkpg qvaggtlafr
      241 ltgeydtsry wrsfgrerna liapalswhd antsidvryq yvdytmpfdr gtvlvngrpd
      301 dalryrryee awaqsggiqe tlrariehrl sdawrvraty gwgrdrydqy itratafnat
      361 tgalsrtsda nlgrndsdqi atlgllgnlt lagmnhalyi ggeyerqrsf rgdtirgaat
      421 kgfnlydpvy gllapggtvs tkqsdslskv htysmivqds vkitdrltav gglrweewqq
      481 esgmgrpfvf adrshgnvwl pqfglayalt psltayanvs rsfkpnvasn vaaplapefg
      541 rvleaglkfs lkpgitgtla ayqidkrnva vtvgditsti gtarsrgiel dvagqltrhl
      601 sligsyaytn andrdsntpl vnvarhtgsl favydtaian lpgrwrfggg arlvgarpgd
      661 tansftlpgy vtvdafaaye ttigkfptri qlnvknlldk tyypssnsnl ivavgeprlv
      721 tltttvsf
//
LOCUS       WP_175916776             732 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: penicillin-binding protein 1A [unclassified
            Burkholderia].
ACCESSION   WP_175916776
VERSION     WP_175916776.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 732)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..732
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=80509
     Region          37..704
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mnrfvpflrd lwlrcrtgar vlgagawhrl rhptrrgval tlaaipvlgl lvllafvpft
       61 psigdirkar idrparvlsa dgqliaefrp vnrewvplkq isphmvdali atedhrfyah
      121 hgidwrrtla aglhtfsgsr qggstitqql arnlypdevg raptltrkvk elitafkiet
      181 vyskdeilet ylntvpflyn aygvemaart yfgksadqld ivesatlvgm lkgnsyynpv
      241 lnperaeqrr nivlarmaam gmlsprqlaq lqrrplrvdf epqtaqpgpa phfavqlrkw
      301 liawadrnny dlyadglvvr ttldaqlqdm atqaltqqtd rlqaiaddaw hnpsgcglrn
      361 dlfrgfirqt pdyraardag ladaaalkql ganhafiral cerktqvqag fvaidprnga
      421 irawvgspdf gsepfdhvvq arrqpgstfk pfvygaafad gmrpgdtfvd rpvaipigah
      481 avwhptdaep ptdapmtlrd alalsrnrit aqvmqregaa rvaqlaramg vrdsaldavp
      541 slalgtspvt lkemvsaygt ianrgvyvap qmitriedrd gkvlaafgsa pperalpvaa
      601 aqtlvdvmrg vvdygtgadi rsrygirvdv agktgttqdn tdgwfilmhp qlvagawvgf
      661 ddgsvtlrsd ywgagahsal pivgsfydaa lraraidpra qfspdfrprs apapvpkrhp
      721 hpglfdwlki fr
//
LOCUS       WP_175916786             403 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: benzoate/H(+) symporter BenE family transporter
            [unclassified Burkholderia].
ACCESSION   WP_175916786
VERSION     WP_175916786.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..403
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41463
     Region          15..403
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mnpsptasag raggrrfftd tsvstlvagf vammtgytss lvlmfqagra ahltdaqiss
       61 wiwalsigma lttiglslrf rapvvvawst pgaalliasl pgvpyaeaig afvvcalllt
      121 aiglsglfdt lmrripagia aallagilfe igieifraaq fqtalvlamf ftylivkrla
      181 pryaivttli vgtavagglg lldfsrfhia laqpvftmpa fsiasivsig iplfvvamas
      241 qnvpgiavlr adgystpssp liattglasl llapfgshgv nlaaitaaic tgpeahedha
      301 krytaavwcg tfyliagifg atiaalfaal pkalvvsvaa lalfgsimsg lanamqdvkq
      361 reaalvtfmv tasgltllsi gsafwglvag ivtqvilnar rpa
//
LOCUS       WP_175916804             439 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Burkholderia sp. BCC1638].
ACCESSION   WP_175916804
VERSION     WP_175916804.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1638
  ORGANISM  Burkholderia sp. BCC1638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 439)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 439)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 439)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 439)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 439)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia sp. BCC1638"
                     /db_xref="taxon:2681391"
     Protein         1..439
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46193
     Region          54..373
                     /region_name="RepA"
                     /note="RecA-family ATPase [Replication, recombination and
                     repair]; COG3598"
                     /db_xref="CDD:442817"
ORIGIN      
        1 mtdhlaeldl dravdagrvk aareaffara pgsndtqarp avtitrasnv vpeairwlwp
       61 gwlpegkltl lagspgtgkt tlalaltatv trggtwpdgs acnhagdvli wsgednpadt
      121 ivprlmaaga dldrvhiitg rtdeagellp fdpaadmpll aerlsdmcda qllildpivs
      181 avsgdahrvn dvrrnlqslv dmasahhccv lgishfakgt kgsspaervi gsqafvalar
      241 mvlvagkdea aerrilarak sniapddggv ayslemtetd gitasrvawg alidgsardi
      301 lgdverqdee tktervease flegllsdgp msskqvrkda deagfswrtm hraadalgve
      361 krkigmkegw qwaipkmpss ehanedatly tvassgsrgt fgnhgglrav dfgssaedan
      421 pkgvspsgss sasepggdv
//
LOCUS       WP_175916854             452 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cytochrome-c peroxidase [unclassified Burkholderia].
ACCESSION   WP_175916854
VERSION     WP_175916854.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..452
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=48597
     Region          79..443
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mhsllkslaf arslipaaat lalmgglapl agcdarpgan aqavsvvsaa qaapaapaap
       61 avapagqpqt raqvfegvkq mtalgkqlff dpslsgsgkl acaschsveh afgppnalsv
      121 qlggddmhrm gfravpslky vrgippfteh fhdspdegde sidagptggl twdgrvdtrd
      181 aqaripltsp femsssparv aqavraapya dafrkafgdr vlgddqatfg avlraldafq
      241 qqpalfdpyt skydaylagh aqltpaelhg lqlfndekkg ncaschvsqr tleggppqfs
      301 dfgliaiavp rnralpvnrd prfhdlgacg pertdlkgrd efcglfrtps lrnvalrktf
      361 fhngvyhsle dvmrfyverd ihpekfypvv hgkvqvyddl pkrywpninr eppfdrkrgd
      421 apalnaaeik dviaflntlt dgyqpaatsa ar
//
LOCUS       WP_175916871             506 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CoA-acylating methylmalonate-semialdehyde
            dehydrogenase [unclassified Burkholderia].
ACCESSION   WP_175916871
VERSION     WP_175916871.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..506
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53716
     Region          13..490
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(70,72,76,79,83,116,119..120,129..136,141,144,147,
                     240,244,247,250,252,426,428..429,431..432,435,438..439,
                     441,443..446,455,459,461,475,482..487,489..490)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(156..159,167,182,185,215,232..235,238,256..258,290,
                     391,393,419)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(159,256,287,290)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnpvpaytsd advghyvdga pvagrsgrfq dvlnpalgra vrrvalagdd evqqavasah
       61 aafpawaatp pirrarvlhr flqlmnehrd vlaaiitaeh gkvfsdaqge vargidiief
      121 acgvpqllkg dftdqvstgi dnwtmrqplg vvagitpfnf pcmvpcwmfp valatgntfv
      181 lkpserdpsa alfmadlltq aglpagvfnv vqgdkgavda lldhpdvqav sfvgstpiaa
      241 yvqqravqsg krvqalggak nhlvvmpdan ieqavdalig aaygsagerc maisvavlvg
      301 dvadkivpav aerarklvig dgmspevemg pivtgealkr iegyieqgvs egaqlvvdgr
      361 glrvpgreag fftggtlfdh vtpdmriyke eifgpvlgcv rvkdfgeavd linahefgng
      421 vscftsdggi arefarriqv gmvginvpip vpmawhgfgg wkkslfgdmh aygeegvrfy
      481 trqksvmqrw assigkgaef amptak
//
LOCUS       WP_175916860             304 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175916860
VERSION     WP_175916860.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33022
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          90..273
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(105..106,108..109,112,116,118..124,216..221,
                     227..228,230..231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdlaalaifr avvrengitr aaaklnrvqs nvttrikqle eelgaalfvr dgrrlvltpa
       61 ghtllpyaer lleladeard avredtprgr lrlgtmesta asrlptvlar yhhawpdvsl
      121 elvtgttgwl idkvrdfeid aalfarppep dtlpdtfetv pifredlvll tprghppvrt
      181 prdvilptli afergctyrk yverwyaahg mkparvlelg syhaivacva agagiavapr
      241 svlelqpetg nvaahtiael egidtllawr hgyasaalaa lrdalgdaar esgdavkpsv
      301 atpv
//
LOCUS       WP_175916876             200 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: YbhB/YbcL family Raf kinase inhibitor-like protein
            [unclassified Burkholderia].
ACCESSION   WP_175916876
VERSION     WP_175916876.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..200
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=20770
     Region          43..199
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mrvdrritsp aspgrpspfi aalpcaaacv afavlparae gpftvssndl tpggrvsaan
       61 vfdrgdckgg nrspqlswrn pppgthgyai tifdpdapgh gwwhwavagi pasvtslpad
      121 asasgflrri gasearndfg vdgyggpcpp pgkphryvit vyalkgtdlr vaqgrpapmf
      181 eheigtlaig taqltvtygq
//
LOCUS       WP_175916934             766 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor [unclassified Burkholderia].
ACCESSION   WP_175916934
VERSION     WP_175916934.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 766)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..766
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81461
     Region          48..724
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mketdgakrr fvarragvtl cfggmlggwl tpasaqvepa gnvdaptlap ivvvgttpll
       61 gigtplsrvp anvqtirged itrqhggvlt dyfeknvssv dineaqgnpy qtdvnyrgft
      121 aspvvgtpqg lsvfvdgvrv nepfgdvvnw dlipqvaidt mqlipgsnpt yglntlggal
      181 aittkngkts pggaaqvsvg swgrktaqie qggriggnld yyvtgnvand ngwadhnasr
      241 vrqgfgklry tdadttlsis aggadnalqg sqtiprsfld nraqaytypd lnrnsaayvt
      301 vsgdhsfgdh vqlsgnvyyr hyrntntssn vnddfgsvdg sgatdavqat ndrsvittds
      361 yganvqltll gklagmdnqf gvgasadlan sgfdqssqda mftdaratvg igdftrktra
      421 ktrnasygvy fddtlaltrq wsltlagryn wsraaiedas glqplltarh tfsrfnpavg
      481 vtwnpvpgft ayatynegmr sptaielaca dpaapcslpn dfladpalkp viaktvelga
      541 rgrsgeattw saavysttld ddiqfissng gastlgyfqn vgktrrqgfe laghtqlgpv
      601 gigvsysyvd atyrstwtes sasnssanvq gnivvrsgdr ipgipsstvk lrldyaatpk
      661 wnvgtnityr sgvfargden nqdangkvpg yvlidldttw qvtkrlqlfa sitnlldkhy
      721 asfgmlgrnf fngpnhsfdg lnpvneqfvg pgaprgawvg aryawd
//
LOCUS       WP_175916904             204 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CGNR zinc finger domain-containing protein
            [unclassified Burkholderia].
ACCESSION   WP_175916904
VERSION     WP_175916904.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..204
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22547
     Region          11..204
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mvtrheparq ahawtaadfv gghpaldfln tvadtgktrd edklvdwaav rawaeksgll
       61 arpdltrflr yprqdgadel aalhgfreda yvalahltsg gggsagaraa hrlaevirda
      121 igrstfdavd grfawrpdar aasrwvdaaa lgfehllrgd dfarvrqcgr ctwffvdrgr
      181 gvgrrwcdmr tcgnrakvea frer
//
LOCUS       WP_175916950             237 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: dienelactone hydrolase family protein [unclassified
            Burkholderia].
ACCESSION   WP_175916950
VERSION     WP_175916950.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..237
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26111
     Region          6..229
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 msqtsgsmit frrpdgqelq gylatpekte gtpavvviqe wwglndqirg vadrlarcgy
       61 ialvpdlyrg kstveeeeah hlmtgldfgd aasqdipgav qylktrasrv aitgfcmgga
      121 ltllslqfad adagvtwygf ppldyldpsk ikvplmghwg tqdaffaidq vdalekkltd
      181 akvnvefhry lahhgfanet avgpgriggt qfdpvwsqia wdrtltffgr tlwdkqq
//
LOCUS       WP_175916947             243 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [unclassified Burkholderia].
ACCESSION   WP_175916947
VERSION     WP_175916947.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..243
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=25975
     Region          5..220
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mqsygiahvw aqgdfvtrai aitllvmsvl swivivvkgw nvvrlnrltk naeqafwhsd
       61 dfddgikklg laastpsdnp flalalsgke aadhhhqtqp hlhdrmdvsd wvtrclkdtm
      121 degisrmqag lailasigst apfvglfgtv wgiyhallai gatgqtsidq vagpvgesli
      181 mtafglfvai pavlgynalt rankgvvskl rrfahglhay fvtgarlass sardglrlas
      241 ras
//
LOCUS       WP_175916974             150 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Burkholderia sp.
            BCC1638].
ACCESSION   WP_175916974
VERSION     WP_175916974.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1638
  ORGANISM  Burkholderia sp. BCC1638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Leiros,H.K., Tedesco,C. and McSweeney,S.M.
  TITLE     High-resolution structure of the antibiotic resistance protein NimA
            from Deinococcus radiodurans
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 64 (Pt 6), 442-447
            (2008)
   PUBMED   18540048
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Burkholderia sp. BCC1638"
                     /db_xref="taxon:2681391"
     Protein         1..150
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16572
     Region          6..134
                     /region_name="NimA"
                     /note="Nitroimidazole reductase NimA or a related
                     FMN-containing flavoprotein, pyridoxamine 5'-phosphate
                     oxidase superfamily [Defense mechanisms]; COG3467"
                     /db_xref="CDD:442690"
ORIGIN      
        1 mdaqikqkil slldqhrimt iatlrpdgwp qattvgyesq gltlyflcgl esqkaanlar
       61 ddrvsltidh dtsdlmaitg lsmaahaqpv tdraeaekvl rmlplkypdm qtppmpmpsp
      121 devrifrvip tvisvldysq gfghtdlftc
//
LOCUS       WP_175916998              77 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator, partial [Burkholderia
            sp. BCC1638].
ACCESSION   WP_175916998
VERSION     WP_175916998.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1638
  ORGANISM  Burkholderia sp. BCC1638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Burkholderia sp. BCC1638"
                     /db_xref="taxon:2681391"
     Protein         <1..77
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
     Region          <2..62
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 awlrrfcevv agipevievy rmsghidyll kvvvphiaay dgvykrlise leifdvsssf
       61 smetikhttr lpldyvc
//
LOCUS       WP_175917062             283 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Burkholderia pyrrocinia].
ACCESSION   WP_175917062
VERSION     WP_175917062.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 283)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 283)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..283
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30427
     Region          31..283
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mlhavfsarf psgrfarpar llvaallagl fgvgllngar adtaplkvgi stspqiealk
       61 iaakeakaqg ldvriveftd wntpnaalan kdidvnyfqh ipflenankq ggynfvsiap
      121 gtimkiglys kkvksfaelk dgarvaiand pvnggrglll lqraglialk pgadyratth
      181 divsnpkhlk iipleasqla rslddvdlaq gypsfiklag ttdpnsallf dgtenksfai
      241 qwvvrpdsvn dprirkfiai yqhspavrka ldnafgslya iaw
//
LOCUS       WP_175917089             334 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Burkholderia pyrrocinia].
ACCESSION   WP_175917089
VERSION     WP_175917089.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..334
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36278
     Region          7..317
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(12..14,44,49,75,138..139,179..180,201,230..236,272,
                     289..292,297,300..301)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(44,49,75,138)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 mritlpsrlg fgtaplgnmy rdipneeala tvdaawesgi ryfdaaplyg aglaelrlge
       61 alagrprdey slgtkvgrlv ldehedasqr dlgekgglfr hglpnkivyd ytedgtlrsi
      121 easlerlrtd rldtvwihdp aidfhgerwl dvfdvamsga akaltrlrde kvikgwglgv
      181 nrvepcelal ersdpdgfll agrytlldha galerlmpes varglgiivg gpynsgvlag
      241 gthfeyqpat qdmldrvari rqiserfgvd vravalqfsl ahlavaavia gasrpdride
      301 nlrlaaapip selwdalkae rliaehaptp agaa
//
LOCUS       WP_175917093             315 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175917093
VERSION     WP_175917093.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..315
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33786
     Region          2..315
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhtvavlalp dvvpfdlgva cdtfarvrsp gvehayrvrv cseharvagd lfelrpafrl
       61 daladadtiv vpgtsvplap tsrrviaalr aaaargcria sicsgafvla eaglldglra
      121 tthwlaagel arrypnvtvd anvlfidngr iltsagaaag ldlclhmiqa dygaavavda
      181 aryavaprvr eggqaqfiap ewpagtdglq slmdwllanl rkpltldama rqastsvrtl
      241 trrfqeqtgt sprqwlqtar vrhaqqllev telsiehvat eagfgsvtaf rerfarivgt
      301 spqryrhafr arsga
//
LOCUS       WP_175917123             558 aa            linear   BCT 11-JAN-2025
DEFINITION  alkaline phosphatase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175917123
VERSION     WP_175917123.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 558)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..558
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=58540
     Region          48..536
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 misffgkqrk maamvagala lasvgayavq qdgnaqgedh gnarrvvkhv llisvdglhe
       61 qdlarcigan tcpniavlak sgvtytnayt pglsdsfpgl aalvtggspk taglfydvsy
      121 drnlyapsdt tcsgkqgwnv vfdettgida inggklvhld gggafnpqai pharvggqcv
      181 pvyphnyvkt ntvfeavkag vpnahtawad khawgydwln gpsgtgvddl mrteinsidp
      241 atntdytdvy shtarfdnlh vqalinqieg rdstgtksap vptlfganfq tlsvaqkspv
      301 akgggyldad ftpngqvana ityvdnsigh vvaalkqanl ytstavivta khgqsptdrt
      361 klvkngdtlt klleannyld pngnfgqnnt stgnlndgsg lvgtgfvqtd dvgliwlrdr
      421 sqraavvqtl kanlgcnapg icadgsqayi lygaaladrf gdpangrtpd iivqpnpgvi
      481 ytsstkkdee hggnapddsh lgllvsypgi hrartvndlv gtkqvaptil ellgadprll
      541 havvaentrv lpglgigr
//
LOCUS       WP_175917160             468 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175917160
VERSION     WP_175917160.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..468
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47705
     Region          18..443
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(25..26,29..30,33,65,115..116,118..120,123,144,
                     147..148,151,274,277..278,281..283,286,314,318,370..371,
                     375,379,395,398..399,402..403,406)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtaaapnraa arrvlaatcv sytlvlldas ivnvaltdia htfgsrvagl qwivsaytla
       61 fasllmtggt lcdrlgdrtv yvaglavfva asalcgfapn lpalaiaral qgvgsallvp
      121 cslalinraf pepaarasai svwmgcggia masgpliggv lidlfgwrsi ffvnlplgla
      181 giwlgrsvar aavdasrhfd wggqaaaiva iaaligtlie gpslgwrsap ivggavtsvv
      241 awlaffaiea rrrepmlpla lfrnrlfags tfvsmasafv fygllfvlsl fyrqvrgagp
      301 ldtglaflpm tvmvalgglg sgrlvarfga rgtmcaafgl yaagalgmta mssttpawla
      361 vapmlaigfa sgfispaats palgtvdrrr tgvaaaalna arqsgsalgv aifgaciatl
      421 qpfpaamrva lgmatglsal aaatwwiaar avpaaserav rmqapgrr
//
LOCUS       WP_175917178             468 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia pyrrocinia].
ACCESSION   WP_175917178
VERSION     WP_175917178.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..468
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50691
     Region          2..448
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mqqnesdlhr glgqrqmrlm algaaigvgl flgsanaikm agpaiilsyi iggavifvim
       61 ralgemavhe pvagsfsrya rnylgplagy ltgwnywflw lvtciaeita vgiymgiwfp
      121 dvprwiwala algmmgsvnl ltvkaygele fwfalikvvt ivvmiavglg mivfgygnhg
      181 vptgisnlwa hggflpngmq gvmmsmqmvm faylgvemig ltageaanpq ksipnainsv
      241 fwrivifygg alfvilsiyp wneigtqgsp fvmtferlgi ktaagiinfv vltaalsscn
      301 ggifstgrml yslaqqghap rgfavttagg vprrailvsa aallvgvlln ylvpekvfvw
      361 vtsistfgai wtwgvilvtq mkfrqslaps eqrtlgfrmp fwpygswfal aflafviglm
      421 ayfpdtrval lvgpawlall vafyyglkle saaspdagpt rrserqra
//
LOCUS       WP_175917196             453 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175917196
VERSION     WP_175917196.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..453
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48632
     Region          32..435
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(46..47,50..51,54,86,136..137,139..141,144,164,
                     167..168,171,268,271..272,275..277,280,307,311,361..362,
                     366,370,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtttqhpsat paaaqsgpsa avderqlmrm ltrrlvpfla liyvvayvdr tvvgfaklhm
       61 naavglsdaa yglgaglffi gyflcevpsn lalgrfgarv wfarilatwg vitmamalvq
      121 gpasfyalrf llgaaeagly pgilyfltqw fpmrgrarvi gllvlaqpia givtgplagw
      181 llsthglfgl snwqtlfvvs glpavllvwp tlrllpespd rarwlndder rwiarqlaad
      241 rdtyrpdahr nplatladrr vlllaalflp fplciyglsl wlptiihafg agdtatglls
      301 avpylfavvg llvvprhsdr trerywhivv vsaaaaltma asawvrqpal qflficltaf
      361 slysiqavvw alpgefltgt saavgiaain slanlggyvg pygiglikqa tgslaaglyf
      421 laatllfavl itfvvratlr apqpaagala res
//
LOCUS       WP_175917198             316 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175917198
VERSION     WP_175917198.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..316
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34005
     Region          16..73
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          104..304
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(119..120,122..123,126,130,132..138,233..238,
                     244..245,247..248)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mtdaspwgnr srlktrqlll vvaladegsi hraaaalnmt qpaaskllre leesigavlf
       61 erlprgmrpt lygdalirha raalgsldqa reelaalkag hlghvavgai tspglrlvpp
      121 avaavkgtha glhvsveidt snvllehlaq dkidivlgrl saehdklrlr yepltgetva
      181 avvrpdhpll aqaplsladv qraawvvppa gsvlrhrfel vfqraslapp anlvetsall
      241 fitqllersd miavlaedva ryyarhgivt vlplemdcrm ddfgiitrtd rlhspavtvm
      301 adairaaare vygval
//
LOCUS       WP_175917216             353 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia pyrrocinia].
ACCESSION   WP_175917216
VERSION     WP_175917216.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..353
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=39402
     Region          82..314
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mkpsqfakgf qarpdittse krtaldrlna idgivksetp aaaptksakk diaplpvpef
       61 tldpsidesp qyrawrlenr yapgqviels lkaikhspfn prhfylkssi aelavnlakq
      121 gqqqaihvip dydnpgtyfv sdggrrvral keankesvka ividvpigiq syklgydlnv
      181 qrdsqtvfdn avvwrrfldd khfqsqkels ehlgldestv avalsigklp eaimqemvar
      241 pdrfgsnmay qvgryhnarg teatlrlink ivsddlstrq vsdivkgrva aqetpkaagr
      301 qryaqrleik lggksvgdlk sygedrielr lrglpkdkrd aileqlerml lse
//
LOCUS       WP_175917218             343 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [Burkholderia].
ACCESSION   WP_175917218
VERSION     WP_175917218.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..343
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=38169
     Region          31..304
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mslpaspdtp arpeekdlfd rgasdwivsp eaafdawlam qdyrrssadv yrtqwgaflt
       61 wmrahqknla tvdtatianf vgelpirktq rlrylrlier vldhirrtey astnparfia
      121 qdgeanwrka rdneptgflt paeratllay lfspigvsgs aywkerrdra lvaaflgagi
      181 ktgearslti scvntsgtsl qiqsahpaya rethlasfai alleawlter krqeipgelv
      241 fpashagrpm hkatmlraid aivesaglts srtaraspqt lrntyaaelf endvppervg
      301 kwlgfmrpis snrlhrawkn wrdgltdsng dgdgdasdsd eth
//
LOCUS       WP_175916807             506 aa            linear   BCT 11-JAN-2025
DEFINITION  terminase large subunit [Burkholderia sp. BCC1638].
ACCESSION   WP_175916807
VERSION     WP_175916807.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1638
  ORGANISM  Burkholderia sp. BCC1638
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Burkholderia sp. BCC1638"
                     /db_xref="taxon:2681391"
     Protein         1..506
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56111
     Region          11..504
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 mgtprvkrvs rgernirwie ehcripegrl vgqpvkltke qrgwikqiyd tptrtfilsm
       61 arknaktals aflvllhlvg pearpnsqly saaqsrdqaa vlfelaakvv rmsedlsqyv
      121 tirdtakell chdlgtiyka lsadaatkfg lspaltihde lgqvkgprsq lyealetasa
      181 aqesplsivi stqaptdgdl lslliddals gadprlkval ytapldmdpf sdeairlanp
      241 hfdvfmnree vrrmasdakr lpsresayrn lvlnqrvear npfvaraiwm ensgepaeld
      301 gedvyggldl ssvsdltalv llseggdvhp tfwlpedgle akaradrvpy dvwardgllq
      361 ttpgsaieye fvaeylrgvf drcnvralaf drynmrflkp wlervgftde elsrfaefgq
      421 gfvsmspair elearllark lrhgghpvlq mcavnavavs dpagnrkftk qkstgridgm
      481 valamavgat qqnsteseie pqmffi
//
LOCUS       WP_175917228             273 aa            linear   BCT 11-JAN-2025
DEFINITION  siderophore-interacting protein [Burkholderia pyrrocinia].
ACCESSION   WP_175917228
VERSION     WP_175917228.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..273
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=29842
     Region          5..266
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mqntsertvt rvrhtlkfrl lqvlrvhavt phllrvtlgg pdladfesas fddhvkvffp
       61 psgaerpamp tlgengpefp egepkpvard ftprrfdraa celdlefvln hpgpasqwaa
      121 qarvgqwlgi ggprgsfvvp tgfdwhllig ddtalpavar rleelpagar aavvlevadr
      181 taqisfdtra dvheiwrfra eanaedgdal lnavrdlplp psgdgyvwaa gealsmravr
      241 qhltgergvd ksriraaayw krgaaavhet led
//
LOCUS       WP_175917229             236 aa            linear   BCT 11-JAN-2025
DEFINITION  PadR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175917229
VERSION     WP_175917229.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..236
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25670
     Region          82..161
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mrhtpsrgha rcdghgahar pdwfaglwya igrhrrghdp fgggpfggrg grggfgdfgd
       61 dgmprgrqfs sddlqlllla lvaeqpshgy elikaldtrs ngfyspspgm vypaltylee
      121 vgfvasqaeg nrkryaltda grahldaqre rvdtlfarlt hlarkmefmr rafagesagn
      181 daqdesqagw lpefvearva lkrallhksa agpdeqrria aimrrataei eggtga
//
LOCUS       WP_175917238             177 aa            linear   BCT 11-JAN-2025
DEFINITION  2,4'-dihydroxyacetophenone dioxygenase family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175917238
VERSION     WP_175917238.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14449000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..177
                     /product="2,4'-dihydroxyacetophenone dioxygenase family
                     protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20079
     Region          37..160
                     /region_name="cupin_DAD"
                     /note="2,4'-Dihydroxyacetophenone dioxygenase (DAD), cupin
                     domain; cd20302"
                     /db_xref="CDD:380436"
     Site            order(53..54,57,63,65,82,84,86,88,101,104..108,110..112,
                     129,135,137,145,148,151)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:380436"
     Site            order(77,79,94,115,130)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380436"
ORIGIN      
        1 mvdkavaefw qnippianpf kpdalpeayi anaatddery yvpftetvss rplwispsqn
       61 kwcdilmake aglvnrhyhp hevfaytlsg kwgylehewt atkgdfvyet pgeghtlvaf
      121 dhpepmraff ivkgpliwld edgnpdgyfd vhsyiamcna hyekvglgaq aieklfr
//
LOCUS       WP_175917277             315 aa            linear   BCT 11-JAN-2025
DEFINITION  YncE family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175917277
VERSION     WP_175917277.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..315
                     /product="YncE family protein"
                     /calculated_mol_wt=35390
     Region          <12..207
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          <141..293
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mndilllvqk cahtfsfydl dtkaalkhiv lpnfpheftv dvneryayvg ifgietawsr
       61 ghegdhriae idlverthtr mldlwpyyrp hgmasdrdgr lyamseahdm llvfdeptrq
      121 pvpnmavpsg gvkthlvtlt rdasraygvh llsntvtqfh prdatiapra vmpgprpegn
      181 alsadertlf vanrgddtlv eidtetmtcg rrvktrsdpn riyrtsapdg rdlllltnsg
      241 eqsisvfdar qleeierial panptalsfh psrrvayvsf qddyvreldl dtwrfvgala
      301 tlrepdasyv lagar
//
LOCUS       WP_175917278             430 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175917278
VERSION     WP_175917278.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..430
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46112
     Region          22..424
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(36..37,40..41,44,77,127..128,130..132,135,155,
                     158..159,162,256,259..260,263..265,268,296,300,351..352,
                     356,360,376,379..380,383..384,387)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnsltpatpa yeageaiprr rwlrvippll laciisymdr vniafampgg mnaelgmdat
       61 maglaggiff fgylflqipg grraargsgk tfiawslmsw avlsvltglv thtwqllalr
      121 fllgvaeggm lpvvltmvsh wfpdrergra namvimfvpl agmitaplsg filaaydwrh
      181 lfysagalsl lclvawmlla ddgpetarwv sprekayild alrdeqerkr aagtpaaasf
      241 gemlrnptiw lliainfcyq vgiygytmwl ptllknlthg gmgkvgllam lpyvamvigm
      301 fvtsylsdrt gkrrlfvllp lvgfaaclal svlthasmav sfafligcgf flqaaagvfw
      361 aippklcsve tagsarglin algnlggfcg pyavgvltqh vssaagvysl avtlavagll
      421 altlpkrced
//
LOCUS       WP_175917279             305 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: dihydrodipicolinate synthase family protein
            [Burkholderia].
ACCESSION   WP_175917279
VERSION     WP_175917279.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..305
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33001
     Region          4..297
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mnaryqgvfp vaptifdahg aldldgqrrc ldfmidagsq glcihanyse qfalgdderd
       61 litrttlehv agrvpvivtt shfsaricae rnrhaqalga amvmvmppyh gatfrvpeaq
      121 vraffaeaad glriplmiqd apasgvalta sflatlarei davsyfkiet agaasklrel
      181 ialggdaieg pwdgeegitl ladldagatg amtgggypdg irritdayfa grrdeaceqy
      241 arwlplinye nrqsgfltak almreggvia cdrprapwpe lhpqvragll dvarrldplv
      301 lrwgh
//
LOCUS       WP_175917297             452 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia pyrrocinia].
ACCESSION   WP_175917297
VERSION     WP_175917297.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..452
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=48422
     Region          16..434
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mdnitpnlat draprmpriv ivgggagglq latrlgdtvg rrgqaevvlv drypthfwkp
       61 llheaasghr dpashtieya aqakrhgfrf vqgalqqvdr aactatiaav qdadgteilp
      121 qrelgyddlv lavgsvtnff nvpgaarhal plenldqaed frrkflaact kanhqaeqhp
      181 akraapicin vigagatgve laaalrhaiq qlttyrfkal vsardvhirl ieggprilpa
      241 ldarlsakmh aqlrtlnvdv ltdtrvaevs adavttatge rlasditiwa agvagpailr
      301 eigdialnrs nqvivtdtlq tpddphvyaf gdcaacpsag asgflppraq vahqqavylv
      361 nafarrvagk pvagftfrda gtvvslghtg avyqadlgvr srslivdgla aiglykflyr
      421 khlfsvygvk ralfqslshw lqsrnqpsik lh
//
LOCUS       WP_175917327             210 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Burkholderia].
ACCESSION   WP_175917327
VERSION     WP_175917327.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22105
     Region          2..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 midfstlalf sgaclaltat pgpdmllias rsvsqgrrag fatlagiqag tychaltatl
       61 glsqlflavp iaydlvrfag aayllylawk tfrsdatals pvasqrrhst vaifrqgltt
      121 nllnpkmalf vlalfpqfvr pghgsiavqi lvlatvlnli glvvngavil sasrlsqrig
      181 arrrpsklpq yllgtvfvgl aarlavagrn
//
LOCUS       WP_175917356             298 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175917356
VERSION     WP_175917356.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32542
     Region          8..>51
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..290
                     /region_name="PBP2_LTTR_like_4"
                     /note="TThe C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08440"
                     /db_xref="CDD:176131"
     Site            order(109..110,112..113,116,120,122..128,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176131"
ORIGIN      
        1 mkidtlgvqa fvaiadggsf rqaadalhvt qtaitqrlrk lesylgvalv erttrrttlt
       61 eigrrflpqa rrllnelsda lteiretgls qrgdvtiacv ptvgvqylpr ilrafsghrp
      121 hdrvkildha sasvlqavlr reaefgisia gdqhpelvsv pltndpyvlv crddhplakr
      181 rrirwaalqp hplifagems gnrgllegal ktsgvslhsf yevqrsstal glvaeglgaa
      241 vvpklaiqkn aypmirtiel vepsvsrtlv lvtrksaqls paaralydmi veratpgr
//
LOCUS       WP_175917368             315 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175917368
VERSION     WP_175917368.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..315
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34117
     Region          2..315
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhrigffvcs ghdaldlggp lsafnqvaga aghtpydlhv isqsggpvrg ntglsietkp
       61 vgrrmfdtvv fvggdigpmq tpgniaaark lcarasrvas vctgafllae tglldglrat
      121 thwryaallq srfprarveg dsiyivdgri wtsagiasgi dlalglierd mgaevaravs
      181 rllvvpyrrp ggqsqfsams qmepesdrir ialnfarehl aealpverla daarlsprqf
      241 grafrretge tpakaverlr veaarlrlqd gsepieqial avgftdperm rrafiklygh
      301 ppqairresr lnsar
//
LOCUS       WP_175917371             402 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175917371
VERSION     WP_175917371.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..402
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42293
     Region          17..390
                     /region_name="MFS_MJ1317_like"
                     /note="MJ1317 and similar transporters of the Major
                     Facilitator Superfamily; cd17370"
                     /db_xref="CDD:340928"
     Site            order(27..28,31..32,35,68,119..120,122..124,127,147,
                     150..151,154,227,230..231,234..236,239,266,270,319..320,
                     324,328,344,347..348,351..352,355)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340928"
ORIGIN      
        1 mqteastril rqiprsvwvl gcvsllmdvs seiihsllpm flmaglgasa ttigviegia
       61 eatapvvkvf sgtlsdylrn rkwlavagyg lgalskplfa iaptigvvvt arivdrigkg
      121 irgaprdalv advtpvhlrg aayglrqsld tvgaflgpll avaimlmwrd dfrlafwlav
      181 ipgmlavall afgidepara sddkrinpir rdvvkqlgar ywwvvavgav falarfseaf
      241 lvlramgggv pvalvplvmv amnivyalsa ypfgkladtt shtklmvagl vmliaadlvl
      301 ahgthwgtvl vgvalwglhm gmtqgllatm vahaapselr gtafgvfnll sgvatlvssv
      361 vagilwdrvg aaatfyagav fsaativllv rlrgsfgteq ar
//
LOCUS       WP_175917415             315 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175917415
VERSION     WP_175917415.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..315
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34733
     Region          11..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrkfkipnmg alvafeaaar hesfthaake lfltesavsr qiatleaslg vrlfarvkqr
       61 vvltragkly gtqvrralea ldrdtlsiia hgsgggylel avlptfashw lipriksfyd
      121 rtpdvrvnmg srtdlfsfed thfeaaihyg kptwpgtssd ylfgeevvpi cspalldgpv
      181 eriedllayp llhsttrpga waqwfethgv edirtmqgvr yelhtmlisa aaaglgialv
      241 pkffveeqlq qlglvvpcda atvgdsayyl vyptefshsk plelfrgwll eqasayaape
      301 gdaddtdaed dedve
//
LOCUS       WP_175917450             382 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Burkholderia].
ACCESSION   WP_175917450
VERSION     WP_175917450.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..382
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41220
     Region          19..363
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mnddykvelp eaaaiargrr lrvgviglgi grkhiegwre hpdvdvvaia dpdakrlakv
       61 gdafgidary asadamlaae rldvvsvctp nkfhreltla afdagchvlc ekpmalnade
      121 gremliaaqr agkrlminfs yrfsaqsral kaqvdsglfg dfyfgrtvwh rrrgmpgfgg
      181 wfgtkalagg gplidlgvhr ldlalwlmgy pkpvwvmgst ydpiarelat ragktfdved
      241 laaalirfdn gatlaleasw atniqeaelm etrllgtrag llqknlnegy tfdahvfieq
      301 ngaqfdmrln ppaegahsam ydyaeailcd vphpapgeeg livmeildai yasaaagepi
      361 rihapgpaav sappvldldv ag
//
LOCUS       WP_175917461             450 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175917461
VERSION     WP_175917461.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..450
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46989
     Region          21..414
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(34..35,38..39,42,81,139..140,142..144,147,167,
                     170..171,174,257,260..261,264..266,269,297,301,354,358,
                     362,378,381..382,385..386,389)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 matvrpaass palhaapndl kriavasvig ttvewydlfv fatasalvfn kvffpsfvpi
       61 vgtllafgtf asaylarivg aalfghfgdr lgrksmllvs lilmgcatfa igllpsygai
      121 giwapvsllt lrivqglalg gewggavlma vehapagkrg lfgswvqigv pagtlianla
      181 flvsstmltp asllawgwri pflasallvg vglyirlnts etptfakvke aaaqvklpia
      241 avlgrygkqv vlggvatmst gtafnlmvaf gltygtqtlg fsrgamlsia liscalcivm
      301 lplfgrlsdr igrkpviigg ilaealfafp mfwlldsref sfalagyllm mtafaanygp
      361 iatflaelfg tevrysglsv symlsgllgs aatpivttal lsatgrgssv awymvasalv
      421 salallllie tlkrdlssnt yrdeaaggra
//
LOCUS       WP_175917471             240 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD family hydrolase [Burkholderia pyrrocinia].
ACCESSION   WP_175917471
VERSION     WP_175917471.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..240
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26411
     Region          6..233
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mrlpdvsals fdlddtlwpf gpsvaraeaa lrawliehap dtasvlptqq tlselreeye
       61 rlrpdlvsdy ralrigsirl aleranedva lteraydvfy aarnnvefye dalpalawls
      121 arfpliavtn gnadlrltgg geffretlsa rafgiakpep eifhaaakal dvrpaellhv
      181 gddyhldivg alnaglqaaw vvrdhqpeve hdpqhaatph ltlrdlsmlc ralggpdnvs
//
LOCUS       WP_175917479             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175917479
VERSION     WP_175917479.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33522
     Region          1..>123
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mndlrvlesf lrtveagsfs aaasrlgvtp aavskhvakl erslgtrlfr rttrsltlte
       61 agerlyaets taanalsqam atlterdarp agtlrisiap gfgrqyvlpl mptflerfpd
      121 lrldwslenr hvdlvkegfd aaigsgvedd anvvarelvp irlltvaspa ylakhgepat
      181 laelsrhdci rlrsattgrv rdwaftvnge tvtvpidgrv vltdldaicd aavagmglar
      241 lgahhvlphl degrlvrvlt rypaiggtiy vyytharltp pkvrafvefl tesfsrsdwr
      301 arvdtfg
//
LOCUS       WP_175917482             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175917482
VERSION     WP_175917482.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47182
     Region          23..422
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,154,
                     157..158,161,256,259..260,263..265,268,295,299,349..350,
                     354,358,374,377..378,381..382,385)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnatetldpa saeeqrimsk marrllpilv vmfliafidr qnvgfaklqm vhslgmteaa
       61 fglasslffi gyllfevpst lalhrygarv wlarimltwg litvlmgftt smpafcslrf
      121 llgiaeagfy pgviyyltlw fpqsyrakvl giftlgsala nmlgslvggv llslngvwgl
      181 agwqwvfiat gipavivavv vfrvlpasfr eapflderek qivaaalere kpaqaehgqp
      241 wkalldprvm lfaatymlms tslygvtywl ptlvksfgvs sstngflsml pwalavlllv
      301 wlpaklrrak silrtiaiva algalgflls lvlpstplrf ialvlggaci pllypcfwsm
      361 ppryftgara aasvaainsi gnlggffsqn lmpfagkvtg tafgpmivpi vclallgiga
      421 lvawtrserg mvaarv
//
LOCUS       WP_175917546             431 aa            linear   BCT 11-JAN-2025
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175917546
VERSION     WP_175917546.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..431
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=46337
     Region          5..428
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 mtdqassnwr letiavhggy rpdpttrava vpiyqtvaya fddtqhgadl fdlkvqgniy
       61 trimnpttdv lekriaaleg gigalalasg qsavtyaiqt iaeagdnivs asslyggtyn
      121 lfahtlpqyg ittrfadprd pasfeplida rtkaifaesv gnplgnitdi aalaeiahrh
      181 giplivdntv pspyllrpfe hgadivvhsl tkylgghgts lggaivdsgk fpwvehadrf
      241 krlnepdvsy hgviyteafg paayigrarv vplrnmgaai spfnafqilq gvetlalrve
      301 risdnalkia qhlarhehve wvnyaglpdh pdhplvaryl sgrapgiltf gvkggrdgga
      361 kfqdalklft rlvnigdtks lathpastth rqlspaelak agvkeetvrl sigiehiddl
      421 ladldqalgq l
//
LOCUS       WP_175917556             330 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175917556
VERSION     WP_175917556.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..330
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35358
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..294
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(103,107,146,160,162,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(104..105,109..110,112..113,116,120,122..128,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdnpiramri ftrivemnsf traaqtlgis ratatrtvqe leaalgmpll vrttralrat
       61 pegdayyrrc lritadvdel easirgaalq psgplrvelp gsvagaivlp algefharhp
      121 dlvlmlgasv raadmvgdav dcsirlgelp dsslvarrlg mlervtcasp ayldrhgvpc
      181 tledlaahra vcgssgsgqr taeldfvadg avrkvrldgi vsvddehayl acgvhglgli
      241 qpprvaaqpl idagrlrevl prwrpdaiav savyvkrphv spgvrafvdw igerfeqdre
      301 gvvvagpmar qpvpeavemn dregsqvama
//
LOCUS       WP_175917564             356 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Burkholderia].
ACCESSION   WP_175917564
VERSION     WP_175917564.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..356
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38243
     Region          2..265
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mtaplptrlp sllrhalrpl ldpyrryrha klihaarval ailvsiglst glrvphgews
       61 titvlivvgg lqhhgnirkk aaeralgtsi galaglglil lysaahapia iyllmavacg
      121 icayhaigka gyiallsait mvivaghgdn eivdglwrav nvligiaial afsfalplya
      181 tyswryklad alracaavha rvagdrqvgd dahlkemaal sallvqlrsl mpsvskecet
      241 smaqleaiqr slrlcigyle ilssavpard dvaareymrv gmkavnrrir dtlvgasral
      301 kfgkpsrlap rrrpadpphd apppqlsgyv sitaklagev dqlreklldt aqswni
//
LOCUS       WP_175917577             144 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia pyrrocinia].
ACCESSION   WP_175917577
VERSION     WP_175917577.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..144
                     /product="cupin domain-containing protein"
                     /calculated_mol_wt=15707
     Region          23..126
                     /region_name="cupin_bxe_c0505"
                     /note="uncharacterized protein bxe_c0505, cupin domain;
                     cd06980"
                     /db_xref="CDD:380385"
     Site            order(28..34,43,45,47,49,67,69,71,73,91,93,95,112,114,116)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380385"
ORIGIN      
        1 mstptttafs hvkphdtayq geglrdffly rdlgiaaatn gkvvaqlvra nhaptagtgw
       61 hrheaefhiv fmlkgwarfm ygeqetlvsa gdcvhqapgi vhylfdyspd meyleivgpa
      121 dfksidveep cavpaptpwg etga
//
LOCUS       WP_175917594             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175917594
VERSION     WP_175917594.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33667
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdyidklrif rsvvemrsft raadmhglar pvvsravadl earfgsrllh rttrqvslte
       61 taeriyerca avldeldale veaqtqtrep egllrlvaht taalnrlvpl iagfkrahpk
      121 vrldvtlter pvdlvgegyd igivvpymlt settvvrlve ripvvivatp aylgahsrpe
      181 tpadladhpf vplspslrrp alsfrvdgdt ltvpyrfdis snspvfnrem vmhdfgigvv
      241 pktlveaela sgalvqlled adlvdafvei klayanrall pakvkafidy taaycdrvgr
      301 nvpaaa
//
LOCUS       WP_175917610             779 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175917610
VERSION     WP_175917610.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 779)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 779)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..779
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..779
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=85983
     Region          1..754
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msmilptqay elklaphpap fsiltftgld rvsqlyryei eftspaagip mdqvlgrpak
       61 fsadpidpnm dylrkmfgen aaqfsakpaa ytvhgvitqf deletsadet ryrvvleptl
      121 adldrgvtsr lfqkqsveei vtdtlrhygy ragvdfqfql rgqykrreyv tqynettfaf
      181 irricaeegi wfrweqkkdr avvvfgddld ayarkqrtvp yrrdsglesa gadaiktlgr
      241 emkrvpaavr lhdynhrqae vlllveenta rddkttnavd yrwgehyetp eegkrvarlr
      301 heaylaeqit fkgagnpfwl eagevmrvep sqvnakhgif vtsvesrggr sdaywvafeg
      361 ipsdrvwrtp mtsvsrpvvd gilparitsp gnykyaylte qgwyviklpf dldewspggt
      421 srpvrfakpy sgdnyghhfp lidgaevaiv htdgdpnrpv iigamhdsvh pdlvnnlnht
      481 rnlirtaarn elrmedkesn ehvhlitpfr asqlnlgfmv dtdrkargkg aelatdghas
      541 iraadgvlvs aeaqpgaage qlamqnadat faqaeeilrs lndaanaaka lqaeanqqrv
      601 lieqklrrlq kpvivasape gvgiasgqhv qiaarkqmfv tagegldigv mkritvaage
      661 aisflaakfg irlfaakgkv qiqaqgdgme lmamqdmlms ssdgevtitg rkgvtigdga
      721 gayiklsggr iilgspagei elkgnltvnd aaggsfkfpt wstvplndvk nalnfgfse
//
LOCUS       WP_175917638             133 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [Burkholderia].
ACCESSION   WP_175917638
VERSION     WP_175917638.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..133
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=14572
     Region          16..133
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mslihaaavl dadapdyvvq lqagthaltg deapreggqd rgpapyefvl aglaqctaat
       61 lrmymqrksw paaridvrte lhadregvqy vrrvvtldgp lddaqrqrla eicektpvtq
      121 fikrgtriet tln
//
LOCUS       WP_175917724             157 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175917724
VERSION     WP_175917724.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..157
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16998
     Region          3..153
                     /region_name="COG3865"
                     /note="Glyoxalase superfamily enzyme, possible
                     3-demethylubiquinone-9 3-methyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:443074"
ORIGIN      
        1 mtiqkitpfl wysteaeeaa afyagifpds rivrvtsvsg tdgtrmvefe lfgqpfiams
       61 htrtetfnha isllvscadq aeldrywsal ldnggtadgc gwlrdrygvs wqivpealip
      121 mmadpdavka arvaaammqm tkfddaalka ayagtag
//
LOCUS       WP_175917652             140 aa            linear   BCT 11-JAN-2025
DEFINITION  rubrerythrin family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175917652
VERSION     WP_175917652.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Cooley,R.B., Arp,D.J. and Karplus,P.A.
  TITLE     Symerythrin structures at atomic resolution and the origins of
            rubrerythrins and the ferritin-like superfamily
  JOURNAL   J Mol Biol 413 (1), 177-194 (2011)
   PUBMED   21872605
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Li,M., Liu,M.Y., LeGall,J., Gui,L.L., Liao,J., Jiang,T.,
            Zhang,J.P., Liang,D.C. and Chang,W.R.
  TITLE     Crystal structure studies on rubrerythrin: enzymatic activity in
            relation to the zinc movement
  JOURNAL   J Biol Inorg Chem 8 (1-2), 149-155 (2003)
   PUBMED   12459910
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099327
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..140
                     /product="rubrerythrin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15156
     Region          8..138
                     /region_name="Rubrerythrin"
                     /note="ferritin-like diiron-binding domain; cd01041"
                     /db_xref="CDD:153100"
     Site            order(20,23,27,53,56,89..90,93,124,127)
                     /site_type="other"
                     /note="binuclear metal center [ion binding]"
                     /db_xref="CDD:153100"
ORIGIN      
        1 maqlkgskte dnlkaafage sqanrrylyf askadvegqn dvaalfrsta egetghahgh
       61 leyleavgdp atglpfgssr lnleaaiage theytdmypg maktareegf deianwfetl
      121 akaershanr ytkalevlvd
//
LOCUS       WP_175917737             135 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF427 domain-containing protein [Burkholderia pyrrocinia].
ACCESSION   WP_175917737
VERSION     WP_175917737.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Lupas,A.N., Zhu,H. and Korycinski,M.
  TITLE     The thalidomide-binding domain of cereblon defines the CULT domain
            family and is a new member of the beta-tent fold
  JOURNAL   PLoS Comput Biol 11 (1), e1004023 (2015)
   PUBMED   25569776
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..135
                     /product="DUF427 domain-containing protein"
                     /calculated_mol_wt=14695
     Region          <40..129
                     /region_name="COG2343"
                     /note="Uncharacterized conserved protein, DUF427 family
                     [Function unknown]"
                     /db_xref="CDD:441912"
ORIGIN      
        1 msissdtpsr pvkspgpdhp itiephpwrv vvtvagkvva dtrralalre asypavlyvp
       61 redadmsllr rtdhatycpy kgdcayysip aggeratnav wtyehpypav eairghlafy
      121 pdrvdsides aadaa
//
LOCUS       WP_175917748             468 aa            linear   BCT 11-JAN-2025
DEFINITION  CpaF family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175917748
VERSION     WP_175917748.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..468
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50706
     Region          77..457
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mtfgnrnrqp pdpapasapa aprapalapa aapapppara paatdtheal irsgkfdair
       61 tavfasmnms aalmktrdev rvgieqvaah tvererlkit ageqvlivda ilndmfgvgp
      121 ieplladetv tdilvngpdq vyveragrle ltslkfrdda hvtsvaqria aavgrrvdes
      181 spmvdarlad gsrvnvvlpp iamrgpsisi rkfakrditl armahqgnis hpmlqvlkva
      241 clcrlnivis ggtgsgkttm lnalsqhieq herivtieda aelqlqqphv vsletrpent
      301 eglggisqrd lvrnalrmrp driilgeirg peafdvlqam ntghdgsmtt ihansprdai
      361 srlesmvmma nanlqllsir rqiasavhlf vqvermrdgv rrvtriteiv gmegevvitq
      421 dlfafrqegd ttrdavkgvf dasslrpafa praayygved alaevfrq
//
LOCUS       WP_175917750             142 aa            linear   BCT 11-JAN-2025
DEFINITION  TadE/TadG family type IV pilus assembly protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175917750
VERSION     WP_175917750.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..142
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=14539
     Region          8..137
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mtrgatgarr argvvslefv mmlpfllmvl igiidtslil cdkavitnas reaaragvml
       61 rvpmltttqv agvaqtymqn slitggtatt ptvtvtqang ttagtaltvt vtytysglvl
      121 gsafsaltgp vtvsatsvml ye
//
LOCUS       WP_175917761             508 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Burkholderia pyrrocinia].
ACCESSION   WP_175917761
VERSION     WP_175917761.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..508
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=54001
     Region          16..491
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(72,74,78,81,85,118,121..122,131..138,143,146,149,
                     242,246,249,252,254,427,429..430,432..433,436,439..440,
                     442,444..447,456,460,462,476,483..488,490..491)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(158..161,169,184,187,217,234..237,240,258..260,292,
                     392,394,420)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(161,258,289,292)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnaavpqttl alptakllid gafvesqste wgdivnpatq etigrvpyat ldevdaaias
       61 aqrafqtwkt tpigarlrim lkfqdlvrrn leriahtlta eqgktlpdaq gdifrglevv
      121 ehacsigtlq qgefaenvag gvdtytlrqp igvcagitpf nfpgmiplwm fpmaivcgnt
      181 fvlkpseqdp lstmqlvela ieagvpkgvl nvvhggktvv drlcthpdik aisfvgstrv
      241 gthvynlgsq hgkrvqsmmg aknhavvlpd ahreqtinal vgagfgaagq rcmatsvvvl
      301 vgqardwlpe lvekakllkv nagaeagtdv gpvvskaake rilslidegv kagakleldg
      361 rnvkvpgyer gnfvgptifs gvttdmsiyt eeifgpvvvv leadtldeai alvnrnpmgn
      421 gvglftqsga aarkfqseid igqvginipi pvpvpyfsft gsrgsklgdl gpygkqvvqf
      481 ytqtktvtar wfdddatagg vnttialr
//
LOCUS       WP_175917762             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175917762
VERSION     WP_175917762.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47009
     Region          28..433
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(39..40,43..44,47,86,144..145,147..149,152,172,
                     175..176,179,261,264..265,268..270,273,301,305,358..359,
                     363,367,383,386..387,390..391,394)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mqtrstldeh atvatpaper takhyllagw asmagttiew ydfflygtaa alvfnriffp
       61 sldpvvgtla afgtfavgfi grpmggivfg hfgdrigrks mlmitlllmg vpsmiiglip
      121 sydsigywaa alliamrflq gmavggewgg avlmavehap kgrkglfgsl pqtgvglgli
      181 lsslamaava alpeadmlsw gwrvpflasi alvglgwfir akvpespdfe kmrrqgkaek
      241 spvtaalrrh prevltivga raaentwfym vvtfalayat qqlhlpkaem lhaitagavl
      301 slvtmplcgh lsdrigqrrm faiglvlmca faapffmmlg tqqtsyawwa ivlglgvvfp
      361 ilyapesllf aqqfpaeiry sgislsvqla gvigggfapm iatsllkagg gqphyviayl
      421 vgfgvfalvc talmrppra
//
LOCUS       WP_175917771             501 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia pyrrocinia].
ACCESSION   WP_175917771
VERSION     WP_175917771.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..501
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53052
     Region          22..477
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mkhtserpad taggadsrha dpdamfashe agyakhlkpr hvqmiamgga igtglflgag
       61 grlqsagpal alvylvcgvf aflimralge lvmhrptsgs fvsyarefmg erasfvagwm
      121 yylnwattgi vditavaiym kywavftdvp qwvfalgalg ivsvmnmigv kvfgemefwf
      181 slvkvgtlav flavgavfla sghpvagqmp glhlvadhgg ifphgilpav livqgvvfay
      241 asielvgvaa getadarkvl pkaingvmwr ialfyvgsvv lltlllpwta ysshespfvt
      301 ffgklgvpyv gtvmnvvvlt aalsslnsgl ystgrvlrsl amggsaprfv srmnargvpy
      361 ggilitvain aigvplnyiv paqafeivln maslgiittw gfivmsqilf rravnrgelk
      421 avsfrmpgap ftswltlafl vgvlvlmafd ypggtwtvat ipvvvlalvi gwklakrgae
      481 reqavaapaa vravadpaqn a
//
LOCUS       WP_175917772             227 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia pyrrocinia].
ACCESSION   WP_175917772
VERSION     WP_175917772.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..227
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23839
     Region          23..223
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mtdalplttd pdsglqyrlr paagrpaarl lllhgvggne tnllnvadvi dprieiafvr
       61 gpltfgpnqh awfpvrfgpn gpeidaarad asrvqliall ralraqdgag aalptviagf
      121 sqggimsasv gltspadvag favlcgrilp eidpliaprd alrplhaliv hgrfddklpv
      181 awadtadarl talgvahdtr lyaaghelta emaadfgrwv certgln
//
LOCUS       WP_175917814             271 aa            linear   BCT 11-JAN-2025
DEFINITION  SH3 domain-containing protein [Burkholderia pyrrocinia].
ACCESSION   WP_175917814
VERSION     WP_175917814.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..271
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27700
     Region          7..96
                     /region_name="YraI"
                     /note="Uncharacterized conserved protein YraI [Function
                     unknown]; COG4991"
                     /db_xref="CDD:444015"
ORIGIN      
        1 mrntivrslc vvllgfaaap gvadaqssay tnspaelyag papdypvvaq ippdtaldvf
       61 gclsdyswcd valpgvrgwi daqlleypyq gnyvplleyg aiigvpvtgf aigaywdryy
      121 rhrpwyhdrd rwehraeprl gpggfppgqg rpqpggprqv apggppqgqh darpsatrgg
      181 wnganrtppp apapapmpga agnarpaspp pavsrpspap ggeartmppp vrqggggggg
      241 gggyarpqgg gngggshggg gsgggpdefr h
//
LOCUS       WP_175917818             306 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175917818
VERSION     WP_175917818.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..306
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33069
     Region          7..294
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 msrkaiqwtg vfpavstqfk pdfsldidat hrvvknlvnd gvsglvvcgt vgentslsts
       61 eklqvieaar daaggkipvi agiaefttef arntvreaqr vgvdgvmvmp alvysakphe
      121 taahfravat stdlpvmvyn nppiykndvt pdvlialqdc enivcfkdss gdtrrfidlr
      181 navgdrfvlf aglddvvves iavgaegwvs gmsnafpkeg etlfrlakqk rfdealalyr
      241 wfmpllhlda rpdlvqcikl ceelvgrgsa vtrpprlalq gdtlaevkai vskaletrpa
      301 lpdvgl
//
LOCUS       WP_175917831             673 aa            linear   BCT 11-JAN-2025
DEFINITION  BCCT family transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175917831
VERSION     WP_175917831.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..673
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73192
     Region          3..514
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mpdsrpsprt tfkpqvvlpa lavigallvv callpseaga lfsagqqwvi arfdwfyvla
       61 vtgflvflvl iaasdfgnir lgpddaepef sflswtamlf aagmgiglmy fgvgepmqhf
      121 lkpptvdpgt paaareamlm tffhwgfhaw aiyglmglvl ayfgfrynlp ltlrsglypv
      181 lreringwig htvdafalvg tvagiattlg ygvmqisagl htvagwdtgs nafriglval
      241 vvilaglsaa sgldkgvrrl selnlllafl llafvavagp taflfralgd nigqylsslv
      301 dlsfrtyaya spreegwfgg wtilywawwi swspfvgmfi arisrgrtir qfvigvllvp
      361 tafnlvwmtv fgnsaiwldt hgaagalaqt atnvdallfr ffdflplsql lsivaivlia
      421 vffvtsadsg afvidqiatr gaahspvwqr lfwaallgvt aavllvaggl galqamtlia
      481 alpvalimla lcyglwrgla adrahysqei apaasfwtgq hwrhrlthil rqtteadarq
      541 fvaetvepal rkvadelrtg gvdahvqrds ddavrltvpt aehrdfvygv rvtvksaaaf
      601 lvreaaepea arahvygivt ffedgrlgyd leylrgdevi advlrqyery vslaadkrth
      661 llsrapghat eae
//
LOCUS       WP_175917843             424 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia pyrrocinia].
ACCESSION   WP_175917843
VERSION     WP_175917843.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..424
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41816
     Region          5..>332
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpahadspaa hhagsltifq gaalyigavl gtgvialpal aaevagpasl lawaalvvls
       61 gplaatfaal garypdaggv styarrafgp kaaaivgwcf yfavpagapa aamfggayva
      121 avtggghttv ivtaaaliat vsaanafgvt vsgrmqlvls allvtlllaa vlasaphart
      181 anlqpfaphg wlavgqaaal lvwsfagwea ithlaaefrr pahdmprsag iavvvvgfly
      241 lsvaaasvmv lgpsagtsga plaeliaggi gghaqvlaaa aallltlgtm nayfagaakl
      301 gaalgrdgal pawlaqgsqi ggvprrslgv isvlaavala attisdvgpk plvlvtsgcf
      361 vmvyglgaaa alkllprggi ayrcawislv avaglflttg wyllcpllla ggallylqmt
      421 gprk
//
LOCUS       WP_175917876             260 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175917876
VERSION     WP_175917876.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..260
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=28681
     Region          14..218
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mfhlhssysa naildalped sirtiaphle lvrikagmld rvgepmrhlh fpttammsvq
       61 hlmedgamve vavvgregvv glgtlvggva assrvevrig gmayrvpacv mraeferspe
      121 tyrlllnycq atmaqisrsa lcnrhhsvse qlsrwlllah dridgdelav tqqtianmlg
      181 vrregvteaa gnlqeaglir qrrgritvld rhglehhace cydliradyr rllgtrgnar
      241 ptpvrprvpe vrlgfparga
//
LOCUS       WP_175917921             281 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175917921
VERSION     WP_175917921.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..281
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30761
     Region          23..158
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <101..281
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          195..277
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msrtanrsav pspfwrdaal pfieartvdd graicyvkht hdtfslgaiv ggtstyvnga
       61 tnahvgrgvl viidpeqvha cnpygpdawa yrmvyvdvpw larlqhslgr dpngdfhgfs
      121 pklterrdlf aqfggfyrtl vspgidplgk esaavefftq lhgaldrelp girpaddnak
      181 laraadyiaa hcregvtlda icaaadlsps ylirafnary gmtphaflid rrvqygrtel
      241 rrgrpiadva ldagfadqah fqrafrriaa atpgqyrsam s
//
LOCUS       WP_175917925            1082 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia pyrrocinia].
ACCESSION   WP_175917925
VERSION     WP_175917925.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..1082
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115756
     Region          1..1065
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mwivnlalrr pytfivmaim ivlatplalm rtpvdvlpai nipvisviwn yggfsatemt
       61 nritavheri ltttvnniqh vestslpgia vvkvflqpga nvqtaiaqtv ssaqaivrqm
      121 pqgatpplvi tysassipvi qlglssttls eqsladialn flrpqlitip gaqvpfpygg
      181 rtrvvaidld pqallakglt padivnavna qnlvlptgta kmgqteyrid tnasadtvad
      241 isrlpiqtvn gattylreva svrdgfapqt nvvrqngqrg vlvsilksgd astlkvvsdl
      301 kallpkvipt lpegltitpl fdqsvfvnaa vqgviheali aavltammil lflgnwrstl
      361 iiaisiplsi ftslialsal getinimtlg glalavgilv ddatvtieni erhlhlgtrr
      421 aapsvpsgpl ggqrpegawg ssfstnlhea ilegageiav pafvstlcic ivfvpmfflt
      481 gvarflfvpl aeavvfamla syvlsrtlvp tlamllfrpq qastgpdhat srfarihhaf
      541 nnaferlraw yivllsmllv rrrfyamcfl gfcvlstglv falgrdffpn adsgnirlhm
      601 raptgyriee tarladrver virevvppne lgaivdnlgl pvsginlsys nagtigtldg
      661 ellialkpgh ratqhyvqtl rtllperfpg vefffqpsdi itqilnfgqp aaidvqvlgn
      721 dlasnmtias nlmkkvrqip gavdvhvlqr ndeptlladm drtrmqqlnl saqnvaqnml
      781 islsgssqtt psfwinprtg vqyplqiqtp qysissvddl lgtpisasgr tgmplqllgn
      841 lvqvrttanp avithynirp aidlyvsveg rdlgsvagei drivsdmras lprgtdltmr
      901 gqietmrtsy iglgagvama ivlvyllivv nfqswldpli iisampaala giawmlfitg
      961 thlsvpaltg aimtvgvata nsilvvsfar qrlaagappl taaleagatr irpvlmtala
     1021 miigmvpmal glgegaeqna plgraviggl lfatvstllf vplvfggvhs rlarrrarqa
     1081 gh
//
LOCUS       WP_175917929             549 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175917929
VERSION     WP_175917929.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..549
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=56248
     Region          15..272
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
     Region          297..546
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mqnhevsadd appkaqrgiq svevggrlld alarrrkplg lselaaaadl staqahtylv
       61 sltrlalvkr daitgnyepg plslrlglms ierqpayraa lphavrlaet vglsvalsvp
      121 gvlgptivri ehggyplhvn lhvgsvmsld ttatgrvfra fgdpaqldam aasqagagdt
      181 lagaegtqpa qdagaqlael dtirargier svdrpspgvs amcvpvfdah grlqlaltvi
      241 gssgsidvgw dgpiatalrd aarqataslg aavsepppap sagaprvppa laddakaqrg
      301 inaldstgel llalvsagra lplrdlaaaa gmpaakafph lvslqkvgll srddagcfdg
      361 gplgqalgli amqrvsptrd aeaeivalaa atdmsvaaat lgplgptvir leesarpqhv
      421 slqvgtvmsl vntaigrifa agmsddvlad llanepvrla grgpaqadda frarlaaira
      481 daldfafdap vpgigtvaap vfdhtgsirl viaiigssrg fprgpdsdla qtllaatrrl
      541 swrfgwigr
//
LOCUS       WP_175917943             505 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Burkholderia pyrrocinia].
ACCESSION   WP_175917943
VERSION     WP_175917943.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..505
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53620
     Region          11..488
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(67,69,73,76,80,113,116..117,126..133,138,141,144,
                     237,241,244,247,249,424,426..427,429..430,433,436..437,
                     439,441..444,453,457,459,473,480..485,487..488)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(153..156,164,179,182,212,229..232,235,253..255,287,
                     389,391,417)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(156,253,284,287)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mkhdsnvtst lghlidgkrv dggsrvqpvf dpatgeshks valadkltve aaiasaqaaf
       61 pawrntpplk rarvmsrfkt lleehadelc alitaehgkv ladamgelqr gienveyasy
      121 vpellkgehs knvgpaidsw sefqalgvaa gitpfnfpvm vplwmwpmav acgntfvlkp
      181 sertpsstlr maelaleagl ppgvlnvvng dkeavdtilt dprvkavsfv gstpiaeyiy
      241 stgcahgkrv qalggaknfa vvmpdadign avnalmgaay gscgercmai plvvaigdet
      301 gdqvvaglka eidkmkvgpg ngagvdmgpl vtqqhfekvt gfveagvaag atlvvdgrgv
      361 kvdghdggyy lgpclfdnvk pgmpiyqhei fgpvlgvirl ksldeamali daheygngtc
      421 lftrdgeaar yfsdniqigm vginvplpvp vayhsfggwk rslfgdlhay gpdavrfytk
      481 rktitqrwps agvregtvfs fpsnr
//
LOCUS       WP_175917985             206 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            pyrrocinia].
ACCESSION   WP_175917985
VERSION     WP_175917985.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22217
     Region          3..169
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnassgaevr qhilniakpi mlhkgfsavg lneilaaagi pkgsfyhyfg skeafgeall
       61 esyfegylah ldnllkhqag tgaerlmtyw gnwlhtqcad dpegkclavk lgaevsdlse
      121 amravlrrgt sqiierlagg ieagladgsl tavddpthta ailyelwlga tllekihrnr
      181 kpleramaet rrmlnlppaa hdgaqs
//
LOCUS       WP_175917966             865 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia pyrrocinia].
ACCESSION   WP_175917966
VERSION     WP_175917966.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 865)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 865)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..865
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..865
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=93467
     Region          60..712
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mhpfqpsstr vnrrnvssvr dfcaswvara qpvaaaavar vkplaaaawq hlrhptrrga
       61 lltaaavpal fvlyvvvlip ftpgigdirk arvdqpaqvl sadgkllaef kpsnrewvpl
      121 kqisphmvda liatedhrfy ehhgldwkrt asaalhtfsg srqggstitq qlarnlypde
      181 igraptltrk vkeaitalki eavyskdqil etylntvpfl ynaygvemaa rtyfdksade
      241 ldvldsatlv gmlkgnsyyn pvlnperalq rrntvlgqmv kygklspaqf aqlqrrplri
      301 dferqkeppg paphfaqqlr kwliawadrn dyniysdglv vrttidwrlq qmatqaltlq
      361 gnqlqgiann awsgrdgcgt dnevfrtfmr espeykaaqd agkddaaamk llaadrgfmr
      421 alcktktdvq agfvaidprd gqirawvgsr dftdepfdhv aqarrqpgst fkpfvygvaf
      481 asgmkpedtf idqpveiplk ggeiwrptdd vpptgkpmtl rdavalsrnr itaqvmekvg
      541 paavarlard mgvrespler vpslalgtsp vtlkemvasy atiangglyv epqmvtrien
      601 rqgdvlaeya papperalda eadktlldvm rdvvtrgtgg sirarfgirg dvagktgttq
      661 dnadgwfilm qpglvagawv gfddgrvtlr sdywgqgahs alpivgdffq raqrarivdt
      721 kakfdtepsp gwfaslrera tdlfdtwfrp epkktpapvr tqraelppea degaasaasa
      781 asapeaasgg iveewipasd vaasaaalsa gasqpqtaqp pagastasgg sagigaapaa
      841 apsatpaqpp apvapvapdt tgasq
//
LOCUS       WP_175917970             472 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia pyrrocinia].
ACCESSION   WP_175917970
VERSION     WP_175917970.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..472
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50573
     Region          9..463
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mtaaacgcqe tdlkqpedql hrgleerhin lmalgatigv glflgsatai rtagpaillt
       61 yllggiaifl imralgemai tnpvagafsr yardylgpla gyltgwtywf vwivtcmaei
      121 tavgvymhmw fpgvpnwiwa laalmamgsv nfiavklyge fefwfaliki vtivlmiigg
      181 glmiafgign ggvatgisnl wahggfmpng iggviaalpi amfaylgvem lgltagearn
      241 peksltkavn svfwrvlify igalfvimsl ypwdqigtqg spfvmtfsrl gipaaagiin
      301 fvvltaalss cnsglfstar mlynlaqqgq apsklgrvnr ngvpvygviv svallligvl
      361 lnylapqhvf twltsvstfg aiwtwcvili aqmrfrgtls adriarlpir vpfyplgsyv
      421 algflalvvv lmaftpdtrv alvigpawia llgiayalfy anrpaasvst ks
//
LOCUS       WP_175918084             288 aa            linear   BCT 11-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Burkholderia
            pyrrocinia].
ACCESSION   WP_175918084
VERSION     WP_175918084.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..288
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=29899
     Region          195..279
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mslsllpcat iwlalfaaaa lawhrpqhgl slilaalgya galafgklep valaslalla
       61 aaawgvspar plavriaaha vfaalaials lhlipgfhnp lviaptrftp davpftmyln
      121 ldkplvglwl lwvlpwvapd valsralrtg avaavataaa clagalafgm vgwapkwpas
      181 gwlwlvnnll lvtlaeealf rgyvqggltr alrafawgpw valaigavlf gaahaaggwq
      241 wivlgtvagi gyglawrrgg llasalahag lnvvhfglft ypmldaar
//
LOCUS       WP_175917987             744 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia pyrrocinia].
ACCESSION   WP_175917987
VERSION     WP_175917987.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..744
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=78661
     Region          75..>209
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          215..737
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msrglieagk vagqtagagv srrgflkfgm slgaaagggl llgfslpaag ddtrrsvigg
       61 dadetaragv fapnafvqid rsgkvtlvmp kvemgqgvyt alpmliaeel evplssvtld
      121 happneklfl dpllggqltg gstsvryawe plrragatar tllvaaaakq wnvdpascra
      181 angevqhpps grrasygqlv daaaklpvpk dvalkkpedf kligtpakrl dspekvdgta
      241 qfgldvrlpg mlyavivnsp vfggtvasvd dtaakkipgv rqvvradnav avvgdhtwaa
      301 krgasalvvk wnegtgakvs mkdivadlaq aaangkgava rkdgdvgkaf anaktridav
      361 yeqpflahat mepvnctvhv rsdgceiwvg tqvptravdt vqrltsfppe kivvhnhllg
      421 ggfgrrletd migqavkiak qvgapvkviw treediqhdm yrpyyydris agldangkpv
      481 awqhrivgss ilarfappaf kdgvdpdave vatdlpydlp nqlidyvrqe prhvptafwr
      541 gvgptrstfv vesfidelaa qtktdpvqyr rallgktpra rnvldvatra agwgpalpkg
      601 qgrgvsvmha fgsffsivid vavddgdvqv krvvcavdcg msvnpntiea qvqggiifgi
      661 tgalygeiti edgrvvqsnf tdyrmlrine tppievhlvk sgeapggige pgtaataaal
      721 snaifaatgk rlrklpvgnq lkta
//
LOCUS       WP_175918108             224 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175918108
VERSION     WP_175918108.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..224
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25486
     Region          2..221
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 masekargqs vadrishqlr ehiisgklpp gtaliemdla aeydtsrnsl revlhqlgre
       61 glvtfvrhkg vvvrtlnrqd vrdlyvarrt lelhalntae laqpallekm qtaigaaere
      121 lakenwqavg thslrfhqhi valqksalld effrtisaql rlvfasdpde krvqtadwiq
      181 reyriyellt qnrrseavta larylddser mlldairrsq rdaa
//
LOCUS       WP_175918122             413 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175918122
VERSION     WP_175918122.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..413
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45056
     Region          69..387
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mtlneswfap lvgilvllaa agaitaavhf llfrvvarla rlsatrvdda lfefgafswl
       61 nrivpfvvik lglgavpgip dtaaqavdkv lfalivflvt mtisatlsal ehthrthhrd
      121 qprlslkgam qlvklvmfit aalvvigdat gkqiglllsg igamsavlml ifkdtllglv
      181 agvqlssndm lrigdwitmp sagadgtvid itlntvkvan fdhtiitvpt wklitesyqn
      241 wrgmteaggr rikralfvda tsvrflande ierlerltll kdyledkvda ieqwngtlga
      301 agdcpanrrq ltnlgtfray vanylkghpr irrdmtcmar qlpltaegip lelycftdtt
      361 swvdyetiqa dlfdhliavl pefglrvyqh psgfdmrqma gaaqaglpap rag
//
LOCUS       WP_175918125             306 aa            linear   BCT 11-JAN-2025
DEFINITION  bestrophin family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175918125
VERSION     WP_175918125.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..306
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33598
     Region          1..299
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 mivrprehwl rmllvwngsv lptilpqlvl tlaislvavw gggrvlgekv plnptpftli
       61 gltlaifagf rnnasydryr earqlwggvl tatrtlvsqa lcygavdhdd darrafvrtv
      121 vafvyalkhq lrgtdpaadl ralldhgtya rvgasrfrpv aivhelreaf aaradaghla
      181 dtrlwmldar ldelvamvsg ceriastpip fsydvllhrt iyaycvllpf glvdsigaat
      241 pfvtvfvayt lialdaiaha iaepfgdgpn hlaldaitrq iertllelnr eplpaevtpg
      301 rsfrlt
//
LOCUS       WP_175918126             682 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175918126
VERSION     WP_175918126.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..682
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=71498
     Region          30..667
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mkfafpslpp laaaraalrd ahpalppgav afalrntaas llalyiafrm nlddpkwaas
       61 tvwivaqgsr gmglsksqyr ilgtaigaav alaltgafaq tpelflaala awiglcagva
      121 tfqrnfraya avlagytaai iamdaasapl hafdiaiarf lyvvvgilcg aafetifapg
      181 apltdvrtrl aryldraiav gagalrrepn gaavhrlfad aleldtaaey aaagappvrn
      241 aighlraaal gvltaqaagq airehaargg dapdplvdda arvldgvtas rasgasgdpg
      301 remaalrarv ddalraevag pagpdtsrll mldrlaalla gfdhalasqa lldrpepppt
      361 rvryafhrdp vlawhngira fvavlaasal wivtawpsga gfvaitavvg alfstrpnsv
      421 raavgflkgs acaavagvvc nfillpavsg femlayilgv fligtgiamr hprtaamgsa
      481 fsiffwnfts pdntvrigda aflnaavstl lgiafgalvf alvfpgdpgt srrrlhravr
      541 rdlagiardp rawsastwls rtadrlarel gfagslpqtl ierdmrdlla iwgfgdslls
      601 laelaarepa vrraatvvrg rveraefaql drtcdvaarv lrrrvaardg ddthallrgi
      661 vllrriadta aehggflrgr hg
//
LOCUS       WP_175918154             339 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175918154
VERSION     WP_175918154.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12168323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36913
     Region          27..201
                     /region_name="AraC_binding_2"
                     /note="AraC-binding-like domain; pfam14525"
                     /db_xref="CDD:434015"
     Region          255..335
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mpltsnaevl salyrncvfr sglradaheq vslelaehal rwkqgvpdaa lfkgelnhls
       61 vyalqygaev evaprpfdgf slvhtslagg aeiecdghvm rvsegrtavl aprthvrlrw
      121 rsgtrqlivk vpdslmravc grrpddaapg lapgfllpta lasqwdliaq sllnmlaiad
      181 dggiraewrd hferslalfl llhcppspaa ahagavpqar gapaqagsrg girqmdalhe
      241 fiharlcapi sledlaraag vslrtlnvlc rryhgatpme llrnirldaa rvqlltdpma
      301 sitdtaltfg fghlgrfsay yfarfdelpr dtqkkrapn
//
LOCUS       WP_175918150             504 aa            linear   BCT 11-JAN-2025
DEFINITION  MDR family MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175918150
VERSION     WP_175918150.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..504
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52950
     Region          38..422
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(39..40,43,74,124..125,127..129,132,152,155..156,159,
                     284,287..288,291..293,296,324,328,381..382,386,390,406,
                     409..410,413..414,417)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mttdtlltpp aaetarrdap tglivaalll vmllsaldqt ivstalptiv gelggldqls
       61 wvvtayllss tvvlplygkl gdlygrkivl qaaivlflag salcgiaqdm tqlivlralq
      121 glgggglmvv tmaaigdlvp pdrraryqgm fggvyglati vgpllggflv ehlswrwift
      181 inlplgflal avigiafrph aahvkhridy mgaaflatal tcvilftseg gsllpwtspq
      241 lwmtlvlglv aiggfiyeer laaepiiple lfrhrtfvlv sligfvvgta lfgsvtftpl
      301 ylqvvkgstp sqagmqllpm mggmlamsvi sgrlisrlgs yrifpiagtl iggialalls
      361 tlsldtplqt myaymallgi glgmvmpvlt lavqntvefr hmgvatsgat lfrsigssig
      421 vaafgalfsh glqarmlqal pagtelppal gpgavhqlpd avrdaylhaf agslhvvyla
      481 aatvvaiafv lawfvedapl rthn
//
LOCUS       WP_175918156             280 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175918156
VERSION     WP_175918156.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..280
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30458
     Region          19..239
                     /region_name="HTH_MerR-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     transcription regulators from the MerR superfamily;
                     cd04778"
                     /db_xref="CDD:133405"
     Site            order(21..23,37,53..55)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133405"
     Site            order(67,70,74..75,84,105,109,115,119,122..123)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133405"
ORIGIN      
        1 mskqthstpd eaaadsrney tvdelarvsd ttvrnvrayq drgllappek rgrvgiyddt
       61 hvarlklinh llargytlsn iqdlikaide ghdlrsilgl enaiggrwsh elpktyslaa
      121 laqmfgpqat tqlsrvtelg llerhglsfv akspalleaa aamtkegipp relldvisla
      181 rphfdaiarl lvdlvvkrld rydadtlppa tdvpelvdai wrlrplaavf vegetnrale
      241 taasaylggr vatildkkls ddeaarqsgt pdtqgdvdka
//
LOCUS       WP_175918174             466 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175918174
VERSION     WP_175918174.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..466
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49543
     Region          42..449
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(51..52,55..56,59,91,141..142,144..146,149,169,
                     172..173,176,284,287..288,291..293,296,324,328,379..380,
                     384,388,404,407..408,411..412,415)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mstfdnvvag ratmeaaast pgaiiarler lpgnamqira rvligtatff dgfdvitiaa
       61 tlpllihkwg lsptqigmli asgaigqlig aflfpalaek hgrvkaiaws savigitsia
      121 cgfaptfevf vllrilqglg lggelpvaat yineitrahg rgrfvllyei vfpigllvsm
      181 algawlvprf gweimyfvgg lplilslvlt rlvpesprwl asrgrlaeag ravgvfeasv
      241 rgelppvtqa aafdemvrqh pkrrmsdlfs aayrkrtlav atlwatcgfi qyglstwlpt
      301 iyknfyhapl qlalnlavig svmgvlgsla sallvdklgr kpvivwsfvl calslafagi
      361 yhassvyvva ifcslslglm asgfitayvy tpeqyptsir asgcglgsaw lkiasfvapm
      421 vvphaiiggn lapafyligv vpliaavtvh fvgietkgkv lealea
//
LOCUS       WP_175918203             303 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia contaminans].
ACCESSION   WP_175918203
VERSION     WP_175918203.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia contaminans
  ORGANISM  Burkholderia contaminans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Burkholderia contaminans"
                     /db_xref="taxon:488447"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32672
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like_2"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08471"
                     /db_xref="CDD:176160"
     Site            order(102,106,145,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176160"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176160"
ORIGIN      
        1 mnrlesmsml vavidagsms aaarqlgipl atvsrkiadl eaylntrllh rttrqlslte
       61 agesyvagcr rilddiaete raatgeyaap rgelivtapi vfgrlhivpv laaflahype
      121 idvrlvltdr vahlmeeqid valriselpd ssfmatrvgs vrrvicaspa ylaahgtpae
      181 padlarhqci tfevlasrra wvfdgekgel tvpvhsrfav ntaeaaidaa vlgvglirvl
      241 syqvaqalrd rtldvvldaf esqplpvslv hkgqapmplk lrafldfvap rlreriagvg
      301 agg
//
LOCUS       WP_175918214             217 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            pyrrocinia].
ACCESSION   WP_175918214
VERSION     WP_175918214.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..217
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23770
     Region          29..180
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maevteraps krrtrgrpla gasvgpdvil raarrtfakr gydatsvrev arelgvdaal
       61 iahhfgtket lwlavveqiv dlatpmfdal ralrtsslph rdrvrralel cvdhefdepd
      121 igmffstaat evggrldrlq erlvrpyhda mfplltdavd agairpvdpd vlffmiasai
      181 gttvsyshmm laftslptqr dafkqavlaa alniigd
//
LOCUS       WP_175918219             292 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Burkholderia
            pyrrocinia].
ACCESSION   WP_175918219
VERSION     WP_175918219.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..292
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31933
     Region          1..276
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mgtsiralll sqmdsftpse qkvahalldr ypslglgpia sfakqaevsd ptvfrfvvri
       61 gfpnyssfqq alygeidtam nsplarmdaf hseagmrdsh saifqrlses lattieglda
      121 aafdaavtll aapdvrifcg ggrytaplas lfsftlayar phvqyvepnv nlasvaltdm
      181 grddvlvifd frryqkdsir faqaahrlgt rillitdewm spigafaeiv lriqgrpfam
      241 lqtnvpalal aealvigvtn rlpelarqrm ekiehlstgg idldanqrdl pe
//
LOCUS       WP_175918283             561 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175918283
VERSION     WP_175918283.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..561
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=57991
     Region          147..266
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(149..150,201..202,209,213,215,257,261)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
     Region          295..>397
                     /region_name="PRK11907"
                     /note="bifunctional 2',3'-cyclic-nucleotide
                     2'-phosphodiesterase/3'-nucleotidase"
                     /db_xref="CDD:237019"
ORIGIN      
        1 mtirspivlg valcvsgcai npqtgqpevv asvksqfnsi fnnedpcsnn grnigiavga
       61 maggvigyla hgakgaaagv vigagggflv ghtldarrce lyriaqangl klasapitqa
      121 kpgvansadk patigldvql enksdefvag taeltpqark ylaqiatqys pktllaalps
      181 natpeqraqv gsrrvlivgh tdendsslga dpatlsqqra kavakvfadq gvpvqnifyq
      241 gagdtlpiap nttdqgreen qrvqivdvpt ekdlqqflsa rtadpanyrf anantvspqg
      301 tssgertntv tptsathatt gqttikrrsk pttvakagna sniktevsas ptvastaapa
      361 svappqatag vrdagagydf ggtptagggi pvrlgstpak sssfsliana nagspmtlns
      421 clgdrphvts avrnlatdqv lnvrdylpgf ygapwaaglg gnlialldvr vpsdagspvp
      481 epelkiykdy sgnvsqkpsy sarvpvnvyr gsdatlyrvf vrgpmqcmdl vvpvskprat
      541 gnvyytnrsv dytasgnfal r
//
LOCUS       WP_175918312             314 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia pyrrocinia].
ACCESSION   WP_175918312
VERSION     WP_175918312.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..314
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33194
     Region          83..286
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mlvdppiaaf ldaleksgek klyegmpeea rasyrtlaag lhppgttisv gsveniavdg
       61 algelparvy rpegngpfpt aaffhgggwv igdldthdnv craicresrv vvvsvayrla
      121 pehpfpaavd daiaatqwvv dhapdlggna lvavagdsag gnlsavvaha fradgvelag
      181 qlliypatdv pgtrhlswqq natgylldrp liewflhhys ggrqrledpr itpihagtfs
      241 glppavivta qfdplrdvgl ayaealsagr vpvhvepgqg lihgffemgq lspaaqgaie
      301 rscrrfgevi raar
//
LOCUS       WP_175918319             515 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FGGY-family carbohydrate kinase [Burkholderia].
ACCESSION   WP_175918319
VERSION     WP_175918319.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..515
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=55394
     Region          3..448
                     /region_name="ASKHA_NBD_FGGY_RrXK-like"
                     /note="nucleotide-binding domain (NBD) of Rhodospirillum
                     rubrum xylulose kinase (RrXK) and similar proteins;
                     cd07804"
                     /db_xref="CDD:466806"
ORIGIN      
        1 meyvigvdig tqstkallvd rhgtivarrs agyqpdtprp lwaeqwpqvw fdavlecvag
       61 cvsdaraqgv padairalcv sslyggsgip vdsdmrplhp cliwmdrrat aqvdwvgehv
      121 nverlrvitg ngvdsyygft kmlwlrdqrp dvwanvryfl ppnayviyll tgevavdhss
      181 agniggvydv arrewsddal dmlgipatmm perlvdstei vggllsqwte qlglpagtpv
      241 vaggvdaava tfaagatrig qhvamigtsm cwgyvnrhvd arhglvsmph vfdgqrdlyv
      301 fggaitagas vawfrdqfch aeidaarvlp hgdphvllee aaervpagad gvlflpylmg
      361 erspvwdaka sgafvglsla htrahlyrav legiafalrh nieagrrgav alddrlivvg
      421 gaahsalwmq iiadvtgfpv wtieqdveaa mgaallagvg aglvshgdaq ggwvtlvera
      481 rpdaerakay aarfalytal ypalkpimhe lhtps
//
LOCUS       WP_175918431             441 aa            linear   BCT 11-JAN-2025
DEFINITION  leucine-rich repeat-containing protein kinase family protein
            [Burkholderia pyrrocinia].
ACCESSION   WP_175918431
VERSION     WP_175918431.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Shen,K., Hines,A.C., Schwarzer,D., Pickin,K.A. and Cole,P.A.
  TITLE     Protein kinase structure and function analysis with chemical tools
  JOURNAL   Biochim Biophys Acta 1754 (1-2), 65-78 (2005)
   PUBMED   16213197
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
REFERENCE   7  (residues 1 to 441)
  AUTHORS   Hanks,S.K. and Hunter,T.
  TITLE     Protein kinases 6. The eukaryotic protein kinase superfamily:
            kinase (catalytic) domain structure and classification
  JOURNAL   FASEB J 9 (8), 576-596 (1995)
   PUBMED   7768349
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..441
                     /product="leucine-rich repeat-containing protein kinase
                     family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=47365
     Region          <2..>193
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          39..61
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          62..84
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          85..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..175
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          211..438
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(214..217,220,222,238,240,269,287..290,345,349..350,
                     352,362..363)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
ORIGIN      
        1 mtttleqlqa gqlsgarqlk lacgltefpr eifdladtle vldlsgnalt alpddlsrlh
       61 rlrilfasgn rfttfpdvlg acaqldmigf kanrirtvpr gslpralrwl iltdneidal
      121 paeigdcsrl qklmlagnrl ralpaemaac ralelvrlsa nrldelpdwl trlprlawla
      181 ysgnpfsaap evaasagpev advdwaslsc eqklgegasg viyraqwqad ghapravavk
      241 lfkgtvtsdg lpdcemaacl hagrhpnvip vigkvrghpy gthglvmelv dpalanlagp
      301 psfatctrdv yaadarfepe eavriahgia saarhlharg imhgdlyahn ilhdgeggal
      361 lgdfgaasfy dtsdaqhgar lerlevrafg hllgellahc aphtwgrard lealamacvs
      421 edidtrpsfd givdalaawk v
//
LOCUS       WP_175918473             318 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia pyrrocinia].
ACCESSION   WP_175918473
VERSION     WP_175918473.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..318
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33623
     Region          80..293
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mlepeiaafv aavdawypad aaarspdeqr rlydrfaaaw tpaalpagiv qqdavwhapd
       61 graialrryt aahgkprgtv lffhgggfvv gsldshalit aqlaadtgld viavdyrlap
      121 ehrapaaled clavtraard arwpfgpcvh pltlagdsag gmlaaavata lrdageggid
      181 gialvypmlg fepqsparet eahapmltld dvyryralyw egglsdalte gdpllrasvp
      241 laasrfdglp pvlaigaehd plrddarvyv erisaaggaa rywmgeglvh gcwralgtsp
      301 qaawmhrtvg gfllaphv
//
LOCUS       WP_175918490             388 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: electron transfer flavoprotein subunit alpha/FixB
            family protein [Burkholderia].
ACCESSION   WP_175918490
VERSION     WP_175918490.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..388
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39918
     Region          90..368
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mntikridpr rpfiitaagl kritlgeegs adasaahwsa hghaaaakpr ravqepkhvv
       61 lvvahgerga lddharqaia aaavladaqt evallafgel kddvaelgvd klvelagfdr
      121 rafdpeselq alqacvaals pkhvfvpdna tgdgdlgrry aaaagasvat nvveidakhv
      181 gayaqagraf atrglpdvil laqnavdakl pfvgagerla adfirpahda aqpyrdlgle
      241 eidaarvale eadfivsagn gvsdigafeq lagafgaaig asrvavdngh ftrdkqvgat
      301 gktveasvyi afgisgavqh lqgikdcrhv iavnldgsap iakranltvv gdaqatiaal
      361 ieqvqaarva rgqspaavgn repegvaa
//
LOCUS       WP_175918493             424 aa            linear   BCT 11-JAN-2025
DEFINITION  serine hydroxymethyltransferase [Burkholderia pyrrocinia].
ACCESSION   WP_175918493
VERSION     WP_175918493.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Appaji Rao,N., Ambili,M., Jala,V.R., Subramanya,H.S. and
            Savithri,H.S.
  TITLE     Structure-function relationship in serine hydroxymethyltransferase
  JOURNAL   Biochim Biophys Acta 1647 (1-2), 24-29 (2003)
   PUBMED   12686103
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Chan,V.L. and Bingham,H.L.
  TITLE     Complete sequence of the Campylobacter jejuni glyA gene encoding
            serine hydroxymethyltransferase
  JOURNAL   Gene 101 (1), 51-58 (1991)
   PUBMED   2060796
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10793727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..424
                     /product="serine hydroxymethyltransferase"
                     /EC_number="2.1.2.1"
                     /GO_function="GO:0004372 - glycine
                     hydroxymethyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019264 - glycine biosynthetic process
                     from serine [Evidence IEA]"
                     /calculated_mol_wt=45380
     Region          4..424
                     /region_name="PRK13034"
                     /note="serine hydroxymethyltransferase; Reviewed"
                     /db_xref="CDD:237280"
     Site            order(16,18,25..26,35,40,58,76..77,85,100,107,142..143,
                     268,286)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:99733"
     Site            order(39,59,69,102..103,130,180,205,208,233..234,240,366)
                     /site_type="other"
                     /note="glycine-pyridoxal phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99733"
     Site            order(39,130,234,366)
                     /site_type="active"
                     /db_xref="CDD:99733"
     Site            order(61,68,125,129,131,260,350)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:99733"
ORIGIN      
        1 msntqpffsq tlaerdapvr sailkelerq qsqveliase nivsravlea qgsvltnkya
       61 egypgkryyg gcefadevea laiervkqif nasyanvqph sgaqangsvm lalakpgdtv
      121 lgmsldaggh lthgakpals gkwfnavqyg vnrdtmlidy dqvealaheh kpnliiagfs
      181 aypraldfar fraiadsvga klmvdmahia gviaagrhan pvehahvvts tthktlrgpr
      241 ggfvltnded iakkinsavf pglqggplmh viagkavafg evlhadfkty idnvlanaqa
      301 lgevlkaggv dlvtggtdnh lllvdlrpkg lkgapveqal eragitcnkn gipfdtekpt
      361 vtsgirlgtp agttrgfgva efrevgrlil evfdalranp egdhateqrv rreifalcer
      421 fpiy
//
LOCUS       WP_175918494             341 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175918494
VERSION     WP_175918494.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..341
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37485
     Region          11..318
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mspdrtasls hfafmplpnf tmiaftnaie vlrmanylsg qplyrwsvis pdggpvtasn
       61 gltvdtgpae cvgqpdivfv cggidvqrat tpahlsalrr farsgiplgs lctgtyalak
      121 sgllagyaca ihwenmsalk eefpdtrflk elfvidrdri tctggvapld mmlnliaarv
      181 gtarvtqiae qfivehvrdt saqqrmplva rlgsankslf evislmenni eeplsreela
      241 rlanmsqrql qrlfrehlgm tpthyyltlr lrrarelllq tdmsimhitm acgfqsachf
      301 sksyrdsfgv aptrerrkqv aplaqgavsa tpafpvravh a
//
LOCUS       WP_175918530             800 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia pyrrocinia].
ACCESSION   WP_175918530
VERSION     WP_175918530.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 800)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 800)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..800
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..800
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84158
     Region          83..763
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mirrpkavgr gnamrgdrra rhagailglt lgptlgaial fglstagvha qpnadgttdg
       61 aaaasaaapp aaaaapqasa dmlpavvvvg ttpllgigtp lskvpanvqt vraaefdaqh
      121 ratltdffaa nlqsvtisea qgnpyqtdvn yrgftaspll gtpqglsvfv dgvrvnepfg
      181 divnwdilpa qaidrmqlip gsnpvygrnt lggalaittk ngksnpgsea evsggswgrk
      241 tadieqggti gsnldyyata nvandggwad hnasrvrqaf gklrytdadt tlsiaaggad
      301 nalygtqtip rsfldnrkqa ytypdlnrns agyltlsgdh ffgeqvelsg nayyrhlrns
      361 nissnnnntd ygsvgadgtv dtvqgtnaqs tivtdsyggs lqltllgklg gmsnqliagv
      421 aadvanssyv assqdayftd traaigvgdf vqrtnaktrn anlgvylsda lsltphwtlt
      481 lsgrydwsks qigdesgsqp lldgnhtfsr fnpavglnwn pvagftayat ynegmrspta
      541 ielacadpaa pcslpndfia dpalkpvisk tfevgargri gaattwsaaa yrttltddiq
      601 fisspasaqg yfrnvgdtrr qgielagrtq lgpvgvglsy syvdatyrss wtehspansa
      661 adasgnvavk agdripgipa htvmlrldya athawnigan vtwrsgvfar gdennkdang
      721 riagyvlvdl dmryriskrf evfasvtnlf dkryasvgvl gqnffngpnh tfdganpvne
      781 qfvgpgaprg awvgvryawd
//
LOCUS       WP_175918549             160 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia pyrrocinia].
ACCESSION   WP_175918549
VERSION     WP_175918549.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 160)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 160)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..160
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17479
     Region          <30..156
                     /region_name="CccA"
                     /note="Cytochrome c, mono- and diheme variants [Energy
                     production and conversion]; COG2010"
                     /db_xref="CDD:441613"
ORIGIN      
        1 mnglnrvshr vgrnwrlils vaacvgvgwl altrlqapva shdarfeqgr rlyeavvpmr
       61 arlvgqgfdl pstatrcvnc havtaqpgqs gfapaltgam ltenrrrrgg pasaydmaaf
      121 crvlregidp aqvmvnsvmp rydvdreqca aiwlyltrtp
//
LOCUS       WP_175918557             258 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia pyrrocinia].
ACCESSION   WP_175918557
VERSION     WP_175918557.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 258)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 258)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..258
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26299
     Region          58..242
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mtmhsarptr salrrllpay aaratalall lvlllrpawl qglfapfadn gapviydras
       61 lldltlahlg tvalssligt ivavaagifv trpagadflp varsvvdigq tfppvavlal
      121 avpavgfglk pvlialvlyg llpifestia gledvprdvv daargmgmsg wqqlvsvelp
      181 lafpvivngi rlavvinlgt atigstvaar glgdviiagl qtsntafvlq ggvivgllav
      241 lvsdaigaia rvaaarra
//
LOCUS       WP_175918601             143 aa            linear   BCT 11-JAN-2025
DEFINITION  GFA family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175918601
VERSION     WP_175918601.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..143
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15391
     Region          3..130
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mtrtqsarcl cgavtvtlrg epaaranchc atcrdfygtp mlsatawppe rvaidggnat
       61 fphpsksmsr twcascgeiv fgtnrlgmrv vpnslaarah ggqlpddlqp tmhlfyrqrv
      121 idvvdalpky ldgwdgptld nan
//
LOCUS       WP_175918595             242 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175918595
VERSION     WP_175918595.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..242
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27130
     Region          20..237
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 msetaafeed vvvtalqgfs ldesrsyteq vhvllrhaiv rgalpphtal seavisttik
       61 vsrtpvreaf aqladerlvq ihrkvgtfva pipmsileeg rfarstleca nhvelaqkit
      121 aeqlaelsri idaqraavaa hdveaffeld eamhgrmfaf agrphvweml qpmkrqfdrv
      181 rwllldrved harralqehe qilahiasrn mallgasvat hvdrigshlp dvrsraphyf
      241 vd
//
LOCUS       WP_175918620             252 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [Burkholderia].
ACCESSION   WP_175918620
VERSION     WP_175918620.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..252
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27039
     Region          1..252
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlaeqrhqyi lselgrsgal svaelvrsld vsretvrrdl nalaargllv mthggalaad
       61 rrepslsere aanaeakrti grraaefvpd dasvlidsgs tphavalala drhrlsiytn
      121 dwrtafvlar rngnrvtllg gelsddedat fgldtihqla qyhvdfafvg aggitpdgec
      181 tdysriaaev rsrmiaaagt aiivadhskf grvtpvring aaaarylvte rapdkavrra
      241 ltargiellv cd
//
LOCUS       WP_175918642             457 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia pyrrocinia].
ACCESSION   WP_175918642
VERSION     WP_175918642.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..457
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47970
     Region          221..412
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mrlnlrfrla reqgqparrg vrcfpirral lrgvvaaaca agtqgataha fhdaapftpv
       61 tpetadlvdv pffssarttw gglrasaavp ldvaygshas nvpmgtdrdd pvtrfgacva
      121 yrvlcdaarg aiergyatrf aygiasplps igaqpafers avdlasaepf mlaepdrgtr
      181 agaitgslra slaraelpag vaaqvirlla gridpkqrge igdtfrvafe pdgdaslpng
      241 vrvtaldirf rgqqvagvwf apatgspgay ydldgmplfg arfsmpvaat rissqfgarv
      301 hpvtgarhvh sgvdlaaptg ravhasehgv vsfigtepsg ygkyvvirhd ggyasyyahl
      361 safeptlrtg arvergqrvg avgstgtatg phlhfevrrq nrivdpvalv qaakaatlkg
      421 drrvafnrva vdartrlasa awsqpvaiat pvaphag
//
LOCUS       WP_175918671             418 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia pyrrocinia].
ACCESSION   WP_175918671
VERSION     WP_175918671.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 418)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 418)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..418
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45150
     Region          <195..412
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mtiapsspst aalkrelkaa earkrtmall lvaplaifll lifvvpigtl ltravqnpei
       61 atalpntvaa lsgwdrkapp adaayvalaa dmtkvadsea mgalarrlnt eipgyrslva
      121 ktaramplkg dndatltpaq trakfields rwgelaywqs iakngsqvsp fyllaaldhk
      181 qdgfghivea dpdqsiylsi fgrtfvigva vtlfalllgy playwistqs erranlvmil
      241 vlipfwtsvl vrvaawivll qseglintal igsglishpl tllfnrvgvy ismthillpf
      301 milplysvmk sipptyqraa vslgshpfaa fwrvyvpqty pgigagallv filaigyyit
      361 pallggpndq mvsyyvayft nvtinwgmac algglllaat lvlyavygrf trtnvslg
//
LOCUS       WP_175918677             325 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175918677
VERSION     WP_175918677.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..325
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34367
     Region          6..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..302
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 medidlnlvt aldallsegs vtgaarrlgl stsamsrtlt rlrlstgdpl lvragrklvp
       61 tphaaalrdr vhaiasdara vlrpatadvd matlastfti rasasfmeml sgpvvaaige
      121 vaphvrirfv pkpdrdpqal rdgtvdleig krgddapelh trmlghdwhv avaraghplf
      181 asaritpary aacrhviasq lgdfsgptda ptgpsgpgqa vhvvvpgypd amrvaastdl
      241 ialvprsslg nafspgfaea lglrsfeipv rlpailvsal whprmhadpv hrrlrdavia
      301 vcqraypdsr apraparstk trtag
//
LOCUS       WP_175918678             382 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175918678
VERSION     WP_175918678.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..382
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=42102
     Region          27..84
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          116..318
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(131..132,134..135,138,142,144..150,244..249,
                     255..256,258..259)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrdplapnap prdasaatdv ldvldarlmr illvlltert vsraavrlnm sqpatsaalk
       61 rlrtllgdpl lvrsrygmvp tefgarliep lrnalrvidf irvqqptfda rtsvrtyrig
      121 cpdylnvlfv pklvalfrer apnaqlvfhp lgdgfddera ladgeldvvi dnrparssrf
      181 rqddlfddrv vclmrathpl arrgtitaad faaapqlcpt pswleasgai drqlervglq
      241 rrivvtlphf elaahalvrs dmiltttyrl arhyakllpl aavalpaepp divyrmtwne
      301 sgscvegvsw lrgliaeatr gwldaeaalp avaavaaatv patpapeplr sprarkathc
      361 rashrplvar aarhqrhttk sh
//
LOCUS       WP_175918742             390 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175918742
VERSION     WP_175918742.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..390
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42783
     Region          12..282
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 midgqillgh sirwgmvggg lgsqigyshr saalrdgsfe lvagafdidp ergrqfgvkl
       61 gvaaercypd yatmfdaear rpdgiravsi atpnnthfei craalnaglh vvcekplcft
      121 tdeaetlqrl sieknrivgv aygysghqmi eqaremiarg dlgeirivqm qfahgfhseg
      181 veaasaaarw rvdpkfagps yvlgdigthp lyisevmape lkirrlmcsr qsfvksrapl
      241 ednaftimey dtgaigyvws savnagsmhs qkvrvigska svewwdehpn qlryevqgqp
      301 aqvldrgmgy lhpnalredr igaghpeglf eawsnlyarf alamdaadrg daatlkgirf
      361 pdvhagvegv rwvencvrsa daggvwvdyr
//
LOCUS       WP_175918795             232 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175918795
VERSION     WP_175918795.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..232
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24711
     Region          37..230
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mlahrrweal daanhgwlra kyhfavtadg tpehaplgpl ivwnddeiav gsgfpmhghr
       61 dmeiityvrq gvlghrdtlg segtifagdv qvmsagagir haefnrgdlp lkvyqiwlrp
      121 rasggapgwd tkqfpkgdrs grfvvlasgf agddgalpir adarvlgatl kageqvrqel
      181 gasrraylva asgridvnge rvgpldgvai tnetaldita vedselvmvd ag
//
LOCUS       WP_175918780             201 aa            linear   BCT 11-JAN-2025
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175918780
VERSION     WP_175918780.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Sciara,G., Clarke,O.B., Tomasek,D., Kloss,B., Tabuso,S.,
            Byfield,R., Cohn,R., Banerjee,S., Rajashankar,K.R., Slavkovic,V.,
            Graziano,J.H., Shapiro,L. and Mancia,F.
  TITLE     Structural basis for catalysis in a CDP-alcohol phosphotransferase
  JOURNAL   Nat Commun 5, 4068 (2014)
   PUBMED   24923293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Koga,Y.
  TITLE     From promiscuity to the lipid divide: on the evolution of distinct
            membranes in Archaea and Bacteria
  JOURNAL   J Mol Evol 78 (3-4), 234-242 (2014)
   PUBMED   24573438
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Koga,Y.
  TITLE     Early evolution of membrane lipids: how did the lipid divide occur?
  JOURNAL   J Mol Evol 72 (3), 274-282 (2011)
   PUBMED   21259003
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..201
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21159
     Region          28..196
                     /region_name="PgsA"
                     /note="Phosphatidylglycerophosphate synthase [Lipid
                     transport and metabolism]; COG0558"
                     /db_xref="CDD:440324"
ORIGIN      
        1 mslyalkpkf qdrlrpfans laergvtanq vtlfaaggsi vvgalaglgv farvlfllip
       61 lwlfarmaln aidgmlareh gqkstlgayl nelgdivsdv alvlpflais vfapadvwlf
      121 altaviveca gligplvgat rrydgpfgks dralalgafa lwigfglpvg siaawlwrll
      181 ivlsivtvvr rvqagiaekg g
//
LOCUS       WP_175918862             257 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Burkholderia].
ACCESSION   WP_175918862
VERSION     WP_175918862.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..257
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28041
     Region          1..>240
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mnllelddlr laydtpqgrr tvvdglslal prgdigcllg asgcgkttvl raiagfepvr
       61 mgrivldgmp vaapsldvpp errrigmmfq dyalfphlsa adnvafglrr mpkaerrarv
      121 admlelvgla esggayphel sggqqqrial aralapspel llldepfsnl dvdtrerlaf
      181 elrdilkrtg htailvthnq aeafaiadri gvmkdgrlaq wdtpyalhhh paspfvadfv
      241 rrdaladera ralargr
//
LOCUS       WP_175918885             288 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: pirin family protein [Burkholderia].
ACCESSION   WP_175918885
VERSION     WP_175918885.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..288
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30710
     Region          12..278
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mkkiqgvysa prghwvgdgf pvrsmfsyqs hgthlspfll ldhagpttfe pataprgvgq
       61 hphrgfetvt ivydgevahr dstgaggvig pgdvqwmtaa sgilheefhs eaftkrggpl
      121 emvqlwvnlp aadkmgapgy qtllnadipv velpdgagra riiageldgr rgparthtpi
      181 dvwdvrlvag gharfpiadg rtlavvvlsg tvqvngetva reaqfvqlgr egrdveiean
      241 gdakllilsg epidepvvgy gpfvmnsqae irtaiedfnn grfgkmpa
//
LOCUS       WP_175918919             249 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Burkholderia pyrrocinia].
ACCESSION   WP_175918919
VERSION     WP_175918919.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26425
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkilvpvkrv vdynvkvrvk sdntgvdian vkmsmnpfde iaveeavrlk eagvatevva
       61 vsvgvtqaqe tlrtalaiga drailvestd sveplavaki lkalvdkeqp qlvilgkqai
      121 dddsnqtgqm laalaglpqa tfaskvtvad gkatvarevd ggaetlsltl pavittdlrl
      181 nepryvtlpn imkakkkple tvkpedlgvd vaprlktlkv veppkraagv kvpdvktlve
      241 klkteakvl
//
LOCUS       WP_175918934             226 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175918934
VERSION     WP_175918934.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..226
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24860
     Region          10..225
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mntltditrd rpaasaisla drayaliqrd iitmrlkpga alneadlvar tgigrtpvhq
       61 avhrlvlegl lsvmprkglm vqplslddiv avidvrrine ahcaelaarh atpddlarma
      121 allddgqacv dthdvegmme ldrafhqaia aaarnavlte ilralhersl rfwfvtlsep
      181 hhladvqheh relferlsar daagaraave ghidsfrstl lqhlrp
//
LOCUS       WP_175918957             436 aa            linear   BCT 11-JAN-2025
DEFINITION  replication-associated recombination protein A [Burkholderia
            pyrrocinia].
ACCESSION   WP_175918957
VERSION     WP_175918957.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..436
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=47876
     Region          1..434
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 msdlfqvepr rplaealrpk tlaevigqth llgegkplrl afesgkphsm ilwgppgvgk
       61 ttlarltala fdcefialsa vlggvkdire smeqakdtln rtgrhtilfv deihrfnkgq
      121 qdallpfves glvtfigatt enpsfevnsa llsraqvyvl ksldddemrq llkraqetal
      181 dglafddkai dtlvgyadgd arrflnlleq aqtaassagv atidaefvss amtlnarrfd
      241 kggdnfydqi salhksvrgs spdgalywfc rmidggadpk ylarrivrma wedigladpr
      301 alqmandaae tyerlgspeg elalgqaviy lacaaksnag ynafnqamaf vkqdksrevp
      361 vhlrnaptkl mkelgyghay ryahdepnay aagetylpdg vrephwykpv prgleskiad
      421 klawlreldr eagkkg
//
LOCUS       WP_175918967             116 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DUF190 domain-containing protein [Burkholderia].
ACCESSION   WP_175918967
VERSION     WP_175918967.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..116
                     /product="DUF190 domain-containing protein"
                     /calculated_mol_wt=13275
     Region          5..103
                     /region_name="COG1993"
                     /note="PII-like signaling protein [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:441596"
ORIGIN      
        1 mdriflrfyl heqhrlhwkp lwewlleean rmgvaggsaf ramagfgqhr vlhedrffel
       61 qgslaievef ivtedeaqrl lerlsrekvr vcyamiparf gvidtlgapp aqgpaa
//
LOCUS       WP_175918987             226 aa            linear   BCT 11-JAN-2025
DEFINITION  urease accessory protein UreF [Burkholderia pyrrocinia].
ACCESSION   WP_175918987
VERSION     WP_175918987.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Soriano,A. and Hausinger,R.P.
  TITLE     GTP-dependent activation of urease apoprotein in complex with the
            UreD, UreF, and UreG accessory proteins
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11140-11144 (1999)
   PUBMED   10500143
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Moncrief,M.B. and Hausinger,R.P.
  TITLE     Purification and activation properties of UreD-UreF-urease
            apoprotein complexes
  JOURNAL   J Bacteriol 178 (18), 5417-5421 (1996)
   PUBMED   8808930
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..226
                     /product="urease accessory protein UreF"
                     /GO_function="GO:0016151 - nickel cation binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23897
     Region          1..226
                     /region_name="UreF"
                     /note="Urease accessory protein UreF [Posttranslational
                     modification, protein turnover, chaperones]; COG0830"
                     /db_xref="CDD:440592"
ORIGIN      
        1 mtitelvall hlaspalpig aysysqglea aldanlvhda dsardwiasg ltdvlahgel
       61 pflahqlarw hahdahalaa enawfiasre saelrreteq mgwslaqlca slewgdaarr
      121 atlasmspva lptafayaaa ahnasadatl aayafgwven qtsaalkavp lgqlagqrii
      181 valrgaidaa vrralatppd avntfapqlg ilsarhetqy srlfrs
//
LOCUS       WP_175919003             249 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Burkholderia].
ACCESSION   WP_175919003
VERSION     WP_175919003.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..249
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27188
     Region          4..249
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 mayielknvt ldlpifdvqg rslkkqvlrm grrnriaedn dgvivvrald nvnlrfergd
       61 rvglighnga gkstllrama giypptagtv srdgkvvpll diglgmdens tgmqnirlrg
      121 lllgmsdsev rskqreiaef celgdyldlp irtyssgmkv rlafavstav daeillldev
      181 mgvgdasfmh kaearladlh sraevvvlam hsnseirkvc nkvlwmergs vrafgpteev
      241 vsayeatta
//
LOCUS       WP_175919041             205 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: phosphatase PAP2 family protein [Burkholderia].
ACCESSION   WP_175919041
VERSION     WP_175919041.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130209
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..205
                     /product="phosphatase PAP2 family protein"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22580
     Region          42..198
                     /region_name="PAP2_Aur1_like"
                     /note="PAP2_like proteins, Aur1_like subfamily. Yeast
                     Aur1p or Ipc1p is necessary for the addition of inositol
                     phosphate to ceramide, an essential step in yeast
                     sphingolipid synthesis, and is the target of several
                     antifungal compounds such as aureobasidin; cd03386"
                     /db_xref="CDD:239481"
     Site            order(98,106,138..140,170,176,180)
                     /site_type="active"
                     /db_xref="CDD:239481"
ORIGIN      
        1 mntvslrddr rpdirqmlaa tfgmaaglai ffllersvtp ryvfataida ripfiawswf
       61 vyvgffpfvi alaayarppa faafkeavli afvlgvvcfl lfpeavprpd vaeigntfvr
      121 hrlvrmwqld laangfpslh vavtclacrm ltdrrrivat aigllicast ltlkqhtvad
      181 vlggvalamv galwgerrsl rrrla
//
LOCUS       WP_175919056             275 aa            linear   BCT 11-JAN-2025
DEFINITION  carbon-nitrogen hydrolase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175919056
VERSION     WP_175919056.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10166075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..275
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30432
     Region          12..272
                     /region_name="nit"
                     /note="Nit1, Nit 2, and related proteins, and the
                     Nit1-like domain of NitFhit (class 10 nitrilases);
                     cd07572"
                     /db_xref="CDD:143596"
     Site            order(50,106,123,127,138,163..164,166..167,186)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143596"
     Site            order(50,123,163)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143596"
     Site            order(124..125,144..146,164,167..171,173..174,194..195,
                     198..199,201..203,205..206,236,266..267,270..271)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143596"
ORIGIN      
        1 mtdhtrsatp frvaalqmvs tpdvarnlae arrliaeaag egaqlvllpe yfcfmghrdt
       61 dklalaepyq dgpiqrflad aarrhgiwvi ggtlplkape pdrvlnttlv fdpsgneaar
      121 ydkihlfnfe kgdesfdear tiragdtvvt fdapfgrvgl svcydlrfpe lyrrmgdcal
      181 ivvpsaftyt tgrahwetll raravenqcy vlaaaqggkh dngrrtwghs mlidpwgeiv
      241 avrdvgasvv fgaidpqria dvrqslpawr hrvlt
//
LOCUS       WP_175919088             215 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            pyrrocinia].
ACCESSION   WP_175919088
VERSION     WP_175919088.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..215
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22882
     Region          14..129
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          75..211
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mkdkpaqgpr gldkdaivaa alvlledvge aafsvrklaq svgcdpmsvl yhfkskdgls
       61 raianalsrs lvpvddaqpw rerlrdlarq yralalrhpa afallqrhms tgpadlahie
      121 avhralvdag ipraalpsvc vgwyasvigl aaaeaggltr pandveleem nalsdtehpl
      181 vrsaaplyaq ldpeivhdtm ldvlldgiak rahaa
//
LOCUS       WP_175919167             304 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175919167
VERSION     WP_175919167.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..304
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35175
     Region          85..242
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mrfdvellll alapvfllci aweawhlart raqdhvyawr dtlcnaalal mhqgadkiaw
       61 lfvipvyayc yrhyrlftwh dgwlsfavlf vaqdflyyvf hrashrvrwl waahvvhhss
      121 ermnfstafr qslmypvagm wvfwlplafa gfppqqvvgi vlinlafqff vhtqaigklg
      181 wleyvlntps ihrahharnp ryidrnyagv lviwdrlfgs yveetpddpp qygiverlgs
      241 nnpfvatfhe wvsmvadalr vdgwrnklra ifgppewasa yhaqiaeaat qdprtvphaa
      301 areq
//
LOCUS       WP_175919149             415 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia pyrrocinia].
ACCESSION   WP_175919149
VERSION     WP_175919149.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..415
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43284
     Region          23..409
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtnhrvmaiv gaghaggraa qvlresgwrg rivligaesh lpyerpplsk gvltgersaa
       61 qcrlrdpdaw aadgiepvva tveridphar evrvsggrvf gydalllatg ararrlaipg
      121 aaldgvfalr tlddaaalgp rlvpdarivm igggfiglev aaaarlrgcr vtvldaaprl
      181 lgravpesia arvqalheeq gvairvnrkp vaierisgga lavalddgdt liadtvvagi
      241 giepadelar daglavdrgi vvnarletsa rgihaagdva vfpsalsgrp irqetwhgae
      301 tqaraaarnm lgadepyrdm pwfwsdqyda qlqvagepal gelvvarrld gdaeihfhfd
      361 gggrlvaasg fgrasgfvke mklartlver gaaaapaava dsnvklksll ptaga
//
LOCUS       WP_175919175             318 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Burkholderia pyrrocinia].
ACCESSION   WP_175919175
VERSION     WP_175919175.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..318
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32970
     Region          3..296
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(36..37,40,91,105,107,136,168,256,259,295)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(227,232,247,256..258,261,283,287)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 maeivvagel laefvaterg qgfdtpglfa gpfpsgapai fadqaarlga rvayagcvgr
       61 dafgdgivar lerdgvdvar irrvarptgt afvayrddgs rsfvfslsts aaacvdasdv
      121 dtamfdgcry fhvmgsslts esaiaavqrg vieaaragak vsfdpnvrpe mlsfrpmraa
      181 ldemlaachl flpseadlpf fcgpqpaera iagllathpl lervvlkrga egsvafdras
      241 raeapafqvd eidptgagdc fggtlvaslv agvpidvalr ranaagaiav trrgpmegns
      301 saaeidrflt ergvacpa
//
LOCUS       WP_175919216             459 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia pyrrocinia].
ACCESSION   WP_175919216
VERSION     WP_175919216.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..459
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48955
     Region          13..457
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mtqqqrsfdn ivareqglrh altsgqmami aiggaigtgl flgsgfaigl agpsvlvsya
       61 igalialllm galaemtvah ptagsfgaya ehyvgplagf lvryaywfav vfaigteisa
      121 iavfmkywfp avpgwywvig fsalliavnl asvtlygsve yafsllkiaa ivvfvvlgas
      181 lvwsapaasg igfanytahg gfmpkgpwgt wvavivaifs ymsieavaia ageardpqha
      241 vtrafrstvf rlvlfylltl slmlaivpwt qagtdespfv kvmaathvpy aagvinfvll
      301 iaalsamnsq lyvttrmmfs lsrarlapav fgrlgtngvp raalwistsg vavaavlval
      361 apdtaftvmm aiamfgalft wlmifvthlc frsqyrgpal pfrmwghpfg gllgaglvaa
      421 ilfttaftre frmtmvvgvv fvvlltlaya lhyrhqhar
//
LOCUS       WP_175919238             273 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia pyrrocinia].
ACCESSION   WP_175919238
VERSION     WP_175919238.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 273)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..273
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29134
     Region          21..267
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtgtarhaaa sgndiacatv dltlkagtrt lldgftqafr pgeiwcvagp ngagkttlla
       61 tlaglhapag grveidgrpl aawpparlaq rralmpqqlh dafsatvfdt vllnrfpylg
      121 gwgwerdgdr aaardalatf dltalasrdv lslsggerqr valaatlcqd aplmlldepl
      181 ahldlhhqid clsalaawld agprtvlfsc hdlnlarrfa thallldgrg hawagpvhdv
      241 ltperasdaf gyplvliren grdallpawp erq
//
LOCUS       WP_175919291             403 aa            linear   BCT 11-JAN-2025
DEFINITION  benzoate/H(+) symporter BenE family transporter [Burkholderia
            pyrrocinia].
ACCESSION   WP_175919291
VERSION     WP_175919291.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..403
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41523
     Region          15..403
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mnpsptasad raggrrffad tsvsalvagf vammtgytss lvlmfqagra ahltdaqiss
       61 wiwalsigma lttiglslrf rapvvvawst pgaallissl pgvpyaeaig afvvcalllt
      121 aigvsglfdt lmrripagia aallagilfe igieifraaq fqtalvlamf ftylivkrla
      181 pryaivttli vgtavagglg lldfsrfhia laqpvftmpa fsiasivsig iplfvvamas
      241 qnvpgiavlr adgyqtpssp liattglasl llapfgshgv nlaaitaaic tgpeahedra
      301 krytaavwcg tfyliagifg atiaalfaal pkalvvsvaa lalfgsimsg lanamqdvkq
      361 reaalvtfmv tasgltllsi gsafwglvag ivtqvilnar rpa
//
LOCUS       WP_175919280             323 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 2 protein [Burkholderia].
ACCESSION   WP_175919280
VERSION     WP_175919280.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..323
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36132
     Region          6..187
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(9,11,96)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(43,95..96)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            94..96
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mkhitvvtpc fneeenvrav yeetrrvfst ipevtydhlf idnastdstv silrtiaadd
       61 pavgvivnar nfghirspmy gllqakgdav illvadlqdp pelmrefvks wlagapvvvg
      121 vkpeskesal ffalrrmyyr lvtqianvtl iqnftgfgly drkvieilrq iddpypyfrg
      181 lvceigfeik qipyvqprrk rgisknnfyt lydiamlgit shskvplrla tiagfvlsgl
      241 slfvsfmyfv lklvfwssfs mgsapmligl fffasvqlff igllgeyvga iltyaqkrpl
      301 vvererinsg gaaieaqaas rpn
//
LOCUS       WP_175919313             853 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia pyrrocinia].
ACCESSION   WP_175919313
VERSION     WP_175919313.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 853)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 853)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 853)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 853)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 853)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 853)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 853)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..853
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..853
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89929
     Region          13..853
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mpahagrfgl rdlirqaarm tardwragel tllvlalvla vasltsvgfl adrlrhgler
       61 darqmlgadf vvradrpvdp sfdrqaralg lraattaifp smiasaaggq asgaaparla
      121 avkavspgyp lrgaveilpa gaavahkata ipapgtvwad palldalhlk agdtvrvgll
      181 tftvaasisr eldrgfsfvn fsprlmmrad elaatgltgy gsrvtyrllv agdaqavarf
      241 etyahervdg gklrgvgles lqegqpqvrq tldrarhflt lvalltalla avaiamaaqr
      301 ymrrhldgca tmrclgvsrr tlgalfalef vgigivsgaa gavlgygghw allaalggli
      361 evvlppptpw paligvgaal vlllgfalpp lvpltrvppv rvlrrewgda srtawaayav
      421 gvllfaglli vaagnlklgl ivaggfagal vgfaliarlv lfaaaravrn arvaagvgwr
      481 yalaslhrrg ttsalqital alglmcllli aitrndlvag wrqstppdap nqflidiqpd
      541 qrddvatyla ahgvrdavpa pmvrgrlvai ngkpvnpday psdearrlvd refnlsytte
      601 lpsdnrivag dwfgtaatpq isiedglakm lnvkpgdtlr fdvtgltvda pitsvrkldw
      661 gtfrvnffvl mpppvlkdfp avyltsfhlp asdaalldpl iarypnltai dvapilaqlq
      721 rmmlqvvgav qflfaftlaa gvlvlytala gsrdervrea allralgasr aqvnavqrae
      781 fvvvgalaga lasagaiavg wvlasrvfdf rlavdpwlvp agivagvaca gaagwlslhn
      841 vlrrpalqsl rda
//
LOCUS       WP_175919338             234 aa            linear   BCT 11-JAN-2025
DEFINITION  TerC family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175919338
VERSION     WP_175919338.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..234
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24474
     Region          12..191
                     /region_name="R_switched_YjbE"
                     /note="integral membrane protein, YjbE family; TIGR03717"
                     /db_xref="CDD:163429"
ORIGIN      
        1 mlefltslhw gavlqiviid illggdnavv ialacrdlpa nqrlrgvvwg tagaillrva
       61 litfavalld vpflkigggl lllwigvklm apaadahdhi kpadrlwdav ktiviadavm
      121 sldnviaiag aaeqadpshr ialvifglvv svpiivwgst lvlkmldrfp ivvtlgaall
      181 gwiagglivn dpvgdrwpvl dtppaiygas magalfvvaa gyalrrrrga sgar
//
LOCUS       WP_175918960             372 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia pyrrocinia].
ACCESSION   WP_175918960
VERSION     WP_175918960.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 372)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..372
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40551
     Region          1..371
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 maslsirdvy ktypngvpvl kgvdieiedg qflilvggsg cgkstllnmi agletvtsge
       61 icidgkvvnd lspkdrdiam vfqsyalyps mtvrenisfg lnirkvpkne qqqivdrvsq
      121 mlqiqhlldr kpgqlsggqr qrvamgrala rdpslflfde plsnldaklr iemraeikll
      181 hqrlgttivy vthdqieamt lgdriavmkd gvvqqfgapq eiydspanlf vagfigappm
      241 nfingklveq gsgialeidt glarsalklp fdvkrmnghv grevilglrp eritdarnah
      301 ngeasslqpi dvrvdvtept gpdthvfaqv ngkrivsrvh paanpqpgqt qsllfdvska
      361 vlfdpaseer ia
//
LOCUS       WP_175919401             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175919401
VERSION     WP_175919401.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33655
     Region          15..74
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          103..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(113,117,156,170,172,231,248,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(114..115,119..120,122..123,126,130,132..138,199,
                     225..229,236..237,240)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 maldpipapd kpldlldval fvraallanv taagrefgvs aavasariaq lerqlgarll
       61 hrttrrislt qdgevfmara dallsaadaa rasvgrgrse pygrlkvsms ssfgrqhvap
      121 vipaflrryp svsldlrlsd eivdlvddgy dvairlgalk dstlvarkla vnrrvlccsp
      181 aylaergtpr hpadltqhec vilgdqrdws fatpqgpltv rvggrlvasn geairealvd
      241 gfgiaikstw dvgpllasga lvtvlddypf addvaiwavy psrahvplkt lafiaflaeh
      301 fgdppywdra dgr
//
LOCUS       WP_175919496             358 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: porin [Burkholderia].
ACCESSION   WP_175919496
VERSION     WP_175919496.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..358
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=38294
     Region          27..358
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkafarrasr tsvkliaaaa cvaatapvya qssvslygqv dewvgatkfp ggdrawnvsg
       61 ggmstsywgl hgaedlgngy kaiftlesff raqngqfgrf qgdtffarna yvgisspygt
      121 vtagrltthl flstilfnpf ydsytfspmv yhvflglgtf ptypsdqgav gdsgwnnavs
      181 ytspsfggln fgamyalgnq agdnrskkws aqfnyangpf aatamyqyvn fnngpqdlsa
      241 lvtgmksqgi alvgatydlk lvklfgqymy tkndqvagsw hvntaqggvs vplgvgnama
      301 syaysrdagg ldqtrqtwav gydyplskrt dvyaaymndh isglstgntf gagirakf
//
LOCUS       WP_175919408             393 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase [Burkholderia pyrrocinia].
ACCESSION   WP_175919408
VERSION     WP_175919408.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 393)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..393
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40351
     Region          1..393
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mtdvvivsaa rtavgkfggs lakiaapelg atviravler agvkpeqvse vimgqvltag
       61 sgqnparqsl ikaglptavp gmtinkvcgs glkavmlaan aivagdaeiv iaggqenmsa
      121 sphvlpgsrd gfrmgdaklv dtmivdglwd vynqyhmgit aenvakeygi trdeqdafaa
      181 lsqnkaeaaq kagrfndeiv pvsipqrkge plqfatdefv rhgvtaesla glkpafskdg
      241 tvtaanasgl ndgaaavlvm saqkaaalgl tplarikays nagvdpsvmg mgpvpasrrc
      301 leragwtpgd ldlmeineaf aaqalavhkq mgwdtskvnv nggaiaighp igasgcrilv
      361 tllhemvkrd akrglaslci gggmgvalav erp
//
LOCUS       WP_175919506             384 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia pyrrocinia].
ACCESSION   WP_175919506
VERSION     WP_175919506.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..384
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41821
     Region          23..384
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mqsipssaaa rqtqpaaaar tqndafvrie nvvkkfgdst avdnvnltia knelfallgs
       61 sgcgkstllr mlagletats gkifvdgedl aslppyrrpv nmmfqsyalf phmtvesnva
      121 fglkqegtpk neikervada lalvqmskya krkphqlsgg qqqrvalars lvkrpkllll
      181 depmsaldkk irqktqlelv niiekvdvtc vmvthdqeea mtmasrlavm segkivqigs
      241 pgevyefpns rfsaefigst nlfegcvved epdhifvesd dlearmyvsh gvtgplgmpv
      301 gisvrpervh vsrdkpgskh nwargvvtdi aymgayslyh vrlpsgktvv snlssshlmt
      361 dsapawnddv fvswspasgv vltq
//
LOCUS       WP_175919559             279 aa            linear   BCT 11-JAN-2025
DEFINITION  polyphosphate kinase 2 family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175919559
VERSION     WP_175919559.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Motomura,K., Hirota,R., Okada,M., Ikeda,T., Ishida,T. and Kuroda,A.
  TITLE     A new subfamily of polyphosphate kinase 2 (class III PPK2)
            catalyzes both nucleoside monophosphate phosphorylation and
            nucleoside diphosphate phosphorylation
  JOURNAL   Appl Environ Microbiol 80 (8), 2602-2608 (2014)
   PUBMED   24532069
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Sureka,K., Sanyal,S., Basu,J. and Kundu,M.
  TITLE     Polyphosphate kinase 2: a modulator of nucleoside diphosphate
            kinase activity in mycobacteria
  JOURNAL   Mol Microbiol 74 (5), 1187-1197 (2009)
   PUBMED   19843229
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Nocek,B., Kochinyan,S., Proudfoot,M., Brown,G., Evdokimova,E.,
            Osipiuk,J., Edwards,A.M., Savchenko,A., Joachimiak,A. and
            Yakunin,A.F.
  TITLE     Polyphosphate-dependent synthesis of ATP and ADP by the family-2
            polyphosphate kinases in bacteria
  JOURNAL   Proc Natl Acad Sci U S A 105 (46), 17730-17735 (2008)
   PUBMED   19001261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..279
                     /product="polyphosphate kinase 2 family protein"
                     /EC_number="2.7.4.-"
                     /GO_function="GO:0008976 - polyphosphate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016776 - phosphotransferase activity,
                     phosphate group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006797 - polyphosphate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31761
     Region          7..277
                     /region_name="PPK2_rel_1"
                     /note="polyphosphate:nucleotide phosphotransferase, PPK2
                     family; TIGR03709"
                     /db_xref="CDD:274737"
ORIGIN      
        1 makqpslddf rvptstreke aaafkldafd paakpfssgs keadrerlsa vsteldvqqe
       61 rlhtqqkkrv llvlqgmdts gkdgtvravf revdplglrv vsfkaptpie avhdflwrvh
      121 aqvpgagela ifnrshyedv lvprvldtid skecerryrq irdfetmlve ngttivkcfl
      181 hiskdeqrar lqariddptk hwkfdisdld arkhwdayqs ayrdalaats aehapwyvip
      241 adskthrnvm iaelllrtmt dmklefpppk pelegvkir
//
LOCUS       WP_175919729             249 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175919729
VERSION     WP_175919729.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..249
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27240
     Region          3..241
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mplvetrgle knfgthhvlk gidfsvergq vvsiigrsgs gkstllrtln glesidagti
       61 aidgervdar hadlralrlk vgmvfqqynl fphlsagqnv mlaqsvvkks hrqqaraiae
      121 lmlervglgd kfdafpeqls ggqqqrvaia ralamkpsvl lcdeitsald pelvgevlgv
      181 veqlarddmt limvthemnf aravsdkvvf mhqgrvwesg tpeeifvrpg tvelkrflgg
      241 lqktaefvn
//
LOCUS       WP_175919720             261 aa            linear   BCT 11-JAN-2025
DEFINITION  peptidylprolyl isomerase [Burkholderia pyrrocinia].
ACCESSION   WP_175919720
VERSION     WP_175919720.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..261
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=27994
     Region          100..247
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mndvlsdapv alsingvaid ddaiaaeaah hgdapdplda arrvlavrel lrqravslal
       61 ldehapldda avdallerel thvpepdrad ceryyaqhpa rfrrndivya shvlfavtdr
      121 vplaplrqra esaladvvaa pdtfeavara ssncpsaevg gslgqllrgd tvpefeaalf
      181 dteglgvlpk lvntrfgfhi vrierrvpgd avpfdeaaaq iaaylservr qramrqyvai
      241 lagsarvegv efdgangplv q
//
LOCUS       WP_175919752             281 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia pyrrocinia].
ACCESSION   WP_175919752
VERSION     WP_175919752.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19425591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..281
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30234
     Region          130..233
                     /region_name="N-Acyltransferase superfamily: Various
                     enyzmes that characteristicly catalyze the transfer of an
                     acyl group to a substrate"
                     /note="NAT (N-Acyltransferase) is a large superfamily of
                     enzymes that mostly catalyze the transfer of an acyl group
                     to a substrate and are implicated in a variety of
                     functions, from bacterial antibiotic resistance to
                     circadian rhythms in mammals. Members...; cl17182"
                     /db_xref="CDD:473072"
     Region          188..265
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mnrirqnlap qiatlldgmi kknayfprri ggtmqahehp dhavvdsgla tdtfnlvisk
       61 aagqpqaaat asiaqrfnda glpaawwtcr eladpafpqv lrehgflede tsvgmlagld
      121 llppvdypag fgvrqisape dvarfgalig alfdppdayv dafyrnvaal aidaaeplkl
      181 fvgeidgeav staavyldgd tahifdists aavrkrgfas atthfvltha rerlgakraa
      241 lqaspdglnv ylrlgfepvc eflvysnrav iqershdqhr a
//
LOCUS       WP_175919793            1000 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175919793
VERSION     WP_175919793.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1000)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 1000)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1000
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..1000
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=107222
     Region          17..771
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mpsshqhgtr aartdgssra nllrftfvse aydattfdvv dmsgrdaisq pyrfeltlvs
       61 kqpqidfakm lsraatltil ppygeagttr ysgvlaefeq lkdirgftvy ratlvprlwq
      121 lslykvtdvy lneqtipdiv kqvlrtasfg srdyrlrcgs gyrkrsfvcq ydeshldfvs
      181 rwmekeglyy yfehdgkret laivddrrhq pgpaadlalr ylpvaefdtg aesdrvqafa
      241 cratplprev vlrdfnhrka elslevrehv srdgigervs sdehfhtkde grryaklrae
      301 alvcdgrrfa geataaglra grfialeghy radfdgrylv taithrgsqa rllfpdldkp
      361 fgatpdvpvy rtefdalpag vqyrpprttp kpraagvvsa ivdgegggkl aeldehgqyk
      421 vrfpfahtah pankgsarir matpyagsdr gmhlplakgt evkiafeggd pdrpviigav
      481 pnsshrsvvt rrnpaahril tehnqlymkd gsgaatwlha pnnhiglgsv gpgeglallt
      541 sgnrfdfslg naysfsgglk csvsiggntd vyvgvrnsld vsanflttlq gnlrwmlpgs
      601 rtfeindsas tllqtlhkqs atgairlsag qdasalvqkq ldklkgavrk fmivsglana
      661 gsaaaaagli kgggavadlp wsgfgvsaaq fagvtaasta lmatsrtmla nvaklqealp
      721 lvadlslskh gialaaknlt hatrmsltvd gltwstdaka pgaagvamsa gngrwgvesa
      781 khahvhahdt llfavaadpt tklalkdlik qrsdldaclk eiadleadis enevlsthqn
      841 afgvsalvpk psspadavaa vaikakeakl falkakrkav glkidklqen lakqvknqsa
      901 armsasesef sfkgnrlvat aegvtlahaq gkakldvcda kigidagkss leldkdkiaa
      961 gcgsaslklg sdgtidvrat nvklngsasl kldsqliqlg
//
LOCUS       WP_175919877             342 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia pyrrocinia].
ACCESSION   WP_175919877
VERSION     WP_175919877.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..342
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37496
     Region          69..298
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 makdtskdkk ptgnlhlaag llrglaqena aletrlpepp aapnvvdaap avppaaaasa
       61 gisdlgapqk vlvkdcipnp fnprvfyses slhelaltlk regqiepikv trlpefpgkl
      121 vvidgqrrlr atsingdeti natfrtdhtp eqlytiayra nhdherqtif ddavawkrll
      181 dekvfpdqnt laekigkdka sisktlslna lpntllerma sandvvglqa ayflklifer
      241 lgeptadrll tavidrkksv rdlenflraq sddnkkagrt rysvrhdfal esraigqlkt
      301 ypdgrldlql kgvdtshqea ladklktvid ayvaelaavt qk
//
LOCUS       WP_175919878             375 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia pyrrocinia].
ACCESSION   WP_175919878
VERSION     WP_175919878.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..375
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42053
     Region          87..327
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 masplvlihr ilgfaaarrg ralsggspqh ngerfsnvap rpvegigktf giawtmlfnk
       61 prntvpagal pvdwltraql daapdrslyr lghstlllkl rgefwltdpv faeraspfrs
      121 vgpkrfhapp ialedlpplr gvilshdhyd hldrdtvlal aattdvfvtt lgvgdrlidw
      181 gidatkirql dwwqsvnvag ltltatpaqh fsgrslfdgn stlwaswviv dddlrvffsg
      241 dtgyfdgfrt igerlgpfdv tlietgayda qwpyvhmqpe etvqahidlr grwlipihng
      301 tfdlamhrwh epfervtals ivrgielstp rmgerldlde phrgerwwrt vdehakapat
      361 tkprrrqfca sqatk
//
LOCUS       WP_175919891             215 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Burkholderia].
ACCESSION   WP_175919891
VERSION     WP_175919891.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..215
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22258
     Region          6..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mhtsgslygf lviggmlavt pgpnmvyvms rsiaqgraag lislagvmig ylfymfgaaf
       61 gittlfmsvp yagsvlgavg aayllylawq avrpggrspf evralpneqp lrllamgatt
      121 svlnpklaml fvsllpqfid yrqgsvfgqs lflgslliaa faaanglvai cssgiakfln
      181 grpalllaqr wamglilggl gvqmvvdask magva
//
LOCUS       WP_175919981             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175919981
VERSION     WP_175919981.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33944
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,222,239,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     216..220,227..228,231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mldlndlalf vqvvragsfs eaarrlrmpa ntlsrridqf eaqlgtrllh rstrklapst
       61 egqalferya paldrlfeie rlhadgqaps gtvrvtamag lfeffrlewl aefyarypqi
      121 sidfllddtp sdligeridl alrmgietgg sfrvrriapg tmilaaspay lerraaprtp
      181 rdladhdclt vssrqgrsmw rlqgprgtqe isidsrfsvn dmrvvvqaci aglgiallpq
      241 llaepaieqg klvrvlpsyr rsstglglql vytsrpplpp avtvfaefll eklgngmpgq
      301 pkgdadr
//
LOCUS       WP_175919986             346 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia pyrrocinia].
ACCESSION   WP_175919986
VERSION     WP_175919986.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..346
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34811
     Region          11..301
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mmrvrtlfrh plawpvltla llfaldvahr pgflsialld ghlfgapidi lnraaplviv
       61 slgmtlviat rgidisvgai vaiagaaaai vleaepsrvg talaaalgvg llagawngll
      121 vafvgmqpii atlilmvagr gvaqlltggq iipigapgyl algggylatv pcavwiavat
      181 iaatallvnr talglfirai gvnpvatrlv glrsgavvfg vylcsgvmsa vagilassnv
      241 rsadgnnagl lleldailav tlggtsllgg rfslagsvlg aliiqtltyt tysigvppea
      301 tlvvkavvvi vvtliqsdaa ralvarhasr llpsarsrtt sgatpr
//
LOCUS       WP_175920010             300 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Burkholderia].
ACCESSION   WP_175920010
VERSION     WP_175920010.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..300
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32153
     Region          16..148
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
     Region          166..278
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 mkqehvmnds rsttalryrr ftvadlpaah alstalrwpf rledwqfsad tsvafaaeen
       61 cavigtamcw kfgadrasig hvivssahqg rgigralmet lleelgprit flhatpagqp
      121 lyeklgfdvc gsldqfqgnv srpaavvlpd garlragtpa dlrrlvelda casglerdal
      181 lsalltrges vvlerdgeia gfsvlrrfgr gyligpvvap rstgdtcara liahwlggle
      241 nefvridvps gtslpdwldm qglkrvdtcs kmvrnapaaa cggaldpayg lyglvsqaml
//
LOCUS       WP_175920111             536 aa            linear   BCT 11-JAN-2025
DEFINITION  GspE/PulE family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175920111
VERSION     WP_175920111.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..536
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=58189
     Region          <115..514
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mshaaqrpda ppvraalpas gdaapprgpr avseagdfaa sveerkfvcl lddgrlliad
       61 ghemnpfvls yrarldrmgr pyrptpatlm qvreaylqna agggerldht vmqvlakeli
      121 gracrerasd ihirvrrfst evyfrihnel mrvnehtreh gerllatlyg amttvsdnsy
      181 rpserqdasi gdrdklpddl ygvriattpt negslmvlrl lyndagdatd laalgfapeh
      241 vaafralraq phgmniisgp tgsgksttlq rmlaaqides rgslhvitve dpieypidga
      301 vqtpvanapt edaralafaa aitnamrldp dtimigevrd rasgqtalra smtghqvwtt
      361 vhansalaia drlidlglha rmvtdhtvis glisqrlvkl lcphcklrlv dhpdriepgl
      421 farlrlalds rmhdvciagd gcehcrtvgt igrtvvaevi lpdarlfeyl rdgdkvgale
      481 ywtgtrggmt vgehalrkva tglvdprgve rvvgtlapva gearqqlslv gfsygt
//
LOCUS       WP_175920122             233 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: pentapeptide repeat-containing protein
            [Burkholderia].
ACCESSION   WP_175920122
VERSION     WP_175920122.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..233
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=25331
     Region          38..224
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mdrlmtrgvs itgrtldrae llllvegspt plhledcdle gadlsrldlr garfercala
       61 easfvgstla qtswircrgr qasfassdle davfqscdln ntswrrsklg sarfnecrlt
      121 gadfeecksl glefentllv gaslrrfsfr ktrlaaldfs dadlagadfr davfeggslr
      181 nahlndvkfe gadlrdvdls gtpkllasgv lrgatvsydq aamlienlgi rva
//
LOCUS       WP_175920128             225 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175920128
VERSION     WP_175920128.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..225
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24887
     Region          1..206
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mkiisgplsm fgakveiaah ekgidfelvm apfsqlrgyd pkhpdvlrin pkrqvpvlmd
       61 gtleifdstq ifeyledlkp dpalwpahpa araiarqleh csdeiyfphv irlmgleatp
      121 ddpaaqaara easeyyrrme rvlvdrefla gaysyadiaf ymaqlfgark gapmtaetpg
      181 llawrarmta rpavrkvaga magylasige avpdflrgld qvplr
//
LOCUS       WP_175920138             319 aa            linear   BCT 11-JAN-2025
DEFINITION  ketopantoate reductase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175920138
VERSION     WP_175920138.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..319
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32983
     Region          1..307
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkiailgaga lgcaigaalt eaghetwlln rsmphveamc rdglrvddda gsrrvmvrat
       61 traaeagtad lvvvlvksfh tesamrgaha ligpdtlvls lqnglghedv ladlvgrerv
      121 lagktyvggv mrgpgqiqsg vagkttyvge ldgrltprvl aiaeafnaag ldtivsdniv
      181 gtmwdkllvn vatgaltgvt gltygqlyde pllkatavaa vaeamavara agvklsmtds
      241 eqawtlaaag lspafktsml qslekgsvte idfingsvvr lgqrhgvptp vnatlvacik
      301 gieramadrq hfntcmgpa
//
LOCUS       WP_175920186             186 aa            linear   BCT 11-JAN-2025
DEFINITION  group III truncated hemoglobin [Burkholderia pyrrocinia].
ACCESSION   WP_175920186
VERSION     WP_175920186.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Keppner,A., Maric,D., Correia,M., Koay,T.W., Orlando,I.M.C.,
            Vinogradov,S.N. and Hoogewijs,D.
  TITLE     Lessons from the post-genomic era: Globin diversity beyond oxygen
            binding and transport
  JOURNAL   Redox Biol 37, 101687 (2020)
   PUBMED   32863222
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Bustamante,J.P., Radusky,L., Boechi,L., Estrin,D.A., Ten Have,A.
            and Marti,M.A.
  TITLE     Evolutionary and Functional Relationships in the Truncated
            Hemoglobin Family
  JOURNAL   PLoS Comput Biol 12 (1), e1004701 (2016)
   PUBMED   26788940
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Wajcman,H., Kiger,L. and Marden,M.C.
  TITLE     Structure and function evolution in the superfamily of globins
  JOURNAL   C R Biol 332 (2-3), 273-282 (2009)
   PUBMED   19281958
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Vinogradov,S.N., Hoogewijs,D., Bailly,X., Arredondo-Peter,R.,
            Guertin,M., Gough,J., Dewilde,S., Moens,L. and Vanfleteren,J.R.
  TITLE     Three globin lineages belonging to two structural classes in
            genomes from the three kingdoms of life
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11385-11389 (2005)
   PUBMED   16061809
REFERENCE   5  (residues 1 to 186)
  AUTHORS   Wittenberg,J.B., Bolognesi,M., Wittenberg,B.A. and Guertin,M.
  TITLE     Truncated hemoglobins: a new family of hemoglobins widely
            distributed in bacteria, unicellular eukaryotes, and plants
  JOURNAL   J Biol Chem 277 (2), 871-874 (2002)
   PUBMED   11696555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..186
                     /product="group III truncated hemoglobin"
                     /GO_function="GO:0005344 - oxygen carrier activity
                     [Evidence IEA]"
                     /GO_function="GO:0019825 - oxygen binding [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20626
     Region          21..130
                     /region_name="TrHb3_P"
                     /note="Truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 3 (P); cd08916"
                     /db_xref="CDD:381257"
     Site            order(33,46,49..50,57,60..61,64..65,75,77..79,82..83,86,
                     89,93..94,97,121,124..125,128)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381257"
ORIGIN      
        1 mtalpalpdt aparprdaep tednirdlvy afydrvradp llgpvfdakl agrwddhlpk
       61 mvtfwsslvl gtkgyrgnvq qahqpldgie pahfsrwlsl flktvearya ppaairfmep
      121 alriaqslql srfgwdsrip peqqalldai aprrrdagdd phalpsrarg epfptkiigr
      181 sadpda
//
LOCUS       WP_175920184             327 aa            linear   BCT 11-JAN-2025
DEFINITION  thiamine pyrophosphate-dependent dehydrogenase E1 component subunit
            alpha [Burkholderia pyrrocinia].
ACCESSION   WP_175920184
VERSION     WP_175920184.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Frank,R.A., Titman,C.M., Pratap,J.V., Luisi,B.F. and Perham,R.N.
  TITLE     A molecular switch and proton wire synchronize the active sites in
            thiamine enzymes
  JOURNAL   Science 306 (5697), 872-876 (2004)
   PUBMED   15514159
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Jordan,F.
  TITLE     Current mechanistic understanding of thiamin diphosphate-dependent
            enzymatic reactions
  JOURNAL   Nat Prod Rep 20 (2), 184-201 (2003)
   PUBMED   12735696
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Hawkins,C.F., Borges,A. and Perham,R.N.
  TITLE     A common structural motif in thiamin pyrophosphate-binding enzymes
  JOURNAL   FEBS Lett 255 (1), 77-82 (1989)
   PUBMED   2792374
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..327
                     /product="thiamine pyrophosphate-dependent dehydrogenase
                     E1 component subunit alpha"
                     /EC_number="1.2.4.-"
                     /GO_function="GO:0016624 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, disulfide as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=34645
     Region          6..327
                     /region_name="AcoA"
                     /note="TPP-dependent pyruvate or acetoin dehydrogenase
                     subunit alpha [Energy production and conversion]; COG1071"
                     /db_xref="CDD:440689"
ORIGIN      
        1 mtvstqlsrd klldayrlmr tirefeerlh vefatgeipg fvhlyageea savgtmlhlg
       61 ladyvatthr ghghciakgv dvhgmmaeiy gkktgvchgk ggsmhiadls mgmlgangiv
      121 gaggplvcga alaakhkksg gvgvcffgdg asnqgvifes mnlasvwrlp aifvaenngy
      181 aeatssswsv atdniadran gfgmpgvivd gfdffavhea lgeaverarn gggptlvevk
      241 ftryfghfeg daqtyrapge vqklrdekdc lkhfetrvvr aealtiadlr avdaqvnali
      301 ddavaqakaa plpdatdllt dvyvsyp
//
LOCUS       WP_175920229             256 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175920229
VERSION     WP_175920229.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..256
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28617
     Region          10..245
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mtqpnvvpls aaplyvqikd tlrarildgt yaphsrmpse helctmfdvs ritvrqalgd
       61 lqkegllfkl hgkgtfvskp kafqnvtslq gfaeamssmg yeivnqlrsf rtvkadrhla
      121 tklhvpegap lveihrvrll nrepvsleqt wvpealgkrl agadlaardi flilendcgi
      181 plghadvsid ailaddeivd alrveesspv lrierlthda sgapidyeyl yfrgdafqyr
      241 lridrqkark parnpr
//
LOCUS       WP_175920198             281 aa            linear   BCT 11-JAN-2025
DEFINITION  NRDE family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175920198
VERSION     WP_175920198.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Bard,F., Casano,L., Mallabiabarrena,A., Wallace,E., Saito,K.,
            Kitayama,H., Guizzunti,G., Hu,Y., Wendler,F., Dasgupta,R.,
            Perrimon,N. and Malhotra,V.
  TITLE     Functional genomics reveals genes involved in protein secretion and
            Golgi organization
  JOURNAL   Nature 439 (7076), 604-607 (2006)
   PUBMED   16452979
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..281
                     /product="NRDE family protein"
                     /GO_process="GO:0007030 - Golgi organization [Evidence
                     IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=30847
     Region          1..252
                     /region_name="Tango2"
                     /note="Uncharacterized stress-responsive protein, TANGO2
                     (Transport and Golgi organisation 2) family, contains NRDE
                     motif [General function prediction only]; COG3332"
                     /db_xref="CDD:442561"
ORIGIN      
        1 mcliafdwqp daaagpvftl ianrdeffrr tsapltwwed vpgvlagrdl eaggtwlgit
       61 rdgrfaaltn yrapfdirag aptrgklvsd flrgpsvapl dylgqlaeha avyngfnllv
      121 gdwkrrelaw fcnrapeges avaapvaiap gvhalsnarl dtpwpkvvrk raelgtlltd
      181 nptpsldemi dlmrdphvad ddalphtgip iereralsaa fietpeygtr gttalrvtmk
      241 egvrltveik ercdddgshr tvrpgafera ftfdvdatrp r
//
LOCUS       WP_175920241             144 aa            linear   BCT 11-JAN-2025
DEFINITION  NfeD family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175920241
VERSION     WP_175920241.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Green,J.B., Lower,R.P. and Young,J.P.
  TITLE     The NfeD protein family and its conserved gene neighbours
            throughout prokaryotes: functional implications for stomatin-like
            proteins
  JOURNAL   J Mol Evol 69 (6), 657-667 (2009)
   PUBMED   20012272
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Kuwahara,Y., Ohno,A., Morii,T., Yokoyama,H., Matsui,I., Tochio,H.,
            Shirakawa,M. and Hiroaki,H.
  TITLE     The solution structure of the C-terminal domain of NfeD reveals a
            novel membrane-anchored OB-fold
  JOURNAL   Protein Sci 17 (11), 1915-1924 (2008)
   PUBMED   18687870
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..144
                     /product="NfeD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=15271
     Region          3..142
                     /region_name="YbbJ"
                     /note="Membrane protein implicated in regulation of
                     membrane protease activity [Posttranslational
                     modification, protein turnover, chaperones]; COG1585"
                     /db_xref="CDD:441193"
ORIGIN      
        1 mmsghlfwwv avgvlvvael ltgtfyllmi afgflaggll qlagfaphvq fgaaatvaiv
       61 amialrrsgl grkqkrdtst npdvnldiga tvtvdawrdg rarvqyrgad wdveladger
      121 ddahvyqvsa vrgsclvvva kpag
//
LOCUS       WP_175920282             262 aa            linear   BCT 11-JAN-2025
DEFINITION  TatD family hydrolase [Burkholderia pyrrocinia].
ACCESSION   WP_175920282
VERSION     WP_175920282.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..262
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28747
     Region          2..242
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mwidthchld aaefdtdrda varaaraagv srivipsigr dnftmvrela qrtpgaayal
       61 gihpmytpha rdedldrlrm eieaslddpr fvaigeigld yfvpgldedr qqffyqgqlk
      121 larefdlpvl chvrksqdrv laglrrfgvr rgiahafngs fqqaeaylaq glhlgfggnv
      181 tftralqirr latelpldai vvetdapdia pewayksrnt pdqvprigdv laelrgldas
      241 slglstsana laalprlals sa
//
LOCUS       WP_175920329             328 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Burkholderia].
ACCESSION   WP_175920329
VERSION     WP_175920329.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..328
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34466
     Region          7..319
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mndndhrpvr fgivgagsia rrfaqslahv pgatlagawa rradaaaafc etcggtpaas
       61 leallasdid avyiatlhds haqytlaala agkavlcekp atlnaaqldt vlraardagl
      121 lfmeamkppf fplyrqlrah lradpigeir lvragcasss vpgdhsvyrl draggalldi
      181 giyeaflavd wlgaaldvqt lgrvgatgvd mfaslnslha nggiaqlfcg ldvmgrgdal
      241 iaaagghvti hekwwnpara tiryadgriv eldapaeggg lnyetahfcd llragetesp
      301 imthehsrqm iamtdaarav lgvrysge
//
LOCUS       WP_175920408             227 aa            linear   BCT 11-JAN-2025
DEFINITION  SOS response-associated peptidase [Burkholderia pyrrocinia].
ACCESSION   WP_175920408
VERSION     WP_175920408.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..227
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=25939
     Region          <73..222
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mctnyvapge dpglselrid sfvdlyrwhp wkpeiyqdyd apiiasidgq fkpliagfgf
       61 wpralqkanv ekakeqgrkp piirstmnvr ddnlgksply apawragrrc lipaawiyep
      121 nwetgkhvry riglagwrpl cvagiwrtlq hpdggerhtm amitvnadeh aimkhmhrpg
      181 dekrsvvilr pedweewltt snlegaraml qlypademav epklqse
//
LOCUS       WP_175920336             318 aa            linear   BCT 11-JAN-2025
DEFINITION  toll/interleukin-1 receptor domain-containing protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175920336
VERSION     WP_175920336.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Nimma,S., Gu,W., Maruta,N., Li,Y., Pan,M., Saikot,F.K., Lim,B.Y.J.,
            McGuinness,H.Y., Zaoti,Z.F., Li,S., Desa,S., Manik,M.K.,
            Nanson,J.D. and Kobe,B.
  TITLE     Structural Evolution of TIR-Domain Signalosomes
  JOURNAL   Front Immunol 12, 784484 (2021)
   PUBMED   34868065
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Essuman,K., Summers,D.W., Sasaki,Y., Mao,X., Yim,A.K.Y.,
            DiAntonio,A. and Milbrandt,J.
  TITLE     TIR Domain Proteins Are an Ancient Family of NAD+-Consuming Enzymes
  JOURNAL   Curr Biol 28 (3), 421-430 (2018)
   PUBMED   29395922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10615567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..318
                     /product="toll/interleukin-1 receptor domain-containing
                     protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=34531
     Region          43..177
                     /region_name="TIR_2"
                     /note="TIR domain; pfam13676"
                     /db_xref="CDD:463954"
ORIGIN      
        1 mrfqnledgk qepaearafl rplyavrylr rgagmssfrk plifishihe egelakllkd
       61 aieiefggfv evfvssdhqg iaqgtgiaag thfveaveag lvnciaalyl ispksisrpw
      121 vnfelgavwc rgavqksngg nrimalpich seasrsslpa plnalnaing nvsadlefaf
      181 kslqrelgva gsalrtdfnq latkvidfeq rntvgdalkr viwglggddr rrvtqlidtc
      241 rqealrgtrt ltvkadrtlq ssvdsirsem dkalkgkmtl kivssgtafg sdgthhicdi
      301 elvfdpnlvv ahantils
//
LOCUS       WP_175920432             389 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia pyrrocinia].
ACCESSION   WP_175920432
VERSION     WP_175920432.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..389
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=41148
     Region          <256..389
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mktirrrrlg rvgrvmrrla tagyilafgt hamaqggsga talnctfsnp easswrmitp
       61 ltsttpvgai lyqrtvslmv sftygtapma helvsaahwt pgsviadgva qtnvngigfk
      121 wagvsddsse rtlqqgalpv vtaktdlgra geggndiqma rfrqylvldk pvsdlpqgkl
      181 vvknlpgnpt vaiyaidfpk gvasiggtvt vpeqtppnlc kqmkafvgvg nvcigsecei
      241 hvpnrceiqs nmivpvtlgn fainhfpsvn amskpvsfdi alsrcaaaak psisfrdkaa
      301 qpnpdktllq lsapagqtva rgfnivmtna ltgeriayge pgtatqypmr rtgdmavmpl
      361 raqyirtgvd aelkpgyagg gaefsftfp
//
LOCUS       WP_175920435             421 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia pyrrocinia].
ACCESSION   WP_175920435
VERSION     WP_175920435.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..421
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44612
     Region          164..353
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mvkpaatpdv fapgraqrvv ralvpaavlg alaalglaaa lpavsqlpga vdsgtavlpq
       61 rvlsdtpfpt aqhfvtselt rtigernehg erndrslqpg lfaplsahrn dmlgyaslfq
      121 lappenqhgm ragdieltls dtlnrldvpp evriqlgdlv tgkvalrasa qrgdyyrvay
      181 dtndgtprlt alelrvagrt fgaiwfrapg aehgayyald gspleaaaft mpvkwtriss
      241 ffgervhpls qamafhtgvd laapsgtpva aaadgvvsfv gtdpggygry vivdhadgys
      301 tyyahlsafa hglktgetvk qgqrlgsvgm tgaatgphlh fevrvandpv dplvtlanaq
      361 talsdmqlta frqeaaqwrf rlasvntapf afaqndgplw gdfatdkstl ravfnahysa
      421 s
//
LOCUS       WP_175920491             194 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Burkholderia pyrrocinia].
ACCESSION   WP_175920491
VERSION     WP_175920491.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..194
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22296
     Region          18..186
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mespptsrtm tdpdrditai vtrertrlvs firrrirdpd daedilqdvf hefvqayrlp
       61 apieqasawl fraarnrivd rfrkkkeqpl tdlfeaedea ngeyrldlal pahdagpeal
      121 yvrtlvlkal qdaldelpan qrevfvahel dgrsfkemaa qsgvalntll arkryavlhl
      181 rarlqriyde ldnt
//
LOCUS       WP_175920494             487 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175920494
VERSION     WP_175920494.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..487
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52011
     Region          58..467
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(68..69,72..73,76,110,160..161,163..165,168,188,
                     191..192,195,307,310..311,314..316,319,346,350,399..400,
                     404,408,424,427..428,431..432,435)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mnsqsldlgg tagepasarp paapagvgad aaalparrvt lgdfmddlpv galhrfvvwv
       61 igvglffdmy eiflvstigs alqneyglsr qstdfkllla safigmfvga mclgsladri
      121 grrkaflltl vwysvfslvg afsvnadmlv acrfltgigv gaiypvadsf lseilpkekr
      181 grlaawaytt syvavplvgf lalwlnpmhv agvagwriil aigslgavyv lfvqhrlpes
      241 prwllaqgrt adahaalrrf aegtgvcvpe qfaepaepqr plglgerial lrrepygary
      301 vmlaifhllq gfgyygfgtl agtvvksrgf dvtdstlfia lsfvgypigs llsipllnwi
      361 errtlvivsi lsiavfglcf aysgnivliv gfgllttcas nvfsnayhvy qaeifparvr
      421 staigstyal srivsgalpf vllpvlvsyg agamfgvisi algivavtlr vlgplttrrs
      481 qdeinpv
//
LOCUS       WP_175920511             111 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: c-type cytochrome [Burkholderia].
ACCESSION   WP_175920511
VERSION     WP_175920511.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 111)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 111)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 111)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..111
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11954
     Region          30..111
                     /region_name="CytC552"
                     /note="Cytochrome c551/c552 [Energy production and
                     conversion]; COG4654"
                     /db_xref="CDD:443692"
ORIGIN      
        1 mnvtrllaac mlaatagiaa aqtavpepta lvdaqhcmfc htsdmpflap sfhqiaeryr
       61 gvphaqeqle iklrhggrah wgdtpmpsaa erggplsrdd arqlvqwvls q
//
LOCUS       WP_175920563             349 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175920563
VERSION     WP_175920563.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..349
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=38843
     Region          13..331
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mtithtrrrn dgprkqiala lqgggmhgaf twgvldslle dsrleiegvs atsagamnaa
       61 vlayglqkgg edgarqalhd fwhavaqsae rynplrwvpw lkgthsfgld hsplyafadm
      121 mlrifspyqf npnnlnplre vlesqvdfda lrkhcpirly lcatnvetgk iriftgedvs
      181 adavlasacv ptlfqavaid geyywdggym gnpaiypliy ncatrdvviv hinplvrrgv
      241 piaaaeilnr iseisfnssl mremraisfv tdliqqgaik rgemkemlih siraddalca
      301 lsvsskynad wgflselhdy grreadtwla hhygnigqrs sidirrefl
//
LOCUS       WP_175920626             203 aa            linear   BCT 11-JAN-2025
DEFINITION  cysteine hydrolase family protein [Burkholderia latens].
ACCESSION   WP_175920626
VERSION     WP_175920626.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..203
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21145
     Region          24..192
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mqhptirtla gasaptsida artallaidf qneyfsgrlp ipegpralan aqrviafadr
       61 agipvfhvqh vgaadgplfa dssdgfrfhp dlqpaphhav vkktsvsvfp ttdldarlka
      121 agidtlivtg lmthacvaga ardavplgya vivvddacat rdldvadgst vphrelhrat
      181 laalsdtfgd vltteqvlal dva
//
LOCUS       WP_175920684             502 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: class I adenylate-forming enzyme family protein
            [Burkholderia].
ACCESSION   WP_175920684
VERSION     WP_175920684.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..502
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=53959
     Region          3..498
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mnlvaaldra aratpdkpfl vsesatitya aarershraa avlsalgiaa gdrvaamcfn
       61 tpafvdlmfg vwrlgatfvp vnhklqapev dyvlehsrsk allfdvalap vverivhpar
      121 qlvtegeldg vpcfdtmcat mdgvagiepa dgdiaqilyt sgttgrpkgc vhshrtvtla
      181 amsaalaigi grnertlmam piwhssplnn wfggtlyagg tvvllreyhp lrflravere
      241 rvtlyfgapv symlpldtid gfaafdlssv rawlygggpi gaaqaerlar ayrsdaffhv
      301 ygmtetgpag ttlypdeqia kagsigrhgg pgvdlrvvrm dgidaqpget geiwlktdsm
      361 mlgylddaaa traafapggw yrtgdvarid qdgylfivdr lkdmivtgge nvyskevedv
      421 lgahpdiaea avvgvphpdw getvvahvvm ragsapdada lrafcgerla aykiprefaf
      481 aqalprtptg klqkfllrvr ke
//
LOCUS       WP_175920761             183 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175920761
VERSION     WP_175920761.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..183
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19268
     Region          1..148
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 meaaiqlles ggleklttna vaakagvsig tlyqyfgskh alldalvtre lsamsakvva
       61 slrtgapasa gdrirqivra vnasyggrnr vhrlliehas atqsagrlmp lfaqlidlwt
      121 negiaahgdg rrrltradaf vmvhaiagvl rtlaashdap paeevedalv rmivgfvsss
      181 esr
//
LOCUS       WP_175920711             142 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175920711
VERSION     WP_175920711.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..142
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15427
     Region          7..>128
                     /region_name="COG3576"
                     /note="Predicted flavin-nucleotide-binding protein,
                     pyridoxine 5'-phosphate oxidase superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442796"
ORIGIN      
        1 msdpapltdd avafireqvf livatadaag nsdcsyrgrq pradgsfepl vdipdrrtlv
       61 lpdfagnnlf ntignllvnp aiallfvdfv rqttwlvqgr atidedaesr ahlwpdarry
      121 vvievehaqa radaalsplv la
//
LOCUS       WP_175920768             778 aa            linear   BCT 11-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Burkholderia pyrrocinia].
ACCESSION   WP_175920768
VERSION     WP_175920768.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 778)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18771781
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..778
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=84978
     Region          20..134
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Site            order(29..30,32,56,59..60,63..64,66..67,90,93..94,97..98,
                     101)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          54..84
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          107..756
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          213..241
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(252,255..256,258,282,285..286,289..290,292..293,316,
                     319..320,323..324,327)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          252..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          280..310
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          315..343
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mpssdssiaa ptsdqqfehd ialvlqsaie rhhagaldda kalyeailga lpehgdanyn
       61 lavlkvdtgd pgsavphfei algtvphngn ywvgyinaly rsgqtpaawi avemaqqrgv
      121 hgpaldglia qmaaptavfp tapaapapat ldislaalpa ndatqatpta hrpilhrvps
      181 rklqahtalf nkgrnveaia larelvaayp adaaswralt vslyrdrryr etidaayqli
      241 erephdlmtr tllaealrta drateaepqc rhiiamqpdn aeghrilglv lhglrrhdea
      301 iaacrravel apqvasmhsa lgfllldqga sleaipwfrr aieinpmdsi thssllfcli
      361 hddavdeetl lrehrafakl hearvkpprh antraphrkl rvgfvsgdlm nhavasylap
      421 vvhhlsddpg lslhfysnhl fedhiteklr ekaetwtdvt vlddaalvdt irrdridili
      481 dlsghtgrnr ltafahkpap vqaswigyag ttgltaldyy ltdrfvappg lldsqfveki
      541 arlpavapfs ppphcppina lpalhaghvt ygsfnrlnkl rpdvvalwak ilradpharm
      601 tigaigqehd qhtlvdwfga egisaerltf rpraqtavyl qqhhqvdicl dtfpyagstt
      661 tlnalwmgvp tvtiagrslp srgsacwlsh lgleqfiahd andfvertle lskrldelnv
      721 lrtsmrnrcl asaafqpqtv aaglssalrt mwtrwcsgep pvsfdatatt pgvvtdpa
//
LOCUS       WP_175920774             197 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia latens].
ACCESSION   WP_175920774
VERSION     WP_175920774.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..197
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21373
     Region          7..163
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          104..>163
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 msdlvcalph hidelvelic ttgpyrtaaa nnlerldyra flarflvapr lgssyvllda
       61 acggrvigal vcaplkdlvs tdwsrcsrrs idglhapfkh lqipesfyid tlavvsdmqg
      121 kgigkrlfre aeamaraagy qddlslavsa satgaigfyh amglivtdcv rmklpafppf
      181 llmqsasrfl syeqvcn
//
LOCUS       WP_175920780             398 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia latens].
ACCESSION   WP_175920780
VERSION     WP_175920780.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..398
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41471
     Region          4..>179
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mtllsslald gvaavtalgr elrawkgtrt ralfnaqavl svalavllar mlhlehtwwa
       61 aisgfailrd nvrgcverga hrmlgtlaga afgmlagpwi adrpwlvvpv laavagctvl
      121 randsaasya wvlggvtamm viaaarvlgs arttldfals rvtevavgtl acvlvatvvt
      181 rivarhrrvs thalstprrt digacghddt ivrastravr vrlgicaala talmaalgcv
      241 vhvpgsaqam vtsiallilp adalvgrtpa airermmqrl igcvlagalg vtllplinga
      301 alpcmlalsl gvwagchvqt gaegasyvgr qfavafvmvf vqdhhwsadp hpalmrfcgi
      361 ltgvvvlslv mlatsavwpr ridrtrggsa dagesalr
//
LOCUS       WP_175920619             442 aa            linear   BCT 11-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Burkholderia latens].
ACCESSION   WP_175920619
VERSION     WP_175920619.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..442
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=47195
     Region          3..408
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mnkrmsaavw illamaagif igymiytrfp dkqsateiag yislvsdvfl rlikmvigpl
       61 vfstlvvgia hmgdassvgr vfvkafgwfv taslvslllg llmanllhpg enlglplpdi
      121 gasanlatsk ftlkdfvshm vpksiaeama nneilqivvf smffgvalaa lgergkilva
      181 aidqlahvml kitgyvmkla plavlaamas tvainglsil lkfavfmgdf yvslfllwtt
      241 lvvagllflg rrvfkllali keafmlsfat asseaaypki ldaldrfgvk rkissfvmpm
      301 gysfnldgsm myctfaslfi aqaynihlsl gtqitmllvl mltskgmagv praslvviaa
      361 tlhqfnipea glllilgvdt fldmgrsatn avgnsiasav vakwegelms esearahaah
      421 ldaelerqng dpaygagrat sv
//
LOCUS       WP_175920822             120 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia pyrrocinia].
ACCESSION   WP_175920822
VERSION     WP_175920822.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 120)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 120)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..120
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12424
     Region          32..118
                     /region_name="CytC552"
                     /note="Cytochrome c551/c552 [Energy production and
                     conversion]; COG4654"
                     /db_xref="CDD:443692"
ORIGIN      
        1 mkivqmkqmk qwmvqgaaav alvagtlgaa qadvgdglkv argnacmgch avdrklvgps
       61 fkdiaaryks dpqavaklqk kvkeggsgvw gaipmpahpr msdadvrsvv ewvlagapsk
//
LOCUS       WP_175920782             168 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia latens].
ACCESSION   WP_175920782
VERSION     WP_175920782.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..168
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17897
     Region          1..140
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mtrpilvavs artaehvfah aaaasrerga simllnvidt ascfigaadf dcglvmevmq
       61 aqsrqivsaa erwfvsrrca vdthvlqlpa yghtvghaia afadaieadv vllgarqhdg
      121 wqwfrddiaa dvvrntraav qrvpgpisad emrggarprp aaratgra
//
LOCUS       WP_175920832             384 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia].
ACCESSION   WP_175920832
VERSION     WP_175920832.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..384
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41194
     Region          18..184
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          128..382
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 myvlkliarn alrhrlrtll tvlgltiavl afgllhtvvd awyagaaaas sgrlvtrnai
       61 slvfplpvsy enrirgidgv tavvrsnwfg giyrdpknff asfavsenyl dlypefivpa
      121 qqradydrdr rgclvgrqla tqfgfkvgdv iplkgtiypg twdfvvrgil dgrddstitr
      181 qlvfhwdyln etvrqrtpkq adqvgvfvlg vanpddgati arnvdavfkn slaetltete
      241 qafqlgfvam snqiiaairl vsyvviliim avmanamams arertaeyat lkalgfgpgf
      301 lalivfgesv viavaggglg ilatppaasl fkqaaggifp vfkvsaetva lqaacsvavg
      361 iaaaivpawq aarvrvvegl raig
//
LOCUS       WP_175920848             174 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175920848
VERSION     WP_175920848.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..174
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19383
     Region          4..159
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 maqaeldaid rrilailqen grlsnqeiae rvnlspspcl rrirrleeig vitgyvalld
       61 pqklgldlla yvsvrlekrg glapvrsdet saragathae lfraavqtwp evvachamtg
      121 dmdyllrvqv edmahfsrfv qehllhhpsv idvktsfsle cfkettalpi rsvr
//
LOCUS       WP_175920896             441 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia latens].
ACCESSION   WP_175920896
VERSION     WP_175920896.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48588
     Region          17..404
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(31..32,35..36,39,71,121..122,124..126,129,149,
                     152..153,156,253,256..257,260..262,265,294,298,348..349,
                     353,357,373,376..377,380..381,384)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mqanpvider aivrkitwri ipfvfilyii syidranigy aalqmnhela ltseafgfas
       61 giffigyflf evpsnvllkk ygarvwiari litwgivsvg safvqnatql yvlrfllgva
      121 eagffpgiiv yltywfrake lattvalfta aipvsyiiga plstwvmdnt hwfdwsgwrw
      181 mlvlegapal lggilcflyl tdrpadakwl apaerdwlln elandqkarp hakhfgsvka
      241 mtnpkvlyls fiyfvyqcgs lgvgywmpqi ikgfsktlsh tqigliamlp yivatismvm
      301 wsrssdhrne rrlhsaiplg vaalallgag lttnpyvsit mislslagly afkspfwalp
      361 tlfltrstaa vsiavinsig nlggfvgpfa igyikgagks atpgllllaa llvtsflmty
      421 firineredd gatgavpnqs h
//
LOCUS       WP_175920874             405 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Burkholderia
            latens].
ACCESSION   WP_175920874
VERSION     WP_175920874.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..405
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43407
     Region          8..403
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(103..105,129,179,211,240,242..243,251)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(106,139,204,249..251,280,283)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            243
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mtaaaeslnr flaaarpsat ykvmdrvaar rasgatvisl sagepdfdtp ehvreagisa
       61 iraghtrytq vaglralrev iaakfqrend ldvdwrdtlv csggkqvifn alaatlnegd
      121 evvvpapywv sypeivqlcg aksvivpcga esgfkltada lqsaitprtr wlilnspsnp
      181 tgavysrpel qalaevllah pqvlvlsddi yehlifdgie fftlaqvepr lrdrvltmng
      241 vskayamtgw rigfgtgpgw ligameklqg qqtsgastis qhaalaaltg pqdfiqhsri
      301 afqrrrdlvv dqlnqargly ctvpqgafyv fascegligk ttragvhldg deavvnalld
      361 eagvatvhgs afglgpyiri ayalddksla ractaiqdfc ttlad
//
LOCUS       WP_175920938             252 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome c1 [Burkholderia pyrrocinia].
ACCESSION   WP_175920938
VERSION     WP_175920938.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 252)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..252
                     /product="cytochrome c1"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28237
     Region          18..252
                     /region_name="CYT1"
                     /note="Cytochrome c1 [Energy production and conversion];
                     COG2857"
                     /db_xref="CDD:442105"
ORIGIN      
        1 mkkllstlal igatacallv apgvraegnf pldrapdnte nlvslqhgaq lfvnyclnch
       61 sanlmrynrl tdlgispkei etnllfttdk vgntmsvamr pedaknwlgt sppdlsveer
      121 argrdwlyty lrsfyrddtr psgwnnavfe nvgmphvlwq lqgqriakfe dktdeetgek
      181 ahtlvgfqqv tpgtlsspdy daavadlvay mtwmsepaqh trkrlgvwvl vflgvltfla
      241 wrlnaaywkd ik
//
LOCUS       WP_175920995             224 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175920995
VERSION     WP_175920995.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..224
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25548
     Region          2..221
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 masekargqs vadrishqlr ehiisgklpp gtpliemdla aeydtsrnsl revlhqlgre
       61 glvtfvrhkg vvvrtlnrqd vrdlyvarrt lelhalntae laqpallekm qtairaaere
      121 ldkenwqavg thslrfhqhi valqksalld effktisaql rlvfaadpge krvqtpdwiq
      181 rdyqiydllt qnrrseavtt larylddser mlveaikrsh reaa
//
LOCUS       WP_175921022             322 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175921022
VERSION     WP_175921022.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..322
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35844
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,220,
                     222..225,232..233,236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdmlenmrlf vrvveagsft avakeidatt aqvsravsnl eahvqtrllh rttrhlglte
       61 sgeryferak silaeidyan aearnallrp tgkmrihamt glgqshvvss ivryqednpd
      121 vsvdltlaqr mpnlveegyd vsivtasqlp dsgyvaqtcg tscsvlvasr eylarhdtpk
      181 tpddlpnhvc lrldtpaspa sewrlergdg eetvyelqpa pfqvnvpdal cvavragrgi
      241 acvalytvld diregrlirv lpeyrlqtvs vyavyatrry ldakirtfld hlrttltpal
      301 endlreldrl aleqsparrq ra
//
LOCUS       WP_175921097             925 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175921097
VERSION     WP_175921097.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 925)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 925)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..925
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..925
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=99345
     Region          16..828
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mntaellraf asgvvdqnnr pirmnwgpaq ktleqvlalq yadvreglmt gieghltcvs
       61 aradlpirsf iglpvsvemt tdrgrlhtin givtdvrtgq sdgsltcyql tirdvlsvme
      121 rrtnsrlfrt kslpdilavl lqewrqrssa lagafefdls glqgerypar eltrqvnesd
      181 ahfirrllrr dgatvfvkag kageraigna ndtpvhtlvf addsmklpet vagtvryhrd
      241 aateerdsit lwatsrrlip gkivrptwdy ksgrmsqteq atiidqgdgg ndlghllada
      301 vidiphagns ssdldrigkd rmlahelrae svdgvsnvrd lavghwfala ehpqldtlpa
      361 eqrqfvvtsl hhrvrnnlpk elneraqslf aasrvlfnav ptdvsskpgd esdtryentf
      421 scvrrgvplt paydphvdlp pvhpmtavvv gpqgeevfcd emgrirvriq glnaddhaha
      481 qgagasgtps dsapvrvsca lagpsfgant lprvgmevli ghiggdpdrl vvmgvlangp
      541 nmpatfshtg alpgnrylsg tktkeikgqr ynqirfddtp gqissqlase haysqlnlgy
      601 ltqprdngqg aargegaelr sdahvairsg kamlisawer lrasdghlar deylqlmqec
      661 velfkslgdy agqhqgvapd tqphdalmtt vkgwpngeas gggessdasv aaigitapag
      721 ismatpktvt thaggnvdvv aqnhlqytsg qrinlqaghg vamfahsegv saianqgkvs
      781 lqsqnddtqi dsakniqmta gggklagmas eqvvfvtsgg aylklhggdi efgcpgsftv
      841 ksashtwagp asmsadfpkf dqgslgrvpk lvratdgqpv egmeaevrka sgelikgktd
      901 aqgklspvss dqfeqlavrf fksrt
//
LOCUS       WP_175921060             319 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175921060
VERSION     WP_175921060.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..319
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35312
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mngiraittf vraatlgslr gaavdqrisp qaashavmql ekelgvrlfh rttrklslte
       61 egqrlldnvk palemlssal ddarrstedv ggvlrvsapr alglpvlwph fdafqkrypn
      121 vhldvqlddq ftdlvadrsd vgfrgghpps ggsiarplvp iqlivcaspd yverngaprt
      181 idelaahrct gyrrattgkl aqwqfrigde lvyrdvpaai cvndtemetq avlsglgigq
      241 lgsfnaaphi rsgrlvpllt qhvseygmiy iyyrhrteqs qrvrtfidfm vermagnrdf
      301 fldpselrag rqsaqkprg
//
LOCUS       WP_175921102             459 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia latens].
ACCESSION   WP_175921102
VERSION     WP_175921102.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..459
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46092
     Region          22..447
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(29..30,33..34,37,69,119..120,122..124,127,148,
                     151..152,155,277,280..281,284..286,289,317,321,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mpdtgervah plkrrgvtll tlciavlvaq idtavvnlat raigayfhag vgalqwvvds
       61 ynltyavlll tgglladlyg rrrifmagta vftvasllca laptvsvlig aralagvgaa
      121 lllpaslaii rvvwrdsver gralgiwaac ngvamaigpt lggvlirhfg wrsiffvvvp
      181 lsiaamllam pavpessdpr grhfdggaqv tgalalgtla yaaivyresp vasaiaacva
      241 iasfvafvri errhgdaalv pldlfrlsaf rgaiaattgm tfgmygvlfl lpltwqsigr
      301 ldstgaglal lpmalvfvav spcsgrlsec vgtrattagg vaviasglav igasaaspgl
      361 lgaeiglalt glgmgvatgp lmtvavgavd aarsgtasal vnvarmtgat lgiavlgtlf
      421 avahsgtagl raamfagaav qlagaagsav svqrarqsa
//
LOCUS       WP_175921133             155 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Burkholderia latens].
ACCESSION   WP_175921133
VERSION     WP_175921133.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..155
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=16165
     Region          30..140
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 msethvsvdv aqharfsfev tfagtdlspv ltdeppplga grgpnpvrll aasvasclaa
       61 sllfalekqr vdpqpvaahi dvdmvqndag rvrvgamava lsvgkawadl aaatrlldrf
      121 daycvvtesm regipisvtv qdvngavldr ettgv
//
LOCUS       WP_175921134             268 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia pyrrocinia].
ACCESSION   WP_175921134
VERSION     WP_175921134.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..268
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=27831
     Region          9..247
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mrarpivavt adrilrgahp shtagekyla alvdgagala fvlpalgarq padaivaavd
       61 gllftgsysn vephhyggaa sapdtlhdpa rdatalplir aaidagvpvl aicrgmqeln
      121 vayggtlhqr lhattgfddh rerlsdpler qygpshvvql apggllqrva rgahdamvns
      181 lhdqgiarlg aglvveasap dglveavsvr garafalgvq whpewrfaeq plsrdifaaf
      241 gaacrahmth rihaaggatp spaasdvd
//
LOCUS       WP_175921158             958 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia latens].
ACCESSION   WP_175921158
VERSION     WP_175921158.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 958)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..958
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..958
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=104038
     Region          42..957
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mknhglsrrg flkasmlagv avyvapigsr afaalfeekl ltpvkwdsvt gipkfridgi
       61 akvtgskvfa rdvraadmph wpqqqshali lrvtradrvy egfdlsllgd elkpdrvvta
      121 ddlardgvaf pafygddmll pagktpaylg havailiyhd farfrfakna lkfrddviry
      181 gavtgplerd pwgtfryvrv ggktahdddv ysslkdapif psmmrkhlpv wpdgkehgkl
      241 deqgmflagq iaaeldhppa dwlvfdreys tqsvdtaale pdnancwyda aaqslhlvvp
      301 tqsplevaen aaamvakcrf pvkklfvhpc ytvgygskdh cnvpfyglvc alyadgrpvr
      361 fandryeqfq tslkrhafnm ryriavdrnt gllqsfkgdf eangggrsnf spsvamvgat
      421 aaqsiyyfpk sdlaavaias raidagsarg ygtlqsmaat emaideiaaq lnidpiefrl
      481 rnalrsgmkn tqgaipagal rvdevlerak qhplwtrraa rktefdaanp gkrygvgfac
      541 vqkdfgtgae asfakvefde ngnvslhhta aeigtgmsts qavavvkwlg rpatdvrvav
      601 tewpdlpiet sgdpylmsqa dqdrlsanpr wspgyaspss atnsayyfth streaaravf
      661 ryglwpaams iwtrglgggq aapytvried arwvdgklta dglepltfeq lakqahalgl
      721 ptgavvhvfn rwqwtdaefd vggvverlpi dglslrvgap rtgddgpipg taapagatal
      781 rgtlpptang yrvldrkrvf ipptsrnnaa vtyytavgtl velavheatg kvellahhsi
      841 mecgnqispq lvsgqlqggl amgighalhe ylplyedgpg ngtwnfnryq lpratdvavw
      901 sqtgdilppl setdppkgva evvmipvvga ivngiahaig hrftdlpvtp qkiqevla
//
LOCUS       WP_175921181             511 aa            linear   BCT 11-JAN-2025
DEFINITION  catalase [Burkholderia latens].
ACCESSION   WP_175921181
VERSION     WP_175921181.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..511
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56697
     Region          21..504
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 msntanrffq sviaaacval assshaaelt rdngspvgdn qnsqtagpng pvllqdshli
       61 eklqrfdrer ipervvharg tgafgefvps adisdlttak vftpgtktpv fvrfstvmgy
      121 rgspeqardp rgfavkfyte qgnwdlvgin lpiffirdai kfpdfvhank psavtgvqda
      181 nlafdffaha peatsmltrl ystegmpdsy rnmdgygvha fkfvnadgey tyvkfhwksa
      241 qgmhglrpkd ipgsigadwn lmtndlygal kagnapkwdl yiqvlkpsel dafdfnpldd
      301 tkvwtgvper kigtltlnrv pdnyfestee safapsrmvp giepsedrml qgrmfsyadt
      361 qmyrlganfn qlpinrprvp vtnnnqdgam nfgdrkgevn yepstqnela qnpryksvet
      421 plagatqqaa irktlnfrqa geyyrmlpaq erqdlvaals adlnhvtnea nkysmlsyfy
      481 kadadygtrl arathadlar vksladklae n
//
LOCUS       WP_175921194             221 aa            linear   BCT 11-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Burkholderia
            latens].
ACCESSION   WP_175921194
VERSION     WP_175921194.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..221
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=23007
     Region          17..>159
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mqrtsramph vyaatsrvla vslainllll vaeavaawsa hssglfadva haaidlaadt
       61 lilvacrlda rlpperrpty eplalaglga llvatgvqmi whaasrfdap pavqpdamtv
      121 aliaftltgk aalsrwmlck aretgsalle asgwhvrsda lsallaalat caawvglgrl
      181 ddvaavaigv vvirtgagfi rrgcaqwpal sawvnrstrg l
//
LOCUS       WP_175921217             400 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid aminotransferase [Burkholderia latens].
ACCESSION   WP_175921217
VERSION     WP_175921217.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Alexander,F.W., Sandmeier,E., Mehta,P.K. and Christen,P.
  TITLE     Evolutionary relationships among pyridoxal-5'-phosphate-dependent
            enzymes. Regio-specific alpha, beta and gamma families
  JOURNAL   Eur J Biochem 219 (3), 953-960 (1994)
   PUBMED   8112347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..400
                     /product="amino acid aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43438
     Region          1..396
                     /region_name="PRK09257"
                     /note="aromatic amino acid transaminase"
                     /db_xref="CDD:181731"
     Site            order(102..104,130,183,214,243,245..246,254)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(105,140,207,252..254,290,293)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            246
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mfehidaypg dpiltlnenf qkdprdrkvn lsigiyfdae gripvmdavr eaetalqrdl
       61 gpkpylpmig laayrdavqa lvfgadhpar aagriatvqt lggsgalkvg adflkryfpd
      121 aqvwlsdpsw enhrfifera gftvntypyy deatgglkfd amlaaidalp arsvvllhac
      181 chnptgvdld egqweklidv idargllpfv dmayqgfgag ldadafavre larrgvpalv
      241 ansfsknfsl ygervgglsv vcedaaaaer vlgqlagavr snysnpqtyg akvvatvlnt
      301 palrkqweee laamcrriar mrqsihdglr dhvggealar yvkqrgmfty tgltesqvda
      361 lrevhgvyil rsgrmcvagl ndsnvgivad aigkvlksgv
//
LOCUS       WP_175921199             766 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Burkholderia latens].
ACCESSION   WP_175921199
VERSION     WP_175921199.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..766
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=83880
     Region          170..765
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 msyvvavram ceftarrgdl dlrftpapta legiaghgav tskrgaryet eialtgtwgt
       61 ltvrgradgy dpvanrldei ktyrgsldam pgnhralhwa qakvyahlmc earglaeihv
      121 alvyfdivse retvltetls asalaaffae qcacfvgwae resahrtard aalraltfph
      181 gqfrsgqrel avsvyraard erclmaqapt gigktlgtif pllkacgege ldhvffltak
      241 tpgralalea attlgagtpa lplrvlelva rdkacehpdr achgescpla qgfydrlpaa
      301 rdaaigagll drgtvraaal ahdvcpyyla qelarwadmv igdynyyydg samlhtlaqq
      361 nqwrvgvlvd eahnlldrar kmysasldpf afaaareaap aalrkafdrl arawgtlnra
      421 qaeryaaypd ipgpivsavq nlvaaigehl tdaprandda llrfhfdaiq fgvladafds
      481 asifdatlhg epmprqagfd gvapagrrrr iqstlcvrnv ipagflapry eaaratvlfs
      541 gtlspfhfyr dtlglpadtg wldvdgpfra eqltvrvash vstrwrdrdr slepivdlia
      601 aqyaarpgny lgflssfdyl grvvalmqar hpdvpvwaqa pgmaeserda flarfdtggr
      661 gvgfavlgga fsegvdlvge rligafiatl glpqvndvne qmrramdarf gngydymyly
      721 pglqkvvqaa grvirtehde gvvhliddry rrrevrdllp rwwrig
//
LOCUS       WP_175921240             215 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia latens].
ACCESSION   WP_175921240
VERSION     WP_175921240.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..215
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22906
     Region          1..212
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msfrlylsfl aasavliyap gpvnlltmnh alragwrral pcvwggtlav llqlaltalc
       61 lnslvhlder altvlrwaga aylvwlgckq wlsrapagaa tasaetggpa addtdtgral
      121 fwrgvatsgl npktllffps ffpqfivada dwslnaqfll laatfavlfa ggvasmalfs
      181 hrlsrvlqrp armramnrvt ggllvgmgai magwn
//
LOCUS       WP_175921234             382 aa            linear   BCT 11-JAN-2025
DEFINITION  epoxide hydrolase family protein [Burkholderia latens].
ACCESSION   WP_175921234
VERSION     WP_175921234.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15920060
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..382
                     /product="epoxide hydrolase family protein"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42444
     Region          5..108
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          73..>199
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
     Region          93..367
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mqaapfdiai pdhalddlrr rlrnvrspql tlaepwqqgm dgawlrelta ywadrfdwre
       61 teralnrlpq fvadiggqrv hfihrrgtgr apyplvithg wpgsvfefda lldrlcdpaa
      121 fggdpddafd vvapslpgfl fspapaapgm safqvadcwa almsglgyrr fgaqggdlga
      181 gvsialgarh adavdgihln ylpgsyeppa daaspptdde rafvaqrnew aaleggyahv
      241 hmtkpqtlav alndspagla awiaekfrsw sdcdgdvarr fsqdtlltgi slywftgcig
      301 ssmqmywenr lqplrfaagq rvtvpvafar fpkeisrppr swlervfdvv qwtdmprggh
      361 faameepell addirrffrr fr
//
LOCUS       WP_175921347             541 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia latens].
ACCESSION   WP_175921347
VERSION     WP_175921347.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..541
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57610
     Region          19..463
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpgqgnthps vplsrsvpad gghgkfkkql sltdltfigl gaifgsgwlf aashvstiag
       61 pagifswllg gfavlllgiv ycelgaalpr aggvvrypvf shgpllgylm gfitliafss
      121 liaievvaar qyaaawfpgl tqtgssdptt lgwlvqaall cfffylnyss vktfakanni
      181 isvfkfvvpl sviavlftff kpanltthgf apfgmpgiem avsaggiifa ylgltpivsv
      241 asevrnpqrt ipialilsil lstliyvllq lafigsiptd mlaagwhdvs kafslpyrdi
      301 alalgvgwla vmvvadamis psgcgniymn atprvvygwa ktgtffkvft rvdeasgipr
      361 aglwltfgla ifwtmpfpsw ealinivsaa lvlsyavapv svaalrrtap glprpfrava
      421 fgitgpasfv iaalivywsg wstvswllgl qiamfviyla crrwvptahl slaeqvrssa
      481 wliafyaami vlsyfggfgg tgqlahpydt avvaaaalvi yywgantgvr sdklqledde
      541 d
//
LOCUS       WP_175921247             201 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia latens].
ACCESSION   WP_175921247
VERSION     WP_175921247.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..201
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20890
     Region          1..199
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msmlvsmaaf alassitpgp vnivalsaga rhglgaslry vagatlgfva lflliglglh
       61 avlarwpmlt tatqwsgiaf llylalrlal ddgqlsavqd dpaapkvagp saaagaamqw
      121 lnpkawlacv aamgayaadg draqvwqfaa lylvicfasi acwayagasl rhrlanarrm
      181 rlfnramall lagsalylld i
//
LOCUS       WP_175921488             834 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia latens].
ACCESSION   WP_175921488
VERSION     WP_175921488.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 834)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 834)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..834
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87695
     Region          548..797
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mrnlllgwll aavvsaahaa aapaaasaas saapvltpqq aqqalsvlqn prerqqvett
       61 lraiaavgvl sapalpasga apasaasaaa paalttngla smvvrqgsrw ageiggalne
      121 slrslldvgs vgrwwherla nadaranlar alaiivavlv palvvewfak rllrralaal
      181 sarraeasdh tdaepvepep pgtgddpapa heaaataagt atasdatdtt aaagarpaas
      241 qgrgharrqt tllrrmpral vslalravpl lvfvgvaslt msvldgagtp tdtaleslid
      301 iyvicrlvti vsrlffqpda rqlrllhisd awaafaqrsi arivivvgac taaveiagsf
      361 glsdaghval lkavalvghl misalivrcr qpvavriraa gearpafatl thaladawap
      421 vsvfvvmalw fvwaldvhng yrvlitlggr siavmigmri vsivvfggla rlfqrrdddr
      481 tlvhlhayry yplvrrivsa viavvtamll lqtwgvpifh afqagtighr lasalltiai
      541 aaiaalivwe aaniaierrl qlwtregnlv raarlrtllp mlrsllfimi alvvvltgls
      601 eigvnigpll agasifgval gfgsqklvqd fitgifllme namqvgdwvt lagvsgtvey
      661 lsirtvrlra gdgslytipf ssvttvnntn rglgnaavkv siaygqdidq aiatlkeiga
      721 alrddpdykd gilsdfsywg vdqvdgatit lagqmqckds arwgvqrefn rriavmfrer
      781 giwianpqrs vvaydptaqp vaagngdsre dggnaggppa aeppppaapa hkpd
//
LOCUS       WP_175921411             316 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175921411
VERSION     WP_175921411.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..316
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33251
     Region          6..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..302
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,223..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mddidlnlvt aldvlltegs vtaaarrlgl stsamsrtla rlraatgdql lvragrtlvp
       61 tphaaalrdr vhavaadara vlrpatadid maalsstfti ragasfmdml agpvvaaigd
      121 iapgvrvrfv akphrdpgpl rdgtvdleig krgddapelh trelfydrhv avaraghplf
      181 apgngaskvt aaryarcrhv iaaqlgdfsg padtlapaha vhvvvpgypd amrvaagtdl
      241 ialvphsslg naftpglada lglrsfeipv qlseilvsal whprmhgdpa hrrlrdavid
      301 vckraypdtg aprrar
//
LOCUS       WP_175921606             208 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia latens].
ACCESSION   WP_175921606
VERSION     WP_175921606.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..208
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22151
     Region          12..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mfdlttlttf tavvlglfli pgpavllvls rtvqggrktg iltglgvasg dfvhtlfaav
       61 glsallmtsa lafnvvklvg aayliylgvr allekpsdps lpkvssvtpl kaylqaipae
      121 vlnpktalff lafmpqfvhp ergstfvqfa vlglifvvls slyttliacs irplgrivkr
      181 lawlarwqgk iigsifialg lrvavqqr
//
LOCUS       WP_175921610             741 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia latens].
ACCESSION   WP_175921610
VERSION     WP_175921610.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 741)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..741
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79537
     Region          50..741
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mtvnrttaar vrrrrtkvrl gvglgitlfa aqtaaaqgga paadaagsat lpaitvsger
       61 gsafrvreas vaglddaplr dtpasvsvvt raqlddqqak rlsdvvrnda svvndyapvg
      121 yfegfairgf pvdlasairi dgltvsgeqn vplenkerve ilkglagids gvvapggvin
      181 fvtkrsanva svtagvdsrg stsaavdlgr rfgpdhqfgf rinaakenmh syvdgtngrr
      241 tfgsiaadwd igpraslqln aefqqwiqrs apgyqllggt vvpsvktask algtqpwakp
      301 vttdalnlna rfdyqfnddw kayvaagrsr tmiddnsafa ygcyyaasca agatspfffg
      361 angdydvydf rspgeyrrnd dvravttgqf atgplrhelt lgvsvqrrvv hmadavydyv
      421 gseniygpdv afapspntpg psyprldawq ygvfgldris igehwqvlag gkevllrqrs
      481 wdsidgdaah tdrsvflpqv alvykpvnal slyasyskal slgdqapvra tnayaflppv
      541 eshqvelgak ydwldrlslt aavfsiskpf qfadpdasgt sytfvqrgtq rhqgielgaa
      601 grlterlslt asaaairara ydsgspayeg hqiinvpalr aslyadyavp gvaglnmlgg
      661 veysagrnan eegtarvpsw fvfnlgaryt tkigghrtvl rvsvdnlfnk fywrdageqq
      721 gdaylfpgap rtarvsltyd f
//
LOCUS       WP_175921688             512 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia latens].
ACCESSION   WP_175921688
VERSION     WP_175921688.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..512
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52142
     Region          16..444
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,142,
                     145..146,149,273,276..277,280..282,285,313,317,371..372,
                     376,380,396,399..400,403..404,407)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtlsdsrrna valaavclts lmfgleissv pvilptlehv lhgdfngmqw imnaytiact
       61 tvlmaagtla drfgrkrvyv igtvlfgats llcglapnvp vlvagrvlqg asggamlicq
      121 iavlshqfre grergrafgi wgivfgiglg fgpivggaiv alaswpwvfl vhaplaaval
      181 vliggavqes rdphagtldv agivtlslav lglafyitqs aelglasaag lgvlgatala
      241 lagffvaers sarpmfdfsv friraftgai fgsmgmnfsf wpfmiylpiw fqvalgydsv
      301 taglallayt lptlvappfg erlalrygpg vvipgglfti aagfalmrig sgiehaswvt
      361 mlpgcviagi glgltntpvt ntttgavpsa ragmasgidm sarmislaln iaamgfvlva
      421 givaslkagv agavdagtlr alaqqiasgr tdglqaiapa laqtdptgaa lhaalvhgfg
      481 wvmvygaagv avlatasava faparrgaav ce
//
LOCUS       WP_175921713             433 aa            linear   BCT 11-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Burkholderia latens].
ACCESSION   WP_175921713
VERSION     WP_175921713.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..433
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46514
     Region          5..431
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 msmnddatfw rnarqhliry ggtfepiiie raqgsfvyda dgraildfts gqmsavlghs
       61 hpeivavige yagkldhlfs gmlsrpvvdl atrladltpp gldralllst gaesneaair
      121 maklvtgkye ivgfaqswhg mtgaaasaty sagrkgvgpa avgsfaipap ftyrprfern
      181 gtydylaeld yafdlidrqs sgnlaafiae pilssggiie lpegymaalk rkceergmll
      241 ildeaqtgvg rtgtmfacqr dgvtpdiltl sktlgaglpl aavvtsarie erahelgylf
      301 ytthvsdplp aavglrvldv vqrdglvera nvmgdrlrrg lldlmerfdc igdvrgrgll
      361 lgveivkdrr tkepadglga kitrecmklg lsmnivqlpg mggvfriapp ltvseaeidl
      421 glslleqaia rsv
//
LOCUS       WP_175921707             441 aa            linear   BCT 11-JAN-2025
DEFINITION  leucine-rich repeat-containing protein kinase family protein
            [Burkholderia latens].
ACCESSION   WP_175921707
VERSION     WP_175921707.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Shen,K., Hines,A.C., Schwarzer,D., Pickin,K.A. and Cole,P.A.
  TITLE     Protein kinase structure and function analysis with chemical tools
  JOURNAL   Biochim Biophys Acta 1754 (1-2), 65-78 (2005)
   PUBMED   16213197
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
REFERENCE   7  (residues 1 to 441)
  AUTHORS   Hanks,S.K. and Hunter,T.
  TITLE     Protein kinases 6. The eukaryotic protein kinase superfamily:
            kinase (catalytic) domain structure and classification
  JOURNAL   FASEB J 9 (8), 576-596 (1995)
   PUBMED   7768349
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..441
                     /product="leucine-rich repeat-containing protein kinase
                     family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=47131
     Region          <2..>186
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          39..61
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          62..84
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          85..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..175
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          211..>371
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(214..217,220,222,238,240,269,287..290,345,349..350,
                     352,362..363)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
ORIGIN      
        1 mtttleqlqa gqlagsrqlk lacgltefpr eifdladtle vldlsgnals elpddlarlh
       61 rlrilfasgn rftefpevlg scaqldmigf kanrirtvpr galpralrwl iltdneidel
      121 pagigdcprl qklmlagnrl ralpaemaac ralelvrvsa nrldalpdwl lrlprlawla
      181 sagnpfgaap eaeasaepgv adihwtsltc eqklgegasg viyraqwrad grapravavk
      241 lfrgavtsdg lpdcemaacl hagrhpnmip vigqvhghpd gahglvmelv dpaltnlagp
      301 psfasctrdv yaadarfapa dasriahgia svaahlharg imhgdlyahn ilhdgaggal
      361 lgdfgaasvy dvndrvraar fervevrafg hllgelrerc eprawdgaha ldalaaacln
      421 edvdarpsfd qivaalatam d
//
LOCUS       WP_175921727             309 aa            linear   BCT 11-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Burkholderia latens].
ACCESSION   WP_175921727
VERSION     WP_175921727.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..309
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34034
     Region          44..299
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mfyltspdvr eadvftrmpe kfrkpdvrte waranrggmv tdsflegpvw dpdgylfvtd
       61 iphgrifris psgdwelvae ydgepngmkr fdashlivtd yrnglmlvdi argevrpyle
      121 rrnterfkgv ndltfdsagn iyftdqgqtg lhdptgrvyr lspdgkldml lgtcpspngl
      181 vlsrdekvlf vamtrgnavw rmplqadgsi skvsqfftsy gpsgpdgltv dlegrlfvan
      241 pglgrvwvln hyaepveilt gpkgasltsv cfggpdmktl fitestsgsi lkadmsiagp
      301 lpkqaakkd
//
LOCUS       WP_175921740             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175921740
VERSION     WP_175921740.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33171
     Region          7..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(105,109,148,162,164,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(106..107,111..112,114..115,118,122,124..130,191,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 marlpdfegl amfakvaeeg sfaaaarsmg vsvatvsrgv arledrlggr lfnrtsrqla
       61 ltefgrtlse kagdmyrhae eaesaarema vqprglvrla vpmsfglrwv apllpaffra
      121 ypevsidlhl sdasvdliad gfdaalriaa lpdsslvarr lcavtqyvva spaylkregr
      181 pahprelagr pclsyayrah sdvwrftnda gdeepimpng plrvtnadal lptlldglai
      241 gelpefiage yladgrleai ltdwsltkgg lyfvtpsara rpakvaalsd yfaehlsdpv
      301 wrwpk
//
LOCUS       WP_175921755             551 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia latens].
ACCESSION   WP_175921755
VERSION     WP_175921755.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Gournas,C., Athanasopoulos,A. and Sophianopoulou,V.
  TITLE     On the Evolution of Specificity in Members of the Yeast Amino Acid
            Transporter Family as Parts of Specific Metabolic Pathways
  JOURNAL   Int J Mol Sci 19 (5), 1398 (2018)
   PUBMED   29738448
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Vangelatos,I., Vlachakis,D., Sophianopoulou,V. and Diallinas,G.
  TITLE     Modelling and mutational evidence identify the substrate binding
            site and functional elements in APC amino acid transporters
  JOURNAL   Mol Membr Biol 26 (5), 356-370 (2009)
   PUBMED   19670073
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146941
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..551
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59542
     Region          31..470
                     /region_name="AA_permease_2"
                     /note="Amino acid permease; pfam13520"
                     /db_xref="CDD:404414"
ORIGIN      
        1 msqaglranr tsdveatish dstghtlhrg ltwkdafwvt sgvpagvlft iggvcatigq
       61 pawaiwiaai tmglvqsaty aeisglfphk sggasvygai gwvrysklia pvsvwcnwla
      121 wspmlalgcg laasyaltsl fpanaavlqw qlkvadlgfi kpglslrina tfiiatilll
      181 itfklqhsga skaartqril giasltplli vgivpfvtgd vpmsnllpll plghdaqgnl
      241 taatfgswng qgvtmalgam fmagwasygf etavcytref rdprrdtaka ifwsgalclv
      301 vmtlvpmafq galgtqamld paigdgtgva aamakivggg awvanavvvm lmlsillivm
      361 tsmmgssrtl yqasvdgwlp kylshvnehg sptramwtdl gfnlvllmms dymtvlsisn
      421 vcymlfvfln lqsgwihrmd rgnwdrpfrc ptwllvagsi cgyanlvyvg aganlqgegt
      481 lrngliamll ivpvflyrhy wqdrgrfpaq mqrdmelevp kramwlslmp yaalvgaalt
      541 iwlsyyfawv k
//
LOCUS       WP_175921910             247 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175921910
VERSION     WP_175921910.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..247
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27018
     Region          3..240
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mdvklvartl dlfelfaaer rplpltelar llnvpasscl amartlvsrg ylyevrkrgg
       61 yyptrrlqtv aaaidatdpv vdlvhphlva lrdasretav lgkiqgtsvt yldvveseqa
      121 irytrqpgel rplhansigk aifaelghdv qqalgaqlsf erftdasvpd lpalvaqtvr
      181 frelgwaenf gesapelsai avalmldgdw yglsivgpte rirqhrdaha allvetkarl
      241 laeqgrg
//
LOCUS       WP_175921887             234 aa            linear   BCT 11-JAN-2025
DEFINITION  chemotaxis protein CheW [Burkholderia latens].
ACCESSION   WP_175921887
VERSION     WP_175921887.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..234
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=25106
     Region          79..228
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mnrdavaadv ttigvddcwn rigtrgdrsc erladclrcl ncpvyayhaa kllerplgaa
       61 emadatqris aadalrahad ddtrhaalaf rvadewlalp igvlreiagt rpihslpyrr
      121 hsavrgvvni rgtlriaisi gallgldagr sgergadgrf trllvaahhg epvvfpvdev
      181 egvlrfgase wvpvpatvgr asaglsrgvl swrgksvgll dddrlfdavt rsmr
//
LOCUS       WP_175921933             291 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia latens].
ACCESSION   WP_175921933
VERSION     WP_175921933.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..291
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30763
     Region          7..260
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtrstaalaa rgltvgyrdh vvidgldlsi aagrvtalcg pngcgkstll rtlaglqpar
       61 aghidvngrp lasfrrrala reltmlaqfn qipsgltvre lvaygryayg gflrglsrad
      121 haavdealdt sglaadaerd vgalsggerq rawiamalaq qapivlldep ttyldihhql
      181 dildalreln rtrgltivwv lhdlnqaaay sddivlmrag rvvaqgspda mlepaqlraa
      241 fgvdmlklah pqtgapmcvp aygpprspep gsraagaaha feraigrdia v
//
LOCUS       WP_175921937             817 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia latens].
ACCESSION   WP_175921937
VERSION     WP_175921937.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 817)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 817)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 817)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..817
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=87042
     Region          1..803
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mlvvgsqsha tefnssfldi ggssnvdlsq fsqpdftlpg eymldvqvnd lfyglhaiqf
       61 valdgsgagk pcvapelvaq fglkpslakd lprlqggrcv dlgaiegatv rylksdgrlk
      121 itipqaalef tdstylpper wsdgipgaml dyrviantnr sfgaageqtn aiqaygtiga
      181 nwsawrfrgd fqaqsnagss ayadrtfrfs rlyafralps irstvtfgdd ylssdifdtf
      241 altgasirsd drmlppslrg yapliagvar tnatvtvsqa grvlyvtrvs pgafalqnin
      301 tsvqgtldvt veeedgsvqr fqvttaavpf lartgqlryk vavgkprqfg gagitpffgf
      361 geaayglpfd vtvyggfiaa sgytsialgv grdfgrfgav sadvtharar lwwngatrng
      421 nsyrinyskh fdgldadvrf fgyrfserey tnfaqfsgdp tayglanskq rysatlskrf
      481 gdtstyfsyd qttywarase qrvgltltra fsfgvlrnln vslsafrtqs agasgnqfsv
      541 tatlpiggrh tvtsnlttgn gstsanagyi yddpagrtyq inagatdgra sanasfrrrt
      601 styqltaqas tlanayaaas leldgsfvat qygvsahang nagdtrllvs tddvpgvpls
      661 gtlthtdsrg yavldgispy nvydatvnve klplevqvsn piqrmvltdg aigfakfsaa
      721 rgsnlyltlt dadgkplpfg asvqdaangk elgivgegga afltqvqpks alavragert
      781 lctvdtlpnq lqlegtpipv acqpagepha avrrter
//
LOCUS       WP_175921940             427 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia latens].
ACCESSION   WP_175921940
VERSION     WP_175921940.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..427
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=45393
     Region          <225..357
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mwtpvvkpaa ppdtfapgra rrfvralvpa avlgalaafg laaalpavsq lpgavdtgaa
       61 alpqrvlsdt pfptaqhfvt selvrtlger neldersnrg vqpglfapls ahrndmlgyt
      121 slfqyaapdn phgmragdie ltlsetlnrl dvppevriql gdlvsgkvam rasaqrgdyy
      181 riaydtnngt phltavelrv agrtfgaiwf rapgadhgay ytldgaplea aaftmpvkwt
      241 rissffgeri hplsqamafh tgvdlaapsg tpvtsaadgv vsfvgtdpgg ygryvivdha
      301 dgystyyahl sayarglkvg etvkqgqrig svgmtgaatg phlhfevrva dapvdplvtl
      361 anaqtglsdm qltafrqeaa qwrfrlasin tapfafaqsd gplwgdfatg pstlrsvfdt
      421 hysaers
//
LOCUS       WP_175921979             561 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia latens].
ACCESSION   WP_175921979
VERSION     WP_175921979.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..561
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=60172
     Region          10..560
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mksrldrwmm llaiaaagta haqtraagnp ldslpqinap ktgpsvtvqv apqapqlqel
       61 lsrhltpatf qvegvksipf eeisrrftpl vgkditigel ieaangvtkl yqergyalsf
      121 afipaqtfes gvvrvtvveg yvsdvkvtgk pgameskira iaahitadrp lrratferyv
      181 ntfgllpgvt vkanvpppqt tdgattlela vdrkafnist gidfnhpgvq glitatengl
      241 tsfgeqlsis alvppgrdkq tyvafsgavp vgssglvtrl dastyrgkpt dnpglpssve
      301 rtvkneklgl sasyplllnn qrsllgtvsg yashnedryq sklngnsidt rsqvrvlqmq
      361 ldytsvsdkq vrklsvnvak gfnilgaska qditigsntt svdspvsltf vrtgatftqt
      421 newpfkigts vsltgqyspd slptseqisf gstryalgyq pgetsgdsgw gmslevnrgf
      481 tpgwtymksi tpyiaydmar vylhtgtpsp srlssvgigv rltdsryysl dlniakpvgd
      541 apvesasrsp rvnatfsyql n
//
LOCUS       WP_175921991             137 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175921991
VERSION     WP_175921991.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..137
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15326
     Region          19..106
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(20..22,36,53..55)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mtttvekvvl ppipakryft igevselcgv kphvlryweq eftqlrpvkr rgnrryyqhh
       61 evllirrire llyeqgftin garnrldspg geraaaepve pgvpaadarg egksgamvdv
      121 valrqalldv idglkhd
//
LOCUS       WP_175921818             321 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia latens].
ACCESSION   WP_175921818
VERSION     WP_175921818.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..321
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34684
     Region          11..224
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(52..53,55,69..71,77,79..80,121,223)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(52,54..55)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(77,80,83,90)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(113,117..120,122)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(118..119,142..144,196..197)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          237..321
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 mndatltvrv arkwqeardi cgfefvsddg splpcfdaga hidvhlpggl vrqyslcnhp
       61 dqrdryqiav lrdadgrggs raihdevrqg dtvrigiprn qfplapdaph hlllaggigv
      121 tpilsmaerl fssglpfdmh ycarsadrma fvdrinaagf hdrarfhvdd gdpaqrfdlt
      181 avlagapegt hlyvcgprgf mdavlhaare rnwaearlhy effggavass gadrafqvkl
      241 assgkvidvp aectviaala angidvltsc eqgvcgtcat rvlegepdhr dayltddeka
      301 agdlfmpccs rsrsellvld l
//
LOCUS       WP_175921996             557 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Burkholderia latens].
ACCESSION   WP_175921996
VERSION     WP_175921996.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60484
     Region          25..384
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          453..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mtpaslieqy gpresmeydv vivgggpagl saairlkqla aekgteigvc vlekgseiga
       61 hilsgavmdp raitelfpdw keqgaplnve vtedrflfls eksavqtpnw alpdnfknhg
      121 nyvislgnvt rwlgqqaeal gveifpgfpa aeilynddgs vkgvatgnmg vgkdgepten
      181 fqlgmelhak ytlfaegcrg hlgrqlistf kldanadpqa ygigikelwe idpakhkpgl
      241 vihtagwplk sdtyggsfly hmdnnqvvvg fvvglgytnp ylspfeefqr ykthpsiraf
      301 leggkrvsyg araitaggll slpktvfpgg aligddagfl nasrikgsha aiktgmlaad
      361 aafdavqagr qsdelnaypd afkqswlyte lyrarnfkqw makglylgtl mvgleqkvmg
      421 gnvpwtlhhk hadhemlkpa sqcepiaypk pdgkltfdrl ssvfisntnh eenqpahltl
      481 kdasvpvnvn lrtyagpear fcpaavyefv knddgsdrlv inaqncvhck tcdikdptqn
      541 ivwvtpeggg gpnypnm
//
LOCUS       WP_175921997             315 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia latens].
ACCESSION   WP_175921997
VERSION     WP_175921997.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..315
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=34441
     Region          11..301
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mqhhqqssat iegivpvmlt pfddagaidy aglarlvewy lahgsdalfa vaqssemqfl
       61 slaeraelar fvvdrvagrv pvvasghise dfdsqvaelr aaaesgaqgv vlvtnrldpq
      121 rkgsaafldh lhkllarlps dlplglyecp apyrrllsdd elracidtgr fvmlkdvscd
      181 letvkrrval aagsplkiln anaaiawdam kagsagfngv ftnfhpdlyr wlrlhgdsdp
      241 aladelstfl vvsavsealg ypalakiyhq rigtfasirc raidydvrer fwaldavldk
      301 ivsgtehfrr rigvr
//
LOCUS       WP_175922005             733 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia latens].
ACCESSION   WP_175922005
VERSION     WP_175922005.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 733)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..733
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..733
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79691
     Region          33..716
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 msasspasth aggplaawya afgdwartdg aawlylfkal laafiatgvs mrldlpapkt
       61 amttvfivmq pqsgavlaks fyrvagtifg liatlafvgl fpqqpqlfll avalwvalct
      121 agaarnrnfr sygfllagyt taliglpasq hpdgafmsam trvaeimvgi vsagvvsalv
      181 fpqttgqqmr ttvrkrfgnf vdyvaaalsg kldrahieti htrfvadvvg feaarsmavf
      241 edpdtrmrsg rlarlnsefm svssrfhalh qlmnrlraag aqaaidaiep yfreiapllt
      301 rngepvrssa daalaaeqll awrdalprri ratraaletq pdfplldfdt aaellyrfit
      361 dlheyaatya slssathere rwieryeprt nvtamviaai rtatvilvlg wfwiatawps
      421 gvtmtltaaa tcalasstpr ptamsaqmgm gtalavctgf lltfgiyphi dgfpllcval
      481 apllaigiym tlkpklagyg mgyliffcfl agpdnithyd pmsfmndala lvlsmlvsai
      541 afavlfppta pwlkkrlfad lrhqvvaach arlaglrtrf esgardlmyq ahtlsadqpd
      601 vqrdalrwmf avleagnaal dlraelatlp sdpryapatp wrraietmrt alsalfskpd
      661 aerfdatlaa vnaaidatrq tldavapsrd erhrlqrils hlhfvrtall dpesplepln
      721 rnravraqpg ass
//
LOCUS       WP_175922024             312 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            latens].
ACCESSION   WP_175922024
VERSION     WP_175922024.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..312
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=31946
     Region          1..310
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mhalalqafn glsyglllfm lsagltlifs vqgvlnfaha sfymlgayvg ysiaaragfw
       61 aalafaplav gllgagcerw llrrvqargg htnellltfg layligeaak llwglaplpa
      121 pvpplfdgap vtvfgvalpr yrlfmmgmsa amlvalgall rasriglvvr aalthraave
      181 algydvprmm tglfgagtal aalagvigap laviepalae tvgsivfavv vigglgslgg
      241 afvaslavgf aqtfaassdt slrdfaqwag valpdniaav svaqlaplvp ylllvavlva
      301 rprglfgerv dg
//
LOCUS       WP_175922051             197 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia latens].
ACCESSION   WP_175922051
VERSION     WP_175922051.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..197
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21519
     Region          7..161
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mdshiapvel kkayrllnhg ptvlvsarhd gvdnvmaaaw acaldflppk ltvvldksak
       61 trelversga fviqvptaaq lqlthavgsr slaerpdklr eagvtlfdve grdlpfvagc
      121 sgwlacklip ephnqqtydl figevtgaws dtrvfrdghw yfesadpalr slhyiaggnf
      181 yaigeslhvd pdrtdaq
//
LOCUS       WP_175922111             270 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia latens].
ACCESSION   WP_175922111
VERSION     WP_175922111.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10549394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..270
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30527
     Region          <97..143
                     /region_name="Methyltransf_11"
                     /note="Methyltransferase domain; pfam08241"
                     /db_xref="CDD:462406"
ORIGIN      
        1 msdrqiidwp awtdsppgry vlgweqvqld rivsdvfgfh alqlglpqld alrenrmpyr
       61 glvldpasga sapyqypwar dahagehapa drsttwcdll dlpfesqsvd livmphtlef
      121 tsdphrllre aervlmpegq lvitgfnsls lwgmrqsfgr manrpfvpaa rdqiafirlk
      181 dwikllgfdl ergrfgcyrp plvtdkwlar ygfmeaagdr wwpifgavym vtavkrvrgm
      241 rlvgpirmkk pvlapgltpa atptthqess
//
LOCUS       WP_175922152             183 aa            linear   BCT 11-JAN-2025
DEFINITION  peroxiredoxin [Burkholderia latens].
ACCESSION   WP_175922152
VERSION     WP_175922152.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Jeong,W., Cha,M.K. and Kim,I.H.
  TITLE     Thioredoxin-dependent hydroperoxide peroxidase activity of
            bacterioferritin comigratory protein (BCP) as a new member of the
            thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide
            peroxidase C (AhpC) family
  JOURNAL   J Biol Chem 275 (4), 2924-2930 (2000)
   PUBMED   10644761
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..183
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.24"
                     /GO_function="GO:0008379 - thioredoxin peroxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19462
     Region          30..171
                     /region_name="PRX_BCP"
                     /note="Peroxiredoxin (PRX) family, Bacterioferritin
                     comigratory protein (BCP) subfamily; composed of
                     thioredoxin-dependent thiol peroxidases, widely expressed
                     in pathogenic bacteria, that protect cells against
                     toxicity from reactive oxygen species by reducing...;
                     cd03017"
                     /db_xref="CDD:239315"
     Site            order(69,72,142)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239315"
ORIGIN      
        1 mkrklwvgat aallvaghal vaqaqlkpgd aapvfttqas lggktytyal adalkrgpvv
       61 lyfypaaftk gctieahafa davdryaayg atvigvsadn idtltkfsvs ecrskfpvaa
      121 dpdakiirey daklpavdra nrvsyvispe gkvlyeytsl spdkhventl aavkawadah
      181 pkq
//
LOCUS       WP_175922270             422 aa            linear   BCT 11-JAN-2025
DEFINITION  sialidase family protein [Burkholderia latens].
ACCESSION   WP_175922270
VERSION     WP_175922270.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..422
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44987
     Region          57..>154
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Region          104..153
                     /region_name="Sialidase propeller 2"
                     /note="Sialidase propeller 2 [structural motif]"
                     /db_xref="CDD:271234"
     Region          <370..>414
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
ORIGIN      
        1 mvvvksfaag calwlaalss agahdahdap kaadphaahm smqaapaqqk qplatgaafg
       61 arhrlwvawv egahvvvahs ddagrtlsap vtvnampepi ytsaenrpkv atspdgravy
      121 vswsmpldap ytgmvrfsrs ldggatwsvp vtvhrdrqai thrfdmmavd pagniaiawi
      181 dkrdlvaaka aahaydgaav yyavsldgga sfeperkvvd htceccriam aigpaghiea
      241 vwrnvfpgqi rdhalavlpv sasepvvpvr atfsnwhvea cpehgpalai tpdgtrhiaw
      301 fgvvdgradv fysrigadge prgtpwafga npavpaeqas haalaargdv vwlawkafdg
      361 dmmqiklrrs ddrgehwsap sviastsgas dnpqllddag rvylswrtrn dgyrlipveg
      421 tr
//
LOCUS       WP_175922271             785 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia latens].
ACCESSION   WP_175922271
VERSION     WP_175922271.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 785)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 785)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..785
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..785
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85229
     Region          67..767
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msfifaarps rgrlalacaa afawpaaqaa sldrasagsa aagpghaaas gaeavaavtp
       61 apagdtlsav svtaqrqpid pdtpavvqsi treqidahtn vttedalkya pnlmvrkryi
      121 gdrnsvfagr dfnelqsarg lvyadgllls nllgssyayp prwsliapdd iarvdvlygp
      181 fsalypgnai gstvllttrr pdkleaslst qfftqryrdg ygvadsfggn hqtarianri
      241 gkfwfslsld rlendsqpmq yaspnstynp rlgapvpvtg aatdigpngk prtivgaqni
      301 erteqlnetv rmgyaftdhv datltlghwe nhyrqhgetf lrdaagnpvy ggnvsiggrn
      361 vtvapsafap qrgdqenwly alglngrlds gwrlsgvvsa ydvsrdvlrs astvqggagt
      421 lfqgdgtgwr tldlkaealq vkghtftfgy hydnyflrnv tyntadwlag pttslasvyr
      481 gdtrtqalfa qdawrfapgw latlglryer wdayggalgn asgtlgyadr ganalspkva
      541 vqwdatdvwr frlsfatgtr fptvgelfqg tisnnaivnn npnlrpekai dwdftaerdv
      601 gvgvvrasvf qsdlrdsiys qttvagastv tnisnvdrvr vrgvelafsg qnvglrgldi
      661 danvsasnaq ilsdtanpay vgsrfpripr mranllasyr fdehwlasvg lrysgrqfnt
      721 ldnsdvnpdv yggtstftiv dlkaryrfdr hwsasvgidn ltdrryyvlh pypgrtffge
      781 lkwsl
//
LOCUS       WP_175922325             328 aa            linear   BCT 11-JAN-2025
DEFINITION  FkbM family methyltransferase [Burkholderia latens].
ACCESSION   WP_175922325
VERSION     WP_175922325.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..328
                     /product="FkbM family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=36984
     Region          29..191
                     /region_name="Methyltransf_21"
                     /note="Methyltransferase FkbM domain; pfam05050"
                     /db_xref="CDD:428282"
     Region          243..>328
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mtflsfaqnf edivlwrals dveqgfyidv ganepiedsv tkafyergwh giniepvteh
       61 fdalvqdrpr dinlacalge kpgrltlyei darglstnap eianryresg rlhgerevev
      121 rtladiceah apadihflki dvegfernvl lgadfkrfrp wilvieatep nspvdnsaew
      181 esivtdagye yayfdglnrf yvaaehrdlk prialapnvf draklrrghc fvldpevspd
      241 ehralqatla areralaeln delaalrsel aavraelsda hlnaahsdaq vmdlkrqlat
      301 lqadharqse rlaqplvrma lrlhrasr
//
LOCUS       WP_175922373             136 aa            linear   BCT 11-JAN-2025
DEFINITION  GFA family protein [Burkholderia latens].
ACCESSION   WP_175922373
VERSION     WP_175922373.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..136
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14870
     Region          5..131
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mphpetmegg cacgairyri agipadagfc hcrlcqrttg aavvasasvp idafeylqge
       61 ptvyassawg errfcgrcga qleyrradap ttveinyaml depsrlhpaw hvwyadrfpg
      121 ididddlpky ddggre
//
LOCUS       WP_175922383             336 aa            linear   BCT 11-JAN-2025
DEFINITION  sodium:calcium antiporter [Burkholderia latens].
ACCESSION   WP_175922383
VERSION     WP_175922383.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schnetkamp,P.P.
  TITLE     The SLC24 gene family of Na/Ca(2)-K exchangers: from sight and
            smell to memory consolidation and skin pigmentation
  JOURNAL   Mol Aspects Med 34 (2-3), 455-464 (2013)
   PUBMED   23506883
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Besserer,G.M., Nicoll,D.A., Abramson,J. and Philipson,K.D.
  TITLE     Characterization and purification of a Na+/Ca2+ exchanger from an
            archaebacterium
  JOURNAL   J Biol Chem 287 (11), 8652-8659 (2012)
   PUBMED   22287543
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..336
                     /product="sodium:calcium antiporter"
                     /GO_function="GO:0008273 - calcium, potassium:sodium
                     antiporter activity [Evidence IEA]"
                     /GO_process="GO:0006874 - intracellular calcium ion
                     homeostasis [Evidence IEA]"
                     /calculated_mol_wt=35117
     Region          19..332
                     /region_name="ECM27"
                     /note="Ca2+/Na+ antiporter [Inorganic ion transport and
                     metabolism]; COG0530"
                     /db_xref="CDD:440296"
ORIGIN      
        1 mtlmlvelaf mllvilvaae lftnalehlg erlkisegvt gslfaavgta lpetmvplla
       61 laggtsnaav neeigvgail gaplmlatlt tflmtlavig srgltgtitp ertgfvrdln
      121 yfiaafalat iamfvphhvw avrallaaml vgiyalyvvm tfrastqlvd aghgteapha
      181 mflsrvglpt nlatialqla vgvallvgga kgfihgvegv shllgisall lsliivpiat
      241 elpekvnsvl wirrkkdtla fgnitgamvf qgtllpaigi mltpweprpe vlsgvvitla
      301 aavwlrvnar arglaiwall angagyagyl lvtltr
//
LOCUS       WP_175922358             212 aa            linear   BCT 11-JAN-2025
DEFINITION  2-hydroxychromene-2-carboxylate isomerase [Burkholderia latens].
ACCESSION   WP_175922358
VERSION     WP_175922358.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Thompson,L.C., Ladner,J.E., Codreanu,S.G., Harp,J., Gilliland,G.L.
            and Armstrong,R.N.
  TITLE     2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class
            glutathione transferase from Pseudomonas putida
  JOURNAL   Biochemistry 46 (23), 6710-6722 (2007)
   PUBMED   17508726
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122490
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..212
                     /product="2-hydroxychromene-2-carboxylate isomerase"
                     /EC_number="5.99.1.4"
                     /GO_function="GO:0018845 - 2-hydroxychromene-2-carboxylate
                     isomerase activity [Evidence IEA]"
                     /GO_function="GO:0043295 - glutathione binding [Evidence
                     IEA]"
                     /GO_process="GO:1901170 - naphthalene catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24096
     Region          12..191
                     /region_name="DsbA_HCCA_Iso"
                     /note="DsbA family, 2-hydroxychromene-2-carboxylate (HCCA)
                     isomerase subfamily; HCCA isomerase is a glutathione (GSH)
                     dependent enzyme involved in the naphthalene catabolic
                     pathway. It converts HCCA, a hemiketal formed
                     spontaneously after ring cleavage of 1; cd03022"
                     /db_xref="CDD:239320"
     Site            18
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239320"
ORIGIN      
        1 mttgldttqp awffdfvspf syllleqhdk wpdvpfepvp vslpdlqrhw gqrpsadvpa
       61 krvftyrhal fraeqlgirf kmppahpfds dkvlrlaial radiatvlem frfiwhdgnd
      121 pstpdgfaal cervgvghgd eliefeetsa qlrrntddai algvfgvptf wmnkqlfwge
      181 dalpmvlyca rtpnwlesre vkrisalpkg ra
//
LOCUS       WP_175922427             269 aa            linear   BCT 11-JAN-2025
DEFINITION  TlpA disulfide reductase family protein [Burkholderia latens].
ACCESSION   WP_175922427
VERSION     WP_175922427.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..269
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=29094
     Region          <53..>106
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
     Region          133..265
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mlslgpfsir vvavaaaall awlvarliqr rppdgrhkta sslildvlll gliaarigyv
       61 aqwwrdyaaa prsivalgdg gfdwrigiaa almfavwrlr rlpalrkpva agiaaglaaw
      121 giaqgtlatl qrvappfaam qlealdatpv lpqrfagkpv vvnlwatwca pcrrempile
      181 qahrdhpela vlmlnqgena qavrafleqq glrfdnvlld pslhamhayg srglpttlff
      241 nangelvesh mgeitaarlk davaqrfgq
//
LOCUS       WP_175922434             402 aa            linear   BCT 11-JAN-2025
DEFINITION  benzoate/H(+) symporter BenE family transporter [Burkholderia
            latens].
ACCESSION   WP_175922434
VERSION     WP_175922434.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..402
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41684
     Region          11..399
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mqpntshgai rsigndwsvs aitagflavl isyagplaif fqasqaahvs nemvtswvwa
       61 isvgagvsgl faswklkvpv vtawsapgta llvglfpqlt lhqavgayit aaliilaigi
      121 tgyfdrlvrh iprgiacgmm vgillpfgmh afsaataqpv lgfgmiaayv ifkrllprys
      181 ivlvlltgaa latllgmthv gnvspsiarp ifiapewtlg ttlslalplv vvsltgqflp
      241 gmtilrvsgy htsarpiita tsvmslvvac fggitivvaa itaalctgkd shedperryi
      301 agiangviyl igglfagtiv alffalpkaf vailaglali gaiganvhgi fedddhreas
      361 vitflatasg mtwlglgsaf wgivigsvay avssrargrr gd
//
LOCUS       WP_175922439             452 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia latens].
ACCESSION   WP_175922439
VERSION     WP_175922439.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..452
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=48561
     Region          17..434
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mdtitrtlat qraarvpriv ivgggagglq latrlgdtig rrgqadvvlv drypthfwkp
       61 llheaasghr dpashtieya aqakrhgfrf vqgalqrvdr aartatiaav hdadgteilp
      121 qreldyddlv lavgsvtnff dvpgaarhal plenldqaed frrkflaact kanhaaeqqp
      181 arraapvcin vigagatgve laaalrdaiq qlttyrfkal vsardvhirl ieggprilpa
      241 ldarlsakmh aqlrslnvdv ltntriaevg adavttatre rlasditiwa agvagpailr
      301 elgdialnrs nqvivtdtlq tpddphvyaf gdcaacpsad aggflppraq vahqqavyls
      361 dalarrlagk pvagftfrda gtvvslgqag avyqadlrvr srslivdgla aiglykllyr
      421 khlfsvyglk ralfqslghw lqsrnqpsik lh
//
LOCUS       WP_175922438             317 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175922438
VERSION     WP_175922438.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..317
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34522
     Region          11..70
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          100..296
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(114..115,117..118,121,125,127..133,225..230,
                     236..237,239..240)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mysligktat frqlkaldmi arlgsvsraa eelnltqpav slqvrlleea vgaallqrvg
       61 rgvqltaage ivaryareil hlwseagdev aaltgdlggt lrigaittae ylippllvkf
      121 tatrphvkty fkvgnrddii rmlatheidl avmgsapkel rthavefakh pmvfvaapgh
      181 plmqrkrval kdlesahllv rergagtrst veslfktagy rfhvgselss neaikqmaea
      241 glgvaflslh acalelrtgl lgqlpfpgnp ivrewyvitl adrrisqvtg lfrdflikqg
      301 apvidgatvt pherrrk
//
LOCUS       WP_175922450             329 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175922450
VERSION     WP_175922450.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..329
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35473
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdmlenmrtf vrvvqagsft avakqtdvat aqvsraiasl eayaqirllh rttrkialtd
       61 sgrryferll silgdvdqan aearnalvrp ygrlrvhtmp glgqshvtaa aiayqagfpd
      121 vsiemtysqr mpnlveegyd vsivtasnlp dsgyiahscg tshsvlvasr aylerhgapa
      181 tpadlanhtc lrldtpaeah gewrlhgaag dtvvhavpda pfqanapesl sialhaglgi
      241 gslaiysvid dlrsgrlvrv lpdyrltmld vyvmyasrrf vdakvrtfvd hvratlalal
      301 qaderalaal avprgrgrar vhaltvata
//
LOCUS       WP_175922460             235 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia latens].
ACCESSION   WP_175922460
VERSION     WP_175922460.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 235)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 235)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..235
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24130
     Region          31..130
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          130..218
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mkrawmigta lviagvatag tlygpdlidg mryqkamaai ggadnangga wpqpqetcaf
       61 chgahgqsrn awypslsgqp agyiaaqlra fasdtrrnay mgplareldd akidalaayf
      121 arqapernea vpadealaqr gmalvaargc qachgaaltg kdrmprvagq gqqyldaqla
      181 afrsgqrrdp tgamngvaat lsgddtraia hylaslspdg aggasaagta shaar
//
LOCUS       WP_175922466             207 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175922466
VERSION     WP_175922466.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22156
     Region          9..172
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdpvrltraq rrdatrerll aaaravfaek gyaaasiedi aaaagysrga fysnfrgkte
       61 mlfellrrdh ddmatalqri aatpagsvdd aqrallacwr shaardasrl mwleaqlqaa
      121 rdpqfraqfs allrerqara tacidafvah agvspalpap vlalglaalr dgvhacraad
      181 argtvdtlae avlagfltha vfgrtrg
//
LOCUS       WP_175922481             403 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia latens].
ACCESSION   WP_175922481
VERSION     WP_175922481.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..403
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42411
     Region          17..391
                     /region_name="MFS_MJ1317_like"
                     /note="MJ1317 and similar transporters of the Major
                     Facilitator Superfamily; cd17370"
                     /db_xref="CDD:340928"
     Site            order(27..28,31..32,35,68,119..120,122..124,127,147,
                     150..151,154,230,233..234,237..239,242,269,273,322..323,
                     327,331,347,350..351,354..355,358)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340928"
ORIGIN      
        1 mstpspiagk paiprtvwal glvslfmdls selihallpi ylvttmgmsv aalgmlegaa
       61 eatamivkvf sgaisdwlgr rkgllllgyg laaltkplfp mastpavvvt arlldrvgkg
      121 irgaprdalv advappeirg acfglrqsmd tvgaflgpll aiglmlwfgd rirtvlwfav
      181 apafiaiali vfgvrepepa hdtrrrgfrs plrwralsef prgywfvvaa gatftlarfs
      241 eaflvlraqq tgldaawipa vmvamsvays lsawpvgmls drldrrvlla agmvlliaad
      301 lllgigtstl smfvgvavwg lhmgftqgil aamvsetspa alrgtafgvf nlvsgicmll
      361 assiagalwa rygasttfva gavlvvvplg lcrfiprpgs spa
//
LOCUS       WP_175922502             236 aa            linear   BCT 11-JAN-2025
DEFINITION  PadR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175922502
VERSION     WP_175922502.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..236
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25831
     Region          82..161
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mrhnphrdha rcdghgahar sdwfvglwha igrhrrghdp fgggpfggrg grggfgdfgd
       61 dgmprgrqfs sddlqlllla lvaeqpshgy elikaldtrs ngfyspspgm vypaltylee
      121 vgfvvsqaeg nrkryaltda grahldaqre rvdmlfarlt hlarkmefmr rafagdsags
      181 dtpddaqsgw lpefvearla lkrallhksa adadeqrria aimrrataei eggtga
//
LOCUS       WP_175922526             665 aa            linear   BCT 11-JAN-2025
DEFINITION  beta-galactosidase [Burkholderia latens].
ACCESSION   WP_175922526
VERSION     WP_175922526.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 665)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 665)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 665)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 665)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448998
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..665
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=74394
     Region          1..624
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
ORIGIN      
        1 mrlgvcyype hwpesmwadd arrmkalgia qvriaefaws riepspgeyd wgwldravdv
       61 lgaagleivm ctptatppkw lvdrhpdila igadgrprkf gsrrhydfss piyleasrri
      121 ctavaerygr hpavrywqtd nelgchqtvv syspaalvrf rewlqarygt idalnrawgt
      181 vfwsmeyrhf devdapvgtv teahpthrld yrrfasdela ryhrmqvdvi rahspgrpva
      241 hnfmqlftef dhyevardld vatwdsyplg aleelwfapd vkarwlrtgh pdfasfnhdl
      301 yrgmsklpfw vmeqqpgpvn wahwnpaplp gmvrlwswea fahgagcvsy frwrqapfaq
      361 eqmhaglhtp ddkldeggre aqrvareiaa vldagadada ngavrapval vfdyeakwlf
      421 evqpqgadfh yprfafeyys alrslgldvd ivsahapldg yrlvvvpplp ivpddfatrv
      481 aasgahvvfg prtgsktadl qippalppgp lasmlpvrvw rveslrpnvt aridgtlrdg
      541 spvtgdarhw rdlvelhdda rsvvrvrvrf adghpacvsh gtlhywaalf ddgttarlfa
      601 dvaaeaglap splgdavrvs rrggltyvfn yggtphtida vppsafvvga aqvepqgvav
      661 yrsrs
//
LOCUS       WP_175922520             130 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia latens].
ACCESSION   WP_175922520
VERSION     WP_175922520.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..130
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14338
     Region          8..115
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mttpkayleh vaiwvkdihw higffeevlg mtmrevdgtl daprqywtlg glqfihapeh
       61 dgpegrlahl gvmcedleaa laaarrfgvt empqgrnwlr lpdglaveli qarpascvaq
      121 alainprtea
//
LOCUS       WP_175922529             701 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia latens].
ACCESSION   WP_175922529
VERSION     WP_175922529.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..701
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75906
     Region          7..701
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 msrkkwaaap maivvgtagl stadaqelsl paieisgqrt kapfrapest satrtetdvm
       61 eipfavssvd tkliqtvaat rgedlydwva gvarqnnfgg lwdnyavrgf agdgntsgtd
      121 ylvngfswnr gmsvprdtat lermevlkgp asalygrgdp gglisyttkq pqfarsntig
      181 vsagsygalr etldstgpvt kslayrfiam nedngsfrdt vsskrylfap sftwdvgadt
      241 tlhyefetar qrapldrgvv avggqlgavp asrfmgeprd gdydvrnsgh qftlehrfna
      301 dwsvnagfaq rdtdlsgrss eafslqpdgr tlwrryrqva fhsndvqgrv evagkartgg
      361 ighsfvmgvd ayrfnydqfv arstptaaap yaidifdpvy gqpapvprta tnllerddgq
      421 glyaqdtlaf gphwkvlagl rwdrfhqsve nrlkgvttsq lqtavsprlg ivyeaspals
      481 lyantaysfr pnngadvhgq afdpekghgy eagvkwagtr wlatvaafyv nkrnvltadp
      541 anagfsraag evrsrgvefe wngelghglr givnlayvda qvthdsvltp garlvdiprv
      601 sgsallmyet alplvdkaga gagviyvgrr agntantqdg fdlpayatvq lngyvqvnkh
      661 lrasvvlnnl fnrtyyvssy nslwvtpgap rslfaslays f
//
LOCUS       WP_175922536            1285 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia latens].
ACCESSION   WP_175922536
VERSION     WP_175922536.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1285)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 1285)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1285
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..1285
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=140562
     Region          1..788
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mpilnqtrtl sisgaalpty gmdalpvlvp arlqgteaig ridecrylvt lrtddayafs
       61 psatanldld kvvgtevtvs iqldgkgrfv helaesseld nigagtreit glveaarivg
      121 qdqdsilyel elrpwlyrat ltqdsrlfqe mnvveitdav lskypyrvdk rltgafrggy
      181 pkrdvqrqaf esdwaflqrl weewgiwwwf eheggrhrli lcdaigghha hapayetlry
      241 lppdskqide ehihalsvts rltagrvtvt dydytrprak lavteenprd tanadgeiya
      301 wghysqplag aqglagqpne tdlearhlar vqldaqrcag lrangagnlr gltvgrtftl
      361 tgypqqtanr eyvvvscald ieeigvrtgv aqtyrvetqf ellpanepfr lkrsvdkpvl
      421 sgpekavvvg pagqevqtdq ygrvrvqfew drqglhders giwlrvlspw qgidlgatfi
      481 prighevavm hyygdpdlpv iagslvnafr qpaldmphnq gvsilrgreh hgtasghiai
      541 ddtqgqihtq iasdagtsql slgnlrrmlk kqgradargk gfdlrtddwg vmralkglfv
      601 ttdgqsggag hakdakeavg rlarardlqe slsalaqrhd aqrhradqse vvkainarnd
      661 aikgnpsgnp dhfpeltead ivlagragis laaersahia ssedvavtsg rhvgvavgrs
      721 lfasvantfa lfvhkagmal iaaggkvrve aqndgidlta krairitsta dsihlhaake
      781 ivlhagstev cisergyvvr tagehrvhag shqtdtarlr pirfpvtsdn pgrfaahfvl
      841 lehangfalp nqpyritldn grviegvsnd lgetevvtdh evafgmveil aasdpdkvia
      901 vnraavvrdn tvpytakgpn adkratkirg ktvstpeqga tsenqrpefa acdplnfglr
      961 fhhfidganq advdagmpvr rdvvypvtka ytlaikkalk giewsrfrtl ngeisdeake
     1021 sialavgnvl dsaltagpfg lakgalgnpm gstgatpnid ivnekdgnsr ynmrpevsas
     1081 fvaipwviai qereitkiia ssnnavaldg tlkafadlly hearhcqqtf wmmallqqhs
     1141 sdyamftcam qtyktnclqe ifetaqkaki pddtrisagl hrllvfhyyw misyiknqpg
     1201 gsyvepdvpi aqaevckllr vspetaakmv sfeegyrsql heedayacae vvqaywdrpd
     1261 rafvrnpgtc tgeydaslda igggi
//
LOCUS       WP_175922607             419 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia latens].
ACCESSION   WP_175922607
VERSION     WP_175922607.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10396284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..419
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=44011
     Region          1..261
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Site            order(7,9..10,12,66..68,104..106,116,120,139..142)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187535"
     Site            order(82,106,116,120)
                     /site_type="active"
                     /db_xref="CDD:187535"
     Region          310..402
                     /region_name="DoxX_3"
                     /note="DoxX-like family; pfam13781"
                     /db_xref="CDD:463982"
ORIGIN      
        1 mnilvcgang figralserl eagghrvlrg vrhaagpddv aidfandvdp dawlarlegi
       61 dvvinavgil sdrrdatlda vhraapcalf aaccragvrr viqisalgve rgdtpyfask
      121 laadtflqtl pldyrivrpa lvygasgasa rlfrmlaslp vhalpaggrq rlrpvhvddl
      181 aelvarlvds paaggpvida vgsdeveyre mlgayraalg fppalrialp gslvgaaavl
      241 lgmlpgamlt rdtwtmlrgg ntgdpaalea vlgrpprglr hfigagadav alrhdalamw
      301 rrpllrgala ivwiwtaivs afihpqrdsl amlarahltg lpalvalyaa caldfafgva
      361 tvaapsrrlw aaqgvlivay saviavtmpg llaepfgpvl knlpilaill ilfseeqpa
//
LOCUS       WP_175922638             486 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia latens].
ACCESSION   WP_175922638
VERSION     WP_175922638.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..486
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50067
     Region          31..476
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,156,
                     159..160,163,293,296..297,300..302,305,333,337,390..391,
                     395,399,415,418..419,422..423,426)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtdntlarca pagaaaaapp rshhgwalvv llvgailppl dyfivnlalp airdgigarp
       61 aelqlvvsay acanavvqit ggrlgdlygr krmfmvgmag fvvasalcgl agsgavlvgg
      121 rvlqglfaai lapqvlatir svfspqeqvr vmgfygfvfg laavigqlgg galislhpfg
      181 lgwraiflvn vpigllallg swrfipesrp prgqridvpg tvllslfllm lvyplthgre
      241 agwplwmvac vvgalpvlgv llavearrla ggrdplldvr llrnpvvalg lalaflfyml
      301 saffltygiy lqgcldwspl asglailplg vgflaspllm prlvgrfggy rvltlgfaml
      361 aagvatagal agehapgpgf yagiaaigig qglvlpsvvr ivlaevdaar agvasgmvta
      421 llqigaavga atlgglffar lgaqpdaldy vhgfrttmaa ltavllacva lsaalrplhr
      481 rmraga
//
LOCUS       WP_175922652             500 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia latens].
ACCESSION   WP_175922652
VERSION     WP_175922652.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..500
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52344
     Region          28..451
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msgwsgvtga agdtpaggpa eagggtvlka gavgfptala savglimasp viltatsgfg
       61 mggwafavam iiafvmmqaq attfseaaam lptagsvydy lscglgrfwa itgtisayfl
      121 vhvfagtaet ilsgimalvn feslnaafek hnsawlvgvg lvvtfaitni igikvfskle
      181 ivltagmwls lmifgilgla aapavhldgw fgssevgttv pavlslvgma mfmfvgcefv
      241 tplapemkap grtipramal glvgvavcmf lygaairrqv anvpvsadgl thlldtpgai
      301 pafalqvlgp fgriwfgiaf lcagaatint lmaglprily gmaidgalpr cfaylhprfk
      361 tpvvgivasa ivpifhawli ngnldsilhl vlaatcawgt ayllvtasvv mlrirrpdlp
      421 rpyrspwfpl pqivssvgiv laiwyitppg mnardiyvpf gamlgltaly alfwtvvvqr
      481 rhpfkpvpve dvlrnehvas
//
LOCUS       WP_175922725             347 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Burkholderia latens].
ACCESSION   WP_175922725
VERSION     WP_175922725.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..347
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38857
     Region          12..194
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(15,17,102)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(49,101..102)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            100..102
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mreslytplv slvvpfyneg eaverffdvv iplmsgldti rfeivcvndg srddtlerli
       61 rvsmgdrrvr vidltrnfgk eaaltaglde aagdavipld adlqdppsli pvmlehwrdg
      121 aevvaakrss racdsfakrt aaaiyyrvhn llsdvklpen vgdfrlmdrk vvnalrslpe
      181 rhrfmkglfa wvgyrtvive yqrdarsagh skfsgwklwn falegitsfs tvplrswtyi
      241 glgiaalafl ygtfivgrtl lfgnpvlgys sllsvvlfig gielvgigvv geyigriyde
      301 skqrpvylir rryqsqgkvv elpvardarr ttarrrvqpa rvrvgar
//
LOCUS       WP_175922731             147 aa            linear   BCT 11-JAN-2025
DEFINITION  TadE/TadG family type IV pilus assembly protein [Burkholderia
            latens].
ACCESSION   WP_175922731
VERSION     WP_175922731.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..147
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=15500
     Region          9..>94
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 msarhvplrq sraergaaiv efaliasili mlligifefg rvlfywntas eamrlgarta
       61 vvcdvnaagi akrvksmlpl lssanvsvgy tpsgcdissc sfvtvsvtnv tvktmipfvn
      121 vsikmppftt tlpreslnss tggaacq
//
LOCUS       WP_175922733             455 aa            linear   BCT 11-JAN-2025
DEFINITION  CpaF family protein [Burkholderia latens].
ACCESSION   WP_175922733
VERSION     WP_175922733.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..455
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50589
     Region          54..438
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mslreqmsly raqpqaagte pvtaahssvr dayqklrrei hlavlervel erlsrlsqdq
       61 vrqeisalia rildeqrlpa ndierrqlai dvydemfgfg pleallrdpg isdilvntyr
      121 qvyverggql eltdvtfydd ahlmkvieki vsrvgrride stpmvdarlp dgsrvnaiip
      181 psaidgplms irrfavnplk mddlvryhsl tppmaellda laqakvnvlv sggtgsgktt
      241 llnilsgfip rserivtied aaelqlqqph vlrletrppn iegkgeitqr tlvrnalrmr
      301 pdriilgevr gaealdmlna mntghegsla tihantprda ltrlenmisv ggltlppktm
      361 rqqiasaisv vvqatrltdg krkivsiqel tgmegdiinm qeiftfkrtg vdrdgtvrgh
      421 fcatgvrpkf aerlqafgin lpdslydpsq ryean
//
LOCUS       WP_175922735             172 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia latens].
ACCESSION   WP_175922735
VERSION     WP_175922735.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..172
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=18254
     Region          4..166
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 msdpvrmiin gepveadagd admslidflh errdltgtkl ccgigvcrac tvgvrnapga
       61 pmektlscst pvsamagmhv ytieglaqgg alsplqqsfl esfafqcgyc asgflmaata
      121 mldhlraqpv herdldamie twvggnicrc tgyvkyieai rkvaarytkg aa
//
LOCUS       WP_175922757             287 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia latens].
ACCESSION   WP_175922757
VERSION     WP_175922757.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..287
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30973
     Region          2..214
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mtilvtgatg rvgrhvvhql vergadvrvl vrdpskadfp aavavvqgdm ldldalrtaf
       61 tgvrtlflln gvagdeftqa lialnvarda giervvylsv mhadrfanvp hfavksgaer
      121 mieqagfsat ilrpayfmen ermvkdviag hgvypmpigs kgvamvdvrd iaevaaieli
      181 rrndapgklp vetinlvgpd tltgpqlasi wsevlgrpva yggddpaafe nnltsfmpkw
      241 mayemrlmae ryvtdgmvpl agdvarltai lgrplrtyrd faaalar
//
LOCUS       WP_175922784             433 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Burkholderia latens].
ACCESSION   WP_175922784
VERSION     WP_175922784.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 433)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 433)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 433)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..433
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=46384
     Region          <150..411
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mnepvaapgs mhdretraai darvdalfrs apipiliedw sgikrwvdtl kargvtdlda
       61 yldahpgvid evrrmhafvd andatlslfd aeskdaffaa aaqllpasrv snsqvlramf
      121 egrtscqger tlstltgrkv pivwrcslpa dgdayrrlhf yafdvteyke ngerldalra
      181 qlartarasm mgqlvasith eigqplgair taldaavrwl draepdipea taafrhasrw
      241 tddlanicrr lrgflagapv eaveldcadv vgsamqlvas eagahaitlt seiaagatay
      301 adriqlqqvl tnllingiha igaapadara pllrvragry ddthtlfeva dtgcgiassp
      361 pdaifqpfss tkrdgmgmgl pisksiveah ggtiwiddtg phgtrlcftl psseharrrp
      421 sdgaaavsaq agn
//
LOCUS       WP_175922804             343 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia latens].
ACCESSION   WP_175922804
VERSION     WP_175922804.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..343
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35995
     Region          63..314
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(77,160,162,164..165,192,246,267,270,283,285,314)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mknpsrhaiv araarlfvaa gcagllasaa faqadasaga hadarsapap vvgqqppgfy
       61 rqrigaftvi alsdgthpfp vdtvfrdisk keirrdldra fleppvqgsi naflvdtgsk
      121 rvlvdagagt lygdccgkll dslraagyap aqidevllth lhkdhvggia sngamtfpna
      181 ivranavead ywldpankar apaflasffd aaaaavapya aagrfktfrg eatlapgira
      241 vpmpghtpgh tayliesgna gmlawgdivh vaaiqlrdvn atvqydsdaa aarrtrrdtl
      301 arvaarrylv gaahiafpgl ghlrrdgary dwvpvnydat avp
//
LOCUS       WP_175922853             309 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175922853
VERSION     WP_175922853.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33365
     Region          11..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..293
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(106,110,149,163,165,229,246,273)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(107..108,112..113,115..116,119,123,125..131,192,
                     223..227,234..235,238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 msfdgrllsg msvlaavvea gsfsragevl glsasgvsrs iarleerlgv rlldrttrtl
       61 hltsegadly eraaphlegi eeaasyvsga avtvrgtlrv alnpvfaryv fapnlpllre
      121 rhpdldltiv qqpdvgdlvs egidvavrfg pqppstmtsr lllqtrvltv aspaylarhg
      181 rpkrpeklad hdciqyidpr rgkpftwefh rgrevlsvet nghltttdvd vmveacvags
      241 gvaqvlalnv rhllaggalv elfpewpget yplyvirpsr rlapaaveaf lefctsican
      301 vgdglpdar
//
LOCUS       WP_175922876             160 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia latens].
ACCESSION   WP_175922876
VERSION     WP_175922876.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..160
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=16730
     Region          83..145
                     /region_name="BON"
                     /note="BON domain; pfam04972"
                     /db_xref="CDD:428229"
ORIGIN      
        1 mtsrnrstnp llnlavavac gaaamyffdp asgkrrrayv rdkaaagrhg vadyaatqak
       61 raadhargai aglradwlag dandaqvter vraalghlvs hprdvdvtve hgnvrlsgqv
      121 eeterhavvd gvaalhgvka vedamgarse ykappggsmh
//
LOCUS       WP_175922878             559 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia latens].
ACCESSION   WP_175922878
VERSION     WP_175922878.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..559
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=62168
     Region          56..541
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mgadslhadq prgcdgrapd plrvggwlpm rmfrddepvd fvivgtgagg gtlacrlaeh
       61 gfsvvaldag awwrpleefa sdeshqrklf wtdericdga npltlgtnns graiggstvh
      121 famvslrfrp ewfrsrtllg ygvdwpldwr emwryyreve qalkisgpvn ypwgpprpry
      181 pyrahelnaa alvlargada lgidwtptpl atlsaprgra hpcvyrgfcv agcatnakqs
      241 alvtwiprav aagaevrdla mvlrieaegd rvtgvhyrrd grtrfqrarn vvvagyaiet
      301 prllllsang rhpqglanss glvgrymmaq lnqaswgtmd devrwykgpp slaitehwny
      361 adegkdffgg ycwmsqgplp iewarkvagr glwgdalkre marynfqagl kivgetlpre
      421 snrvtlader dafglpvarv tysyddndrr mmrhafaqmd rsleaagard iwheeddtch
      481 lagtarmgdd patsvvdadc rswdipnlwv cdgsvfptvg gvnpsltiqa iacrtadrir
      541 alvargeaqa rarwrrwpr
//
LOCUS       WP_175922925             235 aa            linear   BCT 11-JAN-2025
DEFINITION  PIG-L deacetylase family protein [Burkholderia latens].
ACCESSION   WP_175922925
VERSION     WP_175922925.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..235
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25718
     Region          6..>163
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mtvptrwlvi sphlddavfs cgqvlaqapg svvvtvfagi pprdtaappw drragfrtad
       61 eamrkrrded rralealdar pvwldflddq ygtraastdi aahladtida hpdfgvlapa
      121 glfhrdhlqv qqaalsllre harvggasrv wrfyedvpyr rieglmakrv igwrehgwva
      181 hpvaapagnr tggaaakaaa vdayasqial fephmradlr epeaywrlec ggtsa
//
LOCUS       WP_175922959             222 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator transcription factor [Burkholderia latens].
ACCESSION   WP_175922959
VERSION     WP_175922959.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..222
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24106
     Region          20..216
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mpeirmpsva lssedrggrv vyvvdddefv raaligllrs iglevyafas teaflaapkg
       61 ngpsclvldv rlrgqsgiaf qkslvenggp qmpiifmtgh gdiamtvkam kagamdfltk
      121 pfhdqemida vvaalerdak rleasqslld lrecwesltp rerevlqhva tglmnkqvag
      181 nmgiaeitak ihrgqamrkm kcrsvaelvr kmsalgievp vr
//
LOCUS       WP_175922981             348 aa            linear   BCT 11-JAN-2025
DEFINITION  microcin C ABC transporter permease YejB [Burkholderia latens].
ACCESSION   WP_175922981
VERSION     WP_175922981.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..348
                     /product="microcin C ABC transporter permease YejB"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042884 - microcin transport [Evidence
                     IEA]"
                     /calculated_mol_wt=37979
     Region          1..348
                     /region_name="YejB"
                     /note="ABC-type microcin C transport system, permease
                     component YejB [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4174"
                     /db_xref="CDD:443333"
ORIGIN      
        1 mfayllrrvv lmvptllgvv tlsfvvtqfv pggpveqmvm qlrrgavhge saasggyhgs
       61 qgvdpqqieq ikkqfgfdkp pltryglmla syarfdlgqs yfqhdsvwhv irarlpvsls
      121 lgcwtivlty lcavplgiak avrngsrfdt atsvlvlvgy aipgfvlgvl llmlfgggtf
      181 wdvfpmrglt sddfdsltpv gklldylwhm alpvtasvvg nfavvtiltk ntfleeigrq
      241 yvltarakgv prrhvlgrhv lrnaaipllt glpaafvgaf lngnllietl fslngmgqls
      301 ydaairrdyp vvlgslflft liglltklia dvcyvlvdpr iqfdsadr
//
LOCUS       WP_175923003             247 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia latens].
ACCESSION   WP_175923003
VERSION     WP_175923003.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 247)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 247)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..247
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25500
     Region          2..201
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mkivviggsg ligsrvvtll geaghqalaa sprtgvntit gegltdaltd advvvdvana
       61 pswepqavld ffrtsarnlg kaevaagvrh hvalsivgcd rmpengyfla kvaqeqaiea
      121 agvpytivra tqfmefiggi adagtadgtv rigdglfqpi aaedvsalva qialagphng
      181 tveiagpdra pfaeivaryl ksvgdtravv tdrdaryygg rveetslvpl gaarlgrigl
      241 gewlars
//
LOCUS       WP_175923006             303 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia latens].
ACCESSION   WP_175923006
VERSION     WP_175923006.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..303
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=33580
     Region          26..283
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mqnpqavpdy liqsdavrer farlkardvi ldvrhvgkrf atpqgecval ddisfrthrr
       61 efvcvigpsg cgkstliril agldaqtsge vlldgkpvdg pgadrgmvfq gytlfpwltv
      121 kknvmfglrm ngssssvaer ealqwldlvg ltrfadvyph qlsggmkqrv aiaralanrp
      181 rillmdepfg aldaqtrarm qthlldiwrn idvtilfith dldeaiflad rilvlkanpg
      241 gvqelievpv prprdysqvn tpefiatkar lealihpkea apaeddgikp hmirmtdvad
      301 nve
//
LOCUS       WP_175923024             293 aa            linear   BCT 11-JAN-2025
DEFINITION  glycine betaine ABC transporter substrate-binding protein
            [Burkholderia latens].
ACCESSION   WP_175923024
VERSION     WP_175923024.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Wolters,J.C., Berntsson,R.P., Gul,N., Karasawa,A., Thunnissen,A.M.,
            Slotboom,D.J. and Poolman,B.
  TITLE     Ligand binding and crystal structures of the substrate-binding
            domain of the ABC transporter OpuA
  JOURNAL   PLoS One 5 (4), e10361 (2010)
   PUBMED   20454456
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Gu,Z.J., Wang,L., Le Rudulier,D., Zhang,B. and Yang,S.S.
  TITLE     Characterization of the glycine betaine biosynthetic genes in the
            moderately halophilic bacterium Halobacillus dabanensis D-8(T)
  JOURNAL   Curr Microbiol 57 (4), 306-311 (2008)
   PUBMED   18661182
  REMARK    Erratum:[Curr Microbiol. 2009 Dec;59(6):65]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194542
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..293
                     /product="glycine betaine ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31737
     Region          33..292
                     /region_name="PBP2_OpuAC_like"
                     /note="Substrate binding domain of Lactococcus lactis
                     ABC-type transporter OpuA and related proteins; the type 2
                     periplasmic binding protein fold; cd13639"
                     /db_xref="CDD:270357"
     Site            order(41,43,89,117,152,156..157,203)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:270357"
ORIGIN      
        1 mnthtfksll aklavstvva csagvgavsa aepvkiavtn wadvlavanv akyvletqlk
       61 qpvqfvqadi giqyqgvarg dldimvggwl pvthgtyyak ykndlddvgv iytggkngwa
      121 vpayvpesel ssvadlnkpe vksklngtiq giepggglmq asektikayn ldgynlqass
      181 eagmlasvsr ayqskqwiva tvwsphwlfq kwqmrylkdp kgtlggeeqv hafaskkfag
      241 kfpradvffk hlkltladve aielegnstn dyataakkfv dahpdklkaw lqq
//
LOCUS       WP_175923169             339 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-quinone oxidoreductase [Burkholderia latens].
ACCESSION   WP_175923169
VERSION     WP_175923169.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..339
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=35576
     Region          1..333
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(40..41,127,131,134,157,160..162,181..182,186,201,
                     225..226,247..248,250,272..274,322,327)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mkaieitefg apdvlklaer prpepqrgev likvaasgvn rpdvfqrkga yapppgasdl
       61 pglevageiv ggdlsdaasn pfglklgdrv callagggya eyavaplpqc lpvpdgltdi
      121 eaaslpetff tvwsnvfdra llgageggeh etllvqggss gigvtaiqia halgfrvfat
      181 agnedkcrac ealgaerain yktedfvevv kslthdrgvd vildmvagsy vprelsalad
      241 ggrlvliall ggakaevnln eilrrrltvt gstlrprpve fkariaaqlk arvwplladg
      301 rikpviyrvl pageaaqaha lmesgehigk ivldwgana
//
LOCUS       WP_175923179             243 aa            linear   BCT 11-JAN-2025
DEFINITION  alanyl-tRNA editing protein [Burkholderia latens].
ACCESSION   WP_175923179
VERSION     WP_175923179.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V.
  TITLE     Evolution of aminoacyl-tRNA synthetases--analysis of unique domain
            architectures and phylogenetic trees reveals a complex history of
            horizontal gene transfer events
  JOURNAL   Genome Res 9 (8), 689-710 (1999)
   PUBMED   10447505
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Cusack,S., Hartlein,M. and Leberman,R.
  TITLE     Sequence, structural and evolutionary relationships between class 2
            aminoacyl-tRNA synthetases
  JOURNAL   Nucleic Acids Res 19 (13), 3489-3498 (1991)
   PUBMED   1852601
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Schimmel,P.
  TITLE     Classes of aminoacyl-tRNA synthetases and the establishment of the
            genetic code
  JOURNAL   Trends Biochem Sci 16 (1), 1-3 (1991)
   PUBMED   2053131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..243
                     /product="alanyl-tRNA editing protein"
                     /GO_function="GO:0002161 - aminoacyl-tRNA editing activity
                     [Evidence IEA]"
                     /GO_function="GO:0002196 - Ser-tRNA(Ala) hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004813 - alanine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006419 - alanyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=26170
     Region          3..243
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
ORIGIN      
        1 mttqalfred aymtqcdaiv aavgddgill drtvfyplgg gqagdsgtlt lpdgstiaia
       61 dtrkakfdga tpddavhvpd agqalraaal apgtrvvaqi dwlrryrhmr lhtaahlmca
      121 vlpypvdgcs vtadyvrldf atsdaidrvd verrlaalvh gahavttewi tdaemaerpe
      181 lvrtmsvkpp mglgrvrllr idgidlqpcg gthvrntsei galrvaklek ksartrrlvl
      241 efa
//
LOCUS       WP_175923199             365 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia latens].
ACCESSION   WP_175923199
VERSION     WP_175923199.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..365
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40077
     Region          9..335
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mangkptgri lviridflgd mlcttaflga lkqrwpdael hvvanrynaa alagnpdvha
       61 vhtyvysrqc erndrpgwmr affdrlrlvr rlrrlrfdlv vvpnggmhrs siqfarqlgv
      121 kdcrwhdads efddrkpehv atrpicheal sgfrlvpelg rtdldglals vhpdralqdt
      181 wyrllgartk prvglfvsnk aaerrwpadr wrelarrlap vadvivfrdp avpaaadaag
      241 dawrdvnarh vtpssvaelm aaaslldviv sadsapvhla salgvpvaal fedrpekylr
      301 whplgvphvi lragatvdai gvdaleravl hlltqaaqpd darrggtmpl paattaapei
      361 gaial
//
LOCUS       WP_175923223             455 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia latens].
ACCESSION   WP_175923223
VERSION     WP_175923223.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..455
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46796
     Region          19..447
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(26..27,30..31,34,66,116..117,119..121,124,144,
                     147..148,151,273,276..277,280..282,285,313,317,369..370,
                     374,378,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mnadtglplp qrywaivcva lgitlavldg aianvalpti ardlhasdaa siwivnayql
       61 avtitllpla slgerigyrr iyigglalft aaslgcalsg slptlavmrv iqgfgaagim
      121 svnaalvrmi ypssmlgrgl sinamvvals saigptvasa ilsfaswpwl favnvpigia
      181 avlgsvralp anplhdapyd fpsalmnacv fgllitavdg lghgerhayv aaelavafgv
      241 gyffvkrqls qpapllpvdl mripmfalsi gtsvasftsq mlafvalpfw lqhslgfsqv
      301 etglymtpwp lvivfaapla gvlsdrysag ilggiglalf aagllslati gahpgtadiv
      361 wrmalcgagf glfqspnnra mlssaprers ggaggmlsta rltgqtlgaa lvalifglap
      421 drgptialyv atafaavaav vsmlriaspr pdpat
//
LOCUS       WP_175923210             151 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia latens].
ACCESSION   WP_175923210
VERSION     WP_175923210.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..151
                     /product="VOC family protein"
                     /calculated_mol_wt=16478
     Region          3..135
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(3..8,24,62..63,66,83..88,90,94,123,133)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 mqvqpyltfy graeealqfy ekalgaktmf kmhfkdappn pdypiapema dkvmhasfti
       61 gesmimcsdg dcsqpagaah agyslslnpa tvdegqklfd aladggevtm pfgktfwalg
      121 fgmakdrfgv hwmvnvedls qreelakraq g
//
LOCUS       WP_175923236             434 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia latens].
ACCESSION   WP_175923236
VERSION     WP_175923236.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46958
     Region          24..425
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,156,
                     159..160,163,258,261..262,265..267,270,298,302,353..354,
                     358,362,378,381..382,385..386,389)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 matstqslpg ssgafeeaty rkvswrltpl lllcyvvayl drvnvgfakl qmasdlnlsd
       61 tvyglgagif ffgyflfevp sniilhkvga rvwiarimat wgvisiltmf vttpamfyvm
      121 rfllgvaeag ffpgvilylt ywypahrrgr mttffmtava lsgviggpis gfilkafngv
      181 sgwhgwqwlf llegipsvla gvlvffaldd rianakwltd dekallarnv daeeatkedl
      241 plgtvmsspr vwlmaliyfs fvmglygvgf wlptiikttg vtdtvtigll savpyaaavi
      301 amiliarsad rrrerrwhla ipaafgavgl vlsviwahet alamlgltla tmgilttlpl
      361 fwslptaflg gaaaaagiam insignlagf lspylmgwlk qatgtndagm ymlagflvlg
      421 gllalsvpkr lvdk
//
LOCUS       WP_175923261             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175923261
VERSION     WP_175923261.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32196
     Region          8..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..298
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,230..235,
                     241..242,244..245)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mpeptpdlrq wryfvtvade rhfgraaerl smtqpplsqa iraledalgv alfartkrsv
       61 altavgaall pdvrrllasa dalpplarrl argeagslsl afvstadygl lpsllrafaa
      121 rypqvrlqla eatsdvqide lvagridagl vippvpprha aglsylpvvr eplvvampaa
      181 aapdvpetep vhladlaalp lvifprrlap gfydiitgcy gaagetprig qeaiqmqtiv
      241 slvsagmgva lvpqslrnlr rtgvvyrpla gdaplvetgl vwrtgdvspv lagfidvvra
      301 hgaaa
//
LOCUS       WP_175923275             461 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia latens].
ACCESSION   WP_175923275
VERSION     WP_175923275.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..461
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=49052
     Region          161..437
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 menlqsrlls hrlasvirdf hqpvmiwqaa ilvgalgiaw vvarfvhgri darrraagra
       61 pgagaqslkr alfplfggvf vgiaqlafep fmstslllla lvplfgigli yvlfffarrv
      121 fardghthaw lsivekivst vvwvamvltv lgiqrdvlgw ldsvqfrvan ahltllsvis
      181 galwvcmtlm vamwlgsvle erltrattld anlkvvlsrv grallvfaai liglslvgid
      241 vtvlgvfgga vgvglgfglq kiasnyvsgf iilldrslrl gdaisvgglq gvvtqirtry
      301 tvvrgldgne tlipneklit dvvqnqssyl trgyakaavq vaytsdveqa lallaqaang
      361 vprvledpap tpylvgfgad gidlelgfwi edaakgtsgv rsavnrniwr lfsehgvsip
      421 fpqrevrvvg lpegfaatgv vadgvpvagd ggdvasrasa a
//
LOCUS       WP_175923268             309 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175923268
VERSION     WP_175923268.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33667
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..294
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdkldqvrif lqvaelgsfi kaagaldvpr atvsaavqql esalgtrllh rttrqvqlta
       61 dgalllergr rllaeadeld rlfrrrdrdv igrlnvdaps riarrviapa lpslfcrypk
      121 lqlslgstdr sidlvqegvd cairvgrlad sslvvrplgq falincaspg ylrecgvpeh
      181 pdalahghwa igyaspttgr eleweycadg grhaltlpsr vivnnaetyi asciagmgli
      241 qiprfdvvhl ldsgalvevm pghraapmdv savyphrrhr srrlnafvew fgelmkdaln
      301 dtgaagsgd
//
LOCUS       WP_175923315             472 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia latens].
ACCESSION   WP_175923315
VERSION     WP_175923315.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..472
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50755
     Region          8..462
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mqpegqfqhi aarehglrrt lsarqmamia iggaigtglf lgsgfaigfa gpsvlvsyai
       61 gafislllmg claemtvahp tsgsfgayae hyvspwagfl vryaywaciv lavgtevtai
      121 alymkywfpg vpgwlwivgf sallvfvnar svdvfgavey gfsvvkiaai vgfivlgayv
      181 vfadpalvgd gaaragfhhy tghggffpkg mwgmwvaviv sifsylsiem iavaageaed
      241 peravtrafr stivrlvlfy lvtlalmlai vpwtaagrde spfvkvmeai rlpgaaglin
      301 fvvliaalsa mnsqlyittr mmfslsragy apkalgdvna rgvpfgalll stlgialatv
      361 lsvlypdasf timmavsmfg alftwmmifv thycfrrrra alglpapafr mrgfplltll
      421 gaalmlavmv ttcftaefhm tlifgipfli alsvvyavwy rraqpalqpe ak
//
LOCUS       WP_175923321             324 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Burkholderia latens].
ACCESSION   WP_175923321
VERSION     WP_175923321.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..324
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37500
     Region          134..275
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mlhlidafvs diqtwlyvdv vqpllfkfnl mdydedtyda lywviigalq mvlmfallrp
       61 lealapverw knrravrvdv iytaisklgi ytlffffalq pvfdrfqawl rlhgvsnfnl
      121 dylwpgvtsq pivafaiylv vldfagywyh rwqhkfgvww elhavhhsqr qmslwcddrn
      181 hllddviqsc ffaaialvig vtpsqfvvlt altnflqsiq htnarlsygr lgerllvspt
      241 fhrrhhavgy ghegtkygcn fgvlfpwwdm mfgtaswnrt veptgireqv egvsygdgfw
      301 aqhglafvri frrlvpakrg aasa
//
LOCUS       WP_175923333             240 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: (Fe-S)-binding protein [Burkholderia cepacia
            complex].
ACCESSION   WP_175923333
VERSION     WP_175923333.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..240
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25834
     Region          <2..237
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mrvglfvtcl vdlmrpeigf salklirdag yevfvppaqt ccgqpaynsg dralardlae
       61 ktlrefeqfd yvvapsgscg gmirahygdl frddpelmgr yvrfqqkvye ltdflanvak
      121 vtlapgefag pvtyhdscsg lrelgvkaqp rallaqrgva vtemkdcehc cgfggtfavk
      181 ygdisaaiad ekcanvrasg agavvlgdlg cmlniegrlr rtgdrdtrvl hvaqvlagdv
//
LOCUS       WP_175923369             512 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia latens].
ACCESSION   WP_175923369
VERSION     WP_175923369.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..512
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54458
     Region          34..442
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mtssintspl naiadqalgl daaapaaaep asdeptfasl glspeivsal qaagyakptp
       61 vqqraipagi agrdllvssp tgsgktaafm lpaierfaql qkaqaqqpra prepnqgdrr
      121 arrpqpvarp gllvltptre lamqvttaas tygkhlkrlr tvsilggvay gqqlmllakn
      181 peilvatpgr lldhlergri dlselkmlvl deadrmldmg fiddietiva atpesrqtml
      241 fsatldgkig sltsrllkdp erieitakie sraniaqtvh yvddrdhkdr lldhllrdda
      301 ldqaiiftat kidadqlagr ladagfqsaa lhgdlpqgar nrtiralrer rvrvlvatdv
      361 aargidipgi thvfnydlpk faedyvhrig rtgragrsgt avslvhhaeq galkrierfv
      421 rsplpvnvie gfeprkappr neraggrgrp gggnggrrfg gkpgggysgn ggrsygggng
      481 ggwsgkpggs rdggprrdgq rsggprrsns as
//
LOCUS       WP_175923398             234 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175923398
VERSION     WP_175923398.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..234
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25186
     Region          4..224
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mrnmnepdss psgaagpeei aerirtaile hrlapgaklt eaqlcdvfgv krgtirqala
       61 qlatdklvdl epnrgafvas ptlqdvhevf emrriielav verlatgpga krlkgvaali
      121 dkerraferh dfaawirlsg efhtalaalv gnatlceclg glvarstlms alyeshgrsp
      181 csfddhgeil aaleagdakr aaalmahhlq hvelkmldrp aqgqvdlrev fgga
//
LOCUS       WP_175923404             297 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia latens].
ACCESSION   WP_175923404
VERSION     WP_175923404.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..297
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=29886
     Region          1..287
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mevgfcgpgl mgapmirhll aaghrvsvwn rtrtkaeale hdgaevvdtp relaervdtv
       61 fvcvldgrav gevvfgehgl lagaanirrl krivdhssia paatrayaar aaalgvgwid
      121 apvsggvpga qagtlavmag gavadldavr plidtyasri thmgdagagq taklcnqavv
      181 tatvtaiaea vglaqasgid aarladalag gwadsvllqt fvprmtsggh ppigalatfq
      241 kdvdaiadaa rdtgavmpvs atvqqvlrlg aaqglagadf aafidivrpg ngrgaap
//
LOCUS       WP_175923420             381 aa            linear   BCT 11-JAN-2025
DEFINITION  glycerate kinase [Burkholderia latens].
ACCESSION   WP_175923420
VERSION     WP_175923420.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..381
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38473
     Region          10..376
                     /region_name="GlxK"
                     /note="Glycerate kinase [Carbohydrate transport and
                     metabolism]; COG1929"
                     /db_xref="CDD:441532"
ORIGIN      
        1 mphhpsapvv viapdsfkgs lsaeqvadai atgirrarpd avvrccpmad ggegtldaml
       61 agggtrrtlr vagaslaard aavgvidars aivetaeivg itdavgmsvp vdarstrgmg
      121 eairmlldeg vrrffvalgg sstndagagl laglglrcfd aagnpvepvp arladiaqvd
      181 asaldprlke aefigmsdvd npltgahgat avfgpqkgvt peqvatldaa lgrfadllea
      241 aldrrgrdla gagaagglgf alhmlgaqfe agaevvarqv gldaalagad wlitgegrsd
      301 vqtlhgkapf vacrharaag vpasllsgai dpaalprlse hfsgcfspap gpitldvair
      361 daanllanea eqltrlkyga h
//
LOCUS       WP_175923495             297 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175923495
VERSION     WP_175923495.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31138
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176112"
ORIGIN      
        1 mtpdqlitfa avaehlnisr aavalhlsqp avsgqlrllq defgeplyqr dgrgirltpv
       61 geqlaqyana qrdafaqara frdavrglda gtlrigastt pasyllpyli aafqpraprv
      121 aiqtmsgnta dvvaalasld iamiegppge alppgtavha whedeivavv paghplaapd
      181 hdagvtldal aahpvvlree gsgvrqlver afahggtpir valeiagvea vkeavragmg
      241 vgfvsamslr heddalvprs lapepltrhf silvphgaap srvaaqflem slahdpk
//
LOCUS       WP_175923500            1049 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia latens].
ACCESSION   WP_175923500
VERSION     WP_175923500.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..1049
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114629
     Region          11..1027
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mtgpreegrf nlsawalrhq alvvyliala tlagilaytr laqsedppft frvmvirtfw
       61 pgatarqvqe qvtdrigrkl qetpaidflr sysrpgesli fftmkdsapv kdvpetwyqi
      121 rkkvgdigyt lppgvqgpff ndefgdvytn iwtlegdgft paqlhdyadq lrtvllrvpg
      181 vgkvdyfgdp dqrifievnn aqltrlgisp qqlgqainaq ndissagvlt taddrvfvrp
      241 sgqfdnvaai adtliringr tfrlgdlatv krgyddpqvt qmranghavl gigvtmqpgg
      301 dvirlgkald aesktlqaql paglkltevs smphavshsv ddfleavaea vaivlvvslv
      361 slglrtgmvv visipvvlav talfmylfdi glhkvslgtl vlalgllvdd aiiavemmav
      421 kleqgysrar aaafaytsta fpmltgtlvt vsgflpiala ksstgeytrs ifevsaiali
      481 aswfaavvli pllgyhllpe rkkhaheahl pddhehdiyd trfytrlrgw idwcierrfv
      541 vllitgalfv vallgftlvp qqffpssdrp ellvdlrlpe gasfaatlre terlekvldk
      601 rpeidhsvnf vgsgaprfyl pldqqlqlpn faqfvvtaks vedreklatw lettlrdqfp
      661 avrwrlsrle ngppvgypvq frvsgddiaq vrsiaeqvaa tmrgdartvn vqfdwdepae
      721 rsvrfeldqk karelnvtsq dvssflamtl sgttvtqyre rdkliavdlr aprpdrvdpa
      781 klaglalptp ngpvplgslg rftptleygv vwerdrqpti tvqsdvraga qgidvthaid
      841 gklntlraql pvgyqvnigg sveesakaqs sinaqmplma iavftllmiq lqsfsrvlmv
      901 vltaplglig vvgtlllfgq pfgfvamlgv iamfgiimrn svilvdqieq diaaghgrfd
      961 aivgatvrrf rpitltaaaa vlalipllrs nffgpmatal mggitsatvl tlfylpalya
     1021 awfrvkrder dphdgpppgg stpaapsga
//
LOCUS       WP_175923557             214 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia latens].
ACCESSION   WP_175923557
VERSION     WP_175923557.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789896
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..214
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23058
     Region          9..214
                     /region_name="COG2945"
                     /note="Alpha/beta superfamily hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:442188"
ORIGIN      
        1 mnvhtqksli agpagqieia vdvpdavreg saaprgialv ahphplfggt mdnkvaqtla
       61 rtlvqlnyvv yrsnfrgvga tegvhdngig eaddllavla hmraqpayad lplvlagfsf
      121 gkfvlshvak rlrdaggtie rmvfvgtaas rwqvadvpen tlvihgetdd tvpiasvydw
      181 arpqelpvvv ipgaehffhr klhvlkriiv dawr
//
LOCUS       WP_175923605             396 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia latens].
ACCESSION   WP_175923605
VERSION     WP_175923605.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..396
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=42185
     Region          18..381
                     /region_name="MidA"
                     /note="SAM-dependent methyltransferase, MidA family
                     [General function prediction only]; COG1565"
                     /db_xref="CDD:441173"
ORIGIN      
        1 mnpkahepas lpapgpdala qsetlaaqlr deiaaaggwl pfdrfmeral yapglgyysg
       61 garkfgrrad dgsdfvtape lsplfaqtla npvaealaas gtrrvmefga gtgklaagll
      121 aaldalgvel deylivdlsg elrerqreti aaaapalaak vrwldalper fdgvvvgnev
      181 ldampvrlfa kaggawlerg valdarhafv fddrpvdaag lppmlatldv ddgyvtethe
      241 aalaftrtvc tmlgrgavll idygfpahey yhpqrdrgtl mchyrhhahd daflypglqd
      301 itahveftgi ydagiatgad llgytsqarf llnagitdal aaidpsdvhq flpaanavqk
      361 liseaemgel fkviafsrgi dgtldafarg drshal
//
LOCUS       WP_175923612              66 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy-metal-associated domain-containing protein [Burkholderia
            latens].
ACCESSION   WP_175923612
VERSION     WP_175923612.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 66)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 66)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..66
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6655
     Region          1..62
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mefevqdmtc ggcanaiara vtaadpaakl didvaakivk vesaqgaerv qsiieaagfh
       61 palrsa
//
LOCUS       WP_175923614             260 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia latens].
ACCESSION   WP_175923614
VERSION     WP_175923614.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..260
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=27041
     Region          9..242
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 merkplvglt adstqigaha shtvgdkyva aivdgarafa mvlpalgerq svddvlatvd
       61 gllftgsysn vephryggep sapgtkhdpa rdattlpllr aaiaagvpvl avcrgfqeln
      121 vvcggtlhqr vhevpgladh redddapmdv qygpahvvhl mpggvlhala ggrddvrvns
      181 lhkqgiaqlg sglaveavap dglieavsvv dapafalgvq whpewrhahd alssaifraf
      241 gdacrarrda rtraaaaala
//
LOCUS       WP_175923643             546 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia latens].
ACCESSION   WP_175923643
VERSION     WP_175923643.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..546
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58460
     Region          1..533
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mqydyiivgg gsggssvasr ladacpdati alieagshte rnllvnmpvg iaalvpfklg
       61 tnygyetvpq pglggrrgyq prgrgmggss ainamiytrg hpgdydewaq lgatgwgwqd
      121 vlpyfrraeg nergadawhg adgpltvsdl rfrnpfserf iqaahaagyp lnhdfngatq
      181 egvgfyqvth rdgsrcsvar ayiygrnrpn lhvitdatvl rvgfdgkraa gvvvsrdgrv
      241 etlgaraevi lsagafnspq llmcsgigpa eqlrrhgiav vhdapdvgsn lidhidfiin
      301 trvnsselvg iclrgiakmt palaryfssr tgmmtsnvae aggfiksdps ldrpdlqlhf
      361 ctalvddhnr kmhwgfgysl hvcalrpfsr gtvalasgda rdaplidprf fsdtrdldll
      421 vrgahamrri lsqaplasqg grelytrpdq seeelrativ ahadtiyhpv gtcrmgsdar
      481 avvdpqlrvr gveglrvvda svmptliggn tnapsvmige raadfivaar qggvprgeaa
      541 aavhgr
//
LOCUS       WP_175923633             276 aa            linear   BCT 11-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Burkholderia
            latens].
ACCESSION   WP_175923633
VERSION     WP_175923633.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..276
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30340
     Region          13..268
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 msadalslpf aephaapdei tavswnlhkg rsplgftawn amrnwmqsth advyflqeam
       61 arrmprpmla agfgapmdda vddvwhcqat eiaqaldwqi algpnvfkps wrhgnailsp
      121 hpldlggrwd isahrferrg llvaratlag srpvtllcah laltraarlr qmhwiahwiv
      181 rnagddplvl agdfndwrnd svalfgeigl sevatllges grtfpafspa laldkmfvrg
      241 ltplewqaps getawlsdhl pyiarlrldp appaaq
//
LOCUS       WP_175923711             561 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia latens].
ACCESSION   WP_175923711
VERSION     WP_175923711.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..561
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=60951
     Region          10..546
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mttqrtlege fdyvivgagt agcvlanrlt edpeirvlll eaggkddyhw ihipvgylyc
       61 ignprtdwly ktqpeaalng ralsyprgrv lggcssingm iymrgqredy dswaqetgda
      121 gwswdsvlpi fkrsedhhag asgahgaggy wrvekqrlrw eilesfaqaa qqtgipatdd
      181 fnrgdntgvg yfevnqkrgv rwntskaflk pamtrpnltv itgahaqrvi fdgrravgve
      241 yhgggtgyva raraevllts gavnspqlle lsgvgdgarl qalgidvvhd lpgvgenlqd
      301 hlqlrmafrv egvrtlntls ahwwgklmig aeyallqrgp msmapsqlga faksdpddpa
      361 ltrpdleyhv qplsldrfge plhsfnafta svchlrpssr gsvhiaspda gvaptiapny
      421 lstdhdrhva analrltrri asapalaryr pqeilpgtqy rteaelvdaa gavgttifhp
      481 vgtcrmgrad deravvdsrl rvrgiaglrv vdasvmpfit sgntnsptlm iaerasdmir
      541 adrraaqeaa qvrkeaavtv a
//
LOCUS       WP_175923726             476 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia latens].
ACCESSION   WP_175923726
VERSION     WP_175923726.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..476
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49423
     Region          36..476
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mqsldtdaaq gghgtaplag aaleaalvaa lgdalvtrsa didpryftay nepagvrpra
       61 lvrprsvddv srtlalctrl gqpvvpqggl tglargaval ggeivlsmer fagvdaidaa
      121 agtmtvragt plqtvqeaad sagftfgvdl gargscqigg mlatnaggtr airygmmreq
      181 vlgleavlad gtvvssmnrm lknnagydvk qlfigsegtl gvitravlrl hpklaepata
      241 lcrvrgydav vglwnrlral peivsfeamw pafydyvarh tpgvaapfas dgafavliec
      301 atsapggdar aaletalada fdagliddaa latserqard lwtlreglai dalphlanfd
      361 vslptgelga faarceaalr ehwpgiaclf fghvgdgnvh igvsladmrd adadaiddcl
      421 yavvrdmggs vsaehgigvl krrylahars daeialmrrl kaaldpagvl npgkvl
//
LOCUS       WP_175923727             190 aa            linear   BCT 11-JAN-2025
DEFINITION  PadR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175923727
VERSION     WP_175923727.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..190
                     /product="PadR family transcriptional regulator"
                     /calculated_mol_wt=21087
     Region          5..97
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          <48..175
                     /region_name="AphA_like"
                     /note="Putative AphA-like transcriptional regulator;
                     pfam14557"
                     /db_xref="CDD:317018"
ORIGIN      
        1 msasrpspla lavlatltes pmhpygmlqq lkarghdeav nvrqrtslyq tidrllrdgl
       61 iavhdterdg afpertlytl teaghtagqa wlhallaepa refpafgagl aflplldand
      121 arhqlerria aleaererle alrnaaqndq vprlfllqne halvllnael dwvrsvvehl
      181 kigalrwvdg
//
LOCUS       WP_175923780             211 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia latens].
ACCESSION   WP_175923780
VERSION     WP_175923780.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..211
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22397
     Region          1..211
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mnlhtwwlfv atvfvvsaip gpnmllvmth garhglrrss atmagclsal vlmlavsaag
       61 lgavleawpa mfntlrfaga ayliylgvka wrarvddapa advdavshgv sasrwtlfrn
      121 gflvagsnpk ailfaaallp qfinaaeptl pqfgvlvvtf aaievswylv yasfgtriga
      181 tlksqsvarl fnrltgslfv gfgammalvr h
//
LOCUS       WP_175923768             404 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia latens].
ACCESSION   WP_175923768
VERSION     WP_175923768.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..404
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40548
     Region          31..398
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(41..42,45..46,49,81,131..132,134..136,139,158,
                     161..162,165,233,236..237,240..242,245,273,277,326..327,
                     331,335,351,354..355,358..359,362)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 msesssrsss dfaappdahr mlalpvrqra rtatmalffv agmmyaswgv hvptvrdkfa
       61 lspgllsial favaggsiaa mltiarwiar vgsrtacvag glvmsacaav ilvvpdywml
      121 lvvlalfgfs matldvamna easavelalg kpimsslhgm fsiggmsgaa aggallsagm
      181 apavhlalaa alnaavllaa spavlphvph hdhahgggnr wrsaalwmlg gialvaliae
      241 gamydwatvy mrdvvaaspa lasaayaafs ggmaiarfag davrarfgap qlvfasasla
      301 cagmigalll pnavavltgf tlmglglanm mpvlfaaaar vkgihaaegl ahvaglayfg
      361 llfgpvvigg vaqtagltvg lsvvalcaal iavvapkvla llki
//
LOCUS       WP_175923792             158 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia
            latens].
ACCESSION   WP_175923792
VERSION     WP_175923792.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..158
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17033
     Region          11..146
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtaklnpfav apalmknwma vsvaaagsle ptlielvkir asqinacanc lnmhtveare
       61 qgeteqrinl laawreapcy tdreraalgw tdaltrlseg hgaleaaysa lndhfsqeeq
      121 vkltlminvi ngwnrlavgf glwvdpaeak aaaakmva
//
LOCUS       WP_175923798             492 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Burkholderia latens].
ACCESSION   WP_175923798
VERSION     WP_175923798.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..492
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51959
     Region          3..487
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mhsdylahda iglaalvrer kasprellda aigqaeavng avnaivlqdy daarkrtesa
       61 haaapdapfa gvpylvkdlg aavaglplsm gsrhyryfvp addspviars raaglnvfgk
      121 tntseigqmp ytepelfgac rnpwnldhtp ggssggaaaa vaagivplah asdgggsiri
      181 pasccglfgl kpsrnpllvd lpsngelvvq havsrsvrds allldvttgq tlppgapgtf
      241 vgaldtppgp lriglvtdpm lapaldddtr aalddaaalv eslghhvepa tlhidrarta
      301 etfltlwati aeemvlgara ltgrtpkrae fepatwamav vgrrvararl advlewqrql
      361 tvqvagvvsr ydailcatla gppvkigelq psaleaaqmk llgalpvkpl lremlarsse
      421 kafawagcte lfnltgqpam svplywnarg lpigvqfvar haddalllkl arqleqarpw
      481 fdrrpplmqa qr
//
LOCUS       WP_175923802             171 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175923802
VERSION     WP_175923802.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..171
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19099
     Region          4..159
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 maqveldaid rrilailqen grlsnqeiae rvnlspspcl rrirrleemg vitgyvalld
       61 pqklgldlla yvsvrlekrg gvapvrtdet varagathae lfraavqtwp evvachamtg
      121 dmdyllrvqv edmahfsrfv qehllhhpsv idvktsfsle cfkettalpi r
//
LOCUS       WP_175923815             218 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia latens].
ACCESSION   WP_175923815
VERSION     WP_175923815.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..218
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23684
     Region          7..192
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mpqdrhltly hsprsrsaga rmlleelsah yelhafdlsa gkhheadyla inpmgkvpal
       61 rhgdvivteq aavymyaael yseaglspap gdalrgpyls wmtfygscle pavvdrsmnr
      121 ppaaystspy gdfdavihai daqlakgpyl lgerftaadv lwgsalnwtt mfklvpetpl
      181 irayidrvla rpaiqraqaa daalaaeqdk akeataak
//
LOCUS       WP_175923830             318 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175923830
VERSION     WP_175923830.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..318
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35069
     Region          11..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrkfkipnmg alvafeaaar hesfthaake lfltesavsr qiatleaslg vrlfarvkqr
       61 vvltragkly gtqvrralea ldrdtlsiia hgsgggylel avlptfashw lipriksfyd
      121 rtpdvrvnmg srtdlfsfed thfeaaihyg kptwpgtssd ylfgeevvpi cspallngpv
      181 ervedllayp llhsttrpga waqwfdahgv ddirtmqgvr yelhtmlisa aaaglgialv
      241 pkffveeqlq qlglvvpcda atvgdsayyl vyptefshsk plelfrawll eqasayaapg
      301 qdahdadded deddedve
//
LOCUS       WP_175923843             307 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia latens].
ACCESSION   WP_175923843
VERSION     WP_175923843.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..307
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32862
     Region          92..297
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 matanrtdvs piarrkpkap slrvrlgrra frvlnafaph aagrraadaf gftrgyglav
       61 sdrvplgake afidgnedid raycwdggas rvllvhgwgt dsssmlsfvk pmqalgfsva
      121 afdapahgrs pgkhttmtqf tratgavlda idgaqvviah slgsiaavsa laersrrasl
      181 rcivliapts gltevlerwa srdmalprpv iervyaelqr rngvpvshwd ilargasldv
      241 pvlvvhdpad avvpyceaqr vvaglqeatl wpapgaghgr ilsdarvreq vcefvtrqts
      301 nfgelar
//
LOCUS       WP_175923872             337 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175923872
VERSION     WP_175923872.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..337
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35746
     Region          3..61
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..287
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 melhqleafs avmsagsvtg agellgrsqp avtrqiqele adlgyalfdr hgprvtptrr
       61 afllyeever slvglraiea raralgaeaa epvriaatps laatlvpaal aalpddahap
      121 hyqlrsesae hvvhevlagt adigvvtlpi ahagldvhwi aqtpcvavlp addplaskpr
      181 ialrdlarrr ivtvanrhrl rqridaafaa arvdarvfve tnaslnavma aragigigiv
      241 dpatgvalpv dgvvarpldv dipfafgvat pagktrtaav dalldalhrt trtllddvvf
      301 hdasvhdall rgdrlrsdrp sraarptrta rtrqeta
//
LOCUS       WP_175923874             603 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia latens].
ACCESSION   WP_175923874
VERSION     WP_175923874.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 603)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12379621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..603
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62859
     Region          1..289
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
     Region          329..603
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 maswldytln glivgniyal lavglalifg vshlinfahg svymvgafig wlcltrfglp
       61 lpialaavvv gcgalgiaie riglrplrha ariapllati gisfildqla qlafgadpra
      121 vptplpdwhl riagatlgsl dlliagigia aaallygflr ftrlgwavra taqdrdaalq
      181 mgvdvdrvnq tvfaiacalg gvsgllvgmy ynsidpamgf qatlkgvval ligglgnvpg
      241 aiagslllgl vesygvalfg tsyrdlfafg llivflvwrp nglfsakral ppepmtgtfl
      301 aaakavrvpr pmlaalivla avlpwlgasp yvlqtltnaw lygllalslt lvagtvgqis
      361 lghaallvig ayasallssd lgwspavtip cagaitavlg tllvypafrl rghyvsiatl
      421 gigevvslvi lnwdgltrgp lgitgivplp watsaraayw ftlavlvafa lvqlrllrsh
      481 lgrtlravre ddvaarahgi apnrykaiaf avggvaagvs ggiaahlysy inhqtfdsqv
      541 silaltmvil gglgnvlggv vgaialiglp elfrwaadyr mliyglvlll lvrfrpqgll
      601 gtv
//
LOCUS       WP_175923877             341 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia latens].
ACCESSION   WP_175923877
VERSION     WP_175923877.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..341
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36579
     Region          11..324
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mltsarrrtm laaglgmlga lgapslvrak prtvriskgy gvlylpllvm ekqrlferha
       61 arhglrdvav ewvlldggns vndammagtl dfagagapgf ielwarargi pnvevigisg
      121 lsttslslna nrpglaslrd ftpsdriavp girtslsavv lqmvasrqlg arhfaqldsi
      181 tvnlphpqam qalirresgv tahftsppfs tlelrqpgvh rvvnsidvlg pmtldvvfap
      241 krlvdaepal asaflgalde anrliaqdpr taaalyaass gvgvshddvm rmlaapdtrf
      301 svrpnqlmdy veflylagti kakprawhem fapmlddypt g
//
LOCUS       WP_175923908             208 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia latens].
ACCESSION   WP_175923908
VERSION     WP_175923908.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..208
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21849
     Region          1..197
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mnilhidfsp raeshsrqls aavvrkllev vpgtsinrrd fgavplphat pgyatalstp
       61 atlanppkas ldlsetlird vetadvivig tpmnnftips vfkawidhvl rvgrtmkstp
      121 tgkvgllrdr pvfigvaagg ifsgehanqp dfltpylsaa fgciglntlk flpvqgtafl
      181 spdqaasaie qalaaidvss iravasgr
//
LOCUS       WP_175923878             437 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia latens].
ACCESSION   WP_175923878
VERSION     WP_175923878.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..437
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47266
     Region          24..423
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(37..38,41..42,45,77,127..128,130..132,135,155,
                     158..159,162,257,260..261,264..266,269,296,300,350..351,
                     355,359,375,378..379,382..383,386)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnattetldp asaeeqrims kmarrllpil vvmfliafid rqnvgfaklq mvhslgmtea
       61 afglasslff igyllfevps tlalhrygar vwlarimltw glitvlmgft tsmpafcslr
      121 fllgiaeagf ypgviyyltl wfpqsyrakv lgiftlgsal anmlgslvgg vllslngvwg
      181 lagwqwvfva tglpavivai vvfrvlpasf reapfldere kqivaaaler ekpahaehaq
      241 pwkalldprv mlfaatymlm stslygvtyw lptlvksfgv ssttngflsm lpwalavvll
      301 vwlpsklrra ksilrtiaiv aalgalgfll slvlpstplr fialvlggac ipllypcfws
      361 mppryftgar aaasvaains ignlggffsq nlmpfagkat gtafgpmivp ivclallgig
      421 alvawtrser gmvaara
//
LOCUS       WP_175923907             181 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia
            latens].
ACCESSION   WP_175923907
VERSION     WP_175923907.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..181
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /note="This protein belongs to a clade of uncharacterized
                     proteins related to peroxidases such as the
                     alkylhydroperoxidase AhpD."
                     /calculated_mol_wt=19229
     Region          40..177
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 martavltpe qvpaeskatl aaftknigft pnmmasfaqs piafnawatl lgalskaldv
       61 ktrdsiglav sevngcnycl tvhsmtaehm aklpadeiil arkghatdpk rdaavqfark
      121 vietrgkvgd adlkavreag ytdanvmeiv alvamysltn ffnnvfdpeq dfpavppags
      181 i
//
LOCUS       WP_175923940             136 aa            linear   BCT 11-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Burkholderia latens].
ACCESSION   WP_175923940
VERSION     WP_175923940.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10577308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..136
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=14408
     Region          21..>80
                     /region_name="SnoaL_2"
                     /note="SnoaL-like domain; pfam12680"
                     /db_xref="CDD:432716"
ORIGIN      
        1 mntaqtaqsa qsaqsahael idryfdawne pdaaarrali datyasdaay rdplmagdgh
       61 agidamiaav qerfpayrfh rttdvdgfgq hlrfswalvs pdgaaivkgs dfgtvdasgr
      121 lksvtgfide mpaavs
//
LOCUS       WP_175923954             598 aa            linear   BCT 11-JAN-2025
DEFINITION  fatty acyl-AMP ligase [Burkholderia latens].
ACCESSION   WP_175923954
VERSION     WP_175923954.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10148874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..598
                     /product="fatty acyl-AMP ligase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=64030
     Region          25..588
                     /region_name="FAAL"
                     /note="Fatty acyl-AMP ligase (FAAL); cd05931"
                     /db_xref="CDD:341254"
     Site            order(186,189..194,196..197)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341254"
     Site            order(213,233..235,309,312..315,340..344,349,392,462,473,
                     476)
                     /site_type="active"
                     /db_xref="CDD:341254"
ORIGIN      
        1 magsilpsal paerttssll dilreraeht periafhflr dgeddvvsws ygqfaaaavh
       61 vrnmvlqhal herrvlllle pglsyvaalf gillagatav psfppagsra varfasicrd
      121 arpdvviagk hhrslqqeld glhggeraap alltideraf ddidtsahdv rsllaegvdp
      181 drpallqyts gstgepkgvi vthanlvsnc aviaerlgdd parvgctwlp pyhdmglmga
      241 lllavfsgfp lvilspqhfv qrpyrwlkai tdyrvttsva pnfafdlcvd nisdeeaatl
      301 dlgslqhvfc gaepvshttl erffarfgrh gfarsavvpc ygmaeatlyv sgkvgrspit
      361 lidvdkeala rgvcephdpq sdargrttlv gcgpvaaghr llivdpatqr vlpertigei
      421 wfsgpnvaag ylgradsadv faaaisggrg dddscrylrt gdlgflnhge lfvtgrikdv
      481 vivagrnlyp tdiersvqsa hdairtngvv afsidggpte slvivaelkr srrlspeqmr
      541 evraaitsav trdhgvapav vhlgptgaip lttsgkvrrq ackqafqqgs lstldara
//
LOCUS       WP_175923955             394 aa            linear   BCT 11-JAN-2025
DEFINITION  thiolase family protein [Burkholderia latens].
ACCESSION   WP_175923955
VERSION     WP_175923955.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 394)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..394
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41056
     Region          4..394
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mvarqvvics pvrtpigafg gtlkdvaama lgavalreav hrsnvdpaal asvvmgnvvq
       61 agnkmnparq aavaggipva vpaftvnrvc gsgaqaivna aqeiwlgfge vaaaggmesm
      121 erapylldsg rwghrmgnae ivdsmlgdgl vdafsnrhsg whtedlvsam gitreqqdrw
      181 aersqkrfad arergafdae lvaveidgrk qtvrferdeq prpdttfesl aklkpafrsd
      241 gtitagnapg lnsgaaamiv aerryadthg iepiatlvay gvgavepgmf glgpvpavrm
      301 alaragwsls dverfeinea faavpiavvr elgidealvn vegaaiahgh aigatgavlt
      361 trlahsmrrd gikrgivtlc igggqgiaia leaa
//
LOCUS       WP_175923958             318 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175923958
VERSION     WP_175923958.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..318
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34598
     Region          5..194
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          228..311
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msqvdslsql lqmititgql elrcgsgspw qlawaraaah eipyhvvlkg ravledvgtg
       61 sirelvcgdi vllphgsahv lhdgsrhqrr qlgnrhgasv rfrgghdshg erldllcgrf
      121 firpphdrli rdylpttltv ryvagdrdgd ngsashqlas lvdlmrmvsv gakpggrail
      181 naltsalftl vlraasetgq apagllalag hprlapaisa mfaeparpws lpeladlcnm
      241 sratfmrhfh dnlgrsatel ltdirmtlaa nelkkpavst eavaesigyr svaafrrvft
      301 dkmgmtpgqw rrrtdeve
//
LOCUS       WP_175923972             265 aa            linear   BCT 11-JAN-2025
DEFINITION  (Fe-S)-binding protein [Burkholderia latens].
ACCESSION   WP_175923972
VERSION     WP_175923972.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..265
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28207
     Region          <8..255
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mnerhypaap ahvylfatcl vdlfvpeagl davrllereg ltvhyphgqs ccgqpayssg
       61 npdearrvaa aqldlfagaw pvivpsgsca gmirhhwpal faddpvhgpk araiaertye
      121 laeflvnvld mrldraaant gphervvlht scaarremgt rvhgvalvda lpgvtriehe
      181 reseccgfgg tfslkhpdis gamvrdkvas acatgcdrlv sadcgcllni ghaaakagma
      241 lpvehlasfl wrrtagagsl rgesq
//
LOCUS       WP_175923984             147 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: HIT family protein [Burkholderia].
ACCESSION   WP_175923984
VERSION     WP_175923984.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..147
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16682
     Region          1..126
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mecvfcredg gevlwqddvl rvvlatgehd ypgfcrviwg ahvaefsdlg eperahlmrv
       61 vyaveravrr vmqpnkvnla slgnmvphvh whviprfsnd ahfpqpvwap rqrsvseall
      121 rsraaqasll hnavreeiqr ttdsrqp
//
LOCUS       WP_175924012             115 aa            linear   BCT 11-JAN-2025
DEFINITION  GFA family protein [Burkholderia latens].
ACCESSION   WP_175924012
VERSION     WP_175924012.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..115
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12870
     Region          1..>101
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mlyrgschcg dvkfeaegdl qgvmacncsi crrkgalmwf vprnhmtlvt sddnlatylf
       61 nkhvirhrfc krcgihtfge grhpdgtema ainvrcledv didalpvthf dgrsl
//
LOCUS       WP_175924019             325 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175924019
VERSION     WP_175924019.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..325
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36116
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdriqamevf trvvdansft raadtlampr asvttiiqnl eallgvrlmh rttrrlsltp
       61 egaayyehcm kiiseiaevd ssfqtgnrkp sgvlrvhmps slgrrvvlps lsifrqrypd
      121 itldlglsdr yvdpveegid cmirvgpled ssmvarrigm lkrvtcaspd ylarhgepqe
      181 iadladhhav nfrashgara ipwvfmidgk pvevrmngtv tvndsdayvt cglegfgmiq
      241 ptlfmvlphl rdgslvevlp dcnpkpkpis ivyphnrhls qkvrvfadwm aelfestpsl
      301 eggenwrgke araeapdvqr ravva
//
LOCUS       WP_175924020             552 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia latens].
ACCESSION   WP_175924020
VERSION     WP_175924020.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..552
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58975
     Region          18..538
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(31..32,35..36,39,77,135..136,138..140,143,163,
                     166..167,170,256,259..260,263..265,268,296,300,464..465,
                     469,473,489,492..493,496..497,500)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 matlggqish spmtseekkv ifasslgtvf ewydfylags laayisksff sgvnptaafi
       61 ftllgfaagf avrpfgaivf grlgdlvgrk htflvtivim gvstfvvgfl pgyasigiaa
      121 pvifiamrll qglalggeyg gaatyvaeha panrrgfyta wiqttatlgl flsllvilgv
      181 rtfigeeafg swgwrvpfva silllavsvw irlqlnespv flrikaegkt skaplteafg
      241 qwknlkivil alvgltagqa vvwytgqfya lffltqtlkv dgasanilia ialligtpff
      301 lffgslsdki grkpiilagc liaaltyfpl fkalthyanp qlelatqkap isvvadpatc
      361 sfqfnpvgts kftsscdivk salakaglny envaaptgtt aqikvgdtvi qaydgkaada
      421 kaqgaafdkt lastlkaagy pakadpaqln wpmtivilti lviyvtmvyg piaamlvemf
      481 ptrirytsms lpyhigngwf ggflpatafa ivaakgniys glwypivial itfvigllfv
      541 ketkdsniya qd
//
LOCUS       WP_175924046             369 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia latens].
ACCESSION   WP_175924046
VERSION     WP_175924046.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..369
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39543
     Region          1..355
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masvllrnia kryddtevlr nvnldiadge fvvfvgpsgc gkstlmrmia gledissgdl
       61 lidgakvndv psakrgiamv fqsyalyphm tlydnmafgl klagakkpei dqavkqaaki
      121 lhidhlldrk pkqlsggqrq rvaigraitr kpkvflfdep lsnldaalrv kmrlefarlh
      181 delkttmiyv thdqveamtl adkivvlsgg avqqvgtpne lyhapanqfv agfigspkmn
      241 fltgtvesad aagvlvrfds getqrvavea aglqrgaavt vgvrpehllv gaaadgvaar
      301 tmaveslgda aylyaesava pdgliaripp ldtyrtgeal hvhaqpehch lfdeagqafr
      361 rlsahakaa
//
LOCUS       WP_175924063             520 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Burkholderia
            latens].
ACCESSION   WP_175924063
VERSION     WP_175924063.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..520
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54630
     Region          39..520
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mtaparsatp ldvaallaal pgriadvpar raahapaypa liedarrlsy gelaqavdta
       61 aerlthlgvr ggdrvmivae nsiaqivllf aaarvdawal msnarlsage ldaiaaharp
      121 kliafateas pdarahaary vataadalpv digawshhvd asapgepvaa dgaaqcaali
      181 yttgttgtpk gvmlshrnll fiaatssalr rvspddvvyt vlpvshvygl asvcigslya
      241 gatlrlaprf speavrvala degvtifqgv pamhaklleh lhthahawra prlrfaysgg
      301 spldadlkar vervygvplh ngygmtessp titqtpldap rtdcsvgvpi psvemrivap
      361 dgtdvprgev geirvrgpnv mlgyyrnaea traavspdgw latgdlarqd adgsvtiagr
      421 skeliirsgf nvypveveqv lnahadvvqa avvgravegn eevlafvelv pgatateatl
      481 hawcaerlap ykrparirvl dalpaastgk vlkhklrelv
//
LOCUS       WP_175924184             341 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia latens].
ACCESSION   WP_175924184
VERSION     WP_175924184.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..341
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37370
     Region          65..268
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 makdtskekk ptgnlhlaag llrglaqena aletrlpdpt pasnpaveas tpaatatpad
       61 alelgapqkv avkdcipnpf nprvfysess lhelaltlkr egqiepikvt rlpefpgklv
      121 vidgqrrlra tsingdetin atfrtdhtpe qlytiayran hdherqtifd davawkrlld
      181 ekvfpdqntl aekigkdkas isktlslnal pntllermas andvvglqaa yflkliferl
      241 geaaadrllt avidrkksvr dlenflraqs dgnkksgrtr ysvrhdfale sraigqlkty
      301 pdgrldlqlk gvdasqqeal adrlktvida yvaelaataq k
//
LOCUS       WP_175924224             147 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: HNH endonuclease [Burkholderia cepacia complex].
ACCESSION   WP_175924224
VERSION     WP_175924224.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..147
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17123
     Region          6..81
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 msgltkaqre alrrkydgrc aycgtplter whadhfepvr rdlklvntdr gwrwrsgppt
       61 rpefdvvenf mpscapcnid khamdleewr kklsrtldvl nrnyptyrha rrfglvveta
      121 spivfyferv akevapvvpf vnqesis
//
LOCUS       WP_175924191             321 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175924191
VERSION     WP_175924191.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..321
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34370
     Region          5..315
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpkvvgifav pgvqlldvsa pldvfaqana ecgkpfytlr iiasesgpir tssgarllad
       61 wivpdipdri dtllvagapg vgrialrtdv lawlrsaavq skrygsictg afilaatgll
      121 kgrrltthwa tadalaeayp sltveadaly vrdgklrtga gvtagldlal alveedlgre
      181 varrvaaqlv mffkrpggql qfsrggdarp agrsvlqevq rwvashpele hsvaelakha
      241 gmsprhfarl fraevgmtpa awveatrist arqllesghh tpkqvaakcg ftnvdtlrrs
      301 fakhvgitpa eyrkrqavvg e
//
LOCUS       WP_175924250             175 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia latens].
ACCESSION   WP_175924250
VERSION     WP_175924250.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..175
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=18226
     Region          9..175
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mikysrpyla igiifcsvqs yaadgtvtft gainggtcev ttsnvqvalp tvqadtlktd
       61 gatagdtrfd irltrcdpqi sngvraafas nthldpatgn ltieqgdgda dnveiglrnl
      121 dytainigdp taahafpinq dgnakltyia qyvatggaav mgtvktnaif tlnyq
//
LOCUS       WP_175924263             343 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia latens].
ACCESSION   WP_175924263
VERSION     WP_175924263.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..343
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37900
     Region          70..301
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mtkkdfsaal nagvkrdqtm rqaavpsrfd rvdealsgrs slleraeetv atpapsaaea
       61 ylanleqtgk vraryvtmpi shiddnplns rtiykeelia arassmardg qlvpvlagrh
      121 pdfpdraili dgqfrklgal rnraetldvk llegldpidf yrlaraanne reqetvldla
      181 lgykklldqg haksndelav lveegkskvs kilalldlpq svldviashp kqfglstsye
      241 ltlymkasde krtlafaeri rdeelpfqkv kaireslehg raprkslsrq ykvstgdgae
      301 igaikewgdg kiridlvlgs aekaeayita frklladdgh hlk
//
LOCUS       WP_175924288            1084 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia latens].
ACCESSION   WP_175924288
VERSION     WP_175924288.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..1084
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115703
     Region          3..1062
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mlkivrlala rpytfivlal liliagpiaa trtpidifpd iripvisvvw nysglqpddm
       61 sgrivtfyer tlgttvndiq hiesqsfrgy givkiffqpt adirtataqv asisqtvlkq
      121 mppgitppqi lnynastvpv lqialtsntl deqkledyae nfirpqllsv pgvaiptpyg
      181 gkarevqidl dqralqskgl saqdvahala qqnqiipagt qkigrfeyni klnnsplald
      241 alndlpiksv dgttitirdv ahvrdgyppq snivrvdghr avlmsilkng sastldiiag
      301 vkaklplieq tlpprlklvt mgdqstfvkg avngvaregl aaaaltslmi llflgswrst
      361 liiaasipla vlsaiallaa tgetlnvmtl gglalavgil vddatvtien vnwhleqgkd
      421 trtaivdgak qivmpalvsl mcicivfvpm lmldgisrfl fvpmakavif smvssfvlsr
      481 tfvpmlaqyl lkphasagha sgelaaimdp hachtgapdi ppprnplvrf qraferrfea
      541 irasyrillg laltrrnpfv vaflgivtas fllapwlgrn ffptidsgei slhvrapvgt
      601 rveetaaefd riestirgvi ppaqlrevid niglpksgin ltynnsgtlg pqdgdilisl
      661 skdrsptady vrklrellpr aypgttfsfl padivsqiln fgapapidlq vagpnqqanl
      721 ayahelyrnl rliagvadpr iqqastypqf tvavdrthad qlgiteqdvt nsvvatlagt
      781 sqvdptywln psngvsypiv aqtpqyrmtt lsalqslpvt gasgqsqllg glatitrgvg
      841 navvshynie plfdiyattq grdlgaiard iggivkatar dlpkgstvtl rgqvqtmnga
      901 faglllglvg aigliylliv vnfhswadaf vivsalpaal agivwilftt htplsvpalt
      961 gailcmgvat ansilvvsfa rerlaetgna lasaleagft rfrpvlmtal amiigmapma
     1021 lglgdggeqn aplgravigg lacatiatlf fvpvvfslvh rrdalkydgp rasfppasga
     1081 shvh
//
LOCUS       WP_175924430             322 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia latens].
ACCESSION   WP_175924430
VERSION     WP_175924430.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..322
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33375
     Region          50..320
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          217..320
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(222..223,256..257,260,264..265,268,310,314)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mqrtiqvrrm rfpryprvss fvaallaagl vgggaayaqn tggatvtpvg ngtvataalp
       61 atpnaggapg tasgtvvhgt agtltpppan aapgqvvvgg kvpdeatkaa vlqklrdtyg
      121 aanvvdqiev gdvatppnws anvqkllgaq lkqiskgqlk ingtqiemkg evhneaqrqq
      181 lasdmantln ptytiknglr vsaseqglld qtlanrtief etgsatltpq gkqildqmaa
      241 alskmqnrtv diightdnsg nrtsnialsq aradavkgyl itksippqqm tttgvgpdqp
      301 tapndtaegr arnrriefrv gq
//
LOCUS       WP_175924441             152 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease [Burkholderia latens].
ACCESSION   WP_175924441
VERSION     WP_175924441.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..152
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16621
     Region          55..130
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mtigagnegr yvvfiaseid aellslttpe vpadetielv agnpiecids lglaripksv
       61 kdkvakenqe ffgkgtcecc gvkvvpgkks qrgitpptne rqfdriepda lggandednt
      121 qvlcrkcnrr lwdkikdnfk rlnrlgrtpc ds
//
LOCUS       WP_175924467             338 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia latens].
ACCESSION   WP_175924467
VERSION     WP_175924467.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..338
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=36911
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..292
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109,111..112,115,119,121..127,219..224,230..231,
                     233..234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdrtlhamsv fshvarlgsf taaadmlgis aasastlvrr leeylgvtll qrstrcvrlt
       61 aegeqyqehc qrilgeielm qqqlsgagki argrlavdld qevahsvlpf lpvfranhpe
      121 vglrvdvggd adgliangvd cavvvgqlad sslrsrrvgq fhavtvaspd ylkargtpvd
      181 pdglhchdvi hytprrlgpv refrytvdga etrlklaeri svndvrsavr yavegvgiaq
      241 vsermvaeel atgtlvsilg eygppplpis vlypdrrqvp msirafidwm qtqlrdleia
      301 sfdhtsapng rrdaapywts nserpfittg frqlsata
//
LOCUS       WP_175924534             703 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia latens].
ACCESSION   WP_175924534
VERSION     WP_175924534.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..703
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=77912
     Region          12..703
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mqlsdipgff glqsnrlfti qtpmkgrsdl vlvdfqgteg lsqnfefhvr lasqdpniel
       61 kkligqpvti tlqltdalas seeryfhgyv anfshldhdg sftiytatlv pwlwmlsrsr
      121 dirifqeent etilakvfre ygkiasfefr lskatknrsy ctqyretdle fverlmqedg
      181 lffffehakd ghklvisdns iaakpisgrs ptlqytkgea ldnlavvtsf qasrqlesss
      241 vglktfdykv pharrfvsgg tevdqgevps yevydylgeh gfpdsdrgea ltrfrtqala
      301 ahskvfigts tsrrlspgqy felddhydhg tskaedrqfl lttvthsgtn nyqaseggat
      361 yqcsfvcirk kipyrpafti erpsiigpqt avvvgpqgee iytdnlgrvk vqfhwdrlgk
      421 rdqgsscwvr vgqpwagrgf gmiqiprigd evvvifldgs pdrpliissv ynsanmppwv
      481 lpgsatqsgi ltrstktgnv ntanairfed kkgaeevwlh aekdqrfeve ndeshwvgnd
      541 rtknidhdet vhvkhdrtet vdnnetvtig vdrtehvgnn etltvggnrn etihgmenll
      601 ialtstetvg lakaltvggg yqvtvagavn ttaglasaee vglsktsivg ksytikagkv
      661 fevtvgkstf rmdedgnitl kgvklliegs gpieingkdv dvn
//
LOCUS       WP_175924587             200 aa            linear   BCT 11-JAN-2025
DEFINITION  J domain-containing protein [Burkholderia latens].
ACCESSION   WP_175924587
VERSION     WP_175924587.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10446266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..200
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=22706
     Region          5..66
                     /region_name="DnaJ"
                     /note="DnaJ domain; pfam00226"
                     /db_xref="CDD:395170"
     Site            order(31..33,43,46..47,50..51)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
ORIGIN      
        1 mttmyellgv cenatneeik rgyrkaamka hpdrnvgcea daharfqeik eayailsdpe
       61 lrrvydtaya eemlrharlr eeeerlraer eaeyarfvaw amrfaeqgnn rdvvfgvllg
      121 rdcdvqlaer iadsvvelha srqpgasrde qrdeqmpqcg erateaasaq apksdarrsd
      181 apahtdffsa lwrglfglrq
//
LOCUS       WP_175924599             866 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia latens].
ACCESSION   WP_175924599
VERSION     WP_175924599.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 866)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 866)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 866)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 866)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..866
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..866
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=92079
     Region          31..823
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mrkhygwail llgmtataha etpqaapans atsasqdaqn vqfdpsflag qavdvtrfer
       61 dnpvmpgtym vdlyvngeli ghravkfeah gkgsaqpllt rslleaagvd lsqwkstkdd
      121 agqpvnlaer ipgaslhyds sdqhlelsip qiamrhtdrg wiapsrwdsg itagilkydf
      181 nayrsmgnga pddsmylglm agfnvggwrf rdrsalnyde hggfqwqqld ayaqhditkw
      241 kstltlgdss ttgdtfdsfa lrgvqlgsde rmlpdselgy apvvrgvahs nakvevrqng
      301 yviyqttvap gpfairdlnp tgyggdlrvt iteadgtkrt ysvpyatvpq llragasrys
      361 faagqyrgyg egpdshpyvf qgiyrrginn litgyggvqa segymsallg aalntpygaf
      421 aldvtgarts ipyqpaqtgm swrlsyaksl pktdtnltva ayrystagfy slqdavnarn
      481 aadigsypaq elyrsrsrvq lninqpigsg slyamgsltd ywnrqgsdlq mqigysgttr
      541 wggyslslqr vrdafgnvdn qiyasvsipl ganrvdshpl fsdldfsvaq gksttfntsa
      601 sgtaghnnew syglnagysg dnqsksvgay gtyngpkgtv nasasagtgn sqlsfgmsgs
      661 aivhkggvtf gqavgaddai glvkakgakg aevtnapgva vdgsgyaivp fltpyrentl
      721 vldpsnmsds aeleetsedv vpragavvea kfetkvgvpv imrvkqange pvpmgadvld
      781 thnqkvgvvg qggtvyvrgv spkepltvrw skepggtcsf gyttdgkghg vaqvcavpgm
      841 qadqkatpkd dhtakpetsv asagqh
//
LOCUS       WP_175924601             180 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia latens].
ACCESSION   WP_175924601
VERSION     WP_175924601.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia latens
  ORGANISM  Burkholderia latens
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Burkholderia latens"
                     /db_xref="taxon:488446"
     Protein         1..180
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=18490
     Region          9..180
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mklvrqlplv malglcatha fadttagdgt vtfkgkviaq tcqvttkdvt vnmptvqmqs
       61 lgaagdtagq erfqiqltgc ahgdhdekhv aaafsnpqad antgnlvnid ssnsaaqkve
      121 vqllnadgsa itvndpkssk gvvigddgta tipylaqyya tgaasqgplt anttftlsye
//
LOCUS       WP_175924737             551 aa            linear   BCT 11-JAN-2025
DEFINITION  S8 family peptidase [Burkholderia cepacia].
ACCESSION   WP_175924737
VERSION     WP_175924737.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..551
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55143
     Region          239..518
                     /region_name="Peptidases_S8_13"
                     /note="Peptidase S8 family domain, uncharacterized
                     subfamily 13; cd07496"
                     /db_xref="CDD:173820"
     Site            order(246,314,318,385..387,413,415..416,486)
                     /site_type="active"
                     /db_xref="CDD:173820"
     Site            order(246,314,486)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173820"
ORIGIN      
        1 mrtkrfnlal arsaharmla gmlsaaallp lagcgggggg dgsnpsssna apapapaptp
       61 apgtpttppa sagsnacatq qaavqmaaqa apaeapidhl ivklktltat ramaaidngt
      121 rldaviqrsm trwtapvags arayastvgq apvnvqvert isngaavlsl gqrmaatdaa
      181 alaqafaads dvdyaepdhp mqirdtpsdp lynqqwylsd ptagidlppa wnvtkgsptv
      241 vtavldtgyr phadlmgnll sgysfisnvn tsnngltrnp datdpgdwvt qqeldnangp
      301 yyhcasqpsd sswhgtrvmg vigatanngt giagvswlsq ilpvrvlgkc ggvtsdiadg
      361 mrwaagipvn gvptnprpak vinlslggvg acsttfqqai ddvtakgvtv vvaagndgls
      421 tgldqpancr gvisvgatda tgrrasfsnf gadvslsapg vnilstsntg tttpgsdtyg
      481 langtslatp qvsgvaalml svngnltpaq iqqklqggar ttklaagtsc tampagsgiv
      541 dagaaiaaag q
//
LOCUS       WP_175924773             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cepacia].
ACCESSION   WP_175924773
VERSION     WP_175924773.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21974
     Region          4..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mpvlptllaf glvslgmvlt pgpnmiylvs rsicqgrrag lvslggvalg fvfymvcaal
       61 gitalvlavp yaydvlrfag alylaylawq alkpggrsaf qvrqlphdsr arlftmgfvt
      121 nlanpkiavm ylsllpqfil pghgsvlaqs lalgsvqiav svsvnaliac magaiagfla
      181 grpvwasvqr wlmgtvlagl avrialesrs
//
LOCUS       WP_175924796             331 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cepacia].
ACCESSION   WP_175924796
VERSION     WP_175924796.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..331
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34883
     Region          130..304
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mkdqpdgvvl psrvvpfpas iseearaalq rlvgsdgvpl nalhvmpapd dfdawmrvka
       61 aadahyaaav eqlgghlrss vetiragaad vhvatpeava sgecayidlh ggalvlggga
      121 acragaqmqa drlgircygv dyrlppehpy paalddciaa yayvleryap gnvviggrsa
      181 ggnlaaamvl rardeglplp aalvllspev dltesgdsfe tnrlvdvvlp tslmpnnlly
      241 angadlahpy lsplfgdfaa gfpptfiqsg trdlflsnav rlhralrraq vptelhlfeg
      301 mphggfmgap edmelgeeia rfvrahlpal n
//
LOCUS       WP_175924824             231 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia cepacia].
ACCESSION   WP_175924824
VERSION     WP_175924824.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..231
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=24255
     Region          55..225
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mttaqtaasa asasaaatga sapaqasavp dsapavpasa paaverplvr fqskplsini
       61 ngksvgpmqv peglmmiefl heyagltgsr lgcgqgicha cvvivdkpdg tseemrtcit
      121 gahffhgrti rtieghakrn eagevvelsp iqqkflehfs fqcgyctpgf vnaatvlier
      181 lkrepvakad vertiteald ahlcrctgyv ryyeavkdvv lttpglvkda a
//
LOCUS       WP_175924819             489 aa            linear   BCT 11-JAN-2025
DEFINITION  sialidase family protein [Burkholderia cepacia].
ACCESSION   WP_175924819
VERSION     WP_175924819.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 489)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 489)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 489)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..489
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51820
     Region          152..436
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Region          185..246
                     /region_name="Sialidase propeller 2"
                     /note="Sialidase propeller 2 [structural motif]"
                     /db_xref="CDD:271234"
     Region          251..304
                     /region_name="Sialidase propeller 3"
                     /note="Sialidase propeller 3 [structural motif]"
                     /db_xref="CDD:271234"
     Region          319..372
                     /region_name="Sialidase propeller 4"
                     /note="Sialidase propeller 4 [structural motif]"
                     /db_xref="CDD:271234"
     Region          383..436
                     /region_name="Sialidase propeller 5"
                     /note="Sialidase propeller 5 [structural motif]"
                     /db_xref="CDD:271234"
ORIGIN      
        1 mrrstvshpl vtglprltrl savaavamaa aaaahadpva vsgpspfaac tiggpgtnyv
       61 naevepwlsv npanpmnmig vwqqdrwsng gahglvagyt fdagatwart pqpfsacapg
      121 glkyerasdp wvsfgpdgta ysvsisfnqs nnanavaasv stdggqtwss pavliandep
      181 ttqffndkes vtanpvkagt ayavwdrlel pngnpyanlh thayrgptlf skttdggktw
      241 stpkvivnvp srqqtignqi vvdpksgtly dffdliqppf skaagkvafi kstddgatwt
      301 kpqviaglqt vgvtdpntge pvrtgdiipe paidpasgql yvvwqdsrfn ggtydeiavs
      361 tskdggatws tpqqlntptg rpafnpsvrv dntgavmvty ydfrdlqagn tttlptgfwr
      421 kishdggttf aderrvggpf dlklapnaeg ffigdyqgld vmpsssfhpf fvqtnagnlt
      481 nrtdvffap
//
LOCUS       WP_175924835             790 aa            linear   BCT 11-JAN-2025
DEFINITION  serine/threonine-protein kinase [Burkholderia cepacia].
ACCESSION   WP_175924835
VERSION     WP_175924835.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 790)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..790
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=80438
     Region          32..531
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
     Region          <566..>721
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
ORIGIN      
        1 mkdagsrdne hdtatrgdas gftvrplplg hrlgelqlde vlgiggfgiv yrafdrtlrr
       61 avaikeymps mlatrggdyt vslrserfaq afdagrgafl nearllaqfd hpglvkvlhf
      121 weshgtaymv mpfyegrtlk qlldggmris etqlrnivga llgaldtlhr aqcfhrdval
      181 dnvlirpngs ailldfgaar krigdlvddg ammikpgyap ieqytddpaf sqgpwtdlya
      241 lgavmhamit gelppaavvr sikdtyrpla srelpagevy spaflaavdh alqlripdrp
      301 esvaafaael glrdfdrtgs gygahavppv gdagrgegdk gaasvetgta paaaatsiga
      361 ggtasgsaap darpptqaga gpvstptdta saspgvsdgk petddgsstl kaatqgtaat
      421 aaagalaasa shasrpaakp vesdapngnv erakepaaar tdthdeasar sagpdteiga
      481 rgaagsgktn aftaeaagad adatsttapy paasssaasg gasvqtgaqr dhqppagsrk
      541 rrlpvyagga vvaliavgla aiylsrparv adepapvasq pqagtsppas tpaatlaqqg
      601 ptplvvppss lpagssaqvp pprvaaepas mpaveaaapa pqvattvtna apppagaspa
      661 iapagsldas ervvnvppse aavppvttps papkppdsqt avaavnalpa eqqprapkaq
      721 etvqvrfnvr pwgdvyvnga rrgaspplrs vsltpgvyvi eirngslppl hrtvaidfgs
      781 kpvnidyafe
//
LOCUS       WP_175924859             862 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia cepacia].
ACCESSION   WP_175924859
VERSION     WP_175924859.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 862)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..862
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=93211
     Region          59..712
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mhpfqpsstr vnrrnvssvr dfcarwvara qpvaaaaaar vkplaavawh hlrhptrrgv
       61 llagaavpal fvayvvvlip ftpgigdirk arvdqpaqvl sadgkllaef kpsnrewvpl
      121 rqisphmvda liatedhrfy ehhgldwkrt asaalhtfsg srqggstitq qlarnlypde
      181 igraptltrk vkeaitalki eavyskdqil etylntvpfl ynaygvemaa rtyfdksade
      241 ldvldsatlv gmlkgnsyyn pvlnperalq rrntvlgqmv kygklspaqf aqlqrrplri
      301 dferqkeppg paphfaqqlr kwliawadrn dyniyadgli vrttidsrlq qmatqaltlq
      361 gsqlqgiann awsgrdgcgt dnevfrtfmr espeykaaqd agkddaaamk llaadrgfmr
      421 alcktktdvq agflaidprn gqirawvgsr dftsepfdhv aqarrqpgst fkpfvygvaf
      481 angmkpddtf idqpveiplk ggeiwrpndd vpptgkpmtl rdavalsrnr itaqvmekvg
      541 pasvarlard mgvrespler vpslalgtsp vtlkemvasy atiangglyv epqmvtrien
      601 rqgdvlaeya papperalda etdktllsvm rdvvtrgtgg sirtrfgirg dvagktgttq
      661 dnadgwfilm qpglvagawv gfddgrvtlr sdywgqgahs alpivgdffq raqrarivdt
      721 kakfdtepsp gwfaslrerv tdlfdtwfpp kpekapapvr tqrverapea dtgtesaasa
      781 asapeaasgg iveewvpase vaasaaalsa gasqpqpaqp pagastpggg ssglgtapaa
      841 appvapaqpp vpagpdasga sq
//
LOCUS       WP_175924872             310 aa            linear   BCT 11-JAN-2025
DEFINITION  AEC family transporter [Burkholderia cepacia].
ACCESSION   WP_175924872
VERSION     WP_175924872.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..310
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31331
     Region          18..305
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 migpillala pvallvacgh glrrtgfiad afwpqaerlc yyvllpalfa dglanarlqa
       61 lpvlplaaal vgstalaaal lllvrpfvrv dgagftsvfq gavrfnnyvg talaaglfga
      121 kgialaavcv aaivptvnlm cvlvfarygs trlgaaalvr qilsnplvva calgiamqgg
      181 gvtfpaavep avrtlgaasm plgllcvgaa lkfdaarawl qpvcvasafk fmamplitla
      241 agrlfglgda altvallfqa lptssasyim arqlggdapl magitafqti aaalampvvl
      301 talasapafr
//
LOCUS       WP_175924874             418 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175924874
VERSION     WP_175924874.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..418
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44614
     Region          17..395
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(27..28,31..32,35,69,124..125,127..129,132,152,
                     155..156,159,234,237..238,241..243,246,270,274,325..326,
                     330,334,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 msvpaagvfr slrsfnyrvw aigslvsnig twvqrtaqdw lvltqlthhd asavgtvmal
       61 qfgpqllllp wtgyaadrfd qrkllmvtqa lmgvlalvlg altvtgvarl ehvyvfaflf
      121 gcaaafdapv rqtfvaelvg drelanaval nstsfnaarm igpaaagfmi asvgtgwafv
      181 anglsffavl vsllllrede lranlragrs rggllegfry vwrrddlkai lvmlfligtf
      241 glnfqlfist maasvfhvda rgfgvlssmm avgtvsgall aarreqprfr hlwfgaalfg
      301 lgctlaalap gywlfaaalv ltgiaaitfm nstnslmqls tepamrgrvm alrlavalgg
      361 tpigapvagw vanhlgprwa lgvgamsgfg aalvathfvk rsraqaqadr ardrfdgv
//
LOCUS       WP_175924891             460 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia cepacia].
ACCESSION   WP_175924891
VERSION     WP_175924891.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..460
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=48724
     Region          40..419
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msaslaassp spqppalrll ptddaddarv aallerlape laadaarndv dgrfphenfa
       61 rlhragliaq vvprehggag atlaqasriv aavaradpat alvltmtylq hralgradnr
      121 wpaqvrravf dsavtqgali nalrvepalg spsrgglpet varrdgdgwr lsghklystg
      181 ipalrwlavw artdepaprv gvflvprnrd adgdrirvie swnhlglras gshevvfddv
      241 rlpadhavdv rapdawavsa athadadaqa dqqawmvall gslydavara srdwvvefat
      301 trapsglgap latlprvqea vgeiegwlha nrvllddhia rtdaghappv ttsglvkrtv
      361 tehairaveq alklsgnhgl sranplerhy rdvlcsrvht pqddaiavaa gravldaasr
      421 veakgevtge akgetkgeas getetgeasv dgtergrsda
//
LOCUS       WP_175924909             826 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 2 protein [Burkholderia cepacia].
ACCESSION   WP_175924909
VERSION     WP_175924909.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 826)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 826)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 826)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 826)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..826
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..826
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90163
     Region          10..>626
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mtrtraqpaw smlataagva reprdlpaag ngwipaavpg tvaqslalag rldeavslde
       61 rdhwyrielr ghgprvlrfh glatlaqawl ddtpilrsds mfvahdvpvs ldgshrltlc
      121 fralaphlgd araprrarwr trlaepaalr tirtslfghm pgwfpphvpt gpwrpvdvld
      181 padgpvladc nlhariegdt gwldadltfa aplpdalaar lscgqhhatl eragpdrlra
      241 svavpnvcrw wphthgepvl ydialhigde rrplgatgfr tievdpgadg kgfglrvngv
      301 pvfargacws saaplalhad datyarllgl ardagfnmir vggtmtyead afhawcdrlg
      361 llvwqdfmfa nfdyalddpa faanvdrear qflsrhgasp slavlcggse iaqqaamsgl
      421 gpkqrflelt adrlaghaaa crpdvpyvpd spdggvlpfm prervshyyg vgaylrpldd
      481 arradvrfas eclafsnvpc datlaelgwp gvheprwkaa vprdpgtswd fedirdhylq
      541 tlydvvpdrl rredparyfe lsravvadlm retfsewrrt gsrcagalvw qfqdvmpgag
      601 wgvidaahrp ksawhalrqv lqpvqvllvd eglngldvhv vnerpaplsa alelvalrdg
      661 rtavaragcp vriaahdtvr igsaellgrf fdwtyayrfg pcehdtvvat lrgddgtlls
      721 qafhfpsrth pavlarrelg leacvsrtgd twhvdidtrh varhvqidap gfvprddwfh
      781 lapgtparvv lvplgtagkn gaadeppave iravnaarav ramqag
//
LOCUS       WP_175924953             160 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia cepacia].
ACCESSION   WP_175924953
VERSION     WP_175924953.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..160
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17276
     Region          14..134
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mtsgdplfti asidaaqthp lraaillngd lnacelagdh apttlhvgvr dgrsnivava
       61 slceelrddd parpawrlrg mavdpavrgm gfgrvlvqvc vrhaqahgaa lvwctareva
      121 yrfyeklgft adgemvtmpg rtdtafyvmr ryidrhspaa
//
LOCUS       WP_175924967             238 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175924967
VERSION     WP_175924967.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 238)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..238
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=24990
     Region          10..237
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 mdgwgwvsyl gmdpdgwgva llqgagvtle islgafavgi vlgllgaaak lsgvraleri
       61 aqgyttlcra vpelllilll yyagtdainl lmtvigagpv avngfaaavi vlgivqgaya
      121 aeiirgaila ipygqieagr afgappglvf rrvtlpamap yalagfanlw lilvkdsali
      181 svvgyselly takqaagstr eymhyylmva avyfaitsls gvlfrnierr fgrwmpas
//
LOCUS       WP_175924970             320 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Burkholderia cepacia].
ACCESSION   WP_175924970
VERSION     WP_175924970.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..320
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32362
     Region          2..319
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtilviaeyd apkeaplggs asikaatlnt vaaaakiggd ihvlvaghna qavadaaaki
       61 agvskvllad aqqladglae nveatvlnia kdyshilapa taygknvapr iaakldvaqi
      121 seitavvsad tferpiyagn aiatvqssdp ikvitvratg fdpvaaeggs asvekieaaa
      181 dagksqfvsr evtkldrpel tsasiivsgg rglgsgenyt kvlepladkl saalgasraa
      241 vdagyvpndy qvgqtgkiva pqlyiavgis gaiqhlagmk dskvivaink dseapifsva
      301 dyglvgdlfs tvpelhaelg
//
LOCUS       WP_175924994             523 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175924994
VERSION     WP_175924994.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..523
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52511
     Region          37..515
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,157,
                     160..161,164,288,291..292,295..297,300,328,332,384..385,
                     389,393,409,412..413,416..417,420)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msqsspasra gaaaaprmgg rmpaaatlav asatcslivl dtnvvavslp siarsfhasf
       61 adiewvvsay mtafaacllp aggladrfgr krmlgaglal fflaslgcgv apsagwliaa
      121 ravkgggaal lltaalavia nrfpdgrera rawaiwgmcm giatavaplv ggaitqwigw
      181 rwvfllnlpv cmllaagarv aidesrdpha krvdaagsll fgaalacaia aligapshgw
      241 lsaatlgrla laaalfaafv gaerwqarpm idlalfrqpr fvgavlamfg yaacaqvmmt
      301 flplylqnaf gmsaidaglg mlpfafamia gpslgaalaa rvssggvlag glaligagnl
      361 ataaltaggd yrlvaigmfv tgcgagimng dtqkaimacv ppnrtgmasg istttrfsai
      421 vtavgvlgav laastqarld rllsaapglr afadapfmss llagdlaral ervppsaaga
      481 lakaapvafa sgfadaltvs gvlalvvaiv awkllaqpmr ega
//
LOCUS       WP_175924971             388 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175924971
VERSION     WP_175924971.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..388
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41945
     Region          31..381
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msvvmetsag veeagpgaha araesvgcat sgaglqidhv skrygvvqal rettidiprg
       61 efltilgpsg sgkttlltiv agfehpttgd lrvggrsive lppekrnfgm vfqgyalfph
      121 mtveqnvayp lmvrkqkgpd avkrvkaald lvrlghladr lprqlsggqq qrvaiaralv
      181 fdpdlvllde plgaldrklr gevqvelkal herlgatflf vthdqeeals msdriaimrd
      241 grleqigtpd glyeqpanrf vadflgksnf ieavalggdd atthyrvgda rfvapafgar
      301 pddtllfalr pekvavsats crgahnevag rirhwsyfgs syrfeietaa lgcvtadvpa
      361 wrglasprtg mdvfvqwerd atcriasd
//
LOCUS       WP_175925002             322 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175925002
VERSION     WP_175925002.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..322
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35385
     Region          4..>170
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,223,240,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 meslrsmrvf vraielgnfs avareegtgq ptiskivaaf ekelgvrlle rsttslaptd
       61 egrrfydrck rvideyasav aevrgqtvrp vgklvvnapl glgelrlnal vleflaawpe
      121 ievelqltdr vidlveegvd vairlghllp pdvvarpias sprllvatpk yvaqaprlrr
      181 pedlarhayv gyaradigne lafargdeqv avpvrgryrv nssmalrecf lagnavgsgp
      241 awlvqdlids gqlvrllpkw dmvpphalhl vyasrrylpl rtrtflqfme qripglpgfh
      301 attaatansa ansaarasrr pr
//
LOCUS       WP_175925049             232 aa            linear   BCT 11-JAN-2025
DEFINITION  chemotaxis protein CheW [Burkholderia cepacia].
ACCESSION   WP_175925049
VERSION     WP_175925049.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..232
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=24952
     Region          80..226
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mnraaaafde ttidvddcwn rigtrgdrtc erlneclrcl ncpvyayhaa kllerplgga
       61 emadatrrms apgaphvrda dadtrhaala frvadewlal pigvlreiag trpihslphr
      121 rnsavrgvvn irgtlriais igallgldvg kggddgrftr llvaahqgep vvfpvdeveg
      181 vlrfgasdwv pvpatvgras aglsrgvlsw rgksvglldd drlfdavtrs mr
//
LOCUS       WP_175925038             482 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175925038
VERSION     WP_175925038.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..482
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48680
     Region          21..421
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(28..29,32..33,36,68,118..119,121..123,126,148,
                     151..152,155,287,290..291,294..296,299,327,331,383..384,
                     388,392,408,411..412,415..416,419)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mdtplpssaf ppalarvvat vstgfvvtql dvtivniala hlagdlrlpv aglqwvvday
       61 tlafavlmls ggalgdrfga rrlyiaglvl falaslacga asapamliaa ralqgvgaaa
      121 mlpnslalln dacrhdprlr aravgwwtaa gsisiaagpv vgglliaawg wrgiflvnlp
      181 lcaaglaaaf awiparraaa tpaapsrsvr aldlrgqfia iamltaltga viewrplgft
      241 hpvvaggfal aalaalafva vetrtatpml plslfrhrtf saavlfgicv nltyygtvfv
      301 lalylqrarg esalqaglaf lpltggflls nlasgrvvah hgprapmlag alvaalgygs
      361 lhfidastpl avllmpflli psgmgfavpa mttavlasva peragiasav lntarqagga
      421 mgvaafgala ggggaaqvvd glrietavsv allvaaalla tlvrpdahrg assvrqavpa
      481 ad
//
LOCUS       WP_175925081             431 aa            linear   BCT 11-JAN-2025
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Burkholderia cepacia].
ACCESSION   WP_175925081
VERSION     WP_175925081.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..431
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=46191
     Region          5..431
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 mtdqassnwr letiavhggy rpdpttrava vpiyqtvaya fddtqhgadl fdlkvqgniy
       61 trimnpttdv leqriaaleg gigalalasg qsavtyaiqt iaeagdnivs asslyggtyn
      121 lfahtlpqyg ittrfadprd pasfeplida rtkaifaesv gnplgnvtdi aalaevarrh
      181 giplivdntv pspyllrpfe hgadivvhsl tkylgghgts lggaivdsgk fpwaehadrf
      241 krlnepdvsy hgvvyteafg paayigrarv vplrnmgaai spfnafqilq gietlalrve
      301 risdnalkia qhlagheqve wvnyaglpdh pdhplvaryl sgrapgiltf gvkggrdgga
      361 kfqdalklft rlvnigdtks lathpastth rqlspaelak agvkeetvrl sigiehiddl
      421 ladldqalaq v
//
LOCUS       WP_175925091             311 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175925091
VERSION     WP_175925091.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..311
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33114
     Region          9..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..294
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,229,246,273)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,193,
                     223..227,234..235,238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 madlrdvnln rlavfvavvd agsltaaaer lglaktvvst hmqrlesevg anllvrttrr
       61 lsvtdagraf ydacrdivra aesaldavss dagplrgtlr vsvpidygal vvapavvalr
      121 drhpgldvel vandrvvdlv adnldvairi grladsnyra vqlgtyekwl vaspafvarh
      181 grpqdtdala alpfvmlstl prpqtleled anggtasvrc vahvvsntat acraivlagg
      241 gfglltdfst addlaagrlv rllpawrsap agihavypst rlpspkvraf idamkqridd
      301 trparktkre r
//
LOCUS       WP_175925109             329 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175925109
VERSION     WP_175925109.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 329)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 329)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 329)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..329
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34915
     Region          41..322
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mrqparplpn dgapaalaaa taapgaadam spraggghap raswrahapl wlmcapafal
       61 faalvlvpla mtfmltfyrf dpatgpiaaf qfgnyaevlg ssyfhtifar tfgiaaltta
      121 icvaigtpea yvlskmrdpw rslfllaila pllvsvvvra fgwsmllnts glvnqalglt
      181 glgpykleyt tfaivialvh vmlpfmvipv wtalqrldpq tehaalslga spfttlrriv
      241 lpqlmpgvls gslmvfglsa safaipgllg grrlkvaata vydeflgsln wplgatiavl
      301 llvanlvvml tyyrvlerry arslggasr
//
LOCUS       WP_175925174             211 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia cepacia].
ACCESSION   WP_175925174
VERSION     WP_175925174.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..211
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23392
     Region          1..206
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mtthtlfycp ghlsfaphvi lrelgepfel alvsikdgat qsaefrqlnp kgkvpvlhtg
       61 ddvltessai llylalrfpq arlvpdtpmg laravewmnw lasvlpgtva lnfhpsrfse
      121 dpaahdgira kgragilaay aqvderlaar dwalgehysi vdpmlliffk wgnmlkldmr
      181 gfehwaahte rmlrrpavat alsveqisiw a
//
LOCUS       WP_175925187             177 aa            linear   BCT 11-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Burkholderia cepacia].
ACCESSION   WP_175925187
VERSION     WP_175925187.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..177
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18653
     Region          1..165
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtpahlipsp lgdiavried daltglyfvg qkyfppvaiv teadalatpp iarkvaeeia
       61 eyftgtretf svpiqlrgta fqrrvwkell aipfgelvty gditervglp msgaravgga
      121 vgrnpvsimv pchrvvgasg sltgyaggid rkrallsleg agfergtgdp aqqalsf
//
LOCUS       WP_175925208             431 aa            linear   BCT 11-JAN-2025
DEFINITION  multicopper oxidase family protein [Burkholderia cepacia].
ACCESSION   WP_175925208
VERSION     WP_175925208.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..431
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=47312
     Region          64..327
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mvsrrqflsh sgaallgsam vskagaaslp eaatmtktgt qpplvppngr pytpvatlng
       61 wtlpwrmkng wkefhltaep vvremapgmn anlwgyngqs pgptieaveg dkvrifvtnr
      121 lpehttihwh glrlpngmdg vggltqphip pgktfvyefq leahgtfmyh phademvqma
      181 mgmmgmfivh pkdrgtmpvd rdfvfllaay didpgsytpr vnemtdfnmw tfnsrvfpgi
      241 dplpvragdr vrirfgnltm tnhpihlhgy sfevagtdgg wippaarwpe vtadvavgqm
      301 raieftadrp gdwafhchks hhtmnamghq vpnligvpqq dlakrigklv pdymamgstg
      361 gamggmempl pdntlpmmtg tgpfgplemg gmftvckvrq glgrndyrdp gwfrhpkgtv
      421 ayeytgelpd g
//
LOCUS       WP_175925222             574 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia cepacia].
ACCESSION   WP_175925222
VERSION     WP_175925222.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..574
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62777
     Region          7..560
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mqmqpthaat tpadfvltha kvytvdphkp waqavavrdg rivyvgdtaa vqayvgaqtk
       61 vvdaagrlvl pgfveshwhf ettafafqaf vnyedpqkvl galrayvesh pdepaitgmg
      121 wvqatippal lrketldaic adrpvcllst dfhtmwvnsk aleiagidas tppvqegasw
      181 fekdaatgep tglivdgaay sllmqrisaa gllptgidly lksippwqkk lcaagvttvf
      241 dagffdasgd qsllyetlqt meragdlklr vvgsvavige iddpvgtlvr yrerydsplv
      301 karalklfld gteanhtayl lepyadrpdt cgaptmpadt fnrylveadr ananvmvhcv
      361 gdaavrmald gfdavnrtnp prdrrhvith aflthpddip rfrragvman tqlqwgvvda
      421 yteqlrdhyg herwsnmykf rtfldegvtv sigmdglacq crcqhkpleh iesghtrqla
      481 gepdapvfpd iaerlsipql iaaytihgay qlgmehevgs ltpgkradlv vlendlfevg
      541 qydigridvg ltmmggrith vgddfgartg mqac
//
LOCUS       WP_175925252             233 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia cepacia].
ACCESSION   WP_175925252
VERSION     WP_175925252.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..233
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25239
     Region          15..169
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mnaphcvtep nilyfgtpvv lvstlnengt pnlapissaf wlgwrgvigi aassqttrnl
       61 mrtgecvlnl pssaqadavd riarttgthp vpdgkrakgy vfepdkfgta gltatasqtv
      121 appralecpv hmeavvaath gigdeapdlr ghirvfelri qrvhvhpdll mdgyadridp
      181 dkwsplimsf qkfygleprq vhasrlaeip erayrspdie rsreagiltg agr
//
LOCUS       WP_175925347             418 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175925347
VERSION     WP_175925347.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..418
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44081
     Region          6..411
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtssqkaplv ivgasyagth laaaarelgf dgpivligde phapyqrppl skglltgktg
       61 mgqlalrspd fyteqcidlr vgqrataldl aarrvrladg ehleygwlal atgarcrplp
      121 vpgaelqgvh qlrtlddala vqrrlgrcss acivgggfig levaaalssa gtrvtvvesq
      181 trllarafpa fmsdyvahah rrrgvslelg rsvrallgrq gsveavqfdd grtldcdlvv
      241 tgigvlpnme ladaagiacd dgilvdalgr tsvrnilavg dvanmtqppf pgsparmrfe
      301 siqaasdgar aaasvlvgrp qplsavpwfw seqhdlrfqm aglpssgdqv vlrgapasdr
      361 ftvfylhdga maaahsvnrp sdhvlarkli aqrsripaat ladptadlrs midagqvn
//
LOCUS       WP_175925358             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175925358
VERSION     WP_175925358.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33840
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdnlgdirlf vetasqgsls aagrklglsp aaasarlvkl egelhtqlfe rstrklrltd
       61 egrlylvhcq halqtledar aalqagrasv sgalrvsats dfgrtvlrrw ldefnerhpn
      121 vtltlvlsds lshllqddid lairfgvpad ssmvakrmad nrralcaspd yiaahgmpnh
      181 pddlrehrfv ilssaagaan nwrfardget alftapldss rqtndgslar ewaiegrgva
      241 mksiwdigad lqagrlklll pewrcpdvpv nalfqrtqym aprvrtlldf lekqfsease
      301 alapflr
//
LOCUS       WP_175925372             167 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia cepacia].
ACCESSION   WP_175925372
VERSION     WP_175925372.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..167
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17833
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mysnilvald gsdtssrald aaltlaaetg arltpvyvvd flvpaydmyg ydpsilvdaf
       61 reeglrvted aarrlkardv agtpqisnve pagediprri vrladetgad livmgthgrr
      121 gfqrlflgsv aervlrlatc pvlmipancp pekpaetaaa stekess
//
LOCUS       WP_175925383             320 aa            linear   BCT 11-JAN-2025
DEFINITION  1-phosphofructokinase family hexose kinase [Burkholderia cepacia].
ACCESSION   WP_175925383
VERSION     WP_175925383.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003020
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..320
                     /product="1-phosphofructokinase family hexose kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008443 - phosphofructokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=33054
     Region          4..306
                     /region_name="FruK"
                     /note="1-phosphofructokinase or 6-phosphofructokinase II
                     [Carbohydrate transport and metabolism]; COG1105"
                     /db_xref="CDD:440722"
ORIGIN      
        1 mteivtvtln pavdvstsve hivdthklrc arprrdpggg ginvartvhr lggdcvalyl
       61 aggptgdvlt llleaehvps arlriagetr envcvtetat greyrflmpg psvtaaewrd
      121 caariaalqp aprylvlsgs lppgapddly atlartaaen gsrvvvdaag palraaldag
      181 vhlvkpslde lsalagepld easacrkage lvaqgradiv altlgargaw vvtreralrl
      241 pgrpaavcst vgagdsfvgg miwalargvp fddacryala asaasvehpg talctredve
      301 rihaelvaqa rgtamargaa
//
LOCUS       WP_175925466             401 aa            linear   BCT 11-JAN-2025
DEFINITION  zinc-dependent alcohol dehydrogenase [Burkholderia cepacia].
ACCESSION   WP_175925466
VERSION     WP_175925466.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..401
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41863
     Region          1..401
                     /region_name="FDH_like_1"
                     /note="Glutathione-dependent formaldehyde dehydrogenase
                     related proteins, child 1; cd08283"
                     /db_xref="CDD:176243"
     Site            order(38..40,43,86,162,166,185..186,188..190,209..211,215,
                     229,253..255,303,320..322,345..347,387)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176243"
     Site            order(38,40,60,162)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
     Site            order(90..91,93,96,104)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
ORIGIN      
        1 mkavvfhgig diridtvpdp evaaptdavv rltasaicgt dlhmvrgtlg gmkpgtilgh
       61 egvgiveavg rdvrnlrrgd rvlipstiac gscaycragy taqcdvanpg gpragtaffg
      121 gpadsgpfdg lqaeyartph ahaslirlpd aidddrailm sdifptgyfg aqlaevkpgd
      181 tvavfgagpv gqfaiasakl mgagrviavd riasrlemac aqgaeivdfs eddpvetvlr
      241 ltggigvdrv idavgvdamr athgpaaadr daarafdaev daiaprrnpd grnwvpgdgp
      301 sqvlqwavra vakagtiavi gvypptsrvf pvgdamnrnl tikmgncnhr tvtpplvelv
      361 rsgafdplsv ltrcepltna idayrafdvr epgwmkvkla p
//
LOCUS       WP_175925499             392 aa            linear   BCT 11-JAN-2025
DEFINITION  YncE family protein [Burkholderia cepacia].
ACCESSION   WP_175925499
VERSION     WP_175925499.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..392
                     /product="YncE family protein"
                     /calculated_mol_wt=41967
     Region          52..272
                     /region_name="Vgb"
                     /note="Streptogramin lyase [Defense mechanisms]; COG4257"
                     /db_xref="CDD:443399"
     Region          166..360
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mqprlrlhir fprpaivvaa alagfcaqga iaasavaavp gvppvinpdn lygeaqagrm
       61 saavagalpr iyvpnlrsnd vyvidpatyk vvdrfavgrs pqhvvpawdl rtlwvannae
      121 grtdgsltpi dpktgkpgpa vrvddpynmy ftpdgkeaiv vaeaharldf hdpgtmtlks
      181 slevpqckgi nhadfsidgr yalftcefgg klakidlvnr kvlgyleldr kgmpqdirvs
      241 pdgklfyvad mmadgiyvvd gerfaktgfi ptgvgthgly psrdgtklyi anrgsnlvhg
      301 prhgkgsvsv ldfatrkvva nwpipgggsp dmgnvsadgk tlwlsgrfdd vvyaidttsg
      361 tvrsipvgme phgltvwpqp gryslghtgn mr
//
LOCUS       WP_175925534             630 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia cepacia].
ACCESSION   WP_175925534
VERSION     WP_175925534.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..630
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=67582
     Region          12..543
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mlratasaaa adlivcngki atqddrqsfv talavkdgri laagsghdvm chahagtqci
       61 dlngrtvipg lndshlhmir gglnfnlelr wdgvptlada lamlrrqvlr tpaphwvrvv
      121 ggwtefqfae krgptaaeln aiapdtpvfi mhlgdsalln aaalraigyg rdtsnppgge
      181 iqrdrlgrpt glliarpdma vlhealerap klghddqmns mrhfmrelnr lgvtsaidag
      241 gdfqsfpddy gailalarrg emtvrvaysl fvqhagreld dyarwvtlak pgdgdaflrm
      301 ngagellvys aadfgnflep rpdlpaalea elaavvrllv rhrwpfrlha tydesigrfl
      361 nvleavnret pfdglrwffd hcetitdani ariaalgggv tvqhrmafqg eyfiarygaq
      421 aamrtppira mlaaglpvga gtdatriasy npfvslywmv sgrtvggtal ypernrlgrm
      481 ealrcytvgs awfsgeddck galvpghyad favltddyft idearitsls svltvvggri
      541 vhaddefasl appppavspa wspvaefgga grrrstesas lsaaagaaga gplaagaarg
      601 fgrafvqrlh aaametaeqc easgypgfay
//
LOCUS       WP_175925532             216 aa            linear   BCT 11-JAN-2025
DEFINITION  DsbA family oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175925532
VERSION     WP_175925532.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..216
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22702
     Region          6..205
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(14,17)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 mkpvevtvty dlicpwcwia ehrlaeaiea aglagavnvr fvpfelnptm paggidrkay
       61 rsakfgswar sqaldahvad agraaglvfd hariartpnt rlahrlvwfa qqhgsavalv
      121 dalfaayfrd grdigdtdvl vevaagagls gdavraflas gegldavval eeaavrdgit
      181 svpstrigtt vvsgaqpadv fraalldaqr vrnraa
//
LOCUS       WP_175925608             346 aa            linear   BCT 11-JAN-2025
DEFINITION  LLM class flavin-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175925608
VERSION     WP_175925608.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..346
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37903
     Region          37..335
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 msnvridhia fltpgnyage daaagfeqtl elfsagealg ydsawvrqrh leravssaat
       61 flaaatqrtt riglgaaviq mgyenplrla edlatvdvls rgrlnvglsa gapnhgallg
      121 erlfdtdpdl vdfsharvar lrrnlagdwl gdddtfvesa agrvrprvsp fapgltgrlw
      181 ygggsrrsie waarngfnll ignittgegt dshidaqlrq ldlyrdhwhe ahaprialgr
      241 vivptdgasa kereryrafa dtrhartlap qgerrtlfap dlvgssdeiv erlladpvvg
      301 qvrelrlelp ydlpfenyrq iledfitria palgwqpvdr pepaaa
//
LOCUS       WP_175925621             244 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175925621
VERSION     WP_175925621.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..244
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25745
     Region          <61..>98
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          127..235
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 mtaafvlhra dgapcstsfr kqafgdgdpf arhreiaweg pdsmaagria fvgeldvarf
       61 phietiavie geltleaaga aplvlgpgeg avigagtavr iraesrvllm fcaaacttpt
      121 khglfplrad adfkpsaslp pevllgpapq crsdnvfldd gagycagtwd stpyhrivrp
      181 hrvnefmlll agsvrfadpd gsvlslgigd alfvprgasi gwesservak fyvvqnvpas
      241 terd
//
LOCUS       WP_175925653            1075 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia cepacia].
ACCESSION   WP_175925653
VERSION     WP_175925653.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..1075
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113613
     Region          1..1057
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mwivrlalrr pytfvvlall ifiagtlail rtptdifpni dipvvsivws yngfsaedma
       61 krittnyera ltsdvddieh iesqslngvs vvkiffhpga dinraiaeas snsasilril
      121 ppgtlppnii tynastvpil qlglssstla eqqlydlgns firtqlatvq gaavplpfgg
      181 kvpeivvdln mralqakgla pidvvnaina qnlilpggta kigareynvq mngstqtvaa
      241 lndlpvktvg gnvvyvrdva hvrngyapqt nivrsdgkra alltvektgs astltiigqv
      301 kamlpkiaag lpkalhitpl gdqsvfvkaa iqgvareali aacltalmil lflgswratl
      361 iiavtiplav ltslcalaal getinimtlg glalavgilv ddatvaieni thhlergapl
      421 eeailtgage iavptfvstl sicivfapmf lltgvarylf vpmaeavifa miasyffsrt
      481 liptlamvlm rakgqgktpr gifarfarfq aafehrfeav raryrallsa aianrrrfaa
      541 afllacvast slfavagqdf fpsvdtgeir lhlraptgtr ieetarltde vetrirsvip
      601 anelagvldn igvpvsginl tydssdpvga gdadimitlk pnhrptaqyv tklrnllnqa
      661 fpgvtfaflp adivsqilnf glpapidiqi vgnrldanra vanrllaqlr gvrglvdari
      721 qqpgdapain vdvdrtkaiq aglqqrdvaq nllislsgss qttpnfwlnp angvsypvlv
      781 qapqydvnsl qslaniampt aaqspqtpag gpaagagaqn llgtlgtfsr aeqqavvshy
      841 nvqpvldifa svqdrdlggv tadvtklvda araqlppgss ivlrgqmqam hqsfagllsg
      901 lvlaialvyl lmvvnfqswl dplvivsglp aslagiawml fvtnttlsvp altgtilcig
      961 iatansilvv naarelsagg tppwqaalda gfsrfrpvvm talamligml pmalglgdgg
     1021 eqnaplgrav igglafgtvs tllfvpvvfg fvhawlerrr daaaarrvpd tpalp
//
LOCUS       WP_175925643             701 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cepacia].
ACCESSION   WP_175925643
VERSION     WP_175925643.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..701
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75551
     Region          7..701
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 msrrnwaaap maivvgatgv gtadaqeatl ptieisgqra sapfrtrdst satrgdadvm
       61 eipfavssvd akliqtvaat rgddlydwva gvsrqnnfgg lwdnyavrgf agdgntsgtd
      121 ylvngfswnr gmsvprdtvn lermevlkgp asalygrgdp gglisyttkq pqfarantvg
      181 vsagsygalr qtldstgpvt kslayrfvam nenngsfrdt vsskrylfsp sftwdigadt
      241 tlhyefesar qrapldrgvl avngqlgaip asrflgeprd gdydvrdtgh qftlehrvda
      301 nwsvnagfaq rttdlsgrss eafalqpdgr tlwrryrqva fhsndlqgri eaagkfstgg
      361 ightlvlgvd ayrfnydqfv arstptaaap yaidifdpvy gqpaptprta tnllerddgq
      421 glyaqdtlaf gphwkilagl rwdrfhqsve nrlkgttssq vqtalsprig ivyemspals
      481 lyantaysfr pnngadvngn afdpekghgy eagakwagar wlatvaafyv nkrnvltadp
      541 anagfsraag evrsrgvele wngdlghgvr glvnlayvda evthdavltp garlvgiprl
      601 sgsalllyet avpfadkaga gagliyvgrr agntantqdg felpayatvq lngyvqvnkh
      661 lrasvvlnnl fnrttyvssy nslwvtpgap rslfaslayt f
//
LOCUS       WP_175925660             199 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cepacia].
ACCESSION   WP_175925660
VERSION     WP_175925660.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..199
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21388
     Region          2..195
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mptfqvmlkm alyvslvlat pgptntllls sgirvgfrqs srllvaeasg ygfaislwgf
       61 flatfaatrp wlydvlklgs sayifylalq lwksphldgi rsgtigfrdm fvattmnpka
      121 llfataifps qafvsvpfyl csiavftvla vtigsmwlvv ggvltarrsl athtgtllrg
      181 asvvlamfag tlvfsvlnr
//
LOCUS       WP_175925683             342 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175925683
VERSION     WP_175925683.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..342
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34469
     Region          13..334
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mnrildrapp gaafsrlpgt fgaqfwlrwg aalafavvca vfaassplfl tvanlanvlq
       61 qsavvgilgf gltavliggg pdpirggldl svaanmglca avqavalrdg apdgaalalm
      121 latgaavgal nafavialri vpllatlttm nlcagfelvl tqntsvaaas pvlaflidsg
      181 pfdvphlapa llivallsgv llhrtrfglr laatgahrda araaglrvna yvaasyvlsg
      241 vsaalaalas sallsgsspg agenllavva vallgvvfsr rlvptipgtl laalfvgivg
      301 ngfqldnvss ywvngvegal ilfvvattal irrrhtehha hd
//
LOCUS       WP_175925692             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175925692
VERSION     WP_175925692.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33128
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..295
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,190,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mqnldallif arvaemtsft raaeslgiqk grvsmvirel erdvgvallh rttrrvqlte
       61 dgrafysrac dllaevqelq smfsgngtpl rgrlrvdmpt elarsvvipa lpqlmaahpe
      121 lelelsstdr rvdlvqegfd cvirlgpivd etliarplgk lrmtnaasps ylarygtpht
      181 lddlrtqghr mihytltlga rhagweypdg dgyaslplps amqvnsvqty haaglaglgl
      241 iqagyptlah yiesgalvev lpdlrpepla aslvvahrrn lsprvrafmd wiegvlepyl
      301 d
//
LOCUS       WP_175925730             344 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cepacia].
ACCESSION   WP_175925730
VERSION     WP_175925730.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..344
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36165
     Region          109..316
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mkivkpllia aavaavlsas ttafaagadi vrpdtttsaf laalngqkgp gletlspaka
       61 rqvlvdaqng tkvdlsgidv snrtveqdgl svpvtivrpq gatgtlpvfv fihgggwvlg
      121 dfptherlvr dlvvqsgava vfvnytpspe ahypvainqa yaatkwvaah gaeigvdgsr
      181 lavvgnsvgg nmaavvalma kdkggpairf qglmwpvtdh nfntgsynay qqghfltrpm
      241 mkwfwdaytk neaqrneiya splrastaql kglppaliqv aqfdvlrdeg eaygrkldaa
      301 gvdatttryd gtihdfglln alagdaptka atkamanela trlk
//
LOCUS       WP_175925755             322 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175925755
VERSION     WP_175925755.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..322
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35112
     Region          43..196
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <196..305
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 meidarttpl qrtapdhapr sltarlaali aayaphdgtf elpvrglria rvsaspphwn
       61 hgvhraclsi vgqgakstrv gdaayvines rmlvttadlp vtgrvtrasp aepflcaqle
      121 ldpariatlt prvfprglpk tvdcgaldth dappeivdav vrlmqliahp ddidllapli
      181 vdeilirllr gpsgarvaqv gqddsttqri sravawirdh yldpmtvesl arqvdmspst
      241 fhhhfravts msplqcqkml rlqearrlmc lsamdaqqac rsvgyvsasq fsreyarlfg
      301 dapgrdvvkl rdqavplsrv ap
//
LOCUS       WP_175925842             254 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175925842
VERSION     WP_175925842.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..254
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=28143
     Region          2..218
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mhalivvahp epqsfnaals haaadawraa ghtatvadly adgfdpceap rhyadrldta
       61 rfdaqreqrh hwergtlape vghhvgllqq adalilqfpl wwfgapailk gwmdrvfvyg
      121 glyssrrrhd sgvlhgrral lsvttgssaa acapdgregd trlllwplmh alryvgfdvl
      181 ephlihavrs dpagdnarld darlaqalad yrarlrawht wprvpfnrdt dfeagvrlkp
      241 dapaygpfir hagp
//
LOCUS       WP_175925981             467 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175925981
VERSION     WP_175925981.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..467
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50656
     Region          21..435
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(31..32,35..36,39,71,121..122,124..126,129,149,
                     152..153,156,271,274..275,278..280,283,310,314,363..364,
                     368,372,388,391..392,395..396,399)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mspvaarler lpfsrfhfkl limgglgfmf eavdaaiiaf ilpvvrikwh ltsfetgllg
       61 sstyvgflvg alfagllgdr fgrrvvmmwa ltffcvltfa nafvndwhtf allraiagig
      121 mgaegaiiap flvefvsnry rgaftgalag ffsfgfvaaa ligyfvipln pegwrialii
      181 vsapvvvllw wrrslhespr wletrgrhae aeavvadier riersgvtlp pvqsggvnia
      241 tyehagsffg nlkllwqrpl akttlmtwcl wlsvtfcsya ffvwipgllv qhgmtitksf
      301 svsiaiylaq ipgyyssayf ceklgrktti vtymglacas giwlasagsd tsivlasiam
      361 sfamngvnag eyaytpevfp thlratgmgt asafgrlgai cspmlvgyiy plwgfagvfg
      421 mttvmlliga laviflgvst tgktleeita deygstdada ralhtak
//
LOCUS       WP_175926000             312 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175926000
VERSION     WP_175926000.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..312
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34675
     Region          7..>129
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..283
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,162,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mirlddvqif vhtvdygsfs eaarqlniap ahasasvqrl ekaldtrlft rstrsmqlse
       61 agerylphar vmigaleqgq qalvngreal sgplrlsaps dfgrnlllpw ldefqhqhpg
      121 lslhlkmsdr aadlirqpld avvrygalpd ssllalklvd nnrralcasp sylkrhgapa
      181 kvddlrrhnc lryvwseqlh erwrftppgg ertvavtgnr isddadavrr wavageglvy
      241 ksrldliddl kagrlvelfp pedcepaplh licahraqlt painqlhffl rercsallas
      301 hpyggtqavl at
//
LOCUS       WP_175926035             208 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia cepacia].
ACCESSION   WP_175926035
VERSION     WP_175926035.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..208
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21733
     Region          1..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mshpswlpfi atslliivtp gqdmvlvmsr tlsdgtragl vtaagvsvgl lvhtmlatlg
       61 lgallqasew lftalkvvga lyllylgitl lrssgelala sgdgaqasrl rtfaqgalsn
      121 vsnpkvalfy laflpqfvpe gaahpmlslf vlgatfaglt flvkgpvavf agllsasirr
      181 npriltrmhr vsgvvllglg vklalerr
//
LOCUS       WP_175926084             290 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia cepacia].
ACCESSION   WP_175926084
VERSION     WP_175926084.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..290
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30794
     Region          12..280
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mkkiqgvysa prghwvgdgf pvrsmfsyqs hgahlspfll ldyagpatfe pgsasaprgv
       61 gqhphrgfet vtivydgeva hrdstgaggv igpgdvqwmt aasgilheef hsegftkrgg
      121 plemvqlwvn lpardkmgap gyqtlldadi pvvelpdgag rariiageld grrgpartht
      181 pidvwdvrlv aggharfpva egrtlavvvl sgtvqvnget vareaqfvql grdgsdveie
      241 aigdakllil sgepidepvv gygpfvmnsq aeirtaiedf nngrfgqmpa
//
LOCUS       WP_175926098              93 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175926098
VERSION     WP_175926098.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..93
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10116
     Region          1..93
                     /region_name="COG5606"
                     /note="Predicted DNA-binding protein, XRE-type HTH domain
                     [General function prediction only]"
                     /db_xref="CDD:444337"
ORIGIN      
        1 mtneryasvw daiegqppea enmklrselm ialkqriaql elsqaqaakq lgvtqprvsd
       61 llrgkinlfg ldalvnmaaa vglrvdlqvr esa
//
LOCUS       WP_175926195             328 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia cepacia].
ACCESSION   WP_175926195
VERSION     WP_175926195.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..328
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34414
     Region          7..324
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mndndhrpvr fgiigagsia rrfaqslahv pgatlagawa rradaaaafc gahggspaas
       61 leallasdid avyiatlhds haqytlaala agkavlcekp atlnaaqldt vlqaardagr
      121 lfmeamkppf fplyrqlrah lqddpigeir lvragcasss vpgdhsvyrl draggalldi
      181 giyetflavd wlgaaldvqt lgrvgatgvd lfaslnsvha hggiaqlfcg ldvmgrgdal
      241 iaaagghvti hekwwnpera tisyadgrtv eldtpaeggg lnyetahfcd llragktesp
      301 imthdhsrqm iamtdaaraa lgvrysge
//
LOCUS       WP_175926200             147 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia cepacia].
ACCESSION   WP_175926200
VERSION     WP_175926200.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..147
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15538
     Region          27..147
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mtvvkrpnvs skialtggah miaslgilvp veddrfravv dfyrlalalp vhsegvsaag
       61 npwhrfvigg atltvhtgsg grfpypefrp tdhgialave vphvseavar lescrvgiln
      121 kwdygdgtva isvadptgnv ceiwgrp
//
LOCUS       WP_175926242             275 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cepacia].
ACCESSION   WP_175926242
VERSION     WP_175926242.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..275
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29111
     Region          66..269
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mtilyrgmdr aaldaaylnt kvvpdfsall asmqarsaal ydttrgrrdl rygaqpaqrf
       61 dwlscgrpds plfvfihggy wqhcakedfa yaasgplalg fdvilaeytl apvatmtgiv
      121 geigalldyl andpdaigta grpihlgghs agghltavyr ahpavvsala isplvdlepi
      181 slcvlndklq lsarevdays plrhvgpgap tvvavgdael pelvrqardy ataceaager
      241 ivhvglpgmr hfdvlddlak pdgamlaalq siapr
//
LOCUS       WP_175926244             486 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175926244
VERSION     WP_175926244.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..486
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51935
     Region          57..466
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(67..68,71..72,75,109,159..160,162..164,167,187,
                     190..191,194,306,309..310,313..315,318,345,349,398..399,
                     403,407,423,426..427,430..431,434)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mnshsldlgg ntgepaparp aaaagtgaag salparrvtl gdfmddlpvg alhrfvvwvi
       61 giglffdmye iflvstigsa lqneyglsrq stdfklllas afigmfvgam clgsladrig
      121 rrkaflltlt wysafslvga fsvnadmlva crfltgigvg aiypvadsfl seilpkekrg
      181 rlaawaytts yvavplvgfl alwlnplhvg gvagwriila igslgavyvl fvqhrlpesp
      241 rwllaqgrta dayaalrrfa dgtgvrvpeq faepvepqrp lglgeriall rrepygaryl
      301 mlaifhlfqg fgyygfgtla gtvvksrgfd vtdstlfial sfigypvgsl lsipllnwie
      361 rrtlviasil siaafglcfa ysgqtvlivg fgflttcasn vfsnayhvyq aeifparvrs
      421 taigstyals rivsgalpfv llpvlggyga gamfgvisva lgivavtlrv fgplttrrsq
      481 deinpv
//
LOCUS       WP_175926261             379 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia cepacia].
ACCESSION   WP_175926261
VERSION     WP_175926261.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..379
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40725
     Region          1..379
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mpfdwtqeqh atlarfrdig teiaaaerda rapagldaag wtrlgqeglw dmivpetygg
       61 dghgwwhfsa aleglastir rpalllsvia qagmvraler ygtatqqdry fgailrgels
      121 ataiaepgtg tdvrsiatkl vehgdgyrlt gskfniahap larfilvvtr vetlgrrnta
      181 lvivdrdqpg mtvaapdskl glddlptgal hfddcpiarg qllgepgagl gnlidiislg
      241 rlyyglvaaq vtapylrdai aycrdrrsfd stidahqyvq rrlvdlqigi ergtwlarga
      301 laqlltdhpq almtcsiakl vgaqdlvdga lglvrlygsl gyqagpvaaf asdalgfmsv
      361 ggteemhrkn ifnqmmrag
//
LOCUS       WP_175926289             330 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Burkholderia cepacia].
ACCESSION   WP_175926289
VERSION     WP_175926289.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..330
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=36541
     Region          6..285
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mgplsatfde ileacalgrs gpprqvserv whlptddggv avklyasghq araareaavl
       61 ahvethgdtr fhvqalkrta agaplwtgan ahamltrwep gqfrtydtfs paewdalgas
      121 laalhlsler lqlpsldtir arliaidada vrrslldaln rarsnenaan lrryvdlalr
      181 mldryypgsi dafpaddpqh pihndynqfn ylftgtlppl ildweatiga preyelvrcl
      241 nhlpleapql aeafvrayrr vrpvdparia wavdaaclqh alklwivqgw lddpsrfash
      301 lsgavtmasa mvdardrlvd ffsrcieagr
//
LOCUS       WP_175926364             356 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175926364
VERSION     WP_175926364.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..356
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38680
     Region          1..352
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtflqldalq kryagavavh dvsltvergq fvsllgpsgc gktttlhmia gfvtpsagsi
       61 rldgrdllai kanarglgiv fqsyalfphm tvaqniafgl etrrvpraer qrrvahalel
      121 vrlaalgdry paqlsggqrq rvalaralvi eppillldep lsnldaklre dmqdelrriq
      181 qrtgtttimv thdqaeamal sdcvavmngg rieqagtpre vydhprttfv atflgktnmi
      241 dgeatpgpdg aiqirthgqc lqttqrtlir ghtrvslrpe nidllpnaad adkdgctvtg
      301 tvsartyggd hwmyeidtal gvlrvrspyg eaaeghlvgl rwrpddlrvv teagha
//
LOCUS       WP_175926400             692 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia cepacia].
ACCESSION   WP_175926400
VERSION     WP_175926400.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..692
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=78269
     Region          1..668
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mtiqsdlrft ftagdesfev veftlhegls etfllqvela sanaaidfgq vldcngllti
       61 wqggvpvrfv hgavssfvqg dtgfrrtryv avveprlarl klssdwrifq tlsvpeiatv
      121 vlkahhqtld yeqrvtnehl areycvqagd tdydfveril reegffyafq hkvdghrlih
      181 cdrlfifgrq qcepvlyhpt pggdqsdpcl rtfaytenvr tarqvqrdyt ftspryphey
      241 pregtdldhq grgyarydyp grykheasgk aftqdrlrgh rrdarmarvs gddarlqpgi
      301 afdltghpre dmnrgwrpvs ivhhgvqyts qaeegadaqq gthyryeavl vpddaewrae
      361 plprpridgp qpatvvgpeg eeiytdaygr vkvqfpwdre gkydehsscw iqvaqnwaga
      421 twghmaipri gqevivvnld gdpdqpliig raynrlqlpp yelprhktrm tiksqthkga
      481 gynelrfede kdqeeiyvha qkdqnihvnh dettfvgndr seqvehdeti aigndrketv
      541 grdeqvtigq drrhdigqdd flsigrnhti htgkdrteev gnhrrdktaa nhtvdigghl
      601 eqrvqgrael eagqairhrt kvvelhagev irlrgpggti tlddggitld avvirfkgpl
      661 tadsvgrgnr lgidgnplpg eptdptdlpl se
//
LOCUS       WP_175926442             369 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175926442
VERSION     WP_175926442.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..369
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39020
     Region          1..367
                     /region_name="LhgO"
                     /note="L-2-hydroxyglutarate oxidase LhgO [Carbohydrate
                     transport and metabolism]; COG0579"
                     /db_xref="CDD:440344"
ORIGIN      
        1 meqmdcvvig agvvglaiar elaargretl vleaadaigt gtssrnsevi haglyyprgs
       61 lkatscvhgr dllyefceth hvphrrtgkl lvatsvaqvk qlkaiaaraa engvldlmpl
      121 traevqtlep alecvealfs pstgivdshq lmlallgdae hdgavcalks pvesidvlrg
      181 grfvvrtggd apaeieaacv insaglgaqa larrtrgldp rwvpplylar gnyfslsgra
      241 pfshliypmp draglgvhlt fdlggqarfg pdvewcdslr yevdparata fyasirafwp
      301 glpddalqpa yagirpklag pgeppadfiv qgaaqhgvrg lvnlfgiesp gltaslalaq
      361 rvgdmaayr
//
LOCUS       WP_175926454             314 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175926454
VERSION     WP_175926454.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..314
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34320
     Region          35..186
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <164..296
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 msfeplfadt gdrvqrrmie lhtrlapneg dtlaaldgvr lirvsrpapr mpvlyepnii
       61 vvcqgrklgy lgdrsfvyda qqylvlsvpl pfecetfasm depflaisir vdlaviaela
      121 llldetlgaa aseplgvyst pldapladav vrllevlasp hdtrvlgpai mreiayrvlt
      181 gaqgdairaa lvqqhhfgri akalrrihae lktdldvetl areagmslav fhahfkhvta
      241 tspmqyvkaa rlhqarlmmv qdgvgagtaa arvgyasasq fsrefkrlfg rspgdevrwm
      301 reigirpava dtda
//
LOCUS       WP_175926503             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175926503
VERSION     WP_175926503.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33139
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..290
                     /region_name="PBP2_CrgA_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08475"
                     /db_xref="CDD:176164"
     Site            order(103,107,146,161,163,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176164"
     Site            order(104..105,109..110,112..113,116,120,122..128,190,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176164"
ORIGIN      
        1 mtdrldgvtt fvqvvesgsf alaaerldmt rsavgkavar lekrlgarll qrttrsqslt
       61 ddgqayydrc vralaeleaa eadldcgrne prgklrlsvp lafghhcvtp vvldlartyp
      121 dlridvsitd rfvdlveegi nlavrigtla dstslavrrl gtqygslgaa psylarhgmp
      181 ktlddlkhhr tiaysrsgvv qpwdlrapdg ttvridmphq lsfddvqaia aagasgfgia
      241 wlpswlldhy vkrgemtvvl drcfvcegdi haiwpktryl prktrcvida faqaippmie
      301 r
//
LOCUS       WP_175926522             257 aa            linear   BCT 11-JAN-2025
DEFINITION  thioesterase II family protein [Burkholderia cepacia].
ACCESSION   WP_175926522
VERSION     WP_175926522.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..257
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=28697
     Region          17..250
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 msarpigsnw irelrlspcp raqlvcfpha ggtanffrnw sralpwdvdl lalqypgree
       61 rfgepcptti dalagpaada lqryahaplv lfghslgaal ayevavrlea rgaaplylav
      121 salppphrqr lsdlhlqsdd alvadvarls gehaalladp emraiylpmi rhdyraiety
      181 rrdrpprldt plgvmlplad seldddeaha wqdvasrpir ietfsgdhfy lrhqypalia
      241 hlveridqsl rygkeyt
//
LOCUS       WP_175926551             389 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Burkholderia cepacia].
ACCESSION   WP_175926551
VERSION     WP_175926551.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..389
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40135
     Region          61..369
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mnmikridpr rpfiitaagl kritlgeegs adanaahwsa hghgaaaakp rravqdpkhv
       61 mlvvahgerg alddhsrqai aaaalladaq tevallafge lkddvaelgv dklleltgfd
      121 rrtfdpesel qalqacvaal apkhvfvpdn atgdgdlgrr yaaaagasva thvveidakh
      181 vgayaqagra fatralpdvv llaqnavdak lpfvgagerl aadfirpahd aaqpyrdlgl
      241 deidaaqval eeadfivsag ngvsdigafe rlagvfgaai gasrvavdng hftrdkqvga
      301 tgktveasvy iafgisgavq hlqgikdcrh viavnldgsa piakranltv vgdaqatiaa
      361 lieqvqaara argespaavg trepegvaa
//
LOCUS       WP_175926602             722 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cepacia].
ACCESSION   WP_175926602
VERSION     WP_175926602.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..722
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77642
     Region          26..722
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mpsrrtprrv rtprpwrssl palitlcvas gahaanaeag atasapatpa gkelpainvn
       61 asstvdptig yqprtssiag gsdrplkeip qsvavvsssv mqdqqarsld dvlgnisgvt
      121 qtntlggtrd afikrgfgsn ndgsvlvdgv rtpvlhsyla tidrvevlkg pasllygmqd
      181 pggvinlvtr kpedtfggsl sasrtnhggs naqfdltgpl gkpgqvaggt lafrltgeyd
      241 tsrywrsfgr ernaliapal swhdantsid vsyqyvdytm pfdrgtvlvn gqlddalryr
      301 ryeeawsqss giqetlrtri ehrfsdawrv ratygwgrdr ydqtitrgns fnsktgamtr
      361 ssdanlgrnd sdqiatlgll gnvtlagmnh aiyiggeyer qrsfrgdtir gkattgfnly
      421 dpvygllaag gtpnakqsds rsvvhaysti vqdsvkiidr ltavgglrwe nwqqesgmgr
      481 pfvfadrsrg svwlpqfgla yaltpaltay anvsrsfkpn vasnvaapla peygrvleag
      541 lkfslkpait gtlavyqidk rnvavtvgdi tstigtarsr gieldvagqi trhlsvigsy
      601 aytnatdrds ntpltnvarh tgslfavydt aianlpgrwr fgggarlvga rsgdtansft
      661 lpgyvtvdaf aayettigkf ptrfqlnvkn lldktyypss nnnlivavge prlvtltttv
      721 sf
//
LOCUS       WP_175926605             143 aa            linear   BCT 11-JAN-2025
DEFINITION  GFA family protein [Burkholderia cepacia].
ACCESSION   WP_175926605
VERSION     WP_175926605.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..143
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15220
     Region          3..130
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mtrtysascl cgtvtvtlrg epaaranchc atcrdfygtp vlsatawppe qvavegghat
       61 fphpaksmar tycascgeiv cgtnrfgmrv vpnslaarah ggqlpgdlqp tmhlfyrhrv
      121 idvvdalpkf ldgwdgptld dan
//
LOCUS       WP_175926652             515 aa            linear   BCT 11-JAN-2025
DEFINITION  FGGY-family carbohydrate kinase [Burkholderia cepacia].
ACCESSION   WP_175926652
VERSION     WP_175926652.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..515
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=55088
     Region          3..448
                     /region_name="ASKHA_NBD_FGGY_RrXK-like"
                     /note="nucleotide-binding domain (NBD) of Rhodospirillum
                     rubrum xylulose kinase (RrXK) and similar proteins;
                     cd07804"
                     /db_xref="CDD:466806"
ORIGIN      
        1 meyvigvdig tqstkallvd rhgtivarrs aayqpdtprp lwaeqwpqvw fdavlecigg
       61 cvsdaraqgv padairavcv gslyggsgvp vdsdmrpvhp cliwmdrrat aevdwinanv
      121 nverlrvitg ngvdsyygft kmlwlrdqrp dvwanvryfl ppnayviyll tgevavdhss
      181 agniggvydv arrewsddal dmlgipatmm perlvestdv vggllsqwte plglpagtpv
      241 vaggvdaava tfaagatrag qhvamigtsm cwgyvsrhvd arhglvsmph vfdgqrdlyv
      301 fggaitagas vawfrdqfch aeidaarllp hgdphmllee aaesvppgad gvlflpylmg
      361 erspvwdaka sgafvglsla htrahlyrav legvafalrh nieagrrgaa alddrlivvg
      421 gaahsalwmq iiadvtgfpv wtieqdveaa mgaallagvg vglvshedaq ggwvtlvera
      481 rpdaeraaay aarfalytal ypalapimhg lhtps
//
LOCUS       WP_175926753             533 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia cepacia].
ACCESSION   WP_175926753
VERSION     WP_175926753.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..533
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57005
     Region          10..449
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msttsslnle gklrrdagii gllfasttsm vgsgwlfgay hasriagpls igswvlgaii
       61 imlialcfae laamfprsga lvhmshashg vglgriwcgl lflayapvpa veaeaivtya
      121 nnylpwfiqp gsaglltaig fmacggllgi mallnlmvir wllsvnstit wwkilvpllt
      181 iaglmgasth wgvmqaapds yhlsgmftal paagivfsyl gfrtaidlgg esanphrnip
      241 lavigavlla aviyillqia fiyalapadl aagwnhlsfk gemgpfagla atlgmgwmat
      301 llyidayvsp ggtglmyvtg gsrilfaage ldagprmltr lnsnkipwva vlimwavgvl
      361 fllpfpawqq mvsyitsitv ltyglgpval lvlrrnmpdl erpfrmsgag liapiafvcs
      421 nlviywtgfk tnnflfslva igfvlyalyh hvvlrrsard fgwkhiawll pwfgglwlls
      481 wmggiggglg vigfgwdill vvvwslvvla lamrsalsag etsemmgrmn ets
//
LOCUS       WP_175926804             164 aa            linear   BCT 11-JAN-2025
DEFINITION  arsenate reductase ArsC [Burkholderia cepacia].
ACCESSION   WP_175926804
VERSION     WP_175926804.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Messens,J. and Silver,S.
  TITLE     Arsenate reduction: thiol cascade chemistry with convergent
            evolution
  JOURNAL   J Mol Biol 362 (1), 1-17 (2006)
   PUBMED   16905151
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Mukhopadhyay,R. and Rosen,B.P.
  TITLE     Arsenate reductases in prokaryotes and eukaryotes
  JOURNAL   Environ Health Perspect 110 Suppl 5 (Suppl 5), 745-748 (2002)
   PUBMED   12426124
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Messens,J., Martins,J.C., Van Belle,K., Brosens,E., Desmyter,A., De
            Gieter,M., Wieruszeski,J.M., Willem,R., Wyns,L. and Zegers,I.
  TITLE     All intermediates of the arsenate reductase mechanism, including an
            intramolecular dynamic disulfide cascade
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8506-8511 (2002)
   PUBMED   12072565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..164
                     /product="arsenate reductase ArsC"
                     /EC_number="1.20.4.4"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030612 - arsenate reductase
                     (thioredoxin) activity [Evidence IEA]"
                     /GO_process="GO:0046685 - response to arsenic-containing
                     substance [Evidence IEA]"
                     /calculated_mol_wt=17508
     Region          4..143
                     /region_name="LMWP_ArsC"
                     /note="Arsenate reductase of the LMWP family; cd16345"
                     /db_xref="CDD:319973"
     Site            order(9,11..16,112,114)
                     /site_type="active"
                     /db_xref="CDD:319973"
ORIGIN      
        1 mttnvlilct hnsarsvlse gmlnhwaakl gkdvraysag sapsgrlnpf alealtnagi
       61 dvsgyrsksw defvgdgape mrvvitvcds aaaetcpywp gspvkvhwgy adpsnalggd
      121 egkrlafelt rqaigyrmlq llalpldris iaelqtalse isqn
//
LOCUS       WP_175926686             541 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia cepacia].
ACCESSION   WP_175926686
VERSION     WP_175926686.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..541
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59256
     Region          2..537
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mqyadtayln gllytgdaqr rfaqalatrd gkivavgrde dirpligpat rtvdlagrlm
       61 lpglidghvh pleghqilgd fdlsgindpd tilqriraca datpnepwvy lgganlaafg
      121 ayptrelldr vvpdrpllvv gfdvhsgcln tkgleaagih adtpdpaggv yerdasgapn
      181 gvvheaafyr vcplipqlsp agypkslaka hamahgygit gwfdarveea elkayadaqr
      241 agtlkvymsa glyanprrdp reqverfaaw rrayecdnlr lhtvkifvdg vpesktaall
      301 epyagtddcg lalwsqdaln eiclladsag fdlhfhtlad ravrmtldal eyvqirngmr
      361 drraqlahlq lvdpadmsrf nrlgaiasvq tlwtaareeq qqlyrdllga ertarnypfr
      421 slrnagamla agsdwsvstm dpmqiiqtgv thllidqpds ppwnpherld lltmldaytv
      481 ntayalrfdd ctgsleagkd asfaildrnp fahpvetfaq trvietcfrg evvyaapgwa
      541 d
//
LOCUS       WP_175926830             205 aa            linear   BCT 11-JAN-2025
DEFINITION  SCO family protein [Burkholderia cepacia].
ACCESSION   WP_175926830
VERSION     WP_175926830.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..205
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22400
     Region          51..205
                     /region_name="Sco1"
                     /note="Cytochrome oxidase Cu insertion factor,
                     SCO1/SenC/PrrC family [Posttranslational modification,
                     protein turnover, chaperones]; COG1999"
                     /db_xref="CDD:441602"
ORIGIN      
        1 mlqsrfgrra rqgwmlacaf taalllagcd napkfqnldi tgntqfgsdf slpdtagkmr
       61 tlgdfkgkav vmffgythcp dvcpttmael sealkqlgpd aakrvqvlfv tvdperdtpa
      121 llgqyvpafd psfiglrpad eaalkkvtkd frvyyakvpg ktpgsytmdh taasyvfdrd
      181 gklrlfvrdg qgpgpwvhdl kllvd
//
LOCUS       WP_175926862             203 aa            linear   BCT 11-JAN-2025
DEFINITION  trimeric intracellular cation channel family protein [Burkholderia
            cepacia].
ACCESSION   WP_175926862
VERSION     WP_175926862.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..203
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=20974
     Region          1..196
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mhtlyliaiv aeamsgalmg mrrgmdrfgl alvgavtalg ggtvrdvllg hyplgwiahp
       61 eylvitlaaa tvaswaarhv armktlfvtv daiglaafti igcdigastg aapiivvlag
      121 aitgvcggml rdllcnempl ilreelyasv afvtgalyvg mqhldvdaga atvvalaagf
      181 smrmlavrlg wkmrtfgaad vgr
//
LOCUS       WP_175926874             194 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175926874
VERSION     WP_175926874.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..194
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20089
     Region          5..157
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgvsrqqaae nrsaivaaae rlfrvrgvda vgltelmkea gftqggfynh fkskdalvae
       61 vmekamqdra dspnagslga qvasylsaah rdnveagcpl sgfagdaprl tdaaracyah
      121 glatyldrle rmvaveggtp aqtrrdaiav fsqmvgalvl sraiagtepa ladeilaagr
      181 daltagrddp vapa
//
LOCUS       WP_175926887             347 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia cepacia].
ACCESSION   WP_175926887
VERSION     WP_175926887.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..347
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37461
     Region          2..342
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mslefehvsf qypgarhgvd dvtlsaaqge llavmgrsgs gkstllrlaa glldgwrgri
       61 aiggddvagv pvwrrevgmv fqhyalfpnl svvdnvaygl kmrgvaadlr rrraldmler
      121 vglsahatrg vamlsggqqq rvalaralvi epklllldep laaldagirh qlrdeiralq
      181 racgattlfv thdqdealsm adrvaivggg rvlqagtprd lyerpataqv arfvghstll
      241 rgrvlahgei dvrfatlrae tgahrpgeqi avlvrpehvq adppmqstnr iegrcgevry
      301 fgatqrydfm pdgsadvllc egrepaahsi aieprhllvl paspdah
//
LOCUS       WP_175926940             158 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Burkholderia cepacia].
ACCESSION   WP_175926940
VERSION     WP_175926940.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..158
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=17404
     Region          5..153
                     /region_name="OsmC"
                     /note="Organic hydroperoxide reductase OsmC/OhrA [Defense
                     mechanisms]; COG1764"
                     /db_xref="CDD:441370"
ORIGIN      
        1 masgehkyrv avawtgnrgt gtsgyreygr dhviragskp eipgssdpaf rgdasrwnpe
       61 dlllasasac hklwylhlcs eagirvlayf ddaegtmvdr depgrfteiv lrphvtiqag
      121 ddreraehlh hdahakcyia nsvnfpirce ptiefaaa
//
LOCUS       WP_175926964             459 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia cepacia].
ACCESSION   WP_175926964
VERSION     WP_175926964.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..459
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49214
     Region          7..457
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mtqqqrtfdd ivareqglrh altsgqmami aiggaigtgl flgsgfaigl agpsvlvsya
       61 igalialllm galaemtvah ptagsfgaya ehyvgplagf lvryaywfav vfaigteisa
      121 iavfmkywfp avpgwywvig fsalliavnl asvtlygtve yafsllkiaa ivvfivlgay
      181 lvwsapvasg igfanytahg gfmpkgpwgt wvavivaifs ymsieavaia ageardpqha
      241 vtrafrstvf rlvlfylltl slmlaivpwt qagtdespfv kvmaathvpy aagvinfvll
      301 iaalsamnsq lyvttrmmfs lsrarlapav fgrlgtngvp raalwistsg vavaavlval
      361 apdtaftvmm aiamfgalft wlmifvthlr frsryrgpal afrmwgypfg sllgaglvaa
      421 ilfttaftre frmtmvvgvv fvvlltlaya lhyrhqhar
//
LOCUS       WP_175926967             454 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia cepacia].
ACCESSION   WP_175926967
VERSION     WP_175926967.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..454
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=48573
     Region          161..436
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 menlqsrlls hrlesvirdf hqpvmiwqaa ilvgalcfaw vtarfvhgri darrraagra
       61 pgagaqslkr alfplfgsvf vgaaqlafdp fmstsllsla lvplfgigli yvlfffarrv
      121 fardghthaw lsivekivst vvwaamvltv lgiqrdvlgw ldsvqfrvan ahltllsvis
      181 galwvcvtlm vamwlgsvle drltrastld anlkvvlsrv grallvfaai liglslvgid
      241 vtvlgvfgga vgvglgfglq kiasnyvsgf iilldrslrl gdaisvgglq gvvtqirtry
      301 tvvrgldgne tlipneklit dvvqnqssyl trgyakvavq vaytsdveha lvllaeaakd
      361 vprvlaepap tpylvgfgad gidlelgfwi edsakgtsgv rstvnrniwr lfsehgisip
      421 fpqrevrvvg lpdsfpaagv aagngavdgr apaa
//
LOCUS       WP_175926972             311 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175926972
VERSION     WP_175926972.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..311
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34182
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..294
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdkldqvrif lqvaemgsfi kaahaldvpr atvsaavqql etglgtrllh rttrqvqlta
       61 dgalllergr rllaeadeld rlfrrrdrdv igrlnvdvps riarrmvapa lpslfrrypk
      121 lqlslgstdr sidlvqegvd cairvgrlad sslvvrplgq ftlincaspd ylrecgvpeh
      181 pdalahghwa igyaspttgr eldweycsdg qrytltlpsr vivnnaetyi asciagmgli
      241 qiprfdvehl ldsgalvdvm pghraapmdv savyphrrhr srrlnafiew faalmadaln
      301 gtgatatatg d
//
LOCUS       WP_175926996             690 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia cepacia].
ACCESSION   WP_175926996
VERSION     WP_175926996.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..690
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=78112
     Region          1..684
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 maiqsdlrft ftvgdeafev veftlqegls dtfllqvela sanpaidfge vldrngllti
       61 wqggqpvryv hgaissfvqr dtgfrrtrys avveprlarl klssdwrifq tlsvpeiata
      121 vlkahnqtld yeqrvtnehl areycvqagd tdydfieril reegffyafq hkadghrlih
      181 cdrlfifgrq qgepvlynpt pggdqpqpcl rtfaytenvr tarqvqrdyt fksprfphey
      241 pregtdldhq srgyarydyp grykhessgk aftqdrlrgh rrdarialan gddarlqpgv
      301 afdltghpre dmnrgwrpvs ivhhgvqyts qaeegadaqq gthyryeavl vpddaewrae
      361 plprpridgp qpatvvgpeg eeiytdaygr vkvqfpwdre gkydehsscw iqvaqnwaga
      421 twghmaipri gqevivvnld gdpdqpliig raynrlqlpp yelprhktrm tiksqthkge
      481 gynelrfede kdqeeiyvha qkdqnihvnh dettfvgndr neqvehdeti aigndrketv
      541 grdeqvtigq drrhdigedg fltigrnhti ttgkdhaeev gnhrrdktaa nhtvdigghy
      601 eqrvqgradl eagqairhrt kvyemhaaea vvvkgpggtv ridssgitld avairvkgpm
      661 tqqgggdgnn lslgsqileg qqadclerar
//
LOCUS       WP_175927034             308 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175927034
VERSION     WP_175927034.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34150
     Region          16..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          101..300
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(116..117,119..120,123,127,129..135,229..234,
                     240..241,243..244)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mmhpdlrrld lnlllvfdal yrhrsvaaaa helalspsal shalarlrda igdalfvrlg
       61 nemqptvrad diatwagdal damskglara rrfdpaqsdr tfvfaatdyt afavlpafla
      121 riqhvaprlr irivhsdrki svdelaagri dfalgyhees aadapgiedf dwfsddyvvi
      181 asaahpdirr rltldqylaa rhvvvtpwne srgvvdhvld rlglarqvav qlptvlaapf
      241 viaesallmt vpnraalalr haapirifpa pfeiprytvk vyshakhart dahrwirtql
      301 learpepa
//
LOCUS       WP_175927036             362 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 9 protein [Burkholderia].
ACCESSION   WP_175927036
VERSION     WP_175927036.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..362
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40128
     Region          5..333
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mangnppqri lviridflgd mlcttaflga lkerwpgael hvvanrynaa alagnpdvdm
       61 ihtyvysrqc erndrpgrmr affdrlrlvr rlrrlrfdlv vvpnggmhrs smqfarqiga
      121 kdcrwhdaet efddrkpehv aqrpmcheal sgfrlvpelg radldrlels vhpdralqda
      181 whrllgartk prvglfvtnk aaerrwpaer whdlaerlap svdvivfrdp avghapedds
      241 wrdvnarhva pssvadlvaa aslldaivsa dsapvhlasa lgvpvaalfe drpekylrwh
      301 plgvphvilr agatvdaigv daveravrhl lpqathrdep ladaacprpa advatpvila
      361 as
//
LOCUS       WP_175927062             537 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175927062
VERSION     WP_175927062.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..537
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53695
     Region          23..500
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,279,282..283,286..288,291,319,323,375..376,
                     380,384,400,403..404,407..408,411)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mdqpfsaast qsarrrawvl aavcmaaval plsfsggava tpaigrdlhg gtvamnwitn
       61 afmlafgscl maagaladqf grkrvfaigv ggftlmsval afapsmlavd llraaqglaa
      121 aaalaggtaa laqefdgaar trafsllgtt fgiglafgpv lagalighgg wrtifvtsav
      181 agglslgfgl prmhesrdph atgldwpgta aftaaltlft fgvieaparg wsnalviall
      241 agaalgacaf vaietrvarp mldlslfria hfvgvqvlpv stcccyivll vvlplrfigi
      301 dgfseidagw lmlaisapml vvplvaatlt rwltagvisg lglliaaagl vwldvalrgg
      361 agpaaiapml aigvgagmpw glmdglsvsv vpkeragmat gifsttrvag egialaivga
      421 vlaalaqtgl rqaagaagtp aatlraaarl atgdlagaaa alpgvghaal lasyahafdr
      481 lliglagvtv lcavvvfvfl ggrrvaaeag dgadahahad vpvrsridaa ctethgr
//
LOCUS       WP_175927101             455 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175927101
VERSION     WP_175927101.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..455
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49182
     Region          23..412
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,154,
                     157..158,161,259,262..263,266..268,271,299,303,352..353,
                     357,361,377,380..381,384..385,388)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnppspalpg rdplasavsk vkwhvlplvl imfitnyidr vnvgfvdrhl easigigaaa
       61 yglgaglffv gyalfevpsn llmqrygarv wlarimatwg ivaaamafvw ndtsfyalrf
      121 llgaaeagff pgvvlylsqw lppqergkam aiflggsafa svlsgpvtga llsirgfgle
      181 gwqwmflieg lfsvalcgas wlllkshird atwltaeert alqnaldeer atrdvrsnvp
      241 vratallrdp qivlfcflyf siqltiyaat fwlptiirkm ggltdfqvgl yntipwmiai
      301 gamygfavls skwkhpqrwl afalvlaacg lfastshdpa wsfasicfaa lgfkaaaslf
      361 wpipqgyldt rvaaaviali nsvgnlggfv aptafgylkq htgsitggly alaiaslvaa
      421 vaalfarthr rsdpprglpa dtaltnasml rhaeh
//
LOCUS       WP_175927112             268 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia cepacia].
ACCESSION   WP_175927112
VERSION     WP_175927112.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..268
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=27795
     Region          9..247
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mharpivvvt adrilrgahp nhtagekyla alvdgagala fvlpalgarq padaivaavd
       61 gllltgsysn vephhyggaa sapdtlhdpa rdatalplir aaidagvpvl aicrgmqeln
      121 vayggtlhqr lhattgfddh rerpadpler qygpahvvqf apggllqria hgapeatvns
      181 lhdqgiaqlg aglvveasap dglveavsvr garafalgvq whpewryaeq plsrdifaaf
      241 gaacrarmth rihaaggamp spaasdvd
//
LOCUS       WP_175927162             454 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia cepacia].
ACCESSION   WP_175927162
VERSION     WP_175927162.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..454
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48015
     Region          220..408
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mrfdqrfrla reqgqparrg ascfpirrvl lrgviatacv agvhgaaaqa ahdaarlape
       61 ttdlvdvpff sstrttwggl rastaapldi ayplhasnms tdtgrddpva rfgacvayrv
      121 lcdaardave rgyasrfdyg lasalpamvt qpafergavd lalaepftla epgrgtragt
      181 iagslhtsla raelpagvaa qivrvlagri dpklrgetgd tfrvafepdg sttrpgrvrv
      241 taidirfrgq hvtgvwfapq agspgayydl dgmplagarf ampvaakris spfgtrvhpv
      301 sgarhvhsgv dlaapagrav hasergvvtf igteprgygk yvvirhdggy asyyahlsaf
      361 eptlrtgmrv vrgqrvgavg stgtatgphl hfevrrharl vdpialvqta kaaklkgeqr
      421 vafnrvarda rtqlasatwa qpvamsktsa shag
//
LOCUS       WP_175927186             375 aa            linear   BCT 11-JAN-2025
DEFINITION  J domain-containing protein [Burkholderia cepacia].
ACCESSION   WP_175927186
VERSION     WP_175927186.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10644999
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..375
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=42617
     Region          <210..250
                     /region_name="DnaJ"
                     /note="DnaJ molecular chaperone homology domain;
                     smart00271"
                     /db_xref="CDD:197617"
     Site            order(226..228,237,243..244,247..248)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
ORIGIN      
        1 mtarrgaavv iapghetasl skaqktfntl vqqiearrer lgawdavtpa fhkkfvdgll
       61 pleqaatalr isllnrldda flqkglskae qrtlsdvian mardlldvsd daqlkilynr
      121 hrasgdddgt aadrarpkqa pepapaptqe ddldtlspde laermqaeld eqfrrdmaeh
      181 eareaqrakr kkaprqsaaq arreaeqaes sksirdvyrk lasvlhpdre tdpkeqerkt
      241 vlmqrvnhay akgnllqlle lqleieqidr raidglgedr lmryngilee qvreldqeir
      301 hvethfrrty giassvkiap dtvmriltrd iagmqrsnqd ltiavrefdd pdnvrewlkd
      361 mkrrpassrf dddsy
//
LOCUS       WP_175927204             312 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia cepacia].
ACCESSION   WP_175927204
VERSION     WP_175927204.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..312
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33255
     Region          80..286
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mpidtdiasl lerlavtaap asldalrrat dttlrgwhgp leavdhtetf avptrdgqqi
       61 rvraywpava sesaarrpal vyahgggwcl gtlelydnpc ralanatqcv vlsvdyrlap
      121 ehrfpvpled fcdaldwvvr eaaglgldaa riavggdsag gnlaaaaclv arerggpsia
      181 hqlllyppld asmsttsyrt cgqgyyltqd vmrycfdmyl tdpadggspc vsplqaasle
      241 glppatllac eydpvrddah ayaerlreag vaadfvvlpg mihacihlag vtsaarqvfd
      301 vagaqmrraf qr
//
LOCUS       WP_175927285             409 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175927285
VERSION     WP_175927285.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..409
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42081
     Region          8..396
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(18..19,22..23,26,61,108..109,111..113,116,139,
                     142..143,146,227,230..231,234..236,239,269,273,322..323,
                     327,331,347,350..351,354..355,358)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mpdsryrwvi vaagglmgci aigamfslpv flralardtg wsmtgisgam tlgfiamafa
       61 smgwgslsdr vgtrtvvmtg avllsaslal asrapsllaf qltfglavgg ataaifapmm
      121 acvtgwfdth rslavslvsa gmgmapmtma plaawlvsvr dwrtsmllia alaavvmipv
      181 sllvrrapal dgahaapaas aapepagdpa amsvthalrs pqfivllltn ffccathsgp
      241 ifhtvsyavt cgiplivavs iysveglagm ggrivfgilg drigakrtlv aglfaqalga
      301 lgydfvrtld gfyavatlfg fiyagvmply avlarenfpl rmmgtviggc amagslgmaa
      361 gpvagglivd tfgsygwlyv gsfaigigaf lmammfrpfv karpdtvaa
//
LOCUS       WP_175927221             927 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia cepacia].
ACCESSION   WP_175927221
VERSION     WP_175927221.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 927)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 927)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..927
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..927
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=99321
     Region          14..833
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mniresfrnf isgidanrrp vvlnwgkaqh alasqvalqh asihesmmtg iigyltcisq
       61 qgdlppklfi gapvsvgivt drgqlraina ivsavqvgrt dgeltvyqft vtdavnllqk
      121 rtnsrifrnv svvdvlgvvl newrqrsval aqafefdlsq ldrsrypsrs fvrqvnesda
      181 rfisriarrd gitmfvragr vsgetkdgdp pvhtlvfcdd pqklnesaag tvrvhprdag
      241 teqrdtital tmrqqlisge sgrpswdyry arvdqssast kidqgesgnd laklltdivi
      301 dvphmadswa dhermtedri laheaqavry dgvsgirdla vgswitiagd dewgtlpsdk
      361 qqfvitsvhh evwnnlpkgl neraqalfaa shtfqrprtm tdgdrsgqdt ryentfscvp
      421 rgtpltplyd pktdlpptpl itgrvvgvdg eevscdengc vfvqilgqds rdhahaqgag
      481 tnsnesdsap irvasslagp nfgetflprv gtevllgslg gdpdrlviig vlanganmpa
      541 sfthtgslpg nrflsgiktk eikgqrynql rlddtpqqis aqlasehahs qlnlgyltqp
      601 rdngqgadrg qgaelrtdaa aalraaqgml lttyartqas ggqldrdelv ellgecaelf
      661 kalgdyagqh ggtatdatgq qavvtafkgw tpgghasgdd rasnadagds qalmafgaka
      721 galnitpkty vtyagenidq iarqnlqfag gqrvittagq gihlfgrgeg vraiagegpv
      781 vlqaqqdtla ataqkgiqim svgdevlisg ksirlvaedg syvkigggve vgsdgaftah
      841 taghdfvgpn tdhvappafn rggadqkfrl rypgtdgddg thpvpnrpyk itlrngqvin
      901 gvsdahglte lassdamhia hiqvfdv
//
LOCUS       WP_175927334             573 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent helicase [Burkholderia cepacia].
ACCESSION   WP_175927334
VERSION     WP_175927334.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..573
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63218
     Region          1..564
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mldelnpqqr evallrrhcl aiacpgagkt kmsatkaafl lkdptavvga vtfskdaave
       61 lrerilalap pdakrrliag tfhslaykql rrpgrgrpdi asegdrlgml grvlaelgfd
      121 wkveeavpii eriktnfgra degsaeatly aayqdalern gkidfqdmlr lavermqsgd
      181 ilpyrftdll vdefqdtdpl qfrwvelhar agthvtvvgd ddqsiygfra algfrgmesf
      241 astfeaqrvv lgsnyrcrae ilaaadrviq nnvdrmpkvl hadrgaggvv aarrfddeyg
      301 davaavetlq prlaagasca ilartnrild pieavcrshg vpyhrasggs vlnkpqaalm
      361 cnllqvvegh kqngidavlg ymgmssydlg alhkrmgaaf vqmqkqelvg lglredtaaa
      421 yrafmkrlge wqalcqrsfh slalegvyew mmtyakgdva iraiqciydi vsrlngsfte
      481 rieflkrdnn kpgdgvlvlt tmhsskgley dhvwisrsee gvvpdekspe seerrlfyva
      541 mtrardslti ssikknavsr fviesgiesk saa
//
LOCUS       WP_175927401             999 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia cepacia].
ACCESSION   WP_175927401
VERSION     WP_175927401.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..999
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=106820
     Region          87..740
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msfapnggip agsggnllgs lsalgglagp vastvagqig plagvashid tvqravqlaq
       61 tgfslmnktp aaiadalnna aggvarltql nryvtidspl gpdvllvsta videhvnrlp
      121 eihldllshq hdlvpdqlig qpikirfdqs arqstleriv ssggadsiry fdgyvtsfdr
      181 agnpgkvtqy qmtvapwfwf ltrstdcrif qnktaqdilt eifqdhgftd fefdirtaqk
      241 pleyivmyqe syynfcarlm eqegliwthr yekekhflvi gdtnfvfrpi dglaslpyna
      301 saasedngid qlhegrrfgv gkiafrdfnh qnpssplmla qaepenlrha gletterfeh
      361 qslfdhgddg dryariamqa eeasahrytg sgyawrmsaa gsvtvtnhpv mannqeyail
      421 hvrheavndy tehnaklpyr ntfsllpkkf pyrsprstpk pvihgtqsai vvgpkgeeih
      481 tngsavkvhf lwdrrgkldg sdsmwirvsq pwagdgwgaa aiprinqevl vafnqgdpdn
      541 pvivgrvyng eqgnpyhgaa gqtmgiksqt hkgagsnelr fsdvngaqev flhaqkdmnt
      601 vvkdsethtv eaggrtvsll kgsetkqiaq gglketialt rdttanvint kaiaskagpg
      661 mqshqasdgi ehrvgdgvvt mtpdsikltf gpstivinan giyldgpvih lnrgsaqsae
      721 qalalewaae qatiakglas pdpatraaaa klasslkaqq lakladhvyh pndppptgwk
      781 matndpealk afglkpsdfe ksgsnfgsqm yvpdpnvfgd smkptvafkg tqqlfgedms
      841 nnmaqglgad apyyrnavti gkniettgas agvdftghsl ggglasaaae asggsavtfn
      901 aaglnpetva qyggtaqpan itayrvdgdi ltglqegrlg pisdgtaalm pkavgspvtl
      961 dgesvttvgr hlmgdvtngi nqqvakdqld lvsqlnssh
//
LOCUS       WP_175927448             853 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175927448
VERSION     WP_175927448.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 853)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 853)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 853)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 853)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 853)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 853)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 853)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..853
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..853
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89898
     Region          13..853
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mrahagrfgl rdlirqaarm tardwragel tllvlalvla vaaltsvgfl adrlrqgler
       61 darqmlgadf vvradrpvdp sfdrqaralg lrtattaifp smiasatggq asdtapsrla
      121 avkavspgyp lrgaveilpa gasasqkaag ipapgtvwad palldalhlk agdtvrvglr
      181 tfkvaasisr eldrgfsfvn fsprlmmrad elaatgltgy gsrvtyrllv agdqqavarf
      241 eayaharvdg gklrgagles lqegqpqvrq tldrarhflt lvalltalla avaiamaaqr
      301 ymrrhldgca tmrclgvsrr tlgalfalef agigvvsgaa gavlgygghw allaalggli
      361 dvvlppptpw paligvgaal vlllgfalpp lvpltrvppv rvlrrewgda srtawaayai
      421 gvvlfaglli vaagnlklgl ivaggfggal vgfaliarlv lfaaaravrn arvaagvgwr
      481 yalaslhrrg tasalqital alglmcllli aitrndlvag wrqstppdap nqflidiqpd
      541 qradvaaylt ahgvrdavpa pmvrgrlvai ngkpvnpday psdearrlvd refnlsytte
      601 lpsdnriveg dwfgnaatpq isieaglakt lnvkpgdvlr fdvtgltvda pitsvrkldw
      661 gsfrvnffvl mpppvlkdfp avyltsfhlp asdaalldpl iarypnltai dvapilaqlq
      721 rmmlqvvgav qflfaftlaa gvlvlytala gtrdervrea allralgasr aqvnavqrae
      781 fivvgalaga lasagaiavg wvlasrvfdf qlavdpwlvp agiaagvaca gaagwlslhn
      841 vlrrpalqsl rda
//
LOCUS       WP_175927480             228 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia cepacia].
ACCESSION   WP_175927480
VERSION     WP_175927480.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..228
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25490
     Region          5..199
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mslllvshal cpyvqraaiv laekdvpyer hdvdlahkpe wflaisplgk tpvlmvndvp
       61 ifesavicey leetlphplh pqdplhraqh rswiefgsav lnaiggfyaa pdaealerkr
      121 qdlrarftql eeelgdgpyf agpqfclvda vfgpvfryfd vfdtiadfgi faqrpkvqaw
      181 rhalakrpsv iaavsadypm alekflvarg selsrlirah rsesllss
//
LOCUS       WP_175927548             129 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Burkholderia
            cepacia].
ACCESSION   WP_175927548
VERSION     WP_175927548.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         <1..>129
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
     Region          <28..109
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 gytnpylspf eefqrykthp sirafleggk rvsygarait aggllslpkt vfpggaligd
       61 dagflnasri kgshaaiktg mlaadaafda vqagrqsdel naypdafkqs wlytelyrar
      121 nfkqwmakg
//
LOCUS       WP_175927551             124 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease, partial [Burkholderia cepacia].
ACCESSION   WP_175927551
VERSION     WP_175927551.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 124)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 124)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 124)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         <1..>124
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          <1..124
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 awigilkddg llnhtlialg iihtplrlyh sdagvyigmv ysylpfmvmp lyahlvkmdl
       61 tlleaaydlg akpwvaftri tlplskngii agsllvfipa vgeyvipell ggadtlmigr
      121 vmwd
//
LOCUS       WP_175927573             425 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GspE/PulE family protein [unclassified Burkholderia].
ACCESSION   WP_175927573
VERSION     WP_175927573.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..425
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=44906
     Region          <36..415
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mhfpssgasl htqsspahad arpaaappal daaqlddapa vrlltdtlha arvrdasdih
       61 vepfeagwri rlridgvlhe harpplhlrd alvtrikvls rmdiaerrlp qdgrlriaid
      121 ggtrgdyrvs slptlfgekl vlrrletlpp dltlanlgfd arqaaameaa iraphglvlv
      181 tgptgsgktl slycalqmld rdahnvctve dpaeiqldgi nqvgvadktg ltfatalral
      241 lrqdpdvimv geirdaetad vaikaaqtgh lvlstlhtnd apaavarlld igvapynlaa
      301 alhlvtaqrl vrrlcvacrv hsdasahalr eagcdpaala agwrpfvarg cpachgigyr
      361 griglhqtmp vspglaeriv arasvgelar cvaaegvrtl rdaafarvmd gttsiaeava
      421 atpaa
//
LOCUS       WP_175927634             282 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175927634
VERSION     WP_175927634.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..282
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29741
     Region          1..276
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mlprieairp elrpserkla dyilaaprev ldlamtelst ragvsqptia rfchalgcsg
       61 frefkirlaq svapgvssvy rdvepnepap giigkvfdrt igalievrns lsagsvadai
      121 allsnasrie fygaggsgia aqdiqhkffr lgvpsvaysd phtfsmssal lgphdvvvai
      181 sntgrtrdiv daarsalacg akvvaitqsh splaklatvs lasnvaeetd vfspmtsrms
      241 hlaigdilav gvalsrgpal mervgrakea itrrriddgt kd
//
LOCUS       WP_175927654             221 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: histidine phosphatase family protein [unclassified
            Burkholderia].
ACCESSION   WP_175927654
VERSION     WP_175927654.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..221
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24191
     Region          6..204
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mattqilfir hgetawnrik riqghidipl adtglaqaqr laarlgrear dgaridavys
       61 sdlmraqqta qpfadalglp lllreglrer sygafqghds teiealfpda yaawqtrdpg
      121 fapeggesqr efyhrvlhal epivaahpgg riacvahggv ldcvyrfang ielsaprtyq
      181 llntsinvvd yadgraqvvk wadvshldaa sddddgyrkv l
//
LOCUS       WP_175927712             119 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DUF427 domain-containing protein [unclassified
            Burkholderia].
ACCESSION   WP_175927712
VERSION     WP_175927712.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Lupas,A.N., Zhu,H. and Korycinski,M.
  TITLE     The thalidomide-binding domain of cereblon defines the CULT domain
            family and is a new member of the beta-tent fold
  JOURNAL   PLoS Comput Biol 11 (1), e1004023 (2015)
   PUBMED   25569776
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..119
                     /product="DUF427 domain-containing protein"
                     /calculated_mol_wt=13159
     Region          4..113
                     /region_name="COG2343"
                     /note="Uncharacterized conserved protein, DUF427 family
                     [Function unknown]"
                     /db_xref="CDD:441912"
ORIGIN      
        1 msdpadprle ivpnrhrvrv ihrgityads hgaltvreag lpdihylprr dvnmrrlvks
       61 gvttacpfrg qavhfdlqte dgvienaaws yeepkeaaav lahyvafdva rvdslvets
//
LOCUS       WP_175927799             117 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FmdB family zinc ribbon protein [unclassified
            Burkholderia].
ACCESSION   WP_175927799
VERSION     WP_175927799.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..117
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11113
     Region          1..73
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 mpiyayrcea cgfakdvlqk msdaplsqcp ecgkdafrkq vtaagfqlkg sgwyvtdfrg
       61 gsggtsapat asgdaapaap aaeaapaaaa paaasgsgst tttsaapapa atpaags
//
LOCUS       WP_175927805             147 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: HIT family protein [unclassified Burkholderia].
ACCESSION   WP_175927805
VERSION     WP_175927805.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..147
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16744
     Region          1..126
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mecvfcredg gevlwqddml rvvlatgehd ypgfcrviwg ahvaefsdlg eperahlmrv
       61 vyaveravrr vmqpnkvnla slgnmvphvh whviprfsnd ahfpqpvwap rqrsvseall
      121 rsraaqasll hnavreeiqr mtdsrqp
//
LOCUS       WP_175927812             312 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175927812
VERSION     WP_175927812.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..312
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32849
     Region          26..303
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mntpasppsp saaephpaqa appvldivar iaecapelre aerkvaafil adlaraahas
       61 igalardaev svatvtrfak avgcrdvrel kvlvaqaaav gqrflvpsdd apaddtspas
      121 mvydeirval ahnhqllrnt sfdaaadlla gakmtyvygq gggstalade lrfrlvrfgr
      181 pvasyqdsll qrmvaatlsg dtvvvalsvs grvpellenc rlakrygakl iaitapaspl
      241 atladhlipv vafetdfiyk pstsryammm aidvlvtgva lrlgdagres lrrikhalda
      301 hrgggdrqpv gd
//
LOCUS       WP_175927817             320 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [unclassified Burkholderia].
ACCESSION   WP_175927817
VERSION     WP_175927817.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..320
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34808
     Region          81..282
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mswqskfacw llrwqfrpet trevldpara rrftdlrmiv prrppsgyrl rqcygagdap
       61 lrgewlertd agagrapgrt llyfhgggyy fcstrthrpl vfgltkragv rafsldyrla
      121 pesrfpaald dalaayrqll algtppesiv fggdsagggl alatlvalrd rgeplpagai
      181 lfspwtdlag tggtmrsndg ldpmfaaaal pkaaklylgd tpathpyasp fyadftglpp
      241 lhiqvggtev llddsrrvad kakaagvqve levwpdmphv wqlyapmvpe ardaldraaa
      301 flrrvavera vqrageasia
//
LOCUS       WP_175927759             238 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MIP/aquaporin family protein [unclassified
            Burkholderia].
ACCESSION   WP_175927759
VERSION     WP_175927759.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..238
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24573
     Region          1..218
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mspyiaefig tailvllgng avanvllakt kgkgadlivi vmgwamavfv avyvtasfsg
       61 ahlnpivtis lalagkfaws kvggyvlaqm lggmagallv wlayrqhfak eadadlklav
      121 fctapairsv thnvlteaic tfvlilgvly laspqvglga ldalpvgllv lgigislggp
      181 tgyamspard lsprimhall pipgkrdsdw ryawvpvigp llggaaaagl ylrlhama
//
LOCUS       WP_175927862             244 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175927862
VERSION     WP_175927862.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..244
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26502
     Region          16..244
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 metgwselap dplddtplyl qlarnlasai hagawragea lpserllsgs vgvsritarr
       61 alallveqgl ikrargagsf itprvadpls rlvgftakmr qrgfvpdsvw lsrtlraatr
      121 deltrlglap gatvarlerl rradgivmav ehstlpaavv pdpqalgasl yeyletrgmt
      181 vvralqhfra anathaiakw mavkpgsall vitrigygad qraievtety crddyydfva
      241 elkr
//
LOCUS       WP_175927852             127 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: nuclear transport factor 2 family protein
            [unclassified Burkholderia].
ACCESSION   WP_175927852
VERSION     WP_175927852.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629346
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..127
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=14096
     Region          8..113
                     /region_name="DUF4440"
                     /note="Domain of unknown function (DUF4440); pfam14534"
                     /db_xref="CDD:434023"
ORIGIN      
        1 makvvdaira lerdrframv dgdgealdal lsdkvffvht ngkretkqqf idaivagrrr
       61 yrqieiqsqd vlpvgdatcv vtgralieme tnngglvfpi aytsvhthdq grwclfawqa
      121 trcatea
//
LOCUS       WP_175927870             271 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MetQ/NlpA family ABC transporter substrate-binding
            protein [unclassified Burkholderia].
ACCESSION   WP_175927870
VERSION     WP_175927870.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 271)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..271
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29058
     Region          1..271
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkrrsllkvf svlatgaalt lsagaraedk aikvgtvagp daevwqvvqk vakekeglnv
       61 kviefndyvq pnaaldagdl dansfqhqpy ldsqvkqrgy kivsagltyi spigvyskkf
      121 kslkdlpqga klavpndpsn enrallllqt qgviklkaga gtggnnatvl diaenpkklk
      181 iseldaaqlp rvlsdvdaav intnyalaan lqptkdaial esltspyanl iavrakdkdq
      241 pwvkklvkay qspevkefik kqfkgsmvas f
//
LOCUS       WP_175927887             512 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: S41 family peptidase [unclassified Burkholderia].
ACCESSION   WP_175927887
VERSION     WP_175927887.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..512
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55995
     Region          43..393
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mrmnlknigl iaaglatgvf atlqvsasae qtataplpld qlrlfaevfg qikreyvepv
       61 ddkklltaai kgmvssldph ssfldktdyd elqeqtkgrf aglgieisqe dglvkvispi
      121 edtpafragi rpgdlitrin dkpvrgmtld kavkqmrgep gtkvtltifr ksddrtfpvt
      181 vtraiikvqs vkmkmldpgy ayvritsfqe rttpdlaqkl qdiarqqpnl kglildlrnn
      241 gggllqsavg vagaflppds vvvstngqip dskqvyrdty dnyrlpsfdg dplknlppif
      301 ktvpmivltn aysasaseiv agalqdskra qimgkttfgk gsvqtvrpmt adtalrltta
      361 yyytpsgrsi qnkgitpdvp vdqyadgdpd dvlvtrevdy tnhlantqdp nekkeqeere
      421 qrrmdqlrvl eeqndkktpe qrqkdrdrkp iefgsaddfm mqqalnkleg kpvqesksll
      481 aesttkspaa kaakgasaak pasapkpasa pq
//
LOCUS       WP_175927950              96 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: flagellar hook-basal body complex protein FliE
            [unclassified Burkholderia].
ACCESSION   WP_175927950
VERSION     WP_175927950.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004146
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..96
                     /product="flagellar hook-basal body complex protein FliE"
                     /calculated_mol_wt=10468
     Region          1..96
                     /region_name="FliE"
                     /note="Flagellar hook-basal body complex protein FliE
                     [Cell motility]; COG1677"
                     /db_xref="CDD:441283"
ORIGIN      
        1 mtpidaiawp mdarspavss platdsfvtq lmsgmqhvdr alraaeaast afalgdeqpp
       61 hqvvlaleda rfklqfalnv rtrlvegyqe lmrmql
//
LOCUS       WP_175928009             741 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: xanthine dehydrogenase family protein
            molybdopterin-binding subunit [unclassified Burkholderia].
ACCESSION   WP_175928009
VERSION     WP_175928009.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..741
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=78200
     Region          6..741
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mntstgqpld rvdgvlkvtg gahyaaefpd arlahavlvt stiasgries idaararamp
       61 gvlivithen amrlpnggrp plsppagrrl tllqddtvry snepvaivva etleqatdaa
      121 havqvryras dpvvdfaqak rgarvppkqq gramdtqrgd veaglregav ridatyttpm
      181 qhhnpiepha tmarwdgptl tlhdatqgvs gtsaavaavf giapehvrvm spflgggfgc
      241 kgsswshvsl camaakqvgr pvrlaltrpq mfgpvggrpf teqrvvlaar qdgtltamrh
      301 dtiattstfe dwmemcgmps rimyavpnha tthrivslnv gtptfmrapg easgsfales
      361 amdelawrlg mdpvalrlan yaevdpqdgk pwssnklrec yeagarrfgw srrtgaprtm
      421 regdtliglg maaatypanr seasararil pdgtaevasg tqdigtgtyt vmtqvaadal
      481 gfaprnvrfa lgdsslprap vsggsqsaas vapavreaal qarakliala iadsgsplhg
      541 taaddvtvdd gwvvhrgdps rrdpaaavia raggqpidaq atakpgdeka ryashsfgav
      601 faevhvdael gtirvprivg vysvgrllna ktarsqligg mvwglgtale egshldvrhg
      661 rftnanlaey hvpvnadige ldvsfvdesd thfnplgirg igeigitgvp aaianavyha
      721 tgvrvrdlpi tldkvampvr a
//
LOCUS       WP_175928028             396 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase [unclassified
            Burkholderia].
ACCESSION   WP_175928028
VERSION     WP_175928028.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..396
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=42187
     Region          18..381
                     /region_name="MidA"
                     /note="SAM-dependent methyltransferase, MidA family
                     [General function prediction only]; COG1565"
                     /db_xref="CDD:441173"
ORIGIN      
        1 mnpkahepas lpapgpdala qsetlaaqlr deiaaaggwl pfdrfmeral yapglgyysg
       61 garkfgrrad dgsdfvtape lsplfaqtla qpvadalaas gtrrvmefga gtgklaagll
      121 aaldapgvel deylivdlsg elrerqrgti eaavpalaak vrwldalper fegvvvgnev
      181 ldampvrlfa ktdgawrerg valdarqafv fddrpvgaag lptglagldv gdgyvtethe
      241 aalaftrtvc tmlargavll vdygfpahey yhpqrdrgtl mchyrhhahd dpfvypglqd
      301 itshveftgi yeaaiatgvd llgytsqarf llnagitdal aaidpsdihq flpaanavqk
      361 liseaemgel fkviafsrgi dgtldafarg drshal
//
LOCUS       WP_175928038              66 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: heavy-metal-associated domain-containing protein
            [unclassified Burkholderia].
ACCESSION   WP_175928038
VERSION     WP_175928038.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 66)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 66)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..66
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6697
     Region          1..62
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mefevqdmtc ggcanaitra vtaadpaakl didvaakivk vdsaqgverv qaiieaagfh
       61 palrta
//
LOCUS       WP_175928055             248 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: YoaK family protein [unclassified Burkholderia].
ACCESSION   WP_175928055
VERSION     WP_175928055.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..248
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=25348
     Region          7..222
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mdldgasrnl tvaalltlsg gyldaytyvg hghvfantmt gnvallginl sagewaaalh
       61 hvpplggfvl avfvahllgl aaqrgwmrht afvsliveia flgvaasglv gassawlipg
      121 isfvatlqtl sfthleelsy tsvmttgnlr raaqklfvgl iprydagalh dsallatisf
      181 cflagavvgg lvtrlvpdia lwgavlllag afaeivrraw rragdggagn adghgdagng
      241 sdgatqsa
//
LOCUS       WP_175928084             332 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Burkholderia].
ACCESSION   WP_175928084
VERSION     WP_175928084.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..332
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35709
     Region          5..319
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtqnlltirn lavnfnglpa vdrinlsvap gevvgvvges gsgksvtmma lmglidapgk
       61 vtadevtfdg vdllkaspka rrrivgkdia mvfqdaltsl npsytvgyqi kevlklhegl
      121 rgdalhrral elldqvgipd aknriasfph qmsggmnqrv miamavacnp klliadeptt
      181 aldvtiqaqi mdllvklqke rgmalvlish dlavvsevah rvavmyagei ietnrvpdif
      241 raphhpytea llaaipehnk garrlaalpg mvpgrddrps gclfaprcky vvddcrkarp
      301 aldtlvpand amrarcikpl nlsnldltgg ar
//
LOCUS       WP_175928107             546 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GMC family oxidoreductase [unclassified
            Burkholderia].
ACCESSION   WP_175928107
VERSION     WP_175928107.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..546
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58378
     Region          1..533
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mqydyiivgg gsggsslagr ladacpdati alieagshta rnllvnmpvg iaalvpfklg
       61 tnygyetvpq pglggrrgyq prgrgmggss ainamiytrg hpgdydewaq lgatgwgwqd
      121 vlpyfrraeg nerganawhg adgpltvsdl rfrnpfserf iqaahaagyp lnddfngatq
      181 egvgfyqvth rdgsrcsvar ayiygrdrpn lhvipdatvl rvafdgkrav gvavsrngrv
      241 etldaraevi lsagafnspq llmcsgigpa eqlrrhgiav vhdapdvgtn lidhidfiin
      301 trvnsselvg vclrgiakmt palaryfssr tgmmtsnvae aggfiksdps lerpdlqlhf
      361 ctalvddhnr kmhwgfgysl hvcalrpfsr gtvalasgda rdaplidprf fsdsrdldll
      421 vrgaqamrri lsqaplasqg grelytrpdq seaelrativ ahadtiyhpv gtcrmgsdar
      481 avvdpqlrvr gveglrvvda svmptlvggn tnapsvmige raadfivaar rggvprgeaa
      541 aavhgr
//
LOCUS       WP_175928130             350 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: M48 family metallopeptidase [unclassified
            Burkholderia].
ACCESSION   WP_175928130
VERSION     WP_175928130.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Lew,R.A.
  TITLE     The zinc metallopeptidase family: new faces, new functions
  JOURNAL   Protein Pept Lett 11 (5), 407-414 (2004)
   PUBMED   15544561
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..350
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37011
     Region          135..318
                     /region_name="M48C_Oma1_like"
                     /note="Peptidase M48C, integral membrane endopeptidase;
                     cd07331"
                     /db_xref="CDD:320690"
     Site            order(201..202,205,258,262,302)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320690"
     Site            order(201,205,258,302)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320690"
ORIGIN      
        1 mrgnrrqrla haaaalsvga aalaatgaha tdtgaaaags apaaaqptpp apatsaapvp
       61 psaaegaqpt gaavpakayt ptpqqvrygn aiafrtlips plleqltase yaqivqaaad
      121 snrllsanqp rvkrlraiva klapysvkwn drvkswawdv nvirsrdirl sclpggkvlv
      181 yggmlervrl nddefgvlla hgiahalreh arsnfsatsq tslraaalpp lfgvgeplpq
      241 alnlgerlqs lhydptdete adviggdiaa ragfdpraai tlwdklaaat rankasgfiy
      301 thpysnarrq dllnrlpdlm plyakatgkr veslpdyagi saqrrkivrr
//
LOCUS       WP_175928147             213 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [unclassified Burkholderia].
ACCESSION   WP_175928147
VERSION     WP_175928147.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..213
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22355
     Region          4..213
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mfgithfgff vfavfllnit pgpdtayivg rsvaqgrvag lmsafgisag ccvhalacaf
       61 gltallaasa taftviklvg aayliylgvr mivakqvaap sgaeaaraaa aqplrrlfmq
      121 gfwtnvlnpk vvlffvsffp qfvsadsphk awaflalgav fvamstvwts lvawvagsvt
      181 rrfsgkpgvk kwldrtvgsa fvglglrlaa sqr
//
LOCUS       WP_175928152             349 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175928152
VERSION     WP_175928152.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..349
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38419
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdhlqsmrvf vkvadlgsfa raasamdisn avatrhvadl egrlgtrlln rttrslslte
       61 sgqvylerar qildeledve qmvvarnhep vgtlrivapv vfglhnlapv lqsytenfpk
      121 vvpdltlvdr qvdlveegfd vgivvtrqmr sasivtrrlt tgcmtvcatp sylekhgvpt
      181 hpeqlaehpa lslpteywgd ervftgpdge vrvrptnviv anntamlrqf allgmgvail
      241 psyligsdia rgalvrllpd frlpqveini aypsrrhlpa kvrtfidhlv ehfshstdvm
      301 mgeqwaaqga tlppigvemr aeqpestdpn lqprvarspr trvaapspl
//
LOCUS       WP_175928180             141 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [unclassified Burkholderia].
ACCESSION   WP_175928180
VERSION     WP_175928180.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 141)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..141
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15695
     Region          20..136
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04667"
                     /db_xref="CDD:467552"
ORIGIN      
        1 mpqtlapdqa setsavpike ratvvcyrde rvllvtraas rwalpggtik rgetpleaah
       61 relreetgmt gqplvysmqf tglakihhvf ftevgpdqtp qanneiekck wfpidgvdal
      121 rasiptkriv elvynheirk t
//
LOCUS       WP_175928181             462 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: nucleobase:cation symporter-2 family protein
            [unclassified Burkholderia].
ACCESSION   WP_175928181
VERSION     WP_175928181.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..462
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47494
     Region          40..459
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mqpastaqsa shgadaaeaa rdlvygpndr paptvafvaa lqhllaiivp ivtpgllicq
       61 algvssrdtt livsmslvis giatfvqcrr fgplgaglli vqgtsfnfvg pliaggslmv
      121 kqgtpvetvm aaifgvviag sfvemgvsri lpfvkrlitp lvtgivvlli gltlikvgli
      181 smgggfgama kgtfasaenl tlsglvlgti illnrvpvvw vrstalvial aigylaaafl
      241 grldftgmhq aalfqvptpl hfgigfswal fvpmliiylv tsleaigdvt atskisnepv
      301 egpvwmqrik ggvlvngans llagvfntfp ssvfaqnngv iqitgvasrh vgiwiagmlv
      361 vlglfpvvag vlqavpepvl ggaamvmfga vaasginila gvhldrrall iiavslalgl
      421 gvsqvpdiln slphalknvl esgvatggic alvmnwflpe rk
//
LOCUS       WP_175928191             135 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DUF427 domain-containing protein [unclassified
            Burkholderia].
ACCESSION   WP_175928191
VERSION     WP_175928191.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Lupas,A.N., Zhu,H. and Korycinski,M.
  TITLE     The thalidomide-binding domain of cereblon defines the CULT domain
            family and is a new member of the beta-tent fold
  JOURNAL   PLoS Comput Biol 11 (1), e1004023 (2015)
   PUBMED   25569776
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..135
                     /product="DUF427 domain-containing protein"
                     /calculated_mol_wt=14902
     Region          9..129
                     /region_name="COG2343"
                     /note="Uncharacterized conserved protein, DUF427 family
                     [Function unknown]"
                     /db_xref="CDD:441912"
ORIGIN      
        1 msmnpdtpsr pvkspgpdhp iliephssrv tvkvadkvva dtrhalvlre asypavlyip
       61 redadmslle rtdhatycpy kgdcayysip aggersinav wtyehpnpav esirghlafy
      121 pdrvdsiees llvte
//
LOCUS       WP_175928201             403 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175928201
VERSION     WP_175928201.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..403
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=44175
     Region          27..84
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          116..318
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(131..132,134..135,138,142,144..150,244..249,
                     255..256,258..259)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176152"
ORIGIN      
        1 mrdpldpaap lrdtsdaaga ldvldarlmr illvlltert vsraavrlnm sqpatsaalk
       61 rlrtllgdpl lvrsrygmvp tefgarliep lrnalrvidf iriqqprfda rtsvrtyrig
      121 cpdylnvlfv pklvalfrer apnaqlvfhp lgdgfddera ladgeldvvi dnrparqsrf
      181 rqddlfddrv vclmrtthpl arrgamtaat fvaapqlcpt pswleasgai drqlervglh
      241 rriavtlphf elaahalvrt dliltttyrl arhyakllpl aavalpaepp divyrmtwne
      301 sgscaeggrw lrgliaeatr awldaearlp avaavaavaa vttatavaas gaeadaakts
      361 psaadppept rrtrrrrath chashrarva qaarihriat ksp
//
LOCUS       WP_175928222             229 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [unclassified Burkholderia].
ACCESSION   WP_175928222
VERSION     WP_175928222.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..229
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24105
     Region          23..225
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mtdvlplttd sgsglqyrlr patgrpaarl lllhgvggne tnllnvadai dprieiaflr
       61 gpltfgpnqh awfpvrfgpn gpeidaarad ksrvqlitll halrkqdgaa salptviagf
      121 sqggimsasv gltspgdisa favlcgrilp eidpliaprd alstlhalvm hgrfddklpv
      181 awadtadakl talgvahdtr lyaaghelta emagdfgrwv geraglnri
//
LOCUS       WP_175928280             291 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SH3 domain-containing protein [unclassified
            Burkholderia].
ACCESSION   WP_175928280
VERSION     WP_175928280.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..291
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29252
     Region          7..96
                     /region_name="YraI"
                     /note="Uncharacterized conserved protein YraI [Function
                     unknown]; COG4991"
                     /db_xref="CDD:444015"
ORIGIN      
        1 mrntivrslc vvlaglaaap gvadaqssay tnspaelyag papdypvvaq ippgtaldvf
       61 gclsdytwcd valpgvrgwi daqlldypyq gsyvplleyg aiigvpvtgf aigaywdryy
      121 rhrpwypdrd rwahraeprl gpggmppgqg rpqpgapmqv apggpppvhd trpsatrggw
      181 nganrmpppa vatpmpggag narpaspppa apaptpmpgg agntrpaspp pavlhpspap
      241 gaeghtmppp vrqggggggg ggggyarpqg ggngggnhgg gggggpddrr h
//
LOCUS       WP_175928329             463 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54 dependent transcriptional regulator [Burkholderia sp.
            BCC0801].
ACCESSION   WP_175928329
VERSION     WP_175928329.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0801
  ORGANISM  Burkholderia sp. BCC0801
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia sp. BCC0801"
                     /db_xref="taxon:2676291"
     Protein         1..463
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51078
     Region          <36..130
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <151..454
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mnmpitrdks agvgsgngqh pliywtqsps vmlrkelsrr dwkvsvvaha selrdtsgei
       61 tcgildlsgg hadaigsias tcasmrdvvw valvdagqta spnvrallrd ycfdyvtlpa
      121 shqriadtvg haygmeclfa rdreqlesde kgivgtcsam lrlfdtvrrf artdapvfvf
      181 getgtgkelt avaihrhser rngpfvavnc gaipphllqs elfgyergaf tganarkigy
      241 veaanggtll ldeigdlphe sqasllrflq eraihrlggs dpvpvdvriv sathvdlrea
      301 meegrfradl fhrlcvmrid qpplrargkd iellahhmle rfrgdarhrv rgfstdaita
      361 lykhdwpgnv relinrvrra vvmtegrlit aqdleleycl daaspsvadi rksiereaie
      421 tallrtrgrv aasarelgvs ratlyrwmea ygierprgtg ssd
//
LOCUS       WP_175928356             363 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: porin [unclassified Burkholderia].
ACCESSION   WP_175928356
VERSION     WP_175928356.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..363
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=38488
     Region          17..363
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mksraqrslr aavltgsaav aglatgaaha qssvtmygim dagieftnha apeggnsvkl
       61 ksgnkntsrw glrgvedlgg glkavfrles gidlangasd dgpdsifarr atvglkgkwg
      121 elslgrnftv tydymlpfdp mgyaqnyswa tssmatggrk dglftrssna vrydgefsgf
      181 kfgalygfgn vpgsmktssk ydfavgyetg pfaavvtfdr qngaadsvtp adtvnyiqgi
      241 haglsydfgn lktmagyrny krtfrttaan qlsdmvwlgg syqftptfsl iaavyhqnik
      301 ggtdadptlv svraqyalsk rtvlyaagaf aiakhdqkvg vsrdfagygt tqvgvtagiq
      361 qrf
//
LOCUS       WP_175928364             288 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MOSC domain-containing protein [unclassified
            Burkholderia].
ACCESSION   WP_175928364
VERSION     WP_175928364.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..288
                     /product="MOSC domain-containing protein"
                     /EC_number="1.7.-.-"
                     /GO_function="GO:0016661 - oxidoreductase activity, acting
                     on other nitrogenous compounds as donors [Evidence IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=31074
     Region          1..281
                     /region_name="YcbX"
                     /note="N-hydroxylaminopurine reductase subunit YcbX,
                     contains MOSC domain [Nucleotide transport and metabolism,
                     Defense mechanisms]; COG3217"
                     /db_xref="CDD:442450"
ORIGIN      
        1 mpaitalfvy pikscagial traqlletgl aydrhwlitd phgqmltqrt hprlalirpt
       61 ldgdalvlna pgmpairtpl dgdatpatpk maatvwrdtv daidtgveta awlseflgvp
      121 tklarfgpdt rrgcnrkwtg eidthtqfad gypllvigqs slddlnarla akgapaipmn
      181 rfrpnivvsd ldayeedfve hldadgdtpv rlrlvklctr cpmptidqvt gapdpawphe
      241 ptdtmqtyra npnydgaltf ginaivvaga gawlevgqpv eaeigfgd
//
LOCUS       WP_175928369             344 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [unclassified Burkholderia].
ACCESSION   WP_175928369
VERSION     WP_175928369.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..344
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37201
     Region          33..328
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mtettapaph dahddqrrrl lraagaaala vpaitlgrka wsapplkklt fawnqnafcl
       61 tpivvaqerg ffeknglqve linysgstdq llesiatgka daavgmihrw lkpleagfdv
      121 kiigsshggc vrllgakaag vttlqalkgk tvgvsdlaap gkhffsilla kngvdperdi
      181 twrqypadll gvavdkgeih aiadgdpnly llekrsngay telatnlsge yarkvccvig
      241 argdlvrndr paaaalarsi vqateythdn pneaakvfak yspkispddl rklyatltyt
      301 hhptnvdlqq eiafyaddfr risvlkkstd pqrfaqqvya nvlg
//
LOCUS       WP_175928372             451 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [unclassified
            Burkholderia].
ACCESSION   WP_175928372
VERSION     WP_175928372.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..451
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47774
     Region          38..409
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msaslaassp pqqpalrllp advarpaadd agdeandarl aalldrlape laadaarndv
       61 dgrfphenfa rlhragliaq vvprehggag atlaqasriv aaiaradpat alvltmtylq
      121 hralgradnr wpapmrravf dsavahgali nalrvepalg spsrgglpdt iarragdgwr
      181 lsghklystg ipalrwlavw artdepaprv gvflvprdpe agdarirvie swnhlglras
      241 gshevvfddv plpadhavdv rapdawavsa athadadaqa dqqawmvall gslydavara
      301 srdwlvefat trapsglgap laslprvqea vgeiegwlha nrvllddhia rtdagnapsv
      361 ttsglvkrtv tehairtveq alklsgnhgl srgnplerhy rdvlcsrvht pqddaiaiaa
      421 graaldatrg athaqadats rngiervrrd a
//
LOCUS       WP_175928397            1055 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit [unclassified
            Burkholderia].
ACCESSION   WP_175928397
VERSION     WP_175928397.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..1055
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112792
     Region          1..1038
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mwivnlalrr pytfivmaim ivlatplalm rtpvdvlpai nipvisviwn ytgfsatemt
       61 nritsvheri ltttvnniqh vestslpgia vvkvflqpga nvqtaiaqtv ssaqaivrqm
      121 pqgatpplvi tysassipvi qlglssqtls eqsladialn flrpqlitvp gvqipfpygg
      181 rtrvvaidld pqalqakglt padivnavna qdlvlptgta kmgqteyrid tnasadtvad
      241 isnlpvqtin gattylreva avrdgfapqt nvvrqngqrg vlisilksgd astlkvvsdl
      301 ktllpkvipt lpegltitpl fdqsvfvnaa vqgviheali aavltammil lflgnwrstl
      361 iiaisiplsi ftslialsal getinimtlg glalavgilv ddatvtieni erhlhlgtnl
      421 hdailegage iavpalvstl cicivfvpmf fltgvarflf vplaeavvfa mlasyvlsrt
      481 lvptlamllf rpqqagtgpd hatsrfarlh hafnhaferl rawyivllsi llvrrrfyal
      541 cflgfcvlst glvfvlgrdf fpnadsgnlr lhvraptgyr ieetarladq verviratvp
      601 pdelgaivdn lglpvsginl sysnagtigt ldgellialk pghratghyv etlrtvlpqr
      661 fpgvefffqp sdiitqilnf gqpaaidvqv lgndlasnma iasslmkkir qipgavdvhv
      721 lqrndeptll admdrtrmqq lnlsaqnvaq nmlislsgss qttpsfwinp rtgvqyplqi
      781 qtpqynlssv ddllgtpisa sgrtgtplql lgnlvqvrst vnpavithyn irpaidvyvs
      841 vegrdlgava geidrivsda ratlprgtdl smrgqietmr tsylglgagv amaivlvyll
      901 ivvnfqswld pliiisampa alagiawmlf itgthlsvpa ltgaimtvgv atansilvvs
      961 farqrlaaga ppltaaleag atrirpvlmt alamiigmvp malglgegae qnaplgravi
     1021 ggllfatvst llfvplvfgg vhsrlarrra rqagh
//
LOCUS       WP_175928446             400 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid aminotransferase [Burkholderia sp. BCC0801].
ACCESSION   WP_175928446
VERSION     WP_175928446.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0801
  ORGANISM  Burkholderia sp. BCC0801
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Alexander,F.W., Sandmeier,E., Mehta,P.K. and Christen,P.
  TITLE     Evolutionary relationships among pyridoxal-5'-phosphate-dependent
            enzymes. Regio-specific alpha, beta and gamma families
  JOURNAL   Eur J Biochem 219 (3), 953-960 (1994)
   PUBMED   8112347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Burkholderia sp. BCC0801"
                     /db_xref="taxon:2676291"
     Protein         1..400
                     /product="amino acid aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43401
     Region          1..396
                     /region_name="PRK09257"
                     /note="aromatic amino acid transaminase"
                     /db_xref="CDD:181731"
     Site            order(102..104,130,183,214,243,245..246,254)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(105,140,207,252..254,290,293)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            246
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mfehidaypg dpiltlnenf qkdprdqkvn lsigiyfdae gripvmgavr eaelalqrds
       61 gpkpylpmvg laayrdavqs lvfgadhpar aagriatlqt lggsgalkvg adflkryfpd
      121 aqvwlsdpsw enhrfifera gftvntypyy deatgglkfd amlaaidalp arsivllhac
      181 chnptgvdld egqweklidv ieargllpfv dmayqgfgag ldadafavre larrgvptlv
      241 ansfsknfsl ygervgglsv vcedaaaaer vlgqlagavr snysnpqtyg akvvaavlgt
      301 palrkqweee lsamcrriar mrqsihdglr dhvsgealtr yvkqrgmfty tgltesqvda
      361 lrevhgvyil rsgrmcvagl ndsnvgivad aigkvlksgv
//
LOCUS       WP_175928457             864 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia sp. BCC0801].
ACCESSION   WP_175928457
VERSION     WP_175928457.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0801
  ORGANISM  Burkholderia sp. BCC0801
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 864)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 864)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..864
                     /organism="Burkholderia sp. BCC0801"
                     /db_xref="taxon:2676291"
     Protein         1..864
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=93294
     Region          60..712
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mqpfqpsptr vnrrnvssvr alcarwvara qpaaaaavar ikplaatawh hvrhptrrgv
       61 llsaaavpal favyvvvlip ftpgigdirk arvdqpaqvl sadgkllaef kpsnrewvpl
      121 kqisphmvda liatedhrfy ehhgldwkrt asaalhtfsg srqggstitq qlarnlypde
      181 igraptltrk vkeaitalki eavyskdqil etylntvpfl ynaygvemaa rtyfdksade
      241 ldvldsatlv gmlkgnsyyn pvlnperalq rrntvlgqmv kygklspaqf aqlqrrplri
      301 dferqkeppg paphfaqqlr kwliawadrn dyniysdgli vrttidarlq qmatqaltlq
      361 gnqlqgiana awsgrdgcgt dnevfrafmr espeykaaqa agkddaaamk mlaadrgfmh
      421 alckaktdvq agflaidprd gqirawvgsr dftrepfdhv aqarrqpgst fkpfvygaaf
      481 asgmkpedtf idqpveiplk ggeiwrpndd vppsgkpmtl rdavalsrnr itaqvmekvg
      541 pgavarlard mgvrespler vpslalgtsp vtlkemvasy atiangglyv epqmvtrien
      601 rqgevlaeya papperalda etdktlidvm rdvvtrgtgg sirtrfgirg dvagktgttq
      661 dnadgwfilm qpglvagawv gfddgrvtlr sdywgqgahs alpivgdffq raqrarivdt
      721 kakfdtepsp gwfaslrerv tdlfdtwfpp epkkapapvr tqrierpaea degaaseasa
      781 asapdaasgg iveewvpase vatsaaalss gasplqpqpa qppagasaps gsgagvgvgv
      841 apsavpappp vqapaapdap gasq
//
LOCUS       WP_175928463             168 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia sp. BCC0801].
ACCESSION   WP_175928463
VERSION     WP_175928463.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0801
  ORGANISM  Burkholderia sp. BCC0801
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Burkholderia sp. BCC0801"
                     /db_xref="taxon:2676291"
     Protein         1..168
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18311
     Region          1..141
                     /region_name="CFF1"
                     /note="Predicted sugar epimerase, cupin superfamily
                     [General function prediction only]; COG3542"
                     /db_xref="CDD:442763"
ORIGIN      
        1 mpisatdlir qfdlqphpeg gyfretyrat dsvvrpadga praastaiyy llcdgayssw
       61 hrirsdevwh fyagdplevw vldahdglti hrlgnplthp gtvfqavvpa grwfgarcas
      121 pehvalvgct vapgfefaef eladaaalaa efpdyaehva klaqrsdv
//
LOCUS       WP_175928479             766 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ATP-dependent DNA helicase [unclassified
            Burkholderia].
ACCESSION   WP_175928479
VERSION     WP_175928479.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..766
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=84027
     Region          178..765
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 msyvvavram ceftarrgdl dlrftpapta legiaghgav tskrgaryet eialtgtwgt
       61 ltvrgradgy dpvanrleei ktyrgsldam panhralhwa qakvyahlmc darglaeidv
      121 alvyfdivse retvltetld agtlatffae qcacfvgwae retahraard aalralafph
      181 gqfrsgqrel avavyraard erclmaqapt gigktlgtvf pllkacgege ldhvffltak
      241 tpgralalea attlgagtpa lplrvlelva rdkacehpdn pchgescpla kgfydrlpaa
      301 rdaaieagll drdtvrtaal ahdvcpyyla qelarwsdmm igdynyyydg samlhtlaqq
      361 nqwrvgvlvd eahnlldrar kmysasldpf afaaardaap aalrkafdrl arawgtlnra
      421 qaeryaaypd vpgpivsavq nlvaaigehl tdaprandda llrfhfeaiq fgvlaeafds
      481 asifdatlhg epmprqpald gvaaagrrrr iqstlcvrnv ipagflapry eaarttvlfs
      541 gtlspfhfyr dtlglpgdtg wldvdgpfra eqltvrvash vstrwrdrdr slepiadlia
      601 aqyaarpgny lgflssfdyl grvvalmqtr hpdvpvwaqa pgmaeserda flarfdaggr
      661 gvgfavlgga fsegvdlvge rligafiatl glpqvndine qmrramdarf gngydymyly
      721 pglqkvvqaa grvirtehde gvvhliddry rrrevrnllp rwwrig
//
LOCUS       WP_411198007              67 aa            linear   BCT 11-JAN-2025
DEFINITION  transposase, partial [Vibrio cholerae].
ACCESSION   WP_411198007
VERSION     WP_411198007.1
KEYWORDS    RefSeq.
SOURCE      Vibrio cholerae
  ORGANISM  Vibrio cholerae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009281
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Vibrio cholerae"
                     /db_xref="taxon:666"
     Protein         <1..67
                     /product="transposase"
     Region          <1..63
                     /region_name="YhhI"
                     /note="Predicted transposase YbfD/YdcC associated with H
                     repeats [Mobilome: prophages, transposons]; COG5433"
                     /db_xref="CDD:444184"
ORIGIN      
        1 ldtefgedac rkrveeraen farirqmcln mfqsettlka sikhkramca mdpeyllkvl
       61 gslnlgv
//
LOCUS       WP_175928495             113 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: OmpA family protein [unclassified Burkholderia].
ACCESSION   WP_175928495
VERSION     WP_175928495.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458387
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..113
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12589
     Region          <13..102
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
ORIGIN      
        1 mfwlftgsge pkrivvrghs dirritgpla davgdnqrls elradavvsm lrrlltyqdv
       61 eivaegagsr epkikrpaet agtryeieqc nalnrrveir vtyargvsrs nih
//
LOCUS       WP_175928532             153 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175928532
VERSION     WP_175928532.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..153
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16729
     Region          1..132
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mddldwkila llqdngrisy telarqvhls vpavtervkr leaagvvegy tarinpsaag
       61 ypvsaligit vpqpakakfl klletipevv echhvtgads yvmrfvavsm ihleqlieri
      121 nlygetrtsi vmstplparg marppskpgd trr
//
LOCUS       WP_175928556             210 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [unclassified Burkholderia].
ACCESSION   WP_175928556
VERSION     WP_175928556.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21880
     Region          4..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mpalptlfaf glvslgmvlt pgpnmiylvs rsicqgrrag lvslagvalg fvfymvcaaa
       61 gitalvmtvp yaydalrvag alylaylawq alkpggrsaf qvrqlphdsr arlftmgfvt
      121 nlanpkiavm ylsllpqfiv pghgsvlaqs lalgcvqiav svsvnaliac aagsiagfla
      181 grplwaavqr wlmgtvlagl avrialesrs
//
LOCUS       WP_175928586             288 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CPBP family intramembrane glutamic endopeptidase
            [unclassified Burkholderia].
ACCESSION   WP_175928586
VERSION     WP_175928586.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..288
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=29947
     Region          195..>258
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mslsllpcat iwlalfvaaa fawhrplhgl siglaalgya galafgqlap itlaplallv
       61 aagwgvlpgr plamriaahl vfaalaials lhlipgfhnp rvigptrftp davpftmyln
      121 fdkplvglwl lwtlpwvapd vapsralrtg vvaavataga clagalafgm vgwapkwpps
      181 gwlwlvnnll lvtlaeealf rgyvqggltr vfgarswgpw valaagavlf gaahaaggwq
      241 wivlgtvagv gyglawrrgg llaaalahag lnvvhfglft ypmlaaar
//
LOCUS       WP_175928608             834 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: type VI secretion system Vgr family protein
            [unclassified Burkholderia].
ACCESSION   WP_175928608
VERSION     WP_175928608.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..834
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=91772
     Region          15..796
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mvsdllnktl raqyvqhgri vrldtplged wlvplyvrgr aclgrdfeft idaastrlet
       61 iranalirqs vtlwirqtdg sempihgyvt afsrlggdga ntyyqfrfns flallrlgsd
      121 rrdwietpaq qtvsdvlaky pqssgnvnwq lrqalrsysq rmqwesdwny vhrtfeelgl
      181 fprfdiapdg kshkvvimdd lfsvpelkrk iilfsgavqd eefdglgewi dsqeiqsael
      241 dtgtfdykrp dlskhvtmpa fdlddvpglg eqyeytgsht wsdrdmgetq anvvaeewrs
      301 raqrfhgvga lrcawpgryg vltghpvhda qseqdremai lsvnwliqnn vpgienlmrf
      361 rkslraeveq aratgagsav rhddgsvgff hveieaqrrr vafrspfehk kpvmqlqtgi
      421 iggpdneeiy tdewlrakvr ltsdrlndgd qnvsawiraa mpdagykrgg mfplrkndev
      481 lidfingdcd rpvilsrmhg geskpewhth gltsgllsre yggegynqlm mddasgqnrv
      541 hlystsycsh lhlgyliqhs gntrgafigh gfdlkslgyg avraeqglyv stqpaatqpl
      601 svtaaseqlt raeamlatts kasqtnraqs qqdghdalkt ftdatqhpva gttkggrtag
      661 ggtgnangfa kpimllsspe giaastqgsa hisankqtnv vagedinlaa grallasvle
      721 qislfaeklg vkiyaasgpi dlqaqndsms ltasqdvkit agkkmylsad eiwigangsy
      781 ikltanmien atsgqiiekc anwekagaas gtlknplhst pvsvdggrft vfsg
//
LOCUS       WP_175928621             224 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175928621
VERSION     WP_175928621.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..224
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25608
     Region          2..221
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 masekargqs vadrishqlr ehiisgklpp gtaliemdla aeydtsrnsl revlhqlgre
       61 glvtfvrhkg vvvrtlnrqd vrdlyvarrt lelhalntae laqpallekm qtairaaere
      121 ldkenwqavg thslrfhqhi valqksalld effrtisaql rlvfaadpde krvqtpdwiq
      181 rdyqiydllt qnrrseavtt larylddser mlveaikrsh reaa
//
LOCUS       WP_175928652             183 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: fimbrial protein [unclassified Burkholderia].
ACCESSION   WP_175928652
VERSION     WP_175928652.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..183
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=18526
     Region          9..183
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mknlkrsaip fllvaagvaf ssaahasdgt infngkvvas tcsveggsdl tvplppvstt
       61 aladvgsvaa rsafslalkg catgdenpvk vgvifengtn vdqssgrlti dagdkaaegv
      121 qinvlddqqk lvpigaqtpa stqlatigtd gtaklnyfae yyasgavkag dvnsrveysl
      181 iyq
//
LOCUS       WP_175928663             246 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [unclassified Burkholderia].
ACCESSION   WP_175928663
VERSION     WP_175928663.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..246
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25283
     Region          10..239
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; pfam01925"
                     /db_xref="CDD:460386"
ORIGIN      
        1 mqmhtltiia lvfllagavk gmiglglpti amglltlamp psaaaslllv psfitnvwql
       61 wlgpsfgall rrlwpllvgl tvgtltgglp alaagstwth aalgvvlvly glwglaaarl
      121 papgrhekwl savvgyltgv vtaatgvfvv pavpylqalr lskddliqal glsftastiv
      181 lglqlrvtga lqtvdlgvsa lalvpalagm aggqyarrvm sekmfkrcff vglialgaym
      241 agagrg
//
LOCUS       WP_175928705             194 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: fimbrial protein [unclassified Burkholderia].
ACCESSION   WP_175928705
VERSION     WP_175928705.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..194
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=19221
     Region          1..194
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mkkttlvmsm fglacaaant ahasdgtinf tgsvvastck inggtndltv alpkastnql
       61 aavgatagrt pftltlsgca tdkkdgesvi papvkkvsva fepgpnvdla tgrlkltgad
      121 aangvqiail ndkydpikig aessaqgaqt vdidtaaggt gtatlqfaaq yvatsatvtg
      181 gsansfvtys lvyp
//
LOCUS       WP_175928710             282 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: fimbrial protein [unclassified Burkholderia].
ACCESSION   WP_175928710
VERSION     WP_175928710.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..282
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=28778
     Region          <153..281
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mkvsadtpin tvlwqltgvq irascvktpe aivkrveatl yrpandpqla anglalfvty
       61 rgsrgsgmaa iptgtvigsv lmptivsatv dlelvktgpt pvaptplpvl svptvliggs
      121 gsgddsdaar fltrgfdnis fqattcattt pavsvdlgty tarpgaavgt tspsrrfsig
      181 lrcdtgvagk fglamrldgn npvdasagll altststarg maiqvlkddg splplgepwe
      241 vaasvssaet iavplqaryf qtgapvvpgt angratfsid yr
//
LOCUS       WP_175928748             339 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DNA-binding protein [unclassified Burkholderia].
ACCESSION   WP_175928748
VERSION     WP_175928748.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13774834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..339
                     /product="DNA-binding protein"
                     /calculated_mol_wt=37412
     Region          26..144
                     /region_name="KfrA_N"
                     /note="Plasmid replication region DNA-binding N-term;
                     pfam11740"
                     /db_xref="CDD:432038"
     Region          <118..>337
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
ORIGIN      
        1 msdlaadepr ltaeierlka dfpktrelyr eacallffrf gitptanrly qlvrrgsmst
       61 ptavlgefwa elreksrvri ehpdlpadlq aaagelvaal wkrsstdaaa aldalraeve
      121 aqraaaqaev atlqaelart etaleqrtaa llaaqvriqe leqaraadea srhalqadie
      181 rlkadnaead ralaqaradf ttqldrlrdd agraearlra sekralqeid rerlaaarlq
      241 keldavtsra eerdaqqrkd taalqaqlgd alhrcgvlqg qldgalaaea arrdeldalr
      301 remaalvrrp plrgvktapa aqrserrart rkradeapr
//
LOCUS       WP_175928822             198 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0801].
ACCESSION   WP_175928822
VERSION     WP_175928822.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0801
  ORGANISM  Burkholderia sp. BCC0801
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia sp. BCC0801"
                     /db_xref="taxon:2676291"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21496
     Region          6..169
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maprgrprsf dreqalerlm evfwskgyeg tqlndlmaai nvgppsfyaa fgskeaafme
       61 avdlylaevg arpmqpleha ptaregirgm legsvevals tkpggcmlil gvvnclpenq
      121 pareyllnar rktvelirac lrrgvedgnl pegtdidrla afyhgvmqai sfqardgatr
      181 pelealiepa lsalplpa
//
LOCUS       WP_175928819             271 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia sp.
            BCC0801].
ACCESSION   WP_175928819
VERSION     WP_175928819.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0801
  ORGANISM  Burkholderia sp. BCC0801
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Burkholderia sp. BCC0801"
                     /db_xref="taxon:2676291"
     Protein         1..271
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=30522
     Region          10..89
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(35,60)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(42..43,54,57,61..62)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          114..258
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mrtlertrpe laeflrarre rlspedvgls takrrrtpgl rreevaalag vgltwytwle
       61 qgreigvsad fldnlarvlk ldaaerrhlf llaherppae pgktfcivps laarlvedla
      121 phaayiinlr wdvlafngpa drlfgfgrhd pghrnllwal ftdselreaf vnweqqapam
      181 lasfrrdfaa aredadarav veelervspe fkewwrsqdv hapctgtrti svegapvdfe
      241 htsltidggq hlrlvvyaek qksasglpvd l
//
LOCUS       WP_175928826             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0801].
ACCESSION   WP_175928826
VERSION     WP_175928826.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0801
  ORGANISM  Burkholderia sp. BCC0801
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia sp. BCC0801"
                     /db_xref="taxon:2676291"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32123
     Region          12..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..294
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,221..226,
                     232..233,235..236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176169"
ORIGIN      
        1 mgslhqnrsg emevfvrvve lggfspaara eymtpsavsk liarlearlg arllnrstrq
       61 lqltpegcaf yeratrilad ledaeraagv geqavgrvrl ntsasyfnhv lapvlpqfla
      121 lhpgvtldiv qtdavvdlla ertdvavrag plkssslvar klgetsltiv aapayleryg
      181 eprsiadlea hnrlgfgyar avdgwplren getivvpatg rvqasdgegl rrlavagvgl
      241 arlaaftvre diaagrllrv vgnldtgete afhavyvgqg gplpsriral ldflaehgrv
      301 s
//
LOCUS       WP_175928829             204 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0801].
ACCESSION   WP_175928829
VERSION     WP_175928829.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0801
  ORGANISM  Burkholderia sp. BCC0801
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia sp. BCC0801"
                     /db_xref="taxon:2676291"
     Protein         1..204
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22111
     Region          16..150
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msstpddgqs aakrvrlsre drlrqlldva wrlareegtd altlprmaee agvtkpliyd
       61 hfgtrngllt alyqdfdarq taeidaalea reltlegtar viatsyvecv laqgreipgv
      121 laglagspel etvkrdyqla fiekcrkvla pfsgptgirr ssfwamlgaa dalshaaatg
      181 eitseqaqae lyeiivamvs rsrs
//
LOCUS       WP_175928844             697 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia sp.
            BCC0801].
ACCESSION   WP_175928844
VERSION     WP_175928844.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0801
  ORGANISM  Burkholderia sp. BCC0801
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 697)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 697)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Burkholderia sp. BCC0801"
                     /db_xref="taxon:2676291"
     Protein         1..697
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=76077
     Region          12..>204
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mtttantapt aehgatvlip lnklkkhprn arktphseas ieakaasiaa kgilqnlvve
       61 pemdaagept gfylvsigeg rrlaqmlrvk rkeikknepi rcvidtanda aeisldenvt
      121 redlhpadqf erfrelsedr gwgaeeiaar fgvtahvvkq rmrlgavspk llqvyrdgel
      181 tldqlmafai tddharqehv yenlsynrdp siirrdltkm nvpatdrcav fvgaqayaea
      241 ggniirdlft edrggffedp allerlavek leriaaevqq aegwkwtaay ldfphahgmr
      301 rvyphsvels eedaaaydaa qdelerlsae cedagidlpp evdarfaele aeieridakr
      361 yaydpteiar ggvfvvvahn geariergfi raedeapepe ekaeggetvi dgvrvnadge
      421 ildgdgegse gedgsatepe peeeggdagk plsdslirdl tahrtlglrl algeqpdmal
      481 iavvhalaaq tyyrgstahc leiiptsnyl aahadgiedt aaakmladrh agwaadmprd
      541 vadlwgfvag leraslmall ahcaaltvna vklpwesskr rahetadkla savtldmteh
      601 wtptvraylg rvtkahilaa vrealgdeaa eriadmkkve maeaaeqlla gtgwlppvlr
      661 tarsawfdqq peapasddve arpvpephdd hfavaae
//
LOCUS       WP_175928871             197 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: 2'-5' RNA ligase family protein [unclassified
            Burkholderia].
ACCESSION   WP_175928871
VERSION     WP_175928871.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Remus,B.S., Jacewicz,A. and Shuman,S.
  TITLE     Structure and mechanism of E. coli RNA 2',3'-cyclic
            phosphodiesterase
  JOURNAL   RNA 20 (11), 1697-1705 (2014)
   PUBMED   25239919
  REMARK    Erratum:[RNA. 2014 Dec;20(12):2011]
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Arn,E.A. and Abelson,J.N.
  TITLE     The 2'-5' RNA ligase of Escherichia coli. Purification, cloning,
            and genomic disruption
  JOURNAL   J Biol Chem 271 (49), 31145-31153 (1996)
   PUBMED   8940112
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..197
                     /product="2'-5' RNA ligase family protein"
                     /EC_number="3.1.4.58"
                     /GO_function="GO:0004113 - 2',3'-cyclic-nucleotide
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0008664 - RNA 2',3'-cyclic
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=21841
     Region          18..189
                     /region_name="ThpR"
                     /note="RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA
                     ligase) [Translation, ribosomal structure and biogenesis];
                     COG1514"
                     /db_xref="CDD:441123"
ORIGIN      
        1 mtqltlpgfd vpppvpvhrf ffaampdpat avriagmadn mrlkkdrpvg terlhitlgs
       61 lgdfayvpda klararavad ridvrsfpvr fdkivsfngr pgrqplvlmg kagledvidf
      121 rrqlrdalkr vgvpvfpssf tphvtllyga qrpdeyriep itwtvfdfvl idswlgkshy
      181 dvlgrwplgt gsasgrs
//
LOCUS       WP_175928921             838 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: penicillin-binding protein 1A [unclassified
            Burkholderia].
ACCESSION   WP_175928921
VERSION     WP_175928921.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 838)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..838
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=91038
     Region          56..776
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mpiikrppss sdrnephytl rrspsgayyp ddddrddgrr thersggggr rtfgsrvalw
       61 fvglfatlav vgalivgyal vvmapqlpsl daltnyqpkv plrvftadhv ligefgeerr
      121 slvrfqdipd vmkkavlaie dyrfyehggv dfvgilragv adlmhggarq gastitmqva
      181 rnfflssekt ytrkiyemll aykiekaltk dqilelymnq iylgqrsygf aaaarvyfgk
      241 dlkditlaea amlaglpkap saynpvvnpk rakvrqeyil krmldigyit qpqydeaike
      301 eihvrtpgnq yavhgeyvae mvrqmmyeqy kdetytrglt vtttinsadq eaayqavrrg
      361 ildyerrhgy rgpeasinlp aagderdeai ddaladhpdn gdlqsavvls aspnavevqf
      421 vggatttigp aglrfvsaal gprannalri kpgsvvrvlk dgktgwqvvq lpqvegalva
      481 iapqdgairs lvggfdfnks kfnhvtqawr qpgssfkpfi ysasldkgmg patiindapl
      541 yfppsvpggt awepkdddqp dgpmsmrtgl qrsknlvsir ilasigtqya qqyvtqrfgf
      601 dpaktppylp malgaglvtp lqlatgyavf anggykvdpy liaevddarg qplqksqpvv
      661 aggtaprtie grnayvmnsl lhsvatagtg agtnalgrnd lqgktgttnd akdgwfagyq
      721 qslvavawmg fdqpkslgsr efgaqlalpi wvnymrtaln gvpeqqmpmp dglttidgel
      781 yyadrtpgng fvanvdinpa enaisandal gsagaaglap ppvtpqekqq imdmfenk
//
LOCUS       WP_175928990             236 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ankyrin repeat domain-containing protein
            [unclassified Burkholderia].
ACCESSION   WP_175928990
VERSION     WP_175928990.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..236
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=24469
     Region          7..230
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          101..130
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(102,106..107,110..112,114..115,119,122,132,136..137,
                     140..142,144..145,149,152,161,163,165,169..170,173..175,
                     177..178,182,185,194)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          131..161
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          163..194
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mtkptnhlpk ralvaaafva sglfaaagah aesldaivka vkfddiadig kqlksgkldp
       61 ntvapngdpi lviaareksd kvaaaiattp nvdlekedka genalmlasl ngdldlvkll
      121 idkgaevskk gwaplhyaat ngqdavvkvl ldhdayidta spngttplmm aargnhastv
      181 tllldqgadp qvknqlgita lefakhynap daieilskrt trigaatpad aqksak
//
LOCUS       WP_175929032             153 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175929032
VERSION     WP_175929032.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..153
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16619
     Region          14..126
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(15..17,31,48..50)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(62,65,69..70,79,97,101,107,111,114..115)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 msktvsqsta agpltigqva eltgvsthtl ryyeqagllr aisrtaaghr lyapadldwl
       61 afvmrlkatg mpiaqmqafa vlreqgestf garrdllvah rdavrahiae lqasldaigd
      121 kiayyearer etdrranpsh slseqdghdg ttr
//
LOCUS       WP_175929068             747 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ATP-dependent DNA helicase [unclassified
            Burkholderia].
ACCESSION   WP_175929068
VERSION     WP_175929068.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..747
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=81100
     Region          43..742
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mnspleatpd arrdttsagr arapegtfel srkrvdeldt ifgeggllar aldgyrprts
       61 qiemaravas ameasarrmp dpeifetrkr parrlgdgdt aagpaadaaa aaesddagdn
      121 tliveagtgt gktyaylvpa mlwggkvivs tgtkhlqdql flrdiptvrn alavpvsvam
      181 lkgranylch yylqrtadng rlpsrqdtay lqeivrfaki tksgdkaela svpenapvws
      241 mvtstrdncl gqecphykec fvmqarreaq qadvvvvnhh lffadimlrd tgmaellpna
      301 ntiifdeahq lpetatlffg etlsttqile lardtvaegl shardavewv klggdleraa
      361 rdlrlafadg qivrmslaql gddhpmfgal daldaaldal asalasqaer aeslgaclrr
      421 arelqdllag wvapgaaeaa aqadaaagen aatdgdpnek vrwvevfaht vqlhetplsv
      481 apifakqrag vprawvftsa tlsvrgdfth yaaqmglssr rsmtlaspfd yqsqgllyvp
      541 rnlpqpsspa ftdavfdaal paieasgggv fmlcttlrav driasklrdv iesrgwnmpl
      601 lvqgdasrte lldrfraygn ailvgsqsfw egvdvrgdal slvvidklpf appddpvlaa
      661 rldaltkkgl spfavhqlpq avitlkqgag rliraetdrg vlmicdtrlv dkpygrriwq
      721 slppfkrtre iavvqdffde hrsdkrt
//
LOCUS       WP_175929072             393 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acetyl-CoA C-acetyltransferase [unclassified
            Burkholderia].
ACCESSION   WP_175929072
VERSION     WP_175929072.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 393)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..393
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40285
     Region          1..393
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mtdvvivsaa rtavgkfggs lakiaapelg atviravler agvkpeqvse vimgqvltag
       61 sgqnparqsl ikaglpnavp gmtinkvcgs glkavmlaan aivagdaeiv iaggqenmsa
      121 aphvlpgsrd gfrmgdaklv dtmivdglwd vynqyhmgit aenvakeygi treeqdafaa
      181 lsqnkaeaaq kagrfddeiv pvsipqrkge plqfatdefv rhgvtaesla glkpafakdg
      241 svtaanasgl ndgaaavlvm saqkaaalgl tplarikaya nagvdpsvmg mgpvpasrra
      301 leragwtpgd ldlmeineaf aaqalavhkq mgwdtskvnv nggaiaighp igasgcrilv
      361 tllhemvkrd akrglaslci gggmgvalav erp
//
LOCUS       WP_175929087             267 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Burkholderia].
ACCESSION   WP_175929087
VERSION     WP_175929087.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..267
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28432
     Region          7..261
                     /region_name="FetB"
                     /note="ABC-type iron transport system FetAB, permease
                     component [Inorganic ion transport and metabolism];
                     COG0390"
                     /db_xref="CDD:440159"
ORIGIN      
        1 mspalqdlsl vdvgiaaalv avngaisaal slglgrklal aavrtvvqll aigyvlgwvf
       61 ghphwyvvlp ltalmtliag fagagrgkrt yrgqrvdsia siwfsswfva avglfvviri
      121 hpwfapqyai pilgmilgnt ltgvslgver mmeeltarrd rvetalalga trweaaqdaa
      181 rqavragmlp tlnqmavvgv vslpgmmtgq vlagqsplqa vryqivimfl iaaasalgtv
      241 gavlmtyrrl fsadhrflas rleerth
//
LOCUS       WP_175929112             268 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [unclassified Burkholderia].
ACCESSION   WP_175929112
VERSION     WP_175929112.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..268
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26770
     Region          1..264
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mlisfvlggf vgavlgltga gggilavpal vvgmswpmqq atpvalvava gsaalgaleg
       61 frrglvryra allmavagvp lttlgvrlah vlpqrllltl faltmlavag rllrqalrpq
      121 aadadasplc vgrvnpdtgr lvwswpvgla lastgavtgl mtgllgvggg fvivpmlrkf
      181 tnvsmhgvva tslmvialvg tggvlatlvs gtrapldvtl wfavatalgm aagrgasrrl
      241 aarhvqagfa avlvcvalgl lakaafga
//
LOCUS       WP_175929094             586 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ShlB/FhaC/HecB family hemolysin secretion/activation
            protein [unclassified Burkholderia].
ACCESSION   WP_175929094
VERSION     WP_175929094.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..586
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=63990
     Region          59..586
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mnifhrltvl piaalvsfgv haeqaptlad qaaaaranae qdrqaqqqrd aqqraaevra
       61 psvrsevphv eaypaiptet pcfridrfmv nvpdalpdgl kaqgasalpm drfafarewl
      121 ehytgqcvgk qgldvlvkal sqdilsrgyi ttrvllpeqd lssgtlkvsl ipgvirhvrf
      181 adeklrgtwk tafptrdgel lnlrdleqgl eqmkrvqsqd vsmqivpadv pgesdvvlnv
      241 krgkpwtvva sidnsgtrat gklqgnlsig idnplglndi fnvgvsqdle lgdkrlgshg
      301 wngfysipwg ywtatlsayt ntyyqqiagv nqtfvasgns ktidfklarv larsqndvfg
      361 gyvrlsrrfg qsfiedteis qqrrnntfve fgltdrhyfd gaqfdgtlay rqgvgglgaq
      421 ddilaagggp tyrfkmavld anlsvpfaia kqpfryvtsi hgqytgnsly yiddltigsr
      481 ytvrgfdget mlaaargfyw rnelqmpigq tgqaiyagld ygrvwgpqpv alvgtqlaga
      541 vigikgsvat pfggygydlf agtpvykpsg fptarvtvgf qvtaqf
//
LOCUS       WP_175929117            1048 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit [unclassified
            Burkholderia].
ACCESSION   WP_175929117
VERSION     WP_175929117.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..1048
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114451
     Region          11..1027
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msvsheegrf nlsawalrhq alvvyliala tlagilaytr laqsedppft frvmvirtfw
       61 pgasarqvqe qvtdrigrkl qetpaidflr sysrpgesli fftmkdsapv kdvpetwyqi
      121 rkkvgdigyt lppgvqgpff ndefgdvytn iwtlegdgft paqlhdyadq lrtvllrvpg
      181 vgkvdyfgdp dqrifievnn aqltrlgisp qqlgqainaq ndissagvlt taddrvfvrp
      241 sgqfdnvaal adtliringr tfrlgdlatv krgyddpqvt qmrmngkavl gigvtmqpgg
      301 dvirlgkald aeskdlqaql paglkltevs smphavshsv ddfleavaea vaivlvvslv
      361 slglrtgmvv visipvvlav talfmylfdi glhkvslgtl vlalgllvdd aiiavemmav
      421 kleqgysrar aaafaytsta fpmltgtlvt vsgflpiala ksstgeytrs ifevsaiali
      481 aswfaavvli pllgfhmlpe rkrhaheahl pddhehdiyd trfyrrlrgw idwcierrfv
      541 vllitgalfv valmgfslvp qqffpssdrp ellvdlrlpe gasfaatlre terlekaidk
      601 rpeidhavnf vgsgaprfyl pldqqlqlpn faqfvitaks vedreklagw lettlrdqfp
      661 avrwrlsrle ngppvgypvq frvsgdsiat vrsiaekvaa tmrgdartvn vqfdwdepae
      721 rsvrfeldqk karelnvtsq dvsgflamtl sgttvtqyre rdkliavdlr apradrvdpa
      781 klaglalptp ngpvplgslg rftptleygv vwerdrqpti tvqsdvraga qgidvthavd
      841 aklnalraql pvgyqinigg sveesakaqa sinaqmplma iavftllmiq lqsfsrvlmv
      901 vltaplglig vaatlllfgq pfgfvamlgv iamfgiimrn svilvdqieq diaaghgrvd
      961 aiigatvrrf rpitltaaaa vlalipllrs nffgpmatal mggitsatvl tlfylpalya
     1021 twfrvkrder dpqdgpppga tpaapsga
//
LOCUS       WP_175929127             426 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Burkholderia].
ACCESSION   WP_175929127
VERSION     WP_175929127.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..426
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45666
     Region          10..407
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(24..25,28..29,32,65,115..116,118..120,123,143,
                     146..147,150,239,242..243,246..248,251,279,283,335..336,
                     340,344,360,363..364,367..368,371)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 maanlaarrw wtimpivfit yslayldran ygfaaaagin qdlgiskgls sligalfflg
       61 yfffqipgai yaerrsvkkl vfvslvlwgg caaltgvvsn ipslmairfv lgvveaavmp
      121 amliyisnwf tknersrant flilgnpvtv lwmsivsgyl vhefgwrhmf iaegvpaiiw
      181 avcwwclvqd kpadspwlsa qekrdldaal aaeqaaikpv rnygeafrsp aviklcaqyf
      241 cwsigvygfv lwlpsivkng sdlgmvatgw lsalpylaat iamlaaswas dkvgsrrgfv
      301 wpfllvgaaa faasyalgss hfwisyallv vagaamyapy gpffaivpel lpknvaggam
      361 alinsmgalg sfvgsyfvgy lngatgspva syafmsaalv aaviltlsvk pqardahpla
      421 aplqgk
//
LOCUS       WP_175929140             233 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: energy transducer TonB [unclassified Burkholderia].
ACCESSION   WP_175929140
VERSION     WP_175929140.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..233
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24757
     Region          162..232
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mkveehlvas nsglatlgrp refgkkqqnp vrrfggiavv lllhavliya llnglatkvv
       61 qviqhpietr iiepvkpppp pplpvvklpp pkfapppppf vpppevpvqa ppqaapithq
      121 sapvpsapav qapviappap akpvshevgv vcpnsdsira smqypkeaqe nnitgdvtie
      181 fvvdaegnit nervaqsadp vldraayntv krfkcvaqgq avrvqvpfsf nln
//
LOCUS       WP_175929194             140 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [unclassified Burkholderia].
ACCESSION   WP_175929194
VERSION     WP_175929194.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 140)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..140
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15318
     Region          13..127
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04667"
                     /db_xref="CDD:467552"
ORIGIN      
        1 mstgpdtlav ikerativcr rsssvllvar taarwslpgg tirggetple aaqrelaeet
       61 rleglaldya vqfggltklh hvfvadvpah ltprasneia rckwfavdrl dtlrasvptr
      121 kiiellrldc faafvreplr
//
LOCUS       WP_175929141             299 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [unclassified Burkholderia].
ACCESSION   WP_175929141
VERSION     WP_175929141.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..299
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31170
     Region          73..279
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mtkrslaala asllmsvaai dglvapqlay aqasgstats daltqaaapa psaaepappp
       61 apatteaven pyglgalwkn gdfvarfvlm llvimsmgsw yimitkfveq lranrrakla
      121 daqlwsapsl aegaklldea spfrfiaeta ieagehhdea lleavdrntw idvsversit
      181 nvsnrlqdgl aflatvgsta pfvglfgtvw giyhaltaig iagqasidkv agpvgealim
      241 taiglavavp avlgynflvr rnksvmervr nfgaqlhtvl lagskrpara pspaaslvn
//
LOCUS       WP_175929219             282 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Burkholderia].
ACCESSION   WP_175929219
VERSION     WP_175929219.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..282
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29802
     Region          7..260
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtrrtaalaa rglsvgyrdh vvidgldlsi aagrvtalcg pngcgkstll rtlaglqpar
       61 aghvdvngkp lasfrrrala reltmlaqfn qipsgltvre lvaygryayg gflrglsrvd
      121 haaidealet sglagdaerd vgalsggerq rawiamalaq qapivlldep ttyldihhql
      181 dildalraln rtrgltivwv lhdlnqaaay sdeivlmrag rvvaqgtpda mldparlraa
      241 fgvemlklah pqtgapmcvp aygpstgaap qaagvfdrdl av
//
LOCUS       WP_175929227             170 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: fimbrial protein [unclassified Burkholderia].
ACCESSION   WP_175929227
VERSION     WP_175929227.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..170
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=17209
     Region          1..170
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mkksiltava laalstsafa agtgtinftg eivagacgid agsvdqtvrl gfvptnvfkq
       61 agdkstptnf dikltdcdts iaknafftft gssnatqpkl iatvgsatnv girlqassge
      121 yldngaeqka pvvlqngtnv arfaamyeat aagvtpgtad gvanftvryq
//
LOCUS       WP_175929248             339 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Burkholderia].
ACCESSION   WP_175929248
VERSION     WP_175929248.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..339
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34828
     Region          36..338
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtqppvsptd agaqqdvtgr rartlsgtrl glsnylglag alaamialfs vlsshfltyd
       61 tfstianqip dlvvmsvgmt fvliiagidl svgsvlalaa smvsvaalkw qwgplpaali
      121 giavatatgt ltgavtvgwr ipsfivslgv leaarglayq ltnsrtayig dafdflsnpi
      181 algispafli avavmiaaqf vltrtvfgry lvgigtneea vrlagvnprp ykilvfalmg
      241 alaglaslfq isrleaadpn agaglelqvi aavviggtsl mggrgsvist ffgvliisvl
      301 aaglaqigan eptkriitga vivvavvldt yrsrrarar
//
LOCUS       WP_175929258             165 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [unclassified Burkholderia].
ACCESSION   WP_175929258
VERSION     WP_175929258.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..165
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17899
     Region          4..141
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 masynkillc ydgtlegrka lrcganlamd lkaethllsv vdmrssiaqs aglltdvacg
       61 rfeetareil qegvnwlrer gvqaeghfaf gypideianl aselkvdlvv vghrcrsgls
      121 rwwmgsgntq lldrvncsil vacssaeeqk aeiarereaa iangt
//
LOCUS       WP_175929289             237 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [unclassified
            Burkholderia].
ACCESSION   WP_175929289
VERSION     WP_175929289.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..237
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25453
     Region          151..232
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mpdamtanag dahvldrvvw naltgrqrrf aleagrarrf ptaiapfaal ddtrpasfda
       61 lcgliaahgp aalvtpdeia ppaslsvirr atllqmtwqr tsdpadeseh valgeadvpd
      121 mlaltaaaqp gpfgprtfel ghyigvrieg rlaamagqrm qvdgyteisa vcvdaafrrq
      181 glatrlirsl iatidardet pflhvlttnr vaierylalg favrremhll vlgdaha
//
LOCUS       WP_175929299             137 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MerR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175929299
VERSION     WP_175929299.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..137
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15358
     Region          19..104
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(20..22,36,53..55)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mtttvekvvl ppipakryft igevselcgv kphvlryweq eftqlrpvkr rgnrryyqhh
       61 evllirrire llyeqgftin garnrldspg seraaaepve sgaqpadarg avkpgasvdv
      121 ialrqalldv ldglkrd
//
LOCUS       WP_175929307             557 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: electron transfer flavoprotein-ubiquinone
            oxidoreductase [unclassified Burkholderia].
ACCESSION   WP_175929307
VERSION     WP_175929307.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60484
     Region          25..384
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          453..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mtpaslieqy gpresmeydv vivgggpagl saairlkqla aekgteigvc vlekgseiga
       61 hilsgavmdp raitelfpdw keqgaplnve vtedrflfls eksavttpnw alpdnfknhg
      121 nyvislgnvt rwlgqqaeal gveifpgfpa aeilynddgs vkgvatgnmg vgkdgepten
      181 fqlgmelhak ytlfaegcrg hlgrqliskf kldanadpqa ygigikelwe idpakhkpgl
      241 vihtagwplk sdtyggsfly hmdnnqvvvg fvvglgytnp ylspfeefqr ykthpsiraf
      301 leggkrvsyg araitaggll slpktvfpgg aligddagfl nasrikgsha aiktgmlaad
      361 aafdavqagr qsdelnaypd afkqswlyte lyrarnfkqw makglylgtl mvgleqkvmg
      421 gnvpwtlhhq hadhemlkpa sqctpieypk pdgkltfdrl ssvfisntnh eenqpahltl
      481 kdasvpvnvn lrtyagpear fcpaavyefv knddggdrlv inaqncvhck tcdikdptqn
      541 ivwvtpeggg gpnypnm
//
LOCUS       WP_175929312             473 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FAD-binding oxidoreductase [unclassified
            Burkholderia].
ACCESSION   WP_175929312
VERSION     WP_175929312.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..473
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50262
     Region          2..473
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mmsseafvsa crdaigaehv ltdphdtepf ltdwrrrytg aacavlrpan taevaalvkl
       61 anahgvalvp qggntglagg atpdasgsqa vlsvarlnrv raldphnnti tveagvilad
      121 vqarareggr lfalslaaeg sctiggnlst naggtavlry gnarelclgl evvtpqgeiw
      181 dglrglrkdn tgydlrdlfi gaegtlgiit aavmklhplp aaqvtalaal esphaaldfl
      241 alaqraagpl ltgfelmsdf cmqlvgkhyp qlrypfaqah aqtvllelsd neseaharal
      301 feklmeeafe aglvvdavva enlaqsrafw dlrehiplaq adeglnikhd iavpissiar
      361 fidetdaaiq qaapgarmvt fghlgdgnlh ynvqmpeggd akaflaafqa pinrivydnv
      421 hrhhgtisae hgigqlkidd aqrykspvet slmrtlktal dprglmnpgk vlr
//
LOCUS       WP_175929317             734 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [unclassified Burkholderia].
ACCESSION   WP_175929317
VERSION     WP_175929317.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..734
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79889
     Region          33..717
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 msasspastp aggpfaawya afgdwartdg aawlylfkal laafiatgvs mrldlpapkt
       61 amttvfivmq pqsgavlaks fyrvagtifg liatltfvgl fpqqpqlfll avalwvalct
      121 agaarnrnfr sygfllagyt taliglpasq hpdgafmsam trvaeimvgi vsagvvsalv
      181 fpqttgeqmr ttvrkrfgnf vdyvaaalsg tldrahieti htrfvadvvg feaarsmavf
      241 edpdtrmrsg rlarlnsefm sassrfhalh qlmnrlhaag aqaaidaiep yfreiaplll
      301 tpagepvrts adaghaaeql lawrdalprr iratraelet qpdfplldfd taaellyrfi
      361 tdlqeyaaty aslatather erwieryepr tnrtaatiag irtatvilal gwfwietawp
      421 sgvmlvlnaa atcalassap rptamaaqmg mgtalavctg flltfgiypr idgfwllcaa
      481 lapllaigiy mtlkpklagy gmgyliffcf lagpdsithy dpmsfmndal alllsmlasa
      541 iafavlfppt apwlkkrlfa dlrhqvvaag harlaglrtr fesgardlmy qahtlsadqp
      601 dvqrdalrwm favletgnat idlrhelatl ppepryapam pwrraidtmr talsalfskp
      661 saaqfdatla atnaaidatr qtldafepsr derhrlqril sylhfvrtal ldpesplapl
      721 nrnrpvrpqp gass
//
LOCUS       WP_175929332             390 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [unclassified
            Burkholderia].
ACCESSION   WP_175929332
VERSION     WP_175929332.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..390
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42638
     Region          12..282
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 midgqillgh sirwgmvggg lgsqigyshr saalrdgsfq lvagafdidp ergrqfgvkl
       61 gvaaercypd yatmfdaear radgiravsi atpnnthfei craalnaglh vvcekplcft
      121 teeaealqrl sveknrivgv aygysghqmi eqaremiarg elgeirivqm qfahgfhseg
      181 veaasaaarw rvdpkfagps yvlgdigthp lyisevmapd lkikrlmcsr qsfvksrapl
      241 ednaftimey dtgaigyvws savnagsmhg qkvrvigska siewwdehpn qlryevqgqp
      301 aqvldrgmsy lhpaalredr igaghpeglf eawsnlyarf alamdaadrg dagalkairf
      361 pdvhagvegv rwvencvrsa daggvwvdyr
//
LOCUS       WP_175929336             341 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Burkholderia].
ACCESSION   WP_175929336
VERSION     WP_175929336.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..341
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35517
     Region          10..341
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mgnlnpvada qtmtlksrha kwppelsifl vlvgislffe ivgwvvvgqs flfnaerlei
       61 ivlqmavigi iavgvnlvii tsgidlssgs vvaaaavvsa slaqvsdfpr avfphltdlp
      121 viwpvlagvc vgllvgllng sliamtgipp fiatlgtmva argfakwftn gmpvsmltdq
      181 faaigaganp viifvviaai fhvvlrytrf gkytyaigan rhaavvsgin vtrhlvfvya
      241 iagllsgiag tvtaaraisg qsgmgvmyel daiaavvigg tslsgglgrv tgtvigvlil
      301 gvmtsgftfi ridayyqemv kgaiivaavi adqyrnkksr r
//
LOCUS       WP_175929347             409 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [unclassified Burkholderia].
ACCESSION   WP_175929347
VERSION     WP_175929347.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 409)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..409
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41362
     Region          32..313
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mrsrtlagca rwalfvacfa lpawlwphga vlgylaqtaa lvvlalsynl qlgttgllsf
       61 ghaafaglga faaahwfnhi ggplpllplv ggaagagfgf vagllatrrs gtafamitlg
      121 lgecvaaaaw svpawfggig gvpidragga pwgngyfgap ahayaliaaw cvvsawamha
      181 ltrtplarla navrdnparv aalgtdprrv rlamvtcasf fagvagtltl idveiatpds
      241 vsmarsatvl iaaviggtgt ffgpaagaav ltvlsivvag vsrawalylg vlfvavvvaa
      301 pggiagvart lahalrrgap aaerwrvlcg vgacvfwgva ivcaaelgya wrfaqddgtg
      361 fafgawgida dtpigwavac saagigallw gwrarfahga agatqeegr
//
LOCUS       WP_175929358             157 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [unclassified Burkholderia].
ACCESSION   WP_175929358
VERSION     WP_175929358.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 157)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10120901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..157
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17033
     Region          11..99
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cd02883"
                     /db_xref="CDD:467528"
ORIGIN      
        1 mtkrggaprt vscgvvilda agrvflahat dtthwdipkg qgepgetpad aalrelleet
       61 givfaparll dlgrfayrhd kdlhlfavqa aegeidpaqc tctslfpsrr dgsmipemda
      121 yrwtvpgdvd tyasrslarl frtklslael hrrlsga
//
LOCUS       WP_175929368             304 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [unclassified Burkholderia].
ACCESSION   WP_175929368
VERSION     WP_175929368.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..304
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32582
     Region          <213..303
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mksirsvlla amlagglava pvtfakppvp pavapavavg pqydtthvcv apedfdrftd
       61 sfvatfggkk skqgvfqvtp tpsqtmsqlv ltpvgtisvf gfktpipypf caertgylvt
      121 dmdvvvksar ehgadvivdt fpdpigrdai iawagdvkmq lywhtqapqy dalqtvpenr
      181 vyvspqsvrk fvhdfvkfst gkvvsddpka pgveigrpgd tyrririesg fgkmtvlvtd
      241 ghlpypfgre mtgyevpdla atlkqaeaag vtvlvppfrs dgrdaalvqf pggyvaeiha
      301 saar
//
LOCUS       WP_175929376             130 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [unclassified Burkholderia].
ACCESSION   WP_175929376
VERSION     WP_175929376.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..130
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=13682
     Region          14..129
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mseltveasi gpvdylvhft dgvhqwrade paslgggdta ptpvalllss lgactaitlk
       61 mvaqrkgwpl devhvklahe sssagstivr ritldgdltg eqrerllqia nacpvhkilt
      121 hpiaidtaia
//
LOCUS       WP_175929388             473 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: phosphatase PAP2/dual specificity phosphatase family
            protein [unclassified Burkholderia].
ACCESSION   WP_175929388
VERSION     WP_175929388.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Pulido,R. and Lang,R.
  TITLE     Dual Specificity Phosphatases: From Molecular Mechanisms to
            Biological Function
  JOURNAL   Int J Mol Sci 20 (18), 4372 (2019)
   PUBMED   31489884
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Patterson,K.I., Brummer,T., O'Brien,P.M. and Daly,R.J.
  TITLE     Dual-specificity phosphatases: critical regulators with diverse
            cellular targets
  JOURNAL   Biochem J 418 (3), 475-489 (2009)
   PUBMED   19228121
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   4  (residues 1 to 473)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   5  (residues 1 to 473)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12932297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..473
                     /product="phosphatase PAP2/dual specificity phosphatase
                     family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=50624
     Region          46..220
                     /region_name="PAP2_Aur1_like"
                     /note="PAP2_like proteins, Aur1_like subfamily. Yeast
                     Aur1p or Ipc1p is necessary for the addition of inositol
                     phosphate to ceramide, an essential step in yeast
                     sphingolipid synthesis, and is the target of several
                     antifungal compounds such as aureobasidin; cd03386"
                     /db_xref="CDD:239481"
     Site            order(121,129,155..157,192,198,202)
                     /site_type="active"
                     /db_xref="CDD:239481"
     Region          326..463
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
ORIGIN      
        1 msalgggaga gasgglaepa agardasfar rlcwlaamga vffstygfan wlaarraavp
       61 tfafgwehai pfvpwtivpy wsidllyals fffwtrrddl ldhvkrlltv qlvsvacfia
      121 wplrfgferp daggvagalf tllmgfdkpf nqapslhigl lvvlwavyak hlrgtfarav
      181 lhlwfaaigv svlttyqhha idvptgaavg clalflfplr daagrlpgad aspsaagral
      241 arryafgaal vavvalalac vprapgwala agwvalalac vawayrrgap gafqkdahgr
      301 fpvfigwlla ptiagafvns rlwtfrqpap vridarvsig rtpttrdirr hgftalvdlt
      361 aemprwaaad aslayasvpq ldlvaptaaq laqavaaler lhdegrdvlv ccalgygrsv
      421 lcaaawlalr rgltdardal aavravrpha vwsddgvavl qqwidrrrda erv
//
LOCUS       WP_175929398             194 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: flavin reductase family protein [unclassified
            Burkholderia].
ACCESSION   WP_175929398
VERSION     WP_175929398.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..194
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21079
     Region          7..161
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mdshiapval nkayrllnhg ptvlvsarhd gvdnvmaaaw acaldflppk ltvvldksak
       61 trelversgt fviqvptaaq lqlthavgsh slaerpdklr dagvtlfdvd ghdlpfvagc
      121 sgwlacrlip ephnqqtydl figevvaaws dtrvfrdghw yfesadpalr slhyiaggnf
      181 yaigeslhvd pdaq
//
LOCUS       WP_175929410             934 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: type VI secretion system Vgr family protein
            [unclassified Burkholderia].
ACCESSION   WP_175929410
VERSION     WP_175929410.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 934)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 934)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..934
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..934
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=98278
     Region          16..858
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mstqsdliqa ffrgwsqhdr flwlttplga dklvaeslqg wesldrggfr fqltalterp
       61 dlpldkliga svliewqvad gqdarrpfhg hvtaaelvgy ngglarvrlv vepwlallhq
      121 rvdsynfvna svveiseqif ahyargaiap awrwaladpa kyanrsltaq agesdfafle
      181 rlwaeegify wfehqgdahs tdlgkhtlvl adtnqrfapa epevigfhqt sdgdprggir
      241 qfmnarrwri gsvaraswdh rslstrpssv rasgavapge drdvagpyaf qtaaigdqra
      301 qqqldaqrva alqtegsgtr rdlrpglrfa msrhpsldps rafvclrveh daranvsadv
      361 hgaiaqrlga ippgldiapg epgdaqalha afdatthagg alvdgdevyr nrfaalpfdq
      421 ayrplapsgh garvhpvavm pgaqtsivvg agdpvhterd hririqhhaq rgqnsasrde
      481 hpraanapad rgagtwtrmv tsiggdnwgg vsvprvgqev wtewlegqpd rpvavaalyn
      541 gqgnadaqhn alaggpsgst anaaawfagn dhaavltgfk tqdlsasqtg aggsrqfmld
      601 dtagqssarl yttdhgsglt lghikqvqdn rrladrgyga elstqaaaal ragagllist
      661 apgvnqmdas aasqvlaqqr emlqglakfa rqqgaepgas maqpdgvasv gdttsplvai
      721 eglqqsqvsl gatregsgag gagggavawq hphlvahgaa gvaaltaqsh vwtsgtqtvl
      781 sagrdvqvtv qgkssivake gialythgtp ggsrpvpaag ialhaatgtv tvqaqnggtl
      841 dasaqravtv ssakasvalq spkrllltaa naflkmegnd ivigapgkat fhaaqhtltg
      901 prsanvqlps mnkpacvecm rdlahrheai atrg
//
LOCUS       WP_175929416             931 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: type VI secretion system Vgr family protein
            [unclassified Burkholderia].
ACCESSION   WP_175929416
VERSION     WP_175929416.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 931)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 931)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..931
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..931
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=97389
     Region          15..875
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msvitefasl fgafnrlysl dgsgalaafq ierwtgresl sdlfewnvda lstdpaldld
       61 amlgqrvair ttlangtttl rsglvaeaec rgydaglary hlrivpwlaa lahardertf
      121 vnqtladvld tvfapyagia rwrltpdagr rldalgptay rvqyrththy efvqhllaea
      181 glgfcfvede dapaghtmlv fddsaqlaed dtsarrggvp rrssgtatga ddvilgigqs
      241 lsltadritl issdyrvnra ttasttlgrp agarelyddv gpeafdslre aedtvrrqad
      301 aivsrasfwt gygtlrtara gralklvdag wqpvrgaaap edflltrveh vginnlpatv
      361 meaierqlgp lpaaaldprv vrqakaggya nrfdavprtq vwrptladgt gqrlnpvpta
      421 lgaqtaivvg pagdarpgst gpvhadaqgr lrvrfhwqaq ddagtyptra iqrlasdghg
      481 lqqvprighe vlvqfhhgli hrpivlgglf ngrgeggesp spggaagkpl dasiytqagd
      541 hapsaqgnla sglspawhga gggtdrhnha galsgfksqg fdghghnqlv addsdgmgrl
      601 qmatthaatq lnlghlrhqa dnylgsfrgq gvelrsdayg amratrgllv ssyapagaaq
      661 pagdasalqa llarhtalvr rfdqtadthg tlpfaaqrgv eqagqsslng saapldalaq
      721 sfattvgang ytqasadaaq rstgnalpht gdavlgiear gghglvagqa lqwaagetls
      781 lgsggdfnla aaqqlrihsg qgigwlagas haervgigmi agkdgltlqa qrdvlglhar
      841 ddltlasasa dveiaakktv hlavsggahv tieggdvtfg cpgkfvvyaa qhafvgpaql
      901 ntplpqfpek vcvecllham qsgsalagka i
//
LOCUS       WP_175929399             141 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [unclassified Burkholderia].
ACCESSION   WP_175929399
VERSION     WP_175929399.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..141
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15780
     Region          1..141
                     /region_name="COG3565"
                     /note="Predicted dioxygenase of extradiol dioxygenase
                     family [General function prediction only]"
                     /db_xref="CDD:442786"
ORIGIN      
        1 mrlspfhlai pvydlpaard fygrvfglee grssaqwvdf nfyghqlvih ehpktasqas
       61 ahtnavdghd vpvphfgivl dwaswealae rlrafgvtfv iepyvrfqgq vgeqatmflf
      121 dpcgnalefk afrdigqlfa k
//
LOCUS       WP_175929430             258 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175929430
VERSION     WP_175929430.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..258
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=28322
     Region          21..222
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 miheannvie lphalganhf lsaldgmdla ewaphlqlan lrtgevlcda genlgavyfp
       61 vtagislqyt aggkatlgvt eigregvvcd diigsamqrr vvvyrggfay rlpayrfaha
      121 cdasaavrrq vfvrmqlals qasqvmfcgr hhvmrhqlgr wllvayersr sieipvthgm
      181 lgqllgvrre tvsdttrqlh elglihqhrg aivltdlanl erqgcdchri irdetrrilt
      241 vdavanagdv sscrvrti
//
LOCUS       WP_175929445             774 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: xanthine dehydrogenase family protein
            molybdopterin-binding subunit [unclassified Burkholderia].
ACCESSION   WP_175929445
VERSION     WP_175929445.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..774
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81521
     Region          <68..>194
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          203..764
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msapalavhn esrralllgf asgglllafg vpslahaavp vqppvsanpq yggagmphgl
       61 rddpnlfvai apdgtvtvtc irsemgqgvr tsvalvvade lgadwarvkv aqavgdepry
      121 gnqntdgsrs lrqsfaalrr agaaartmla qaaaaawgvd vrqvkvtvhe vvdtksgrtl
      181 gfgelaakaa alpvpdtntl vlkapaefry igkgktalid grdivggraq ygidtrldgm
      241 lyavvarppa ygdtvasfda saaeklpgvv kvvqlastpl psgfqplggv aviardtwta
      301 iqaraqlkid wkhgphagyd saayrktlea aaaqpgdvir ndgdaaaala gaakrvraty
      361 yiphlahatm eppaavarvv dgrcevwtct qapqttrdev akalglpteh vtvnvtllgg
      421 gfgrkskpdy vveaallska vgtpvkltft reddiahdyf havsleafeg gidasgkvva
      481 wqhrtvapsi qstfragvvh eqpgelaqgi adlpfaipnv rienpaaeah trigwfrsvy
      541 niphafgiqs fvaelahaag rdpkdflldl igparrfeph itvkntnyge dpalypvdtg
      601 rlrrvvetva reagwgrklp kghglgiaah rsfvsytaav cevqvgadgr isvprvdiai
      661 dcgpqvnper vrsqlegavv mglgialhge itfkdgrpeq snfngfqvlr mneapreirv
      721 hlvapddyat plggvgepgl ppvapaltna ifaatgtrir slpvadqlak pnaa
//
LOCUS       WP_175929446             153 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: (2Fe-2S)-binding protein [unclassified Burkholderia].
ACCESSION   WP_175929446
VERSION     WP_175929446.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..153
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=16144
     Region          1..152
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mitltvngse qhfdgnpdmp llwylrdvlg htgtkfgcgm alcgactvhl dgvairacit
       61 pvasasgkrv ttieglstdl thplqqawqe lnvaqcgycq sgqimqaasl lktnphptda
      121 diddamsgni crcgtytrir aairlavrrg gaa
//
LOCUS       WP_175929486             220 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: RlmE family RNA methyltransferase [unclassified
            Burkholderia].
ACCESSION   WP_175929486
VERSION     WP_175929486.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Hirata,A., Okada,K., Yoshii,K., Shiraishi,H., Saijo,S.,
            Yonezawa,K., Shimizu,N. and Hori,H.
  TITLE     Structure of tRNA methyltransferase complex of Trm7 and Trm734
            reveals a novel binding interface for tRNA recognition
  JOURNAL   Nucleic Acids Res 47 (20), 10942-10955 (2019)
   PUBMED   31586407
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Caldas,T., Binet,E., Bouloc,P., Costa,A., Desgres,J. and
            Richarme,G.
  TITLE     The FtsJ/RrmJ heat shock protein of Escherichia coli is a 23 S
            ribosomal RNA methyltransferase
  JOURNAL   J Biol Chem 275 (22), 16414-16419 (2000)
   PUBMED   10748051
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..220
                     /product="RlmE family RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=24670
     Region          1..217
                     /region_name="RlmE"
                     /note="23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ
                     [Translation, ribosomal structure and biogenesis];
                     COG0293"
                     /db_xref="CDD:440062"
ORIGIN      
        1 maknrfnqhw lhdhindpyv kmaqregyra raayklkeid eqdklirpgq vivdlgatpg
       61 swsqyarnkl aqgkkrdaer eggidgtiva ldilpmepia dvhflqgdfr eddvlhqlee
      121 vlegravdlv isdmapnlsg vasadaarie hlcdlalefa qnhlkpegal lvkcfhgsgy
      181 sqivekfkqq fkvvaprkpk asrdkssetf ilgrqlkhpr
//
LOCUS       WP_175929525             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Burkholderia].
ACCESSION   WP_175929525
VERSION     WP_175929525.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46220
     Region          13..417
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(25..26,29..30,33,72,130..131,133..135,138,158,
                     161..162,165,247,250..251,254..256,259,287,291,343..344,
                     348,352,368,371..372,375..376,379)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mtqslpsarq pgraataafi gtmiewydfy iyataaalvf gelyfpshdr fvstmasfat
       61 favgffarpl ggvifghlgd rigrkkalmt tlmmmgvatv cvgllpdysk vgilapvllv
      121 alrvvqgiav ggewggavlm agehapqgrr tffasfaqlg spaglilslv afravtsmdk
      181 adflawgwrl pflassvllv vgilirlgvn espefarike thrtvklpva evfrsasglv
      241 llcigantig iagvyftntf miayttqyvg vsrslildsl favaiiqffa qplaawiaer
      301 iggarflkla alfamlspyp mfmlvqggts asliagiala vvcmagfysv iagfvsdvfp
      361 ahvrysaisl ayqicgaiag gltplvgtwl ahrfagqwwp lavfytclag isllcivald
      421 arraaqpaaa ealgsh
//
LOCUS       WP_175929534             437 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: dihydrolipoamide acetyltransferase family protein
            [unclassified Burkholderia].
ACCESSION   WP_175929534
VERSION     WP_175929534.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..437
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46742
     Region          2..437
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mgihvikmpd igegiaevel vawhvevgqt ikedqpladv mtdkaaveip spvagkvlel
       61 ggrigemmav gselirleve gdgnlkaaap vretkvatap vaaaapskpv adapaeppaq
      121 peaprapakp rrdepvappr aalapgerpl aspavrqraw dmgielryvr gtgeagrivh
      181 adldayartg ggaahasqpr gyherhdetd vpviglrrai arkmqeakrr iphfsyveei
      241 dvteleslra elnrrhgdtr gkltplplli ralvialrdf pqinarfdde agvvtrygav
      301 hmgvatqtdg gltvpvlrha eardvwsisa eiarladavr anraqrdels gstitisslg
      361 alggivstpv inhpevgivg vnriverpmi rdgavvarkm mnlsssfdhr vvdgadaaef
      421 iqavravler pallfve
//
LOCUS       WP_175929560             257 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Burkholderia].
ACCESSION   WP_175929560
VERSION     WP_175929560.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..257
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27987
     Region          1..>240
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mnllelddlc iaydtphgrr tvvdglslal prgdigcllg asgcgkttvl raiagfepvr
       61 tgrivldgvp vaapsldvpp errrigmmfq dyalfphlsa aenvafglrr mpkaerrlrv
      121 aemldlvgla dsgdayphel sggqqqrval aralapspel llldepfsnl dvdtrerlaf
      181 elrdilkhtg htailvthnq aeafaiadri gvmkdgrlaq wdtpyalhhh paspfvadfv
      241 rrdvladera ralargl
//
LOCUS       WP_175929565             397 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ammonium transporter [unclassified Burkholderia].
ACCESSION   WP_175929565
VERSION     WP_175929565.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..397
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41344
     Region          1..395
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mdglksgvdt lflligavmv lamhagfafl elgtvrkknq vnalvkilvd fsvstlayfl
       61 igytiaygve ffddigtlsq hngyalvrff flltfaaaip aivsggiaer akfnpqlvat
      121 liivgfiypf fegiawnerf gvqawlahaf gapfhdfags vvvhafggwv alpavlllga
      181 rhgryakdgr iaahppsnip flalgawvla vgwfgfnvms aqtldkisgl vavnslmamv
      241 ggtlaawmag rndpgftyng plaglvavca gsdvmhpiga lvtgaaagal fvamftcvqn
      301 rwriddvlgv wplhgmcgal ggiaagvfgl palgglggvs flsqlvgtlg giaiataggt
      361 lvygalkatv glrldreaef dgadlsihri satperd
//
LOCUS       WP_175929567             274 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175929567
VERSION     WP_175929567.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..274
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29651
     Region          16..268
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 msttvtspal rdresspdei talarglavl rriaaadapv snrelteltg ipkptvsrit
       61 atlvsagflf qlpdserfvl tasvlelshg flrnfdirar srpfmielae rtslsvhlav
      121 rdrldmvaid vvrprsavlv trleigsrmd iartavgray laaledderr llleslrtta
      181 gddwphvsar ltpaldeamr dghaiaigew reglnavaag fvgpsgqrys vncggashqc
      241 ppewlkehvv palqeciaki theiggapar rigv
//
LOCUS       WP_175929652             255 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AzlC family ABC transporter permease [unclassified
            Burkholderia].
ACCESSION   WP_175929652
VERSION     WP_175929652.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 255)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 255)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..255
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26845
     Region          21..247
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 meerflnktp aspprrplne wldgardtip mmvgaapfgv ifgtligggp laawhgalms
       61 lavfagsaqf ialgliagsa sfvvvlattl ivnlrhllys atlapyvahl plrwratlga
      121 lmtdevfava yghyrhyppg tigphyffgs glamylnwqv wtlagigfga afpglqslgl
      181 dfamaatfia ivvpqlgtlr yfaaaatagt layfwqgwpy klgllgavaa gvaigvaltl
      241 lhdrtragsr peaas
//
LOCUS       WP_175929576             503 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: HDOD domain-containing protein [unclassified
            Burkholderia].
ACCESSION   WP_175929576
VERSION     WP_175929576.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..503
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=55003
     Region          18..218
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 mstteylprt alldklwarm nergdfplls eslratmaam knddldftal vrvvlsdfal
       61 tqkvlrlans amymafggni ttvtralmvl gmdavghlvv glklvdhfhq stprridakl
      121 elnrallsgc varkltehae lrggeeavvc tlmrqvgkll vvcyldsewd rirrraaeln
      181 gddaaacidv lgvgfdeigl eaaarwrlpd viragmadgd rlsrddpfdd edgdacrmgp
      241 aaddgptdri rwlravsrcs tdvagalvmp aspqrdaria alaqhcgael dmesealvei
      301 aeclareeas dtvmreivel ranadaiara qaepeaclea gladlralps ehvltpvlal
      361 asesllagla ftrtvmfvrh ddgtfaarlg fgpdvdtvld rlrfderfep dvfhlaisns
      421 vgifieqaqe pkmmkrlpaw yldafddtra fvllpvrvga ttvallygdw agaqparkis
      481 qqemavlnel arelgrffpa ppg
//
LOCUS       WP_175929753             244 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia sp.
            BCC0801].
ACCESSION   WP_175929753
VERSION     WP_175929753.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0801
  ORGANISM  Burkholderia sp. BCC0801
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia sp. BCC0801"
                     /db_xref="taxon:2676291"
     Protein         1..244
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25718
     Region          77..244
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          184..240
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mqtftstqfa ecvraagfdd fvatlahaln givaidcall vdadpddaal scsashsagp
       61 cfdpsseara ctsvfgawra aerstatara rrdplllhrs thacanrivy gpvpmadrcf
      121 ivmprgggta ilglyrhpgs rpfcdddraa iaaaidviaa ladihlrvga vrnvprdleq
      181 awnaglsere ravarllarg etsrtiaaml gvaptsvity kkraflklgv trqceltalv
      241 galg
//
LOCUS       WP_175929764             171 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [unclassified Burkholderia].
ACCESSION   WP_175929764
VERSION     WP_175929764.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..171
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18496
     Region          1..118
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 msktivvain hnftdaflaa aletarerda riaavhvidl thcyagvgdc nyglvvgaml
       61 aygraaldra mttldrnarg adahlltlpv sgsrigrqia svctatnaer vllgarkhaw
      121 wrvvsedvat tlrratstpi qivderpatq ktahladahp gvrhrqrrwq a
//
LOCUS       WP_175929774             557 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: electron transfer flavoprotein-ubiquinone
            oxidoreductase [unclassified Burkholderia].
ACCESSION   WP_175929774
VERSION     WP_175929774.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60543
     Region          25..384
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          453..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mttqdllaqy gpresmeydv vivgggpagl saairlkqla aekgteigvc vlekgseiga
       61 hilsgavmdp raitelfpdw keqgaplnve vtedrflfls eksavttpnw alpdnfknhg
      121 nyvislgnvt rwlgqqaeal gveifpgfpa aeilynddgs vkgvatgnmg vgkdgepten
      181 fqlgmelhak ytlfaegcrg hlgrqliskf kldanadpqa ygigikelwe idpakhkpgl
      241 vihtagwplk sdtyggsfly hmdnnqvvvg fvvglgytnp ylspfeefqr ykthpsiraf
      301 leggkrvsyg araitaggll slpktvfpgg aligddagfl nasrikgsha aiktgmlaad
      361 aafdavqagr rsdelnaypd afkqswlyte lyrarnfkqw makglylgtl mvgleqkvmg
      421 gnvpwtlhhq hadhemlkpa sqctpieypk pdgkltfdrl ssvfisntnh eenqpahltl
      481 kdasvpvnvn lrtyagpear fcpaavyefv knddggdrlv inaqncvhck tcdikdptqn
      541 ivwvtpeggg gpnypnm
//
LOCUS       WP_175929794             116 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: BON domain-containing protein [unclassified
            Burkholderia].
ACCESSION   WP_175929794
VERSION     WP_175929794.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..116
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=11917
     Region          50..113
                     /region_name="BON"
                     /note="BON domain; pfam04972"
                     /db_xref="CDD:428229"
ORIGIN      
        1 mrpiklavla liplltvata avaqdaapap asavssagkk qlrranwhte tqvrkaltst
       61 rglatsdirv varantitld gtvpeqaqie laqtaaqtaa paksvvnhls vkepgh
//
LOCUS       WP_175929800             303 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SDR family oxidoreductase [unclassified
            Burkholderia].
ACCESSION   WP_175929800
VERSION     WP_175929800.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..303
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32074
     Region          3..264
                     /region_name="17beta-HSD-like_SDR_c"
                     /note="17beta hydroxysteroid dehydrogenase-like, classical
                     (c) SDRs; cd05374"
                     /db_xref="CDD:187632"
     Site            order(9,11..14,34,63..65,91..94,114,141..143,157,161,190,
                     192..194)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187632"
     Site            order(115,143,157,161)
                     /site_type="active"
                     /db_xref="CDD:187632"
     Site            order(143..145,150,157,188..189,195,217,220)
                     /site_type="other"
                     /note="steroid binding site"
                     /db_xref="CDD:187632"
ORIGIN      
        1 mskvilvtga ssgfgrltae alaraghtvy asmrdiggrn apareqlhal ardagidlrp
       61 leldvqsdas idravaqvie qagridvlih naghmafgpa eaftpeqyaq lydinvlstq
      121 rvnravlphl rgrreglliw vssssaaggt ppylapyfga kaamdaiavl yarelsrwgi
      181 etsivvpgaf tqgtnhfaha sapadaaraa eydagpyadf grevqeafaa ivpahahasl
      241 vadaivdvva tpagkrpfrv hidptedgan vgfavldrlr aemlhrvgls dllsprvpep
      301 nra
//
LOCUS       WP_175929812             218 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: response regulator transcription factor [unclassified
            Burkholderia].
ACCESSION   WP_175929812
VERSION     WP_175929812.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..218
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23694
     Region          12..206
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mtsmtgetad pvvfviddds amreavetll dsvglrvrsf daapaflald lpdvpscvvl
       61 dvrlrgqsgl avqehitrel ripvvlmtah gdipmsvqam kagavdflak pfrgqdmida
      121 vtralendrk rrevdrsaai lracyasltp rertimamva ngllnkqiat alnlseitvk
      181 lhrgqamkkm ksqsladfvl kadalglvdr esrlvdha
//
LOCUS       WP_175929832             216 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [unclassified Burkholderia].
ACCESSION   WP_175929832
VERSION     WP_175929832.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..216
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22216
     Region          7..190
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtlhypllfa ylaaivllia tpgpvvmlvt gtvarrglrq gvltavgana aslvliagam
       61 lmvfgvvmvs arllaglhva gclfiavlai rtllgewrac rarggdgmaa gepvaqrrgl
      121 pgivrgflvg ianpkdllff vaffpqfvgi tpdsrvslai laalwiavdf tilagymaai
      181 nhpaihrkqr wisassalal laialaglgg tiagaa
//
LOCUS       WP_175929974             252 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: YoaK family protein [unclassified Burkholderia].
ACCESSION   WP_175929974
VERSION     WP_175929974.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..252
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=26646
     Region          11..243
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mpaqyfrnlt gkhrsaaanr qlgfslafva gaanaggfla vrqytshmsg ivsaiadqta
       61 lgdvrlalag isslgsflig agcsailvnw grrrglhsqf mlpllveaal lllfgllgsh
      121 lalwetffvp vtvtllcfim glqnatitkl sgaeirtthm tgivtdlgie lgklfywnrs
      181 aidvdahavi anrsklriha tmlasffvgg lagaigfkrv gyvstvplaa vlvtlaivpv
      241 iddllallrs kr
//
LOCUS       WP_175929977             244 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Burkholderia].
ACCESSION   WP_175929977
VERSION     WP_175929977.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..244
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=25465
     Region          6..242
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 maaddsllal lafgdggygr vfasafaltf gvaaasfctg vllglagalg klsryaalaw
       61 larlytmlvr alpellclll afyavapave halrgsgivs gdfsfdpfvv aalslgfiqg
      121 ayltdifraa lvnvpagqie aayaygmtpw qtltrirlpa aarlalpgvg nvwlnatkda
      181 sfisvlgsft dllkasqlaa gatrhhvffy lvtaalflll svtsaglfaa lerhanrgtr
      241 ratt
//
LOCUS       WP_175929978             255 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Burkholderia].
ACCESSION   WP_175929978
VERSION     WP_175929978.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..255
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=27632
     Region          3..235
                     /region_name="ArtM"
                     /note="ABC-type arginine/histidine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4160"
                     /db_xref="CDD:443325"
ORIGIN      
        1 mifslpflld tvmpkllaav pttlaltlvs gaasvllgvp lalaagarht plrwsargwl
       61 mlirgtpllv qlyllyygfg qivprewmrd swaspllrda fwyaivalsv nesayvatil
      121 rgaiagvpag eieaghaygm trvqvlrriv gprawrlalp altgeailll kstvlastvt
      181 vfdvmgtant lrfetlrvye plagaaivyv vlvalltipa arleqrvnry ltrvpdarpr
      241 arhrrassga waapn
//
LOCUS       WP_175929870             946 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ATP-dependent Clp protease ATP-binding subunit
            [unclassified Burkholderia].
ACCESSION   WP_175929870
VERSION     WP_175929870.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 946)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 946)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 946)
  AUTHORS   Ingmer,H., Vogensen,F.K., Hammer,K. and Kilstrup,M.
  TITLE     Disruption and analysis of the clpB, clpC, and clpE genes in
            Lactococcus lactis: ClpE, a new Clp family in gram-positive
            bacteria
  JOURNAL   J Bacteriol 181 (7), 2075-2083 (1999)
   PUBMED   10094684
REFERENCE   4  (residues 1 to 946)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11909043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..946
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..946
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103179
     Region          4..>54
                     /region_name="McsA"
                     /note="Protein-arginine kinase activator protein McsA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3880"
                     /db_xref="CDD:443088"
     Region          83..876
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mpalcdicha rpavaratvm qdgerktisi cdyhfrqlmr hqsmlnpfds llggggpssl
       61 fgglgdaspl aaeipresvd ptdafseqtl ellqraaeka helrrgelds ehllyaladt
      121 dvcaallkel klspqdiqsy idahahtgta dpdapldkls isprvkkavq yafqasrdlg
      181 hsyigpehll iglasvpdsv agtllkkygv tpealrqkvv kvvgkgaedg rvntptgtpn
      241 ldkfgrdlta iacqgkldpv lgraqeiest ievlarrkkn npvligepgv gktaivegla
      301 qrivngdvpe vlrdkrlvev ninsmvagak yrgefeerak qlidevtakq delilfidel
      361 htivgagqgg geggldianv lkpalargel sligattlne yqktiekdaa lerrfqpvfv
      421 pepsveqtiv ilrglrdsle ahhqvtfadd afvaaaefad ryitsrflpd kaidlidqaa
      481 arvrigatsr pvdiqegeaq iaqlkreqdy atsrkrfdea kqfeeqinak qkavdemmea
      541 wqrktgsetl evtvesvaev vsrltgipvs eltqeerqkl lkmeeqlrer vvgqndavva
      601 vsdavrlsra glgqthrpia tflflgptgv gktelakala etvfgdeqai iridmseyme
      661 rhavarliga ppgyvgydeg gqltervrrr pysvilldei ekahpdvynv llqvfddgrl
      721 tdgkgrvvdf sntiiiatsn lgaaiimdnl tqpeaarktd kairdelmqv lkghfrpefl
      781 nridevivfh alskdnirai vqiqldrvvr taaaqdialv mgdslvehlt evgyqpefga
      841 relnrqirqt ietrlakeil adrlksgdkc eldydkasde vkfnklaape akdtteakpd
      901 adgkaksngk aakatgdakp dvapadappp aakpgkkssg akkdah
//
LOCUS       WP_175930031             243 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DsbA family oxidoreductase [unclassified
            Burkholderia].
ACCESSION   WP_175930031
VERSION     WP_175930031.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..243
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=26113
     Region          15..214
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(23,26)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 mttapapaar ptltveiwsd licpwcwigk rrfdealaaf ahaervdval rayrlmpgqp
       61 vepveamlas kyrmspaqvd qmlrqvtdaa asvglrydlp gtlvgdtldg hrlvklaqas
      121 grayalterl yrayfcehgs lfdhaeltef aleaglersa veavlrsday rdeveadiar
      181 aaqiggrgvp lfvfggryav sgaqpadtfa qaldqawrdg ivelggsdaa acgpdgcelp
      241 ars
//
LOCUS       WP_175930049             268 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Burkholderia].
ACCESSION   WP_175930049
VERSION     WP_175930049.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..268
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29068
     Region          1..238
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 msssitardi svefpiyens hrslkktvln lttggrigqd sgrhaivqal snlnfnfehg
       61 eriglvghng sgkttllrtl sgvyapvrge lkvqgkiasl ldvsmgldpd atgfeniylr
      121 gildglkper irgkideiad fselgdylnl pvrtyssgmm lrlafaists ieadilimde
      181 wlsvgdaefs rkaaqrlesl vgqasilvla shdpelvarv ctrkismehg qmvadepvir
      241 peptgdtvle glpvadlvpd drpkhvpq
//
LOCUS       WP_175930070             418 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: lipopolysaccharide biosynthesis protein [unclassified
            Burkholderia].
ACCESSION   WP_175930070
VERSION     WP_175930070.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..418
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45192
     Region          12..395
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mlkrfgnpdv akavanlvwl glerltqigv aiaisgllar yfgpdvfgkw qyantlllvl
       61 apltwvcgae ilvptivqrp paqlgavlgs afvlriavsv aalaatwiai aagafdplvg
      121 amlaglavtm vfrepfvgvi nawlqsmtys kpqlvtsmvt alakallvwl lvraaagpar
      181 fawlwaleaa aigvalllyy rhrnggtlgw tfdtplfrhf atagtvfwlg licmylflkl
      241 drlmlerhvs fadlgrysaa qqlnenwitl almlaqtiap afvyrvqdva rlrrnivrli
      301 amtaglmtag alvldaaapl ivgkvfgrgy easvdifrwa vwlsvpagie aignlivlky
      361 qakfvlltkw llalaiaalv nlfaiprlgl ygalvglaag ylaaaavnfh yirfklqt
//
LOCUS       WP_175930103             222 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [unclassified Burkholderia].
ACCESSION   WP_175930103
VERSION     WP_175930103.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..222
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23126
     Region          12..213
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msfppasmls dgfflslslc ldiglvnvam lsltlshgfr pgfwlgvgsc vgdlvyaala
       61 lagmavllqf epvrwivwig ggavllfltw kmarealtpa taadddanda ppprasarrs
      121 flrgmllams spsailwfaa vggaliakag attpatasvf lsgfflggla wtlfmctlas
      181 qgrkragagl mrachvasal lfayfsysvi vggyrdlivh aa
//
LOCUS       WP_175930121             216 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: trimeric intracellular cation channel family protein
            [unclassified Burkholderia].
ACCESSION   WP_175930121
VERSION     WP_175930121.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..216
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23686
     Region          19..216
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mrrrptggrv phprltlaia vleaiatlaf aisgfieark nrldsvgtfv valatafggg
       61 tlrdillerr pfywvvhddy viaifvlalf apfvlrmlsr lsaerlllia daiglgifsi
      121 sgtsialdae mprfiavmmg vitgvvggiv rdvlcndipl ilrdsrpyat cafvgcwfyl
      181 llvwlqfdsv ysvllatgfi lvarlatfkf dvrlph
//
LOCUS       WP_175930136             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Burkholderia].
ACCESSION   WP_175930136
VERSION     WP_175930136.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45684
     Region          21..426
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(34..35,38..39,42,81,139..140,142..144,147,167,
                     170..171,174,257,260..261,264..266,269,297,301,353..354,
                     358,362,378,381..382,385..386,389)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msasppavah atgsagavsh rrivfasfig taiefydfyv yataaalvig pvffphgsat
       61 aqalsafvtf giafiarpig sflfghfgdr igrkstlvas llvmgvstta igfvpgydti
      121 galapvllcv lrfgqgiglg gewggaalla tehapqgkrg wfgmfpqlgp svgflmsngl
      181 ffalalslsd eqfrswgwri pflvsavlva lglyvrlkia etpafqaald rnervrvpva
      241 tlvtqhwrpt llgalamvvc ytlfyistvf slsygvsalh iprqsflgll cfavvfmgla
      301 tplsawasdr fgrkpvlvvg aiaallsgfa mepllgsgsm alvalfltie lflmgvtfap
      361 mgallpelfp tnvrytgagv aynlggilga siapyiaqll aargglswvg gyvsvaaais
      421 ligvllmret rdaslv
//
LOCUS       WP_175930196             695 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DUF262 domain-containing protein [unclassified
            Burkholderia].
ACCESSION   WP_175930196
VERSION     WP_175930196.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Bair,C.L. and Black,L.W.
  TITLE     A type IV modification dependent restriction nuclease that targets
            glucosylated hydroxymethyl cytosine modified DNAs
  JOURNAL   J Mol Biol 366 (3), 768-778 (2007)
   PUBMED   17188297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..695
                     /product="DUF262 domain-containing protein"
                     /calculated_mol_wt=78220
     Region          5..568
                     /region_name="GmrSD"
                     /note="DNAse/DNA nickase specific for phosphorothioated or
                     glycosylated phage DNA, GmrSD/DndB/SspE family, contains
                     DUF262 and HNH nuclease domains [Defense mechanisms];
                     COG1479"
                     /db_xref="CDD:441088"
ORIGIN      
        1 mafssaelqr lgdllagyhf hipdyqrgfa wgeaqlealw ndlhvtvssq akehftgvvl
       61 lrqlnednat lqsvelidgq qrvisamtla salarrasas egesqraarh dfkvsfldna
      121 elqtyfnfwt lndenaaarv gpdcssyaan lknaaqyfrk raaelpdafh arqyldvlld
      181 rfrlfvldah pdfdihvafe tlnnrgkkls tlellknrli yltnvlpsrd aevdvstdep
      241 hlngralreq vhlawkgiyt slgrspatqn hddeflraha vayfgevkda dwldnvllne
      301 tftaknksla ledvsayirn leqaavwwsh vhetklmptt hqlhleriar ighayfkpll
      361 laaymratal nsealgepra yeadikpvag lleqverfiv lvlnlsgras hlgrshmnrm
      421 ahsllrpdsf dcpwkdkglp tmpaddaiaf aksyvkayid neevgdswsd prfewvgays
      481 aadvqrqvaa rlregtgyyr wpfarlllle yeearreagn kpialewpwd efsfdktveh
      541 ifpqtpdedg ywdraipidg rakalrkavv hslgnlmlls nkvnssvsnl pfrakggtns
      601 klmsyevgsh setqvaqvfr grdwtvacia argiamlkfa eerwsfrlte apdnystylp
      661 ylfgdkadav yageasngrq vdgralnalv dallg
//
LOCUS       WP_175930210             920 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: type VI secretion system Vgr family protein
            [unclassified Burkholderia].
ACCESSION   WP_175930210
VERSION     WP_175930210.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..920
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=98983
     Region          18..816
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msiaatlrnf asglvdlnkr pvslhfgqaq ravghllalh hadiheglms giegqltcvs
       61 tydhlspalf lglpvsvrlt tdrgdirain aivhevrtgq sdgeltvyql hvcdalslmd
      121 rrtnarlfrs rsvpdilatl mnewkqrspa farafdfdls tlqadrypar eltrqvnesd
      181 arfirrllrr egitvfakaa pvdgrrgaad erpihtlvfc ddphrlpdap agivrlhprd
      241 agveqrdtvt lfaydqrlsp gkvrrpswdy ktarmddfeg vtgidqgesg ndlarlltdv
      301 aidiphvgds wndhariahd rmlahqfeaa rfegigtvrd mlvghgftla gdpeldmksi
      361 drrrfvvtsi rhviwnnlpt dlsgrasglf aasrnlsptt pppdasestd tryensftcv
      421 qrgvplkpay dpaidvppvh lltgtivgtq geevfcdkag rvrvlihgld padhahaqga
      481 gtnglagdsa plrvvaslag ecfgalflpr vgmevllgnl sgdpdrlvii gvlsnganpp
      541 atfsntgalp gnryvsgikt revrgrrhnq lrlddtpsqi saqlasehah sqlnlgyltq
      601 prvdghgndr gegaelrtda aaalraaqgm llttyartra tggqldrdel irlldqcmal
      661 fkslgdragq hggqfadtag qdnianafrh wkpggsasga tgdasafmaf gaqagslnvt
      721 pkthvtyage nidqiaqqhm qitsgerinl haghgvamfa hgdgvsaiah qgkvalqsqn
      781 ddtqiesgkn iqltaadgrl agtasdevvf vtsggaylkl hgtdielgcp gkftvksdgh
      841 awdgpasmsv dlptfdrrtl grvpklirpt dgnaapgfeg qiekasgtls slttdsagel
      901 pavdtdrfer lavqfikknv
//
LOCUS       WP_175930253             553 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ShlB/FhaC/HecB family hemolysin secretion/activation
            protein [unclassified Burkholderia].
ACCESSION   WP_175930253
VERSION     WP_175930253.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..553
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=59060
     Region          8..553
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mdaatrragc vaatllaagv ahaqvpvpsa gqsirdieav rpslpaathp didmaptepq
       61 sapsedagpr vavrafvveg nttvptgeld allaeftgrd lsfaelqqat sritqyyrdh
      121 gyvlaraylp rqdiddgivr iavvegrygk idvqnhsrvl dgvlrqqiga lqpgmvahgg
      181 slertlmlld empgvtakgt lrpgaepgtt dlvidaergp fatgsveldn ygdaltgryr
      241 atgsvdvnap lrvgdrfslr gltsdahqry yraayqlpvg pastrvgvay sdmnyriggr
      301 lkdlgyhgsa dvrsvfvtqp lvrsrratln aqvtyenkhl rdtygifdit ndkavdlltl
      361 glsgnsddtf ggggrngfsi avgtgrlrgn daldmndlth aqgrftklnv salrlqalgs
      421 rlqlytqfna qlasrnldss ekfnlggpyg vrayalgagn gdqgwqasae lrylaspgwq
      481 vstfvdtgrv qlskqpwsre rntvqlsaig vgaswfgsgr qvtvaaalpl gradpvasat
      541 rspsvwlqaa qyf
//
LOCUS       WP_175930261             352 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: porin [unclassified Burkholderia].
ACCESSION   WP_175930261
VERSION     WP_175930261.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..352
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=36911
     Region          3..352
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mrsliaascf aalatgvhaq snvtlfgtlg egvrwtdgvk gghqigfdnn aiagntiglk
       61 gtedlgsglk avfllqsgfs lgtgalktss vlfsqrayvg leggfgrltl grqlnafedv
      121 gtqldpnean gpslatvpgi vwggnfftld arfnntikyv graggftlra syspggvagn
      181 tragtnfaaa asyqfstlll agayqktyna aatqwaqstl ggltwqlgpt rlylgysgle
      241 vsapnaksva rrdhipstgl vyritptlql tgaayydias nlknvagadg rkmttyamle
      301 yflskrtely vefdrngfsg aykkdpanvs alnlrpdgrs vtgvsvgvit qf
//
LOCUS       WP_175930264             204 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175930264
VERSION     WP_175930264.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..204
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23300
     Region          7..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvrqaqqers eltraeilai aleqfstrgf davslrdiad aagvnhamir yyfgnkenlw
       61 rasvtqlfer fmegietpdp assgfsidea kryvrnyvry caahpeharl mmqeanrdse
      121 rlkwmaetfv rsrhartvpl vrylsekmkg lsgidpvmll ymitsiaqvp ylltaemrya
      181 hgidalsers idahcdavva fifr
//
LOCUS       WP_175930274             233 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: flavin reductase family protein [unclassified
            Burkholderia].
ACCESSION   WP_175930274
VERSION     WP_175930274.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..233
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25328
     Region          15..175
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mnaphcvtep nilyfgtpvv lvstlnengt anlapissaf wlgwrgvigi aassqttrnl
       61 lrtgecvlnl pssaqadavd riarttgtyp vpdgkrakgy vfepdkfgta glteaasqti
      121 appralecpv hmeavvaaty gigddmpdlr grirvfevri qrvhvhpdll mdghpdridp
      181 dkwsplimsf qkfyglaprq vhasrlaeip erayrspdie rsrevgtltg tgr
//
LOCUS       WP_175930286             293 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175930286
VERSION     WP_175930286.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..293
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31123
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mlldnlalfl rivekgglaa agrevglspa tvserltale rhygaalltr ttraisltde
       61 grtlvdgarr llaeadeles rvrlgvqtls gpvrlsapad lgrervvpvv dafladhpgv
      121 tvdlhlgdgy vdlvgqgldf airrgtlads slrsrslgra rrvvcaspay laahgtpahp
      181 delashdciv mrfgqelyae wpfsidgalk rvvvrgrrva ndgalvrawc vaghgialks
      241 lvdverdlas galvevlgaf spgdvdlqiv ypgsvaqprr vralidrlaq ala
//
LOCUS       WP_175930292             269 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TlpA disulfide reductase family protein [unclassified
            Burkholderia].
ACCESSION   WP_175930292
VERSION     WP_175930292.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..269
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28731
     Region          42..>97
                     /region_name="Lgt"
                     /note="Prolipoprotein diacylglyceryltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0682"
                     /db_xref="CDD:440446"
     Region          136..263
                     /region_name="TrxA"
                     /note="Thiol-disulfide isomerase or thioredoxin
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0526"
                     /db_xref="CDD:440292"
ORIGIN      
        1 mlsigpfsir vvavavaall awlvarfiqr rppdghhksa sslildvllf gliaarvgyv
       61 aqwwpdyaas praivalgdg gfdarigiaa alafagwrlr rlpalrrpvl agivaglgaw
      121 giaqgtlatl qrgapplaam plqaldatpv lpagfvgkpv ivnlwatwca pcrrempile
      181 qaqrdhpgit vlmlnqgena qavrafleqq glrfdhvlld pslhamhayg srglpttlff
      241 nakgelvesh mgelsaarlk davtqrfgq
//
LOCUS       WP_175930293             474 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TolC family protein [unclassified Burkholderia].
ACCESSION   WP_175930293
VERSION     WP_175930293.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..474
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50404
     Region          135..468
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkrifllaal lwvtaadaet ldvfrtgddv paspsapmvr dascrptpdd rplelddail
       61 eaicahpsar rawadaraqa aavgiaeaay lptlnatagi qrntlsttyd ysaiglgsqs
      121 qsqnssskyg mlnlswvlfd fgkrsaglrq arallaaana ehggalqtvf fdaaqayyam
      181 hsaqasvdaa kqaeriards laaasakhaa gagtlsdqlq aqtlysravl drvgaegdlr
      241 aatgvlavam greanmpvri aaekpvpnda aitqgvdqli teaaarnprl laarakldaa
      301 ranvdaaraq rrptvsllgs ytrnnpsyqq qpesfpiths hgstigvqvt iplfegfasg
      361 yrveqaqaqa daqeaalrdt elqvsldvwk cyqslladts nlqtssalls daqrsleiar
      421 grykegvgsf tellnaqtaf vdaqkqrvla vskwhterlk laaslgklgi waeq
//
LOCUS       WP_175930297             278 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ion transporter [unclassified Burkholderia].
ACCESSION   WP_175930297
VERSION     WP_175930297.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11997982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..278
                     /product="ion transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0034702 - monoatomic ion channel complex
                     [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30070
     Region          29..234
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
ORIGIN      
        1 mispiqssld aardavthva rrpsflrkld iavlalivas vlvvmadsvq elhaqyghal
       61 yaaewaftll fsaeyllrlc takkpaayar sffgivdlvs vlptylafff pglhalidvr
      121 llrllrvfri lglsiyleeg qmliraltra rrkifvfigg mfvlvvilgt viflvegpeh
      181 gitsipvgvy waavtmsttg ygdltpvtpl grlitscail lgygiiafpt gimgaelvas
      241 amerkrpnad tdtrccpncg aavpppepid aaaprrpe
//
LOCUS       WP_175930338             452 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [unclassified
            Burkholderia].
ACCESSION   WP_175930338
VERSION     WP_175930338.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..452
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=48472
     Region          17..434
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mdnitpnlat eraarvpriv ivgggagglq latrlgdtvg rrgqaeivlv drypthfwkp
       61 llheaasghr dpashtieya aqakrhgfrf vqgalqrvdr aartatiaav ldadgteilp
      121 qrmldyddlv lavgsvtnff nvpgaerhal plenldqaed frrkflaact kanhraeqqp
      181 arraapicin vigagatgve laaalrhavq qlttyrfkal vsardvhirl ieggprilpa
      241 lderlsgkmh aqlralnvdv ltdtrvaevg adavatvtge rlasditiwa agvagpamlr
      301 digdialnrs nqvivtdtlq tpddphvyaf gdcaacpsat aggflppraq vahqqavylv
      361 nafarrvagk pvagftfrda gtvvslghag avyqadiggr srslivdgla aiglykllyr
      421 khlfsvvgmk ralfqslshw lqsrnqpsik lh
//
LOCUS       WP_175930360             517 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: class I adenylate-forming enzyme family protein
            [unclassified Burkholderia].
ACCESSION   WP_175930360
VERSION     WP_175930360.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..517
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=56308
     Region          3..516
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 maiidfydrg wrlnpdgiay iqdernytfq eigelscria ngllaagfak eakaavwadn
       61 dvigwscalg mwraglayip vngrnavaen qyvldafdce vlffhqafaa aidalrpslp
      121 kirlwvclda dlpwapslas wsehqpatpp vvdyamddvv alsatggttg apkgvmnthr
      181 slqtyfaqfm iamtygdarp vnlaaapmth tagmmslpct arggtvvvlp kpdpalllga
      241 ivkhrvteff lpptviyrll dipgieqvdf sslryflyga apmsveklkr aidvfgpvmt
      301 ggygqteapa sisyltpaeh fvdgklasdt rlasvgrpnp lvrveivger gellkqgetg
      361 eicvrgdlvm kgyyrapdkt aetivdgwlh tgdighldqd gylhitdrkk dmiisggfnv
      421 ypseieqviw ahpavqdcav igvpddkwge avkavvelna gqqvsaeelv alckeklgsv
      481 kapksvdfva alprstagkv lkkdlreqyw qgrqrri
//
LOCUS       WP_175930373             219 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: c-type cytochrome [unclassified Burkholderia].
ACCESSION   WP_175930373
VERSION     WP_175930373.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 219)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 219)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..219
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22978
     Region          <55..123
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          138..217
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mkkrivlita lvaigallal ygptllgfyr lqrhidtaaq addadggpwp rvtdacmgch
       61 gvkgtslsqa ypslagqpaq yvaaqlhafa sgqranptmg plamtmseae itrlagyyak
      121 qapldnryfk pdarlrtkge qlvtggacaa chgarltgqa qfprlagqgy dyllaqldaf
      181 asgsrseatg tmqrvaqams addraavaty laslgparq
//
LOCUS       WP_175930460             466 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: mechanosensitive ion channel family protein
            [unclassified Burkholderia].
ACCESSION   WP_175930460
VERSION     WP_175930460.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..466
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=49544
     Region          161..437
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 meslqsrlls hrlasvirdf hqpvmiwqaa ilvgalcfaw vaarfvhgri darrraagre
       61 pgagaqsler alfplfgslf vgaaqlafdp fmstsllsla lvplfgigli yvlfffarrv
      121 fardghthaw lsivekivst vvwaamvmtv lgiqrdvlgw ldsvqfrvat ahltllsvis
      181 galwvcvtlm vamwlgsvle drlarastld anlkvvlsrv grallvfaai liglslvgid
      241 vtvlgvfgga lgvglgfglq kiasnyvsgf iilldrslrl gdaisvgglq gvvtqirtry
      301 tvvrgldgne tlipneklit dvvqnqssyl trgyakvavq vaytsdveqa lalladaakd
      361 vprvlaepap tpylvsfgad gidlelgfwi edaakgtsgv rssvnrniwr lfsahgisip
      421 fpqrevrvvg lpdgfpaagv aagldpaagl dpaaadgald grrpaa
//
LOCUS       WP_175930510             137 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DoxX family protein [unclassified Burkholderia].
ACCESSION   WP_175930510
VERSION     WP_175930510.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..137
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14239
     Region          4..129
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mntnrlndfa atllrvalgv lylahvaqkv fvftlpgtaq ffaslglpgw laylttfvel
       61 agglalivgl rvriaalvll pfmlgavaah lpngwsfasp nggweypafw avtlavqall
      121 gggafaigaq eaavqra
//
LOCUS       WP_175930524             269 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175930524
VERSION     WP_175930524.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..269
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29508
     Region          19..98
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(44,69)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(51..52,63,66,70..71)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          117..267
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mnqptsapvp pldatparal gefirahrer lspqavglpp gprrrtpglr reevaqlcgv
       61 sptwytwieq grpvsasada lariavalql skaeraylfe laaqrdpaep dvaggdlppt
      121 laatvaaiat payvldrqwn alawnapaaa lfsgwldgeh drnllrftfm spaartlivd
      181 wetrarrlaa efradairhl tdaptralid altagsdafa qywasqdvfe reggrrefdh
      241 padgrlvyqq itlkpahred lklvvlvrd
//
LOCUS       WP_175930562             193 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [unclassified
            Burkholderia].
ACCESSION   WP_175930562
VERSION     WP_175930562.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..193
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22042
     Region          21..186
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 meppltsqpm tdadrditat vmrertrlgn firrrirdpd daedvlqdvl hefvqayrlp
       61 apieqasawl fraarnrivd rfrkkkeqpl tdlldaddea dseyrldlal pahdagpeal
      121 yartlllkal qdaldelpan qrevfiahel dglsfremaa qsgvtlntll arkryavlhl
      181 rarlqpiyde ldi
//
LOCUS       WP_175930565             238 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: O-methyltransferase [unclassified Burkholderia].
ACCESSION   WP_175930565
VERSION     WP_175930565.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..238
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26156
     Region          79..238
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mastthallq rlheesqrei iararaqfqg pneafptlvd eyealaprlr grfletfglf
       61 tedfessags alslavsaet grflrnmvla qrparilelg sscgvstlyf adalrtlgrg
      121 vviatecdaf kcarlrahve taglgahvdv regdvfetva gldgtvdmvf idvwadaylk
      181 lfkqierllr pgsvvladnm ytaedavrpy khyldenprf stttldfesg veftvvva
//
LOCUS       WP_175930601             414 aa            linear   BCT 11-JAN-2025
DEFINITION  lactonase family protein [Burkholderia sp. BCC0801].
ACCESSION   WP_175930601
VERSION     WP_175930601.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0801
  ORGANISM  Burkholderia sp. BCC0801
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Burkholderia sp. BCC0801"
                     /db_xref="taxon:2676291"
     Protein         1..414
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44181
     Region          52..411
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 mpnrlrerda rastrgfplr fahwmkgfai vlslsathaf aqqssapadg vynllvgtyt
       61 gggsdgiyvy rfdtktgsva pvssaktenp syllpsrdgr tvyavnelpg dngpatqrgg
      121 vsafrfdakt galsfidrvs segndpcyla lspdgkylvt anysvaadpg gsfavfplrd
      181 dgavgqavls vhhegtgpvk grqdgahvhs tvfspdgryl fvqdlgadki ygyrytvdgs
      241 rglisptdtr ytpvkagsgp rhlvfsadgr fayvtselna svevfgyhdg kltpietvpm
      301 tapgfkgkvg ggaihlspdg rflyvsnrgd andlviyavn radgrlkhvg rqsslgktpr
      361 eflidptgkw livgnqdsdt fyvfsrdvet gqlganpqkv avgkpvdfkl vpvq
//
LOCUS       WP_175930610             363 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 9 protein [unclassified
            Burkholderia].
ACCESSION   WP_175930610
VERSION     WP_175930610.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..363
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40275
     Region          5..334
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mangkptqri lviridflgd mlcttaflga lkarwpdael hvvanrynaa alagnpnvht
       61 ihtyvysrqc erndrpgrmr affdrlrlvr rlrrlrfdlv ivpnggmhrs svqfarqlra
      121 kdcrwhdaet efddrkpehv srrpmcheal sgfrlvpelg cadldrlels vhpdralqev
      181 whrllgartk prvglfvsnk averrwpadr wrdlgerlap vadvivfrdp aigghatadd
      241 gwrdvnarhv apssvaelma aaslldaivs adsapvhlas algvpvaalf edrpekylrw
      301 hplgvphvil ragptvdaig vdaveravrh llshadhrde apagttlaqr aaatapaiet
      361 ias
//
LOCUS       WP_175930680             388 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: pyridoxal phosphate-dependent aminotransferase
            [unclassified Burkholderia].
ACCESSION   WP_175930680
VERSION     WP_175930680.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..388
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=41391
     Region          40..375
                     /region_name="AspB"
                     /note="Aspartate/methionine/tyrosine aminotransferase
                     [Amino acid transport and metabolism]; COG0436"
                     /db_xref="CDD:440205"
ORIGIN      
        1 mrrhrpvrlq hiagigvdrm gsiadhadvd llrlenldtd ipptaealaf traaiqrdsa
       61 nsylpfvgqd rlrasaaahv salsgqhfta dqvvvsaggl sgilntllat vetgdevivt
      121 dptyagllnr vrlaggvprq vpfiftpgge wkldqaalra aigpqtrvml lmspsmpsgg
      181 cfdasdwhli aslcvqndll lildsamerl lfdgrtvihp aglpgmaert vtvgaaskel
      241 rmigwrvgwi vapawlipdl vavslanvvv pvgiaqeaaa valehsasdl pgyvselerr
      301 rdtvaaelsg lpfgmpaggw smllrvsdfg ltgsqmserl lshgvcatam tgwgvvhgeq
      361 yvrfvfsnep verlrtlgdk vrfaleda
//
LOCUS       WP_175930705             479 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [unclassified Burkholderia].
ACCESSION   WP_175930705
VERSION     WP_175930705.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..479
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50591
     Region          6..477
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mnesssrsea glsrnavgls hivffvvaaa apltamvgat paafslgngp gvpgvfvlag
       61 vmylifsigy aamsrhisna gafyayiang lgrpagvgga fvaivaynav qiaiycmfgf
      121 flndsiqrhy gvdvpwwafa lacvavvhfc garhiefsgr llgmlmigei aivmlldlai
      181 vvhgagtggf sakpfspamv fapglgtalv fvlgsymgfe ataifseear dpkrtiprat
      241 ylavilimaf yalsswaive awgeraiaaq aardpanlwf avsgrllgsi atdamnvllv
      301 tslfaailsf hntitryfya mgrervlwrk lghtcpvhrc pdvagkvqtl ialaalagsa
      361 afrldpfavv fswmsalati giiavqilva asviaffard hrdagvvhrl iaplvsvial
      421 gaclvlvvrn lsvlsgsdst fvamfpyflv avgalgiraa lrlkrsdpdl yrelgraaq
//
LOCUS       WP_175930716             171 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [unclassified Burkholderia].
ACCESSION   WP_175930716
VERSION     WP_175930716.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..171
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19262
     Region          29..143
                     /region_name="CatE"
                     /note="Catechol-2,3-dioxygenase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2514"
                     /db_xref="CDD:442004"
ORIGIN      
        1 mtpsdirqha eranasglpl ptprvqrthl slfvrdpvrs stwyaevlgm tetargeqwv
       61 fmsfgqkhhd ialiraasda elgtiglqhy gleiagglte lrrlygmlir rdvpivkitd
      121 hkvgigvyft dpdgnrleff cetvmddeeg krvlhrynap sdpfqleplf d
//
LOCUS       WP_175930735             475 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Burkholderia].
ACCESSION   WP_175930735
VERSION     WP_175930735.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..475
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50854
     Region          40..459
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(50..51,54..55,58,90,140..141,143..145,148,171,
                     174..175,178,287,290..291,294..296,299,328,332,388..389,
                     393,397,413,416..417,420..421,424)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mssidlspvt pvsspirsas dvarlintvd ssvsharmiv llalggvfld aydlttlsyg
       61 iddvtrefgl tpaltglvgs aimigtifgs liggwltdri gryqvfmadm lffvvaaiaa
      121 glapnvwvli garfvmglgv gidlpvamaf laefskfngr gnkasrlaaw cpmwyvassv
      181 cfllifglyf llpaehagwl wraslifgaa palviilfrn rfmnesplwa anqgdlanaa
      241 rilrksygih aheaedarre pspppvrirv lfqrpylgrt ivasvmnlci pfeytaiaff
      301 lpsilsqflg agvfetiaas lalnvlfaft ggllgmrlay rypsrhvaia gfalqtvalv
      361 alalaghphg alavgvvllm lgtwlfaegf gpgaqmmiyp tlsypatirg tgvgfgrslc
      421 gigqalalfv lpilqarlgt dmfwvvaisa vtpivflliv ryeptardid desaa
//
LOCUS       WP_175930760             325 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: type II secretion system F family protein
            [unclassified Burkholderia].
ACCESSION   WP_175930760
VERSION     WP_175930760.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..325
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=36480
     Region          112..322
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mnaifygfvi ltfvavvlsi egiyqwwnar hgaaarries riramsaggn vqqerlsilk
       61 krmldeskpf drlllrvprv haldlviqqs gldwtlpkli tlgatfaalt wcaasfaslp
      121 qlaavplalf agwmpmlyvl rcrarrmrkl erqlpdicdm iaralrsghs ftstlgmvgd
      181 efsepmggef rvtfdevnyg vslhdalmnl atrvpvqdlr yfviavliqr etggnlaell
      241 esiaglirer fklfdkvrvl saegrmsawi lgllpfgtaa vmallnrefl svlwedpagi
      301 rmvgtmlvsm lfgllwirri vrirv
//
LOCUS       WP_175930753             384 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Burkholderia].
ACCESSION   WP_175930753
VERSION     WP_175930753.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..384
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41507
     Region          1..370
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mtaismkdvs krygdhapvl rdvnleiash efcvflgpsg cgkstllrmi agledvtege
       61 lriggarmnd tppaergvam vfqsyalfph mtvfdnigfg lriagtpkde irrrvteaar
      121 vlqlealldr kpkalsggqr qrvaigraiv reprvflfde plsnldatlr gqtrveiarl
      181 harftqsssv yvthdqieam tladrivllh agddvarfgs iaqagaplel yhrpanrfva
      241 gfigsprmnf lpavvdagda hgcrltlegt getltlrdra lprhvgrgar vtlgirpehl
      301 tigvpgdtdl palvrdvalv eqlgeaayvh ldqpggvpll aklpgqaalr rgerhafhvp
      361 psrchlfdea giavpalhae aafa
//
LOCUS       WP_175930790             306 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175930790
VERSION     WP_175930790.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34032
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..294
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,223..228,
                     234..235,237..238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176166"
ORIGIN      
        1 mdllkamavf vrivetgslt aaaqasdlsp tmvgnylqal enrlgtvlvh rttrkqkvsa
       61 fghayyercv eilglvddte qlaldhleqp rgrlrvtapv vftneclipa ladyyqrypg
      121 irldivatds ladlfdegfe aairigqlan pdvvarplap yrlvlcaspa yvrehgaptt
      181 phalrehhcl tyaypprsew haaqsrwmlk gpdgpmslsv dgrlridsad alrraalqgl
      241 giamlpslli hddirderli eimpdfaape rsmnllylre rqqspklrsf tefvvdrfga
      301 etacra
//
LOCUS       WP_175930794             316 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ketopantoate reductase family protein [unclassified
            Burkholderia].
ACCESSION   WP_175930794
VERSION     WP_175930794.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..316
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32537
     Region          1..307
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkiailgaga lgcaigatlt egghetwlig rspahvdamr rdglrvddas gtrqvrvhat
       61 anaaevgaad lvvvlvksfh tdaairgals lmgpdtvvls lqnglghedi lidavgrerv
      121 lagktyvggv rrgpghieag vigkntyige ldgritpriq aiaaafdaag lattisdniv
      181 gtmwdkllvn vatgaltglt gltygqlyde pllkatslaa vaeaiaaara agvklsmtdp
      241 eqawtlaaeg lpaafktsml qslekgsite idfingsvvr agqrygvptp vnttlvacik
      301 gleramadrq reeaaa
//
LOCUS       WP_175930806             310 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175930806
VERSION     WP_175930806.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33851
     Region          14..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,232,249,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,195,
                     226..230,237..238,241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mrssseklsg sisvfaavvd agtfsaaadv igmtppgvsr aiarlerkln irlfnrttrs
       61 vslteegrrf yeqvmphlag leeaaaaaag gasavrgklr inldpvvyra ilgprldafm
      121 dahpeleiel iardslgdlv mdgfdlavrf geprasslia rklldtgvvt vaapsyiarr
      181 grparpedle srnhrclefr npetgkpfaw efhrrrkriv vdtrgrltvn dpgallnacl
      241 agsgiaqmll lgaepliadg rlidlfpewa deryplyayy psrhhvpakt rafldflvel
      301 tgihggvgtr
//
LOCUS       WP_175930872             120 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: c-type cytochrome [unclassified Burkholderia].
ACCESSION   WP_175930872
VERSION     WP_175930872.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 120)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 120)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..120
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12386
     Region          31..118
                     /region_name="CytC552"
                     /note="Cytochrome c551/c552 [Energy production and
                     conversion]; COG4654"
                     /db_xref="CDD:443692"
ORIGIN      
        1 mtgrqmtqmk rwmvqgaaam alvagtlgta hadvgdglkv arsnacmgch aadrklvgps
       61 fkdiaaryka dpqavaklsk kvkdggsgvw gaipmpahpr msdgdvrsvv ewvlagapsk
//
LOCUS       WP_175930890             165 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [unclassified Burkholderia].
ACCESSION   WP_175930890
VERSION     WP_175930890.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..165
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17958
     Region          5..164
                     /region_name="COG3865"
                     /note="Glyoxalase superfamily enzyme, possible
                     3-demethylubiquinone-9 3-methyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:443074"
ORIGIN      
        1 mtpriqritp flwfdrdaea aaafyvsvfd harivhvary gkagahasgn aegavmtvaf
       61 eldgqafval nggpvfqmtp avsfvvncrd qgeidhywar lseggderaq qcgwlrdrfg
      121 vswqvvpvqm aelmtgdpar aervmaqvmt mkkldlgalq raaag
//
LOCUS       WP_175930933             294 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175930933
VERSION     WP_175930933.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..294
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32540
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="PBP2_CrgA_like_7"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08476"
                     /db_xref="CDD:176165"
     Site            order(101,105,144,158,160,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176165"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176165"
ORIGIN      
        1 menltgivaf vrtaealsfv aagralgisa savgktiakl eqslgvrlfn rttrrvtltd
       61 egrhfyercq riledfrdae atvtasaqrp rgklrvslpv igyrfllpvl pefrqrypdi
      121 eldldfndrm vdvveggfda virsgplsds slmsrrlgpf afvlcatpay laqagmprtp
      181 releahdcvr ycfpttgklq dwalaaddgt plklrtamtc nnmealrgav laglgigymp
      241 dflardaleq galvtvlddy riapgqfsiv wpssrqlspk lrvfvdflce rlfr
//
LOCUS       WP_175930966             294 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [unclassified Burkholderia].
ACCESSION   WP_175930966
VERSION     WP_175930966.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 294)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..294
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=31329
     Region          11..293
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 meifgiplpa mlsqlllglv ngsfyailsl glavifglln vinfahgalf mlgamlawmg
       61 lsyfglpywa mlvlaplivg afgiaiersm lrwlykldhl ygllltfglt lvvegvfrsi
      121 ygssgqpydv psqlagatnl gfmflpnyra wvvvaslavc latwfviekt rlgaylragt
      181 enpklveafg vnvpmmitlt ygfgvalaaf agvlaapviq vsplmgqpmi itvfavvvig
      241 gmgsilgsiv tglllgvieg ftrvfypeas atvvfvimai vllfrpaglf gkek
//
LOCUS       WP_175930977             404 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cation:proton antiporter [unclassified Burkholderia].
ACCESSION   WP_175930977
VERSION     WP_175930977.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..404
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43670
     Region          13..390
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mksafsflpn wpltpdavfw aglalfaagl cgelcyrawr lpritgyavi gliagsfgfg
       61 vidtstdets rllmdvalgl llfelgsrld lrwirrnpwl vasslaeatl tfvlvlfvml
      121 algvsgmval vlsaiaiats psmviqlkte lraegqvsqr litltalnsv yaivltklvt
      181 swlhqeaygn vfatilqply llagsfivay lvarscnylf rhmtatmrde hsfvalfglv
      241 mlaiavaqal klstlltlll agiivknlea rpqlwpehfg tagwlltvvl fvltltsftw
      301 gdialgglla ivlivtrlva klagvvafak psglgmkqgv algialtpms alsyllvddt
      361 yqlypnfdph lraivmctiv ilqlvspfvv yrclsavger sdgn
//
LOCUS       WP_175931010             343 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: fimbrial protein [unclassified Burkholderia].
ACCESSION   WP_175931010
VERSION     WP_175931010.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..343
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=35779
     Region          199..343
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mkrntmkmkr grsgcgptll rtaaaalllg sagigaaqaa alakceaits aklatlpenl
       61 kiawdapvnt vlwkqsgiqi sarcwqvlpm sgemeamfyr yrddpklian giamyityng
      121 nrghgdaaip tgtmiprtgd vkvtatvdve lvkigatpst ptdlpmrtvl agmisapneq
      181 sdsarymlyg fenvsfqktt cgtttpslqv elgthvlrka ggigsgigst spskdfaigi
      241 qcdsgvagdf vvnmmlegna ldaangvlal spersatgvg iqllkgdgqp vhlgtpwkia
      301 dspsslgrss nfsvplsary yqtdatakpg tangtatfti iyk
//
LOCUS       WP_175931013             265 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Burkholderia].
ACCESSION   WP_175931013
VERSION     WP_175931013.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..265
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29528
     Region          6..263
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mnqavspstp aiefrnvscr fispegkatv alrdfsmsva rgefiaivgp tgcgksttln
       61 litgllkpas gevrvmgrpv dgidprigfv fqadavfpwr nvidnvaagp lfrgrskdva
      121 yaqaeewirk vgldkftkhy phqlsggmrk rvalaqtfin qpeillmdep fsaldmqtrt
      181 lmqdellqlw sankgsvvfv thdleeaial adrvfvltar patlkrvyei dlprprvmse
      241 vrydarfiei skdiwhdlre evqig
//
LOCUS       WP_175931016             376 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: porin [unclassified Burkholderia].
ACCESSION   WP_175931016
VERSION     WP_175931016.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..376
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=40682
     Region          22..376
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkrknlalsl aaaaglcagh aqaqssvqly glmdlsfpty rthadangkh migmgndgep
       61 wfsgsrwglk gaedigggtk iifrlesefv vangqmedeg qifdrdawvg vederfgklt
      121 agfqntiard asaiygdayg saklsteegg wtnsnnfkqm ifyaagptgt rynngvawkk
      181 lfsngifasa gyqfsnstsf atgsayqaal gynggpfavs gfynhvnhng frnqtfsvgg
      241 nytfdivrln agyfryngdq gplgqrhdds wtvsmkiapk galdyelgyq qmriknaann
      301 adgftpnanl gafsltngva ngfketiygs vfyhlskrte vylagdymkl hggytvsstf
      361 gaknqlelts girtrf
//
LOCUS       WP_175931045             201 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175931045
VERSION     WP_175931045.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..201
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21904
     Region          14..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mntpldssge pgvrdrllda aealiysggi hatgvdaivk rsgaarksfy shfeskealv
       61 vaalerrdar wmrwfvdgtl argksprahl lgmfdvlrdw fgqpdfhgca flnasgeipd
      121 addpvrvvar mhkarllafv rerfdahade tgierrglar iarqwlvlid gaigvalvsg
      181 danaardara taellldtvs r
//
LOCUS       WP_175931055             184 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NADPH-dependent FMN reductase [unclassified
            Burkholderia].
ACCESSION   WP_175931055
VERSION     WP_175931055.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..184
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20167
     Region          4..165
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 msyriavivg slrrastnra lahavislap adfsfefvei gelplysqdy dadfpevakr
       61 fkqsieaada llfvtpeynr sipgvlknal dwgsrpwgsn swsgkpgavl gtspgavgta
      121 laqqhlrnvl ayldvktlgq pemfikhdpa riddqgqivs edtrkflqgf vdryaswvrl
      181 lksa
//
LOCUS       WP_175931051             353 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ParB/RepB/Spo0J family partition protein
            [unclassified Burkholderia].
ACCESSION   WP_175931051
VERSION     WP_175931051.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..353
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=39442
     Region          82..314
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mkpsqfakgf qarpdittse krtaldrlna idgivksetp tpvstksakk diapppapef
       61 tidpsvdesp qyrawrlenr yapgqvielp lkaikhspfn prhfylkssi aelavnlakq
      121 gqqqaihvip dydnpgtyfv sdggrrvral keankesvka ividvpigiq syklgydlnv
      181 qrdsqtvfdn avvwrrflde khfqsqkels ehlgldestv avalsigklp eaimqemvar
      241 pdrfgsnmay qvgryhnarg teatlrlink ivsddlstrq vsdivkgrva aqetpkaagr
      301 qryaqrleik lggksvgdlk sygedrielr lrglpkdkrd aileqlerml lse
//
LOCUS       WP_175931058             312 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [unclassified
            Burkholderia].
ACCESSION   WP_175931058
VERSION     WP_175931058.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 312)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..312
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34584
     Region          44..311
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mtaaapslsd lviervgfgl fvldrsmtvl mwnrfmqdhs gipaadvigr nlfdrfpdlp
       61 rawlsrkles vfqlgsfafs sweqrpylfr fehdrpitgg vdymqqdctf mpltrgrdve
      121 avcvtisdvt hvsvmqrere eavaklreha nrdgltgian rrffearlgd efarwqrygg
      181 dlsvllfdld hfktindrfg haagdavlre tarrvasivr aqdtfgrfgg eefalllpct
      241 nleeamrvad kvrdaiggmp vdaegvsvpv tasvgaacak agaptcdvlv neadaalyra
      301 krlgrdrsva ya
//
LOCUS       WP_175931080             213 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175931080
VERSION     WP_175931080.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..213
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23966
     Region          7..211
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 meakldstad avaaslrdmi vngelaager lverdlaerf gisripmrea iqrleregll
       61 difrnrgaiv rmlsasdvqe iydlrvlleg daiyrsvkrl ddetlarael vhrllgnatv
      121 prrqgelnre fhallyshcg narqlksiae lrsqveryer lqatlladtp sfqvehddil
      181 qacrernarg aramtvahle sarrivlrlv egg
//
LOCUS       WP_175931115             282 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: phytanoyl-CoA dioxygenase family protein
            [unclassified Burkholderia].
ACCESSION   WP_175931115
VERSION     WP_175931115.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..282
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31551
     Region          11..263
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mtsirdrvaq avtpeliaaf redgavcikg ifspdevaal ragidanlaq pserakvasr
       61 pddpgwffed fcnwrhnday rdfivrspap svaaalmgtq tvrlhhdhll vkepgtrqrt
      121 pwhqdqpyyd iegddnvsmw ipvdpvples tlefvagshr gpwlmprtfm dkeakwfpeg
      181 sladlpdiea draafpirhw alepgdmvcf rmltlhasgg trnrrrafsi rfvgddirha
      241 prrwktspdf pglaaqladg apldhplfpv vwsrdagqvd ai
//
LOCUS       WP_175931125             251 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SDR family oxidoreductase [unclassified
            Burkholderia].
ACCESSION   WP_175931125
VERSION     WP_175931125.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 251)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..251
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26106
     Region          2..202
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mkivviggtg ligskvvrnl iarghdavaa apstgvdtit gaglddalag aqvvvdlans
       61 psfeeaavka ffeasgrnlf aaehaagvrh hvalsvvgtd rlqqsayfrg kiiqenlird
      121 agvpytivrs tqffefvgai aqagaqgdtv rlstahfqpi asddvaaavt dfaldaprng
      181 iaeiggperv riadlvesfl sathdartvt rdasadyfga vlqddtlvpa pgarlgattf
      241 dawfrqhala r
//
LOCUS       WP_175931128             159 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: carboxymuconolactone decarboxylase family protein
            [unclassified Burkholderia].
ACCESSION   WP_175931128
VERSION     WP_175931128.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..159
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17964
     Region          11..144
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtqrlnyiqq spelfrkfle lsnllrnsai eesirdlvsv rasqingcaf cvdmhvkear
       61 ihgerelrlh hlatwrestl fspreraala wtevlttlpa hgvpddlydr vrgqfseqel
      121 sdltfevvai ngwnranvaf rtvpgssdka fgldkanla
//
LOCUS       WP_175931164             273 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175931164
VERSION     WP_175931164.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..273
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29961
     Region          21..266
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mqtnndplpg cdaresmaat dryrapaldk gldilellse qkegltrtei tkelgrnase
       61 iyrmlerlva rryvmrstgg drytlslklf alahrhppmn rliaealppm qrfadaaeqs
      121 chlsvydrgn llviaqvdgp gpwgvsvrlg srvgladtas grmmlafqgp eqrahmlaeh
      181 rkvkgeapln eqelanacqs irqsgylrqd srqaygvtdl tvpilgpagh aiavltcpym
      241 rridahmaps vdvvvgalrd tathlsmcrt etc
//
LOCUS       WP_175931146             506 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: peptide MFS transporter [unclassified Burkholderia].
ACCESSION   WP_175931146
VERSION     WP_175931146.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..506
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55165
     Region          7..462
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mmhapvsqtr sfttvfliem werfgyygma allvlfmvdr lgftdshanl twgaftalvy
       61 aapsiggwig dkvlgarrtm iigasvlcag ylmlavpndh laymyaslgv ivvgnglfka
      121 naanlvrriy egddaridsa ftiyymavni gstvsmlatp wikdhwgwht afavccggml
      181 lailnfalmh rtlahvgsqp ddepirwkrl gavaaggval alitlyvlqh kqlavasvwt
      241 aafailaifa ymiakserse ragliaalvl igqvilffif yvqmstsltl falrnvdprf
      301 mlfgttlftw saaqfqalnp iwimllspvl vwvynavakg grdlpvaaky algfgavaag
      361 ylvftisgry avdgrvsswf mvwgyglysl gellvsglgl amiaryvpar msgfmmgayf
      421 vatgvsqylg svvanfaqmp shelpatesl plylslfekl gwlaaigmll allllplmnr
      481 lsrqhqrcae erreealqaq gvaaaq
//
LOCUS       WP_175931193             212 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: 2-hydroxychromene-2-carboxylate isomerase
            [unclassified Burkholderia].
ACCESSION   WP_175931193
VERSION     WP_175931193.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Thompson,L.C., Ladner,J.E., Codreanu,S.G., Harp,J., Gilliland,G.L.
            and Armstrong,R.N.
  TITLE     2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class
            glutathione transferase from Pseudomonas putida
  JOURNAL   Biochemistry 46 (23), 6710-6722 (2007)
   PUBMED   17508726
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122490
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..212
                     /product="2-hydroxychromene-2-carboxylate isomerase"
                     /EC_number="5.99.1.4"
                     /GO_function="GO:0018845 - 2-hydroxychromene-2-carboxylate
                     isomerase activity [Evidence IEA]"
                     /GO_function="GO:0043295 - glutathione binding [Evidence
                     IEA]"
                     /GO_process="GO:1901170 - naphthalene catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23364
     Region          8..188
                     /region_name="DsbA_HCCA_Iso"
                     /note="DsbA family, 2-hydroxychromene-2-carboxylate (HCCA)
                     isomerase subfamily; HCCA isomerase is a glutathione (GSH)
                     dependent enzyme involved in the naphthalene catabolic
                     pathway. It converts HCCA, a hemiketal formed
                     spontaneously after ring cleavage of 1; cd03022"
                     /db_xref="CDD:239320"
     Site            15
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239320"
ORIGIN      
        1 mnaartatwy fdfvspfayl qqerfdrlpp aaafeprpiv lgallthwgq kapaeiaakr
       61 vftyrhaqyr adklgiafrm ppahpfnpik plrlaiamgg sldaiqrifr hiwrdghdvs
      121 tpegfaalce avgfpegvta vdaqpvkdal rantdraiad gvfgvptfvl dgdlfwgeda
      181 tdmfvdcats rawldspevr risalpegir rg
//
LOCUS       WP_175931208             289 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: thiol-disulfide oxidoreductase DCC family protein
            [unclassified Burkholderia].
ACCESSION   WP_175931208
VERSION     WP_175931208.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..289
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=32002
     Region          1..121
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mnaselvlyf dgrcplcvae irrlgerdar hrlafvdiae pgfdptplgv dlpalnrelh
       61 arlpdgrmlt gidgiaaaha ligrrwfarl lrspamravs aplyrrlarn ryavsrwlgy
      121 rteagcegga csigrsaena aanrpprdsa rrivvrcmya aaiahllvgv vmpwiagasw
      181 ldayhrsies hfwtgaapea araqqvwwvs llgatvqcaa vwmlalvhlg nrlrnrevwg
      241 wllaglsiwa pqdmllswqa qvwghvaidv valvamvppl vwlwrrdta
//
LOCUS       WP_175931237             451 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: uracil-xanthine permease family protein [unclassified
            Burkholderia].
ACCESSION   WP_175931237
VERSION     WP_175931237.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..451
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45842
     Region          9..423
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mshdpisppv darlpawqla lfglqhvlsm aaspitavfl iakvlalpad ltvqligatf
       61 facgvgtllq slgagpigar mpfvmvpgga ptmlfagiaa qsglptaaga allasafywv
      121 llpvftrclr lfprivvgam lllvsinlir iyativvgqp gsadfaqpra lglalativa
      181 tvvvagafrg tagrlavlig lmagaalgwa lgampaladv wrgplfthpv wlpfgmprfd
      241 llaalpllif taismaeata qtvavgetcg kaislprdvp ktirgdalas lagalfgtpl
      301 ivtsaenigv vqttgvrsry vtaaagaili vialfaplar layaipaavv ggtalvvfam
      361 igvmgirlla svdlharanq ytlaaalvig lapilvpnly rhfgapvqiv lgngmaagtl
      421 aaiatqlafa alprlrghah agttaapsrd a
//
LOCUS       WP_175931239             311 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [unclassified
            Burkholderia].
ACCESSION   WP_175931239
VERSION     WP_175931239.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..311
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=33697
     Region          27..294
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mdtnrwihdp vgafrawqet aatgagrrpf aprsvvqhva mferflrhls aqrvslatfg
       61 pdhvaaflak ldrtcapgts trvryaklid rlgrhlvdag vrtvhpggrs trdfawpdse
      121 pepcylppda daalqrhvqp raddtpadcr nraivallla sgitsaeira atgdapdlda
      181 rppvlsvprd rarparrial atfavaplaa wrarstdapp sallfpaprg gamndmflll
      241 vvrdalnaig fhaadmsprv lrntyarrql laghahadvt amlglasmrt vtrirqtlpp
      301 daaadraahe r
//
LOCUS       WP_175931257             374 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MBL fold metallo-hydrolase [unclassified
            Burkholderia].
ACCESSION   WP_175931257
VERSION     WP_175931257.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..374
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41892
     Region          87..327
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 masplvllhr ilgfaaarrg ralsgrspqh ngerfanvap rpaeglgktl riawnmlvnk
       61 prhtvpagal pvdslnrael daapdrslyr lghstlllkl rgefwltdpv faeraspfrr
      121 vgpkrfhapp ialedlpplr gvilshdhyd hldrdtvlal aattgvfvtt lgvgdrliew
      181 gidanqvrql dwwqsinvag ltltatpaqh fsgrslfdgn stlwaswviv dddlrlffsg
      241 dtgyfdgfre igerlgpfdv tlietgayda qwpyvhmqpe etvqahidlr grwlipihng
      301 tfdlamhrwq epfervtala lvrgielstp kmgerldlda phrgerwwrt vderaaapta
      361 ksrrwqlcas qatk
//
LOCUS       WP_175931259             163 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: flavodoxin family protein [unclassified
            Burkholderia].
ACCESSION   WP_175931259
VERSION     WP_175931259.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..163
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=17133
     Region          4..149
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mktllivyht mtggtrqmae aaagaareqp gvdvrlqrad atsaddvlaa daylfatpen
       61 laamsglmkd ffdrcyyaal drvngrpyaa micagsdgqn alrqidriat gwrlknvapg
      121 livcthaqtp erilatktid sdalarcael gaglaaglal gif
//
LOCUS       WP_175931264             703 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [unclassified Burkholderia].
ACCESSION   WP_175931264
VERSION     WP_175931264.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..703
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76610
     Region          9..687
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mtypslrdwl fsgktfaasm lalylglyfq lprpywamas vyivsnpfvg atrskalyra
       61 lgtalgaaaa iffvppfvet pllfsiivat wcgtllylai sdrtarsyvf mlagytmplv
      121 alptvtdpst vfdvaiarte eivlgivcas vvgstvfpnr laptliertd awfkdaafyg
      181 retlsghlag kalsacrqrl aatitglefl lsqlgydhah prvlaraqal agrmqlflpl
      241 mssladplia lmrdlrvrpp aldalladaa kwfdaplpav ksgsdgdmah dpvaddlrar
      301 iaalqppdga laswdgalms nalwrlrqvi diwqdcrslr alianesgvw qpryrhwrlg
      361 gterffdrgm mlfstltvvf aivfacwlwi ssgwhdgaaa vtlvavscsf faaldepapl
      421 vfkfflstaa svvfaglylf vvlphvhdfa mlvlmfagpf iligtllprp qfnmvtmlva
      481 vntatfisiq sayeadffvf lnsnlagvag llfayvwtra trpfgaelav rrllrsgwed
      541 varsastqpl ddqrnhasrm ldrvtqllpr lgasddhrhp siesfrdlri alnaldlrrs
      601 rrrlsgdvpd aidrvlagvt dhytrcaaan arqpvppall atiddalqrv agrtapadga
      661 aapavpathr rlrdtlhalv glrlslypaa aaqapqapdg ara
//
LOCUS       WP_175931298             305 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175931298
VERSION     WP_175931298.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32767
     Region          1..>157
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          91..286
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,221,238,265)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     215..219,226..227,230)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 melndlrifv atvdagsfta aadqlmlskq fvsrrtmale aslgvrllhr ntrnlavtes
       61 gqefyaraqr ilaevadaeq amsvrstelh gslkisapls fgithvspli aeflsahpav
      121 rlnldltdrr vdligegfdl vlrigsleds tliarplgaw rmiacaspay lkrqgtpqtp
      181 adlaghtcll ygrerrvgwe frvdgaartf dvqgplvann gevvrdaaia glgiallphf
      241 ivgaaldrga lvpvldayvp ppitlnavfp qhregfvtlr tfigflaerl geptptgasg
      301 agrvr
//
LOCUS       WP_175931302             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Burkholderia].
ACCESSION   WP_175931302
VERSION     WP_175931302.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46162
     Region          22..420
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,150,
                     153..154,157,245,248..249,252..254,257,285,289,347..348,
                     352,356,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mndhppvpha pprirrgqri alallmasgi vnyldrgtla vassairgdl glslsqmgll
       61 lsafswsyal cqfpvgglvd rigprrllgi glivwsfaqa aggivstfgw fivarivlgi
      121 geapqfpsaa rvvsnwfplr argtptgifn aasplgtala plllsvlvaa fhwrwafivt
      181 galglvvavv wfalyrdpvr aqlsaaeray ldadaqsvaa apkltfaewr slfshgttwg
      241 mligffgsvy lnwvyltwlp gyltmerhms lirtgfaasv pflcgfvgsl vagwlsdlvt
      301 rrsrspvvsr rnavvaamlg mvaftipaal vqsntvalac isvviflana asacswalat
      361 aaappsrias lgaiqnfggf iggalapilt giiaqqwsfv palltaaaia ftgamaylll
      421 vrkpipeqaa naapgplpa
//
LOCUS       WP_175931309             249 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Burkholderia].
ACCESSION   WP_175931309
VERSION     WP_175931309.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..249
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=26862
     Region          3..231
                     /region_name="ArtM"
                     /note="ABC-type arginine/histidine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4160"
                     /db_xref="CDD:443325"
ORIGIN      
        1 msidfaflvd tlrqllaavp ttlglffasl vlggllslvi vtmrvsphwl pnrfarayil
       61 vfrgsplliq mflvyyglgq fgviresfmw pllrepyvca vlslalctag ytaeivrggl
      121 mavpvgqiea gysiglsgfa llrrvigpia lrqclpayst eavllvksta laslvtvwev
      181 tgvaqqiiqq tyrttevfvc aaviylglnf ivvrllgale wrlsahlrap kpssgasaaa
      241 trnaqrvas
//
LOCUS       WP_175931349             227 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175931349
VERSION     WP_175931349.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..227
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23768
     Region          43..172
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkkrlepapr dvsapvetag tpgvrapegs sapaaavagv rrkkapdqvr aqllaaasei
       61 athhgvaalt ldavaeragv tkgalqyhfa nkqglldalf gqaterfgaq maariaadsg
      121 gdgaaarayl havldtahpa asievlrvlv asmiteqdtr arwsvpmrew trpdpvplgq
      181 aatlmicrla adglwisell dsvevsaelr aeivrqldam tkgvfpk
//
LOCUS       WP_175931368             307 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175931368
VERSION     WP_175931368.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33475
     Region          23..80
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          111..303
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(124..125,127..128,131,135,137..143,233..238,
                     244..245,247..248)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176171"
ORIGIN      
        1 misdrngesd sqsiradlps lmalrcfdaa arhenfsraa delclthgav sravrlledd
       61 lgvalferrs rrvfltdagr tlaqavhdgl glmrhavhal rseaararrs vlsceptllm
      121 rwliprwpdf qarhagidih laaaggpfsf dsgidmairr ndfawpaayh aehlfaervg
      181 pvcrpdkvga wfasrrggrv lkpdaallht rtrpdawrtw avaanqpaas grgqrfdhfy
      241 fslqaavagl gvaigpwhlv rddiesgvlv apmgfvedgs dyylltpapv adgsaqaall
      301 gwlrgtv
//
LOCUS       WP_175931400             236 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Burkholderia].
ACCESSION   WP_175931400
VERSION     WP_175931400.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..236
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25452
     Region          8..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtaaspgavl elrdvtrvye gagrvvavrg atisigrrdv ialvgpsgsg kstllnlagf
       61 ldvpssgerw legrriddtp dtlerirrer igfvfqqfnl ipvmsalenv elgcfawgtp
      121 rtrreraram ldavglaare rhrpgelsgg eqqrvalara lakepaivia deptasldst
      181 naravaelil dtnrtlgtaf liashddrlc ahlprriemr dgvpgvnrel vdvcva
//
LOCUS       WP_175931437             209 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [unclassified Burkholderia].
ACCESSION   WP_175931437
VERSION     WP_175931437.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..209
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22066
     Region          1..207
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mpiqtwllfa aaylattlsp gpnvllvirn tvrygahgta atiagnlvaq gavvllvalg
       61 vgavlaampp lfvamkvvga ayliflgvrq lrgdrkaaap sgaaelavpd rrklfrealf
      121 vsgsnpktmi flsafmpqfi vhdrplalqf vvmyatiact vvvvhciysa gvrrlhrgfg
      181 msravralkr asgllfvglg iklltarqa
//
LOCUS       WP_175931438             437 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: leucine-rich repeat-containing protein kinase family
            protein [unclassified Burkholderia].
ACCESSION   WP_175931438
VERSION     WP_175931438.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Shen,K., Hines,A.C., Schwarzer,D., Pickin,K.A. and Cole,P.A.
  TITLE     Protein kinase structure and function analysis with chemical tools
  JOURNAL   Biochim Biophys Acta 1754 (1-2), 65-78 (2005)
   PUBMED   16213197
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   5  (residues 1 to 437)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   6  (residues 1 to 437)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
REFERENCE   7  (residues 1 to 437)
  AUTHORS   Hanks,S.K. and Hunter,T.
  TITLE     Protein kinases 6. The eukaryotic protein kinase superfamily:
            kinase (catalytic) domain structure and classification
  JOURNAL   FASEB J 9 (8), 576-596 (1995)
   PUBMED   7768349
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..437
                     /product="leucine-rich repeat-containing protein kinase
                     family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=46304
     Region          <2..>193
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          39..61
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          62..81
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          82..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..175
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          176..196
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          214..432
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(214..217,220,222,238,240,269,287..290,345,349..350,
                     352,362..363)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
ORIGIN      
        1 mthtleqlqa gqlsgarqlk lacgltefpr eifdladtle vldltgnals alpddlprlh
       61 rlrilfasgn rftafpaglg acerlemigf kanrirtvpr galpralrwl iltdnaidal
      121 padigdcarl qklmlagnrl ralpaemaac ralelvrlsa nrlealpdwl prlprlawla
      181 vagnplgagp eaaasggadv aeidwaalsc eeklgegasg viyraqwqae sqpprtvavk
      241 lfkgavtsdg lpdcemaacl hagrhpnlip vigkvrghpg gthglvmelv dpaltnlagp
      301 psfasctrdv yaadatfdpa halriahgia saaghlharg imhgdlyahn ilhdgaggal
      361 lgdfgaaspy dlnerthgar ferlevrafg yllgellarc ephtgaldal aaacvnedvd
      421 arpsfdeitt alaarlr
//
LOCUS       WP_175931524             314 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Burkholderia].
ACCESSION   WP_175931524
VERSION     WP_175931524.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..314
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34222
     Region          5..225
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mqpilsvsdl sktyasgfqa lkhvtldirp geifallgpn gagkttligs icgivtpteg
       61 rvtvgghdir dqyraaremi glvpqelttd afetvwatvs fsrglfgkap dpayiektlk
      121 alslwdkrdn klmtlsggmk rrvmiakals heprilflde ptagvdvelr rdmwklvdsl
      181 resgvtillt thyieeaeem adrigiilgg elvlveekhe lmrklgkkql tvqleqplad
      241 vppalapfgl eraedgaalv ytydsqrdda siaklinalg sagigfrdlh ttqssledif
      301 vslidnrrng aqga
//
LOCUS       WP_175931539             776 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor [unclassified Burkholderia].
ACCESSION   WP_175931539
VERSION     WP_175931539.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..776
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=82185
     Region          60..734
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mirrpkaagr dgamrrgrra rcvgaavgtl alfglapgsv raqqqadgaa idppessvml
       61 pavvvvgttp llgigtplsn vpanvqtvra aeldaqhrat ladffaanlq svtisdaqgn
      121 pyqtdvnyrg ftaspllgtp qglsvfvdgv rvnepfgdvv nwdilptqai drvqlipgsn
      181 pvygrntlgg alaittkngr snpggeaeis ggawgrkaag ieqggtigph ldyyatahva
      241 ndggwadhna srvrqafgkl rytdadttls laaggadntl sgtqtiprsf ldnrkqayty
      301 pdrnrnsagy ltlsgdrffg ehvelsgnay yrhlrntnts snnntdygsv dedgtvdtvq
      361 gsnarstivt dsyggslqlt llgtlggman qlvagvsadv anstyvassq dasftdaraa
      421 igigdfvqqt raktrnanvg vylsdalslt phwtltlsgr ydwskaqigd esggqplldg
      481 nhafsrfnpa vglnwnpvag ftayatyneg mrsptaiela cadpaapcsl pndfiadpal
      541 epvisktfea gvrgrigaat twsaaayrtt ltddiqfiss pastqgyfrn vgdtrrqgie
      601 lagrarlgpl gvglsyshvd atyrsswteh spansaadah gnvtvkpgdr mpgipahtvk
      661 lrldyaatpa wdlganvtwr sgvyargden ngdvngrias yvlvdldmry ritkrfevfa
      721 svtnlfdkry asfgalgrnf fngpnhtfdg ghpvdeqfvg pgaprgawvg aryawd
//
LOCUS       WP_175931562             441 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Burkholderia].
ACCESSION   WP_175931562
VERSION     WP_175931562.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48339
     Region          30..433
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(43..44,47..48,51,83,133..134,136..138,141,161,
                     164..165,168,265,268..269,272..274,277,305,309,360..361,
                     365,369,385,388..389,392..393,396)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtaldaaasr spaaaahsge ldrtykkvfw rivpflmlcy vvayldrvnv gfaklqmsqd
       61 lafsetvfgl gagifflgyf lfelpsnllm hrigariwia rimitwglls alfafvktpt
      121 qfyvlrfllg laeagfypgv ilyltywfps hrrakiiavf msaipvsgif gnplsgwime
      181 rfhggsgfhg wqwmfmieav pavlvgiati lyldnsirga kwlderekql ledeiaaqpq
      241 eqqqhghslk avfadprmww msliyfafvt gqygltfwmp tlvkstgitd tlqigllsai
      301 pfvvaivvmn lfghsadkrr errwhlivpa lmgaigfava asyshntavs ivflslaagg
      361 vltcaplfws lptaflagsa aaagiaiins vgnlagfasp yvigylkdvt hstssgmyvl
      421 agmlvigaia vwltpaklvn r
//
LOCUS       WP_175931573             332 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175931573
VERSION     WP_175931573.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..332
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36585
     Region          21..328
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mtsavavapa acvspvssla hfgfltlpnf smiafssave vlrmanyvgr adhyqwsiys
       61 ldgapahasn giavrptqal dydnlpdvmi vcggirirdv vderaretla alaerglplg
      121 gictgayalm ssglldgyrc tvhwenlsal hsefpqvgfa delfvvdrdr ltctggtapl
      181 dlmlnlvgmr fgqqlaaqvs eqfilerirs stdtqpipvd arvgfsrael ievvrlmean
      241 ieeplsleel arlvrlsqrh lqrmfkvyln vspthyyltl rlkrardllr ttdasiarvt
      301 tvcgfhspch fskayraqfg hapsyerrlp gr
//
LOCUS       WP_175931579             314 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175931579
VERSION     WP_175931579.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..314
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34908
     Region          7..314
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpedfhflll pgfsalgfms aveplrvanr frtelyrwhv isadgapvaa sngipvaaea
       61 acadvprvdt vfvvagfdpl vcytralgdw lrrqhrhgat lggidtgsfv laeaglfdas
      121 qpltlhweal aafrerypgl natqelfeid drritcaggt asidmmldli grrhgadlaa
      181 aiseqfvvsr irqrsdsqrl eiaarygvhn rkliqvigtm qrhmdnplgs dalarevsit
      241 rrqlerlfsa tlndtptrfy lnlrldrare llqqtdmsit svcvacgfes pshfsrtyra
      301 rfgmsprsdr ratr
//
LOCUS       WP_175931600             203 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ankyrin repeat domain-containing protein
            [unclassified Burkholderia].
ACCESSION   WP_175931600
VERSION     WP_175931600.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..203
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=21556
     Region          <49..202
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(77,79,83..84,87..89,91..92,96,99,108,110,112,
                     116..117,120..122,124..125,129,132,141,143,145,149..150,
                     153..155,157..158,162,165,174)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          77..108
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          110..141
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          143..174
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          176..201
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mrserfthai raaaaalala alagcahlpd rptygkadpa alrrydgdwf daarvgrvdi
       61 lralhdagyp vdatdshgyt avilasydgq paaldyllsv gadacagdrh gntalmgalf
      121 rnepdiarrl ldtrcpidqt ngagetalgf atlfnrfeli pllvahganp nhvdrrglsl
      181 lqlalthdnt yaadalreag akr
//
LOCUS       WP_175931603             528 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MDR family MFS transporter [unclassified
            Burkholderia].
ACCESSION   WP_175931603
VERSION     WP_175931603.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..528
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56747
     Region          37..516
                     /region_name="MFS_LmrB_MDR_like"
                     /note="Bacillus subtilis lincomycin resistance protein
                     (LmrB) and similar multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17503"
                     /db_xref="CDD:341046"
     Site            order(39..40,43,75,125..126,128..130,133,153,156..157,160,
                     287,290..291,294..296,299,327,331,383..384,388,392,408,
                     411..412,415..416,419)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341046"
ORIGIN      
        1 madtpastpl pphegrasvt dwiavaagal galmatldis itnsalpqiq geigatgteg
       61 twistgylms eivmiplaaw ltrvfglrnf lltnsalfia fsmmcgwshs lpmmiagrig
      121 qgftggalip taqtiirtrl plsqlpvgmt lfglivllgp lfgpvlggwl aenvnwswcf
      181 flnlpvclll mallvfglps drpqwsaffn adwlgifgla iglssltvvl eegqrerwfe
      241 sqmivtlsvv sfvgmilial sqrfakrpim rlslmrnpry asvivivsav gaglygvsyl
      301 lpqflaivag ynaeqagaim llsglpaflv mpilprllgk vdfrilviag lllfclscml
      361 didltaqsvg hdfvwsqlir glaqmlammp lnqasmaava redsgdaagl ynmarnlggs
      421 iglaiigtvi drrttfhtav lresvnansl igqdrlsaya anwfahtgdl aysnmralgq
      481 laqqiqiqav vmtysetfyl lglallacvp lalllrtprr pqpmssgh
//
LOCUS       WP_175931636             154 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175931636
VERSION     WP_175931636.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..154
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17544
     Region          6..132
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mtdkkmqldk idlrildilr tdgrisyrkl servnltprp cqarverlea lgviegyrav
       61 ikapratkpi iviaqivlad hgrsqapfee emranpavld cwlvsgtfdf lvrlacedld
      121 eyrrianawl esprfrieki vttaelqaik rsvv
//
LOCUS       WP_175931503             424 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: serine hydroxymethyltransferase [unclassified
            Burkholderia].
ACCESSION   WP_175931503
VERSION     WP_175931503.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Appaji Rao,N., Ambili,M., Jala,V.R., Subramanya,H.S. and
            Savithri,H.S.
  TITLE     Structure-function relationship in serine hydroxymethyltransferase
  JOURNAL   Biochim Biophys Acta 1647 (1-2), 24-29 (2003)
   PUBMED   12686103
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Chan,V.L. and Bingham,H.L.
  TITLE     Complete sequence of the Campylobacter jejuni glyA gene encoding
            serine hydroxymethyltransferase
  JOURNAL   Gene 101 (1), 51-58 (1991)
   PUBMED   2060796
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10793727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..424
                     /product="serine hydroxymethyltransferase"
                     /EC_number="2.1.2.1"
                     /GO_function="GO:0004372 - glycine
                     hydroxymethyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019264 - glycine biosynthetic process
                     from serine [Evidence IEA]"
                     /calculated_mol_wt=45322
     Region          4..424
                     /region_name="PRK13034"
                     /note="serine hydroxymethyltransferase; Reviewed"
                     /db_xref="CDD:237280"
     Site            order(16,18,25..26,35,40,58,76..77,85,100,107,142..143,
                     268,286)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:99733"
     Site            order(39,59,69,102..103,130,180,205,208,233..234,240,366)
                     /site_type="other"
                     /note="glycine-pyridoxal phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99733"
     Site            order(39,130,234,366)
                     /site_type="active"
                     /db_xref="CDD:99733"
     Site            order(61,68,125,129,131,260,350)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:99733"
ORIGIN      
        1 msntqpffsq plaerdapvr sailkelerq qsqveliase nivsravlea qgsvltnkya
       61 egypgkryyg gcefadevea laidrvkqif nagyanvqph sgaqangsvm lalakpgdtv
      121 lgmsldaggh lthgakpals gkwfnavqyg vnrdtmridy dqvealaheh kpsliiagfs
      181 aypraldfar fraiadsvga klmvdmahia gviaagrhan pvehahvvts tthktlrgpr
      241 ggfvltndee iakkinsavf pglqggplmh viagkavafg evlhadfkty idnvlanaqa
      301 lgdvlkaggv dlvtggtdnh lllvdlrpkg lkgapveqal eragitcnkn gipfdtekpt
      361 vtsgirlgtp agttrgfgva efreigrlil evfdalranp egdpateqrv rreifalcer
      421 fpiy
//
LOCUS       WP_175931716             467 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: HdeD family acid-resistance protein [unclassified
            Burkholderia].
ACCESSION   WP_175931716
VERSION     WP_175931716.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..467
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=51367
     Region          10..185
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mvrlvllllg ieylrtrwrg ltvlgwlwva agvgifidal dgalhfpiel fawlfliegl
       61 atlavagsgv ggqrilryvk giavvvaagl vfaghhhghf llsmifgtlf lvdgllqcts
      121 awmvryrrwn vafawgvvei llaifffqpy pthyvgtvpy clglllmfgg mhmlslaarv
      181 rrltrnpafa tspapalapd lddaqhlpqf aqsewdgppa dgeraltvhv wtptgtskae
      241 aqrypvidry iaavdvngvi stghaalesp egiyislypa veidrspdef arilratren
      301 dvpglfqpdy atestawcps tvrvrirnyd pakleafwss yrqnttynlt hrncsstvsn
      361 aleaaldgav wrlkgaragw gafgrllltp elwvaaqirk ravtmawtpg ltldyarals
      421 mladprpfaw wkvarsavsa imasrrawre qdsaalspgg seaasmk
//
LOCUS       WP_175931718             211 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cysteine hydrolase family protein [unclassified
            Burkholderia].
ACCESSION   WP_175931718
VERSION     WP_175931718.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..211
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22402
     Region          34..188
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mnrdnaseva ttiltnvnts tsapippiap sktallvmhy qtdilglfps vapellantr
       61 tlcdaarsag vgvwfanlrf spgypevspl nkngqgikql glflddgpcp elarqpdepl
      121 ilahrasvff gtdlqarlva qgvdtlimvg iastgvmlss iahasdadfr lytvkdccyd
      181 pdpvvhahlf atafesrttv lslaqalrll a
//
LOCUS       WP_175931795             307 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175931795
VERSION     WP_175931795.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..307
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33563
     Region          34..186
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <174..293
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mdmtdivasr esgrrelasl igrfaptdgs hstavpglml hrhtrpvdlg cavsraalvi
       61 aaqgakrviv aghayeydah nclitsidlp ilsrvtrasa depylclslt ldpqrivela
      121 aemrlpepda gpegegiala eltpplldaa lrllrlldtp adiavvapli ekevlyrlmt
      181 sgqgtrlrhm aiagsqthri araiewirdh faepmrvesl aqavnmsvss lhhhfkhvtt
      241 lsplqyqkql rlhearrlll rqggdvgsva avvgyesasq fsreysrlfg appmrdvvhl
      301 rkkellg
//
LOCUS       WP_175931816             515 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FGGY-family carbohydrate kinase [unclassified
            Burkholderia].
ACCESSION   WP_175931816
VERSION     WP_175931816.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..515
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=55325
     Region          3..448
                     /region_name="ASKHA_NBD_FGGY_RrXK-like"
                     /note="nucleotide-binding domain (NBD) of Rhodospirillum
                     rubrum xylulose kinase (RrXK) and similar proteins;
                     cd07804"
                     /db_xref="CDD:466806"
ORIGIN      
        1 meyvigvdig tqstkallvd rhgtivarrs agyqpdtprp lwaeqwpqvw fdavldciag
       61 cvsdaraqgv padairavcv sslyggsgip vdidmrplhp cliwmdrrat aevdwvnehv
      121 nverlrvitg ngvdsyygft kmlwlrdqrp dvwanvryfl ppnayviyll tgevavdhss
      181 agniggvydv arrewsdaal dmlgipatmm perlvdstdi vggllsqwta plglpagtpv
      241 vaggvdaava tfaagatrag qhvamigtsm cwgyvnrhvd arhalvsmph vfdgqrdlyv
      301 fggaitagas vawfrdqfch aetdaarllp hgdphvllee aaervpagad gvlflpylmg
      361 erspvwdaka sgafvglsla htrahlyrav legvafalrh nieagrrgav alddrlivvg
      421 gaahsalwmq iiadvtgfpv wtieqdveaa mgaallagvg aglvsrddaq ggwvtlaera
      481 rpdadrakty darfslytal ypalkpimhr lgsss
//
LOCUS       WP_175931854             229 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Burkholderia].
ACCESSION   WP_175931854
VERSION     WP_175931854.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 229)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..229
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24704
     Region          1..229
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 mifqgfgpll wagtvetvkl avlslaasli lglagaaakl sanralrsvg tfyttlirav
       61 pdlvlmlllf ygiqillnev tdligwdqid idpfvagvvt lgfiygayft etfrgaflav
      121 prgqleagfa ygmsgwrvfh rilfpqmmrf alpgignnwq vlvkatalvs iigladvvka
      181 sqdagkstld fffftlaaga iylaittvsn vvlhhlekry svgvrrlal
//
LOCUS       WP_175931848             416 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175931848
VERSION     WP_175931848.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..416
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=45675
     Region          8..>119
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mnrqqswtrt aapgeiiyse gfagepvifl iadgkvelst rcddkrviva tlgrgeffge
       61 sallaaepra htakalsfcq ltvvpvamld eeiervsall rhivrtmirr vkrkddqlat
      121 ythadfmpgv lsyahvlslm agadtresgd twtrrpmqah atetsvplae virkcraiag
      181 hsrphvlaml rrmeklnlvt ieaaqgdgag gttdyaassd arqvvtfdaa rvvdraqqva
      241 dhdldlsins elelieladl esligvdktl llnklsngei aeevfafrks kvlsyveqkg
      301 vayfsrrnar rggdvraled lvwidprtlf dvvsafdtyd laklianldd ravadklfsv
      361 mtearrnevs wvmrrelkvd pveiedieqr vleavraaka paagvasgvp asssda
//
LOCUS       WP_175931882             431 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: O-acetylhomoserine
            aminocarboxypropyltransferase/cysteine synthase family protein
            [unclassified Burkholderia].
ACCESSION   WP_175931882
VERSION     WP_175931882.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..431
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=46313
     Region          1..430
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 mteqanpnwr letiavhggy rpdpttrava vpiyqtvaya fddtqhgadl fdlkvqgniy
       61 trimnpttdv leqriaaleg gigalalasg qaavtyaiqt iaeagdnivs asslyggtyn
      121 lfahtlpqyg iatrfadprd pasfeplida rtkaifaesv gnplgnvtdi aalaqvahrh
      181 giplivdntv pspyllrpfe hgadivvhsl tkylgghgts lggaivdsgk fpwaehadrf
      241 krlnepdvsy hgvvyteafg paayigrarv vplrnmgaai spfnafqilq gietlalrve
      301 risdnalkia rhlarhehve wvnyaglpdh pdhplvaryl sgrapgiltf gvkggrtgga
      361 kfqdalklft rlvnigdtks lathpastth rqlspaelak agvkeetvrl sigiehiddl
      421 ladldqalaq l
//
LOCUS       WP_175931887            1070 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit [unclassified
            Burkholderia].
ACCESSION   WP_175931887
VERSION     WP_175931887.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..1070
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=114943
     Region          1..1040
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mferlirfai ahrwlvmlai aavaalgvfs yqrlpidavp ditnvqvqin tsapgysple
       61 aeqritypve tvmaglpgle qtrsisrygl sqvtvifkdg tdiyfarqlv neriqeakdk
      121 lpagiapamg ptstglgeiy lwtveadara rkpdgtryta adlrelqdwv vrpqlrnvrg
      181 vtevnsiggy vkeyrvapnp aklmsygltl advvralern ndnvgagyie krgeqylvrv
      241 pgqarnvddi anivltnvgg vpvrmkdvgv vdigrelrtg aatsngeevv lgtvfmlmge
      301 nsrtvskava akmedvnrtl pagvkaipvy drtvlvekav atvkknlleg avlviavlfl
      361 flgniraali talviplsml mtftgmvnak vsanlmslga ldfgiivdga vvivencvrr
      421 lahaqsaagr pltrderfae vfgasqearr alifgqliim vvylpifalt gvegkmfhpm
      481 attvvmalaa amvltvtfip aavalfigar veekenrlmg warrayepvl aafmtrparv
      541 migagaivlv tlglatrlgs efipslnegd lavsalripg tslsqsvemq ksiektlkar
      601 fpeiervfar tgtaeiaadp mppnlsdgyi mlkpadtwpd pkkpreqlvr eiedalaglp
      661 gnayefsqpi qlrfnelisg vrsdvavkif gddmavlnrt geqiaaalqk vpgasevkve
      721 qttglpvltv nvdrdklary gvsvadlqds vaaavggqka gtlfqgdrrf divvrlpdel
      781 rtdieaikrl pialpapaag astplaaapy vplaelatid vapgpnqisr edgkrrvvvs
      841 anvrgrdvgs fvadareqlq qdvrvpagyw vswggqfeql qsaserlklv vplalfmvfv
      901 llfvmfnnvk dgllvftgip falsggvvsl wlrgiplsit aavgfialsg vavlnglvmi
      961 sfirnlrdeg mpldaavhdg altrlrpvlm talvaslgfl pmafatgtga evqrplatvv
     1021 iggilsstal tllvlpvlyr vshavswraa wrggvgasvl rrlgffkgna
//
LOCUS       WP_175931899             219 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175931899
VERSION     WP_175931899.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..219
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23700
     Region          27..182
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msnsgmekal etekrgrsyg gvapevraae rrdaliraat rvfgtvgfrk atvrsicqea
       61 klndryfyaa fdstedllrc tylhhaqqlh davaqavaar ggdlrervda glaaffaflr
      121 dpcaarvlll evmgvsadtd mtyqrmlidf gklimaigap reavtpaert eqrliglalv
      181 gamtnvgaaw lltdyrdpea qmiascrkvl lgtlgdagg
//
LOCUS       WP_175931918             285 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175931918
VERSION     WP_175931918.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..285
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31260
     Region          9..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(32,57)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(39..40,51,54,58..59)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          105..270
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 madapdnllg aylrdrrekl dpvalglpat rrrtpglrre evaqrahvsa awytwleqgr
       61 ggapsadvld rlaralmlne aerehlfllg lghppevryh apagvtprlq rvldsldasp
      121 aiirsatwdv vawndaaaat ltdyaalppa arnilrlifv dagvryaqpn wervarfavg
      181 afradvarsg atqavqafvd emratsaefd amwrdhdirt hdegtkeirh pragrialdy
      241 safsvtgnpe lslviftpat padrarirel vaarertraa qapaa
//
LOCUS       WP_175931925             301 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175931925
VERSION     WP_175931925.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..301
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31847
     Region          33..279
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mqdphspgts saaraprsdd davdaadsve pagapgtgml qrafailral agmqqdgvrv
       61 thlakavglt qgtahrilqs liaegmveqd eqsklyrlsv dffalaaqag npssmrtlcr
      121 pallrlcasl getifllvks gfdavcldlc egpfpirsft gdiggrialg vgqgslaila
      181 flpeaereev irfnvprirg ygvldevylr teiervrqlg yagrnsgvld gmagvavpil
      241 drtgypvgal svgtlasrlg ddrmpmvvel lrrqadaigp rtnpfdaalr rpmhglsgka
      301 v
//
LOCUS       WP_175931937             395 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [unclassified
            Burkholderia].
ACCESSION   WP_175931937
VERSION     WP_175931937.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..395
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42875
     Region          8..390
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mfdhlqrpef valraavqrf vddelrpier elgldsedvw prdvlrrvwr rsaalgfyta
       61 slpveiggqg lsiaevcalk adlaacgaal aphvlgelgg pprignmlky atpaqldryf
      121 kpvmrgekst cfaltephsg sdamsirtta vddgdslvin gtkhyisgap fadfaivmcv
      181 tdanatppqi mavlvdldlp gvsvqheyvp msgqhidadi rfvdvrvpre nvfggvgngf
      241 klgmsrisvn rllhcptmlg lamsayraal dyartrqqfg gpiarfqaiq hmladmaaal
      301 wacesmiaht aaladagadl rmmssackly vsercfeiad kavqihgnvg vtrghpveqt
      361 frklrmfril tgtseiqrna iakailepar agrda
//
LOCUS       WP_175931941             151 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175931941
VERSION     WP_175931941.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..151
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16264
     Region          6..137
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mpdealdrld lailealqen artplsevgr riglsqpats ervkrleerg iiagygarid
       61 paalglgmma iirlkttheh ikpalrafad mphvievhrm tgedcfllkv lvptpgqlet
      121 lidaiarfga vttslvlrse ptkaigkall g
//
LOCUS       WP_175931967             207 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: HAD family hydrolase [unclassified Burkholderia].
ACCESSION   WP_175931967
VERSION     WP_175931967.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..207
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23053
     Region          3..>172
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mtikavvfdf ggvlidwspe ylyrelipda aerrwflthv camdwvvrqd ggqtieegta
       61 elvakfpehe alirafyarw hemiggvlee gaalvdrlda qgmplfgltn wsaqtfpyaw
      121 dnfpvlrrfk divvsgrvkl vkpdpaiyre mharidphlp giaphelvfi ddnannaaaa
      181 talgwhgihh tsaaatearl relgala
//
LOCUS       WP_175931979             206 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175931979
VERSION     WP_175931979.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22544
     Region          24..175
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msgievakpl arrtrrpidg ataqehllra aeelfykegv rtvgveavve ragvnkmsly
       61 rqfsskdeli laylermdac fferfdasva khpgqpkaql iqyfvdlaer atqkdyrgcp
      121 fvnvaaefpd ashparerva qnkeqlmkrl valcegagar qpkaladala lvvegiyaas
      181 qtyrhgetpi giapalvtql ieaaca
//
LOCUS       WP_175932094             392 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: methionine ABC transporter ATP-binding protein
            [unclassified Burkholderia].
ACCESSION   WP_175932094
VERSION     WP_175932094.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 392)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..392
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40844
     Region          37..390
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mtqlfdtlgf ieasavraga gaaaheegvt paagaavsle hvgkvfatpr gqaaalrdvt
       61 ldvrrgevfg iigrsgagks tllrllngle rpssgrvrvq gvdvgalded glvalrrrtg
      121 mvfqhfnlls aktvfenval plkiagvpka erarkvdall dlvglaakrd aypaslsggq
      181 kqrvgiarsl vhdpevllcd eatsaldpet tqsilallad inrrlgltiv lithemevir
      241 avcdtvavie qgevvetgpv wrvfgdprhg atrallstlq hdlpaelaar vrplpehaal
      301 pdgaqivldv rytgesggep dvgalaaalg gsvrflhggi esiqghaqgr lviaatprad
      361 dagspaargg avaallerar rhanhaevlg yv
//
LOCUS       WP_175932158             313 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175932158
VERSION     WP_175932158.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34603
     Region          1..293
                     /region_name="trans_reg_YafC"
                     /note="DNA-binding transcriptional regulator YafC;
                     NF040888"
                     /db_xref="CDD:468824"
ORIGIN      
        1 mkttldelqa fiavvdtgsi taaaqqldlt vsatsrtlar leeklkttll rrttrrlelt
       61 eegraflqda raivesvesa eeqmlarrem psgrlrvdaa tpfmlhvivp lvrgyrerfp
      121 kvelelnsne gitdllerrt dvairigrlk dstlhsrrig nsrvrmlasp ayieahgqpr
      181 kvedlakhtl lgftqpesln vwpilgadge acriepdvys ssgetlrqla legtgvvcls
      241 dfvtardrea grlaqvlarq tldvqqpiha vyyrntaiss riasfvdyli evlgggsggd
      301 aqarrkaawm vpq
//
LOCUS       WP_175932168             462 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NCS2 family permease [unclassified Burkholderia].
ACCESSION   WP_175932168
VERSION     WP_175932168.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..462
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46639
     Region          22..457
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 msdtpvqptv gvgaaetdfg tqgvidryfg issrgstqrr eiiagvttfl amvysvfvvp
       61 gmfgkagfdt savfvavcvt tafgsllmgl waklpiaigc aisltaftaf glvlgkglpp
      121 tvalgavflm glvftgisit gvrswilrnl pagvahgtgi giglflllia sndvglvikn
      181 pgaglpvslg qitafpvims vvglaaifgl ekrrvpggil lvviaislvg lifdpgvkyr
      241 gifalpslsa pghasligam dvkgalsmav lpsvlalvmt avfdatgtir avagqagqld
      301 angriinggr altadsissi fsgflggapa aayiessvgv aagaktglaa avvgllflvv
      361 mffsplaglv psyatapalm yvgllmlgsv sklhmddmvd amsglvcavf ivltanivtg
      421 imlgfstlvi griasgelrk lnvgtvliaa vlvtfylggw ai
//
LOCUS       WP_175932319             237 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheW [unclassified Burkholderia].
ACCESSION   WP_175932319
VERSION     WP_175932319.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..237
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=25288
     Region          79..231
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mnrdaaatde atldvddcwn rigtrgdrsc erlndclrcl ncpvyasnaa kllerpldva
       61 emtdvtrrms afgtaragdd gdtrhaalaf rvadewlalp igvlreiagt rpihslphrr
      121 nsavrgvvni rgtlriaisi gellgldagk ggsagsgsdd grftrllvaa hqgepvvfpv
      181 devegvlrfg asdwvpvpat vgrasaglsr gvlswrgksv glldddrlfd avtrsmr
//
LOCUS       WP_175932329             133 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [unclassified Burkholderia].
ACCESSION   WP_175932329
VERSION     WP_175932329.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..133
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=14570
     Region          16..133
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mslihaaavl eadapdyvvq lqagthaltg deapreggqd rgpapyefvl aglaqctaat
       61 lrmymqrktw pavriavrte lhadregvqy vrrvvtldgp lddaqrqrla eicektpvtq
      121 fikrgtridt tln
//
LOCUS       WP_175932337             350 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [unclassified Burkholderia].
ACCESSION   WP_175932337
VERSION     WP_175932337.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..350
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38274
     Region          10..345
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mdsghdhqkf fyfllfavtv glcwilapfs gavfwgtila ilfqpvqrwl aarfgkrrnl
       61 aalvtmslii livilplvfv aatlvqeiay vyqelkdaqp nysqyfhdii halptsiqnl
      121 lqkygltnip giqkkltdga aqisqfaatq alsigqntfq fvvsfgvmly mvffllrdgg
      181 eigrrvrral pldeehknll lakfttvvra tvkgniaval vqgalgglif wilgiegvvl
      241 wgalmaflsl lpaigaslvw vpaalyflmi gavwkcvilv afcvgviglv dnllrpilvg
      301 kdtkmpdwvv listlggmal fgingfvigp lvaalfmasw diyaraeqge
//
LOCUS       WP_175932355             479 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Burkholderia].
ACCESSION   WP_175932355
VERSION     WP_175932355.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..479
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48504
     Region          21..418
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(28..29,32..33,36,68,118..119,121..123,126,148,
                     151..152,155,284,287..288,291..293,296,324,328,380..381,
                     385,389,405,408..409,412..413,416)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mdtttpspaf ppalarvvat vstgfvvtql dvtivniala hlaadlhlpv aglqwvvday
       61 tlafavlmls ggalgdrfga rrlyiaglll falaslacga avapamliaa ralqgvgaaa
      121 mlpnslalln dacrhdprlr aravggwtaa gsisiaagpv vgglliaawg wrgiflvnlp
      181 lcaaglaatf awvparreqa aparsprsld lrgqfiaiam ltaltgavie wrplglahpv
      241 vaggfvlaal aalafvaaes rtatpmlpls lfrhrtfsaa vlfgicvnlt yygtvfvlal
      301 ylqrargesa lqaglaflpl tggfllsnla sgravarhgp rvpmvagalv aalgygslhf
      361 vdastplgvl lvpflliplg mgfavpamtt avlasvaher agiasavlnt arqaggaigv
      421 aafgalaggg gasqvvsglr ietvvsvall iaaallatrv radahrgasr srqgvpahd
//
LOCUS       WP_175932358             499 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sigma-54 dependent transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175932358
VERSION     WP_175932358.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..499
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=53409
     Region          18..139
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <157..465
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mvarspdang qaapemtdvs vtapeagrkl fvimrtpdep llaqlrglgw eiavaktaga
       61 aqnmtsgvsv aaglidftgf tardypalkm clsqpaigwi siaqagitig pavrelirsy
      121 cfdyvtlplp yewishvlgh argmaaldrv dgaayaasig ehgmigncea mqqlfstirk
      181 vaktdasvfi sgesgtgkel talaiherss rgkgpfvain cgaiphhllq selfgyerga
      241 ftganqrrag riesanggtl fldeigdmpv esqasllrfl qegkierlgg qesiavdvri
      301 isathvdldg aveagrfrad lyhrlcvlri hepplrargk didilahyvl qkfkadsgrk
      361 isgftsaald amrryewpgn vrelinrvrr aivmaesrll tphdlgldtp getepvtleq
      421 aralaertai enallrndhr inkaaaelgi srvtlyrmmi ehglndhdnn ggsggnggng
      481 dsgghdgaps gdaghqrvg
//
LOCUS       WP_175932384             330 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175932384
VERSION     WP_175932384.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..330
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36061
     Region          6..330
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpliriwavd halasgiaap tdiltaanhi assmtsgrpa ppfrwrvesi ggrpvrtasg
       61 qvipvdgaid ggsaadaiwl tgplvanldr lldrpaslap lfdalrrqha rgtliatyct
      121 gafllaeagl ldgrvatthw skassfrary pdvalrasdv lteqdgllcg gavtsyqnla
      181 lrvvdklana rvaasvarlm lidmnrdsqd sfidldrmgh aghddpaiar aqrwmekhlr
      241 epfslarlsd hvamsertlh rrfrdavgap plrylqtlri evakrllaet klaidtvcer
      301 vgyadisgfr qlfkretgis psqyrrrfar
//
LOCUS       WP_175932402             281 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [unclassified
            Burkholderia].
ACCESSION   WP_175932402
VERSION     WP_175932402.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472037
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..281
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=29683
     Region          93..217
                     /region_name="TadD"
                     /note="Flp pilus assembly protein TadD, contains TPR
                     repeats [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG5010"
                     /db_xref="CDD:444034"
     Region          123..151
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          191..220
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
ORIGIN      
        1 mkrinerlvl agvtavamll lggcatkdsg ygvsaqtera almqaadqkq svpdtpgmyl
       61 gliqrmqaqg lyfaslahid sydktygvip esillradal rmtdqpaass vaytqllktp
      121 laargyrglg liagaagnfd qaaqalaqas slaptdasll sdlayaklrs gdvvgarvpl
      181 mkaaeldqrn pkivsnlaly liaagraqda qrlmnqqhlp adirkdingd aakvmaavha
      241 qqraiatppv vsrpaittpi tpmannfgyd qtvpllqrfa q
//
LOCUS       WP_175932425             328 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [unclassified
            Burkholderia].
ACCESSION   WP_175932425
VERSION     WP_175932425.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..328
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34494
     Region          7..324
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mndnehrpvr fgivgagsia hrfaqslahv pgaalagvwa rradaaaafc gtyggrpaas
       61 ldallasdid aiyvatlhds haqytlaala agkavlcekp atlnaaqldt vlhaaraagl
      121 lfmeamkppf fplyrqlrah lrddpigeir lvragcasss vpedhsvyrl draggalldi
      181 giyeaflavd wlgaardvqt lgrvgatgvd lfaslnsvha nggiaqlfcg ldvmgrgdal
      241 iaaagghvti hekwwnpara tiryadgrtv eldapadggg lnyetahfcd llragetesp
      301 imthdhsrqm iamtdaaraa lgvrypge
//
LOCUS       WP_175932517             514 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TolC family protein [unclassified Burkholderia].
ACCESSION   WP_175932517
VERSION     WP_175932517.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..514
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52001
     Region          90..493
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrlpeppaas iaaaalatav alagcatssi dlapeasdrp wqpqtsaagd ivaapprasa
       61 qgahdytlpa spalasvpap aaldashayt lpelidlaes anpltriawn darnaalavg
      121 lakaaylprl satamgayqa nhgststilg dassnttvhg tisalslqwl lfdfggraar
      181 veaaeqasia snvaftavhq qvihdvtvsy yryeaarsra lsaqqglana dailaasrar
      241 lehgvgtvve laqatqnraq anlalvqang aesdsylalv salgisplsk ptiaalpkrp
      301 lpaalgssvd aivsdaiarr pdlqgafave kanrakikaa qaafmpkifl sastsyangg
      361 tsisalpaig dqaptvnlng srygggvflg vtiplydggl rsavlmqarn daesasarlt
      421 rtkeeavrqv vaaqnavqts lashdaakal vdaaqtsyda altayrngvg svtdatiaqs
      481 qllaarnaev dsyagalsaa aalalatgti gstq
//
LOCUS       WP_175932556             297 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175932556
VERSION     WP_175932556.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..297
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32211
     Region          25..280
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mvkttmsgap epaasgdees sggassylvp glerglrila efsarepvlg apelskrigi
       61 prtttfrllq tlealgfler vngdryfrlg vgvlrlgfey lnsleltdlg tpvlerlrds
      121 tglsthllir dqrdvvfvak aqsnasmfgs vkvhvgtrlp ahatvhghvl mgdltrdamr
      181 qlypekklep ftertpgtvd elydrvrhya rlgyavseaa fesgisavta pvrdhsgsiv
      241 aaitatvprs eigeageker lveavcgaav dlsqrlnyrp lesdptfaha rhkvamf
//
LOCUS       WP_175932628             147 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Hsp20/alpha crystallin family protein [unclassified
            Burkholderia].
ACCESSION   WP_175932628
VERSION     WP_175932628.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..147
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=16067
     Region          43..147
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 msdiffpsdl laefdrlqrq masmftgfpa slraprpgaf ppvnigstdd tieivafapg
       61 ldpakidisv drrlltisge rtppddgttd derriyaner fmgafrrvve lpqhadpdki
      121 daryangclt isvgkseask praitvq
//
LOCUS       WP_175932659             174 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: c-type cytochrome [unclassified Burkholderia].
ACCESSION   WP_175932659
VERSION     WP_175932659.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 174)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 174)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..174
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17735
     Region          <27..159
                     /region_name="TsdA"
                     /note="Thiosulfate dehydrogenase TsdA, contains C-terminal
                     cytochrome c domain [Inorganic ion transport and
                     metabolism]; COG3258"
                     /db_xref="CDD:442489"
ORIGIN      
        1 mrkplaclla acamtsgafg agfglgqpve raalaawdid vapdgsglpp gagtvarggh
       61 vfadkcamch gaggeggvgd plvggigsla sakpkktvgs ywpyattlfd yirrampyna
      121 pqslsaddvy avtayvlhln givpgdarld artlprvkmp nrdgfvpdpr pgkl
//
LOCUS       WP_175932663             329 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Burkholderia].
ACCESSION   WP_175932663
VERSION     WP_175932663.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..329
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=35593
     Region          64..320
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mvgphdarpy vdafpardsi vnatsprtwl ppyaarggas paasaapdtr aaaqpaahaa
       61 qagthserll aidqvsleyr sgarivrath qvsfdvygsd rfvllgpsgc gkstllkaia
      121 gfiepvsgsi aldgrpvrgp gpdrvvvfqe fdqlppwktv venvafplra aaklsraear
      181 eralhyldkv glgafadayp htlsggmkqr vaiaralamq prvllmdepf aaldaltrrk
      241 mqeellrlwd efrftllfvt hsieealvvg nrilllsphp grvraelnsh ehslesvdtg
      301 dfrdnvarih rllfdtdaph vpttegaas
//
LOCUS       WP_175932695             209 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [unclassified Burkholderia].
ACCESSION   WP_175932695
VERSION     WP_175932695.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..209
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21860
     Region          1..206
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mslsallafa lilsvgvatp gptvllamsn gsryglrham vgmlgavtad vvlvalvgfg
       61 lgvlldaset afvtlkllga awlayvgirm lmssggsave qadvpgtpdr rsaflksffv
      121 amsnpkyylf msallpqfvd rshaiapqya ilaativaid aigmtayall gvhsvrvwka
      181 agekwlnrvs gslllmlagy valyrkavh
//
LOCUS       WP_175932696             925 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: type VI secretion system Vgr family protein
            [unclassified Burkholderia].
ACCESSION   WP_175932696
VERSION     WP_175932696.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 925)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 925)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..925
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..925
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=99178
     Region          16..833
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mntaellrtf asgvvdqnnr pvrmnwgpaq ktleqvlalq yadireglmt gieghltcvs
       61 aradlpirsf iglpvsvemt tdrgrlhtin givtdvragq sdgsltcyql tirdvlsvme
      121 rrtnsrlfrs kslpdilgvl lqewrqrssa lagafefdls glqaerypar eltrqvnesd
      181 ahfirrllrr egatvfvkag kagerasgnv hdtpvhtlvf addpmklpqt aagtvryhrd
      241 aateerdsit lwatsrrlip gkiirptwdy ksgrmsqteq ativdqgdgg ndlghlladv
      301 vidiphagds ssdldrigkd rmlahelrae svdgvsnvrd lavghwfala ehpqldtmpa
      361 eqrqfvvtsl hhcvrnnlpk elneraqslf aasrvlfnav psdvngtsgd egdrryentf
      421 scvrrgvplt paydphvdlp pvhpmtavvv gpegeevfcd emgrirvriq glspddhaha
      481 qgagtsgtps dsapvrvaca lagpgfgant lprvgmevli ghiggdpdrl vvmgvlangp
      541 nmpatfshtg alpgnrylsg tktkeikgqr ynqirfddtp gqissqlase haysqlnlgy
      601 ltqprdngqg aargegaelr sdahvairsg kamlisawer lrasdghlar deylhlmqec
      661 velfkslgdy agqhqgvald tqphdalvtt vkgwpngdas gggessgasm aaigitapag
      721 ismatpktvt thaggnvdvv aqnhlqytsg qrinlqaghg vamfahsegv saianqgkva
      781 lqsqnddtqi dsakniqmta gggklagmas eqvvfvtsgg aylklqggdi elgcpgsftv
      841 ksashtwagp asmsadfpkf dqgslgrvpk lvratdgqpv egmeaevrka sgelikgktd
      901 aqgklapvss dqfeqlavrf fksrt
//
LOCUS       WP_175932706             455 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Burkholderia].
ACCESSION   WP_175932706
VERSION     WP_175932706.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..455
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49302
     Region          23..410
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,154,
                     157..158,161,259,262..263,266..268,271,299,303,352..353,
                     357,361,377,380..381,384..385,388)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnppspalsg rdplasavsk vkwhvlplvl imfianyidr vnvgfvdrhl easigigaaa
       61 yglgaglffv gyalfevpsn llmqrygarv wlarimatwg ivaaamafvw ndtsfyalrf
      121 llgaaeagff pgvvlylsqw lppqergkam aiflggsafa svlsgpvtgg llsirgfgle
      181 gwqwmflieg lfsvalcgas wlllkshird atwltaeert alqnaldder atrdvrshvp
      241 mrattllrdp qivlfcflyf siqltiyaat fwlptlirkm ggltdfqvgl yntipwmiai
      301 gamygfavls skwkhpqrwl afalvlaacg lfastspdpv wsfasicfaa lgfkaaaslf
      361 wpipqgyldt rvaaaviali nsvgnlggfv aptafgylkq htgsitggly alaiaslvaa
      421 laalfarthr rsdpprglpa desfthasml rhaeh
//
LOCUS       WP_175932708             410 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Burkholderia].
ACCESSION   WP_175932708
VERSION     WP_175932708.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..410
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42763
     Region          12..394
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(22..23,26..27,30,65,112..113,115..117,120,145,
                     148..149,152,224,227..228,231..233,236,266,270,320..321,
                     325,329,345,348..349,352..353,356)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mtpieqevrr rwlpvlaggl imgvalgirh vqglflapvs ldhgwsreaf glalalqnli
       61 wgvaqpftgm vadrfgsvrv iaagmllyaa glvtmahaat tglftvgagl vigialsgsa
      121 fasiygalsr lfppdrrgwa lgvagaiggl gqfcmvpvaq eliggigwrh afialalvaa
      181 llaplavllr drpaqaagaa agsdqsigea vreafahrgf wllnagffac gfqlafiath
      241 lpaylldhgl parhasvala lialtnvagt yacghlggll rrkyvlsvly lvrafamaaf
      301 vavplspasv yvfaavmgft wlgtvpltng visqvfgvry iatlfgfvff ghqlgsffgv
      361 wlgalvydat hsylplwigs ialgvlaall hlpiddarva rpaagnaawa
//
LOCUS       WP_175932754             472 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Burkholderia].
ACCESSION   WP_175932754
VERSION     WP_175932754.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..472
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51134
     Region          39..457
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(49..50,53..54,57,97,147..148,150..152,155,175,
                     178..179,182,293,296..297,300..302,305,332,336,385..386,
                     390,394,410,413..414,417..418,421)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mastdslpqa qapspsidpg sisarldrlp ptrsvwklvv llslgfffel ydllysgyva
       61 pglvksgils atthglfgtt gvasfiaalf sglfigtiac gfladrfgrr aiftwsllwy
      121 taanivmafq dtatglnfwr fvvglglgve mvtigtyise lvpkqirgra faceqavgfv
      181 avpvvaflay llvphaplgl dgwrwvvlig ahgalfvwwi rrelpesprw laqqgrvdea
      241 drimrvleak veaeygrplp ppapaepvpp rgsfrdmwvp pyrsrtimmt ifnvfqtvgf
      301 ygfanwvptl likqgitits slmyssvial aaplgpligl viadrferks vivamaaaiv
      361 vcgllfsqtt vgaflivlgi gltlasnims ysfhayqael fptsirarav gfvyswsrfs
      421 aifssfviaa vlrgfgtfgv fafiagamvi vmaaigwmgp rtkgialeti sk
//
LOCUS       WP_175932761             743 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: penicillin-binding protein 1A [unclassified
            Burkholderia].
ACCESSION   WP_175932761
VERSION     WP_175932761.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..743
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=81795
     Region          48..715
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mnrfvpflrh awlrcrarva plaaasrarl ralgagalhr lrhptrrgva ltlaaipvlg
       61 llvllafvpf tpsigdirka ridrparvls adgrliaefr pvnrewvplk qisphmvdal
      121 iatedhrfya hhgidwrrtl aaglhtfsgd rqggstitqq larnlypdev graptltrkv
      181 kelitafkie avyskdeile tylntvpfly naygvemaar tyfgksadql dlaesatlvg
      241 mlkgnsyynp vlnperavqr rnivlgrmaq tgmlspqqla klqrqplrvd fepqtaqpgl
      301 aphfavqlrk wliawadrnn ydlysdglvv rttldarlqe matqaltrqt erlqaiadsa
      361 wrgpagcglr ndlfrgfirq tpeyrqarda gladvvavkq lganrefvrv lcerktqvqa
      421 gfvaidprng airawvgspd fgsepfdhvv qarrqpgstf kpfvygaafa dgmrpgdtfv
      481 drpvaipvdg ravwrptdae pptgepmtlr dglalsrnri taqvmqhega akvaqlaram
      541 gvrdspldav pslalgtspv tlkemvsayg tianrgvyva pqmitriedr dgkvlaafgs
      601 apperalpva aaqtlvdamr gvvdygtgad irsrygirid vagktgttqd ntdgwfilmh
      661 pqlvagawvg fddgsvtlrs dywgagahsa lpivgsfyda alraraidph vqfspdfrpr
      721 sapapkrrap qhsglfdwlr lfr
//
LOCUS       WP_175932769             210 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [unclassified Burkholderia].
ACCESSION   WP_175932769
VERSION     WP_175932769.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21967
     Region          1..192
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mhettllifa avafvgiatp gptvllaltn gsrygvrraa ygfagamlsd fvlivavalg
       61 lgallmasaf wfsvvkwlga aylayvgirl lmskgsldva vaqrgtasgr nasifaksfl
      121 tavtnpkgyl ffsaflpqfl dpaaplvpqy valavtfall dgavmfgyal lgaravrllk
      181 rsgalwlert cgamllalag slalyrrhaa
//
LOCUS       WP_175932822             252 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: amino acid ABC transporter ATP-binding protein
            [unclassified Burkholderia].
ACCESSION   WP_175932822
VERSION     WP_175932822.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..252
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27210
     Region          1..244
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mirleridks fgqhrvlsei dlalqpgsvt aligpsgsgk stllrcvnll evpeagtlav
       61 gdaridfvpg rrpsrdavfa vrkqtgmvfq nfqlfphlsv vqnvmeglvt vqrwprerar
      121 qralalldkv giadkadawp atlsggqqqr vaiaralaps pqvllcdept saldpelsve
      181 vvevlrqlar egttmlmath dlrlaasiah davfladgri veagasrelf grprdprtak
      241 fvatraqgvp af
//
LOCUS       WP_175932824             204 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CGNR zinc finger domain-containing protein
            [unclassified Burkholderia].
ACCESSION   WP_175932824
VERSION     WP_175932824.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..204
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22678
     Region          12..204
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mvtrpdparh ghdwraadfv gghpaldfln tvadtgktrd eeklvdwpav rawagkarll
       61 apddlarllr rprqdgpdel aalhrfrdda yaaiahltae dggsagtraa drlaaairea
      121 igrstfdavg grfawrpdar aasrwvdava lgfehlmrsd dfarvrqcgr ctwffvdrgr
      181 gvgrrwcdmr tcgnrakvea frer
//
LOCUS       WP_175932832             585 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ShlB/FhaC/HecB family hemolysin secretion/activation
            protein [unclassified Burkholderia].
ACCESSION   WP_175932832
VERSION     WP_175932832.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..585
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=63975
     Region          6..585
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mtikrllilq lsalvtlsaq aqqaptpndq aaaaranaeq nqqvqqrrda qqrdatvqap
       61 gmrsdvprpe aypvlptetp cfridhfald vpdslppask aqgasalpmd rfafardwla
      121 hyagqcvgkq avdlivkgls qailargyit trvlvpeqdl stgtlklali pgvirhvrfe
      181 deklrgtwkt afptrdgdvl nlrdieqgle qmkrvssqdv smriapgdmp gesdvvldvk
      241 rgkpwtvvas idnsgtratg klqgnvslgi dnplglndif nvgfnqdlef gdkrfgshgw
      301 nafysvpwgy wtgtlsayts tyfqplaavn qtfvasgnmk tvdfklnrvl trsrndvfgv
      361 qvrltrrfgd syiegttips shqnatflef glndrhyfgs sqfdgslayr qglgwlgstd
      421 smfaaeggqt yrfkmvvlda nlstpfvigt qpfkyvttfh gqytgntvsy ldsvtigsry
      481 tvrgfdgerl laasrgfywr nelqvpiaqt glaayagldy grvwgpepva lvgtqlagav
      541 igvkgsvatr fgsyaydlfa gtpvykpsgf etarvtlgfq ltaqf
//
LOCUS       WP_175932849             348 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [unclassified Burkholderia].
ACCESSION   WP_175932849
VERSION     WP_175932849.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 348)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..348
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38389
     Region          2..325
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mttlaaqata cdalwytrcp vptalgiavh rgwfdeefgp dgialhslqe tadadkresh
       61 fdhslrhsfr qggnipalwa rargadtrvi glswtnefqa ivtlperdir tardlrgrrl
      121 glprhpisid fwraaalkgf lsaleleglg hgdaewvdlp dtrerhtgpa sftrgpheyg
      181 leiaalvrgd vdavfvkgva gletvhlida qividlgahp dplvrigngt prtltvdral
      241 idarpdlvsr flsvvvgagd waarhpaetv ayigretras dewvryayga dvhrhletgl
      301 aptsidglva fkdflvewgf lehdfdaraw idpapftqid rhrhawva
//
LOCUS       WP_175932852             354 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter substrate-binding protein
            [unclassified Burkholderia].
ACCESSION   WP_175932852
VERSION     WP_175932852.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 354)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..354
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38550
     Region          12..335
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 msttashnvq siwytrcpvp tplgiaahlg wldhefagdg itvralqesq haalhhahvd
       61 hsldnafrqg gsipalwara sgadtrvial twvdeaqaiv alpeaglarp kdlrgrrigl
      121 prrdgeridi fraaalrgfv salsldglgp gdvewvdvpa snlrapvatp atrdaafshp
      181 aslssrrlya aeaaalvrgd vdaiyvkgsl gletahliga qpvvdigfhp dpqirinngs
      241 prpltvnast lerhpdivsr flarvtdveg warehehevl gylgretgsg hdwlrlayga
      301 dvhrrlrtdl deasiaaldd fkrflvdwrf lpadfdvraw idrraldgia tlsr
//
LOCUS       WP_175932873             349 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175932873
VERSION     WP_175932873.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 349)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..349
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37419
     Region          29..225
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          257..340
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtynpfllie rpyldmsapl lppipdthdl vselllgmrl sgvqyrriqv arpfglnfgh
       61 apgraqfhfv vrgpvllrdd sgetmrleag daillphggm halvsdpdvp creingfeia
      121 kicdtvasva sagvspstca taepgagdal ifsacmeldl ggmqplvgtm pafmhvgtll
      181 arypeirpml damereacta ragfagilar ladvvaafiv rgwvecgcgd atgwvqalre
      241 pklgraival hrdpgrnwsv aelateagvs rsvfaerfla atgmtpvryl telrmrlaaq
      301 wiardretie avayrlgygs laafsrafkr vigkppgavr adgavhaea
//
LOCUS       WP_175932914              63 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CsbD family protein [unclassified Burkholderia].
ACCESSION   WP_175932914
VERSION     WP_175932914.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..63
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..63
                     /product="CsbD family protein"
                     /calculated_mol_wt=6841
     Region          1..59
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 mdrnriegrl kqvrgsvkea lgkvtgdret eaeglaeqqa gkrqekagea adavrdhtdt
       61 drh
//
LOCUS       WP_175932935             178 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: methylated-DNA--[protein]-cysteine
            S-methyltransferase [unclassified Burkholderia].
ACCESSION   WP_175932935
VERSION     WP_175932935.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..178
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18921
     Region          1..165
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtpahlipsp lgdiavried daltglyfvg qkyfpslaiv rdadalamsp varrvaeeia
       61 eyftgardtf svpihlrgta fqrrvwkell aipfgervsy gditervglp msgaravgga
      121 vgrnpvsiiv pchrvvgasg sltgyaggid rkrallsleg agfsrgarqp mqqaqlaf
//
LOCUS       WP_175932973             292 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175932973
VERSION     WP_175932973.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..292
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32025
     Region          1..276
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mgtsiralll sqmdsftpse qkvaqalldr ypslglgpia qfakqadvsd ptvfrfvvri
       61 gfpnyssfqq alhdeidtam nsplarmdaf hsetgmrdsh aaifqrlses lattidglda
      121 aafdaavavl adpdvrvfcg ggrytaplas lfsftlayar phvqyvepnv nlasvaladm
      181 gpsdllvifd frryqkdsir faqaahrlgt rillitdewr spigefaeiv lriqgrpfam
      241 lqtnvpalal aealvigvtn rlpelarqrm ekieqlnagg iewdasrrdl pe
//
LOCUS       WP_175932936             163 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175932936
VERSION     WP_175932936.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..163
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17895
     Region          4..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 magitldeld lrilailqdd asvsnlqlae ralsspptcm rrvrrlteag virrqvavld
       61 pvaigtavta lieisldrqt aedydafeay vcaepavtqc yrvspgpdfv viadladvae
      121 ydefarrlft gasnvrnvrt ffsthrakfe anarvahalr krt
//
LOCUS       WP_175932977             430 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia sp. BCC0801].
ACCESSION   WP_175932977
VERSION     WP_175932977.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0801
  ORGANISM  Burkholderia sp. BCC0801
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia sp. BCC0801"
                     /db_xref="taxon:2676291"
     Protein         1..430
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=47146
     Region          4..412
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mttptriviv gggiaglqla trlgerlgrs graqitvvdr spthiwkpml htiaagtrdv
       61 qqqqviflah ardhgytyqp gelkgldrar rriqlgeirs qngdvaidar eleydvlila
      121 lgsqandfgv pgvrehcyfi dsqqqaetfn ealrmrvfrs iardepfrva ivgagatgve
      181 laaelsrlle vaqaygdetv rerlqltlle sgprilnafp prisasaqrr leqigfrvlt
      241 strvtsadan gfhygdgsfa eadlmvwaag vkapdfmqal ggldtnranq ilvgptlqat
      301 gddhvfaigd cgsllpdghe rplpptaqva tqqaehlakh lpawldgtpi ppfafhdfga
      361 lvsisdydaf gtlgqfgffr ggfiqgrfaq fshlmlyrrh qqalhgfska tllwiaerin
      421 gwvqprirls
//
LOCUS       WP_175932978             217 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175932978
VERSION     WP_175932978.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..217
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23982
     Region          29..180
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maevteraps krrtrgrpla dasvgpdvil raarrtfakr gydatsvrev arelgidaal
       61 iahhfgtket lwlavveqiv elaepmfdal ralrtsslsh rdrvrralel cvdhefaepd
      121 igmffstaat eeggrldrlq erivrpyhda mfplladave agairpvdpn vlffmiasav
      181 sttvsyshmm leftslparp eafreavlgv afnflgd
//
LOCUS       WP_175933017             469 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FAD-binding oxidoreductase [unclassified
            Burkholderia].
ACCESSION   WP_175933017
VERSION     WP_175933017.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..469
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50228
     Region          14..467
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mnhpappaam rrplppamld alraafgerv stadairahh grdespfdpq lpdavvfahn
       61 tdevrevvsl cslysvplip ygagsslegh llavrggvsl dlsemnrvls inaedltvtv
      121 epgitrkaln ealrdtglff pidpgadasi ggmtatrasg tnavrygtmr envlgltavl
      181 adgrvvktgs rarkssagyd ltrlfvgseg tlgviteitl rlhplpeavs aaictfptmg
      241 davrtvieti qigvpiarve fvdalavrsi nrhsnltlte aptlffefhg tdagvkeqae
      301 lvqalaaqna gqgfewatrp edrsrlwsar hnayfamlql kpgcravttd vcvpisqlaa
      361 cveeteadlr asslpcpivg hvgdgnfhva ilidpdqpee laeaehindr iveralrlgg
      421 tctgehgvgl hkmrflpkeh gdnaidtmra iklaldprnl mnpgkiftc
//
LOCUS       WP_175933035             327 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Burkholderia sp. BCC0801].
ACCESSION   WP_175933035
VERSION     WP_175933035.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0801
  ORGANISM  Burkholderia sp. BCC0801
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 327)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia sp. BCC0801"
                     /db_xref="taxon:2676291"
     Protein         1..327
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36431
     Region          89..327
                     /region_name="COG1223"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440836"
ORIGIN      
        1 mataeqikal lrshadrddr rfyatalqva aqearqghhk latdikqmve ksqsfaspgl
       61 alarptplas qpkgdlhgll elthtaarfs elvlshevkd rldrvlleqr qkdklaqygl
      121 lprrkllftg ppgtgktmsa aalatelklp lytivldsli trfmgetaak lrlvfdhikq
      181 travylfdef daigtqrgsq ndvgeirrvl nsfllfveqd sseslivaat nhpelldkal
      241 hrrfddiirf ekpdegqvea iienrlsmfe tndltwsqlt taavglsaae vtracedaak
      301 eailhhsnki stkllikaie qrhtgrk
//
LOCUS       WP_175933055             388 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Burkholderia].
ACCESSION   WP_175933055
VERSION     WP_175933055.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..388
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41125
     Region          19..227
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          143..387
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 maipltyiar nlwtrrltta ltaggmalvi fvfatvqmld agltktlvst gepdnavvir
       61 kgaeteiqss idhqqanale mhpavalgpd grplvskeav vlislvktss gkpsnvvirg
      121 vspaglalrp hvtlaagrpf apgsseivvg saiakgfsgt qlgdrlhfaq rdwtvvgifd
      181 aggsgfdsei wgdvdqlmqs frrtsyssmv lripsadgfa rfkadidvdp rltdeakreq
      241 tfygdqskal stfinilgit lstifsiaam igamitmyas vanrvaeigt lralgfkrts
      301 vlaaflleal llgfvggvag lacaslmqfa sfsttnfqtf sdlsfrfvlt paivvktllf
      361 slvmglvggf lpamraarlk ivdalraq
//
LOCUS       WP_175933066             211 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [unclassified Burkholderia].
ACCESSION   WP_175933066
VERSION     WP_175933066.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..211
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22222
     Region          1..211
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mnlhtwwlfv atvfvvsaip gpnmllvmth garhglrrss atmagclsal vlmlavsaag
       61 lgavleawpa mfnalrfaga ayliylgvka wrarvddapa advdavthga aasrmvlfrn
      121 gflvagsnpk ailfaaallp qfinaaeptl pqfgilvvtf aaievswylv yasfgtriga
      181 tlksqsvakv fnrltgglfv gfgammalvr h
//
LOCUS       WP_175933113             201 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175933113
VERSION     WP_175933113.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..201
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22284
     Region          1..158
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrankrqlvv dkatelfskh gfhpvgvdwi iddsgvarmt lyrhfaskde lirevlvqry
       61 dlivgsidaq lqhvvdpver vktifdwyaa wfrtpefagc lferalaefg tayapisdva
      121 iryrrkmvew iaelieealv padtanrlat vfmmlldgat vearafndsa aaarawqaah
      181 alleqamhaa appadgagnp t
//
LOCUS       WP_175933198             238 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: YdcF family protein [unclassified Burkholderia].
ACCESSION   WP_175933198
VERSION     WP_175933198.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..238
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26643
     Region          9..238
                     /region_name="ElyC"
                     /note="Lipid carrier protein ElyC involved in cell wall
                     biogenesis, DUF218 family [Cell wall/membrane/envelope
                     biogenesis]; COG1434"
                     /db_xref="CDD:441043"
ORIGIN      
        1 milfdsfvll figfmlcrkq rrtisiaaga lswllatgwl aapliawtea gvtpvehpdm
       61 hgrttlilig agthrtdtgl qpppdgfari lkvatlyrtc rqqaerctvv msggdpqhhg
      121 dseaavygrq lvaqgvapad lvlepnsrtt yenakftasi lrsqhddari lvtssyqmrr
      181 alldfhrfdi dpqpvyanrr raqtgwlprw rnvvnaelal helvgiaqfh vyrwlgwf
//
LOCUS       WP_175933224             148 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TadE/TadG family type IV pilus assembly protein
            [unclassified Burkholderia].
ACCESSION   WP_175933224
VERSION     WP_175933224.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..148
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=15961
     Region          16..132
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mkrqkqrwgr rrqrgatave faivfpllfm vfygivsfgm iftiqqsltf aasegaragl
       61 syapslaari anatataqnv vswlnvgtpq vvappcsydt stppalycls vtvnyspqsw
      121 itnmpflgtv ltqpltstav vqipqsil
//
LOCUS       WP_175933253             186 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: YceI family protein [unclassified Burkholderia].
ACCESSION   WP_175933253
VERSION     WP_175933253.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..186
                     /product="YceI family protein"
                     /calculated_mol_wt=19465
     Region          23..186
                     /region_name="YceI"
                     /note="Polyisoprenoid-binding periplasmic protein YceI
                     [General function prediction only]; COG2353"
                     /db_xref="CDD:441920"
ORIGIN      
        1 mkvsfsrsml talaaavlva sgaahadvdl akskvsavsk qmnvptegaf kkfsaqvkfd
       61 pakaaqgtaq mtidvasfdl gdkmyndqva gkdwfdakty pqatfvssai apaggnkynv
      121 tgkltikgka etvtvpvtva qngatqtfdg vlpikrstfn vgtgewkdts ivadevqikf
      181 hlvatk
//
LOCUS       WP_175933295             377 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [unclassified
            Burkholderia].
ACCESSION   WP_175933295
VERSION     WP_175933295.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..377
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40330
     Region          1..366
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfsftdeqq qfadalrryl geqygfearq aivrsdagvs daqwsaftdl gltalpvpda
       61 qggfgggpvd mlvvmqelgr alviepywat avgvealria gsgtgddaal leavaqgrkr
      121 lavafhepra rydlyeldtr areqggtyrl tgtksvvqhg aqahawivpa rvdgggiglf
      181 vverdaasak vadyrtidgq raatiafddt parlltggar daaaleqiad yatfllcaea
      241 vgaldelnra tveytktreq fgvpiarfqa lqhrmvdmli haeqarslty laavryangd
      301 adarrkavsa akarvgtaar fvgqqavqlh ggmgvtneva aahlfkrlsi iettlgdtdh
      361 hlariaalpd faqtdva
//
LOCUS       WP_175933319             462 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Burkholderia sp. BCC0801].
ACCESSION   WP_175933319
VERSION     WP_175933319.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0801
  ORGANISM  Burkholderia sp. BCC0801
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Burkholderia sp. BCC0801"
                     /db_xref="taxon:2676291"
     Protein         1..462
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51151
     Region          4..445
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mdifdafhla rlqfaftvsf hivfpaisig masflavlew rllltgdaay kdmyrfwsri
       61 favgfgmgvv sgvvmayefg tnwsgfstva gnitgpllty evltafflea gflgvmlfgw
      121 nrvspkahff atlmvaigtl istfwilasn sfmqtpqgya iqngrivpvd wwkvifnpsf
      181 pfrlahmtia afivaafiva acgawhllhg rrdvpvkrsf smalwillll apvqifvgda
      241 hglntreyql akiaaieglw etehggtaln lvglpdmnae vtryaikvph lgslilthsw
      301 ngeirglkef ppedrpfspi ifwtfrvmag lgmlmlltav lglilrrggr lyearwfqwf
      361 vfcmgpsgil allagwitte vgrqpwtvyg vlrtadsisp igsqqagvsl lifvivyflv
      421 fgtgiyymlk mmkkgpasgv egteslkypg lhnrtldavv ge
//
LOCUS       WP_175933575             469 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Metamycoplasma hominis].
ACCESSION   WP_175933575
VERSION     WP_175933575.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma hominis (Mycoplasma hominis)
  ORGANISM  Metamycoplasma hominis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 469)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Metamycoplasma hominis"
                     /db_xref="taxon:2098"
     Protein         1..469
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54869
     Region          14..444
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 menkiktpnk neepiiqlvd vvkefedktv ldnvnlsink gefitllgps gsgkttilri
       61 iggfewvtrg evkffgkdik dlsphkrdvs tifqdyalfp hlnvenniky glrlkripkd
      121 dipksfynkl kyqqkkwtkk asiemkkldk tmaqyekile nqklpekkrn kyqswiddmd
      181 fkysywenfk dlktenyekr yltrkitnne mnqevseimd lvglkgnekk nvnflsggmk
      241 qrvalarslv iepeilllde plsaldakir qkmqtllrdi qkelkitfif vthdrnealq
      301 lsdriaiird gkveqfaspk dlydypvnkw vanfigesnf fdavfidenk vkfmgkifdt
      361 ihkefepgen ldalirpedv yvtkvkaksk figkiiksty sgsyynyevl vknkiikmet
      421 sinyevgkev yldwykdsih lmkkdikfak elaeqneinn gktteinfl
//
LOCUS       WP_175933592             338 aa            linear   BCT 11-JAN-2025
DEFINITION  serine/threonine-protein kinase [Metamycoplasma hominis].
ACCESSION   WP_175933592
VERSION     WP_175933592.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma hominis (Mycoplasma hominis)
  ORGANISM  Metamycoplasma hominis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Metamycoplasma hominis"
                     /db_xref="taxon:2098"
     Protein         1..338
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=38548
     Region          17..279
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(23..24,26..29,31,44,46,79,95..98,102,104,141,143,
                     145..146,148,159..160,163,180..183)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(23..24,26..29,31,44,46,79,95..98,102,143,145..146,
                     148,159..160)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(27,102,104,141,143,145,163,180..183)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(40..41,71,76,81..84,96)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(159..167,176..183)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mnkikelpgm fvlnkyftdf eligtggfge vysatykkdn krvaikilnc iddsrwteqr
       61 trfineinil kkihssnvvk ilgwhhngne vfyvmelikg qglktiiakn kkidpdtaim
      121 yakqicqgli eihaakivhr dlkpsniiid eetnslklid fgisigestq rvtrnyktvg
      181 svqymapell rgiadpsprs diyafgiilf emlegkvpfn nhddinqimm mhinnelprm
      241 sdvnviipqa lenivircta ksaeqrytdc ielmhdletc ldskrvnekr lelnpskskm
      301 kakrifnskl fniiffttgg flvafivifv vlflkgil
//
LOCUS       WP_175933665             155 aa            linear   BCT 11-JAN-2025
DEFINITION  single-stranded DNA-binding protein [Metamycoplasma hominis].
ACCESSION   WP_175933665
VERSION     WP_175933665.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma hominis (Mycoplasma hominis)
  ORGANISM  Metamycoplasma hominis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Bianco,P.R.
  TITLE     The tale of SSB
  JOURNAL   Prog Biophys Mol Biol 127, 111-118 (2017)
   PUBMED   27838363
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Metamycoplasma hominis"
                     /db_xref="taxon:2098"
     Protein         1..155
                     /product="single-stranded DNA-binding protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=17602
     Region          1..109
                     /region_name="Ssb"
                     /note="Single-stranded DNA-binding protein [Replication,
                     recombination and repair]; COG0629"
                     /db_xref="CDD:440394"
ORIGIN      
        1 mnkvfligrl sakpyknvtp snveysrftm airreyaapn sepvvdfvpc vawrsnatfi
       61 nkyldkgsll lvegtfqssr fnngdgqist syvvsvekiq sletremsen rrknnngkef
      121 niateesnti dnnlennhqp nesndnpfdq ldwdl
//
LOCUS       WP_175933827             610 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Metamycoplasma hominis].
ACCESSION   WP_175933827
VERSION     WP_175933827.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma hominis (Mycoplasma hominis)
  ORGANISM  Metamycoplasma hominis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Metamycoplasma hominis"
                     /db_xref="taxon:2098"
     Protein         1..610
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=70479
     Region          49..>188
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
     Region          <218..>379
                     /region_name="235kDa-fam"
                     /note="reticulocyte binding/rhoptry protein; TIGR01612"
                     /db_xref="CDD:130673"
ORIGIN      
        1 mktalnnyhn flfkvtakkk stiiipiill lcslilcfvf vgtkpapryf nviifaytlv
       61 ailftvlygs lkslnifkdl eqdgieliif skpisrkaii wgkilsfnsl gliwtlfafv
      121 ssiivysqvs kgnmfgylvl lslvahflay tifgyiaali aykvnqkiai tvpiiifapm
      181 aigggfifan ststnenfah yinskykyhr agnevnsevf ylnknddkyy lvpnginnnk
      241 fsdvqnqyln lawkysnssa newqkyswla mpyqfvdifn ienqnifsnl ssdsinnsls
      301 nylyyknqen tiykyklnrn sdllklptle nkikinkyyv pgmlnlnsni dnevnngviy
      361 arknasnfsa sfeednfvya spnnlvgklk wkimsqvlky hkfteaaeef yskvkneisl
      421 kklvkphdik kllletisne vnntnskffn idnvnlavfd phgvrdgrlq seterkiyia
      481 tallyfiyfk dnqgqviksl lksesdktty apsqieikvd gyiyeiggye syepkqqvqe
      541 nkitknkqvv vryelipsnk nylfqtvddv ysierdrkiv nkqfyiliwv vvaiilmman
      601 rflylrkdyk
//
LOCUS       WP_175933868             515 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia ubonensis].
ACCESSION   WP_175933868
VERSION     WP_175933868.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         1..515
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52153
     Region          91..494
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrlpeppaas iaaaalatav alagcatssl dlapeasdrp wqpptsaage ivpgaapaha
       61 praphdytlp atpalaavpp paaldaahay tlpelidlae stnpltriaw ndarnaalav
      121 giaktaylpq lsatamgayq sshgstttpl gtgssdttvh gtisalslqw llfdfggraa
      181 rveaaeqasi vsnvaftavh qqvihdvtia yyryeasrsr alsarqslan adaiaaaara
      241 rlkqgvgtvv evaqatqnra qanlalveas gaesdgylgl vsalgispls kptiaalppr
      301 plppalrasv dsivadaiar rpdlqsayal enanrakvka aqaefmpkvf msastsyssg
      361 gtaitalpai gqqaptvnln gsrygggvfv gvtiplydgg lrsavlmqar ndaesasarl
      421 trtkedavrq ivaaqnalqt slasheaata lvaaaqttyd aalsayrngv gsvtdatlaq
      481 sqllaaknad vdsycgalsa aatlalatgt igsaq
//
LOCUS       WP_175933874             789 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia ubonensis].
ACCESSION   WP_175933874
VERSION     WP_175933874.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 789)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 789)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..789
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         1..789
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85834
     Region          71..771
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msfivaarps rgraalacaa afawpaafaa qpdggradpi qapapqasra aapaptatpp
       61 apveaaagdt ltavsvtaqr qsvdsdtpav iesisrdrid ahtnvnteda lkyapnlmvr
      121 kryigdrnav fagrdfnelq sarglvyadg lllsnllgss yaypprwsli ppddiarvdv
      181 lygpfsalyp gnaigstvll ttrrperlea slstqfftqr yrdgygfads lggnhqtari
      241 anrvgrfwfa lsldrlenng qpmqyaspna gynpklgrav pvtgaaadig pngkprtlvg
      301 aqsierteqi setvrmgyaf tdhvdatltl ghwenhyrqh getflrdaag npvyggnvsi
      361 ggqnmtvapg afapqrgdqe nwlyalglna rldsgwrlsg vvsaydvsrd vlraastvqg
      421 gpgtqfqgdg tgwrtldlka eapevkghtf tfgyhydnyf lrnvtfntad wqagpttsla
      481 svyrgdtrtq alfaqdawrf apgwlatlgl ryerwdvygg algnasgtfg yadrsanals
      541 pkvalqwdat dvwrfrlsfa tgtrfptvge mfqgtisnna ivnnnpnlrp ekaidwdfta
      601 erdvgvgvvr asvfqsdlrd siysqttvsg astvtntsnv drvrvrgvel afsgqnvglk
      661 gfdvdanvsa snaqilsdaa npayvgsrfp riprmranll asyrfdehwl asvgvrysgr
      721 qfntldnsdv npdvyggtss ftvvdlkary rfdrhwvasv gidnltdrry yvfhpypgrt
      781 ffgelkwsl
//
LOCUS       WP_175933907             307 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            ubonensis].
ACCESSION   WP_175933907
VERSION     WP_175933907.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         1..307
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30863
     Region          6..286
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mgalpfdala lgasyallas gftlvfgvlr rvnlaygatv mfglyaairl taplppvaal
       61 vaaplvavaa tlvanlyver lcfaphrgga kvganvtama asfavwmqve easvlllpah
      121 anpfpspfar lpaawqagpl radhaialgc aalatlgcwl lihrtrfgla vravvddaaa
      181 aafmgvdvrr vsarvfalaa algalggcli aglhgqvsam famwatlkgl aaavlggfgs
      241 mpgaiaggla lgavetvlqa rvgaeyrdla snllllavlc vrpgglaslv pgtraraall
      301 graeagp
//
LOCUS       WP_175934004             403 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia ubonensis].
ACCESSION   WP_175934004
VERSION     WP_175934004.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         1..403
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=42532
     Region          10..403
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 mnahtppret rfawrgrrpd gaprrgtvva fdpagaratl aragitvlsl dargaarppt
       61 artreitrft qqlasllqag lplapaleml artrgpdgmp riaaglarei vggrrfaaal
      121 arypsqfgsl yrqlieiget sgalgpvlar iadhrerada qrrklraala ypvavilfal
      181 aitialmlwv aptfrqifdg fgaalpaptr mllalasata awgtpllagv vaaglaarha
      241 irhspalrls lsrhllrmpl vgpmlsrfaa arwcrslatl lgagvplada fttlertagh
      301 pvfeqatari aarvlrgarl adamhaagcf pddvvqpiav aeetgaldtm ltdiaalcer
      361 qldahldtla algepliviv lgalvgslvv amylpilqlg nvv
//
LOCUS       WP_175933991             197 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia ubonensis].
ACCESSION   WP_175933991
VERSION     WP_175933991.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         1..197
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=19185
     Region          1..197
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mkkiammmsa aglafaamna ahaadgtinf tgeivaascg itggngtsvt ggkgaqsidv
       61 kmgkvstdal ggtagggiaa gtainlsldc gstgkglntv kvrfdpasgs gvdgtnnkll
      121 kttgtakgvg igiyntagtl lnlnanetfd aplvkggtee aptytanlal ragyvkngtd
      181 veagtangtl pftltye
//
LOCUS       WP_175934011            1041 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit, partial [Burkholderia
            ubonensis].
ACCESSION   WP_175934011
VERSION     WP_175934011.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ubonensis
  ORGANISM  Burkholderia ubonensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Burkholderia ubonensis"
                     /db_xref="taxon:101571"
     Protein         1..>1041
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
     Region          1..1040
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnvsrffvdr pifagvlstl illagvisly flpiaeypev vppviavnaq ypganpkvia
       61 etvaspleeq ingvegmlym qsqangdgnl tltvtfkvgt dpdkaqqlvq nrvsqafpkl
      121 padvqrlgvt tvkssttqti avhlvspnnr ydvnylrnyg ilniksrler ipgvgevriw
      181 gggdysmriw ldpqkiaarg ltatdvvnai reqnvqvaag vigsqpmrgn vplqlsvntr
      241 grlqsedefg aiviktaqag gvtylrdvah ielgasdygl rsmvdgkpav gfgifqapgg
      301 naltisdkvr eamaeikadm pagvdyrivf dptkfvrssi aavvstllea ialvvvvvil
      361 flqtwrasii pllavpvsiv gtftlllmfg fsinalslfg mvlaigivvd daivvvenve
      421 rniarglspk datylamkev stpiiaialt lssvfiplaf mpglsgefyr qfaltiaist
      481 iisafnsltl spalsalllk ghgdpedgat rfirrylggf fdafnrffkr gstaygtgld
      541 glighkalvm glyavligit ilvgkivptg fvpaqdkeyl vgfaqlpnga sldrtekvvn
      601 tmadiamkqp gvesilefpg msvnglmnss sagtvfitlk pfdkrgdkal saqaiaealn
      661 rqyagikesf vaifppppil gfgtlggfkl qiedrgavgy akladatndf ikraqqapel
      721 gplftsyqin vpqlnvdldr vkakqlgvsv tdvfdtmqiy lgslyvndfn rfgrvyqvrv
      781 qadapfraya edigqlktrn aagemvplss lvnvtptfgp emvvryngyt aadinggpap
      841 gfssgqaqaa ieriahetlp rgvrfewtdl tyqqilagds aiwvfpisvl lvflvlaaly
      901 esltlplavi livpmsilsa ltgvwltqgd nniftqiglm vlvglsakna ilivefarel
      961 ehdgrtplea aieasrlrlr pilmtsiafi mgvvplvtst gagaemrham gvavffgmlg
     1021 vtlfglmltp vfyvvlrtla g
//
LOCUS       WP_175934206             610 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Metamycoplasma hominis].
ACCESSION   WP_175934206
VERSION     WP_175934206.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma hominis (Mycoplasma hominis)
  ORGANISM  Metamycoplasma hominis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Metamycoplasma hominis"
                     /db_xref="taxon:2098"
     Protein         1..610
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=70505
     Region          49..>188
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
     Region          <218..>379
                     /region_name="235kDa-fam"
                     /note="reticulocyte binding/rhoptry protein; TIGR01612"
                     /db_xref="CDD:130673"
ORIGIN      
        1 mktalnnyhn flfkvtakkk stiiipiill lcslilcfvf vgtkpapryf nviifaytlv
       61 ailftvlygs lkslnifkdl eqdgieliif skpisrkaii wgkilsfnsl gliwtlfafv
      121 ssiivysqvs kgnmfgylvl lslvahflay tifgyiaali aykvnqkiai tvpiiifapm
      181 aigggfifan ststnenfah yinskykyhr agnevnsevf ylnknddkyy lvpnginnnk
      241 fsdvqnqyln lawkysnssa newqkyswla mpyqfvdifn ienqnifsnl ssdsinnsls
      301 nylyyknqen tiykyklnrn sdllklptle nkikinkyyv pgmlnlnsni dnevnngviy
      361 arknasnfsa sfeednfvya spnnlvgklk wkimsqvlky hkfteaaeef yskvkneisl
      421 kklvkpydik kllletisne vnntnskffn idnvnlavfd phgvrdgrlq seterkiyia
      481 tallyfiyfk dnqgqviksl lksesdktty apsqieikvd gyiyeiggye syepkqqvqe
      541 nkitknkqvv vryelipsnk nylfqtvddv ysierdrkiv nkqfyiliwv vvaiilmman
      601 rflylrkdyk
//
LOCUS       WP_175934239             970 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175934239
VERSION     WP_175934239.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 970)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 970)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..970
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..970
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=107961
     Region          <115..565
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mtslsdelqq hqpqqqsepa paltdqtala pglmvkvrde lwlvtsvtqs tdgyllkvrg
       61 lsdyvrdtta sfytalddvk vfdpakvevv adhspgyrtt rlwlettlrq tpvplyqeql
      121 svaedmlmdp ldyqltavrk alsddnlrpr vliadavglg ktleigmils elirrgrger
      181 ilvvtpkhim eqfqqemwsr faiplvrlds agiqrvqril pasrnpftyf prvivsmdtl
      241 ksgkyrayle kvrwdavvid eihnatnvgt qnnelartla pttealllas atphngdpes
      301 fkeilrlldp tavlpdgtid qeavarllir rhrhsqevas vvgekwaerr epinipveas
      361 aeenavaael ehvwmrnnpa sdrlfpwtli kaflsspaal eetiqnrlkn pkldttqraa
      421 ldrlqqlnak vtrensnkya alvnylqdig iaknsptrvv vfservatlh wlqqnltkdl
      481 klgkeqvqvm hgglsdeeqm rlvdefkred sklrvlvtgd vasegvnlht lchnlvhydi
      541 pwsliriqqr ngrvdrygqt eppqiaalll dtkqggyvge lhvltklinr eneahrllgd
      601 vgslmgkhtv kgeeeeirkv iqnqlafddv vkapqdiass qpqtaeelda fwmsgfglid
      661 dalpeqpalt psnrggqpsl ypseiayled alneafhaap erplaaggvg yqlhkngvae
      721 lkppedlrrr levlpqdylt drkvrenfql atthargdev lrnartgddg stwpkshflg
      781 plhpvtdwaa dralaslsag qipaiagdva eptvllmgtl tnkrgqvvsr afvtvagmrp
      841 dtiadpvewl rgvglterai npggltlped taeliegavl laggqlqpmm saarkhader
      901 iahwvqrted wedaregaqt tlrltrsenl iaqekalias lqpdrelirp lvlvlpsttt
      961 nntadthqeh
//
LOCUS       WP_175934223            1027 aa            linear   BCT 11-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Metamycoplasma hominis].
ACCESSION   WP_175934223
VERSION     WP_175934223.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma hominis (Mycoplasma hominis)
  ORGANISM  Metamycoplasma hominis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1027)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1027)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1027)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1027)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Metamycoplasma hominis"
                     /db_xref="taxon:2098"
     Protein         1..1027
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=120099
     Region          29..1025
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mekyniiven endtvvseyk plankakdyq teselesqfi smlknqgyey lnihneedli
       61 nnlrqqiell nkinfsdnew kkffnenian knfsikdksr iiqedyrqll trddgshkni
      121 ilidkdnihn nklqvinqye eetgnyknry dvtilvngip mvhielkrrg valkeafnqi
      181 iryqrdsfwa snglyeyvqv fvisngantk yysnttrlqh vnkksdmids ktsksfefth
      241 fwsdsknnpi hdlidftstf fskhtilnil tkyciftsee mllvmrpyqi vavekiinki
      301 nishnykkyg siaaggfiwh ttgsgktlts fktaklasql pyinkvifvv drrdldyqtm
      361 keydklekga ansnrstlil qrqlesndpn kkiiittiqk lsifiknnrn hpvfdkevvl
      421 ifdechrsqf gsmhtavikn fkkyylfgft gtpifaanin ksspeviktt eqafgqklht
      481 ytiinaindr nvlpfkieyi ktidvdksln dkedqkvrdi dresvfldqr riklvveyil
      541 khfdqktrrn sniiyshsis dnldktikrn vsgfnsimav ssiemakkyy lefknqlaqd
      601 pknnlkiali ysygvntees ygglideedn entlqlskpd rdflddaikd ynnmfntnfn
      661 segeqfqmyy kdvslklknk dldmlivvnm fltgfdaptl ntlwvdkklr ehgliqafsr
      721 tnrilndkkv ygnivcfrnl eketdqaisi fgdgeasgiv kiknfvdyyy gyndsqqvhh
      781 ngycdyiqkl nnefplnnwn viseqknkef iilfgkvlkl knilasfdef igkeilnvrd
      841 fqnysskyld ikdefknkyk eeiasinddv ifetellkty evnidyilqk veefrgktit
      901 einnlrseis lasssspelr skkqliekfv stinnneqdi ptkfqefmel ekkkeldkii
      961 seenldfdkt hkfmddsfel geiktagsei gdllpkmplf gskgkersik kkavlekfen
     1021 yfqkfyi
//
LOCUS       WP_175934299             370 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease signature motif containing protein
            [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175934299
VERSION     WP_175934299.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10052677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..370
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40423
     Region          270..323
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(296,298..300,302,313..314,318..319,322)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 mttfhtllqa ltsvdaladf drqaaidagl rpcqvrdlar vhetyftptr crkqqrlald
       61 aaregglsld qlvyvekqla rvdteleqwr lrrellavrg nydalkrrak ellpppeptp
      121 pqptvrfsas rlgmrtlvlv gperdiadle hylrqglnpd lpagpqlltr fvalirgqla
      181 aatgkpgeai ppavapaapr pvlavpldth vailgghgdd tvlglsdgtt itgaeylnll
      241 aenggvaeaa lfhpqegpvn lyrnerlank kqrdlmrlay ssclvpgcrh gsdnceshhv
      301 eawarggetn ianlaplcsy hnrvndddpr aarrgrisli dgsatwispr gypapntrhr
      361 ygamhtlfaa
//
LOCUS       WP_175934057             282 aa            linear   BCT 11-JAN-2025
DEFINITION  ribonuclease III family protein [Metamycoplasma hominis].
ACCESSION   WP_175934057
VERSION     WP_175934057.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma hominis (Mycoplasma hominis)
  ORGANISM  Metamycoplasma hominis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Nicholson,A.W.
  TITLE     Ribonuclease III mechanisms of double-stranded RNA cleavage
  JOURNAL   Wiley Interdiscip Rev RNA 5 (1), 31-48 (2014)
   PUBMED   24124076
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Gan,J., Shaw,G., Tropea,J.E., Waugh,D.S., Court,D.L. and Ji,X.
  TITLE     A stepwise model for double-stranded RNA processing by ribonuclease
            III
  JOURNAL   Mol Microbiol 67 (1), 143-154 (2008)
   PUBMED   18047582
REFERENCE   3  (residues 1 to 282)
  AUTHORS   MacRae,I.J. and Doudna,J.A.
  TITLE     Ribonuclease revisited: structural insights into ribonuclease III
            family enzymes
  JOURNAL   Curr Opin Struct Biol 17 (1), 138-145 (2007)
   PUBMED   17194582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426290
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Metamycoplasma hominis"
                     /db_xref="taxon:2098"
     Protein         1..282
                     /product="ribonuclease III family protein"
                     /EC_number="3.1.26.3"
                     /GO_function="GO:0004525 - ribonuclease III activity
                     [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=32942
     Region          17..266
                     /region_name="Rnc"
                     /note="dsRNA-specific ribonuclease [Transcription];
                     COG0571"
                     /db_xref="CDD:440336"
ORIGIN      
        1 mgieewqeyi yqieytigyf fknkfllyqa ftrssysnqy gvennevlef igdsvlsfcv
       61 vqlmaeefgf lksasqyynk yedleeycli anknesdftd lknqivsnkt lakkinklgf
      121 akylvlgdnd krnnvanqds vkadlfeaii gaiaidsgwd ikrlkniiik mldiehffrd
      181 vdcrekrpdk fklenaintl kelaergecs mpiyqisekp iiddngkqww hcrcnvnfrn
      241 lqwmglwtky tegygtskkl akkmaayivl cdhyglpney kn
//
LOCUS       WP_175934343             769 aa            linear   BCT 11-JAN-2025
DEFINITION  MMPL family transporter [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175934343
VERSION     WP_175934343.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 769)
  AUTHORS   Viljoen,A., Dubois,V., Girard-Misguich,F., Blaise,M., Herrmann,J.L.
            and Kremer,L.
  TITLE     The diverse family of MmpL transporters in mycobacteria: from
            regulation to antimicrobial developments
  JOURNAL   Mol Microbiol 104 (6), 889-904 (2017)
   PUBMED   28340510
REFERENCE   2  (residues 1 to 769)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..769
                     /product="MMPL family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=82581
     Region          30..696
                     /region_name="YdfJ"
                     /note="Predicted lipid transporter YdfJ, MMPL/SSD domain,
                     RND superfamily [General function prediction only];
                     COG2409"
                     /db_xref="CDD:441964"
ORIGIN      
        1 mfyswgryay rhrkiipvvv vvlilllqvf fgaklgerls gegwedprad sttaavieqd
       61 tfgrdnsgdv ivlvsapngv qdpavfdaan rqisalkadf pneiahitsy fdhpnpqqvs
      121 sdgtkafaai glagdgeqtl kdfrtiqpal esielpdgas vqiagatava daldkgmadd
      181 iaraekiglv fiavillfvf ggvvaagmpl ivgilsiigs lsllailaky qqvnifsqsi
      241 itllglglai dyglfmvsrf reeldqgkpv edavasttat agktvffsal mvgvalsgll
      301 mfpqaflksv aygaisavvl aavisvtmlp slfgmlggni dkwsvrrrts rkgrsvedtv
      361 wyripswamr hakgvvvgvt avlilltvpi akisfggine tylppdqatr qvqdefneef
      421 pqfrtdpikl vvagatneql idvyvqarqi eglaaplkpa hptqdgitvl sapladrngg
      481 advvkqlrni daevdtyvag tpamevesie allerlpwma lymvlatfll mallfgslil
      541 pakavimnvl gigatlgflt lvfvqgvgag alnftpgplm spvlvliiai lyglstdyev
      601 flvsrmvear degaptdrai kegtahtggi itaaaaimiv vaaafalsdi vmmkyiaygm
      661 ifslaldati irlllvpavm hllrednwwa pkwvqrtass lgdgsrapaa rprgedavad
      721 mvvdtqpyrs gvsveedttl vpfdelirri dernrrdalg qlkkkeler
//
LOCUS       WP_175934404             280 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfurtransferase [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175934404
VERSION     WP_175934404.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..280
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30514
     Region          22..276
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 msvfvsaael fdtiqsghkh tviaalwepk egkawskfqs ehiptalfcd pssqlaglpg
       61 rkngrnplpp fdvvekavae wgieegrptf vydggnglfa arlwwvlrwa gvedvqildg
      121 gfanwdangy ptvagpggmv vprgmeleqg klptasidev ksfsgmlida rgqrrfqgrr
      181 evldlraghi pgalnlpved ffdaethrvk dddyirdrfa qvgithnssp ddaitysgsg
      241 nhsalllaam ehaglpvlrh yvggwsqwsa dpenpvstql
//
LOCUS       WP_175934477             482 aa            linear   BCT 11-JAN-2025
DEFINITION  serine/threonine-protein kinase [Corynebacterium sp.
            Marseille-P4321].
ACCESSION   WP_175934477
VERSION     WP_175934477.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..482
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=51444
     Region          22..291
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(22,46..47,76,81,86..88,90,102)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(29..30,32..35,37,50,52,84,101..104,108,110,160,162,
                     164..165,167,176..177,180,197..200)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(29..30,32..35,37,50,52,84,101..104,108,162,164..165,
                     167,176..177)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(33,108,110,160,162,164,180,197..200)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(176..184,193..200)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mmehgfsshq wdglvehlts qgyelgevag rggmgvvlka rdmhlgrdva ikaintnlig
       61 eqrsidrfnk emqtmaqlrh paivqvyqgq vapggvpyfa meycpgptla daldrttqry
      121 svaqtvkilt piasaldylh npddpgragg sltepivhrd ikpaniilqp rgamltdfgv
      181 shvadnprvt qeghfvgtpr ymapemfkpg edllapeptp asdnyafalv alemvsrqql
      241 antmsdvawr gdrpldyler vpasevftra ldndpakrfp tagafleale qsrlstaprt
      301 dpepnrtpdq apdqapdqap dtptprrrgw kkpvvatvtv aalaaaggly vfggeqpwaa
      361 peapiaaafp qlvaehqgga gwagttctag epegaqrakv sctgpgvsfv vadygsggqr
      421 aaavpadgle eftsarctir sgqlpgasdn ayavvleapr dryailvagp daqrdrlnlp
      481 vc
//
LOCUS       WP_175934512             342 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA thioesterase [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175934512
VERSION     WP_175934512.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..342
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37319
     Region          20..163
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
     Region          182..323
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 madtpetapa atvaeerspq ltlrfmaspt dvltagshgv sggrvlewid kaayacaaqw
       61 sgtycvtayv ghihftrpip sghivevrsr iamtgrtsmh ivnevlsadp regvftracd
      121 clvvfvakdp etgaptpvps fhptdseeir vaeaaksrig lrkaieeeml sqtytddsta
      181 priihrfmak ptdvnwggnv hggtamewid eaglactmew sgertvavya ggirfykpvh
      241 igdlievdar ltrtdsrsnh vsvhlragdp rggrdalena ihatftyigi dvdgnplpar
      301 qftpvtdedk rlwehtqtlk dlrgqyepvp lvepqpaaqr ld
//
LOCUS       WP_175934578             462 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175934578
VERSION     WP_175934578.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..462
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49654
     Region          34..450
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(43..44,47..48,51,91,149..150,152..154,157,177,
                     180..181,184,273,276..277,280..282,285,319,323,377..378,
                     382,386,402,405..406,409..410,413)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mtavgnhptp ppstsanpaa irettreerr rvriastigt tiefydfyay ataavavfpf
       61 lffpksesst vallssfatf glafiarplg silfghfgdk vgrkatlvga lltmglatfi
      121 igllptyaqa giwapallal mrfcqglglg gewsgaalls tetaakgrra wagmwpqlga
      181 pfgfflangl flilvtvlgh tsgdfegafm rwgwripfll sivmvaiglw vrlqveetpv
      241 fqqveqndqk aasplaevfk tawkpliqgt fimvgcytlf yivttwflsy gigsaeegvg
      301 lgiayptflk lqlvcifgfm agipvaahla dtygrrpvlg ltsvaiivyg lsfkwllnpe
      361 tftmislgif lfigmilmgf ifgpmsailp elfpsnvryt gsgiaynvss ilgaaiapfi
      421 atalnakygp qavgiylvvv taislvaivt apetkdkemh ei
//
LOCUS       WP_175934507             299 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter permease [Corynebacterium sp.
            Marseille-P4321].
ACCESSION   WP_175934507
VERSION     WP_175934507.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 299)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 299)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..299
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30237
     Region          18..269
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mswlasawdt ttelltldfv qvtlvacvll gilsgvmapl ivlrqmsfsv hatselalmg
       61 asaallfgln vglgavagai vaavvlaalg frgqqdsavg vvmsfgmgls vlfihlypgn
      121 snralslltg qivgvsgqnl imlavtallv vaavvvlwrp mlfasadpvm aaacgvrvrt
      181 mslifavlvg iasaqsvqiv gallvmslli tpgaaaaqit anpvhavwws vlfaevsavg
      241 gmilslapgv pvsvfvafis fgiylvcrli grvrgrrirv aagrsgaggg agqsgagtl
//
LOCUS       WP_175934587             355 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease signature motif containing protein
            [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175934587
VERSION     WP_175934587.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10052677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..355
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39089
     Region          256..308
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(281,283..285,287,298..299,303..304,307)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 mtfdellgal lgaglealag fdrdaalrag lnptqvrawe rvhhayygst napkqqaral
       61 sealesgksl dqlayiesri ahvdnpgerr elrltllrvr gnfdalkrra aeivpkperk
      121 apddalrtsk syqgksrlsl tadddviadm vaaarvklds rapeskqmak nliaafyagg
      181 vtravkrpiv gvplpdcirv lrhegdetif gldngttmtg aellplllgd tlefalfhpq
      241 sgpvnlyrgs rhanskqrdl armanpvcpf pdcgrgaihc ethhvtawkh ggetnvgnlv
      301 plcryhnrvn dddrhrrkrg hieiirgrgi wvsprgtpva npyhpygmmq llfdg
//
LOCUS       WP_175934599             334 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175934599
VERSION     WP_175934599.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..334
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=33949
     Region          7..318
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mpvsnavlvv pdisfdgsvd lgaaeligaa savgtpvvlt tnaahaeelg rlgaevvvtv
       61 dvdkqvqsia lidatvaafd tyhpvaalfa htvrgrdvag gvavragkal ltdatdvrrd
      121 degivtdhqn yggafsataa athsapvitv rpgaierrae paagavgtlt vepsgrrgat
      181 iesvtpvert strpdlvtae kvvaggvslg dadmfedlvg gladalgaav gatrsavded
      241 qvgyeaqigq tgvmvspkly igvgisgavq hlvgmqtsdv ivainndeda pifdiadfgi
      301 igdifdvvpd likeiearte dgieprtepg kaqs
//
LOCUS       WP_175934608             184 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Corynebacterium sp.
            Marseille-P4321].
ACCESSION   WP_175934608
VERSION     WP_175934608.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..184
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19943
     Region          7..180
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mrseqsrave krksilraat elllseglkg vthrqvasaa gvpvgsigyy ystrekliat
       61 cfeqlaatrq vayenamsgr vdltdpvqfa esvvdviscg rphrtrelss afidaqregg
      121 eveqlvertl tqlrsmltem mgragvegit ssrvlqmvig talteehpta pvaavtdllr
      181 laeh
//
LOCUS       WP_175934619             232 aa            linear   BCT 11-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Corynebacterium
            sp. Marseille-P4321].
ACCESSION   WP_175934619
VERSION     WP_175934619.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..232
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=24073
     Region          105..192
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mntavrplke lgwlalcwva fttaasllmq pphgllrpll vvacalpapf iaaraagrhe
       61 rdvlgparrv rwdvltrslv vaalvygalg lwrygqgpgg vdkqmllvla ivplqaaaee
      121 avfrgalpqi igawvraplv ayglpallfs lghgdvlgal afgacaaala wytggleasf
      181 alhvganlaf ylpiysgapv hlgpdtlaav vaaggtaawl waskgyaqrn gn
//
LOCUS       WP_175934668             268 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD-IIA family hydrolase [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175934668
VERSION     WP_175934668.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..268
                     /product="HAD-IIA family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28705
     Region          3..247
                     /region_name="HAD_Pase_UmpH-like"
                     /note="UmpH/NagD family phosphatase, similar to
                     Escherichia coli UmpH UMP phosphatase/NagD nucleotide
                     phosphatase and Mycobacterium tuberculosis Rv1692 glycerol
                     3-phosphate phosphatase; cd07530"
                     /db_xref="CDD:319832"
     Site            order(7..11,39..42,145,178,202..204,207..208)
                     /site_type="active"
                     /db_xref="CDD:319832"
ORIGIN      
        1 misyltdmdg vlhregdvip gaqefitalr ehdiefmvlt nnsmqtprdl saklrrmgld
       61 ieperiwtsa tatakflsqq ageasayvig eaglttalhe mgwiltdadp dfvvlgetrt
      121 ysfealttas nlirggsrfi atnpdltgpg pngvvpatgs vasmitavtg qrpyyvgkpn
      181 pvmmrsalnn igahsehtvm igdrmdtdvk agleaglrtv lvrtgisdde eiakypfrpt
      241 avvdsvaala ervhdpfgdg fyadaegd
//
LOCUS       WP_175934708             323 aa            linear   BCT 11-JAN-2025
DEFINITION  ROK family protein [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175934708
VERSION     WP_175934708.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..323
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=34334
     Region          9..315
                     /region_name="ASKHA_NBD_ROK_SgGLK-like"
                     /note="nucleotide-binding domain (NBD) of Streptomyces
                     griseus glucokinase (GLK) and similar proteins; cd24061"
                     /db_xref="CDD:466911"
ORIGIN      
        1 mvemergltv gfdiggtnar aavvdaegai idarhtatph dgpaltrtiv dtvariredy
       61 didavgvala gfldpecevv rfaphlawrd deplrrelqd aiglpvrleh danaaawgey
      121 kygaaremdt wvffavgtgi gatlmhegei yrgafgtape fghitvvpgg rvcscgkqgc
      181 leryasgtsl vdcaidkatk ggyrhsglyr avvekratgh dimnaaregd elglaavdsf
      241 atwlgrgfai vadvldpahi vlggglseda dlflthavas meenivgsqy rphpqihcae
      301 lgpragmigv adlargaedq krt
//
LOCUS       WP_175934804             343 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175934804
VERSION     WP_175934804.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..343
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38564
     Region          55..335
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mttrethdet apardwkpdv lggdfaqlvl pqgkdpdtgk kvrgvlvrht psgeadtdkp
       61 avlwvhgmsd yffqdhvaee faeqgypfyg ldlrrcgrah qkgerfhftl dmeryfdelt
      121 daldiiaeqh gaviplahst gglivplwad ylrrerpaeh aklagiilns pwldlqfnpl
      181 lvkilrpvvn vfgaifpslp lpggglgayg qsihkdehge wefntkwkpi eghrkyfgwi
      241 ravlkaqrei hsgevetgvp tltlcsshsy lgeeyspaad tadtvldveq iqhwapqlaq
      301 dhttevidga rhdvflserh areaafkasf ewldeltkrq pln
//
LOCUS       WP_175934838             229 aa            linear   BCT 11-JAN-2025
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175934838
VERSION     WP_175934838.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..229
                     /product="energy-coupling factor ABC transporter
                     ATP-binding protein"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25467
     Region          4..226
                     /region_name="EcfA2"
                     /note="Energy-coupling factor transporter ATP-binding
                     protein EcfA2 [Inorganic ion transport and metabolism,
                     General function prediction only]; COG1122"
                     /db_xref="CDD:440739"
ORIGIN      
        1 mpliefigas vtydgdevla pltvsfdeqr vgiigsngsg ksttvrming lvepstgqvl
       61 ydgsdptreg kevrkrvgfv fsdaesqivm prvrddvafs lrrfklsree vrqrvdnvlh
      121 rfeldhladn sphtlsggek qmlalasvlv iepdtiiade pttlldlrnr rriirefeal
      181 dqqlivvthd lemlrgfdrv lciddahlaf dgapddaiaf ytdlmdakp
//
LOCUS       WP_175934850             425 aa            linear   BCT 11-JAN-2025
DEFINITION  uracil-xanthine permease family protein [Corynebacterium sp.
            Marseille-P4321].
ACCESSION   WP_175934850
VERSION     WP_175934850.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..425
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43778
     Region          13..414
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 msetfgwslh gdgrhvrpga vvapeerlsw prtigigmqh vvamfgatll vptltgfpvn
       61 ttllfsglgt iifllitrnk lpsylgssfa fiaplsasqq ygigaqlggv lvtglaliav
      121 galvhvagkr vidavmppvv tgaivaligf nlaptavdnv etqpgvagvt laaivlvtva
      181 trgmlsrlsi ligvligway aaltgglsdd alatigaasw vglpqfhtpe fdvsailvtl
      241 pvlvvliaen vghvkavsem thrdldylqg raligdgiat tlaggfggsg tttyaenigv
      301 maatkvysta aywvaaifai ilafipkfga viftipagvl ggaclvlygl igmlgvriwq
      361 dnrvdftdpv nltaaavali vgignltlev gpvtlegial gsvgiiviyp lmrwvfgtvg
      421 egqyr
//
LOCUS       WP_175934869             415 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent RNA methyltransferase [Corynebacterium sp.
            Marseille-P4321].
ACCESSION   WP_175934869
VERSION     WP_175934869.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..415
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=43574
     Region          9..408
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 madalergqr vqlhvramah ggegiadapd grvvfvpgai pgdvvdatlg rvkkrwarae
       61 satvvkpspd riepgcpaaa agagccdysh irpeaqlrlk aevltgqlrs lagsssvlag
      121 lkgpgdfdav qlqpatgwrt rvrlgvdskg ragmrkarsn dvvagivctq pvpglldglv
      181 gpdaqrftpg aelvavmdsd garhvvetaa prrgqrveha erviegdgev vqrvrghsfr
      241 fpptafwqah vnapeaysnf iaatelpqea prvgwdlygg vgafvpaiha algrgevhtv
      301 dmsdsaarsn aaladadwhy hraigqegva qlprpglvvl dppragagqq vveavatvnp
      361 arvvhvgcdp atfardaayf gqqgyvierm vlidafpsth hfevlaalap assrg
//
LOCUS       WP_175934931             308 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Corynebacterium sp.
            Marseille-P4321].
ACCESSION   WP_175934931
VERSION     WP_175934931.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..308
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33170
     Region          6..220
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtkealvvrd vvkrygdkta vagltlsanr gellallgpn gagktttiem cegftrptsg
       61 dirvlgmdpv aqpqkvrdri gimlqgggsy sgikvremlk ltasynanph dpdwlidllg
      121 lrgvantsyr rlsggqqqrl slalamigrp elifldepta gmdaqsrhav wdivqamkrd
      181 gttvvltthl mdeaetladd vviidhgqlv aqgspaelts hsefpvvsvh taapldeqll
      241 idalaphhlt aealrplnyv vrgdarpevi savaaeaarq gvlirelnvs hrnledvfld
      301 ltgkelrs
//
LOCUS       WP_175934939             544 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease signature motif containing protein
            [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175934939
VERSION     WP_175934939.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10261582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..544
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59740
     Region          <170..396
                     /region_name="DUF222"
                     /note="Domain of unknown function (DUF222); pfam02720"
                     /db_xref="CDD:397024"
     Region          390..443
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(414,416..418,420,431..432,436..437,440)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 maqeleklva tmahamlrin difsdpstls fadvhecmet feaamapkav idaafafice
       61 rdeagryvgs khattylqrc lglqpgqayd rlaagrdmfg epeieepeve gpapeedcde
      121 pfdlfggaag deddaaasee earreeerkk eearrkdear rkqeqarkda aevgeaklri
      181 irleldklvd aakgarnrly aaamheaker dakdlrsllr rwvneenakh vdpadpnagm
      241 ekrsarvldq nadgtfdili kavagdaalf kaitdkglap hsnldedapd yrrpeqrryd
      301 efvrilkhfd tcerpagggc asvvvsvtld qiadadastl fqtncgveln afdlvrlgvg
      361 gaadfvltld nathlplhlh rsrrtaslaq riallalqgv cawagctapi secevhhida
      421 wiqgggtdin nlaalcrhhh rmnndfkdhr sntshidrcp etgrpgvrvp gstgvtlnss
      481 dpaersaanq lrkhsvraak ppsppppesi plphrpqepq pappprepaq pppwardqdp
      541 yppf
//
LOCUS       WP_175935065             472 aa            linear   BCT 11-JAN-2025
DEFINITION  hemolysin family protein [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175935065
VERSION     WP_175935065.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..472
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=50647
     Region          1..457
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mdiflsilsl lafvlltast glfvaiefam tgmerstvea hvkergdkta kaiyrdhtnl
       61 sfvlsgaqlg itlttlaagy laepvlgqff tpvleavgln asasrtvalv lalvvatfls
      121 mvfgelvpkn laitnplata rvvvppvhwf ntafkwfinf lnaaanwvvr klgiepadel
      181 asarsaqelg amvrssaeag gldaataavl drslrfgdtt aeevmtprst iesldaddtv
      241 adlialaret ghsrfpvrrg dlddtlgvvh ikdafsvdrd erattklsel arripfvpgt
      301 ldgdsvlnrv rsagsqvvlv adeyggtqgl vtiedlveei lgevydeydd rdserdfiry
      361 gtswevsglv rldelaqrtg fnapdgpyet lgglimaalg ripelgdevv ltdqaatfqe
      421 efasgvagdw laqvsemdgr ridramlrpi tpeqaqdqta raehaasagg ea
//
LOCUS       WP_175935080             302 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175935080
VERSION     WP_175935080.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..302
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=33735
     Region          60..289
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mtpparrdgt pdtperdepf ypsyakpakk qnvhlnerre naepnplddn wwddapeknd
       61 gvrlqkvlaq agvgsrrhae amidqgrvev ngktvnvqgm rvnpnvdiir vdgarinvne
      121 eleyfafnkp rgvhttmsde mdrtsvgsyl sertasgqrl fhvgrldadt eglllltndg
      181 elanrlthps yevsktylat vlgeadnklv relkqgield dgpakvdfaq ivdvyngqsl
      241 irvelhegrk hivrrllkas gfpvqrlvrt kvhtvqlgel kpgrmralna selaslfkev
      301 gm
//
LOCUS       WP_175935094              58 aa            linear   BCT 11-JAN-2025
DEFINITION  Trm112 family protein [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175935094
VERSION     WP_175935094.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 58)
  AUTHORS   van Tran,N., Muller,L., Ross,R.L., Lestini,R., Letoquart,J.,
            Ulryck,N., Limbach,P.A., de Crecy-Lagard,V., Cianferani,S. and
            Graille,M.
  TITLE     Evolutionary insights into Trm112-methyltransferase holoenzymes
            involved in translation between archaea and eukaryotes
  JOURNAL   Nucleic Acids Res 46 (16), 8483-8499 (2018)
   PUBMED   30010922
REFERENCE   2  (residues 1 to 58)
  AUTHORS   Bourgeois,G., Letoquart,J., van Tran,N. and Graille,M.
  TITLE     Trm112, a Protein Activator of Methyltransferases Modifying Actors
            of the Eukaryotic Translational Apparatus
  JOURNAL   Biomolecules 7 (1), 7 (2017)
   PUBMED   28134793
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006712
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..58
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..58
                     /product="Trm112 family protein"
                     /calculated_mol_wt=6394
     Region          3..54
                     /region_name="Trm112"
                     /note="RNA methyltransferase activator Trm112/YbaR
                     [Translation, ribosomal structure and biogenesis];
                     COG2835"
                     /db_xref="CDD:442083"
ORIGIN      
        1 msldpklldi lvcpkdkgpl tykedeqllv nerlgvayri dgdipvllid eaqpypsn
//
LOCUS       WP_175935116             545 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Corynebacterium sp.
            Marseille-P4321].
ACCESSION   WP_175935116
VERSION     WP_175935116.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 545)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..545
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59266
     Region          15..544
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mttayrpgaq panqqvvlev rnlrlgtleg teilhgidfd lhrgeivglv gesgsgktta
       61 glaamghfra glslydgsvt lhthagetvd vldldedglr elrgarvayv pqdpalslnp
      121 tmrvgeqire vldihgfdgd avarvrevmr dvdlpdtdey larwphqlsg gqqqrvgiam
      181 afamypdvli ldepttgldv stqahvleti rtmtqrndva slyithdlav vaelsdrvvv
      241 mlrgdiveeg pvdtvlydpq hpytekllas ipdlqgrkdi tghgrpapfg ggseepapll
      301 avrdlemayg dnkvlhginl tleqgesill lgesgsgktt larsvaglnp dytgevalrg
      361 evlehgsrkr tvgqrqdiqy ifqspfssln prrtigeslt vplqmsgels rseqrqaved
      421 vleavqldrs ffdrrpgdls ggerqraaig ralvnapsvl vcdeitsald vsvqasilrl
      481 laelrqergl smlfvthnia larhtatrva vlnkgvivde gpvdevlenp qheytqqlla
      541 nipef
//
LOCUS       WP_175935128             700 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase RecG [Corynebacterium sp.
            Marseille-P4321].
ACCESSION   WP_175935128
VERSION     WP_175935128.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Singleton,M.R., Scaife,S. and Wigley,D.B.
  TITLE     Structural analysis of DNA replication fork reversal by RecG
  JOURNAL   Cell 107 (1), 79-89 (2001)
   PUBMED   11595187
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..700
                     /product="ATP-dependent DNA helicase RecG"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=75736
     Region          14..700
                     /region_name="RecG"
                     /note="RecG-like helicase [Replication, recombination and
                     repair]; COG1200"
                     /db_xref="CDD:440813"
ORIGIN      
        1 mlgfkdnrel aevipakqak aigkalgitt cgellahypr ryvhygtgad lsdvlpgdtv
       61 tvigtvthsq tipsakqpkr pitrvtvhdg ktefqvtffg sayarnvlkp grramftgky
      121 dtfrgqhqlq hpdfvlldgp teatgslrql ahfgdleeim sgrewlpiyp tvkglttwti
      181 mgavhavlqs lppieeplgf tpigmlplns airqihepgp egpakakyrl kydealsval
      241 amgvrrhdad aqnapalpfv rdgdqqalld nlpfplttgq kevvaditad mrgttpmsrl
      301 lqgevgsgkt vvalvamlqa vdngaqcall aptevlvlqh arsltltlmr aglptrvval
      361 tgsmpaaqkq eallkivtge adivvgthal lqegvdffnl glvvvdeqhr fgveqrdklr
      421 akagettphl lvmtatpipr tiaitvfgdl evstlrelpg grkpiqsavv pefkerwver
      481 awekiredva aghqayivcp ridgeggvle vasklaagel kgltvevlhg rmkgdekdrv
      541 madfaaggid vlvsttviev gvdvanatvm mvreaehfgv sqlhqlrgrv grggnqslcl
      601 fhtlaaegtp sfrrvsevaa ttdgfalael dlltrregdv lgtdqsgekr tlrlinlved
      661 fkiveraykd agsivknnle faravtadfa psdfeylnks
//
LOCUS       WP_175935162             181 aa            linear   BCT 11-JAN-2025
DEFINITION  PH domain-containing protein [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175935162
VERSION     WP_175935162.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10566658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..181
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=19859
     Region          59..124
                     /region_name="bPH_6"
                     /note="Bacterial PH domain; pfam10756"
                     /db_xref="CDD:431475"
ORIGIN      
        1 mtetpnaark vfkpsrehvl aivlmtgial igilwapkyl awllifpalw lawvlttstt
       61 vgeegisvky lfrknrtlaw sdlqglsfkg atayavdqag tehplpgvtf nklpelaeas
      121 rgritdvits aheaadgkye vidkdgykvl mnreeyeayl aehpdlpgpr pagvdkhtps
      181 e
//
LOCUS       WP_175935213            1045 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175935213
VERSION     WP_175935213.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..1045
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=115264
     Region          326..1020
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mpkfllhglw lsetglavwa erveghrivt isqvpegtfp pvvhslldds rfrhrqdivl
       61 qtprgrqvtl rapvavfape eavrflasla fldgpspaat paqresvapd mywllrmyng
      121 lvqfaqagrv sihvpyrhgq wfaqwqlgtg veergwlaem laaapgvltv nnpnlsedca
      181 qtfthwitsa llyepfqeas qrrpypwhdf vfslvfgtpl rrggaqlakq vsdwngtita
      241 vnlqlvfvte ppedpvdgst daeegalvtr evlwpvrvqv rsgtdaprpv rlsdydsvta
      301 ealrdelsta vevtplvdpw vrgwsrrspg tvpdagagdw dvlltsdeiv dfvtraatal
      361 rvngfavmlp rawstaetts klhvtrasdp hdsstvsmmg ldtlmrydwr lsvggvelsd
      421 eemaelvrsk sglvklrgew vlantreiek tkkyleslkn tsveeakrea eaaetrarla
      481 eaagsddaee laaaaraare hyeqlkeaeg tgevpasalr qlaleagpeq pveftgspwf
      541 tslmggadrp apervelpet vqaelrdyqr rgvdwlyfms rnnvgavlad dmglgktlql
      601 ltllaveeae gkktgptlvv aptsvvgnwa reaarfvpgm kvmvhhgpar akgdelfadi
      661 eaadlvitsy gtisrdvqdf srvrwdhvvl deaqaiknag tqasksvral psrhrialtg
      721 tpienklsel rsildfvnpg mlgsqtffrn hfakaiesqr dpvlaeemgq rlqrltasfi
      781 lrrlktdtti iedlpdkdeh vvavdmtseq aalykalvde mkrelenrqg iarkglvlat
      841 itrikqicnh pahflgdgsp vtvkgkprsg kveklmella taaetgqrvl iftqykafgd
      901 ilqpylsdrl gedvpflhgg vgknardrmv erfqspdgpq amllslkagg tglnltaasm
      961 vihldrwwnp avenqatdra frigqdkdvt vyklitkgtm eesiqdildg ktqlagavvg
     1021 qgegwiteld tdelaqlisy rgrde
//
LOCUS       WP_175935240             533 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxylesterase/lipase family protein [Corynebacterium sp.
            Marseille-P4321].
ACCESSION   WP_175935240
VERSION     WP_175935240.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..533
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=58258
     Region          1..497
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 miaaknpvah taagkvrgiv deltgvrtwr gvpygastas acrfrapqpv grwagerdat
       61 tfappamqgt fgwrdavvgt edcltldivr pdtddvlpvv vyfhggtfvt gasnekvlqg
      121 hylakatdvv yvsvnfrlgv lgyldfrsvg kdcvanpaim dqilslewih dnianfggdp
      181 nkvtimgesa ggaavmhlmc apaarglfhh avaqspppas vhsrlqaamw vrelinrlgl
      241 prtttidelr evdaeelvra gqsmllngkq lvqlnssfmp tvdgatmpkh pidtfeegeq
      301 aavplivgtn sdeasfakai yqttkqrqra arralenfda enaldvlray gyvgergdfa
      361 dliadavfwa psvilatahr rkaptwmyrf eyasatmrrl glgamhtadl vavfgdanat
      421 raskldrfgs keafeevsrv mqyhwgsffh tgapgaewpv ygfrsddkpg ratavfdlep
      481 rveydpkasq rlawesfdmr ewgnnrqdli dsaaeffgvd vpdlptedel gte
//
LOCUS       WP_175935295             257 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Corynebacterium sp.
            Marseille-P4321].
ACCESSION   WP_175935295
VERSION     WP_175935295.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..257
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27935
     Region          7..108
                     /region_name="HTH_TipAL-Mta"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators TipAL, Mta, and SkgA; cd01106"
                     /db_xref="CDD:133381"
     Site            order(8..10,24,40..42)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133381"
     Site            order(54,57,61..62,71,83,87,93,97,100..101)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133381"
     Region          132..243
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 madgieytis eaaealgvst kalrhwealg litpartwad hrvyseadle rgaaialyrg
       61 vgvplaqiaq lldasgatlt galrhhqeal asrrrtldaq ltsvqhiidn atkgsidmda
      121 mkkylgkdmp ayqeeaeqrw gdtpewaqsq eklaqmgegd fkrlqeeqda laadliaard
      181 sgvdpgseea aalverhras iaqwyeatpa rqlilarmyv ddarfheayg gaqdyllelv
      241 tahaaaegvd vgnpqwg
//
LOCUS       WP_175935348             276 aa            linear   BCT 11-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Corynebacterium sp.
            Marseille-P4321].
ACCESSION   WP_175935348
VERSION     WP_175935348.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..276
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30165
     Region          66..269
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mrlatirtgn ttaaarmvsd realliddya dvgallrepe watiaqgvqg epravedtdf
       61 apliprpgki icvglnyakh iaemgheqpd vptlfikfpe alvgpfddae vpefnadtld
      121 fegelavivg kharhvteae ageyiagysv indysqrhyq krtqqwhqgk slektagfgp
      181 wldtewrpgp ritttlnger mqhaptddlv ftpaklvefi shlyplqpgd viatgtpdgv
      241 ghardpqryl adgdtvrvei egigaientt rvssag
//
LOCUS       WP_175935351             181 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Corynebacterium sp.
            Marseille-P4321].
ACCESSION   WP_175935351
VERSION     WP_175935351.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..181
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19712
     Region          2..162
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mttigvflgs vrggrtgeav akwvmdtaae rdgvqyklld lhdfdvphlv aetmpgvank
       61 qyddpvvtrw sqaveecdgy vfvtaeynhs vpgtmknafd slygewvekp vafvgyggdg
      121 gvravehwrq ivsnlsmfdi rnqvalrifg edavggtftp addkraaldr vlgdlekqlg
      181 a
//
LOCUS       WP_175935395             424 aa            linear   BCT 11-JAN-2025
DEFINITION  S1C family serine protease [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175935395
VERSION     WP_175935395.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..424
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42785
     Region          145..421
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mtnafpprdp aqngdtssfp ryeepqdqry tqpqyevppv aqtqpqqppk pqkkqrggag
       61 tafavalvta llagagagyl agtagsggfg glggaetkep enalenpsva kpaeapegsv
      121 eqvaanvlpa vvsievgtlr ggaegsgsii ssdgyvltnh hviadaqdpr aeimvtlndg
      181 srhpaafvas dvntdvgvik iegvdnlpvi qfgnsddlrv gqqvvavgsp lglsatvttg
      241 ivsalnrpvr asqgggessl mdgiqtdaai npgnsggplv dmngnligmn sviaslstgg
      301 fgsqgqagsi glgfaipsnf akrvadqliq ngqasqpmlg vqvsimqdtt ggavvagvep
      361 gspaddaglv pgdvitrldd rpidsadali aatrsqdfgq tvtlqvereg enapipvdvt
      421 lsse
//
LOCUS       WP_175935403             232 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175935403
VERSION     WP_175935403.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..232
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24045
     Region          75..227
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mnrrmlsgil sagaaaaval alvpapasal tlhvggapva nngqalsslv kaadsivsng
       61 atitaggyki vydpralqgp ladafapate tdwvatqrgr tadgrtvvfp ttgrytsgyg
      121 srwgtihrgi diandlgtpi yavmdgtvin agpaqgfgnw vvikhdggev svyghmryyd
      181 vqvgqrvkag qkiasigneg qstgphlhfe ikpdgvnhad pevwfkqqgi ti
//
LOCUS       WP_175935418             503 aa            linear   BCT 11-JAN-2025
DEFINITION  gluconokinase [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175935418
VERSION     WP_175935418.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..503
                     /product="gluconokinase"
                     /EC_number="2.7.1.12"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046316 - gluconokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /GO_process="GO:0046177 - D-gluconate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53499
     Region          24..495
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
ORIGIN      
        1 msakpkarki ptmsipldes rgpyvlgidv gstasrggly dvtgcpvkgs kqrvaheftt
       61 aadgtstida dqvveevrsv idgivafare kglrieavcm gsfassflli dasgdpltpl
      121 styadsrcre yveklragid etayhqrtgv rlhnsyhpar lawakaelpe wadaakvmti
      181 geyvylklag ieglavstaa wsgianahtg eldteildav gvspdmiqpl rfpdepahpt
      241 gtawpeldgl pwfhcipdgw psnvgpgatg pdtvavaaat sgamrvilpe vpaeippglw
      301 cyrvardkai lggalndvgr avswleqtiq pvtpddlaaa laaepsastp lvlpfftger
      361 stgwaagaka qllgvtaatt pldlrrgvie gialsyqrvf eqlgqagarp ervvasgrvt
      421 tdhpewlrvl adtlgttvvp lemkratlrg taiialdqia pgekravppf gvgcgavdkh
      481 rayyddlret fddaygrliq kyt
//
LOCUS       WP_175935443             264 aa            linear   BCT 11-JAN-2025
DEFINITION  inositol monophosphatase family protein [Corynebacterium sp.
            Marseille-P4321].
ACCESSION   WP_175935443
VERSION     WP_175935443.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..264
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=27499
     Region          14..264
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mistqqfida hrsssdaela aalvehagal alrmraagle tdqktsvsdv vtdadraaee
       61 fvaealealr iddgvlgeeg asresssgrt wvidpvdgtf nfsqgsdyfc salalidasg
      121 apligavhrp atsttwlaad gkatrdgeel dglrqsslsn calvtylhpt smsddavret
      181 wqraasgaat vrmfgagsvd lasiasgqfg gwlqhsvadw dwlpgkalie avggraekvd
      241 aggvtwcvag naqlvgevme klra
//
LOCUS       WP_175935448             571 aa            linear   BCT 11-JAN-2025
DEFINITION  BCCT family transporter [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175935448
VERSION     WP_175935448.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..571
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=63382
     Region          2..512
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mkrklqsdpl iffsalgfil vfvavtlafg dearqvyssi sgwlmdnlaw myiggisavl
       61 vylivvfisr ygnlrlgddd depeysypvw famlfaagmg atlmfwgaae plhhaynppr
      121 gdmesmsrea irqafeftfy hfgihmwvif tlpglaigyf vykrkmparl ssmfapllgr
      181 rvyetpgkli dalgivgtvf glavsvglgv lqisaglnim wgvplvtpvq igiilaitva
      241 aslsvatgld kgvkilsnln ivgtillmlf vlltgptlkl vgqitesfgi yaqslpelmf
      301 wvdsyndnpg whgmwtafyw awticwspfv gmffarisrg rtvrefiggt illpaafdli
      361 wfsifgraai emetsepgvl tgpvvedget pralftlleq ypiygitgtl alivivfyfv
      421 tsmdsaamvi dmyatgeenk sptyyrvgwv lavglvtaal lfindsgida lqevviiial
      481 pfffmyfvmm yslakamgdd saaarktksr twektdtpek leahenipap gydsegneve
      541 rpeleydhed dswrlpegfr ldrrtatdnk g
//
LOCUS       WP_175935449             317 aa            linear   BCT 11-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Corynebacterium
            sp. Marseille-P4321].
ACCESSION   WP_175935449
VERSION     WP_175935449.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..317
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33448
     Region          26..309
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mkqapvpsen aparneqkld eqkllekfmw lsiaasvvvi llkaaaalvt gsvgflsdai
       61 esvinlvaac vglwalklsa kpaddnhnfg hsraeyfsaq vegtlilias vviiytavdr
      121 iihpqpveql gvglgfsvaa aavnaavgva liragkkyrs ttldadgrhl itdvwtsvgv
      181 vvgmalvwlt gwavldpvva livgvnilit gykllkgaiq gllsetlpdd evetvhellr
      241 afadengvef tsvrtaaagr drlisivmqv pgewsvshsh ehadaveegl aeslggaeti
      301 vhveplghpt rtgpmwg
//
LOCUS       WP_175935453             432 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease signature motif containing protein
            [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175935453
VERSION     WP_175935453.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10052677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..432
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=46687
     Region          <311..410
                     /region_name="COG3440"
                     /note="Predicted restriction endonuclease [Defense
                     mechanisms]"
                     /db_xref="CDD:442665"
     Region          328..374
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(344,346..348,350,361..362,366..367,370,374)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 mtatiaappg snlaeaslsq iedtfikltr gkadllrqir hfeeaglarl agasstahal
       61 irrlgisdst ayeyvniacr lgtfplleqa fgagevsysk vrlvlpyite dneaelvela
      121 relgyhelei alvgrkkngd gedsgdgsyl rikktdtgdv kfwgqlnpvn gaafiaglkl
      181 geiswngvdt idetaeegql ldddaldram dkaaavepvr parqtasgfg lpigkhlvha
      241 llgmvhmvrt kptdalltpa ahvniivtkd graympnnig apsqalaniv anaalrqniv
      301 denglviktg rkfrlatpaq inallvmwgs qcaapgctht rflemhhlee wnnaghtdle
      361 nllplcsach slvtdgyiki lrdeddlhfv ygdgsrfvsr nyslprrndd avtmgefcdm
      421 idaedgfgdv gv
//
LOCUS       WP_175935494             250 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Corynebacterium sp.
            Marseille-P4321].
ACCESSION   WP_175935494
VERSION     WP_175935494.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 250)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..250
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26563
     Region          3..249
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtlsaqnltv nygsttilhs lsfgplgrgk vvgligpnaa gkstlvktia gikkpsggtv
       61 svtaggrell gkqrvealgy vpqdllssat ltafesvmvs arrrgdaswd piehtaailh
      121 rlgithladr lvsdmsggqr qlvavaqmlv repsimllde ptsaldlrhq iellqiiree
      181 vagtdrlalv aihdlnlaar fcdelvvmkn grvlaqdepv avltpdllee vyevrarvld
      241 dagvpvvcpv
//
LOCUS       WP_175935573             254 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD family hydrolase [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175935573
VERSION     WP_175935573.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..254
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26812
     Region          1..248
                     /region_name="Cof"
                     /note="Hydroxymethylpyrimidine pyrophosphatase and other
                     HAD family phosphatases [Coenzyme transport and
                     metabolism, General function prediction only]; COG0561"
                     /db_xref="CDD:440327"
ORIGIN      
        1 mkvaafdfdg tlhhpgagin psdiaaidaw rnaghlaisa tgrsrsalay alrgsglefd
       61 yqvlsnggsa tdganteliy gyevdaavlh aaldafgere glaifgttlg rvdgvfannt
      121 gaahtftahf epmtradipa hrfavvpiwv pgnealraev vewahtldgv tvaqnqdyid
      181 lmapgrnkga gveellagvg vepdqlitfg dswndltmhe iatvshsfrh sppevqdatd
      241 rvigavhevl agyl
//
LOCUS       WP_175935736             507 aa            linear   BCT 11-JAN-2025
DEFINITION  adenylate/guanylate cyclase domain-containing protein
            [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175935736
VERSION     WP_175935736.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..507
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=54953
     Region          107..500
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 mdrfwrglkw lrgtswplya atvlgtnlag aiacmvfiry fipmeevdql gldgqlglig
       61 igyaaaavlv gtvvtfflfr pvlewqrspd dhdpnmvrhl vmrlpvlqti ivvavwvigi
      121 aivtaaavrv dtrlslvvli ttgltcfvma vltylqaerl vrpiaaeala rrfedstlqp
      181 piksrlyltw fttsavpmvg vllltraqah gfftghvgel tpaiaaliva glatglmgtm
      241 favmsvvdpi relqgaimrv rrgegdaqvd iydgseigvl qagfnemmrg lgdrqrvrdi
      301 fgkyvgaeva qkaleerlel ggedrkvavl fidvigstty avnhtpeevv ealneffdvv
      361 vevvhrnkgv inkfqgdaal avfgapvalh daashalqta relqdelsel elkagigvas
      421 ghvvaghigg sdrfeytvig davngaarlt emakdtpglv ltnaatlraa neveqqrwtl
      481 mksvelrgrg kmtqlarpvr stmadra
//
LOCUS       WP_175935748             270 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175935748
VERSION     WP_175935748.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..270
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29282
     Region          16..201
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd16278"
                     /db_xref="CDD:293836"
     Site            order(75,77,79..80,132..133,158,198)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293836"
ORIGIN      
        1 mqhpaysqlr pvttsaavvl apnpsyaale gtnswvirgp edeysivvdp gpadeghlnv
       61 lqskadkval tllthrhhdh adgavrfrql tgapvrafda qyshgadele dgeiikvdgv
      121 tpqikvvstp ghtsdsvcff iysgeadnse legiitgdti agrhttmise tdgdlgayme
      181 tlemleekgk dvkllpghgp egddlsafar kyidrrnqrl dqirgalkeh genadvntiv
      241 daiyddvdpv lrgaaeqstr valrylqrsn
//
LOCUS       WP_175935751             809 aa            linear   BCT 11-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Corynebacterium sp.
            Marseille-P4321].
ACCESSION   WP_175935751
VERSION     WP_175935751.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 809)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..809
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=84495
     Region          24..682
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
     Region          <671..>754
                     /region_name="PASTA"
                     /note="PASTA domain, binds beta-lactams [Cell
                     wall/membrane/envelope biogenesis]; COG2815"
                     /db_xref="CDD:442064"
     Region          695..749
                     /region_name="PASTA domain"
                     /note="PASTA domain [structural motif]"
                     /db_xref="CDD:275384"
ORIGIN      
        1 msalkslgnl llallaagva talclapvag lggaaiarad etmqsnladl thgevpgvtt
       61 vtdvhgkpla wiykqrryev esedisqfak dalvstedrr fyehegvdmq gfaralvtni
      121 laggveqgas tinqqyvkny lwlieaddee eakaateqsi prklremrma sdlnktlekd
      181 eiltrylnlv sfgnhafgie aaartyfdts akelnpaqaa llvgllqsve glnpytnpdg
      241 avhrrnvvln nmaaegyipq teadrwagap lgildkpktl pegcitagda gfmcdyaley
      301 laskglpqee iergsytitt tldpqvqeva vnavrgnvsp ytngvagvmn vikpgqdsrd
      361 iqamassryy gldleqsqti mpqptslvgn gagsvfkift aavaldqgyg ldtmldtpar
      421 sevygmgtgg aagcppgayc venagsyapr mtlqdalaqs pnttfieliq qtgvapvvdt
      481 avrlglrsyl densfgdgrs iaqaakeenm gaftlgptav nplelsnvga tlvsngrwce
      541 pnpiksvtde rgqqvfidrp aceqavdpev aaalaagmsk davdgtgeea akrhgwtspv
      601 aaktgttesh qssaflgfnl gmaaatyifn dgtqtsplct gpvrqcgngd lfggneaadi
      661 wfqaangvpg aagaglpess kvyqqgtkra aldavvgmtq taaksqlesq gftvtvstvf
      721 gngapagtvv savpsdpnls agsvitlnis dgsgartsta pttgttpptg tsapssrplp
      781 grawdppidv ggierslgea rdaladvfs
//
LOCUS       WP_175935752             149 aa            linear   BCT 11-JAN-2025
DEFINITION  GatB/YqeY domain-containing protein [Corynebacterium sp.
            Marseille-P4321].
ACCESSION   WP_175935752
VERSION     WP_175935752.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..149
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=16113
     Region          3..149
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 msalkdqira dlkeamkake kertgtirml laaiqtaete gskhevddee iqkiiarevk
       61 krresaeiyq tngredlaqa elgeaeilag yqpkqltdee lallideava etdatsmadm
      121 gkvmkaatak aagradgkrl stavkakla
//
LOCUS       WP_175935756             460 aa            linear   BCT 11-JAN-2025
DEFINITION  CAP domain-containing protein [Corynebacterium sp.
            Marseille-P4321].
ACCESSION   WP_175935756
VERSION     WP_175935756.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Gibbs,G.M., Roelants,K. and O'Bryan,M.K.
  TITLE     The CAP superfamily: cysteine-rich secretory proteins, antigen 5,
            and pathogenesis-related 1 proteins--roles in reproduction, cancer,
            and immune defense
  JOURNAL   Endocr Rev 29 (7), 865-897 (2008)
   PUBMED   18824526
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..460
                     /product="CAP domain-containing protein"
                     /calculated_mol_wt=48201
     Region          27..201
                     /region_name="YkwD"
                     /note="Spore germination protein YkwD and related proteins
                     with CAP (CSP/antigen 5/PR1) domain [Cell cycle control,
                     cell division, chromosome partitioning, General function
                     prediction only]; COG2340"
                     /db_xref="CDD:441910"
ORIGIN      
        1 myrsripava lavalplaav qvvpapvaav eqsatsipqq tekrarlaaq aieelineyr
       61 vanglhplvt helydaqala wskqmvsdlp tlgyprndsp lgedgsafrh sdpaewghsg
      121 enilfdngvv npdaddpapg lreekpfqdt eedwaraaai lfedwrnspt hnanmlapef
      181 qgmglglvla dkgvvwgttm ffidntplqg aggkrgrmar dpltaravas gepfytpsga
      241 rellgigava dptdtkghvv srevdfgeqg ifeviaesef rtgpdtwekl fldktkdapq
      301 gldpevtgtk iqaepvkpts tpkpstpkps tpkpttpkps tpkpstpkpt tpkptsatpt
      361 sttkspasap ktsdvvvtpt ggqgsvdkqs ptptptgttt stttskepkp vepnpkdegs
      421 skagiaigvv lgllavigia aaalpmvapd larqlgipga
//
LOCUS       WP_175935816             561 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease [Corynebacterium sp. Marseille-P4321].
ACCESSION   WP_175935816
VERSION     WP_175935816.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..561
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62679
     Region          291..351
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mttaapprpk ffasqrpgdp dcinaqaird ahwnlfglfs vpgheeedfd atvtrlrtlt
       61 gfqpafvrka ilahaqlqql pllralqaet rvldmahlta vnkaveelga dveqevleli
      121 dellvrtftp kranqelpqv savtrrirdl vrgvapanay dpkarkrred dadtytsaaf
      181 mdggrerfli qlltdtakge lihesvlava rehgtsmsda ackllmgeis pqanvvmhly
      241 apkdrvegdp vyipgrgwtd peatatveew lkggaaktid ldvaaehevd gykptaamra
      301 yafardgtcv ypgcsiradr cqldhripyd eggattpsnl fslcarhhna ktdrrafyvp
      361 dpatgdiiwl fpdgtytvve sdgllhrqlt ptaprwqvsl qsvralradt aafnakchai
      421 ldrfdidlnf drarreiael eekyglffpi kfempempip epwldeeaer aekippnlve
      481 pveapfpedd dlppgdnpfh epkvlwdyse gfgtdedvag mmsfeekieq lgfddfaegm
      541 qalsklygfr vweeddedea v
//
LOCUS       WP_175935839             508 aa            linear   BCT 11-JAN-2025
DEFINITION  serine/threonine-protein kinase [Corynebacterium sp.
            Marseille-P4321].
ACCESSION   WP_175935839
VERSION     WP_175935839.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..508
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=53397
     Region          17..271
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(23..24,26..29,31,44,46,78,99..102,106,108,145,147,
                     149..150,152,162..163,166,183..186)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(23..24,26..29,31,44,46,78,99..102,106,147,149..150,
                     152,162..163)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(27,106,108,145,147,149,166,183..186)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(40..41,70,75,80..83,100)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(162..170,179..186)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mntenrddlq elvggtyqlq wiighggmst vwladdvane revaikvlrp efssnqefle
       61 rfrnealsaq ginsdnvvat ydyrevespa gftvcfivme yirgesladl iaregqleep
      121 laldvleqaa hglavihrmg lvhrdikpgn lmitqngqvk itdfgiakaa savpltrtgm
      181 vvgtaqyvsp eqaqglqvta asdvyslgvv gyemlsgkrp ftgdssvsva lahvsaeppa
      241 lpisvsapar elieialrkn panrfrdgne lqlataqvrq glrpaqpggh tqvvatepsp
      301 tastqmlaqv adertsrpeg ayppsaarav asrrapapqp ipsraaapvp aerpapaped
      361 rggakagpii atvlflalla magawaytag vfdrfgggga aptttsetpt tvteteviep
      421 etgnaepeqp areretvter hapgtvsfve pperqpapap eqpgepsvvd tpapapstpa
      481 papapqdtpa papglelpnl enllgggr
//
LOCUS       WP_175935883             357 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Corynebacterium sp.
            Marseille-P4321].
ACCESSION   WP_175935883
VERSION     WP_175935883.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..357
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38471
     Region          1..357
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 matvtfdnat riypgadaps vnrlnleiad geflvlvgps gsgkstalrm lagleetngg
       61 riligdrdvt gedpkerdia mvfqnyalyp hmtvrenmgf alklakkpka einerveeaa
      121 atldlteyld rkpkalsggq rqrvamgrai vrepqvflmd eplsnldakl rvqtrtqian
      181 lqrrmgvttl yvthdqteal tmgdriavld rgvlqqvgtp relyerpenv fvagfigspa
      241 mniatfdvdg rvarlgpvsv elpsavvpdg pqvtlgfrpe glslidgsaa haipltvefv
      301 eelgsdsyvy gtitglegqq vvvrvpplsg lhegdtvhva vddgalhafs aetgerl
//
LOCUS       WP_175935903             336 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Corynebacterium sp.
            Marseille-P4321].
ACCESSION   WP_175935903
VERSION     WP_175935903.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-P4321
  ORGANISM  Corynebacterium sp. Marseille-P4321
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Corynebacterium sp. Marseille-P4321"
                     /db_xref="taxon:2736603"
     Protein         1..336
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=36441
     Region          70..334
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 maqerkgglg rglaalipsa paemdktgkt gaiggdasdv ifgekkraia gaptvnasre
       61 evmqpvpvgg aryqeiplge iipnpkqprq vfdeddlael vhsirefgll qpivvrdtrd
      121 gfelimgerr wraaskaglk qipaivrdts dedmlrdall enihrvqlnp leeaaayqql
      181 leefgvtqeq ladrlgrsrp vitnairlln lpvpvqrrva agvlsaghar allgiklddg
      241 saeaqeqlad rivaeglsvr ateeavtlin aggkmpqkqk rqplpqpeyf tqaadslada
      301 wdtkvsvtmg krkgkivvef gdkddferim gliqge
//
LOCUS       WP_175935926             848 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175935926
VERSION     WP_175935926.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 848)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 848)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..848
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..848
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=93264
     Region          36..750
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msnlfddarr fvsdltgvsg rqayffevpg tesavalsvv svmavermgy ptevrvvlth
       61 plqlartdyl nrdavctivp ddgvphrfsg fiarfstlqt tadftkyeiv lkshfarlea
      121 vstsriyqhq ttpqiieavl rshgleghqf afrlrreypk hlfrfqykld dlsyvrilmq
      181 kagiysyive tehgdqavfa ddvdhyqwdp hltaayreta gleatgaeav talkthtvtv
      241 pqsfvvadyn peqawerfkd eanvapqdqt tygrpyvygt nhldqdgakw eaqlrheaai
      301 awqvvyeges nvlalqpgrv lnldaalpda pdgqvvievt hrgardrayt nsykaipanr
      361 rfrlqledak wrkiagtlsa rvtspdkyky ayltaagyyt vrfdvdfadw paggesvplr
      421 lakpfagklq tgfhfpaldn deaviafrda dpdkpeiigf hhhsqardlv tsdrrwlsrn
      481 virtqsnnkl rmedwagqeg vklstehsgt shldlgylvd eklerrgegf elrtsghgve
      541 ragkglhlta ydrpgasgkq ldmqetiaql eqalalaksl gdaartakam padtdaqqqm
      601 kdefdglkqp gllasapasi gvvagggvqm aakesisava gknadfsvmk rftaaageav
      661 slfaqklgik ifaakgpvel qaqsnamalt aekdvsiasa ngkvnlsaak elilecggaf
      721 ikiadgnitl ggpgdlflkv ltiqkqgaqs lnlpvpqlpv pagvemfsqr ldvspllgke
      781 fslplhhipy avkdstgriv dsgmldeagy tgrtftkqss klkyhigndp wrlfldskha
      841 eidnepqe
//
LOCUS       WP_175935948             926 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175935948
VERSION     WP_175935948.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 926)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 926)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..926
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..926
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=100866
     Region          25..840
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mdirssalgd lklrelyeai sngvlqqgrv lmldtplgkn alvplrargs arigrdysyt
       61 idvastrddt allslmhqpv tlqiqqvtap faipvyrpvh gfvhrvaylg gngglstyqi
      121 efssalvfle kthneegwle kdareiisdv ldrypqlrgq yrfsllsdpa krswcrqses
      181 dlhfvnrlae aegwyfywih envaegdapk ttlvivdhvs tlpdakavef irandsnesd
      241 gfahwagvqt mqstryisra fdykrpasdf qaesalaats yvaeerrqkv ersvpdvpmt
      301 vyestaygys ssdtgearar rlvevwdara sryfgvggvr wldagsrfvl nghprheggd
      361 akkreflvie arwfiennvp igqqtaefpq slratlaeqq aihserfktp ghaadgsagf
      421 fvieveaqpt aveyrspldh pkpimsieha lvvtpdgaea wtndrnqirv hfawdrknpp
      481 daftssplls slqsdtgngy gavhvprare wvivgywngd cdkpfvlgri nggatpspwh
      541 snallsgfks egfgktgayn sfvhddstnq ggtrlvsytg ksyaaltqgy likhegntrg
      601 kylgagfilh adefgavras kglsisahsk syddeqmgvd earsqlqqag mlveslssas
      661 ttaqaeslqt gqdalkalsk diqhpvsgdt sggvtagggt gsangfsqpn ilvstpkdia
      721 lvadnsthiv aekeinvvsn entyvatgks lvvaaaekvs ffaqklgaff vtakgpikls
      781 antddvnvna gkdvtvkakr ivldadeiii kaggsytrwv aagiedgtqg prtiksasls
      841 rqgpssiaqh mnslpqakfn dpyvlrdrlt gevlknhpye lirgdgtrlt gttnelghva
      901 eqksddvesl mlhalrrtpd aggdtq
//
LOCUS       WP_175935965            1024 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia
            vietnamiensis].
ACCESSION   WP_175935965
VERSION     WP_175935965.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..1024
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=109045
     Region          1..993
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnfgqwmqmh rrsllfvval lavagaltaf rlpislfpnv sfpravvsld agdrpaeqma
       61 tlvtmpxxxe ealrrvpnvr dvesrtsrgs aeislnfdwg tdmaqatlqa qsaiaeilps
      121 lppgtkmqvk rmdptvfpvl aysltssrqs laqlrdlaql qlrpllssvd gvarvevtgg
      181 aqdelqvaid parlaaykls vedvskaiga gnvlmatgri edhyklylvv adttitsldt
      241 lrnavvssag gnqvrvgdia tvsrgtvpqw irvtadgqda vlvnvfqqpg ansvamakai
      301 raklgafekq mppgvhlanw ydqsqlvias assvrdaili gvvlaaitlf vflrnwkita
      361 iavalvpvvm sstillldvf gmgfnimtlg gmaaavglvi ddaivmiehi arrvreagth
      421 afhgrvmsaa leftrplags saatliifvp laflsgvtga ffkalsitma salfisfvvs
      481 wlaipilcdh wltpadaeeh resrlshwmn iryaalierv sgkpllalag vvpllivaal
      541 aftrvgsgfm psmdeggfvl dyhtapgtsi tetdrlmrev etiirenpnv atysrrtgag
      601 lggdlnepnr gdffvrlksg srepidtvme eirskietnv pgvsielaql medligdlta
      661 vpqpvqikiy sddphvldlt arrvaarigk iqgivdvddg inpagdaldl hirpdaaaae
      721 gmdpqaiaqq vsdllegnva tqfqqgpktv gvrvwvanam rtngtglgel qirapdghlf
      781 pldrvtdlvt vsgqpeisrd nlkrmvavta ridgrdlgst iadvqhalge adllppgvyy
      841 elgglyqqqq iafrgllavf gaavalvfgl llflyerfrv alavmamplc atgavfiglw
      901 vtgielnisa mmgmtmivgi vtevaifyvs efqalvrdeg mapdvallaa grnrlrpiam
      961 ttiaailall plafalgqgs amqqplavai isglivqlpl vllvlpvllr vlvagsgsag
     1021 lsdh
//
LOCUS       WP_175935984             575 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Burkholderia cepacia].
ACCESSION   WP_175935984
VERSION     WP_175935984.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..575
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=62896
     Region          <9..152
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          327..570
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mrtkltvknp kpasptrapv rsgslvarka vrpaappagd kparpkkasp aaagersfkp
       61 rgaagaerpg adrapakrap rdggaergtr apyrdnaage gakrsfgdrr tssdrpprrd
      121 ddarprragg dddkrssyrd kaagegakrs fgdrrpssdr pprrdddarp rraggeggar
      181 apyrdnasge gakrsfgdrr tssdrpprrd ddarprragg eggarapyrd nasgegakrs
      241 fgdrrpssdr pprrdddarp rragaddgkr psyrdkapge gakrsfvdrp arpardgerr
      301 sfgavktaqp vkraaadvdy gdetglmrls krmselgmcs rreadewiek gwvlvdgeri
      361 dtlgtkvrad qkieideras aaqaaqvtil lhkpvgyvsg qaedgyepaa vlitranrws
      421 gdhspvrfsp qhlhalapag rldidstgll vltqngviak qligeqsdid keylvrvrfg
      481 erlididqhf paeslaklrh gleldgvalk pamvswqnge qlrfvlregk krqirrmcel
      541 vgldviglkr vrmgrvmlga lpqgqwryls adetf
//
LOCUS       WP_175936020             159 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia
            cepacia].
ACCESSION   WP_175936020
VERSION     WP_175936020.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..159
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18241
     Region          11..144
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtqrinyfqq speltrklie ldglfqktti eapvrelvei rasqlngcaf cvdmhikmak
       61 ihgerelrlh hvaiwlestl fspreraale wtevltrlpa hgvpdelyar vrehyseqel
      121 sdltvlvgai nswnrlnvaf rivpgsfdkm fgldkanle
//
LOCUS       WP_175936031             237 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175936031
VERSION     WP_175936031.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..237
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26699
     Region          57..237
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          181..234
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mnlsvsditp eelrlfgdiv arleelgpvv dvrtvvlpei trlmradfaa sfdcdehtgq
       61 wrngfaynvd plqiaryeaw fqhidpvtpq lcarrvatcv devvsrhele rtefyndflr
      121 rggmhhginv yafdgathvg dlriwraqgr pdfterdkll lngiepffrr allrrrhact
      181 glteresdva rlvaagytdk dvartlgigl stvrthlrrv makkgvanra slaaala
//
LOCUS       WP_175936096             234 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Burkholderia cepacia].
ACCESSION   WP_175936096
VERSION     WP_175936096.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..234
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24688
     Region          163..233
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mkiedgvlas gggparpgrq rqfggkqrnp vrrfggiaav lllhvllvya llnglatkvv
       61 qviqhpietr iiepvkpppp ppplpvvklp ppkatlpppp fvppaevpvq appqaaithq
      121 aapvpsapav qapvvappap aakpvshevg vvcpnsdqmr asmqypkeaq ennitgdvti
      181 efvvdadgnv tnvrvsqsad pvldraaynt vrrfkcmaqg qpvrvqvpfs fnln
//
LOCUS       WP_175936125             223 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175936125
VERSION     WP_175936125.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..223
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24321
     Region          13..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mssdedadag qkayhhgdlr raiietaldt lqeqqgwqft lreiarranv shsapyrhfp
       61 dkaallhela ligfdrlrde laasidpaas apdvllalay ahlafgqrnp dlyrlmfaad
      121 agepsdihld prvqapfllv vdilehgqra gtirprpalg qatacwahlh gltmlaidrr
      181 lvrekvgdha iedalttlld glilpaspar aaktktrtkt kgs
//
LOCUS       WP_175936154             347 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            cepacia].
ACCESSION   WP_175936154
VERSION     WP_175936154.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..347
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=36642
     Region          48..330
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 miesskplps gaavsqrvpv wrsalqrpeg wlavavvcvl pvvlssgsla tevlvfalaa
       61 lgcnlllgft gllsfgqgif fglgsyaagl vlthgvasvt aalaaatvlg avaaalvgwf
      121 sirqrgtyfv mltlafgqlf yflayttpdv tggdnglldi prpalaafgh plvsldspwr
      181 yygfvavlfv avfwlllrvs rsvfgrtlla irdnearaaa agydvkrfkl aafvlsgavt
      241 glagalhalm tgiaplsnid yhtsemilvm tviggtgnlf asvlgaafyv lfadwlstlw
      301 prwllllglv liavslfmqr glwglgerva tslrrtgrta atareqq
//
LOCUS       WP_175936169             188 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175936169
VERSION     WP_175936169.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..188
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20710
     Region          1..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 metkptvreq ildhattlmm lrgyngfsyr dlsdlvgvkt ssihyyfpsk ddlvleavaa
       61 ysdevlsamr aidpalpadv klslytklfg rtlgdgnlic lcgmlaadie tlpenvrqav
      121 qaffkanesw laellkqgaq egtlqfsgep etaartlyaa fqgsvlasrl fhtrarledv
      181 eavwkkra
//
LOCUS       WP_175936194             319 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia cepacia].
ACCESSION   WP_175936194
VERSION     WP_175936194.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..319
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34832
     Region          40..193
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <193..302
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 meidarttpl qrttpdqspt arlaaliaay aphdgtfelp vrglriarvs aspphwnhgv
       61 hhaclsivgq gakstrvgda ayvidesrml vttadlpvtg rvtraspaep flyaqleldp
      121 ariavltprv fprglpkavd cgaldthdap peivdavvrl mqliahpddi dllaplivde
      181 ilirllrgps garvaqvgqd dsttqrisra vawirdhyld pmtveslarq vdmspstfhh
      241 hfrtvtsmsp lqcqkmlrlq earrlmclsa mdaqqacrsv gyvsasqfsr eyarlfgdap
      301 grdvvklrdq avplsrvap
//
LOCUS       WP_175936228             452 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175936228
VERSION     WP_175936228.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..452
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48228
     Region          17..411
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(24..25,28..29,32,64,114..115,117..119,122,142,
                     145..146,149,268,271..272,275..277,280,308,312,364..365,
                     369,373,389,392..393,396..397,400)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtnssskvrk yvgltgicia sflgcidltv vntilpaigr dfsipiqttq witsifmval
       61 safmvpvatl adnlgrkkll ivglvifgaa sllagiahqf wllvgfrflq gigcailytv
      121 sgaivsytfd eneqgkalgi lfgangvgla lgpiigglfa galdwhdafl inipfiaisl
      181 alcawaipef kaqarkridv tgclllvvgl ttlvsylsvd ggglnlwllp vslvalalfv
      241 whelrtrdpi vefhffrepr flsallatff laffycivll tlpiffstql hksditigly
      301 llpatitfsi asswiggrse rlgpsrvivt glslfvvasi llsivagqpd aawfivplll
      361 fgigwgailg pstlvalgal prekaavamg tswtvhnvgg asgiafaifl mrqvddfrhg
      421 yqtlmlalaa iilaagalyh vlsresvava id
//
LOCUS       WP_175936025             270 aa            linear   BCT 11-JAN-2025
DEFINITION  creatininase family protein [Burkholderia cepacia].
ACCESSION   WP_175936025
VERSION     WP_175936025.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Yoshimoto,T., Tanaka,N., Kanada,N., Inoue,T., Nakajima,Y.,
            Haratake,M., Nakamura,K.T., Xu,Y. and Ito,K.
  TITLE     Crystal structures of creatininase reveal the substrate binding
            site and provide an insight into the catalytic mechanism
  JOURNAL   J Mol Biol 337 (2), 399-416 (2004)
   PUBMED   15003455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..270
                     /product="creatininase family protein"
                     /EC_number="3.5.2.10"
                     /calculated_mol_wt=28405
     Region          29..265
                     /region_name="ArfB"
                     /note="Creatinine amidohydrolase/Fe(II)-dependent FAPy
                     formamide hydrolase (riboflavin and F420 biosynthesis)
                     [Coenzyme transport and metabolism]; COG1402"
                     /db_xref="CDD:441012"
ORIGIN      
        1 mkclpravfa avaftvaqaa laqapatvrl edmtwtelrd siragkttil ipvgateqsg
       61 pyvalgkhna rvavlseria qglgnaivap viayvpeggy apptshmrfp gtitvpddvf
      121 ektlesaans frvhgftniv flgdhggyqn dirqsvarln kswagtgara fvpaeyygts
      181 sdgydrllre rgvpaadigt hagladtsll lavapdmvrv dklrnaakpg avdgvyggdp
      241 rhasvelgrl gtdaivsrtv dairkdtagr
//
LOCUS       WP_175936249             493 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175936249
VERSION     WP_175936249.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..493
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51230
     Region          20..468
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(27..28,31..32,35,67,117..118,120..122,125,145,
                     148..149,152,214,217..218,289..291,294,322,325,383..384,
                     388,392,408,411..412,415..416,419)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msrndpvspd prrwamfail lvgaflppld ffivnvalps iraelgasss aeqlvissya
       61 glyavtlitg grlgdlfgrg rvfflgligf aiastlcgfa sspwtlivgr alqgvtaaim
      121 apqalasiqa ifpeaekpla lslygavfgl aavvgqalgg ilislnllnl gwrtiflvnl
      181 plamlvvlfg ipllketraq harkldlggt alsmltlgal ivpliegrea gwpgwawvsl
      241 lavpalagff wryerrlgrr ggaplldpaa lrapglgral lialllysig affllfsvyl
      301 qnalhvdals aglvflpfgv gfllgplstp actrvigayv npfgmsleiv glvglawlid
      361 atpigmplaa aplavvlfii gfgqglalpt lmrmvtgrva palsgmiagi asstlqvsts
      421 lsvaiiggif yttlgtrhdp aaiahafiva llsisvflav gaalgislar agaahtsmrt
      481 aarpgfgper erp
//
LOCUS       WP_175936255             701 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia cepacia].
ACCESSION   WP_175936255
VERSION     WP_175936255.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..701
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75661
     Region          7..701
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 msrrnwaaap maivvgaagv gtadaqeatl ptieisgqra sapfrtrdst satrgdadvm
       61 eipfavssvd aklvrtvaat rgedlydwva gvarqnnfgg lwdnyavrgf agdgntsgtd
      121 ylvngfswnr gisvprdtan lermevlkgp asalygrgdp gglisyttkq pqfarantvg
      181 vsagsygalr etldstgpvt kslayrfvam nenngsfrdt vsskrylfap sftwdigadt
      241 tlhyefesar qrapldrgvv avggqlgaip asrflgeprd gdydvrntgh qftlehrvda
      301 nwsvnagfaq rttdlsgrss eafalqpdgr tlwrryrqva fhsndlqgri etagkfrtgg
      361 ightlvlgvd ayrfnydqfv arstptaaap yaidifdpvy gqpaptprta tnllerddgq
      421 glyaqdtlaf gphwkilagl rwdrfhqsve nrlkgttssq vqtalsprig ivyemspals
      481 lyantaysfr pnngadvdgr afdpekghgy eagakwagar wlatvaafyv nkrnvltadp
      541 anagfsraag evrsrgvefe wngdlghgvr glvnlayvda evthdavltp garlvdiprl
      601 sgsalllyet avpfadkaga gagliyvgrr agntantqdg felpayatvq lngyvqvnkh
      661 lrasvvlnnl fnrttyvssy nnlwvtpgap rslfaslayt f
//
LOCUS       WP_175936251             448 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175936251
VERSION     WP_175936251.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..448
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48396
     Region          27..434
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(40..41,44..45,48,80,139..140,142..144,147,167,
                     170..171,174,268,271..272,275..277,280,308,312,363..364,
                     368,372,388,391..392,395..396,399)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mpsltqaaaa paaadsseda lyrkvmrril pllllcyvva yldrvnvgfa klqmlddlnl
       61 sdgvyalgas iffwgyflfe mpsnlllhry garfwiarim itwgivsssm afivplaqff
      121 hvqtttmfyt lrfllglcea gffpgvilyl nywfparrqs vamsgflvai plsltlgsvl
      181 sgwlmeqthg lsgmsgwqwm llleglpsiv vafivlaclg dgpqtakwls adekavlsrn
      241 leseaahksh sigaalrspr vwlltfillt fntgfyglaf wlpsiirasg vhgplhigvl
      301 taipyltaif amvwnashsr ktgerrlhaa ipaliggvfl ilsaafahnv alsivfltia
      361 tcgilalmpi ywtfpgqils gtaaaagial insvgnlsgf tgsmitgvak qmtgninngt
      421 yalgacllvs cvliasiprd ilrppvgr
//
LOCUS       WP_175936263             346 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia cepacia].
ACCESSION   WP_175936263
VERSION     WP_175936263.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..346
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34691
     Region          13..301
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtplrtlfrh slawpvltla llfaldvahr pgflsialld ghlfgapvdi lnraaplviv
       61 slgmtlviat rgidisvgai vaiagaaaai vldadpsrvg aalaaalgvg llagawngll
      121 vafvgmqpii atlilmvagr gvaqlltggq iipigapgyl algggylatv pcsvwiaiat
      181 iaatallvnr talglfirai gvnpvatrlv glragavvfg vylcsgvmaa lagilassnv
      241 rsadgnnagl lleldailav tlggtsllgg rfslagsvlg aliiqtltyt tysigvppea
      301 tlvvkavvvi vvtliqseaa ralvvrhasr llpsarsrat tgatpr
//
LOCUS       WP_175936294             472 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175936294
VERSION     WP_175936294.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..472
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=48563
     Region          27..466
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 msalpdraaq rhalaaalgd gwldgasaes cepyatdvtr hsglalgvar pastadtsal
       61 arvavahrva lvaqgartgl vgaavpdrsg tqcvvsfdrm ravrafdaan rsitveagar
      121 lsdinrvaad aglclpvdlg sdpaagglvg anaggsrlik ygdvrrnvlg vevvladaag
      181 tvidalaplr krnagfdvtq cfigangahg lvtavsfala plersscaaf vafasydaal
      241 agllaferaf gemlsafefm saaavgcvaa afpalripfe adaaacyalv eiatgmpgld
      301 glleertiat ldtlagervv ldaacapaer fwrirdalpv avaqhgipls fdvsfprgal
      361 aafvadaeqw iaaahpslrc hafghfgdgg chlvvsipha daerygplqq valrgalyer
      421 vvraggcfsa ehgvgpvnva yyrkhvpaaq relaaavqha vdplgligrv ry
//
LOCUS       WP_175936424             477 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia cepacia].
ACCESSION   WP_175936424
VERSION     WP_175936424.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..477
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47716
     Region          34..420
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(40..41,44..45,48,80,130..131,133..135,138,160,
                     163..164,167,291,294..295,298..300,303,331,334,387..388,
                     392,396,412,415..416,419..420)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msdrapalgg tpaavapphr tslrailptv aaaslgfaiv qldvtvvnva ipslghsfgs
       61 svhglqwivd aytlsfaall ltsgtladrf gsrrlfaygl alfllaslgc alapslaali
      121 aarvaqgvga amilptslal ithacandaa arvravawws atggaisaag ptlggllids
      181 lgwraiffin lpicaaglwl tvrhvrdsaa artrlfdpag qivavlvlal ltggiiraga
      241 qgpgdpyaag alaasvvlga lfvaierrva apmvplaffr iarvpgvlai gaitnaafyg
      301 lifslslyfq nargftates glalapltii mlaniasarl avrhgfratv ivglavslag
      361 yvwlwrtlga htpyallapg laamaigggi aipaltstll gsveagrsat asailntarq
      421 vgaavgvaal galvagqgaa ivagasrafa vaaalvavci vlaarwpgda pepgpra
//
LOCUS       WP_175936353             592 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia cepacia].
ACCESSION   WP_175936353
VERSION     WP_175936353.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..592
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=64862
     Region          7..585
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mpqitkpevd avlvgmgwtg simgmelaea gltvvglerg anrdtspefa ypaiadelay
       61 iqrrklmqnl ahetvtirha pnedalpyrq lgafllgtgv ggsgvhwngt twranaadlk
      121 irshyvqryg agfipgdmti qdwpysldel epyferleav mgtsgkagnl rgrivdggnp
      181 feamrrrdyp cppladnypa tlfrnaarda gfhpfpipas nasiayqnpy gmqlgpcnfc
      241 gycegfgcym yskaspqaci lpallakpnf elrdrshvtr vqldsdgkra tgvtyldaqg
      301 revfqpariv vlcafqmhnv rllllsgigt pydpatgtgt vgrnfayqkn stvslffdkd
      361 vhidpfigag sggqafddfn adhfdhsavg fvggayisam vtggrpigqt llpegtpkwg
      421 sawkkalkdn ylhsfsigta gsvmsyrtny ldldptyrda yglpllrmtf dwhdnemrmt
      481 rfvtgkaeqv aramkpksms vhagkigdhf dmrpyqttht tggavcgdrp dtsvvnkylq
      541 swdvhnvfvt gacafpqnwa ynptgmvgaq ayfsaraire qylknpgpll pt
//
LOCUS       WP_175936499             500 aa            linear   BCT 11-JAN-2025
DEFINITION  catalase [Burkholderia cepacia].
ACCESSION   WP_175936499
VERSION     WP_175936499.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..500
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55484
     Region          10..493
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 miaaacvala ssshaaeltr dngspvgdnq nsqtagpngp vllqdshlie klqrfdreri
       61 pervvhargt gafgefvpsa disdlttakv ftpgtktpvf vrfstvmgyr gspeqardpr
      121 gfavkfyteq gnwdlvginl piffirdaik fpdfvhankp savtgvqdan lafdffahap
      181 eatsmltrly siegmpdsyr nmdgygvhaf kfvnadgkyt yvkfhwksaq gmhglrpkdi
      241 pgsigadwnl mtndlygalk agnapkwdly iqvlkpseld afdfnplddt kvwtgvperk
      301 igtltlnrvp dnyfestees afapsrmvpg iepsedrmlq grmfsyadtq myrlganfnq
      361 lpinrprvpv tnnnqdgamn fgdrkgevny epsalnelaq npryksvqtp lagttqqaai
      421 rktlnfrqag eyyrmlpaqe rqdlvtalsg dlnhvtndan kyamlsyfyk adadygtrla
      481 rathadltrv ksladklven
//
LOCUS       WP_175936534             210 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein, partial
            [Burkholderia cepacia].
ACCESSION   WP_175936534
VERSION     WP_175936534.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         <1..>210
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
     Region          1..>152
                     /region_name="COG3576"
                     /note="Predicted flavin-nucleotide-binding protein,
                     pyridoxine 5'-phosphate oxidase superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442796"
     Region          175..>210
                     /region_name="FNR_like"
                     /note="Ferredoxin reductase (FNR), an FAD and NAD(P)
                     binding protein, was intially identified as a chloroplast
                     reductase activity, catalyzing the electron transfer from
                     reduced iron-sulfur protein ferredoxin to NADP+ as the
                     final step in the electron transport...; cl06868"
                     /db_xref="CDD:447143"
ORIGIN      
        1 psqytdiapl efdhldarar aiisaadtff vasyvgegea rqvdvshrgg nagfvrided
       61 drltvpdfag nlffatlgnf lvnpraglvf vdfetgdmlq mtgeasvele seeiaafqga
      121 erlwhfkprr vihrrqampl rwrfrvdgws pnslmtgswd eaasrlkaaa lahawrpfev
      181 trivdetpai rsfhlrpadg agllphaagq
//
LOCUS       WP_175936573              97 aa            linear   BCT 11-JAN-2025
DEFINITION  cysteine hydrolase family protein, partial [Burkholderia cepacia].
ACCESSION   WP_175936573
VERSION     WP_175936573.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         <1..97
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
     Region          <4..74
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 lhhrrtsgfi gtpleqvlaa hdvrhlivag vathstvemt vrhavdlgyt atvaadacsc
       61 adrqqhaasl esmrllasis tvaelfgegd aspepda
//
LOCUS       WP_175936594             690 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Klebsiella quasipneumoniae].
ACCESSION   WP_175936594
VERSION     WP_175936594.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella quasipneumoniae
  ORGANISM  Klebsiella quasipneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella
            pneumoniae complex.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Klebsiella quasipneumoniae"
                     /db_xref="taxon:1463165"
     Protein         1..690
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75586
     Region          2..690
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 maaenhaakd nndaeetiiv vandarqsat sgyqplssst atltsmplmd ipqvvntvsd
       61 rvledqhats ldealynvan vvqtntlggt qdaftrrgfg anrdgsimtn glrtvlprsf
      121 naatervevl kgpastlygi ldpgglinvi tkrperqfsg svsgtstsfg ggtgsvdvtg
      181 piegtnlayr ligeyqnedy wrnfgknksr fiapsltwfg dratvtasys hrdysapfdr
      241 gtifdlntgh avnvdrktrf deafnitdgy sdlaqlnaey rlndawtarf dysysqdhyn
      301 dnqarvvayd satgnltrrv dgthgstqkm hstradlqgn vvvggfynel ltgvayenyd
      361 llrtdmlrck nvkgfniyhp vygtldtcnt vsasdsdqri qqesyaayvq dalyltdnwi
      421 avagvryqyy tqyagkgrpf nvntdsrdek wtpkaglvyk vtpnvslfan vaqsfmpqss
      481 iasyigelpp eestayevga kfdllegita nialfdihkr nvlytesigd etvaktagkv
      541 rsqgvevdla gsitdnlsmi asygytdakv ledpdyagkp lpnvpkhtgs lfltydihnv
      601 ynsntltigg gghavskrsg tngadyylpg yavadvfaay kmklqypvtl qvnvknlfdk
      661 tyytssigtn nlgnqigdpr evqftvkmdf
//
LOCUS       WP_175936983             468 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Staphylococcus hominis].
ACCESSION   WP_175936983
VERSION     WP_175936983.1
KEYWORDS    RefSeq.
SOURCE      Staphylococcus hominis
  ORGANISM  Staphylococcus hominis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
            Staphylococcaceae; Staphylococcus.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Staphylococcus hominis"
                     /db_xref="taxon:1290"
     Protein         1..468
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54671
     Region          12..199
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkvikskein hrpkvsvlis tynkekfink tldsvlkqsm dmrdfelivv ddcstdqtvd
       61 ivskkidsfs nykfiqldqn sgtpakprnl sidlskgkyi mfidgddwlp edaleklytl
      121 lktnktdyat gltkyvhsdr iarsgvalsk iaynkvdlkh frksfyhlap agrmikasvi
      181 kknhiqfpem ifgedlqffa evffntkris ttqdvvycan ryddnislvk seksthinrm
      241 kwqgeayrhl mskyknnklm pnllyriink dvleakfykk nfikninell pifqniihmv
      301 dehfdaldya dddlnrqaik liregnkedi isfvkfylkk ddkplheknd iyyysfkgth
      361 ykkrmhptll kisqdndkvf lkilsknsel kylevkhrkn ptqfivldik khrfksgeyt
      421 vqfttknlpn gklaltvldk dlngsviksg mrfdfyetvg gnlgyikk
//
LOCUS       WP_175936641             515 aa            linear   BCT 11-JAN-2025
DEFINITION  TrkH family potassium uptake protein [Metamycoplasma hominis].
ACCESSION   WP_175936641
VERSION     WP_175936641.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma hominis (Mycoplasma hominis)
  ORGANISM  Metamycoplasma hominis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Metamycoplasma hominis"
                     /db_xref="taxon:2098"
     Protein         1..515
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=58347
     Region          22..496
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mikkgnpkks nvlfvflkkl gtirfifliy ilftilmslm lywevshnps khisyldall
       61 laassftttg lsgvavsevf nmfgqiliav cfilggigif tfklyifqsl lglrtnlfsg
      121 qihqterggs niyetkkmik vsisfliiis ilfslifsli fyydntalfs dekmsqlnal
      181 sknnpwtfnp yeesirnpyh nfgmslrfgi fhtlsainna gldiigtksl qpyyhnyyfl
      241 fltsiiflig gmgfpvfydv wqkiksikkd nprhcftlft kftiityift sligllltfi
      301 fettakgany fwnsseygsi gdkvfaiyfq tmstrsagfs tinyynftqp timvhgilmf
      361 igfspvstag girnitvaii fmsiitlikn rkninafhrq igkeslikav nifaiaifit
      421 limtiviyht lpsdlknvyn esypmvyvmf evfsafgnsg lnigltpnlg itgkilliit
      481 mivgqlgisq flkiftfsks kpqryqyiye disig
//
LOCUS       WP_175937128             159 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Wolbachia endosymbiont of Madathamugadia
            hiepei].
ACCESSION   WP_175937128
VERSION     WP_175937128.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Madathamugadia hiepei
  ORGANISM  Wolbachia endosymbiont of Madathamugadia hiepei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Wolbachia endosymbiont of Madathamugadia
                     hiepei"
                     /db_xref="taxon:1241303"
     Protein         1..159
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17856
     Region          43..154
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(48..49,82..83,86,90..91,94,144,148)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mwsrlvvmcc fcllltgvss cpkkgvntan kmnsvvkrvs ekrvffdydk snigeagadv
       61 lldvmevlqn npdmkvtvtg htdnrgsyey nvalgerrad aakkfmvsct pylenrikta
      121 srgeaeplvy vqddsknsky ekqhaknrrv eflfseakk
//
LOCUS       WP_175937156             217 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Wolbachia endosymbiont of
            Madathamugadia hiepei].
ACCESSION   WP_175937156
VERSION     WP_175937156.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Madathamugadia hiepei
  ORGANISM  Wolbachia endosymbiont of Madathamugadia hiepei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Wolbachia endosymbiont of Madathamugadia
                     hiepei"
                     /db_xref="taxon:1241303"
     Protein         1..217
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25495
     Region          1..199
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 milyhfplcp fsrkvrallk ekklgcdlvy enpwekrnef meinptgqvp vlmdnnfiit
       61 dstaiceyle etyssdikll dfstivkski ralvnwfdnk fynevtkyii nekviinrsp
      121 dsrflhaaqh nlschieyie hlisknvwla tdkftladit lashisvmdy vnsfpweksr
      181 ilkewysivk srpcfremll erisgltppv hyanfdf
//
LOCUS       WP_175937225             236 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Wolbachia endosymbiont of
            Madathamugadia hiepei].
ACCESSION   WP_175937225
VERSION     WP_175937225.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Madathamugadia hiepei
  ORGANISM  Wolbachia endosymbiont of Madathamugadia hiepei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Wolbachia endosymbiont of Madathamugadia
                     hiepei"
                     /db_xref="taxon:1241303"
     Protein         1..236
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25970
     Region          1..230
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 mhspiisisn lslsfddkti lnnisfdifk geslvilggs gsgksvltkt iiglltpdsg
       61 sikinskskn kfgvlfqnst lfdyvtvwen isfnytkrfn inkkeakqla ieklsdvgle
      121 kniadmfpie lsggmkkrva laraiahnpe iivldeptsg ldpimsdavn eivmklskdl
      181 nptiitithn ihsafkiadk iavlyggsii shgtvqeikn tkneyvrkfi ryvrtk
//
LOCUS       WP_175937168             391 aa            linear   BCT 11-JAN-2025
DEFINITION  elongation factor Tu [Wolbachia endosymbiont of Madathamugadia
            hiepei].
ACCESSION   WP_175937168
VERSION     WP_175937168.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Madathamugadia hiepei
  ORGANISM  Wolbachia endosymbiont of Madathamugadia hiepei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Wolbachia endosymbiont of Madathamugadia
                     hiepei"
                     /db_xref="taxon:1241303"
     gene            1..391
                     /gene="tuf"
     Protein         1..391
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
                     /calculated_mol_wt=42933
     Region          10..391
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 mtqvveafgk phmnvgtigh vdhgkttlta aitkyygnfv aydqidkape erkrgitiat
       61 ahveyqtekr hyahvdcpgh adyvknmivg aaqmdaailv vsgvdgpmpq trehillakq
      121 vgvkhivvyi nkadvadhdm iglvemevre lltkygfpgd evpvivgsal kvlegdense
      181 ygkksmdklm kaldeyvpdq prpvdlpflm piedvfsisg rgtvvtgrie kgevkmgeei
      241 eiiglkatqk tictgvemfk klldkgcagl nvgillrgtk reevergqvl akpgtitphk
      301 rfkaevyilk keeggrhtpf fanyqpqfyi rttdvtgsik llegkemvmp gdnvsievel
      361 qvsiamdkgl rfaireggrt vgsgvvseil e
//
LOCUS       WP_175937228             464 aa            linear   BCT 11-JAN-2025
DEFINITION  NADH-quinone oxidoreductase subunit N [Wolbachia endosymbiont of
            Madathamugadia hiepei].
ACCESSION   WP_175937228
VERSION     WP_175937228.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Madathamugadia hiepei
  ORGANISM  Wolbachia endosymbiont of Madathamugadia hiepei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Wolbachia endosymbiont of Madathamugadia
                     hiepei"
                     /db_xref="taxon:1241303"
     Protein         1..464
                     /product="NADH-quinone oxidoreductase subunit N"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=51371
     Region          1..458
                     /region_name="NuoN"
                     /note="NADH:ubiquinone oxidoreductase subunit 2 (chain N)
                     [Energy production and conversion]; COG1007"
                     /db_xref="CDD:440631"
ORIGIN      
        1 msyiqilpet fsivsslvll llgivfnrrt inllalgcta vtlivlvlla ennevfffns
       61 llklnlyirs aqglilivgv sillllnlsk ydykyefsil ilfalfgmit lvsannlisf
      121 ylafelmsip lyvlasfnkd svysceagvk yftlsalssc imlygmslly gytgqidfsq
      181 lslfvqnhqv tygivfglvf iliglcfkla ivpfhmwapd vyqgaptivt affstapkaa
      241 lvtflirlmn eelvnvknyv qpvllyvsal svlisafgal rqknlkrlla yssighvgfi
      301 faslsiftrm gtdssltylm myivtsiglf syfiqidddd cnianlsgvg kkhpvlafhl
      361 silllsmagi pplagffakl fifkglinsg fislplilvv asviscyyyl niikamyfdk
      421 ssgnkitypk glfiitsvas liniilfiyv edlyslihlv tkgl
//
LOCUS       WP_175937229             480 aa            linear   BCT 11-JAN-2025
DEFINITION  NADH-quinone oxidoreductase subunit M [Wolbachia endosymbiont of
            Madathamugadia hiepei].
ACCESSION   WP_175937229
VERSION     WP_175937229.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Madathamugadia hiepei
  ORGANISM  Wolbachia endosymbiont of Madathamugadia hiepei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01972.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Wolbachia endosymbiont of Madathamugadia
                     hiepei"
                     /db_xref="taxon:1241303"
     Protein         1..480
                     /product="NADH-quinone oxidoreductase subunit M"
                     /EC_number="1.6.5.-"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_process="GO:0042773 - ATP synthesis coupled electron
                     transport [Evidence IEA]"
                     /calculated_mol_wt=52958
     Region          12..474
                     /region_name="NuoM"
                     /note="NADH:ubiquinone oxidoreductase subunit 4 (chain M)
                     [Energy production and conversion]; COG1008"
                     /db_xref="CDD:440632"
ORIGIN      
        1 mlllsifllp ligalilsli kinhksiylr flslffavlp fllsivacig fdynnadfql
       61 vsypirnagi gvdgislpfl llttflfvvc llynckmsyt tlkaymalfl llesfvvgff
      121 islnavsfyv ffevvlvpmf fiigiwggkq rvyaafklfl ytlagsslfl lglvyiynvf
      181 gtfdiqklat lmpsldlgvq sllwiaffvs faikvpmfpf htwlpdahvq sptsgsvila
      241 gllikmggyg flrfsipmlp qasfyfsnfi vvlsaiaviy aslvafaqnd ikkliayssi
      301 ahmgivtagl fsfyeegvlg avfqmishgl isaalflcvg mlytrtgtle iakyfgivnt
      361 mpkfgfmfil fsmasiglpg tsgfigefla migmfksigf ftgfialgti lsavymlnlc
      421 kqtiwgvsys kllnnrldsi essvlillav lvillgfypt lalnylkpcm anllvkynvl
//
LOCUS       WP_175937244             285 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Wolbachia endosymbiont of
            Madathamugadia hiepei].
ACCESSION   WP_175937244
VERSION     WP_175937244.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Madathamugadia hiepei
  ORGANISM  Wolbachia endosymbiont of Madathamugadia hiepei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Wolbachia endosymbiont of Madathamugadia
                     hiepei"
                     /db_xref="taxon:1241303"
     Protein         1..285
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32292
     Region          21..278
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mkddrrlgrg lagligdnyd nkkdrqeylp isllhpskfq prkhfdeesl kelassiekn
       61 giiqpivvrk dsnndgyeii agerrwrask ianldsvsvi vkdlsdkecl klsiieniqr
      121 qdinpieege aykklidefs ytheelastv gksrshitnm irmlslpgsv ktminekkls
      181 mgharalinv enaesiteki isqglnvrqt eklikdlhqs sdkkeqkytq nqdiaaiegt
      241 issqlglkik indnnskgkv mirynnpnel dlilkilnrk lescq
//
LOCUS       WP_175937275             117 aa            linear   BCT 11-JAN-2025
DEFINITION  NADH-quinone oxidoreductase subunit A [Wolbachia endosymbiont of
            Madathamugadia hiepei].
ACCESSION   WP_175937275
VERSION     WP_175937275.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Madathamugadia hiepei
  ORGANISM  Wolbachia endosymbiont of Madathamugadia hiepei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012780
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Wolbachia endosymbiont of Madathamugadia
                     hiepei"
                     /db_xref="taxon:1241303"
     Protein         1..117
                     /product="NADH-quinone oxidoreductase subunit A"
                     /EC_number="1.6.5.9"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=13306
     Region          1..117
                     /region_name="PRK06602"
                     /note="NADH:ubiquinone oxidoreductase subunit A;
                     Validated"
                     /db_xref="CDD:180638"
ORIGIN      
        1 mseyltivif icvsiivslt lgvlpmflav snpdseklst yecgfnplsk arknfdikfy
       61 lvsilfiifd leiaflfpwa vslskisycg fwsmmiflai ltigfiyewc kgalewe
//
LOCUS       WP_175937457             224 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Wolbachia endosymbiont of
            Madathamugadia hiepei].
ACCESSION   WP_175937457
VERSION     WP_175937457.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Madathamugadia hiepei
  ORGANISM  Wolbachia endosymbiont of Madathamugadia hiepei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Wolbachia endosymbiont of Madathamugadia
                     hiepei"
                     /db_xref="taxon:1241303"
     Protein         1..224
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24366
     Region          4..218
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mggdvalelt sidksfkeap avikdinlrv akgqvvalig ssgsgkttil qiagllnkpt
       61 sgivtidgvn ctqasnkhkt hirrsflsfv yqfhyllqel pvlenvmlpq liagrsktea
      121 iknvqimlek fgledkassm iseisggerq rvaiarsvvn sprllladep tgnldltnsl
      181 nvflllysyv kennssmliv thnhllaeka dcilqlkdrs lvkl
//
LOCUS       WP_175937511             249 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Wolbachia endosymbiont of Madathamugadia
            hiepei].
ACCESSION   WP_175937511
VERSION     WP_175937511.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Madathamugadia hiepei
  ORGANISM  Wolbachia endosymbiont of Madathamugadia hiepei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142575
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Wolbachia endosymbiont of Madathamugadia
                     hiepei"
                     /db_xref="taxon:1241303"
     Protein         1..249
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27292
     Region          9..244
                     /region_name="SDR_c"
                     /note="classical (c) SDRs; cd05233"
                     /db_xref="CDD:212491"
     Site            order(13,15..18,37..39,66..68,98..100,122,149..151,166,
                     170,196,198..200,202..203)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:212491"
     Site            order(123,151,166,170)
                     /site_type="active"
                     /db_xref="CDD:212491"
ORIGIN      
        1 mgklegkial itgasggigs avakrfvkeg acvilisrsi dhlkplynei eefeefkegp
       61 vkliqldlld fenvkiltnm ieslklsesg aldilvactg ilgklnpvhd celeelqnvm
      121 ntnftanwyl lknldpmlkk snsgrvifmt sevtlspssy pywvpyaask aaleimvkiy
      181 asetkhtklc vnavypegpv dsemykqafp gkdtpelvlp dkltdkfvel asedcsvsgq
      241 ilplsksle
//
LOCUS       WP_175937516             452 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA recombination protein RmuC [Wolbachia endosymbiont of
            Madathamugadia hiepei].
ACCESSION   WP_175937516
VERSION     WP_175937516.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Madathamugadia hiepei
  ORGANISM  Wolbachia endosymbiont of Madathamugadia hiepei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Wolbachia endosymbiont of Madathamugadia
                     hiepei"
                     /db_xref="taxon:1241303"
     Protein         1..452
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=51253
     Region          142..424
                     /region_name="RmuC"
                     /note="RmuC family; pfam02646"
                     /db_xref="CDD:460637"
ORIGIN      
        1 mlfnsiflgl nflslllfly titkknrkls eekiksanle gnlckleref qgakqaltnk
       61 deeivclkvs naelevtlqk ereekkkeie lltkaeerlt nafkalslda lqannnnfln
      121 lakevidgkl ketendfkkr qatinevvvp ikeklekfds eirelekerv gayeglkeqi
      181 galmnqtssl analrkphir gkwgemqlkr vvemagmiey cdfftqpsvi dknednllrp
      241 dliikmpsgk qiiidakvpl dsyldamsqn dlqiqkeklk nhslaikkhi sdlgkkeywn
      301 qfentpelvv lfltgegvfs aaleyepali eigvkkkvii atpitliall raiaygwkqe
      361 miaesakkis elghilyeri ctmgenfdnl rrslksavdh ynktagslea rvfpaareln
      421 klgihaknke lsaakelesl prslhaeelk vd
//
LOCUS       WP_175937425             132 aa            linear   BCT 11-JAN-2025
DEFINITION  EVE domain-containing protein [Wolbachia endosymbiont of
            Madathamugadia hiepei].
ACCESSION   WP_175937425
VERSION     WP_175937425.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Madathamugadia hiepei
  ORGANISM  Wolbachia endosymbiont of Madathamugadia hiepei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Bertonati,C., Punta,M., Fischer,M., Yachdav,G., Forouhar,F.,
            Zhou,W., Kuzin,A.P., Seetharaman,J., Abashidze,M., Ramelot,T.A.,
            Kennedy,M.A., Cort,J.R., Belachew,A., Hunt,J.F., Tong,L.,
            Montelione,G.T. and Rost,B.
  TITLE     Structural genomics reveals EVE as a new ASCH/PUA-related domain
  JOURNAL   Proteins 75 (3), 760-773 (2009)
   PUBMED   19191354
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006808
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Wolbachia endosymbiont of Madathamugadia
                     hiepei"
                     /db_xref="taxon:1241303"
     Protein         1..132
                     /product="EVE domain-containing protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=15257
     Region          2..131
                     /region_name="EVE"
                     /note="Predicted RNA-binding protein, contains EVE domain
                     [General function prediction only]; COG2947"
                     /db_xref="CDD:442190"
ORIGIN      
        1 mqfwllksep seyswqemek ekvakwdgvc nyqaqsymra mklgdsaffy htgkekavlg
       61 iveifkeyyl vndskfglvd vkfsnplsnq vtlsdikrnp llknmamlkq prlsvspvse
      121 aewneiirms ec
//
LOCUS       WP_175937598              84 aa            linear   BCT 11-JAN-2025
DEFINITION  cold-shock protein [Wolbachia endosymbiont of Madathamugadia
            hiepei].
ACCESSION   WP_175937598
VERSION     WP_175937598.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Madathamugadia hiepei
  ORGANISM  Wolbachia endosymbiont of Madathamugadia hiepei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 84)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Wolbachia endosymbiont of Madathamugadia
                     hiepei"
                     /db_xref="taxon:1241303"
     Protein         1..84
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=9435
     Region          1..82
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mefgnikwfn aekgygfikp eakgsdvfvh istlehsgir pdslrgenke kgikgervsy
       61 elkkergrng eekksainlk lled
//
LOCUS       WP_175937678              93 aa            linear   BCT 11-JAN-2025
DEFINITION  co-chaperone GroES [Wolbachia endosymbiont of Madathamugadia
            hiepei].
ACCESSION   WP_175937678
VERSION     WP_175937678.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Madathamugadia hiepei
  ORGANISM  Wolbachia endosymbiont of Madathamugadia hiepei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF001533.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK00364
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Wolbachia endosymbiont of Madathamugadia
                     hiepei"
                     /db_xref="taxon:1241303"
     gene            1..93
                     /gene="groES"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140662 - ATP-dependent protein folding
                     chaperone [Evidence IEA]"
     Protein         1..93
                     /product="co-chaperone GroES"
                     /calculated_mol_wt=9984
     Region          1..93
                     /region_name="groES"
                     /note="co-chaperonin GroES; Reviewed; PRK00364"
                     /db_xref="CDD:178988"
     Site            order(6,9,34..35,56,66,71,73,89..91)
                     /site_type="other"
                     /note="oligomerisation interface [polypeptide binding]"
                     /db_xref="CDD:238197"
     Site            order(18..20,21..29)
                     /site_type="active"
                     /note="mobile loop [active]"
                     /db_xref="CDD:238197"
     Site            order(43,54)
                     /site_type="active"
                     /note="roof hairpin [active]"
                     /db_xref="CDD:238197"
ORIGIN      
        1 mdlsvlddsv likpiseekq ggivlpssae kkptkgevia tgegsrnssg erialtvkig
       61 dkvfyrqwag teiehgdekf ivmkesdila ivk
//
LOCUS       WP_175937818             454 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Wolbachia endosymbiont of
            Madathamugadia hiepei].
ACCESSION   WP_175937818
VERSION     WP_175937818.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Madathamugadia hiepei
  ORGANISM  Wolbachia endosymbiont of Madathamugadia hiepei
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Wolbachia endosymbiont of Madathamugadia
                     hiepei"
                     /db_xref="taxon:1241303"
     Protein         1..454
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=51324
     Region          <3..232
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          23..54
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          56..86
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(88,90,94..95,98..100,102..103,107,110,119,122,124,
                     128..129,132..134,136..137,141,144,153,155,157,161..162,
                     171..173,175..176,180,183,192)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          88..119
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          122..153
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          142..382
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          155..192
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          194..232
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          234..265
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(267,269,273..274,277..279,281..282,286,289,298,300,
                     302,306..307,310..312,314..315,319,322,331,333,335,
                     339..340,343..345,347..348,352,355)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          267..298
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          300..331
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          333..363
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mvheedinql vesgfdinsk dangitllhk ftkegdaarv rsllehaadf nvvdsenrnp
       61 lhyavmhghk kiakllvnql tinskdkngf tplhlaalqd dteligflia kgakinerda
      121 kegytplhia slygskksvq alvdsganle cednnlhtpl fltiyqctah yesreeiiey
      181 likkeaniea kdaennttlf laaynnkmqi vklivkkqqa kanfkefict knshgfdald
      241 cavehnngkm viflvskgid andqdfngna rlhkasyngd tkavrfllel kvnvnavtkc
      301 nrtplllavk kghtkivkml levkanmnic eqqgytplhl avqrdyfdia qwliekgadl
      361 sikckdgyta idmfinkang radinenykk fcrflilylk elhskykasc mfstlalslt
      421 ilglpfifkp iikyrernrm ykktkamlen llyi
//
LOCUS       WP_175937981             615 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp70 family protein [Burkholderia plantarii].
ACCESSION   WP_175937981
VERSION     WP_175937981.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia plantarii
  ORGANISM  Burkholderia plantarii
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   Fernandez-Fernandez,M.R. and Valpuesta,J.M.
  TITLE     Hsp70 chaperone: a master player in protein homeostasis
  JOURNAL   F1000Res 7 (2018)
   PUBMED   30338057
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 615)
  AUTHORS   Mayer,M.P. and Bukau,B.
  TITLE     Hsp70 chaperones: cellular functions and molecular mechanism
  JOURNAL   Cell Mol Life Sci 62 (6), 670-684 (2005)
   PUBMED   15770419
REFERENCE   3  (residues 1 to 615)
  AUTHORS   Bukau,B. and Horwich,A.L.
  TITLE     The Hsp70 and Hsp60 chaperone machines
  JOURNAL   Cell 92 (3), 351-366 (1998)
   PUBMED   9476895
REFERENCE   4  (residues 1 to 615)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   5  (residues 1 to 615)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   6  (residues 1 to 615)
  AUTHORS   Rensing,S.A. and Maier,U.G.
  TITLE     Phylogenetic analysis of the stress-70 protein family
  JOURNAL   J Mol Evol 39 (1), 80-86 (1994)
   PUBMED   7545947
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Burkholderia plantarii"
                     /db_xref="taxon:41899"
     Protein         1..615
                     /product="Hsp70 family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0051082 - unfolded protein binding
                     [Evidence IEA]"
                     /GO_function="GO:0140662 - ATP-dependent protein folding
                     chaperone [Evidence IEA]"
                     /calculated_mol_wt=64961
     Region          7..608
                     /region_name="DnaK"
                     /note="Molecular chaperone DnaK (HSP70) [Posttranslational
                     modification, protein turnover, chaperones]; COG0443"
                     /db_xref="CDD:440212"
ORIGIN      
        1 mseprfsigi dlgtthcals yvdlaagdgd apqqqvlpia qltspgaigs psllpsflyl
       61 phpgeltpgd ltlpwtatrd yavgemarsr gagtpirlvs sakswlchpg vdrraailpn
      121 dappevervs pldasvrylt hlretwdhah pdapfaaqdv tvtipasfdp aareltaeaa
      181 qaagyarmtl leepqaalys wiqksgggwr kdvkvgdiil vvdvgggttd lsliavverd
      241 gnlelhrvav gehillggdn mdlalahvva rklaaqgtqa dpwqlralty acrgaketll
      301 gdrtldtvpl vvpsrgskli ggsirteltr aeltqilleg ffpqvdaaar pavrtraglt
      361 qlglpyaqda gitrhlaafl gkqvgaladl gglpappaeg asflhptavl fnggvfksel
      421 lteriltiln gwlaadgaap arllggadld lavargaayy gyvkrgrgvr irggtarayy
      481 iaiesampai pgmeppvsal cvapfgmeeg sdaalpeqef glvvgepvtf rffgssvrrq
      541 dqvgalldyw sadelqelea iqatlpaegr tpgevvavrl harvteagtl eleamprggg
      601 erwkvefdvr ggvda
//
LOCUS       WP_175938099             465 aa            linear   BCT 11-JAN-2025
DEFINITION  NADH-quinone oxidoreductase subunit N [Wolbachia endosymbiont of
            Litomosoides brasiliensis].
ACCESSION   WP_175938099
VERSION     WP_175938099.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Litomosoides brasiliensis
  ORGANISM  Wolbachia endosymbiont of Litomosoides brasiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Wolbachia endosymbiont of Litomosoides
                     brasiliensis"
                     /db_xref="taxon:1812117"
     Protein         1..465
                     /product="NADH-quinone oxidoreductase subunit N"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=51052
     Region          27..459
                     /region_name="NuoN"
                     /note="NADH:ubiquinone oxidoreductase subunit 2 (chain N)
                     [Energy production and conversion]; COG1007"
                     /db_xref="CDD:440631"
ORIGIN      
        1 mnyiqilpet fsiisslvll llgiafnrrt inllalgcti vtliililsa knngvfpfns
       61 llklnlyirs aqglilvagi lvllllnlsk ydyeyefsil ipfalfgmit lvsannlisf
      121 ylafelmsip lyvlasfnkd siysceagvk yfalsalssc imlygvslly gytglinfse
      181 lssflenhqi tygivfglvf iliglcfkla iapfhmwapd vyqgaptivt affstvpkaa
      241 lvtflvrfla geelvgvaky fqpallyvsa lsvlisafga lrqrnlkrll ayssighigf
      301 ilaslsiftr mgtdssliyl iiyiiasigl fsyfiqiddd ncgvanlsgi gkkspvlafh
      361 lsilllsmag ipplagffak lfilkslvhs gfigmslilt vasviscyyy lsimkamyfn
      421 kssdskviys kslfivtsva slinivlfmy venlyslihl vtksl
//
LOCUS       WP_175938151              96 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Wolbachia endosymbiont
            of Litomosoides brasiliensis].
ACCESSION   WP_175938151
VERSION     WP_175938151.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Litomosoides brasiliensis
  ORGANISM  Wolbachia endosymbiont of Litomosoides brasiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 96)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Wolbachia endosymbiont of Litomosoides
                     brasiliensis"
                     /db_xref="taxon:1812117"
     Protein         1..96
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11064
     Region          <20..93
                     /region_name="COG5606"
                     /note="Predicted DNA-binding protein, XRE-type HTH domain
                     [General function prediction only]"
                     /db_xref="CDD:444337"
ORIGIN      
        1 mqnlqlnypi tieldnikdt klklikivar linkryrtqk kaaialkidq pkvsqinksk
       61 iegfsleyll nllvaldqdi nmkikhdpqp tqrniq
//
LOCUS       WP_175938188             368 aa            linear   BCT 11-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Wolbachia
            endosymbiont of Litomosoides brasiliensis].
ACCESSION   WP_175938188
VERSION     WP_175938188.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Litomosoides brasiliensis
  ORGANISM  Wolbachia endosymbiont of Litomosoides brasiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Wolbachia endosymbiont of Litomosoides
                     brasiliensis"
                     /db_xref="taxon:1812117"
     Protein         1..368
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=41698
     Region          23..362
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mlgklvilll vfvlpfsshs yqfrtkakqa vvldlasdsf ifehnsdekm apssmsklmt
       61 lyvafdylka giidmndkfq vsrkawerkg ssmflkegqs vtvkellegi atvsgndaci
      121 tlaegiagse egfvvemnev aqnlnlsnsy fvnssgwpde dhfmsakdlv vlakrifidf
      181 peyydlfseq yltynniaqk nknlllfhdi gvdglktgyt ntggygivvs akrndrrifa
      241 vvnglnteke rieeakrliq ysfnhfntkk ifakdsvvee invlygkerk vsvtvandit
      301 itynrnlrdk ikvrvehkdi ipapirkgqe vgkifieipg veqqttplya vndvqelnyi
      361 eklfrmlf
//
LOCUS       WP_175938223             705 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA translocase FtsK [Wolbachia endosymbiont of Litomosoides
            brasiliensis].
ACCESSION   WP_175938223
VERSION     WP_175938223.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Litomosoides brasiliensis
  ORGANISM  Wolbachia endosymbiont of Litomosoides brasiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 705)
  AUTHORS   Jean,N.L., Rutherford,T.J. and Lowe,J.
  TITLE     FtsK in motion reveals its mechanism for double-stranded DNA
            translocation
  JOURNAL   Proc Natl Acad Sci U S A 117 (25), 14202-14208 (2020)
   PUBMED   32513722
REFERENCE   2  (residues 1 to 705)
  AUTHORS   Crozat,E., Rousseau,P., Fournes,F. and Cornet,F.
  TITLE     The FtsK family of DNA translocases finds the ends of circles
  JOURNAL   J Mol Microbiol Biotechnol 24 (5-6), 396-408 (2014)
   PUBMED   25732341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Wolbachia endosymbiont of Litomosoides
                     brasiliensis"
                     /db_xref="taxon:1812117"
     Protein         1..705
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=78684
     Region          3..>98
                     /region_name="PRK10263"
                     /note="DNA translocase FtsK; Provisional"
                     /db_xref="CDD:236669"
     Region          82..704
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 mlkkylkaai ylsllmyiym svfsynyedp slntvtdkav tnlggivgsy ladilvqffg
       61 lisvtiattv vyflifrpsr rllkilysil inlgicavlp qlplgitagy mhsgvignal
      121 inncpfymfm iavligiigl igwrrtiyll fllckkaasl fvrvlffrly kaaeyptvpl
      181 vvdkkyrakv atrqqpkemr kkvveeifes fnefkfpsvh llskaeeslq rkqlsemesn
      241 knllllkqvl sdfgiqgkii svcygpvvtl yklepqagtk sarvigladd iarsmsalsa
      301 risiirgqna mgielpnker eivmlrdlle sseyqnanln lpialgkeis gkpvvadlak
      361 mphllvagtt gsgksvavnt milslvyrls pdackmimid pkmlelsiyd aiphlitpvv
      421 tepkkavial rwvvkemenr yrmmsylnvr nvinynqkit eamnsgiele rvvqigfsst
      481 tgkplfekmp ikmetfpyiv viidemadlm lvagkeiecs iqrlaqmara agihivvatq
      541 rpsvdvitgv ikanfptris favtskidsr tilgeqgaeq llgmgdmlym asggkiirvh
      601 gsfvsdeevq nivdhlktqg epnymeeitk edssaelege tedgendlyk qavaviqrdq
      661 kvstsyiqrq lrigynraan ivermekegi isapnylgkr eilve
//
LOCUS       WP_175938295             197 aa            linear   BCT 11-JAN-2025
DEFINITION  YbhB/YbcL family Raf kinase inhibitor-like protein [Caballeronia
            sp. BCC1704].
ACCESSION   WP_175938295
VERSION     WP_175938295.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..197
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=20917
     Region          40..193
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mrvasrivrs ghavtaftlg vasaaallch argavaqdvf svtspelalg ktirhellfd
       61 dsdckggnrs pqlswrgapa qtrsfavtif dpdapgrgww hwavagippt vthlpanasa
      121 sgalrkigav earndwdtdg yggpcpppgk phryivtvya lnrddlrlrq gtpalmfdhe
      181 irataiasaq ltfsvgr
//
LOCUS       WP_175938306             211 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Caballeronia sp. BCC1704].
ACCESSION   WP_175938306
VERSION     WP_175938306.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..211
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22298
     Region          1..211
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mslhvwwmfv atvfvisaip gpnmllvmth garfglrrsv atmagslsal vlmlsvsaag
       61 lgvfleawpg ffdalrltga aylvwlgvks wrakasamav restpdartr satpaalyrn
      121 gflvagsnpk silfaaallp qfidaarpvl pqfavlvatl avievswftv yaglgarige
      181 klksaavaqa fnrltgglfv gfgammallr h
//
LOCUS       WP_175938315             103 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175938315
VERSION     WP_175938315.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002085
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..103
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11294
     Region          1..98
                     /region_name="ManC"
                     /note="Mannose-6-phosphate isomerase, cupin superfamily
                     [Carbohydrate transport and metabolism]; COG0662"
                     /db_xref="CDD:440426"
ORIGIN      
        1 mkviesgkft aerawgaldi cvmngtscrl hwtdapykwh vndgeevfav mdgvvrmhvr
       61 daegertltl kagdifyaqa gdehyaepvg aarilvieke gsv
//
LOCUS       WP_175938321             366 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Caballeronia sp. BCC1704].
ACCESSION   WP_175938321
VERSION     WP_175938321.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..366
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39154
     Region          1..366
                     /region_name="LhgO"
                     /note="L-2-hydroxyglutarate oxidase LhgO [Carbohydrate
                     transport and metabolism]; COG0579"
                     /db_xref="CDD:440344"
ORIGIN      
        1 mdriecvvig agvvglaiar alalrgrevm vleageaigi gtssrnsevi hagiyyprgs
       61 lkaelcvrgr emlyafceah gvphrqcgkl lvatarnqip qlaaieqkgv enrveglvri
      121 sgaeakemep qlqcveavys prtgivdshq ymlalqgdae nhgagvvfht pvvsieareg
      181 cfivetggea parfrasyli nsaglhandi arrirglddr hvpplyfakg nyfsvsgrap
      241 ferliypmpn eaglgvhlti dmggqakfgp dvewvpsiny dvdprradsf yaairaywpg
      301 lpdgalqpay agirpklsgp gqaaadfmiq gksahgvpgl vnlfgmespg ltaslaiger
      361 vadmlr
//
LOCUS       WP_175938347             204 aa            linear   BCT 11-JAN-2025
DEFINITION  SCO family protein [Wolbachia endosymbiont of Litomosoides
            brasiliensis].
ACCESSION   WP_175938347
VERSION     WP_175938347.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Litomosoides brasiliensis
  ORGANISM  Wolbachia endosymbiont of Litomosoides brasiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Wolbachia endosymbiont of Litomosoides
                     brasiliensis"
                     /db_xref="taxon:1812117"
     Protein         1..204
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23024
     Region          43..179
                     /region_name="SCO"
                     /note="SCO (an acronym for Synthesis of Cytochrome c
                     Oxidase) family; composed of proteins similar to Sco1, a
                     membrane-anchored protein possessing a soluble domain with
                     a TRX fold. Members of this family are required for the
                     proper assembly of cytochrome c...; cd02968"
                     /db_xref="CDD:239266"
     Site            order(76,80,162)
                     /site_type="other"
                     /note="Cu(I) binding site [ion binding]"
                     /db_xref="CDD:239266"
ORIGIN      
        1 mirfvrllss vlvalsvvfl gycyftkkgi fapavthnvg vkisgdfsli nqdgqvihss
       61 dfkdkymmif fgfssckkvc pmnlgiisei lakldkkind klqtffitvd perdskerlk
      121 efqqqfdhri qmltgkrkki deviasykvy tskvggeeei nhssimylig pggeyvahfv
      181 adlnsdesqs dkiaaeikky inel
//
LOCUS       WP_175938418             214 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Wolbachia endosymbiont of Litomosoides
            brasiliensis].
ACCESSION   WP_175938418
VERSION     WP_175938418.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Litomosoides brasiliensis
  ORGANISM  Wolbachia endosymbiont of Litomosoides brasiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Wolbachia endosymbiont of Litomosoides
                     brasiliensis"
                     /db_xref="taxon:1812117"
     Protein         1..214
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23243
     Region          12..213
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mielkgpeic tdgskknlvi clhgwgssgd nfihlakvms kslpnscfia pnapsereig
       61 egyqwfsled cseevlyngv ksaasivnhf idkklkefsl kdtqlslvgf sqgamlaiha
      121 altrsqccas viaysgrfls plrvapkiks rpnmciihgd tddvvpfssl dlavkalken
      181 ginveghpir alghvineeg iklgvefikk nfke
//
LOCUS       WP_175938469             207 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Caballeronia sp.
            BCC1704].
ACCESSION   WP_175938469
VERSION     WP_175938469.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122607
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..207
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22320
     Region          2..75
                     /region_name="GST_N_1"
                     /note="GST_N family, unknown subfamily 1; composed of
                     uncharacterized proteins, predominantly from bacteria,
                     with similarity to GSTs. GSTs are cytosolic dimeric
                     proteins involved in cellular detoxification by catalyzing
                     the conjugation of glutathione (GSH) with...; cd03043"
                     /db_xref="CDD:239341"
     Site            order(13,15..16,18..19,22..23,68,71..72)
                     /site_type="other"
                     /note="putative C-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(13,52..54,66..67)
                     /site_type="other"
                     /note="putative GSH binding site (G-site) [chemical
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(52,65..66,68..69,72)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239341"
     Region          96..200
                     /region_name="GST_C_3"
                     /note="C-terminal, alpha helical domain of an unknown
                     subfamily 3 of Glutathione S-transferases; cd03194"
                     /db_xref="CDD:198303"
     Site            order(98,102..103,106..107,166,169)
                     /site_type="other"
                     /note="putative substrate binding pocket (H-site)
                     [chemical binding]"
                     /db_xref="CDD:198303"
     Site            order(98,158,161..162,165,169)
                     /site_type="other"
                     /note="putative N-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:198303"
ORIGIN      
        1 mklvigdknl sswsmrpwvl lrhfgipfde alirlgqpgt kakildvtps gkvpclitds
       61 getvwdslai metlaerypq halwprdaaa raharsisae mhagfadlrq nmpmqitare
      121 pgigatpgtl adiaridaiw tgclaqsggp flfgdfciad amfapvvmrf nsyapaiseg
      181 areygarvta lpavaawidd akkdnar
//
LOCUS       WP_175938492             343 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175938492
VERSION     WP_175938492.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..343
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37192
     Region          4..323
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtdlltirnl qvtfggtqav drinlsvkpg evvgvvgesg sgksvtmmal mglidhpgkv
       61 tadqitfdgh dllkasarar rkiigkdiam vfqdaltsln psytvgyqik evlrlheglr
      121 gdalnkrale lldqvgipda knridtfphq lsggmnqrvm iamavacnpk lliadeptta
      181 ldvtiqaqim ellvrlqker gmalvlishd lavvsevaqr vavmyageii etnhvpaifs
      241 ephhpyteal laaipehsrg aarlaalpgm vpgrddrpsg clfaprckyv vddcwkgrph
      301 lyqldardaa vrarcikpln vaqevaqavr aereaqivee gar
//
LOCUS       WP_175938471             318 aa            linear   BCT 11-JAN-2025
DEFINITION  complex I NDUFA9 subunit family protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175938471
VERSION     WP_175938471.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Parey,K., Wirth,C., Vonck,J. and Zickermann,V.
  TITLE     Respiratory complex I - structure, mechanism and evolution
  JOURNAL   Curr Opin Struct Biol 63, 1-9 (2020)
   PUBMED   32058886
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Babot,M., Birch,A., Labarbuta,P. and Galkin,A.
  TITLE     Characterisation of the active/de-active transition of
            mitochondrial complex I
  JOURNAL   Biochim Biophys Acta 1837 (7), 1083-1092 (2014)
   PUBMED   24569053
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..318
                     /product="complex I NDUFA9 subunit family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0010257 - NADH dehydrogenase complex
                     assembly [Evidence IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=34057
     Region          5..274
                     /region_name="NDUFA9_like_SDR_a"
                     /note="NADH dehydrogenase (ubiquinone) 1 alpha subcomplex,
                     subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs;
                     cd05271"
                     /db_xref="CDD:187579"
     Site            order(10,12..15,34..36,74..76,93,116..118,129,133,
                     152..155)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187579"
     Site            order(129,133)
                     /site_type="active"
                     /db_xref="CDD:187579"
ORIGIN      
        1 mqhqnvaiig gsgfigshlv nalvdlgknv riatrrrsna ahltllpvdv letdvhdpik
       61 laafvaeada vinlvgvlqg rrgdpygpef arahvelprk ivaacaakgv rrlihmsaig
      121 adsegpsmyl rskgdgekqv resgldwtif rssvvfgped nllnqfafle rlfpviplac
      181 anaefqpvfv gdvakaivnv ldldaanrmv yelagpavyt laelvrfaga tigkharivk
      241 lpeslgrlqa mtlemapgep lmsrdnldsm ktpsiasgpl apelgigepa sieaiaplyl
      301 tgmsprsrfn tfratahr
//
LOCUS       WP_175938647             315 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Caballeronia sp. BCC1704].
ACCESSION   WP_175938647
VERSION     WP_175938647.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..315
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34178
     Region          80..286
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mtidsdllqy ysrvaeafpp lgpdadasav rqrfkavaqa ysgerddaia vedidvslqs
       61 rtiaariyrp kaasgplpll vyfhgggwvv gdiethdgla arlaldaqca vasvdyrlap
      121 enpfpapcdd aldallwlae hrsrlgfatd rlgvggdsag ahlavvaarg anqrvaglvn
      181 mqlllypvmr rqfdspscla nangpgltnd emrwywtqfl sgaapdehdv rafplaepye
      241 rtparaliva aaydplydda yelqrflean ggrvemidat nmthgfgrlh aqsgaardwl
      301 rqigeragel lradr
//
LOCUS       WP_175938759             399 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent rRNA methyltransferase [Caballeronia sp.
            BCC1704].
ACCESSION   WP_175938759
VERSION     WP_175938759.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..399
                     /product="class I SAM-dependent rRNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=43408
     Region          3..398
                     /region_name="RlmK"
                     /note="23S rRNA G2069 N7-methylase RlmK or C1962
                     C5-methylase RlmI [Translation, ribosomal structure and
                     biogenesis]; COG1092"
                     /db_xref="CDD:440709"
ORIGIN      
        1 mntitlkpak dkslvrrhpw iyanaiarid gnpapgatvt vraadgrfla rasysphsqi
       61 rarvwtfdea epvdhaffkr rvqravahrq tmvrdtgatr lvfgeadglp glivdyyvad
      121 qgshaqlvcq fmatgveawk paivdaliaa tgcpnvyers dvsirqkegl eqttgvlagd
      181 pppdtlitne cgvryhvdvk hghktgfyvd qrdnrvlvqq naqgrdvlnc fcytggfsla
      241 alkggaarvv svdssgeala larenvkang fdaekaewld adafktlrrl ydegqrfdli
      301 vldppkfaps retvdraara ykdinlsgfk llrpggllft yscsgaidad lfqkivagaa
      361 adarvdaril krlgagvdhp lltafpegey lkglllqia
//
LOCUS       WP_175938834             263 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: BON domain-containing protein [unclassified
            Caballeronia].
ACCESSION   WP_175938834
VERSION     WP_175938834.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..263
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=27217
     Region          42..196
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mkktrvkaal aqatltvsll sgvaltmqgc alavvgaaag gtliatdrrt lgaqtedrei
       61 qvkalsrike nvsdqahinv tvfnrrvllt gevpddaskq kaeavvrdin nvggivnels
      121 vqpassissr andsylegrv ktamvgekdl sanyykvvce rsiiylmglv tqdegahgad
      181 vaarvsgveq vvkvyqyikp eeakalaaaa sgassstapt papaeatvgt vpdssvtsrp
      241 ldqqtpapvk nsdvrpgsss sak
//
LOCUS       WP_175938831             596 aa            linear   BCT 11-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Wolbachia endosymbiont of
            Litomosoides brasiliensis].
ACCESSION   WP_175938831
VERSION     WP_175938831.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Litomosoides brasiliensis
  ORGANISM  Wolbachia endosymbiont of Litomosoides brasiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Wolbachia endosymbiont of Litomosoides
                     brasiliensis"
                     /db_xref="taxon:1812117"
     Protein         1..596
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=65961
     Region          67..271
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
     Region          206..385
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
     Region          <521..595
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mirflililv gylcygnean daknsvgdfl dtlhkikyvs yskkdfakfl vqchkegiqe
       61 dfrkgfgsnl ngadfsklyl ngsifngvsl igadfshtdl sgvsfinsdl rganfsnanl
      121 rgikikdtnl gfakfvsanl idiifdqsdv scaefvssdl knvrmhsmtg lhtnfsdvkm
      181 sfsslldsnm gyvnfsdsei nntvvqrsnl dnanffgvds yklkiqfssl enanvygtei
      241 kesaftgsnl snvclnssti idsnfdgtnl sktqisyvns dnssfvqsil ngskikhsya
      301 sevsfqdadl snidfsfsel hqvdvsdsdv rhgefrdarv ahsnmngsff dhslfisaki
      361 egtdlsstsm yrvkirdsqv ynsrlfynsi dsseienstf fnliasnssw snlkvtssnf
      421 vendfesslf rdsafkktsf flsnfsssti sgtsfhsssi ykgsvvdahl vdckfdhsil
      481 idnegqekla glegaitsie klqekilqgk kfnvnysyfe fkdmnlgnvd fsnsilsrak
      541 finvnldkan lgksdlryai fnnssligtn lsgsnldhss flksdlksai lenvks
//
LOCUS       WP_175938861             416 aa            linear   BCT 11-JAN-2025
DEFINITION  PstA family ABC transporter permease [Wolbachia endosymbiont of
            Litomosoides brasiliensis].
ACCESSION   WP_175938861
VERSION     WP_175938861.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Litomosoides brasiliensis
  ORGANISM  Wolbachia endosymbiont of Litomosoides brasiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 416)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11672565
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Wolbachia endosymbiont of Litomosoides
                     brasiliensis"
                     /db_xref="taxon:1812117"
     Protein         1..416
                     /product="PstA family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45994
     Region          18..152
                     /region_name="DUF3333"
                     /note="Domain of unknown function (DUF3333); pfam11812"
                     /db_xref="CDD:463357"
     Region          174..412
                     /region_name="PstA"
                     /note="ABC-type phosphate transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG0581"
                     /db_xref="CDD:440346"
ORIGIN      
        1 mgiktkflkl lqsrrvhari krknkkdkal yfcsfitlii slgcpvcill silinsysal
       61 tvtkvllpie vntdfdlann lsdlryksin llndslqkif egtdfkssde ilsrnsykel
      121 enfvrrkvkh sgkyeiwfta ssitnsinkg kyfnshyagl lswlkeqgrv gkffnkslfl
      181 esdsrepena gilgafvgsl mtiivclala lpvgimsgic lhefmprnnm itnvievsin
      241 nlaavpsiif gvvgltlyle ifglprsspl vggmtlsfim lpniiiatkn afanvpitik
      301 daafalgaph irvildhslp ialpriihgt mlavarvlge sspllvigmv afiadtprsf
      361 fdpatvlpvq iyiwssspei afvelaaiai iallimlfal nlvanfvkrk feffnf
//
LOCUS       WP_175938889             365 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Caballeronia].
ACCESSION   WP_175938889
VERSION     WP_175938889.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..365
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40325
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdhlqsmkvf vrvadlgsfa raasamdisn avatrhvadl esrlgtrlln rttrslslte
       61 sgqvylerar qildeledve qmvvarnhep lgslrivapv vfglhnlapv lqtyaqrypk
      121 vvpdvtlvdr qvdlveegfd vgiviarqvk sasvvtrrlt tgcmtvcatp eylekhgtpt
      181 rpehllehpc lslpseywgd ervftgpdge vrvrpqnvii anntemlrqf allgmgiail
      241 psyligndmn rnqlvrllgd yqlpqveinv aypsrrhlpa kvrtfidhlv ehfsqtpnhq
      301 lgeqwirdgi gkpaaassae ahyahadeak apppaprsrs mdgelgpkla kpsrtrgrvp
      361 aaspf
//
LOCUS       WP_175938942             246 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Wolbachia endosymbiont
            of Litomosoides brasiliensis].
ACCESSION   WP_175938942
VERSION     WP_175938942.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Litomosoides brasiliensis
  ORGANISM  Wolbachia endosymbiont of Litomosoides brasiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Wolbachia endosymbiont of Litomosoides
                     brasiliensis"
                     /db_xref="taxon:1812117"
     Protein         1..246
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27122
     Region          20..245
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mshesveknl nfvkklndvn dsvlkienla laydnkkvln ginisiekgd vvtilgpngg
       61 gktslmkvva gisknytgsi ifadnikisy mpqnfsisnl mpitvkyfll nsfskklkkn
      121 qsfiteviel vgisdilksq vleisagqmq llllahclia epdliildep vsamdinara
      181 kfydiigkia knrlisilmt shdlssivpc sdyiicinrt iycqgkpnei medktlseif
      241 ssyiak
//
LOCUS       WP_175938973             367 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Caballeronia sp. BCC1704].
ACCESSION   WP_175938973
VERSION     WP_175938973.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..367
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=39418
     Region          36..367
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mptvnraprn tlkaavrata vaamigffaa gaahaqssvs lygqvdewvg atkfpgsqra
       61 wnvsgggmst sywgmkgaed lgngykaift lesffraqng rygrfdgdtf farnsyvgiq
      121 gpigtftagr lttqlfvsti lsnpfvdsyv fspmvahvfl gqgtfptytt dqgvtgdsgw
      181 nnavqyttpd fnglsgsamy afgnsagdnr skkysaqfly fhgpfaatgv yqyvnfnntp
      241 gdlptsnaft ipgfksqsvg qlgasfdmky vkffaqymyt kndieptsfh vntgqggvtv
      301 pvgpgtvmas yaysrsnggl dqthkswavg ydyplskrtd vyaaylndky tgmssgdtfg
      361 vgirakf
//
LOCUS       WP_175939223             527 aa            linear   BCT 11-JAN-2025
DEFINITION  S41 family peptidase [Caballeronia sp. BCC1704].
ACCESSION   WP_175939223
VERSION     WP_175939223.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..527
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=57432
     Region          43..393
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mrknlknfsl iaagvavgal atlqisasaq qaassplpld qlrlfaevfg qikheyvepv
       61 ddkklltaai kgmvssldph ssyldktdye elqeqtkgrf aglgieisse dglikvispi
      121 edtpafragi rpgdlitrin dkpvrgmtld kavkqmrgep gtkvtltifr ksddrtfplt
      181 vtralirvqs vkmkvpepgy gyiritsfqe rtvpdlaakl qdlarqqpdl kgivldlrnn
      241 gggllqsavg vagaflpdna vvvstngqia dakqtfrdty dnyrlpsfds dplknvpdif
      301 kkvpmvvltn aysasaseiv agalqdhhra livgkttfgk gsvqtvrpmt adtalrltta
      361 yyytpsgksi qnqgvrpdvp vdqyaegdpd dalvtrevdy snhlantqdp nekkeqeqre
      421 qdrldqlrll eeqndkktpe qrrkdrdrkp vefgsnddfm lqqalnkleg kpvvesksfs
      481 erklaqnkpa rsasapvvaq palpatpgss pasgaapass ptaqqsk
//
LOCUS       WP_175939069             513 aa            linear   BCT 11-JAN-2025
DEFINITION  UDP-N-acetylmuramate--L-alanine ligase [Wolbachia endosymbiont of
            Litomosoides brasiliensis].
ACCESSION   WP_175939069
VERSION     WP_175939069.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Litomosoides brasiliensis
  ORGANISM  Wolbachia endosymbiont of Litomosoides brasiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Sangshetti,J.N., Joshi,S.S., Patil,R.H., Moloney,M.G. and
            Shinde,D.B.
  TITLE     Mur Ligase Inhibitors as Anti-bacterials: A Comprehensive Review
  JOURNAL   Curr Pharm Des 23 (21), 3164-3196 (2017)
   PUBMED   28201974
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433731
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Wolbachia endosymbiont of Litomosoides
                     brasiliensis"
                     /db_xref="taxon:1812117"
     Protein         1..513
                     /product="UDP-N-acetylmuramate--L-alanine ligase"
                     /EC_number="6.3.2.8"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008763 - UDP-N-acetylmuramate-L-alanine
                     ligase activity [Evidence IEA]"
                     /GO_process="GO:0007049 - cell cycle [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=55697
     Region          19..498
                     /region_name="MurC"
                     /note="UDP-N-acetylmuramate-alanine ligase MurC and
                     related ligases, MurC/Mpl family [Cell
                     wall/membrane/envelope biogenesis]; COG0773"
                     /db_xref="CDD:440536"
ORIGIN      
        1 mndiqegiih iigiggigms aiaeilhnsn ykvqgsdaqs snnvdrlqkl gmeiytghna
       61 nnikqaqvvv yssaiksdnv elvaarnnnk ailhrsdila eivkdkyvia vsgssgkttt
      121 tamiasifdh sgadatvivg gilnsyqnns rlgksdifli eaddsdgtml kipaniavit
      181 sinddhidhy gtfdniknaf srfinsadfa ilpnsvgisd skssyvtfgi egvypfviqs
      241 lfvtpvcdig iqkkklashh akainikarn irqynnsief dvliddcsis rshwipvsca
      301 gitavpplls tqmtpvrsri iknvvlsnai gihkvsnala aisvamklgv ndldikkgll
      361 gfkgvarrfs lvadikgvkl iedyahhpse iqatltaars iakgkiigii ellrfarihn
      421 ffnefirifm mfdyiilvpi hppedkpipg criddiqeal inngfnnvki mddallisnf
      481 isdstnsgdi vlfigagnnv arlaretvvf mle
//
LOCUS       WP_175939290             232 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: fumarylacetoacetate hydrolase family protein
            [unclassified Caballeronia].
ACCESSION   WP_175939290
VERSION     WP_175939290.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..232
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25072
     Region          22..232
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mtyvfppapa tavpvagsne qfpvrriycv grnyeahare mghdpdrepp fffskpadav
       61 lyvapgstge lpypsqtknl hfemelvaai gkqgkdipad kgldyvygya lgldmtrrdl
      121 qaeakklgrp wdtakgfdhs aplgpihpvs kvghleksai wltvngeekq rsdisqliws
      181 vgetvaylst lfelfpgdli ftgtpegvga vvkgdllkgg vdgigdfsvr vv
//
LOCUS       WP_175939398             138 aa            linear   BCT 11-JAN-2025
DEFINITION  HIT family protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175939398
VERSION     WP_175939398.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..138
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15576
     Region          1..124
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mdcvfcredg gevlwsddal rvvladepdw pgfcrviwga hvaemsdlad adrarvmtav
       61 ngveramrrv lvpekinlas lgnqvphlhw hviprfsnds rfplpvwapr qrtvseaqla
      121 krraqatllr eavrreln
//
LOCUS       WP_175939419             121 aa            linear   BCT 11-JAN-2025
DEFINITION  FmdB family zinc ribbon protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175939419
VERSION     WP_175939419.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..121
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11579
     Region          1..77
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 mpiyayrcas cghekdvlqk lsdapltqcp acgkdafskq vtaagfqlkg sgwyvtdfrg
       61 gsngsaapks gdnagnsnsg dsakagsass sdastsasaa paagasttat patpatpsga
      121 a
//
LOCUS       WP_175939489             471 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Caballeronia sp. BCC1704].
ACCESSION   WP_175939489
VERSION     WP_175939489.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..471
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=51207
     Region          15..468
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mnhpalphai rrpfpaalld alkqhfaerv stsqavrehh grdespfdpq lpdavvfars
       61 teevqaivrl caehdvpiip ygngsslegh llavqggvsi dlsemnsvvs inaedltatv
      121 qpgisrkqln ealkdtglff pidpgadasi ggmsatrasg tnavrygsmr envlaltvvl
      181 adgrvihtgt rarkssagyd ltrlfvgseg tlgviteitv rlypqpeais aavcafpsmg
      241 davravieti qmgvpiarve fvdklavrai nrhsnltlre spmlffefhg teagvkeqaq
      301 tvqeitaqnh gtdfewatrp edrsrlwtar hnayfamlql kpgcravttd vcvpisrlae
      361 cveetekdll gsslpcpivg hvgdgnfhva mlldpakpee rdeaerlnrr iveralkvgg
      421 tctgehgvgl hkmdfmldeh gedgidvmrs ikhaldprnl mnpgkifaft r
//
LOCUS       WP_175939493             277 aa            linear   BCT 11-JAN-2025
DEFINITION  carbon-nitrogen hydrolase family protein [Caballeronia sp.
            BCC1704].
ACCESSION   WP_175939493
VERSION     WP_175939493.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10166075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..277
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30247
     Region          15..274
                     /region_name="nit"
                     /note="Nit1, Nit 2, and related proteins, and the
                     Nit1-like domain of NitFhit (class 10 nitrilases);
                     cd07572"
                     /db_xref="CDD:143596"
     Site            order(52,108,125,129,140,165..166,168..169,188)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143596"
     Site            order(52,125,165)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143596"
     Site            order(126..127,146..148,166,169..173,175..176,196..197,
                     200..201,203..205,207..208,238,268..269,272..273)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143596"
ORIGIN      
        1 mteqssestv rpfpvaalqm vstpdrdrnl aeagrliaea aqsgaqlvll peyfcfmgfk
       61 dtdklairet pgdgpiqqfl sgaarkhgvw viggtlplks peasrvlnts lvfgpdgeqv
      121 arydkihlfn fekgdesfde arsivpgadv rtfdapfgrv glsvcydlrf pelyrkmgdc
      181 alivvpsaft yttgrahwet llkaraienq cyvlaaaqgg khengrrtwg hsmlidpwge
      241 vvavreegag vvagvidper iasvrqslpa yrhrvia
//
LOCUS       WP_175939479             123 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DUF805 domain-containing protein [unclassified
            Caballeronia].
ACCESSION   WP_175939479
VERSION     WP_175939479.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..123
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=13611
     Region          11..121
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 mdffdairva lfekyatfng rasrseywff qllslviaiv atvlsetknd spiavwtmci
       61 igfalllpgl avtvrrlhdt drsgwfylia cvplvgsill lfwscergtp gvnrygsdpl
      121 gns
//
LOCUS       WP_175939523             274 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ferritin-like domain-containing protein [unclassified
            Caballeronia].
ACCESSION   WP_175939523
VERSION     WP_175939523.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10090058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..274
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32094
     Region          44..171
                     /region_name="Ferritin_like"
                     /note="Ferritin-like superfamily of diiron-containing
                     four-helix-bundle proteins; cd00657"
                     /db_xref="CDD:153097"
     Site            order(75,78,130,160,163)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 mhtdsthvmp wriedidlnr idrqkaasne hlllllcacs fiesgtdlyt snlstyfrdd
       61 peiaawlnne wepeemqhgr alktyinhvw pefdwdtafk nffaeysltc syeqfekkra
      121 lemvarcvie tgtatlyrai necsdepvlk eitdnirvde vrhykhffrf fkkwnkiegn
      181 grlavlgalv rrvaelksed seialrhvfa irypervkds tynrelfaqv nalvrrnlsa
      241 dqcikmllkp ldlpariqpg vhyplakitq lffr
//
LOCUS       WP_175939478             319 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: hydrogen peroxide-inducible genes activator
            [unclassified Caballeronia].
ACCESSION   WP_175939478
VERSION     WP_175939478.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Jo,I., Chung,I.Y., Bae,H.W., Kim,J.S., Song,S., Cho,Y.H. and
            Ha,N.C.
  TITLE     Structural details of the OxyR peroxide-sensing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 112 (20), 6443-6448 (2015)
   PUBMED   25931525
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444038
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..319
                     /product="hydrogen peroxide-inducible genes activator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35095
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..301
                     /region_name="PBP2_OxyR"
                     /note="The C-terminal substrate-binding domain of the
                     LysR-type transcriptional regulator OxyR, a member of the
                     type 2 periplasmic binding fold protein superfamily;
                     cd08411"
                     /db_xref="CDD:176103"
     Site            order(103,106..107,110,114,122..126,225,228..229,232,
                     235..236,238..239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176103"
ORIGIN      
        1 mtltelkyiv avarerhfgr aaeacfvsqp tlsvaikkle delnvqifer gtsevsvtpi
       61 geqivtqaqr vleqtlaike iakqgkdplv gplrlgviyt igpyllptlv kqmiksvpqm
      121 plmlqenytl kliellkqge idvaimalpf petglmvral ydepfvvamp sghawenrsk
      181 idpddlkqet mlllgsghcf rdhvlgvcpe lmrfsqnadg iqktfegssl etirhmvasg
      241 vgitvlprms vmevkphapg idsgllsyvp fdepvpdrrv vlawrksftr mpaidaisda
      301 iaacdlpgvk kldmpvavn
//
LOCUS       WP_175939525             499 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Caballeronia sp. BCC1704].
ACCESSION   WP_175939525
VERSION     WP_175939525.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..499
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=53624
     Region          1..431
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfdslglse pllravnelg ytnptpiqlq aipavlkggd llagaqtgtg ktagftlpil
       61 qrlsqmapaa agskrpvral iltptrelaa qveesvrayg kylklrstvm fggvginpqi
      121 dalrrgvdiv vatpgrlldh mqqktidvsq leilvldead rmldmgfihd ikrvlarlpq
      181 krqnllfsat fsdeikalad slldspalie varrnttaer ieqkihpvdr drkrellthl
      241 irqhdwfqvl vftrtkhgan rlaeqltkdg isalaihgnk sqsartrala efkdqtlqvl
      301 vatdiaargi didqlphvvn fdlpnvpedy vhrigrtgra gaegeavslv cvdelqllkd
      361 ierlikrpip qeviagfepd pnakpepiqr rsqgrggpre ggrahggsqd qarapkagng
      421 agqgqrdgrg skpanakpag hgnagvkpap rrpeaahaag hapaprakag npgallggks
      481 rndnggarrd gmrtggrgr
//
LOCUS       WP_175939545             552 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Caballeronia].
ACCESSION   WP_175939545
VERSION     WP_175939545.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..552
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59369
     Region          18..538
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(31..32,35..36,39,77,135..136,138..140,143,163,
                     166..167,170,256,259..260,263..265,268,296,300,464..465,
                     469,473,489,492..493,496..497,500)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 matvegrish apmtneerkv ifasslgtvf ewydfylags laiyisktff sgvnptagfi
       61 ftllgfaagf avrpfgaivf grlgdmvgrk ytflvtivim glstfligfl pgyatigiaa
      121 piifiamrll qglalggeyg gaatyvaeha pankrgawta wiqttatlgl fislivilav
      181 rtatgeeqfg awawrvpflv silllavsvw irmklhespv feriksegkt skaplteafg
      241 ewknlkivll alfgltagqa vvwytgqfys lffltqtlkv dgtsanimva valligtpff
      301 vffgslsdri grkpiimagc liaaltffpl fkalahytnp tleaatqksp itvianpdec
      361 sfqfnpvgts kftsscdiak salskaglny qnvaapagtl aqikvgetvv ntydgkaada
      421 kaqgaafdkt lagtlksagy pakadpalin wpmaivilti lvifvtmvyg piaamlvemf
      481 parirytsms lpyhigngwf ggflpatafa ivaargdiys glwypvvial atfvigmlfv
      541 kdtrksnvyh ed
//
LOCUS       WP_175939592             463 aa            linear   BCT 11-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Caballeronia sp.
            BCC1704].
ACCESSION   WP_175939592
VERSION     WP_175939592.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..463
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48156
     Region          26..434
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 masstshpkv hpcderlptg qlltlgiqhv lvmyagavav plilgaamhl skdevaflis
       61 adlfscgvat liqtlglwif girlpvimgc tfaavgpmva igtnpslgil dvfgatiaag
      121 vigiflapmi gkllrffppv vvgtviavig lslmgvginw aaggvgnpdy gnpvylllsl
      181 vvlslillin kfargfiani svllgivagf viaamlgrvn mdgvahapwv givlpfhfgm
      241 phfdalsvat mvivmfvtfi estgmflavg dlverpvdqk alvrglrvdg lgtliggvfn
      301 sfphtsfsqn vgligvtgvk srfvcatggv ilvvlglfpk maqvvasvpp fvlggagivm
      361 fgmvaangik vlskvdfvkn hhnlfivavs vglglvpvva pkffsqlpha lepilhsgil
      421 lasvsavvln ivfngvrker earceirqag hdfdgaaras eaq
//
LOCUS       WP_175939638              68 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [unclassified Caballeronia].
ACCESSION   WP_175939638
VERSION     WP_175939638.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..68
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7253
     Region          1..65
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mstgtvkwfn dakgygfitp deggedlfah fsaiqmngfk tlkegqkvtf eivqgpkgkq
       61 asniqdaa
//
LOCUS       WP_175939646             435 aa            linear   BCT 11-JAN-2025
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Caballeronia sp. BCC1704].
ACCESSION   WP_175939646
VERSION     WP_175939646.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..435
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=47188
     Region          11..419
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mrlhgfligq tetlladvlr fsgpadaats rffrahpklg hgergviaea vfavlrrkme
       61 fshlaesgtg nqarrlallg lmqtagltal kpfvsadehq wlaqvskidp aslpvrvrtn
      121 lpqwiydama krfepdelaq laaalnypap ldlranpika srdvvrkali dagidafdmp
      181 fapfgirveg kpaltrlqpf qegwievqde gsqllcslva prrgemivdf cagaggktla
      241 lgammrstgr lyafdvsdrr laklkprlar sglsnvnpvl idsehdakik rlagkidrvl
      301 vdapcsglgt lrrnpdlkwr qspatvaelt pkqlsiltsa arlvkaggrl vyatcsmlea
      361 enegvvaqfl ethpnfrvvp ardvlaeqri eldtgeylsl wphkhgtdgf faavlervpg
      421 akaqaaeega geasa
//
LOCUS       WP_175939683             318 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Caballeronia].
ACCESSION   WP_175939683
VERSION     WP_175939683.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..318
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33926
     Region          10..69
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          100..307
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(114..115,117..118,121,125,127..133,238..243,
                     249..250,252..253)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176144"
ORIGIN      
        1 mdernapiel rllryfvtva eemhfgraaa rlamtqppls qairaledal gvalfartkr
       61 tveltpvgkd llpevrrila aadalrplaq slsrgeagvl slafvstady gllpallrdf
      121 garypgvrlq lteatsdvqi eelvagrvda glvipplppr hamslsylai areplvvams
      181 sdaaeqlqqg taewadtpvd lrdlaaaplv vfprrlapgl ydiimgcyga agltprigqe
      241 aiqmqtivsl vsagmgvalv pqslrhlrrt gvvyrplrpv adapvvetgl vwraaevspv
      301 lagfieivra raaavsal
//
LOCUS       WP_175939814             232 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175939814
VERSION     WP_175939814.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..232
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25092
     Region          10..232
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mfeirrsner ghanhgwlds yhtfsfadyh dpehvhfgal rvinedrvag gqgfgthghr
       61 dmeivsyvle galahrdsmg ngstirpgdv qrmsagtgvr hsefngspte tahflqiwii
      121 pdapggapgy eekrftddek rgrlrviasp egtdgsvkig adarifaglf dgderaefdv
      181 pagrrvyvhv argkvsvnge algagdaaki ediakvtidg geraevllfd la
//
LOCUS       WP_175939737             438 aa            linear   BCT 11-JAN-2025
DEFINITION  replication-associated recombination protein A [Caballeronia sp.
            BCC1704].
ACCESSION   WP_175939737
VERSION     WP_175939737.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..438
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=48300
     Region          2..430
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 mfeenrgtvp laerlrprti devigqkhll gpskplrvaf esgeahsmil wgppgvgktt
       61 larlmaaafd aefislsavl sgvkdireav etaqihrang rqtlvfvdev hrfnksqqda
      121 flphvesglf vfvgattenp sfevnsalls raavyvlksl dadelkelle rataelgglt
      181 ftdearealv gsadgdgrkl lnnleivara aaqqkktevd gallgsalae nlrrfdkggd
      241 afydqisalh ksvrgsnpda alywfcrmld ggadprylvr rivrmawedi gladprgari
      301 aldaaetyer lgtpegelai aqaliylava pksnagynay nearrfvsrd qsrgvpvhlr
      361 naptklmkel gygheyryah depdayaage tylpdgmrdp hwyqptprgl egkigeklar
      421 lseldeawrr ehpdpkkr
//
LOCUS       WP_175939879             399 aa            linear   BCT 11-JAN-2025
DEFINITION  benzoate/H(+) symporter BenE family transporter [Caballeronia sp.
            BCC1704].
ACCESSION   WP_175939879
VERSION     WP_175939879.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..399
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41315
     Region          13..398
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mkatpsvaha plrpfadtsv savvagfvam mtgytsslvl mfqagqaahl sdaqisswiw
       61 alsigmalct iglslrfrap ivvawstpga allvtslpnv pyaeaigafi acavlltavg
      121 vtgwfdalmk ripsgiaaal lagilfeigi eifraaehqt alvlamffty lvvkratpry
      181 aipatlaagv avadalglld fsrfhvalah pvftmpafsf saivsigvpl fivamasqnv
      241 pgiavlradr yttpsaplia ttgiasllla pfgshgvnla aitaaictgp eaherhdrry
      301 taavwcgvfy liagifgati aalfaafpka lvvsvaalal fgsimsglan amhdarqrep
      361 alvtfmvtas gltllsigpa fwgliagvvt hvilnarrg
//
LOCUS       WP_175939847             287 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SDR family oxidoreductase [unclassified
            Caballeronia].
ACCESSION   WP_175939847
VERSION     WP_175939847.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..287
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=31362
     Region          2..214
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mtilvtgatg rvgrqvveql vsrhadvrvl vrdpskaqfp aevtvalgdm ldidslrraf
       61 agvrtlflln avagdeftqa litlniares gvervvylsv mhadrfvnvp hfavksgaer
      121 miermgfsat ilrpayfidn elmirdvvvd hgvypmpigs kgvamvdtrd iaevaaiell
      181 rrdeaaadlp vevidlvgpd tltgsalasi wsdvlgrpva yggddpggfe qnlssfmpkw
      241 mayemrlmae ryvsdgmvpe agdverlvrm lgrplhtyrd fvtqlag
//
LOCUS       WP_175939883             121 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: c-type cytochrome [unclassified Caballeronia].
ACCESSION   WP_175939883
VERSION     WP_175939883.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 121)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 121)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 121)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..121
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12698
     Region          20..102
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mnyfvgklav iavlsglagf atqasadvvg nakaaegkva mcigchgipg yrtaypevye
       61 vpmlggqnaq yisnalhayk kgdrhfdtmr aiavtlsdqd iadiaayyaa qtpqsknnpd
      121 k
//
LOCUS       WP_175939884             134 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Caballeronia sp. BCC1704].
ACCESSION   WP_175939884
VERSION     WP_175939884.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 134)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 134)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 134)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..134
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14004
     Region          35..128
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mkpyqapsqa qsqafrfsfk aacaaaaiig ssafgtahaa dagngkvlse shncaachgp
       61 glnkpvsgey pklagqhaty iywalrqyqm gngnpnfgrn naimaaqvqn lsqsdlkdia
      121 ayiesldgsl vlkk
//
LOCUS       WP_175938786             127 aa            linear   BCT 11-JAN-2025
DEFINITION  TraR/DksA family transcriptional regulator [Wolbachia endosymbiont
            of Litomosoides brasiliensis].
ACCESSION   WP_175938786
VERSION     WP_175938786.1
KEYWORDS    RefSeq.
SOURCE      Wolbachia endosymbiont of Litomosoides brasiliensis
  ORGANISM  Wolbachia endosymbiont of Litomosoides brasiliensis
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 127)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 127)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Wolbachia endosymbiont of Litomosoides
                     brasiliensis"
                     /db_xref="taxon:1812117"
     Protein         1..127
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14744
     Region          22..120
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mkessktklp ksytpsedee ymsikqleyf nlklesmlae lekqeledsa yysdedggne
       61 klikrrkdkk ekikealeki klgtygycnr tgeeigvarl kanplavyci eeqerlekek
      121 nvyntdd
//
LOCUS       WP_175939968             338 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175939968
VERSION     WP_175939968.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..338
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38520
     Region          138..294
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mfhvilssld sfvssvqttl yvdvvqpllf kigmmdyded tydalywviv gvleviamya
       61 ilrplealrp aeqwqdrkgv rvdvlytwiv klgilnlfff ftfqpvfdsv qswlrihgvp
      121 tleidnlwpg vttqplvtfa iylilldlag ywyhrlehrf giwwelhavh hsqqkmslws
      181 ddrnhllddv lqasffaava lvigvepsqf vvlvaitnlm qsvqhanirl hfgwlgdrli
      241 vspafhrrhh aigyghegta ygcnfgvlfs fwdilfrsas fdrtveptgi rdqlgapgta
      301 pvnygdgffe qhwlafkrig arlaarraad sgkrpaal
//
LOCUS       WP_175939985             708 aa            linear   BCT 11-JAN-2025
DEFINITION  M3 family metallopeptidase [Caballeronia sp. BCC1704].
ACCESSION   WP_175939985
VERSION     WP_175939985.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..708
                     /product="M3 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=79253
     Region          14..700
                     /region_name="Dcp"
                     /note="Zn-dependent oligopeptidase, M3 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0339"
                     /db_xref="CDD:440108"
ORIGIN      
        1 msdttaatpt taasnplldf sdlprfgdik pehvtpaldv llaaaksavd rasapdtpat
       61 wqdvvetver eseklsrawg ivghlnavad tpelraahae nlprvtefsa svgqnlalye
      121 kykaiaagde faglsperkk ilenalrdfr lsgaelpedr kprfaqlqee qaalskafsd
      181 hvldstnays yvvtqqsdla glpddvieaa reaaqkegke gwkftlhfps yfpvlqyaeh
      241 rpmreamyra yvtraselge tyghgkpewd ntqnivehlk lrqeeartlg yqnfaevsla
      301 pkmaespaqv iafledlakr arpyaendwm elrafaatel gmpelqpwdv ayaaeklrqk
      361 rysfsenevk qyfpqeavlk glfkvtetlf nvsirrdeaa vwnpdvrffr venkdgslva
      421 qfyldlyare gkrggawmdd ararhkrtqg dvqtpvaylt cnfsapvggk pacfthdevi
      481 tlfhefghgl hhmltrvdel gvsgingvew davelpsqfm enfcwewdvl tdmsahvetg
      541 qplprelfdk mlaaknfqsg lgtlrqivfs mfdmvlhtsy dpangtqnvn dlareinekf
      601 hvipqapfsr wpntfshifa ggyaagyysy kwaevlsada yaafeeaaka angsvlnaet
      661 gtryrreile vggsrpamds fkafrgreps idallrhngm sehtqtvh
//
LOCUS       WP_175939994             244 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: (Fe-S)-binding protein [unclassified Caballeronia].
ACCESSION   WP_175939994
VERSION     WP_175939994.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..244
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26498
     Region          <2..237
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mrvglfvtcl idmmrpeigf sviklierag fevsvppaqt ccgqpaynsg drrlardlae
       61 ktlrefeqfd yvvvpsgscg gtirahygdl frddpelmnr ysrlqprvfe ltdflvtvak
      121 armepgvfdg ivtyhdacsg lrelgvksqp rellaqagvp vkemagcehc cgfggtfavk
      181 ygdistaivd ekcanikasg aeavvlgdlg cmlniegrlr rtgdtttrvl hiaqvlagda
      241 qrlt
//
LOCUS       WP_175940006             135 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175940006
VERSION     WP_175940006.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..135
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=14259
     Region          9..126
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 msapvvtati gsadyetrle dgthtwfade paslggadsa pqpsslllss lgactsitlr
       61 myakrkgwpl eslrvelsmn ttadgtvidr risldgplde aqrerllqia nacpmhkvlv
      121 gairidsglv paepv
//
LOCUS       WP_175940010             248 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MotA/TolQ/ExbB proton channel family protein
            [unclassified Caballeronia].
ACCESSION   WP_175940010
VERSION     WP_175940010.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..248
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=26539
     Region          5..220
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mqnygiahvw aqgdfvtrgi alalvimsvl swtvivvkaw nvvrlkrltk naeqafwhsd
       61 dfndgiqklg aqsssaadnp flalalagqe aadhhhqtqp hlhdrmdvsd witrclkdvm
      121 desvgrmqag lavlasigst spfvglfgtv wgiyhallti gatgqtsidq vagpvgesli
      181 mtafglfvai pavlgynalt ranksivtkl nrfahglhaf fvtgsklsst krattgqsds
      241 lrlatras
//
LOCUS       WP_175940037             229 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Caballeronia].
ACCESSION   WP_175940037
VERSION     WP_175940037.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 229)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..229
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24583
     Region          1..229
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 mslygfgpll wagaketlal allslavsvl lglvgasakl srhgllrgia tayttlirsv
       61 pdlvlmlllf ysiqiainhv tdafgwdqfd idpftagvlt lgfiygayft etfrgaflav
      121 prgqleagsa ygmsgmrvfg rilfpqmmrf alpgignnwq vlvkatalvs iigladvvka
      181 aqdagkstfn mfffiliaal iylaittasn fvlmaleqry stgvrhadl
//
LOCUS       WP_175940056             235 aa            linear   BCT 11-JAN-2025
DEFINITION  SOS response-associated peptidase [Caballeronia sp. BCC1704].
ACCESSION   WP_175940056
VERSION     WP_175940056.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..235
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=26212
     Region          1..232
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mcgrisqyrl pmhyaerlhl knpfvlvdaa drrpgynlsp gthplavypd etiravhwgy
       61 cppwarekkl pqtinarvet astsayfrdl wrnarilvpa dgwfewrvep rpgdragkpf
      121 kqpyyirrad gepmflaalt sivgdedaat pgagfvivts kadeglvdvh drrplvfsps
      181 agrrwldata tpadlhalvk sdgvpaahfv whrvtsdvnr tvndeprlie plaaa
//
LOCUS       WP_175940058             485 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Caballeronia sp. BCC1704].
ACCESSION   WP_175940058
VERSION     WP_175940058.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..485
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=52072
     Region          1..474
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mtasaatfid acvqllgash vltddhdtep yrvdwrkryr gnacavllpa dteqvagivr
       61 larehrvaiv pqggntglag gatpdasgaq aiislkrlnr irgvdphnnt itveagvvla
      121 eiqaraesaq rlfplslaae gsctiggnls tnaggtgvlr ygntrelclg levvtpqgei
      181 wdglrglrkd ntgydlrdlf igaegtlgii taavmklhpa pvakvtalag lasphaaldf
      241 lamaqqhagp lltgfelmsd fsmrlvgrhf pqlrypfgep hgqtvllels dsesdehara
      301 lferlmeqai eegivedavv aenlaqsqaf wdlrehipla qaqeglnikh diavpissig
      361 rfidetdaii akavpgarmv tfghlgdgnl hynvqapegv dqkafliefq tpinalvyeq
      421 vhkhrgsvsa ehglgqlkvd eamrlkspve vrlmqtikaa ldpenlmnpg kvvrwnaeag
      481 kekta
//
LOCUS       WP_175940180             368 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Caballeronia sp. BCC1704].
ACCESSION   WP_175940180
VERSION     WP_175940180.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 368)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..368
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39324
     Region          6..368
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 mifpyrlear ptpsramqla vpvvaavatl vigflifsvv gqdplramha ffieplstvn
       61 gwselvlkas plcliglgla vgyranvwni gaegqmllgg ivaggiaihv gdasgwwtlp
      121 lmviggiagg mlwaaipall ksrfntneil tslmltyvat qlliylvsgp wrdpegmnfp
      181 isamfvddal fprlygdwhw sflkgtrina svfltviaip lvwlfmrksf agfrmnvggl
      241 aplaaryagf sdkktiwtsl llsgglagla gvgevagpig qlqagwspgy gftaiivvfv
      301 grlhpvgivl asllmallyl ggeavqtslq lpqalagvfq glllfcllgc dlfvnyrirr
      361 rtpahraa
//
LOCUS       WP_175940307             262 aa            linear   BCT 11-JAN-2025
DEFINITION  TatD family hydrolase [Caballeronia sp. BCC1704].
ACCESSION   WP_175940307
VERSION     WP_175940307.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..262
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29125
     Region          2..257
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mfvdshchin fegladrlpd vldkmrahav thalcvsvdl etlpsvldia ercenvyasv
       61 gvhpdhedak epsvaelvel aahpkvcaig etgldyyrle grsiadmewq rerfrthira
      121 ahatgkplii htrsssedtl rimeeerasv pggvmhcfte pwdvaeaala qnffislsgi
      181 vtfkkatdvq dvarrvpldr llietdspyl apvpyrgkpn epayvsyvgr fiaqlreqtd
      241 eavaqattdn ffrlfkiara aa
//
LOCUS       WP_175940323             351 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [unclassified Caballeronia].
ACCESSION   WP_175940323
VERSION     WP_175940323.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..351
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38140
     Region          11..344
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mnnnqsvhqn ffhillfvvt valgwvllpf fgaifwgail allfqpmqrw ltvrfgkrrn
       61 laalttlaaa iliviipvsv vavtlvqeva lvytriksgd lnfgmyfqhv lhalpasvqq
      121 llgryglddi ggvqsklmeg asrisqfaaa qalligqntf qfivsfgvml ylvffllrdg
      181 geigrrirra lpldpapkqh liakfttvvr atvkgniava avqgflggli fwilgingsl
      241 lwgvlmafls llpavgaalv wapaalyffm tgeiwrglvl vafcvvvigl vdnvlrpilv
      301 gkdtkmpdwv vlistlggma lfgingfvig plvaalfmas wdifsqdedg q
//
LOCUS       WP_175940335             459 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175940335
VERSION     WP_175940335.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..459
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51986
     Region          <374..437
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mleqyddlyp klyagdvesc arflderrav dgntaeywhw raivhlragq flqaldicfm
       61 ltrlsdsfaf hvhcmcdvaa hlglkevala giesfaqkas tpeiaaflwr vygwhylged
      121 nrvlelrpdg idehsafvlg hhqarsrmrl hgiehgveam hqywssddar rvlfphvnre
      181 gywtgqralp armsvrlias gfgdlvnwar yigalqamgv avdydadlfr vatpeadrad
      241 yvrameaagf trptgdgamw tdpftlftal fpvlghapsh ryvepanpas vdavidriwh
      301 rargrrcvgv fwsscesann fasrsltlpd ldplfdtqsd vywvvmqrgf errrwlndpr
      361 sndldrfttl dldmtlgqca alidrldafi gndgglthfa galgkrtylf lnhvaewrye
      421 regattawyp nvrlvrarel gawgdvvgtl qrllnadar
//
LOCUS       WP_175940389             296 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Caballeronia].
ACCESSION   WP_175940389
VERSION     WP_175940389.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..296
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31352
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176112"
ORIGIN      
        1 mtpdqlitfa tvaehgnisr aavalhlsqp avsgqlrlln eefgeplyqr dgrgirltpa
       61 gegllgyatr lreayqqaha lrdamrgles gtlrigastt pasyllpyli aafrkrypdv
      121 vvttidgnta eivaalgsld vaiiegpagl glpptagvtp wlddeivaiv raghpladgr
      181 agatlevige hslvlrergs gvrqiveraf aeagvemrva leiagvegvk eavragmgig
      241 fvsamsirhe ddalrrlhia peplmrrfsl lvphaaapsr aaarfveice draaig
//
LOCUS       WP_175940399             271 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Caballeronia].
ACCESSION   WP_175940399
VERSION     WP_175940399.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..271
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29125
     Region          2..256
                     /region_name="FetB"
                     /note="ABC-type iron transport system FetAB, permease
                     component [Inorganic ion transport and metabolism];
                     COG0390"
                     /db_xref="CDD:440159"
ORIGIN      
        1 mngyqnlslv diglaaaliv vngalsvald lglerrllia avrtvvqllf igyvlgwvfa
       61 fsrwyvvlpl mvlmtviagl aasdrgrrty agqradsivs iwgsswliga fglfvvirih
      121 pwyepqytip ilgmvlgntl tgvslgierm teeltagrga vemslalgat rweaakgpar
      181 qavragmipt lnqmavvglv slpgmmtgqv lagqsplqav ryqivimfli aaasglgvvg
      241 avvmtyrrlf spdhrfnask lverkakkrr a
//
LOCUS       WP_175940401             155 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [unclassified Caballeronia].
ACCESSION   WP_175940401
VERSION     WP_175940401.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..155
                     /product="VOC family protein"
                     /calculated_mol_wt=16729
     Region          14..137
                     /region_name="VOC_like"
                     /note="uncharacterized subfamily of vicinal oxygen chelate
                     (VOC) family; cd07246"
                     /db_xref="CDD:319910"
     Site            order(14..19,21,36,50..51,58..59,61..63,82..84,86..91,97,
                     118,123,131..134)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:319910"
ORIGIN      
        1 mshspvkaip egmhsltphl vcagaaeaie fykrafgave mgrlpgddgk lmhamvkigd
       61 smlmlvdehp dfgmlgaksl kgspvtihly vedvdatvkq aeaagarvtm pvadmfwgdr
      121 ygrledpfgh qwsvathkrd vspaemqqgk capre
//
LOCUS       WP_175940418             393 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acetyl-CoA C-acetyltransferase [unclassified
            Caballeronia].
ACCESSION   WP_175940418
VERSION     WP_175940418.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 393)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..393
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40565
     Region          1..393
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mtdvvivsaa rtavgkfggs lakiaapelg atviravler aglkpeqise vilgqvltag
       61 sgqnparqsv ikaglpemvp gmtinkvcgs glkavmlaan aiiagdseii vaggqenmsa
      121 aphvlpgsrd gfrmgdakli dsmivdglwd vynnyhmgtt aenvakeygi treaqdafaa
      181 lsqnkaeaaq kagrfndeiv pvsipqrkge piqfatdefv rhgvtaeala glkpafskeg
      241 tvtaanasgi ndgaaavvvm sakkaealgl tplarikaya sagvdpkimg mgpvpaskrc
      301 leragwsidd ldlmeineaf aaqalavhkq mgwdqekinv nggaiaighp igasgcrilv
      361 tllhemqkrd akkglaslci gggmgvalav erl
//
LOCUS       WP_175940489             149 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF2147 domain-containing protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175940489
VERSION     WP_175940489.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Barison,N., Cendron,L., Loconte,V., Proctor,E.A., Dokholyan,N.V.
            and Zanotti,G.
  TITLE     Protein HP1028 from the human pathogen Helicobacter pylori belongs
            to the lipocalin family
  JOURNAL   Acta Crystallogr D Biol Crystallogr 69 (Pt 8), 1387-1394 (2013)
   PUBMED   23897462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..149
                     /product="DUF2147 domain-containing protein"
                     /calculated_mol_wt=15918
     Region          1..149
                     /region_name="COG4731"
                     /note="Uncharacterized conserved protein, DUF2147 family
                     [Function unknown]"
                     /db_xref="CDD:443765"
ORIGIN      
        1 mkhfvriaag aliamsaaga faqasspagt wqtiddatgk pkaiiqiidd gsgqlsgkvv
       61 rgigefdhpd rrctactddr kdqlvkgmti itgmkqngdt weggqildpe ngklykckmk
      121 ledggqklvv rgyigvsllg rsqtwvrqq
//
LOCUS       WP_175940538             204 aa            linear   BCT 11-JAN-2025
DEFINITION  LemA family protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175940538
VERSION     WP_175940538.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..204
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22344
     Region          6..193
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mgwntalfal ilglagcgyn siqaedeqvk aswaevlnqy qrradlvpnl vntvkgyanq
       61 erevltrvte arsrvgsiqa tpevlsdpqa farfesaqgq ltsslsrllv vsenypqlks
      121 danfrdlqaq legtenriav arnryiksvq qynstvrsfp nnltakafgy qqkpnfsvan
      181 eaeitkpprv dfgatpasas gvnn
//
LOCUS       WP_175940573             410 aa            linear   BCT 11-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Caballeronia
            sp. BCC1704].
ACCESSION   WP_175940573
VERSION     WP_175940573.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..410
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=44816
     Region          24..397
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mrffpsgfsv spvsafvptt aihrrafkaa vvlpavlaaa safaqvpppa vtahswvlvd
       61 atsnqvlasg npdervepas ltklmtaylv fdalkskkin mdqtvmptea vrrvrtdesr
      121 mfieankpvt vhdlvygmii qsgndaaial aelvggsean fvnlmngaaq rigmkhthya
      181 dvngmpdpqh yttagdlavl strlirdfpe yysifsekef tynkikqpnr nrllwldpsv
      241 dglktghtka agycliatak rslpgmpdas rrlvavmmge pkesarvqds lkmlnygyta
      301 ydalrlykan qviesprvyk gasdnvqagv etdqyitvpk glgdkvkpti trndlliapi
      361 kkgqqigtvr mmadgkdvaq fplvalqdvp qaglfgrlwd sallmwqkkk
//
LOCUS       WP_175940619             384 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: porin [unclassified Caballeronia].
ACCESSION   WP_175940619
VERSION     WP_175940619.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..384
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=40373
     Region          14..384
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkkallaaaa lltfsavaqa qssvtlygrl dagleymngv ptgvgangaa tgsshrfrae
       61 sgdwgtslwg mkgvedlggg yravfqlegs fntmtgqgpg ggglfnrwat vgiannnfgt
      121 lllgrelfia ngvwdfdpfg qsnwssaslv rgrnwpqssn nisyqspkfa gfdfygqyal
      181 snatnwngng ttpqgregga yityttplfq irgmydeirn pangtlggay nalnggtnng
      241 ngvyaysrey tamfnlflgq fkvqgayqai rssgmvgqlp gqpttldhew ggvtwqatpa
      301 aaligavyhv ngnngagnat iytvggsynl skrtlfdlqv atvqnsksan yglnannfgt
      361 aaatdnpfag hsqtgvyagi qhsf
//
LOCUS       WP_175940768             157 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA thioesterase [Caballeronia sp. BCC1704].
ACCESSION   WP_175940768
VERSION     WP_175940768.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..157
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17620
     Region          3..135
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mnfhtrkwvk pedlnpngtl fggsllrwid eeaaiyaisq lgnqrvvtkf mseinfvssa
       61 rqgdiielgi tatnfgrtsi tlraevrnki trksiltvek mvfvnlneqg epaphgrtqi
      121 ryadelfeay rrdqraveap kastddigre etaeaah
//
LOCUS       WP_175940787             674 aa            linear   BCT 11-JAN-2025
DEFINITION  AI-2E family transporter [Caballeronia sp. BCC1704].
ACCESSION   WP_175940787
VERSION     WP_175940787.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 674)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 674)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..674
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=72192
     Region          37..376
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mpplpgprrp pakilppdap glralaslva vvvvicalyf gravmipiil aillsfllap
       61 fvdflrrlrf gqvpsvivav fvalsvltav galigaqvaq lasdlpkyqv averkvdsvq
      121 rmtvgradaf lgrasralkr lspareqeph anednpaasp idqpmpvevh epapsplela
      181 qrflspvisp lettgivlvv avfillqred lrdrlirlfg srdlhratta mdeaarrlsr
      241 yflaqlginv gvgivicigl avigvpgall fgvmtallrf vpyvgtwiaa llavifaaav
      301 gpgwtmliwt ivlygatdii agqiveplly ghstglspfa vivaaifwsw iwgpiglvls
      361 tpltlclvil grhvdrlefl dvlfgdrpal tpaenfyqrl landpdealv qaesllkdrs
      421 lvayydeval eglrlahndv lrgvvtadql krinesaldi iegledaedv tpvvqrkeep
      481 lvnlaaddtt aiasesppey fdaaaeghta svlciagrsp lddlaatiav qlfrkhglga
      541 dltgyerfsr grfgevdlsg vtiicvvsfd aaesppylrn llrrlhqrap aaelivglvv
      601 aesplqgevl vrtssaavsf kelvdacvaa arrqstdgvs wagldsqasa ptvdnrsraa
      661 qadapalrnv lgda
//
LOCUS       WP_175940796             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Caballeronia sp. BCC1704].
ACCESSION   WP_175940796
VERSION     WP_175940796.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33445
     Region          9..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,232,249,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,195,
                     226..230,237..238,241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 magfneriln gisvfaaivd agtfaaagek lgmsqpgvsr aiarlearln irlfdrttrt
       61 vsltddgrrf feqvmphlig leeaastasg satavrgrlr vnvdpifsrl vlgpkleafm
      121 eahpelelel ltrdrlgdmi adgfdlavrf geprnsslva rklldtpvrt vaapsyiarc
      181 grpatpqala sgahtciefr dpetgrpfpw efhrkkkrlt vetrghltln dpgtmlsacl
      241 sgygiaqile lghahlmaeg alidlfpdwp derfplyafh psrhhppakt rafldmvial
      301 tgaetgg
//
LOCUS       WP_175940834             361 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [unclassified
            Caballeronia].
ACCESSION   WP_175940834
VERSION     WP_175940834.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..361
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39863
     Region          20..339
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mnpaeslppl sidgqsksri rfgivllpnf tltafsgfvd llrlsadegd fsrpvrcsws
       61 vigetlspvr ascgiqitpw etyeqaepfd yvvvvggllh sgasasdatl qfirraaard
      121 ativgmctgv ftlmragvld ghrvcvswfh ywdfverfpq adeqllvadr lfvidrrrit
      181 csggrasidv aaaillrhfe tatvqkalri llvddmqkgn apqphppgla pathpkvkra
      241 illmeqhvgr sltldelahk ldmstrqler lfkaetgkap qayakqvrlr taawlltssd
      301 ktvadiassc gfsdashlgr efrkqfglpp mmyreqrgad teevhhamdy detfpgraqa
      361 i
//
LOCUS       WP_175940841             142 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: dihydroneopterin aldolase [unclassified
            Caballeronia].
ACCESSION   WP_175940841
VERSION     WP_175940841.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Illarionova,V., Eisenreich,W., Fischer,M., Haussmann,C.,
            Romisch,W., Richter,G. and Bacher,A.
  TITLE     Biosynthesis of tetrahydrofolate. Stereochemistry of
            dihydroneopterin aldolase
  JOURNAL   J Biol Chem 277 (32), 28841-28847 (2002)
   PUBMED   12039964
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..142
                     /product="dihydroneopterin aldolase"
                     /EC_number="4.1.2.25"
                     /GO_function="GO:0004150 - dihydroneopterin aldolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0046656 - folic acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16251
     Region          15..125
                     /region_name="FolB"
                     /note="Dihydroneopterin aldolase [Coenzyme transport and
                     metabolism]; COG1539"
                     /db_xref="CDD:441148"
ORIGIN      
        1 mkpyeplhtg gqgwrvivde lvvmtrvgly ehehrapqai sidaslryrg mpredelidy
       61 eawcnrvtvy lqekthtrll etlaveiaal sfdawpalda ltlalhkpki regtrrlale
      121 ldwrradyda wrvqqalavs sa
//
LOCUS       WP_175940852             388 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Caballeronia sp. BCC1704].
ACCESSION   WP_175940852
VERSION     WP_175940852.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..388
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39859
     Region          59..361
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mntikridpr rpfivttagl rritlgevgt galqdfasah aahrdtakpr rttkparrsv
       61 lvaahtdrga fddharqala aaalladdet eivliafgaf dddaaslgad riieldafds
      121 rrfapdeelr alaacaaafa pahlfmpdna tgdgdlgrry aalagasiat hvveldatha
      181 asyaqagraw asralpevvm lapnavdakl pfvgagerva segivpaata sayvdlgiee
      241 ldaaqialee adfivsagng vsdvaafeal astlgaaiga srvavddgkf trdkqigatg
      301 ktvqasvyia fgisgavqhl qgikdcrhvi avntdasapi akranltvva dthetikalt
      361 daaaaarasr gngasivlda plaegvfa
//
LOCUS       WP_175940888             112 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: thioredoxin family protein [unclassified
            Caballeronia].
ACCESSION   WP_175940888
VERSION     WP_175940888.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 112)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..112
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=12263
     Region          23..104
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(33,36)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mtmtteyakt apdrseidam taptvvefgt dwcgfcraaq pliaqafqah rgvhhikied
       61 gsgrplgrsf rvklwptlif mlegkevarl vrpgdvgeir dalalidepl ae
//
LOCUS       WP_175940933             421 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: flippase [unclassified Caballeronia].
ACCESSION   WP_175940933
VERSION     WP_175940933.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..421
                     /product="flippase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45887
     Region          6..403
                     /region_name="MATE_Wzx_like"
                     /note="Wzx, a subfamily of the multidrug and toxic
                     compound extrusion (MATE)-like proteins; cd13128"
                     /db_xref="CDD:240533"
ORIGIN      
        1 masfrknfti lmtlqvstyl aplltlpwla rvlgpseygr lsfamaftay fitltnfsfs
       61 ltatpkisin rdnravrsqi fwetmyaqia lsvagflvll vltfvvptla enrqlllvgf
      121 gmaigsmlip twyfqgvedl gvisalvfvg ralsipamyl fvrhhddvnn amlvntlvpl
      181 gsgiaiciyl yfrrdidfvh vslktvidrl kdgwsvfmat slvdiyassn ivlltfisgn
      241 vaggyfaaad kliraalnml rplktaaypr vsflmhhare dafaflrkmf vvqgtivsli
      301 svgiffgapl avkllygpqf gptvdvlrwm afvplmsglt dlfgvqtmlp lgmkshfsrv
      361 ligsailnfs llavlavlfg eqgaaatvli vetaiaaama ftlhlegvpl lkrpmtpgga
      421 g
//
LOCUS       WP_175940935             453 aa            linear   BCT 11-JAN-2025
DEFINITION  hemolysin family protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175940935
VERSION     WP_175940935.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..453
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=49624
     Region          17..448
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 maqvvalvga lllvalngff vaaefglvkl ratrvkaiar tnglpgrlla kvhgqldayl
       61 sacqlgitla slglgwigep afaallhplf alvgvhseqv iesvslffaf svisflhivv
      121 gelapkswai rraeqvglwl atplygfywl mypfiwvlnt sanlvlrlfg msaehghdaq
      181 ystdelklil rgrrhggass ynadewntia hsldfsrmtv sdlmrpahel vglrndlpar
      241 enlaiisrhr fsryplyada sgervigmvh lkdllldrgl asrtfsfsit kdasklekls
      301 ryarpvqyva pnlsalelfr rfrkgaphla ivgrkgakpi gfitldnllg alvgqihdef
      361 rqgdadwsrm ddgtlmgkgs lpvvsleral gididegrae svgglvinal gdlpsegqrv
      421 gfdhfdivvk kmngprivlv rvypreeale gae
//
LOCUS       WP_175940964             291 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: dienelactone hydrolase family protein [unclassified
            Caballeronia].
ACCESSION   WP_175940964
VERSION     WP_175940964.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..291
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31575
     Region          48..285
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mlspevdsli prvpfdrrtf ikaafgtgfa aavlpvsaqt ihtdadglea gaigvrgadg
       61 tlipayraqp lgkthlpvii viheifgvhe hiadvcrrfa klgylaiapd lytrqgdasv
      121 ypsiqqlndq ivskvpdsqv lsdidetvkw agehggdlkr lgitgfcwgg ritwlyaehn
      181 prvkaavawy grlagnktan spsnaidnag elkvpvlgly grqdpsipqd tieqmkqaia
      241 ngppsargsq fvvyddapha ffadyrpsyr kadaedgwkr alawfhehgv k
//
LOCUS       WP_175940984             878 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AAA family ATPase [unclassified Caballeronia].
ACCESSION   WP_175940984
VERSION     WP_175940984.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 878)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 878)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 878)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 878)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 878)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 878)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 878)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..878
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..878
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=96192
     Region          76..708
                     /region_name="RloC"
                     /note="Wobble nucleotide-excising tRNase [Translation,
                     ribosomal structure and biogenesis]; COG4694"
                     /db_xref="CDD:443729"
ORIGIN      
        1 mqiinkiaaw aaeqpawidd avrrlmagkl tdkdlhelaa lakaehglad pnhpvpkrld
       61 pevmpvagnd grdvslkalr spqhlnaidp gqaltfeaag ltvvygyngs gksgyaralk
      121 macrarnven ilpdvyaask gpassgavfd wnegqtaqsq awivgtvppa plsqisvfda
      181 hcarvfvdsq akvlfvpdgm evihglsdal gaiqrlieid rksnvfdhsq laslagttvv
      241 grahaqlgrk sdvealkkla vlsdeeeaer qvlskllkea dpvklaaair rtatrlgslr
      301 nelaaleapl sdkatghlad afvvmvamea asklaaeale adgatvagtg tepweilmrs
      361 aikyatevay pghafpgpeh dahcvlcqqp lteeangrlk sffqflqada qkkaiearev
      421 skrlylaika lnfgafpadp alfeelqenh paletairey vaaltrrqas vaamtpnrkl
      481 dplqalpasp famldelisk qlreaarlek altpqerelk tklladfdar aklaemlpkv
      541 leaidwhkrd nsfgeaikgc strtvtskis elyeahvtee lrkafaqela dlglsrldva
      601 lemtgqkgar mqqlklrtss qyarakasdi lsegeqrvia malflaevgi epgrsglifd
      661 dpvssldhmr reriakrlvl eakrrqiivf thdlafpwal kdfaedngvs vadrhiyaag
      721 prkgicqdgl pfegkkltar vndlleqakr arkvleeehn nelyndivrn cyrrmrdtwe
      781 llieehlfag tvkrfrrave tsklryvsvg daeasavfng mtrcsnfthe ggaeappalp
      841 dpdeflsdie alaaalkmid enkketekrr leaglatq
//
LOCUS       WP_175941044             588 aa            linear   BCT 11-JAN-2025
DEFINITION  thiamine pyrophosphate-binding protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175941044
VERSION     WP_175941044.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..588
                     /product="thiamine pyrophosphate-binding protein"
                     /GO_component="GO:0005948 - acetolactate synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0009097 - isoleucine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009099 - L-valine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=62848
     Region          33..586
                     /region_name="IlvB"
                     /note="Acetolactate synthase large subunit or other
                     thiamine pyrophosphate-requiring enzyme [Amino acid
                     transport and metabolism, Coenzyme transport and
                     metabolism]; COG0028"
                     /db_xref="CDD:439799"
ORIGIN      
        1 msevvssrpe vapatttadd tlkqktrgag vvsgghlvar alknegvdti ftlcgghiid
       61 iydgcvdegi riidvrheqv aahaadgyar qtgklgcvvt tagpgctnav tgvatafrse
      121 spmihiggqg altqhkmgsl qdlphvdmms pitkfaatvp stervadmvs maareafnga
      181 pgpayleipr dvldreidvs kavipqpgry rastksvgdp kdiekladll vnserpaily
      241 gqqvwtargq eeaiallrgl dipgyfngas rgllppgdph hfdrtrsqaf akadlivivg
      301 tpfdfrmgyg kriskelklv qidmdyrtvg knrdidlglv gdpgailgav lqaasgrlkn
      361 dkrqsrqawm relaaaeeta taklmplfts daspihpyrv aheinqflsd dtiyigdggd
      421 vvtisaqavr prrpgqwmdp galgslgvgt gfaiaaglan pekevlcyyg dgafsmtsfd
      481 metanrfgvp yiavignnsa mnqirygqla kygeergnvg nllsdvpygr faemlggyge
      541 evyeaskiag alqraresia ktgksavini wvdptvyapg tmaqtmyk
//
LOCUS       WP_175941047              84 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CsbD family protein [unclassified Caballeronia].
ACCESSION   WP_175941047
VERSION     WP_175941047.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..84
                     /product="CsbD family protein"
                     /calculated_mol_wt=8594
     Region          1..60
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 mvqdqvegta qnvvgkvqda vgaltgdsgt qvegkarqal gslqqtygqt ldnvrsavsd
       61 qpingvliaa avgfllgalw nrdr
//
LOCUS       WP_175941053             172 aa            linear   BCT 11-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Caballeronia sp. BCC1704].
ACCESSION   WP_175941053
VERSION     WP_175941053.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..172
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18428
     Region          1..167
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 miechvrpsp lgpilyraed acltglffvg qkhfpaglpp haivhdgrpa prvieaacde
       61 iaqyfagerl tfsvpvrlrg tpfqqqvwdl lrqipfgdaw tygdlarrlg lppgasravg
      121 gangrnpvai ivpchrvigg dgeltgyagg vdrkrslltl eggrgraqla lf
//
LOCUS       WP_175941076             199 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175941076
VERSION     WP_175941076.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..199
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20750
     Region          <18..>134
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mrahpfselt dvlspdlalv pdapsagpra psgdmsdaey delvafhgie rerlvlihpg
       61 shlstpawsa eqyadvadql aadgwqiaiv gdapdperta gvlgamqtaa lflagavgpr
      121 tlprliadaq lllsddaaap spvavaralg tphivlaeqp ravgsdtitr raraelsdve
      181 hahpgrpftl hmpavydas
//
LOCUS       WP_175941118             520 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175941118
VERSION     WP_175941118.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..520
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54417
     Region          38..520
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mpspirsses ldvdallaal pdriadvpar waarapahpa liedarrlsy gdlsqavdaa
       61 aerlaslgvq ggdrvmivae ncvaqivllf avarvdawal vsnarlsage ldaiaaharp
      121 kliafatdas pdarahaarl gatpagalpv digawsyrvd asapaepvaa dgaaqcaali
      181 yttgttgapk gvmlshrnll fiaatsstlr rvspddvvyt vlpvshvygl asvclgslya
      241 gatlrlaprf apeavriala degvtifqgv pamhaklleh lhthghawha prlrfaysgg
      301 spldanlkar vervygvplh ngygmtessp titqtpldap ranssvgvpi pgvdmrivap
      361 dgtdvpqgev geirvrgpnv mlgyyrnada traavspdgw lstgdlarqe adgavtiagr
      421 skeliirsgf nvypveveqv lnahpdvvqa avigravegn eevlafvelv pgaaadeaal
      481 hawcaerlap ykrpahirvl dalpaastgk vlkhklrela
//
LOCUS       WP_175941140             664 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Caballeronia sp. BCC1704].
ACCESSION   WP_175941140
VERSION     WP_175941140.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..664
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=72117
     Region          1..461
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          594..659
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(616,625..627,634)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            626
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mfnkilianr geiacrvaat arrlnvasva vysdadakak hvdvcdeavr vggsaasesy
       61 lrieriveaa katgaqavhp gygflsenee fanaceqagi vfigppveai ramgskaaak
      121 almqsasvpl vpgyhgddqd aallqreadr igypvllkas aggggkgmrv versedfmqa
      181 lasckreaas sfgndrvlie kyllrprhve vqvfadthgn avylfdrdcs vqrrhqkvle
      241 eapapglsde trramgeaav aaaravnyvg agtvefimtq dgqfyfmemn trlqvehpvt
      301 emvtgldlve wqlrvaagep lplkqdelrv nghaieariy aenpsrgflp stgtlkhlal
      361 peaveftldg nvridsgvre gdaitpfydp miaklivhgr drrdalarma ralaqceivg
      421 lqtnveflqr ivksepfsqg eldtglierh rdalfapspv srgkalalac aalltregge
      481 ahghspwdal shwrmaggys qdlnwravdt dealkvvftk drekrlqwde ktarfdwshr
      541 getsftvqld dalikghvft dgdtfhvfye gaafafewqn lmahagdaeh egrltapmpg
      601 kviavlveag asvekgapli vmeamkmeht ivaptagkig eilfdvgdqv adgsqllvle
      661 aqpa
//
LOCUS       WP_175941131             297 aa            linear   BCT 11-JAN-2025
DEFINITION  ferritin-like domain-containing protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175941131
VERSION     WP_175941131.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10090058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..297
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33370
     Region          70..194
                     /region_name="Ferritin_like"
                     /note="Ferritin-like superfamily of diiron-containing
                     four-helix-bundle proteins; cd00657"
                     /db_xref="CDD:153097"
     Site            order(78,108,111,147,184,187)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 msdtltpvea dhamrnwiyr segririgse lhkrmfceml ltthnpykpa viewpkldpa
       61 alrrvtslpi wdiavqtegr asirvatyaa svsdpllnea lrmnggeear hklvlsklve
      121 aygielapep pypapddalr awmltgysec idsffafglf eaarqsgyfp ealvetfepv
      181 iqeearhilf fanwvawyrr slpwyrkpgf llktagvwlt lirdrislar gfdksgaaqd
      241 anfpanvgds vagnvsvgal idlclvener rmagydarll rpttvpmlar larrfvk
//
LOCUS       WP_175941139             314 aa            linear   BCT 11-JAN-2025
DEFINITION  ketopantoate reductase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175941139
VERSION     WP_175941139.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..314
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32661
     Region          1..312
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkiailgaga mgslfgglla esgeavtlid vndahldair rdglriddgr gerrirvlqa
       61 vrpeaanada aaspdasfdl livftkslht rtaldgvral ltphthvltl qnglgnvetl
      121 ntfvplesil igvttwpada agpahvrshg agtirmmtad gyahpfatav adalsragla
      181 ctldadvwaa iwekvafnaa lntlcavtgc tvdqlgnqhd gprlalaiaa etaavarang
      241 iavdgeriar nvehaigehr ghrpsmlqdv lagrrteida isgkvvaaar eagvavphte
      301 tllalvrlid arvn
//
LOCUS       WP_175941185             421 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Caballeronia sp.
            BCC1704].
ACCESSION   WP_175941185
VERSION     WP_175941185.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..421
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47432
     Region          94..398
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mnldwlpdtl srhlptqpwa qlllglaalf viaefaqwvi arvllriahr llvlaghaaw
       61 dqafirhray hrlwyaapfa vvalgigevp highwatava rvahgaawvc vflamgsals
      121 awqdvyaask eaqtrsikgy iqigklalgl icfvlvlsil idrsplwmls glgalsavll
      181 lvfkdtllsl vastqltsnd mlrigdwiem pqaladgavk dialhtvkvq nwdntittvp
      241 tyklfsesyr nyrhmfesgg rrikrtmrid aqcvrfltde etqrmmrfrl lhdyllqkqt
      301 eveqanrnlg elaaepanrr rltnigtfre yglaylqhhp eirqdmtimv rmmepesqgi
      361 pvevycftat tawaqyeriq gdvfdhllai lpemglrlyq apsgtdfagv agrlrgempt
      421 l
//
LOCUS       WP_175941201             895 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175941201
VERSION     WP_175941201.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 895)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 895)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..895
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..895
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=97865
     Region          15..827
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnsqalrsal lagpvqherl vkldtplgpd lllphrvkgr srlgrhfeft vdtvsvsdsl
       61 elkkliaqpv tlwvqqadrs yaphhgyvha arrlgsdsgv thyqivfasf lhflkfrrdq
      121 riwqdrsadd iiadvlnqhp qakgrftfkl yqplpsrsfc mqyeddwnfv hrlmesegly
      181 gfweqdkdgk shrlvivdri dalpalsprt vrfhhagtgd eadtlvqfsg trtlrsvert
      241 trtfdykqpp tasnpkathr ptianqgdlp qqlevyeytg aytypeqsrg dhlskiwmee
      301 qeshakrfhg vggvrrmdag rtfefadhpe hdkddagqre favietawii vnnlpvgdgq
      361 aafphslqae igsivqagga dssrvrhpdg segffrisie aqrttvpfrs plehakppmh
      421 lqsaivvape geevhtdeln rvkvrfhwdr lndgdekasc wlraatsdsg nsygavhphr
      481 sgeevlvdfl ggdcdrpiiv gklyngatsp qwhtngilsg yrskeyagag ynqlvlddat
      541 sqnrvhlyss qtnahlhlgy lidhtgnnrg sylgsgfdlr sdaygavran rglyvtthpk
      601 rpasqpldve etqqqlvrae glmeamsdvs aqhqgesldp ghaalkqftd atqnsvsgsa
      661 sggrtagggt gsanafkepv mlfgspagig mstqqstqla adrhinlvsg qsthvaagks
      721 liasvldris lfaqnagmkl fagkgkvevq ahadnielta qkalklmavt esiegaaake
      781 illtsggayi riadgnievh apgkidikga qhafsgpthl sqtmptlpns tgnydqafia
      841 hwagtdipva ntryqmfsng kllsegvtna agetgltqsh vphdvvvkfl gksng
//
LOCUS       WP_175941226             481 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia pyrrocinia].
ACCESSION   WP_175941226
VERSION     WP_175941226.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..481
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51788
     Region          1..389
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfeslglae plvkavnelg ytsptpiqqq aipavlgggd llagaqtgtg ktagftlpil
       61 qrlhtfyaeh rgakravral iltptrelaa qveesvrays kylklrstvm fggvsinpqi
      121 dalkrgvdiv vatpgrlldh mqqktidlsd ldilvldead rmldmgfihd ikrvlaklpp
      181 qrqnllfsat fsdeikalad nlldspalie varrnttaes vaqkihpvdr drkrellthl
      241 irehnwfqvl vftrtkhgan rlaeqltkdg isamaihgnk sqsartrala efknstlqvl
      301 vatdiaargi didqlphvvn fdlpnvpedy vhrigrtgra gatgeavslv cvdekqllrd
      361 ierlikreip qeviagfepd pnvkpepilq rrgqqqprgg ggggggnrqp raggsgqpaa
      421 krdanaqpka sqqkaakprt qggaggnggr pagggnsarp asgnaahpnr nrssrsgqrg
      481 h
//
LOCUS       WP_175941233             415 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia pyrrocinia].
ACCESSION   WP_175941233
VERSION     WP_175941233.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..415
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43273
     Region          23..409
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtnhrvmaiv gaghaggraa qvlresgwrg rivligaesh lpyerpplsk gvltgersaa
       61 qcrlrdpdaw aadgiepvva tveridphar evrvsggrvf gydalllatg ararrlaipg
      121 aaldgvfalr tlddaaalgp rlvpdarivm igggfiglev aasarlrgcr vtvldaaprl
      181 lgravpesia arvqalheeq gvairvnrkp vaiertsgga lavalddgdt liadtvvagi
      241 giepadelar daglavdrgi vvnarletsa rgihaagdva vfpsalsgrp vrqetwhgae
      301 tqaraaarnm lgadepyrdm pwfwsdqyda qlqvagepal gelvvarrld gdaeihfhfd
      361 gggrlvaasg fgrasgfvke mklartlver gaaaapaava dsnvklksll ptaga
//
LOCUS       WP_175941293             320 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia pyrrocinia].
ACCESSION   WP_175941293
VERSION     WP_175941293.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..320
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34572
     Region          81..282
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mswqskfacw llrrqfrpet trevldptra rrfadlrtav prrapsgyrl rqcngagdap
       61 lrgewlertd agagrgpgrt llyfhgggyy fcstkthrpl vfgltkragv rsfsldyrla
      121 penrfpaald dalaayrqll algtppesiv fggdsagggl alatlvalrd rgeplpagai
      181 lfspwtdlag tgdtmrtndg adpmfagaal akaaklylgd apatnpyasp lyadftglpp
      241 lfiqvgstev mlddsrrvae kakaagvpve ievwpdmphv wqlyapvvpe ardaldraaa
      301 flrrvavera vqrigdasia
//
LOCUS       WP_175941343             143 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: response regulator [unclassified Caballeronia].
ACCESSION   WP_175941343
VERSION     WP_175941343.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..143
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=15372
     Region          26..143
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mpvnlhspqc alwtnrsidv dlpcwrilvv ddnassaeal aaaltadgfe trvalsgvda
       61 lhavdgwvph ivildismpe hdgfatarvl rriartrdag iiaftalgee lvrtkglhag
      121 fdaycqkgns patlvhlmqr lvh
//
LOCUS       WP_175941366             205 aa            linear   BCT 11-JAN-2025
DEFINITION  SCO family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175941366
VERSION     WP_175941366.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..205
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22430
     Region          51..205
                     /region_name="Sco1"
                     /note="Cytochrome oxidase Cu insertion factor,
                     SCO1/SenC/PrrC family [Posttranslational modification,
                     protein turnover, chaperones]; COG1999"
                     /db_xref="CDD:441602"
ORIGIN      
        1 mlhtrfgrra rqgwmlacaf aaalllagcd napkfqnldi tgntqfgndf slpdtagkvr
       61 tladfkgrav vmffgythcp dvcpttmael sealkqlgpd aakrvqvlfv tvdperdtpa
      121 llgqyvpafd psfiglrpad eaalkkvtkd frvyyakvpg ktpgsytmdh taasyvfdrd
      181 gklrlfvrdg qgpgpwvhdl kllvd
//
LOCUS       WP_175941370             267 aa            linear   BCT 11-JAN-2025
DEFINITION  ComF family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175941370
VERSION     WP_175941370.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..267
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=27970
     Region          85..242
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mnrssaprtm rvvlsqvral aarvaavalp nrcalcgnls havicvacda vywnearlrc
       61 dvcalplgvg qprsrplrgg hggaaraday rcdacrtaap pfdatlalad yrapldglar
      121 glkfharlal gaefaarlar lvddtrgtgg fdlvapvpls hrrlvvrgyn qawaiarpla
      181 rrlgvhadaa lltrvadtap qsrlalrarr dnvmaafava gdvagrhval vddvmtsgat
      241 leaaahavka agaarvtnlv alrtard
//
LOCUS       WP_175941398             101 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF485 domain-containing protein [Burkholderia pyrrocinia].
ACCESSION   WP_175941398
VERSION     WP_175941398.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..101
                     /product="DUF485 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=11012
     Region          4..100
                     /region_name="YjcH"
                     /note="Uncharacterized membrane protein, DUF485 family
                     [Function unknown]; COG3162"
                     /db_xref="CDD:442396"
ORIGIN      
        1 melsviesvt arrdyeqlvr arrrfsftlt almiatyygf illvalaphv laaplyrgat
       61 ttvgiavgva iilvaiglta cyvlranraf drrvdailqr s
//
LOCUS       WP_175941403             478 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Caballeronia sp. BCC1704].
ACCESSION   WP_175941403
VERSION     WP_175941403.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..478
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47801
     Region          19..455
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(26..27,30..31,34,66,116..117,119..121,124,146,
                     149..150,153,278,281..282,285..287,290,318,322,374..375,
                     379,383,399,402..403,406..407,410)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mngmnsnlss rqlcvvaats vgfvvsqldv sivnvalasi ahdlgasvas lqwtvdayal
       61 gfaalmllag slgdrlgarr lfvgglavfa faslacafsr daaqliaara iqgvgaaaml
      121 pnslallnaa cghdrrvrar avglwtaaga vsiaagpivg galiaafgwr sifwvnlpic
      181 aagvaatlaw vdetpshgrg dgidlsgqal aivaltalvg tviearplgl shplvtgafa
      241 iavtataafi averrsrapm lplalfsert fsaavlfgia vnftyygsvf vlslylqrvl
      301 gqtplqagla flpltggfll snlasgpvva rfgsrgpmia galldaagfa slafvdahtp
      361 tvalllpfll ipsgmgvavp amttallgtv gqrragtasa vlntarqaag amgvaafgal
      421 aghaggaaas aqivdavrws aaasvamlac aaviargvrg gtaadgneaa nrprravk
//
LOCUS       WP_175941421             204 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)-dependent oxidoreductase [unclassified
            Caballeronia].
ACCESSION   WP_175941421
VERSION     WP_175941421.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..204
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=21848
     Region          3..204
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 msriaiigat gnvgsrlthe alrrghtvta lardtsklet regldardvd aldldalada
       61 iaghdavfsa trfstvpesa ivgavkragv erllvvggag slylapgqrl ldapgfpday
      121 raeatagaaf ldalrrdrel nwtfvspsae fvsgprtqrf rtgvdellvd angrswisfd
      181 dfaiafldef ergahikqrf tvgy
//
LOCUS       WP_175941430             314 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia pyrrocinia].
ACCESSION   WP_175941430
VERSION     WP_175941430.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..314
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33134
     Region          39..280
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 mnasnespad aaaagaapah taavgvasag tppaaaanag dlvievrnlt krygrnivhq
       61 kldfdvrrge ivaivggsgs gkttlvrqil glerptsgti kvfgedtati ddasarmmrt
      121 rsgmlfqqga lfssmtvfdn vaqplrelgr vppdllhdiv mlklemvglp ckhaskmpaa
      181 lsggmvkrvg iaraialepe llfldeptag ldpqasdefv eliatlhrtl gltvvmithd
      241 ldtmvalstr vavladrkvl vaapveeaan vdhpfiheyf lglrgrralq alpperrakl
      301 pkaalepals svel
//
LOCUS       WP_175941431             272 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [unclassified Caballeronia].
ACCESSION   WP_175941431
VERSION     WP_175941431.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..272
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29182
     Region          44..242
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 matlldqeqr prlcieevhi aghvqpivlr syrpasdgtv lpivlyfhgg gfthgnldda
       61 diaastiard tpawvvsvgy slapaypfpa apedgyraaq wafahargqr adpqrmgvag
      121 hdaggnlatc vaaiardrgd irvsaqalla plldpsmtrv aderkvlcpd lelsecarcy
      181 raylpnpsqr lhpyaaples rrlaglppal iasaehdllh ieaekyaael iaagvptevt
      241 rhckashqal aahaaalkdv vaffrkrlar tt
//
LOCUS       WP_175941435            1066 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit [unclassified
            Caballeronia].
ACCESSION   WP_175941435
VERSION     WP_175941435.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..1066
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114880
     Region          1..1042
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mniskffidr pifagvlsvv vllagiiamf rlpiseypev vppsvvvhaq ypganpkvia
       61 etvaspleeq ingvedmlym qsqansdgnl tttvtfklgt dpdkntqlvq nrvnqalprl
      121 pqdvqrlgvt tikssptltm vvhlnspngr ydmtylrnya linvkdrler iagvgevqlw
      181 gsgdysmrvw ldpqkvaqrg ltatdvvnai reqnvqvaag viggsptlpn vplqlnvnar
      241 grlqnesefr divlktspdg avthlgdvar velaaseygl rslldnksav aiainqqpga
      301 nslqisdevr ktmkelqadm pagleyqivy dptqfvrssi eavihtlaea ialvvlvviv
      361 flqtwrasii pllavpvsiv gtfslllafg fsinalslfg mvlaigivvd daivvvenve
      421 rnieaglsar eatyqamrev sgpiiaialt lvavfvplaf msgltgqfyk qfamtiaist
      481 visafnsltl spalaalllk ghdepkdwlt rgmdrvfggf frrfnavfhr gsesyskgvk
      541 gvinrkaimm vlyavllgga vlmgkivpgg fvpaqdkeyl isfaqlpnga sldrtegvir
      601 emsaialkqp gvesavefpg lsvngftnss sagivfvtlk pfkdrvhdka lsanaiagal
      661 nqkyagikgs fiavfppppv lglgtlggfk mqledrgalg yaaladatqa fikrasqtpe
      721 lgptfssyqi nvpqlnvdld rvkakqlgvs vtdvfdtmqv ylgslyvndf nrfgrvyqvr
      781 vqadapfran pedigllktr nangdmvpls slvkvsptyg pemvvryngy taadinggpa
      841 pgyssgqaqa aaeriaaevl prgikfewtd ltyqqilagn aalwvfpisv llvflvlaal
      901 yesltlplav ilivpmsils allgvwltdg dnniftqigl mvlvglsakn ailivefare
      961 lemqgrsivq aaieasrlrl rpilmtsiaf imgvvplvls sgagsemrha mgvavffgml
     1021 gvtlfglmlt pvfyvilrkl srtehvtdkh gthpqmrgig asyeaq
//
LOCUS       WP_175941446             288 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175941446
VERSION     WP_175941446.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..288
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30910
     Region          29..283
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mpasplpddd ladsdtddaa sgehdekvrs giqsievgfr lldvltsepr ammlrdlaqr
       61 agmspakahr ylvsfsrlgv vsqdpvsgry elggfalqmg larlarvdgv klarialtef
      121 rdrldqtvgi avwgnqgpti vhwmesshpa kaslklgdvm pllgsatgll faaylprskt
      181 aamlerelad trrsphhggp rtldevdavl advrehqaar vegmllptih afcmpvfdav
      241 gelalaival gqegsfdiaw ggeidtalra carklsyelg yspdarda
//
LOCUS       WP_175941485             212 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175941485
VERSION     WP_175941485.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..212
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23114
     Region          4..195
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mnayrlylsp gacslaahia leetgapfdv eivsvqkqqn learylaina karvpvlaip
       61 geprvltetp ailtylarry pdarllpldd plrearchew lawlvgwvhg vgygalwrpg
      121 rfigdpalhg avsthgrgti daanekieaa ladgrtwaep gghsivdpfl lvlyrwgvai
      181 gldmtrhpaw tahaqreaer paarralare ag
//
LOCUS       WP_175941516             261 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia pyrrocinia].
ACCESSION   WP_175941516
VERSION     WP_175941516.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..261
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=27038
     Region          9..242
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 merkplvgit adhtqigaha shtvgdkyva aivdgaqala mvlpalgerq saddildtvd
       61 gllftgsysn vephlyggkp sapgtkhdpa rdattlpllr aaiaagvpvl avcrgfqeln
      121 vvcggtlhqr vhevpgladh seddaapmdt qygpahvvhl tpggklhala ggrdevhvns
      181 lhkqgiaqlg sglaveavap dglieavsvv dapafalavq whpewrhahd plssaifraf
      241 gdacrarrna raramaaaal a
//
LOCUS       WP_175941534             404 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: amino acid aminotransferase [Burkholderia].
ACCESSION   WP_175941534
VERSION     WP_175941534.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Alexander,F.W., Sandmeier,E., Mehta,P.K. and Christen,P.
  TITLE     Evolutionary relationships among pyridoxal-5'-phosphate-dependent
            enzymes. Regio-specific alpha, beta and gamma families
  JOURNAL   Eur J Biochem 219 (3), 953-960 (1994)
   PUBMED   8112347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..404
                     /product="amino acid aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43641
     Region          1..396
                     /region_name="PRK09257"
                     /note="aromatic amino acid transaminase"
                     /db_xref="CDD:181731"
     Site            order(102..104,130,183,214,243,245..246,254)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(105,140,207,252..254,290,293)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            246
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 myehipaypg dpilslfqaf qqdahphkvn lsiglyydda gripvldstr iaagrvreag
       61 aphtylpmeg laayrqgvqr lvfgddcaal aegriatlqt lggsgairlg aefvkryfpd
      121 saiwisdptw dnhrvifsaa gldvhtypyy dearndirvd amlatldalp arsvvllqpc
      181 chnptgldld rdawravidv larrglipfl dmayqgfgdg laddawavra ivdaglpaiv
      241 gnsfsknfsl ygervgglsi vcanageaat vlsqlqagvr rtysspplfg aqlvstvlnd
      301 dalracwede vaqvrtrikr mrgelkarld trlparafda lvtqrgmfsy tgigaadvdr
      361 lrashgvyll rsgrmciagl ndanvdhvan aiadvlggas rraa
//
LOCUS       WP_175941536             472 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia pyrrocinia].
ACCESSION   WP_175941536
VERSION     WP_175941536.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..472
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50847
     Region          8..462
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mqpegqfqhi aareqglrrt lsarqmamia iggaigtglf lgsgfaigfa gpsvlvsyai
       61 gafislllmg claemtvahp tsgsfgayae hyvspwagfl vryaywaciv lavgtevtai
      121 alymkywfpg vpgwlwivgf sallvfvnar svdvfgavey gfsvvkiaai agfivlgtyv
      181 vfgnpglvgd gaaragfhhy tdhggffpkg lwgmwvaviv sifsylsiem iavaageaed
      241 pehavtrafr stivrlvlfy lvtlalmlai vpwtaagrde spfvkvmeai hlpgaaglin
      301 fvvlvaalsa mnsqlyittr mmfslsragh apkalgevna rgvpfgalml stlgialatv
      361 lsvlypdasf timmavsmfg alftwmmifv thycfrrrra alglpaaafr mrgfplltll
      421 gaglmlavmv ttyftvefhm tlifgipfli alsvvytvwy rraqpvlqpe vk
//
LOCUS       WP_175941669             156 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175941669
VERSION     WP_175941669.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..156
                     /product="VOC family protein"
                     /calculated_mol_wt=16827
     Region          13..136
                     /region_name="VOC_like"
                     /note="uncharacterized subfamily of vicinal oxygen chelate
                     (VOC) family; cd07246"
                     /db_xref="CDD:319910"
     Site            order(13..18,20,35,49..50,57..58,60..62,81..83,85..90,96,
                     117,122,130..133)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:319910"
ORIGIN      
        1 msapvdpipe grhgvipyia vaggvaaidf ykkafgatev ftmqepggrv ghaelliggn
       61 pfylsdefpe mevrgplaig gtpvmlhlyv edvdavvqra vdegatilrp vedqfygdrg
      121 gklrdpfghv wwiathkenv speelrarae rlfgga
//
LOCUS       WP_175941681             143 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [unclassified Caballeronia].
ACCESSION   WP_175941681
VERSION     WP_175941681.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..143
                     /product="OsmC family protein"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /GO_process="GO:0006972 - hyperosmotic response [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=14802
     Region          3..137
                     /region_name="osmo_induc_OsmC"
                     /note="peroxiredoxin, OsmC subfamily; TIGR03562"
                     /db_xref="CDD:274650"
ORIGIN      
        1 mqktasakws ggikdgkgfi stqtgvlnea pygfksrfee gpgtnpeeli gaahagcftm
       61 alslqleqag mkaesletks tvtlekdgeg ftitscqldl kakipgadka afdkaaqaak
      121 egcpvsklfa gnakitlnae les
//
LOCUS       WP_175941700             239 aa            linear   BCT 11-JAN-2025
DEFINITION  PIG-L deacetylase family protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175941700
VERSION     WP_175941700.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..239
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26065
     Region          7..215
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mievprktll isphlddavf gcgaslagaa dvlvctvftg cpaadastdw daqcgfvdak
       61 qamaarieed nralgllgat plhlgfldsq yvpfapdadk ptramltqaf ldaidehrpe
      121 tlliplglfh sdhalvheaa cdawlrhpel pciayeealy rchrallqqr ladlikrgid
      181 atplnarlpe hgqatrreal kreavaayas qlkafgpngy ddvfrperfw tlevaeara
//
LOCUS       WP_175941705             142 aa            linear   BCT 11-JAN-2025
DEFINITION  TadE/TadG family type IV pilus assembly protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175941705
VERSION     WP_175941705.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..142
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=14578
     Region          8..137
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mtrgatgarr argvvslefv mmlpfllmvl igiidtslil cdkavitnas reaaragvvl
       61 rvpmltttqi anvaqtymqn slitggtatt ptvtvtqang ttagtaltvt vtytysglvl
      121 gsafsaltgp vtvsatsvml ye
//
LOCUS       WP_175941711             358 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Burkholderia pyrrocinia].
ACCESSION   WP_175941711
VERSION     WP_175941711.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..358
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40025
     Region          12..194
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(15,17,102)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(49,101..102)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            100..102
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mptharkplv slvvpfhded etidaffaet lpvlesvdtv rfeivcindg srdrtldrll
       61 evmagdarvr vvdltrrfgk eaaltaglde aagaavilid adlqdppali pamverwlag
      121 aevvaakrtd rmcdplmqrl aaalyyrvhn rlsevempen vgdfrlmdrq vvdtlralpe
      181 rrrfmkglfa wvgfrieiie ytraprsggr skfsgwrrwn falegitsfs tvplrvwtyi
      241 glafamlalv ygtfivvrtl lfgnpvhgya slisvvlfig giqlvgigvi geylgrvyhe
      301 skqrpvylvr wryraerdaa ahpaskllqf plkrahaarr rtatpaaagh garkisvk
//
LOCUS       WP_175941719             520 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175941719
VERSION     WP_175941719.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..520
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52478
     Region          35..446
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,155,
                     158..159,162,286,289..290,293..295,298,326,330,382..383,
                     387,391,407,410..411,414..415,418)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msqsfpasra ataphagarv pavatlavas atcslivldt nvvavslpsi arsfhasfad
       61 iewvvsaymt afaacllpag gladrfgrkr mlgaglalff vaslgcgvap sagwliaara
      121 lkgggaalll taalavianr fpdgrerara waiwgmcmgi ataiaplvgg aitqwigwrw
      181 vfllnlpvcv llavgarvai desrdphakr vdmagsllfg aalacaiaal igapshgwls
      241 aatlgrlala aalfaafiga erwqarpmid lalfrqprfv gavlamfgya acaqvmmtfl
      301 plylqnafgm saidaglgml pfafamiagp slgaalvtrv ssggvlaggl aligagnlat
      361 aaltaggdyr lvaigmfvtg cgagimngdt qkaimacvpp drtgmasgis tttrfsaivt
      421 avgvlgavla sstharldrl lsaapglraf adapfmssll agdlaqaldr vppsaagala
      481 raapvafasg fadalivsgv lalvvsvvay kllaqpmrda
//
LOCUS       WP_175941762             132 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: RidA family protein [unclassified Caballeronia].
ACCESSION   WP_175941762
VERSION     WP_175941762.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..132
                     /product="RidA family protein"
                     /calculated_mol_wt=14098
     Region          3..128
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mppieainap glpipaghys hatragnlic vsgqlpvrpd gthtgdlpfe eqaeqtlrnl
       61 rtvleaagaa ladcievtvy lvgvehwkaf ndiyarhfga wkparavvpv galhygylle
      121 isarawvepa pv
//
LOCUS       WP_175941766             227 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia pyrrocinia].
ACCESSION   WP_175941766
VERSION     WP_175941766.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..227
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23870
     Region          23..223
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mtdalplttd pdsglqyrlr paagrpaarl lllhgvggne tdllnvadvi dprieiafvr
       61 gpltfgpnqh awfpvrfgpn gpeidaarad asrvqlitll ralraqdgag aalptviagf
      121 sqggimsasv gltspadvag favlcgrilp eidpliaprd alrplhaliv hgrfddklpv
      181 awadtadarl talgvahdtr lyaaghelta emaadfgrwv certgln
//
LOCUS       WP_175941875             514 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Caballeronia sp. BCC1704].
ACCESSION   WP_175941875
VERSION     WP_175941875.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..514
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=54294
     Region          22..497
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(78,80,84,87,91,124,127..128,137..144,149,152,155,
                     248,252,255,258,260,433,435..436,438..439,442,445..446,
                     448,450..453,462,466,468,482,489..494,496..497)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(164..167,175,190,193,223,240..243,246,264..266,298,
                     398,400,426)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(167,264,295,298)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnivaehpaq garpgasvrt akllidgafv esttgewrdi vnpatqeivg rvpfatadev
       61 naavaaaqka fetwrttplg trmrlmlrfq dlirqnmkri aqtltaeqgk tladaegdif
      121 rglevvehac gigtlqmgef aenvaggvdt ytlrqpigvc agitpfnfpa miplwmfpma
      181 ivcgntfvlk pseqdplstm elvelameag vppgvlnvvh ggkevvdalc thpdikavsf
      241 vgstavgthv ynlasqhgkr vqsmmgaknh avvlpdanke qtlnalagag fgaagqrcma
      301 tsvvvlvgas kdwlpdlver arslkvnagt epgadlgpvv sraakerilg miakgveega
      361 tlaldgrdit vtgyengnfi gptifsdvst dmaiyqteif gpvlcvleaa tlddaialvn
      421 rnpmgngvgl ftqsgaaark fqseidigqv ginipipvpv psfsftgsrg sklgdlgpyg
      481 kqvvqfytqt ktvtarwfdd atvndgvntt islr
//
LOCUS       WP_175941888             232 aa            linear   BCT 11-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175941888
VERSION     WP_175941888.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..232
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25249
     Region          25..232
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mtfvfppeap valpvagsda rfavrrvycv grnyaahare mgfdpdrepp fffckpadsi
       61 vpvaygetld laypsqtqny hyeaelvavi gkggadiple ralehvwgya vgldmtrrdl
      121 qmkmremgrp wemgkafdrs apigpvhpas eaghfeqggl wltvngatkq ksdvshliws
      181 vaetvadlsk ffrlepgdvi ftgtpegvga vvagdvmkvg verlgeltvr vv
//
LOCUS       WP_175941981             220 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia pyrrocinia].
ACCESSION   WP_175941981
VERSION     WP_175941981.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..220
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23903
     Region          41..178
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mtlaaphgtn asvrysvlka sredrimewh ccefghlsav dlyailrarn avlvvedaht
       61 hldidgkdag alhvyasvrn gdtaevaaya rilpgddidp dvvidkvlts eacrdgdtle
      121 rlieraltaa laawpdaalr thvpaprqaf ykrfgfrkay gpyleqgapf vgmirpadra
      181 sgalrqllsr avstprprne dvladgrahn rlpadtganr
//
LOCUS       WP_175941983             463 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sigma-54 dependent transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175941983
VERSION     WP_175941983.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..463
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51176
     Region          <36..130
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <151..454
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mnmpitrdkr agggsgngqr pliywtqsps vmlrkelarr dwkvsivaha nelrdtsgei
       61 tcgildlsgg hadaignias tcasmrdvvw valvdvgqta spnvrallrd ycfdyvtlpa
      121 shqriadtvg haygmeclfa rdreqlesde kgivgtcsam lrlfdtvrrf artdapvfvf
      181 getgtgkelt avaihrhser rngpfvavnc gaipphllqs elfgyergaf tganarkigy
      241 veaanggtll ldeigdlphe sqasllrflq ersihrlggs dpvpvdvriv sathvdlrga
      301 meegrfradl fhrlcvmrid qpplrargkd iellahhmle rfrgdarhrv rgfstdaita
      361 lykhdwpgnv relinrvrra vvmtegrlit ardleleycl daaspsvadi rksiereaie
      421 tallrtrgrv aasarelgvs ratlyrwmea ygierprgtg ssd
//
LOCUS       WP_175941985             827 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 2 protein [Burkholderia pyrrocinia].
ACCESSION   WP_175941985
VERSION     WP_175941985.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 827)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 827)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 827)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 827)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14311966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..827
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..827
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=90352
     Region          10..649
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          636..727
                     /region_name="Mannosidase_ig"
                     /note="Mannosidase Ig/CBM-like domain; pfam17786"
                     /db_xref="CDD:465505"
ORIGIN      
        1 mtrahalpaw smlataagav eeprdlpaag kgwiaapvpg tvaqalalag rldeaasldq
       61 rdhwyrielr grgprvlrfh glatlaqawl ddtpilrsds mfvahdvpvs ldgahrltlc
      121 fralaphlrd araprrarwr trlaepaalr tvrtslfghm pgwfppyvpa gpwrpvdvld
      181 padgfvpvdc dlrarvegdt grldaeltfa aplpdalaar lscgehhatl eragadrlra
      241 svavpnvrrw wphthgepal yeialhigde rrplgstgfr tieidagadg kgfglringv
      301 pvfargacws saaplalhad daaygrllgl ardagfnmir vggtmtyead afhawcdrlg
      361 llvwqdfmfa nfdhalddpa fadnvdread qflarhgasp slavlcggse iaqqaamsgl
      421 gpkqrflelt aerlaghaaa rrpdvpyvpd spdggvlpfa prervshyyg vgaylrpldd
      481 arradvrfas eclafanvpc datlaslgwp gvheprwkaa vprdpgtswd fedvrdhylq
      541 tlydvapdrl rredparyfe lsraviadvm rdtfsewrrt gsrcagalvw qfqdvmpgag
      601 wgvidathrp ksawyalrqv lqpvqvllvd eglngldvhv tnerpaplsa avelvalrdg
      661 rtpvaraacp vriaahdtvr igsaellgrf fdwtyayrfg pcehdtvvat lraddgtlls
      721 qafhfpsrth pavlarrelg ieacvsrtgd twhvdidtrh varhvqidsp gfmpqddwfh
      781 lapgtparva lvpletvgki rdadggppsv eiravnaart vratqag
//
LOCUS       WP_175941990             398 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175941990
VERSION     WP_175941990.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..398
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42421
     Region          31..382
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msallpelaa dseshrldea ahavaqiaaq hadavdrdar cpveaieamr arrllgamvp
       61 phlggagasl ediasacsil gqacassamv famhqiqvac ivnhavdqgw hklflqqlvr
      121 hqwllasats edgvggnlra sqcaletdgs efrlcksapt isygdyadgi latarrdada
      181 paseqvlvtl lregytltrr gewdtlgmrg tcsngfvlda qgaavqclpv pfakiaeetm
      241 vpvshilwaa vwigvagdaf hrahqffraq arqtdgapsp asrriaesla lmqamqarvd
      301 nvlrlhants arswsagmaw aaeintlkty vstsalevaq qammicgmag ykqgtpfsig
      361 rhirdlhaap lmisndriaa ntsslllalr patlekhs
//
LOCUS       WP_175942011             663 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 28 protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175942011
VERSION     WP_175942011.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 663)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 663)
  AUTHORS   Abbott,D.W. and Boraston,A.B.
  TITLE     The structural basis for exopolygalacturonase activity in a family
            28 glycoside hydrolase
  JOURNAL   J Mol Biol 368 (5), 1215-1222 (2007)
   PUBMED   17397864
REFERENCE   5  (residues 1 to 663)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 663)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..663
                     /product="glycoside hydrolase family 28 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=68867
     Region          145..619
                     /region_name="Pgu1"
                     /note="Polygalacturonase [Carbohydrate transport and
                     metabolism]; COG5434"
                     /db_xref="CDD:444185"
ORIGIN      
        1 mkqrptapas arrrsllkfa gasasaplig glgslsvlag cggghhesga patpedpiwg
       61 psgaatqiin alknvstsmv psrqflvtdy gakpctviaa tspytdpsks plstgadqtq
      121 apgsfdsrpa flaaiaacsa agggrvvvpa gnwycagpii lqsnvdfhls anceiffspn
      181 padyakdgpi dcgangklyy srwqandcln ygppvyarnq tniaitgegd tsvlngqamt
      241 pfagsgntst cwwtwkgnsg aygyagsstp sqafanpnnv dlktavpgis dalyakltdp
      301 atpwqqdqny lpalseagva iekrifgigh ylrpsmvefi gctnvlmqgy rtintpfwqh
      361 hptdcknvvi tgvtvdsigp nndgfdpdac dmvlcdsvtf ntgddciaik sgkdldtqyg
      421 paqnhviqnc tmnsghggit lgsemgggvq niyarnlqml nkfwatnsln iairvktnmn
      481 rggfvknfyv dnvtlpngvs ltpsgygssl lagspinatv plgvvtasaa npsaaqggii
      541 tfdcdyqpsk dairtrpalv qnvnisnvka snvtlngvtg scfqaivaqg pvafdyngpa
      601 ptpaipaiag vtitncdfgt pvaagpatat tpgpiyaynv hdivlnntvi agktlnqtit
      661 dar
//
LOCUS       WP_175942016             592 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia pyrrocinia].
ACCESSION   WP_175942016
VERSION     WP_175942016.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..592
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=64972
     Region          7..585
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 maeekkphvd avivgfgwtg ailakeltea glkvvalerg eyrdtypdga ypntidelty
       61 nirkklfldl skttvsirhg vqdtalpyrq laaflpgegv ggaglhwsgv hfritpeelr
      121 lrshyeeryg kkfipagmti qdtgvsydel ephfdfaekv fgtsgqaykv ggkvvgdgnv
      181 feanrsnnfp lpaqlntysa qrffdaaqsl glhpyrlpsa ntsgpytnpy gvqmgpcnfc
      241 gycsgyacym yskaspnlni lpalkqapnf elrskchvlr vdlddtrkra tgvtyvdpag
      301 revhqpadlv ivaafqyhnv hllllsgigk pydpisgegv vgrnfayqnl stikaffdkd
      361 tytnpfigag gngvavddfn adnfdhgplg fvggsplwvn qagakpisgi amppgtpqwg
      421 sawkksvkdy yahtismdah gtnmsyrdvy ldldptyrds ygqpllrmtf dwkdndirma
      481 qyvtgqmkki aeamgpkaig vstrefgkhf dsrayqtthl vggaimgtdp ktsvlnrylq
      541 cwdvhnvfvm gasalpqgig ynptgiiaal aywsaraire qylknpaplv ta
//
LOCUS       WP_175942021             160 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TadE/TadG family type IV pilus assembly protein
            [unclassified Caballeronia].
ACCESSION   WP_175942021
VERSION     WP_175942021.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..160
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=17048
     Region          1..138
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 msaarrpfwr rclrddrgis tiefaivgpl sfilvlmtme laldmcvdat vqiaaqqasr
       61 tglttvdpas gtrsdqakki intilggwtn igatividtv sygaygaigt snstdgslgg
      121 fgdvvsynit ltmppftgip klvginqlvf qrnyivqnek
//
LOCUS       WP_175942080             316 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Caballeronia sp. BCC1704].
ACCESSION   WP_175942080
VERSION     WP_175942080.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..316
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34058
     Region          7..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(105,109,148,162,164,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(106..107,111..112,114..115,118,122,124..130,191,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mtklpdfegl amfakvaeeg sfaaaaramg vsvatvsrgv arleerlgar lfnrtsrqla
       61 ltefggtiae kagdiyrqae eaenaarems vqprglirva vpmsfgvrwl apllpeflra
      121 fpdisldlhl sdatvdivaq gfdaalriaa lpdsslvarr lcavsqllva speylerfgq
      181 pthprdligr pclsyayrag tevwrfvnda gdeepvtpvg plrvtnsdal lptlldglai
      241 aelpefiage yladgrleai ltdwhltrgg lyfvtpsara rparvtalad flaahlaepa
      301 wlspqakaaa rgkrra
//
LOCUS       WP_175942092             303 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175942092
VERSION     WP_175942092.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..303
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34097
     Region          85..242
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 meaigklsvy vlvivlaasm ieavwlsrkh kgtdkafawh evwisladlv grkllafvpl
       61 slatpffafa wehrihtvts ntpltvfllf igmefcyywy hrashtvrff wathavhhsp
      121 nqltlssayr lgwtskitga alfftplvwl glkpevvlaa lsinllyqfw lhatwipklg
      181 wleyvfntps ahrvhhasna ayldanfggv lvifdrlfgt yaeeradepc ryglttptts
      241 rnpvvvqmeh wvslakdvfh aksvsqavgf llrppgwrpd gegettealq krarnagkam
      301 eas
//
LOCUS       WP_175942093             445 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175942093
VERSION     WP_175942093.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..445
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47414
     Region          44..422
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msaslaassp spqppslrll paddaadaed ariaalldrl apglaadaar ndvdgrfphe
       61 nfarlhragl iaqvvprehg gagatlaras rivaavarad patalvltmt ylqhralgra
      121 dsrwpgqmrr avfdsavaqg alinalrvep algspsrggl petvarrdgd gwrlsghkly
      181 stgipalrwl avwartdepe prvgvflvpr drdadgdrir vieswnhlgl rasgshevvf
      241 ddvrlpadha vdvrapqawa vsaathadad ahadqqawmv allgslydav arasrdwlvg
      301 fattrapsgl gaplatlprv qeavgeiegw lhanrvlldd lisrtdagna psvttsglvk
      361 rsvtehaira veqalklsgn hglsrdnple rhyrdvlcsr vhtpqddaia vaagravlea
      421 arrdetkaea ggasrneier drnda
//
LOCUS       WP_175942106             316 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia pyrrocinia].
ACCESSION   WP_175942106
VERSION     WP_175942106.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..316
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33842
     Region          10..227
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mnapaapyai dvdrlnkrfg dkhvvkdvsl rvargeifgf lgpngsgktt sirmmcgllt
       61 pdsgsgtclg ydivrdsaqi krhvgymtqr fsywedlsir enldfvarvy gmpdrkaava
      121 raldglglag radqltgals ggwkqrlala acmlhepell lldeptagvd paarrdfwee
      181 lhrlaaqgis vlvsthymde aerchklayi asgellaqgt saeivasqhl strtitgerl
      241 telsarlrtm pgvdqtvvfg salhvsgrdr aaldatlarv asddaslqva pidtgledvf
      301 ifmmgrasgp pggass
//
LOCUS       WP_175942119             316 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Caballeronia sp. BCC1704].
ACCESSION   WP_175942119
VERSION     WP_175942119.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..316
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35247
     Region          18..76
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          107..307
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(122..123,125..126,129,133,135..141,236..241,
                     247..248,250..251)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176126"
ORIGIN      
        1 msqdstlsaa qvltklrfrh lqllellgrt rnlriaaeqm hitqpaatki lsdleamfda
       61 plferlprem rptdlgtlsv ryasttlsnl gkfsgefatl knggyghltv gfipasasql
      121 vtaaikeiqr rrprliiklv eqssdqlaaw leerridvmv grptearhea lfhvvdllae
      181 pvravvgqhh pllkerrvem tslgqwpwil ypqgtamrql feetfaaagm vapvgivetp
      241 sifstlellq atdmislqpq aamdkyvkhg llgylnvpir rtmsnysvit rkdettsqam
      301 defvaillai aaqysr
//
LOCUS       WP_175942142             902 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Caballeronia sp.
            BCC1704].
ACCESSION   WP_175942142
VERSION     WP_175942142.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 902)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 902)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 902)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..902
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..902
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=99531
     Region          84..878
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mphmcdvcga rpatvrlavl rdgrrhvlnv cdfhyaqltr hqralspfea lfmsdtpgqa
       61 eaapqhispe retsaegvgi erylsdsake mlmraaerav qfgrtevdte hllyeladna
      121 vvqsmlknig idanevrrfi danvqrregv pppaggaigv sprlksaldr afvasrqlrh
      181 syigpehlli glsevpdsfa gqllgkmsvd aqalrrlttq tvgaggppnk dgppsrtpnl
      241 dkfsrdltal areghldpvi graseietmv evlarrrknn pvligepgvg ktavveglaq
      301 rmiggdvpes vrdkrlieln vnsmvagaky rgefeervkq videitanre tlllfvdevh
      361 tlvgagqggg eggldianvf kpamargeln ligattlaey qkhiekdaal errfqpvlip
      421 epsvaqtini lrglrdrlea hhkvtiqdda ivaaaelsdr yisgrflpdk aidlvdqaaa
      481 rvnlsatsrp aailelesel aqlrreqdya asrkqydrah aldaeiagkq kafndatdew
      541 kkrigtntsn vtvtqiaeiv atltgipvtq lteqererll nmearlherv igqeeavrav
      601 sdavrrartg lqgrnrpiav flflgstgvg ktelakalae vvfgdedaml rvdmseymer
      661 havsrligsp pgyvgyeegg qltervrrrp ysvilldeie kahadvynvl lqvfddgrlt
      721 dgkgrvvdfs ntliiatsnl asdviggqrr atlgftssds daddsvrsgv mnvlrqhfrp
      781 eflnriddii lfkslgreei rqivqlqleh vkrmahsqdi dlefdasvve ylgeagyrpe
      841 fgarelrrqi rqlienelak emlkgdiveg arvrcaydre arrivfdaer ktaadlgtpp
      901 tp
//
LOCUS       WP_175942143             319 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175942143
VERSION     WP_175942143.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..319
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35060
     Region          2..312
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhrigflisd gfqimalaaq svfeyanmga gepfylmdny svdggdvrss lglsvatral
       61 rgriavdtwi vagvndplaa papagvvafl rrtnararri agictgafvl aeagllaqrr
      121 atthwafgrd mqrhypeirv eedriyivdg piwtsagmta gldlalamve kdlgadaars
      181 vahklvmnqr raggqsqhse mldlapksdr iqnalnyarq nlgraltved ladavhlspr
      241 qfsrvftlet gqspakaier lrleaarlmi eqsrhpldvi akengfrdrr hmreafvrgf
      301 gvppqamrrd armddrggr
//
LOCUS       WP_175942159             163 aa            linear   BCT 11-JAN-2025
DEFINITION  2,4'-dihydroxyacetophenone dioxygenase family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175942159
VERSION     WP_175942159.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14449000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..163
                     /product="2,4'-dihydroxyacetophenone dioxygenase family
                     protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17557
     Region          24..143
                     /region_name="cupin_DAD"
                     /note="2,4'-Dihydroxyacetophenone dioxygenase (DAD), cupin
                     domain; cd20302"
                     /db_xref="CDD:380436"
     Site            order(40..41,44,50,52,69,71,73,75,88,91..95,97..99,117,
                     123,125,133,136,139)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:380436"
     Site            order(64,66,81,102,118)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380436"
ORIGIN      
        1 mtqpsaplst dlppisclpg dalpwlpmsa dlpglaikyl hinaaedtlt allkmpaggt
       61 lprhrhdgev fvhtlqgawr yleydwiaha gstvlepags vhtpetlgap gedvitlnvm
      121 rgdlvllddd gretarencr vallrqrkha rtapddavaf vtr
//
LOCUS       WP_175942164             212 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Caballeronia sp. BCC1704].
ACCESSION   WP_175942164
VERSION     WP_175942164.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..212
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22018
     Region          9..211
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtaqtffdan lllawsayfv gtaspgpsnl aimsiastsg rraalafaag vmsgsltwav
       61 laalglsaal aaysgflvav klcggayllw laaksaraaw rpplrpasrh apapdarrly
      121 argallhltn pkailvwmsi aalgsstatp pmhtltvvag clcigmsvfg gyavlfsmaa
      181 prrlyarmqr ylnaclallf gaagirllms rv
//
LOCUS       WP_175942173             310 aa            linear   BCT 11-JAN-2025
DEFINITION  AEC family transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175942173
VERSION     WP_175942173.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..310
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31420
     Region          18..305
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 migaillala pvallvafgh glrrtgfiae afwpqaerlc yyvllpalfa dglanarlqa
       61 lpvlplaaal vgstavaaal lllirrfvrv dgagftsvfq gavrfnnyvg talaaglfga
      121 kgialaavcv aaivptvnlm cvlvfarygd trlgagalvr qilsnplvva calgismqag
      181 gvafpaavep avralgaasm plgllcvgaa lkfdaarawl qpvcvasafk fmamplitla
      241 ggrlfglgda altvallfqa lptssasyim arqlggdapl magitafqti aaalampvvl
      301 talasapvfr
//
LOCUS       WP_175942194             344 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Caballeronia sp. BCC1704].
ACCESSION   WP_175942194
VERSION     WP_175942194.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..344
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37905
     Region          29..83
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          113..310
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(123,127,166,180,182,245,262,289)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(124..125,129..130,132..133,136,140,142..148,209,
                     239..243,250..251,254)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 msdtqtpfrp ggedslassf aksyagvvaf lavvsegsfa rasdrlgigr savsrnvqkl
       61 eaqlnarlfl rttrstsltr egelfyqnch pgvqrivqaf edmrdlrdgp prghlrigst
      121 tsfgraivap lmrgfneafp eitvelllsd hpanftsdri dvsfrdgrve dsqviarqli
      181 pmqllvcasp ayarmhglpr diaelhahrc inlrtasgri aewefsvegr tqklvpagrh
      241 tfncaelalq avhagqglaq lagyqvceal rdrrlvsclt efspsdrghy lcylsrkhlp
      301 arirvfvdym tehvraldlg cspalshear arpsvaanrh ieag
//
LOCUS       WP_175942195             159 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Caballeronia sp.
            BCC1704].
ACCESSION   WP_175942195
VERSION     WP_175942195.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..159
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17762
     Region          11..144
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtqrinyvqq spelfkrfvs fglavkesgi easiceltsl rasqingcaf cvdmhvkear
       61 ihgerelrlh hvaiwrestl fspreraala wteiltklpa dgvpddvfeq vktqftdqel
      121 snltfhvmai ngwnrvnvaf rtvpgssdaa fglekanls
//
LOCUS       WP_175942198             189 aa            linear   BCT 11-JAN-2025
DEFINITION  YbhB/YbcL family Raf kinase inhibitor-like protein [Caballeronia
            sp. BCC1704].
ACCESSION   WP_175942198
VERSION     WP_175942198.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..189
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=19853
     Region          49..185
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mklnallrav ccmsllamlp avaaaapfav rvdglergrf eneqvyggfg chgenvspri
       61 swthvppgtk sivitlhdpd aptgglgwrh wqvvniapsq tsiekgasgh vdllpagave
      121 tltdfgasay ggpcppqges hryivtasal avssldvdak sspalvayqm hgkvigqahy
      181 varyrrspe
//
LOCUS       WP_175942199             310 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Caballeronia sp. BCC1704].
ACCESSION   WP_175942199
VERSION     WP_175942199.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..310
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33608
     Region          30..285
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(45,131,133,135..136,165,219,240,243,254,256,285)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 msaiirnvqp vtqaigkrgs gelvpsryav rvgdvdvvli sdgvlplpts tmstnvseaq
       61 rnewfdgrfl qrdmfdwaln ialvrsgerl ilidsgvgdg feyfsragks vmrlesagid
      121 laaitdivit hmhmdhvggl nvdgvkaklr rdvrihvsaa evafwknpdf sktvmpeavp
      181 palrkaaatf melygdnivk fdrevevatg vsarvtgght pghcmvdvas ngekltfvgd
      241 avfevnfdnp dwqngfehdp eaavdvrlal fneaaesgal laaahvafps ighvaktndg
      301 frfvpvqwdy
//
LOCUS       WP_175942216             473 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia pyrrocinia].
ACCESSION   WP_175942216
VERSION     WP_175942216.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..473
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=51109
     Region          83..470
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mtarpafpsp dasgtpaprs psrlprraaf vlgaavlgyg afaiafparv paaigtvvag
       61 wtganphpvv lqrpaaqpls avaqlgrtlf vdpslsasgq qscaschspd haygppnald
      121 vqpgglamtq rgyrpppslm ylyrqpnfsi gpdagendaa psvaqqaasa agvvkaqkva
      181 gtsaapqlvp qggmfwdgra dtlqqqafgp llnpvemana siddvarkla qsshraqfeq
      241 lfgvrvfdsp qlavseamfa iaryqvedps fhpynskydr wlegrarlsq aelrglrlfn
      301 dpdkancagc hlskpgkdgl ppmftdyqye algvprnqql aqnrnaafyd lgvcgpfrdd
      361 lkdqtqycgm fltptlrnsa trqvffhngv fhtldqvmaf ynersispqk fysrgtdgkv
      421 deyddippkf ranvdvtdap fdrkpgdkpa mtaqdikdie aflgtlndep vrh
//
LOCUS       WP_175942264             311 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia pyrrocinia].
ACCESSION   WP_175942264
VERSION     WP_175942264.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..311
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=33299
     Region          12..155
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          168..307
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mqpdqsiptl arialavdpt peslsaarya rtllrpgmrl rivcaidnpr lvlpdiprid
       61 alltsaredm ireaqatnar iaalfddsgi eveqvvvdts vtggtvadal vndtlawrad
      121 vlvvganphh gllrlvegam sdtlttrarc allivpaaye rpsdgtlqrl mfavdgseps
      181 lhavrvglgf aapttllyaa yvidravrlt divpvraled ayraegedal akigplfhat
      241 gnptkrgive trptsddvah almrdavhwr aellvvgthg rrgiaawlig svarriahla
      301 qvpvllvrga q
//
LOCUS       WP_175942275             252 aa            linear   BCT 11-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Caballeronia
            sp. BCC1704].
ACCESSION   WP_175942275
VERSION     WP_175942275.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..252
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27778
     Region          15..244
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 mtlmhdagid iesataarak elriatynvh gavgidgkfa perigeviae idadifalqe
       61 vplggrsspn vldllqrmtn lhavpgptld tperrygnav ltrypvqavr tldlsfgsre
      121 prgaldadid cggetwrvva thlglasser raqveqvlqs fdtpalpvil lgdlnewfvy
      181 grtlrrlvth fhrasalrtf ptrwplfald riwvhpgerl mrvdvhrtrl sriasdhypl
      241 iahianassn gg
//
LOCUS       WP_175942281             204 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [unclassified Caballeronia].
ACCESSION   WP_175942281
VERSION     WP_175942281.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..204
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21969
     Region          18..194
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msstllsalp aaalfalvms itpgpnntml lasgvnfglr rtvphvlgis agvallmlaa
       61 gfglaeafgh lpwlytvlet asvayllyla wkigtsssvq trdgerrpmr fheavafqwv
      121 npkawmmvlt aattihlhas lslnaafmal vfiviglpci tawaafgvsl rrflanprll
      181 rlfnltmaal lvlslypiva hffe
//
LOCUS       WP_175942297             744 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia pyrrocinia].
ACCESSION   WP_175942297
VERSION     WP_175942297.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..744
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=78613
     Region          75..>209
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          215..737
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msrglieagk vagqtagagv srrgflkfgm slgaaagggl llgfslpaag ddtrrsvigg
       61 dadetaragv fapnafvqid rsgkvtlvmp kvemgqgvyt alpmliaeel evplssvtld
      121 happneklfl dpllggqltg gstsvryawe plrragatar tllvaaaakq wnvdpascha
      181 angevqhpps grrasygqla naaaklpvpk dvalkkpedf kligtpakrl dspekvdgta
      241 qfgldvrlpg mlyavivnsp vfggtvasvd dtaakkvpgv rqvvradnav avvgdhtwaa
      301 krgasalvvk wnegtgakvs mkdivadlaq aaangkgava rkdgdvgkaf anaktridav
      361 yeqpflahat mepvnctvhv rsdgceiwvg tqvptravdt vqrltsfppe kivvhnhllg
      421 ggfgrrletd migqavkiak qvgapvkviw treediqhdm yrpyyydris agldangkpv
      481 awqhrivgss ilarfappaf kdgvdpdave vatdlpydlp nqlidyvrqe prhvptafwr
      541 gvgptrstfv vesfidelaa qtktdpvqyr rallgktpra rnvldvatra agwgpalpkg
      601 qgrgvsvmha fgsffsivid vavddgevqv krvvcavdcg msvnpntiea qvqggiifgi
      661 tgalygeiti edgrvvqsnf tdyrmlrine tppievhlvk sgeapggige pgtaataaal
      721 snaifaatgk rlrklpvgnq lkta
//
LOCUS       WP_175942302             409 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175942302
VERSION     WP_175942302.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..409
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=44125
     Region          119..323
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mstmtgtldp aalpprvarl vlvtpdgavv gclppmpvav pwwqevesvv raarerhgvd
       61 vtilrlletv rdrapggevt ylaeiakpva aeswtgniep hslrrsyarp ggpaadlgwa
      121 arvlaghgls ptaepvqvrt wnlssvwrip igaqsawlkv vppflghegr vitalagrrv
      181 ptllghdecg riliaeipga dlfdaalpql ldmvtllvdi qaswfgrvde lhamrlpdwr
      241 gaglaadiad vvertgeels raeraslrhf vsglaarfaa idacglpntl vhgdchpgnf
      301 rgtrseltll dwgdsgighp lldqsaflda vprdyaaaik dhwnrewlak lpgsdpvraa
      361 allapiatar raviyqrfid niepseqiyh rgdpadwlgq taalvatrd
//
LOCUS       WP_175942325             337 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Caballeronia sp. BCC1704].
ACCESSION   WP_175942325
VERSION     WP_175942325.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..337
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=37468
     Region          22..294
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mptttdlfdq qradwqadph aafdawlaqq efrassadvy raqwgnflew lqakratlht
       61 vqrpvieqfv sqldirrpqr mrylrlierv ldhvrkieaa gtnparfiaq dgdaawrkar
      121 dneptgflth deralliahl fsplgalpag qrwreqrdra lvaaflgagv ktgeaaqltv
      181 dcyapgapyi tvdasnplli rqarlapfav elldgwiter raaglegell fpaapsgrpm
      241 hkatmlraid avvaasgiaa srvaraspqt lrnsyaaelf degvepehvg qwlgfqqmis
      301 vhrlhrawqd wmgeqirerd iaqaragssd eagitgl
//
LOCUS       WP_175942425             496 aa            linear   BCT 11-JAN-2025
DEFINITION  phenylacetate--CoA ligase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175942425
VERSION     WP_175942425.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Luengo,J.M., Garcia,J.L. and Olivera,E.R.
  TITLE     The phenylacetyl-CoA catabolon: a complex catabolic unit with broad
            biotechnological applications
  JOURNAL   Mol Microbiol 39 (6), 1434-1442 (2001)
   PUBMED   11260461
REFERENCE   2  (residues 1 to 496)
  AUTHORS   El-Said Mohamed,M.
  TITLE     Biochemical and molecular characterization of
            phenylacetate-coenzyme A ligase, an enzyme catalyzing the first
            step in aerobic metabolism of phenylacetic acid in Azoarcus evansii
  JOURNAL   J Bacteriol 182 (2), 286-294 (2000)
   PUBMED   10629172
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Ferrandez,A., Minambres,B., Garcia,B., Olivera,E.R., Luengo,J.M.,
            Garcia,J.L. and Diaz,E.
  TITLE     Catabolism of phenylacetic acid in Escherichia coli.
            Characterization of a new aerobic hybrid pathway
  JOURNAL   J Biol Chem 273 (40), 25974-25986 (1998)
   PUBMED   9748275
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..496
                     /product="phenylacetate--CoA ligase family protein"
                     /EC_number="6.2.1.30"
                     /GO_function="GO:0047475 - phenylacetate-CoA ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0010124 - phenylacetate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55897
     Region          49..490
                     /region_name="PaaK"
                     /note="Phenylacetate-coenzyme A ligase PaaK,
                     adenylate-forming domain family [Coenzyme transport and
                     metabolism]; COG1541"
                     /db_xref="CDD:441150"
ORIGIN      
        1 mntlyrlfle ailwtlwflr rvisvdgrly vflnapvfqp ylayvgrmra rvaflkasta
       61 cpayieflka egyraggkwr ladlpamtke nyikrysieq rcyggaipks gvvidessgs
      121 tgqpnnwvrs aaersdvkri lqlnyqlvfr hsgkmllncf algpwatgmn vsmslvdvgi
      181 mksigpdkak lintlklfgp kyqylifgyp pfirsvvdec dldltpyhid fivggeglse
      241 alrdhllrka stvissygas dleinigvet pttiglrral msrpelcrel fgretlpmif
      301 qynaldyvie tnadgellvt igrqsgaapk irynirdsgg tykfrvlnkr lsahgmrltd
      361 fasrtshfpf lfvygrndss vpfygakvfp sdieqvlsas pvlhdaistf qlavtedehl
      421 tsflhvhler aagsaqmqld davlhaemfe gmkrvnqdfr evsrlfdpkq vivrvhdhdt
      481 gpfqgrdiri knkyia
//
LOCUS       WP_175942441             417 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175942441
VERSION     WP_175942441.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..417
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43298
     Region          8..393
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mkanewdtsy ewkavtllal gfglvgldrw liaplfpsim kdlnltaqdv gncigvlgls
       61 wgvfaalmgg isdkigrrkv lipaiiafsl lsgfsglagg llglmairgl mgvaegsfcp
      121 tsfaatadas hprrrglnlg lqqsgfalfg lalspiiatq llgfvswrwv falvaipgli
      181 lgaimffvir epkvvkevas ehapaslghv lksrnilvam aalccamtgv fvlgallply
      241 ltdylslgtq kmglvvsaig fggflgqfgl pglsdlvgrr lasivgfagt avmlyifrgl
      301 gpqplalfgv lfvasfftlg lvsllsgpva teaapvglvs tsigvvvgvg eifgggiapa
      361 mggyvaahfg iqnimwlpmc avmlgivvsm llketapavl qrrvvvqpel aageqpr
//
LOCUS       WP_175942473             494 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175942473
VERSION     WP_175942473.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..494
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53193
     Region          72..450
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
     Region          453..>493
                     /region_name="kgd"
                     /note="multifunctional oxoglutarate
                     decarboxylase/oxoglutarate dehydrogenase thiamine
                     pyrophosphate-binding subunit/dihydrolipoyllysine-residue
                     succinyltransferase subunit; cl39092"
                     /db_xref="CDD:476867"
ORIGIN      
        1 mkklaispri gaaaivlafl agcttfskdg gfgtvsstas erigkdavvv rtdadreavd
       61 krttellakp lsmddavqva llnnrglqas yaelglsead lvqagrlpnp rfsfsrtrag
      121 dgelslgrtf sanvfalltm platnierrr feqtkletad amlkvaadar rayveavaae
      181 qaanyaqqvr daasaaaela qrmrqagnfs rldyareqaf hadavaqhak arqqavaare
      241 kltramglwg ertqyalpdr lpdlpkarpd lpdlerfams nrldiqaakl qtqgvasslg
      301 lskatrfvna vdlgyvnnye tgkghehgye isveiplfdw ggakvaraea vymqsanrla
      361 ktaidarsev resyaayvts ydvakhyrde vvplrktisd elllryngml asvfelltda
      421 reqvgavngy idslkdywla etdlqmavgg rlptagpapr aaasaepepg tdaapqpass
      481 paaqpapath pegh
//
LOCUS       WP_175942495             336 aa            linear   BCT 11-JAN-2025
DEFINITION  sodium:calcium antiporter [Burkholderia pyrrocinia].
ACCESSION   WP_175942495
VERSION     WP_175942495.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schnetkamp,P.P.
  TITLE     The SLC24 gene family of Na/Ca(2)-K exchangers: from sight and
            smell to memory consolidation and skin pigmentation
  JOURNAL   Mol Aspects Med 34 (2-3), 455-464 (2013)
   PUBMED   23506883
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Besserer,G.M., Nicoll,D.A., Abramson,J. and Philipson,K.D.
  TITLE     Characterization and purification of a Na+/Ca2+ exchanger from an
            archaebacterium
  JOURNAL   J Biol Chem 287 (11), 8652-8659 (2012)
   PUBMED   22287543
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..336
                     /product="sodium:calcium antiporter"
                     /GO_function="GO:0008273 - calcium, potassium:sodium
                     antiporter activity [Evidence IEA]"
                     /GO_process="GO:0006874 - intracellular calcium ion
                     homeostasis [Evidence IEA]"
                     /calculated_mol_wt=35578
     Region          19..332
                     /region_name="ECM27"
                     /note="Ca2+/Na+ antiporter [Inorganic ion transport and
                     metabolism]; COG0530"
                     /db_xref="CDD:440296"
ORIGIN      
        1 mtfmfvelaf mllvilvaae vftnalehlg erlkisegvt gslfaavgta lpetmvplla
       61 laggtanqav neeigvgail gaplmlatlt tflmtlavir srglrgtiap ehtgfvrdmn
      121 yflaafslat aamfvphhnw avrallsaml vgiyamyvvm tfrassqlvd aghgteapht
      181 mflartglpt nlatialqll lgvallvgga kgfihgvegv shvlgisall lsliivpiat
      241 elpekvnsvl wirrkkdtla fsnitgamvf qgtllpaigi mltpweprpe vltgvivtla
      301 aaawlrinar krglaiwall angagyvvyl fltlar
//
LOCUS       WP_175942521             237 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Caballeronia sp.
            BCC1704].
ACCESSION   WP_175942521
VERSION     WP_175942521.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..237
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25011
     Region          38..195
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvdnsesgla eptrarkraa kptekeqhkp yhhgslpqal lqaaevvlkr dgisglslra
       61 iareagvsht apqhhfgdta gvlselaadg fmrlsacian sardvqdase rpraiargyi
      121 efakknpdlm rlmsraemfd adrpsliear rtaglalagv fgdaplgpps gkhtfgpmda
      181 sravaltaaw ayvhglalll idgrldglaa saegirhadd lvmaaidqvq lnigkas
//
LOCUS       WP_175942550             463 aa            linear   BCT 11-JAN-2025
DEFINITION  alkaline phosphatase [Burkholderia pyrrocinia].
ACCESSION   WP_175942550
VERSION     WP_175942550.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Vimalraj,S.
  TITLE     Alkaline phosphatase: Structure, expression and its function in
            bone mineralization
  JOURNAL   Gene 754, 144855 (2020)
   PUBMED   32522695
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..463
                     /product="alkaline phosphatase"
                     /EC_number="3.1.3.1"
                     /GO_function="GO:0004035 - alkaline phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0106219 - zinc ion sensor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48093
     Region          1..463
                     /region_name="PhoA"
                     /note="Alkaline phosphatase [Inorganic ion transport and
                     metabolism, General function prediction only]; COG1785"
                     /db_xref="CDD:441391"
ORIGIN      
        1 mstikciaaa lavvgfacgp aqaagqaknv ifflgdgmgp ttvtasriyk vgesgqltme
       61 klartarvkt fsndaqttds apsmaaymtg vkmnnevlsm ssdtravapg sdangnktvn
      121 ncapgngqpv atllelakar gkavgaittt elthatpaat yshichrdaq ydiaaqaapg
      181 gaghnaalgd gvdvlmgggr nhwtpfdpva nkrgradgrn lldemkakgy tvvatkdqla
      241 qagngklvgl fsstshleye ldrvagkgeg ptqpsladmt skaidvlskn sngyflmveg
      301 gridhalhgt nakraledta afdeairval skvdlsntli vvtadhdhtm tingyskrgn
      361 pildisrnyr dgqpskdadg ntyttlvfgn ganrpnvrap vdsatamnda ylqevgvrmg
      421 sagsethggg dvmlfadgad akafkgtidn tkvfglvrsa fgf
//
LOCUS       WP_175942552             477 aa            linear   BCT 11-JAN-2025
DEFINITION  alkaline phosphatase [Burkholderia pyrrocinia].
ACCESSION   WP_175942552
VERSION     WP_175942552.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Vimalraj,S.
  TITLE     Alkaline phosphatase: Structure, expression and its function in
            bone mineralization
  JOURNAL   Gene 754, 144855 (2020)
   PUBMED   32522695
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..477
                     /product="alkaline phosphatase"
                     /EC_number="3.1.3.1"
                     /GO_function="GO:0004035 - alkaline phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0106219 - zinc ion sensor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49383
     Region          1..477
                     /region_name="PhoA"
                     /note="Alkaline phosphatase [Inorganic ion transport and
                     metabolism, General function prediction only]; COG1785"
                     /db_xref="CDD:441391"
ORIGIN      
        1 mnrikmaall cagafglagc nsddgptsst papvqaaarn vifflgdgmg mttltaariy
       61 avgedgaltm dtlpesafvk tysndaqvtd sapsmsaymt gvktnnevis mspdtkaiep
      121 tagltgncga sngksvstll eiakakgmat gvvtttrvth atpaatyahv chrdaendia
      181 aqlvpggagy ngalgdgvdv vlgggtqffv pkdgggkrtd grnlvnelka kgyafaqnrd
      241 dllaadatks gklvglfsss hmsydldrga tkepsladma traldvlqnn pngyflmveg
      301 gridhalhdt nakralqdtv afdnaikatl dkvrksdpdl kntlivvtad hdhtlvlngy
      361 aartgkteag kpgvlgvlrs yqtgavakda dgapytiigf gngenrvqgs ragtaltdav
      421 tgaddyrqea vvrmdkgset hggtdvflga igrgadafhg viennkvfel vrnavql
//
LOCUS       WP_175942568             314 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Caballeronia sp. BCC1704].
ACCESSION   WP_175942568
VERSION     WP_175942568.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..314
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34253
     Region          9..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..295
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,230,247,274)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,193,
                     224..228,235..236,239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 meqiaierlt gliafaraas lgsytaaars lsvspsaisk siqrleqhfg lrlfsrttrs
       61 ltltpegrdl lertqrllre aegieqgvaa araepagtlk vtaplpvgvn ilapalpafr
      121 rqhrkvtvdv rlsdryvdli eegvdvairv gdpgdtrlia rrlaphrica faspeylrer
      181 gvprhpndlv qhdcvnfryq stgqeaawpf nvggklveft pasalmidvs davasalaag
      241 agigisttyi aasyvlrrel vpvlhefayd rfhlhavwpe srrsnpavka fvaflqgifp
      301 spapwdvlvr dhas
//
LOCUS       WP_175942596             320 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Caballeronia sp. BCC1704].
ACCESSION   WP_175942596
VERSION     WP_175942596.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..320
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34484
     Region          10..221
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(50..51,53,67..69,75,77..78,119,220)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(50,52..53)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(75,78,81,88)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(111,115..118,120)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(116..117,140..142,194..195)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          237..320
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 melfkvrvda vreeahgvrs fsisrvdglp feqyepgahi dvtgpsgitr qyslcgdpec
       61 vesqvfavkk eeqsrggsrs lheevsigte lsvgaprnlf kleesasehi ligagigitp
      121 llsmayrlaa rnarftlhyf arserhaafm tlltrapfes hvklhfgvqr dalpaaldac
      181 lrdagpdahv ytcgpapfmd lvvdraqarl paesihlerf kaepapavet sldsfdvqla
      241 stgqtvhvda ktsivdalas igievdtscg egvcgtcmvd vvsgepehrd hclskaeras
      301 ntvicccvsr srspvlvldl
//
LOCUS       WP_175942598             435 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Caballeronia].
ACCESSION   WP_175942598
VERSION     WP_175942598.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46685
     Region          22..428
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(35..36,39..40,43,83,141..142,144..146,149,169,
                     172..173,176,258,261..262,265..267,270,297,301,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mstvqststt erstamqdra lrrivvasva gnamewydff vygtaaalvf gqlffpanad
       61 pligtlgafa afamgfvarp lggivfghig drygrraslv wtllimgfat fgigllptyd
      121 hvglwapaal vglrllqgva sggewgggvl misesappek rgyyaawsql gvgggfvlss
      181 aaflgaqalp hdqfiswgwr lpflasilif algvyirhnl pesrdfenad kagktshmpv
      241 vevikrhpke ilmamglrva enggayifla fslvygkfag isnsvmltgv mlamviemva
      301 mllwgklsdr igrkpvymig avslavmafp ffwllnthst pliwlalvlg tavchgamig
      361 tlpalvgelf stevrysgva lghevasifa ggmspliata llsryhaywp valflivlgl
      421 itvvtlkfth etrqq
//
LOCUS       WP_175942600             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Caballeronia sp. BCC1704].
ACCESSION   WP_175942600
VERSION     WP_175942600.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34078
     Region          11..69
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          101..301
                     /region_name="PBP2_DntR_NahR_LinR_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators that are involved in
                     the catabolism of dinitrotoluene, naphthalene and
                     gamma-hexachlorohexane; contains the type 2 periplasmic
                     binding fold; cd08459"
                     /db_xref="CDD:176148"
     Site            order(107,109..110,114,172,209,276)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176148"
     Site            order(108,111..112,115..116,119..120,122..123,126..127,
                     129..133,135,198,226..230,233..234,237..238,241,255)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 mnkphlgiad lnllrvflai wdlrsltaag drlgltqpav shalrrlrtl fddplflrtp
       61 ggmvptdaay rlypplaqaf aiindavqql gkfdpataqr vfrvsmsdms eyyflpplva
      121 mldrdargir ievanlpves vsaamragei dlalgyvpgl degcvsqtlf vdehvcvvra
      181 ghplrrakpt redlaalryv yastnatghr mveqwldeln lkrdvvlrlp hfivapeivm
      241 ntdlavifpk siarrfnrgk afrvlplpfs lppieievhs htqfasdpgi awlretlvam
      301 fhqsep
//
LOCUS       WP_175942622             159 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Caballeronia sp.
            BCC1704].
ACCESSION   WP_175942622
VERSION     WP_175942622.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..159
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17847
     Region          11..144
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtqridyfqq spelskkliq lgtllqesti ethirelvei rasqlngcaf cvdmhvklak
       61 ihgerelrlh hvaiwrestl fspreraala waevltnipa egvpddiyds vraqysdkel
      121 sdltflvgii nswnrlnvaf rtapgssdka fgldkagle
//
LOCUS       WP_175942623             250 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Caballeronia sp. BCC1704].
ACCESSION   WP_175942623
VERSION     WP_175942623.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 250)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 250)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 250)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..250
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=26047
     Region          2..201
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mkivviggsg lvgsrlvall neaghqalaa sprtgvntit geglttvlmd advvvdvtna
       61 pswepqavld ffrtsarnlg kaevaagvgh hvalsivgtd rmpenayfaa kvaqeeaika
      121 agvpytivra tqfmefiggi adfstesgtv rvgdgrfqpi avddivails qvalaaplnd
      181 tvdiagpdra pfaeiiaryl ksvgdarpvv tdpkaryygg vveelslvpl gearigqtgl
      241 dqwlarakrg
//
LOCUS       WP_175942634             168 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [unclassified
            Caballeronia].
ACCESSION   WP_175942634
VERSION     WP_175942634.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Ho,Y.S., Burden,L.M. and Hurley,J.H.
  TITLE     Structure of the GAF domain, a ubiquitous signaling motif and a new
            class of cyclic GMP receptor
  JOURNAL   EMBO J 19 (20), 5288-5299 (2000)
   PUBMED   11032796
  REMARK    Erratum:[EMBO J 2001 Mar 15;20(6):1483]
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10482064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..168
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18315
     Region          31..151
                     /region_name="GAF"
                     /note="GAF domain; pfam01590"
                     /db_xref="CDD:460259"
ORIGIN      
        1 mseypvlyne edrldavaqc glldtpddpr ldritrlaay vtacpialvs ivaahrqwfk
       61 srhglavrqt prdvafcnya lvepgifvve datkddrfrm nalvtgdpgi rfyagiaitg
      121 asghrlgtlc vidtsprals pvqrrlfedl agcaadvlrv veaevtar
//
LOCUS       WP_175942646             246 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia pyrrocinia].
ACCESSION   WP_175942646
VERSION     WP_175942646.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..246
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25610
     Region          2..182
                     /region_name="POD-like_MBL-fold"
                     /note="ETHE1 (PDO type I), persulfide dioxygenase A (PDOA,
                     PDO type II) and related proteins; MBL-fold
                     metallo-hydrolase domain; cd07724"
                     /db_xref="CDD:293810"
     Site            order(56,60,112,137,140,144..146,182)
                     /site_type="active"
                     /db_xref="CDD:293810"
ORIGIN      
        1 milrqflhpd tggisylfgc ggkatgavvd pvddpadylr aaeaagmkia yvidthvhad
       61 hlstgralad aagasyvlsa raevalpfsg vedgdrialg nvvvdvlhtp ghtpehvsll
      121 vtdrtrsdep wfvltghtlm igdvgrtela vsaeagardl frsvrrlaal pdhvevlpga
      181 fsgsacgrgl sgkpastigf ekrynaalri dredafvrfm ltdvppvppa aaqlraanag
      241 hdaagg
//
LOCUS       WP_175942692             400 aa            linear   BCT 11-JAN-2025
DEFINITION  benzoate/H(+) symporter BenE family transporter [Burkholderia
            pyrrocinia].
ACCESSION   WP_175942692
VERSION     WP_175942692.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..400
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41377
     Region          11..399
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 mqpntppgai raigndwsvs aitagflavl isyagplaif fqaaqaahas namvsswvwa
       61 isigagvsgl faswklkvpv itawsapgta llvglfpqlt lnqavgayit aaliilligv
      121 tgyfdrlvrh iprgiacgmm agillpfgth afaaaseqpa lafgmiaayv ifkrllprys
      181 ivlvlltgaa latllgmthl gnvspsiaqp ifiapewtlg ttlslalplv vvsltgqflp
      241 gmtilrvsgy htparpiita tsvvslvvac fggitivvaa itaalctgkd ahedpdrryi
      301 aglangafyl igglfagtiv tvffalpkaf vailaglali gaiganvhgi fedenhreas
      361 vitflatasg mtwlglgsaf wgivigslsy avlnkvrrqa
//
LOCUS       WP_175942697             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Caballeronia sp. BCC1704].
ACCESSION   WP_175942697
VERSION     WP_175942697.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33591
     Region          <22..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          99..297
                     /region_name="PBP2_DntR_NahR_LinR_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators that are involved in
                     the catabolism of dinitrotoluene, naphthalene and
                     gamma-hexachlorohexane; contains the type 2 periplasmic
                     binding fold; cd08459"
                     /db_xref="CDD:176148"
     Site            order(105,107..108,112,169,205,272)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176148"
     Site            order(106,109..110,113..114,117..118,120..121,124..125,
                     127..131,133,195,222..226,229..230,233..234,237,251)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 mspselpdlk llqlfdllyd vrsvtraaeq lgqsqptisi wlgrlreylq dplfvrtpgg
       61 mtptpqadal igpcreiles lrrfaaweis fdpstakrrf ricmtdashi tllprilarv
      121 reeapgirle aaridgnter alesgeadla ighvpwlggg myqqqlymqd wvclvnrtha
      181 rvrsrltlkq yrseghvvia ggtgaqqleq allrenierd vvlelpgmlg lgsiiastdl
      241 iatlprnige tlarvngiaa hscplpvdqf avrqhwhaky hheagnrwlr sivadlfldk
      301 s
//
LOCUS       WP_175942715             450 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Caballeronia sp. BCC1704].
ACCESSION   WP_175942715
VERSION     WP_175942715.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..450
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48689
     Region          29..438
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(41..42,45..46,49,81,140..141,143..145,148,168,
                     171..172,175,269,272..273,276..278,281,309,313,364..365,
                     369,373,389,392..393,396..397,400)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mptitqaaas raavgdeaed qlyrkvlkri lpllllcyvv ayldrvnvgf aklqmldalg
       61 lsdsvyavga siffwgyflf empsnlllhk ygarfwiari mvtwgivssa lafisplasf
      121 fhvgtgtmfy ilrfllgvce agffpgiily mnywfparrq svamsgflia ipvsltlggv
      181 vsgwlmehth glfgmggwqw mlllegipsi lvafvvlfrm gdgiqsakwl tdaekallhk
      241 nlqqesakkt hsvaaalksp rvwlltfill tfntgfygla fwlpsiikas gvkstfnigl
      301 ltaipymcav vamiwngahs rktgerrlha aipacigglg lilsahfann vplsiflltv
      361 atcailglmp iywtfpgqil sgtaaaagia linsvgnlsg ftgsmitsva kdltgninng
      421 tyalgacllv scvlilaipk nmlnveraer
//
LOCUS       WP_175942736             305 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175942736
VERSION     WP_175942736.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..305
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=32992
     Region          4..297
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mnaryqgvfp vaptifdahg aldldgqrrc ldfmidagsq glcihanyse qfalgdderd
       61 litrtslehv agrvpvivtt shfsaricae rnrraqalga amvmvmppyh gatfrvpeaq
      121 vraffaeaad glriplmiqd apasgvalsa sflatlarei davsyfkiet agaasklrel
      181 ialggdaieg pwdgeegitl ladldagatg amtgggypdg irritdayfa grrdeaceqy
      241 arwlplinye nrqsgfltak almreggvia cdrprapwpe lhpqvragll dvarrldplv
      301 lrwgh
//
LOCUS       WP_175942738             430 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175942738
VERSION     WP_175942738.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..430
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46050
     Region          22..424
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(36..37,40..41,44,77,127..128,130..132,135,155,
                     158..159,162,256,259..260,263..265,268,296,300,351..352,
                     356,360,376,379..380,383..384,387)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnsltpatpa yeageavprr rwlrvippll laciisymdr vniafampgg mnaelgmdat
       61 maglaggiff fgylflqipg grraalgsgk kfiawslvsw avlsvltglv thtwqllalr
      121 fllgvaeggm lpvvltmvsh wfpdrergra namvimfvpl agmitaplsg filaaydwrh
      181 lfysagalsl lclvawmlla ddgpetarwv sprekayild alrdeqerkr aagapaaasf
      241 gemlrnptiw lliainfcyq vgiygytmwl ptllknlthg gmgkvgllam lpyvamvigm
      301 fvtsylsdrt gkrrlfvllp lvgfaaclal svlthtsmav sfafligcgf flqaaagvfw
      361 aippklcsve tagsarglin algnlggfcg pyavgvltqh vssaagvysl avtlavagll
      421 altlpkrced
//
LOCUS       WP_175942740             315 aa            linear   BCT 11-JAN-2025
DEFINITION  YncE family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175942740
VERSION     WP_175942740.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..315
                     /product="YncE family protein"
                     /calculated_mol_wt=35390
     Region          <12..207
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          <141..293
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mndilllvqk cahtfsfydl dtkaalkhiv lpnfpheftv dvneryayvg ifgietawsr
       61 ghegdhriae idlverthtr mldlwpyyrp hgmasdrdgr lyamseahdm llvfdeptrq
      121 pvpnmavpsg gvkthlvtlt rdasraygvh llsntvtqfh prdatvapra vmpgprpegn
      181 alsadertlf vanrgddtlv eidtetmtcg rrvktrsdpn riyrtsapdg rdlllltnsg
      241 eqsisvfdar qleeierial panptalsfh psrrvayvsf qddyvreldl etwrfvgala
      301 tlrepdasyv lagar
//
LOCUS       WP_175942798             205 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia pyrrocinia].
ACCESSION   WP_175942798
VERSION     WP_175942798.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..205
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22322
     Region          4..200
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mefltlsalp agmlfalvts itpgpnntml lasgvnfgfr rtmphlfgis igvailmlcv
       61 gfglgeafrr lpllytilea asvayllyla wrigtsgevk ahgakprpmt fieaaafqwv
      121 npkawmmvlt aattirlsad ygmnaawmav vfiligfpci slwaafglgl rrflsnrral
      181 rifnvtmavl lilslyplia hllpq
//
LOCUS       WP_175942801             807 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Caballeronia sp.
            BCC1704].
ACCESSION   WP_175942801
VERSION     WP_175942801.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 807)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 807)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..807
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=88595
     Region          12..759
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msttdvatap plasvetpla delrflslra saelgrmprc eltlvskrad idfsrilgkh
       61 vkvslrvdga kprvfggyvv sfrqtgmrgr lyayeaavrp wlwlltrrsn crifqnktve
      121 eivkaifadp vykqlelgei kwkansrahr preycvqyre sdfnfvsrll edegiyywfq
      181 dkdgreslvl tdtlaahesv egcealpyga vmsaapgtey vsewrvnhmi etrnwiltdy
      241 dfkhpsrplq kqavkqmpgf dafaglehfd ypggyveadh gesraksrad egfveasvtd
      301 dpainwhqvd arsnsksvra gtllkltrhp radqnaqylv trtlyeidla dheafdgaqs
      361 nrcecwfsai dakqpftpar vtrrpfvqgp qtavvvgpgg deihtdqygr vkvqffwdrq
      421 gkrdensscw irvsqpwagk gfgavaiprm gqevivdfle gdpdrpiitg rvynaeqmpp
      481 ydlpgnmtqs giksrsskgg saancnelrf edkkgaeqvl lhaernqdie vekdethwvg
      541 hdrkknidhd ettvvkhdrt etvgnnekid vtmnrtetvg vnesitigan rtktvkaset
      601 atvylqrths vginetitvg aaqevtigaf qavtvgayra vtvgayhtet vgasqtvsvg
      661 skqsvsvgsd qtvnvggkqs ttvggdravs vsgnrkidvk gnqttnvakd rsveikgkds
      721 lkvgatlvve aaesitfktg dstitmkkdg tisvkgktit idgsskiast aanisseata
      781 ksvtkgaave leasgintik gslvkin
//
LOCUS       WP_175942806             308 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175942806
VERSION     WP_175942806.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34472
     Region          6..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..299
                     /region_name="PBP2_DntR_NahR_LinR_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators that are involved in
                     the catabolism of dinitrotoluene, naphthalene and
                     gamma-hexachlorohexane; contains the type 2 periplasmic
                     binding fold; cd08459"
                     /db_xref="CDD:176148"
     Site            order(102,104..105,109,168,206,274)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176148"
     Site            order(103,106..107,110..111,114..115,117..118,121..122,
                     124..128,130,195,223..227,230..231,234..235,238,252)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 mdsldlnlip ylvalddtrn vsragdllgv sqprvsmalg rlreyfgdpl fvrtsrgmep
       61 tpraltllpa ardalaqier glvaphdfdp aasthtfsia lsdvgeivfl pkllqafatr
      121 aphanlrsvs lahdevgrgl eagsidlavg yfpdldgnnf fqqrlfthrf vclmrrghpl
      181 eqtppftveq flacghavvr aegrsqevle kylakqrmqr ravletphfm slpfilsrtd
      241 liatvphaig yayaaehafi vpvepplalp rfdlkqhwhr kyhndprtaw lrgvvaslfn
      301 deqdewpk
//
LOCUS       WP_175942813             207 aa            linear   BCT 11-JAN-2025
DEFINITION  SMI1/KNR4 family protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175942813
VERSION     WP_175942813.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10558574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..207
                     /product="SMI1/KNR4 family protein"
                     /GO_process="GO:0042546 - cell wall biogenesis [Evidence
                     IEA]"
                     /calculated_mol_wt=22900
     Region          40..189
                     /region_name="SMI1_KNR4"
                     /note="SMI1 / KNR4 family (SUKH-1); pfam09346"
                     /db_xref="CDD:430545"
ORIGIN      
        1 mrakgepimn detfraliva lratlekart nktnaawppp asdadiaame qrlharvsps
       61 yrrflsmqdg wpdyafgfti vgtrvaafet amkdialtvd serdawidsh geptseavmq
      121 yeqagdelnp neadwcpyvp gkmhiatdfn ggllfldper adadgemevf rwyadtgtqa
      181 rfisfeamlh adlaelgaae qsrtcsd
//
LOCUS       WP_175942838             333 aa            linear   BCT 11-JAN-2025
DEFINITION  FHA domain-containing protein [Burkholderia pyrrocinia].
ACCESSION   WP_175942838
VERSION     WP_175942838.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12811216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..333
                     /product="FHA domain-containing protein"
                     /calculated_mol_wt=36429
     Region          20..>157
                     /region_name="COG3456"
                     /note="Predicted component of the type VI protein
                     secretion system, contains a FHA domain [Signal
                     transduction mechanisms, Intracellular trafficking,
                     secretion, and vesicular transport]"
                     /db_xref="CDD:442679"
     Region          <20..86
                     /region_name="FHA"
                     /note="Forkhead associated (FHA) domain, binds pSer, pThr,
                     pTyr [Signal transduction mechanisms]; COG1716"
                     /db_xref="CDD:441322"
ORIGIN      
        1 mailkndssg eacllrayhv fgrdaarcdt virdasvsrv hahirwiggr welhdhssng
       61 tsvsgvplrd gehavlqrgd virfgragia pwrvdalddp adtlwpirga ahpivlaprq
      121 ilaaraaqpv tivrspagew lcddtlppra lhdgdevstg dvtwrlalvr ngstmmlaap
      181 adpavpaqll effvsrdeeh vrmllhvrgg vvdlgerahh yslvtlarar sadmqagyda
      241 atqgwieldr larmlgidts hvnvqihrar sqfaalpgld asqlverrrg svrfgdfpfr
      301 vmrgehlecq svpgaqprig vhrpapdpvv hys
//
LOCUS       WP_175942892             138 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175942892
VERSION     WP_175942892.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..138
                     /product="RidA family protein"
                     /calculated_mol_wt=14786
     Region          15..131
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mttvarvqce qvpdaphatw snalvignei vmsgmtahpa gqlstydqtm rvlekiralv
       61 etaggdigci tklvvyvtdi adktevgrar qaffdehvqa ggvypcstlv evsglvfpel
      121 rveieacarl diarraak
//
LOCUS       WP_175942895             309 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Caballeronia sp. BCC1704].
ACCESSION   WP_175942895
VERSION     WP_175942895.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..309
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33702
     Region          43..297
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 maratttrtt kpskadtard tqehdapgve satasdddpa agsgysvpgl erglrilaef
       61 sshepvlgap elsrrigipr tttfrllqtl eslgfleraa dersyrlgva vlrlgfeyls
      121 sleltdfgqp ildrlrddtg lsahllirde rdvvfvaraq trdpmfssvk vhvgtrlpah
      181 atvhghvlmg dltpadlrrl yperqlerft ertpatvdel yqrirataaq gyavseasfe
      241 rgisaisapv rdqtgrivaa ltvtvprsdi sederaplva racqaaldls arlnyrprvg
      301 dptlsyana
//
LOCUS       WP_175942904             277 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Caballeronia sp. BCC1704].
ACCESSION   WP_175942904
VERSION     WP_175942904.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..277
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30286
     Region          11..265
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mtpaeeqgdl ayrvpglerg lrilsefspr epvlgapels rrlgiprttv frllqtlesl
       61 gfleradser nyrlgvavlr lgfeylssle ltdhglplie alrddtglst hivirdgrdv
      121 vfvakaqsha sgfsavkvnv gtrlpahatt hghvlmgdls lddlrelyag ltlerftsqt
      181 pgtveelfdr vkvdaergya tsessfehgi svvsapvrgd tgriaavvtt tvprahidtt
      241 liesglidkv rdtahqlslr lnyrpaaehr fmkalgl
//
LOCUS       WP_175942905             316 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175942905
VERSION     WP_175942905.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..316
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33905
     Region          16..73
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          104..304
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(119..120,122..123,126,130,132..138,233..238,
                     244..245,247..248)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176126"
ORIGIN      
        1 mtdaspwgnr srlktrqlll vvaladegsi hraaaalnmt qpaaskllre leesigavlf
       61 erlprgmrpt lygdalirha raalgsldqa reelaalkag hlghvavgai tspglrlvpp
      121 avaavkgtha glhvsveidt snvllehlaq dkidivlgrl saehdklrlr yepltgetva
      181 avvrpdhpll aqaplsladv qraawvvppa gsvlrhrfel vfqraslapp anlvetsall
      241 fitqllersd miavlaedva ryyarhgivt vlplemdcrm ddfgiitrtd rlhspavtvm
      301 adairaaage vygval
//
LOCUS       WP_175942939             158 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia
            pyrrocinia].
ACCESSION   WP_175942939
VERSION     WP_175942939.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..158
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17816
     Region          4..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mttpldafdr kllmevqrda qtpqselgar vnlstaavnr rlkrlaedgv iarytavvap
       61 ekvdhpltiv vnveveseqi dlldamkrtf elcpqiqqcy yvtgewdfvl ilavrnmdqy
      121 naltrelffa nnnvkrfktl vsmsrvkvgl evpvdsge
//
LOCUS       WP_175942975             468 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175942975
VERSION     WP_175942975.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..468
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47691
     Region          18..443
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(25..26,29..30,33,65,115..116,118..120,123,144,
                     147..148,151,274,277..278,281..283,286,314,318,370..371,
                     375,379,395,398..399,402..403,406)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtaaapnraa arrvlaatcv sytlvlldas ivnvgltdia htfgsrvagl qwivsaytla
       61 fasllmtggt lcdrlgdrtv yvaglavfva asalcgfapn lpalaiaral qgvgsallvp
      121 cslalinraf pepaarasai svwmgcggia masgpliggv lidlfgwrsi ffvnlplgla
      181 giwlgrsvar aavdasrhfd wggqaaaiva iaaligtlie gpslgwrsap ivggavtsvv
      241 awlaffaiea rrrepmlpla lfrnrlfags tfvsmasafv fygllfvlsl fyrqvrgagp
      301 ldtglaflpm tvmvalgglg sgrlvarfga rgtmcaafgl yaagalgmta mssttpawla
      361 vapmlaigfa sgfispaats palgtvdrrr tgvaaaalna arqsgsalgv aifgaciatl
      421 qpfpaamrva lgmatglsal aaatwwiaar avpaaserav rmqapgrr
//
LOCUS       WP_175942984             225 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Caballeronia].
ACCESSION   WP_175942984
VERSION     WP_175942984.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..225
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25414
     Region          28..186
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvkdgneldg rlsstsarrp grpranesee rrrailaaar qsfvelgfar tttaevaara
       61 kvskraiyea ftnrtelfae virdcqhliv dlprpedeel plldtlirif rldldddaer
      121 areamlnliv restllpels dylyengalr srealiewll lesargrisv ddplvdagml
      181 mdmvfgallp rrrsteatdr mlrrdhikkr laiylrgiga dplsg
//
LOCUS       WP_175943022             236 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [unclassified
            Caballeronia].
ACCESSION   WP_175943022
VERSION     WP_175943022.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..236
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26078
     Region          14..229
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mqrlkdvrgt pattapgqgs attlnqeayr rleemivtle lapgtlvsea ilsrqlgigt
       61 tpirealqrl areylveiip rrgvvvttid vrrqfevlet rreldrllss aaarrsnale
      121 rkafaanfer teksvadgdt reflrldael nqllskaarn ataaalastl htvsrrfwfy
      181 hhdqhnplge igpvhchlve aiasgdpara ghasnrlidy lttfaqstlp hpltld
//
LOCUS       WP_175943035             956 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Burkholderia pyrrocinia].
ACCESSION   WP_175943035
VERSION     WP_175943035.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 956)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 956)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 956)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 956)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 956)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11534155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..956
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..956
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=97463
     Region          11..77
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          126..188
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(132..134,137)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          210..954
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mteplasaal qtielsvdgm hcggckgrvq halatvpgvv eatvdldaha atvtaqetve
       61 pgqlvdavre agyraavrda avetvaaapa ahtlrdeapp aaplataaat atatatatat
      121 atatieldid gmtcascvsr vekalanvpg vtrasvnlat eratvdaaad vsaarlveav
      181 kqagygatpv agaaaiairp vesvasadle leldiggmtc ascagrveka laavpgvara
      241 svnlaterat vhgtgaldaa tliaavttag yraslaaasa agamagadaq paspaqdsda
      301 rkrreavrer nlvtwsavls apliapmlva pfgidlmlpg wlqlalasiv qfgfgarfyr
      361 aawhavkara gnmdllvalg tsaayglslw mllrdpahpg hlyfeasavi vtlvrfgkwl
      421 esrakrqtte airalnalrp drarvvehgv erdvplsqvr vgtnvsirpg ervpvdgqiv
      481 sgrshidesl itgeslpvpk ddgdavtags ingegalvve ttaigaettl ariirlvesa
      541 qaekapiqrl vdrvsevfvp ailgialltl agwliagagt etailnavav lviacpcalg
      601 latpaaimag tgvaarhgvl ikdaqalela qratviafdk tgtltegkps vtafeavgmp
      661 rdealalaaa vqrqsdhpla raviaahdad vasrgaaaps avaadarava grgvearvgg
      721 qllalgstrw rdelglvvpp aldaraaele ragntiswlm radapralla liafgdtvkp
      781 gardaiaals argvasvlvt gdnrgsaaav aaslgigevh aqvlpddkar vvaelkrthg
      841 givamvgdgi ndapalaaad vgiamatgtd vamhtagitl mrgdpalvad aidiskrtyr
      901 kiqqnlfwaf vynligvpla algwlnpvia gaamafssvs vvtnalllrr wkgrar
//
LOCUS       WP_175943066             272 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175943066
VERSION     WP_175943066.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..272
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28566
     Region          20..218
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mpttqadhag eapdpsteea ssgvavldra failrafgpt ddrlslaels rrtglyksti
       61 lrllvalehg gfmrklddgq yavgheplrl aalyqrsfrv gpvvepllea lsrelgetas
      121 fyvrqgdmrs vlyrveptrm vrvsirvgee fpvgqgasgk vllaftdtqd arwndvrerl
      181 waasygerdp etasasapvf daagacvgal tvsgpksrla atpamaaala mllplaqkat
      241 valggagary daaavrdsla rlapaagdaa ga
//
LOCUS       WP_175943088             194 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            pyrrocinia].
ACCESSION   WP_175943088
VERSION     WP_175943088.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..194
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20168
     Region          5..157
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgvsrqqaae nrsaivaaae rlfrvrgvda vgltelmkea gftqggfynh fkskdalvae
       61 vmekamqdra dspkagslaa qvasylsaah rdnveagcpl sgfagdaprl tdaaracyar
      121 glaayldrle rmvategatp eqtrrdalav fsqmvgalvl sraiagtdpa ladeildagr
      181 gtltdgrdgp vapa
//
LOCUS       WP_175943096             324 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: PDR/VanB family oxidoreductase [unclassified
            Caballeronia].
ACCESSION   WP_175943096
VERSION     WP_175943096.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..324
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35545
     Region          17..229
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(58..59,61,75..77,83,85..86,127,228)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(58,60..61)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(83,86,89,96)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(119,123..126,128)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(124..125,149..151,203..204)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          242..324
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 mkdsasnels frtvvvtkkd qvaegifrfe lrdeagralp afaagahltv rvpsganrny
       61 slcndpaetd ryviavkrda agrggsvsma ddvaegdrid vsephnefgl serarsfvfv
      121 aggigitpil smmrhlkats gprfklyyvs rspettafld eltsaewkph vvihhdhgdl
      181 anafdfwpvf ekpgsgahiy ccgpralmds vrdmtghwpt gtvhfesfgv dqsraaentp
      241 fnirlertgr sfeipkdrsi leilrdngir apsscesgtc gscrttlcag eadhrdmvlg
      301 ddekrdhimi cvsraksqel vldl
//
LOCUS       WP_175943121             237 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [unclassified
            Caballeronia].
ACCESSION   WP_175943121
VERSION     WP_175943121.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..237
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25826
     Region          9..213
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mtpsllkirs rpdyveevyq aladaicdgs lppgtrltqe diaeqlavsr spvlqalrll
       61 kkdglvqdap grgvlvapln sdwlsdlyev ratldalaar laankkatld pqlfsrgrka
      121 wasgnvrami dadmefhfav yaasgnrlis dtarvhwvhl rrvmgaslqv sgqresiwde
      181 haaiakaier gdaslamsls dahtkraqah fiddfdlllg prnshqdlrv vdealag
//
LOCUS       WP_175943132             375 aa            linear   BCT 11-JAN-2025
DEFINITION  J domain-containing protein [Burkholderia pyrrocinia].
ACCESSION   WP_175943132
VERSION     WP_175943132.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10644999
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..375
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=42383
     Region          <210..250
                     /region_name="DnaJ"
                     /note="DnaJ molecular chaperone homology domain;
                     smart00271"
                     /db_xref="CDD:197617"
     Site            order(226..228,237,243..244,247..248)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
ORIGIN      
        1 mtarrgaavv iapshetasl skaqktfntl veqiekrrer lgaweavmpv fqkkfvdgll
       61 pleqastalr irllnlldda flqkglskae qrtlsaliad marnlldvsd daqlkviynr
      121 haasgdddra ttdraptkqa sestpaaepa ddldtlspde laermqaeqd eqfkrdmaah
      181 eareaqrakr kkaprqsaaa akreaeqaes sksirevyrk lasalhpdre tdpqeqqrkt
      241 vlmqrvnhay akgnllqlle lqleieqidr raidglgedr ltryngilee qireldqeil
      301 hvetgfrrty giarsvklap dtvvrmltrd iagmqrsnhd lavalrefdd pekvrdwlkd
      361 mkrrqassrf ddgpf
//
LOCUS       WP_175943133             438 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Caballeronia sp. BCC1704].
ACCESSION   WP_175943133
VERSION     WP_175943133.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..438
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47189
     Region          19..422
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,150,
                     153..154,157,254,257..258,261..263,266,293,297,347..348,
                     352,356,372,375..376,379..380,384)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 msiastttle rqtmrkviwr llpflmicyl mafidrgnvg maslqmnhdi gmsakvfgfg
       61 aslffvsyfi cevpsnlale kygarvwiar imitwglvsa atalvhnatt fyilrfllga
      121 aeagfapgvl lylsywvpka yrarvvatfm vsipaasfig spisalllqm dgiaglrgwh
      181 wlfilegvpt vllgiaclfm ltdkpakatw lnederawll galaaenaqp kkvapmpltk
      241 lfrnryvlcl alvdtcasaa gstlsvwqpq llksygltvl qtgllnavpy alasilmifw
      301 grhsdrtkeh rwhtvvpmll iggglfatsl sgslvptvcm lccvlvgaya fkgpfwalas
      361 dmlsnstiaa glatvnaian llggglmvnv ygwvkaatgs yslalmplai ltlvsvatll
      421 lltrkgqsgr mvgkteaa
//
LOCUS       WP_175943152             393 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DNA-binding protein [Burkholderia].
ACCESSION   WP_175943152
VERSION     WP_175943152.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13774864
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..393
                     /product="DNA-binding protein"
                     /calculated_mol_wt=43348
     Region          25..143
                     /region_name="KfrA_N"
                     /note="Plasmid replication region DNA-binding N-term;
                     pfam11740"
                     /db_xref="CDD:432038"
     Region          <86..334
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
ORIGIN      
        1 mtldemrqvi rdeleslras garrqelslh ackrlffdlg irpsaanvrd ltqtgsasdi
       61 pkdidhfwer irsaskirld gaaipkavee kagallgaly eealkaards ldgdreqvra
      121 giadaeqrlr datvrhetle salargearn eqlqarvtel evqlvsqtth gsaseatllt
      181 tvarlekelt asagrvdaeq aqnavlrdri dalqaelqqr tehyaqqikd avaeaerrvk
      241 pmlveldslr smastyqsgl rdvqrkefdf lqqlssakar adrleeqlrs qsdeleratr
      301 dasslrasrg mnpeiaalir rladagqlda eafavigtsl dqeipvpaqc prcdgepels
      361 qseegfevac pecehasgaw psrfeaiarf aht
//
LOCUS       WP_175943184             513 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Caballeronia sp. BCC1704].
ACCESSION   WP_175943184
VERSION     WP_175943184.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..513
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54801
     Region          10..512
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mekrsaidvd latltvdavq dgfrtgrfta eelaracfdw ierhndryna liflnpaaid
       61 darriderra agealgplag vpvvikdpmd mvgfpttagw skfysktggi dlmperdapv
      121 varmrragav llgktnvpil shtgshands wagptinvam pdrvpggssa gtasavasgm
      181 avlglaeetg gsiqnpasaq dlvgikptig lvpnagvmpl sgnrdvvgpi arnvkdaalc
      241 ldviagytse dpktlagvgr qpeggyasal nrdalqgkri glygpgwrdq plsdeaaaly
      301 ervqgelvsl gatliddpfq gsgfaelrrt tpplrnfdar glesipydve kylerlgkha
      361 siksfaqfae atkdedafsp dgvlnfmhsl adfkaalanp sqppempefi elkarylrif
      421 ervfdeqrld alvfpqmrce lpplhgkdti qettvgeini agvpgiavpa gyyesgspfg
      481 lifvgrqwde aallglayay eqgagrrkap vlg
//
LOCUS       WP_175943187             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175943187
VERSION     WP_175943187.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33148
     Region          9..>143
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..296
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,162,164,231,248,275)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,193,
                     225..229,236..237,240)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mvsldrfavf ravvesgsft aaaaqlnqar aavsfnikql etelgvtllt rttrrveltd
       61 agerfyarcl rvleeaesai ddarsehggm hgvlrvtstv eygtmvvapa lhefmqrhpa
      121 lrvrlethas qvdlvrervd vairlgrleq fqdlpyrgac latyevrpvi apsllaaagl
      181 sridspdvla rlpqlghtrl eriatwtlad rdgnphafqp gpkprlvvdn asvlrvlarq
      241 gsgvallpew lvrddlasga lvdalpdyrf ppqavyalyp stphvpqkvr awvdfmkayl
      301 a
//
LOCUS       WP_175943204             472 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175943204
VERSION     WP_175943204.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..472
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48240
     Region          23..450
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,277,280..281,284..286,289,317,321,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msefassaga repavnwram savllavala tldtaianta lpaiaadlha spaasvwiin
       61 ayqlamvatl lpfaslgdiv ghkrvyiagl avftlaslgc slastlpmlt aarivqgfga
      121 saimsvnval irglfpahrl grgvgfnalv vgvsfavgpt iaslilsvaa wpwlfavnvp
      181 lgvfalavai pslpqtargk hafdpvaalf nvitfaslif algefaqrgp lrivlaaaav
      241 alvfgwllir rqaghpapml pidlfrrpvf tlsaltavca faaqglafvs lpfyfetvlh
      301 rnavetgflm tpwsaivala apiagrlsdr yppgllgaig lallsagmas laalpvspnv
      361 fdigwrmmlc gagfgffqsp nlkalmssap persggasgi iatarligqa tgaalvalsf
      421 giagrhgptl almlgagfag aasvasglrl fasshrngvp aapervkepa te
//
LOCUS       WP_175943224             328 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Caballeronia sp. BCC1704].
ACCESSION   WP_175943224
VERSION     WP_175943224.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..328
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33610
     Region          9..326
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msdvsangrt tfvsrlarri dkpiliafgc ivalllvggm fsrnftspey illqlkvgaf
       61 lgiiatglmm villghidls lpwtvtvgam macavaghge lgrvlaipag igcgvligiv
      121 ngvlvallri psmiatlatn avaqgimivy tggsspqdsa pdvmrwlaag wlvpgvpnav
      181 alwvvigaat mfllsrttfg rtlyaignte raaylsgint rlvtvaafav csgfaafggv
      241 llagyaskaa qsmgdayllp aiaavvlggt silggrgsyl gtvagailit llqsilsvaq
      301 mpeagrqiiy gvviaamlll ygrskrqg
//
LOCUS       WP_175943226             326 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Caballeronia sp. BCC1704].
ACCESSION   WP_175943226
VERSION     WP_175943226.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..326
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33677
     Region          15..310
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msglrywyae nrgsafafgl fvlmfaiyli nypsslsanv iqtaankavl lalvsmgqtl
       61 vvltagidls igmmlvltnc laswmvtgda shsalgiagv laagalcgal ngviiifgrl
      121 qpivttiatg avyyglalll rpvpggsine eladvltgkv agvvpaslli llaavvivwv
      181 pfkrsavgra ayatgssepa aflsgmpirr aklvsytlag llaaigglfl tfftdtgeas
      241 lgsansytlf siaavviggv sllggrgsai gaifgafafr sigdllfvfn vdalwqplfq
      301 giilllavsi gacglfrvrn rlewfq
//
LOCUS       WP_175943227             218 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175943227
VERSION     WP_175943227.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10583942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..218
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23572
     Region          25..168
                     /region_name="Pyridox_ox_2"
                     /note="Pyridoxamine 5'-phosphate oxidase; pfam12900"
                     /db_xref="CDD:432864"
ORIGIN      
        1 mkdqtlispt srttirrlpe lanhdramly rivddayvch iafgdgqdth ciptahwrrg
       61 ddlyihgsng srmikalsag tqasvaitll dgfvlarsaf shsmnyrsav iygqfdaveg
      121 saeklaalda fmdkiaagrk hearpgnske inatsvlris laeaavkvsd slpsdkeedl
      181 elavwagvlp lkttrgtpvh adgndgvpvp dyvrnwad
//
LOCUS       WP_175943239             289 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfurtransferase [Burkholderia pyrrocinia].
ACCESSION   WP_175943239
VERSION     WP_175943239.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..289
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30404
     Region          15..284
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mphthyttli saanlaerla aapgsvvlfd crfdlvdpga geaayaaghp pgaqylhldr
       61 dlsgrktgtn grhplptrda latllasrgl kqgqqvvayd aqggayaarl wwllrwlghd
      121 svavldgglq aweaagqplt tdvpqpaagd fraaaplest vdaaavlanv tsrtrivida
      181 rapdryrgen etidpvgghi pgarnrffkd nltadgrfkt ghelretfst llagtepnlv
      241 ilqcgsgvta chnalaleia glhgaslypg swsewsadps rpiatgpnp
//
LOCUS       WP_175943241             291 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175943241
VERSION     WP_175943241.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..291
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31751
     Region          52..285
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mlkpevdslv phvpfsrrkf mqaalggtfa aavlpvsaqt vttdsagldv dtveirsgds
       61 svpayraqpa gktnlpviiv iheifgvhah iadvcrrfak lgylaiapdl farqgnasky
      121 ptmkdlfdni iskvpdrqvt edldatvawv gknggdparl gvtgfcwggr hawlyaehnp
      181 hvravvawyg fvegktdemt pfnpvdhaal lkvpvlglyg ekdtnitqas ladmrkaiqt
      241 sdsklarese ivvypdagha ffadyrpsyv kvdaedgwkr aiawfhkygv m
//
LOCUS       WP_175943279             487 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54 dependent transcriptional regulator [Burkholderia
            pyrrocinia].
ACCESSION   WP_175943279
VERSION     WP_175943279.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..487
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=52510
     Region          21..139
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <157..465
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mvarspdadg qaapemthvs vtapeagrkl fvimrtpdep llaqlrglgw eiavaktaga
       61 aqnmtsgvnv aaglvdftgf tsrdypalka clsqpaigwi siaqagvtig pavrelirsy
      121 cfdyvtlplp yewishvlgh argmaaldrv dgaayaasig ehgmigncea mqqlfstirk
      181 vaktdasvfi sgesgtgkel talaihersg rgkgpfvain cgaiphhllq selfgyerga
      241 ftganqrrag riesanggtl fldeigdmpi esqasllrfl qegkierlgg qesiavdvri
      301 isathvdldg aveagrfrad lyhrlcvlri hepplrargk didilahyvl qkfkadsgrk
      361 isgftsaald alrryewpgn vrelinrvrr aivmaesrll tphdlgletp getepvtleq
      421 aralaertai enallrndhr inkaaaelgi srvtlyrmmi ehglndhdnn gghdgtppgd
      481 agrervg
//
LOCUS       WP_175943286             185 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175943286
VERSION     WP_175943286.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..185
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=19240
     Region          23..170
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mntsstattl dadaphaqrv actlkingea rsfdiepwtt lldllrehcq ltgtkkgcdh
       61 gqcgactalv dgqrintcla lavsydgaai ttieglangd tlhpmqqafi dcdafqcgyc
      121 tpgqicsavg mlaeghahda aevreamsgn lcrcgaypni vqaileasgg qgvegnaiqn
      181 eearp
//
LOCUS       WP_175943320             225 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF1028 domain-containing protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175943320
VERSION     WP_175943320.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..225
                     /product="DUF1028 domain-containing protein"
                     /calculated_mol_wt=23471
     Region          2..212
                     /region_name="COG3342"
                     /note="Uncharacterized conserved protein, Ntn-hydrolase
                     superfamily [General function prediction only]"
                     /db_xref="CDD:442571"
ORIGIN      
        1 mtfsivgrcd ktgqlgiais sssiavgarc pwlragvgav atqnvtlpal gpqvlellen
       61 krlapaealq qaldanewre yrqvtvidaq grtaffsgke algthhavag dqcvaagnml
      121 agthvidamp lafaqadgll adrllaamqa amaaggeagp vhsaalkivs dlswplvdlr
      181 vdwadddpig klrdlwtaya pqmndyvtra lnptaapsyg vpgde
//
LOCUS       WP_175943322             144 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: RidA family protein [unclassified Caballeronia].
ACCESSION   WP_175943322
VERSION     WP_175943322.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..144
                     /product="RidA family protein"
                     /calculated_mol_wt=15893
     Region          28..137
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 msqpthtrir mfntkdtypn qtldndlcqa vragntvyvr gqvgtdfegn lvglgdaraq
       61 aeqamknvkq lleeagsdls hivktttylt dvryrepvyr evgkwlkgvf pistgltvva
      121 lgqpqwlmei dviavipdgw tpea
//
LOCUS       WP_175943337             349 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Caballeronia sp. BCC1704].
ACCESSION   WP_175943337
VERSION     WP_175943337.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Thorn,A., Egerer-Sieber,C., Jager,C.M., Herl,V., Muller-Uri,F.,
            Kreis,W. and Muller,Y.A.
  TITLE     The crystal structure of progesterone 5beta-reductase from
            Digitalis lanata defines a novel class of short chain
            dehydrogenases/reductases
  JOURNAL   J Biol Chem 283 (25), 17260-17269 (2008)
   PUBMED   18032383
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..349
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=38799
     Region          5..291
                     /region_name="5beta-POR_like_SDR_a"
                     /note="progesterone 5-beta-reductase-like proteins
                     (5beta-POR), atypical (a) SDRs; cd08948"
                     /db_xref="CDD:187652"
     Site            order(10..15,35..37,50..52,74..76,113..114,143,166..167,
                     169,176..178)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187652"
     Site            order(117,143)
                     /site_type="active"
                     /db_xref="CDD:187652"
ORIGIN      
        1 mkrykalvag gvgvigrqlv dhlaslpdwd viglsrrtpd qaqpgehiav dlldpedvra
       61 klgglgdvth ifhaayqekp tpqalidvnl gmlrnlvsvv sdsssalqrv vlyegakyyg
      121 ahlgrfktpa reddprhmpp nfyydmedwl vqeaadkhwd avvlrpdvvc gfalgnpmnl
      181 smviavyaai skelglplrf pgtatcygkl aqvtdaaqla rgsvwaatda pggesynltn
      241 gdvfrwdqlw paiadhldmp laepqtislr dymadkgplw ermvkkyglv dipyehvavw
      301 gfgdfifrcd wdvissttki rqagfhdvvd stdmflrlfd efrerkaip
//
LOCUS       WP_175943370             316 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Caballeronia].
ACCESSION   WP_175943370
VERSION     WP_175943370.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..316
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32708
     Region          1..316
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtparttfqg tqarlrallp aislvavlvp ilimqptvms yfgsslllnl avpivlatla
       61 qlaiitvndl dlsigsfvsl vacigatllv kqpwlgtlal vgcvlayaav galielrqip
      121 sivvtlglsf vwsglaivll pspggtspgw lgtamgyqtp fiaapivwsv liavighfll
      181 mrtsagvrir gaggnpramr rfgwslvrsk atlygiagif gvlsglsllg lttsadanla
      241 lrytllsiaa vilgggefvg grvsvigavl gaitltlaas flaflnisad wqvgmqgail
      301 iivlslrvll qrgerq
//
LOCUS       WP_175943378             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175943378
VERSION     WP_175943378.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33638
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdyidklrif rsvvemrsft raadmhglar pvvsravadl earfgsrllh rttrqvslte
       61 taeriyerca avldeldale veaqtqtrep egllrlvaht taalnrlvpl iagfkrahpk
      121 vrldvtlter pvdlvgegyd igivvpymlt settvvrlve ripvvivatp aylgahsrpe
      181 tpadladhpf vpispslrrp alsfrvdgdt ltvpyrfdis snspvfnrem vmhdfgigvv
      241 pktlveaela sgalvqlled adlvdafvei klayanrall pakvkafidy taaycdrvgr
      301 iapaaa
//
LOCUS       WP_175943349             486 aa            linear   BCT 11-JAN-2025
DEFINITION  FGGY family carbohydrate kinase [Caballeronia sp. BCC1704].
ACCESSION   WP_175943349
VERSION     WP_175943349.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Yeh,J.I., Kettering,R., Saxl,R., Bourand,A., Darbon,E., Joly,N.,
            Briozzo,P. and Deutscher,J.
  TITLE     Structural characterizations of glycerol kinase: unraveling
            phosphorylation-induced long-range activation
  JOURNAL   Biochemistry 48 (2), 346-356 (2009)
   PUBMED   19102629
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426119
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..486
                     /product="FGGY family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=52327
     Region          1..485
                     /region_name="GlpK"
                     /note="Glycerol kinase [Energy production and conversion];
                     COG0554"
                     /db_xref="CDD:440320"
ORIGIN      
        1 mshilaidqg tsgtkalvfd qtgqvhargf apvtcttprt gfveqdanal yasvlkavde
       61 clsgfkgdia gigisnqret vvlwnakgep iapgvswqcq rslgicerlk rdglqpliaq
      121 ktgllidpyf sgtkliwlne nderarahia agdayfgtvd swllyrltng aayrtdvtna
      181 srtmllnlrt lewdreliet fglqglrlpe lrpsasdfgm tdfdglldap lpilsmigds
      241 haaavgegcl spgvakatmg tgssimmnvg gkarepehgl vstlcfatdk rvdyalegii
      301 isagstpafl keklnlfddf akaeqaftey dnggvfvips fsgigcphwk ypggaqivgl
      361 nfstswqhva raayesivyq ikdvinvmeq aadvplaqly ldggltqrpf llqflsdtln
      421 rpvstlavse isasgaaala ayqaglaasl ddwqthrvva rrvepgsgve aaaenhaqwl
      481 rwierl
//
LOCUS       WP_175943391             133 aa            linear   BCT 11-JAN-2025
DEFINITION  tautomerase family protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175943391
VERSION     WP_175943391.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004965
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..133
                     /product="tautomerase family protein"
                     /EC_number="5.3.2.-"
                     /calculated_mol_wt=13953
     Region          2..60
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
     Region          75..122
                     /region_name="PptA"
                     /note="Phenylpyruvate tautomerase PptA, 4-oxalocrotonate
                     tautomerase family [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG1942"
                     /db_xref="CDD:441545"
ORIGIN      
        1 mpfisvkaig eplaphqvka iqegitalmv nvlrkvgplv gvlveqvpak swtvggepva
       61 caaqvdaivs agtntaeeka rfireasall qsviggtlae vsyvvihdvp kdswgydglt
      121 qayradqrss res
//
LOCUS       WP_175943425             339 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Caballeronia sp. BCC1704].
ACCESSION   WP_175943425
VERSION     WP_175943425.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..339
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36823
     Region          3..316
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 maktiailav pgvqmldvcg pldvfaqanv etgrdeydlk ivgtragqlk sssgarllpd
       61 evvgddfval htllvagaph assmtisntl rewlrtvakr skrfgsvctg afilaeagll
      121 ekrrvtthws cidelsrryp tvtaepdaly vrdgklrtaa gvtagldlal alveedlgre
      181 iamrvasqlv mffkrpggql qfsrkgraqp agrsvlqevq rlvaarpeld hsvasmaaha
      241 hlsprhfarl fqaevgvtpa vwvetarvaa arnlietrgd apkqlaakcg fanadvlrrt
      301 fvkhvgvtps eyrkrfmtlt radqtadqil arsvrqprp
//
LOCUS       WP_175943434             356 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175943434
VERSION     WP_175943434.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..356
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38213
     Region          2..265
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mtaplptrlp sllrhalrpl ldpyrryrha klihaarval ailvsiglst glrvphgews
       61 titvlivvgg lqhhgnirkk aaeralgtsi galaglglil lysaahapia iyllmavacg
      121 icayhaigka gyiallsait tvivaghgdn eivdglwrav nvligiaial afsfalplya
      181 tyswryklad alracaavha rvagdrqvgd dahlkemaal sallvqlrsl mpsvskecet
      241 smaqleaiqr slrlcigyle ilssavpard dvaareymrv gmkavnrrir dtlvgasral
      301 kfgkpsrlap rrrpadpphd apppqlsgyv sitaklagev dqlreklldt aqswni
//
LOCUS       WP_175943456             431 aa            linear   BCT 11-JAN-2025
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175943456
VERSION     WP_175943456.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..431
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=46351
     Region          5..430
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 mtdqassnwr letiavhggy rpdpttrava vpiyqtvaya fddtqhgadl fdlkvqgniy
       61 trimnpttdv lekriaaleg gigalalasg qsavtyaiqt iaeagdnivs asslyggtyn
      121 lfahtlpqyg ittrfadprd pasfeplida rtkaifaesv gnplgnitdi aalaeiahrh
      181 giplivdntv pspyllrpfe hgadivvhsl tkylgghgts lggaivdsgk fpwvehadrf
      241 krlnepdvsy hgvvyteafg paayigrarv vplrnmgaai spfnafqilq gietlalrve
      301 risdnalkia qhlarhehve wvnyaglpdh pdhplvaryl sgrapgiltf gvkggrdgga
      361 kfqdalklft rlvnigdtks lathpastth rqlspaelak agvkeetvrl sigiehiddl
      421 ladldqalaq l
//
LOCUS       WP_175943466            1074 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia pyrrocinia].
ACCESSION   WP_175943466
VERSION     WP_175943466.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1074)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1074
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..1074
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=115314
     Region          1..1040
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mferlirfai ahrwlvmlai aavaalgvfs yqklpidavp ditnvqvqin tavpgysple
       61 aeqritypie tvmaglpgle qtrsisrygl sqvtvifkdg tdiyfarqlv neriqeakdk
      121 lpagiapamg ptstglgeiy lwtveadaaa rkpdgtryta adlrelqdwv vrpqlrnvrg
      181 vtevnsiggy vkeyrvapnp aklmsygltl advvralern ndnvgagyie krgeqylvrv
      241 pgqartvddi anivltnvgg vpvrmkdvgl vdigrelrtg aatsngeevv lgtvfmlmge
      301 nsrtvskava akmedvnrtl psgvkaipvy drtvlvekav atvkknlleg ailviavlfl
      361 flgniraali talviplsml mtftgmvnak vsanlmslga ldfgiivdga vvivencvrr
      421 lahaqaaagr pltrderfae vfgasqearr alifgqliim vvylpifalt gvegkmfhpm
      481 aitvvmalaa amvltvtfip aavalfiger veekenrlmg warrayepvl tvfmtrparv
      541 mlgagaivlv tlglatrlgs efipslnegd lavaalripg tslsqsvemq ksiektlkar
      601 fpeiervfar tgtaeiaadp mppnlsdgyi mlkpadqwpd pkkprdtlvr eieealaelp
      661 gnayefsqpi qlrfnelisg vrsdvavkif gddmavlnqt geqiaaalqk vsgasevkve
      721 qttglpvltv nldrdklary gvsvadlqdt vaaavggqka gtlfqgdrrf divvrlpdel
      781 rsdidaikrl pialpapaag asaplaaapf vplaelatid vapgpnqisr edgkrrvvvs
      841 anvrgrdvgs fvadareqlq qdvrvpagyw vswggqfeql qsaserlklv vplalfmvfv
      901 llfvmfnnvk dgllvftgip falsggvvsl wlrgiplsit aavgfialsg vavlnglvmi
      961 sfirnlrdeg vpldaavreg altrlrpvlm talvaslgfl pmafatgtga evqrplatvv
     1021 iggilsstal tllvlpvlyr vshamswraa llgsfgggfg mgvlrrlgff kgna
//
LOCUS       WP_175943478             558 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GMC family oxidoreductase [unclassified
            Caballeronia].
ACCESSION   WP_175943478
VERSION     WP_175943478.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..558
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=61603
     Region          120..549
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mharrtpvsa espkdaehfp rgkngrapdv fhsgawvpmr eypqdeavdf aivgtgaggg
       61 tlacrlaekg fkvvafdaga wwrpleefas dethqgklfw tddricdgen plklgnnnsg
      121 kavggstvhf amvslrfrpe wfksrtllgy gadwpvdwre mwhyyaqved alkiagpvny
      181 pwgpkrpryp yrphelnaag lvlargceal gidwsptpla tvsaprgeah pcvyrgfcvs
      241 gcatnakqsa lvtwipravr agaeirdlam vgrivmgddg ratgveymre gqwqfqrarn
      301 vvvagyaiet prlllmsatd rypdglanss glvgknlmvq mnqavwgtme eevrwykgpp
      361 slaltehwny edkgkdffgg ycymsqgplp vawasvqngr glwgqqllde mqkynhqagl
      421 kivgetmpqe rnrvtladek dqyglpvarv tyslcdndkr lvahsldfms valeaagard
      481 vwretddtch lngtarmgnd patsvvnadc rswdidnlwi cdgsvfptvg gvnpsltiqa
      541 iamrtadrie alaargel
//
LOCUS       WP_175943479             224 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175943479
VERSION     WP_175943479.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..224
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23131
     Region          21..223
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 msvaskhaav epvagvpvap irvysfllsg hahrvrlfls llglpseivd vdlaagaqre
       61 paflalnplg qvpviddggt vladsnailv ylakrygdah wlpddpagaa avqrwlsyaa
      121 gpiasgpaaa rlvtvfgapl dqeaakrtaa klldvidrel agkpfaagvq ptiadiaayt
      181 yiahapeggv slepyphvra wlarvealpg fvgmpttrag llaa
//
LOCUS       WP_175943499             335 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Caballeronia sp. BCC1704].
ACCESSION   WP_175943499
VERSION     WP_175943499.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..335
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33891
     Region          18..335
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mkahlseglp gakavqttrt gtglkatlar aasalpalvm llavivcnaw lqpdfltlds
       61 lasnmqnaap vilvcmaqav vvlmgeldls vgagislvnc vlaaapglmg wgtgatclaa
      121 llaalaagac ngflvgyakq saliatfatg avwfgcalll mpqpggtvpe algewfaari
      181 gvvpvaalpv laavviwavl qrhrfgrrli atgsnadamf kvgvdvrlvk llgymlawlf
      241 vfaaavclsa qtasgdarlg lpytlnsvaa vviggislag grgamlgaic gslvlalign
      301 vvyfagipsn yqevfkgavi vialgftfvg akrra
//
LOCUS       WP_175943463             374 aa            linear   BCT 11-JAN-2025
DEFINITION  VIT1/CCC1 transporter family protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175943463
VERSION     WP_175943463.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Kato,T., Kumazaki,K., Wada,M., Taniguchi,R., Nakane,T.,
            Yamashita,K., Hirata,K., Ishitani,R., Ito,K., Nishizawa,T. and
            Nureki,O.
  TITLE     Crystal structure of plant vacuolar iron transporter VIT1
  JOURNAL   Nat Plants 5 (3), 308-315 (2019)
   PUBMED   30742036
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Li,L., Chen,O.S., McVey Ward,D. and Kaplan,J.
  TITLE     CCC1 is a transporter that mediates vacuolar iron storage in yeast
  JOURNAL   J Biol Chem 276 (31), 29515-29519 (2001)
   PUBMED   11390404
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..374
                     /product="VIT1/CCC1 transporter family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006873 - intracellular monoatomic ion
                     homeostasis [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=39729
     Region          8..129
                     /region_name="Ferritin_CCC1_N"
                     /note="Ferritin-CCC1, N-terminal ferritin-like
                     diiron-binding domain; cd01044"
                     /db_xref="CDD:153103"
     Site            order(17,47,50,96,116,119)
                     /site_type="other"
                     /note="diiron binding motif [ion binding]"
                     /db_xref="CDD:153103"
     Region          138..370
                     /region_name="Nodulin-21_like_2"
                     /note="Nodulin-21 and CCC1-related protein family;
                     cd02433"
                     /db_xref="CDD:153124"
ORIGIN      
        1 maskqelkry ranladelhs aalyetlarv evradrkrif aelaasekqh aqvwadklra
       61 nherartgpa lktalmqglv hvfgarfvlp tlaasefadr nkyagnpdta tmsadehrha
      121 nvvqslaneg kkaatkgaei adaeswhrgv ssgndlraav lgandglvsn fclimgvaga
      181 sapnraillt alagiiagac smalgewlsv tnarelartq iqreadeleh tpeaeehelr
      241 miyrakgldg eeasrvasqi mrdkdkalda ltreelgldp aelggnpwsa aavsfclfsa
      301 gavfpampfl wssgrpaivq cialsilala aigmftslfn grstvfsaar qiviglaaaa
      361 ftfgvghllg vsvs
//
LOCUS       WP_175943509             292 aa            linear   BCT 11-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Caballeronia sp.
            BCC1704].
ACCESSION   WP_175943509
VERSION     WP_175943509.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..292
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31642
     Region          68..292
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mklatlrvdg aktvavvdse ggkywpvsel cdgfsgdmvq lvqqfadlre tlkprgegrp
       61 lasaqvlapi dqprrnvfcv gknyhdhaee fsksgfdksa qagehipeap vvftkpvsti
      121 iatgeriprh advtqqmdye veigvvigka grgikkadam shvfgytiin dvtardlqkl
      181 hrqwfigksl dgfcpmgpfl vtadeidaen idvrcwinge lrqesnskll ifdiptiiet
      241 lsagmelqpg dviatgtpag vgigfnppkf lqsgdvvrme ipgigilene va
//
LOCUS       WP_175943535             470 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Caballeronia sp. BCC1704].
ACCESSION   WP_175943535
VERSION     WP_175943535.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..470
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=51136
     Region          80..468
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mstivdpalg qssdkpnrkr rvlrvaalli vaagafgaya vvapsrvpav igdivenltg
       61 anahpvvlqr pptvqlsava qlgkriffyr slsasgqqsc aschdpahaf gppndlavqq
      121 ggphltlpgy rpppslmyly rqpafsigpd qgdadeapdl aklaaqasgt traqksagva
      181 paapamvpqg glfwdgradt lqaqasgpmv npvemantsl aqvadklaht sykgdfeklf
      241 gprifdsgdl avseamfava ryqveeqafh pytskydywl egkarltqae lhglrlfndp
      301 dkancagchv skpspdglpp mftdfqyesl gvprnnalai nrdptfydmg vcgpfredlr
      361 eqtqycgmfl tptlrnvatr ralfhngiyr slddvmafyn erntapqkfy pkdakgevrk
      421 yddlppqfha nvddkdapfd rkpgdkpamt qedihdivaf lhtlndgykp
//
LOCUS       WP_175943552             447 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175943552
VERSION     WP_175943552.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..447
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47365
     Region          22..426
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(35..36,39..40,43,83,141..142,144..146,149,169,
                     172..173,176,258,261..262,265..267,270,297,301,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 myptdtvqsp saarpladrq lrriviasva gnamewydff vygtaaalvf ghvffppgas
       61 plagslaafa afalgfvarp lggivfghvg drygrkaslv wtllimgast faigllptya
      121 qvglwapaal vvlrllqgia sggewgggvl misenappeq rgyyaawsql gvgggfvlss
      181 aaflaaqalp ddafrtwgwr lpflasiaif aigiyirrhl pesrdfeqag krgahthlpi
      241 vecirrhpke illamglrva enggayifla fslvygkyvg ipngvmltgv miamivemga
      301 mlawgrlsdr igrkpvylig alslvacafp ffwlldtrat plvwlaltvg tavshgamig
      361 tlpalvgelf stevrysgva lghevasifa ggmspliata llaryhaswp vslflvalgl
      421 vtvatlcvmr etrivraapv aastdta
//
LOCUS       WP_175943556             368 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD/NADP-dependent octopine/nopaline dehydrogenase family protein
            [Burkholderia pyrrocinia].
ACCESSION   WP_175943556
VERSION     WP_175943556.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13367875
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..368
                     /product="NAD/NADP-dependent octopine/nopaline
                     dehydrogenase family protein"
                     /calculated_mol_wt=39525
     Region          1..>107
                     /region_name="GpsA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0240"
                     /db_xref="CDD:440010"
     Region          187..333
                     /region_name="Octopine_DH"
                     /note="NAD/NADP octopine/nopaline dehydrogenase,
                     alpha-helical domain; pfam02317"
                     /db_xref="CDD:426715"
ORIGIN      
        1 mkvcvlgggh gchaaaidlf ekghdvtwwr rdrepharlr elgtlnvtdy rgkryvplgd
       61 apgairltdd leaalrgarl vvvplpatsh dalaarvapl ledgqvvfmp pgtfgsfvfa
      121 raaadagnrs rvafaetgtl pylvrkhgdn dvvisayatr lptgvfpana agwafdvlra
      181 gypsvepved alsgalmnag pvihpplilm nagplehfda wdihnegtqp airrvtnald
      241 aerisvreal gyraphfpla dhyaaegdew mygrgahgkl tdsgdwreki dlrthrymle
      301 dtrlglsfiv scgswagvpt pvaqgllsia savavrdlya egrtlerlgl aalstdamra
      361 lldagyaa
//
LOCUS       WP_175943561             579 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Caballeronia sp. BCC1704].
ACCESSION   WP_175943561
VERSION     WP_175943561.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..579
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=62455
     Region          1..562
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mrrfdyvivg ggsagcvlah rlsalpslrv alieagadtp pgavpeaild sypmpvfcgd
       61 tyiwpdlkak atkqaaprvy eqgrvmgggs sinvqsanrg lprdyddwaa tgadgwawrd
      121 vlpyfrkler dldfpggelh ggdgpvpirr impkdwpafc hafgkglraq gvaelqdqng
      181 efgdgffpga fsneddkrvs taiaylddat rkrpnlriys klrverilmd gatargviav
      241 dedgermrfd agevilsaga lqspallmra gigdarelaa lgitcavnlp gvgrnlqdhp
      301 sltfchflep rfrmplarrr asmmaarlss gvagcdesdl ylssatraaw halgnrlglf
      361 flwcnrpysr grvqlvsada aaaprvdlnl ldderdlerl avgvrmlari vegsglsrda
      421 rdffpaafsp rvkalsrvge gnalltsalg llldtpapvr rmlierfftr glkmnallad
      481 draladfira nvfgvwhasg tcrmggandr davtdgqgrv hgarglrvvd aslmprlpsa
      541 ntniptimia ekiadamvaa rreraaldvs gspplaaah
//
LOCUS       WP_175943562             330 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia pyrrocinia].
ACCESSION   WP_175943562
VERSION     WP_175943562.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..330
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35295
     Region          15..222
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(52..53,55,69..71,77,79..80,121,222)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(52,54..55)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(77,80,83,90)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(113,117..120,122)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(118..119,142..144,196..197)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          247..330
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 mqanrhqvri dalidaaqdi rcfrvsrvdg qpfdayepga hidvtapsgi trqyslcgnp
       61 dergsylfav kkeaqsrggs rslhddvtvg aeltigaprn lfrltddase hvliaagigi
      121 tpllsmayal hkrgacyrlh yfarsrehaa fvdellaepf ashvtfhygv epdalatelr
      181 rcvesidvra hvytcgpgpf mdavvaaaat ripedsihle rfaaaaatad anadanastg
      241 pangfevrlq rsgqsvhvtp dtsivdalar igievdtscg egvcgtcmvp vidgepdhrd
      301 hclskaeras ntvicccvsr arsavlvldl
//
LOCUS       WP_175943564             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175943564
VERSION     WP_175943564.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34052
     Region          9..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          99..299
                     /region_name="PBP2_DntR_NahR_LinR_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators that are involved in
                     the catabolism of dinitrotoluene, naphthalene and
                     gamma-hexachlorohexane; contains the type 2 periplasmic
                     binding fold; cd08459"
                     /db_xref="CDD:176148"
     Site            order(105,107..108,112,170,208,275)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176148"
     Site            order(106,109..110,113..114,117..118,120..121,124..125,
                     127..131,133,197,225..229,232..233,236..237,240,254)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 mtsvdhldln llrvfqaive ersltkager lalsqpavsy slgrlrtlfd dplfvrtrsg
       61 mqptpvalel agivgkaldm vraalryaer fdpatstrtf rlslsdagem aylpaicqal
      121 rerapratls vqpmpveeie ealrasrldf aignlpelmp rtrhhvlfee tyvcmtgrrr
      181 glpagtalsl eqfvsaahvn vksvehshha lddalraqgv grnialevph fvalpsvlsv
      241 tdlyatlpkr laqilnrdna frlyelpvtl ppapvtmhwh ehfhedegna wmrallaeiv
      301 erfdda
//
LOCUS       WP_175943573             374 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Burkholderia pyrrocinia].
ACCESSION   WP_175943573
VERSION     WP_175943573.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..374
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37487
     Region          17..364
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mtgfidtftl ggpgptiaik dtidiaghpt raasralada ppaaehadvv cllldagwqi
       61 agkanmhela fgmtgindyt gtpvnpqdas ripggsssgs aslvglgsvd aalgtdtggs
      121 irgpaaccgv vglkptfgrv srrgvapvdt tldcvgpfar dirtlaavma aiapgfdrar
      181 aaassadsti aqitvdadpa iaaaldaalr asglrshaiv ldempaafaa glavinaets
      241 rafghlvata klgadldarl rmaatttpaa laeaeavrlr ftaqvdaale hadvlvlptl
      301 palpitlqqa rdgvsviams slirpfnlsg hpalsmplpl agsplkaglq ivgrkgader
      361 vcaiaahfea alaa
//
LOCUS       WP_175943590             434 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Caballeronia sp. BCC1704].
ACCESSION   WP_175943590
VERSION     WP_175943590.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46945
     Region          18..409
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,150,
                     153..154,157,250,253..254,257..259,262,290,294,352..353,
                     357,361,377,380..381,384..385,388)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mdvssssrvq avkmtnvrwk ifllllmlvs inyidraals vampaisqef sltperqgii
       61 lssffwtylf mqvpsgmlad rlkpraliaa atvgwgffqa lgalstgwfl llltrlglgv
      121 teapiypggg klnalwltqn ektrgaalld ggsalgsgvg aivvatlmtv lgswraafvv
      181 agvgtilcgv wawwyirntp rehpsiseee aayierahae edanepkvaa ggsllrffay
      241 rsvwgmclsh tctnliffgl mtwlptylfk vhgfdlkslg gatfliffcg fvgevlggql
      301 adkwkasgag anlvyrsmmi igaaavalsm lgvafvktpf lvvtllcval fflrwnggcn
      361 watpamlatr artgtlngim nfvgniagif vpifigyivq ttgsyflalm ffvavavfqv
      421 vsvlninyqr klpv
//
LOCUS       WP_175943641             135 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Hsp20/alpha crystallin family protein [unclassified
            Caballeronia].
ACCESSION   WP_175943641
VERSION     WP_175943641.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 135)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..135
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=14872
     Region          33..135
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 msdntqiaer ekgavarqes sqerrrttla pnvdivedvh avtlwadlpg vskdrldvkv
       61 hdgsliiege svvpvpsnlr lahaevrapy fsrtftvsed fdtskveatl kdgvlkltlp
      121 rreeakprri evtaa
//
LOCUS       WP_175943757             430 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_175943757
VERSION     WP_175943757.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..430
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46507
     Region          17..419
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(31..32,35..36,39,71,121..122,124..126,129,149,
                     152..153,156,244,247..248,251..253,256,284,288,345..346,
                     350,354,370,373..374,377..378,381)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mqsavvgtvr avasryrwtv callffatvi nymdrqilgl lapmlqhdig wsqvqygriv
       61 mafsafyalg llgfgrivdw lgtrvsyava mlvwsiaaml haavgsvmgf afvrallgig
      121 eggnfpaaik ttaewfprre ralatgifns ganigavfap aiipaiavay gwraafviig
      181 aigivwlavw lvlyrqadtr alaaeydepr deaeamdaan anagaprwge lirkretwaf
      241 ligkfltdpv wwfylfwlpk wlnesrgmdm qhiglplvci yalttvgsig ggwlssmllr
      301 agwsvnrark tamlicaccv lpiafvsqvq slwiavlivg laaaahqgws anlfttasdl
      361 fprravasvv giggmagsig gvlfsevigq vlqrtghywv lfaigasayl ialavmhvlt
      421 pkmkpaklda
//
LOCUS       WP_175943763             177 aa            linear   BCT 11-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Burkholderia pyrrocinia].
ACCESSION   WP_175943763
VERSION     WP_175943763.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..177
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18766
     Region          1..165
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtpahlipsp lgdiavried daltglffvg qkyfpplsia qdanalvtsp iarkvaeeia
       61 eyftgtretf svpihlrgtt fqrrvwkell aipfgelvsy gditervglp msaaravgga
      121 vgrnpvsimv pchrvvgasg sltgyaggid rkrallsleg agfergahhp vqtalaf
//
LOCUS       WP_175943762             325 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Caballeronia sp.
            BCC1704].
ACCESSION   WP_175943762
VERSION     WP_175943762.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..325
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=35386
     Region          63..>207
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 msnnireqlm aktanlpkpa dfkgeskkdr nargpqtmpg itsalaaaql riqeleskgv
       61 etdipieaiv pnpwqprrqf negklselar sidevgllqa vtvrrigesf qlvagerrlr
      121 ahklinketi ravviecsdq dmaalalmen vtrddlsdye iaiairraea efpnrtrlae
      181 amgisrsdly rflafdalpd fvkrdldltp svlgassaqd vanalkksge aglkalqelw
      241 pqvlsgdlvq tklaaslgah isrggaatda ggrsilkifa gkvqagsitk dvkgltfkfk
      301 agvvteeqen qlrehigkmf sirse
//
LOCUS       WP_175943788             166 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [unclassified Caballeronia].
ACCESSION   WP_175943788
VERSION     WP_175943788.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..166
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18421
     Region          15..155
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mkkttprrep pasgieidrv drailrqlqr dasisnvala akvhlsppac lrrverlrea
       61 glirgtvall npkaldagml vligvvldrs tpesftdfek aaqkvpgcme chvvtgefdf
      121 fmlirtrdsd sfnrlhaekl lylpgvrqir tfvvlreils ttafpv
//
LOCUS       WP_175943805             324 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175943805
VERSION     WP_175943805.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..324
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36496
     Region          4..224
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mpipkvsill pmydvegcia ecvrsilaqt rtdfeiiavd dcspdrsgev aralleaqdv
       61 ipwklvrnek nvgiaetrri avshasgeyv lcvdsddfva pnvvevacre adqhgadvvi
      121 faakcidpqg revyrvktgn etitglqavg rimdlslqay cwnklfrrel fasvehpagl
      181 iyedilvcvq alsrarvvrl ipdelyyyvk rgnglsvrfn privdlfeim drverdtrgl
      241 aidngsqlff rlkyvyayrn iafeaarlap dyataapild svasklrfth vgkiyadkrp
      301 klsvamcllk ihprifyrfv rsfn
//
LOCUS       WP_175943814             441 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175943814
VERSION     WP_175943814.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46695
     Region          9..414
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(22..23,26..27,30,69,127..128,130..132,135,155,
                     158..159,162,243,246..247,250..252,255,283,287,339..340,
                     344,348,364,367..368,371..372,375)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mgtsvkqpkr aalasfvgtt iewydfysya taaaivfgpl ffpgenrfvs llasfgsfav
       61 gffarplggv mfgylgdrfg rkrsllatlm lmavstvaig llpthaqagv iapillvlmr
      121 vlqgiavgge wggavllage hapegkrtff asfaqlgsas glilsmlafg aistlskddm
      181 mswgwrvpfl asavllvvgf virasvsesp efeeirksgs tarnpvreal kywpllllai
      241 ganvygiagv yfsnifmisy atqflsldrs mvlhcmaiva vlqfvvqlaa aflaqhfgtt
      301 rvllitgawa aivpfvmlpl vhmgtplsit vgvglatlae sgyysvvagf vsgifvarir
      361 ytaisiayqv cgalaggltp lvatiiaqna tpqwwplaiq ytsaavlssl cvwlisrrvs
      421 iddagapgka neplprgart v
//
LOCUS       WP_175943851             441 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Caballeronia sp. M1242].
ACCESSION   WP_175943851
VERSION     WP_175943851.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. M1242
  ORGANISM  Caballeronia sp. M1242
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Caballeronia sp. M1242"
                     /db_xref="taxon:2814653"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47474
     Region          11..409
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(22..23,26..27,30,62,112..113,115..117,120,140,
                     143..144,147,234,237..238,241..243,246,274,278,336..337,
                     341,345,360,363..364,367..368,371)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mpqrprvtrs vlalmcamsf imyldrvnls aaaglirddl hlsntdvgfv fgafaytyai
       61 cqviggwfsd rmgakttlvi catiwiiatv atgfaggvvs lfcarmllgv gegaalpaqa
      121 ralvnwypas krgfvqglth sfsrlgnalt ppliamlvaf aswrasfllv galtaiwlaf
      181 yawyfrddpr khrhitaeev aelppetias asktreptpw gklikrigpt mavyfcygwt
      241 gwlfftwlpt ffmhgrgldl kssalfsagv flsgvvgnta ggvlsdrilk rtgnvvaarr
      301 nmiivaflga lvflapvmiv hslpvmaasl slsffflemt igpiwavpmd itpkhvgias
      361 gmvnagsaia gifspiafgf ivdrtgswtl pfvgslglla vgiamtffmr pdikldaqtg
      421 neadvaesma efalaeqrgs r
//
LOCUS       WP_175943865             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia pyrrocinia].
ACCESSION   WP_175943865
VERSION     WP_175943865.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21814
     Region          1..192
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mhqttllifa avafvgiatp gptvllaltn gsrygvrraa ygfagamlsd lvlivavalg
       61 lgallmasaf wfsvvkwlga aylayvgirl ltskgsldva aahgsaapgr nasifgksfl
      121 tavtnpkgyl ffsaflpqfl dpsaplapqy valavtfall dgvvmfgyal lgaravrmlk
      181 rsgalwlert cgamllalag slalyrrhaa
//
LOCUS       WP_175943869             143 aa            linear   BCT 11-JAN-2025
DEFINITION  GFA family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175943869
VERSION     WP_175943869.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..143
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15427
     Region          3..130
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mirtqsahcr cgavtvtlrg epaaranchc atcrdfygtp mlsatawppe rvaidggnat
       61 fphpsksmsr twcascgeiv fgtnrlgmrv vpnslaarah ggqlpddlqp tmhlfyrqrv
      121 idvvdalpky ldgwdgptld nan
//
LOCUS       WP_175943880             242 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175943880
VERSION     WP_175943880.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..242
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27144
     Region          20..237
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 msetaafeed vvvtalqgfs ldesrsyteq vhvllrhaiv rgalpphtal seavisttik
       61 vsrtpvreaf aqladerlvq ihrkvgtfva pipmsileeg rfarstleca nhvelaqkit
      121 aeqlaelsri idaqraavaa hdveaffeld eamhgrmfaf agrphvweml qpmkrqfdrv
      181 rwllldrved harralqehe qilahiasrn mallgasvat hvdrigshlp evrsraphyf
      241 vd
//
LOCUS       WP_175943910             252 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Caballeronia sp. BCC1704].
ACCESSION   WP_175943910
VERSION     WP_175943910.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..252
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27340
     Region          30..248
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mlassteikp avspsseavi vsspydalhk iaagqrgslt gaveealrea ivtlalepgm
       61 midkiavcer mgvsrfpvsa alarlehagl vevlpqrgtr vkpialrdir qhlfirsale
      121 vetvrgvaam hdpaileale tnltqqream angarlafha ldlafheill daialprvke
      181 ivavsrnald rarqllaspe rlvhtldehe rifdalkkgk adaaakamhd hldqvvaelh
      241 rsakdrpdlf ep
//
LOCUS       WP_175943962             291 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175943962
VERSION     WP_175943962.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..291
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32694
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..284
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,220,237,264)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     214..218,225..226,229)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mellndmalf vevvkakgfr saadalgmpn stlsrrigal ekaiglrllh rttrrielte
       61 agqlyferck rivdearlah eqlgellaep agvlrasfpv dfaviyltpl ivefanrhpk
      121 ltfdfeltsr rvdlvsepfd vairmgesad sqlvarrlat frnhlyaspr ylersgepre
      181 pddltrhqcl svqrvdawtl hddarevevp vggrfvvnsv gmvrqlavhd agiiqmpeev
      241 vaddvaagrl rrvlpgwega qvpvyamtet rllpaktqif ieflrehfaq t
//
LOCUS       WP_175943999             673 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Burkholderia pyrrocinia].
ACCESSION   WP_175943999
VERSION     WP_175943999.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 673)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..673
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=72865
     Region          2..660
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mrddvdqaar traahpagwp apsiqkaher setfglqvsa rpdydvlssa alvlkreqsr
       61 vlcvhampvm etlheqivnt qsmivltdae glilhsigdd dflqraekva lrpganwaes
      121 rqgtnaigta laelcpmvvh gdqhflaanr fltcssvpil dpygdaigvl dvtgdhrsyh
      181 qhtmalakms vqmienhlft ttfqetlqvs fhgrpeflgt lmegivafta dgrflsanrs
      241 aqfqlgmpla vlrahtlssl fditsaqlid rmrastdrhl mlnlgtgavv carvhfrrat
      301 laegsrptdv hdagapaara stvpapaagt saglsrlnyl dtgdpqvacv iakvrkvigk
      361 dipilitget gtgkellaqa ihndsprrda pfvavncasi petlieself gyeegaftga
      421 rrkgaigkll qanggtlfld eigdmpyplq vrllrvlqer lvnplgstkt iavdisiica
      481 thrdlrdmia qnrfredlyy rlnglvvrlp plrdrtdlai vvqkmlqrea fagsdcppls
      541 vapdvmalfv rctwpgnfrq lgnllrtaaa mvdddgeirr ehlpddffdd lrrgdapvep
      601 aaqhdpavap caveafppad arlqdvaasa iaaalarhgg nvsaaaralg vsrntiyrkm
      661 paadaerqqa des
//
LOCUS       WP_175944054             551 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia pyrrocinia].
ACCESSION   WP_175944054
VERSION     WP_175944054.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Gournas,C., Athanasopoulos,A. and Sophianopoulou,V.
  TITLE     On the Evolution of Specificity in Members of the Yeast Amino Acid
            Transporter Family as Parts of Specific Metabolic Pathways
  JOURNAL   Int J Mol Sci 19 (5), 1398 (2018)
   PUBMED   29738448
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Vangelatos,I., Vlachakis,D., Sophianopoulou,V. and Diallinas,G.
  TITLE     Modelling and mutational evidence identify the substrate binding
            site and functional elements in APC amino acid transporters
  JOURNAL   Mol Membr Biol 26 (5), 356-370 (2009)
   PUBMED   19670073
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146941
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..551
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59479
     Region          31..470
                     /region_name="AA_permease_2"
                     /note="Amino acid permease; pfam13520"
                     /db_xref="CDD:404414"
ORIGIN      
        1 msqaglrans tsdveatish dstghtlhrg ltwkdafwvt sgvpagvlft iggvcatigq
       61 pawaiwiaai tmgliqsaty aeisglfphk sggasvygai gwvrysklia pvsvwcnwla
      121 wspmlalgcg laasyaltsl fpvdaavlhw qlkladlsfi kpglslrina tfiiatilll
      181 itfklqhsga skaartqril giasltplli vgivpfvtgd vpmsnllpll plghdahgnl
      241 taatfgswng qgvtmalgam fmagwasygf etavcytref rdprrdtaka ifwsgalclv
      301 vmtlvplafq galgtqamld paigdgtgva aamakivggg awvanavvvm lmlsillivm
      361 tsmmgssrtl yqasvdgwlp kylshvnehg sptramwtdl gfnlvllmms dymtvlsisn
      421 vcymlfvfln lqsgwihrmd rgnwdrpfrc ptwllvggai cgyanlvyvg aganlqgegt
      481 lrngliamll ivpvflyrhy wqdrgrfpaq mqrdmelevp krsawlnlmp yaaligaglt
      541 iwlsyylawv k
//
LOCUS       WP_175944127             223 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: C40 family peptidase [unclassified Caballeronia].
ACCESSION   WP_175944127
VERSION     WP_175944127.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..223
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=23656
     Region          24..201
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mqpltltqtc araaagmllg llmtttsgaf adevssnsqn agngittask atdtaaiaat
       61 adtasaprga kaffsgvask agdvvvgaln migvryrwgg dtpdsgldcs gfvryvfqdt
      121 lgmtlprrae emsrvgekvr vsdlkpgdlv ffntmrrsfs hvgiyigdnk fvhspstgst
      181 irvddmengy wekrftgarr ienaqfndgt elrqrvsatl ggy
//
LOCUS       WP_175944074             239 aa            linear   BCT 11-JAN-2025
DEFINITION  histidine phosphatase family protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175944074
VERSION     WP_175944074.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..239
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26196
     Region          12..209
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mahydlpkrr riflmrhgdv tyfddtgrai dpesvplnar greeasaagr efaaqnvrfd
       61 rviasglprt ietaervlae tgqaaqieiw pewqeirggr lanlstsdie raflsvfdgv
      121 vpeetqflgg etigqlldra lpamtrlrad tswdtvllvl hggvnralls haitaggraf
      181 fghlsqatgc inaldvgekp gdwvvhainh sppsplhadv rnttmellya qfvkfkase
//
LOCUS       WP_175944142             433 aa            linear   BCT 11-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175944142
VERSION     WP_175944142.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..433
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46317
     Region          5..431
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 mslnddatfw rdarqhlvry ggtfepmiie rakgsfvyda dgraildfts gqmsavlghs
       61 hpeivsvige yagkldhlfs gmlsrpvvdl atrlaaitpd gldralllst gaesneaair
      121 maklvtgkye ivgfaqswhg mtgaaasaty sagrkgvgpa avgsfaipap ftyrprfern
      181 gaydylaeld yafdlidrqs sgnlaafiae pilssggiie lpegymaalk rkceergmll
      241 ildeaqtgvg rtgtmfacqr dgvtpdiltl sktlgaglpl aaivtsaaie erahelgylf
      301 ytthvsdplp aavglrvldv vqrdglvara namgdrlrrg lldlmerfdc igdvrgrgll
      361 lgveivkdrr tkepadglga kitrecmnlg lsmnivqlpg mggvfriapp ltvseeeidl
      421 glsllgqaie rav
//
LOCUS       WP_175944188             209 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia pyrrocinia].
ACCESSION   WP_175944188
VERSION     WP_175944188.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..209
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21998
     Region          1..207
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msiqtwmlfa aaylattlsp gpnvllvirn tvrygshgta atiagnlvaq gvvvllvalg
       61 vgavlaampp lfvamkvvga aylmvlgvrq lrgdrkaags tgaaeiavpd rgklfrealf
      121 vsgsnpktmi flsafmpqfv vhdrplalqf vvmyatiact vvvvhsvysa gvrrfhrgfg
      181 msravrtlkr asgllfvglg iklltarqa
//
LOCUS       WP_175944216             309 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175944216
VERSION     WP_175944216.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34176
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..291
                     /region_name="PBP2_CrgA_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08475"
                     /db_xref="CDD:176164"
     Site            order(103,107,146,161,163,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176164"
     Site            order(104..105,109..110,112..113,116,120,122..128,190,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176164"
ORIGIN      
        1 mtdrldgvtt fvqvvesgsf alaaerldmt rsavgkavar lekrlgarll qrttrsqslt
       61 ddgqayydrc vralaeleaa eadldcgrne argklrlsvp lafghhcvtp ivldlartyp
      121 hlridvsitd rfvdlveegi dlavrigtla dstslavrrl gtqygslgaa psylarygmp
      181 kslddlkhhr tiaysrsgvp qpwdlrapdg stvrvdmqhq lsfddvqaia aagasgfgia
      241 wlpswlldyy vkrgemavvl drcfvcegdi haiwpktryl prktrcvida lvqaippmie
      301 rrdefsemk
//
LOCUS       WP_175944218             512 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175944218
VERSION     WP_175944218.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..512
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52413
     Region          16..426
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,142,
                     145..146,149,273,276..277,280..282,285,313,317,371..372,
                     376,380,396,399..400,403..404,407)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtlsdsrrna valaavclts lmfgleissv pvilptlehv lrgdfngmqw imnaytiact
       61 tvlmaagtla drfgrkrvyv igtvlfgats llcglapnvp vlvagrllqg asggamlicq
      121 iavlshqfre grergrafgi wgivfgiglg fgpivggaiv alaswpwvfl vhaplavial
      181 vliggavqes rdphagtldv agivtlslav lglafyitqs aelgltsaag lgvlgatvla
      241 lagffvaera sarpmfdfsv friraftgai fgsmgmnfsf wpfmiylpiw fqvalgydsv
      301 tagvallayt lptlvappfg erlalrygpg vvipgglfti aagfvlmrlg saadhaswvt
      361 mlpgcviagi glgltntpvt ntttgavpss ragmasgidm sarmislaln iaamgfvlva
      421 givaslkgga agaigdaalr rlaqeiasgr tdglqqiapa laqadpsgaa lhaalvhgfg
      481 wvmvygaagv avlatasava faparrrapv ce
//
LOCUS       WP_175944249             167 aa            linear   BCT 11-JAN-2025
DEFINITION  RDD family protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175944249
VERSION     WP_175944249.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..167
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18682
     Region          1..165
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 msvsaaatip plrapslrrr lstmvyegvi lfgvvfvagy lfstltqqrn glthhdwlms
       61 wiglvlaayf vwfwthggqt lpmktwrlkv vdargepltv gralaryvla wlwflpplal
      121 hpllslavpq tlivlavwia fwaaavwldp srqflhdrla gtrivpa
//
LOCUS       WP_175944282             189 aa            linear   BCT 11-JAN-2025
DEFINITION  peroxiredoxin [Caballeronia sp. BCC1704].
ACCESSION   WP_175944282
VERSION     WP_175944282.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 189)
  AUTHORS   Jeong,W., Cha,M.K. and Kim,I.H.
  TITLE     Thioredoxin-dependent hydroperoxide peroxidase activity of
            bacterioferritin comigratory protein (BCP) as a new member of the
            thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide
            peroxidase C (AhpC) family
  JOURNAL   J Biol Chem 275 (4), 2924-2930 (2000)
   PUBMED   10644761
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..189
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.24"
                     /GO_function="GO:0008379 - thioredoxin peroxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20119
     Region          35..177
                     /region_name="PRX_BCP"
                     /note="Peroxiredoxin (PRX) family, Bacterioferritin
                     comigratory protein (BCP) subfamily; composed of
                     thioredoxin-dependent thiol peroxidases, widely expressed
                     in pathogenic bacteria, that protect cells against
                     toxicity from reactive oxygen species by reducing...;
                     cd03017"
                     /db_xref="CDD:239315"
     Site            order(74,77,148)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239315"
ORIGIN      
        1 mkrrtkmagv alsgliacav aayplmarat lkpgdvappf vtqaslggnv fdysladalk
       61 kgpvvlyfyp aaftkgctie ahefaeavdq ykaqgatvig vshddigtlq rfsvsecrsk
      121 fpvaadtdak iigaydaalp fkssmanrvs yviapdgkvi yeytslspdq hvantlqalr
      181 dwnakhkaq
//
LOCUS       WP_175944289             245 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175944289
VERSION     WP_175944289.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..245
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=24991
     Region          1..245
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mlalvilagl waglqntlag ggsfitlpal ivsgmsplaa nitstvalfp aqvttgwasr
       61 nmvrgagkls fralfaisvv ggalggllll ktpssifsrl vpwlvlfati vfawgsffrk
      121 psegaahlgt ipaaisqfmi aiyggyfggg lgflmmatlt maglsprham stknalagvm
      181 nasavvlflt spqlhwgaal algggaivgg llgtwalhcv nervlrigiv cigalltvgl
      241 fvkpi
//
LOCUS       WP_175944320             389 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Caballeronia sp. BCC1704].
ACCESSION   WP_175944320
VERSION     WP_175944320.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 389)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..389
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41497
     Region          46..384
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mgvagkhypp hanpqhdsad aatdkdrssd ervrrqswfg hllnrpefaa isgtvlvfiv
       61 fgfgagssgm fnldgvmnws qvaaylglla vgacllmiag efdlsigsmi gfagmmvalp
      121 svyfhwpisv silfafaasm llgalngylv mrtrlpsfiv tlaflfilrg ltlalsimfa
      181 drtiisgvgd laqkdwvadt lfhgvalhgf ftwlahlgig klldsgeplv pgipkviiww
      241 lvlaaigafv laktrygnwi lavggdanaa knvgvpvkrv kislfvltaf csclfavlqv
      301 cdigsaaadr glqkefeaii aaviggtllt ggygsvvgac fgalifgvvq igitytnvss
      361 dwfrvflgvm lliavlfnhy vrrrvsqaq
//
LOCUS       WP_175944330             342 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175944330
VERSION     WP_175944330.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10859374
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..342
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38675
     Region          3..98
                     /region_name="HTH_NolA-AlbR"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators NolA and AlbR; cd04788"
                     /db_xref="CDD:133415"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133415"
     Site            order(51,54,58..59,68,80,84,90,94,97..98)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133415"
     Region          <259..336
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 mqlkvgelak rsgltvrtlh hyhaiglltp saradngyrl ydrhdiarlh qiqalrrfgl
       61 slteigdyln qpgtplvdlv akqialldrq laqtaqlrer lvhlhaqlaa gtepeladwl
      121 ttlelmtvyd kyfseeelar mpmyrksqtg daewialvgd vralhdagvp pedervrala
      181 grwmtllvrd tnndprllak lnlmherepa mqskigista lrdyvlrata etkmrifeky
      241 lapdeirfmr ahygkramew pqlmgdvrda idagakpdsp egralaqrwl dlfcsyaghd
      301 pathakfrha mtnepaltkd awvddtllgf ireamaqlap ar
//
LOCUS       WP_175944423             152 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia pyrrocinia].
ACCESSION   WP_175944423
VERSION     WP_175944423.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..152
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15461
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 myerifaald dsrgarlald eaitlarasg glviavcvvs dtppltnigs ayvdriasgg
       61 vdadraavai adaetafrlc gvrgtaqtid acgesvpsvl araaadcdad livmgthgrr
      121 gvrrallgsv aesllrtadr pvllvrddpg aa
//
LOCUS       WP_175944405             410 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Caballeronia].
ACCESSION   WP_175944405
VERSION     WP_175944405.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..410
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43222
     Region          1..365
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mpssvrlrvf flfaagyfvs yvfrgvnlgf aplithdlgl saadlgllts lyfigfaiaq
       61 ipvgvlldhy gprrvtagml vfaaagiwtf gashglgglm vgrlligvgv svclsaafka
      121 saqhfpvarl plvngftmav gglggvvvgs plasllqtat wrqvsiglgv ftlvvaaaia
      181 lfaprkadth hqadiisqfk gtwhilksga fwkiasfsvv tqgvfyamqs lwirpylldv
      241 mnltpahaaa lvsvlgfamm lgcvgfgaaa rgmerrgvsv yafcgvgmal yvlvqvlmvl
      301 rvplppatll aaygvfggtg ilsyavmaey fpshmigrat ttltlvifll ifgfqvgvga
      361 vlsrwtpesg hypaaahvtv wsvlialqla savwyvlpsr vlhktgrtas
//
LOCUS       WP_175944428             210 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SCO family protein [unclassified Caballeronia].
ACCESSION   WP_175944428
VERSION     WP_175944428.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..210
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23115
     Region          53..205
                     /region_name="Sco1"
                     /note="Cytochrome oxidase Cu insertion factor,
                     SCO1/SenC/PrrC family [Posttranslational modification,
                     protein turnover, chaperones]; COG1999"
                     /db_xref="CDD:441602"
ORIGIN      
        1 mhtsfpaspl tlaarwrrfa aplaflalaa csrpgepwhl tdvsghlpdl nfsltddsga
       61 pvtgrsfegh ttlvyfgyth cpdvcpetma rlmqvlqrvg pdadnarilf vsvdpardtp
      121 pllrayvraf dekhavgltg sdraieavaq ryriayqmek rdprgayevs hssgvyifdr
      181 egharllatd rdsidaiaad lrriihskda
//
LOCUS       WP_175944452             487 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175944452
VERSION     WP_175944452.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..487
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52108
     Region          58..467
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(68..69,72..73,76,110,160..161,163..165,168,188,
                     191..192,195,307,310..311,314..316,319,346,350,399..400,
                     404,408,424,427..428,431..432,435)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mnsqsldlgg tagepasarp paapagvgad aaafparrvt lgdfmddlpv galhrfvvwv
       61 igiglffdmy eiflvstigs alqneyglsr qstdfkllla safigmfvga mclgsladri
      121 grrkaflltl vwysvfslvg afsvnadmlv acrfltgigv gaiypvadsf lseilpkekr
      181 grlaawaytt syvavplvgf lalwlnplhv agvagwriil aigslgavyv lfvqhrlpes
      241 prwllaqgrt adahaalrrf aegtgvrvpe qfaepaepqr plglgerial lrrepygary
      301 vmlaifhllq gfgyygfgtl agtvvksrgf dvtdstlfia lsfvgypigs llsipllnwi
      361 errtlvivsi lsiavfglcf aysgnivliv gfgllttcas nvfsnayhvy qaeifparvr
      421 staigstyal srivsgalpf vllpvlvsyg agamfgvisi algivaitlr vlgplttrrs
      481 qdeinpv
//
LOCUS       WP_175944456             194 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Burkholderia].
ACCESSION   WP_175944456
VERSION     WP_175944456.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..194
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22354
     Region          18..186
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mespptsrtm tdpdrditai vtrertrlvs firrrirdpd daedilqdvf hefvqayrlp
       61 apieqvsawl fraarnrivd rfrkkkeqpl tdlfeaedea nseyrldlal pahdagpeal
      121 yvrtlvlkal qdaldelpan qrevfvahel dgrsfkemaa qsgvalntll arkryavlhl
      181 rarlqriyde ldnt
//
LOCUS       WP_175944521             247 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: (Fe-S)-binding protein [unclassified Caballeronia].
ACCESSION   WP_175944521
VERSION     WP_175944521.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..247
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27104
     Region          <2..242
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mkvalfvpcf idafypqigi atlellerlg ldvdypqdqt ccgqpmansg ahadaagaer
       61 vfarnfadyd yvvgpsasct hhvrehftai eqtsavqkvr kstyelvefl hdvlqvrdfp
      121 waefphrvgl hnscsavrhl retsnsevag tpyskprall ervkgiefvs parpdeccgf
      181 ggtfsvteea vsvrmgqdkv rdhigagaey ivsgdmsclm hqqgcaermk ldakfihiaq
      241 vlngara
//
LOCUS       WP_175944476             442 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175944476
VERSION     WP_175944476.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..442
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45935
     Region          17..420
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mlihhvepsl rdltaaerra payawlvfgl tvglllsdym srqvlnavfp llkhawnlsd
       61 tqlgslsgvv allvglltfp lsvladrfgr vrsivlmaal wsvatlgcal stnyaemlva
      121 rglvglgeaa ygsvgvalil sifparlrat ltgafmagga fgsvfgmalg glvgahlgwr
      181 wsfgvmaalg ivllvayrca vterrlaayr vepcrcdada prdmrgsara lmsglfasrs
      241 vicaylgsgl hlfvpgalfa wlpsylnryy amapdraavl aagfvllagv gmvgcgivtd
      301 rvghadgsrk wltaiaycvl tgvclavafr lppgplqlal icagmlvgag asgasgamva
      361 nltpaaihas afatltlann llgmapgpll tgwvadragl vgalqwipvv plaaavlfai
      421 grasyaadlv rvererratp ls
//
LOCUS       WP_175944534             707 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ATP-dependent helicase [unclassified Caballeronia].
ACCESSION   WP_175944534
VERSION     WP_175944534.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..707
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77792
     Region          20..668
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mltlpddtat adassenvaa ylaklndaqr ravefgvdap grcggpllvi agagsgktnt
       61 lahrvahllv kgadphrill ltfsrraale mtrrvtriat nalgsksaia qgltwsgtfh
      121 gigarllrdy adlvglapsf tindredsad lmnlvrhelg lsskekrfpa kstcfaiysr
      181 vvntgaslat vldqaypwcr eweadlkrlf aayvsakqaq svldyddlll ywshlaaeps
      241 iaadlssrfd hvlvdeyqdt nrlqatilla mkpdgrgltv vgddaqsiys frgatvrnil
      301 dfpqhfdppa atvtldrnyr stqpileasn aviglatery tkdlwtdkas aqrprvvsva
      361 deadqaryvv ekvleareag mklksqavlf raahhsatle ieltrrnipf vkfgglkfld
      421 svhvkdvlav lrwaenprdr vagfrvaqll pgigpaiagr lldsvaqaer aptaiaafga
      481 parasedwpr fvalmgklcg respwpaefe mirrwyephl ernhedaair igdvlqmesi
      541 astyptrerf lteltldppd atsdesgvpl idedylilst ihsakgqewr nvfvlngvdg
      601 cipsdmgtgs deeideerrl lyvamtrake dlhivtpqrf yvhnqtnlgd rhvwaqrtrf
      661 ipphlmqhfe agawppvpva aaptaaglaa aakakidiaa rlkgmwe
//
LOCUS       WP_175944539             344 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia pyrrocinia].
ACCESSION   WP_175944539
VERSION     WP_175944539.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..344
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37423
     Region          180..323
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mlaevrpdgf tmpdtcrlaf adglfaardg teirvaqgdg igaqllraql addgalrlva
       61 ynhratpadq rrallaalsa afsdgahhaa irldpaawpa valnalrasg vladggrcmr
      121 dgwaqqadlw lvgthlrcat lpmltdgrrh prrpraprge vyardlpals vrftlrgwqp
      181 aedagrlarw fdeprvrngw pgaqpgadgt qgaapdadph vtplvgcfdg epfayfeavw
      241 lkedalaphv aacdydrglr mlvgesrwrg phcvagwlps vvhylflddp rteavgcavp
      301 agharvadhl arhgfarqrr laladaqplw mrtlretffs grhv
//
LOCUS       WP_175944551             171 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [unclassified Caballeronia].
ACCESSION   WP_175944551
VERSION     WP_175944551.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..171
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18414
     Region          14..148
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mttptppaal ragraettfr flaepisvnf ggkvhggalm kwidetayac aamwsgryav
       61 tvsvgnirfr rpilvgnlve lrarvvltgr tsmhihvsvh agdpkvgele qttdclmvfv
      121 avdekgqptp vpafvpesee ekrlakyamd vkdaldaive lkpeevaagk v
//
LOCUS       WP_175944554             282 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia pyrrocinia].
ACCESSION   WP_175944554
VERSION     WP_175944554.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..282
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29736
     Region          7..260
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtrsaaalaa rgltvgyrdh vvidgldlsi aagrvtalcg pngcgkstll rtlaglqpar
       61 aghvdvdgkp lasfrrrala reltmlaqfn qipsgltvre lvaygryayg gflrglsrad
      121 haaidealet sgladdagrd vgalsggerq rawiamalaq qapivlldep ttyldihhql
      181 dildalraln rargltivwv lhdlnqaaay sdeivlmrag rvvaqgspda mldparlraa
      241 fgvemlklah pqtgapmcvp aygpssadmp qaagvfdrdl av
//
LOCUS       WP_175944598             249 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Caballeronia sp. BCC1704].
ACCESSION   WP_175944598
VERSION     WP_175944598.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26506
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkilvpvkrv vdynvkvrvk sdntgvelan vkmsmnpfde iaveeavrlk eagvatevia
       61 vscgvtqcqe tlrtalaiga drailvetse elqplavakl lkalvdqekp elvilgkqai
      121 dddsnqtgqm laalaglpqa tfaskvviad gratvsrevd ggaetlslkl pavvttdlrl
      181 nepryvtlpn imkakkkplt tvtpadlgvd vaprlktlkv teppkrsagv tvpdvktlve
      241 klkteakvi
//
LOCUS       WP_175944655             447 aa            linear   BCT 11-JAN-2025
DEFINITION  CpaF family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175944655
VERSION     WP_175944655.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..447
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49114
     Region          44..406
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mahdiqfadg aapfsqtqqf hdiknaaheh lltrieelga efgrwsrqai nqfvdleids
       61 fvrlrripln enevraiaea ltkelagfgp iedlladpav edilingynd vyvsrhgila
      121 klpvrftdna hllrivrril apigrrldes npmvdarlpd ggrvnvviep lsidgpvvsi
      181 rkfrkdplkp sdllangtfn eeidtllqaa vearcnilvs ggtssgktsl lnalafhipe
      241 iervvtiedt aelslnhphv vrlesrpggf dgtgivsird llrntlrmrp driivgevrg
      301 gevlemlqam ntghdgsmgt vhassprecl yrlemlagfa gfqgtesslr rqianaidfi
      361 vqigrlsngr rrilsitevt glsdniiamq elyryearvt pegeevdhwe tlgihphspk
      421 larfrqtlts ggfggggfgr ggggfnv
//
LOCUS       WP_175944670             585 aa            linear   BCT 11-JAN-2025
DEFINITION  cation:proton antiporter [Caballeronia sp. BCC1704].
ACCESSION   WP_175944670
VERSION     WP_175944670.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 585)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 585)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008671
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..585
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=62289
     Region          3..536
                     /region_name="RosB"
                     /note="Predicted Kef-type K+ transport protein, K+/H+
                     antiporter domain [Inorganic ion transport and
                     metabolism]; COG4651"
                     /db_xref="CDD:443689"
ORIGIN      
        1 mhhaigfiqd lavlmaiagv vtvlfhrlrq pvvlgyivag viigpytppf qlindeatiq
       61 tlgelgvvfl mfslglefsl rklfrvgata fvaalseivl miwigyeigr wfgwsamdsl
      121 flgamlaiss ttiivkalse lglkgegfaq lvfgilived ilaiamlvll sgiaqtgavs
      181 agmaavtlgk lllfmtvslv vgivvvpral dyvarsrsde mllvtvlgfc fgfcllvvkl
      241 dysialgafl igaimaeskh lariehliap vrdmfsaiff vtiglllnps vlvdyawpia
      301 vitvavvlgk ivscglgsfl agkdgrtamr vgmsvaqige fsfiiaslgl slkvtssfly
      361 piavavsalt tlltpylmra adpltlrlar ampaplaqtf gaysqwlasl apasegatlv
      421 amtrrivlqi avnlalvaai flgasyaapf asshlarwle tdnaqrvvlw saalvialpf
      481 lvavyrkles lalllaevsv qpakagrfth airsavsgli pvvamfgvfl lvaalsggil
      541 ppfglmlgvl lcvallltvl wrwcvkihat mqialretlq eprdh
//
LOCUS       WP_175944690             312 aa            linear   BCT 11-JAN-2025
DEFINITION  LOG family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175944690
VERSION     WP_175944690.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Naseem,M., Bencurova,E. and Dandekar,T.
  TITLE     The Cytokinin-Activating LOG-Family Proteins Are Not Lysine
            Decarboxylases
  JOURNAL   Trends Biochem Sci 43 (4), 232-236 (2018)
   PUBMED   29525484
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..312
                     /product="LOG family protein"
                     /EC_number="3.2.2.-"
                     /GO_function="GO:0016799 - hydrolase activity, hydrolyzing
                     N-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0009691 - cytokinin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35373
     Region          123..289
                     /region_name="PpnN"
                     /note="Nucleotide monophosphate nucleosidase PpnN/YdgH,
                     Lonely Guy (LOG) family [Nucleotide transport and
                     metabolism]; COG1611"
                     /db_xref="CDD:441219"
ORIGIN      
        1 msvvkptavr arqrrarpsr alsrpmrrra etanciqade dttllkrpgm rgirlqldyw
       61 kaeerlqqer ightiviygs trivapaean arlreasral aerphdarrr ravstasrlv
      121 kysvyyrvar efgrivgrad rrartarlav itgggpgime aanrgayerg apsiglniel
      181 preqapnpyl tpalcfrfhy fairklhlle rakaavffpg gygtcdelfe vltllqtrki
      241 aplpvilvge aywrrvvdfa fladdgmidr sdldlfvyce sapdiwhaig cwyaqrrsqp
      301 prrvtsranr am
//
LOCUS       WP_175944694             157 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia pyrrocinia].
ACCESSION   WP_175944694
VERSION     WP_175944694.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..157
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16906
     Region          1..144
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mytnimvald gsvssrqald eglkmarlyq arlfavfvvd ksillsyagr idpnalieev
       61 rhdgvtvlrd aeraiaragv ngeteivete lgqdvaerlq rhvadhaidl avlgthgrrg
      121 irrvmlgsva erflrtsscp vllvrgddat raaaaaa
//
LOCUS       WP_175944773             311 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175944773
VERSION     WP_175944773.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..311
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34063
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..294
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdkldqvrif lqvaemgsfi kaahaldlpr atvsaavqql eaglgtrllh rttrqvqlta
       61 dgvlllergr rllaeaddld rlfrrrdrdv vgrlnvdvps riarrmiapa lpslfrrypk
      121 lqlslgstdr sidlvqegvd cairvgrlad sslvvrplgq ftlincaspg ylrecgvpeh
      181 pdalahghwa igyaspttgr elgweycvdg erhtltlpsr vivnnaetyi agciagmgli
      241 qiprfdvehl ldsgalvdvm pghraepmdv savyphrrhr srrlnafvdw fgelmadalt
      301 gaaagkgaeg d
//
LOCUS       WP_175944815             322 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Caballeronia].
ACCESSION   WP_175944815
VERSION     WP_175944815.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..322
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=36135
     Region          12..69
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          100..301
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(115..116,118..119,122,126,128..134,227..232,
                     238..239,241..242)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176152"
ORIGIN      
        1 mnepadsldi wlirvlrtll lersvtqtaq rlnqtqpais talrrlreil ndpilvrgkq
       61 gmvpteyget llapaqralr evefvatphg dfdpahsrrt frlaapdyln dffmptlvaa
      121 frdaapharl eieslnpmrd heraldegei dlmvanwtkp eprferqdlf sdvfvclmra
      181 nhplareplt veryalaahl aptpysgakr hpidiglara girrrivtti pyfglvpqvl
      241 lqsdliftap rrfaqhyaam lplavldspv pfprikcyrl sqpqsdqstd vawlcalmsr
      301 vsdsligrkt apvhesaaav ak
//
LOCUS       WP_175944817             305 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [unclassified
            Caballeronia].
ACCESSION   WP_175944817
VERSION     WP_175944817.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 305)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 305)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 305)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401353
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..305
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32191
     Region          2..116
                     /region_name="cupin_YkgD-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to Escherichia coli YkgD, N-terminal cupin domain;
                     cd06995"
                     /db_xref="CDD:380399"
     Region          215..298
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdaldrliql aqlsgaldlr cllrgplevd hapapageaa yhvvldgact varkghapid
       61 lkagdilflp rgdahvlhva ggdtrggdmq trdngavtvr sncgeaqpav dllcgrftya
      121 prallidvlp davhvsftra sapylgplva amrreaeeaq lgapsivaal stalfamvlr
      181 awlaeqpsls gvlallahrr lgasviamle rpadpwtldm lakeaamsra tfmrafsahs
      241 essplallgh vrmqlastml thtkksiadv aanvgyqsea afskrfkevy gvapgkfrae
      301 rgfga
//
LOCUS       WP_175944828             248 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [unclassified
            Caballeronia].
ACCESSION   WP_175944828
VERSION     WP_175944828.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..248
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27793
     Region          17..248
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mnsttedrwr dlrpdpdsdt plylqlarkl anaihdnrwn agealpserv lsealgvsri
       61 tsrkaiallv eqglirreqg agsfirprye dplsrlssfs emlrrrgfqp sskwlsrtie
      121 panreeviql glspaatvar lkrlrladdt vmavenstfp aalipdplai gdslysyldt
      181 rglsivralq hfravnaspe iaeqmgiaph dalllitrvg ytadqraiel tdtycrndyy
      241 dfvaelrk
//
LOCUS       WP_175944843             193 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: superoxide dismutase [unclassified Caballeronia].
ACCESSION   WP_175944843
VERSION     WP_175944843.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..193
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21497
     Region          4..190
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mehtlpplpf dknalaphms eetlefhygk hhqtyvtkln elikgtefen mqleeivkks
       61 sggvfnnaaq twnhtffwns lspngggapt galadainak ygsfdkfkee fakvavgtfg
      121 sgwtwlvkkt dgsldivsts naatplttds kplvtldvwe hayyidyrna rpkfieafwn
      181 ivnwdfaskn fga
//
LOCUS       WP_175944846             392 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia pyrrocinia].
ACCESSION   WP_175944846
VERSION     WP_175944846.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..392
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44632
     Region          7..390
                     /region_name="COG3146"
                     /note="Predicted N-acyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:442380"
ORIGIN      
        1 mkheridyrt gilsspaevp adewnallar daqptpflrh efldalhvsr cavddtgwsp
       61 hfvtltdagt grlvaaapvy akqhsygeyv fdwawadayq rnnlpyypkl lcavpftpvq
      121 gtrllaaddd arrrlaatll afaeqsdvss lhvlfptgde arllesmgmm lregvqfhwi
      181 ndgyrhfddf latleqkkrk niraerrkvh dagvtfrrlt gdrisdadwr ffsrcyrqty
      241 rehysspyln ldffrtigat mpenlllvia eadgqpiasa lavyrrgehg ggtlygrywg
      301 alehvpclhf etayyqllef cieagldtfe ggaqgehkla rgflptvths ahwlahpafs
      361 davarflere tehihayvde lrehdpfrrg ae
//
LOCUS       WP_175944902             165 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [unclassified Caballeronia].
ACCESSION   WP_175944902
VERSION     WP_175944902.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..165
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18403
     Region          5..144
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mtgftldatd crilavlqed grisnldlae rislspsacl rrmrlleeeg viasyracld
       61 rerlgielea fvhvsmrndq enwhekfaaa vrewpevvga fvvtgdthyv lrvlahnlkh
      121 ysdfiltkly kapgvidirs nivlqtmkdd agvpvalieq parga
//
LOCUS       WP_175944914             150 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175944914
VERSION     WP_175944914.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..150
                     /product="VOC family protein"
                     /calculated_mol_wt=16359
     Region          3..134
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(3..8,24,62..63,66,82..87,89,93,122,132)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 mqvqpyltfy gradealqfy ekalgattmf kmhfkdappn pehaitpema dkvmhasfti
       61 gdsmimcsdg dcsqpggtha gyslslnpat veegqklfna ladggevtmp fgktfwalgf
      121 gmakdrfgvh wmvnvedlsq redlakraqg
//
LOCUS       WP_175944938             519 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia pyrrocinia].
ACCESSION   WP_175944938
VERSION     WP_175944938.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..519
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56137
     Region          34..458
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msagpaglth dvpaapfern atmsdsvakp vdatfdqfgl aadilkaive qgyttptpiq
       61 aqaipvvlag rdvmgaaqtg tgktasfslp iiqrllpqan tsasparhpv raliltptre
      121 ladqvaanvh aygkhtplrs avvfggvdmn pqmaelrrgv eiliatpgrl ldhvqqktan
      181 lgqvqmlvld eadrmldmgf lpdlqrilnl lpkerqtllf satfspeikk lastylrnpq
      241 tievarsnst nanvtqivyd vaegdkqaav vqllrdrglk qvivfcnski gasrlarnle
      301 rdgvvasaih gdktqiermq aldafkrgei ealvatdvaa rgldivelpa vinfdlpfsa
      361 edyvhrigrt gragatgdal slcspnerkq ladieklikr plevqtlald kparhrqddr
      421 gsersgdrns erggerggrr erdehrgasg rrsagsersg hhrrheapld dfflkpyeps
      481 aaakqsddae paqqpekkgp krqvaallgg fgmprkpsa
//
LOCUS       WP_175944966             243 aa            linear   BCT 11-JAN-2025
DEFINITION  alanyl-tRNA editing protein [Burkholderia pyrrocinia].
ACCESSION   WP_175944966
VERSION     WP_175944966.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V.
  TITLE     Evolution of aminoacyl-tRNA synthetases--analysis of unique domain
            architectures and phylogenetic trees reveals a complex history of
            horizontal gene transfer events
  JOURNAL   Genome Res 9 (8), 689-710 (1999)
   PUBMED   10447505
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Cusack,S., Hartlein,M. and Leberman,R.
  TITLE     Sequence, structural and evolutionary relationships between class 2
            aminoacyl-tRNA synthetases
  JOURNAL   Nucleic Acids Res 19 (13), 3489-3498 (1991)
   PUBMED   1852601
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Schimmel,P.
  TITLE     Classes of aminoacyl-tRNA synthetases and the establishment of the
            genetic code
  JOURNAL   Trends Biochem Sci 16 (1), 1-3 (1991)
   PUBMED   2053131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..243
                     /product="alanyl-tRNA editing protein"
                     /GO_function="GO:0002161 - aminoacyl-tRNA editing activity
                     [Evidence IEA]"
                     /GO_function="GO:0002196 - Ser-tRNA(Ala) hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004813 - alanine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006419 - alanyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=26370
     Region          3..243
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
ORIGIN      
        1 mttqalfred ayltqcdaiv qavgddgirl drtvfyplgg gqagdtgtlt lpdgstiaia
       61 dtrkakfdga tpddavhvpa pgqearvaal vpgtrvvaai dwprryrhmr lhtaahlmca
      121 vlpyavdgcs vtadyvrldf atsdaidrdd verrlaglvv gahpvttewi tddemaerpe
      181 lvrtmsvkpp mglgrvrllr ieqvdlqpcg gthvrntsei gdlrvaklek ksartrrlvl
      241 efa
//
LOCUS       WP_175944848              68 aa            linear   BCT 11-JAN-2025
DEFINITION  Trm112 family protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175944848
VERSION     WP_175944848.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   van Tran,N., Muller,L., Ross,R.L., Lestini,R., Letoquart,J.,
            Ulryck,N., Limbach,P.A., de Crecy-Lagard,V., Cianferani,S. and
            Graille,M.
  TITLE     Evolutionary insights into Trm112-methyltransferase holoenzymes
            involved in translation between archaea and eukaryotes
  JOURNAL   Nucleic Acids Res 46 (16), 8483-8499 (2018)
   PUBMED   30010922
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Bourgeois,G., Letoquart,J., van Tran,N. and Graille,M.
  TITLE     Trm112, a Protein Activator of Methyltransferases Modifying Actors
            of the Eukaryotic Translational Apparatus
  JOURNAL   Biomolecules 7 (1), 7 (2017)
   PUBMED   28134793
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006712
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..68
                     /product="Trm112 family protein"
                     /calculated_mol_wt=7275
     Region          1..53
                     /region_name="Trm112"
                     /note="RNA methyltransferase activator Trm112/YbaR
                     [Translation, ribosomal structure and biogenesis];
                     COG2835"
                     /db_xref="CDD:442083"
ORIGIN      
        1 mdarlleilv cpickgplny draaqelvcn adklaypird gipvmlvdea rqtvegtpvt
       61 plkpvgdv
//
LOCUS       WP_175944991             256 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Caballeronia sp.
            BCC1704].
ACCESSION   WP_175944991
VERSION     WP_175944991.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..256
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=27165
     Region          9..250
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 msfshalvgs vgwltmdrpa amnslnrema tglteqlkaw rnddnvravv ltgngrafca
       61 gadlieaaap paegvrdfle liveffdtlr afpkpviaav nglalaggle ivlacdivla
      121 setaklgdah snfgvfpgag gaailprkvp vnvaryllft gdamsaaelk thglvnevla
      181 pselaaraqa ladklakksp lvlarmkrva neapdksaad alrhellelr dhqrsydvke
      241 glrafaekre pvfkgc
//
LOCUS       WP_175945010             796 aa            linear   BCT 11-JAN-2025
DEFINITION  LPS-assembly protein LptD [Caballeronia sp. BCC1704].
ACCESSION   WP_175945010
VERSION     WP_175945010.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..796
                     /product="LPS-assembly protein LptD"
                     /GO_process="GO:0015920 - lipopolysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87750
     Region          60..767
                     /region_name="LptD"
                     /note="LPS assembly outer membrane protein LptD (organic
                     solvent tolerance protein OstA) [Cell
                     wall/membrane/envelope biogenesis]; COG1452"
                     /db_xref="CDD:441061"
ORIGIN      
        1 mpprqfpask iqgdaqprrr rlvaallsvp glmpalahaq lagpaadaqp idgpdslrla
       61 pqlqerplks gqqpttfllg dkatgtsded maakgsaevr rtvtvikada lhydqdtdma
      121 dafghvrlin ngvsfvgpea hlkvdsnegf mtnpkyhfnl tggsgsaeri dlidnerarv
      181 dhgtytacqc dtnpawyikg ssfdfdtgse egiahngvlf fqgvpvfasp wlsfpltgdr
      241 rsgllpptfs lssttgfeat ipyyfniapn rdltvtprim srrgvlgean yrylsptysg
      301 sltvdylpnd rethtnryai fwqhrqnfgg gfggyvnynk vsddqypedl gnasnqflng
      361 tqllyqqeag ltynngpwsv lareqrwqtl qpsippyare pqlnvqynky nvggfdygae
      421 adftrftitq egatdgqrmy lnpyvsygin apgyfftpkv qwhfasydls hiatgpipgq
      481 pltpagqpkn ftesiptvsl dtglvfdrsv rlfgqdyiqt leprlyyvyt pyrnqnfapi
      541 fdtaeadfgl aeiytpntfv gndriadanr ltaglttrfi npatgderar fviaqqyyft
      601 sqrvtisqdq pineakhsdl iagaaiklga gfasetafqy nvdnnqlvrt svgfafspad
      661 rkvinvgyry trsnqttlvn epinqllvsg ewpltnrlya varvnydlag hrlvdglvgf
      721 qydadcwalg fgaqryangv ntsgqpssgt rvlaqitfkg lskvdnglvs afrasvqgyq
      781 ppppsappla rfsdye
//
LOCUS       WP_175945034             279 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Caballeronia sp.
            BCC1704].
ACCESSION   WP_175945034
VERSION     WP_175945034.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..279
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29276
     Region          1..277
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mllsqveamr eqlrpserkl adyvleapre vldlsmtdfa aragvsqpti arfcqalgfs
       61 gfrefkirla qsvaadvptv yrdvrsdepa agvaakvldr tigaliavrn slssdsvaaa
      121 iailsearri efygaggsgi aaldmqhkff rlgvpsvaya dphtyttsaa llgpgdvvva
      181 isntgrtkdi ldacksalng gakviaithg nsplarlasv glfanvdedt difspmtsrv
      241 shlaigdila vglalargpq laeklaeakd vlegrrvgt
//
LOCUS       WP_175945043             315 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175945043
VERSION     WP_175945043.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..315
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33900
     Region          5..314
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpkvvgifav pgvqlldvfa qanaeygkpf ytlrivases gpircssgar llpdwivpdi
       61 peridtllva gapsagqitl rtdvlawlrs aavqskrygs ictgafilaa tgllkgrhlt
      121 thwaaadala eaypslavda dalyvrdgkl rtgagvtagl dlalalveed lgreiarrva
      181 aqlvmffkrp ggqlqfsrkg earpagrsvl qevqrwiaan pelehsvael akhagmsprh
      241 farlfrtevg mtpaawveat risaarhlle nghdtpkqva akcgfanvdt lrrsfarhvg
      301 itpaeyrkrq avlae
//
LOCUS       WP_175945055             342 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia pyrrocinia].
ACCESSION   WP_175945055
VERSION     WP_175945055.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..342
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37522
     Region          69..298
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 makdtskdkk ptgnlhlaag llrglaqena aletrlpepp aapnvvdaap avppaaaapa
       61 gisdlgapqk vlvkdcipnp fnprvfyses slhelaltlk regqiepikv trlpefpgkl
      121 vvidgqrrlr atsingdeti natfrtdhtp eqlytiayra nhdherqtif ddavawkrll
      181 dekvfpdqnt laekigkdka sisktlslna lpntllerma sandvvglqa ayflklifer
      241 lgeltadrll tavidrkksv rdlenflraq sddnkkagrt rysvrhdfal esraigqlkt
      301 ypdgrldlql kgvdtshqea ladklktvid ayvaelaavt qk
//
LOCUS       WP_175945102             268 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)H-dependent oxidoreductase [Burkholderia
            cepacia complex].
ACCESSION   WP_175945102
VERSION     WP_175945102.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..268
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=30006
     Region          2..212
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mkvlivfahp epksfngalk dkavatltal ghevrvsdly qmkwrpdlgl ddftgpranp
       61 dyldlsaeqe hmfvtskptp dvaaeqekvl wsdliifqyp mwwfgmpail kgwvdrvmtr
      121 gfayatgrky dtgmfkgrka mistttgtas slyepdgvdg dinhllwpih ngifkylgfd
      181 vlpphvswmp arvsaeeraa ylasyeerlr tleqtpplff hpfadygtdq rlkpgviars
      241 gfqwnpgagq sreeaadqft apnaakfg
//
LOCUS       WP_175945117             312 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: carbohydrate kinase family protein [unclassified
            Caballeronia].
ACCESSION   WP_175945117
VERSION     WP_175945117.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..312
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33697
     Region          4..290
                     /region_name="ribokinase_group_A"
                     /note="Ribokinase-like subgroup A. Found in bacteria and
                     archaea, this subgroup is part of the ribokinase/pfkB
                     superfamily. Its oligomerization state is unknown at this
                     time; cd01942"
                     /db_xref="CDD:238917"
     Site            order(52,250,253)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238917"
     Site            order(192,220,248,251..252,255,277,280)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238917"
ORIGIN      
        1 matlicgsla ydnimtfqgr fgdhilpdqv hmlnisflvp tmrrnfggca gniayalkll
       61 ggdakimatl geadaqlyid rldalglske yvrvlpgqhs aqcfittdla nnqitafhpg
      121 ammeshlnra deaqgitlgi vapdgadgmr ehakqfavag vpfifdpgqg lpilegvelc
      181 rmielatyvt vndyeaklls nktgwsiedi ksrvealvvt rgehgaqiyh edgvmdvpav
      241 karqvvdptg cgdafrggll ygienklgwe ktgrlaslmg alkiehqgpq tyaptraeie
      301 erfkqafgss ls
//
LOCUS       WP_175945133             249 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Burkholderia pyrrocinia].
ACCESSION   WP_175945133
VERSION     WP_175945133.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26381
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkilvpvkrv vdynvkvrvk sdntgvdian vkmsmnpfde iaveeavrlk eagaatevia
       61 vsvgvaqaqe tlrtalaiga drailvestd sveplavaki lkalvdkeqp qlvilgkqai
      121 dddsnqtgqm laalaglpqa tfaskvtvad gkatvarevd ggaetlsltl pavittdlrl
      181 nepryvtlpn imkakkkple tvkpedlgvd vaprlktlkv veppkraagv kvpdvktlve
      241 klkteakvl
//
LOCUS       WP_175945153             399 aa            linear   BCT 11-JAN-2025
DEFINITION  GspE/PulE family protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175945153
VERSION     WP_175945153.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..399
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=42636
     Region          <26..392
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mnsappaafp rpadstfeat sdghlpavsl ladtlreaae rgasdihvep sehewrirlr
       61 vdgalhvlrr ppphlrdafv trikvlarmd iaerrvpqdg rlrlalpggq tgdyrvsslp
      121 tlfgeklvlr rldalprdls lgalglsdeq srvvesaira phglvlvtgp tgsgktlsly
      181 cflqmlnaea rnicavedpa eiqlaginqv svrekagltf avalrafmrq dpdvimvgei
      241 rdaetadvav kaaqtghlvl stlhtndapa aiarlidigv apynlasalr lvtaqrlvrk
      301 lcdacrapsa ltlpdgfrpf eprgcpachg igyrgrvgvh qlmpvsdgir elivgraath
      361 avarlaqseg mpalrdaafa rvregvtsva eaadateia
//
LOCUS       WP_175945200             315 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: dihydrodipicolinate synthase family protein
            [Burkholderia].
ACCESSION   WP_175945200
VERSION     WP_175945200.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..315
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=34315
     Region          11..>243
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mqhqqqssvt iegivpvmlt pfddagaidy aglerliewy lahgsdalfa vaqssemqfl
       61 slaeraelar fvvervagrv pvvasghisd dldaqvaelc aaaesgaqgv vlvtnrldpq
      121 rqgsaalldh lhkllarlps dlplglyecp apyrrllsdd elracidtgr fvmlkdvscd
      181 letvkrrval aagsplkiln anaaiawdam kagsagfngv ftnfhpdlyr wlrtqgdtnp
      241 aladelstfl vvsavsevlg ypalaklyhq rigtfgsikc raidydvrer fwaldavldk
      301 ivagtehfrr riaaq
//
LOCUS       WP_175945198             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175945198
VERSION     WP_175945198.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46111
     Region          22..420
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,150,
                     153..154,157,245,248..249,252..254,257,285,289,347..348,
                     352,356,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 msenqsvpha pprirrgqri alallmasgi vnyldrgtla vassairgdl glslsqmgll
       61 lsafswsyal cqfpvgglvd rigprrllgi glivwsfaqa aggivstfgw fivarialgi
      121 geapqfpsaa rvvsnwfplr argtptgifn aasplgtala plllsilvas fdwrwafiat
      181 galglavavv wfalyrdplr aqltaeergy ldadaksvva apkltfaewr slfshgttwg
      241 mligffgsvy lnwvyltwlp gyltmerhms lirtgfaasv pflcgfvgsl vagwlsdvvt
      301 rrsrspvvsr rnavvvamlg mvaftipaal vqsnavalac isvviflana asasswalat
      361 aaappnrvas lgaiqnfggf iggalapilt giiaqkwsfv palltaaaia fagamaylll
      421 vrkpipeqaa naasgplpa
//
LOCUS       WP_175945215             429 aa            linear   BCT 11-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Burkholderia
            pyrrocinia].
ACCESSION   WP_175945215
VERSION     WP_175945215.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..429
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=45197
     Region          1..405
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mknrltlyil agmvlgvavg yvchrsvaga aeakaiagyf siitdiflrl vkmiiaplvf
       61 atlvsglagm egtsdvrrig frsvgwfvca slfslalglv lanalqpgag lhmtqtsadv
      121 atglntagln fkdfvthafp ssiidamarn dilqilvfsv lfgvvlsaik kdprvtplia
      181 gidalvpaml kltdyvmrla pvgvfgalas aitvngldvl ttygklvgsf ylglvllwia
      241 livvghvflg ksiwkllrav repamlafst asseaayprl tekleafgid kkvvgftlpl
      301 gyafnldgsm myqafaaifi aqafgidmpv gtqimmllvl mlsskgmagv argsvvvvaa
      361 vapmfhlpps gvvlilaidq ildmgrtatn vignsistav iakwelkrla kqedgansva
      421 laqlqgetk
//
LOCUS       WP_175945259             286 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            pyrrocinia].
ACCESSION   WP_175945259
VERSION     WP_175945259.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 286)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..286
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30187
     Region          1..286
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mnvyllqivn gigvgmlyfl lavglsivfg llrfvnfahg afyllgaylc yqalqwsanf
       61 wvalavvplv vgafawgvek lvlrhvyaqq hefhilatvg lalvlqecai lawgplgdnv
      121 pppdalngvv iwggfvypky rlfvigftav laamlwwvle gtrlgstvra gsestemvsl
      181 lginvtrvfs lvfalgaata alagvlaapi rgvdpfmgie algvafvvvv vggmgnfiga
      241 lvggllvgiv qslmstlwpe garlmiyvam aavlllrpng llgraa
//
LOCUS       WP_175945286             214 aa            linear   BCT 11-JAN-2025
DEFINITION  HD domain-containing protein [Burkholderia pyrrocinia].
ACCESSION   WP_175945286
VERSION     WP_175945286.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..214
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23109
     Region          23..214
                     /region_name="RnaY"
                     /note="HD superfamily phosphodieaserase, includes HD
                     domain of RNase Y [Translation, ribosomal structure and
                     biogenesis, General function prediction only]; COG1418"
                     /db_xref="CDD:441028"
ORIGIN      
        1 mttpafapfq dlaeallahw ssangdgshd tshlqrvwkn aaaihaeegg daevlfaatl
       61 lhdcvavekn splraqasrl saekatqvlk sldwpdakid avahaveahs fsagvapttl
      121 eaktlqdadr ldaigmlgva rcfyvagrmg salydpvdph aserelddtr faidhfhtkl
      181 lklasgfqta tgarlakirh drlrrfldef adei
//
LOCUS       WP_175945287             291 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: hydroxymethylpyrimidine/phosphomethylpyrimidine
            kinase [unclassified Caballeronia].
ACCESSION   WP_175945287
VERSION     WP_175945287.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..291
                     /product="hydroxymethylpyrimidine/phosphomethylpyrimidine
                     kinase"
                     /EC_number="2.7.1.49"
                     /EC_number="2.7.4.7"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008902 - hydroxymethylpyrimidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008972 - phosphomethylpyrimidine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009228 - thiamine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009229 - thiamine diphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=30672
     Region          8..248
                     /region_name="HMPP_kinase"
                     /note="4-amino-5-hydroxymethyl-2-methyl-pyrimidine
                     phosphate kinase (HMPP-kinase) catalyzes two consecutive
                     phosphorylation steps in the thiamine phosphate
                     biosynthesis pathway, leading to the synthesis of vitamin
                     B1. The first step is the phosphorylation of...; cd01169"
                     /db_xref="CDD:238574"
     Site            order(8,15,17..18,20,24,27..28,31,34..39,41,44..48,53..54,
                     56,58..59,62,65,69..70)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238574"
     Site            order(14,26,47,83,214)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238574"
     Site            order(108,142,181,211,213)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238574"
ORIGIN      
        1 mtgdsppivl tfglsdptgg sglqadlltl asmgchsatv ltgyavrdsa tcdevngldp
       61 davaaqarml ledmpiaafk igaatraevv saiaevvsdy ddvplilapd ftlddehvls
      121 adelreslad llvpqttmli adhatllqla qpdsdaeapt ldsaishila qgceyvlame
      181 tgthrhvntl yseegqvrqd lwdrglhrvm gltdtlgaav aallangqep aeaareaqey
      241 vfqaaraafr pgmgaylpdr ffwarsndad detdaaslpd dsaglpgear h
//
LOCUS       WP_175945295             174 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: methylated-DNA--[protein]-cysteine
            S-methyltransferase [unclassified Caballeronia].
ACCESSION   WP_175945295
VERSION     WP_175945295.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..174
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18718
     Region          22..174
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mlseggfiav eptapptrqf davidapfgk vgiraddrav reivylpahv enieahaplv
       61 qeaayqirry fetpsmrfdl plalggtafq qrvwrgisgi garqvwtygq lareigsvpr
      121 avgqacgsnp lpivipchrv vaaggiggfa hhpgdgffrd vkrwllaheg vsia
//
LOCUS       WP_175945296             210 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia pyrrocinia].
ACCESSION   WP_175945296
VERSION     WP_175945296.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..210
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22992
     Region          1..209
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mtrvlyiegs pnkaysasie vcnafldayr hahpdheirk ldvwdlampe fdgaalaaky
       61 aglngtaltp eqaatwqqie qlaapfhead kflfgvplwn fsipyklkhl idaisqkdvl
      121 ftfdgsgfag klagkkaavv yarglsyesp gsltpaaefd lqrpyvetwl kfvgvkdiag
      181 lvvertlfgp dgnvdrsrai dearaiaraf
//
LOCUS       WP_175945308             350 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia pyrrocinia].
ACCESSION   WP_175945308
VERSION     WP_175945308.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..350
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=37809
     Region          <54..>169
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(72,74,78..79,82,85..86,88..89,93,102,104,106,
                     110..111,114..116,118..119,123,126,135,137,139,143..144,
                     147..148,150,152..153,163,166)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          72..102
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          104..135
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          137..172
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mpkakkkllp kdfealldeg dlaklqavfd tcdvnarggv skrtalsfdr cpddlarwlv
       61 aqgadvgaad aygntaphvr arsrrgrfdv llelgadvhd dgasvgtalh aaadsrnaqs
      121 arvlldhgar vdalnrdgqt pleralrtcg nadleymval aevllgagaa rtpsmqtsvt
      181 eigerfefmr erfnpesvda asaalerlyt lfdvppvprr qlhdarspiv vaagtwqaqh
      241 qalwtqlvpg aghaatvqge lirisgriay eldhnggcnw dadfrkmada faavvrtgtp
      301 lpsadlsdve avvhdikrqs gdpaqlcrfa vawvrlnpdp vklepppyrr
//
LOCUS       WP_175945320             309 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175945320
VERSION     WP_175945320.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33796
     Region          13..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(105,109,148,162,164,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(106..107,111..112,114..115,118,122,124..130,191,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 msrlpdfegf amfakvaeeg sfaaaatamg vsvatvsrav trleerlggr lfnrtsrrla
       61 ltdyghtlie raaklytdae etedfareas srprglvkla aplsfgarwv apllpeffgl
      121 ypdiavdlhl tdtqsdlige gfdaalriai ledsslvarl iapvrrfvva spaylsrhgr
      181 prhpqalgah pcltyanrsq rdvwrftrhd getcavtpgg mlrgtsveal lptvlaglai
      241 telpefvatq yfadkrlepi ltdwrlpegg lyfvtpsara rpakvsalad ffiaklatae
      301 wrapvkrsr
//
LOCUS       WP_175945335            1076 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia pyrrocinia].
ACCESSION   WP_175945335
VERSION     WP_175945335.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..1076
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113638
     Region          1..1056
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mwivrlalrr pytfvvlall ifiagplall rtptdifpni dipvvsivws yngfsaedma
       61 kritsnyera ltsdvdnieh iesqslngvs vvkiffhpga dinraiaeaa snsasilril
      121 ppgtlppnii tynastvpil qlglssdtla eqqlydlgns firtqlatvq gaavplpfgg
      181 kirqivvdld tralqakgla pidvvnaina qnlilpggta kigtreynvq mngstqtvaa
      241 lnnlpvktig gsvvyvrdva hvrdgyapqt nivradgkra alltvektgs astltiidqv
      301 kamlpkiaag lpkalhisal gdqsvfvkaa irgvvreali aacltalmil lflgswratl
      361 iiavsiplav ltsllalaal gqtinimtlg glalavgilv ddatvaieni thhlergapl
      421 edailtgage iavptfvstl sicivfvpmf lltgvarylf vpmaeavifa mvasyffsrt
      481 lvptlamalm rakghgrppr gvfariarfq aafehrfeav rlryrallsa aiarrrrfaa
      541 afllacaast glfafagqdf fpsvdtgeir lhlraptgtr ieetarltde vearihdvip
      601 andiasvldn igvpvsginl tydssdpigt adadvmitlk pnhaptaayv aklrnllvqs
      661 fpgvtfaflp adivsqilnf glpapidiqi vgnkldqnra vanallaklr gvrglvdari
      721 qqpgdepain vnvdrtkaiq agleqrdvaq nllialsgss qttpnfwldp rngvsyplmv
      781 qspqysvdsl qalanvplpa gtarspqtpa ggpaagapaq nllgslgsfs ratqqavvsh
      841 ynvqpvldif asaqgrdlgs vtadvtqlvd aaraqlppgs sivlrgqvqa mhesfagllg
      901 glalaivlvy llmvvnfqsw ldplvivggl paslagiawm lfvtrttlsv paltgtilci
      961 giatansilv vnaareliag gappwqaald agfsrfrpvv mtalamligm lpmalglgdg
     1021 geqnaplgra vigglafgtl stllfvpvvf gfvhawldrr rdaaaarraq dtpalp
//
LOCUS       WP_175945345             201 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia pyrrocinia].
ACCESSION   WP_175945345
VERSION     WP_175945345.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..201
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20715
     Region          1..185
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mkllhvdssi lgqgsvsrel seeavatfrg rdpgltvtrl dlaatpighl taehlaaaqg
       61 apiddalkad veigqralde flaadivvvg apmynfgias qlkawidris vagktfryge
      121 ngpvglcvgk kvvvassrgg vysegspvaa fdhqetylka afgflgvtdi tfiraegvam
      181 gqdmrsgaia sakeaaaala a
//
LOCUS       WP_175945359             351 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [unclassified Caballeronia].
ACCESSION   WP_175945359
VERSION     WP_175945359.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..351
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37279
     Region          37..350
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msesirgaas etvpqavsnv aprvrkgsly aqlmrkpewf tvglilvtcl ivgslnprff
       61 qfatlfdmlh sattvslfal gtlvvlasgg idvsftaiaa ltmysitkav fawwpecpfa
      121 livltgalgg vllgvvngml vhrlkapsli vtigtqylfr gllltfvgtq ffmniphsmd
      181 vfgrlplfyy htadglravl pvsvlalvia aivtwwllnr tmmgrgvyam ggslaiaerl
      241 gynlraihlf vfgytgllag vagilhvstn rlanpfdlvg teldviaavi lggaritggt
      301 gtvtgtllgv vlvtlinsvl ilvgvpstwq kviigafili agtlfalgrr q
//
LOCUS       WP_175945371             133 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator [Caballeronia sp. BCC1704].
ACCESSION   WP_175945371
VERSION     WP_175945371.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..133
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=14700
     Region          6..124
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mkdenrtrhv livddevaia yvfqryfelr gfrvsaaydg naalaigqse sidalvtdfr
       61 mpgmngqeli erlrqtvphl paiivsgfgg eigerpagvr vigkpvepty lvecvkemla
      121 dadtvqwlnr pkd
//
LOCUS       WP_175945386             286 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia pyrrocinia].
ACCESSION   WP_175945386
VERSION     WP_175945386.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15202679
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..286
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30548
     Region          12..132
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          <182..266
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 madlnssrtl tyrpfaesdl paahrlsqaf nwphrvddwr fvlqlgsgfv aeddtgvvgt
       61 algwrfgesh aslgmvivsp ehhgrgigre llarivdgfg srtvflhatp ageplyakfg
      121 fhaigtidqh qgtvfqppli slppgerlrp lgtndgprla alasraagyp rdavtdalld
      181 vangialdrd gellgfalfr rfgrghaigp viapdalraq alishwlalh egmfvrldap
      241 gdsgltdwlq glglprvdtv vamvrgdapa rdpalrafai vnqalg
//
LOCUS       WP_175945409             300 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia pyrrocinia].
ACCESSION   WP_175945409
VERSION     WP_175945409.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15202679
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..300
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31995
     Region          19..134
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          166..278
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 mkqehvmnds rsttalrhrr ftaadlpaah alstalrwpf rledwqfsad tsvafaaeen
       61 gavigtamcw kfgadrasig hvivssahqg rgigralmet lleelgprit flhatpagqp
      121 lyeklgfdvc gsldqfqgnv srpaavvlpd garlragtpa dlrrlvelda casglerdal
      181 lsalltrgas vvlerdgeia gfsvlrrfgr gyligpvvap rstgdtcara liahwlggle
      241 nefvridvps gtslpdwldm qglkrvdtcs kmvrnapaaa cggaldpayg lyglvsqaml
//
LOCUS       WP_175945442             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Caballeronia sp. BCC1704].
ACCESSION   WP_175945442
VERSION     WP_175945442.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33344
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mesfnflesf vvtaqtgsfs aaarrlgmtp agvsknvarl eqqlglrlfh rstrsltltd
       61 sgesfyqevr apfdalrdav shaaeqngap sgtlkvsvgv gfgreylvpi lgefldrypa
      121 ivpdvhfdnr pvdligegyd aaigggieln egvvarelap ahvivvtspa ymadkpmpah
      181 pseleafdgi arrsvssgrv fawklrnavg eqclvrhrtr lifddpeama aaamqglgia
      241 lipmphaarw iqqgslirll pgwfaelgai slyypskkll ppktrvfvdf vvdafrsgri
      301 narldsr
//
LOCUS       WP_175945439             401 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Burkholderia
            pyrrocinia].
ACCESSION   WP_175945439
VERSION     WP_175945439.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..401
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43495
     Region          1..400
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(99..101,125,175,207,236,238..239,247)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(102,135,200,245..247,276,279)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            239
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mniiadrigq iapaetmama araaelrrag rdvislsqge pdfqtpeniq eaairamrsg
       61 ktryteaagi pelrdaiaak laidnaliyp vagisvssga kqaifaaffa slnvgdeviv
      121 ptpcwvsype ivkmsggtpv cvpcpetagf kltpeqleaa itprtkwlml nspsnptgav
      181 ysrdelasla evlrrhphvw vlsddiyekl iytdtpfnni vnvapdlyer tlvingvskv
      241 yamtgwrigy aagptqlika mnlvqgqivt satsiaqyas vealtgsqaf vqtslkafdq
      301 rrkrvvealr ripglqcrep egafyafvgc religrrtls garidsdqdf vryllddanv
      361 avvsgtgfll spyfrlsyaa sieqldealq rieaacakll t
//
LOCUS       WP_175945454             233 aa            linear   BCT 11-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Burkholderia pyrrocinia].
ACCESSION   WP_175945454
VERSION     WP_175945454.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..233
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=25301
     Region          38..224
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mdrlmtrgvs iagrtldrae llllvegspt plhledcdle gadlsrldlr garfercala
       61 easfvgstla qtswircrgr qasfassdle davfqscdln ntswrrsklg sarfnecrlt
      121 gadfeecksl glefentllv gaslrrfsfr ktrlaaldfs dadlagadfr davfeggslr
      181 nahlndvkfe gadlrdvdls gtpkllasgv lrgatvsydq aamlienlgi rva
//
LOCUS       WP_175945494             746 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Caballeronia sp. BCC1704].
ACCESSION   WP_175945494
VERSION     WP_175945494.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 746)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..746
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=79842
     Region          <61..>207
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          216..739
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msrglleagr haasagfsrr sflkfgltas vtasggflig fslpaasqdq skgksviggd
       61 gvepaqagvf apnafvqidk agkvvliipk vemgqgvyts lpmliaeele vpidsvtidh
      121 appdeklfmd pllggqltgg stsvryawep mrkagaaarm mliaaaaqqw qcdastchae
      181 ggkvvhasgd rtasygelvq aaasmpvpqd kdiklkdpkd fkiigtkvrr ldspekvdgt
      241 amfgldvrlp dmvyaaivnc pvfggklasv ddtnarkipg vrqvikfdng vavvgdhtwa
      301 akrgaaalsi hwdegadgnv stkqiidela vasqksgava rkdgdvgkgf ndaktrvdav
      361 yqqpflahat mepvnctvhv rpdgcdiwlg tqvptrivda gvaitglpre kivlhnhllg
      421 ggfgrrlevd matqalkigk qlgtpvkvtw sreediqhdm yrpyyydkls agldangkpi
      481 awthrivgss imarfappay kngidpdaie vaadlpydfp nqvieyvrqe prhvptafwr
      541 gvgptrgtfv vesfidelav qakidpvqyr rnllnktpra rnvldvatqa agwgkrslpq
      601 gqgrgvsvmh afgsffsmva dvtvnkdgev rvnrivcavd cgmvvnpntv eaqvqggiif
      661 gitaalysei tiengrvqqs nftdyrmlri detppievhi vksteapggi gepgtaalap
      721 aitnaiyaat gkrlrqlpvg nqlrsa
//
LOCUS       WP_175945567             291 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [unclassified Caballeronia].
ACCESSION   WP_175945567
VERSION     WP_175945567.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..291
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30698
     Region          4..264
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mlplqilidg faisslyalg aigftlifgv sgvlnlahgg vmlvaallgw mfageaglgt
       61 ylgtllgvac gmvaayityl mvvrpiqrsa aipreekeif vltgtllwgi miqqgmaylf
      121 tdnpitmrpl iggvlsiagv rvpyneimia vvcwvvisll wlfvnrtrag kallaasmnp
      181 rgltllgfel sriyllawti ygvlagiagv llasflgvst nntgqltasa fsivvlgglg
      241 svsgslmaay vvgyletvta yliaptlrpl pallllvlvv yvrpqgflgr r
//
LOCUS       WP_175945590             455 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia pyrrocinia].
ACCESSION   WP_175945590
VERSION     WP_175945590.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..455
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48488
     Region          2..449
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mknlqrhlsa rhirflalgs aigtglfygs asaiqlagpa vilayilgga aaymvmralg
       61 emavrepvag sfghyatenl gpfagfvtgw tytlemviva iaditafgiy mgfwfpdvpq
      121 wiwvlgvvai icglnlchvk vfgelefwls iikvgaivam igggvaillt gmhfghsadv
      181 ptfanlwnhg gflpngiggl iaslsvvifa yggievigms ageakdperv iprainavpa
      241 rillfyvltm vvlmsispwt gvgnggspfv qifsalgvks aatilnlvvi saaisainsd
      301 ifgagrmmfg marqgqaprv lmttsrhgvp wvtvlvmaga lligvllnfl mpkdvflmva
      361 aiatfatvwv wlmillsqva mrrrlsnaev aalkfkvplw pvapaltiaf mgfvivmlgw
      421 fddtrvalyv gaawlallaa lfyvrirpkf apasr
//
LOCUS       WP_175945610             500 aa            linear   BCT 11-JAN-2025
DEFINITION  HDOD domain-containing protein [Burkholderia pyrrocinia].
ACCESSION   WP_175945610
VERSION     WP_175945610.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..500
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=54760
     Region          18..218
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 mstteylprt alldklwarm nergdfplls eslratmaam knddldftal vrvvlsdfal
       61 tqkvlrlans amymafggni ttvtralmvl gldavghlvv glklvdhfhh stprridakl
      121 elnrallsgc varkltehae lrggeeavvc tlmrqvgkll vvcyldsewd rirrraaeln
      181 gdeaaacvdv lgvgfdeigl eaaarwrlpd viragmaned shaaradafd deyddrnagh
      241 aaddgpadrv rwlravsrcs tdvasalamp aspqrdaria tlaqhygael dmesdalvei
      301 adrlareeas dtvmreivel ranadaiara qaepeaciea gladlralps ehvltqvlal
      361 asesllagla ftrtvifvrh ddgtfaarlg fgpgvdtald qlrfderfep dvfhlaitns
      421 vgifieqaqd pkmlkrlpaw yldalddtra fvllpvrvgt ttvallygdw agaqparkit
      481 qqemsvlnel arelgrffpa
//
LOCUS       WP_175945642             398 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid aminotransferase [Caballeronia sp. BCC1704].
ACCESSION   WP_175945642
VERSION     WP_175945642.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Alexander,F.W., Sandmeier,E., Mehta,P.K. and Christen,P.
  TITLE     Evolutionary relationships among pyridoxal-5'-phosphate-dependent
            enzymes. Regio-specific alpha, beta and gamma families
  JOURNAL   Eur J Biochem 219 (3), 953-960 (1994)
   PUBMED   8112347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..398
                     /product="amino acid aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43856
     Region          1..396
                     /region_name="PRK09257"
                     /note="aromatic amino acid transaminase"
                     /db_xref="CDD:181731"
     Site            order(102..104,130,183,214,243,245..246,254)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(105,140,207,252..254,290,293)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            246
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mfehidaypg dpilslnenf qkdprtnkvn lsigiyfdda grlpvmqavr eaelsilqel
       61 gpkpylpmag fahyrdavqa lvfgtgstar aegriasvqt lggsgalkvg adfikryfpa
      121 skvwvsdptw enhrfifera gfevntypyy deatgglrfd amleaidalp aksvvllhac
      181 chnptgvdld eaqwvkiidv lhkrdllpfv dmayqgfgsg leddafavre larrgvpafv
      241 ansfsknfsl ygercgglhv icddaaeadr vlgqltsavr anysnppthg akivtkvltt
      301 pelaqswkee laamceriar mrraihdglr ehvhgealsr yvkqrgmfty tgleapqvdr
      361 lreefgvyil rsgrmcvagl nesnvqtvad aigkvlak
//
LOCUS       WP_175945706             339 aa            linear   BCT 11-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Caballeronia sp.
            BCC1704].
ACCESSION   WP_175945706
VERSION     WP_175945706.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180972
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..339
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38663
     Region          6..315
                     /region_name="CE4_u5"
                     /note="Putative catalytic domain of uncharacterized
                     bacterial proteins from the carbohydrate esterase 4
                     superfamily; cd10929"
                     /db_xref="CDD:200555"
     Site            order(13..14,123,127,164..166,224)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:200555"
ORIGIN      
        1 mpsdhgvftv sldfellwgv retrtiesyg enlrgvrrai pemlrvfgas gihatwatvg
       61 flfhrdiael kanlpdarpr ytrpgispye yieaareldp lyhfapelie riahqpgqai
      121 gthtyshyyc leegqgvcef eadlaravev arrtgvyvrs ivfprnqcnd aylasltrfg
      181 vlcyrgtqqg hayaasdkag qsrlmratrl ldayidvsgh ntyaldecyr ampfnfpass
      241 flrpykrkta wldglrlkri tdamtyaain krlyhlwwhp hnfgrdtaqn iaflqriadh
      301 yahlrdkygf vsmnmeelca laahhrtdep eystseaat
//
LOCUS       WP_175945700             488 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Caballeronia sp. BCC1704].
ACCESSION   WP_175945700
VERSION     WP_175945700.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   4  (residues 1 to 488)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..488
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54178
     Region          97..464
                     /region_name="BcsL"
                     /note="Acetyltransferase involved in cellulose
                     biosynthesis, CelD/BcsL family [Cell motility]; COG5653"
                     /db_xref="CDD:444374"
ORIGIN      
        1 magwkacaei gskrqciffg dvklrrqaty ygvlpqgieh sreplygiar capcspmqdf
       61 rrrtpkgpds rtfvqpvdpc stgdpkpskg lgtfmiapap hieiikspev fkalepewqa
      121 lwrrangrhh esfpvawlsw ecvakplgrt lrliavrseg rliavwplvr srnrlwtilr
      181 plspesadyt tlladpdyas agltkavwqa aqekcpadii llpyldkegd lyrlasahdg
      241 mmvanehpya iarlsrekdw esfsaplgtl sgkkpgallr rlerqgkvei rilgpqdade
      301 narmvdwmla ckrnwaervd kkgawlyspl frnylvniln ypsgpdseps armmvlmldg
      361 apiaanmigm gtqsilgamg gfdrqhskla pgaitteawv rwaiehrldf dlgvgseafk
      421 pywskgnlsv avsiqiaqss wgrvafamqd gmaklaaira gmrrpntevp pgktrsesve
      481 trtseaak
//
LOCUS       WP_175945724              67 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CsbD family protein [unclassified Caballeronia].
ACCESSION   WP_175945724
VERSION     WP_175945724.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..67
                     /product="CsbD family protein"
                     /calculated_mol_wt=7149
     Region          1..60
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 mnkdategik eqvkgwvdta igtvtgdedr klkgdveitn gasrkdyadq kdniekgved
       61 pgeptnt
//
LOCUS       WP_175945717             419 aa            linear   BCT 11-JAN-2025
DEFINITION  M48 family metallopeptidase [Burkholderia pyrrocinia].
ACCESSION   WP_175945717
VERSION     WP_175945717.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Bode,W., Grams,F., Reinemer,P., Gomis-Ruth,F.X., Baumann,U.,
            McKay,D.B. and Stocker,W.
  TITLE     The metzincin-superfamily of zinc-peptidases
  JOURNAL   Adv Exp Med Biol 389, 1-11 (1996)
   PUBMED   8860988
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Stocker,W. and Bode,W.
  TITLE     Structural features of a superfamily of zinc-endopeptidases: the
            metzincins
  JOURNAL   Curr Opin Struct Biol 5 (3), 383-390 (1995)
   PUBMED   7583637
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..419
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46645
     Region          8..415
                     /region_name="M48A_Zmpste24p_like"
                     /note="Peptidase M48 subfamily A, a type 1 CaaX
                     endopeptidase; cd07343"
                     /db_xref="CDD:320702"
     Site            order(279..280,283,361,365,405)
                     /site_type="active"
                     /db_xref="CDD:320702"
     Site            order(279,283,361,405)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320702"
ORIGIN      
        1 mspfsftllf alavlamvvt klwlasrqir fvaahrngvp aqfsatiplt ahqraadytv
       61 ertrltmlei vvsaavlvgl tllsgvgald mlltgwlgrg ygqqvalvaa vlvitsvidv
      121 pfeyyrqfgi eqrfgfnrmt krlfftdmlk nsllgaalgl pllfvvlwlm nqagslwwlw
      181 twivwvafqm lvlliyptfi apifnkfepl kddalrsrie slmkrcgfaa kglfvmdgsr
      241 rsahgnayft gfgaskrivf fdtllarlsg qeieavlahe lghfkrrhvm krmlvsfvls
      301 lallallgwl aqrtwfytgl gvtpsldtsn agaalvlffl aipvflffat pfssltsrkh
      361 efeadafaas qtdaqdlvsa lvklyednas tltpdpvyta fyyshppasq ridrllqla
//
LOCUS       WP_175945795             248 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [unclassified
            Caballeronia].
ACCESSION   WP_175945795
VERSION     WP_175945795.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..248
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26685
     Region          3..248
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mektydvpal rrandileal adaakpvraa alaertglsr stlylmletl armqwiekrd
       61 dgyvigvglf elgnayvrhd alqaafrega gafinthnev vqlavldgvq vvyvaredah
      121 rpvrlvsdlg srlpahccal gkallaglad eavierlper leavtprtit rraallrela
      181 airtsglave reevaeglac faayvgvtpa gkrvavstsv pvgrldakre kqismgivql
      241 aaklrqal
//
LOCUS       WP_175945828             254 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175945828
VERSION     WP_175945828.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..254
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27219
     Region          12..234
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mskvetsnpa eggvaavnra ltallafgna pgglmlaqvs eetglnmstl lrmfesleqf
       61 rfikrlpdgr yvlgpavfql gmmyresfql reyvmpilsk lsaetgetaa fyvregdqrv
      121 clfriqaqrs vrthlregdr fpldvgaagr vllafsgtrg gdyektaeqg yavsiaerdp
      181 esaaiacpaf gvgrvlsgai slgvpryrfn kkvladylpr vqaaaaelth alggdlpaag
      241 aafraadqlg vlle
//
LOCUS       WP_175945857             240 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia pyrrocinia].
ACCESSION   WP_175945857
VERSION     WP_175945857.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..240
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=25328
     Region          1..235
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 mailemlgfg tegwggvlll aalmtvaltl aalavgavig aaiaaaklsr hrsarllgdl
       61 yttvfrgvpe llviylfyfg gstlvttvgq wfgaegfvgv ppfvigalav gmisgayqae
      121 vyraavlavs kgeleaarsv gmsrgmvlrr ilipqvlrfa lpgignvwql slkdsalisv
      181 tglaellrts qiaansthqy fvffvaggal ylvmtglsnr vfnraeaivg rsfrrnfarn
//
LOCUS       WP_175945849             500 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175945849
VERSION     WP_175945849.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..500
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52330
     Region          41..485
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(48..49,52..53,56,93,143..144,146..148,151,175,
                     178..179,182,256,259..260,320..322,325,353,357,409..410,
                     414,418,434,437..438,441..442,445)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mktnhdrpaq atpsspggtp agggnaraag lrlpsrlvgp ivlgtllnal nssmiavalv
       61 siqqaftpqg aaheridtmw lvsglylata vgqptmgrla drfgakrifc iglaivlias
      121 alapfapslg wliasrvalg igtsaaypag mamirtwsqr hangatptgg lgaisvaaqv
      181 avafgpplgg alvqfagwra ifwinlpivl lafvlawlwi padvvprgal arrtlrgtlm
      241 eldlpgvalf ivtltslllf lqsvsrepdw lllvatlvlc pllvrrerla atplidirml
      301 sdnraltsty lrcvgtyavf yaifyalpmw lqearrlsaa daglvmlpia gvgtvatmla
      361 triahrhgsr pvlivgsaml cvgsvvmsll tsampvwsiv llsivfgvpn gfnnlgnqaa
      421 lyqsaphdri gtasglyrta qyvggslsfa lvglalghpa sdrglrelai vlavisvlll
      481 lnaassrhld aaassisqqk
//
LOCUS       WP_175945859             148 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175945859
VERSION     WP_175945859.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..148
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15651
     Region          18..137
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mstttgrcsp gwirvllaqp wvgalvrlal vsafliggvn kamhfgdaia eqahfglhpp
       61 afwaalavlv eiggslcvvf rrftwlgags lgmltlvaml vandfwnqtg varfmalnsf
      121 fehlgliaal vlvtmlgdvq rgegdgra
//
LOCUS       WP_175945865             302 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175945865
VERSION     WP_175945865.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32961
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,219..224,
                     230..231,233..234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176122"
ORIGIN      
        1 mklsfealea ldaidrtgtf aeaaellhrv psaltylvqk lesdldvalf drsgrraklt
       61 hagrvvveeg rrllhaaqql elkalraqqg wetevricid eilpfealwp yvhtfyglem
      121 ntrlrlstev lggtwdalis rradlvvgav geppelpdiv arpigtlrhv favapthpla
      181 alpeplsmas vveyrgavis dtsrelqprs vavdagqpyl avptlaakla aqceglavgt
      241 lpdciaarai aqgklvarqv tgmrdtthcy iawrgdeagr alhwwvdqla rpdlvdrfta
      301 la
//
LOCUS       WP_175945877             503 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Caballeronia sp. BCC1704].
ACCESSION   WP_175945877
VERSION     WP_175945877.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..503
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=54494
     Region          12..487
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(67,69,73,76,80,113,116..117,126..133,138,141,144,
                     237,241,244,247,249,423,425..426,428..429,432,435..436,
                     438,440..443,452,456,458,472,479..484,486..487)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(153..156,164,179,182,212,229..232,235,253..255,287,
                     388,390,416)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(156,253,284,287)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mqafndtadv vhyihgervs gsgarsqpif npatgerprk lvlgeaadve aavqsakaaf
       61 pawrdtppir rarimqrfle lmnqhrdela aiitaehgkv ftdaqgevtr gieviefacg
      121 ipqllkgdft eqvstgmdnw tlrqplgiva gitpfnfpcm vpcwmfpvai atgnafilkp
      181 serdpsaslf manllkkagl pdgifnvvqg dkvvvdalle hpdvraisfv gstpianyiy
      241 etgakhgkrv qalggaknhm vvmpdadidq avdaligaay gsagercmai svavlvgdva
      301 dkivprlaer arqlvvkngm epdaemgpiv traalerieg yiamgvdega qlvvdgrglk
      361 vpghedgfft ggtlfdhvkp gmriykeeif gpvlacvrak dfseavdlvn ahefgngvac
      421 ytrdghiare fgrrievgmv ginvpipvpm awhgfggwkr slfgdthayg eegvrfytkq
      481 ksimqrwpes tekgaefvmp tak
//
LOCUS       WP_175945892             224 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator transcription factor [Burkholderia pyrrocinia].
ACCESSION   WP_175945892
VERSION     WP_175945892.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..224
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23989
     Region          21..216
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mastpdmtsi girggggsap ivyvvdddet lrralssllr sagwrvetfa ssraflafer
       61 pdvpsclild vrlvdesgla vqeeavragl nvpilfmtgy gdvattvkam kggaldfltk
      121 pfddeamlda vghalardge rlareralga vrqayasltp rerevmsqvv aglmnkqiaa
      181 nlglqeitvk vhraqvmkkm qvrtlpdlvr qaealgvrpa gard
//
LOCUS       WP_175945918             628 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia pyrrocinia].
ACCESSION   WP_175945918
VERSION     WP_175945918.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 628)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..628
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=68325
     Region          7..545
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mkvlratesa eaadlivyng kiatqdtkrs fvtalavrdg rvlatgtgpe vmrharaytr
       61 ridlngrtvi pglndshlhv irgglnfnle lrwdgvptla dalcmlrrqv lrtpapqwvr
      121 vvggwtefqf aekrgptaae lnaiapdtpv fimhlgdsal lnaaalraig ygrdtsdppg
      181 geiqrdrlgr ptgmliarpd mgilhaalek gpklghddqm nsmrhflrel nrlgvtsaid
      241 aggdfqaypd dyaaimalaq rgeltvriay slfvqhagre lddyarwatl akpgdgdafl
      301 rmngagellv ysaadfgnfl eprpdlpaal eaelaevvrl lvrhrwpfrv hatydesigr
      361 flnvleavnr dmpfdglrwf fdhcetisda niariavlgg gvtiqhrmaf qgeyfiaryg
      421 aeaatrtppi ramlaaglpv gagtdatria synpfvslyw mvsgrtvggt mlypernrls
      481 rmealrrytv gsawfsnedd rkgalvpgqy adfavltddy ftiddaqiks lssvltvvgg
      541 kvvhaddefa plappplpvs pawspvaefg gvgrrrpaas aqpraaaddg pdagsalarg
      601 rrfaqrlhaa ateaveqcea fgqhgvaf
//
LOCUS       WP_175945941             437 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Caballeronia sp. BCC1704].
ACCESSION   WP_175945941
VERSION     WP_175945941.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 437)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 437)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 437)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..437
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49039
     Region          207..431
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mtnqkriddw rarrrtngyr igagaqmeda gphapattla lilaalrrsp retpsqrrqv
       61 yeslearlsd dvshadeetl dlrrrqlrtv irllendira gvdvfaprya patlareeah
      121 ladahekrvr rrreeearea rrsasredra ltpdvsagea sdlaalksri aslharqrpr
      181 avqagrsdlr allpmlifql dtmqgesrfa lawaffgpav lltlisslyl ltgtqfilgm
      241 dvptfsllga ttwimfrqii frsstsyisa rgwlnlqgvt pllcacvqav lyqaifvlvf
      301 atlilvghaf dlislpaswp affgyviamg fggastgvff gaiaskwrff lrlataierl
      361 leifssvffv seqlpeqyrg wflwspfahg mqllrsayfe syrstdarls yfvtslvfla
      421 avalcaerfa rcnvqpm
//
LOCUS       WP_175945988             180 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175945988
VERSION     WP_175945988.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..180
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18685
     Region          42..180
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msriaipaie satgatadvy aqvrkvaggt vpnlfaavgh lapnalaavl naegvlaggt
       61 lskqdletik llvsadtgcd ycvaahnllg kmtglsadal rsirsaqpkt gdakrdalir
      121 fvlnlqrtsg titddefasi reagytdaql aeislaialt iftntfnrin dtvvdfppvk
//
LOCUS       WP_175945954             242 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175945954
VERSION     WP_175945954.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 242)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..242
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26671
     Region          1..237
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mikfsnvdkw ygeyhalvdi naevrkgevv vvcgpsgsgk stlirtvnrl eeinrgkisf
       61 ggqdihdrkm svnayrsrig fvfqqfnlfp hlsvlenitl apmrvsgvkr aeaeskaldl
      121 larvglsnka nayppqlsgg qqqrvaiara lamnppamlf deptsaldpe mvgevlsvmk
      181 slaqegmtmm cvthemgfar evadriwfmd agtiletadp dafftapkhd rakkflsdlr
      241 sh
//
LOCUS       WP_175945992             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175945992
VERSION     WP_175945992.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32257
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrlaamety vsvveagsfs aaakrmnlgq paisksiaql eerlgvrlll rstrelattd
       61 agqrfyehak raiheadeae hvvrdasasl sgklrvsaav sftclhvlpl ldtflnrhpd
      121 leidltlddr nidlleegtd valrmgtlid ssmiarriar sprlvvgapa yfaragvpas
      181 padlarhqai vyaqrggges wsfsrngsev avavsgrlrv saaegmrtav iggmglavas
      241 rwmfspelas gavqavltdw elppidlwav fpagrlvtar arafvefveq alaegepapt
      301 q
//
LOCUS       WP_175945998             333 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Burkholderia].
ACCESSION   WP_175945998
VERSION     WP_175945998.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35391
     Region          6..313
                     /region_name="chlor_reg_RclR"
                     /note="reactive chlorine-specific transcriptional
                     regulator RclR; NF040475"
                     /db_xref="CDD:439702"
     Region          6..119
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
ORIGIN      
        1 mtldsdwlsr fmtlvtvtgk leircafgap waiayerspa ceipyhvvlr grailenpdd
       61 gtvrelgggd lvllphgsph vlhdgsglpp vpaikrpggh vfigenagtg arldmlcgrf
      121 vvapphdrli rrhlptdlvv rsaadsrvpd alaatarlta lvemmraesl eqqlgglail
      181 nalsaalfal alraisesgq aptgllalag hprlapaiva mlddparpwt lpelaalcsm
      241 sratfmrhfq sklghsaadl ltdirmslaa nalrqpsasa eavsadvgyq svaafrrvft
      301 rwagmtpgdw rrqafgdrrd aaaaddgvvd dak
//
LOCUS       WP_175946117             190 aa            linear   BCT 11-JAN-2025
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Burkholderia
            pyrrocinia].
ACCESSION   WP_175946117
VERSION     WP_175946117.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..190
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=20685
     Region          44..183
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 mttftesrag lpddplrags hshpadttdp htepppaiaa gfevrvqyaa idagaelapi
       61 vrnpnvgavv nflgvvrneg dvddvvalei ehypamteqa lwsiveeasa rwrleavriv
      121 hrvgriplgq avvlvvvaaa hrgsafdace flmdflktha pfwkkeirhd gesgwveaka
      181 hddqamrrwg
//
LOCUS       WP_175946086             447 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Caballeronia].
ACCESSION   WP_175946086
VERSION     WP_175946086.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..447
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48266
     Region          14..424
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(26..27,30..31,34,66,125..126,128..130,133,153,
                     156..157,160,257,260..261,264..266,269,296,300,350..351,
                     355,359,375,378..379,382..383,386)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mdletrtmkh vmvrlvpfli vcyfvayldr vnvgfaalqm nkalgfsasa fgfgagiffi
       61 ayfffevpsn lllerfgarr wiarimftwg ilaaamayip hiaqatglsn ayvfyglril
      121 lgvaeagffp giiflltlwf pakyrgrvvg yfmaaiplst viggpisgal lqldglhgma
      181 gwqwlyliea lpalllafvv yfyltdkpad ahwladderq wlvdrqaher ahreavhsfs
      241 vkealfnrrv laialiyfga natnyglsff lpqivkafgl snvqtgfvts lpyavgvism
      301 vlwgrhsdrk lerrwhvaia llvaaggiaa sagldnpvlk mialsiagfg ifgclpviwt
      361 lpaaflsgaa aaggiaains lgnlagffgp yvmgwikdst ggfgagllcl sgagligvaa
      421 vlllhhdtal etisgpqdme egepvrs
//
LOCUS       WP_175946104             260 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: enoyl-CoA hydratase/isomerase family protein
            [unclassified Caballeronia].
ACCESSION   WP_175946104
VERSION     WP_175946104.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..260
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28097
     Region          6..254
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 maeasivttr dgdiatvtid rpeklnamtk hlwqslgeti ealsgddalr civlrgagek
       61 afspgndiae frtdrsnveq arvygaimhr tlaalrncrt pliamihgic vgggleiaam
      121 cdlricgess rfgapiknlg lvmahaemeg lvqlagpava leillegrif gasealakgl
      181 vtrivpdgdv tshtyetarr iadgaplvar whkqfirrvm dptplsdddr degfacfgtd
      241 dfrigyeafl sktkpefkgr
//
LOCUS       WP_175946124             308 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175946124
VERSION     WP_175946124.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33423
     Region          6..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..286
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 marsdlsdit aflavaregs ftkaaakldv sqsalsqtvr nlearlglrl ltrttrkvsp
       61 tqagerliqs vgprleeiea elsalsalrd rpagvvriaa gehaaesllw pvierllpdy
      121 pditieivid ngltdiveqr ldagvrlgeq vakdmvavri gpdvrmvvvg tpgyfekhpk
      181 pktpqdltgh ncinirlpta ggiyawefrk gerqlnvrve gqlvfntatm avkaalagvg
      241 lafvpeqrvs sqlesgelvq vlsdwcpsfs gfhlyypsrr qptpafviva nalregagaq
      301 ksgvkrrk
//
LOCUS       WP_175946159             396 aa            linear   BCT 11-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Burkholderia pyrrocinia].
ACCESSION   WP_175946159
VERSION     WP_175946159.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18775051
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..396
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=42226
     Region          184..>322
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Region          <257..>351
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          288..318
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mtsrllaalv aaalsctalp aahartyvas tqsfgkgahv hqlvlrdpvt hqplpnaryr
       61 lflpgqviag lpvkpdqhds vifgttdaag rtvkirlpkv hpqkqwvfnp ivgegdmges
      121 frlvdpsgne plgnfpyvld veneylacgy sdasgytyya qsrtprnisl yagtlagsad
      181 ddwcagpgaa iangasdpga pdlytqylgs lvangsrisv elrqqivtkl lslaiaghda
      241 grvaavldlg eipdsrlndi gyrlvdagve vdrglamida hlakspdday aldskgwaly
      301 rlgrndeala wfdrsiaifa kdgddgdahe ayatglthkg evlwklgrqd earaafarar
      361 kiqpknaele etvkrleiqi gqdgakapgt aggqte
//
LOCUS       WP_175946192             584 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Caballeronia sp. BCC1704].
ACCESSION   WP_175946192
VERSION     WP_175946192.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..584
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=62515
     Region          93..576
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mralavavaa lcahigdaaa qayrdvapia ppaaerprap qppqqpades qavaiedlrg
       61 iafarageaa sgnrrsaaqs aaqgaitstd lpladaafld tfaadlgkpl tfarlaqirr
      121 avvqryrdag qplvdvyvpe qdvsngvvti avaefragrv makgnryfsd alltrempla
      181 sgepiheadv aaglallnan pyrrvdviya pgeaqnttdv vlqtddrlpl rvyggynndg
      241 vrdlgrdrfl agfdygnlfg idarigyqat asndlfsgnp diegrpdrar fiahsfnffa
      301 plpwldriel fgvlaqstpr lpdsygqtgi ssqlsfrydr llppldnaga wqqqiqfgyd
      361 fkrsnndlef ggfqvfnant hihqfvlayd ltnsdpaggt hlnasifasp grldssnnea
      421 afdaarlgat pryqyvqlsg qhesalgasg fsvsarglfq wtgntllpse elglggdatv
      481 rgyepyaaqg drgwnvqtem rapaftlgva alqpfvffda ghvwnripea gevnnaslas
      541 vgagirfqmg rfvsvrgtfg fplkavvpng skaplgevfv vigs
//
LOCUS       WP_175946207             313 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia pyrrocinia].
ACCESSION   WP_175946207
VERSION     WP_175946207.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..313
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33652
     Region          33..284
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(47,130,132,134..135,162,216,237,240,253,255,284)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mllvawcvgi lasvafagep gggnqapgfy rqklgdlriv alsdgthpfp vdtvfrdvsk
       61 deirrdldra fleppvqgsi naflvdtgtk rilvdtgagv lygdccgkll anlraagyap
      121 eqidevllth lhkdhvggiv sngrmtfpna vvrvneiean ywldpdnkaq apaflasffd
      181 aaaasvapyv aagrfktfrg eatlapgira vpmpghtpgh tayliesgda gllawgdivh
      241 vaaiqlqdpd atvqydsdad aarrtrrdtl krvvdkrylv gaahiafpgl ghlrrdgqqy
      301 dwvpvnydat plr
//
LOCUS       WP_175946222             257 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175946222
VERSION     WP_175946222.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..257
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27899
     Region          20..240
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mdslitdkek plpsneddqp avsklsnval rervydelan alragrfapa tmvtirglae
       61 mlgtstmpvr eavsrlvter alemlpnrtl rvpiispdkl delidiranv eghaaalaaq
      121 rmtpaefsri kaaneaygha ldagdmvaav aaneqlhfai yraarsglll sivetlwlqs
      181 gpylaavmkg msvaadslhd rgvmhhfnil aalakrdpda ansavqadir daaewykrql
      241 fvegalepvp aksrkrk
//
LOCUS       WP_175946225             376 aa            linear   BCT 11-JAN-2025
DEFINITION  YncE family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175946225
VERSION     WP_175946225.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..376
                     /product="YncE family protein"
                     /calculated_mol_wt=38529
     Region          8..187
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          <241..376
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mkfgilkfai llapvlgmaa cgggddihta phlittipvq tpgagflfdi syvdqirgqy
       61 yladvsnnai dvvnvgsnql tskikpgfag fsgsadttgp egivgipntt flyvadvdsv
      121 kvldvsngql vknipvansg lrtdsvcfdp dddvimatnp adsppfatfi stvtqnvvat
      181 lqfpdsagle qcqydkvtks fllnndgtpv nvhgemdvis assvvagapk vsdvyalpac
      241 npngmalgpk ndvlvacipd dgaplvslvl drttgsilst ipfggadqva ydavtnryfi
      301 pafreqksgv agaaasavpt lgvvdgssrs viaqlpmgkg ahsiaidgas hqiyvpfags
      361 gtgpfssngi avfstq
//
LOCUS       WP_175946226             419 aa            linear   BCT 11-JAN-2025
DEFINITION  nucleotide sugar dehydrogenase [Caballeronia sp. BCC1704].
ACCESSION   WP_175946226
VERSION     WP_175946226.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..419
                     /product="nucleotide sugar dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=45844
     Region          3..406
                     /region_name="WecC"
                     /note="UDP-N-acetyl-D-mannosaminuronate dehydrogenase
                     [Cell wall/membrane/envelope biogenesis]; COG0677"
                     /db_xref="CDD:440441"
ORIGIN      
        1 mcglgyvglp vavafarryd vigfdvdrrr iehlkkgedw tgeiesdvlr astmrftdna
       61 adladcnffv vavptpvdek cipdfsllvs acrtigpvlr pgsivvfest vhpgateeic
      121 gpelekasgl rcgvdfklgy sperinpgdr ehplerivki vsgqddesad iiaevyggii
      181 dagvhrassi kvaeaakvle ntqrdinial mnemskicdl agisttevle aagtkwnflr
      241 ftpglvgghc igvdpyylts kaqemgyhpe vilagrrind gmaqhvaaki vqmlarkhrl
      301 agstrvgilg mtfkenvpdi rnskvvdlyr alqqygiapl afdpmadkaq meheygislv
      361 dkshfdnldv vvlavphrdi matiwqdlph mltdgallcd lkssldktrl pasvqywal
//
LOCUS       WP_175946227             401 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia pyrrocinia].
ACCESSION   WP_175946227
VERSION     WP_175946227.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..401
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=41777
     Region          28..401
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 maartvdgrm grhtrkiarg avisaglvgl tcapvgvaha qssvtlygvm dvglqyrtaa
       61 gasngkaasa vllasgnelt srwgllgfed igggykatfk iesgfspttg ggnfavpfpn
      121 dtnalfdrga vigvvapwgk vlmgrnwspf fdgisagdat gfmnfgslan avfqnssnvn
      181 pklglggias ganspanggl lytwvnnsvk ymlpdntygl sggvlysfgg tagsfankqt
      241 wsanlnwtng tlgltsayfd ardptgatnn pwlralsvgm syvigtvktg fdfakfrnpt
      301 tganqnyyyl gaawqaspvw ratadwmylq dlknsaagaq lfkvgaqysl skrttlytdi
      361 aysmnkaqgi lgagsdtivl snpatigrnq iaiaagirtl f
//
LOCUS       WP_175946277             963 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia pyrrocinia].
ACCESSION   WP_175946277
VERSION     WP_175946277.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 963)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..963
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..963
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=104440
     Region          42..962
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mknhglsrrg flkasllagv avyvaplgsr afaalfeekl ltpvkwdsvt gipqfridgi
       61 akvtgskvfa rdvraadmph wpqqqshali lrvtqadrty egfdlsllgd dlkpdcvvta
      121 ddlardgvaf pafygddmll pagktpaylg havailiyhd farfrfakna lkfrddviry
      181 gaatgplerd pwgtfryvrv ggktaydddv ysslkdapif psmmrkhlpv wpdgkehgkl
      241 deqgmflagq iaseldhpsa dwlvfdreyn tqsvdtaale pdnancwyda atqslhlvvp
      301 tqsplevaes aaamvakcrf pvkklfvhpc ytvgygskdh fnvpfyglvc alyadgrpvr
      361 fandryeqfq tslkrhafkm hyriavdrnt gllqsfkgdf eangggrsnf spsvamvgat
      421 aaqsiyyfpk sdlaavaias raidagsarg ygtlqsmaat emavdeiaaq lnidpidfrl
      481 rnalrsgmkn tqgaipagal rvdevlerak qhplwtrrva rkaefeaanp gkrygvgfac
      541 vqkdfgtgae asfakvefde hgkvslqhta aeigtgmsts qavavakwlg rpatevrvav
      601 tewpdlpvet sgdpyimsqa dqdrlsanpr wspnyaspss atnsayyfth streaaravf
      661 ryglwpaams iwtrglgggq aapytiried arwvdgklta dglepltfeq iakqahalgl
      721 ptgavvhvfn rwqwtdaefe vggtverlpi dglslrvgap ttgdttgdgs gpvpgtaapa
      781 gatamrgtlp ptangyrvld rkrvfippts rnnaavtyyt avgtlvelav heatgkvell
      841 thhsimecgn qispqlvsgq lqgglamgig halheylply edgpgngtwn fnryqlpras
      901 dvavwsqtgd ilpplsetdp pkgvaevvmi pvvgaivngi ahaighrftd lpvtpqkiqe
      961 vla
//
LOCUS       WP_175946276             438 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Caballeronia sp. BCC1704].
ACCESSION   WP_175946276
VERSION     WP_175946276.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..438
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46019
     Region          48..428
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mltrtlavta llaatisnyt qaspvqliad eggvqesqgl psslpqvsli dvlglaaqsn
       61 pllrgaraes dasagalmqa garpnpelsl lqegfggter tstatvnqli elggkrqarl
      121 dvasygreva laaldgrgaa lradvisafy eelaaqrqeq varesadiaa rsadlaekra
      181 ragkvspvea tkariaasav qievtnavar vitarerlas vtgnprvrgs aaggdiesvp
      241 sleplsvlvn qlndspatrv araemlrsda aisverakrt pditvsagmk rvvtggvpdn
      301 qavigvsipl plfntnkgal leaahkaeka sadfdnerlr lqleltrayt nyetsvqaar
      361 rlkddvlpas kdalnamsrg felgkfafld vldaqrtlfq aqsqyvqslt dahlayaevg
      421 rlvgtplpav slskntlp
//
LOCUS       WP_175946279             241 aa            linear   BCT 11-JAN-2025
DEFINITION  ZIP family metal transporter [Caballeronia sp. BCC1704].
ACCESSION   WP_175946279
VERSION     WP_175946279.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Dempski,R.E.
  TITLE     The cation selectivity of the ZIP transporters
  JOURNAL   Curr Top Membr 69, 221-245 (2012)
   PUBMED   23046653
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Guerinot,M.L.
  TITLE     The ZIP family of metal transporters
  JOURNAL   Biochim Biophys Acta 1465 (1-2), 190-198 (2000)
   PUBMED   10748254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..241
                     /product="ZIP family metal transporter"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24628
     Region          1..223
                     /region_name="ZupT"
                     /note="Zinc transporter ZupT [Inorganic ion transport and
                     metabolism]; COG0428"
                     /db_xref="CDD:440197"
ORIGIN      
        1 mtpavklall tlppvlagaa gaviasvrkp gerttsviqh ftagivfaaa alellpedrk
       61 halwpvvigf alglglmlgi ktvcnrlear legsslptgl vvvtavdlii dglvlgiafs
      121 ageetglilt ialtlevlfl alsvstalsa akvrglwaiv vpvslsalls vsavaahgvl
      181 anlpsvyyag llglgtvali ylvteellve ahevaetala ttaffvgfiv ffvieatikt
      241 g
//
LOCUS       WP_175946457             545 aa            linear   BCT 11-JAN-2025
DEFINITION  S8 family peptidase [Burkholderia pyrrocinia].
ACCESSION   WP_175946457
VERSION     WP_175946457.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..545
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=54667
     Region          233..512
                     /region_name="Peptidases_S8_13"
                     /note="Peptidase S8 family domain, uncharacterized
                     subfamily 13; cd07496"
                     /db_xref="CDD:173820"
     Site            order(240,308,312,379..381,407,409..410,480)
                     /site_type="active"
                     /db_xref="CDD:173820"
     Site            order(240,308,480)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173820"
ORIGIN      
        1 mrakrfnfal arsaharmla gmlsaaallp lagcgggggd gsnpsssnaa paptpapapt
       61 tppttsgsna ctsqqaavqm aaqttpdepp vdhlivklkt ltatramaai dngtrldavi
      121 qrsmtrwtap vtgsarayas tvaqtplnvq vertisngaa vlslgqrvaa adatalaqtf
      181 aadtdvdyae pdhpmqirdt psdplysqqw ylsdptagid lppawnttkg sptvvtavld
      241 tgsrphadlv gnllpgysfi tnvntsnngl srgpdasdpg dwvtqqelgd angpyyhcas
      301 epsnsswhgt rvmgvigata nngagiagvs wlgrilpvrv lgkcggvtsd iadamrwaag
      361 ipvtgvptnp tpakvinlsl ggvgacsttf qqaiddvnak gvtvvvaagn dglstgldqp
      421 ancrgvvsvg atdatgrras fsnfganitl sapgvnilst sntgtttpgs dtyglangts
      481 latpqvtgva almlavngnl tpaqiqqklq ggtraaklaa gtpctampag sgildagaav
      541 aaanl
//
LOCUS       WP_175946480             803 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Caballeronia sp. BCC1704].
ACCESSION   WP_175946480
VERSION     WP_175946480.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 803)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..803
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=87670
     Region          27..744
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mqsssptnpp atpperpkka srpwytrlfl gflvsvfali vcaglvlgya lvvampnlps
       61 lealtdyrpk vplriytadh vligefgeer rsvvrirdvp dhlkkavlai edarfydhgg
      121 vdltgilrag svaltnghas qgastitmqv arnfflssek tytrkiyeml laykieralt
      181 kdqilevymn qiylgqrayg fasaarvyfg kdlkditlae aamlaglpka psaynpvvnp
      241 krakvrqeyi lqrmrelgfi tedeyeqaak qplvvkgqgr efsvhaeyva emvrqmmyaq
      301 yreeaytrgl nvvttidsad qdaayhavrk glmdyerrhg yrgpegfidl psnaddreqa
      361 iddalaehpd ngeivaavvt aastkevkas fidgnvatvs gsnlrfvana lspraqpnqr
      421 irpgaivrlv knddgdwtit qlpqvegali smvpqdgair alvggfdfnk nkfnhvtqaw
      481 rqpgssfkpf iysaslekgl spatiindgp lffsaaetgg qawepknygg gfdgpmtmrt
      541 alqksknmvs irilntigtk ygqqyitrfg fdadrhpayl pmalgaglvt plqmaagyav
      601 fanggyrvnp yliaditdpy gavvshpqpl vaqqsaplai tprnayvmns llqsvaqhgt
      661 aaktnqlkrs dlagktgttn dsrdawfagy qrslvaiawv gydnprslgd ketggglalp
      721 vwmdymsral qgvpeykplm ppdvkslgge lyyddmtpgh gfiatigvsq appqeggvsg
      781 vtapapdvge qekqdimnlf kgq
//
LOCUS       WP_175946557             251 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cytochrome c1 [unclassified Caballeronia].
ACCESSION   WP_175946557
VERSION     WP_175946557.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..251
                     /product="cytochrome c1"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28425
     Region          20..251
                     /region_name="CYT1"
                     /note="Cytochrome c1 [Energy production and conversion];
                     COG2857"
                     /db_xref="CDD:442105"
ORIGIN      
        1 mkkwlstlam tcaamfafsa apvhaaeeav ldrapdnadn faslqhgaqi fvnyclnchs
       61 aslmrynrlt dlgltqkqiq dnllftteki gntmsiamrp ddakawfgas ppdlsveara
      121 rgkdwlytyl rsfyrdptrp tgwnnrvfen vgmphvlwtl qgirdarfet dtdektgekt
      181 krfvgytqvt pgtmsnvdyd savadlvsyl swmsepaqqt rkrlgvwvll flallsflaw
      241 rlnaaywrdi k
//
LOCUS       WP_175946582             219 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Caballeronia sp.
            BCC1704].
ACCESSION   WP_175946582
VERSION     WP_175946582.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..219
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23911
     Region          18..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtrspaapak tparrqvrtd gataqeqlld aaqalfyreg vravgvdavv eragvnkmsl
       61 yrrfaskdel vvaylermdd rfrqrleasf dkhpgdpakq lvqafddlve rasapdyrgc
      121 pfvnvscefg dpahparqlv ernkryvmtr fiekcqaaga eqpvelaesl allldgvyat
      181 sqtygpgsgp lraasrvara lvdaaceksn hpqgnqess
//
LOCUS       WP_175946584             427 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Caballeronia].
ACCESSION   WP_175946584
VERSION     WP_175946584.1
KEYWORDS    RefSeq.
SOURCE      unclassified Caballeronia
  ORGANISM  unclassified Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="unclassified Caballeronia"
                     /db_xref="taxon:2646786"
     Protein         1..427
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44737
     Region          15..415
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(26..27,30..31,34,69,116..117,119..121,124,148,
                     151..152,155,243,246..247,250..252,255,286,290,341..342,
                     346,350,366,369..370,373..374,377)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mnwvakrldg rmhygwvtvg vvflvllaaa gtratpsvmm lplekqlgws rgtislaisi
       61 nlalygltgp faaaamqrfg vrptllaala tlaagvgass mmtapwqmvl vwgvvvggat
      121 gvaaltlsat vvnrwftthr glamgiltas satgqlvflp flasisehhg wrpvvfvvaa
      181 aaavvlplva wllperpadv alrpvgeaag tppaaaaahk npikvafgal ssasrtrdfw
      241 llffsffvcg astngyvgth liamcadygm tqvqgatlla amgifdlfgt tlsgwlsdrf
      301 narvllfwyy glrglslmyl pyafgidffg lpvfavfygl dwiatvpptv rlatdvygke
      361 sapivfgwiv aghqlgaafa algggmlrss lgsytvatmi sgglclvaav avlrinrarr
      421 aagvaat
//
LOCUS       WP_175946613             207 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD family hydrolase [Caballeronia sp. BCC1704].
ACCESSION   WP_175946613
VERSION     WP_175946613.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..207
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23367
     Region          3..>170
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mtikavvfdf ggvlidwnre ylykqlipde aerrwfldnv ckmdwvmqqd ggqsveegta
       61 elvaqypehe plirafyarw hemvagvlee gvtlvdrlda agvplfgltn wsaetfpyaw
      121 erfdvlrrfr eivvsgrvgl vkpdpqifal mraeiekhlp giqphelvfi ddnaanaqaa
      181 tdlgwhgvhh tgaqeteakl ralgvpv
//
LOCUS       WP_175946717             148 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator [Caballeronia sp. BCC1704].
ACCESSION   WP_175946717
VERSION     WP_175946717.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia sp. BCC1704
  ORGANISM  Caballeronia sp. BCC1704
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Caballeronia sp. BCC1704"
                     /db_xref="taxon:2676300"
     Protein         1..148
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=16176
     Region          28..142
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mrktysfgmf lasspsakgy kmeetvtrvl lvdddestra slqvlleser cqvicavnga
       61 dalaqlavte vdvvitdwcm pfldgielck qlrgnptirq iplllvssdp vprcdglwda
      121 ffrkpvsfpd ifravrtlaa thvgvlaa
//
LOCUS       WP_175946745             557 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Burkholderia pyrrocinia].
ACCESSION   WP_175946745
VERSION     WP_175946745.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60439
     Region          25..384
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          453..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mtpaslieqy gpresmeydv vivgggpagl saairlkqla aekgteigvc vlekgseiga
       61 hilsgavmdp raitelfpdw keqgapltve vtedrflfls eksavttpnw alpenfknhg
      121 nyvislgnvt rwlgaqaeal gveifpgfpa aeilynddgs vkgvatgnmg vgkdgvpten
      181 fqlgmelhak ytlfaegcrg hlgrqliskf kldanadpqa ygigikelwe idpakhkpgl
      241 vihtagwplk sdtyggsfly hmdnnqvvvg fvvglgytnp ylspfeefqr ykthpsiraf
      301 leggkrvsyg araitaggll slpktvfpgg aligddagfl nasrikgsha aiktgmlaad
      361 aafdavqagr qsdelnaypd afkqswlyte lyrarnfkqw makglylgtl mvgleqkvmg
      421 gnvpwtlhhq hadhetlkpa sqcepieypk pdgkltfdrl ssvfisntnh eenqpahltl
      481 kdanvpvnvn lrtyagpegr fcpaavyefv knddgsdrlv inaqncvhck tcdikdptqn
      541 ivwvtpeggg gpnypnm
//
LOCUS       WP_175946784             153 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175946784
VERSION     WP_175946784.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..153
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15997
     Region          22..139
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 maapidsggf rnpawvrall gqpwvlplvr falvsaylig gvakaldfgg avaeqahfgl
       61 hpaalwaala iaveiagslc vvlnrftwlg agslgmltlv amlvandfwn qtgvarfmal
      121 nsffehlgli aalvlatvfa dakhpagddr ttr
//
LOCUS       WP_175946786             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175946786
VERSION     WP_175946786.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33743
     Region          7..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..293
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(105,109,148,162,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(106..107,111..112,114..115,118,122,124..130,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mqhlpdleaw aifarvaetg sfakaadllg vsqptvskav arlekrlgam llyrtsrkls
       61 ltptgellrd rairlladae qieseasvha lephglvrvn apmsfgvrhl spvlpvfler
      121 yprididlvl tdhivdivsg gfdvavriae lsdsslrsrr lcavrrplva apayldrhgr
      181 pthpsdleqh vcltytnlpt pehwrfrhaa sgeevgvsvh grirtnnadv ilpalvaghg
      241 lalqpeflvw damqrgelee vmsdwtiadi nvnlvtppgm lraarvtall eflaehfsha
      301 pwalpva
//
LOCUS       WP_175946817             326 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH:quinone oxidoreductase family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175946817
VERSION     WP_175946817.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Shimomura,Y., Kakuta,Y. and Fukuyama,K.
  TITLE     Crystal structures of the quinone oxidoreductase from Thermus
            thermophilus HB8 and its complex with NADPH: implication for NADPH
            and substrate recognition
  JOURNAL   J Bacteriol 185 (14), 4211-4218 (2003)
   PUBMED   12837796
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..326
                     /product="NADPH:quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=33882
     Region          1..322
                     /region_name="QOR1"
                     /note="Quinone oxidoreductase (QOR); cd08241"
                     /db_xref="CDD:176203"
     Site            order(40..41,122,126,147,150..152,171..172,176,191,215,
                     237..238,240..241,262..264,314,316,318)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176203"
ORIGIN      
        1 mkallctafg pidrlriedv aipepaagqv riqvkaasln fpdalivqgl yqvkpalpfs
       61 pgaefagvid avgegvtawr agdsvvaftg hggfaqqcva dvhqiaalpp gmtfeqgaal
      121 vlaygtslha lqqrarlqqg etllvlgaag gvglaaieia kalgarviaa assadklalc
      181 rtagadetid ystedlrrrv deltggrgad vvydpvggay seaalrataw hgrflvvgfa
      241 ageipkialn lallkerdil gvfwgdavrr dpaqhvanmr llaewfaagk vrpaiterva
      301 lagaadaiar manrqvkgkv vilpda
//
LOCUS       WP_175946900             514 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175946900
VERSION     WP_175946900.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..514
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52066
     Region          90..493
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrlpeppaas iaaaalatav alagcatssi dlapeasdrp wqpqtsaagd ivpapprata
       61 qgahdytlpa tpalasvspp aaldsahayt lpelidlaes snpltriawn darnaalavg
      121 iaksaylpkl satamgayqa shgststilg dsssdttvhg tisalslqwl lfdfggraar
      181 veaaeqasia snvaftavhq qvihdvtvay yryeaarsra lsaqqglana dailaasrar
      241 lkhgvgtvve laqatqnraq anlalvqasg tesdsyldlv salgisplsk ptiaalskrp
      301 lppalgssvd aivsdaiarr pdlqgafale kanrakikaa eaafmpkifl sastsyasgg
      361 taitalpaig dqaptvnlng srygggvflg vtiplydggl rsavlmqarn daqsasarlt
      421 rtkeeavrqv vaaqnavqts lashdaakal vdaaqtsyda altayrngvg svtdatiaqs
      481 qllaarnaev dsyagalsaa aalalatgti gsaq
//
LOCUS       WP_175946888             217 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            pyrrocinia].
ACCESSION   WP_175946888
VERSION     WP_175946888.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..217
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23717
     Region          29..180
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maevteraps krrtrgrpla gasvgpdvil raarrtfakr gydatsvrev arelgvdaal
       61 iahhfgtket lwlavveqiv dlatpmfdal ralrtsslph rdcvrralel cvdhefdepd
      121 igmffstaat evggrldrlq erlvrpyhdv mfpllsdavq agairavdpn vlffmiasai
      181 gttvsyshmm laftslptqr dafkqavlaa alniigd
//
LOCUS       WP_175946854             435 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175946854
VERSION     WP_175946854.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45939
     Region          19..423
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(31..32,35..36,39,78,136..137,139..141,144,164,
                     167..168,171,254,257..258,261..263,266,294,298,350..351,
                     355,359,375,378..379,382..383,386)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mstlaqpaah aprrvrnsrl atasmigtsl ewydftiynt laalvfnhlf fpsvdplagt
       61 ilafstyavg yvsrplggfv fgnlgdrigr ravlmltlvl mgvttalmga lptyaqagil
      121 spillvalrf vqgvalggew agavllsveh gdqkrrglsa swtqmgpsfg tllgtgcial
      181 vtlsttsanf lswgwrvpfa asallvvfgf wlrrgvdetp qfeqlaesha taevpvadvl
      241 kyhwrrllia ggarigsdvl yalivvftlt yvttvlhlsr pvaltavmvg tacnalavpf
      301 fgalsdrfgr rpvylagaia gvvwafvffv mldsarpgai vaavaiglvi havmygpqga
      361 fvteqfptrv ryagsslayt lagivgggfa plviaalfrq tgtttavsly vtaslvvtai
      421 allaaretah rplad
//
LOCUS       WP_175947018             257 aa            linear   BCT 11-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175947018
VERSION     WP_175947018.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..257
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28644
     Region          12..248
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mssplqsesi raqvaelrer gfvvarglvg eqqcaalkri aerqlqeaae piefeadlry
       61 pgapeskhap gghtvrrlld aysrdpafae ratapeigaw mreyfgeepv lsrahhncmm
      121 tkhpaygslt gwhrdfrywa fersdmvsvw halgpetnen galwlvpgsh taefgpeafd
      181 eakffrsdlp enrkmidaat cptlqagdvv ffhsntlhsa gqnrsdqvkf slvytyhgas
      241 nrpmpgtrsa akpevqf
//
LOCUS       WP_175947029             279 aa            linear   BCT 11-JAN-2025
DEFINITION  polyphosphate kinase 2 family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175947029
VERSION     WP_175947029.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Motomura,K., Hirota,R., Okada,M., Ikeda,T., Ishida,T. and Kuroda,A.
  TITLE     A new subfamily of polyphosphate kinase 2 (class III PPK2)
            catalyzes both nucleoside monophosphate phosphorylation and
            nucleoside diphosphate phosphorylation
  JOURNAL   Appl Environ Microbiol 80 (8), 2602-2608 (2014)
   PUBMED   24532069
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Sureka,K., Sanyal,S., Basu,J. and Kundu,M.
  TITLE     Polyphosphate kinase 2: a modulator of nucleoside diphosphate
            kinase activity in mycobacteria
  JOURNAL   Mol Microbiol 74 (5), 1187-1197 (2009)
   PUBMED   19843229
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Nocek,B., Kochinyan,S., Proudfoot,M., Brown,G., Evdokimova,E.,
            Osipiuk,J., Edwards,A.M., Savchenko,A., Joachimiak,A. and
            Yakunin,A.F.
  TITLE     Polyphosphate-dependent synthesis of ATP and ADP by the family-2
            polyphosphate kinases in bacteria
  JOURNAL   Proc Natl Acad Sci U S A 105 (46), 17730-17735 (2008)
   PUBMED   19001261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..279
                     /product="polyphosphate kinase 2 family protein"
                     /EC_number="2.7.4.-"
                     /GO_function="GO:0008976 - polyphosphate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016776 - phosphotransferase activity,
                     phosphate group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006797 - polyphosphate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31809
     Region          7..277
                     /region_name="PPK2_rel_1"
                     /note="polyphosphate:nucleotide phosphotransferase, PPK2
                     family; TIGR03709"
                     /db_xref="CDD:274737"
ORIGIN      
        1 makqpslddf rvptstreke aaafkldafd paakpfssgs keadrerlsa vsteldvqqe
       61 rlhtqqkkrv llvlqgmdts gkdgtvravf revdplglrv vsfkaptpie avhdflwrvh
      121 aqvpgagela ifnrshyedv lvprvldtid skecerryrq irdfetmlfe ngttivkcfl
      181 hiskdeqrar lqariddptk hwkfdisdld arkhwdayqs ayrdalaats aehapwyvip
      241 adskthrnvm iaelllrtmt dmklefpppk pelegvkir
//
LOCUS       WP_175947041             288 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175947041
VERSION     WP_175947041.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..288
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=32102
     Region          5..277
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mfdqivfagg gnrcwwqagf wdvaqpalgl rprvitgisa gaatacmlyt rdaawvmryy
       61 eealrhnrkn aywgnlfgre pvfphyriyr qalldiygep faklaaapei rigvshvprw
      121 lgarsavaag lvayniekyv rktlhptlgr tlgfrpefvr aqactqvdel adlilqssct
      181 ppftpvlrrg grpvldggmv dnvpvdaldp spgdvlvlvt rlyprpqmft vahgeqrrly
      241 vqpsskvpis swdytspsqm rhaydlgrrd gehfltrvda mtgdraaa
//
LOCUS       WP_175947087             204 aa            linear   BCT 11-JAN-2025
DEFINITION  CGNR zinc finger domain-containing protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175947087
VERSION     WP_175947087.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..204
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22183
     Region          11..204
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mvtrneparh ahewgaadfv gghpaldfln tvadtgkard edklvdwpav rawagkagll
       61 apadlarllr harqdgpdel aalhrfreda yaaiahltag gggsagaraa grlavgirda
      121 igrsafdavd grfawrpdar aasrwvdaaa lgfehllrsd dfarvrqcgr ctwffvdrgr
      181 gvgrrwcdmr tcgnrakvea frer
//
LOCUS       WP_175947159             262 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175947159
VERSION     WP_175947159.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..262
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28031
     Region          4..250
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mksvrferrd svghivlanp plnliatafs ehlseaihea sesnirallv raegpnfsqg
       61 gdildfidke fnawrtfisd mhhayrkiea lqiptvcavr grawggafel alacdlvvaa
      121 dnasfrciep svgtipvcga vqriaeragp araaryvmls evmsgttage lgiaafvapd
      181 adveqaaldl airlsngptr syaairallk awsaggvpga dqvvldlgmp lhntedarrg
      241 rtarvdamkr gvepepvvfy gr
//
LOCUS       WP_175947160             332 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: PDR/VanB family oxidoreductase [Burkholderia].
ACCESSION   WP_175947160
VERSION     WP_175947160.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..332
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35826
     Region          17..234
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(58..59,61,75..77,83,85..86,127,233)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(58,60..61)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(83,86,89,96)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(119,123..126,128)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(124..125,148..150,206..207)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          249..332
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 merntppsna llrvvvsakt wladgivgye laslsderlp dfeagahidv hlpgglvrqy
       61 slydlpgeps ryrigvlrdp qsrggsaslh ddvragdtls istprnhfal hrgpeqsllf
      121 aggigitpil gmaqqlares rpfalhycgr spsrmafver vqqmssaddp harvqvhadd
      181 gpaaqhldar aaigspsadk hlyvcgptgf mdhilqtara lgwsdahlhr eyfaaapvep
      241 sdedtpfeie ihgsgevirv gagqsvahal ldagfnlpls ceqgvcgtcm trvlagepdh
      301 rdlyltddek arndsfmpcc sraktarlvl dl
//
LOCUS       WP_175947162             318 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia pyrrocinia].
ACCESSION   WP_175947162
VERSION     WP_175947162.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..318
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33261
     Region          87..291
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 msqtkhpspr dllhpslraf adaaaarpsl aqmsaadara giaartaara pgprvdkvfd
       61 laipgpgggi pvriyhpggg agvtmafhgg gwrmgnldsf davcrhlasd sglavisvdy
      121 rlapehpfpa aledvwaatc wavehghehg lptgrltvfg esaggnlaav vcllareqaq
      181 prilaqalvy patdatqkha srsvyaegfv qrtadvahaf reyalehgvs psiwtlspfh
      241 aeshadlppa lvitaecdvl cddgeayark laeagvpttc vryagmphtf ygmrgevgaa
      301 alaqrqvadm lraavqag
//
LOCUS       WP_175947171             199 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia pyrrocinia].
ACCESSION   WP_175947171
VERSION     WP_175947171.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..199
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21362
     Region          2..195
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mptlqvmlkm alyvslvlat pgptntllls sgikvgfrks spllvaeasg ygfaislwgf
       61 flatfaatrp wlydvlklgs sayifylalq lwksprfedi qsgsigfrdm fvattmnpka
      121 llfataifpp qafvsvpfyl csiavftala vtigsmwlti ggvltarrsl athtgtllrg
      181 asvvllmfag tlafsvlnr
//
LOCUS       WP_175947202             127 aa            linear   BCT 11-JAN-2025
DEFINITION  GtrA family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175947202
VERSION     WP_175947202.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..127
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=13569
     Region          5..127
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 midllhaert rlvrfglsgl gstaihtlva salfamfdat lvaanaaafl catafsylan
       61 tlwsfsstvr trnalrflvv tlagfvetll laraaealdv sraasivaia llvppstfvl
      121 hrlwtyr
//
LOCUS       WP_175947209             196 aa            linear   BCT 11-JAN-2025
DEFINITION  flavodoxin family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175947209
VERSION     WP_175947209.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..196
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=20693
     Region          9..189
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mtqhtspvkt vvvyhsghgh termaraaae gagavlvaid tdgniaedaw ntlagadail
       61 fgsptymggp swqfkkfada sskawfegaw qnkifggftn sasingdkln tleyfvllag
      121 qhggiwvsmd ikpanvkasm rddlnrmgsy iapmaqtpad aspaemspgd letarrygar
      181 vatiagqfrs gkshgn
//
LOCUS       WP_175947216             467 aa            linear   BCT 11-JAN-2025
DEFINITION  GGDEF domain-containing protein [Burkholderia pyrrocinia].
ACCESSION   WP_175947216
VERSION     WP_175947216.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 467)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 467)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..467
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52087
     Region          200..467
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 msiaasanep aasiqfitka yarllltgfa lvpamliayl yffqdpslkf enhafhelai
       61 aaatlegvfv tyvcwrcyrl sgepllrwlt lgflgfsliy alhgvftgma hhniwlflly
      121 gpasrlvmsi lifvgqlsys rsadneafrv drrawmtwia lfvlidvlva wvayspvags
      181 pwvrlsmegg alafstinvv alvlrrirtp lmliygisva sfalsslafi igrpwnhmww
      241 lahvifaggf fllsfgvvqa fhttrsfsti ysqeelfarl reamartera lqelqrtnek
      301 leymaatdpl tgaanrrrfi erveveiara rrngapfsll aldldhfkvi ndsyghqtgd
      361 qvlqrfvkkc ldairpydgv arvggeefmv llpqaaldta rlvgeriraa iagtpfetgd
      421 gkpievtvsv gisefgrdge tidailrkad erlyqakhqg rncviaa
//
LOCUS       WP_175947222             462 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175947222
VERSION     WP_175947222.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..462
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48962
     Region          24..430
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,152,
                     155..156,159,265,268..269,272..274,277,304,308,358..359,
                     363,367,383,386..387,390..391,394)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mahtvnaagr ldrlpisrfh wkilgliggg afldafdiyl angsvaamik egftdlrhga
       61 mfvsstfvgm migafvagyv gdrlgrrysy qlnlavfgla siaacfapdi ewlivlrfim
      121 giglgaelvv aagtlaefvp petrgkwvsl laiitnsglf aalaagywvi phlgwrymfa
      181 lagagalivw fmrkrmpesp rwlesvgrld eaeatlsaie levgkqvgtl ppvrrtidlh
      241 vgkvplgvlf srgmrgrtav aaltaigvnv glygfiawlp tffvaeglsv vkslgfvflm
      301 sigspvggli gyltadrlgr akgiviasil sialgwlyvs lrdttaiilv gfclvsaiyt
      361 ittlglfgyi pelfptevrl rgtgvagmcg rmssigtpal alalyqafgv sgviamvsvt
      421 lgvlcvaigl lrvetgrqal eevapgtndv ertavdprvt qa
//
LOCUS       WP_175947269             523 aa            linear   BCT 11-JAN-2025
DEFINITION  S41 family peptidase [Burkholderia pyrrocinia].
ACCESSION   WP_175947269
VERSION     WP_175947269.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..523
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55537
     Region          75..439
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mcvvrrlavc aavaaallpc tqpagaqsas astaappaap pvsqpvappv ppasqpaaas
       61 pspcppdwep qicelkaave vlkkqhltdv digalldaat hdgiktlpya rffnakerqe
      121 qfdderrard gapgigivfe trpdglhiid vipdapaeka gvrpddlvva mndrsvvgid
      181 sselvklakg dagvplklav qrgpnhavls fapvraivkp hpaiakrldg dilytrlssf
      241 pepavgdyid avqavrrtgp pakgiildlr ingggalnaa igiaalfagr drtamvtver
      301 gdanrrrfst nwpdyelpvm hgqdplaplq addwwrtvpl vvlvdgqsas aaeataaalk
      361 dlgrakllgm ptygkglaqt gvdlidgtrl nftfarnlrp ngcpmdgygv vpdwlvpprr
      421 dsdvdgvmlw yrevdlarap yadrqapdpf apvrkerqkl rearvrakvd tsksaalpqr
      481 afgtagdwql qqalaalagr pvrtvdapaq lmpaqpvcer ggn
//
LOCUS       WP_175947274             469 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia pyrrocinia].
ACCESSION   WP_175947274
VERSION     WP_175947274.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..469
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50168
     Region          14..467
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mnhpappaat rrplppamld alraafgerv stadavrahh grdespfdpq lpdavvfahs
       61 addvrevvsl cslysvplip ygagsslegh llavrggvsl dlsemnrvls inaedltvtv
      121 epgitrkaln ealrdtglff pidpgadasi ggmtatrasg tnavrygtmr envlgltavl
      181 adgrvvkagt rarkssagyd ltrlfvgseg tlgviteitl rlhplpeavs aaictfpsmg
      241 eavrtvieti qigvpiarve fvdslavrsi nrhsnltlte aptlffefhg teagvkeqae
      301 lvqalagqnn gqgfewatrp edrsrlwaar hnayfamlql kpgcravttd vcvpisqlaa
      361 cveetevdlr asslpcpivg hvgdgnfhva ilidpdkpee iaeaehindr iveralrlgg
      421 tctgehgvgl hkmrflpkeh gdnaidtmra iklaldprnl mnpgkiftc
//
LOCUS       WP_175947296             205 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175947296
VERSION     WP_175947296.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130209
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..205
                     /product="phosphatase PAP2 family protein"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22552
     Region          52..198
                     /region_name="PAP2_Aur1_like"
                     /note="PAP2_like proteins, Aur1_like subfamily. Yeast
                     Aur1p or Ipc1p is necessary for the addition of inositol
                     phosphate to ceramide, an essential step in yeast
                     sphingolipid synthesis, and is the target of several
                     antifungal compounds such as aureobasidin; cd03386"
                     /db_xref="CDD:239481"
     Site            order(98,106,138..140,170,176,180)
                     /site_type="active"
                     /db_xref="CDD:239481"
ORIGIN      
        1 mntlslrddr rpdirqmlaa tfgmaaglai ffllersvtp ryvfatavda ripfiawswf
       61 vyvgffpfvi alaayarppa faafkeavli afvlgvvcfl lfpeavprpd vaeigntfvr
      121 hrlermwqld laangfpslh vavtclacrm ltgrrrivat aigllicast ltlkqhtvad
      181 vlggvalamv galwgerrsl rrrla
//
LOCUS       WP_175947338             126 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF805 domain-containing protein [Burkholderia pyrrocinia].
ACCESSION   WP_175947338
VERSION     WP_175947338.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..126
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=13647
     Region          5..122
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 mnfseavrsv lnkyakfegr arraeywyfa lltcvlsvaa qaigaigrda slimllllga
       61 iflislalii psiavsvrrl hdtnrsgwfl llgfipivga illlvwmcsr gtagpnrfge
      121 dpipav
//
LOCUS       WP_175947440             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175947440
VERSION     WP_175947440.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32520
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrfkqietf aavaakgsls aaahaegvap aiigrrldal eerlgvkllv rttrkltltf
       61 egsafledcq rvindmqnae asvsaggvka sghlrisapa gfgrrhvapl vpefsgghpd
      121 vsvtldlsdr mvdlvnegfd cavrlgelpd sslvslklge nrrvcvgspa ylarrgtpat
      181 laelarhncl alaananqqr gwafqeddkv vsirvngtme csdgavlhew claghglawr
      241 swwevgedia agrlvsvlda faappigiha vfpqrrhlpl rvrlfldylk htyerpgywg
      301 a
//
LOCUS       WP_175947473             332 aa            linear   BCT 11-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Burkholderia pyrrocinia].
ACCESSION   WP_175947473
VERSION     WP_175947473.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..332
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=34958
     Region          <8..323
                     /region_name="FAD_binding_2"
                     /note="FAD binding domain; cl46878"
                     /db_xref="CDD:481218"
     Site            order(34..35,38,41..42,66..67,70,73..74,97..98,101,
                     104..105,108,128..129,132,135..136,159..160,163,166)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          48..74
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          79..109
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          113..136
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          140..166
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          240..266
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          299..325
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mtafsstsll pgthdpdrva lvarlaapda svrriallel adleesdlvp afiaalrddp
       61 sadvrseaar vlgeweqpdv vdalcralld pddgvrataa qslselkdat sgtvlcswad
      121 rpepfvrsav lrglrelrap dafapalhal dadtatvrae avavlgwlkd sralpplari
      181 atadadadvr raavgaigfa tpgdtavvta llaalrdaaw qvreeaaatl gklrvvdgra
      241 plvaaldddy wqvrlravra lgqlrdaasa pavvallsha isnlrkeaal algelrapat
      301 lpalhdaled rdpevrkavr iaigqieqlg er
//
LOCUS       WP_175947406             404 aa            linear   BCT 11-JAN-2025
DEFINITION  cation:proton antiporter [Burkholderia pyrrocinia].
ACCESSION   WP_175947406
VERSION     WP_175947406.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..404
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43566
     Region          13..390
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mksafsflpn wplapdavfw aglalfaagl cgelcyrawr lpritgyavi glvagsfgfg
       61 vidastdets rllidvalgl llfelgsrld lrwirrnpwl iasslaeatl tfvlvlfvml
      121 algvsgmval vlsaiaiats psmviqlkte lraegqvsqr litltalnsv yaivltklvt
      181 swlhqeaygn vfatilqpvy liagsfilay lvarscnflf rhmtstmrde hsfvalfglv
      241 mlaiaaaqal klstlltlll agiivknlea rpqlwpehfg tagwlltvvl fvltltsftw
      301 gdialgglla ivlivtrlva klagvaafak psgigmkqgv algialtpms alsyllvddt
      361 yqlypnfdph lraivmctiv vlqlispfvv yrclsavger sdsn
//
LOCUS       WP_175947475             256 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175947475
VERSION     WP_175947475.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..256
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28556
     Region          10..245
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mtppnvvpls aaplyvqikd tlrarildgt yaphsrmpse helcamfdvs ritvrqalgd
       61 lqkegllfkl hgkgtfvskp kafqnvtslq gfaeamssmg yeivnqlrsf rtvkadrhla
      121 tklhvpegap lveihrvrll nrepvsleqt wvpealgkrl agadlaardi flilendcgi
      181 plghadvsid ailaddeivd alrveesspv lrierlthda sgapidyeyl yfrgdafqyr
      241 lridrqkark parnpr
//
LOCUS       WP_175947534             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: replication-associated recombination protein A
            [Burkholderia].
ACCESSION   WP_175947534
VERSION     WP_175947534.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..436
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=47888
     Region          1..434
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 msdlfqvepr rplaealrpk tlaevigqth llgegkplrl afesgkphsm ilwgppgvgk
       61 ttlarltala fdcefialsa vlggvkdire smeqakdtln rtgrhtilfv deihrfnkgq
      121 qdallpfves glvtfigatt enpsfevnsa llsraqvyvl ksldddemrq llkraqeial
      181 dglafddkai dtlvgyadgd arrflnlleq aqtaassagv atidaefvss amtlnarrfd
      241 kggdnfydqi salhksvrgs spdgalywfc rmidggadpk ylarrivrma wedigladpr
      301 alqmandaae tyerlgspeg elalgqaviy lacaaksnag ynafnqamaf vkqdksrevp
      361 vhlrnaptkl mkelgyghay ryahdepnay aagetylpdg vrephwykpv prgleskiad
      421 klawlreldr eagkkg
//
LOCUS       WP_175947629             159 aa            linear   BCT 11-JAN-2025
DEFINITION  PaaI family thioesterase [Burkholderia pyrrocinia].
ACCESSION   WP_175947629
VERSION     WP_175947629.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..159
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=16991
     Region          1..134
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 msdvaspadv psiespfvdl lgvrlvsakd gaseivlple erhmntwgia hggvtmtlad
       61 ialamaarsl tddgvgvvtv emkvnfmqpg rgelraygrv mhrsttmayc egevrdsdgn
      121 fvakalgtfk ymrrlavgrd ikrqrsrtap daqpgpsda
//
LOCUS       WP_175947634             390 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175947634
VERSION     WP_175947634.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..390
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42387
     Region          83..339
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 misieelqri adaplhswlg tlavsvivvl vvtivhrlga rivkriaqpy plmsailryi
       61 dkpslvvlal laleflwvqa ddgmsfvrgm rtaaavgsiv sltwllvrla agvgdaiiqa
      121 hpldtadnlq arrihtqakv lvrtvmvliv iigtgaalmt fpnvrqvgas llasagvagl
      181 vagiaarpvl gnliaglqia ltqpirlddv vviqgewgri eeitgsfvsv rlwdqrrlvv
      241 plqwiienpf tnwtrnsaei igtvylsvdy rtplaplree larlvhaape wdgrvqvlqv
      301 tdatertmql ralvsaadss scwdlrcrvr egliaylqdr ypqclprsrm elyphgsapd
      361 apnperphar apaastaant aadpqavegr
//
LOCUS       WP_175947654             195 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175947654
VERSION     WP_175947654.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..195
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=21123
     Region          1..>191
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 msrtfiyarv staeqtpenq ireieaagfa vdqdkrkqri vaecisgsva aserpgfskl
       61 ldrmesgdvl ivtkldrlgr namdvratve rlaadgvrvh clalggvdlt ssagkmtmqv
      121 lcavaeferd lliertqagl arakaegkvm grpsalsaeq qedarsrlaq gatvselara
      181 yktsrttiqr irdrg
//
LOCUS       WP_175947666             158 aa            linear   BCT 11-JAN-2025
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Burkholderia
            pyrrocinia].
ACCESSION   WP_175947666
VERSION     WP_175947666.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..158
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=17195
     Region          1..143
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 matiriqtdd fdlnaevaal rarnpkigai acfvgtvrdl negdsvaame lehypgmtek
       61 alekiaaeag rrwpgidvai vhrvgrllpl dqivmvatva ahrgdafasc efvmdylkte
      121 apfwkkettp dgerwvdars tddaalarwg vesgntsh
//
LOCUS       WP_175947667             186 aa            linear   BCT 11-JAN-2025
DEFINITION  group III truncated hemoglobin [Burkholderia pyrrocinia].
ACCESSION   WP_175947667
VERSION     WP_175947667.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Keppner,A., Maric,D., Correia,M., Koay,T.W., Orlando,I.M.C.,
            Vinogradov,S.N. and Hoogewijs,D.
  TITLE     Lessons from the post-genomic era: Globin diversity beyond oxygen
            binding and transport
  JOURNAL   Redox Biol 37, 101687 (2020)
   PUBMED   32863222
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Bustamante,J.P., Radusky,L., Boechi,L., Estrin,D.A., Ten Have,A.
            and Marti,M.A.
  TITLE     Evolutionary and Functional Relationships in the Truncated
            Hemoglobin Family
  JOURNAL   PLoS Comput Biol 12 (1), e1004701 (2016)
   PUBMED   26788940
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Wajcman,H., Kiger,L. and Marden,M.C.
  TITLE     Structure and function evolution in the superfamily of globins
  JOURNAL   C R Biol 332 (2-3), 273-282 (2009)
   PUBMED   19281958
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Vinogradov,S.N., Hoogewijs,D., Bailly,X., Arredondo-Peter,R.,
            Guertin,M., Gough,J., Dewilde,S., Moens,L. and Vanfleteren,J.R.
  TITLE     Three globin lineages belonging to two structural classes in
            genomes from the three kingdoms of life
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11385-11389 (2005)
   PUBMED   16061809
REFERENCE   5  (residues 1 to 186)
  AUTHORS   Wittenberg,J.B., Bolognesi,M., Wittenberg,B.A. and Guertin,M.
  TITLE     Truncated hemoglobins: a new family of hemoglobins widely
            distributed in bacteria, unicellular eukaryotes, and plants
  JOURNAL   J Biol Chem 277 (2), 871-874 (2002)
   PUBMED   11696555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..186
                     /product="group III truncated hemoglobin"
                     /GO_function="GO:0005344 - oxygen carrier activity
                     [Evidence IEA]"
                     /GO_function="GO:0019825 - oxygen binding [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20676
     Region          21..130
                     /region_name="TrHb3_P"
                     /note="Truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 3 (P); cd08916"
                     /db_xref="CDD:381257"
     Site            order(33,46,49..50,57,60..61,64..65,75,77..79,82..83,86,
                     89,93..94,97,121,124..125,128)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381257"
ORIGIN      
        1 mtalpaspdt aparprdaep tednirdlvy afydrvradp llgpvfdakl agrwddhlpk
       61 mvtfwsslvl gtkgyrgnvq qahqpldgie pahfsrwlsl flktvearya ppaairfmep
      121 alriaqslql srfgwdyrip peqqalldai aprrrdagdd phalpsrarg epfptkiigr
      181 sadpda
//
LOCUS       WP_175947794             892 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175947794
VERSION     WP_175947794.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 892)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 892)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..892
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..892
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=97039
     Region          14..828
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnvtelaqai rggliqqdrl lktdipslpn nalvprravt rselgrdfsv tldlvstasd
       61 ielktliakp mtlwiqqanq sylpingyih tarrlgadgs lssyqltfas wmhflkfrsd
      121 mrywqdqsvd ailadvfdah pqakgqyqfv lsktlptrsy crqsetdwnf vhrlmedegl
      181 fgfwrqsedg nahtlvitdd lhavdelspk tvrfdrsgtg setagftqwa asrtlqsslh
      241 ttrtfdyksp ssagnpngtt lptkagqgdl pdqaeiyeyt gaytyagqdr gehlskirle
      301 ewesrakrff gvggvrgida grrftladhp ehdrdaaqdr efaalkvsry iennlpisdh
      361 eanfphslqd rlaqvkaghg eaaafevghd dgsagfylve veaqraavpy rspfehrkpa
      421 mqletavvvg pkgeevytde lnrikvmfvw drqsegrena scwmrvvqsd tgggyggvhi
      481 prvgeevmig yiggdcdrpi vmhrvyngaa kpqwhsdgil sgfrskeyag sghnemvldd
      541 atgqnrarlf sssansllhl gylieqsgnt rgaylgsgfd lrtdaygavr aaqglyvtth
      601 pkqansqpld aseaqqqlan adgllesmsq vsemhqaenl gaghdalkqf tdatknsvag
      661 assggrtagg gtgsanafae pamlfaspag iglasqqsth laadrhvnlv sgqsthlasg
      721 kslvasvkek lslfvqnagm klfagkgpve iqaqndnvem taqkavkvvs atasiegvak
      781 qeilltsgga yvrikdgnie ihapgkidvk ggqhafsgpt smhktfkteg rkadmriryv
      841 dadgnvphge pirfatedgt ehsvaldteg raelknidfd efvasqvkrt ge
//
LOCUS       WP_175947826             668 aa            linear   BCT 11-JAN-2025
DEFINITION  acyltransferase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175947826
VERSION     WP_175947826.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Bera,A., Biswas,R., Herbert,S. and Gotz,F.
  TITLE     The presence of peptidoglycan O-acetyltransferase in various
            staphylococcal species correlates with lysozyme resistance and
            pathogenicity
  JOURNAL   Infect Immun 74 (8), 4598-4604 (2006)
   PUBMED   16861647
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 668)
  AUTHORS   Slauch,J.M., Lee,A.A., Mahan,M.J. and Mekalanos,J.J.
  TITLE     Molecular characterization of the oafA locus responsible for
            acetylation of Salmonella typhimurium O-antigen: oafA is a member
            of a family of integral membrane trans-acylases
  JOURNAL   J Bacteriol 178 (20), 5904-5909 (1996)
   PUBMED   8830685
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15196437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..668
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=72942
     Region          18..347
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
     Region          410..664
                     /region_name="SGNH"
                     /note="SGNH domain (fused to AT3 domains); pfam19040"
                     /db_xref="CDD:436916"
ORIGIN      
        1 mtktlsapat aaagtlvyrp didglraaav lavvlfhafp salpggfvgv dvffvisgyl
       61 itgillsdlg tdrfsfprfy arrirrifpa lilvllatya mgwfslygde yreltkhiva
      121 gagfvsnwas wteagyfdqa aeakpllhlw slgveeqfyi vwplllwaay karrigwvca
      181 aiglasfvmn valvghhpsa afywpitrmw ellagaalai saahvriigg ranvlsmaga
      241 llclssfafv nsqaafpgww allpvagtvg liaagrdgwf nryvlthpvs vwfgrisyal
      301 ylwhwpllsf alivagrtps savrgtllit avvlawlttm iverpvrfgp atvwkiaapc
      361 llmlgiaylg gmtyvrgglg frkgyspdad vttaklgagh efvnamcgvs pdeqrlfpfc
      421 atdkrvrshf avwgdskada lywglvresa pgegwtliar pscapmagvw rtssnagddp
      481 alcrtannea mrtllatpel ktvvlvmtdr dvigqtfavd gqssaspkaa ldgvdqvvtt
      541 lehagrrval vldnprlrdp rqcmdrrpla wpfvrhalgv tnmsaaqrca igyrehvtrm
      601 apftalvddl krrhpallvy dpaaalcdak rnvcpmtmdr hylysygdhl sdygnglvak
      661 qflpllrr
//
LOCUS       WP_175947851             205 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease [Burkholderia pyrrocinia].
ACCESSION   WP_175947851
VERSION     WP_175947851.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..205
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22948
     Region          18..84
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mspfsypkvr hnrtltpgpy kryqaykdal rqefgnkcvy ccapdlglkh tyavehyrpk
       61 kkfplfecdy knlyyacpac nthkgsfwpt rsqrlngefi pnpcdhvmfs hlrysagqvy
      121 aqsptgifas qvldlnspga vahrqaieaa inglesqlsd akklmawlsq qlasgnisqq
      181 dhdaemnrlt tlasgleani khfgg
//
LOCUS       WP_175947911             290 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175947911
VERSION     WP_175947911.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..290
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31941
     Region          22..264
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mrnpnedpvd pdgsglkkka nyrapalekg ldilellvgr eygmaqadic ralkrsrsel
       61 yrmmqvleer gyiyrvdryd ryaltmklyf lgqhhaptrs lgalvapllq qfalltvqsc
      121 yltvfdgdtm vviatagaet ewnlavrvgt rvplhgsaag emylafqdee vrsrllrtig
      181 hdveswnqlr sdealpthqv dgcicrpner ipgitdiatp ivdksgsaia ilacpylals
      241 geagamsirq igvalcetaq risatvdqrf mqsavempsr eparsarrag
//
LOCUS       WP_175947997             334 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Burkholderia pyrrocinia].
ACCESSION   WP_175947997
VERSION     WP_175947997.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..334
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36318
     Region          7..317
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(12..14,44,49,75,138..139,179..180,201,230..236,272,
                     289..292,297,300..301)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(44,49,75,138)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 mrimlpsrlg fgtaplgnmy rdipneeala tvdaawesgi ryfdaaplyg aglaelrlge
       61 alagrprdey slgtkvgrlv ldehedasqr dlgekgglfr hglpnkivyd ytedgtlrsi
      121 easlerlrtd rldtvwihdp aidfhgerwl dvfdvamsga akaltrlrde kvikgwglgv
      181 nrvepcelal ersdpdgfll agrytlldha galerlmpes varglgiivg gpynsgvlag
      241 gthfeyqpat qdmldrvari rqiserfgvd vravalqfsl ahpavaavip gasrpdride
      301 nlrlaaapip selwdalkae rliaehaptp agaa
//
LOCUS       WP_175948158             583 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia pyrrocinia].
ACCESSION   WP_175948158
VERSION     WP_175948158.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 583)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..583
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=62875
     Region          41..567
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mgwlayrpvh aqtappgarp vqdpaqliie qqreqarqrq leqppasiti aptsettldi
       61 plgtpideiv esgptfpvrr ivlqgtdgkp fdppggvsrk qlnevmapfv nhdlgshrin
      121 vllkrltdvf veggfvttra llgpqnlatg tlnvtvqvgr iasflvngqs ihrlkagesa
      181 agggwltdag yenafpaasg dplrlsdidq gvaqinrlrr nqatiqilpg qsagdsivai
      241 nnppgdrlyy nlgvdnygss atgvtryrag veannllglq eslslnflds ldsnalvgsl
      301 avpfgrntfs ytisdseyqq vigttaleyg rtlshifgwn ylvsrtpsdi tsvdatlswr
      361 rtdrevngid ldpqrlavfr lggnwlhkfv mndsqgnvsl nggvshglpw lganhdqhgi
      421 tredahsqft kvdataaftl plpkisralf ayrgmlggqy tnmalfgseq lylggmdtir
      481 gfrsgeiagd rgfysrnela wvnapawkdv riepylflda gkanlvavsg fptlagagag
      541 lraqwqwhkq alsgellvgr altqpaalgs katlvlgtan wly
//
LOCUS       WP_175948196             383 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia pyrrocinia].
ACCESSION   WP_175948196
VERSION     WP_175948196.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..383
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=39457
     Region          14..383
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mpqvlvnarl gagvalalat tavdevcaaa satvygivdt svvytrnsgs ahdvielqsg
       61 slsgsrigik gveplgsgaa amfqlengfn avngrmnqgr rlfgrqshvg wrspdghaii
      121 agrlydpltd lvqplqgdgf lgqtfstpgd vdnadasvrf nhaikwsspg mggfraagmi
      181 slggvagatg sglshgaals yrrgpfsaga gylrvdfgnp trarrgessa dalfnsavna
      241 ayesaasaqi vrvaaqyalg aitagayysd sryrpdgtsr farpqvyrna svygvwqvts
      301 altaelaynd lrasgdssar yqqlsggasy llskradlya magyahasgs ngrgaasavv
      361 gatavdaggp tqwrlnaglr hrf
//
LOCUS       WP_175948197             196 aa            linear   BCT 11-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175948197
VERSION     WP_175948197.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..196
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21008
     Region          6..180
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mnewagftda lriggwvvyp lsalaiiala itldrayvfw rftsgrgsaa ralperhvtr
       61 rlaaildqga tplwhveakl daaaqqverd msrglwllet ivtaapllgl lgtivgmmhs
      121 frliggdglv spagvsggia qalvataigl vialvslfaf nyfsrrvdrl mddlesfane
      181 qlaemrlare qagtss
//
LOCUS       WP_175948198             786 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia pyrrocinia].
ACCESSION   WP_175948198
VERSION     WP_175948198.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12149321
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..786
                     /product="TonB-dependent receptor"
                     /calculated_mol_wt=84753
     Region          32..112
                     /region_name="CarboxypepD_reg"
                     /note="Carboxypeptidase regulatory-like domain; pfam13620"
                     /db_xref="CDD:433354"
     Region          121..731
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mkinrlllsq aailafavfl qaeafaadag atlagtvadt qghalvhari tlqdadghav
       61 ahaqsgtdgh frfdnvapgt yvavvdapgy atgtsvstva qgkapapvdv tlgkdagtld
      121 vtvnakrldr arngllpevg asvyrfsrad ietlpqgent plnqvllqap gvaydsfgql
      181 hvrgdhanlq yrlngiiipe pisgfgqsld sriidqvnlv tgalpaqygy rtagvvdirt
      241 ksgdtgnggt idvyggnhqt iqtsadvfgs ngpfsyyfsg tlgennlgie aptsngnplh
      301 dhtrqgnafg ylsyllnpft raslmfgtts nrfeipntpg iapaftlngn stfdsaalne
      361 tqaelnnfav lalqgtngga ldyqvalftr ytrtkfnpdp vgdlifngva sddfhsnran
      421 gvqadftyrl ndshtlragl mferehavfn nnvavfpvda ngnqlsdqpt tisdsndksg
      481 ylyslyaqde wkitpkltln yglridrmne yvqagqlspr iglvyqptes ttlhagyary
      541 ftppafelvs dstigtfngt tnqspstqnd pvkpershyf dvgitqrltp altvgldayy
      601 kkvsdlldeg qfgsaliftp fnyqdgrvyg leftssykqg nvsaylnvay sraqgknies
      661 aqfnfgpdel ayiannwvyl dhdqrittsf ggaytlgktt fsadgivgsg lrrgfantdr
      721 lpwyaqvnlg vlehfeepiv gkfdarvalv ntfgrvyqlr dgsgigvgap qfgprraiya
      781 gltkhf
//
LOCUS       WP_175948218             188 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Burkholderia pyrrocinia].
ACCESSION   WP_175948218
VERSION     WP_175948218.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..188
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=20348
     Region          110..186
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mqvvelppsa pptthaeska apmentvskp qplrpaqala pvrpaaavkr fdpvsshevl
       61 ptqqplaste tqtahatldd arsasatkad satthsasad ngqarlisqp lpelpddlre
      121 qgyqamavar flvhadgtfd ialvkptqnp rlnqilletl rrwrffpame ngrpvesqqd
      181 vrvhfnvn
//
LOCUS       WP_175948326             157 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia pyrrocinia].
ACCESSION   WP_175948326
VERSION     WP_175948326.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..157
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16788
     Region          1..143
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mytnimvatd gspcaqrald eglrmarscg arlfavfvvd kstlfayggr lepealldei
       61 rqrgaailrd adrtisraav ngeteiietd fgqdvaerlq qyvvdhaidl avvgthgrrg
      121 vrrlvlgsva erflrasscp vvlgrgedaa ratvaaa
//
LOCUS       WP_175948400             217 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175948400
VERSION     WP_175948400.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..217
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23027
     Region          1..209
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mqtlhieipv dyvtldgile ipddagavvv fvhgsgssrf sprnrqvaag lqhagfatll
       61 fdlltleeqh hddvdatyrf niallarrld atlawlaqrp dvgalqvglf gastgaaaal
      121 vsaagtsivg avvsrggrpd lartmlplvr aptllivgel dtevirlnqk aagqltcehr
      181 iaivagathl feepgaldev trlaagwfer wlsprps
//
LOCUS       WP_175948439             385 aa            linear   BCT 11-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Burkholderia
            pyrrocinia].
ACCESSION   WP_175948439
VERSION     WP_175948439.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..385
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40787
     Region          17..299
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mstfsgdaqs adkhavarks tlvsivlnvv latfqivvgt iahsqaliad gvhsisdlis
       61 dfvvlvanrh sgaspdadhn yghsryetva slflgailia vgigmlwrag drlvnlenip
      121 avhfsaliva ltvlvskeal frymlrearr vrsamlvana wharsdaass lvvaigivgs
      181 lagvrlldpi aaaivgfmva rmgwtfgyda lqdlsdrald tadtaeihal laatpgvrdv
      241 hdlrtrkmgd aalvdahilv dpkisvsegh yiaetararv lsdprvldal ihvdpendaa
      301 rrpalalppr geiasrleaa laqrglraaa inlhylstgl eidvtlvsdp gdtdaalagr
      361 ldadalkref garrigftrt vpaqa
//
LOCUS       WP_175948442             230 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175948442
VERSION     WP_175948442.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..230
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24217
     Region          1..227
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mtaqwidipt gndsfggyla lpkrgkgpav iiiqeifgvn shiravadqy aadgyvalap
       61 dvfwrtqprv eltyegadrd kgiellkktd vglavadiga aadtlrarpe vagklaaigy
      121 cfggqlayra aaagkldaav ayygggiqna ldlagkvtqp ilfhyaendh giplsavdqv
      181 kaafaghgha sfhvypgaeh gfnctdrasy nqraaalahg rtltflaehl
//
LOCUS       WP_175948484             226 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175948484
VERSION     WP_175948484.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..226
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24876
     Region          10..225
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mntltdvtrd rpaastisla drayaliqrd iitmrlkpga alneadlvar tgigrtpvhq
       61 avhrlvlegl lsvmprkglm vqplslddiv avidvrrine ahcaelaarh atpddlarma
      121 allddgqacv dthdvegmme ldrafhqaia aaarnavlte ilralhersl rfwfvtlsep
      181 hhladvqheh relferlsar daagaraave ghidsfrstl lqhlrp
//
LOCUS       WP_175948525             267 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia pyrrocinia].
ACCESSION   WP_175948525
VERSION     WP_175948525.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10508417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..267
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28428
     Region          10..251
                     /region_name="UPF0014"
                     /note="Uncharacterized protein family (UPF0014);
                     pfam03649"
                     /db_xref="CDD:427424"
ORIGIN      
        1 mspalqdlsl vdvgiaaalv aingaisaal slglgrklal aavrtvvqll aigyvlgwvf
       61 ghphwyvvlp ltalmtliag fagagrgkrt yrgqridsia siwfsswfva avglfvviri
      121 hpwfapqyai pilgmilgnt ltgvslgver mmeeltarrd rvetalalga trweaaqdaa
      181 rqavragmlp tlnqmaivgv vslpgmmtgq vlagqsplqa vryqivimfl iaaasalgtv
      241 gavlmtyrrl fsadhrflaa rleerah
//
LOCUS       WP_175948644             290 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175948644
VERSION     WP_175948644.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..290
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31425
     Region          15..280
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mttarsldrt ypalrttegg gfvvhrpfpt rllmdfdpfl lldemgpvdy apgeavgapd
       61 hphrgfetvt yaldgrfchr dssghagtlg pgdvqwmtag agvvhsempd pvfaqaggrs
      121 hgfqlwvnlp rrdkliapry qeipadrips atspdgrarv rviageafgv raaietrtpi
      181 lyqhftlepg atvaqpvpag yrvfaypidg tglygpdrqa vdarhmivyg ddgdtvtfaa
      241 gdtpldllli ggvplnepiv rygpfvmnte eeirqavvdy qtgrmgriea
//
LOCUS       WP_175948646             242 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Burkholderia pyrrocinia].
ACCESSION   WP_175948646
VERSION     WP_175948646.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..242
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24920
     Region          <36..>114
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          162..240
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mqashsapag vspaaprmnp rvivvavgvl aahavmltaa wlhrnapppk eievqsitaq
       61 litpapaaqp vavqsaaqpa ppkptprvkp kvepkptqka vkptpqpvaq spsptpvpaa
      121 adptpapaap apaapaatpg paretmqvsa pknvsalscn fvkptypsms rrrgetgtay
      181 vhfiigvtgk iesvqlqkss gyprldeaal datrastcpp yiengqaira ahtlpfnftl
      241 dd
//
LOCUS       WP_175948684             332 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175948684
VERSION     WP_175948684.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..332
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=36764
     Region          14..>256
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mdqpavtfde irgayalgqs gpprqvgerv whlptdgggv avklyaqehh araakeaall
       61 ahfemhgdar frvqtlkrtt ageplwtgtg shamltrwea grfrtydtfs paewealgas
      121 laalhlsler lhlpsldtir arlgaidada vrrslldala rsrsddgaan lhryvelalr
      181 midryypgsv eafpaddpqh pihndynqfn ylfadvgtpp plildweasi gapreyelvr
      241 clnhlpleap hlaeafvrvy rrvrpvdpar iawavdaacl qhalklwvvq gwlddpsrfa
      301 ahlngavtma samvdargrl vdffsrcvea gn
//
LOCUS       WP_175948837             309 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Burkholderia pyrrocinia].
ACCESSION   WP_175948837
VERSION     WP_175948837.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..309
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=34667
     Region          28..291
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mdeptlwlst pteayqqwqr teaagadrra fsprsivqhe amferfmrhl aaaqrslatf
       61 gpdhlesffa dldrrckpgt ttrlryqkll drlgrhlvdv gvrktnpaaa ytltqtwped
      121 epvpvyllka ddhrlqesva tldglderai rnraivalll atgitaqeir qattsdldls
      181 parphiliak rgprearrin ledfarpvle rwrnhtaaaa sallfpspra ggpmtdemlg
      241 rivrdellav dirvpdmspr tlrntfarrl llagrsnddv kdalgltsqr tviriratlp
      301 prpqaapqt
//
LOCUS       WP_175948875             382 aa            linear   BCT 11-JAN-2025
DEFINITION  epoxide hydrolase family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175948875
VERSION     WP_175948875.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..382
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42339
     Region          5..108
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          73..>199
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mhavpfniei pdhaladlrr rlrdtrvpll tpaepwqqgv dgawlrdlta ywaerfdwra
       61 veqalnrlpq fvadvggqrv hfihrrgagp npyplvithg wpgsvfefda lierlcdpaa
      121 fggdphdafd vvvpslpgfl fspppaapgv aafqvadcwa almaglgyrr fgaqggdlga
      181 gvsialgarh advvdgihln ylpgsyepai daaapltdee rafvkeraew aaleggyahv
      241 hmtrpqtlaa alndspagla awiaekfraw sdcdgdvarr fshdtlltgi slywfsacig
      301 ssmqmywenr lqpmrfaagq rvtvpiafar fpkeisrppr swvervfevv qwtdmpsggh
      361 faameepdll addirrffrr fr
//
LOCUS       WP_175948878             282 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia vietnamiensis].
ACCESSION   WP_175948878
VERSION     WP_175948878.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 282)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..282
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30565
     Region          23..158
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          197..278
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msrsarpaav pspfwrdtal pfiearsvdd grsicyakht hdtfslgaiv ggtstylnga
       61 skervgrgvl vivdpeqvha cnpdgadawa yrmvyvdvpw larlqhslgr spncdfhgfa
      121 akatqrrdlf aqfggfyrtl vaaevdplgk esaaveffta lhraldralp agrrpgadna
      181 klaraadyia ahcrqavtld aicaaaglsp sylirafnar ygmtphafli drrvqygrae
      241 lrrgrsiadv aldagfadqa hfqrafrria aatpgqyrsa as
//
LOCUS       WP_175948957             165 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia
            vietnamiensis].
ACCESSION   WP_175948957
VERSION     WP_175948957.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..165
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18113
     Region          4..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 magitlddld lrilailqdd asvsnlqlae ralsspptcm rrvrrltvag virrqiavld
       61 pvaigtavta lieisldrqt aedydafeay vcaepsvtqc yrvspgpdfi vvadladvae
      121 ydafarrlft gasnvrnvrt ffsthrakfd anarvahamr krrdd
//
LOCUS       WP_175948959             485 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175948959
VERSION     WP_175948959.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..485
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53011
     Region          74..449
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mierrisirl iagavalvvl agcttfsrdg gfntvsttas erlgkealfv rteqdrdava
       61 qrtrellgkp lamddavqva llnnaglqas yaelgisead lvqagrlpnp gfsfsrthws
      121 dnfgitrtfs anvlailtlp latriesrrf eqtkletada mlkvaadarr ayvsavaaeq
      181 sakyaeqvkd sasagaelah rmqqagnasr ldyarqqafy adaatqvaka rqqafaarek
      241 ltrvmgvwga atqyslperl pdlprerpel kdlevfamqn rldiqaarlr tqgvatslgl
      301 skatrfvnal evgylnnfet dkghergyei sveipifdwg sakvaraeal ymqsanklaq
      361 tavdarsevr esyvayvtny diarhyrdev vplrktisde mllryngmla safdlladsr
      421 eqvnavngyi dalkdywlae tdlqlalggr lpppdrpvda parsteqsat aaatlaapht
      481 qsegn
//
LOCUS       WP_175948995             236 aa            linear   BCT 11-JAN-2025
DEFINITION  PadR family transcriptional regulator [Burkholderia vietnamiensis].
ACCESSION   WP_175948995
VERSION     WP_175948995.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..236
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25547
     Region          82..161
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mrhspfdgda rcrghghhpg lewfaslrha igrhrrghdp fgggpsggrg grggfgdfgd
       61 dgmprgrqfs sddlqlllla lvaeqpshgy elikaldtrs ngfyspspgm vypaltylee
      121 vgfvvsqaeg nrkryaltda grahleaqre rvdtlfarlt hlarkmefmr rafagesags
      181 eaaddaqagw lpefvaarla lkrallhksa adadeqrria aimrrataei eggsga
//
LOCUS       WP_175949044             279 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175949044
VERSION     WP_175949044.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..279
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28326
     Region          17..258
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mnltegvlvs alhglslpdl agiavalllg gmvkgitgig vplvampils qflpirdavl
       61 llsmpiilgn ipqaleggql latarkiaap ivgtvlgniv gvvillamna rhaqaasgll
      121 livaaalmls apkltlppaw qrpvgfvlgf gaalmesias vpgpllatyl isagatgraf
      181 tkqiaiilvv sivtlittfs gaahasgadl aistaasvpa iagmwlvrpl rdrmsprvfr
      241 tvvllfvlaa aaqmiwksav lrpaaaptah adrarvdgi
//
LOCUS       WP_175949125             632 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Burkholderia vietnamiensis].
ACCESSION   WP_175949125
VERSION     WP_175949125.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..632
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=67791
     Region          8..632
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mpqpfvlpaa agrndllaqa harstalglr aderpdfspl srlalrelld tnhalfahar
       61 pvmenlhaqi adtqslvllt dadgvilhsi gdadfiekan rvalctgvsw aegtrgtnai
      121 gtalasgqav avhgdehflr anhiltcsca piidpfgrtl gtldvsgdpr gfsphtlalv
      181 rmsaqlienh lfanrcaeal rlrfhahedc vdslfaglva fdrdggliaa nrsaqfqlga
      241 tfdalqhrgc dalfgmqfnq laqqaarapg apfqltlstg vrvlarcefa earkttvavt
      301 ppapapvaar pravdpeait fatldtgdar maavldrvak irgrdlplli lgqtgtgkew
      361 laralhqasp radgpfvavn caalpdslie aelfgyedga ftgarkrgsp gkiaqadggt
      421 lfldeigdmp laqqvrlmrv lqeravmplg garavqvdvr vvcathrdlr amiaertfre
      481 dlfyringla vtlpplaart dlsvlveril arlahsepmp trvaadvlda flrhrwpgnl
      541 rqmtnvlrta gmlaedeaei tlahlpddfw ldcedapats papagtraat tlqshqaavi
      601 davlarhggn vsaaarelgl arntvyrylr rh
//
LOCUS       WP_175949126             209 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia vietnamiensis].
ACCESSION   WP_175949126
VERSION     WP_175949126.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..209
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22253
     Region          1..207
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msvqtwmlfa aaylattlsp gpnvllvirn tvrygshgta atiagnlvaq gavvglvalg
       61 vgavlaampp lfvamkvvga aylifigirq lrgdrhrrap dsgatsvepd rsklfrealf
      121 vsgsnpktmi flsafmpqfi shdrplamqf vamyatiact vivvhslysf gvrrlhrgfg
      181 vspwlraakr asgllfvalg iklltarqa
//
LOCUS       WP_175949127             441 aa            linear   BCT 11-JAN-2025
DEFINITION  leucine-rich repeat-containing protein kinase family protein
            [Burkholderia vietnamiensis].
ACCESSION   WP_175949127
VERSION     WP_175949127.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Shen,K., Hines,A.C., Schwarzer,D., Pickin,K.A. and Cole,P.A.
  TITLE     Protein kinase structure and function analysis with chemical tools
  JOURNAL   Biochim Biophys Acta 1754 (1-2), 65-78 (2005)
   PUBMED   16213197
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
REFERENCE   7  (residues 1 to 441)
  AUTHORS   Hanks,S.K. and Hunter,T.
  TITLE     Protein kinases 6. The eukaryotic protein kinase superfamily:
            kinase (catalytic) domain structure and classification
  JOURNAL   FASEB J 9 (8), 576-596 (1995)
   PUBMED   7768349
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..441
                     /product="leucine-rich repeat-containing protein kinase
                     family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=46955
     Region          <2..>193
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          39..61
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          62..84
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          85..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..175
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          214..433
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(214..217,220,222,238,240,269,287..290,345,349..350,
                     352,362..363)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
ORIGIN      
        1 mtttlerlqs gqlsgarelk lacgltefpr eifdladtle vldlsgnals tlpddlarlh
       61 rlrilfasgn rftefpaalg acpqldmigf kanrirtvpr galpralrwl iltdneidal
      121 padigdcsrl qklmlagnrl ralpaelaac ralelvrlsa nrldalpdwl lrlprlswla
      181 aagnplgagp eaaasaepgv aeidwaslac ehrlgegasg viyraqwrae gratravavk
      241 lfkgavtsdg lpdcemaacl hagrhpnmip vigklrghpd gahglvmelv dpaltnlagp
      301 psfasctrdv yaadarfapa daarlahgia svaahlharg imhgdlyahn ilhdgaggal
      361 lgdfgaasly dvnervraar ferlevrafg yllrellerc eprawaaaqa lgalaaacvn
      421 devdarpsfe qivaalaatm d
//
LOCUS       WP_175949145             731 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia vietnamiensis].
ACCESSION   WP_175949145
VERSION     WP_175949145.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..731
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78160
     Region          62..731
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 msfrrplrra ralrpwragl palitlcvag gahaqaqraa pasaasaada aspaappaae
       61 relpaisvsa savadptvgy qprtssiagg ddralkdipq siavvssavm edqhansldd
      121 vlgnvsgitq tntlggtrda fikrgfgsnn dgsvlvdgvr tpvlhsylat idrvevlkgp
      181 asllygmqdp ggvinlvtrk peaefggsis asrtshggss aqfdltgplg kpgqvaggtl
      241 afrltgeydt srywrsfgre rdaliapals whdantsidv ayqyvdyttp fdrgtvlvng
      301 rpddalryrr yeeawsqsag iqetlrarie hrfsdawrvr atygwgrdry dqyltrataf
      361 nsktgaltrs sdanlgrnda dqiatlgllg nltlagmhha lyiggeyelq rsfrgdtirg
      421 tatkgfdlyd pvygllapgg tvsakqsdsl skvhaysmiv qdtvklterl tasaglrwed
      481 wqqesgmgrp fvfadrshgn vwlpqfglay altpsltaya nvsrsfkpnv asnvaaplap
      541 efgrvleagl kfsmtpaisg tlaayqidkr nvavtvgdlt stigtarsrg ieldvagqlt
      601 rhlsligsya ytnandrdsn tplanvarht gslfavydta ianlpgrwrf gggarlvgar
      661 pgdtansftl pgyvtvdafa ayetmvgkfp triqlnvknl ldktyypssn snlivavgep
      721 rlvtltttvs f
//
LOCUS       WP_175949214             540 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia vietnamiensis].
ACCESSION   WP_175949214
VERSION     WP_175949214.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 540)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..540
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58925
     Region          9..537
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msaidasqpg epllslehlh vrfgdtvave dvtlaigrge rvalvgesgs gksvtalsil
       61 rllrdadvsg tirfagqdla gkseremrgl rgsdiamifq epmtalnply tvgaqiaeti
      121 vlhdgvtage arkrtialla rtgiaepekr vdsyphelsg gqrqramiam alacrprlll
      181 adepttaldv tiraqivdll lelqrdeaek rgmaillith dlnlvrrfae rvavmehgrl
      241 vesgpverif aqpehpytqr llnsrpqrtv apvlpiapvv ldarhvsvqf arkrpglagw
      301 fgtlpvtavd dvsvsvrqge tlgivgesgs gkstlamall glqrtvagei efqgralsty
      361 rgreqtalrs nmqvvfqdpf sslsprqtie rivgeglelh rpelsadarr aksltvlrev
      421 gldrtvlhry phefsggqrq riaiarslvl eprilildep tsaldvsiqq qvlkllanlq
      481 qkynlgyvfi shdlevigam ahrvavmqgg avvesgdvad iftrpshpyt qkllkavwka
//
LOCUS       WP_175949220             397 aa            linear   BCT 11-JAN-2025
DEFINITION  ammonium transporter [Burkholderia vietnamiensis].
ACCESSION   WP_175949220
VERSION     WP_175949220.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..397
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41451
     Region          1..395
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mdglksgvdt lflligavmv lamhagfafl elgtvrkknq vnalvkilvd fsvstlsyff
       61 igytiaygve ffddigslsq hngyalvrff flltfaaaip aivsggiaer akfnpqlvat
      121 miivgfiypf fegiawnerf gvqawlthaf gapfhdfags vvvhafggwv alpavlllga
      181 rhgryakdgr iaahppsnip flalgawvla vgwfgfnvms aqtldkisgl vavnslmamv
      241 ggtlaawmag rndpgftyng plaglvavca gsdvmhpiga lvtgaaagal fvamftcvqn
      301 kwriddvlgv wplhgmcgal gglaagvfgm palgglggvs fmsqligtlg giaiataggt
      361 lvygalkatv glrldreaef dgadlsihri satperd
//
LOCUS       WP_175949230             264 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Burkholderia vietnamiensis].
ACCESSION   WP_175949230
VERSION     WP_175949230.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..264
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28239
     Region          25..264
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mlrrfmlkfa aaisaaalfa sahaqaetik vgvtggphaq imeyvkkvaa rsgldirive
       61 fsdyvqpnaa laagdldans yqhdpylqaq vkdrgyklik vadtvtfpmg iyskrvksla
      121 elapgarvav pndptnggra llllqkqgll klradaglka tpldivdnpr klkiveldaa
      181 qiprslgdvd aaaintnyam eaglkpkqda iaiegpngpy anvlairead rarpwvaklv
      241 aayrspevkq fieqkfggav iaaw
//
LOCUS       WP_175949245             156 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia vietnamiensis].
ACCESSION   WP_175949245
VERSION     WP_175949245.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..156
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16015
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 myrrifaald gsrgsrlald eaislaresg glviamcvvs daprltdvds gyveqrdpag
       61 ldadkaaiai adaetafqls gvrgiaqtve angqdisdvl araaaecdad livmgthgrr
      121 gvrravlgsv aeallrdadr pvlvvregpg agagml
//
LOCUS       WP_175949251             267 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia vietnamiensis].
ACCESSION   WP_175949251
VERSION     WP_175949251.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..267
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28420
     Region          4..261
                     /region_name="FetB"
                     /note="ABC-type iron transport system FetAB, permease
                     component [Inorganic ion transport and metabolism];
                     COG0390"
                     /db_xref="CDD:440159"
ORIGIN      
        1 msptlqdlsl vdvgiaaglv aingaisaal slglgrrlal aavrtvvqll aigyvlgwvf
       61 ghphwsvvlp ltalmtliag fagagrgkha yrgqrvdsia siwfsswiva aiglfvviri
      121 hpwytpqyai pilgmilgnt ltdvslgver mmeeltarrd rvetalalga trweaaqdaa
      181 rqavragmvp tlnqmavvgv vslpgmmtgq vlagqsplqa vryqivimfl iaaasalgtv
      241 gavlltyrrl fspdhrfias rleerks
//
LOCUS       WP_175949277             522 aa            linear   BCT 11-JAN-2025
DEFINITION  S41 family peptidase [Burkholderia vietnamiensis].
ACCESSION   WP_175949277
VERSION     WP_175949277.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..522
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55779
     Region          74..438
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mipvklairr vaasrtgait aavfiafafe lapaalaqtv pasattatta lpapaaaplp
       61 spcppdweaq lcelkaaiev lkkqhltdvd igalldatvh agiktlpyar ffnaaerrqq
      121 ldderrardg tpgigivfet rpdglhiidv ipdapaekag vrpddlvvam ndqsvvglds
      181 advvklakgd agvplkltir rgpgqatlvv apvraivrph pasakrlagd vlytrlssfp
      241 epavgnyvda veaarrngpp pkgvildlri ngggalnaai gitalfagre rtamvtlerd
      301 grnrrrittn wpdyelpvmh gqdplaplqa ddwwrtvplv vlvdgqsasa aeataaalrd
      361 lgrarllgmp tygkglaqtg vdlidgtrln ltfarnlrpn gcpmdgygvv pdwlvpprrd
      421 sdvdgvllwy revdlarapy adrlapdpfa tvrdarrklr darvrakvem sksaalpqre
      481 fgtaadwqlr qalaalagrp vqtvaapaql mpaqpvcerr dd
//
LOCUS       WP_175949369             318 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Burkholderia vietnamiensis].
ACCESSION   WP_175949369
VERSION     WP_175949369.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..318
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32856
     Region          3..296
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(36..37,40,91,105,107,136,168,256,259,295)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(227,232,247,256..258,261,283,287)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 maeivivgel laefvalerg qgfdapglfa gpfpsgapai fadqaarlga rvayagcvgr
       61 dafgdaivar lerdgvdvar irrverptgt afvayrddgs rsfvfnlats aaacldagdv
      121 daamfdgcry fhvmgsslts eaaiaavqrg vieaaragak vsfdpnvrpe mlsfpplraa
      181 ldamlaachl flpsdadlpf fcgpqpaera iagllathsl lervvlkrga agsaafdrts
      241 rvdapawpvd eldptgagdc fggtlvaslv agmptdaalr ranaagaiav trrgpmegns
      301 daaeierflt ergvacpa
//
LOCUS       WP_175949432             307 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Burkholderia vietnamiensis].
ACCESSION   WP_175949432
VERSION     WP_175949432.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..307
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=33994
     Region          28..290
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mddptlwlsa ptdayqqwqr tqaagadrra fsprsivqhe amferfmrhl taaqrslatf
       61 gpdhlesffa dvdhrcrpgt ttrlryqkli drlcrhltei gvreanpaaa faltqawped
      121 epdpvylpdg ddaclqayla savpdgtalr nrsivgllla tgitakevrl akadeldlqs
      181 lrphldvpkr garearrigv eafaqpalgr witqipatea gllfpsprsg gpmtdatlgl
      241 ivrdallaid vrlpdmsprt lrntyarrll lrgrsnedvs rllgltsqrt vvrlrativp
      301 dqvhaqt
//
LOCUS       WP_175949441             568 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent helicase [Burkholderia vietnamiensis].
ACCESSION   WP_175949441
VERSION     WP_175949441.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..568
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63031
     Region          1..564
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mldelnpqqr evallrrhcl aiacpgagkt ktiaakaarl lddptamvga vtfskdaave
       61 lrdrilavag pgakrrliag tfhslafrql gqpgrerrdi asdgdrlgml grvivelgld
      121 wkveeavpii eriktnfgqv eagtadaqly nayqdalern gkidfqdmlr lavagmerne
      181 irpysftdll vdefqdtdpl qyrwvelhar agahvtvvgd ddqsiygfra algyrgmerf
      241 agtfdaqkiv lgsnyrcrae ilsaadrvir nnadripkvl raergegggv gsqrfedeya
      301 davaavealr pvlaagksca ilartnrild pieavcrshg vpyyrasggs vlnrpqgalm
      361 cnlleivegr kqngvdavla hmgmsshdla mlhrdmgaef vqrqkkdlva lglsedtata
      421 yrafmkrlae wqslcerefy slalegvfew mmsyakgdqa iraiqgtydv isrlnglfse
      481 ridflkrdnn kpvdgalvlt tmhsskglew dhvwisraee gvvpdekspe seerrlfyva
      541 mtrardrlvi stikknpvsr fvieskid
//
LOCUS       WP_175949519             422 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia vietnamiensis].
ACCESSION   WP_175949519
VERSION     WP_175949519.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..422
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=44850
     Region          <222..359
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mwtplvkpaa tpdafapgra qrlvralvpa avlgalaafg laaalpavsq lpgavdsgta
       61 vlpqrvlsdt pfptaqhfvt selahtiger hafaersaqp glfaslsahr ndmlgypnlf
      121 qyaepdrshg mragdieltl sdtldrldvp pevriqlgdl vtgkvamras aqrgdyyria
      181 ydtnngtphl tavelrvagr rfgaiwfhap gaehgayytl dgapleaaaf tmpvkwtris
      241 sffgervhpl sqamafhtgv dlaaptgtpv daaadgvvsf vgtdpggygh yvivdhadgy
      301 styyahlsay arglkvgetv kqgqrigsvg mtgaatgphl hfevriandp vdplvtlasa
      361 qtelsdmqrt afrqeaaqwr frlasigttp fafaqgdgpl wgdfavgpst lrsvfdthyg
      421 ts
//
LOCUS       WP_175949548             532 aa            linear   BCT 11-JAN-2025
DEFINITION  multicopper oxidase family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175949548
VERSION     WP_175949548.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..532
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=57492
     Region          86..532
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mirrtflsha igvaaaslfa rsawaqhaah agmvgmepmd dmpgmagmad haqhakpapa
       61 alaavdalpa gaplaplrtl anesgeagtf ratlvaqpva rpmlqhahpt tfwqfgagta
      121 gpvvgplidv hegdtveirf vnklpqpsti hwhglpvppe qdgnpsdpva pgasrvyrft
      181 lpkgsagtyw yhphphmmta eqafrglagp fivraaddpl agwperhlfv sdlklardgs
      241 ippndmmdwm ngregqfalv ngerrpridv agderwrvwn acsaryvcva fddgrafehv
      301 gtdgglfetp rrvtslllap geraellvra gdrasravlq aaeydrrkma mshdggrgsl
      361 ppdpalplad vtfvpaaara lpatlravpa pgepvadkdv algeamdmna mmsgpahgrp
      421 agmrfminga tyaphratlt srrgelerwt irnttdmdhp fhlhgtqfqv terasggtrt
      481 aepfrawrdt vnvrsgetvt llvkqdmpge rmfhchileh edlgmmgtlk vv
//
LOCUS       WP_175949649             328 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175949649
VERSION     WP_175949649.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..328
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34485
     Region          7..236
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mndlndrpvr fgivgagsia hrfaqslshv pgavlsgvwa rradaaiafc nscggtpaas
       61 ldallasdid avyiatlhds haqyaqaala agkavlcekp atlnaaqlda vldaarvagr
      121 lfmeamkppf fplyrrlrah ldddpigeir lvragcasst vpaehsvyrl draggalldi
      181 giyeaflavd wlgavhdvqt lgrvgatgvd vfaslnsrha nggiaqlfcg ldvmgrgdal
      241 laaagghvti hekwwnpara tiryadgrtv eldapveggg lnyetahfce llragalesp
      301 imthdhsrqm iamtdaaraa lgvrysgd
//
LOCUS       WP_175949710             344 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia vietnamiensis].
ACCESSION   WP_175949710
VERSION     WP_175949710.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..344
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36230
     Region          109..316
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mkivkpllia avvaatwsga saataasaqa vlpdtatsaf lavlngqkgp gletlspeka
       61 rqvlvdaqsg vkvdlsgidv snrtieqdgl svpitivrpq qvsgtppvfm ffhgggwilg
      121 dfptherlvr dlvvqsgava vfvnytpspe ahypvainqa yaatkwvaah gaeigvdgsr
      181 lavvgnsvgg nmaavvalma kdkggpairf qgllwpvtdh dfntgsygay aqghfltrpl
      241 mkwfwnaytk neaqrdeiya splrasvaql kglppaliqv aqfdvlrdeg eaygrkldaa
      301 gvdatttryd gtihdfglln alandaptka amkamgneia vrlk
//
LOCUS       WP_175949767             255 aa            linear   BCT 11-JAN-2025
DEFINITION  TatD family hydrolase [Metamycoplasma hominis].
ACCESSION   WP_175949767
VERSION     WP_175949767.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma hominis (Mycoplasma hominis)
  ORGANISM  Metamycoplasma hominis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Metamycoplasma hominis"
                     /db_xref="taxon:2098"
     Protein         1..255
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29271
     Region          3..253
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mkfidlhthp steyysdple ivnewhnlnm eklfvcgtne ddsiqaiela kkvdfvypvi
       61 gihptlsngl qdreilnkiy epnvvaigev gldyhyddsp skeiqkqgfi aqidfakehn
      121 lpvimhirda lddsldiitl pqykdinfif hsfsgdlsfl nkcltysniy ysisgvvtfk
      181 nakplqeavk nipldrifce tdtpylaptp mrgkpnispf vqytyeyian lkqidvdvlv
      241 eqikknvrkv fkiyd
//
LOCUS       WP_175949957             469 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Metamycoplasma hominis].
ACCESSION   WP_175949957
VERSION     WP_175949957.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma hominis (Mycoplasma hominis)
  ORGANISM  Metamycoplasma hominis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 469)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Metamycoplasma hominis"
                     /db_xref="taxon:2098"
     Protein         1..469
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54883
     Region          14..444
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 menkiktpnk neepiiqlvd vvkefedktv ldnvnlsink gefitllgps gsgkttilri
       61 iggfewvtrg evkffgkdik dlsphkrdvs tifqdyalfp hlnvenniky glrlkripkd
      121 dipksfynkl kyqqkkwtkk asiemkkldk tmaqyekile nqklpekkrn kyqswiddmd
      181 fkysywenfk dlktenyekr yltrkitnne mnqevseimd lvglkgnekk nvnflsggmk
      241 qrvalarslv iepeilllde plsaldakir qkmqtllrdi qkelkitfif vthdrnealq
      301 lsdriaiird gkveqfaspk dlydypinkw vanfigesnf fdavfidenk vkfmgkifdt
      361 ihkefepgen ldalirpedv yvtkvkaksk figkiiksty sgsyynyevl vknkiikmet
      421 sinyevgkev yldwykdsih lmkkdikfak elaeqneinn gktteinfl
//
LOCUS       WP_175949961             635 aa            linear   BCT 11-JAN-2025
DEFINITION  M13 family metallopeptidase [Metamycoplasma hominis].
ACCESSION   WP_175949961
VERSION     WP_175949961.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma hominis (Mycoplasma hominis)
  ORGANISM  Metamycoplasma hominis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Bland,N.D., Pinney,J.W., Thomas,J.E., Turner,A.J. and Isaac,R.E.
  TITLE     Bioinformatic analysis of the neprilysin (M13) family of peptidases
            reveals complex evolutionary and functional relationships
  JOURNAL   BMC Evol Biol 8, 16 (2008)
   PUBMED   18215274
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Turner,A.J., Isaac,R.E. and Coates,D.
  TITLE     The neprilysin (NEP) family of zinc metalloendopeptidases: genomics
            and function
  JOURNAL   Bioessays 23 (3), 261-269 (2001)
   PUBMED   11223883
REFERENCE   3  (residues 1 to 635)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10171382
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Metamycoplasma hominis"
                     /db_xref="taxon:2098"
     Protein         1..635
                     /product="M13 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=73090
     Region          9..633
                     /region_name="M13"
                     /note="Peptidase family M13 includes neprilysin and
                     endothelin-converting enzyme I; cd08662"
                     /db_xref="CDD:341056"
     Site            order(34,436,441..444,463,479..480,483..484,487,543,573,
                     576..577,594..595,601)
                     /site_type="active"
                     /db_xref="CDD:341056"
ORIGIN      
        1 mnkklipidf fdavnkkwvd shkipdskts igcfaqldkn ittltkkiln twsedastip
       61 ndpiinelvk fysltknwkl ryqaqlkpik kllskinsln swkdvennfl elklsslntp
      121 lifsvstdfk nsdvqtlyld vnstilpdks fytdpakkek finvwknmvl kllnkidkne
      181 sknnliiena lkwdeltssf lrdsefyfdm vkicntistk elaqniktin ienilrqlik
      241 cfpdeinaid pnsiniaksl tneenfeyyk asliidailt yapyfdysti qiasefnlai
      301 ngnkkieske kyqikqakrf fdipfgtyyg ktyfglknkq tvehmiksmi dvykeqltkn
      361 swlskqtkek aiiklnsigv yvgfpekiqd hykyliveef dgyndlfenv lkfnrilaeh
      421 ilseygkted knlwhmspam vnayynpskn vivfpaailq kpffsadqss ssnfggigav
      481 iaheishgfd nnganfdekg nminwwteed kkafeiktke minlfegret svgkcngtlt
      541 vseniadagg lscalaaakl ekdynpkdfy infatiwrtk yrpelqslll tidchapakl
      601 rtnvqiqnsd dfyttfnvkk gdpmylppek rvkiw
//
LOCUS       WP_175949981             610 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Metamycoplasma hominis].
ACCESSION   WP_175949981
VERSION     WP_175949981.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma hominis (Mycoplasma hominis)
  ORGANISM  Metamycoplasma hominis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Metamycoplasma hominis"
                     /db_xref="taxon:2098"
     Protein         1..610
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=70465
     Region          49..>188
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mktalnnyhn flfkvtakkk stiiipiill lcslilcfvf vgtkpapryf nviifaytlv
       61 ailftvlygs lkslnifkdl eqdgieliif skpisrkaii wgkilsfnsl gliwtlfafv
      121 ssiivysqvs kgnmfgylvl lalvahflay tifgyiaali aykvnqkiai tvpiiifapm
      181 aigggfifan ststnenfah yinskykyhr agnevnsevf ylnknddkyy lvpnginnnk
      241 fsdvqnqyln lawkysnssa newqkyswla mpyqfvdifn ienqnifsnl ssdsinnsls
      301 nylyyknqen tiykyklnrn sdllklptle nktkinkyyv pgmlnlnsni dnevnngviy
      361 arknasnfsa sfeednfvya spnnlvgklk wkimsqvlky hkfteaaeef yskvkneisl
      421 kklvkphdik kllletisne vnntnskffn idnvnlavfd phgvrdgrlq seterkiyia
      481 tallyfiyfk dnqgqviksl lksesdktty apsqieikvd gyiyeiggye syepkqqvqe
      541 nkitknkqvv vryelipsnk nylfqtvddv ysierdrkiv nkqfyiliwi vvaiilmman
      601 rflylrkdyk
//
LOCUS       WP_175949983             966 aa            linear   BCT 11-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Metamycoplasma hominis].
ACCESSION   WP_175949983
VERSION     WP_175949983.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma hominis (Mycoplasma hominis)
  ORGANISM  Metamycoplasma hominis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 966)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 966)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 966)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 966)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..966
                     /organism="Metamycoplasma hominis"
                     /db_xref="taxon:2098"
     Protein         1..966
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=106930
     Region          1..899
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mknskeqinn ipyvldetli ntnlktglss qeadlrlkkf gknelhkakk inpfliyleq
       61 fkdilviill faaiisyala ivsgtqnnwn wsingnrlli efieptiilf vvltnslvga
      121 iqeiksiqav ealsklsplq akvvrdgnli tlassditvg divliesgdv vpsdgyllfs
      181 snltviesal tgesepatkd yqakrnlala madrqfmvys stvvatgtay fvvtsvgenn
      241 eigkisklvn qqkesmtplq ikinklgkif gysglalfla slvtqivfha vsrnsfadtm
      301 fwgnaivgai slavaaipeg liaftsiila igvqrmarkn aivknlmave slgncavics
      361 dktgtltqnk mtivdafdgs qllsnnseik nflniielgs lccdanltrn ekdeyvvvgd
      421 pteiaflyel ekfsnfkykn nleieykrlh lfpfdsdrkm ksvinqndnn ywatvmgape
      481 iiiekcnfds pslkekylqi nnqwannayr vlaiarkslk ketiekfnel sisklqehve
      541 ndleivglva midppresak daitlckqag ikpvmitgdn lntakaiatn lgiysdqdra
      601 itgtelsnis deelvqniek ysvyarvkpe dklrivnawq qrkqvvamtg dgvndapalk
      661 asdigcamgi tgteaskqaa nviladdnfa tivsavangr siyqkiknvi qsllitsiae
      721 iillfiglfl fkaifssaew kvalgksdly imsatqllwi nlfthgfpai alglqdsked
      781 ymnrrpisky esifanqmgf ntlwkgilig ilslityyla alygknngfn aedilkaast
      841 csflvlgisa tfnsinlmtk ksifisnpiy ywkvyasvif slafllivvf vkninlvfgc
      901 yteihskpel lalglalplv iipiysihkl iiylieknki kenkitefkm ilppkqvkrn
      961 qknvdl
//
LOCUS       WP_175949780             278 aa            linear   BCT 11-JAN-2025
DEFINITION  RluA family pseudouridine synthase [Metamycoplasma hominis].
ACCESSION   WP_175949780
VERSION     WP_175949780.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma hominis (Mycoplasma hominis)
  ORGANISM  Metamycoplasma hominis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12894711
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Metamycoplasma hominis"
                     /db_xref="taxon:2098"
     Protein         1..278
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=32601
     Region          15..94
                     /region_name="S4"
                     /note="S4/Hsp/ tRNA synthetase RNA-binding domain; The
                     domain surface is populated by conserved, charged residues
                     that define a likely RNA-binding site; Found in stress
                     proteins, ribosomal proteins and tRNA synthetases; This
                     may imply a hitherto unrecognized...; cd00165"
                     /db_xref="CDD:238095"
     Site            order(26..27,29..30,32..33,36..37,39,46..53,55)
                     /site_type="other"
                     /note="RNA binding surface [nucleotide binding]"
                     /db_xref="CDD:238095"
     Region          84..266
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 minfkakkdd egrilfkylv kvcdnvpisr ierlfrekdi kvnnirvndk qykvkegdli
       61 siyglietsk hidnkantni nfkviyedkn lliidkapni amhseencld dqvlkylnfk
      121 kvssfrpasi gridkktsgl vvyaknyktl vefenkqnkf dkiyqfvsdf dedilditvr
      181 lkkdiknekm ivdnnfgvka qtifykegnr kfakiitgkk hqiratlayl ktpilgdiky
      241 ggkfakrmyl hsysikfhdl sddfkeyneq vficypkw
//
LOCUS       WP_175950144             323 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Metamycoplasma hominis].
ACCESSION   WP_175950144
VERSION     WP_175950144.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma hominis (Mycoplasma hominis)
  ORGANISM  Metamycoplasma hominis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Metamycoplasma hominis"
                     /db_xref="taxon:2098"
     Protein         1..323
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36603
     Region          87..307
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 makeikenkk eikaktnkis knknfvdeqt lqdlnlinis kqkkpfeikd egiaikvldn
       61 atlkkyrlan dkprkkdeya klqnsndniv evdnikktyl sgnvatevlk gitfsikkge
      121 ivvlygksgs gkstllniis aldrptsgnv ivnninlpyl sdakqtlfrr enisfifqny
      181 nllqnlnsyd nvetgsylqr dknkrlnikk lfedfdlsec mykypsqmsg gqqqrvsilr
      241 aiaknseilv adeptgalde ktgiivlknl qqinlkygtt iiivshdpdv aqiadkviyl
      301 glglikevkl qerkwlidre sqf
//
LOCUS       WP_175950218             278 aa            linear   BCT 11-JAN-2025
DEFINITION  RluA family pseudouridine synthase [Metamycoplasma hominis].
ACCESSION   WP_175950218
VERSION     WP_175950218.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma hominis (Mycoplasma hominis)
  ORGANISM  Metamycoplasma hominis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12894711
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Metamycoplasma hominis"
                     /db_xref="taxon:2098"
     Protein         1..278
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=32615
     Region          15..94
                     /region_name="S4"
                     /note="S4/Hsp/ tRNA synthetase RNA-binding domain; The
                     domain surface is populated by conserved, charged residues
                     that define a likely RNA-binding site; Found in stress
                     proteins, ribosomal proteins and tRNA synthetases; This
                     may imply a hitherto unrecognized...; cd00165"
                     /db_xref="CDD:238095"
     Site            order(26..27,29..30,32..33,36..37,39,46..53,55)
                     /site_type="other"
                     /note="RNA binding surface [nucleotide binding]"
                     /db_xref="CDD:238095"
     Region          84..266
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 minfkakkdd egrilfkylv kvcdnvpisr ierlfrekdi kvnnirindk qykvkegdli
       61 siyglietsk hidnkantni nfkviyedkn lliidkapni amhseencld dqvlkylnfk
      121 kvssfrpasi gridkktsgl vvyaknyktl iefenkqnkf dkiyqfvsdf dedvlditvr
      181 lkkdiknekm ivdnnfgvka qtifykegnr kfakiitgkk hqiratlayl ktpilgdiky
      241 ggkfakrmyl hsysikfhdl sddfkeyneq vficypkw
//
LOCUS       WP_175950289             170 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175950289
VERSION     WP_175950289.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..170
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18672
     Region          1..141
                     /region_name="CFF1"
                     /note="Predicted sugar epimerase, cupin superfamily
                     [General function prediction only]; COG3542"
                     /db_xref="CDD:442763"
ORIGIN      
        1 mpisatdlir qfdlqphpeg gyfcetyraa dsvvrpadga praastaiyy llcdgayssw
       61 hrirsdevwh fyvgdpievw vlderdglti hrlgnplthp gtvfqavvpa grwfgarcaa
      121 pehvalvgct vapgfefaef eladatalaa afpdyaehvv qlaqrqrtdr
//
LOCUS       WP_175950329             283 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175950329
VERSION     WP_175950329.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..283
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30139
     Region          23..275
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mrklllsvvl gcacaiasaq tvvhfpstdg ppstmldgyl fpapgagrhp alvflhgcsg
       61 mfaksgkiys rerdwasrfn aagitvlevd sfnprhhgem capghfvgei yrarpfdayg
      121 alkylqsldt vrpdrigvvg wslgggtvln airassparp aslpdgdfra avafypascn
      181 vkaqgavwqs avpllvlige ddvwtpyapc ktlfdsvapg teatfhaypa ayhdfdwpdm
      241 pvhampaftt kagvvpiegt epvaradaqq rvvefvsahl lan
//
LOCUS       WP_175950337             412 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0405].
ACCESSION   WP_175950337
VERSION     WP_175950337.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..412
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43740
     Region          17..395
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(27..28,31..32,35,69,124..125,127..129,132,152,
                     155..156,159,234,237..238,241..243,246,270,274,325..326,
                     330,334,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 msvpaagvfr slrgfnyrvw aigalvsnig twiqrtaqdw lvltqlthhd asavgivmsl
       61 qfgpqllllp wtgyaadrfd qrkllmatqa lmgglalllg lltvtgvaql whvylfaflf
      121 gcasafdapv rqtfvaelva drelanaval nstsfnaarm igpaaagfii asigtgwafl
      181 lnglsfvavl aslsmlrade lraharagrt rgslldgfry vwqrpdlkai lvmlfligtf
      241 glnfqlfist maasvfhvda rgfgvlssmm avgtitgall aarrdrprfr hlwigaalfg
      301 lgcmlaalap gywlfgaalv ltgvaaitfm nstnslmqls tepamrgrvm alrlavalgg
      361 tpigapvagw vanhlgprwa lgvgamsgfa aalvathflk rmraqdgagd gv
//
LOCUS       WP_175950341             319 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175950341
VERSION     WP_175950341.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..319
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35118
     Region          2..316
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhrigflisd gfqimalaaq svfeyanmgm sepfyamdny svdggdvrss lglpvatral
       61 hgriavdtwi vagvndpias papagvvafl rranvraqri agictgafvl aeagllaqrr
      121 atthwafgrd mrrcypeirv eedriyivdg piwtsagmta gldlalamve kdlgadaars
      181 vahklvmhqr raggqsqhse mlklapksdr iqnalnyarq hlgraltved laeavhlspr
      241 qfsrvftlet gqspakaier lrlenarlmi eqsrhpldvi akengfrdrr hmreafvrgf
      301 gvppqairre aragereta
//
LOCUS       WP_175950340             163 aa            linear   BCT 11-JAN-2025
DEFINITION  2,4'-dihydroxyacetophenone dioxygenase family protein [Burkholderia
            sp. BCC0405].
ACCESSION   WP_175950340
VERSION     WP_175950340.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14449000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..163
                     /product="2,4'-dihydroxyacetophenone dioxygenase family
                     protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17550
     Region          24..143
                     /region_name="cupin_DAD"
                     /note="2,4'-Dihydroxyacetophenone dioxygenase (DAD), cupin
                     domain; cd20302"
                     /db_xref="CDD:380436"
     Site            order(40..41,44,50,52,69,71,73,75,88,91..95,97..99,117,
                     123,125,133,136,139)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:380436"
     Site            order(64,66,81,102,118)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380436"
ORIGIN      
        1 mtqppaplst dlppisclpg dalpwlpmsa dlpglaikyl hinaaedtlt allkmpaggt
       61 lprhrhdgev fvhtlqgawr yreydwvaha gstvlepags vhtpetlgap gedvitlnvm
      121 rgdlvllddd gretarencr vallrqrkha rtapdaaapf vtr
//
LOCUS       WP_175950401             251 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175950401
VERSION     WP_175950401.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..251
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=27219
     Region          38..246
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mhdplaappd apadpadalp epgrlpalat lfgqcawfrt lapehqalvl aqshveqcea
       61 gdviahrlap seywigvhrg llklaifnas grgctfsgvp sggwfgegsv ikrelrkyev
      121 vaiqrstvlf vpadtfhall dtslpftrfv ihqlnnrmge fiasiqnsrl ldvdarvaqs
      181 laqlfnpdly pdtgpslsis qeelgmlvgv srqrinqalq qleklgalrl aynqidvvdl
      241 galarvgieq i
//
LOCUS       WP_175950409             356 aa            linear   BCT 11-JAN-2025
DEFINITION  AI-2E family transporter [Burkholderia sp. BCC0405].
ACCESSION   WP_175950409
VERSION     WP_175950409.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..356
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37639
     Region          16..355
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mgvhvpsspd paarprtqqv sravlyaall vialwvirdf ipaiawacvi aiamwpmlkr
       61 veshrlfrnr ptlialvita aisllvvlpv avaatqaigq ahdlrewlrt iqdngipvpd
      121 vvgrlpygaa qvtewwqanl ghplhaasam hgvngekfla fgrqfgtkla hgllefgfml
      181 vtlfvilrag hklsgallqg arrafgrsga aliermvsav fgtvtglvvv glgegallgi
      241 ayalagvpha allglvtaia amlpfcapvv fcgaalwlfv qgatvwavvv avlgfvvvfv
      301 aehfvrpvli gssarlpfll vlfgilggae tfgliglfvg palmtvltml waewia
//
LOCUS       WP_175950415             232 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175950415
VERSION     WP_175950415.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..232
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25883
     Region          21..179
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnakstvarp rgrrpsvddf dlrdhmldva mqlfaergia attvaqiaaa agvtsamvhy
       61 yftnreqlld aiveerlaqv iafvwrptep riesdpfalv aelvdrffdv trrmpwlpsi
      121 wlreivhegg llrermvrri pldhvgrfae rirgaqqagt lnpalepafl fhsiialvml
      181 plataklwqs arglppidrd vlhrhvrall gsglqppaaa prtqarsprs ps
//
LOCUS       WP_175950417             319 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175950417
VERSION     WP_175950417.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..319
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33960
     Region          10..227
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mnvppapyai dvdrlnkhfg dkhvvkdvsl rvargeifgf lgpngsgktt sirmmcgllt
       61 pdsgsgtclg ydivrdsaqi krhvgymtqr fsywedlsir enldfvarvy gmpdrkaava
      121 raldglglas radqltgals ggwkqrlala acmlhepall lldeptagvd paarrdfwee
      181 lhrlaaqgis vlvsthymde aerchklayi aygellaqgt saeivasqgl atraitgahl
      241 selsarlrtm pgvdqtvvfg salhvsgrdr arldatlaqv aaqaggpaal qvapidtgle
      301 dvfiymmgra sgqpggass
//
LOCUS       WP_175950442             355 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175950442
VERSION     WP_175950442.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..355
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38941
     Region          1..353
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mdklivddlh lsyganpilk gvsfelkage vvcllgasgs gkttllrava gleqpsdgri
       61 qldgrvffdg aqrvdlpveq rslglvfqsy alwphrtvad nvgyglklrr vapaeqkrrv
      121 qsaldqlglg hlaerfphql sggqqqrvai aralvynppv illdeplsnl daklreeara
      181 wlrelivslg lsalcvthdq teamamsdri lllrngrieq egtpaelyga prslytaefm
      241 gsnnridarv asidgervtl agdgwelqal ardtfapgqd aqavirlerv qvadgpganr
      301 lqvdlvtsmy lgdrweylfh cgdmrlrafg hvpraagkhw iefptndcwa fakag
//
LOCUS       WP_175950429             344 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175950429
VERSION     WP_175950429.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..344
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37093
     Region          42..328
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 msrttapala dahdgkrrtl lraagavala apaitlgrka wsapplkklt fawnqnafcl
       61 tpivvaqerg ffeknglkve linysgstdq llesiatgka daavgmihrw lkpleagfdv
      121 kiigsshggc vrllgakaag vttlqalkgk tvgvsdlaap gkhffsilla kngidperdi
      181 twrqypadll gvavdkgeih aiadgdpnly llekrsngay telatnlsge yarkvccvig
      241 argdlvrndr psaaalarsi vqatefthdn pneaakvfak yspkispedl rklyatltyd
      301 hhptnvdlqq eiafyaddfr risvlkkstd pqrfaqqvya nvlg
//
LOCUS       WP_175950467             130 aa            linear   BCT 11-JAN-2025
DEFINITION  TraR/DksA family transcriptional regulator [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175950467
VERSION     WP_175950467.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 130)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 130)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 130)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..130
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14369
     Region          3..121
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 msldplqrqt lkqrlneieq tlraeirase gqrasesyad lagaspdegd eanadlfvdv
       61 dhaliamklt elraigraqq rmrdgsygec idcdgsvgye rllarpaaer cthcqsiyer
      121 hyattpratl
//
LOCUS       WP_175950468             260 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175950468
VERSION     WP_175950468.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..260
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=28588
     Region          14..218
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mlhlhssysa naildalped sirtiaphle lvrikagllg rvgepmrhvh fpttsmmsvq
       61 hlmedgamve vaqvgregvv glaamvggaa ashrvevrig gmayrvpscv mraeferspq
      121 tyrlllnycq aamaqisrsa lcnrhhsvse qlsrwlllah dridgdelav tqqtianmlg
      181 vrregvteaa gnlqeaglir qrrgritvld rvglehhace cydliradyr rllgtrgtar
      241 ptpvrprmpe ahrgfparga
//
LOCUS       WP_175950470             398 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175950470
VERSION     WP_175950470.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..398
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42596
     Region          31..372
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msallpelaa dsdsrrldea ahavaqiaaq hadavdrdar cpveaieamr arrllgamvp
       61 phlggagasl ediasacsil gqacassamv famhqiqvac ivdhaldqgw hklflqqlvr
      121 hqwllasats edgvggnlra sqcaletdgg efrlrksapt isygdyadgi latarrdtda
      181 paseqvlvtl lrdgytltrr gewdtlgmrg tcsngfelda rgaavqclpv pfakiaeetm
      241 vpvshilwaa vwigvagdaf hrahqffraq arqtdgapsp asrriaesla lmqamqarvd
      301 nvlrlhanpa srswsagmar aaeintlkty vsttalevah qammicgmag ykqgtpfsig
      361 rhirdlhaap lmisndriav ntsnlllalr patlekht
//
LOCUS       WP_175950614             503 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia sp. BCC0405].
ACCESSION   WP_175950614
VERSION     WP_175950614.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..503
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53431
     Region          22..480
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mnhnserpad paggadsrha dpdamfashe agyakqlkpr hvqmiamgga igtglflgag
       61 grlqhagpal alvylvcgvf aflimralge lvmhrptsgs fvsyarefmg erasfvagwm
      121 yylnwamtgi vditavaiym kywavftdvp qwvfalgalg ivsvmnmigv kvfgemefwf
      181 slvkvgtlav flavgavfla sghpvggqmp gfhlvadhgg ifphgilpav livqgvvfay
      241 asielvgvaa getadarkvl pkainsvmwr ialfyvgsvv lltmllpwta ysahespfvt
      301 ffsklgvpyv gtvmnvvvlt aalsslnsgl ystgrvlrsl amggsaprfm srmnargvpy
      361 ggilitvain aigvplnyiv paqafeivln maslgiittw gfivmcqily rravdrgelk
      421 avsfrmpgap ftswltlafl vgvlvlmafd ypggtwtvat ipvvvlalmv gwklakrgta
      481 reqaadaras aaarvvadpa qga
//
LOCUS       WP_175950525             314 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175950525
VERSION     WP_175950525.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..314
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33364
     Region          11..294
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mtplvlhdas qdesaiaeri asamplmtpi hrrmgefvla npfraatmri delaqavnas
       61 iatanrfaka lgfdgypamr aalvrgfeat lgpverlrsa qeqepgvrga awidavfdqa
      121 vanientraq ldaadveaav eaivgarrvl ilgagssafl tglmehglsv chdnvqslal
      181 lggpshaarr lytadsrdlv ialafpryvk dtielarraa argarvlgis dgpqsplapi
      241 aslnlyvkae rrfaatseaa vlamiealid avalrthrsa ksaaemtefl lpwlvqpqat
      301 lpaanppshr pkkt
//
LOCUS       WP_175950616             324 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175950616
VERSION     WP_175950616.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..324
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35557
     Region          15..72
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          101..301
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(111,115,154,168,170,232,249,280)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(112..113,117..118,120..121,124,128,130..136,197,
                     226..230,237..238,241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mkrgardtgi dhmgamrafv rvvetgsfsa vakemhvsts tvarkitaie ealgvallhr
       61 sthsvtltea ghiyleravt liadlddtlr vvaelnaqps gplkltapva fgrrhlaplv
      121 apflarypti qldvrltdnh ndlvaggfdl dihegenyld nlvvhrlsrn dsilcatpgy
      181 ldrcgrpsap ddlkqhnclr yvhpegdprw alvngdahhs vlpagnlvtd hsellleatc
      241 aglgiaefei wlvrdllasg rleavlpryr lqnrltgeyi yiaylanrrs saklrvlkdf
      301 laehlahige lsereltkir gasa
//
LOCUS       WP_175950644             761 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia sp. BCC0405].
ACCESSION   WP_175950644
VERSION     WP_175950644.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..761
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81178
     Region          <34..181
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          176..742
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mnrsellarn gcltvirppa ppvkpapgqp gslssyvpal pevfvaildd grilafnghv
       61 dlgtgirtsl aqivaeeldv paarvtmvlg dtaatpnqgp tiasatiqis atplrcaaaq
      121 arhallalaa erfgvdpaql qiddatisan gqtatfatlv aahrialtld lntrtkdpaq
      181 yrivgrsspr vdlpakatgq ltfvhdmrvp gmlhgrvvrp pyaghdsgaf vgaslvdvdr
      241 asvadvpgrv avvaigdfvg vvaereehai raarqlrvtw rplpalpplg epaaaiaaap
      301 arrrvlldeg dvdaartqpn titlsrtyaw pfqmhgsigp scaladyrep gdgritvwsg
      361 tqnpvslryd latlvardea dfdvvrmeaa gcygrngadd vcgdalllsr avgrpvrvql
      421 sradehlwep kgtgqlmqvt gtvtrdgrll gydfttryps ndapllaall tgtiapeprv
      481 femgdrtavs pyasphrrfv cedlaplvra swlrgvsalp nsfahdafvd ecaaltgadp
      541 lafrlrhlqd trasdllqav adragwtprm rrtphepaps rlvrgrgiay aryvhsrfpg
      601 fgaawsawiv dlsvdrvsge iriervtvgq dtgtminpdg vrhqihgnvi qvlsrtlker
      661 vrfadgkvas rewasypilt faevpdvdvv lmprqgeppl gagesasvpg paavanalfd
      721 atgvrfyapp ftpetvraal rdagrlmtvd aagehlatga a
//
LOCUS       WP_175950647             435 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0405].
ACCESSION   WP_175950647
VERSION     WP_175950647.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46849
     Region          25..427
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(39..40,43..44,47,79,129..130,132..134,137,157,
                     160..161,164,259,262..263,266..268,271,299,303,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mstahpsaav spddalhgnl yrkvtlrlit lfclcyfaay ldriniglak lqmldalkfs
       61 dtvyglgagl ffagyilfev psnlvlqrvg aklwiarimi twgllsgatm fvhtpmqfyi
      121 vrfllgaaea gflpgvllyl tqwypdarra rivalfmvgl plssmigspi sgwimrafdg
      181 thglggwqwl fllealpsvl lgfavlrwlp nniesaqwlt adekhalran ldadpsgnks
      241 halgkafsdp kvwalglidl cvllglyavs fwlptilrdt gvkdayhigw lmvipnaaav
      301 latlycgass drarerrwhi vvpfmvsava laiaassshg tfgtvllfsl inagaaaamp
      361 vvwalpstfl kgsaaaggia facsianlgg fgstyfigwl rdtfhsqsag lygfaacmvi
      421 gcafalaypa rlvnr
//
LOCUS       WP_175950655             359 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175950655
VERSION     WP_175950655.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..359
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39857
     Region          12..194
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(15,17,102)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(49,101..102)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            100..102
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 msaharkplv slvvpfhded eaidaffatt lpilesvesv rfeivcindg srddtlgrli
       61 dvaagdprvr ivdltrrfgk eaaltaglde aagtavilid adlqdppali pamierwlag
      121 aevvaakrtd rmcdplmqrv aaalyyrvhn rlsevempen vgdfrlmdrq vvdalralpe
      181 rrrfmkglfa wvgyrteive ytraprsggr skfsgwrrwn falegitsfs tvplrvwtyi
      241 glafaalsfv ygafivmrtl lfgnpvhgya slisvmlfvg giqligigvi geylgriyhe
      301 skqrpvylvr rryhaqrdaa ahpastllqf plrrthaarr rtalpaaagh gaarqasvk
//
LOCUS       WP_175950657             142 aa            linear   BCT 11-JAN-2025
DEFINITION  TadE/TadG family type IV pilus assembly protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175950657
VERSION     WP_175950657.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..142
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=14442
     Region          8..137
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mtcgaagarh trgvvslefv lmlpfllmvl igiidtslil cdkavitnas reaaragvml
       61 rvpmltttqi anvaqtamqn slitggtatt pvvtvtqang ttsgtaltvt vtytysglvl
      121 gsafsaltgp vtvsatsvml ye
//
LOCUS       WP_175950661             482 aa            linear   BCT 11-JAN-2025
DEFINITION  CpaF family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175950661
VERSION     WP_175950661.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..482
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51856
     Region          91..471
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mtfgtrnrpp adpvpaatqa atqaatpgap pavtrepapa pipaaadmpa parapvaadt
       61 realirsskf dairtavfas mnmsaalmkt rdevragieq vaahtvdrer lkisageqvl
      121 ivdailndmf gvgpieplla ddtvtdilvn gpdqvyvera grleltslkf rddahvasva
      181 qriaaavgrr vdesspmvda rladgsrvnv vlppialrgp sisirkfakr ditlarmaqq
      241 gnisppmlqv lkvacacrln ivisggtgsg kttllnalsq hieqherivt iedaaelqll
      301 qphvvsletr penteglggi sqrdlvrnal rmrpdriilg eirgpeafdv lqamntghdg
      361 smttihansp rdaisrlesm vmmananlql lsirrqiasa vhlfvqierm rdgvrrvtri
      421 teivgmegev vitqdlfafr qegdttrdav kgvfeasplr pgfaaraayy gvedalaevf
      481 rt
//
LOCUS       WP_175950676             135 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF427 domain-containing protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175950676
VERSION     WP_175950676.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Lupas,A.N., Zhu,H. and Korycinski,M.
  TITLE     The thalidomide-binding domain of cereblon defines the CULT domain
            family and is a new member of the beta-tent fold
  JOURNAL   PLoS Comput Biol 11 (1), e1004023 (2015)
   PUBMED   25569776
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..135
                     /product="DUF427 domain-containing protein"
                     /calculated_mol_wt=14532
     Region          <41..129
                     /region_name="COG2343"
                     /note="Uncharacterized conserved protein, DUF427 family
                     [Function unknown]"
                     /db_xref="CDD:441912"
ORIGIN      
        1 mpvssdtsar pvktpgpdhp itvephprrv vvkaagkvva dtrralalre aaypavfyip
       61 redadlallq rtdhatycpy kgdaayysip aggeravnav wtyeapypav dairghlafy
      121 pdrvdsiees pagsd
//
LOCUS       WP_175950684             111 aa            linear   BCT 11-JAN-2025
DEFINITION  putative quinol monooxygenase [Burkholderia sp. BCC0405].
ACCESSION   WP_175950684
VERSION     WP_175950684.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..111
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12487
     Region          8..95
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mnepylqvia hfhakpgngd rviellaela ratrtepknl dyayfrsped pdhvvilery
       61 rdadgldvhr etphfqrigf gaiiplldrr evshymvqpd tgtatppggt r
//
LOCUS       WP_175950781             309 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Burkholderia sp. BCC0405].
ACCESSION   WP_175950781
VERSION     WP_175950781.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..309
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=34340
     Region          28..291
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mddptlwlsa pteayqqwqr teaagadrra fsprsivqhd amferfmrhl aaaqrslatf
       61 gaeqletffa dldrrckpgt ttrlryqkll drlgrhlvdv gvrktnpaaa yalaqtwped
      121 epvpvyllea ddrrlqdsva sldglderav rnraivalll stgitaqeir qaatgdldls
      181 parphllipk rgprearrin ledfarpvle rwmshtaaaa sallfpspra ggpmtdemlg
      241 rivrdellav dirvpdmspr tlrntfarrl llagrsnddv maalgltsqr tviriratlq
      301 pahqangat
//
LOCUS       WP_175950689             141 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia sp. BCC0405].
ACCESSION   WP_175950689
VERSION     WP_175950689.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 141)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..141
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15357
     Region          20..136
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04667"
                     /db_xref="CDD:467552"
ORIGIN      
        1 mpripapnta aeasaapvke rativchrge qvllvaraas rwalpggtik rgetpleaah
       61 relreetgmt gqplvysmqf tglakihhvf faevgpdhtp qanneiakck wfpidsvdgl
      121 rtsiptkriv elvyqheisk a
//
LOCUS       WP_175950841             213 aa            linear   BCT 11-JAN-2025
DEFINITION  carbonic anhydrase [Burkholderia sp. BCC0405].
ACCESSION   WP_175950841
VERSION     WP_175950841.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Lindskog,S.
  TITLE     Structure and mechanism of carbonic anhydrase
  JOURNAL   Pharmacol Ther 74 (1), 1-20 (1997)
   PUBMED   9336012
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10096752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..213
                     /product="carbonic anhydrase"
                     /EC_number="4.2.1.1"
                     /GO_function="GO:0004089 - carbonate dehydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23072
     Region          11..190
                     /region_name="beta_CA_cladeA"
                     /note="Carbonic anhydrases (CA) are zinc-containing
                     enzymes that catalyze the reversible hydration of carbon
                     dioxide in a two-step mechanism in which the nucleophilic
                     attack of a zinc-bound hydroxide ion on carbon dioxide is
                     followed by the regeneration of an...; cd00883"
                     /db_xref="CDD:238448"
     Site            order(33,35,42,44..46,58,61,83,88,98,101,180)
                     /site_type="active"
                     /note="active site clefts [active]"
                     /db_xref="CDD:238448"
     Site            order(42,44,98,101)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238448"
     Site            order(43..46,48,50..51,53,58..60,62,64,78..79,82..83,121,
                     180,182..183,185,187)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238448"
ORIGIN      
        1 mnhpksmlaa niawaretre rtagffdala rgqnprvlwi gcsdsrvpae aithsapgdl
       61 fvhrnianlf hpdddnsasv leyavrvlev dhvivcghyg cggvrasllp ppsdlphvvr
      121 riaplcalar rhrdvlagld dtaaadrlse lnvleqvrql raspivrnre rpplvhgwif
      181 sladgrlkel dsgyatlpvd asavpndlap alg
//
LOCUS       WP_175950879             151 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175950879
VERSION     WP_175950879.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..151
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=15578
     Region          1..150
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mtslningqt htvaappdmp llwvlrdlvg ltgtkfgcgi aqcgactvhl dgvavrscvl
       61 pvaavgnkkv ttieavgetp agkkvqqawr qidvvqcgyc qsgqvmsaas llaqnpnptd
      121 adidaamagn icrcgtynri raaikqaake a
//
LOCUS       WP_175950873             357 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia sp. BCC0405].
ACCESSION   WP_175950873
VERSION     WP_175950873.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..357
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38194
     Region          4..334
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,226,287,308,310..312)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,174,177,179,226,233,287,308,
                     310..311)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,174,177,179,311)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            179
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 msqlfspirv grytlsnrlv mapmtrsraq fdgtpgelas eyyaqrasvg livtegtqps
       61 edgqgyittp giytdahvag wkcatdsvha kgghlfiqlm hagrmchpdn tphhrpgvap
      121 saiapatgmf takgmqdipv pralstdevr gtvadfrvaa rraieagadg veihganayl
      181 iqqffapnan vrtdayggsi enrarfaiev aaaiadeiga drtairlspg tamwgidega
      241 egpdlyrylv aeldklglay lhimhlgnda lladirklwk gtlilnrpgr lrehigadve
      301 agladleayg qmvlanpdfi arlqvdapmn dadratffgg nargytdypa lheaaga
//
LOCUS       WP_175950917             293 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175950917
VERSION     WP_175950917.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..293
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31522
     Region          13..270
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mtapikallk phvrdignlq vrrtlpalaa rlvgpfiffd hmgpatlppg tgldvrphph
       61 iglatvtylf dgailhrdsl gsrqeivpgd vnwmtagrgi vhsertpdaq renghtvhgi
      121 qtwvalprah ettepsfehh aadtlpkrie dgvsltviag dafglrspvt tfsrtlyvaa
      181 efaaggrlel dasheeravy vvdgelaidg tpvpaeqmav lapgaavtlt sgsgaramll
      241 ggdridgerf iewnfvassr eaierakaaw trqemgkvpg etewiplpes kpr
//
LOCUS       WP_175950920             155 aa            linear   BCT 11-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Burkholderia sp. BCC0405].
ACCESSION   WP_175950920
VERSION     WP_175950920.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..155
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=16792
     Region          1..153
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mfnavidapf gkvgirtdaa vlreivylpe svksvdpdsp lakravkqie ryferasarf
       61 dlplaevgsa fqhrvwdvis dippgtvlty gqvakrigsa pravgqacga nyfplvipch
      121 rvvaagglgg fanhddngyy qkvkrwllah egvpy
//
LOCUS       WP_175950959             421 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: RsmB/NOP family class I SAM-dependent RNA
            methyltransferase [unclassified Burkholderia].
ACCESSION   WP_175950959
VERSION     WP_175950959.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..421
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=45904
     Region          <103..419
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mklhgfligq tetllaevlk fagpadatts rffrahpklg haergviaea vfavlrrkme
       61 fshlaesgtg tparrltllg lmqtagrnal kpflsdtesa wlehvskidp aslpvrirtn
      121 lpdwiyqals arfdgeelaq laaalnypap ldlranaqka trdqviealr vsgidagatp
      181 fapfgvrvvg kpaltrlklf eegaievqde gsqllcslva prrgemvvdf cagaggktla
      241 lgammrstgr lyafdvsekr laklkprlar sglsnvnpvl idsehdakik rlagkidrvl
      301 vdapcsglgt lrrnpdlkwr qtrtaidelt pkqasilasa arlvkkggrl vyatcsvlda
      361 eneriveqfl adhpefvlvp aqkvledqri eletgdylsl wphrhatdgf faavlerraa
      421 q
//
LOCUS       WP_175950999             271 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Burkholderia].
ACCESSION   WP_175950999
VERSION     WP_175950999.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..271
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28963
     Region          16..265
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtgaalhata gdmnyaavgl tlkagartll dgftrafrpg eiwcvagpng agkttllatl
       61 aglqppaggh veidgrplaa wppeqlaqrr almpqqlhda fsatvfdtvl lnrfpylggw
      121 gwerdgdraa ardalatfdl talasrdvls lsggerqrva laatlcqdap lmlldeplah
      181 ldlhhqidcl talaawldag prtvlfschd lnlarrfath allldgrgha wagpvhdvlt
      241 perasdafgy plvlirengr dallpawper q
//
LOCUS       WP_175951074             151 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175951074
VERSION     WP_175951074.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..151
                     /product="VOC family protein"
                     /calculated_mol_wt=16553
     Region          3..135
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(3..8,24,62..63,66,83..88,90,94,123,133)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 mqvqpyltfy gradealqfy ekalgaktmf kmhfkdappn pdypmkpema dkvmhasfti
       61 gdsmimcsdg dcnqpgggth agyslslnpa tveegqklfn aladggevtm pfgktfwalg
      121 fgmakdrfgv hwmvnvedls qredlaqrag q
//
LOCUS       WP_175951083             414 aa            linear   BCT 11-JAN-2025
DEFINITION  lactonase family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175951083
VERSION     WP_175951083.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..414
                     /product="lactonase family protein"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44178
     Region          52..411
                     /region_name="Pgl"
                     /note="6-phosphogluconolactonase, cycloisomerase 2 family
                     [Carbohydrate transport and metabolism]; COG2706"
                     /db_xref="CDD:442025"
ORIGIN      
        1 mpnrlrerda rastrgfplr lahwmkgfai vlslsathaf aqqspapadg vynllvgtyt
       61 gggsdgiyvy rfdtktgsva pvssaktvnp syllpsrdgr tvyavnelpg ddgpatqrgg
      121 vsafrfdakt galsfidrvs segndpcyla lspdgkylvt anysvakdpg gsfavfplrd
      181 ngavgqavlt vhhegtgpvk grqdgahvhs tvfspdghyl fvqdlgtdki ygyrytvdgs
      241 rglisptdtr ytpvkagsgp rhmvfgadgr yayvtselna svevfgyhdg kltpvetvsm
      301 tapgfkgkvg ggaihlspdg rflyvsnrgd andlviyavn qadgrlklvg rqsslgktpr
      361 eflidptgkw livgnqdsdt fyvfsrnvet gqlglnpqkv avgkpvdfkl vpvq
//
LOCUS       WP_175951089             522 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia sp. BCC0405].
ACCESSION   WP_175951089
VERSION     WP_175951089.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..522
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56469
     Region          34..456
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msagpaglth dvpaapfern atmsnsvakp vdatfdqfgl aadilkaiae qgyttptpiq
       61 aqaipvvlag rdvmgaaqtg tgktasfslp iiqrllpqan tsasparhpv raliltptre
      121 ladqvaanvh ayakhtplrs avvfggvdmn pqmaelrrgv eiliatpgrl ldhvqqktan
      181 lgqvqilvld eadrmldmgf lpdlqrilnl lpkerqtllf satfspeikk lastylrnpq
      241 tievarsnst nanvtqivyd vaegdkqaav vqllrdrglk qvivfcnski gasrlarnle
      301 rdgvvasaih gdktqiermq aldafkrgei ealvatdvaa rgldiaelpa vinfdlpfsa
      361 edyvhrigrt gragatgdal slcspnerkq ladieklikr plevqtlald kparhrhder
      421 gndrggdrns ergaergger ggrrdrdehr gasgrrpggs erghhrrhea pvddfflkpy
      481 epsasakqhd daqpaqqpek kgpkrqvaal lggfgmprkp sv
//
LOCUS       WP_175951118             871 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0405].
ACCESSION   WP_175951118
VERSION     WP_175951118.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 871)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 871)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 871)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 871)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 871)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 871)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 871)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..871
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..871
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=91557
     Region          33..871
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mkgrqhaaqp pagqpghevs ahggrfglrd lvrqaarmta rdwrageltl lvlalvlava
       61 altsvgflad rlrqglerda rqmlgadfvv radrpvdpsf dgqaralglr tattaifpsm
      121 iasatggqaa daapsrlaav kavspgyplr gaveilpaga avaqkaagip apgtvwadpa
      181 lldalhlkag dtvrvglrvf kvaasisrel drgfsfvnfs prlmmradel aatgltgygs
      241 rvtyrllvag dqqavarfea yaharvdggk lrgvgleslq egqpqvrqtl drarhfltlv
      301 alltallaav aiamaaqrym rrhldgcatm rclgvsrrtl galfalefag igivsgtaga
      361 vlgygghwal laalgglidv vlppptlwpa ligvgvalvl llgfalpplv pltrvppvrv
      421 lrrewgdalr tawaayaigv vlfaglliaa agnlklgliv tggfagalvg faliarlvlf
      481 aaaravrnar vaagigwrya laslhrrgta salqitalal glmcllliai trndlvagwr
      541 qstppdapnq flidiqpdqr advaaylsah gvrdavpapm vrgrlvaing kpvnpdayps
      601 eearrlvdre fnlsyttelp sdnrivaggw fgnaatpqms ieaglaktln vkpgdvlrfd
      661 vtgltvdapi tsvrkldwgs frvnffvlmp ppvlkdfpav yltsfhlpas daalldplia
      721 rypnltaidv apilaqlqrm mlqvvgavqf lfaftlaagv lvlytalagt rdervreaal
      781 lralgasraq vnavqraefv vvgalagala sagaiavgwa lasrvfdfql avdpwlvpag
      841 ivagvacaga agwlslhnvl rrpalqslrd a
//
LOCUS       WP_175951120             243 aa            linear   BCT 11-JAN-2025
DEFINITION  alanyl-tRNA editing protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175951120
VERSION     WP_175951120.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V.
  TITLE     Evolution of aminoacyl-tRNA synthetases--analysis of unique domain
            architectures and phylogenetic trees reveals a complex history of
            horizontal gene transfer events
  JOURNAL   Genome Res 9 (8), 689-710 (1999)
   PUBMED   10447505
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Cusack,S., Hartlein,M. and Leberman,R.
  TITLE     Sequence, structural and evolutionary relationships between class 2
            aminoacyl-tRNA synthetases
  JOURNAL   Nucleic Acids Res 19 (13), 3489-3498 (1991)
   PUBMED   1852601
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Schimmel,P.
  TITLE     Classes of aminoacyl-tRNA synthetases and the establishment of the
            genetic code
  JOURNAL   Trends Biochem Sci 16 (1), 1-3 (1991)
   PUBMED   2053131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..243
                     /product="alanyl-tRNA editing protein"
                     /GO_function="GO:0002161 - aminoacyl-tRNA editing activity
                     [Evidence IEA]"
                     /GO_function="GO:0002196 - Ser-tRNA(Ala) hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004813 - alanine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006419 - alanyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=26169
     Region          1..243
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
ORIGIN      
        1 mttpalfred ayltqcdavv lavgddgirl drtvfyplgg gqagdtgtlt lpdgsaiaia
       61 dtrkarfdga tpddavhvpa pgqeasvaal vpgtrvvaei dwlrryrhmr lhtaahlmca
      121 vlpyavdgcs vtadyvrldf atsdaidrdd verrlaglva gahpvttewi tddemaarpd
      181 lvrtmsvkpp mglgrvrllr ieqvdlqpcg gthvrntsei galrvaklek ksartrrlvl
      241 efa
//
LOCUS       WP_175951132             213 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: carbonic anhydrase [unclassified Burkholderia].
ACCESSION   WP_175951132
VERSION     WP_175951132.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Lindskog,S.
  TITLE     Structure and mechanism of carbonic anhydrase
  JOURNAL   Pharmacol Ther 74 (1), 1-20 (1997)
   PUBMED   9336012
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10096752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..213
                     /product="carbonic anhydrase"
                     /EC_number="4.2.1.1"
                     /GO_function="GO:0004089 - carbonate dehydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23026
     Region          11..190
                     /region_name="beta_CA_cladeA"
                     /note="Carbonic anhydrases (CA) are zinc-containing
                     enzymes that catalyze the reversible hydration of carbon
                     dioxide in a two-step mechanism in which the nucleophilic
                     attack of a zinc-bound hydroxide ion on carbon dioxide is
                     followed by the regeneration of an...; cd00883"
                     /db_xref="CDD:238448"
     Site            order(33,35,42,44..46,58,61,83,88,98,101,180)
                     /site_type="active"
                     /note="active site clefts [active]"
                     /db_xref="CDD:238448"
     Site            order(42,44,98,101)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238448"
     Site            order(43..46,48,50..51,53,58..60,62,64,78..79,82..83,121,
                     180,182..183,185,187)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238448"
ORIGIN      
        1 mnrpksmlva niawaretre ytpgffdala rgqnprvlwi gcadsrvpae tithcapgel
       61 fvhrnianlf hpdddnsasv leyavrvlqv dhvivcghyg cggvrasllp ppadlphvar
      121 riaplcalar rhrdaldgld dtaaadrlae lnvleqvrll raspivhgre rpplvhgwif
      181 sladgrlqel dsgyttpavd vesvqaatag alg
//
LOCUS       WP_175951212             252 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175951212
VERSION     WP_175951212.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..252
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27129
     Region          1..245
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mirleridks fgahrvlhgi dlalqpgsvt aligpsgsgk stllrcvnll evpeagtltv
       61 gdaridfspa yrpardavfa vrrqtgmvfq nfqlfphlsv vqnvmeglvt vqrwprerar
      121 eralallekv giadkadawp gtlsggqqqr vaiaralaps pqvllcdept saldpelsve
      181 vvevlrqlar egttmlmath dlrlaasiah davfladgrv veagasrdlf gdprdprtak
      241 fistlaqgvp vf
//
LOCUS       WP_175951219             288 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175951219
VERSION     WP_175951219.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..288
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=32144
     Region          5..277
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mfdqivfagg gnrcwwqagf wdvaqpaldl rprvitgisa gaatacmlyt rdaawvmryy
       61 eealrhnrkn aywgnlfgre pvfphyriyr qalldiygep faklaaapei rigvshvprw
      121 lgarsavaag lvayniekyv rktlhptlgr tlgfrpefvr aqactrvdel adlilqssct
      181 ppftpvlrrd grpvldggmv dnvpvdaldp tpgdvlvlvt rlyprpqmft vahgeqrrly
      241 vqpsskvpis swdytspsqm rhaydlgrrd gehfltrvga mtggraaa
//
LOCUS       WP_175951225             213 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0405].
ACCESSION   WP_175951225
VERSION     WP_175951225.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..213
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22209
     Region          4..213
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mfgithfgff vlavfllnvt pgpdtayivg rsvaqgrgag lmsafgisag ccvhalacaf
       61 gltallaasa aaftviklvg aayliylgvr mliakqaaep lgkaatsaqa akplrqlfmq
      121 gfwtnvlnpk vvlffvsffp qfvsadsphk alafltlggv fvamstvwts lvawvaggvt
      181 erfsgkpgvk kwldrtvgsa fvglglrlat sqr
//
LOCUS       WP_175951246             243 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: OmpA family protein [Burkholderia].
ACCESSION   WP_175951246
VERSION     WP_175951246.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..243
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25823
     Region          139..240
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(142..143,176..177,180,184..185,188,230,234)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mnkpqhfvrr gllgafvvll sacttqsgpt ytvraikapd qaapvfrvtc eglvsstqsc
       61 eaaarkfcag kpvtqlqavd rvrrgaamgd preltfmcgv ppqarveppv aaqpqpveqp
      121 qpvvapiaqr qvllqgsanf afdsaaltps arqalnrfld vnrdarfqrv tvtgytdsqg
      181 ahahnvrlse araravatyl ragglradhf atvgkgaaep vasnataegr aqnrrveiel
      241 eta
//
LOCUS       WP_175951267             546 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GMC family oxidoreductase [unclassified
            Burkholderia].
ACCESSION   WP_175951267
VERSION     WP_175951267.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..546
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58449
     Region          1..532
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mqydyiivgg gsggsslagr ladacpdati alieagshte rnllvnmpvg iaalvpfklg
       61 tnygyetvpq pglggrrgyq prgrgmggss ainamiytrg hpgdydewaq lgatgwgwqd
      121 vlpyfrraeg nqrgadawhg adgpltvsdl rfrnpfserf iqaahaagyp lnddfngatq
      181 egvgfyqvth rdgsrcsvar ayiygrnrpn lhvitdatvl rvtfdgkraa gvavarngrv
      241 etldaraevi lsagafnspq llmcsgigpa eqlrrhgiav vqdapdvgan lidhidfiin
      301 trvnsselvg iclrgiakmt palaryfssr tgmmtsnvae aggfiksdps lerpdlqlhf
      361 ctalvddhnr kmhwgfgysl hvcalrpfsr gtvalasgda rdaplidprf fsdsrdldll
      421 vrgtqamrki lsqaplasqg grelytradq seaelrktiv ehadtiyhpv gtcrmgsdar
      481 avvdpqlrvr gveglrvvda svmptlvggn tnapsvmige raadfivaar kgaaprgeaa
      541 aavhgr
//
LOCUS       WP_175951355             358 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: porin [unclassified Burkholderia].
ACCESSION   WP_175951355
VERSION     WP_175951355.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..358
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=38151
     Region          31..358
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkalarrasr tsvkliaaaa cvaaaapvha qssvslygqv dewvgatkfp ggdrawnvsg
       61 ggmstsywgl hgaedlgngy kaiftlesff raqngqfgrf qgdtffarna yvgidspygt
      121 vtagrltthl flstilfnpf ydsytfspmv yhvflglgtf ptypsdqgav gdsgwnnals
      181 ytspsfggln fgamyalgnq agdngskkws aqfnyangpf aatavyqyvn fnngprdlsa
      241 lvagmksqgi aqvgatydlk yvklfgqymy tkndqvagsw hvntaqggvs vplgvgsama
      301 syaysrdagg ldqtrqtwav gydyplskrt dvyaaymndh isglstgntf gagirakf
//
LOCUS       WP_175951405             288 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175951405
VERSION     WP_175951405.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..288
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30708
     Region          29..283
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mpasplpddd ladsdtddaa sgehggkvrs giqsievgfr lldvltsepr ammlrdlaqr
       61 agmspakahr ylvsfarlgv vsqdpvsgry elggfalqmg larlarvdgv klarialtef
      121 rdrldqtvgi avwgnqgpti vhwmesshpa kaslklgdvm pllgsatgll faaylprskt
      181 aamlerelad trrsphhggp rtldevdaal advrkheaar vegmllptih afcmpvfdav
      241 gelalaival gqegsfdiaw ggeidtalra caqklsyelg yspdarda
//
LOCUS       WP_175951384             241 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: copper homeostasis protein CutC [unclassified
            Burkholderia].
ACCESSION   WP_175951384
VERSION     WP_175951384.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Latorre,M., Olivares,F., Reyes-Jara,A., Lopez,G. and Gonzalez,M.
  TITLE     CutC is induced late during copper exposure and can modify
            intracellular copper content in Enterococcus faecalis
  JOURNAL   Biochem Biophys Res Commun 406 (4), 633-637 (2011)
   PUBMED   21362400
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Li,Y., Du,J., Zhang,P. and Ding,J.
  TITLE     Crystal structure of human copper homeostasis protein CutC reveals
            a potential copper-binding site
  JOURNAL   J Struct Biol 169 (3), 399-405 (2010)
   PUBMED   19878721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..241
                     /product="copper homeostasis protein CutC"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24449
     Region          8..237
                     /region_name="CutC"
                     /note="Copper homeostasis protein CutC [Inorganic ion
                     transport and metabolism]; COG3142"
                     /db_xref="CDD:442376"
ORIGIN      
        1 mnrnaassil leviattvgd akaaaragad rlelvtaite ggltpsvgli eavvaavpip
       61 vnvivrphsr sfvydaddlr vierdvraav aagangvvfg aldargdvdl dalariaaaa
      121 dgraltfhra fdvsrdlnaa fdallrvpav tsvltsgghp svldaaatit rlvrqaagst
      181 ctvlagsglt idavgdfvra tgvravhfgs gvrprgevla pvdqqlverv raaidgaaah
      241 v
//
LOCUS       WP_175951418             302 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175951418
VERSION     WP_175951418.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..302
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32303
     Region          27..268
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 mnvsnetdah aaaigagsig tpaaadaadl vievrnltkr ygrniihqkl dfdvrrgeiv
       61 sivggsgsgk ttlvrqilgl erptsgtikv fgedtatidd asarmmrtrs gmlfqqgalf
      121 ssmtvfdnva qplrelgrvp pdllhdivml klemvglpck haskmpaals ggmvkrvgia
      181 raialepell fldeptagld pqasdefvel iatlhrtlgl tvvmvthdld tmvalstrva
      241 vladrkvlva apveevanvd hpfiheyflg lrgrralqal pperraklpk aalepalssv
      301 el
//
LOCUS       WP_175951419             309 aa            linear   BCT 11-JAN-2025
DEFINITION  MlaD family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175951419
VERSION     WP_175951419.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..309
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=32693
     Region          1..289
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 menkshafwa glftialtla iagtvfwfnv drtvrvpydl lartnvtglf pdaavrfrgl
       61 dvgkvqsigf drvhpgqiri rilvdhdapi tqstygslgf qgvtgiafvq ledtgrdlap
      121 lpsstkaiaq ipmrpslfdq iqergdvllr qlelaaksan almspemreq lrataeslqh
      181 aadgattltk qlgpavtalp etmhevnram asantllqpn gplvsnlnka gtaaeqigva
      241 lnglnarvqy dtlprfnala gsvgdasrql kdvagelgrn prsllfgspg aapgpgepgf
      301 vwpgatagq
//
LOCUS       WP_175951475             244 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175951475
VERSION     WP_175951475.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..244
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26513
     Region          14..244
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 metgwselap dplsdtplyl qlarnlasai hagawragea lpserllsvs vgvsritarr
       61 alallveqgl ikrargagsf itprvadpls rlvgftakmr qrgfvpdsvw lsrtlraanr
      121 deitrlglap gatvarlerl rradgivmav ehstlpaavv pdpqvlgasl yeyleargmt
      181 vvralqhfra anathaiakw mavkpgsall vitrigygad qraievsety crddyydfva
      241 elkr
//
LOCUS       WP_175951554             189 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma carbonic anhydrase family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175951554
VERSION     WP_175951554.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 189)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..189
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19820
     Region          1..170
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 mklfafqglr prihpdayvf edaviigdve igpgvsiwpg vtirgdkari ligagsniqe
       61 hamlhadpgy pltlgenvti ghgvmlhgcd vgshsvigig aillngskvg scslvtagsq
      121 lgagppfadn slisgnparv lmtlgvsdig glrdtareyq dlaeayrrdl hplrpdeirl
      181 esrraggvr
//
LOCUS       WP_175951557             627 aa            linear   BCT 11-JAN-2025
DEFINITION  non-ribosomal peptide synthetase [Burkholderia sp. BCC0405].
ACCESSION   WP_175951557
VERSION     WP_175951557.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   2  (residues 1 to 627)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   3  (residues 1 to 627)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   4  (residues 1 to 627)
  AUTHORS   Marahiel,M.A.
  TITLE     A structural model for multimodular NRPS assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 136-140 (2016)
   PUBMED   26429504
REFERENCE   5  (residues 1 to 627)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10147902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..627
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0044550 - secondary metabolite
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=68353
     Region          32..487
                     /region_name="A_NRPS"
                     /note="The adenylation domain of nonribosomal peptide
                     synthetases (NRPS); cd05930"
                     /db_xref="CDD:341253"
     Site            order(145,148..153,155..156)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341253"
     Site            order(148..149,264..265,286..291,313,379,391,394,481)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341253"
     Region          513..572
                     /region_name="PP-binding"
                     /note="Phosphopantetheine attachment site; pfam00550"
                     /db_xref="CDD:425746"
ORIGIN      
        1 mnhhpdphvh epsvlhavhe lvrqscerya grvaieepgq avrydvlaqr idamrsrlaq
       61 avapgsvvav vghrsvetiv aalavcshgc vlmniddelp eerqhlmvgs vpptvtircg
      121 aatqfelaqa sparfaaidt dhayiaftsg stgrpkailg shqglshfvq wqghefcigp
      181 ddrfahltnm sfdvwlrdaf tplvngatlc ipgdrhlgar dlfdfleahv itavhvvpsv
      241 anhwinsapa rpaiasmrla ffageplegv lvrrwhtrfp acevvnlygp tettlakhfk
      301 rvpsqpldgv qpvghpipgs athildeqlr pcaegvvgei cietpwrshg yvheagllap
      361 fvdfrpsggp arsvyrtgdl glrkadgeie irgrlddqvk ingvrvelle vksaivsfpg
      421 vrdvfvcttg agyqrgiaav leaaqevaar lmthlrellp aamvpsrilt lpalprlpng
      481 klnrtelsrl aaaspppspv psllrstgtt aterleslwr evlradlvdq hrnffesggt
      541 sltivelhar ieetfqirlp ivrlfehatl asqaamland adpgtaatpr ahatphtvrs
      601 htlsarhrrt rqlelqrser hnpdaqa
//
LOCUS       WP_175951589             222 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0405].
ACCESSION   WP_175951589
VERSION     WP_175951589.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..222
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23244
     Region          12..213
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mifppasmls dgfflslslc ldiglvnvam lsltlshgfr pgfwlglgsc vgdlvyaala
       61 lagmavllqf epvrwivwig ggavllfltw kmarealtpa katgddadda plprasarrs
      121 flrgmllams spsailwfaa vggaliakag attpatasvf lsgfflggla wtlfmctlas
      181 qgrkragagl mrachiasal lfayfsysvi vggyrdlivr av
//
LOCUS       WP_175951581             251 aa            linear   BCT 11-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Burkholderia
            sp. BCC0405].
ACCESSION   WP_175951581
VERSION     WP_175951581.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..251
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26031
     Region          1..251
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlttqrkkai ldalardgqv lavelsaqfg vsedtvrrdl relaaegllq rvhggalpas
       61 pavapfaqre alepaekrri arraaemiap gqvaivdggt tsallvsqlp adlrativth
      121 spsvavalaa hpsidvilig grlykhsiva vgaaamegia rihadlyfmg vtgvhpvagl
      181 stgdfeeaai kralaeraae tvvlasqskl raasqfvige itlahtvvve ketdaaltkp
      241 ieaagvtvvr a
//
LOCUS       WP_175951597             322 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175951597
VERSION     WP_175951597.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..322
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34092
     Region          20..285
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 maiqtattah ddasphmrad gadtaaalvw ralqiepval vpqlltqsgn tihrveladg
       61 rtvvlrvspq paafahtasn ldalrvlglp vqqvlaagpa apgqsfviln wldgfdlkfa
      121 lpamrpdqma avaervtdcq qrvaglpasr gfgwapigrd aaharwtdlf gapasapaaf
      181 eatplnhlra rlramrstle pyfaartpvc flddlttrnv ivdngalsgf idldfvcygd
      241 pllqvgttla ylaadvgdag raygdalvdc wspsgdarra myfyaglwat gflaaaetag
      301 dawrirtlep aaralldaae tc
//
LOCUS       WP_175951599             341 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175951599
VERSION     WP_175951599.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..341
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35925
     Region          65..274
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mhtttvhraa lrllpafaag mmaacsssat vdsaittsld dgrsglvtfa svtprstgdy
       61 lshhatsekv vvtgelsmpa dgphivpavi ilhgssgvnq gervwarrmn algyasfvvd
      121 sftgrgirnt ekdqtqlamt adiadayaal rllatdprid qnriavmgfs rggvaalysv
      181 lepfrlaame gnlrfaahva fypscgisye sahldgspvl mlvggkddyt paapciayad
      241 klrsegarva vkeypdawhg fdrptrvhti platsardch gsydldsrtf tmiqngqtls
      301 gasavaeskr clstgvtlgg dpdaqakspa evaaflkaaf q
//
LOCUS       WP_175951646             226 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175951646
VERSION     WP_175951646.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..226
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24784
     Region          10..225
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mnaltdvtrk rpaapsgsla drayaliqrd iitmrlkpga alneadlvar tsigrtpvhq
       61 avhrlvlegl lsvmprkglm vqplslddiv avidvrrine ahcadlaarh atpddlarla
      121 alldagqacv dthdvegmme ldrafhqaia taarntvlad ilralhersl rfwfvtlsep
      181 hhladvqheh relfdrlsar daagaraave shidsfrstl lqhlrp
//
LOCUS       WP_175951647             391 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia sp. BCC0405].
ACCESSION   WP_175951647
VERSION     WP_175951647.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..391
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=41602
     Region          157..388
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 msentpspag lpgtssvssd sprpdpakap dapaaqaaaq nvaadgaspv taasgatgaa
       61 vdgaaaaaps kagtpppgfg aqpdfdtprp ppasaqhapp aylkqsdtpw svfgrivaar
      121 arrlfdragq ritqrtlrig vsarifhpep gakglrgktl qyleesiahw vmsrdvlvfm
      181 iptvghqgmi hpsnirlrdy akhldglllq ggadvspqty aasdarpewp gdrvrdmyel
      241 ellhefvesg kpvlgvcrgc qlinvafggs lyqdiatdvp tanahvsehy dqhrhairfp
      301 dsstlasmfp grseaivnsi hhqairdlgr dlnieavsag dgiiegirhr rspfvvgvqw
      361 hpefhraggs elldctplld aflraaretr l
//
LOCUS       WP_175951678             249 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: electron transfer flavoprotein subunit beta/FixA
            family protein [unclassified Burkholderia].
ACCESSION   WP_175951678
VERSION     WP_175951678.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26395
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkilvpvkrv vdynvkvrvk sdntgvdian vkmsmnpfde iaveeavrlk eagvatevia
       61 vsvgvaqaqe tlrtalaiga drailvestd sveplgvaki lkalvdkeqp qlvilgkqai
      121 dddsnqtgqm laalaglpqa tfaskvtvad gkatvarevd ggaetlsltl pavittdlrl
      181 nepryvtlpn imkakkkple tvkpedlgvd vaprlktlkv veppkraagv kvpdvktlve
      241 klkteakvl
//
LOCUS       WP_175951693             166 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrofolate reductase [Burkholderia sp. BCC0405].
ACCESSION   WP_175951693
VERSION     WP_175951693.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11087044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..166
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17942
     Region          3..163
                     /region_name="DHFR_1"
                     /note="Dihydrofolate reductase; pfam00186"
                     /db_xref="CDD:425512"
     Site            order(7,24,29,59,99,105,118)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(9,16,46..48,66,100..103)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 mttltlivar arngiigrdn qlpwklpedl affkrttmga pivmgrkthe sigrplpgrr
       61 nivvtrdatr rfdgcdtvts ladalalaar dgvpevflig gaqlytegla ladklvvtei
      121 dadfdgdasf papdaaqwqe vsrdahqaaa pntfgyafvv yerkrg
//
LOCUS       WP_175951777             183 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: peroxiredoxin [unclassified Burkholderia].
ACCESSION   WP_175951777
VERSION     WP_175951777.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Jeong,W., Cha,M.K. and Kim,I.H.
  TITLE     Thioredoxin-dependent hydroperoxide peroxidase activity of
            bacterioferritin comigratory protein (BCP) as a new member of the
            thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide
            peroxidase C (AhpC) family
  JOURNAL   J Biol Chem 275 (4), 2924-2930 (2000)
   PUBMED   10644761
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..183
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.24"
                     /GO_function="GO:0008379 - thioredoxin peroxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19437
     Region          30..171
                     /region_name="PRX_BCP"
                     /note="Peroxiredoxin (PRX) family, Bacterioferritin
                     comigratory protein (BCP) subfamily; composed of
                     thioredoxin-dependent thiol peroxidases, widely expressed
                     in pathogenic bacteria, that protect cells against
                     toxicity from reactive oxygen species by reducing...;
                     cd03017"
                     /db_xref="CDD:239315"
     Site            order(69,72,142)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239315"
ORIGIN      
        1 mkrklllgaa vaalvaghal vaqaelkpga aapdfttqas lggktytysl adalkqgpvv
       61 lyfypaaftk gctieahafa davdrykayg atvigvsadk idtltkfsvs ecrskfpvaa
      121 dpdakiirey daklpaidra nrvsyvispe gkilyeytsm spdkhventl aavkawadah
      181 pkq
//
LOCUS       WP_175951789             213 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia sp. BCC0405].
ACCESSION   WP_175951789
VERSION     WP_175951789.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..213
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=21693
     Region          7..213
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mtqrtlnial fgatgtigsr iaaeaarrgh rltalsrnpg aagdgitaka adlfdaasia
       61 aalpghdvva saygpkqdda tkvvaaakal vagtrqaglk rlvvvggags levapgkqlv
      121 dsegfpeayk avalahrdal dylktvgdld wtffapaali apgertgafr tgvgkliada
      181 qgnskisaed yaiafvdale qdsfvreiat vay
//
LOCUS       WP_175951791             257 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175951791
VERSION     WP_175951791.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..257
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28070
     Region          1..>240
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mnllelddlc laydtphgrr tvvdglslal prgdigcllg asgcgkttvl raiagfepvr
       61 mgrivldgap vaapsldvpp errrigmmfq dyalfphlsa adnvafglrr mpkterrmri
      121 aemlelvgla dsgnayphel sggqqqrval aralapspel llldepfsnl dvdtrerlaf
      181 elrdilkrtg htailvthnq aeafaiadri gvmndgrlaq wdtpyalhhh paspfvadfv
      241 rrdaladera ralargr
//
LOCUS       WP_175951815             208 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175951815
VERSION     WP_175951815.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..208
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22413
     Region          15..169
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mtessyhfye psqghglphd plnaivgprp igwissrgnd gtvnlapysf fnafnyhppi
       61 igfssvsakd slrnaqetge fvwnlatrdl ahrmnqtcaa vpygvdefel ggltaipsrl
      121 vdvprvaesg vnfeckvtdv irlrdhqgve taaslvlgev vavhirndll kdgifdtfga
      181 giilraggps ayahvrpdsr fdiarpga
//
LOCUS       WP_175951855             403 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar ABC transporter permease [Burkholderia sp. BCC0405].
ACCESSION   WP_175951855
VERSION     WP_175951855.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..403
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42225
     Region          29..403
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mnsdlssstp atpdaqarrp agraaglplr qvfvrykvla llfavvaiwv ffsvltdgaf
       61 vtprnvsnll rqmsitgmla cgmvfviiag eidlsvgsll gllggvaail dvnrhwpvaa
      121 tvpvvlalgv liglfngwws tyrrvpsfiv glggmlafrg illgvtggst iapvsdgfvf
      181 igqgylprma gdglamllfv latllvvrqr gtrrryrlav aplwqdgvki agagavlfaf
      241 vatldryggi pvpvllllal lgvfswiatq tvfgrrvyav gsnleatrls gvdtdrvkla
      301 ifalmglmca faglvntarl aagspsagtm geldaiaacf iggtsmrggs gtvygaliga
      361 lvmasldngm smldvdaywq mivkgavlvl avwidvvsrs nrr
//
LOCUS       WP_175951864             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175951864
VERSION     WP_175951864.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33350
     Region          7..>53
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..292
                     /region_name="PBP2_LTTR_like_4"
                     /note="TThe C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08440"
                     /db_xref="CDD:176131"
     Site            order(111..112,114..115,118,122,124..130,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176131"
ORIGIN      
        1 mginfdlndl qafravvetg sfrkaaetvs isqpalsrri dkleealgvr lferttrrvt
       61 lttvgrvfaq saeqllddld aallgirdvs ssrlghvtia cvpsvayyfl paiiaryhqr
      121 fprirvklld aganevlgav isgeadfgvs figsqeaeie fkvllqerfv aacrrdhpla
      181 rkkrvtwnel yehdyvavdk tsgnrllldq alaavaprgp svcearhvtt llglieaglg
      241 vaavpsmamp ghdhpvltsv plvepvvkrr vgivkrrgrp ltpaaeafhr mivdakrggf
      301 asrgasa
//
LOCUS       WP_175951868             286 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [unclassified
            Burkholderia].
ACCESSION   WP_175951868
VERSION     WP_175951868.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15202679
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..286
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30592
     Region          12..132
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          168..273
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 msdlnpsstl tyrpfaeadl paahrlseav kwphrlddwr fvfqlgggfv aedetgivgt
       61 algwrfgeah aslgmvivsp erqgrgigre lfsrvldslg srtiflhatp ageplyakfg
      121 feaidtidqh qgaafqppli slppgerlrp lgandgprla alasraagyr rdavieallg
      181 vangialdrd gellgfalfr rfgrghvigp vvapdtlraq alishwlalh egmfvrldvp
      241 gdsglsdwlq glglprvdtv vamargatpe rdpalrafai vsqalg
//
LOCUS       WP_175951876             244 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175951876
VERSION     WP_175951876.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..244
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25868
     Region          <59..>98
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          127..235
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 msavfvlhra dgspsstafd mrafgecdpf arhreiaweg pdsmaagrir fvgeldvssy
       61 phietlvvve geltleadga aplvlgpgeg avigggtalr vsaasrvllm fcaaacatpt
      121 krgcfplrad adfkpssslp aevllgpapq crsdnvfidd gaeycagtwd stayhrivrp
      181 hrvnefmfll agsvrfaapd gsvlslgagd alfvprgapi gwesrervak fyvvqnvhvs
      241 terd
//
LOCUS       WP_175951879             467 aa            linear   BCT 11-JAN-2025
DEFINITION  GGDEF domain-containing protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175951879
VERSION     WP_175951879.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 467)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 467)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..467
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51585
     Region          192..465
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mnvnvaaqes artaervtrv yarlllvgfa ltpayliayl yvfqdpsltf enhafhelai
       61 avatlegafv tyvcwrcyrl sgepllrwlt lgflgfsliy alhgaftgma hhniwlflly
      121 gpasrltmsi lilvgqftys hkadsaatra dpriwlpwla lfalvdvava viafspvagh
      181 lwvrlsmegg amllsvanvv alvmrrirsp lmtiygisvt sfafsslafi lgrpwnhmww
      241 lahaifaagf fllsfgvvqa fhttrsfski ysqeelfarl rdamartera lqalqrtnek
      301 lehlaatdpl tgatnrrqfi esveaeinra krngapfsll aldldhfkai ndsyghqagd
      361 qvlqrfvdkc adairpydgv arvggeefmv llpqaaldta lsigerirta iagtpfeagt
      421 gepikvtvsv gasefgrdge tidailrkad erlyrakhqg rnqvvag
//
LOCUS       WP_175951884             293 aa            linear   BCT 11-JAN-2025
DEFINITION  endo alpha-1,4 polygalactosaminidase [Burkholderia sp. BCC0405].
ACCESSION   WP_175951884
VERSION     WP_175951884.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 293)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008090
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..293
                     /product="endo alpha-1,4 polygalactosaminidase"
                     /EC_number="3.2.1.109"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=31756
     Region          1..276
                     /region_name="COG3868"
                     /note="Predicted glycosyl hydrolase, GH114 family
                     [Carbohydrate transport and metabolism]"
                     /db_xref="CDD:443077"
ORIGIN      
        1 msarsfasvv lmlllaacgg dsdslapgta vaaasarasq atawkplapg tswqwqidgn
       61 rinetvldgv nnprkmfdvd meltdagtiq rlkakgiyvv cymevggred srgdagkfpd
      121 svlgnpvegy edherwldir qtailmplml arldqakkkg cdgiepdldd syrqetgfpl
      181 trddqlryna aliaaahdrg msmglkngse iatamakvad walneqcnrf hecgdyasfi
      241 alnkavfnve ytrpdgmtla dfcpadnqan fdgilklssd tlsalprgac rfe
//
LOCUS       WP_175951940             700 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175951940
VERSION     WP_175951940.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..700
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73259
     Region          38..634
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mhdaadqtra vaapprrlnr aaaaliarid iftprgayva rsviaaalal gvayllelet
       61 pysaastvll vinpvqgavi gkgvwrvvgt iagmvvafvl mgcfaqqpll filgfafwlg
      121 lcvagmtllr hfrasgtvva gytiglatyg amqhpeltfe hvigrgstva igvlclslvs
      181 mllgtrdvha klealvtrvt advaraiaaq rnglaaapad dkrhalfagi ygiddllalg
      241 kaesedlaqr aaavrhgmas lfgalaggtp plpadspgaq avaslqprla aawqaaadal
      301 gagpggaaha lallgdarer lrdaldgial gdprdeaawl iagerlieqi ddyraaldgl
      361 velqrprpgd rparvhfhrd tgaalrngvr sacaialsga fwlatgwnqg dmmllvvapy
      421 callatagnp aagaqafvkg tvlavpaafv cafgilprie gfpllvaala lfwmpgiyat
      481 svpktslagl aylvafntlt gatnpfrpdv alflnqsvaw vlatfltllt frlilprnla
      541 tdatrlrrti rddtlaliag krvtaagwqq rqqhriaqlg allasqpaam tqasiealaa
      601 lhvgkellri rrgaardglp daarrrvrag laglarhaaa ptraarharr aahalaglaa
      661 aqpgnaelkw lmaafadvhv llhtyaayft avperardaq
//
LOCUS       WP_175951904             167 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175951904
VERSION     WP_175951904.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..167
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17607
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mysnilvsld gsdtssrald aalglasetg arltpvyvvd flvpaydmvg ydpsilidaf
       61 reeglrvtdd aarrmkardv agtpqianve pagediphri vslaneiead livmgthgrr
      121 gaqrlflgsv aervlrlatc pvlmipascp sgqpaetvaa stekeps
//
LOCUS       WP_175951968             557 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Burkholderia sp. BCC0405].
ACCESSION   WP_175951968
VERSION     WP_175951968.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60409
     Region          25..384
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          453..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mttqsllaqy gpresmeydv vivgggpagl saairlkqla aekgaeigvc vlekgseiga
       61 hilsgavmdp raitelfpdw kergapldve vtedrflfls eksavatpnw alpanfqnhg
      121 nyvislgnvt rwlgaqaeal gveifpgfpa aeilynddgs vkgvatgnmg vgkdgepten
      181 fqlgmelhak ytlfaegcrg hlgrqliakf kldanadpqa ygigikelwe idpakhkpgl
      241 vihtagwplk sdtyggsfly hmdnnqvvvg fvvglgytnp ylspfeefqr ykthpsiraf
      301 leggkrvsyg araitaggll slpktvfpgg aligddagfl nasrikgsha aiktgmlaad
      361 aafdavqagr qsdelnaypd afkqswlyte lyrarnfkqw makglylgtl mvgleqkvmg
      421 gnvpwtlhhk hadhemlkpa sqcqpieypk pdgkltfdrl ssvfisntnh eenqpahltl
      481 kdanvpvnvn lrtyagpegr fcpaavyefv knddgsdrlv inaqncvhck tcdikdptqn
      541 ivwvtpeggg gpnypnm
//
LOCUS       WP_175952038             323 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175952038
VERSION     WP_175952038.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..323
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35324
     Region          38..190
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <186..307
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 msadpasara pslpprdrkr lvallralap degynltalp gvrilrsnra lsrtpvlydp
       61 givivcqgrk rgyfggecyl ydehhylavs vpvpfsmetd atperpllal ylhldftmaa
      121 elaaqidrag taepvqaprs mmstpmdatm hasvlrfvea mhrpldaavl gpallrelyf
      181 rvltgaqgsa mrsalamrgq fgrigrslrv ihadyaqpld vpqlaneagm svpsfhshfk
      241 aitqvspmqy lkstrlhqar llmvredlta eaagyavgyg spsqfsrefk rlfgltpake
      301 aqrmrasfai paafedaafv ssh
//
LOCUS       WP_175952060             235 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175952060
VERSION     WP_175952060.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..235
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26248
     Region          15..229
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mqtpskeddr rlvvnprgyt tatefaaqti rqhildgtla dgtplrqdel aaqlqlsrmp
       61 vrealrllev eglvdfqprk gaivaslspd dimeiyelra qlepyalrvs lphlsaeala
      121 haeklqrdie thpdpvqtga lnlefhltly sgverkrtma flaslslsvd rylrllmsql
      181 gyagksnkeh rtllrlcrkg dvdtacdllr qhlieggtal adfvrqrqag dsrra
//
LOCUS       WP_175952071             159 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175952071
VERSION     WP_175952071.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..159
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16793
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mykkimvavd gsasskqala eavkvalagd thvsavyvvd msvlfnyagr ldphalveel
       61 rddgrkvlre aeqvialaga kgeaelvete sigediaerl qryvkeggid lavvgthgrr
      121 girrvllgsv aerfvrgstc pvllirgddh dlaataaaa
//
LOCUS       WP_175952079             193 aa            linear   BCT 11-JAN-2025
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175952079
VERSION     WP_175952079.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..193
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=20949
     Region          47..186
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 mttftesrag lpddplhtgs papdgttdph pdphpkppps iaagfevrvq yasidagael
       61 apivrnpnvg avvnflgvvr negdvddvia levehyptmt eqalwsivee asarwrleai
      121 kivhrvgrip lgqavvlvvv aaahrgsafd aceflmdflk thapfwkkei rhdgvsgwve
      181 akahddqamr rwg
//
LOCUS       WP_175952130             270 aa            linear   BCT 11-JAN-2025
DEFINITION  creatininase family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175952130
VERSION     WP_175952130.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Yoshimoto,T., Tanaka,N., Kanada,N., Inoue,T., Nakajima,Y.,
            Haratake,M., Nakamura,K.T., Xu,Y. and Ito,K.
  TITLE     Crystal structures of creatininase reveal the substrate binding
            site and provide an insight into the catalytic mechanism
  JOURNAL   J Mol Biol 337 (2), 399-416 (2004)
   PUBMED   15003455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..270
                     /product="creatininase family protein"
                     /EC_number="3.5.2.10"
                     /calculated_mol_wt=28602
     Region          29..265
                     /region_name="ArfB"
                     /note="Creatinine amidohydrolase/Fe(II)-dependent FAPy
                     formamide hydrolase (riboflavin and F420 biosynthesis)
                     [Coenzyme transport and metabolism]; COG1402"
                     /db_xref="CDD:441012"
ORIGIN      
        1 mkclprtifa alaftvaqaa laqapgtvql edmtwtelrd svragrttil ipiggteqsg
       61 pyvalgkhna rvrvlseria eglgnaivap viayvpeggy tpptshmrfp gtitvpddvf
      121 ektlesaans frvhgftnvv flgdhggyqn dirqtvarln kswagtgara fvpaeyygts
      181 sdgydqilre hgvpatdigt hagladtsll lavaprmvrv dklrnaakpg avdgvyggdp
      241 rhasvelgrl gtdaivsrtv dairkeiagr
//
LOCUS       WP_175952139             306 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175952139
VERSION     WP_175952139.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 306)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 306)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 306)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..306
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33188
     Region          2..182
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          214..297
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdplsevlsl letrdsyftg lraggewava ipppdgikfn aivegscwlt vdgagspirl
       61 hagdcfllas prafslasdp svtpvpaasv ylnvergiaq ygepvncfli ggrfsyeegm
      121 plllgslppv vivsgdseqa avlrwalqrl ahefgkpspg aslmvrhlgh mmlveilrry
      181 vddgansdvg wlagfadsrv stalvaihae parrwtvdel atcchvsrst falhfkrrlg
      241 fgpleyvlrw rvqlamrelr rsnasisaia qmlgydsdsa fghafkrivg csprayrhdf
      301 asesgd
//
LOCUS       WP_175952157             146 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Hsp20/alpha crystallin family protein [unclassified
            Burkholderia].
ACCESSION   WP_175952157
VERSION     WP_175952157.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..146
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=15818
     Region          43..146
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 msdflfgtdl lgefdrlqrq maslfagypa slratrsetf pavnigstdd sieivafapg
       61 ldpaaidvsi dkglltisge rkppesneda etrvyarerf mgafrrviel pqhadpdkvn
      121 aryvngclti svgrseaskp raiavq
//
LOCUS       WP_175952163             234 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175952163
VERSION     WP_175952163.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..234
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25509
     Region          3..230
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtmakvaida hgvskwfgeg dartqalrdv smqasfgeml livgpsgsgk ttllsvisgi
       61 lrpesgsvsi dgvdlwaqpn daiadfrlnr igfvfqdyhl fprlttaenv aiplilkrrp
      121 wddaikealg ylevvglanr ahlppvklsg geqqrvaiar aivsqpdlli ldeptasldg
      181 dtgrmiidfv khkvlndtrc ivivthdari feyadrilrm edgrlngier ggar
//
LOCUS       WP_175952246             431 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: O-acetylhomoserine
            aminocarboxypropyltransferase/cysteine synthase family protein
            [unclassified Burkholderia].
ACCESSION   WP_175952246
VERSION     WP_175952246.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..431
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=46215
     Region          1..430
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 mtdqaasnwr letiavhggy rpdpttrava vpiyqtvaya fddtqhgadl fdlkvqgniy
       61 trimnpttdv leqriaaleg gigalalasg qsavtyaiqt iaeagdnivs asslyggtyn
      121 lfahtlpqyg ittrfadprd pasfeplida rtkaifaesv gnplgnvtdi aalaevahrh
      181 giplivdntv pspyllrpfe hgadivvhsl tkylgghgts lggaivdsgk fpwaehadrf
      241 krlnepdvsy hgvvyteafg paayigrarv vplrnmgaai spfnafqilq gietlalrve
      301 risdnalkia qhlarhdnve wvnyaglpdh pdhalvaryl sgrapgiltf gvkggrdgga
      361 kfqdalklft rlvnigdtks lathpastth rqlspaelak agvkeetvrl sigiehiddl
      421 ladldqalaq l
//
LOCUS       WP_175952285             236 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175952285
VERSION     WP_175952285.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..236
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25006
     Region          132..233
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(135..136,169..170,173,177..178,181,223,227)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mtskllrvas igafamvlga cttqsgltyd iravsipgkp dnvfrvscdg llgsanscar
       61 aaeefcrgqg ftplemidrv ysrapmkdpr eitfmcgkpq pvaqpapapq papapqpqpv
      121 qqrqvllqgd anfatdsaal tsqarndldr fiatnrgvef arvaitgftd stgsaahnrt
      181 lsearartvv nylranglqa rsftaeglga adpvasnata dgraqnrrve irldvk
//
LOCUS       WP_175952293             236 aa            linear   BCT 11-JAN-2025
DEFINITION  outer membrane protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175952293
VERSION     WP_175952293.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..236
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=25501
     Region          72..236
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mikqfalpss lallfsgaal adtiapetkr qdpgdagyya tarvvgafdn atnmeltspr
       61 vtnrvggpdg nssvtgaval gyqfgngwra egeytfkrtd nfvsywapfd ananefhvsa
      121 qrlmlngykd vdlgrgfsvy gtlgvgvaiv sadgwqtndt rrfasrtqtn laysagagvs
      181 yainkrfsid vgyryvdmgn vetgyntfan rvlardeqlk sklssnevfi glrgrf
//
LOCUS       WP_175952394             481 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia sp. BCC0405].
ACCESSION   WP_175952394
VERSION     WP_175952394.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..481
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51125
     Region          1..429
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfaslglid pllrnlqdln yqaptpvqak aipavlggkd vmagaqtgtg ktagfalpll
       61 qrlvqhgpav ssnrarvlvl vptrelaeqv lqsfvaygkg ldlrflaayg gvsinpqmmk
      121 lrkgvdvlva tpgrlldlnr qnavqfdqvq alvldeadrm ldlgfareln avfaalpaqr
      181 qtllfsatfs ddiramaati lrgpvnisvs ppnataskik qwvvtvdkrn kpdlfmhlva
      241 enqwehalvf vktrngvdyl aamldeagya vdtihgdkpq parlralerf ktgevqmlva
      301 tdvaargldi ddlplvinvd lpivaqdyvh rigrtgraga sgvavslvca deapqlaaie
      361 alikqtlrre eepgfeaehr vpetsatgqi ikkpkkpkkp kvpqaasgam papgkkprpr
      421 sgenqhkaaa pragsagqgk rlssgspfsa qkprgnpagk paagarkpag kpaggrgkrp
      481 s
//
LOCUS       WP_175952422             347 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175952422
VERSION     WP_175952422.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..347
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39049
     Region          12..194
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(15,17,102)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(49,101..102)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            100..102
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mreslytplv slvvpfyneg eaverffdvv iplmtsidai rfeivcvndg srddtlerli
       61 ristgerrvr vidltrnfgk eaaltaglde algdavipld adlqdppsli pvmiehwrdg
      121 aevvaakrss racdsfakrt aaaiyyrvhn llsdvklpen vgdfrlmdrk vvnalrnlpe
      181 rhrfmkglfa wvgyqtvive yqrdarsagh skfsgwklwn falegitsfs tvplrswtyi
      241 gvgiaalsfl yglfiivrtl lfgnavlgya slisvtlfig gieligigvv geyigriyde
      301 skqrpvylir rryqahskvi dlrvardarr qtarrrvqpa rarigar
//
LOCUS       WP_175952436             325 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175952436
VERSION     WP_175952436.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..325
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=36508
     Region          113..322
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mntifyafvi ltfvavvlti egayqwwnar hgaaarries riramsaggn vqqerlsilk
       61 krmldeskpl dqlllrvprv haldlliqqs gldwtlpklm vlsavfpala wlalsfatlp
      121 qlaalpialf agclptmyvm rcrrrrmrkl erqlpdicdm isralrsghs ftstlgmase
      181 efpdpmggef ritfdevnyg vslhdalmnl atrvpvqdlr yfviavliqr etggnlaell
      241 dsisalirer fklfdkvrvl saegrlsawi lgllpfgtag aiallnrefl svlwedpagi
      301 rmigvmlvsm afgllwirri vrirv
//
LOCUS       WP_175952463             188 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Burkholderia sp. BCC0405].
ACCESSION   WP_175952463
VERSION     WP_175952463.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..188
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=20231
     Region          <21..>113
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          110..186
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mqlvelppsa pptthaaska apiehtvskp vplrpaqpla pvrpaaavkr fdpapshdal
       61 ptqqpvaspe thtahatldd arpasatkad aatthsasag naqarlisqp lpelpddlre
      121 qgyqamavar flvhadgtfd idlvkptqnp rlnqilletl rrwrffpame ngrpvesqqd
      181 vrvhfnvn
//
LOCUS       WP_175952494             154 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia sp. BCC0405].
ACCESSION   WP_175952494
VERSION     WP_175952494.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..154
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17000
     Region          15..134
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mtsqdvcfti cavraeetyp lraailmagd eegsalhgdl apttrhfavr dtggivavas
       61 vckegqsgil sveawrlrgm avhpsvrglg fgrllvnlsi rhvreqhgll lwctaresay
      121 pfyemlgfnr dpepisirgr ddmrfylmqf qiac
//
LOCUS       WP_175952554             196 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0405].
ACCESSION   WP_175952554
VERSION     WP_175952554.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..196
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=19936
     Region          4..190
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mndflfglmi alsvgpvalm ianygmragt asgvraavgv atadgcyavv aftlgamlas
       61 tlaahlslcr lagalvllam garmlwqalr drrrtldgda rppgsrpfas mffvtlanpl
      121 tillfygyat aaagahrhwl lgaacvfags lagqlvfafg gsvigrivks pgllaashvv
      181 aalvvlgygv aglarl
//
LOCUS       WP_175952559             257 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175952559
VERSION     WP_175952559.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..257
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27158
     Region          3..249
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mttyivdavd salklltyva ehpnlgvtel asqlginksr tyrmlctlel hrfvvqdprt
       61 styalgpqaf vigvaasqqn alvraahrhm lalnqainet ivlrvregle svcvarcett
      121 havrtvgavg nrrpihfgas gkvllafapd avrdeylaql rrngqaddpa tlageldava
      181 rkgyavssge vtpgavgiav pvrdltgatv asvsvtgpev rvshadipdy lerlqacsla
      241 isaelgyvpa raalqpa
//
LOCUS       WP_175952594             221 aa            linear   BCT 11-JAN-2025
DEFINITION  O-methyltransferase [Burkholderia sp. BCC0405].
ACCESSION   WP_175952594
VERSION     WP_175952594.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..221
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23545
     Region          65..221
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mttltldpla sllarlfdea dasspatspd faslsrdeqa rlmrsktgyt dlyarlkdyp
       61 lavsretgvl lymlarsgga rsivefgtsf gistlhlaaa lrdngggrli tsefepskvv
      121 raranlsaag ladlveireg dalrtlaadl pdsvdlllld gakalypevl alveqrlrpg
      181 afvvadnaey spgylayvrs lengylsvpf ggdvelsmri g
//
LOCUS       WP_175952316             220 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175952316
VERSION     WP_175952316.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Kane,E.I. and Spratt,D.E.
  TITLE     Structural Insights into Ankyrin Repeat-Containing Proteins and
            Their Influence in Ubiquitylation
  JOURNAL   Int J Mol Sci 22 (2), 609 (2021)
   PUBMED   33435370
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Mosavi,L.K., Cammett,T.J., Desrosiers,D.C. and Peng,Z.Y.
  TITLE     The ankyrin repeat as molecular architecture for protein
            recognition
  JOURNAL   Protein Sci 13 (6), 1435-1448 (2004)
   PUBMED   15152081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12158766
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..220
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=23881
     Site            order(22,26..27,30..32,34..35,39,42,52,54,59,63..64,
                     67..69,71,73,77,80,89,91,93,97..98,101..103,105..106)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          22..52
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <24..111
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          54..89
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 msirwdgitg advlgeaeva rrhaladaar ngdwatmldl vakqpglvna trlggtsryt
       61 plhqaacgga pkevvvellq lgawrmlrda hgarpvdlae rrghrhlvdp ltpqprrfvp
      121 datlrdiqrh fhetilgria hlrvdalrlp eleplleldg qaerawfavp gmyggfgyvl
      181 rndgaaavlv seswsrvagg sgqrheitaq gctlvdegfv
//
LOCUS       WP_175952631             219 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175952631
VERSION     WP_175952631.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..219
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24795
     Region          2..207
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mmptlyahpf ssycqkvlta lyengtpfey ralahddpkp mqelaalwpl krfpvlvdag
       61 rtvieasiii eylglnhpgp vrllpddpha alevrvmdrf fdnyvstpqq kvvhdalrpe
      121 aerdargvad aramletsya wldkkmadre waagdrfsla dcgaapflfy adwthridps
      181 fanviayrrr llarpsfara vdearpfrsf fplgapdrd
//
LOCUS       WP_175952655             147 aa            linear   BCT 11-JAN-2025
DEFINITION  PaaI family thioesterase [Burkholderia sp. BCC0405].
ACCESSION   WP_175952655
VERSION     WP_175952655.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..147
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15768
     Region          1..135
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mtditdharg alraqpfsml lgtelmhigd nevslclpvr eelrqqhgfv hggvisylad
       61 naltfagalv lgprvitaey kinylrpavn gtlvaraklv yagrhqatcq chvfvidgdh
      121 erlvaiaqgt inrvgdgkvp dgpeeta
//
LOCUS       WP_175952699             468 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0405].
ACCESSION   WP_175952699
VERSION     WP_175952699.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..468
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47605
     Region          18..442
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(25..26,29..30,33,65,115..116,118..120,123,144,
                     147..148,151,274,277..278,281..283,286,314,318,370..371,
                     375,379,395,398..399,402..403,406)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtaaapnraa arrvlaatcv sytlvlldas ivnvaltdia htfgsrvagl qwivnaytla
       61 fasllitggt lgdrlgdrdv yiaglavfva asalcgvapt lpalaiaral qgvgsamlvp
      121 cslallnraf pepaarasai slwmgcggia masgpliggl lihlfgwrsl ffvnlplgla
      181 giwlgrtvar aagdgsrqfd wggqataiva iaaliatlie gpslgwrsap ivggaitsvv
      241 awsafiaiea rrrepmlpla ffrnrlfags tfvsmasafv fygllfvlsl fyrqirgasp
      301 ldtglaflpm tamvalggls sgrlaarfga rgsmcaafal yaagalgmtg msaatpawla
      361 vapmlaigfa sgfispaats palgtverhr agvaaaalna arqsgsalgv aifgaciatl
      421 qpfpaamrva lgiatglsal aattwwitar ltpatgepaa plrtatrr
//
LOCUS       WP_175952727             158 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175952727
VERSION     WP_175952727.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..158
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17942
     Region          4..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mttpldafdr kllmevqrda qtpqselgar vnlstaavnr rlkrlaedgv ierytavvap
       61 dkvdhpltiv vnveveseqi dqldamkrtf ercpqiqqcy yvtgewdfvl ilavrnmdqy
      121 naltrelffa nnnvkrfktl vsmsrvkvgl evpvepge
//
LOCUS       WP_175952745             309 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175952745
VERSION     WP_175952745.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..309
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33640
     Region          8..301
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mtssstpryr gifpvvpttf tdtgeldlas qkravdfmid agsdglclla nfseqfaitd
       61 derdvltrti lehvagrvpv ivttshystq vcaarslraq qlgaamvmam ppyhgatfrv
      121 peaqifefya rvsdaiaipi miqdapasgt alaapflarm areieqvayf kietpgaatk
      181 lrelirlggd aiegpwdgee aitlladlha gatgamtgga ypdgirpile awrdgrhdda
      241 yaryqawlpl inhenrqsgi ltakalmrag gviacerprh pmpelhpdtr aellaiarrl
      301 dplvlrwah
//
LOCUS       WP_175952749             158 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175952749
VERSION     WP_175952749.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..158
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=17323
     Region          5..153
                     /region_name="OsmC"
                     /note="Organic hydroperoxide reductase OsmC/OhrA [Defense
                     mechanisms]; COG1764"
                     /db_xref="CDD:441370"
ORIGIN      
        1 mahgehkyrv avewtgnrgt gtsgyreygr dhviragskp dlpgssdaaf rgdaarwnpe
       61 dlllasasac hklwylhlcs eagirvlayv ddaegtmldt peqgrfteiv lhprvtirag
      121 ddralaerlh hdahakcyia nsvnfpirce prvecaaa
//
LOCUS       WP_175952768             394 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175952768
VERSION     WP_175952768.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..394
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=40053
     Region          234..394
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mhemseadam nlgkktnene kpaamrrqtk aahgvsrlaf wlltllalml glgthpvfaa
       61 gtiscsgtaq tvalsmpvsv tiprdaavgt lltgwfstsn apnyytctvs gvvvagmvfe
      121 pqsltkagmt vaspnggtyt vwntnvpgvg vaigvttyan qcgtqawidl asstssqipl
      181 pwagwvcnts gtvtsitngg qiqaalvktg pvtagtvtgg vmvvgasatg tggsapytva
      241 asplmsfslt ptivnvsact tpnvtvnmgs plqseftgig stnkqavsfn vavnacptgl
      301 naiqyqfipv navldatngv lalssgstat giglqlkdgn gnalkyntqy tltsyssttg
      361 gsytipltar yyqtaasvtp gsanavltft mtyq
//
LOCUS       WP_175952779             312 aa            linear   BCT 11-JAN-2025
DEFINITION  GGDEF domain-containing protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175952779
VERSION     WP_175952779.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 312)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..312
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34652
     Region          44..311
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mtaatpslsd lviervgfgl fvldramtvl mwnrfmqdhs gipaadvigr nlfdcfpdlp
       61 rawlsrkles vfqlgsfafs sweqrpylfr fehdrpitgg vdymqqdctf mpltrgreve
      121 avcvtisdvt hvsvmqrere eavaklreha nrdgltgian rrffearlge efarwqrygg
      181 dmsvllfdld hfktindrfg havgdavlre tarrvasivr aqdtfgrfgg eefalllpct
      241 nldeamrvad kvrdaigsap vdaegvsvpv tasvggayak tgaptcdvlv neadaalyra
      301 krlgrdrsva ya
//
LOCUS       WP_175952819             434 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0405].
ACCESSION   WP_175952819
VERSION     WP_175952819.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45192
     Region          7..406
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mtsasssrsa wtyenrllli lfmtfgfvff drlalsflfp fmsaelhltn tqlgmvssal
       61 altwalsgaa tgawsdargt rkplliaavl gfsvcsalsg lvggfaslia fralmgiaeg
      121 pvlplsqslm vesstpsrrg lnmgllqgsa agllgamigp pvvigiatay gwrhafyvsc
      181 ipgfliafci wrwvreappg gvrhaqadta galaasgaav srwallkern illcmliscf
      241 fltwfiviis fapvflvesr hlspsgmgvv mtclgaawvf wgfavpaisd rigrkptmia
      301 falvaaacpi vmihagslwa lgalvfatyt glgcftlfma tipaetvppr aiasalglim
      361 gageliggfv aptvagfaad kyglpfamwt saagailacv lslglvetap avlrkralag
      421 aaasrldaqn lggr
//
LOCUS       WP_175952793             201 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175952793
VERSION     WP_175952793.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..201
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21999
     Region          14..143
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mntphdssge pgvrdrllda aealiysggi hatgvdaivk rsgaarksfy shfeskealv
       61 vaalerrdar wmrwfvdatl algkapraql lgmfdvlrdw frqpdfhgca flnasgeipd
      121 addpvrvvar mhkarllafv rerfdayade tgierrglar iarqwlvlid gaigvalvsg
      181 danaardara taellldtvs r
//
LOCUS       WP_175952822             521 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia sp. BCC0405].
ACCESSION   WP_175952822
VERSION     WP_175952822.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..521
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=55734
     Region          1..521
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 metydhivvg ggsagctvah rlvkagrrvl lledgpkdds lfiripatfi rvlgtrrtvt
       61 fesepqagaa grrtyvpqgr tlgggssvna mlyvrgtrdd yddwaalgct gwgwddvlpv
      121 fkraeshlrl sepfhgtdgp lrvgdtrfrh plslafvkaa qetgiayndd fngaaqqgvg
      181 fyhttifdgq rgstaatyla daighpnlrv ltgcrvtrir fdgrraagvd wrtengatgs
      241 aaahadivla agalstpkll mlsgigpgah lhahgidvlh dsrdvganyq dhlevsiygr
      301 shapvsllge drglkalrhg lqwmlcrtgl ltsnvvesga fvdttgsgrp diqfhvlptl
      361 vgdvdreplr ghglsinpcl lrprsrgsvr lrgndpaapi lfdsgalsdp advdglvrgv
      421 alarqiirap slarivreae tltdtalady vrrraktvyh pagtcrmghd ehavvtprla
      481 vqgvdglric dasvmprivs gntnapaimi aercaafmla e
//
LOCUS       WP_175952804             273 aa            linear   BCT 11-JAN-2025
DEFINITION  siderophore-interacting protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175952804
VERSION     WP_175952804.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..273
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=29691
     Region          5..266
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mqnpsertvt rvrhplkfrl lqvlrvhavt phllrvtlgg pdladfesas fddhvkvffp
       61 ppgaerpvlp algangpefp egepkpvard ftprrfdraa celdlefvln hpgpasqwaa
      121 qarvgqwlgi ggprgsfvip tgfdwhllig ddtalpavar rleelpagar vavvlevadr
      181 taqigfdtra dvheiwrfra eadaaggdvl lnavrdlplp psgdgyvwaa gealsmravr
      241 qhltgergvd ksriraaayw krgaaavhet led
//
LOCUS       WP_175952871             200 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease [Burkholderia sp. BCC0405].
ACCESSION   WP_175952871
VERSION     WP_175952871.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..200
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23017
     Region          <128..178
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 madaivqqfk tctsckserr vqdfakkrst kdglrpecrq cqarayaeya arnkerisaa
       61 naayykknka rkdaaatawq qanrlrener railraddpe sfrinerrrr arkkgaegsh
      121 tkaqasllle rqnfrcance ddlrvspknl dhwmpltlgg snylenlqwl cktcnvrkna
      181 kdpidwlvsi gkacrwpdqi
//
LOCUS       WP_175952930             293 aa            linear   BCT 11-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175952930
VERSION     WP_175952930.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472037
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..293
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=30758
     Region          71..217
                     /region_name="TadD"
                     /note="Flp pilus assembly protein TadD, contains TPR
                     repeats [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG5010"
                     /db_xref="CDD:444034"
     Region          156..186
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrrideivkv agvlamvgll ggcsafkesg ygvgpqaera almdaaaqkq aapdtpgmyl
       61 gliermqsqg lyyaslahid ayekqygasp qtillradal rmtdqpaast avytqllntt
      121 laargyrglg liaggagdfp raaqalsqat vlaptdastl sdlayaklrc gdvegaripl
      181 mkaaeldqnn pkiisnlvly llasgrtrda qklmaqqkls mdvrndirnd atkiaaaaht
      241 wrratqapas vstpigsgsv vdvsgsdvak rpspvaniqg fdptapllqr faq
//
LOCUS       WP_175952936             156 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TadE/TadG family type IV pilus assembly protein
            [unclassified Burkholderia].
ACCESSION   WP_175952936
VERSION     WP_175952936.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..156
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=16534
     Region          10..147
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mkrqcqppsr rrqqgatave falvfplffl imyaivtfgl ifavqqgltl aategartal
       61 nyvyesngsg tqaltdraka aqstaiglts wlanvqiptp vsgacsydat mycvtvtvty
      121 pyktnplvps lpllglvtpt qltgtatvqi npatil
//
LOCUS       WP_175952963             137 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175952963
VERSION     WP_175952963.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..137
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15349
     Region          19..106
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(20..22,36,53..55)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mtttvekvvl ppipakryft igevselcgv kphvlryweq eftqlrpvkr rgnrryyqhh
       61 evllirrire llyeqgftin garnrldspa aertaatpve peaqaadara pgkpgatvdv
      121 ialrqalldv idglkhg
//
LOCUS       WP_175952971             557 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Burkholderia sp. BCC0405].
ACCESSION   WP_175952971
VERSION     WP_175952971.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60422
     Region          25..384
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          453..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mtpaslieqy gpresmeydv vivgggpagl saairlkqla aekgaeigvc vlekgseiga
       61 hilsgavmdp raitelfpdw kergapldve vtedrflfls eksavttpnw alpanfqnhg
      121 nyvislgnvt rwlgaqaeal gveifpgfpa aeilynddgs vkgvatgnmg vgkdgepten
      181 fqlgmelhak ytlfaegcrg hlgrqliakf kldanadpqa ygigikelwe idpakhkpgl
      241 vihtagwplk sdtyggsfly hmdnnqvvvg fvvglgytnp ylspfeefqr ykthpsiraf
      301 leggkrvsyg araitaggll slpktvfpgg aligddagfl nasrikgsha aiktgmlaad
      361 aafdavqagr qsdelnaypd afkqswlyte lyrarnfkqw makglylgtl mvgleqkvmg
      421 gnvpwtlhhk hadhemlkpa sqcqpieypk pdgkltfdrl ssvfisntnh eenqpahltl
      481 kdasvpvnvn lhtyagpegr fcpaavyefm knddgsdrlv inaqncvhck tcdikdptqn
      541 ivwvtpeggg gpnypnm
//
LOCUS       WP_175953009             483 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0405].
ACCESSION   WP_175953009
VERSION     WP_175953009.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..483
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51208
     Region          26..445
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(36..37,40..41,44,84,134..135,137..139,142,162,
                     165..166,169,281,284..285,288..290,293,320,324,375..376,
                     380,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 msdslaasla aridrlpata giwklvlfls iggffevydl fqmtylppgl irdgifhtga
       61 rgvlgmsdqg algaatfigl figemfvsrl adrygrralf tgalllytaa slmmcvqssa
      121 lgvlvcrfva gcgvgaelit igafltelvp kavrgrafav cfavgylamp vlalvswlwv
      181 prdplgwsgw rwvvllggsg avvvwwlqsr lpesprwlvg agraaeaeri vqqlermver
      241 esgrplpavr lpaaavppar hapsmwgary rgrtamliaf ngflsigffg fsqwlptlla
      301 aqgatvaksl gyafviafay pvsplvaglv adrierkwli vasafgvalf gsafamsaqa
      361 sfviafgllv tlsstvlasn gtayqselfp tairgralgf vhsigrltga vssfivalll
      421 eragvsavfa liggsmlivm lsigafgprt nnrslddipd eaadaavakr partldalpt
      481 rrs
//
LOCUS       WP_175953077             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175953077
VERSION     WP_175953077.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34067
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdkwtqieff vqvaelgsls kaaerlgmss aaasrclnal eerlgarlve rttrrlwltd
       61 agheyhrrcv ailmelsead aavneasvnp agtlrvtasv sfasiylapa lpefhrrypn
      121 lnvqivaanr ypdfieagid vairtrehea dsgitvrkla etrrvlaasp gylakhgape
      181 tpdalgdhrl lvynlandpy vlhfrhgakk rsvtiksvld anegqviraa alaglgiliq
      241 plyiihddiv agklvpvltd wqlplltvni ayqsrrhqpa kirvftefli erferlglar
      301 kwkevgr
//
LOCUS       WP_175953028             311 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            sp. BCC0405].
ACCESSION   WP_175953028
VERSION     WP_175953028.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..311
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=31722
     Region          1..256
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mhafalqafn glsyglllfm lsagltlifs vqgvlnfaha sfymlgayvg ysiaastgfw
       61 palvlaplav gllgagcert mlrrvqargh tsellltfgl ayligegakl vwglaplpap
      121 vpalfdgapv tvfglalpry rlfmmgmsta mlvalgallr asriglvvra althraavea
      181 lgydvprvmt alfgagtala alagvigapl aviepalaet vgsvvfavvv igglgslgga
      241 faaslavgfa qtfaaasdts lrdltewagi alpdsvaavs iaqlaplvpy lllvvvlvar
      301 prglfgerad a
//
LOCUS       WP_175953082             326 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH:quinone oxidoreductase family protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175953082
VERSION     WP_175953082.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Shimomura,Y., Kakuta,Y. and Fukuyama,K.
  TITLE     Crystal structures of the quinone oxidoreductase from Thermus
            thermophilus HB8 and its complex with NADPH: implication for NADPH
            and substrate recognition
  JOURNAL   J Bacteriol 185 (14), 4211-4218 (2003)
   PUBMED   12837796
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..326
                     /product="NADPH:quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=33917
     Region          1..322
                     /region_name="QOR1"
                     /note="Quinone oxidoreductase (QOR); cd08241"
                     /db_xref="CDD:176203"
     Site            order(40..41,122,126,147,150..152,171..172,176,191,215,
                     237..238,240..241,262..264,314,316,318)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176203"
ORIGIN      
        1 mkallctafg pidslriedv atpepaagqv rvqvkaasln fpdalivqgl yqvkpalpfs
       61 pgaefagvid avgegvtawr pgdsvvaftg hggfaqqcva dvhqiaalpp gmtfeqgaal
      121 vlaygtslha lqqrarlqqg etllvlgaag gvglaaieia kalgarviaa assadklalc
      181 reagadetid yatedlrrrv deltggrgad vvydpvggay seaalrataw rgrflvvgfa
      241 ageipkialn lallkerdil gvfwgdavrr dpkqhvanmr llaewfaagk vrpaitervs
      301 lagaadaiar manrqvkgkv vilpda
//
LOCUS       WP_175953085             774 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia sp. BCC0405].
ACCESSION   WP_175953085
VERSION     WP_175953085.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..774
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81646
     Region          <68..>185
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          203..764
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msaselsvhn esrralllgf asgglllafg vpslaraavp vqppvsanpq yggagmphgl
       61 rddphlfvai apdgtvtvtc irsemgqgvr tsvalvvade lgadwarvkv aqavgdepry
      121 gnqntdgsrs lrqsfaalrr agaaartmle qaaaavwgvd thqvkamvhe vvdtksgrtl
      181 gfgelaakaa alpapdpatv vlkapaefry igkgetalid grdivggrah ygidtrldgm
      241 lyavvarppa ygdtvasfda saaeklpgvv kvvqlaptpl psgfqplggv avvardtwta
      301 iqaraqlkid wkrgphanyd saeyrktlea aaaqpgdvir ndgdaaaala gaakrvraty
      361 yiphlahatm eppaavarva dgrcevwtct qapqttrdev akalglpter vtvnvtllgg
      421 gfgrkskpdy vveaallska agapvkltft reddiahdyf havsleafdg gldasgnvva
      481 wqhrtvapsi qstfragvvh eqpgelaqgi adlpfaipnv rienpaaqah trigwfrsvy
      541 niphafgiqs fvselahaag rdpkdfllel igparrfeph iavrnvnyge dpalypvdtg
      601 rlrrvvetva rgagwgralp kghglgiaah rsfvsytaav cevqvdadgk itvprvdiai
      661 dcgpqvnper vrsqlegavv mglgialhge itfkdghpeq snfngfqvlr mneapreirv
      721 hlvapddfat plggvgepgl ppvapaltna ifaatgtrir slpvadqlak rrag
//
LOCUS       WP_175953103             156 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia sp. BCC0405].
ACCESSION   WP_175953103
VERSION     WP_175953103.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 156)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..156
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=16818
     Region          8..>96
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mkrggaartv scgvvildga grvflahatd tthwdipkgq gepgespada alrelleetg
       61 iafaparlld lgrfayrhdk dlhlfavqva dgeidpaqct ctslfpsrrd gsmipemday
      121 rwtvpgdida yasrslarlf rtklslvalh rrltgg
//
LOCUS       WP_175953113             389 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Burkholderia sp. BCC0405].
ACCESSION   WP_175953113
VERSION     WP_175953113.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..389
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39978
     Region          61..369
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mntikridpr rpfiitaagl kritlgeegs adanavhgfa hghgaaaakp rravqdpkhv
       61 mlvvahserg alddhsrqai aaaalladaq tevallafge lkddvaelgv dkllelagfd
      121 rrafdpesel qalqacvaal apkhvfapdn atgdgdlgrr yaaaagasva thvveidakh
      181 vgayaqagra fatralpdvi llaqnavdak lpfvgagerl aadfirpahd aaqpyrdlgl
      241 deidaaqval eeadfivsag ngvsdigafe rlagafgaai gasrvavdng hftrdkqvga
      301 tgktveasvy iafgisgavq hlqgikdcrh viavnldgsa piakranltv vgdaqgtiaa
      361 lieqvqaara argespaavg trepegvaa
//
LOCUS       WP_175953148             345 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0405].
ACCESSION   WP_175953148
VERSION     WP_175953148.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..345
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35735
     Region          46..345
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msndthpvpp lasgdtpaga sgfrarffnp aarqkllafa sllllivffs iaspnflevd
       61 nlvailqata vngvlavact yviitsgidl svgtlmtfca vmagvvltnw gmplplgila
      121 alcfgalsgc vsgfviakmk vppfiatlgm mmllkglslv isgtrpiyfn dtpgftsiaq
      181 dsligslipa lpipnavlil flvaigasiv lnrtifgryt falgsneeal rlsgvnvdaw
      241 kiavytfsga vcgiagllia srlnsaqpal gqgyeldaia avviggtsls ggagsivgti
      301 igafimsvlt nglrimsvaq ewqtvvtgvi iilavyvdil rrrrr
//
LOCUS       WP_175953169             285 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175953169
VERSION     WP_175953169.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 285)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033773
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..285
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31312
     Region          24..146
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          201..278
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mtktakdidt pdhwlvarrd qetgieslha hfnghaydah dhddmlvgft eqgvqqfqch
       61 rsvhtsvpgr ailiepgamh dghapeaggf tygmlylpqa wveraarrld lpglggveas
      121 fghtlvddrg lvdairhafl aihgnegkla rdqtldrlll rlggelrgpl vlesgvvppa
      181 iarvrdllha qmdgniglde lasvagidrf rltrlfqraf gtsphaylvr lrlraarrll
      241 aagrtpaqaa advgfadqsh lgrwfrrayr itpaayrqlc tnvpd
//
LOCUS       WP_175953171             249 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia sp. BCC0405].
ACCESSION   WP_175953171
VERSION     WP_175953171.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..249
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26241
     Region          2..236
                     /region_name="17beta-HSD-like_SDR_c"
                     /note="17beta hydroxysteroid dehydrogenase-like, classical
                     (c) SDRs; cd05374"
                     /db_xref="CDD:187632"
     Site            order(8,10..13,33,51..53,75..78,98,125..127,140,144,173,
                     175..177)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187632"
     Site            order(99,127,140,144)
                     /site_type="active"
                     /db_xref="CDD:187632"
     Site            order(127..129,134,140,171..172,178,194,197)
                     /site_type="other"
                     /note="steroid binding site"
                     /db_xref="CDD:187632"
ORIGIN      
        1 mktvlitgcs sgfgleiarh flardwqvva tmrtpredvl ppserlrvla ldvtnadsir
       61 aaidaagpid vlvnnagfga aapaelmpld tvralfetnt igtiavtqav lpqfrqrgag
      121 vivnvtssvt lkalplvgay raskaavnay tesmavelep fgvrahlvlp grapdtrfgd
      181 narahmhgfe heayaafvgk avarmldasg pithardvae avwhaatdps spmripagad
      241 aeawaaetr
//
LOCUS       WP_175953172             433 aa            linear   BCT 11-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175953172
VERSION     WP_175953172.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..433
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46265
     Region          14..431
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 mslnddptfw rnarqhlvry ggtfepmive rakgsfvyda dgraildfts gqmsavlghs
       61 hpeivsvige yagkldhlfs gmlsrpvvdl atrladitpa gldralllst gaesneaair
      121 maklvtgkye ivgfaqswhg mtgaaasaty sagrkgvgpa avgsfaipap fayrprfern
      181 gthdflaeld yafdlidrqs sgnlaafiae pilssggiie lpegymaalk rkceergmll
      241 ildeaqtgvg rtgtmfacqr dgvtpdiltl sktlgaglpl aalvtsaaie erahalgylf
      301 ytthvsdplp aavglrvldv vqrdglvara nvmgdrlrrg lldlmerfdc igdvrgrgll
      361 lgveivkdrr tkepadglga kitrecmhlg lsmnivqlpg mggvfriapp ltvsdeeidl
      421 gvsllgqaie ral
//
LOCUS       WP_175953184             741 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia sp. BCC0405].
ACCESSION   WP_175953184
VERSION     WP_175953184.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 741)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..741
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81007
     Region          58..741
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mryevlepgr srtkgarvar lrrgcwrqsl ylglliaahp aaafadaapa adaevrkeet
       61 tavkpaagel kaisvsasrg vaddpsvatv gkmplalrei pqsvsvttre ridqqnlysl
      121 devmqqsagv tvqpyvlltt ayfvrgfkvd sfefdgvpvv igdmasapqd isvyerveil
      181 rgangllhgs gnpaatvnlv rkrpqyqfsa nasvsvgswd ryraeadigg plnaagtvrs
      241 rlvaayedrh ffydhakqdt rsiygitevd vtrdtlltfg aqyqttrsvp dmsgvpmard
      301 gsslglprst fldtawghfd wdttrafasv eqklgagwka kvsgeyqsvr sdlkyagsyg
      361 aidpatgagg altggayqfs sysrsldanv qgpvhafglt hdllfgvtya nsssgqmsaq
      421 llgnvagtpv nvyrwnpssv pepdvgpyqq sqqndisqkg vyglgrikla epvtlvlggr
      481 vswwnqdslg ahyntghqft pyggliwdfa rdwswyasya evfqpqtksm wgggiltpvk
      541 grtyetgvkg elaggklnvs laafridldn npqvdlahpc agpncyyvng gsvrsqgfef
      601 eangritpww svwasytydt mryadnlana gssfapllnp rhlfrlwtny dlpwqerrws
      661 iggglqvqsn ysaqangvtm sqggyalasv rlgyrydkrw saavnvnnlf drkyylslsn
      721 pgwnnrygep rnvmltvrgq f
//
LOCUS       WP_175953216             379 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175953216
VERSION     WP_175953216.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..379
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41886
     Region          26..362
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 mstpvtnhda faerasevqf rvvnrvalit lnrpaalnal syamigelaa llercrdddq
       61 ivavvlrgag ekgfcaggdv ralyrmvaqr etwlpffvde yrldyaihtf pkpvvalmdg
      121 vtmgggmgla qgaalrvate rskiampetr iglvpdvgat hflsrmpvel elyvgltgam
      181 lsgadaltak ladlcvpsaw ldtfetries vkwegdvlpl lrkvfeppcn vvphaaldsq
      241 mpwivrhfdk rstverivat ltqdlareel srehrqwlqa tlealtghsp tmlsvtreal
      301 lrgrqmtlae sfrmelgiva raieegdfce gvrahlvdkd rkprwapasl velraervrh
      361 fltspwklfa hpladlgaa
//
LOCUS       WP_175953217             309 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175953217
VERSION     WP_175953217.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34134
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..291
                     /region_name="PBP2_CrgA_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08475"
                     /db_xref="CDD:176164"
     Site            order(103,107,146,161,163,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176164"
     Site            order(104..105,109..110,112..113,116,120,122..128,190,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176164"
ORIGIN      
        1 mtdrldgvtt fvqvvesgsf alaaerldmt rsavgkavar lekrlgarll qrttrsqslt
       61 ddgqayydrc vralaeleaa eadldcgrne prgklrlsvp lafghhcvtp ivldlartyp
      121 hlridvsitd rfvdlveegi dlavrigtla dstslavrrl gtqygslgaa psylarygmp
      181 ktlddlkdhr tiaysrsgvi qpwdlrapdg stvrvdmphq lsfddvqaia aagasgfgia
      241 wlpswlldhy vkrgemtvvl drcfvcegdi haiwpktryl prktrcvida laqaippmie
      301 rrdevnemk
//
LOCUS       WP_175953226             467 aa            linear   BCT 11-JAN-2025
DEFINITION  HdeD family acid-resistance protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175953226
VERSION     WP_175953226.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..467
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=51742
     Region          <48..185
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mvrlvllllg ieylrtrwrg ltvlgwvwvv agvvifvdal dgalhfpiqi fawlfliegl
       61 atlavagsgv ggqrilryvk givvvvaagl vfaghhhghf llsmifgtlf lvdgllqcta
      121 awmvryrrwn vafawgvvei llaiffyqpy pthyvgtvpy clglllmfgg mhmlslaarv
      181 rrltrnpafa tspapalapd lddtrdrphf aqsewdgppa dgehaltvhv wtptgtskae
      241 aqrypvidry iaavdvngvi stghaaleap egiyislypg veidrspdef trilratren
      301 dvpglfqpdy ateskawcps tvrvrirnyd pakldafwss yrqdatynlt hrncsstvsn
      361 aleaaldgav wrlkgaragw gafvrllltp elwvaaqirk ravtmawtpg ltldyarals
      421 mladprpfaw wkvarsavka imlsrrtwre qdnaalspgq seaasmk
//
LOCUS       WP_175953305             209 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175953305
VERSION     WP_175953305.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..209
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22448
     Region          18..172
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maesssripl sprkaprqrr slatvdaive aaarilerdg fdgyttnava alagvsigsl
       61 yqyfpnrdal taalveresa hllddvdrag alsscddvlr alvraavahq mrrpvlarli
      121 dfeearlplg artarvtdri hatllhalgl rdaprvaapd vvahdllaiv kgivdaagar
      181 getdadalda rvwramrgyl resreskla
//
LOCUS       WP_175953314             400 aa            linear   BCT 11-JAN-2025
DEFINITION  Fic family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175953314
VERSION     WP_175953314.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..400
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=45248
     Region          18..370
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mttaatfepl fpedrvldpl leqaaelvds shrllavrdt plavalvpql ramnsyytnk
       61 iegqhttpak ieaalhrdys tdiverkkqr favahiatea aleeewrtlp vaalfeptri
      121 saihdrffsg lpvderltge gkaivpgefr rsnvtvgrhl apepemietl lqawatrysr
      181 irakeyqlig iacshhrltw vhpfmdgngr varlhshlgl raadlthglw splrglareh
      241 eqyyarlsea dqtrrndldg rgnlsqeglv kfarffldcc qdqvgfmvhm tefegvtgrl
      301 ldllrylean pwtirseksv ikpeaaalam efvalrrtvt raefaqmlgv sdvlarrivr
      361 slldygllts pshrgelsfg lplnglrflf prlwpevele
//
LOCUS       WP_175953334             319 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175953334
VERSION     WP_175953334.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18598969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..319
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35468
     Region          1..283
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          15..97
                     /region_name="cupin_MtlR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to MtlR, N-terminal cupin domain; cd06976"
                     /db_xref="CDD:380381"
ORIGIN      
        1 mmhpdlevvd vrrdesfkvw shgypyrtir whfhpefelh livatrgkyf vgdhigsfgp
       61 ghlvllgpnl phnwvsdmae getverrnlv iqfdpafvrr cmdafpecrd aqallddarr
      121 gvgfdaatsa aiaplfdell aargmrrial fmtilerlcg aaertllasp aydqadvtpt
      181 rlshalsyig khlaselres dlaqltgqsv safsrafhrh tgmpfvqyvn rlriesacqm
      241 lladdasitd icfqagfnnv snfnrqfrav kgmapsefra lqrlnarsre lalhaaptgn
      301 plpprivtpg vparapqpg
//
LOCUS       WP_175953370             184 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175953370
VERSION     WP_175953370.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..184
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20329
     Region          5..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mstltrndwi aagfdaldge gyagisaesl arrlnvtrgs fyhhfrnred fvrtlltawe
       61 ddytarmlay aagghgagdt larylriaae krpgreiair awalhdplva qfqqrvdaar
      121 lafaietsrg lvrtpgeaei vgqavhlcli ggqqaglrrd adrfngfmqr aaamvervlp
      181 mrrt
//
LOCUS       WP_175953367             294 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia sp. BCC0405].
ACCESSION   WP_175953367
VERSION     WP_175953367.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..294
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30453
     Region          3..286
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mqtavgfigl gvmgtpmaln laragtplvv wsrshgsdda lrhagarvae hiddvfaacs
       61 tvilmlanda aidavlargt pgfaarvggh tivnmgtnap eysrsladdi aaasgryvea
      121 pvsgsrkpae agqlvvmlag apddvdavra lvrplcrdsf vcgdvpsalt mklavnlfli
      181 tmvtglteat hfaqrhgidl arfadvlnag pmasdvsrvk lgklvaadfs vqaaitdvlk
      241 narlvaesar gigiasplld ichalygete raghgahdmv aviraieqrt ddar
//
LOCUS       WP_175953380             311 aa            linear   BCT 11-JAN-2025
DEFINITION  SPFH domain-containing protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175953380
VERSION     WP_175953380.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..311
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33521
     Region          2..282
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 mdsliiwvvl lviaivivsk tvkivpqqha wvlerfgryh atlspglniv lpfvdriayr
       61 hvlkeipldv psqicitrdn tqlqvdgvly fqvmdpmkas ygssnfvlai tqlsqtmlrs
      121 vigkleldkt feerdfinhs ivsaldeaaa nwgvkvlrye ikdltppkei lhamqaqita
      181 erekraliaa segrkqeqin lasgareaai qksegerqaa inqaqgeaaa ilavaeanaq
      241 aiqkianamq sqggmdavnl kvaeqyvsaf snlakqgntl ivpanlsdlg taissaltiv
      301 ksaaaasggk a
//
LOCUS       WP_175953381             144 aa            linear   BCT 11-JAN-2025
DEFINITION  NfeD family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175953381
VERSION     WP_175953381.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Green,J.B., Lower,R.P. and Young,J.P.
  TITLE     The NfeD protein family and its conserved gene neighbours
            throughout prokaryotes: functional implications for stomatin-like
            proteins
  JOURNAL   J Mol Evol 69 (6), 657-667 (2009)
   PUBMED   20012272
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Kuwahara,Y., Ohno,A., Morii,T., Yokoyama,H., Matsui,I., Tochio,H.,
            Shirakawa,M. and Hiroaki,H.
  TITLE     The solution structure of the C-terminal domain of NfeD reveals a
            novel membrane-anchored OB-fold
  JOURNAL   Protein Sci 17 (11), 1915-1924 (2008)
   PUBMED   18687870
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..144
                     /product="NfeD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=15262
     Region          3..142
                     /region_name="YbbJ"
                     /note="Membrane protein implicated in regulation of
                     membrane protease activity [Posttranslational
                     modification, protein turnover, chaperones]; COG1585"
                     /db_xref="CDD:441193"
ORIGIN      
        1 mmsghlfwwv avgvlvvael ltgtfyllmi algflaggll qlagfaphvq fgaaavvaiv
       61 amivlrrsgl grkqkrdtst npdvnldiga tvtvdawrdg rarvqyrgad wdvelanger
      121 ddahvyqvsa vrgsclvvva kpag
//
LOCUS       WP_175953412             513 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia sp. BCC0405].
ACCESSION   WP_175953412
VERSION     WP_175953412.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..513
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=54505
     Region          35..440
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mtssinsspl naiadqalgl ddaaapaave pasdepsfas lglspeivsa lqaagyvkpt
       61 pvqqraipag iagrdllvss ptgsgktaaf mlpaierfaq lqktlaqqpr apreasqgdr
      121 rvrrpqpvar pgllvltptr elamqvttaa stygkhlkrl rtvsilggva ygqqlmllak
      181 npeilvatpg rlldhlergr idlselkmlv ldeadrmldm gfiddietiv aatpatrqtm
      241 lfsatldgki gsltsrllkd perieiqqrl esraniaqtv hyvddrdhkd rlldhllrdd
      301 aldqaiifta tkidadqlag rladagfesa alhgdlpqga rnrtiralre rrvrvlvatd
      361 vaargidipg ithvfnydlp kfaedyvhri grtgragrsg iavslvhhae qgalkrierf
      421 vrsplpvnvi egfeprkapp rnggtggrgr pgggnsggrr fggkpggghg gngrsygggn
      481 gggwsgkpgg srdggprrdg qrsggprrsn sas
//
LOCUS       WP_175953421             308 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175953421
VERSION     WP_175953421.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..308
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31993
     Region          43..294
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mssprlsrrh ftiaaasasl aactsfgdks rpgnasgatq phekpvkigi algggaargf
       61 shigvlkale argipveiva gtsagsvvga lyasgmsalq inkialdmdq aaisdwalpf
      121 rsrgllqgva lqnflnktln nrpiekmakp lgivatdlqs gqpilfqqgn tglavrascs
      181 vpsvfepvki gnreyvdggl vspvpasyar kmgasfviav disarpdgaa tnnpiemllq
      241 tftimgqtik tyeldkyadv virpnlnamg gsdfnqrnaa ilageeavar impelqrkla
      301 aargvaaa
//
LOCUS       WP_175953436             537 aa            linear   BCT 11-JAN-2025
DEFINITION  inorganic phosphate transporter [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175953436
VERSION     WP_175953436.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10475700
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..537
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006817 - phosphate ion transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57316
     Region          71..519
                     /region_name="PHO4"
                     /note="Phosphate transporter family; pfam01384"
                     /db_xref="CDD:460184"
ORIGIN      
        1 mntteplapt ktlghrllga dwkwhtffga ilvaaliwfg awafgyvegg enrilllltv
       61 lfgvfmafni ggndvansfg tsvgaktltm kqalvvaavf evsgavlags svtktvrsgi
      121 vdlesitlep rdfvyimmaa llgaalwllf atwqglpvst thsiiggivg aaiaigirtg
      181 aggldmvqwd qigqivmswv lspllggiaa ymlysaikqh ilvyndhada klreiktera
      241 mhrqrhrehf drlselqqis ytnmmardav tlnmpdfdye elesdyyrel yrieekaegv
      301 nahkalltwv pmlaglgsml iasmlmfkgl knlnltidsl gtaliiamig aavwmavfii
      361 aksqrkkdla kstftlfawm qvftaaafaf shgsndiana igpfaaildv lrhnaiqsts
      421 vvppaltlic gvalvsglwf igrnviktvg sgltemhpas gftaelaaaa vvmaaslagl
      481 pvssthilig avlgigivnr aanwglmrpi alawvitlpa aagvsaaaal tlkavfg
//
LOCUS       WP_175953506             318 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter permease [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175953506
VERSION     WP_175953506.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 318)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..318
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33516
     Region          12..284
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mildiltqtv yqrvlvgtal igfscgllgt ftylrrqali advvghstml gvtsaflfsv
       61 lalgidgrnm ivivivsaiv gvlssalssf leritplghd ttmavilalt fgggmallse
      121 inkrtfpssk aglkdylfgn attltwsdir isgafalaal lvvlilwsdi qlyifdaaaa
      181 tvlgrpvrlv sialtsatvi givigvkavg lvlvvayvil pavsarqwvn smrsmailag
      241 lfgmfasvag siisitagkl ptgpttvivl tlltvfslla aperslilra irrrqarqvl
      301 leqlqreaqg stmqevta
//
LOCUS       WP_175953508             316 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter permease [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175953508
VERSION     WP_175953508.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 316)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 316)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 316)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..316
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32934
     Region          13..277
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mtpyaagvmm lmvltaitca lpgaflvtsr qsmlvdamsh aafpgivlaa liwpigspyl
       61 iigaallall vviaseaveh tglvsrdaaq gllfpglfsv gvvllstkfa hlhlhedavl
      121 vgdpnivavt hltifgvdvg psyayvmlgv lalnalflvl thrqlsvvvf dadyartigl
      181 pvrglrmaam vlvaitltas fyaagavlvi afvvvpaata slfarsfpgv iwgsvgiaav
      241 itvpvflaty ytarptsswt awafgavfvl aavvrhlgrv lhharlrsgv eadsqgeaea
      301 evasapearv raekvv
//
LOCUS       WP_175953531             240 aa            linear   BCT 11-JAN-2025
DEFINITION  (Fe-S)-binding protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175953531
VERSION     WP_175953531.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..240
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25849
     Region          <2..237
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mrvglfvtcl vdlmrpeigf salklirdag yevivppaqt ccgqpaynsg dralardlae
       61 ktlrefeqfd yvvapsgscg gmirahygdl frddpelmgr ylrfqqkvye ltdflanvak
      121 vslapgeftg pvtyhdscsg lrelgvkaqp rallaqcgia vtemkdcehc cgfggtfaik
      181 ygdisaaiad ekcanvrasg tgavvlgdlg cmlniegrlr rtgdrdtrvl hiaqvlagdv
//
LOCUS       WP_175953545             442 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175953545
VERSION     WP_175953545.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..442
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47283
     Region          43..425
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mgffrrngfe trqqiaaflt vvfsgqiiys afesfkipfy qrlvtyyglt dtqfgllfta
       61 lgvavffyip ggwvnnrfna rsilmvglay rcitalilig ltpslpegik fpvmfaitls
      121 wgvwdsvfwp avvkgvvlfs grdnkgfglg vltafragge atlngiligv maiaggslia
      181 fkwgmivyac ltlpmillih rfvpadprte gdasgedtea vtgkealagl lqtlriprvw
      241 lagiagmcvy wvyttlvytt pffvrvyafd envaalyatv naillglsgg ilggiiadkv
      301 fkssattiai tltlgagflv ilaflpggsd nswmavaals afafvtmmak giqqapvael
      361 hlpstmvgsa msvnsfmafa cilwattlng sildahkdsp stgftlifll magvglsgal
      421 lsawlevlnr rhnrrqaaal sa
//
LOCUS       WP_175953582             404 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid aminotransferase [Burkholderia sp. BCC0405].
ACCESSION   WP_175953582
VERSION     WP_175953582.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Alexander,F.W., Sandmeier,E., Mehta,P.K. and Christen,P.
  TITLE     Evolutionary relationships among pyridoxal-5'-phosphate-dependent
            enzymes. Regio-specific alpha, beta and gamma families
  JOURNAL   Eur J Biochem 219 (3), 953-960 (1994)
   PUBMED   8112347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..404
                     /product="amino acid aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43555
     Region          1..396
                     /region_name="PRK09257"
                     /note="aromatic amino acid transaminase"
                     /db_xref="CDD:181731"
     Site            order(102..104,130,183,214,243,245..246,254)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(105,140,207,252..254,290,293)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            246
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 myehipaypg dpilslfqaf qqdahphkvn lsiglyydds gripvldstg iaaarlreag
       61 aphtylpmeg laayrqgvqr lvfgddcaal aegriatlqt lggsgairlg aefvkryfpd
      121 saiwisdptw dnhrvifsaa gldvhtypyy dalrngirvd amlttldalp arsvvllqpc
      181 chnptgldlg rdawravidv larrglipfl dmayqgfgdg laddawavra ivdaglpaiv
      241 gnsfsknfsl ygervgglsv vcanageaat vlsqlqagvr rtysspplfg aqlvstvlnd
      301 dalrvrwdde vaqvrarikr mrgelkarld arlpdrafda lvtqrgmfsy tgmaatdvdr
      361 lrashgvyll rsgrmciagl ndanvdhvan aiadvlggas rqaa
//
LOCUS       WP_175953587             266 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Schaalia sp.
            Marseille-Q2122].
ACCESSION   WP_175953587
VERSION     WP_175953587.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..266
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26592
     Region          15..259
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mtdgptrkkl tpgriaavig igiaagflag lfgvgggmmi vpalvlildm sqrqaaatsl
       61 ssivittavg sisyatqgqv slpamllvag galvgaqigt wllrvlperi lpwifvgfaa
      121 miiiihqlhe svrtatievt vasaiamigv glvsgvfagl vgvggggiiv pgleivvgag
      181 dliargtsll amiptalsgt ysnlkhglvd lpvgliigaa aasttplglw aanavsprtg
      241 sylfgvflva vsistvlkar arrarg
//
LOCUS       WP_175953603             360 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175953603
VERSION     WP_175953603.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..360
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36897
     Region          42..345
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msptptttap tstqasgkes tprtggsapr srqgvlhslt smrempviia lllliavtwa
       61 inprflsaqg vkdlllnati amimaagqsl vittksvdls vgsilgmsay mtgvlfatyp
      121 aipiplvfla ctllgaalga fngmlvtqar vpamvitlgt lyvfrgslnw wagssqyfag
      181 drpaafgdlg vatlagvpll tllaviviii vsmyqryars grdlyaigsd paaaevygip
      241 vgrrvfaafv angalvglag vlyasrfnsv gattgtgmel divaacvvgg vaivggvgka
      301 ygaalgalll ttitsaltav gldkfwqrav vgalilvaiv ldrmvtigrl gkqrktgghp
//
LOCUS       WP_175953680             307 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter permease [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175953680
VERSION     WP_175953680.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 307)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 307)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 307)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..307
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31352
     Region          12..273
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mseqltllfs sslmqrslli allvglsapi vgtylvhrrl amlgdgighi altgvalgwl
       61 agtaanaasa dqyaipgall vsllgavsie vvrssgrtsa dvalamlfyg giaggvllig
      121 laggtsaqlt sylfgsistv twsdititsv lavgilavga glapalysvs ndeefarstg
      181 lpvrtlsmli avmsaltvav smrvvgallv saimvipvai aqlwaksfms tmvysasiga
      241 mvclsgliit yfidlspgam ivmlaiglya lsftgrtlvd rqrraqrhrq aaaasaqsga
      301 tctvqnp
//
LOCUS       WP_175953683             399 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid aminotransferase [Burkholderia sp. BCC0405].
ACCESSION   WP_175953683
VERSION     WP_175953683.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Alexander,F.W., Sandmeier,E., Mehta,P.K. and Christen,P.
  TITLE     Evolutionary relationships among pyridoxal-5'-phosphate-dependent
            enzymes. Regio-specific alpha, beta and gamma families
  JOURNAL   Eur J Biochem 219 (3), 953-960 (1994)
   PUBMED   8112347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..399
                     /product="amino acid aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42457
     Region          3..398
                     /region_name="PRK09257"
                     /note="aromatic amino acid transaminase"
                     /db_xref="CDD:181731"
     Site            order(107,142,209,254..256,292,295)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mslfsavqla prdpilglne afnadarptk vnlgvgvytn eegkipllra vreaekvrve
       61 aglprgylpi dgiaaydaav qklllgndsp liaagrvvta qalggtgalk igadflrtvn
      121 pnvkvaisdp swenhralfe aagfevvayp yydaatngvn fegmlsalng yaagtvvvlh
      181 acchnptgvd ltdaqwqqiv dvvkarnlvp fldmayqgfg enieadaaav rlfaaadlna
      241 fvsssfsksf slygervgal siitsskeea trvlsqlkrv irtnysnppt hggavvaavl
      301 aspelhaswv qelgemrdri ramrnglver lkasgvdrdf gfinaqrgmf sysgltsaqv
      361 drlrdefgiy avgtgricva alntrnldav anaiaavlk
//
LOCUS       WP_175953690             293 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar ABC transporter permease [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175953690
VERSION     WP_175953690.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790449
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..293
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31955
     Region          8..293
                     /region_name="MalG"
                     /note="ABC-type maltose transport system, permease
                     component MalG [Carbohydrate transport and metabolism];
                     COG3833"
                     /db_xref="CDD:443045"
ORIGIN      
        1 maqkqelhts vtgsrwwaev gwryivgvlv viycivplly ilsvslvpga tltgsnelfr
       61 tisfqnyvdl fnhpdykhwv vnslivssit aigtvlmgaa aayafsrfrf kgrrgtltfl
      121 llvqmfpqml afvalfllll giqevfpalg lnshfgliav ylggalgsnt fllygffnsv
      181 preldeaaei dgcshaqtfw tiimplvlpv lavvsllsfi ssfgdfviak vvlqtpdkft
      241 lavgmyqwaa ddriapwglf aagavvaavp villfqylqr yivsgltaga vkg
//
LOCUS       WP_175953797             215 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0405].
ACCESSION   WP_175953797
VERSION     WP_175953797.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..215
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23039
     Region          1..212
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mslhtyllfl pacfalnmaf gpnnvlslsn garngvlhsv tasfgrlaaf aimiaitgfg
       61 lgalllaset lfsvlkfgga aylvwlgikl lrskpaeqpv vetepavark dradllvkhc
      121 kqefyvaagn pkailiftaf fpqfvdrthy tlsftalgat flmlelvaiv tyavigarlr
      181 slatnpkgft wlnrasgslm igfgvllaml rrpaa
//
LOCUS       WP_175953791             312 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175953791
VERSION     WP_175953791.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..312
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33416
     Region          9..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrftcigvf vaavdegsla aaarryglsp amagkyvsal eaelnarllq rttrrlslte
       61 vghtyydrck rileafdean reasdsqgva rgvlrvaapv tfgsmhlgdv varyldahpg
      121 vdvevllddr yadllsigad lairigrlpd sglvarriap crmtvcaspa ylarhgtpht
      181 pddlrrahrl afseavsagd wtlvdadnra haidgacrls annmqmllaa alagagvayg
      241 ptfvfgghla rgelvallpd yhataltiqa vypsarhvsl kmrrfvdylv eafgesppwd
      301 gpwpaqpapp sa
//
LOCUS       WP_175953801             153 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175953801
VERSION     WP_175953801.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..153
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16695
     Region          1..132
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mddldwkvlt llqangrisy telarqvhls vpavtervkr leaagvvegy tarinpaaag
       61 ypvgaligit vpqpakakfl rlletipevv echhvtgads ymmrlaaism thleqlieri
      121 nlygetrtsi vmstplparg larppsqrdv vrd
//
LOCUS       WP_175953850             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0405].
ACCESSION   WP_175953850
VERSION     WP_175953850.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21744
     Region          5..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mpaastllaf glvslgmvlt pgpnmiylvs rsicqgrrag lvslggvalg fvfymvcaal
       61 gitalvmavp yaydvlrfag alylaylawq alkpggrsaf qvrqlphdsr grlfamgfvt
      121 nlanpkiavm ylsllpqfis pghgsvlaqs lalgcvqiav svsvngliac maggiagfla
      181 grpvwasaqr wlmgtvlagl avrialasrs
//
LOCUS       WP_175953854             281 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175953854
VERSION     WP_175953854.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..281
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28499
     Region          20..260
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mhfnltegvl vsslqglsaf dlagiavall lggmakgitg igvpliampi lsqflpirqa
       61 vlllsmpiil gnipqalegg qllatarria apiagtvign ivgvaillsl npghaqaasg
      121 allivaaalm laapklslpd awqkpvgfal gfgaalmesi asvpgpllat ylissgatgr
      181 vftkqiaiil vvsivtlitt fsgaahasga dlaisaaasl paiagmwlvr plrdkmsprl
      241 frmvvllfvl vaasqmiwks gvlrhggshv tqmgnahagk n
//
LOCUS       WP_175953880             563 aa            linear   BCT 11-JAN-2025
DEFINITION  ribonuclease J [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175953880
VERSION     WP_175953880.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Li de la Sierra-Gallay,I., Zig,L., Jamalli,A. and Putzer,H.
  TITLE     Structural insights into the dual activity of RNase J
  JOURNAL   Nat Struct Mol Biol 15 (2), 206-212 (2008)
   PUBMED   18204464
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..563
                     /product="ribonuclease J"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0004534 - 5'-3' RNA exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=61124
     Region          14..562
                     /region_name="RnjA"
                     /note="mRNA degradation ribonuclease J1/J2 [Translation,
                     ribosomal structure and biogenesis]; COG0595"
                     /db_xref="CDD:440360"
ORIGIN      
        1 mkplyenlae papleegalr viplgglgev grnmnvleya gkllvvdcgv lfpeenqpgv
       61 dlilpdfswi edrledivgm ilthghedhi gavpyllklr sdipiygsdl tlafvepkir
      121 ehrlpspdlv vvaegdridv gpfncefvav thsipdalav fvrtdagkvl itgdfkmdql
      181 pldgrltdlr afarfgeegv dlfmvdstna evpgfvtpec eigpvldrvf aeatgqivva
      241 sfashvhrvq qvmnaahrng rrvalvgrsm ernmriaeek gyltvppdvi vdsatigdlp
      301 pnqrvymatg sqgepmaals rmaagshkfv tlepddmvvf asslipgnen svyrlinglm
      361 rlgarvvhqs ntkvhvsgha sagellycyn iiqptnvmpi hgeirhlian gqlavktgvp
      421 venvvlaedg vvvdlkdgkt riagavpcey vyvdgrsige iseeelaarr tlgaegfvsv
      481 yavverdsgm vlaaptirai gmaeddavfe eilpevdaal reaaapggvd pyvlqqvmrr
      541 vigrwvarrl rrrpmivpvv veq
//
LOCUS       WP_175953892             183 aa            linear   BCT 11-JAN-2025
DEFINITION  CinA family protein [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175953892
VERSION     WP_175953892.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Galeazzi,L., Bocci,P., Amici,A., Brunetti,L., Ruggieri,S.,
            Romine,M., Reed,S., Osterman,A.L., Rodionov,D.A., Sorci,L. and
            Raffaelli,N.
  TITLE     Identification of nicotinamide mononucleotide deamidase of the
            bacterial pyridine nucleotide cycle reveals a novel broadly
            conserved amidohydrolase family
  JOURNAL   J Biol Chem 286 (46), 40365-40375 (2011)
   PUBMED   21953451
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Martin,B., Garcia,P., Castanie,M.P. and Claverys,J.P.
  TITLE     The recA gene of Streptococcus pneumoniae is part of a
            competence-induced operon and controls lysogenic induction
  JOURNAL   Mol Microbiol 15 (2), 367-379 (1995)
   PUBMED   7538190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..183
                     /product="CinA family protein"
                     /calculated_mol_wt=18604
     Region          9..161
                     /region_name="PncC"
                     /note="Nicotinamide mononucleotide (NMN) deamidase PncC
                     [Coenzyme transport and metabolism]; COG1546"
                     /db_xref="CDD:441155"
ORIGIN      
        1 mtlddrtpdq sraadaldal rqaglslata esltgggvca rlveipgasd vvrggvctyt
       61 salkhgilgv daellaergp vdgevaaqma qgarklfnad yaisttgvag pgpadghpag
      121 tvymalamps gtiihrfsft gsrnevreqa isqaitllde alraqgasas psftddsahp
      181 aer
//
LOCUS       WP_175953911             232 aa            linear   BCT 11-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175953911
VERSION     WP_175953911.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..232
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24592
     Region          23..229
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 msayvidaae rpsvkvdqss arfpvrrvfc vgrnyadhar emgadpdrep pffftkpada
       61 ivpasgtvay ppltndlhhe ielvvaigkd grsidpadal shvwgygvgv dltrrdlqae
      121 akklsrpwdw akgfdasgpv talraasatg hpttgriwla vngdtrqqgd ladmiwavpd
      181 viayvsrsve lkagdliftg tpagvgalqp gdrvtggvdg vatfefvvga kp
//
LOCUS       WP_175953904             206 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Schaalia sp.
            Marseille-Q2122].
ACCESSION   WP_175953904
VERSION     WP_175953904.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..206
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22457
     Region          10..201
                     /region_name="RsmC"
                     /note="16S rRNA G1207 methylase RsmC [Translation,
                     ribosomal structure and biogenesis]; COG2813"
                     /db_xref="CDD:442062"
ORIGIN      
        1 meqqyfsdqa paneddlrll tftarghdlq mwvsdkvfsg srldlgtrql laeapqppas
       61 grfldlgcgw gpiavtlace speaeiwavd vnsramdltv rnaavnggtn iqvlpapdal
      121 ekaraegarf dliwsnppvr igkeamhaml tdwlsllaee graylvvqrn lgadsliawl
      181 neqgfpaaki askkgyriie vearra
//
LOCUS       WP_175953920             285 aa            linear   BCT 11-JAN-2025
DEFINITION  spermidine synthase [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175953920
VERSION     WP_175953920.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..285
                     /product="spermidine synthase"
                     /EC_number="2.5.1.16"
                     /GO_function="GO:0004766 - spermidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=31125
     Region          30..224
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mashrsgrgm eqrevssgsa sliwdgsrat vflgsvessc vdvehpehle feymqhidvl
       61 aqvffgadrp lkalhvggaa calpwawarr rpgsrqtave vdaqlvdlvr ewfdlprspe
      121 lkirvedgrr vldttregsw dvivrdafdh givpahlatv eaaqaaaral rpggfyalna
      181 ghgggsdart evealarafe vvvaiadpkv grngrrgnvv lcafsplrde egqilgtspe
      241 avcdevdrll rrlplparim radevrrwqa gakslrdtqv gwspq
//
LOCUS       WP_175953957             530 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Schaalia sp.
            Marseille-Q2122].
ACCESSION   WP_175953957
VERSION     WP_175953957.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 530)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   5  (residues 1 to 530)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433522
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..530
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56808
     Region          66..529
                     /region_name="DdpA"
                     /note="ABC-type transport system, periplasmic component
                     [Amino acid transport and metabolism]; COG0747"
                     /db_xref="CDD:440510"
ORIGIN      
        1 mrstrskftg lialtaaaal glsacgggtp aaekpasgea eapaaaagpv geitagvaye
       61 ttnyhpsntt salamgsnwh vveglyemnm atgevyaala ageptkvsdt eyevtlrega
      121 kfsdgkdvtv edvvksfert maegnlyagf lgfvdavkak ddttvtvtlk qpftlvkerl
      181 avakivpaaa sdddltkmpv gsgpykyeki teselsavpn ehyngprpat verlkwsvlk
      241 ddtarttaaq dgsidvmesv padnialleg agwtvdkvpg fnlpfmlfnt nkapfnnakv
      301 rqaflyavdv dkliannmsg eataatsflp kthpnykeae vqyphdveka kallaeagva
      361 dlsitllttd htwianlapq ikndleaagv kvnlqsmass alykdnldie eptfdvavap
      421 gdpsvfgsdp allmnwwygp gkwtdyrtfw akgdnakfte lqniineavt legadqqkkw
      481 deaqdfisre vplyplfhrn iitayngekv ngftpiattg lslldatvkq
//
LOCUS       WP_175953996             271 aa            linear   BCT 11-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Schaalia sp.
            Marseille-Q2122].
ACCESSION   WP_175953996
VERSION     WP_175953996.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..271
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=29881
     Region          65..161
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 msrnetqaqq kaqefriqng lgsqpiydli rlielstgcd vavldvpedd hgltmsdper
       61 dttfigvart mnpmsqrstl ahelghilfe dhtvelgkrd rqeiradafa rhlliphqav
      121 kaflgegdhc slhslssvvq hflvspqmaa iamrdakiid qetvnswkai ttphlatqfg
      181 wsevyatlqe tsnrirppqk liaraisaya dglisaqvia tlrglpedlv lqeleeagit
      241 palpsfadye lrdlpqvdid lsgledasdp e
//
LOCUS       WP_175954019             413 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175954019
VERSION     WP_175954019.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..413
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45077
     Region          69..387
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mtlneswfap lvgilillaa agaitavvhf llfrvvarla rlsatrvdda lfefgafkwl
       61 nrivpfvvik lglgavpgip draaqvadka lfallvflvt mtisatlsal ehthrthhrd
      121 qprlslkgam qlvklvmfit aalvvigdat gkqiglllsg igamsavlml ifkdtllglv
      181 agvqlssndm lrigdwitmp sagadgtvid itlntvkvan fdhtiitvpt wklitesyqn
      241 wrgmteaggr rikralfvda tsvrflsnae ierlerltll kdyledkvda ieqwngtlga
      301 agdcaanrrq ltnlgtfray vanylkghpr irrdmtcmar qlpltaegip lelycftdtt
      361 twvdyeaiqa dlfdhliavl pefglrvyqh psgfdmrqma gaaqaglpap hag
//
LOCUS       WP_175954028             676 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175954028
VERSION     WP_175954028.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..676
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=70221
     Region          30..589
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mkfalphlpp laavrtalrd arpallpgal gfalrntaas llalyiafrm nlddpkwaas
       61 tvwivaqgsr gmglsksqyr ilgtaigaav alvltgafaq tpelflpala awiglcagva
      121 tflrnfraya avlagytaai iamdavaapl hafdiatarf lyvvvgilcg aafetvfapg
      181 spladvrtrl aryldravav gagalrrepn gaavhrlfad aleldtaaey aaagappvrn
      241 aighlraavv gvlsaqaagq alhehaarsg gtpdplvada aqvldgvaas geagaeltal
      301 rahvdaavra eaaepagsdp srlltldrla allagfdaaf agkaqldqpn ppasrvryaf
      361 hhdpvlawhn girafiavlv asalwivtaw psgagfvait gvvcalfstr pnsvgatvgf
      421 lkgaacaava galcnfvllp avsgfemlay ilgvfmigtg iamrnprtag igsgfsiffw
      481 nftspdntar igdaaflnsa latllgiafg alvfalvfpg dpgtsrrrlh ravrddlari
      541 arnprawras awlsrtadrl grelgfagrl pptlierdlr dllaawtign sllalaelaa
      601 repvarrava lvqarvgcad farlaragna aarallrrvt evdsddgral lrgavllsti
      661 aetaaahegf lrgrqe
//
LOCUS       WP_175954085             197 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175954085
VERSION     WP_175954085.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 197)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..197
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21255
     Region          4..>185
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mnsidiiglv ksypdftlgp idlhvprgai vglvgengag ksttirlilg lltpdagqvn
       61 vlgepatpsn saprerigvv fddislpsvf tvanaakfgq rlyrnwdera fgeycqrfnl
      121 satkkvsels rgmrmklgla ialshnaell ifdeatsgld pvvrdevldi mlefiqdpth
      181 silfsgssqm rvwvgvs
//
LOCUS       WP_175954098             262 aa            linear   BCT 11-JAN-2025
DEFINITION  thioesterase II family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175954098
VERSION     WP_175954098.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..262
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=28404
     Region          21..256
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mntasgqglr rwlvssgshl tassrlicfp yggggasiyr ewqselgdav dvcavqlpgr
       61 egrfgetact didellepml aeirplfdrp vflfgysmga alayklaayc rkkriqfdlr
      121 gliccarkap grqpgpdala hlsdeafllh ivslgggeva vhfrnkdlrn ialrllradf
      181 llsasilepd dgvldaplia iggasdptvs ldelgawrrl tsgkftqlvl pgghffmned
      241 idaflnvlrg ivgterepls rf
//
LOCUS       WP_175954101             111 aa            linear   BCT 11-JAN-2025
DEFINITION  putative quinol monooxygenase [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175954101
VERSION     WP_175954101.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..111
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12520
     Region          6..86
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mntpyialsg ilsckderel glvqaflpah ieftraeegc isfevtqdsv npliwhvnel
       61 fdsqasfdah qrrtlasewg aqtahikrey ivseiaaqen areygrkeqi q
//
LOCUS       WP_175954166             285 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175954166
VERSION     WP_175954166.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..285
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31385
     Region          9..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          105..270
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 madapdnllg aylrdrrekl dpaalglpat rrrtpglrre evaqrahvst awytwleqgr
       61 ggapsadvld rlaralllnd aerehlflig vghppevryh apanvtprlq hvldsldasp
      121 aivrtatwdv vawnaaaaat lidyatlppp arnilrlifi ddgvrdaqpn wervarfavg
      181 afradiargg atravqafid emratsaefd tmwrdhairt hdegtkeirh pqagrialey
      241 safsvtgrpd lslviftpat padreriral vaareqarel rapaa
//
LOCUS       WP_175954106              71 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl carrier protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175954106
VERSION     WP_175954106.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 71)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 71)
  AUTHORS   Moretto,L., Heylen,R., Holroyd,N., Vance,S. and Broadhurst,R.W.
  TITLE     Modular type I polyketide synthase acyl carrier protein domains
            share a common N-terminally extended fold
  JOURNAL   Sci Rep 9 (1), 2325 (2019)
   PUBMED   30787330
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 71)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   4  (residues 1 to 71)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10455525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..71
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=8138
     Region          3..62
                     /region_name="PP-binding"
                     /note="Phosphopantetheine attachment site; pfam00550"
                     /db_xref="CDD:425746"
ORIGIN      
        1 mmdairkiyv eelrlphfkd sddffdvggh slimasiqrr lndelkldva mdtlfryptl
       61 dalkshifat p
//
LOCUS       WP_175954102             204 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0405].
ACCESSION   WP_175954102
VERSION     WP_175954102.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..204
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21830
     Region          3..196
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 meiflyafsv myspgpvnal glnagltgqi rrtigffvgv giamfmllli fgytgealis
       61 tkwlpyiali gavytfylaf kmmkskvdts tgardraslg pnltflngfi iqalnpkgml
      121 vvlpittvmf psanirgvmi livsaliaig gagapgvysa lgvvvgrkik nddyfnlfnr
      181 lmgvllvaag afmfydfleg vkli
//
LOCUS       WP_175954180             344 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175954180
VERSION     WP_175954180.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..344
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=37964
     Region          34..93
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          124..324
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(139..140,142..143,146,150,152..158,250..255,
                     261..262,264..265)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 mthaatgrpa aparaesaph dndpselrvq dldlnllktf ravyeerhvg raalrlgvtq
       61 psvshalgrl rlmfrdalfv rtgtgveptp raqrlalsvd kalailqdvl degsrftpds
      121 tqrvfrlhms dfaasaflpt llaafdrrap gavietlhvd ecqlnvales gridfalghf
      181 adasshfqrt allhercvll mprrtarrva lpddyvldge apdtlrfvav tshpqsmqll
      241 erhglmprvr aalpdfmvvp allqdgdyal ilpetiaitf aarqpcalye iagagewavn
      301 aywhrrfdad pghrwlrall lelfnigela pfdawlapqp paca
//
LOCUS       WP_175954186             329 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia sp. BCC0405].
ACCESSION   WP_175954186
VERSION     WP_175954186.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..329
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34961
     Region          15..222
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(52..53,55,69..71,77,79..80,121,222)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(52,54..55)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(77,80,83,90)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(113,117..120,122)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(118..119,142..144,196..197)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          246..329
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 mqanrhqvri dalidaaqdi rcfrvsrvdg qpfdayepga hidvtapsgi trqyslcgnp
       61 dergsylfav kkeaqsrggs rslhddvqvg aelsigaprn lfrladdase hlliaagigi
      121 tpllsmayal hkrgaryrlh yfarsrehaa fvaelsaepf asrvtfhygi epaalaaelg
      181 rcvesvdaha hvytcgpgpf mdavvaaaat rlpdesihle rfaaepaaad agntdagasp
      241 adgfevrlqr sgqsvrvtpd tsivdalari giavdtscge gvcgtcmvpv idgepdhrdh
      301 clskaerasn tvicccvsra rsavlvldl
//
LOCUS       WP_175954035             292 aa            linear   BCT 11-JAN-2025
DEFINITION  siderophore-interacting protein [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175954035
VERSION     WP_175954035.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Valentino,H., Korasick,D.A., Bohac,T.J., Shapiro,J.A.,
            Wencewicz,T.A., Tanner,J.J. and Sobrado,P.
  TITLE     Structural and Biochemical Characterization of the Flavin-Dependent
            Siderophore-Interacting Protein from Acinetobacter baumannii
  JOURNAL   ACS Omega 6 (28), 18537-18547 (2021)
   PUBMED   34308084
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Trindade,I.B., Silva,J.M., Fonseca,B.M., Catarino,T., Fujita,M.,
            Matias,P.M., Moe,E. and Louro,R.O.
  TITLE     Structure and reactivity of a siderophore-interacting protein from
            the marine bacterium Shewanella reveals unanticipated functional
            versatility
  JOURNAL   J Biol Chem 294 (1), 157-167 (2019)
   PUBMED   30420426
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10153083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..292
                     /product="siderophore-interacting protein"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=32150
     Region          42..255
                     /region_name="siderophore_interacting"
                     /note="Siderophore interacting proteins share the domain
                     structure of the ferredoxin reductase like family.
                     Siderophores are produced in various bacteria (and some
                     plants) to extract iron from hosts. Binding constants are
                     high, so iron can be pilfered from...; cd06193"
                     /db_xref="CDD:99790"
     Site            order(98..101,115,117,119,123..126,162,253..255)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99790"
     Site            order(98,100..101)
                     /site_type="other"
                     /note="FAD binding motif [chemical binding]"
                     /db_xref="CDD:99790"
     Site            order(123,126,129,135)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99790"
     Site            order(162..163,183..185,225..226)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99790"
ORIGIN      
        1 mtvtnpmglt eeelvgllsl vndhehdede pahshdripw titaiedraq rmvrlrgrip
       61 dsedftayeq pnaifrievp vqpeelvgla napttasrvy tvahshpetr eisvdfalhg
      121 daspvmrwlt hvkigdvidi wsvaghripa pgkdtilvad staipalgsv lekcelsgri
      181 rlivqgqade lnelpdhsln lvsenlgeaf vklagkgvds vwaageasqm kiirthcrkv
      241 lglskeqtqv fgywrqgtsl taidierlrl lrdtilsggd lqalqeqmee sl
//
LOCUS       WP_175954188             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175954188
VERSION     WP_175954188.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34150
     Region          9..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          99..299
                     /region_name="PBP2_DntR_NahR_LinR_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators that are involved in
                     the catabolism of dinitrotoluene, naphthalene and
                     gamma-hexachlorohexane; contains the type 2 periplasmic
                     binding fold; cd08459"
                     /db_xref="CDD:176148"
     Site            order(105,107..108,112,170,208,275)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176148"
     Site            order(106,109..110,113..114,117..118,120..121,124..125,
                     127..131,133,197,225..229,232..233,236..237,240,254)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 mtsvdhldln llrvfqaive ernltkager lalsqpavsy slgrlrtlfd dplfvrtrsg
       61 mqptpvalel agivgkaldm vrvalryaer fdpatstrtf rlslsdagem aylpaicqal
      121 reraprvtls vqplpveeie ealrasrldf aignlpelmp rtrhqvlfee tyvcmtgrrr
      181 gvpsgtalsl dqfvraahvn vksvehshha lddalraqgv grnialevph fvalpsvlsv
      241 tdlyatlpkr laqilnrgna frlyelpvtl ppapvtmhwh ehfhedegna wmrnllaelv
      301 erfdda
//
LOCUS       WP_175954187             680 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175954187
VERSION     WP_175954187.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 680)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 680)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 680)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 680)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..680
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..680
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73550
     Region          23..499
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mrdsydrvkr vligrpirse alghqllpkk lalpvfasda lssvayapde vlltlalagg
       61 lagyhslwvg vavvavlavv vlsyrqtvha ypsgggdyev vttnlghnwg lvvasallvd
      121 yiltvavsis agsryitaal ptfaghevti avgliviltl lnlrgmreag aafaiptyiy
      181 mlaigvliva gfyqlftgsl aladsahyev vadpthvdgi vglggaflmm rafssgcaal
      241 tgveaisngv psfappkskn aattlallgg iaavmmmsil ilskatglvl vedpqaqllv
      301 dgvpvgeevv lapaigqlaa tifgdgsilf lvitvvtgai lvlaantafn gfptlasvls
      361 rdsflprqlh krgdrlafsn giivlacsav aliiafdaev trliqlyvvg vfisftlsql
      421 gmirhwnrql rtrqtgterg mvlrsravni igfmmtgsvl mvvlvtkfgq gawitlvmmv
      481 svfivqrlir shydqvradl rvedwnmqra lptrvhaivl vsnfarptmr avstarasap
      541 sslelvsvva deteeelvrr eweesglptp ltllyspyrd ithvvethvr alrrrrpnel
      601 vivylpaflv rrwwqnilhn qtavrlrral lhipgvvitt vpwklgeddq vegrqlvndp
      661 fpsnerseat trvvekedpr
//
LOCUS       WP_175954189             473 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent RNA methyltransferase [Schaalia sp.
            Marseille-Q2122].
ACCESSION   WP_175954189
VERSION     WP_175954189.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..473
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=50414
     Region          52..470
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 mtpsrrpsrs sqgqsasgrg gqrssvkgts kggakkgars aqrssrprpp ketlellvge
       61 pahggacvar ddngrvvfvr halpgervia qvtatqksla wadaievlsa sedrvpsvwp
      121 qaghngvggg elahvapeaq rrwkadvlrg qirriggeal adavsdiggv rvqaapgdta
      181 agdpllhrrs rielvanqds nagmhrfrdr vvlplkdmpl aveeivdvgl fgpdspwrhl
      241 wspkdrirvv asntgdnrvl vrtpqglfda erqmleddtc hwrievneqt fdyrvrmdgf
      301 wqthregaqv laqavsdaag lcggekvael ysgaglftqv lasqvgekgr vvsvegaeda
      361 vadatancaa ygtvdtfvga vdegavtdlv gelgsapdvl vcdpprtgag revcariads
      421 eaarvvlvsc dpaagardlr vltesgyele slrawdlfph thhvefvaal nrr
//
LOCUS       WP_175954235             338 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175954235
VERSION     WP_175954235.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 338)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..338
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36222
     Region          9..321
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mttsprrral iaaglgvlaa palvrakprt vriskgygvl ylpllvmekq rlferhaarh
       61 gvrdvavdwv lldggnsvnd ammagtldfa gagapgfiel warargipnv evigisglsa
      121 tslslnanrp gltslrdftp sdriavpgir tslsavvlqm vasrqlgpkh faqldsitvn
      181 lphpqamqal irrengvtah ftsppfstle lrqpgihrvv nsvdvlgpmt ldvvfapkrl
      241 vdtapalava flgaldeanr liaqdpraaa alyaassgvg vshddvmrml aapdtrfsvl
      301 pnqlmdyvef lylagtikak prawhemfap mlddyrsg
//
LOCUS       WP_175954297             937 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175954297
VERSION     WP_175954297.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 937)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..937
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=100894
     Region          33..750
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 maqergvqga faqwitgrqs yflevpgapr ardlsimsfv ldeqfgepyr ieltltspds
       61 lartdylnrp atftiepagi gggadgvrtf agcitafgqv rktrdfvsyr ivvepfvarl
      121 rlteasriyq qqsvpeives ilrrhefrsh qfsfklrray prlafrmqyr msdwdyvrll
      181 meqaglfcff ragqhgdelh fgddidaymy rpdvvipyre asgletghea vlsleslset
      241 ipqsvkvady npekaydrfn aeaniardds ttwgrryvfg thhldgdear yeaqlrheaa
      301 vawqvvysgr ssvvdfapgl vaklderpad aphgivivsv rhaggrdasy intfkaipcg
      361 rpfrlkcder rwptiagtls arvttpdasp yahltndgry tvrfdfdfde wpvggesvpl
      421 rlakpfaggn qtgfhfplla dtevaiafag gnpnrpyiah ahhdsqavdl vtsrdgfntr
      481 nvirtrannk lrfedrtgre giklstdygg ktqvnlghlv dnrketrgeg fevrtdergv
      541 vragkglflt adaqsnargk afdmtvarqq ldaarsrmrs ladavekara tvaacdaqqa
      601 llesrikdle aavllasaph gvaitsgehl qlaagghlft ttggnadaai ggnytvaagn
      661 avsmyanaqg mklyagagkv dvqaqtdale ltalkgvtia stsdavtlna qkaltlmcgg
      721 ayirlaggrv eigsaseiqv kgplsiepaa trrqalplmp eqeqtgmqlw haypngepvr
      781 napyrvtfpd gswregllda ngrgtvanap rgggsveyre edhdlqdaar kwgdpngmpa
      841 fpaasgdagq avpslvgaam aaaipgagtv lqalqsavsv qsaalgvaas gapgdaaala
      901 rsaldsvaqp vanatanrat aaipdvapgl vkttvsr
//
LOCUS       WP_175954310             435 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175954310
VERSION     WP_175954310.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46675
     Region          60..392
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mltqerhadd ltrfhrifll ilvsigssii ytpaylqyvf deplgkalia sgaasqenva
       61 ttlgtllaay swtalvcylp sgivadrvrv rtlawvgfgs talltywyaf fpsytmlial
      121 fvgmgittil iwwgirfklv rliseeeays rniglsygfy glaglilgfv naaivsnltd
      181 qgdiipmrtl llvlgsviml lailsflfip kfegeigsse ggfnfkqlgq vlsnpvvwla
      241 altlffvyff ytgvnqttgy mnnvmniapg ivlvvgtvrt ygvslisapf fgavaeklgs
      301 pskvigagsv vvmiglvifa flpaeaslay vavamailla fiangvfgic ssqltegkvp
      361 vsvfgtatgl lsvigflpdt fsyiwfgsir dahqdnpava ynqiflilag aaliaaicaf
      421 alvvvarkrn arida
//
LOCUS       WP_175954317             349 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175954317
VERSION     WP_175954317.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 349)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..349
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37431
     Region          29..225
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          257..340
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtynpfllid rpnldmsepl lppipdahdl vselllgmrl sgvqyrriqv arpfglnfgh
       61 vtgraqfhfv grgpvllrda sgdtmrleag daillprggm halvsdpdap creingfeaa
      121 kicdtvasva pagvsparca ttepgagdal ifsacmeldl ggmqplvgtm pefmhvgtll
      181 arypeirpml damereacsa ragfagilar ladvvaafiv rgwvecgcgd atgwvqalre
      241 pklgraival hrdpgrnwsv aelateagvs rsvfaerfla atgmtpvryl telrmrlaaq
      301 witrdheaie avayrlgygs laafsrafkr vvgkppgavr adgevraea
//
LOCUS       WP_175954324             656 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia sp. BCC0405].
ACCESSION   WP_175954324
VERSION     WP_175954324.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..656
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=70941
     Region          38..483
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mttfqkvwql lvgkpldpld prtrhaiavt pllawvglga dglssscygp eeaflalahh
       61 tplalflala tsatvfiial gynqvielfp tggggyrvat sllgskpglv sgaallvdyv
      121 ltvatslasg vdaffsllpv saqafkltte ivlillmtgl nfrgmresim vllpifvgfv
      181 ilhfalivyg vavhgsnlam ivpdavheah gmsqslgvfv vlallmrafs lgggtytgle
      241 avsnnvnmla dprvpngkvt mwymstslaf taggiillym lwharpvegq tlnavvfgsv
      301 idhlglgsaf arhallaavl afeagllmvg aqtgfldgpa vlsnmasdsw vprhfrdlsg
      361 rlvrqngiiv vglssllill wthgsvdvlv vlysinvflt fslsllglct ywwrhrseqg
      421 wfkhfflsal glsvtatvlv itliekftag gwltvlvtsa vialcfminr hyaytraqla
      481 kedalfsgnp pevdeatapg kpdpsqptav llvgkhrgas mhallwvnrl fpghfrnvif
      541 lavgevdaka ydghehlerl rhsitealdy yvahcrrngi aadyriafgt nplvefmnla
      601 sstldeypna vcfasklifr rvnfltawlh nqtpvelqar lhvegkqmvl lpmnvg
//
LOCUS       WP_175954405             220 aa            linear   BCT 11-JAN-2025
DEFINITION  flavodoxin family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175954405
VERSION     WP_175954405.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..220
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=23106
     Region          14..199
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 msifqeksvt nasvaivfhs ryghtarqam avkegvgraa gatgflvace daparwdela
       61 ladaiifgap tymagvsaef kafqeatssa vmfrgflwkd kiaagftnsg ahagdklstl
      121 vqlalfaaqh gmhwvnlglp pannsttgsa edlnrlgfwl gagaqsntdq gpeaappead
      181 latarhlgwr vadaalqfar griassgrdc qdlqddkinl
//
LOCUS       WP_175954465             374 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175954465
VERSION     WP_175954465.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..374
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40060
     Region          1..372
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 matvsfkkat riypgadkpa vdgldleiad geflvlvgps gcgkstslrm lagledvnag
       61 qifigdrdvt dvqpknrdia mvfqnyalyp hmtvrenmgf alkiagtpke eikkrvdeaa
      121 rildlepyld rkpkalsggq rqrvamgrai vrkpqvflmd eplsnldakl rvqtrtqias
      181 lqrelgvttv yvthdqteal tmgdriavlk dgllqqvgtp qemydtpand fvagfigspa
      241 mnlgkfdveg nvaklgparv plsaatvsal vpedggqiti gfrpeglevv pegentipie
      301 vdfveelgsd afiyghlagg hgealgsgee gkggqlivrv pprtapargg iihtrilpgq
      361 qhnfsastgm rlpe
//
LOCUS       WP_175954506             116 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: BON domain-containing protein [unclassified
            Burkholderia].
ACCESSION   WP_175954506
VERSION     WP_175954506.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..116
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=11793
     Region          44..>108
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mnktrhlstl lavsaafllg aapltnavaq dastdngmka esnqpvtdtw ittkvksrla
       61 tvdglksvdi svttvdgvvt ltgvlptkia vkkaiavsra vkgvkhvdas glkaka
//
LOCUS       WP_175954637              98 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175954637
VERSION     WP_175954637.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 98)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002085
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..98
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10232
     Region          8..98
                     /region_name="ManC"
                     /note="Mannose-6-phosphate isomerase, cupin superfamily
                     [Carbohydrate transport and metabolism]; COG0662"
                     /db_xref="CDD:440426"
ORIGIN      
        1 malidfrsva aaqavawkst ivgevgpari kvlrmdaqay eaevhdyneg llvldgrmml
       61 evggetvvve agqmylalag tlhavlpgsh gtlaiidv
//
LOCUS       WP_175954744             208 aa            linear   BCT 11-JAN-2025
DEFINITION  trimeric intracellular cation channel family protein [Burkholderia
            sp. BCC0405].
ACCESSION   WP_175954744
VERSION     WP_175954744.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..208
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=21015
     Region          6..204
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mkrieqvvla adlagtvvfa neganaaiga gldlfgvmvl slvvalgggv irdlligarp
       61 psavsdwryp alafasglfa fvfhervaaf spsllttlda aglalfavag avkalefrvh
      121 pfiatlmgav tgcgggvvrd vllarvpvvl vtdiyasaal lgavcvvscr rlgcppivaa
      181 vlggvacfav rmaavrfgwq lpkiatga
//
LOCUS       WP_175954683             291 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175954683
VERSION     WP_175954683.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..291
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32347
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..284
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,220,237,264)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     214..218,225..226,229)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mellndmalf vevvkakgfr saaetlgmpn stlsrrigal ekaiglrllh rttrrielte
       61 agrlyferct rivdearlah eqlgdllaep tgvlrasfpv dfavtylapl ivefsnrypk
      121 ltfdfeltsr rvdlvsepfd vairmgesdd sqliarrlat lgnylyaspg ylaregepht
      181 pddlarhacl slakagtwtl hdgtrtvavp vssrfainsv gmlrrlatld agiivlseei
      241 vaddlaagrl rhvmpawege pipvyamtet rllpaktqhf ieflrerfar a
//
LOCUS       WP_175954748             332 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175954748
VERSION     WP_175954748.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..332
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36478
     Region          21..328
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mtsavaaapa acvspvssla hfgfltlpnf smiafssave vlrmanyvgr adhyqwsiys
       61 ldgrpvhasn giavrptqal dytnlpdvmi vcggihirdv vdegardtla alaerglplg
      121 gictgayalm ssglldgyrc tvhwenlsal haefpqvgfa delfvvdrdr ltctggtapl
      181 dlmlnlvgtr fgqqlaaqvs eqfilerirs stdtqpipvd arvgfsrael ievvrlmean
      241 ieeplsleel arlvrlsqrh lqrmfkvyln vspthyyltl rlkrardllr ttdasiarvt
      301 tvcgfhspch fskayraqfg hapsyerrlp gr
//
LOCUS       WP_175954763             216 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NADPH-dependent FMN reductase [Burkholderia].
ACCESSION   WP_175954763
VERSION     WP_175954763.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..216
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22812
     Region          12..176
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mtafdqhrrp fvvgiggttr aassterals falrgaqaag artrlfdgpf lhtlphyape
       61 hktltdaqre lidtvrqada iiiatpgyhg gvsglvknal dtleelradd rpyldgravg
      121 livtaygwqa agtvltslrs ivhalrgwpt pfgatvntle trfdsadscs dpkvvaqlet
      181 vgtqaaefal afashraash aasvdalapv lkianq
//
LOCUS       WP_175954769             220 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175954769
VERSION     WP_175954769.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..220
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22799
     Region          117..218
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(120..121,154..155,158,162..163,166,208,212)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mnklalalal satalaacst asgptfsase lqprdgvrtf qvdchgllsg pqtcmkaark
       61 icgeepvrav dsaralrdks dpatlvfqcg aapaeaasaa apaaavveqv nlsgdalfat
      121 dhatltptar esldrllser adrtysqvsv tgftdavgsd dynlalskrr aesvaaylka
      181 hglktdsltv tgrgkadpva snatpegras nrrveirlqr
//
LOCUS       WP_175954793             248 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175954793
VERSION     WP_175954793.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..248
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27193
     Region          27..184
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtaatadtmt atvkadradt prapagrksq qrvqdilrag revfaekgye hataaeiaqr
       61 vgvseatvfs yfrgkrelca rviadwyden iaafehgmpq dasvqqqfaf ivrthlrlml
      121 vngtglcalv lsegrakqha lsdeltalqr rytaplmdvl argqaagqvr tdlplsllrs
      181 mvfgpiehvl wdailghrkl dtettatqlv dmlwaavqpp apeqaalvrf rndvaeavrr
      241 legdstrg
//
LOCUS       WP_175954789             665 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Burkholderia sp. BCC0405].
ACCESSION   WP_175954789
VERSION     WP_175954789.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 665)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..665
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70336
     Region          1..460
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          597..661
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(619,628..630,637)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            629
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mfdkilianr geiacrvaat ckrlgiasva vysdadanak hvaacdeavh iggsaaadsy
       61 lrieriieaa ratgaqaihp gygflsened fahaceaagi vfigppvdai aamgskaaak
      121 almhaaavpl vpgyhgddqd aanlhreade igypvllkas aggggkgmrv versddfpaa
      181 lascqreaas sfgndrvlie kyltrprhve vqvfgdthgn tvylfdrdcs vqrrhqkvle
      241 eapapglhdd vrramgeaav aaaravgyvg agtvefimtg dafyfmemnt rlqvehpvte
      301 mvtgldlvew qlrvasgepl plkqdelhvq ghalearlya enpargflps tgtlkhlrlp
      361 agvefaigas vrvdsgvreg daitpfydpm iaklivhgad raealslmlr alracevvgl
      421 htnaaflqri vacepfaaad ldtgliernh dalfapqepp ratlalacaa llarergaaa
      481 qgsspwdalp nwrlnggyrr tlewraaere advtvtyedd galarlaagg aaaqpfawtr
      541 gatpldfdvt lggvrssgrv yadgdtfhvf tqgaaetlew rnllahagda eqgggrltap
      601 mpgkviavlv epgqkveagt plivmeamkm ehtigapsag vvaevlygvg dqvadgaqll
      661 mmaeg
//
LOCUS       WP_175954803             418 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175954803
VERSION     WP_175954803.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..418
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=45853
     Region          8..418
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 mskffllgln ahgelqqfdl lasnredaqr eamrrarqaa vqvveigsts garsgmmrsr
       61 lplaglvrrq rfdlplfgye llallragla ltealealde rgrqsrsgaa eeqghyvlpe
      121 lvrlmrqgks fsaalaahpd cfsalfiami saseqtggmt dalerylqyh aqvsavrqrl
      181 iaaslypall mftgttvaff lvwflaprfa hvyegmlsad lpmlsrwlld agmlvgehtl
      241 aslgclfall igaaaaftrp aaqqrclall grigwigeml klmqlarfyr slgmllqggv
      301 pllpsldmtr dllpltlqdg ltrsmasiaq gkklseslrh dgltttialr llragerngq
      361 iagmleqaam fhereitqwv erfsrlvepi lmliiglgig aivvllylpv fdlagklq
//
LOCUS       WP_175954879             252 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DeoR/GlpR family DNA-binding transcription regulator
            [unclassified Burkholderia].
ACCESSION   WP_175954879
VERSION     WP_175954879.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..252
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27060
     Region          1..252
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlaeqrhqfi lselgrsgal svaelvrsld vsretvrrdl nalaargllv mthggalaad
       61 rrepslsere aanaeakrti grraaefvpd dasvlidsgs tphavalala drhrlsvytn
      121 dwrtafvlar rngnrvtllg gelsddedat fgldtiqqla qyhvdfafvg aggitpdgec
      181 tdysrlaaev rsrmiaaagm aiivadhskf grvtpvring taaarylvte rapdkavrra
      241 ltargiellv cd
//
LOCUS       WP_175954833             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0405].
ACCESSION   WP_175954833
VERSION     WP_175954833.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21616
     Region          1..192
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mheatllvfa avafvsiatp gptvllaltn gsrhgvrraa cgfagamlsd falivavafg
       61 lgalltasaf wfpvvkwlga aylayvgirl lmskgsldva aahggaasgr nasifakrfl
      121 tavtnpkgyl ffsavlpqfl dpsaplapqy valavtfall ggivmfgyal lgaravrllk
      181 ragapwlert cgamllalag slalprrhas
//
LOCUS       WP_175954917             528 aa            linear   BCT 11-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Schaalia sp.
            Marseille-Q2122].
ACCESSION   WP_175954917
VERSION     WP_175954917.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10505910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..528
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56464
     Region          42..291
                     /region_name="Exo_endo_phos"
                     /note="Endonuclease/Exonuclease/phosphatase family;
                     pfam03372"
                     /db_xref="CDD:460902"
ORIGIN      
        1 mtfrtvaagg gvaalclsll tgapalasds ssapmtapit vatfnaslnr sregellehl
       61 angdnvqaqn aaetiqrina diilinefdy dtehkaadlf rknylevghn gaqpitypym
      121 wtgpvntgvp sgfdldndgq ikpgndawgf gmfpgqygfv vyskypikae qvrtfqnflw
      181 kdmpgaalpv nadgsswysv eelakfplss kthadipvdv ngtivhvlaa hptppafdgp
      241 emrnqkrnhd eirmwadyis gagtylyddk ggtgtlaqda nfvilgdyna dpsdgnsyqh
      301 aimqllgnpr vldtlptseg gpqeqalqge anathkgdpk ydtadfsdgr tgnlrvdyvl
      361 pnrgvfveea rvfwptrede lfrltgldkn pqtgerqpfp tsdhravwvr mrfpasadqt
      421 vppttsptpp tppapttppa ppvapgqptp pvqptppatv vppkaddaas sktktpsapq
      481 gktadapskk tseklaatga sgltwvllgg gvlvlvgvll vflkrrgq
//
LOCUS       WP_175954948             128 aa            linear   BCT 11-JAN-2025
DEFINITION  GtrA family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175954948
VERSION     WP_175954948.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..128
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=13524
     Region          11..128
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mirtlytaer arlirfgvsg agstaphali aaamfalfda tpvsangvaf acstafsyla
       61 ntlwsfaspv mrgnfmrfla vamaglvvtm llahgtgtlg larawsvvav vlcvppvtfv
      121 lhrlwtyr
//
LOCUS       WP_175954957             224 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Schaalia sp.
            Marseille-Q2122].
ACCESSION   WP_175954957
VERSION     WP_175954957.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..224
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24658
     Region          9..180
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(12,14,91)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(39,90..91)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            89..91
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mstitdtclv vpmynearvv gevvsdlrtv fpnvvcvdda sedgsvtqal kagavvlphp
       61 vnlgqgaalq tgfewvlrqp eyryvitfda dgqhclndav amreraeahd lafifgsrfl
      121 hhpantgivk qwmlktaaqv trwrtgldvt dahnglrlir rdalaairlt qarmahasei
      181 veqlaatalp weehsvtiry tdysrakgqp llnsvnilvd lamr
//
LOCUS       WP_175954966             447 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: hemolysin family protein [unclassified Burkholderia].
ACCESSION   WP_175954966
VERSION     WP_175954966.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..447
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=48949
     Region          1..447
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mlqifaliga lflvalngff vaaefglvkl ratrvktlar khglrgrilg ivhgrldayl
       61 sacqlgitla slglgwvgep afaqllgpll dligvqserv vhlislvfaf slisflhivv
      121 gelapksmai rqsekvglwv alplyafywa mypaiwvlnn sanavlrlag lsadhggdah
      181 ystdelklil rsrrstagnp aqpargtysn dewntlahsl dfssmtvsdl mrpahemigl
      241 rrdlplpdnm eivarhrfsr yplfedasre qvsglihlkd lllarhagaa ledlsdyvrp
      301 vqyvkpdtpa ldlfrrfrkg aphfalvgnk gekpigfltl dnllgalvgq ihdefrqgda
      361 dwsrlddgtl mgkgslpvvs leqalgidid egraesvggl viqalgdlpt egqrvsfdrf
      421 dvvvkkmngp rivlvrvypk iakeade
//
LOCUS       WP_175954986             232 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: phosphatase PAP2 family protein [unclassified
            Burkholderia].
ACCESSION   WP_175954986
VERSION     WP_175954986.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17575897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..232
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=24529
     Region          1..149
                     /region_name="PgpB"
                     /note="Membrane-associated phospholipid phosphatase [Lipid
                     transport and metabolism]; COG0671"
                     /db_xref="CDD:440435"
     Region          <78..148
                     /region_name="PAP2_like"
                     /note="PAP2_like proteins, a super-family of histidine
                     phosphatases and vanadium haloperoxidases, includes type 2
                     phosphatidic acid phosphatase or lipid phosphate
                     phosphatase (LPP), Glucose-6-phosphatase,
                     Phosphatidylglycerophosphatase B and bacterial acid...;
                     cd01610"
                     /db_xref="CDD:238813"
ORIGIN      
        1 mfdlpshlwi mitafggagl tlplaitiav wlalgyswqr aaawlgvlaa aigvvaltki
       61 aflgwgigir kwdftgfsgh amlstsvypv aiflalirtr tpmriagial glaagiavgv
      121 srvaldahsp sesitgcivg aiaalafiag swravphrws vpavvaslal vtvalhgitv
      181 pshrwvtkva lqlsgherpf vrarwkanpn yrpasqpssl qrtqsslqtl rt
//
LOCUS       WP_175954989             152 aa            linear   BCT 11-JAN-2025
DEFINITION  GtrA family protein [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175954989
VERSION     WP_175954989.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..152
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=16800
     Region          10..141
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mmkgmreaif lstfirfacv gvvntavgal vmfllynfts agywfssamn yivgsilsyi
       61 lnkyftfsqk gqswaeifrf iaaiamsylv aygfalhiig wvladwseis rgnvsmalga
      121 ilytllnyfa qkyyvftgpr rsasdgaaea ge
//
LOCUS       WP_175955020             444 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [unclassified
            Burkholderia].
ACCESSION   WP_175955020
VERSION     WP_175955020.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..444
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=47753
     Region          14..426
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mhriiivggg agglelatrl gdrygargnr paralvtlvd rnpthiwkpl lhevaagsmd
       61 pftqeleyaa qarwhgfefq qggltgldra akritlspvn dsdgeellpa releydtlvi
      121 aigstthffg vqgaaenaia ldtvgeaerf rkrliaacmr aehqapapat pgeaaepriq
      181 vaivgggatg velsaelrnt aqvlsayglh kldprhdvgi vliesgpril palpervssa
      241 taellekigv rlmlaervte vapgavhtas gktvradltv waagikapsv lanldglqvn
      301 klgqldvrrt lqtftddnvf algdcaacaw pgnernvppr aqaahqqasf llkaigcrld
      361 grplpeftyr dlgslvslgh fsavgnlmgg liggnmlieg lfarfmymsl yrmhiaalhg
      421 yprmmldtva hwlrrttlpr vklh
//
LOCUS       WP_175955070             511 aa            linear   BCT 11-JAN-2025
DEFINITION  catalase [Burkholderia sp. BCC0405].
ACCESSION   WP_175955070
VERSION     WP_175955070.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..511
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56875
     Region          22..504
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 mpsssnrvlr havaalcval sasphaaelt rdtgapvgdn ensqtagpag pvllqdsali
       61 eklqrfdrer ipervvharg tgafgefvps adisdltqak vftpgtrtpv fvrfstvmgy
      121 rgspeqardp rgfavkfytq qgnwdmvgin wpvffirdgi kfpdfvhank psavtgvqdp
      181 nlafdffant peatnmltml ytnagmpdsy rhmdgfavha fkfvnahgdv hyvkfhwksq
      241 qgvhglrpqd idasigsdwn mmtndlygal kqgdfpkwdl yvqvlapqdl srfdfdaldd
      301 tkvwtgvper kigtmtlnrv pdnyfqstee safapsrlvp giepsedrml qdrlfayadt
      361 qmyrlganym dlpinrpvvp vvnnnqdgkm nagdrkgevn yepstlhela papqyksvrm
      421 tlggttqqea ihkqlrfrqa geyyrslsqq drddlitals gdlgkvtnah nqyamlsyfy
      481 kadadygtrl aqavhadvrq vqslasklse n
//
LOCUS       WP_175955012             330 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175955012
VERSION     WP_175955012.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..330
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36424
     Region          6..329
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpliriwave halasgvaap tdiltaanhl aattsqgrtr tpfrwrvesi ggrpvraasg
       61 qvipvdgaid gsspadaiwl tspfvadler lldrpaalap lfdalrrqha rgtliatyct
      121 gafllaeagl ldgrvatthw sktssfrary pdvalrasdi lteqdgilcg gaitsyqnla
      181 lrvvdklana rlaasvarlm lidmnrvsqd sfidldrtsh rehddaaiar aqrwmekhlr
      241 epfslarlsd hvamsertlh rrfrdavgap plrylqtlri evakrllaet klaidavcer
      301 vgyadisgfr qlfkretgis pgeyrrrfrq
//
LOCUS       WP_175955081             417 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175955081
VERSION     WP_175955081.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..417
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43900
     Region          13..390
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(23..24,27..28,31,65,120..121,123..125,128,148,
                     151..152,155,230,233..234,237..239,242,266,270,321..322,
                     326,330,346,349..350,353..354,357)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 msrtfaslah fnfrlwfagn ilassamwmq rvaqdwlvlt vltdqsgtqv givtalqflp
       61 mmlispwtgv vadrvdrrrl vqitqsisgi lglglgilil sgviqlwhvh lfallggiss
      121 afdsparqaf vaemvpptsv anavalsgms ftsarligpv gagliidrvg vgwvfvinaa
      181 ifivpvvlia lmrvhelnpr dhaprargqi reglryianr pdlivifvlm svvaslglnf
      241 qltsammatt vfrkgagefg llatfaaigg vtgalvaarv gaarlgflip aatafgimli
      301 vvslapsyva yaalviplgt asmltmtsan svlqtrtpdg irgrvmslyt ivflgttpig
      361 apfigwvget fgarwalavg gaatlgiall mggvlavqqr rerarnagtd vargarv
//
LOCUS       WP_175955090             313 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175955090
VERSION     WP_175955090.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..313
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=31633
     Region          7..147
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          158..296
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mlvstptivv gvdgstasla avdwaihran ligarvhimc myamasysaa aldggyagid
       61 aealekgaqs vvdaaverat slvgadtrvt isssiepgdp asilvemsae vdlivvgsas
      121 gggfmsrllg tvssslpana dcpvvvvpeh ksgkaftpid kivvgvdsss ntsaalkaai
      181 aetelwgaal tavsavpips vggvmgwvpn tgnhdaviae iknglntavd salgdhdlpv
      241 arhvldgspa slliefstav dlvvvgtrgg ggfadiflgs tsqtvishst cpvmvvprgr
      301 dersgesyaw err
//
LOCUS       WP_175955096             439 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Schaalia sp.
            Marseille-Q2122].
ACCESSION   WP_175955096
VERSION     WP_175955096.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..439
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=47642
     Region          50..404
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mtypedytvi qpvwpafdad eavpvmarfg fpqatvlsqs irmmscavtv ltphgpfflk
       61 ryhrsvmsvp elrarhqavn llrdvedeha ltvtgfqltp agdsvveege wlyelndfap
      121 gedryrgrys wnapdslgea eslgralavl hlraeatasl apadpgpgff qarcdlamgq
      181 vsvedyladr pmltewaasy aiqegdaprt vdsapgartn keghggghsg akssaadstg
      241 tlncadeagh aaahrlslaa eveaalawrt pditrayasl prlwihgdgh csnmmyegda
      301 vcavfdfgls avstavadla ialerntllw ldildgnada yrmdmseail rgyqtlrpls
      361 aveaallphi mravhvdpal dwipyhlisg rpsnaqwale tflrghtawf tteagrryld
      421 elaatiqatr pvqatlpps
//
LOCUS       WP_175955106             483 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175955106
VERSION     WP_175955106.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..483
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49114
     Region          4..434
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(14..15,18..19,22,54,115..116,118..120,123,143,
                     146..147,150,279,282..283,286..288,291,313,317,369..370,
                     374,378,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mkyfsvlfag slitsigsgm safalaawif tqqgsaasvg llqmcafapm vllapiagtc
       61 adrydrralm iagdggsilg lllvlwalng gglggegeps vplvllgiti asslaaftep
      121 alratvsdll kpeeyvrasg mlqlaasskf lispvlaalv mtassvqvvl lidaatavvt
      181 vactlyvrrg ltratpvgrl gaarqaskae qaskaeqest agqestagqe stagqaskae
      241 qesaagqess drpsflrdll nswrtitast qvttvvaima altlalgviq tllkpmllph
      301 yspnqvglve slaacgliag galvavltnp rpdwllrvgi gavslgallv glrpsmwwva
      361 gscalvfaal aacnagaeag vrglipneqq grawgsigli tqmgfliaya lagpladhvf
      421 tpalmeggal vpalgwlfdv gpgrgiglli scvgiavgvl tltvpridaa hahnpgnqgg
      481 hsc
//
LOCUS       WP_175955115             472 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0405].
ACCESSION   WP_175955115
VERSION     WP_175955115.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..472
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48064
     Region          23..450
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,277,280..281,284..286,289,317,321,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msefaspaga hepavnwram savllavala tldtaianta lpaiaadlha spaasvwiin
       61 ayqlamvatl lpfaslgdiv ghkrvyiagl avftlaslgc slastlpmlt aarivqgfga
      121 saimsvnval irglfpahrl grgvgfnalv vgvsfavgpt iaslilsvaa wpwlfavnvp
      181 lgvfalavai pslpqtargk hpfdpvaalf nvitfaslif algefaqrgp lsvvfaaaav
      241 altfgwllir rqaghpapml pvdlfrrpvf tlsaltavca faaqglafvs lpfyfetvlh
      301 rnavetgflm tpwsaivala apiagrlsdr yppgllgaig lallsagmvs laalpaapgv
      361 idigwrmmlc gagfgffqsp nlkalmssap persggasgi iatarligqa tgaalvalsf
      421 giagrhgptl almlgagfag aasvasglrl fapshragvp aaservsera te
//
LOCUS       WP_175955208             311 aa            linear   BCT 11-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175955208
VERSION     WP_175955208.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..311
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=32506
     Region          20..289
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mkrqitteat rlaqqqanwa ltafkrfssd rcsamaagia ffsafslapm lvmviavagw
       61 fygddaargq vfeqahqlig ddaaasiqti vqnahrager gglatlisfa alaigasatf
      121 aslsaalsvi wpatenrwss mlglvrvrli sfglvlgvaf llivslvldt aitfigtwll
      181 gnspyvvvtn lvqffvgiav laaafaalmk flpdarvawr daavggvvsa ilfsggkklf
      241 alylahagta safgaagsfa vllmwlyfsa ivlllgaefa aargnahrla gtaapaasaq
      301 tdrpadrlrd d
//
LOCUS       WP_175955244             418 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0405].
ACCESSION   WP_175955244
VERSION     WP_175955244.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 418)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 418)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..418
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45083
     Region          <195..412
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mtiapsspsn aalkrelkaa earkrtmall lvaplaifll lifvvpigtl ltravqnpei
       61 atalpktvaa lsswdrkapp adaayvalaa dmtkvadsea mgalarrlnt eipgyrslva
      121 ktaramplkg dndaaltpaq trekivelda rwgdvaywqs iakngsqvsp fyllaaldhk
      181 qdgfghivqa dpdqsiylai fgrtfvigva vtlfalllgy playwistls errsnlvmil
      241 vlipfwtsvl vrvaawivll qseglintal igsglishpl allfnrvgvy ismthillpf
      301 milplysvmk sipptyqraa vslgshpfaa fwrvyvpqty pgvgagallv filaigyyit
      361 pallggpndq mvsyyvayft nvtinwgmac algglllaat lvlyavygrf trtnvslg
//
LOCUS       WP_175955349             276 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175955349
VERSION     WP_175955349.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..276
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29897
     Region          2..>154
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mihvarrrna qapirlivch gaggysdalw picaqidpaa cdlflpdlpl ygysttvspq
       61 nvryedwiec lrafieetdd grpvilwgfs iggmlaheva crsplvnevi atclvdprsl
      121 rarlhigrwg mgllgtpflg vgrrsplski mipmklvanm grmsrkkals vlcakdprgg
      181 gaaiplgfla tflayahsrr rsegeaavri tlahpaqdaw tpaslsittl rrlegvghiv
      241 mlencghfpi eepgltqlve aveerlhava ggvkps
//
LOCUS       WP_175955257             866 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175955257
VERSION     WP_175955257.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 866)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 866)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 866)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 866)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 866)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 866)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 866)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..866
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..866
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=94503
     Region          99..733
                     /region_name="RloC"
                     /note="Wobble nucleotide-excising tRNase [Translation,
                     ribosomal structure and biogenesis]; COG4694"
                     /db_xref="CDD:443729"
ORIGIN      
        1 msdeaptdvi ssgeeaelgt aefldprall vdwanandew arllvsevia tgravsasti
       61 dkayqlfrqe kaldnrelpt vekidivarq desaprlslt rlsevrgvna lvsgavieph
      121 egltilygen gtgktgysri fkalansrta dtilgnikad asedqaakld fklgdeaqtl
      181 twtgergvsp ftrmsifdsp avtthvdsdl dyvytpasls lfshvtaaiq aveaqidasa
      241 galdtgsssl ldrfqhgsti yplietlgas tdladlkaka itgddvdtkl dglaqavgal
      301 rentigmqit vlkaeqrvla qasvaaealv afdataynna larraqltsd yetfrselfa
      361 aadlpaepdd twsqfiesge tyrqhlveld ahdsdrclyc rqpllapard llsrysayle
      421 dkisadlrtt daflaqlkrq aaavqsnelv aflnenrdtn dqpsyfawvd tiegarsala
      481 aaatsgapan lallellsqp ktdvdkallt vgsrlanlea qqqnrtqala dkqaeyleyk
      541 davelgkswa lieaqvknak eadqlktlkr plqqlvravt glaktasdql inrsfdalfl
      601 eecdalrapa lklqfvgrkg kaqrrkvmsg rhkpskvlse geqkvlalad flaearlagi
      661 tapvifddpv ssldhrrine vaqrvawlae enqvivfthd ilfattllgl fekskrcayf
      721 qitdedgkgk vtratgprwd tlsgikgkin stiqaaqqqd geardalvrv gygwlrswce
      781 vftetellqg vtqryqpnvg mtrlsnintt klgeiipkvt dvfeeacryi dahsqplvtl
      841 gvsptlagle qhwaelqelk kvndgk
//
LOCUS       WP_175955364             282 aa            linear   BCT 11-JAN-2025
DEFINITION  TlyA family RNA methyltransferase [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175955364
VERSION     WP_175955364.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..282
                     /product="TlyA family RNA methyltransferase"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30003
     Region          5..252
                     /region_name="YqxC"
                     /note="Predicted rRNA methylase YqxC, contains S4 and FtsJ
                     domains [Translation, ribosomal structure and biogenesis];
                     COG1189"
                     /db_xref="CDD:440802"
ORIGIN      
        1 mklrridsel vrrglarsrt haqelieagr valdgqvvtk parqmdpaqa iviseetgee
       61 yvsrgafkla galdalgera pivegrrcld agastggftd vllrrgaahv vaadvgygql
      121 awklqqderv evrdrtnvrt laagdvdpap glvvsdlsfi sltlvlpalv avaapdadfl
      181 lmvkpqfeig kerlghggvv rnpdhhvetv etvaraaqal gleirdveas plpgpsgnve
      241 yflsmhatgn gdlrseaddl hnrivdavrr gpagqgkkkg ik
//
LOCUS       WP_175955385             341 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia sp. BCC0405].
ACCESSION   WP_175955385
VERSION     WP_175955385.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..341
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37057
     Region          180..320
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mlaevrpdgf tlldtcrlaf adglfavrdg aqirvaqgdg igaqllraql gddgalrlva
       61 ynhraapadq rrallvalaa afsdsarhaa irldpaawpa valdalrasg vladgglcmr
      121 egwaqqadlw lvgphlpcat lpmftdgrrh prrppaprge vyarglpalg vrftlrgwqp
      181 aedaarlarw fdeprvrdgw pgtppgtqga aadadphvip lvgcfdgepf ayfeavwlke
      241 dalaphvaar dydrglrmlv geprwrgphc vagwlpcvvh ylflddprte avgcavpagh
      301 arvadhlarh gfarqrrlal adaqslwmrt lretffsgrh v
//
LOCUS       WP_175955381             749 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia sp. BCC0405].
ACCESSION   WP_175955381
VERSION     WP_175955381.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 749)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..749
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81079
     Region          62..749
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mkqveqrkme watgtrlrai aaaasvafgv aagqaqaqta pavsagaaas assaqngasa
       61 ngstgtlpti nvnaasegdg tvglvakrsr tgtktstsin eipqtinvvt aqqiemtgat
      121 dvnaalryvp gfssygsdnr sdwyaalrgf tptayvnglq vpntinlasw rvdpymidsi
      181 svlrgptsvl ygagdpggiv dvqtkladge rvreagvqig nyarkqfmid vgdkldpdgk
      241 yayrfvgvar dgnaltgpnn dqrvalapsf rwrpdadtsl tlsatylqdw gdissnflpa
      301 qgtvlpnpng qinkdiyegd gnfnyyrkkq wsvgyqfern ltpawtfrqn trlmhlsldn
      361 gsvfgngfvd gsttdvsrwa gvfqmnysrf didnnlegrf atgplqhtll lgfqynrqta
      421 tdsewlaaap plniynpvyq pvttavftpd atirtntytt mntfglyaqd qvkwnrwtlt
      481 lggredwvnm rmddraggts tkadvtaftg rvgltyqgdy glspyvsyat sfnpligvnl
      541 lggglpqptr gkqieaglrw qppgknlmln aaiyqinqtn vltpalpsqd ntgtksvqig
      601 evrsrgiels atgkltrnls viasyvyqdv knvkandvsl nnwpvdiprp rqmaslwtdw
      661 twhtgplagf glgggvryqs asagaadnsl tvssvtlfda gvhydtrnwr favngtnlfn
      721 rhyisgcqsa nvcvfgtdrt viatakynw
//
LOCUS       WP_175955394             536 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175955394
VERSION     WP_175955394.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..536
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58752
     Region          4..531
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 minvqnfslr igarelvkdv tfrvdkgmri glvgrngagk tttmrllage ddrgiaehdg
       61 misrtgtvgy lpqdtqagdp eqkareriis vrgidtiiar irkaeqemst legprqvkam
      121 eryvrldqef tnaggwaana easqiahalg ledrvldqpl atlsggqrrr velarvlfsg
      181 advllldept nhldhdsivw lrdwlktfpg gaiiishdvk llgdtvnqvf fldatravmd
      241 iyhlgwtayl qqraederrr rreranalkk aeqlraqgek mrakatkava aqqmlrraqe
      301 llesvgderq eekvarlrfp epapcgrvpl saedlsksyg slevfagadl sidrgakvvv
      361 lgyngagktt llrilagiet pdtgqvvpgh glklgyyaqe hetldgeatv yenmarsapg
      421 ldntqirnvl gqflfsgddv ekpasvlsgg ektrlalatl vvsaanvlll deptnnldpa
      481 sreeilsalr tyegavvlvt hdpgavealn pdrvlllpda dedlwdesyl dlvtlt
//
LOCUS       WP_175955498             127 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175955498
VERSION     WP_175955498.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..127
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13665
     Region          20..127
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mierlgilvp veddrfravv dfyrlalalp vhsegvsaag npwhrfvvdg atltihtgrg
       61 gefpypefrp tghgialaie varvseaiar lescrvgiln ewdygdgtia isvadpagnv
      121 ceiwgrp
//
LOCUS       WP_175955559             425 aa            linear   BCT 11-JAN-2025
DEFINITION  GspE/PulE family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175955559
VERSION     WP_175955559.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..425
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=45030
     Region          <19..424
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mhfpppgapl raqpppahsd vssaaaprtl daaqlddapa vrlltdtlha arvrdasdih
       61 vepfeagwri rlridgvlhe harpplhlrd alvtrikvla rmdiaerrlp qdgrlrivid
      121 ggtrgdyrvs slptlfgekl vlrrletlpp dltlarlgfd aqqaaameaa iraphglvlv
      181 tgptgsgktl slycalqmld rdahnvctve dpaeiqldgi sqvgvaekag ltfatalral
      241 lrqdpdiimv geirdaetad vaikaaqtgh lvlstlhtnd aptavarlld igvapynlaa
      301 alhlvtaqrl vrrlctacrv hsdapvpvlr etgcdpaala agwrpfvarg cpachgigyr
      361 grvglhqtmp vspglaeriv arasvgelaq cvaaegvrsl rdaalarvhd gttsiaeala
      421 atpas
//
LOCUS       WP_175955722             220 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: histidine phosphatase family protein [unclassified
            Burkholderia].
ACCESSION   WP_175955722
VERSION     WP_175955722.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..220
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24344
     Region          6..204
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mattqilfir hgetawnrik riqghidipl aetgleqaqr lavrlarear dgarldaiys
       61 sdlmraqqta qpfadalgls prlreglrer sygqfqghds aeietlfpda yaawqtrdpg
      121 fapeggesqr efyhrvlhal epivaehpgg riacvahggv ldsvyrfang ielsaprnyp
      181 llntsinvvd yvdgraqivq wadvshldaa sdddgyrkvl
//
LOCUS       WP_175955770             117 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175955770
VERSION     WP_175955770.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..117
                     /product="VOC family protein"
                     /calculated_mol_wt=12551
     Region          12..112
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 mpirnfvstl pvlnvpdlaa vrewyvallg easvvpdegv lewevapghw iqlaeeaehp
       61 cagsviveta dltqlhssll gegfdigdiv dyevvkfael adpagnvlqf vevvdnd
//
LOCUS       WP_175955827             352 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine recombinase XerC [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175955827
VERSION     WP_175955827.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Castillo,F., Benmohamed,A. and Szatmari,G.
  TITLE     Xer Site Specific Recombination: Double and Single Recombinase
            Systems
  JOURNAL   Front Microbiol 8, 453 (2017)
   PUBMED   28373867
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Grainge,I. and Jayaram,M.
  TITLE     The integrase family of recombinase: organization and function of
            the active site
  JOURNAL   Mol Microbiol 33 (3), 449-456 (1999)
   PUBMED   10577069
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11478354
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..352
                     /product="tyrosine recombinase XerC"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009037 - tyrosine-based site-specific
                     recombinase activity [Evidence IEA]"
                     /GO_process="GO:0006313 - DNA transposition [Evidence
                     IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=38023
     Region          28..352
                     /region_name="xerC"
                     /note="site-specific tyrosine recombinase XerC; Reviewed;
                     PRK00236"
                     /db_xref="CDD:234698"
     Site            order(204,298,301..302,333)
                     /site_type="active"
                     /db_xref="CDD:271179"
ORIGIN      
        1 msanatpatp rragrpqapp sthtqqvpla gdderllhqw lsflsdtkgl ssqtirayet
       61 dlrlcvgfir ersgsdlple dllttralrs wlsstlaega trstaarkts slrsfcawah
      121 hrgflptdps allvsarpdq rlpevvdveg aarllnyaas mvrqaqehar dcddpqevaa
      181 eenvlacalr dwamleliys aglrvselcd ldttsldtsa gtirvigkgn kervvpvgdv
      241 alraveawre ggrplflaah sgqalflgkq ggridpravr avvhnmsaqa gvkdlaphal
      301 rhtaathllq ggadlravqe ilghaslatt qrythvdaqr lsaiylqahp ra
//
LOCUS       WP_175955912             252 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175955912
VERSION     WP_175955912.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..252
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26931
     Region          9..241
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 maentpvsrr avvtgastgi geatvrllca hgwqvvalar radrlqalae etgcqwasid
       61 lrdedsvral aarlqdsgpv dalvnnagga lgtesiadad pdkwlamfdr nvmtalhatr
      121 aflpamrerg gdlvfltsta ahdtypgggg yvaakhaeri iantlrqelv gepvrvmela
      181 pgmvkteefa lnrlgsseaa akvyegvaep lvaedvaeai vwmlerprhv nidsmiirpr
      241 aqatntliar ql
//
LOCUS       WP_175955914             356 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Schaalia sp.
            Marseille-Q2122].
ACCESSION   WP_175955914
VERSION     WP_175955914.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..356
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=38664
     Region          <12..180
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(45,49,50..51,53..54,58,63,72,74,76,80,82,85..87,88,
                     92,95,104,106,108,112..113,116..118,120..121,125,128,137)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          74..104
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          106..137
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 makkkrvtlp kafnelieag dtealialyt qcdlnatydg rfglntalhh rdvpielifw
       61 laeqgadina rnyygqtplh aqaacggeav kalvdlggdl natdkdggtp lhaaaryfra
      121 dtvrllvekg anitarnarg qsplavalsa crnidipqaa eisaellqag eavtldmlen
      181 vkrigqefef hrerfskerl aevdaglerl yslfnvtpva qrrvhdgasp ivvaegpwre
      241 qyetlwnllv pssgpattmq geairiagrv hdeirrnggv nwdqdyrlml saleqhfasg
      301 tpladdklke artliatlsa sgssghgate slcelsvlwv aanpmpivle apaytr
//
LOCUS       WP_175955638             320 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Schaalia sp.
            Marseille-Q2122].
ACCESSION   WP_175955638
VERSION     WP_175955638.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..320
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34220
     Region          1..300
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 myylqghtme niahhlgisr ssisrllaha retglvrisv aaapgtrgtl agqiseifgv
       61 rtsvvpvrev dtevnrlhnv alvaaerlve lmepgailgv awgnttsevt rnlprvhfpg
      121 stvvqlngav natksglpya dsimsqaaqa fgsrtlqfpv paffdypdtr eamwrersir
      181 svldtidrad valfgvgsls gtlpshvyss gyldpqeiae aqadgvvgdv ctvliredgt
      241 tdlplnkras gptpetlqki prrllvvsgt gkalpllgal rakvatdlvl ddaaaralmd
      301 lvrqrahhak aqqarsriak
//
LOCUS       WP_175955948             558 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 39 protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175955948
VERSION     WP_175955948.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14304616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..558
                     /product="glycosyltransferase family 39 protein"
                     /calculated_mol_wt=62675
     Region          9..375
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
     Region          450..555
                     /region_name="Arnt_C"
                     /note="Aminoarabinose transferase C-terminal domain;
                     pfam18583"
                     /db_xref="CDD:465810"
ORIGIN      
        1 mndtpsrlpl nritlvllvv alaivwfapl glrhlipsde gryaemarem fvtgdwitpr
       61 yngykyfekp plqtwlnalt fawfgigewq arlytavasf agillvgytg arlfnplsgf
      121 laavvlassp ywnlmghfna ldmglafwms lslcslllaq rpglrpavar gwmwgcwaam
      181 afavlskglv glilpgavlv lytliardwa lwkrlylvsg lviffaivtp wfvlvqqrnp
      241 effnfffivq qfrryltpeq nrpgplyyfv pvllvgflpw lsvawqslrh alrmprqpng
      301 fspmlvlltw safiflffsa shsklisyvl pvapalalii gaylplmsad rfrrhllgyl
      361 vflvvaafgi iflayqgdar tpnalyrafq mwlyaglava avltlaaawl nrrtgvaaal
      421 aafgaawlvf gtiggtghde fgryssgall apavraelak lpadtpfysi emldhtfpfy
      481 mghttimvqr qdelafgism epnkwiptvd ewvkrweqet halaimppgq ydalvrqgvp
      541 mrviardnrr vivekpqs
//
LOCUS       WP_175955958             158 aa            linear   BCT 11-JAN-2025
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175955958
VERSION     WP_175955958.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..158
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=17325
     Region          1..143
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 mttvriqsdd fdlnaevaal rarnpkigal acfvgtvrdl negdsvaale lehypgmtek
       61 aleriaaeag rrwpgidvai vhrvgrllpl dqivmvatva shrgdafasc efvmdylkte
      121 apfwkkettp dgerwvdars tddaalarwg iesgntrr
//
LOCUS       WP_175955915             391 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Burkholderia sp. BCC0405].
ACCESSION   WP_175955915
VERSION     WP_175955915.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 391)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..391
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41768
     Region          4..386
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 mtalntlaia nyrslreliv plaalnvvtg pngsgkssvy ralrlladta qgrvipslar
       61 egglpstlwa gperfsraml dgdapvtgtv rkgpvslklg facddfgysi dlgmpipsrs
      121 qfsldpvvkr eciwggtllr pstllvdrqg aqirartasg ewrtipqpva sfdsmmtefa
      181 dpsgapemia vrerirswrf ydhfrtdaqa parqshigth tpvladdgad laaalqtire
      241 igdgaaldaa lddafpgasi eidnpggrgr fdvlmrqpgl lrplaaaels dgtlryllla
      301 aalltprppa lmvlnepets lhpdllpalg rliaqaaqrs qvlvvshaar liatlereag
      361 ceslvldkql gatglvdaat rdlpawkwps r
//
LOCUS       WP_175955960             186 aa            linear   BCT 11-JAN-2025
DEFINITION  group III truncated hemoglobin [Burkholderia sp. BCC0405].
ACCESSION   WP_175955960
VERSION     WP_175955960.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Keppner,A., Maric,D., Correia,M., Koay,T.W., Orlando,I.M.C.,
            Vinogradov,S.N. and Hoogewijs,D.
  TITLE     Lessons from the post-genomic era: Globin diversity beyond oxygen
            binding and transport
  JOURNAL   Redox Biol 37, 101687 (2020)
   PUBMED   32863222
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Bustamante,J.P., Radusky,L., Boechi,L., Estrin,D.A., Ten Have,A.
            and Marti,M.A.
  TITLE     Evolutionary and Functional Relationships in the Truncated
            Hemoglobin Family
  JOURNAL   PLoS Comput Biol 12 (1), e1004701 (2016)
   PUBMED   26788940
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Wajcman,H., Kiger,L. and Marden,M.C.
  TITLE     Structure and function evolution in the superfamily of globins
  JOURNAL   C R Biol 332 (2-3), 273-282 (2009)
   PUBMED   19281958
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Vinogradov,S.N., Hoogewijs,D., Bailly,X., Arredondo-Peter,R.,
            Guertin,M., Gough,J., Dewilde,S., Moens,L. and Vanfleteren,J.R.
  TITLE     Three globin lineages belonging to two structural classes in
            genomes from the three kingdoms of life
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11385-11389 (2005)
   PUBMED   16061809
REFERENCE   5  (residues 1 to 186)
  AUTHORS   Wittenberg,J.B., Bolognesi,M., Wittenberg,B.A. and Guertin,M.
  TITLE     Truncated hemoglobins: a new family of hemoglobins widely
            distributed in bacteria, unicellular eukaryotes, and plants
  JOURNAL   J Biol Chem 277 (2), 871-874 (2002)
   PUBMED   11696555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..186
                     /product="group III truncated hemoglobin"
                     /GO_function="GO:0005344 - oxygen carrier activity
                     [Evidence IEA]"
                     /GO_function="GO:0019825 - oxygen binding [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20550
     Region          22..130
                     /region_name="TrHb3_P"
                     /note="Truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 3 (P); cd08916"
                     /db_xref="CDD:381257"
     Site            order(33,46,49..50,57,60..61,64..65,75,77..79,82..83,86,
                     89,93..94,97,121,124..125,128)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381257"
ORIGIN      
        1 mtvlpaspdt aparlrdtep aeeniralvy afydrvradp llgpvfdakl agrwddhlak
       61 mvtfwsslvl gtkgyrgnvq qahqpldgie pahfsrwlsl flktvearya ppaairfmap
      121 alriaqslql srfgwdypip peqqalldai sprrrdagad phslpsrarg epfptkiigr
      181 ssdpda
//
LOCUS       WP_175955992             334 aa            linear   BCT 11-JAN-2025
DEFINITION  SPFH domain-containing protein [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175955992
VERSION     WP_175955992.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..334
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=36618
     Region          <63..307
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 mghisrypfi ahyqgaptdh ivhlingtpr hegvgrtfwf rpttsalaev paidhehsal
       61 fhavtqdrqd lavqavvtyr fsnpalvsqh fdfniypvak dhqpngprqv aklieqlaqs
      121 itthvianlp laealhsgis rvhtalveql sqqtrlsdag isiydvrvls lrptpeveka
      181 lqtplrerlq aeadralytr raqaveqeqr iseneaaakl elarrrkeii aqeaanerlq
      241 aeekaassli aargaaeate vsenaraaal rligqaeadn ererlaayna ispeilrsla
      301 lrelaanlpa igqlnltpdm lstalgqlva tske
//
LOCUS       WP_175956001             324 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175956001
VERSION     WP_175956001.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..324
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32999
     Region          7..319
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtltspilai vdhdeagalt apsaqvltaa ralssgpvva ltlqapdaea larygaarvl
       61 vadlggrspr lsavvaeaaq aamqavgaea vlcvshylgr evaarlavav ggapivdvtr
      121 tweengniha skpalagawe tsihvedvpa ilairpsaid eveapaeaav ealpvdftaa
      181 adaisvvsst pqertgrvpl teartvvvgg rglegdfgpa eeladlldaa vgatrvatde
      241 gwvsrslqvg qtgvsispnl yiglgvsgai hhtvgmqssr hivavcddpd apifeiadfg
      301 vvgdlfevip qaievlrreg ygqa
//
LOCUS       WP_175956055             380 aa            linear   BCT 11-JAN-2025
DEFINITION  MraY family glycosyltransferase [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175956055
VERSION     WP_175956055.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Anderson,M.S., Eveland,S.S. and Price,N.P.
  TITLE     Conserved cytoplasmic motifs that distinguish sub-groups of the
            polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase
            family
  JOURNAL   FEMS Microbiol Lett 191 (2), 169-175 (2000)
   PUBMED   11024259
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Lehrman,M.A.
  TITLE     A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P
            transferases
  JOURNAL   Glycobiology 4 (6), 768-771 (1994)
   PUBMED   7734839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10160596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..380
                     /product="MraY family glycosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=40541
     Region          38..306
                     /region_name="GT_WecA_like"
                     /note="This subfamily contains Escherichia coli WecA,
                     Bacillus subtilis TagO and related proteins. WecA is an
                     UDP-N-acetylglucosamine (GlcNAc):undecaprenyl-phosphate
                     (Und-P) GlcNAc-1-phosphate transferase that catalyzes the
                     formation of a phosphodiester bond...; cd06853"
                     /db_xref="CDD:133463"
     Site            96..97
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133463"
     Site            order(282,296..299)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133463"
ORIGIN      
        1 mkvylllmll amgitvlvtp ivrfaclhwr ivpklrsrdi qsipiprlgg iamttgfvia
       61 mliastipym apvfstsvpw avmggaaams llgviddvie ldwmtklsgq ilitglmals
      121 gvqlvsfpif gitigssrls liltllvvva iinavnfidg ldglaagtvg igamsffiys
      181 ysvsvisdaa tyattaslvv ialvgvcagf lwfnfhpssi mmgggaetlg lilasaaiiv
      241 tgqidpsvlg eqrvlvgllp vllplsvivv pmgdlvatsl irmkngkspf hadrshfhdr
      301 llarghthrg vvtilwlwta qvslsavsll nfpwhyvalv svptlvlvli ftvaefpwmr
      361 eaarkaathg kdeddrhsce
//
LOCUS       WP_175956104             220 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Schaalia sp.
            Marseille-Q2122].
ACCESSION   WP_175956104
VERSION     WP_175956104.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..220
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24221
     Region          1..204
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 msaptsksda vyqqvrsriv dgqytpgfrl tfsaladefg vstvpvreai rsleaeglve
       61 ytlnigarvs evnledyyea mvslallegm atalaaphlt eedlqiahsl nrdmealtrs
      121 syfdsdayrr lngrfhsvlc apcpnsrivs lvnseaervt iirrsslkfe saqsadsiaq
      181 hdrllemirr gadpaeiehf arqhklaslh skvsaparal
//
LOCUS       WP_175956132             208 aa            linear   BCT 11-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Schaalia sp.
            Marseille-Q2122].
ACCESSION   WP_175956132
VERSION     WP_175956132.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..208
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=21693
     Region          92..192
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mglfiselig alvqllllsv vpliwwlvta rtragffswi glraperfgg alvgwsvlil
       61 vatfvlgvgi qwllagtpva askfaglgvg alpailvfaf vgtalgeeif frgfllkrfn
      121 samsfqaant aqgalfgvlh gimffsllpf vstllvivft gvigwslgmv nerlaggsiv
      181 pswlihagan llaglsmafg lfalapga
//
LOCUS       WP_175956111             304 aa            linear   BCT 11-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175956111
VERSION     WP_175956111.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..304
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31504
     Region          76..282
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mtkrslaala asilmsvaai dgfvapqlah aqasgtagts aqtaapsaap apaaaaaepa
       61 pppapattea venpyglgal wkngdfvarf vlillvimsm gswyimitkf veqlranrra
      121 kladaqlwsa pslaegakll deaspfrfia etaieagehh dealleavdr ntwidvsver
      181 sitnvsnrmq dglaflatvg stapfvglfg tvwgiyhalt aigiagqasi dkvagpvgea
      241 limtaiglav avpavlgynf lvrrnksvme rvrnfgaqlh tvllagnrrp vrassspaaa
      301 slan
//
LOCUS       WP_175956144             283 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175956144
VERSION     WP_175956144.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..283
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29578
     Region          81..249
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mssltlhgps stpasssstp rtagilqrms alvaaesklf frnrtvllna lllsplmala
       61 lapllldtlg aesfavlvmq mlvgfgamfv iyynfttivv arreagifqr mntgqasvwe
      121 alvaavvpsa aalvvqvltg miavavlgkv mplvnpvall vaivgavvif aglgawtsaw
      181 sssveaaqys smplmlaalf fsglffpvqf mpetlqtics ysplyavnal vgismgvapv
      241 idggaalsvg esflammvpt vtviawsavg iylarytrfs rra
//
LOCUS       WP_175956145             297 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175956145
VERSION     WP_175956145.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31065
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mtpdqlitfa avaehlnisr aavalhlsqp avsgqlrllq defgeplyqr egrgirltpv
       61 geqlaqyaka qrdtfaqara frdavrglea gtlrigastt pasyllpyli aafqpraprv
      121 aiqtmsgnta dvvaalpsld iamiegppge alppgtavha wredeivaiv paghplaapd
      181 yasgvtldal aahplvlrea gsavrqlver afaqgaapmr vafeiagvea vkeavragmg
      241 vgfvsamslr hddaalvlrs lapaplarhf silvphggap srvaaqflem slahdva
//
LOCUS       WP_175956164             268 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175956164
VERSION     WP_175956164.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..268
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26959
     Region          1..264
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mlislvlggf vgavlgltga gggilavpal vvgmswpmqq atpvalvava gsaalgaleg
       61 frrglvryra allmavagvp lttlgvrlah vlpqrlllal faltmlvvag rlllqalrha
      121 pvdaetsplc vgrvnpdtgr lvwswpvgva lastgamtgl mtgllgvggg fvivpmlrkf
      181 tnvsmhgvva tslmvialvg tggvfatlvs gtrapldvtl wftvatalgm aagrgasrhl
      241 aarhvqagfa vvlvcvalgl lakatlra
//
LOCUS       WP_175956200             277 aa            linear   BCT 11-JAN-2025
DEFINITION  RDD family protein [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175956200
VERSION     WP_175956200.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..277
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=29978
     Region          15..162
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 msasvvplrh iqqesivtge avaleispas pllraaatmv dialtlfytv ialyvaqlyv
       61 evssesmlrv vaigtlvmll vilpmtveva trgrslgkwa fglqvvrddg gvitarhslm
      121 rmlagilevw lslgaiamvt tlvaprskrl gdmaagtmvi rlpepqlyap vlmppdlaew
      181 astaqvvslp tsvssqalhf lrtsrslvph vreagaqqia qqlmtfvepa ppanthperf
      241 iaavlvvrrd rdllrlvard ersqrsfera ttspfgl
//
LOCUS       WP_175956250             313 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_175956250
VERSION     WP_175956250.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33586
     Region          15..73
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          103..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(113,117,156,170,172,231,248,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(114..115,119..120,122..123,126,130,132..138,199,
                     225..229,236..237,240)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 masdpipapd kpidlldval fvraarlanv taagrefgvs aavasariaq lerqlgarll
       61 hrttrrislt qdgdvfmaha dtllsaadaa rasvghgrte pygrlkvsms ssfgrqhvap
      121 vipaflrryp svsldlrlsd eivdlvddgy dvairlgalk dstlvarkla anrrvlccsp
      181 aylaehgtpr hpadlaqhec vilgdqrdws fatpqgpltv rvggrlvasn geairealvd
      241 gfgiaikstw dvgpllasga lvtvlddypf aediaiwavy psrahvplkt lafiaflaeh
      301 fgdppywdra dgq
//
LOCUS       WP_175956315             115 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FmdB family zinc ribbon protein [unclassified
            Burkholderia].
ACCESSION   WP_175956315
VERSION     WP_175956315.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..115
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11033
     Region          1..73
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 mpiyayrcea cgfakdvlqk msdaplsqcp ecgkdafrkq vtaagfqlkg sgwyvtdfrg
       61 gsggtsapat asgdaapaaa teaapaaaap aassssestt tsaapapaaa paags
//
LOCUS       WP_175956344             786 aa            linear   BCT 11-JAN-2025
DEFINITION  LPS-assembly protein LptD [Burkholderia sp. BCC0405].
ACCESSION   WP_175956344
VERSION     WP_175956344.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..786
                     /product="LPS-assembly protein LptD"
                     /GO_process="GO:0015920 - lipopolysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86858
     Region          67..757
                     /region_name="LptD"
                     /note="LPS assembly outer membrane protein LptD (organic
                     solvent tolerance protein OstA) [Cell
                     wall/membrane/envelope biogenesis]; COG1452"
                     /db_xref="CDD:441061"
ORIGIN      
        1 mppkplfpnv fpgdgaprkr rlalallavp glvpavsyaq lsgaaaqpqp ldspwdlrla
       61 pqledhplkd gskpaafvia dhtsgtaeqd laakgsaelr rgdaivkada ihydqdtdma
      121 daygqvrvin ggmsfagpea hlkieasqgf mtapkyhfnm tggsgsaerv dmvddersvf
      181 vngtytacqc stnpawyikg srfdfdtgad egtarngvlf fqgvpifasp wmtfplsger
      241 rsgflpptfs mnssngfelt lpyyfniapn rdltltprii srrgvmaeat frylspsysg
      301 tftanylpdd rlahrnryai ywqhqqnfgg gfggyvyynk vsdntypedl gsanqfingt
      361 qtlyqqeagl tynngpwsvl aryqhwqtlp psiapysrep qlnvkytkyn vggfdfgaea
      421 dysrfritta datqgdriaf npyiaygvyg pgyfvvpkvq yhfasydlny lssttpnnpk
      481 rftesiptvt fdsglifdrs vrlfgqdfiq tleprlyyvy tpyrnqsnap lfdtaesdfg
      541 laeiyqpntf vgndriadan ritagltsrf idprtgdera rfviaqqyyf adqrvtlnsg
      601 qsavlarhsd livgaalklg sgfmsetafq ynqnnnqlvk ssvgfgyspg errvinvgyr
      661 ytrsnttldn qpinqflvsa qwpltrrlya igrfnydlag drvvdglvgl qydadcwalg
      721 vgvqraangi nssgqqnsst rvmmqltlkg lstvdnglvs afragvpgyt plppppppms
      781 rfsnye
//
LOCUS       WP_175956396             292 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175956396
VERSION     WP_175956396.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..292
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32129
     Region          24..286
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mpsstvvrkh dvhhpipylp lptgalipql gfgtykvteg vyeavssalr igyrhidtaq
       61 mygneaevgr aiadsgipre elfitsklnn dvhepgpare afaktlrdlr tdyvdlflih
      121 wplpglyggd llmpwrvlee fyaagqarai glsnfeqhhv eaileggtva phvnqfeahp
      181 ylpndelrtf cwrqgivtea wsplargkat qdarlaaige ahgvsaaqva lrwalqrgdi
      241 ifpksvtsar qeenfdlfgf clsdeqmaai aaldegeagr vgshpdvmnr lr
//
LOCUS       WP_175956468             440 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175956468
VERSION     WP_175956468.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..440
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45880
     Region          15..352
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mlanyaevlt lpgawrfsla gailrmpmsm vgismiltvk aaygnytlag lvvavsivgt
       61 svcapilarm vdrygqrtvm lpslvvcavs lavfsaasmw sapvwvvfva savagatwga
      121 pgalvrsrws tvveeprqlt aayaleaavd efvfvvgpiv attvatalhp atglilsiff
      181 iavgslgffs qmeteppvvq vdraqragtv ithpvvigla ltyvgagamf gatdvavvaf
      241 teehmqpala gvllgifafg slvaaliyga rtwrqplwkl fsvgivalal gtssfllatn
      301 vwvlglamli tgltiaptmt nvnmiiakvv psgqlteglt wmstamnigv slgsmlsgrs
      361 vdvtgaeggf wvvmafawvm vllmvvglps lrrhteraer prhlpevssg edavggagei
      421 tggglyeaqa vpgcvdlrhn
//
LOCUS       WP_175956502             364 aa            linear   BCT 11-JAN-2025
DEFINITION  Fic family protein [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175956502
VERSION     WP_175956502.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..364
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40815
     Region          23..349
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mwttpdvprq dlpplppsee vetpavlkav iaasrelsal kvacsrlpdp ailintipll
       61 eaqasseien ivttndelfr avhnasdqpi tpavkealry rqairiasdl laerplgvpt
      121 alevctqirg iqarirdhag tfignpqtke riytppegre vitrhlglwe dflhrdhgid
      181 plvvmalqhy qfeaihpfsd gngrtgrvln mltlmdkell rdpvlylsgy ivrhkqdyys
      241 llrgvterde wepwilfmvs acevtakwtl elietitamq tevegrirtl vprapaadla
      301 rllftqpyvr ieniteagya qrqaasrwls dlvragilge ekigrgkifi nnalldtlfe
      361 tpla
//
LOCUS       WP_175956491             304 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175956491
VERSION     WP_175956491.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..304
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35062
     Region          85..242
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mrfdvellll alapvfllci aweawhlart raqdpvyawr dtlcnaalal mhqgadkiaw
       61 lfvipvyayc yqhyrlftwh dgwlsfavlf vaqdflyyvf hrashrvrwl waahvvhhss
      121 ermnfstafr qslmypvagm wvfwlplafa gfppqqvvgi vlinlafqff vhtqaigklg
      181 wleyvlntps ihrahharnp ryidrnyagv lviwdrlfgs yveetpddpp qygiverlds
      241 nnplvatfhe wismagdalr vdgwrnklra ifgppewasa yhaqvaeaan pdprteplaa
      301 ardq
//
LOCUS       WP_175956548             158 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175956548
VERSION     WP_175956548.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..158
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17179
     Region          11..146
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtaklnpfaa apalmknwmt vsvaaaqsle ptlielvkir asqinacanc inmhtaeare
       61 qgeteqriyl lsawreapcy tereraalgw tdaltrlseg haaheaayaa lndhfsqeeq
      121 vkltlminvi ngwnrlavgf glwidpadak aaaakmva
//
LOCUS       WP_175956375             310 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175956375
VERSION     WP_175956375.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34552
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrlgdirlf veaaelgsls aagrklnltp aaasarlakl eakvatrlfe rstrqlrltd
       61 egrlylnccr qalqalddad amlqegrnvv ggkvrlssts dfgrnqlldw ldefttrhpd
      121 vtfsltasds ssnlwqdeid lairfaappd galiarrlat nrrvlcaaps fverhgmpad
      181 phdlarfpcn vitiasgpmn vwhftrgdev qihrvpiata fetndggltr ewtlrghgia
      241 lkslwdiadd vragrlrvll pdwrhqdapl haiyhskrym aprvrvlldf laqrfareea
      301 alddllnacr
//
LOCUS       WP_175956631             561 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia sp. BCC0405].
ACCESSION   WP_175956631
VERSION     WP_175956631.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..561
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=61164
     Region          10..539
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mttqrtlege fdyvivgagt agcvlanrlt edpdirvlll eaggkddyhw ihipvgylyc
       61 ignprtdwly ktqpeaalng ralsyprgrv lggcssingm iymrgqredy dgwaqetgda
      121 gwswdsvlpi fkrsedhhag asdahgaggy wrvekqrlrw eilesfaqaa qqtgipatdd
      181 fnrgdntgvg yfevnqkrgv rwntskaflr pamarpnltv itgaqaqrvi fdgrravgve
      241 yrgggtdyva rarsevllts gavnspqlle lsgigdgrrl qalgidvvqd lpgvgenlqd
      301 hlqlrmafrv egvrtlntls ahwwgklmig aeyallqrgp msmapsqlga faksdpddpa
      361 ltrpdleyhv qplslerfge plhsfnafta svchlrptsr gsvhiasadp gmapaiapny
      421 lstdhdrhva analrltrri asapalaryr peeilpgaqy rseaelieaa gavgttifhp
      481 vgtcrmgrad deravvdsrl rvrgiaglri vdasvmpfit sgntnsptlm iaerasdmir
      541 adrraareat pvrteaaatp v
//
LOCUS       WP_175956690             294 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175956690
VERSION     WP_175956690.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..294
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32563
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="PBP2_CrgA_like_7"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08476"
                     /db_xref="CDD:176165"
     Site            order(101,105,144,158,160,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176165"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176165"
ORIGIN      
        1 mdnltgivaf vrtsealsfv aagralgisa savgktiakl eqslgvrlfn rttrrvtlte
       61 egrhfyercq riledfrdae atvtasaqrp rgklrvslpv igyrfllpvl pefrqrypdv
      121 eldldfndrm vdvveggfda virsgplsds slmsrrlgpf afvlcatpay laqagtprtp
      181 rdlethecvr ycfpttgklq dwalaaddgt plklrtaltc nnmealrgtv laglgigymp
      241 dflahdaler galvtvlddy riapgqfsiv wpssrqlspk lrvfvdflce rlfr
//
LOCUS       WP_175956765             194 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175956765
VERSION     WP_175956765.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..194
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=19586
     Region          28..194
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mkiakstsal slfvvaagla aasaahasdg qinftgsvva stckinqgvn dltvtlpraa
       61 tnqltaegst agrtpfkltl tgcttdkeeg gttipapvnk vsvafepgpn vnlatgrlkl
      121 tgddaaknve igilndkyep ikvgaessaq nsqivdidtt agtatlqysa qyvatgeatg
      181 gsansfvtys liyp
//
LOCUS       WP_175956778              95 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175956778
VERSION     WP_175956778.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 95)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 95)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 95)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..95
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..95
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10247
     Region          26..>90
                     /region_name="AF2118"
                     /note="Predicted transcriptional regulator, contains an
                     XRE-type HTH domain (archaeal members contain CBS pair)
                     [Transcription]; COG3620"
                     /db_xref="CDD:442838"
ORIGIN      
        1 matykalrel alsdpkvrae ydrlnreefa lldamlaarr aaglsqaeva ermgtkapav
       61 trleralatg qhspsietlr kyaaacgkkl visfa
//
LOCUS       WP_175956780             152 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175956780
VERSION     WP_175956780.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..152
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16928
     Region          1..139
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mkldaidrri lnalqrdgrm qnvelahevg lspspclrrv rlleeagvie kyvavlnpak
       61 vgkgltiftr vwlkgqdaes vnrfaeavqq mpevvechlm agdcdfllrv vaadiddyrr
      121 fqmetltrip gvlsvktdip mqkvkltsal pt
//
LOCUS       WP_175956885             122 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Schaalia sp.
            Marseille-Q2122].
ACCESSION   WP_175956885
VERSION     WP_175956885.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..122
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=13471
     Region          1..111
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mdlndsrplw iqlveefrrr ivsgewgpgs klpsvrelal elgvnpntiq kalgeldreh
       61 ltqtertagr fvtsdadlvn qariglaqea tdtyvsamkg lgitaelaad littrwdked
      121 pr
//
LOCUS       WP_175956838             452 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia sp. BCC0405].
ACCESSION   WP_175956838
VERSION     WP_175956838.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..452
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=48381
     Region          17..434
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mdnttpnlat graprlpriv ivgggagglh latrlgdtvg rrgqaevvlv drypthfwkp
       61 llheaasghr dpashtieya aqakrhgfrf vqgalqrvdr aartatiaav qdadgteilp
      121 qrelgyddlv lavgsvtnff nvpgaarhal plenldqaed frrkflaact kanhlaeqqp
      181 arraapicin vigagatgve laaalrhaiq qlttyrfkal vsardvhirl ieggprilpa
      241 lderlsgkmh aqlralnvdv ltdtrvaevg anavttstge rlasditiwa agvagpaflq
      301 qigdialnrs nqvivtdtlq tpddphvyaf gdcaacptag angflppraq vahqqavylv
      361 nafarrvagk pvagftfrda gtvvslghag aayqadisvr srslivdgla aiglykflyr
      421 khlfsvvgvk ralfqslshw lqsrnqpsik lh
//
LOCUS       WP_175956929             443 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175956929
VERSION     WP_175956929.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..443
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48003
     Region          65..443
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          260..443
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mtattpptkd eatalaplrs taatrswrrs llaalyalgl vvpltilpaw aeddrdsvar
       61 aqeesanrve eikhdmegid stlaqvylel dslraqipva enelsqaqdr ydaanrthqa
      121 algqletata ektridteia eaeelhdqar laigelarem yrggapspvm lamsaegsqg
      181 iaeraaaaea larsqstais salniqerqr nqatrqqait erisdleska rsaaeeaets
      241 qrqaeakvke ltelkknada kqvqweakkq eaakqldkwq aeydamsakl akideenraq
      301 qriystptgg asgfysplri plimtspfgw rhhpvlgtsr fhngtdfaan cgtpiypsap
      361 gvvsavtfee aggnvvyvnh glmngsswms ayvhmegtnv ypgqsvglds vlgwvgttgy
      421 stgchlhlsf mqngadvdpm dfl
//
LOCUS       WP_175956903             316 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Schaalia sp.
            Marseille-Q2122].
ACCESSION   WP_175956903
VERSION     WP_175956903.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..316
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34983
     Region          9..197
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(12,14,106)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(51,105..106)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            104..106
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 msgvprlaiv ipcyneeavl pvtkplfedk llslieagka ardsalvfvd dgsrdatwtl
       61 ieefscgnph irglrqsrnr ghqstvlagl lesmhdydvt isvdcdgqdd lntmdemlaa
      121 yaegaevvyg vrndratdsf fkrftaesfy rilatmgvev vfnhadyrli ssrvlkefas
      181 fkevnlflrg liplvgfkst svyyarherm ageshypltk mlglavdgvt slsvkpirmi
      241 taagivvsll sfffilwiig tffwgttvpg wasttaasvf lgglqllslg iigeyvgkiy
      301 meskerpryi iserte
//
LOCUS       WP_175956934             434 aa            linear   BCT 11-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175956934
VERSION     WP_175956934.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..434
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=46046
     Region          3..408
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mkkkhnitky ivvamilgia vgyachsafp dpnmakevag yvsllsdvfl rlikmiiapl
       61 vfatltvgia qmgdgnavgr vgvkafgwff iasftslllg lltatilqpg shlslplpas
      121 daalglktga ftlkdfvvhl vpksiaeama nneilqivvf siffgtalsa lgesgkrltg
      181 viddlaqvml kvtgavmwfa pvavfaalas tittqglgil ltfakfmasf ylalallwgv
      241 ltlagvtflg kraftlirli repfllsfat asseaaypkl ldaldrfgvn rkissfvlpi
      301 gysfnldgsm myctfavlfi aqvygihlpl gtqitmllml mvtskgmagv praslvviaa
      361 tlnqfnmpea glllimgvdm fldmgrsatn avgnsiaaav vakwegqldd prddndpdng
      421 ramqvkvpet sasa
//
LOCUS       WP_175956961              88 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Schaalia sp.
            Marseille-Q2122].
ACCESSION   WP_175956961
VERSION     WP_175956961.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..88
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=9468
     Region          7..79
                     /region_name="AF2118"
                     /note="Predicted transcriptional regulator, contains an
                     XRE-type HTH domain (archaeal members contain CBS pair)
                     [Transcription]; COG3620"
                     /db_xref="CDD:442838"
ORIGIN      
        1 mqyqgkvtgp eslgrmlqqa rlvagltqre lakqigttqk yiwelesgkp simmdrlfaa
       61 mqatgmelta tiavptdega tqeegdhg
//
LOCUS       WP_175956966             204 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0405].
ACCESSION   WP_175956966
VERSION     WP_175956966.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..204
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22085
     Region          4..194
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mefltlsalp agmlfalvts itpgpnntml lasgvnfgfr rtmphlfgis igvailmlcv
       61 gfglgeafkr mpllytilea asvayllyla wrigtsgevk ahggkprpmt fieaaafqwi
      121 npkawmmvlt aattirlsad ygmnaawmav vfiligfpci slwaafglgl rrflsnpral
      181 rifnvtmavl lilslyplva hlla
//
LOCUS       WP_175956996             605 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175956996
VERSION     WP_175956996.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 605)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..605
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65836
     Region          32..558
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 mnrgpvgsts gpqrvsasaa qnlspsfper arwgtagslr awqaaalnly lekspkdfla
       61 vatpgagktt falriavelm gsgivdkvtv vcptehlksq wadaaarvgi hidpafsnsq
      121 gmagshydgv avtyaqvasn pavhsartra hrtliildei hhagdslswg dgiseafkda
      181 trrlnltgtp frsdtspipf vryvedeegi rrsqadytyg ygdalrdgvv rpvlfmsysg
      241 tmswrtsage qysarlgepl tkdmmkqawr taldpkgewi pavlqaadqr ltevrrqvpd
      301 agglviasdq tqarayarhl rmitgkaatv vlsddkdase ridtfrendd rwmvavrmvs
      361 egvdvprlsv gvyatntsts lffaqavgrf vrarrrgeta tvfipsvlpl ldlagameve
      421 rdhaldrptn aneegdlcnp edaliaqanr qekassdllg sfealgadae fdavlfdgaa
      481 wgsvaevgsv eeqeylgipg llepdqvttl lrarqeeqia sqkraraaak lrdensgisd
      541 hrvraakrke lqnlvsswsr rsgethavih sqlrqrcggp evaqasteqi aariallrew
      601 fvgrr
//
LOCUS       WP_175957004             880 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175957004
VERSION     WP_175957004.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 880)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 880)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 880)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 880)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..880
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..880
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=93705
     Region          52..859
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mekrqpsiqa etepklkpvc allltiiagw qaqahaadad sgvlqvaqte faqvefeggf
       61 lnngggaidv sryerrnvvr agmykpdvyv ggdwvgriel qfksapntad aqpcfdkaqf
      121 eqigvdlskl sqdvratlda dgaclrigqa ipeasvsydf neqrldlsip qismrrqarg
      181 yvspdqwseg vpvgmlgyna svyhsrtsgq gestqgyvgi dgginvgrwh frhngsfnwd
      241 drgrrkyesv atylqrdlta wssqmivgda ytsgdlfdst sfrgvrlytd drmlpesqrg
      301 yapvvrgvan thakvtvtqn gatlyettva pgafviddly ptgyggdlkv svteadgsvh
      361 sftvpyaavp lslrpgqnry sfttgvvrnl pnttpyfaqa twqrgvtnll tgyggvtfaq
      421 gylsamagav lntslgavgv dvthattsip gerrysgqsf risyakavaa tgtniaiaay
      481 rystngffal ndamlardqt klgagstsvs rqrnrasltv sqslgarggs lnatasasty
      541 wnrsgsdvnf tigysntfrn vaysvsatrq rdawgqsstm yyanlsiplg karpmtlats
      601 lsrdtrgstq aqtslsgalg vdnnlsygvn vnhgnslgts qtnggasiqy rgpiaelsgs
      661 vsaaadyqqf sagargaiva hrggvtlsqp lsetfaiiev pnaegarvtn tsgvridrrg
      721 yavvpyltpf smndigidpk glstdvelke tsqriaplag avpmltfkta ygrsavirar
      781 qadgssvpfg atvtdasgkd vgtvgqggkl larglvdqge lkvrweadrg ksvcalsysl
      841 pvrkraatyq spqilelpcv aseaasyapa vsnrvasahr
//
LOCUS       WP_175957045             837 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175957045
VERSION     WP_175957045.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 837)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 837)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 837)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 837)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 837)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 837)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..837
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87200
     Region          15..836
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 msattdliaa nvrsharryv atgiavaism afvlvslslt salttvlsrs itaqyqgaaa
       61 lvgvdrties deplvlsdlr peiektpgvg aiapmsfnfy efhkdsqrsq rrvsavlpdp
      121 ffrptlrege lpttnsqvai daqlaetlnl avgdtvdvrs ayssdryqqv tvtgvvtspl
      181 samptsyate saisavvgeg spfgylvald aqegaatpeq qealvaalnk alpehpaldi
      241 stgdhareea lnsakldaat tqaiimvfpv iamavalivv sttfqvvlhq rkrelallrt
      301 lgarssqvrr iiiaetlvvg lvaslvavlv gagltavglw atglassfld aigmistanv
      361 gitlalgtll tllvgvrpal gvarispmaa lspideaaav ssraswvkfi lgglltvgag
      421 agmymgvlad sestrfglll gasvvglvgf lvfisplmpa ltrsfglmgr sivgtmaren
      481 ttrnpgrtaa tgvaivigvt lvstmlvgas slratldgev darrpldltv qvregelpss
      541 vrsavpgiag veasveglas mgvvvessmp eaqragavrl givgqpdlnv vshspitlld
      601 ddkvllqdtf gvdagtamtv cvgdelqscg eftavlsett pyaaviseks llelapdavv
      661 drvhvklaeg adatqvqsdl atldetllve gaalerqmyt rminialgmv vallgvsvlv
      721 slvgvtntls lsvrertren gllralglsr rqmrrmlawe avfiavtatl iglvlgvffg
      781 wigmlalpvq vetlvievpw lqlagvvlvs vlsavvaawl pgrraartsp vvaladq
//
LOCUS       WP_175957068             657 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175957068
VERSION     WP_175957068.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 657)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 657)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 657)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 657)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 657)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 657)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..657
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=71608
     Region          205..645
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mklsqvhvil vgddsrgivs sivadweraf pqidlvcvad geeltrwnst llpadhvalg
       61 mvssevpnid eaftgvahmp llqdtqwill tdqdehtdla tltsaghlaa vmrapctlgl
      121 flgqayqvmv ayflqeglsr esiieligpa pkravqgpll qglgadeydm vrellegvee
      181 vigrrpriri pagvdltrqn tsiaavhlvl dgqvslrret drgelllhha tsglliglvs
      241 ltrnekafft attttpaqvv rltneqlrmv idekpsvagt lavlaiqslt rrliraedlh
      301 menavlaedl eeerahlaet ledlkntrae lvertrfaml gelsagiahe lnnpvtalvr
      361 aaehlgedld allettpama aahtamrrar tqavrstaqe relvrqiyev vgdralarrl
      421 vqagvedpve arkltkrrgk elpavelgar agsslrsvls aservielta slkgyarpds
      481 edlkavdvre glddvlrltn hrlrgiever yyedvpavla hpaklqqvwt nllvnaaeai
      541 dderedaaar gespargede plihvavecf rdqvmvtitd ngpgipasvl eriyephftt
      601 kagrvryglg mgmaisrsiv edvggsitvd stpgrtrmiv alpahatlpa tpttpte
//
LOCUS       WP_175957078             196 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia sp. BCC0405].
ACCESSION   WP_175957078
VERSION     WP_175957078.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008163
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..196
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21014
     Region          11..184
                     /region_name="COG3963"
                     /note="Phosphatidylethanolamine N-methyltransferase [Lipid
                     transport and metabolism]"
                     /db_xref="CDD:443163"
ORIGIN      
        1 mmwpnawrvs alfvrewvgr paavgalcps srqlaremad avpdgnglvv elgggtgait
       61 aallergvap rrlvvversp afvrhlrrrf pgipvvsgda rqlerllppg arvdaivscl
      121 plrtlprqdv taivdqchrv lsadgvmiqf tydlrppgrh plgdsafvac gsrivwanip
      181 parivtvrsv taehag
//
LOCUS       WP_175957086             131 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: type II secretion system protein [unclassified
            Burkholderia].
ACCESSION   WP_175957086
VERSION     WP_175957086.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..131
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14168
     Region          6..95
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 masrttngrr arrvagftli ellvvmaiia tltafvapgy lkqgdraret vlrhnlntlr
       61 qsiddyradn grnpdsldtl vanrylrevp ldpvtgkrns wlllagdagg vadvksgakg
      121 raldgsgyet w
//
LOCUS       WP_175957150             480 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Schaalia sp.
            Marseille-Q2122].
ACCESSION   WP_175957150
VERSION     WP_175957150.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..480
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=51210
     Region          206..476
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 madarptqqt gsqssrprrg lgnglgslip dappaprges arpldvlfpe sasasssrtr
       61 ggsarellqp rrssqgrksv sretsvdpak srsargqkvk iqaeagvgae aaareaeapi
      121 qaqavrgsmp tesasnesga atagksapqm dvsretslad dgqtsarvtt nvldaimgtp
      181 qngvsretse depelmavpg asfgvlrvde iipnsrqpre vfdedelael aasitevgvl
      241 qpivvrpika sdeptetlrq lleakpdary elimgerrlr aselagnstv paiirdtedd
      301 dllrdallen lhrvqlnple easayqqlma dfgatqeela kriarsrpqi antlrllklp
      361 pavqrklagg sitagharal lglneaadme rlaerivaeg lsvrtteelv rlglprhpva
      421 tqkpgektls plgerlvstl sdaydtrvti segrrkgkiv iefagaddle riaallvrda
//
LOCUS       WP_175957187             445 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF2325 domain-containing protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175957187
VERSION     WP_175957187.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10562266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..445
                     /product="DUF2325 domain-containing protein"
                     /calculated_mol_wt=48173
     Region          <186..>314
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          324..417
                     /region_name="DUF2325"
                     /note="Uncharacterized protein conserved in bacteria
                     (DUF2325); pfam10087"
                     /db_xref="CDD:431042"
ORIGIN      
        1 mhappfrlar tadlsspggn lpaatgmrvd pccapsraql telkrrtrls eldanlhcsi
       61 igtcltthel rrlvpkftdl drqhatdlei hhaavalaid gtagakalhk aldaryagai
      121 hafdsaqdad ellarwkdal qsgdiapayw almthprttm avrqaafgdl hmlshlvgaa
      181 nradirrlva leeenaalha kierqqarlh emsaqrdaal qerdalaarq naqpppaesi
      241 lrdevhalrd erlalhtsrr eaaeqriaae qasaramrar lddlmamvkt lraeasaieq
      301 avqasadepa eraanplsil qgmrlvyvgg rpgsnraiqr ivetaggavt lhdggvedrk
      361 gllaaalpga hmvvfpvdci dhdsvnqlkr icerhhiayy plrtasvasf veligrldaq
      421 ardvmapeaa rggmggtprf clrhg
//
LOCUS       WP_175957203             248 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Schaalia sp.
            Marseille-Q2122].
ACCESSION   WP_175957203
VERSION     WP_175957203.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..248
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27127
     Region          8..246
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mstpttpvld vqrvvksfgs nmvlrgldls vqshevvvll gasgsgkstl lrcanllerv
       61 ddgqiflsge ditdpridad avrarigvvf qhynlfphms vldnvtlasr mvhkqtreea
      121 evrgmelltr igldakaqef pdrlsggqqq rvaiaralat npelllldei taaldpilvg
      181 evldlvrevk eqggtilmat heisfarsaa drvvflqhgr iveqgppeqv iddplepatr
      241 eflarflh
//
LOCUS       WP_175957245             309 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175957245
VERSION     WP_175957245.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34621
     Region          7..>143
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrflsieaf vrvaeassfa eaarqlgvts svvtnriqql ekfvnaplfh rstrhvrlse
       61 vgeafyreca evvgrvnelt dqmrelratp tgrlriqmlp gfaldhfgap lmefnrrypg
      121 iqldvivndr vvdpveegfd iafqifppis eslierrlft vrrlfcaspa yldahgaphh
      181 prdllhhtta lysgypsrnr wtmtrgdevv emelpgmirs nsvhllreya lsgggvvclp
      241 tlvasealva grlvpiltdf qlaplsfaav ypatqrqalk vkalveflae tigdespwdl
      301 pllergwvr
//
LOCUS       WP_175957305             807 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Schaalia sp. Marseille-Q2122].
ACCESSION   WP_175957305
VERSION     WP_175957305.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 807)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 807)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440013
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..807
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=86712
     Region          24..806
                     /region_name="YprA"
                     /note="ATP-dependent helicase YprA, contains C-terminal
                     metal-binding DUF1998 domain [Replication, recombination
                     and repair]; COG1205"
                     /db_xref="CDD:440818"
ORIGIN      
        1 mssshsasll alverigrqh gqhvhthvip sregvvvpwp qwvdervvaa warrgveapw
       61 ahqaltldai gegadvvlat gtgsgkslaa wtpilsdlae safttrisqv hrrptclyls
      121 ptkalaadql aavhrllaes elevratcad gdtpreakew aranadivlt npdfvhfvll
      181 pghqrwtrfl sslryviide lhhwrgvtgs hialvmrrll raarrlgadp qvimlsatvr
      241 dpervgeami gragvravme dtspagvrhl alwqarevvd etaipmdsfl aalageipvl
      301 eaptrrvsaa teaalltadl vaaggrvltf vrsragaeav aaqarerlda tvggdlsarv
      361 gayrggylpe erraleaalr sgavralatt salelgldvs gldatvtagw pgtraslwqq
      421 vgragragae gvsvlvasdn pldtylvhhp eqvlapveaa vidpsnpwvl aphvcaaaae
      481 fpfsadegdf ecfaladdal lrdlvaqgyl kkrwdgwrwd vtrperacdl tdlrggggdv
      541 qiveaatgmv vgsvpdgdad sqvfpdaiyv hqgktyhvls lmpvapgspq rvaeveevat
      601 rlrtrakqhv svqirevles wtspdhtvtw nfgavdvasr vtdydllrlp gleflrnqel
      661 slptrtlvtk svwytitpta lraigvkkad vpgalhaaeh aaiallplla tcdrwdlggl
      721 staehedtil ptvfvhdayr ggaghsqygf dharewvgav leavescpce dgcpscvqsp
      781 kcgngnepls kagavavlry llertpr
//
LOCUS       WP_175957318             451 aa            linear   BCT 11-JAN-2025
DEFINITION  uracil-xanthine permease family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175957318
VERSION     WP_175957318.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..451
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46037
     Region          9..423
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mshdpiptpv dprlpawqlv lfglqhvlsm aaspitavfl iakvlalpae ltvqligatf
       61 facgigtllq slgagpigar mpfvmvpgga ptmlfagiaa qsglptaaga allasafywv
      121 llpvftrclr lfprivvgam mllvsinlir iyativvgqp gsadfaqpra lglalativt
      181 tvvvagafrg tigrlavlig lmagatlgwa idampaladv wrgplfthpv wlpfgmprfd
      241 vlaalpllif taismaeata qtvavgetcg ktislsrdvp ktirgdalas lagalfgtpl
      301 ivtsaenigv vqttgvrsry vtaaagaili vialfaplar layaipaavv ggtalvvfam
      361 igvmgirlla svdlharasq ytlaaalvvg lapilvpnly rhfgapvqiv lgngmaagtl
      421 aaiatqlafa afarvrgpvs tgavpapsrd a
//
LOCUS       WP_175957330             711 aa            linear   BCT 11-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Schaalia sp.
            Marseille-Q2122].
ACCESSION   WP_175957330
VERSION     WP_175957330.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..711
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=76248
     Region          1..679
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 msksrsrnvr ptqlvtlvgs ffalsglmgt lvagmmipav gsvgivaktv ptvfdglpse
       61 irvvapaees illdaeggvi arffdkrril vpsdkiadvm kqaivaiedk rfyehhgvdp
      121 egmaralvnn lsdggkqgas titqqfvrns iqergylegd aelaysaveq ttqrklrevk
      181 yaltlektms kdeiltgyln iapfgpityg veaasqlyfs hsaaelnwle aallaglvqs
      241 pvdynpltnp eaaetrrntv lmvmrnegii teedyqngln tpvadmlkpn etpqgclgas
      301 ginayfcdfa igqflddpaf gdsyakrerl lktggltirt tlnprlngaa yqslinaipv
      361 hdesgldtam ttvepgtgrv lamaqnteyg vdegktmsny sangvfqvgs tfklftllqw
      421 lkegnsayas vgranriyvn gefscggepi ytdtydvedl pgkngtftai satglsvnqa
      481 finmasrvdf cqifqtaadf gvtdangeiv qalpanilgs astspltman afaaiahdgq
      541 lctpqaltlv tdrsenvike ytpqckevis ptvarqaani lgkstaryyn atrleggrpf
      601 gaksgttnhn antwltgftp qyatsawvgr atasqqpvqd ivingnyyda iygetfvghn
      661 iwapymsvah eghdviglpd vfigniptpp rptptptptp ntagngaqsg r
//
LOCUS       WP_175957369             144 aa            linear   BCT 11-JAN-2025
DEFINITION  Fur family transcriptional regulator [Schaalia sp.
            Marseille-Q2122].
ACCESSION   WP_175957369
VERSION     WP_175957369.1
KEYWORDS    RefSeq.
SOURCE      Schaalia sp. Marseille-Q2122
  ORGANISM  Schaalia sp. Marseille-Q2122
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Schaalia.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Schaalia sp. Marseille-Q2122"
                     /db_xref="taxon:2736604"
     Protein         1..144
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15896
     Region          1..138
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mtleerrtsi keaglrvtap rlavldvlha hphatadmvv taveeklgsi skqaiydala
       61 aftqagllrr qvvegggary eiergdnhhh lwcercgkye dvdcalqqpp clypvddhgy
      121 tirladivyr gvcpdcqkai dqes
//
LOCUS       WP_175957435             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0405].
ACCESSION   WP_175957435
VERSION     WP_175957435.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46054
     Region          22..420
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,150,
                     153..154,157,245,248..249,252..254,257,285,289,347..348,
                     352,356,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnetptvppa pprirrgqri alallmasgi vnyldrgtla vassairgdl glslsqmgll
       61 lsafswsyal cqfpvgglvd rigprrllgi glivwsfaqa aggivstfgw fivarivlgi
      121 geapqfpsaa rvvsnwfplr argtptgifn aasplgtala plllsilvas fdwrwafiat
      181 gaaglvvava wfalyrdpvr aqltaaerny ldadaqsava apkltfaewr glfshgttwg
      241 mligyfgsvy lnwvyltwlp gyltmerhms lirtgfaasv pflcgfvgsl lagwlsdlvt
      301 rrsrspvvsr rnavvvamlg mvaftipaal vqsntvalac isvviflana asacswalat
      361 aaappsrias lgaiqnfggf vggalapilt giiaqkwsfv palltaaaia fagamaylll
      421 vrkpipeqaa naapgplpa
//
LOCUS       WP_175957407             214 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175957407
VERSION     WP_175957407.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..214
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24331
     Region          1..210
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mltvwgrrna fnvqkvmwlv delalahrhi paggqfgvld tpaflamnph grvpviddgg
       61 tvvweshcil rylaarygrp gfwrddpaeq sradrwmdws qstlqptfln cvfrgyfrtp
      121 peqrdttrie qsiaacaqhf qtldaalagq pflagnaltl adiaagthly ryfeldiarp
      181 dlphvqawye rlkarpayrt hvmipfddlr grld
//
LOCUS       WP_175957389             215 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC0405].
ACCESSION   WP_175957389
VERSION     WP_175957389.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..215
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22388
     Region          10..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mhtsgslcgf lviggmlavt pgpnmvyvms rsiaqgrtag lislggvmig ylfymfgaaf
       61 gittlfmrvp yagsglavvg aayllylawq avrpggrspf evqalpserp lrllamgatt
      121 svlnpklaml fisllpqfid yrngsvlgqs lflgallita facanglvai gssriakflh
      181 grptlllaqr wamglilggl gvqmlvdask magva
//
LOCUS       WP_175957490             143 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia sp. BCC0405].
ACCESSION   WP_175957490
VERSION     WP_175957490.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 143)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..143
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15459
     Region          4..119
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04667"
                     /db_xref="CDD:467552"
ORIGIN      
        1 mkaratvlcr rgdrillvar sharwklpgg cpkpgeslgd aarrelaeet glacrnlryl
       61 fraagkhklh hvfladldah aiarpsreia hcawvdrltl asidcsaptp aivelalald
      121 mtpdappvtf mihveaaqav lte
//
LOCUS       WP_175957651             586 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia sp. BCC0405].
ACCESSION   WP_175957651
VERSION     WP_175957651.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..586
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=63682
     Region          7..586
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mkmrkrltal pitalvslgv haqqvptpad qaaagranae qdrqaqqqrd aqqrdaavra
       61 psvrsevpkv eaypalpves pcfridrfal dvsaslpdat kaegasalpm drfafardwl
      121 ghyagqcvgk qgvdvlvkgl sqailargyv ttrvlvpeqd lstgtlklsl ipgvirhirf
      181 adeklrgtwk tafptgdgev lnlrdleqgl eqmkrvtsqd vsmqivpgel pgesdvvldv
      241 krgkpwtvva sidnsgtrat gklqgnlsig idnplglndi lnvgvsqdle fgdkrlgshg
      301 wngfysipwg ywtatlsant ntyyqqiagv nqtfvasgns ktvdfklarv larsqndvlg
      361 gyfrlsrrfg qsfiedteis qqrrnntiie lgltdrhyfd gaqfdgslay rqgvggfgaq
      421 ddtlaadggp tyrfkmalld anlsvpfaig kqpfryvgtf hgqytgntly ylddmtigsr
      481 ytvrgfdget mlaaargfyw rnelqmpigq tgqavyagld ygrvwgpqpi vlvgtqlaga
      541 vigvkgsigt rfgayaydlf agtpvykpsg fptarvtvgf qltsqf
//
LOCUS       WP_175957694             532 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [unclassified Burkholderia].
ACCESSION   WP_175957694
VERSION     WP_175957694.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..532
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58017
     Region          1..449
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mkssiqrnig pfalmltglg siigsgwlfg awkaakiagp aaicawiiga vvilaialty
       61 aelgamfpes ggmvryarys hgslvgfisa wanwiaivsv ipieaeasiq ymstwpypwa
      121 halfvngelt tpglllsavl vviyfmlnyw gvkafarant titifkflip gltilglmlt
      181 syhpenlgta snasfapygw savltavats givfafngfq spvnlagear npsrsvpfav
      241 itsilialvi yvllqvayig svnpadvaqg wshfnfkspf aelaialnln wlaillyvda
      301 fvspsgtgtt ymatttrmiy amernntmpk mfgnvhplyg vprqamwfnl lvsfiflfff
      361 rgwsslaavi svatvisylt gpislmalrr aatdierpls iplmkliapf afvcaslily
      421 wakwpltgei illmivalpv yfyfqaksgw tgwgddlkaa wwlvaylptm avlsligske
      481 fgghgvlpyg wdmlivaais lvfyfwgvnt gyrtkylder esedeilegi ga
//
LOCUS       WP_175957677             320 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175957677
VERSION     WP_175957677.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..320
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33113
     Region          33..318
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          215..318
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(220..221,254..255,258,262..263,266,308,312)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mhrtihvrra rlsaalspav aallaaglfa sgaafaqntg atvtpvgngt vatttlpant
       61 gvapgtassa vvhgtagtan titpppanat pgqvvvggkv pdeatkaavl qklrdtygaa
      121 nvvdqievgd vatppnwsan vqkllgtqlk qiskgqlkin gtqiemkgev hneaqrqqla
      181 sdmantlnpt ytirnglrvs aseqgvldqt lanrtiefet gsatltpqgk lildqmaaal
      241 akmqnrtvdi ightdnsgnr tsnialsqar adavkgylit knippqqmtt tgvgpdqpia
      301 pndtadgrar nrriefrvgq
//
LOCUS       WP_175957750             512 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175957750
VERSION     WP_175957750.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..512
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51822
     Region          88..491
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrlpeppaas iaalataval agcatssidl apeasdrpwq pptsaagdiv pgpprasaqg
       61 shdytlpasp alasvsppaa ldaahaytlp elidlaesan pltriawnda rnaalavgla
      121 kaaylprlsa tamggyqanh gttssilgds ssnstvhgti salslqwllf dfggraarve
      181 aaeqasiasn vaftavhqqv ihdvtvayyr yeaarsrals arqglanada ilaasrarlk
      241 hgvgtvvela qatqnraqan lalvqangte sdgylalvsa lgisplskpt iaalpkrplp
      301 palgasvdai vsdaiarrpd lqgafaleka nrakikaaea afmpkiflsa stsyasggts
      361 isalpaigdq aptvnlngsr ygggvflgvt iplydgglrs avlmqarnda esasarltrt
      421 keeavrqvva aqnavqtsla shdaakalvd aaqtsydaal tayrngvgsv tdatiaqsql
      481 laarnaevds yagalsaaaa lalatgtigs aq
//
LOCUS       WP_175957823             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175957823
VERSION     WP_175957823.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33803
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,160,162,223,240,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mnqlqamrvf trvvelssfn laarqlgmsa aavtrsvgml eahlnmrlln rttrslslte
       61 tgreyldgcr tiiekldeie snlvqatrdp rgtlriaasa tsvaaglgll lsayraahpr
      121 vrfdvttfdt hvdmveggyd vcfcddrrli katfvsrmlm svrdvvvasp eylarhgtpn
      181 dpgelnehsl ltvsngtars wefsdvdgay rvytgnalas sgsmmvriaa lnhmgitqlp
      241 hplvaddlar gtllpllery evnggprcvs mlypsrnyls tkvrsfidyv vdhyralerd
      301 tvqlsaa
//
LOCUS       WP_175957904             796 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia sp. BCC0405].
ACCESSION   WP_175957904
VERSION     WP_175957904.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..796
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=87081
     Region          25..742
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mpmqsttpts pppapepkkr pwwqkvllgf atmcvalvva gglvlgyalv vawpnmpsld
       61 altdyrpkvp lriytsdhvl igefgeerrd vvhfkdvpds lkkailaied arfydhggvd
      121 ltgivragfv altnghasqg astitmqvar nfflssekty trkiyemlla yrieraltkd
      181 qilevymnqi ylgqraygfa saarvyfgkd lkditlaeaa mlaglpkaps aynpvvnpkr
      241 akvrqeyilq rmlelnfisr eqydeavaqp lvvkgpgrdf svhaeyvaem vrqmmyaqyr
      301 eetytrgfnv vttidsadqq vaytalrkgi mdyerrhgyr gpegfidlpa gaddreqaid
      361 dallehpdng eliaavvtaa sprqitvafi dgsnatiegd nlrfasgals anaqpnrrir
      421 pgaivrvvkn dtgtwsitql pqvegaflsi vpqdgairsl vggfdynknk fnhvtqawrq
      481 pgssfkpfiy sasldkglgp atvindgply fsaaetggqp wepknygggf egpmsmrtal
      541 qrsrnlvsir ilnhigtkya qqyitrfgfd aerhpaylpm algagqvtpl qmagaysvfa
      601 nggyrvnpyl iaevtdpnga ivvraqplva eqnapraida rnayvmnsll qsvaqrgtga
      661 rtnvlkrtdl agktgttnds hdawfagyqh tlaaiawigy dnprslgdre tggglslpvw
      721 idymgaalkg vpefkpavpd gveslggely fteftpghgf vstvgvpqap aaqnvdatvp
      781 hvdeqekqdi mnlfah
//
LOCUS       WP_175957933             442 aa            linear   BCT 11-JAN-2025
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Burkholderia sp. BCC0405].
ACCESSION   WP_175957933
VERSION     WP_175957933.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..442
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=47296
     Region          71..440
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 malgehlrqq laakalkrql eratdaaaap gvpgtpaaqg asarsrfesm pqyqqvrimr
       61 emgeklrvds pffrvhdgva gattqiggre ylnfanynyl glagdpavsa rakaaidryg
      121 tsasasrmva gerpvqrdle ralaafyetd dcvafvsgha tnvtvigalf gpgdlivhda
      181 lahnsivqga qlsgakrlsf ahndwqalde llarvrreyr hvliaiegly smdgdfpdlq
      241 rfvdvktrhg afllvdeahs lgvlgatgkg irehcgvapd qvdmwmgtms ktlagcggfi
      301 agcqplvdml rhlapgflys vglaptlaea slaalerlqa epervaqlqa rgrqflaear
      361 aaglntgtsa gfavvpvitg sslkaaqwan amfdeginvq pifypaveek aarlrffics
      421 thepeqisrt vavlsrlagr sa
//
LOCUS       WP_175957859             252 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome c1 [Burkholderia sp. BCC0405].
ACCESSION   WP_175957859
VERSION     WP_175957859.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 252)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..252
                     /product="cytochrome c1"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28346
     Region          18..252
                     /region_name="CYT1"
                     /note="Cytochrome c1 [Energy production and conversion];
                     COG2857"
                     /db_xref="CDD:442105"
ORIGIN      
        1 mkkllstlal igatacallv apavraegnf pldrapdnte nlvslqhgaq lfvnyclnch
       61 sanlmrynrl tdlgisqkei eknllfttdk vgntmsvamr pedaknwlgt sppdlsveer
      121 argrdwlyty lrsfyrddtr ptgwnnavfe nvgmphvlwq lqgqrtakfe dktdeetgek
      181 vhtlvgfqqv tpgtlsavdy dsavadlvay mtwmsepaqq trkrlgvwvl iflgvltfla
      241 wrlnaaywkd ik
//
LOCUS       WP_175957974             121 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: BON domain-containing protein [unclassified
            Burkholderia].
ACCESSION   WP_175957974
VERSION     WP_175957974.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..121
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=12011
     Region          59..>120
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mksivlralg vaavaaclsg svyaqssdaa ameapaaats apkaaaktak kanrklgyav
       61 rkaiskesgv nvsnlvvrsk ggaitlegtm paqdqidkae aaakgvkgvt svtnkltvqq
      121 q
//
LOCUS       WP_175958026             341 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-binding protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175958026
VERSION     WP_175958026.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 341)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10025428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..341
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36961
     Region          13..160
                     /region_name="AAA"
                     /note="The AAA+ (ATPases Associated with a wide variety of
                     cellular Activities) superfamily represents an ancient
                     group of ATPases belonging to the ASCE (for additional
                     strand, catalytic E) division of the P-loop NTPase fold.
                     The ASCE division also includes ABC; cd00009"
                     /db_xref="CDD:99707"
     Site            26..33
                     /site_type="other"
                     /note="Walker A motif"
                     /db_xref="CDD:99707"
     Site            order(27..34,96,134)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:99707"
     Site            92..97
                     /site_type="other"
                     /note="Walker B motif"
                     /db_xref="CDD:99707"
     Site            152
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:99707"
ORIGIN      
        1 mklsparltq llrvyipnrl pvlitgrpgc gksdiveaat deadhdllis hpvvedptds
       61 kglpfpaadg lharflpfgd leralsatrp lvwffddlgq aspavqaakm qlllahrige
      121 hvlpdcvtfv aatnrrsdna gvtgildpli srfaavvele atiddwtawa vrqnvppeli
      181 aflrfrpnll weerssrdiv asasprkwgf laktlpavpa dllpdainat vgegagaelt
      241 sflaiyrvlp svdaillnpd lgaipeepsi lyaltaalah kasdgnferv lryaerlvde
      301 gyreftallv rdatarkpel qshhafiral ggeigkiitg n
//
LOCUS       WP_175958193             264 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC0405].
ACCESSION   WP_175958193
VERSION     WP_175958193.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13673959
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..264
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27609
     Region          12..144
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Site            order(28,30,34,68)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:380405"
     Region          179..260
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mhrvthyrrt gegieaisle sdrafprhah defgvgvivs gahrswsgrg qvdalagdai
       61 mvnpgemhdg spieagtgrr wrmlylapal vagvaaeegl ggvelahpav rdarlaaavg
      121 rlharivage spplardeal vmlvagllar hasrtlppag vapairiare rldaapaapv
      181 slaelaglsg vsrfqllrgf arelgitpha yliqsrarla rallasglpi adaaaeagfa
      241 dqshltrafa rqfgitpgrf tqav
//
LOCUS       WP_175958211             469 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia sp. BCC0405].
ACCESSION   WP_175958211
VERSION     WP_175958211.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..469
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50192
     Region          14..467
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mnhpaqpaat rrplppamld alraafgerv staeavrahh grdespfdpq lpdavvfars
       61 addvrevval cslysvplip ygagsslegh llavrggisl dlsemnrvls inaedltvtv
      121 epgitrkaln ealrdtglff pidpgadasi ggmtatrasg tnavrygtmr envlgltavl
      181 adgrvvktgs rarkssagyd ltrlfvgseg tlgviteitl rlhplpeavs aavctfpsmg
      241 davravieti qigvpiarve fvdalavrsi nrhsnltlte aptlffefhg teagvkeqae
      301 lvqalagqnd gqgfewatrp edrsrlwaar hnayfamlql kpgcravttd vcvpisqlaa
      361 cveetevdlr asslpcpivg hvgdgnfhva ilidpdkpee laeaerindr iveralrlgg
      421 tctgehgvgl hkmrflpkeh gdnaidtmra iklaldprnl mnpgkiftc
//
LOCUS       WP_175958247             266 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175958247
VERSION     WP_175958247.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..266
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=27301
     Region          47..197
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mnqsrvkqtl vrttllaalt aglavslqgc vlgvvgaaag ggaliatdrr tlgaqtedre
       61 iqvkalsqin nglpdqshvn vtvfnrrvll tgevpndask qraeeivrai nnvngivnel
      121 svepasslss randsylegr vkseliatkg isanyykvvs ergnlylmgl vtvdegnrga
      181 eaasqvpgve kvvkvfqyiq pqdaqalqna spasgasgaq aaaapadtat vgavpdasvq
      241 stplqspapi snsssvhpgn pkapsq
//
LOCUS       WP_175958296             243 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175958296
VERSION     WP_175958296.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..243
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25974
     Region          4..210
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mspillygvp agcsfgsiva lewigrpyrl slvtmpgivt sdaylalnpv aetpafvtan
       61 gdvlteslai lghigaqald sglafrqgsa efdrlnrmla wlnttffnaf galwfvyehd
      121 tegaekaalq aygrgkvlka hrqleamler gdgpwllgar rtladayfag iarwadyhav
      181 fepaafpria alrarladda gvqfaqaiee nlplpassaf eghvsvddal asardiaipa
      241 rai
//
LOCUS       WP_175958326             238 aa            linear   BCT 11-JAN-2025
DEFINITION  O-methyltransferase [Burkholderia sp. BCC0405].
ACCESSION   WP_175958326
VERSION     WP_175958326.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..238
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26419
     Region          78..238
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 masptiallq rlheesrtei iararaqfqg snedflslae eydaiaprlr grfletfgls
       61 sddfespegs rlslavspet ggflrnmvls qrparilelg sscgvstlyf adalrmlgrg
      121 vivaterdal kcaqlrthvr tagldayvdm regdvfetva eldgafdmvf idvwadaylk
      181 lfkqverllr pgsvvladnm ytaedtvrpy khyldndprf stttldfesg veftvvvs
//
LOCUS       WP_175958475             217 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175958475
VERSION     WP_175958475.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..217
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23903
     Region          29..180
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtevterapa krrmrgrpla gasvgpdvil raarqmfakr gydatsvrev arelgvdaal
       61 iahhfgtket lwlavleqia elaqpmfdal ralrtsplsh rdrvlraiel cvehefdepd
      121 vgmffstaat evggrldrlq erlvrpyydv lfpllsdgve agvirpvdpt vlffmlasai
      181 gttvsyshmm leytslptqq dafrkavada afnvvgv
//
LOCUS       WP_175958488              86 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl carrier protein [Burkholderia sp. BCC0405].
ACCESSION   WP_175958488
VERSION     WP_175958488.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 86)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..86
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=9507
     Region          5..74
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mdklsdqeil sriervflkr rkstdgelsp dmtledlgld sfdtvemafa leeefgveip
       61 geglrnvstv rdlvvvfrda vnasts
//
LOCUS       WP_175958478            1057 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia sp. BCC0405].
ACCESSION   WP_175958478
VERSION     WP_175958478.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..1057
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113372
     Region          1..1038
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mdfsrffidr pifavvlsiv ifaiglisip mlpageypev vppsvvvrat ypganpkeia
       61 esvaepleea ingvegimym ksvagsdgsl qvvvtfvqgv dpdtaavrvq nrvsqalsrl
      121 pdevrqygvt tqkqsptplm yvslyspdns hdslylrnyl tlhvkdelsr lagigdvgvy
      181 gsgdyamrlw ldpnrlasrg ltasdviaav reqnvqvsag qlgaepspkk ndfllsinvr
      241 grlrtvqefg divlrngddg qvvklsdvar ielgagdytl rsyfndrqsa vvgiflspga
      301 nalevakavy akfdelskrf ppgvayrpvw dptvfvresi ravqhtliea vvlvvlvvil
      361 flqtwrasii plvavpvsvv gtfawlyllg ysintltlfg lvlaigivvd daivvvenve
      421 rniaqglspr daahqamrev sgpivaialv lcavfvpmaf msgvtgqfyr qfavtiaist
      481 visainsltl spalaakllr phgapkdalt rgldrafgwl fhpfnrffdr ssdryhgfvs
      541 rtlkrrgmvf avyaallaat tlllnavpgg fipvqdklyl fagaklpega slartsevte
      601 qmtkialgtd gvemvpafag lnalqgvntp nitnsyvilk pfdqrhrsaa einadlnarf
      661 aaigggmtya lmpppiqglg ngsgyslyle drgglgygal qnalaafqaa vaktpgmsyp
      721 vssyqanipq levkvdrlka kaqgvaltdl fstlqvylgs myvndfnlfg rvyrvmaqad
      781 aghrqtaadi anlrtrnakg emvpigsmvt vapaygpdpv vryngypaan ligdadpkvm
      841 sssqaieklq qiakdvlppg itlewtdlsy qqvtqsnaai vvfplavmlv flvlaslyes
      901 wtlplavili vpvcicaalf gvwlsggdnn vfvqvglvvl mglacknail ivefarelei
      961 qgkgvieaal eacklrlrpi vmtsvafiag svplliggga gsevraatgv tvfagmlgvt
     1021 lfglfltpvf yvairklagg tpavwsehhg tlegenr
//
LOCUS       WP_175958536             379 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia sp.
            BCC0405].
ACCESSION   WP_175958536
VERSION     WP_175958536.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0405
  ORGANISM  Burkholderia sp. BCC0405
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia sp. BCC0405"
                     /db_xref="taxon:2676298"
     Protein         1..379
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=41315
     Region          15..351
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mtasqparmd lpgqvvlvlq gggalgafql gvfqamdeag irpdwvvgts igainaalia
       61 gnppglryek lsafwrrvte rtrfdtapll pgwdrtlael miigggiagf fqpnpaswlg
      121 pmvrlgvdra syyriaplrd tlmslidpdl lnaghprltv savnactgtm ryfdsrdtrl
      181 giahimssga lppafpairi dgepywdggv ysntpvevvl ddnprrssii fsvqmwnpag
      241 pepesiwqvs erqkdiqyas rtdshiarqq qihrlrhvir elarhvpeae raspavrrla
      301 awgcettmhl iklaaprlas dnqlkdidft pdgiaarrqa gyeaaqraia ahpwdtptdp
      361 meglavfdas appipenpa
//
LOCUS       WP_175958651             447 aa            linear   BCT 11-JAN-2025
DEFINITION  hemolysin family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175958651
VERSION     WP_175958651.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..447
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=48977
     Region          1..447
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mlqifaliga lflvalngff vaaefglvkl ratrvktlar khglrgrilg ivhgrldayl
       61 sacqlgitla slglgwvgep afaeligpll dligvhserv vhlislvfaf slisflhivv
      121 gelapksmai rqsekvglwv alplyafywa mypaiwvlnn sanavlrlag lsadhggdah
      181 ystdelklil rsrrstagna aqpargtysn dewntlahsl dfssmtvsdl mrpahemigl
      241 rrdlplpdnm eivarhrfsr yplfedasre qvsglihlkd lllarhagaa ledlsdyvrp
      301 vqyvkpdtpa lelfrrfrkg aphfalvgnk gekpigfltl dnllgalvgq ihdefrqgda
      361 dwsrlddgtl mgkgslpvvs leqalgidid egraesvggl viqalsdlpt egqrvsfdrf
      421 dvvvkkmngp rivlvrvypk iakeade
//
LOCUS       WP_175958811             508 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Burkholderia pyrrocinia].
ACCESSION   WP_175958811
VERSION     WP_175958811.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..508
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53917
     Region          16..491
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(72,74,78,81,85,118,121..122,131..138,143,146,149,
                     242,246,249,252,254,427,429..430,432..433,436,439..440,
                     442,444..447,456,460,462,476,483..488,490..491)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(158..161,169,184,187,217,234..237,240,258..260,292,
                     392,394,420)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(161,258,289,292)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnaavpqttl alptakllid gafvesqsae wgdivnpatq etigrvpyat ldevdaaias
       61 aqrafqtwkt tpigarlrim lkfqdlvrrn leriahtlta eqgktlpdaq gdifrglevv
      121 ehacsigtlq qgefaenvag gvdtytlrqp igvcagitpf nfpgmiplwm fpmaivcgnt
      181 fvlkpseqdp lstmqlvela ieagvpkgvl nvvhggktvv drlcthpdik aisfvgstrv
      241 gthvynlgsq hgkrvqsmmg aknhavvlpd ahreqtinal vgagfgaagq rcmatsvvvl
      301 vgqardwlpe lvekakalki naghepgtdv gpvvskaaha rvtalidegv kagakleldg
      361 rnvtvpgyer gnfvgptifs gvttdmsiyt eeifgpvvvv leadtldeai alvnrnpmgn
      421 gvglftqsga aarkfqseid igqvginipi pvpvpyfsft gsrgsklgdl gpygkqvvqf
      481 ytqtktvtar wfdddatagg vnttialr
//
LOCUS       WP_175958812             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175958812
VERSION     WP_175958812.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46985
     Region          28..433
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(39..40,43..44,47,86,144..145,147..149,152,172,
                     175..176,179,261,264..265,268..270,273,301,305,358..359,
                     363,367,383,386..387,390..391,394)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mqtrstldeh atvatpapar takhyllagw asmagttiew ydfflygtaa alvfnriffp
       61 sldpvvgtla afgtfavgfi grpmggivfg hfgdrigrks mlmitlllmg vpsmiiglip
      121 sydsigywaa alliamrflq gmavggewgg avlmavehap kgrkglfgsl pqtgvglgli
      181 lsslamaava alpeadmlsw gwrvpflasi alvglgwfir akvpespdfe kmqrqgkaek
      241 spvtaalrrh prevltivga raaentwfym vvtfalayat qqlhlpkaem lhaitagavl
      301 slvtmplcgh lsdrigqrrm faiglvlmca faapffmmlg tqqtsyawwa ivlglgvvfp
      361 ilyapesllf aqqfpaeiry sgislsvqla gvigggfapm iatsllkagg gqphyviayl
      421 vgfgmfalvc talmrpprt
//
LOCUS       WP_175958883             130 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175958883
VERSION     WP_175958883.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..130
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14572
     Region          8..115
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mngskayleh vaiwvkdihw hirffedvlg mtmrevdgtv eeprqywtlg glqfihnprh
       61 dapegrlghl gvmcedleaa laaaqkydvs empqgrnwlr lpdglaveli qakpascvar
      121 aldinprsev
//
LOCUS       WP_175958884             316 aa            linear   BCT 11-JAN-2025
DEFINITION  ketopantoate reductase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175958884
VERSION     WP_175958884.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..316
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32627
     Region          1..307
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkiailgaga lgcaigaalt eggnevwlln rsvahveamr rdglcvddan gsrrvkvkat
       61 traaeagaad lvvvlvksfh tdaamrgald ligpdtlvls lqnglghedv ladivgrerv
      121 lagktyvggv mrnpghiesg vagkttyige ldgritsrvt aiaetfnaag lattvsdniv
      181 gtmwdkllvn vatgaltgat gltygqlyde pllkaaalaa vaeaiavaha agvtlsttdp
      241 erpwnlageg lssafktsml qslekgsite idfingavvr wgqrhgvptp vnatlvacik
      301 gieramadrq hretta
//
LOCUS       WP_175958936             424 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia pyrrocinia].
ACCESSION   WP_175958936
VERSION     WP_175958936.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..424
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41696
     Region          5..>328
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpahadspaa hhagsltifq gaalyigavl gtgvialpal aaevagpasl lawaalvvls
       61 gplaatfaal garypdaggv styarrafgp kaaaivgwcf yfavpagapa aamfggayva
      121 avmggghttv ivtaaaliaa vsaanafgvt vsgrmqlvls allvalllaa vlasaphart
      181 anlqpfaphg wlavgqaaal lvwsfagwea ithlaaefrr pahdmprsag iavvvvgfly
      241 lsvaaasvtv lgpsagasga plaeliaggi gghaqvlaaa aallltlgtm nayfagaakl
      301 gaalgrdgal pawlaqgsqv ggvprrslgv iavlaavala attisdvgpk plvlvtsgcf
      361 vmvyglgaaa alkllprgci ayrcawislv avaglflttg wyllcpllla ggallylqvt
      421 gprn
//
LOCUS       WP_175959039            1082 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia pyrrocinia].
ACCESSION   WP_175959039
VERSION     WP_175959039.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..1082
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115763
     Region          1..1065
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mwivnlalrr pytfivmaim ivlatplalm rtpvdvlpai nipvisviwn ysgfsatemt
       61 nritavheri ltttvnniqh vestslpgia vvkvflqpga nvqtaiaqtv ssaqaivrqm
      121 pqgatpplvi tysassipvi qlglssttls eqsladialn flrpqlitip gaqvpfpygg
      181 rtrvvaidld pqallakglt padivnavna qnlvlptgta kmgqteyrid tnasadtvad
      241 innlpiqtvs gattylreva svrdgfapqt nvvrqngqrg vlvsilksgd astlkvvsdl
      301 kallpkvlpt lpegltitpl fdqsvfvnaa vqgviheali aavltammil lflgnwrstl
      361 iiaisiplsi ftslialsal getinimtlg glalavgilv ddatvtieni erhlhlgtrr
      421 aapsvpsgpl ggqrpegarg ssfstdlhea ilegageiav pafvstlcic ivfvpmfflt
      481 gvarylfvpl aeavvfamla syvlsrtlvp tlamllfrpq qastgpdhat srfarlhhaf
      541 nnaferlraw yivllsmllv rrrfyamcfl gfcvlstglv falgrdffpn adsgnirlhm
      601 raptgyriee tarladrver virevvppde lgaivdnlgl pvsginlsys nagtigtldg
      661 ellialkpgh ratrdyvqtl rrllperfpg vefffqpsdi itqilnfgqp aaidvqvlgn
      721 dlasnmtias nlmkkvrqip gavdvhvlqr ndeptlladm drtrmqqlnl saqnvaqnml
      781 islsgssqtt psfwinpktg vqyplqiqtp qydissvddl lgtpisasgr tgmplqllgn
      841 lvqvrtaanp avithynirp aidlyvsveg rdlgsvagei drivsdmras lprgtdltmr
      901 gqietmrtsy iglgagvama ivlvyllivv nfqswldpli iisampaala giawmlfitg
      961 thlsvpaltg aimtvgvata nsilvvsfar qrlaagappl taaleagatr irpvlmtala
     1021 miigmvpmal glgegaeqna plgraviggl lfatvstllf vplvfggvhs rlarrrarqa
     1081 gh
//
LOCUS       WP_175959052             323 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175959052
VERSION     WP_175959052.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..323
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34810
     Region          12..71
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..298
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(110,114,153,167,170,233,250,277)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(111..112,116..117,119..120,123,127,129..135,197,
                     227..231,238..239,242)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mkqnftvrqg aldgveafls varhrsfrra aaelgvtpsa vsqavrmlee rigaalfirt
       61 trsvglteag erflsrakpa feelvaasev arslgqrptg llrlsvprav vpilleplia
      121 sfcraypeie veiaanealv dlaaegfdag irlgqfvaad mvavpltppf rlvivgspay
      181 fagrsrperv ddlrehaclr wrrsngalap wsfndndrei evavsgplia hdfptllgaa
      241 veglglaqlp epmvsealka gtlvhvlepf apvrpgvfly ypgrrqimpk lrafidhvkn
      301 hppglgkvpa hhaperagpg kng
//
LOCUS       WP_175959065             727 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175959065
VERSION     WP_175959065.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..727
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79463
     Region          39..722
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mkpqpaierp sieparwrsw ldplgdaard wavsdgliwl hlaktvfaal lamgiamrle
       61 msqprtamtt vfvlmqplsg mvfaksfyrv lgtaaglvaa lalgglfaqq pelymagitl
      121 wiggcialav rnrhfrwygf vlagytaali glpavmtpqt lfqsaltraa evalgiacsg
      181 avsalilpls sakalmrsln trhttfaaft sgalagdvar gdferrfadf vddivgfean
      241 rafasfedph irarsrrlar lnsefmnact rlhalhqlvk rlrangsdav ldalaphvda
      301 laqrfaalrd erqhgiapat gallelrrfh galpkaaras rrtieehaag glldfdtaie
      361 llyrfigeyl gyadtyasld qddhafersv thyavktnsf fvgfaflrtv iavgamsafw
      421 iasewpsgsl aviataiaca lsstsprapk fvaqmgvgaa fatavgylfl cyvypnidgf
      481 pllcatlapv lglgaflamr pglsgygigf avffcllagp dnaiaytpev linnglavvv
      541 amlacslvfa vvfpthmpwl tgriahdlrr qvtlacegap dglaqrfqss thdlmaqlrt
      601 llvrrtrqhr dalrwmlstl evghavidlr delhafceak ppqmlrwtgs idavlhelpr
      661 ffddptpghh artlksvnla iraaqhtlqa wyavpderrr mqrivgclhf mrsalldrda
      721 pfnrrrh
//
LOCUS       WP_175959062             468 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia pyrrocinia].
ACCESSION   WP_175959062
VERSION     WP_175959062.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..468
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48754
     Region          17..461
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mammsestgt lqaapateda pralsqtlsv rdavmitvsg vtpassifvi apfaiqqags
       61 gavlsfllgg vlalafalcy aelsaahrsa ggeyvmakrv fgtlpgyltf itvlsvsvfi
      121 pavlasgaap ylnnalgthf gnqsvaltiv llsyllgmln iktnawitga flvveigvlm
      181 liaglgfgsl hrgadvlvap vaasgnalvp atlaaivpai gtaifcyngf gsaaylaedl
      241 rggnrnvaka viysllvilv velvpltaiv lgapsltelt ksadpigyvv rslsnpavsr
      301 vvsagiflsv fnaiiaivit mgrllyssgr halwsrtcnr afstihprle spwlatiala
      361 vpsaglvfvs sldeltaftv dlllliylvv glaalasrfv rrdvehhyrm plwpvtplva
      421 vagaaytlyt tlatatkptd liiiagllia alvmyvvwar hseafral
//
LOCUS       WP_175959066             315 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175959066
VERSION     WP_175959066.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..315
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34345
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdtlqnmrvf srvvetgsft aaaqslnstt gamsravsel earlrtrlmn rstrrlalts
       61 agesylrrcr qiladvdrae eeascaherp agvlrmhsfa svghhyvlpa ltryhaqfpg
      121 vsielslsqr mpdlfdgtsd mavvtasslp dselvshllg stfsilcasp dyvkrrgvpa
      181 rpqdlaahac ltlctpafpt hewvlegpeg veqihvagpv qtntaeslal airdgiglgm
      241 lplysaidal rdgtlvrvlp ahilqkmnvy alypsrrfid akvrtwveml raqvpgmiar
      301 dvemlnaigr epqaa
//
LOCUS       WP_175959234             288 aa            linear   BCT 11-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Burkholderia
            pyrrocinia].
ACCESSION   WP_175959234
VERSION     WP_175959234.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..288
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=29951
     Region          195..279
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mslsllpcat iwlalfaaaa lvwhrpqhgl slilavlgya galafgklep ialaplalla
       61 aaawgvspar plavriaaha vfaalaials lhlipgfhnp lviaptrftp eavpftmyln
      121 ldkplvglwl lwvlpwvapd ialsralrtg avaavataaa clagalafgm vgwapkwpas
      181 gwlwlvnnll lvtlaeealf rgyvqggltr alrafawgpw aalaigavlf gaahaaggwq
      241 wivlgtaagv gyglawrrgg llasalahag lnivhfglft ypmldaar
//
LOCUS       WP_175959371             286 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia pyrrocinia].
ACCESSION   WP_175959371
VERSION     WP_175959371.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..286
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30743
     Region          29..269
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 mtdtredapd staarvalwr alhveldapp hvladevglr llapapgwqq rgdmdpqftr
       61 pfrasivara rfiedlvaeq aargvsqyvi lgagldsfvq rrpdmasrvt vfevdppapq
      121 awkqrrlvel gfgvpdwlrf vpvdfeakqs wrdalvgagf dagkpavvvs tgvsmyltre
      181 anaaalreva slapgstlam tfllplenad pdvrpglema akgarasgtp fisffmpaqi
      241 qalalgagfa taahvsaael trryfadrtd glrppnnaee llvatv
//
LOCUS       WP_175959391             382 aa            linear   BCT 11-JAN-2025
DEFINITION  metallophosphoesterase [Burkholderia pyrrocinia].
ACCESSION   WP_175959391
VERSION     WP_175959391.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..382
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=41004
     Region          113..381
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mrsffvrfia igvlfhlyvg mriipdafas pvartisalv lasfvvlipv gmfsrrfdeg
       61 waatlvgwag slvmgffssl lvltvlrefv llgvfawrhl ghdgawsgaa adtalgvlaa
      121 avlvtaigfv garrtaavkr vsipvaglpa aldgltivql sdihvgptik rpyierivra
      181 vnaldadlvv vtgdvvdgsv krlrehtapl grmqsrhgsf lvtgnheyya gahewidefr
      241 rigltvllne hvlierdgar avlagvtdft aggfdpahrs dpeqalagap rdvgtkilla
      301 hqprsaeaan ragftvqlsg hthggqflpw ppfvrmqqpv igglsrfgdl wlytsrgtgy
      361 wgppnrfgvp seialirltr gg
//
LOCUS       WP_175959459             262 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia pyrrocinia].
ACCESSION   WP_175959459
VERSION     WP_175959459.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 262)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 262)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..262
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29230
     Region          9..259
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mfatpfrdsl aiqtrviaal fmreiitrfg rhnigflwlf vepmtftlgi aglwyitrst
       61 hghhvpivef altgystvll wrncatrcvg gltpnlsllf hrnvkpidvf larillevag
      121 atcsfyllai vfhvtglsel pqhagrviaa wlmttylstg lgvfvgavse lsemvervwh
      181 tvtyllfpfs gavfmvdwlp paardavlll pwvhgvemlr sgflgegytw hysvaymvtv
      241 ssflflagll vlrlvhrrve ag
//
LOCUS       WP_175959480            1057 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia pyrrocinia].
ACCESSION   WP_175959480
VERSION     WP_175959480.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..1057
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113101
     Region          1..1038
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mdfsrffidr pifavvlsiv ifaiglisip mlpageypev vppsvvvrat ypganpkeia
       61 esvaepleea ingvegimym ksvagsdgsl qvvvtflqgv dpdtaavrvq nrvsqalsrl
      121 pdevrqygvt tqkqsptplm yvslyspdns rdslylrnyl tlhvkdelsr ltgigdvgvy
      181 gsgdyamrlw ldpnrlasrg ltasdviaav reqnvqvsag qlgaepspka ndflvsinvr
      241 grlrtvqefs divlrngddg qvvklsdvar ielgagdytl rsyfndrhsa vvgiflspga
      301 naldvakavy akldelskrf ppgvayrpvw dptvfvresi ravqhtliea vvlvvlvvil
      361 flqtwrasii plvavpvsvv gtfaflhllg ysintltlfg lvlaigivvd daivvvenve
      421 rniaqglspr daahqamrev sgpivaialv lcavfvpmaf msgvtgqfyr qfavtiaist
      481 visainsltl spalaakllr phgapkdalt raldrafgwl fhpfnrffer ssdryhgvva
      541 rtlkrrgvvf avyaallaat allfnavpgg fipvqdklyl fagaklpega slartsavte
      601 qmtkialgte gvemvpafag lnalqgvntp nitnsyvilk pfdqrhrsaa qinadlnarf
      661 aaigggitya lmpppiqglg ngsgyslyle drgglgygal qnalvafqaa vaktpgmsyp
      721 vssyqanipq levkvdrlka kaqgvaltdl fntlqvylgs myvndfnvfg rvyrvmaqad
      781 aghrqtaadi anlrtrnskg emvpigsmvt vgpacgpdpv vryngypaad ligdadpkam
      841 sssqaiaklq qiakevlppg itlewtdlsy qqvtqsnaai vvfplavmlv flvlaslyes
      901 wtlplavili vpvcmcaalf gvwlsggdnn vfvqvglvvl mglacknail ivefarelei
      961 qgkgvieaal eacklrlrpi vmtsvafiag svplligsga gsevraatgv tvfagmlgvt
     1021 lfglfltpvf yvairklagg tpavwseqhg tlegetr
//
LOCUS       WP_175959493             379 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175959493
VERSION     WP_175959493.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..379
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=41485
     Region          15..312
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mtasqparmd lpgqvvlvlq gggalgayql gvfqamdeag irpdwvvgts igainaalia
       61 gnpperryek mlafwqrvte rtrfdvpall pgwdkmlael miigggiagf fqpnpaswlg
      121 pmvclgvdra syyriaplrd tlaslidhdl lnaghprltv savnactgtm ryfdsrdtpl
      181 gidhimssga lppafpairi dgepywdggv ysntpvevvl ddnprrssii fsvqmwnpag
      241 pepesiwqvs erqkdiqyas rtdshiarqq qihrlrhvir elirhvpeae raspavrrla
      301 awgcettmrl iklaaprldg dnqlkdidft pagiaarrqa gydaakraia arpwdlpmdp
      361 tegltvfdpd appvaekta
//
LOCUS       WP_175959508             500 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia pyrrocinia].
ACCESSION   WP_175959508
VERSION     WP_175959508.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..500
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52577
     Region          22..451
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msewsrvtga agdtsagtpa eagggtalka gavgfptala savglimasp viltatsgfg
       61 mggwafavam iiafvmmqaq attfseaaam lptagsvydy lscglgrfwa itgtisayfl
      121 vhvfagtaet ilsgimalvn feslnaafek hnsswlvgvg lvitfaitni vgikvfskle
      181 ivltagmwls lmifgilgla aapavhldgw fggsevgtsv pavlslvgma mfmfvgcefv
      241 tplapemkap grtipramti glvgvaicmf lygaairrqv anvpvspdgl thlldtpgai
      301 pafalqvlgp fgriwfgiaf lfagaatint lmaglprily gmaidgalpr cfaylhprfk
      361 tpvvgivasa vvpifhawli ngnldsilhl vlaatcawgt ayllvtasvv mlrirrpdlp
      421 rpyrsplfpl pqivssvgiv laiwyitppg mnardiyvpf gamlgltaly alfwtlvvqr
      481 rhpfrpvpve evlrnehvas
//
LOCUS       WP_175959529             264 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175959529
VERSION     WP_175959529.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13673959
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..264
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27843
     Region          12..144
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Site            order(28,30,34,68)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:380405"
     Region          179..260
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mhrvthyrrt aegieaisle sdrafprhah defgvgvivs gahrswsgrg qvdalagdai
       61 mvnpgemhdg spidagtgrr wrmlylapal vagiaaeedl ggvelahpav rdarltaavg
      121 rlharivage tqplardeal vmlvagllar hanrtlpaag vapairvare rldaapaapv
      181 slaeladlsg vsrfqllrgf arelgitpha yliqsrarla rallanglpi adaaaeagfa
      241 dqshltrafa rqfgitpgrf tqan
//
LOCUS       WP_175959541             314 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia pyrrocinia].
ACCESSION   WP_175959541
VERSION     WP_175959541.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..314
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33177
     Region          83..286
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mlvdppiaaf ldaleksgek klyegtpeea rasyrtlaag lhppgttisv gsvenivvdg
       61 algelparvy rpdgngpcpt aaffhgggwv igdldthdnv craicresrv vvvsvayrla
      121 pehpfpaavd davaatqwvv dhapdlggna lvavagdsag gnlsavvaha fradgvelag
      181 qlliypatdl pgtrhlswqq natgylldrp liewflhhys ggrqrledpr itpihagtfs
      241 glppavivta qfdplrdvgl ayaealsagr vpvhvepglg lihgffemgq lspaaqdaie
      301 rscrrfgevi raar
//
LOCUS       WP_175959629             555 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia pyrrocinia].
ACCESSION   WP_175959629
VERSION     WP_175959629.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Kane,E.I. and Spratt,D.E.
  TITLE     Structural Insights into Ankyrin Repeat-Containing Proteins and
            Their Influence in Ubiquitylation
  JOURNAL   Int J Mol Sci 22 (2), 609 (2021)
   PUBMED   33435370
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Mosavi,L.K., Cammett,T.J., Desrosiers,D.C. and Peng,Z.Y.
  TITLE     The ankyrin repeat as molecular architecture for protein
            recognition
  JOURNAL   Protein Sci 13 (6), 1435-1448 (2004)
   PUBMED   15152081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19763717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..555
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=57807
     Region          118..418
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          219..249
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          412..466
                     /region_name="Ank_4"
                     /note="Ankyrin repeats (many copies); pfam13637"
                     /db_xref="CDD:372654"
ORIGIN      
        1 mnklppkanp dhlkkqakal lrlyrqgdaq avarfvrslp aaanrthdea ialglrlhda
       61 qsciareygf aswadlgvfv etqalarqqr sllirrwlgl ayggdvtgsf gtarprvaaq
      121 llrdqpdlvs edltiacaag dldavkaala adpgwiarag galnlpplva vthsrlgqmp
      181 efaarlracm rhlldagadp nqrignrfpp aslaapdesg plsalygaag vnrdpvltam
      241 lleagadpnd geslyhslen pactrllleh garvggtnal rraldmrdaa alelllahgg
      301 dpnepagegp tnrwgspllr aiavrcsash vaallaagad pgagtvagvs ayrlamqtgl
      361 sdvaallraa gaeealgaad afvaacarad gddarriqar hpdlpgalpe drlrllpdaa
      421 awgsgdavkv mvelgwpvaa rggdwdasal nhavfrgdad lltfllahga swrethgfgs
      481 dalgtlswas vnepegvghs dweacarvli ahgvpqavhd psnpdrvlid gramqfseav
      541 tdallgidgg qsast
//
LOCUS       WP_175959660             309 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175959660
VERSION     WP_175959660.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34118
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..291
                     /region_name="PBP2_CrgA_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08475"
                     /db_xref="CDD:176164"
     Site            order(103,107,146,161,163,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176164"
     Site            order(104..105,109..110,112..113,116,120,122..128,190,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176164"
ORIGIN      
        1 mtdrldgvtt fvqvvesgsf alaaerldmt rsavgkavar lekrlgarll qrttrsqslt
       61 ddgqayydrc vralaeleaa eadldcgrne argklrlsvp lafghhcvtp ivldlartyp
      121 hlridvsitd rfvdlveegi dlavrigtla dstslavrrl gtqygslgaa psylarygmp
      181 kslddlkhhr tiaysrsgvp qpwdlrapdg stvrvdmqhq lsfddvqaia aagasgfgva
      241 wlpswlldyy vkrgemvvvl drcfvcegdi haiwpktryl prktrcvida laqaippmie
      301 rrdeftamk
//
LOCUS       WP_175959676             285 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia pyrrocinia].
ACCESSION   WP_175959676
VERSION     WP_175959676.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..285
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30397
     Region          11..259
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(26,107,109,111..112,140,191,212,215,228,230,259)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mseplpcfpf rrigdfsvta isdgtltasl dllsnialdd aagimrragi htpssvninc
       61 yvirgngrtv lvdagaggir nwggrlipsl sragidardi dtillthahp dhigglldpg
      121 gqpvfpdaev vihererafw lddesydran erarvnfria rhtfdvyrak lrtieaggvl
      181 pgivavplpg htpghtgyri esrgeclliw gdlvhfapiq varpdvsiaf dhdpsqafat
      241 raatlaeaas dnlliagmhl teagfariar tngetggaya ltgad
//
LOCUS       WP_175959659             512 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175959659
VERSION     WP_175959659.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..512
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52223
     Region          16..426
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,142,
                     145..146,149,273,276..277,280..282,285,313,317,371..372,
                     376,380,396,399..400,403..404,407)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtlsdsrrna valaavclts lmfgleissv pvilptlehv lhgdfngmqw imnaytiact
       61 tvlmaagtla drfgrkrvyv igavlfgats llcglapnvp vlvagrllqg asggamlicq
      121 iavlshqfre grergrafgi wgivfgiglg fgpivggaiv alaswpwvfl vhaplaaval
      181 aliggavqes rdphagtldv agivtlsfav lglafyitqs aelgltsaag lgvlgatvla
      241 lagffvaera sarpmfdfsv friraftgai fgsmgmnfsf wpfmiylpiw fqvalgydsv
      301 taglallayt lptlvappfg erlalrygpg vvipgglfti aagfalmrvg saadhaswlt
      361 mlpgcviagi glgltntsvt ntttgavpsa ragmasgidm sarmislaln iatmgfvlva
      421 givaslkgga agaigdaalr rlaqeiasgr tdglqqiapa laqadpsgaa lhaalvhgfg
      481 wvmvygaagv avlatasava faparrgatv ce
//
LOCUS       WP_175959721             170 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175959721
VERSION     WP_175959721.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10615366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..170
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17640
     Region          20..130
                     /region_name="Glyoxalase_4"
                     /note="Glyoxalase/Bleomycin resistance protein/Dioxygenase
                     superfamily; pfam13669"
                     /db_xref="CDD:463951"
ORIGIN      
        1 mtaaaapret srpftvlgvh hvaiggpdka rltnlwvnll glsvaerfrs daenvdedil
       61 iagsgagaie idlmqpldpa rkpdvtrpal nhiglavsdl daavawlaaq gvrfadggir
      121 rgaggarvaf ihpaasaqfp lggegvliel veavpaarhd ardervrqpa
//
LOCUS       WP_175959750             288 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175959750
VERSION     WP_175959750.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..288
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31777
     Region          11..277
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mfldhlhper wtflwnalst lsiklcagla llvagwwlsk rvgnwlnrll snkervddtl
       61 rpilcdvavw girivaivga lsqlgvetas ivavlgaagl aialalqgtm qniaagimll
      121 llrpfkvgdy idggtgvagt vdevglfmtr ltkpdgicef vpnsalwgss irnytrnptr
      181 rldlevevsv hddidralda lralaeadpd vlqdpapdvm vmrfddstav anmrvwthtd
      241 nfwamrwrla rqvrkalada dcalpirtre lhivhdaerr adsvrvra
//
LOCUS       WP_175959789             315 aa            linear   BCT 11-JAN-2025
DEFINITION  YncE family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175959789
VERSION     WP_175959789.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..315
                     /product="YncE family protein"
                     /calculated_mol_wt=35392
     Region          <12..207
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          <141..293
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mndilllvqk cahtfsfydl dtkaalkhiv lpnfpheftv daneryayvg ifgietawsr
       61 ghegdhriae idlverthtr mldlwpyyrp hgmasdrdgr lyamseahdm llvfdeptrq
      121 pvpnmavpsg gvkthlvtlt rdasraygvh llsntvtqfh prdatvapra vmpgprpegn
      181 alsadertlf vanrgddtlv eidtetmtcg rrvktrsdpn riyrtsapdg rdlllltnsg
      241 ersisvfdar qleeierisl panptalsfh psrrvayvsf qddyvreldl dtwrfvgala
      301 tlrepdasyv lagar
//
LOCUS       WP_175959817             203 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            pyrrocinia].
ACCESSION   WP_175959817
VERSION     WP_175959817.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..203
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22734
     Region          1..157
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mraskrqlvv dkatelfskh gfhpvgvdwi iddsrvarmt lyrhfpskde lirevlvqry
       61 dlivgsidaq lqhvadpver vktifdwyea wfntpafagc lferalaefg tayapisdva
      121 iryrrkmvew iaelladlvs petaqrlaav ymmlldgatv earafndsas agrawqaaka
      181 lleqeirggt ghakhadadt qra
//
LOCUS       WP_175959833             155 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia pyrrocinia].
ACCESSION   WP_175959833
VERSION     WP_175959833.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..155
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16459
     Region          1..144
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mykriliavd gsntsrhafd aalalakahg aelqpfyvve naeiyynvpg ydpsvlrdql
       61 vaqgnelakd ftklmqaagv kgdtklaeat slndvsqlil egakafgadl lvlgthgrrg
      121 frrlvlgsia eqcvrhatlp vllipaaant deqaa
//
LOCUS       WP_175959822             205 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia pyrrocinia].
ACCESSION   WP_175959822
VERSION     WP_175959822.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..205
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22308
     Region          4..200
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mefltlsalp agmlfalvts itpgpnntml lasgvnfgfr rtmphlfgis igvailmlcv
       61 gfglgeafrr lpllytilea asvayllyla wrigtsgevk ahgakprpmt fieaaafqwv
      121 npkawmmvlt aattvrlsad ygmnaawmav vfiligfpci slwaafglgl rrflsnrral
      181 rifnvtmavl lilslyplia hllpq
//
LOCUS       WP_175959838             834 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175959838
VERSION     WP_175959838.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..834
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=89842
     Region          14..796
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 madlaafira pfflqdkrll alsfpyddap svtdsygrhr parlvaerlv aheglgidft
       61 feltllsgea gvtladmlgk llavsmvrpd gslrhftgyc tefslvrndd siaeyravlr
      121 pwshflrtrv nnrlflgqsl qqqigtllad yqglapswew rvrgddpart mnvqggglge
      181 sdwnyivrhl eavgflywwe hdetgvkliv gddstvqcpa vdgrsqeirf qthdgpmaad
      241 aisqwsavrs laagsysata fdfkapraan aqiptlhppg vapqvehhey vghygfvket
      301 rsgdalarvr meeieaaasr fdaagnhhgi lpgrwfqlsd hfstssgspe dhrylilear
      361 heaannylqa dgkpeyrnrf vaghrhtpwr pgrgfnsepv rvlapqtatv agakgagsvd
      421 vdeygrvcvv yhwdraaqts arirvaagwa ggekgmiahp rvgsevlvmc ldgnpdrpvv
      481 sgttynaerm ppwvlpdqqv ltglrsrels gdggnaaggr snhvllddtp qqlqlklrsd
      541 idaseltlgh nvridntqgr tdqrargfel rtdahgavra akgllvtsea rydarahatd
      601 igetvarlea ahdlheslss sahdvkaqes gdqdavhqal rtqndglkgs ggnpqqgefp
      661 efsqpflala spagilatta gsthvasdqh valtsgahts igagksmlvs akeavrvaaf
      721 ekgirlvaaa adidiqalkd sinvlakldv kvdanritit akeevlingg tsytrwsgsg
      781 ivhgtkgewt ahaashtfig pdslpvpara fpgtacapcm vnaasmaspf aaka
//
LOCUS       WP_175959809             239 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175959809
VERSION     WP_175959809.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..239
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=26254
     Region          24..218
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 msaqpspien hllaalpaea lahispqlvl vdmplgkvly esggalshvy fpttsiisll
       61 yvmedgssae iaivgndgli gialfmgget tpsraivqsa ghayrldasi lkdefrrggs
      121 mqrlllrytq alitqmaqta vcnrhhsidq qlcrwlllsl drlpsselkm tqelianmlg
      181 vrrsgvteaa lklqdaglir ynyghievld rsglekrvce cygvvrrefd rllpdlkrl
//
LOCUS       WP_175959871             184 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Burkholderia pyrrocinia].
ACCESSION   WP_175959871
VERSION     WP_175959871.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..184
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20157
     Region          4..165
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 msyriavvvg slrrassnra lahalislap adfsfefvef gelplysqdy dadfpevakr
       61 fkqsieaada llfvtpeynr sipgvlknal dwgsrpwgsn swsgkpgavl gtspgatgta
      121 laqqhlrnvl ayldvktlgq pemfikhdpa rideqgqivs edtrkflqgf vdryagwvrl
      181 lkaa
//
LOCUS       WP_175959901             213 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175959901
VERSION     WP_175959901.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..213
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23886
     Region          7..211
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 meakldstad avaaslrdmi vngeleager lverdladrf gisripmrea iqrleregll
       61 difrnrgavv rmlsasdvqe iydlralleg daiyrsvkrl ddetlarael vhrllgdatv
      121 prrqgelnre fhallysccg narqlktige lrsqveryer lqatlladtp sfqvehddil
      181 kacrernara arsmtvahle sarsivmqlv egg
//
LOCUS       WP_175959902             158 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175959902
VERSION     WP_175959902.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..158
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=17326
     Region          5..153
                     /region_name="OsmC"
                     /note="Organic hydroperoxide reductase OsmC/OhrA [Defense
                     mechanisms]; COG1764"
                     /db_xref="CDD:441370"
ORIGIN      
        1 masgehkyrv avqwtgnrgt gtsgyreygr dhviragskp dipgssdvaf rgdasrwnpe
       61 dlllasasac hklwylhlcg eagirvlayv dnaegtmlds pehgrfteiv lrphvtiqag
      121 ddreraerlh hdahakcyia nsvnfpirce paiefaaa
//
LOCUS       WP_175959903             316 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175959903
VERSION     WP_175959903.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..316
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33989
     Region          16..73
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          104..304
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(119..120,122..123,126,130,132..138,233..238,
                     244..245,247..248)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mtdaspwgnr srlktrqlll vvaladegsi hraaaalnmt qpaaskllre leesigavlf
       61 erlprgmrpt lygdalirha raalgsldqa reelaalkag hlghvavgai tspglrlvpp
      121 avaavkgthe glhvsveidt snvllehlaq dkidivlgrl saehdklrlr yepligetva
      181 avvrpghpll aqaplsladv qraawvvppa gsvlrhrfel vfqraslapp anlvetsall
      241 fitqlleqsd miavlaedva ryyarhgivt vlplemdcrm ddfgiitrtd rlhspavtvm
      301 adairaaare vygval
//
LOCUS       WP_175959906             309 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175959906
VERSION     WP_175959906.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..309
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33711
     Region          8..301
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mtssstpryr gifpvvpttf sdtgeldlas qkravdfmid agsdglcila nfseqfaiad
       61 derdvltrti lehvagrvpv ivttshystq vcaarslraq qlgaamvmam ppyhgatfrv
      121 peaqifdfya rvsdaieipi miqdapasgt alaapflarm areieqvayf kietpgaank
      181 lrelirlggd avegpwdgee aitlladlha gatgamtgga ypdgirpile awregrhdda
      241 yaryqawlpl inhenrqsgi ltakalmreg gviacerprh pmpelhpdtr aellaiarrl
      301 dplvlrwah
//
LOCUS       WP_175959924             666 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 28 protein [Burkholderia pyrrocinia].
ACCESSION   WP_175959924
VERSION     WP_175959924.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 666)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 666)
  AUTHORS   Abbott,D.W. and Boraston,A.B.
  TITLE     The structural basis for exopolygalacturonase activity in a family
            28 glycoside hydrolase
  JOURNAL   J Mol Biol 368 (5), 1215-1222 (2007)
   PUBMED   17397864
REFERENCE   5  (residues 1 to 666)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 666)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..666
                     /product="glycoside hydrolase family 28 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=69215
     Region          86..622
                     /region_name="Pgu1"
                     /note="Polygalacturonase [Carbohydrate transport and
                     metabolism]; COG5434"
                     /db_xref="CDD:444185"
ORIGIN      
        1 maansrrsss sarspssrpv srrafigwsg alaggavlgg plaatrafag ghmptvsavd
       61 lvwgehgaaa riaaslahvs rlalrgrdfd vthygarpca tvaqtspytn vakspvspgs
      121 elttapgafd srpaflaaid acrregggrv vvpsgnwyca gpivlqsnvt fhlsanctiy
      181 fspnpadyak dgpvdcgang rlyysrwqan dclnygapvy arnatnialt gegptsvlng
      241 qamtpfsgsg agsvcwwtyk gssgaygaga svpsqayanp nnvdlrivap aipdalyall
      301 tspvtpwrqd qnylpalsea gvpvekrifg lghylrpcmv efigctnvlm anyqtqntpf
      361 wqhhptasrn vvirgvttns igpnndgfdp dacadvlced ctfntgddci aiksgkdrdt
      421 eygpakrhli rnctmnsghg gitlgsemgg gveqiyatnl smlnanwqin plniairvkt
      481 nmnrggyvkd fhvkgvtlpn gvtlkgggyg sallagspvn asvplgvvtp sagnpsaaqg
      541 givtfdcdyq pandavrtra pvvqnvtisd vkasnvtlng vtascfqaiv aqgpvafdyn
      601 gtppapavqp isgvtisncd fgtpvasgmp tvtspgpiya fnvsaltltd vtiagqivnt
      661 titdkr
//
LOCUS       WP_175959961             509 aa            linear   BCT 11-JAN-2025
DEFINITION  peptide MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175959961
VERSION     WP_175959961.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..509
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55553
     Region          7..465
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mmhspvsqtr sfttvfliem werfgyygma allvlfmvdr lgftdshanl twgaftalvy
       61 aapsiggwig dkvlgarrtm iigaavlcag ylmlavpndr ltymyaslgv ivvgnglfka
      121 naanlvrriy egddaridsa ftiyymavni gstvsmlatp wikdhwgwha afavccggml
      181 lailnfmlmh rtlahvgsqp deqpirwkrl gavaaggaal alitlyvlqh kqlavasvwt
      241 aafailaila ifaymiakse rseragliaa lvligqvilf fifyvqmsts ltlfalrnvd
      301 prfilfgttl ftwsaaqfqa lnpiwimlls pvlvwvynav akggrdlpva akyalgfgav
      361 aagylvftis gryavdgrvs swfmvwgygl yslgellvsg lglamiaryv parmsgfmmg
      421 ayfvatgvsq ylgsvvanfa qmpshelpat eslplylslf eklgwlaaig mllallllpl
      481 mnrlsrqhqr caeerreeal qaqavtaaq
//
LOCUS       WP_175959983             384 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175959983
VERSION     WP_175959983.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..384
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42224
     Region          1..384
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnfelelehr mikdlvarfv ndelipleaa vmareadgqr falladehar ldersrqlgl
       61 wgldapldag gsdlsavamv gvneaigttv tpyvlppdsp nlrmlcdsad daqraryldp
      121 yargvtrsam aisepgagsd pgalsttaer dgdgwvlngr kiwishasea dwtivmaltd
      181 rskgkrggis afiverdtpg fiierripmi gglstyeivl encrlpatql lgregegfvp
      241 mqgrlsnrrl emaawcigra eravallcey akqrttfgvp laerqavqww vadaltriha
      301 crlmtyeaaa rvdagqdart qismvkvfat emawtvidha mqtlgamgmt kelplqqmas
      361 earlmrifeg psevhrwvva rsvl
//
LOCUS       WP_175959985             350 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia pyrrocinia].
ACCESSION   WP_175959985
VERSION     WP_175959985.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..350
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=37002
     Region          4..350
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mqrkaflvga cvlcaspaha ssvtlygivd syvefdrigs lssvrqsggg sstsrigltg
       61 vedlgggtst kfvlesgfsp adgsfqggtl fyrqayvslq ntrygdlrlg rqytpsfyvv
      121 yegdpfglne rmsplallat stdtitsntt ppiprfnqaa aylspdwngl rvmatygfpt
      181 pnalsmqagr nygaglqyri gglylgagfq gdvsagnlsp vvypsttrhy vfaanyafar
      241 vklyaaflhg astapnlpaf stasvgasin vgaldrvlvs vvrrdvkgsa ndatalgvgy
      301 dhplskrtsl yarylymkng gdarntvvag rqpqpggteq vlalgivhrf
//
LOCUS       WP_175959986             266 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175959986
VERSION     WP_175959986.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..266
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28588
     Region          18..260
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 msaprtfssp tgddapsilr ndddgiawlt ihrphvanal saeairrlcd elvtlddnpa
       61 iraivirgag erafsagidl gdpemrgmrp mrglarnvhe lilelrkpti aaingfavgg
      121 gfeialacdl riaaehayfa lpearvgmga nfasvllprm lpravamell ftgrrfdade
      181 aqrvgllnrv vpgaalddtv relaeaiaan apltirrike tatrsqglpv aaalrldvgp
      241 dvyasedrie garaflekrk pvfkgr
//
LOCUS       WP_175960029             194 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            pyrrocinia].
ACCESSION   WP_175960029
VERSION     WP_175960029.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..194
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20119
     Region          5..157
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mgvsrqqaae nrsaivaaae rlfrargvda vgltelmkea gftqggfynh fkskdalvae
       61 vmgkamqdre dspnagslaa qvasylsaah rdnveagcpl sgfagdaprl tdaaracyah
      121 glaayldrle rmvategatp eqtrrdalav fsqmvgalvl sraiagtdpv ladeileagr
      181 dtlidgrggp aapa
//
LOCUS       WP_175959989             254 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175959989
VERSION     WP_175959989.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..254
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27290
     Region          6..254
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 msgnvvksaa rvfevlelfs tlqrplsvre iatrcgypgs saaalltsmk algylaydda
       61 thayaptarl vnlgealvds aagsrrhwha vakrlaarth eavviavqsd lyvqyidaia
      121 gshripiqfy apigtrreic msslgwalls iqpdstirrl varsirrlgk sgrtidedvv
      181 ldkveqtrrh gysysahtvt qgaamismvi adgwnglpla mgvagpveri dahrdaivla
      241 mrealaerag eaag
//
LOCUS       WP_175960047             268 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Burkholderia pyrrocinia].
ACCESSION   WP_175960047
VERSION     WP_175960047.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 268)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..268
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28557
     Region          22..268
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mrrsiltglg alaaalafat pgahadpqtl kigtmsgpda qiwtevtkva areglaikvi
       61 efndyvqpna aldsgdldan gfqhqpflds qikqrgyriv nvgltytapm gfyskkiksl
      121 kdlpvgakvg iqndpsngnr allllqkygv iklkpgagtn gvnatpldva enpkkirive
      181 ldaaqlpral pdvdaasint dyavkagltp vkdaiaiedl rgpyanliav raqdkdkpwv
      241 kklvaayesd dvrkfidqkf ggaivpaf
//
LOCUS       WP_175960049             315 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175960049
VERSION     WP_175960049.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..315
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33698
     Region          2..315
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhtvavlalp dvvpfdlgva cdtfarvrsp gvehayrvrv cseharvagd lfelrpafrl
       61 daladadtiv vpgtsvplap tsrraiaalc aaaargcria sicsgafvla qaglldglra
      121 tthwlaagel arrypnvtvd pnvlfidngq iltsagaaag ldlclhmiqa dygaavavda
      181 aryavaprvr eggqaqfiap ewpagtdglq slmdwlqanl hkpltldama rkastsvrtl
      241 trrfqeqtgt sprqwlqtar vrhaqqllev telsiehvat eagfgsvtaf rerfarivgt
      301 spqryrhafr arsga
//
LOCUS       WP_175960054             221 aa            linear   BCT 11-JAN-2025
DEFINITION  O-methyltransferase [Burkholderia pyrrocinia].
ACCESSION   WP_175960054
VERSION     WP_175960054.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..221
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23853
     Region          65..219
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mttlildpla sllerlfdea dasspatspd fadlshdeha rlmrsktdya dfyarlkdyp
       61 lavsretgtl lymlarsrga raivefgtsf gistlhlaaa lrdngggrli tsefepskvv
      121 raranltaae ladlveireg dalrtlaadl pdtvdlllld gakalypeil alvesrlgag
      181 afvvadnaey spdylayvra pengylsvpf ggdvelsmri r
//
LOCUS       WP_175960068             160 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175960068
VERSION     WP_175960068.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..160
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17810
     Region          24..152
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mtrlsqtvht rasardallr iaqtlervpy wllaiplria vatvfwnsam tklanwdaal
       61 qlfseeyrlp vlppeiaaym avsielsmpv llvlglavrp aalvllgmts vieifvypqa
      121 wpihiqwaam livllcrgag llsidhvvrt rwlqrtsaek
//
LOCUS       WP_175960075             360 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia pyrrocinia].
ACCESSION   WP_175960075
VERSION     WP_175960075.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..360
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38471
     Region          5..341
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(25,27,58,100,228,295,315,317..319)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(25,27,58,100,102,109,176,179,181,228,235,295,315,
                     317..318)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(27,102,176,179,181,318)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            181
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 msektlfepy alggltlanr ivmapltrnr agaglvpseh aatyyaqras agliiteatq
       61 vsaqaqgyqd tpglytpeqi agwrkvtdav hakggrifvq lwhvgrvsht dlqpggtapv
      121 apsairaetk tfvnngfadv sepralelae lpgivndfrq aaanaiaagf dgveihgang
      181 ylleqfikdr anhrtddygg sienrarlll evvaavvkei gaertgvris pvspangisc
      241 sdpqaqydyi aeqlsaqgvv ylhvvegatg gprdiaafdy dalrrrfkqt ylanngydle
      301 fattqlnegr adlfafgrpf isnpdlverl qhgapltqln patlygggav gyidyptisg
//
LOCUS       WP_175960078             193 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175960078
VERSION     WP_175960078.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..193
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20588
     Region          6..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkrsaarske atherivdag arvirrsgyd gvaigdimkh aglthggfyg hfasreamlv
       61 eladragada iatflrctaa apaehslral lraylskehv knpevgcpia algtemprqa
      121 pavrraitrr ikemievvsr qsadwgepda hkralattat migavilara vdeeplsesm
      181 leaalehlac gad
//
LOCUS       WP_175960103             192 aa            linear   BCT 11-JAN-2025
DEFINITION  YbhB/YbcL family Raf kinase inhibitor-like protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175960103
VERSION     WP_175960103.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..192
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=20180
     Region          50..185
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mrsriflsai lctstalavi patasaepfa irvddlshgh ftneqvyggf gchgqnvspr
       61 iswthvprgt kslvvtifdp daptgglgwt hwevvnipps essiekgasg nptrmpagav
      121 etltdfgesr yggpcppqga shryvvtasa ldvakidvap aaspavvayq mhgkviaqak
      181 yvaryhraat nd
//
LOCUS       WP_175960106             322 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175960106
VERSION     WP_175960106.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..322
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35576
     Region          7..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..291
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(110..111,113..114,117,121,123..129,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrelnqrrlr yfhevlthgs irgaadsint apsvitrqir lleeeigvel ferqargvrp
       61 teaaahlley wrgcrsqqel feerlqalrr lqsgqvrivt segyvdvlmd evltdfcmry
      121 pkldvivdvl pvnnvlqeva esrahiglay nppahpeiey latssqpvva lvhaghplav
      181 rggavcahel geyplalmpp afglgqvaqm laytenlpir ptlttnslav lrhfvkrhdg
      241 itligafaay relesgelva lpiahplfds akarllvkvg rplgvaadtl lncllhdmtm
      301 fagaatgrrp tgkrprvakr tr
//
LOCUS       WP_175960129             130 aa            linear   BCT 11-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175960129
VERSION     WP_175960129.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10577308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..130
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=13882
     Region          15..>74
                     /region_name="SnoaL_2"
                     /note="SnoaL-like domain; pfam12680"
                     /db_xref="CDD:432716"
ORIGIN      
        1 mntaqsaqsa hadlidryfv awnepdvarr ralidatyas datyrdplma gdghagidtm
       61 iaavqarfpa yrfrrttdvd afgqhlrfsw alvspdgaai vkgsdfgtvd asgrlasvtg
      121 fidempvaas
//
LOCUS       WP_175960165             218 aa            linear   BCT 11-JAN-2025
DEFINITION  SOS response-associated peptidase [Burkholderia pyrrocinia].
ACCESSION   WP_175960165
VERSION     WP_175960165.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..218
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=24949
     Region          33..217
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mctnykapge dpgiselkig igdlyrrdpw dldvypdyaa piayasgdgi evvksvfgfw
       61 pkflqpdrld dagkkkkkfd tvnarsetvg esrlyarawr egqrclipvq wiyepcyetg
      121 knvwqrigla gwqpycvagi wkryqdqdgr sligmsmltv nadghplmsr mhkpndekrs
      181 vvilrpedyd ewlhtknvea artmlqiypa edmntqpk
//
LOCUS       WP_175960197             670 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Escherichia coli].
ACCESSION   WP_175960197
VERSION     WP_175960197.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..670
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75226
     Region          21..663
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mnasswslrn lpwfratlaq wryalrntia mclaltvayy lnldepywam tsaavvsfpt
       61 vggviskslg riagsllgai aalllaghtl nepwffllsm sawlgfctwa cahftnnvvy
      121 afqlagytaa iiafpmvnit easqlwdiaq arvcevivgi lcggmmmmil psssdatall
      181 talknmharl lehasllwrp ettdairaah egvigqiltm nllriqafws hyrfrqqnar
      241 lnallhqqlr mtsvisslrr mllnwpsppd atreileqll talassqtdv ytvariispl
      301 rptnvadyrh vafwqrlryf crlylqssqe lhrlqsgvdd harlprtsgl arhtdnaeam
      361 wsglrtfctl mmigawsias qwdaganalt laaiscvlys avaapfksls llmrtlvlls
      421 lfsfvvkfgl mvqisdlwqf llflfpllat mqllklqmsk faalwgqliv fmgsfiavtn
      481 ppvydfadfl ndnlakivgv alawlafail rpgsdarksr rhiralrrdf vdqlsrhptl
      541 sesefeslty hhvsqlsnsq dalarrwllr wgvvllncsh vvwqlrdwes rsdplsrvrd
      601 ncisllrgvm sergvqqksl aatleelqri cdslarhhqp aarelaaivw rlycslsqle
      661 qappqgtlas
//
LOCUS       WP_175960225             427 aa            linear   BCT 11-JAN-2025
DEFINITION  YeaH/YhbH family protein [Escherichia coli].
ACCESSION   WP_175960225
VERSION     WP_175960225.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11148708
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..427
                     /product="YeaH/YhbH family protein"
                     /calculated_mol_wt=49378
     Region          13..421
                     /region_name="DUF444"
                     /note="Protein of unknown function (DUF444); pfam04285"
                     /db_xref="CDD:427839"
ORIGIN      
        1 mtwfidrrln gknksmvnrq rflrrykaqi kqsiseaink rsvtdvdsge svsiptedis
       61 epmfhqgrgg lrhrvhpgnd hfvqndrier pqgggggsgs dqgqasqdge gqdefvfqis
      121 kdeyldllfe dlalpnlkqn qqrqlteykt hragytangv panisvvrsl qnslarrtam
      181 tagkrrelha leenlaiisn sepaqlleee rlrkeiaelr akiervpfid tfdlryknye
      241 krpdpssqav mfclmdvsgs mdqstkdmak rfyillylfl srtyknvevv yirhhtqake
      301 vdeheffysq etggtivssa lklmdevvke rynpaqwniy aaqasdgdnw addsplchei
      361 lakkilpvvr yysyieitrr ahqtlwreye hlqstfdnfa mqhirdqddi ypvfrelfhk
      421 qnatakd
//
LOCUS       WP_175960268             251 aa            linear   BCT 11-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Escherichia
            coli].
ACCESSION   WP_175960268
VERSION     WP_175960268.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..251
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27913
     Region          3..251
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mylvderrkl iledlmsagk vyvsdlarky evtyetirkd lthleqkgll ikshggatlk
       61 qraiehpfqv rekennsykk aiarkaldfi ppnssmiigt gsttfelanl lcmksgfkif
      121 tdslpvasvl iesdnqvflf ggelrrksss vfggwavsmi ndihvdlcfi gtdgfsnmtg
      181 pstpsssdaf ldrtiishsd kkyilgdytk fersslfkic dwseitalit ndhadkegia
      241 evakytsvit c
//
LOCUS       WP_175960284             835 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175960284
VERSION     WP_175960284.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 835)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 835)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..835
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=90266
     Region          16..826
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 menftkerdv wtaaqigmpc lallglmlpa hghavefnes flrkgegpve lsyfekgssv
       61 ppgsydvdvy lnhtlvkrqd vafradaegt vkpavtlgll raagvnvarl ekdgriaaga
      121 ddativdlra vadgasvefe sntlslnisf pqlyvsrtsr gyvdqslwdd gvpalysdyq
      181 vsysrndshg hnneyyfvgl rngfnaggwr frnestltgt tgagsrftsn rsyverdirr
      241 lrskvaagel ytsgdifdsv rfvgaqigtd lgmlpdsevg fapvvrgiae snavvevrqn
      301 gyviystpvp pgafeitdiy psgsngdlei riteadgrvr rftqpysylp vmvrrgslry
      361 afaagqyrvq gqsspkftqg tlvygvsdnf tgyggiiaad nyvaaalgig vntriggmsl
      421 dvttsrsrts agtrqgqsvr flysktlypt nttftmvgyr ystdgyrtms qhvedtdrsy
      481 gprvarqksr ldvnvnqplg sgsmfagvgd ttywngegrs rrlqvgysns yknvsyslsa
      541 shiqesgpfa rpdtqfnvsv siplgkasst hrlyanavss trgdfnvqtg vsgylndsnt
      601 vnygvqagys rdgggsggvs agwdtpnakl tgnftqdrsg rhfdagasgs vvvhgggvtl
      661 gqplgetfav vqvpkvrdvt fggaptvrtd rrgyaivpyl qpyrqnwlni dpssvgthte
      721 itdnakmvvp trgaivktrf daesgrrvqf elsqdaggkv pfgaqaydak gkllgmvdnq
      781 srllvfgied qgsidvrwgd dsckvtyqlp tlnkelayer raamcrgagt vvgar
//
LOCUS       WP_175960292             233 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175960292
VERSION     WP_175960292.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..233
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25376
     Region          15..169
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mnaphrvtep nilyfgtpvv lvstlnpdgt anlapissaf wlgwrgvigi aassqttrnl
       61 mrtgecvlnl pssaqahavd riarttgthp vpeskrargy vyepdkfgta gltetpsqtv
      121 sppralecpi hleavvaavh gladetpdlr gkitvfevri qrvhvhpdll meghqdridp
      181 dkwsplimsf qkfyglgprq vhasrlaeip erayrspdie rsreagvpad agr
//
LOCUS       WP_175960332             463 aa            linear   BCT 11-JAN-2025
DEFINITION  alkaline phosphatase [Burkholderia pyrrocinia].
ACCESSION   WP_175960332
VERSION     WP_175960332.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Vimalraj,S.
  TITLE     Alkaline phosphatase: Structure, expression and its function in
            bone mineralization
  JOURNAL   Gene 754, 144855 (2020)
   PUBMED   32522695
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..463
                     /product="alkaline phosphatase"
                     /EC_number="3.1.3.1"
                     /GO_function="GO:0004035 - alkaline phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0106219 - zinc ion sensor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48176
     Region          1..463
                     /region_name="PhoA"
                     /note="Alkaline phosphatase [Inorganic ion transport and
                     metabolism, General function prediction only]; COG1785"
                     /db_xref="CDD:441391"
ORIGIN      
        1 mstikciaaa lavvgfacga aqaagqaknv ifflgdgmgp ttvtasriyk vgesgqltme
       61 klartarvkt fsndaqttds apsmaaymtg vkmnnevlsm ssdtravapg sdvngnktvn
      121 hcapgngqpv atllelakar gkavgaittt elthatpaat yshichrdaq ydiaaqaapg
      181 gagynaalgd gvdvlmgggr nhwtpfdpva nkrgradgrn lldemkakgy tvvatkdqla
      241 qagngklvgl fsstshleye ldrvagkgeg ptqpsladmt skaidvlskn sngyflmveg
      301 gridhalhgt nakraledtv afdeairval skvdlsntli vvtadhdhtm tingyskrgn
      361 pildisrnyr dgqpskdadg ntyttlvfgn ganrpnvras vdsatamnea ylqevgvrmg
      421 sagsethggg dvmlfadgad akafkgtidn tkvfglvrsa fgf
//
LOCUS       WP_175960352             544 aa            linear   BCT 11-JAN-2025
DEFINITION  GspE/PulE family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175960352
VERSION     WP_175960352.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..544
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=58611
     Region          13..539
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mntqhmiqrw ktesgasgag faqyaddlmr adatrladva aclgiepida dtlraaptrf
       61 dllplhdals lralpiefdg gsrivvadpf artvrdella rfgakpvgva msvpgeverv
      121 lgdiesnerl mddvkidapg etlaqvtesi slasiakdes piirlvnttl ydalqsrasd
      181 ihlesaadgl airyridgvl qsirhipgve aatqtmsrlk vlaaldiaek rvpqdgrfkv
      241 vmqgreidfr vsiipgtyge navmrvldks qrgdsvsldv lgfdaptarr vralahrpyg
      301 lmlvtgptgs gksttlyavl sevntgddki itiedpveye lkgvlqipvn erkgltfarg
      361 lrsilrhdpd tvmvgeirde etasiavqsa ltghrvlstv handgfsvid rfiymgveps
      421 tflealngvv sqrlvrrict scggaatdga dlagasldtl rrevvpgggc dtcrgtgyhg
      481 riglaevltl daplkaalle rsvekraral enstdyqsmr daglaavrar mttfqevqra
      541 iale
//
LOCUS       WP_175960377             282 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia
            pyrrocinia].
ACCESSION   WP_175960377
VERSION     WP_175960377.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..282
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31061
     Region          112..271
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mlpnvnpfhr dndrfnvsfk algelietvg tphfvprltq llndvvpldv vhversrvdg
       61 tmptgyrcew igssgigtat sdisdvmtly yerfldsdpl faglrgktgt mlvvrdiaai
      121 ppgefrqrlf ddvhighecv largtrysqh sialergrdr ppftlaemnr frgisdvlfp
      181 llelhastta vrrvahpape vhplaqfdar iaadgvklsk reyetckhli sgktvpetag
      241 ilgvrvasae syakrafakl gvrtkrelaa wgsattafps ar
//
LOCUS       WP_175960391            1068 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia pyrrocinia].
ACCESSION   WP_175960391
VERSION     WP_175960391.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1068)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1068
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..1068
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=114915
     Region          1..1045
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 miariirwsv rnrflvllat vliaawgvhs lrqtpldalp dlsdtqvivk asypgkapqv
       61 vedqvtyplt ttllgvpgak tvrayssfgd afvyvlfddr tdpywarsrv leylsqvqsr
      121 lpagaavslg pdatgvgwvy eyalvdrtgr hdlgqlraln dwflkfelka vpdvsevasi
      181 ggmvrqyqvv ldpdklrayg itqaavadal rqanqesggs vvelaeseym vrssgylrtl
      241 ddfrrvvlrt ddagtpvllg dvariqvgpa mrrgiaelng qgevtggviv mrsgknaltt
      301 idavkaklad lkrslppgve ivttydrsql ieravgnlkd klieefvivg ivcavflfhl
      361 rsafvailsl plgvlaafiv mryqgvnanl mslggiaiai gamidaaivm ienahkhlea
      421 ydhahpgepi taarrwelva asavevgpal ffslliitls fvpvfslegq egklfaplaf
      481 tktytiaaaa glsvtlvpvl mgylvrgrip hehvnpinrv lirlyrplle atlrrpwfai
      541 gvaivalvlt avplsrlgge fmppldegdl lymptalpgi sadkasellq qtdrliktvp
      601 evdivfgksg radtatdpap lemfettirf kprsawrpgm tpeklvdeld rtvkvpglsn
      661 vwvppirnrl dmlstgiktp vgvkisgpdl kgidaiatqv eaavkhvpgv tsalaerlng
      721 gryidvdidr laaaryglsv adiqsvvssa vggddvgevi agrerfpini rypreirdsl
      781 enlrqlpvvt argaqirlgd variaiadgp pmirsenarl sgyvyvdlrg tdlstavram
      841 qqavaqqval ppgysiawsg qfeyleraaa tlrtvvpvtl vvifvllflt fgsaadalll
      901 mstvpfalvg gfwlvwglgh avsvatsvgf ialagvaaef gvvmllylkg altrrldage
      961 pvtdalllda iregavlrvr pkamtvavvl aglvpimvgh gagsevmqri aapmvggmvt
     1021 apllsmfvip aawlllqrrr vrsasdarhs davphgmnvp stqtgesr
//
LOCUS       WP_175960419             494 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175960419
VERSION     WP_175960419.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..494
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53281
     Region          72..450
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mknlsispri vaaavalafl agcttfskdg gfgavsstas erigkdavvv rtdadreavd
       61 krtrellakp lsmddavqva llnnrglqas yaelglsead lvqagrlpnp rfsfsrtrag
      121 dgelslgrtf sanvfalltm platnlerrr feqtkletad amlkvaadar rayveavaae
      181 qaanyaqqvr daasaaaela qrmrqagnfs rldyareqaf hadavaqhak arqqavaare
      241 kltramglwg ertqyalpdr lpdlpkarpd lpdlerfams nrldiqaakl qtqgvasslg
      301 lnkatrfvna vdlgyvnnye tgkghehgye isveiplfdw ggakvaraea vymqsanrla
      361 ktaidarsev resyaayvts ydvakhyrde vvplrktisd elllryngml asvfelltda
      421 reqvgavngy idslkdywla etdlqmavgg rlptsgpapr aavsaepepg tdaapqpass
      481 paaqsapath pegh
//
LOCUS       WP_175960444             922 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175960444
VERSION     WP_175960444.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 922)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 922)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..922
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=98846
     Region          18..834
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msiaatlrnf asglvdwnkr pvalhfgqaq ravghllalh hadireglms gidgyltcvs
       61 trdhlsptlf lglpvsvrlt tdrgdvrtid aivrdvhigq sdgeltvyql hvcdalslmd
      121 yrinsrvfrs lsvieilatl mnewrqrsaa larafdfdls glgaerypar eltrqvnesd
      181 arfvrrllrr egitvfakag piggarsite erpihtlvfc ddplrlaesp agavrlhprd
      241 agtelrdtvt lfaryrslsp gkagrpswdy kkarmdvsai assidqgdag ndlarlltdv
      301 aidiphvgds wndhdrithd rilahqfeae rydgigsvrd mpvghwftlt gdpeldmqla
      361 eqrqfvvtsv rhdilnnlpk dltsrvnalf aasrnltrtt ppapadapeq tdtryensft
      421 cvrrgvplkp sydpkidlpp ahlltgtivg tqgeevfcda agrvrvrihg fdpadhahaq
      481 gagtngsagd sapirvgasl agkyfgalfl prvgmevllg clsgdpdrlv iigvlsngan
      541 ppatfsdtga lpgnrylsgi ktkeikgdry nqlrlddtps qisaqlaseh ahtqlnlgyl
      601 tqprkdghgs drgegaelrt daaaalraaq gillstyart ratggqldrd elvhlldqcv
      661 elfkslgdya gqhggqsadt agqdkiadaf rhwtpgsaes gaadhasall afgaqsgalh
      721 vtpkthvvya genidqiarq hvqltsgeri nlhgghgiam fahgdgvsai anqgkvtiqs
      781 qnddtrvdsa knihltaagg tlagmandqv vlvtsggayl kldggnielg cpgtftvksa
      841 ghawdgpasm dtdmpkfdka plgrvpklvr atdgdavagf dgqiqkasga lsnlttdaag
      901 elpavhadqf eklavqfikk nv
//
LOCUS       WP_175960410             402 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175960410
VERSION     WP_175960410.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..402
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42210
     Region          17..390
                     /region_name="MFS_MJ1317_like"
                     /note="MJ1317 and similar transporters of the Major
                     Facilitator Superfamily; cd17370"
                     /db_xref="CDD:340928"
     Site            order(27..28,31..32,35,68,119..120,122..124,127,147,
                     150..151,154,227,230..231,234..236,239,266,270,319..320,
                     324,328,344,347..348,351..352,355)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340928"
ORIGIN      
        1 mqtesstril rqiprsvwvl gcvsllmdvs seiihsllpm flmaglgasa ttigviegia
       61 eatapvvkvf sgtlsdylrn rkwlavagyg lgalskplfa iaptigvvvt arivdrigkg
      121 irgaprdalv advtpvhlrg aayglrqsld tvgaflgpll avaimlmwrd dfrlafwlav
      181 ipgmlavall afgieepara pgdkrvnpir rdvvkqlgar ywwvvavgav falarfseaf
      241 lvlramgsgv pvalvplvmv amnvvyalsa ypfgkladtt shtklmvagl vmliaadlvl
      301 ahgtrwgtvl vgvalwglhm gmtqgllatm vahaapselr gtafgvfnll sgvatlvssv
      361 vagilwdrag aaatfyagav fsaatiallv rlrgsfdaaq ar
//
LOCUS       WP_175960647             299 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia
            pyrrocinia].
ACCESSION   WP_175960647
VERSION     WP_175960647.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..299
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33073
     Region          9..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(32,57)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(39..40,51,54,58..59)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          105..270
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 madapdnllg aylrdrrekl dpaalglpva rrrtpglrre evaqrahvsa awytwleqgr
       61 ggapsvdvld rlanalllnd aerehlflig vghppevryh atdsvtprlq hvldsleasp
      121 aivrsatwdv vawndaaaaa ltdyatlppe rrnilrlifv dqrvrdaqsn wqqvarfavg
      181 afradiargg atqtvqafvd emrttsaefd alwrdhdira heegtkeirh pavgrialey
      241 safavngrpd ltlviftpet atdrarirtl vaarekagmk rqtpgtspnr reappdaht
//
LOCUS       WP_175960667             264 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia pyrrocinia].
ACCESSION   WP_175960667
VERSION     WP_175960667.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..264
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28334
     Region          1..253
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mrkngpfala fhtlvmlfvl aplaivvlva ftpdetltlp thglslrwfr aildypdfvt
       61 affnslklaf asatlslaig lpaglaigra afpgraflng lllsplvipg lvlgiallrf
      121 faligatgsf awlvlahmiv itpfvmrlvl asvagldrsv eqaacslgad pwttlrritl
      181 pmivpgitgg wllsfinsfd eltmsifvts pqtvtlpvrm ymyatesidp mmasvsalvi
      241 fitagamlll drvyglnril igqh
//
LOCUS       WP_175960673             252 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Escherichia coli].
ACCESSION   WP_175960673
VERSION     WP_175960673.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..252
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27287
     Region          3..248
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtllavrhas lgysrhpvlr dvsftlsqgt iccllgangc gkttlmrsil gvipllkgei
       61 lldslpvqtl shrqraqaia cvpqahdgif afsvldmvlm glaptigafs vpgkqerlka
      121 teqleklgil hlatrrwntl sggerqlali aralvqqprl llldepassl dfghqiqlld
      181 tlaqlknngm tmlmsthhpl hanaiadsii qvepdgrvtq glpteqlttk klaalyrvsa
      241 dqihhhlsai kh
//
LOCUS       WP_175960706             337 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175960706
VERSION     WP_175960706.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..337
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35751
     Region          1..>172
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..287
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 melhqleafs avmsagsvtg agellgrsqp avtrqiqele adlgyalfdr hgprvtptrr
       61 afllyeever slvglraiea raralgneta epvriaatps laatlvpaal aalpdgahap
      121 hyqlrsesae hvvhevlagt adigvvtlpm ahagldvhwi aqtpcvavlp agdplaakpr
      181 ialrdlarrr ivtvanrhrl rqridaafaa arvearvfie tnaslnavma aragigigiv
      241 dpatgvalpv dgvvarpldv dipfafgiat pagkvrtaav dalldalhrt trallddvtf
      301 hdaaahdall rgdrlrsera prpprttrtr rtrpeaa
//
LOCUS       WP_175960732             230 aa            linear   BCT 11-JAN-2025
DEFINITION  RHS repeat domain-containing protein [Burkholderia pyrrocinia].
ACCESSION   WP_175960732
VERSION     WP_175960732.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..230
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26162
     Region          <24..137
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mlplmcglvp svaktrhatl fyqndhlgtp qelldesgkv vwlgryrawg gektvwrevp
       61 erneatnpir fqgqyyddet glhynryryy dpnsgrfvsk dpiglaggin vyqyasnpie
      121 widplglagt ssggvgrkpt snkpnqnskc pcrkewevtr ydrmceamln gtrvkyfrdp
      181 kakqwwsadt eghggsawkv meergailfi fatrtsmvil wgntkarqek
//
LOCUS       WP_175960735             205 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175960735
VERSION     WP_175960735.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..205
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23102
     Region          1..192
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mklygfagtr tqralwglke ldadfefvsv nlltgehkqp efvrlnpagk vpvlvdgdlv
       61 ipesaaivly ladkypekal lpvdsalraq ayrwvmfavt eleqplwrit rhsfiyppek
      121 rspadielar edfatmaail dkhlegrefi vgnsltvadc vtaylidwas ecnliepfpq
      181 lraylerlys rpkapqriae arkaa
//
LOCUS       WP_175960758             656 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia pyrrocinia].
ACCESSION   WP_175960758
VERSION     WP_175960758.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..656
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=70916
     Region          75..483
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mtafrkvwql lvgkpldpld prtrhaiavt pllawvglga dglssscygp eeaflalahh
       61 tplalflala taatvfiial gynqvielfp tggggyrvat allgakpglv sgaallvdyv
      121 ltvatslasg vdaffsllpv gaqafkltte ivlillmtgl nfrgmresim vllpifigfv
      181 vlhfglivyg vavhgsnlam ivpdamheah gmsqslgvfv mlallmrafs lgggtytgle
      241 avsnnvnmla dprvpngkvt mwymstslaf taggiillym lwharpvege tlnavvfgsv
      301 idhlglgsaf arhallaavl afeagllmvg aqtgfldgpa vlsnmasdsw vprhfrdlst
      361 rlvrqngiiv vglssllill wthgsvdvlv vlysinvflt fsmsllglct ywwrhrserg
      421 wfkhfflsal glsvtatvlv itlvekftag gwltvlvtsa vialcfminr hyaytraqla
      481 kedalfsgkp pevdeasapg kpdpsqptav llvgkhrgas mhallwvnrl fpghfrnvif
      541 lavgevdaka ydghehlerl rhsitealdy yvahcrrngi aadyriafgt npvvefmnla
      601 sstldaypna vcfasklifr rvnfltawlh nqtpvelqar lhvegkqmvl lpmnvg
//
LOCUS       WP_175960791             425 aa            linear   BCT 11-JAN-2025
DEFINITION  epoxide hydrolase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175960791
VERSION     WP_175960791.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..425
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46632
     Region          39..143
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          110..>251
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 msstpfspmr rhllatsvaa gvsamlptal yaatggsgir pftahipdea vadlrrriaa
       61 trwpgretva desqgvrlar mqallrywgt dydwrkgear lngfpmfite idgldihfih
      121 vrsrhanamp mimthgwpgs ifellkaigp ltdptahgas addafhvvvp slpgfgfsgr
      181 ptqtgwgsdh iarawgelma rlgytrfvsq ggdcgsvish rmamqrvqgl agihvnmpat
      241 vppdiaalla tdspapasls pkekaayekl atfyrdncgy sammvtrpqt vgyaladsps
      301 gqaawmydki sqwtysggvp ersiprdeil ddislywltn tatsaaqiyw edhsnnfnav
      361 dislpaaitv fpgeiyqapr swaersyrnl iyfnevdkgg hfaaweepel farevragfr
      421 plrrg
//
LOCUS       WP_175960894             749 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Burkholderia pyrrocinia].
ACCESSION   WP_175960894
VERSION     WP_175960894.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..749
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=81470
     Region          43..744
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mnspleatpd arrdassagr vrapegtfel srkrvdeldt ifgvggllar aldgyrprts
       61 qiemaravas ameasarrmp epeifetrkr parrlgdgdk tagpaaddaa aaesdndagd
      121 ntliveagtg tgktyaylvp amlwggkviv stgtkhlqdq lfqrdiptvr nalavpvtva
      181 mlkgranylc hyylqrtadn grlpsrqdta ylqeivrfak ltksgdkael asvpetapvw
      241 smvtstrdnc lgqecphyke cfvmqarrea qqadvvvvnh hlffadimlr dtgmaellpn
      301 antiifdeah qlpetatlff getlsttqil elardtvaeg lshardavew vklggdlera
      361 ardlrlafan dqivrmslaq lgddhpmfga ldaleaalda lasalasqae raeslgaclr
      421 rarelqdlla gwvapgaaea aakadeaaag dkaasdgdpn ekvrwvevfa htvqlhetpl
      481 svapifakqr agvprawvft satlsvrgdf thyaaqmgls srrsmtlasp fdyqsqglly
      541 vprnlpqpss paftdavfda alpaieasgg gvfmlcttlr avdriasklr dviesrgwnt
      601 pllvqgdasr telldrfray gnailvgsqs fwegvdvrgd alslvvidkl pfappddpvl
      661 aarldaltkk glspfavhql pqavitlkqg agrliraetd rgvlmicdtr lvdkpygrri
      721 wqslppfkrt reiavvqdff dehrsekrt
//
LOCUS       WP_175960931             286 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Escherichia coli].
ACCESSION   WP_175960931
VERSION     WP_175960931.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..286
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=30319
     Region          <41..277
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mniaivtinq ehaamagwla aqdfsgstlt hwqiepqpmv aeqvldalve qwqrtpaevv
       61 lfppgvfgde lstrlawrlh gasicqvtsl diptvsvrks hwgnaltatl qtekrplcls
      121 larqagadkn atlpsgmqql nivpgalpdw lisvenlknv trdplaearr vlvvgqggea
      181 dnqeiamlae kmgaevgysr arvmnggvda ekvigisghl lapevcivvg asgaaalmag
      241 vrnskfvvai nhdasaavfs qadvgvvddw kvvlealvtn ihadcq
//
LOCUS       WP_175960940             558 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 39 protein [Burkholderia pyrrocinia].
ACCESSION   WP_175960940
VERSION     WP_175960940.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14304616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..558
                     /product="glycosyltransferase family 39 protein"
                     /calculated_mol_wt=62538
     Region          24..375
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
     Region          450..555
                     /region_name="Arnt_C"
                     /note="Aminoarabinose transferase C-terminal domain;
                     pfam18583"
                     /db_xref="CDD:465810"
ORIGIN      
        1 mndtpsrlpl nritlvlllv alaivwfapl glrhlipsde gryaemarem fvtgdwitpr
       61 yngykyfekp plqtwlnalt fawfgigewq arlytavvsf agvllvgftg arlfnplsgf
      121 laaavlassp ywnlmghfna ldmglafwma lslcslllaq rpglrpaavr gwmwacwaam
      181 afavlskglv glilpgavlv lytliardwa lwkrlylvsg lviffaivtp wfvlvqqrnp
      241 effnfffivq qfrryltpeq nrpgplyyfv pvllvgflpw lsvawqsirh alrmprqpng
      301 fspmlvlliw safiflffsa shsklisyvl piapalaliv gaylplvsad rfrrhllgyl
      361 vffvaaafgi iflayqgdar tpnalyrafq mwlyaglaia aaltlaaawl nrragvaaai
      421 aafgaawlaf gtiggtghde fgryssgaql apavraelak lppdtpfysi emldhtfpfy
      481 mghttimvqr qdelafgisv epnkwiptvd ewitrwkqet halaimppgq ydalvkqgvp
      541 mrviardnrr vivekpqs
//
LOCUS       WP_175960941             393 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase [Escherichia coli].
ACCESSION   WP_175960941
VERSION     WP_175960941.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 393)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..393
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=41020
     Region          1..392
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mkdvvivgal rtpigcfrga laghsavelg slvvkalier tgvpayavde vilgqvltag
       61 agqnparqsa ikgglpnsvs aitindvcgy glkalhlatq aiqcgeadiv iaggqenmsr
      121 aphvltdsrt gaqlgnsqlv dslvhdglwd afndyhigvt aenlareygi srqlqdayal
      181 ssqqkaraai dagrfkdeiv pvitqsngqt lvvdtdeqpr tdtsaeglar lnpsfdslgs
      241 vtagnassin dgaaavmmms eakaralnlp vlarirafas vgvdpalmgi apvyatrrcl
      301 ervgwqladv dlieaneafa aqalsvgkml ewderrvnvn ggaialghpi dasgcrilvs
      361 lvhemvkrna rkglatlcig ggqgvaltie rde
//
LOCUS       WP_175960971             146 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia pyrrocinia].
ACCESSION   WP_175960971
VERSION     WP_175960971.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..146
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15412
     Region          17..144
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mtdgvvetgd wtvlggdaar irdavfvreq qippeweldd ddplslhava yridaatgir
       61 ravatgrllp sgmigrvavl adargqgvgs avlhallaaa rrrgetvvrl yaqdsavsfy
      121 vrhgfaavge pfveagvphv emarap
//
LOCUS       WP_175960975             159 aa            linear   BCT 11-JAN-2025
DEFINITION  PaaI family thioesterase [Burkholderia pyrrocinia].
ACCESSION   WP_175960975
VERSION     WP_175960975.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..159
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=16923
     Region          1..134
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 msdaaspadg psiespfvdl lgvqlvsakd gaseivlple erhmntwsia hggvtmtlad
       61 ialamaarsl tddgvgvvtv emkvnfmqpg rgelraygrv mhrsttmayc egevrdsdgn
      121 fvakalgtfk ymrrlavgrd ikrqrsrtap daqpgpsda
//
LOCUS       WP_175961081             256 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175961081
VERSION     WP_175961081.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..256
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28513
     Region          10..245
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mtppnvvpls aaplyvqikd tlrarildgt yaphsrmpse helcatfdvs ritvrqalgd
       61 lqkegllfkl hgkgtfvskp kafqnvtslq gfaeamssmg yeivnqlrsf rtvkadrhla
      121 tklnvpegap lveihrvrll nrepvsleqt wvpealgkrl agadlatrdi flilendcgi
      181 plghadvsid ailaddeivd alhveesspv lrierlthna sgapidyeyl yfrgdafqyr
      241 lridrqkark parnpr
//
LOCUS       WP_175961110             240 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Escherichia coli].
ACCESSION   WP_175961110
VERSION     WP_175961110.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18235482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..240
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27052
     Region          <77..125
                     /region_name="Methyltransf_11"
                     /note="Methyltransferase domain; pfam08241"
                     /db_xref="CDD:462406"
     Region          <84..179
                     /region_name="COG4627"
                     /note="Predicted SAM-depedendent methyltransferase
                     [General function prediction only]"
                     /db_xref="CDD:443666"
ORIGIN      
        1 mkpakvpqtv vapdcwgdlp wgelyrkale rqlnpwftkm ygfhllkign lsaeinceac
       61 avshqvnvsa qgmpvqvqad plhlpfadks vdvcllahtl pwctdphrll readrvlidd
      121 gwlvisgfnp islmglrklv pvlrktspyn srmftlmrql dwlsllnfev lhasrfhvlp
      181 wnkhggklln ahipalgclq livarkrtip ltlnpmkqsk nkprirqavg atrqcrkpqa
//
LOCUS       WP_175961117             254 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF899 domain-containing protein [Burkholderia pyrrocinia].
ACCESSION   WP_175961117
VERSION     WP_175961117.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..254
                     /product="DUF899 domain-containing protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28710
     Region          1..254
                     /region_name="COG4312"
                     /note="Predicted dithiol-disulfide oxidoreductase, DUF899
                     family [General function prediction only]"
                     /db_xref="CDD:443453"
ORIGIN      
        1 mtthltgtrd ewlaerrall eaekaltrqs delarrrqal pwvrvdktyr fdteegqatl
       61 ddlfrgrsql lvyhfmfgpd ykagcpscsa ladgfdgfav hlanhdvtla avsraplakl
      121 layrqrmgwt fpwassvgsd fnfdfnvsft etqrrtgdve ynyaragham dmdpppapvv
      181 qfaatcgtda vtysldrpgm safvredgav yhtystyarg ldglwgmyqw ldraprgrne
      241 agpwwrrhde yarg
//
LOCUS       WP_175961197             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175961197
VERSION     WP_175961197.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33787
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,160,162,223,240,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mnqlqamrvf trvvelssfn laarqlgmsa aavtrsvgml eahlnmrlln rttrslslte
       61 tgreyldgcr tiiekldeie snlvqatrdp rgtlriaasa tsvaaglgil lstyraghpr
      121 vrfdvttfdt hvdmveggyd icfcddrrli natfvsralm rvrdvvvasp eylarhgtpn
      181 dpvelnehsl ltvsngtars wefsdvdgsy rvytgnalas tgsmmvriaa lnhmgitqlp
      241 hplvaddlar gtllpllecy evnggprcvs mlypsrnyls tkarsfidyv vdhyralerd
      301 paqlsaa
//
LOCUS       WP_175961271             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175961271
VERSION     WP_175961271.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33083
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 melrqlryfv avaeelhfgr aakrlfisqp alsfdirkfe ealgvqllsr tnktvaltna
       61 gevllgearr lllqaaeaer ltvrsasgla grlrigfvhs mlyrglpdav rrfeadypgv
      121 evvlsemntq aqvqaiqrgq idlgyahwgh fppevestpv yaepfvcclp aahplarrkq
      181 valaalaaep filfpreaap hyhdliiaqc vnagfsplir hearlwqtil smiefgmgia
      241 lvprvlqqvk sdrlafrplk daslesrtla lkrsgtaepv alrfadyvra sidalpalag
//
LOCUS       WP_175961272             472 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia pyrrocinia].
ACCESSION   WP_175961272
VERSION     WP_175961272.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..472
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50767
     Region          8..462
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mqpegqfqhi aareqglrrt lsarqmamia iggaigtglf lgsgfaigfa gpsvlvsyai
       61 gafislllmg claemtvahp tsgsfgayae hyvspwagfl vryaywaciv lavgtevtai
      121 alymkywlpg vpgwlwivgf sallvfvnar svdvfgavey gfsvvkiaai vgfivlgayv
      181 vfgnpglvgd gaaragfhhy tdrggffpkg pwgtwvaviv sifsylsiem iavaageaed
      241 peravtrafr stivrlvlfy lvtlalmlai vpwtaagrde spfvkvmeai rlpgaaglin
      301 fvvlvaalsa mnsqlyittr mmfslsragh apkalgevna rgvpfgalml stlgialatv
      361 lsvlypdasf timmavsmfg alftwmmifv thycfrrrra alglptpafr mrgfplltll
      421 gaglmlavmv ttyftaefhm tlifgipflv alsvvyavwy rraqpvlqse ak
//
LOCUS       WP_175961274             404 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid aminotransferase [Burkholderia pyrrocinia].
ACCESSION   WP_175961274
VERSION     WP_175961274.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Alexander,F.W., Sandmeier,E., Mehta,P.K. and Christen,P.
  TITLE     Evolutionary relationships among pyridoxal-5'-phosphate-dependent
            enzymes. Regio-specific alpha, beta and gamma families
  JOURNAL   Eur J Biochem 219 (3), 953-960 (1994)
   PUBMED   8112347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..404
                     /product="amino acid aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43716
     Region          1..396
                     /region_name="PRK09257"
                     /note="aromatic amino acid transaminase"
                     /db_xref="CDD:181731"
     Site            order(102..104,130,183,214,243,245..246,254)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(105,140,207,252..254,290,293)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            246
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 myehipaypg dpilslfqaf qqdahphkvn lsiglyydda gripvldstr iaagrvreag
       61 aphtylpmeg laayrqgvqr lvfgddcaal aqgriatlqt lggsgairlg aefvrryfpd
      121 saiwisdptw dnhrvifsaa gldvhtypyy daarndirvd amlatldalp arsvvllqpc
      181 chnptgldld rdawravidv larrglipfl dmayqgfgdg laddawavrt ivdaglpaiv
      241 gnsfsknfsl ygervgglsi vcandgeaat vlsqlqagvr rtysspplfg aqlvstvlnd
      301 dvlrarwede vaqvrtrikr mrgelkarld trlpgrafda lvaqrgmfsy tgiaaadvdr
      361 lrashgvyll rsgrmciagl ndanvdhvan aiadvlggas rhaa
//
LOCUS       WP_175961273             128 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175961273
VERSION     WP_175961273.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..128
                     /product="RidA family protein"
                     /calculated_mol_wt=13446
     Region          1..124
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 maetipvdlp qlaqpfswat ragglmftgh gpvaasgaiv gdtmaeqarv tlanlakava
       61 aagatmddva qvlvylsdvk ampefdaeyr rhfrepypnr tcvgvqgfah pamcvelvay
      121 valpvart
//
LOCUS       WP_175961333            1049 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia pyrrocinia].
ACCESSION   WP_175961333
VERSION     WP_175961333.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..1049
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114737
     Region          11..1027
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msapreegrf nlsawalrhq alvvyliala tlagilaytr laqsedppft frvmvirtfw
       61 pgatarqvqe qvtdrigrkl qetpaidflr sysrpgesli fftmkdsapv kdvpetwyqi
      121 rkkvgdigyt lppgvqgpff ndefgdvytn iwtlegdgfs paqlhdyadq lrtvllrvpg
      181 vgkvdyfgdp dqrifievnn aqltrlgisp qqlgqainaq ndissagvlt taddrvfvrp
      241 sgqldnvdai adtliringr tfrlgdlatv krgyddpvvt qmraagkavl gigvtmqpgg
      301 dvirlgkald aeskdlqarl paglklvevs smphavahsv ddfleavaea vaivlvvslv
      361 slglrtgmvv visipvvlav talfmylfdi glhkvslgtl vlalgllvdd aiiavemmav
      421 kleqgysrar aaafaytsta fpmltgtlvt vsgflpiala ksstgeytrs ifevsaiali
      481 aswfaavvli pllgyhmlpe rkrqaheahl pddhehdiyd trfyrrlrgw vdwcierrfv
      541 vllitgalfv vslmgfslvp qqffpssdrp ellvdlrlpe gasfaatlre terlekaidk
      601 rpeidhsvnf vgsgaprfyl pldqqlqlpn faqfvitaks vedreklatw lettlrdkfp
      661 avrwrlsrle ngppvgypvq frvsgdsiat vrsiaekvaa tmrgdartvn vqfdwdepae
      721 rsvrfeidqk karelnvtsq dvssflamtl sgttvtqyre rdkliavdlr apqadrvdpa
      781 klaglalptp ngpvplgslg rfeptleygv vwerdrqpti tvqsdvraga qgidvthavd
      841 aklnalraql pvgyqinigg sveesakaqn sinvqmplma iavftllmiq lqsfsrvlmv
      901 vltaplglig vvatlllfgk pfgfvamlgv iamfgiimrn svilvdqieq diavghgrvd
      961 aiigatvrrf rpitltaaaa vlalipllrs nffgpmatal mggitsatvl tlfylpalya
     1021 twfrvkrder dpqdgpphdg stpaapsga
//
LOCUS       WP_175961331             342 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175961331
VERSION     WP_175961331.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10859374
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..342
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38626
     Region          3..98
                     /region_name="HTH_NolA-AlbR"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators NolA and AlbR; cd04788"
                     /db_xref="CDD:133415"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133415"
     Site            order(51,54,58..59,68,80,84,90,94,97..98)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133415"
     Region          131..>187
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
     Region          <259..336
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 mqlkvgelak rsgltvrtlh hyhaiglltp saradngyrl ydrhdiarlh qiqalrrfgl
       61 slteigdyln qpgtplvdlv akqialldrq laqtaqlrer lvslhaqlaa gtepeladwl
      121 ttlelmtvyd kyfseeelar mpmyrksqag daewialvge vralhdagvp pederarala
      181 grwmallvrd tnndprllak lnlmherepa mqskigista lrdyvlrata etkmrifeky
      241 lapdeirfmr ahygeramew pqlmadvrda idagatpdsp egralaqrwl dlfcsyaghd
      301 ptthakfrha mmnepaltkd awvddtllgf ireamaqlvp ar
//
LOCUS       WP_175961370             167 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia pyrrocinia].
ACCESSION   WP_175961370
VERSION     WP_175961370.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..167
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17294
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mysnilvald gsepssrald aaltlasesg arltpvyvvd flvpaydmyg ydpsilidaf
       61 reeglrvtdg aakrmaargv tgtprianvd pggedvaqrl livakeagad livmgthgrr
      121 gfsrlvlgsv aerllrraac pvlmipasca pvpaaapaaa stekeps
//
LOCUS       WP_175961379             144 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175961379
VERSION     WP_175961379.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..144
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=15675
     Region          42..143
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 msnltrydpf sidpvsdlfq glfrplrgmt ltdepdlasm kidvtesdna ykvnaelpgv
       61 akddidvqvt grtvsisaki ernneqkege rvirrerysg aisrsfslpg eiddanataa
      121 yqdgvlsltl pkktpagqkk ltig
//
LOCUS       WP_175961447              99 aa            linear   BCT 11-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Burkholderia
            pyrrocinia].
ACCESSION   WP_175961447
VERSION     WP_175961447.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..99
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=11449
     Region          6..99
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mavkgrqlrl tplaeldled iwrytvehgs leqadhyhrd lvgtmealar gkkagrtciv
       61 rngyfryavg shvvfyretd dtidvirvlh qrmdierhl
//
LOCUS       WP_175961508             157 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Burkholderia].
ACCESSION   WP_175961508
VERSION     WP_175961508.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..157
                     /product="VOC family protein"
                     /calculated_mol_wt=16499
     Region          13..136
                     /region_name="VOC_like"
                     /note="uncharacterized subfamily of vicinal oxygen chelate
                     (VOC) family; cd07246"
                     /db_xref="CDD:319910"
     Site            order(13..18,20,35,49..50,57..58,60..62,81..83,85..90,96,
                     117,122,130..133)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:319910"
ORIGIN      
        1 mstsvkpipe gmrtltphli cagaaaaidf ykrafdaseq frlpmpdgrl ahaclaigds
       61 tlmlvdempe hgalgpkalk gtavclhlyv pdtdaaiaka vaagatvtip aadmfwgdry
      121 gqvedpfghr wslathqrdl tpeqiaeama sappcgs
//
LOCUS       WP_175961522             328 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175961522
VERSION     WP_175961522.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..328
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34466
     Region          7..236
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mndndhrpvr fgivgagsia rrfaqslahv pgatldgawa rradaaaafc etcggtpaas
       61 leallasdid avyiatlhds haqytlaala agkavlcekp atlnaaqldt vlraardagr
      121 lfmeamkppf fplyrqlrah lhddpigeir lvragcasss vpgdhsvyrl draggalldi
      181 giyeaflavd wlgaaldvqt lgrvgatgvd mfaslnslha nggiaqlfcg ldvmgrgdal
      241 iaaagghvti hekwwnpara tiryadgrtv eldapaeggg lnyetahfcg llragetesp
      301 imthdhsrqm iamtdaaraa lgvrysge
//
LOCUS       WP_175961602             473 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia pyrrocinia].
ACCESSION   WP_175961602
VERSION     WP_175961602.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..473
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50335
     Region          2..473
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mmsseafvsa crdaigadhv ltdphdtepf ltdwrrrykg aacavlkpan taevaalvkl
       61 anahgialvp qggntglagg atpdasgsqa vlsvarlnrv raldphnnti tveagailad
      121 vqarareggr lfalslaaeg sctiggnlst naggtavlry gnarelclgl evvtpqgeiw
      181 dglrglrkdn tgydlrdlfi gaegtlgiit aavmklhplp aaqvtalaal esphaaldfl
      241 alaqraagpl ltgfelmsdf cmqlvgkhyp qlrypftqth sqtvllelsd neseaharal
      301 feklmeeafe aglvvdavva enlaqsrafw dlrehiplaq adeglnikhd iavpissvar
      361 fidetdaaiq qaapgarmvt fghlgdgnlh ynvqmpeggd pkaflaafqa pinrivydnv
      421 hrhhgtisae hgigqlkidd aqrykspvet tlmrtlktal dprglmnpgk vlr
//
LOCUS       WP_175961395             187 aa            linear   BCT 11-JAN-2025
DEFINITION  shikimate kinase [Burkholderia pyrrocinia].
ACCESSION   WP_175961395
VERSION     WP_175961395.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Herrmann,K.M.
  TITLE     The shikimate pathway as an entry to aromatic secondary metabolism
  JOURNAL   Plant Physiol 107 (1), 7-12 (1995)
   PUBMED   7870841
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Bentley,R.
  TITLE     The shikimate pathway--a metabolic tree with many branches
  JOURNAL   Crit Rev Biochem Mol Biol 25 (5), 307-384 (1990)
   PUBMED   2279393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..187
                     /product="shikimate kinase"
                     /EC_number="2.7.1.71"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004765 - shikimate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=20192
     Region          18..181
                     /region_name="AroK"
                     /note="Shikimate kinase [Amino acid transport and
                     metabolism]; COG0703"
                     /db_xref="CDD:440467"
ORIGIN      
        1 msavvaaaea ralparaflv gmmgagkstl gralaaslgw tfadsddeie rrtgrsvavl
       61 fdmvgeggfr llethivdel tqrpnvivat gggavldprt rarlsergcv iylhadpdtl
      121 wrrtrddarr pllrvaeprq tlaalyrmrd plyrecahal vdttaqgvar ataevltvlq
      181 armrapg
//
LOCUS       WP_175961816             297 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia pyrrocinia].
ACCESSION   WP_175961816
VERSION     WP_175961816.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..297
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31841
     Region          3..293
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mndviiiggs faglaaalql grarrkvtvl dtgrprnrfa ghshgllghd hkppldilve
       61 arqqlvrypt irlvdaraes vsgaiddfcv vtddheslra rrlilsygvv dqmpavpgfa
      121 eswgtsivpc pycdgfevaa qhwglvwsgp qsmnqvrlfh dwtdtltvfa dghdialdir
      181 adlahrsipv idgriteiar hggrnatvkl dnapdvavdi lfahprtkps aslhellgla
      241 tvntptgial kvderretsm pgiyaagdla ntgmpsvtta swqgatagis aqqsmla
//
LOCUS       WP_175961802             466 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Burkholderia pyrrocinia].
ACCESSION   WP_175961802
VERSION     WP_175961802.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..466
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51707
     Region          4..440
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 meifdafhla rlqfaftvsf hivfpaisig masflavlew rylvtgdaay ksmfqfwski
       61 faigfgmgvv sgvvmayefg tnwagfsrva gnitgpllty evltafflea gflgvmlfgw
      121 qrvsprahff atlmvavgtl istfwilasn sfmqtpqgyr ienglvvpvd wfkiifnpsf
      181 pyrlvhmtia afivagfiva acgawhllkg rrdepvkrsf smalwmllll apiqivvgda
      241 hglntreyqp akiaaieglw etekggtaln lvglpdmqae ttryaiqvph lgslilthsw
      301 dgeirglkef ppqdrpyspi vfwtfrimag lgmlmlltal lglllrkggr lyetrwfqwf
      361 vvgmgpsgiv allagwvtte vgrqpwtvyg vlrtvdsvap lsaqqvgvsl lifvvvyflv
      421 fgtgiyymmk lmkrgpaaqa gyielhrhpg lrksalstpl nvteae
//
LOCUS       WP_175961913             156 aa            linear   BCT 11-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Burkholderia pyrrocinia].
ACCESSION   WP_175961913
VERSION     WP_175961913.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..156
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=16908
     Region          1..153
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mfnavidapf gkvgirtdaa vvreivylpe svksvdpdsp lakravqqie ryferasarf
       61 dlplaevgsa fqhrvwdvis dipagtvlty gqvakrigsa pravgqacga nyfplvipch
      121 rvvaagglgg fanhddngyy qkvkrwllah egvpyr
//
LOCUS       WP_175961942             318 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Burkholderia pyrrocinia].
ACCESSION   WP_175961942
VERSION     WP_175961942.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..318
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32827
     Region          4..296
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(36..37,40,91,105,107,136,168,256,259,295)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(227,232,247,256..258,261,283,287)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 maaivvagel laefvaaerg qgfdapglfa gpfpsgapai fadqaarlga rvayagcvgr
       61 dafgdaivar lerdgvdvar irrvarptgt afvayrddgs rsfvfslsts aaacvdasdv
      121 dtamfdgcry fhvmgsslts esaiaavqrg vieaaragak vsfdpnvrpe mlsfrpmraa
      181 ldemlaachl flpseadlpf fcgpqpaera iagllathpl lervvlkrga agsvafdras
      241 raeaaafpvd eidptgagdc fggtlvaslv agmpievalr ranaagaiav mrrgpmegns
      301 saaeidrflt ergvacpa
//
LOCUS       WP_175961935             294 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175961935
VERSION     WP_175961935.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..294
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32567
     Region          9..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="PBP2_CrgA_like_7"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08476"
                     /db_xref="CDD:176165"
     Site            order(100,104,143,157,159,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176165"
     Site            order(101..102,106..107,109..110,113,117,119..125,186,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176165"
ORIGIN      
        1 menlggfvvf vqvaetrsfv aagralglsa saigkriarl earlnvrlfh rstrsitlta
       61 egtrflercr rviaeieaae qelthsaeap rgrlrvslpt igtlllpvla dfmaeypeie
      121 ldidfsdrlv dvvdegfdav lrtgqpsdsr lssrllrhfr qhlvaspdyl arhgtprtpv
      181 dlalhrclhy rfpssgklet wplrvprsgt ppevpvsmvs nsaearlcft lrglgiaclp
      241 effvrdaldd gtlcavldeh vasctpiyvl wpsgrhptpk lrafvdfmaa nlrf
//
LOCUS       WP_175961979             234 aa            linear   BCT 11-JAN-2025
DEFINITION  TerC family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175961979
VERSION     WP_175961979.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..234
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24508
     Region          12..191
                     /region_name="R_switched_YjbE"
                     /note="integral membrane protein, YjbE family; TIGR03717"
                     /db_xref="CDD:163429"
ORIGIN      
        1 mlefltslhw gavlqiviid illggdnavv ialacrnlpa nqrlrgvvwg tagaillrva
       61 litfavalld vpflkigggl lllwigvklm apaadahdhi kpadrlwdav ktiviadavm
      121 sldnviaiag aaeqadpshr ialvifglvv svpiivwgst lvlkmldrfp iivtlgaall
      181 gwiagglivn dpvgdrwpvl dtppaiygas magalfvvaa gyalrrrrga pgth
//
LOCUS       WP_175962037             116 aa            linear   BCT 11-JAN-2025
DEFINITION  FmdB family zinc ribbon protein [Burkholderia pyrrocinia].
ACCESSION   WP_175962037
VERSION     WP_175962037.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..116
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11106
     Region          1..73
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 mpiyayrcea cgfakdvlqk msdaplsqcp ecgkdafrkq vtaagfqlkg sgwyvtdfrg
       61 gsggasapaa tsgdaapaaa aaatpasdap aassssestt tsaapapaaa paaass
//
LOCUS       WP_175962048             320 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia pyrrocinia].
ACCESSION   WP_175962048
VERSION     WP_175962048.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..320
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34655
     Region          81..282
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mswqskfacw llrrqfrpet trevldpara rrftdlrmva prrapsgyrl rechgagdap
       61 lrgewlertd agagrapgrt llyfhgggyy fcstkthrpl vfgltkragv rsfsldyrla
      121 penrfpaald dalaayrqll algtppesiv lggdsagggl alatlvalrd rgeplpagai
      181 lfspwtdlag tgdtmrtndg adpmfagaal pkaaklylgd apathpyasp lyadfaglpp
      241 lyiqvgstev llddsrrvae kakaagvpve ievwpdmphv wqlyapmvpe ardaldraaa
      301 flrrvavera vqrvgeasia
//
LOCUS       WP_175962059             260 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Burkholderia pyrrocinia].
ACCESSION   WP_175962059
VERSION     WP_175962059.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..260
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28334
     Region          12..193
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(15,17,98)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(42,97..98)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            96..98
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 msklhassth lvlipsynpg akvdttvrna raqwnpvwvv vdgstdgsae rlqamaehdp
       61 glrvivlpen rgkgaavlag ldaaaasgft hvltmdsdgq hpaelipafm aasqaapdam
      121 vlgvpkfdas apqlrvqgrr lsnawadlet lwagigdsly gfrvypvapl aaimrrqpwm
      181 rgfdfdpeaa vrlcwagvrp iridapvryf grheggvshf hygrdnalla wmhlrlftgf
      241 avrlpmlvar rltrrrdqaa
//
LOCUS       WP_175962054             265 aa            linear   BCT 11-JAN-2025
DEFINITION  (Fe-S)-binding protein [Burkholderia pyrrocinia].
ACCESSION   WP_175962054
VERSION     WP_175962054.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..265
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28090
     Region          <8..255
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mnerqypaap ahvylfatcl vdlfvpeagl davrllereg ltvhyprgqs ccgqpayssg
       61 npdearrvaa aqldlfaesw pvivpsgsca gmirhhwpal faddpvhgpk araiaertye
      121 laeflvqvld vqldaaaasa gpdervvlht scaarremgt rghgvalvda lpgvtriehe
      181 reseccgfgg tfslkhpdis gamvrdkvas acatgcdrlv sadcgcllni ghaatkagas
      241 lpvehlasfl wrrtagaapl rgdkq
//
LOCUS       WP_175962105             449 aa            linear   BCT 11-JAN-2025
DEFINITION  NCS2 family permease [Burkholderia pyrrocinia].
ACCESSION   WP_175962105
VERSION     WP_175962105.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..449
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45978
     Region          14..443
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 msatdtmpar apanwlerrf alaargtsvr tetiagitsf laaayllvvi psllatggme
       61 rgaattativ vfvlfttlmg lyanlpflvg pgiggsvivg vtlattehvg wqtglgiacv
      121 sgvlffllti lgargvvvrl ipvqiklglg asiglfvtml glrnagmvva naktnafalg
      181 dfsrpgalva liglavavvl qarkvpgail iailaaaaag vplgvthlpa sfvslphsia
      241 piafkldigs alslaaapyl faffaaeffs tlgtalavga kanlldehgn lpdinrpflv
      301 dslaatigpv fgipaltali esaagveagg rsglsslaaa vlfaamllfv pvalaipkea
      361 tapaliligl smfatirhth fddftdalpv msmvlltlms nsfgtgiagg llcyvlvkll
      421 agrwrdvswg lvvlaiplgy yfwtvvkph
//
LOCUS       WP_175962107             741 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia pyrrocinia].
ACCESSION   WP_175962107
VERSION     WP_175962107.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 741)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..741
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=81629
     Region          48..715
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mnrfvpflrd awlrcrarva plaaacrart rvlcagalhr lrhptrrgva ltlaaipvlg
       61 llvllafvpf tpsigdirka ridrparvls adgeliaefr pvnrewvplk qisphmvdal
      121 iatedhrfya hhgidwrrti aaglhtfsga rqggstitqq larnlypdev grsltltrkv
      181 kelitafkie tvyskdeile tylntvpfly nafgvemaar tyfgksanql diaesatlvg
      241 mlkgnsyynp vlnperavqr rnivldrmat mgmlsprqla klqrqplrvd fepqtaqpgl
      301 aphfavqlrk wliawadrnn ydlysdglvv rttldarlqd matqaltqqt erlqaiadna
      361 wrgpsgcglr ndlfrgfirq tpdyrsarda gladaaalkq lganrgfmha lcerktqvqa
      421 gfvaidprng airawvgspd fgsepfdhva qarrqpgstf kpfvygaafa dgmrpgdtfi
      481 drpvaipidg ravwrptdee pptgepmtlr dalalsrnri taqvmqqega akvaqlaram
      541 gvrdspldav pslalgtspv tlkemvsayg tianrgvyva pqtitriedr dgkvlaafgs
      601 apperalpap aaqtlvdvmr dvvdrgtgad irsrygirvd vagktgttqd ntdgwfilmh
      661 pqlvagawvg fddgsvtlrs dywgagahsa lpivgsfyda alraraidpr aqfspdfrpr
      721 sapaprrrph pglfdwlklf r
//
LOCUS       WP_175962125             321 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia pyrrocinia].
ACCESSION   WP_175962125
VERSION     WP_175962125.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..321
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34696
     Region          11..224
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(52..53,55,69..71,77,79..80,121,223)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(52,54..55)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(77,80,83,90)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(113,117..120,122)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(118..119,142..144,196..197)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          237..321
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 msaatltvrv arkwqeardi cgfefvsddg splprfdaga hidvhlpggl vrqyslcnhp
       61 ehgdryqiav lrdaegrggs raihdevrqg dtvrigmprn qfplapdaph hlllaggigv
      121 tpilcmaerl fssgmpfdmh ycarstdrma fverinaagf ndrarfhvdd gapaqrfdla
      181 svlaaapdgt hlyvcgprgf mdavlnaare rnwaderlhy effggavats gadrafqvri
      241 assgkvidvp aectviaala angvdvltsc eqgvcgtcvt rvlqgepdhr dsylteaeqa
      301 agdqfmpccs rsrtdllvld l
//
LOCUS       WP_175962239             335 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia].
ACCESSION   WP_175962239
VERSION     WP_175962239.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..335
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34755
     Region          13..317
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mrkpgifgig steawllavi vamavglgia tptfltlsnl fdllnqsavn iifavglliv
       61 liaggidisf avgasvvqyl aaltlmrlgg gnwalgfavs acfgillgav natiiyrfrv
      121 vsivatiatf niffgglmfv tggvsiydlp dwwtnrvtlv qvdtpggvas lalpvavmaa
      181 avvatwfllr rttlgrqlya tgdnpeaarr vgidlatmhy vaygwlgmma giaglmqahy
      241 vqeivpnaly greldvlaav vlggarlggg rgtvlgailg illvsitang lnllgvspya
      301 fkmivgavil vaitvssdgv arlvgsrfls prart
//
LOCUS       WP_175962260             345 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia].
ACCESSION   WP_175962260
VERSION     WP_175962260.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..345
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35764
     Region          34..345
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msndthpvpp lasgdspaga sgfrarffnp aarqkllafa slvllivffs iaspnflevd
       61 nlvtilqata vngvlavact yviitsgidl svgtlmtfca vmagvvltkw gmplplgila
      121 alcfgalsgc vsgfviakmk vppfiatlgm mmllkglslv isgtrpiyfn dtpgftsiaq
      181 dslignlipa lpipnavlil flvavgasiv lnrtifgryt falgsneeal rlsgvnvdaw
      241 kiavytfsga vcgiagllia srlnsaqpal gqgyeldaia avviggtsls ggagsivgti
      301 igafimsvlt nglrimsvaq ewqtvvtgvi iilavyvdil rrrrr
//
LOCUS       WP_175962318             288 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175962318
VERSION     WP_175962318.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..288
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30668
     Region          12..278
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mkkiqgvysa prghwvgdgf pvrsmfsyqs hgahlspfll ldyagpatfe pasaprgvge
       61 hphrgfetvt ivydgevahr dstgaggvig pgdvqwmtaa sgilheefhs eaftkrggpl
      121 emvqlwvnlp aadkmgapgy qtllnadipv velpdgagra riiageldgr rgparthtpi
      181 dvwdvrlvag gharfpvaeg rtlavvvlsg tvqmngetva reaqfvqlgr egrdveiean
      241 gdakllilsg epidepvvgy gpfvmnsqae irtaiedfns grfgkmpa
//
LOCUS       WP_175962372             213 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia pyrrocinia].
ACCESSION   WP_175962372
VERSION     WP_175962372.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..213
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=21685
     Region          7..213
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mtqrslnial fgatgtigsr iaaeaarrgh rvtalsrnpg aaddgitaka adlfdaasia
       61 aalpghdvva saygpkqdda akvvaaakal vagtrqaglk rlvvvggags levapgkqlv
      121 dsegfpeayk avalahrdaf dylktvgdld wtffapaali apgertgtfr tgvgkliada
      181 qgnskisaed yavafvdale qgsfvreiat vay
//
LOCUS       WP_175962367             129 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Burkholderia pyrrocinia].
ACCESSION   WP_175962367
VERSION     WP_175962367.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..129
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=14012
     Region          1..90
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mkhartrrsr gftlieivvv maiigllltl avprymhsie rgkeqvrqqn iavmrnaidq
       61 yygdngqype tldelvakhy lrsvpldpvn gddkwaavas pdeskpgvyd vapasspqga
      121 ppsvtgaak
//
LOCUS       WP_175962387             302 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia pyrrocinia].
ACCESSION   WP_175962387
VERSION     WP_175962387.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..302
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31676
     Region          36..265
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mqslsgssap spaptpasas aqangvarra prvtgaraia alqwgvtlll caflivpvvm
       61 svlagltvny frglssgltl rwleqvwqqy hgsialslyv afatlaivlv vgvpagyala
      121 rsksrvarai eealvlpval pglasalall vvyggftafr mslwfivvgh vvftlpfmvr
      181 avaavaagad lrtleegaas lgasfvtrfv tivlpnlrpg ivagalavlt lsigefnltw
      241 mlhtpdtktl pvgladtyas lrlevgsayt ilfllmtlpl lvamqwlgvd psgtralkrr
      301 pr
//
LOCUS       WP_175962391             449 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrolipoamide acetyltransferase family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175962391
VERSION     WP_175962391.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..449
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47846
     Region          2..449
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mgihvikmpd igegiaevel vawhvevgqt iaedqpladv mtdkaaveip spvsgkvlel
       61 ggrigemmav gselirleve gdgnlkqgvp vrdakaeaap vqttaaaaak sapvtdapaa
      121 apaataapdr aanrapaepr raeraepaaq praalapger plaspavrqr awdmgielry
      181 vrgtgeagri lhtdldayak tgsgtarasq ahgyeersde tevpviglrr aiarkmqeak
      241 rriphfsyve eidvtelesl radlnrrygd trgrltplpl liramvialr dfpqinarfd
      301 deagvvtryg avhmgvatqt dagltvpvlr haeardvwsi saeiarlada vranraqrde
      361 lsgstitiss lgalggivst pvinhpevgi vgvnriverp mirdgavvar kmmnlsssfd
      421 hrvvdgadaa efiqavrgvl erpallfve
//
LOCUS       WP_175962396             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175962396
VERSION     WP_175962396.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46016
     Region          13..417
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(25..26,29..30,33,72,130..131,133..135,138,158,
                     161..162,165,247,250..251,254..256,259,287,291,343..344,
                     348,352,368,371..372,375..376,379)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mtqslpsarq pgraataafi gtmiewydfy iyataaalvf gelyfpshdp fvstmasfat
       61 favgffarpl ggvifghlgd rigrkkalmt tlmmmgvatv cvgllpdysk vgmlapvllv
      121 vlrvvqgiav ggewggavlm agehapqgrr tffasfaqlg spaglilsli afravtsmdk
      181 adflawgwrl pflasavllv vgilirlgvn espefarvke anrtvklpva evfrsasglv
      241 alcigantig iagvyftntf miayttqyvg vsrslildsl favaiiqfva qpiaawiaer
      301 iggarflkla allamlspyp mfmlvqggts aslvagiala vvcmagfysv iagfvsdvfp
      361 ahvrysaisl ayqicgalag gltplvgtwl ahrftgqwwp lavfysclag isllcivald
      421 arraaqpaaa ealgsh
//
LOCUS       WP_175962435             839 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175962435
VERSION     WP_175962435.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 839)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 839)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..839
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..839
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=91658
     Region          14..786
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnmtevaqai rggliqqdrl lktsipslpe nalvprravt yselgrdfsv tldmvstagd
       61 ielktliaqp mtlwlqqank sylpingyih tarrlgadgs lssyqlafas wmhflkfrsd
      121 mrywqdqsvd ailtdvfnah pqargqfefa llktlpsrsy crqsetdwnf vhrlmeeegl
      181 fgfwrqdneg kshrfvvtdd iysldevlpk qigfsrsgts setgaftqwa gsrtlqstvy
      241 ttrtfdykap sslvnpkgtt lptmagqgnl peqtevyeyt gaytylnqdr gehlskihle
      301 ewesrakrfl gigsvraida grrfvltghp ehdrdqagqq efaaikvrry iennlplsnh
      361 eanfpyslqs elaqakfeqt gevvthedgs agfylvevea qrvtvpyrsp fehkkpamel
      421 etaivvgpqg eevhtdalnr vkvmfvwdrq nsgdanascw vrvaqsdsgg gygsvhvprv
      481 geevlvgyig gdcdrpivlh rvyngsvqpq whsngilsgy rskeysgsgy nemvlddatg
      541 qnrarlfsst gssllhlgyl ieqngntrga figsgfdlkt dlsgavraaq glyvttyqkp
      601 anshqldvse aqqqltgaeg aieamsqasq qhqaeslgag rdalktftna tqgtvqgsqs
      661 ggrtgdggkg sanafktpvm lfaspsgial stpqsvhias dqqtnlvsgq stfiasrksl
      721 vasvaerisl fvqnagmklf aakgrveiqa qgaeldmasq kdlsiksvgg kvviaaaqei
      781 glyvggsyir itssgiengt vgqirercss wdveaadskq vpmpsfssge vantylhsl
//
LOCUS       WP_175962462             469 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia pyrrocinia].
ACCESSION   WP_175962462
VERSION     WP_175962462.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..469
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50214
     Region          14..467
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mnhpappaat rrplppamld alraafgerv stadavrehh grdespfdpq lpdavvfahs
       61 addvreavsl cslysvplip ygagsslegh llavrggvsl dlsemnrvls inaedltvtv
      121 epgitrkaln ealrdtglff pidpgadasi ggmtatrasg tnavrygtmr envlgltavl
      181 adgrvvktgs rarkssagyd ltrlfvgseg tlgviteitl rlhplpeavs aaictfptmg
      241 davrtvieti qigvpiarve fvdslavrsi nrhsnltlte aptlffefhg teagvkeqae
      301 lvqalagqnn gqgfewatrp edrsrlwaar hnayfamlql kpgcravttd vcvpisqlaa
      361 cveetevdlr asslpcpivg hvgdgnfhva ilidpdkpee iaeaehindr iveralrlgg
      421 tctgehgvgl hkmrflpkeh gdnaidtmra iklaldprnl mnpgkiftc
//
LOCUS       WP_175962483             270 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175962483
VERSION     WP_175962483.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..270
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28951
     Region          4..256
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mpdlataqqf lmtrgldfgl nllaalvlwf igrwaihiat rllgkvvrrs gkvdptltdy
       61 ltsvvgvllt illilailqi fgvqttsfaa llaglglaig tawggllahf aagvfmqvlr
      121 pfkigdvisa ggvtgtvkel glfgttiita dnivtivgnn kifsdniany satshrrvdl
      181 takiangvda vdainrlkts iqqipnvltd papdvgvlqf tpegpllfvr pstapenywq
      241 vycdtnrvii etfrdaqypt petplshrna
//
LOCUS       WP_175962503             263 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175962503
VERSION     WP_175962503.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..263
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28127
     Region          13..261
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mtlstidett iderkfvval argldllraf rpgetmlgnr dfaertglpk atvnrlaytl
       61 tvlgylryde tlgkyaldag vlslgyalls gsgtielarp hmqalareig aavslgcrdg
      121 ldmiyletir setaltlgla pgsrlsmlts smgraylavq pedvrralya elhraaggaa
      181 dadalvaaaq havaefsagg ccysfrawhm dvnaaavpfr epregrwlil scsgpassmd
      241 eevfrtqvgp klkalaqrlg qta
//
LOCUS       WP_175962545             249 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia pyrrocinia].
ACCESSION   WP_175962545
VERSION     WP_175962545.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..249
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27045
     Region          4..249
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 mafielksvt ldlpifdvqg rslkkqvlrv grrnriaegs dgvivvrald dvsfrfdrgd
       61 rvglighnga gkstllrama giypptagal sregkvvpll diglgmdens tgmqnirlrg
      121 lllgmsdaei rtkqreiadf celgdyldlp irtyssgmkv rlafavstav daeillldev
      181 mgvgdasfmh kaearladlh sraeivvlam hsnseirkvc nkalwmergr vrafgsadev
      241 vlayeaama
//
LOCUS       WP_175962597             251 aa            linear   BCT 11-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Burkholderia
            pyrrocinia].
ACCESSION   WP_175962597
VERSION     WP_175962597.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..251
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26048
     Region          1..251
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlttqrkkai ldalahdgqv lavelsaqfg vsedtirrdl relaaegllq rvhggalpas
       61 pavapfaqre vletaekrri arraaqmiap gqvaivdggt tsallvsqlp adlrativth
      121 spsvavalaa hpsidvilig grlykhsiva vgaaamegia rihadlyfmg vtgvhpvagl
      181 stgdfeeaai kralaeraae tvvlasqskl raasqfvigd itlaqtvvve keteaaltkp
      241 ieaagvtvvr a
//
LOCUS       WP_175962560             367 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia pyrrocinia].
ACCESSION   WP_175962560
VERSION     WP_175962560.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..367
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=40535
     Region          38..145
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
     Region          255..>343
                     /region_name="PilN"
                     /note="Type IV pilus assembly protein PilN [Cell motility,
                     Extracellular structures]; COG3166"
                     /db_xref="CDD:442399"
ORIGIN      
        1 msagsteafy rafenrfrgp reliksrlgv ylpilgplrq fdphpaaldl gcgrgewlev
       61 ltdagfaphg vdldeamldi araehlhvsh gdalgflhei rdetqfvvsg fhiaehlafh
      121 dlqdlvkqsl rvlrpggfli letpnpeniq vgtanfyldp thqrplppdl lsflpgyygf
      181 artsvlrlqe aagvaerqsv tlldvltqvs pdyaviaqka gddaimlatq palevergvs
      241 lqslanqfda hhasvvaglt gavaalrndi aggltdlsgq cqrqqeetar lseqvaklta
      301 qvleyetrqq aaqaqmerll qeqgarqraa hehiekllqe ieryrnsrsw rvtaplraar
      361 sllrkrs
//
LOCUS       WP_175962602             116 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF190 domain-containing protein [Burkholderia pyrrocinia].
ACCESSION   WP_175962602
VERSION     WP_175962602.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..116
                     /product="DUF190 domain-containing protein"
                     /calculated_mol_wt=13284
     Region          4..103
                     /region_name="COG1993"
                     /note="PII-like signaling protein [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:441596"
ORIGIN      
        1 mdrvflrfyv heqhrlhwkp lwewlleean rmgvaggsaf ramagfgqhr vlhedrffel
       61 qgslaievef vvtedeaqrl lerlsrekvr vcyamiparf gvidtlvapp ahgpaa
//
LOCUS       WP_175962689             476 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia pyrrocinia].
ACCESSION   WP_175962689
VERSION     WP_175962689.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..476
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49502
     Region          20..476
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mqnpnpaavg geqggaplsd daldavlvae lgdalvtraa didpryftay nepagvrpra
       61 lvrprsvddv srtlalcarl gqpvvpqggl tglargaval ggevvlsmer fagiealdaa
      121 agtmtvragt plqtvqeaae aagftfgvdl gargscqigg mlatnaggtr airygmmreq
      181 vlgleavlad gtvvssmnrm lknnagydlk qlfigsegtl gvvtravlrl hpllaapata
      241 lcrvrdydav vglwnrvrtl pevvsfeamw pafydyvarh tpgvtapfag dggfavliec
      301 atsapggdah raletglaag ieaglvddav latserqard lwtlreglai dalpqlvnfd
      361 vslptgelga faerceaalr vrwpaltclf fghvgdgnvh igvslatmtd adadaldhcv
      421 yavvrdmggs vsaehgigal krpylahtrs daeiglmrcl kaaldprgil npgkvl
//
LOCUS       WP_175962701             364 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia pyrrocinia].
ACCESSION   WP_175962701
VERSION     WP_175962701.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..364
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38337
     Region          <188..311
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mtvetrtapr ggalshddal vlpgtllapd gtlvapydie hgdaravghv paaaalgllh
       61 aahrpfrldy dgarhvhvin gmgvtlgdsv igltalaalr aahaglrftl yrpartprhv
      121 dalyalaadv vapsrtlpcp vdalpadapc idvgnhlywp afarlpmidf fldalgadpa
      181 avpaaakrnr wlarlplpal paawqrpyvl fcpnastavr svppalraaf verlaqrygl
      241 pvagfgpvah paytdvsgda adtarfiawi kgasllfapd taalhladgf dvptlacftt
      301 igpalrvrdy phcvpveldv paelhglhrs erpadlaave aayraidwda lawpapreaa
      361 aitg
//
LOCUS       WP_175962760             200 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA-3-methyladenine glycosylase I [Burkholderia pyrrocinia].
ACCESSION   WP_175962760
VERSION     WP_175962760.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..200
                     /product="DNA-3-methyladenine glycosylase I"
                     /EC_number="3.2.2.20"
                     /GO_function="GO:0008725 - DNA-3-methyladenine glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=22006
     Region          3..187
                     /region_name="Tag"
                     /note="3-methyladenine DNA glycosylase Tag [Replication,
                     recombination and repair]; COG2818"
                     /db_xref="CDD:442066"
ORIGIN      
        1 msqrcnwvkt eadahyhdte wgvpshddrh lfemlilega qaglswstil nkragyreaf
       61 adfdvdtvar ftpkhiekll enpgivrnra kvqsavtnar avqrirdehg slaaflwsfv
      121 gntpvqnawe syrdapaste qsdalsnalk aygckfvgst icyalmqatg mvndhetgcp
      181 chaqcaalgg kqparrrkag
//
LOCUS       WP_175962813             231 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175962813
VERSION     WP_175962813.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..231
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24404
     Region          10..231
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mfqirraadr dqrshgwhes hhsfpdaagr ggapafgalr elseeciapt rgfgmrpyrd
       61 aeivtyvldg tlayrdslgs gaivraggvq rtsagtgill setnasrdqp lrllrirlaa
      121 agpggrpgya htrfaddekr grlrlvaspd gddgslpvrs darifagwid gderaafdvp
      181 agrrvyahva rgeveingra laagdgagic gvaavtfarg raaevllfdv a
//
LOCUS       WP_175962872             853 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia pyrrocinia].
ACCESSION   WP_175962872
VERSION     WP_175962872.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 853)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 853)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 853)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 853)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 853)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 853)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 853)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..853
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..853
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90061
     Region          13..853
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mpahagrfgl rdlirqaarm tardwragel tllvlalvla vaaltsvgfl adrlrqgler
       61 darqmlgadf vvradrpvdl sfdrqaralg lrtattaifp smiasaaggq tadaaparla
      121 avkavspgyp lrgaveilpa gaaaahkata ipapgtvwad palldalhlk agdtvrvglr
      181 tftvaasisr eldrgfsfvn fsprlmmrad elaatgltgy gsrvtyrllv agdaqavarf
      241 etyahervdg gklrgvgles lqegqpqvrq tldrarhflt lvalltalla avaiamaaqr
      301 ymrrhldgca tmrclgvsrr tlgalfalef vgigivsgaa gavlgygghw allaalggli
      361 evvlppptlw paligvgaal vlllgfalpp lvpltrvppv rvlrrewgda srtawaayav
      421 gvvlfaglli aaagdlklgl ivaggfagal vgfalfarlv lfaaaravrn arvaagvgwr
      481 yalaslhrrg tasalqital alglmcllli aitrndlvag wrqstppdap nqflidiqpd
      541 qrddvaayla ahgvrdavpa pmvrgrlvai ngkpvnpday qsdeerrlvd refnlsytte
      601 lpsdnrivag dwfgtaaapq isieaglakm lnvkpgdtlr fdvtgltvda pitsvrkldw
      661 gtfrvnffvl mpprvlkdfp avyltsfhlp asdaalldpl iarypnltai dvapilaqlq
      721 rmmlqvvgav qflfaftlaa gvlvlytala gsrdervrea allralgasr aqvnavqrae
      781 fvvvgvlaga lasagaiavg wvlasrvfdf rlavdpwlvp agiaagvaca gaagwlslhn
      841 vlrrpalqsl rda
//
LOCUS       WP_175962880             168 aa            linear   BCT 11-JAN-2025
DEFINITION  RDD family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175962880
VERSION     WP_175962880.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..168
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18297
     Region          1..164
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 manarapktp aaapsvrrrl aallyegvll fgvvffagla fslatqqrng lvhhnllaaw
       61 ialvvgayfv wfwthggqtl pmktwrlrle sssgrplsag halvryalgw lwflpplalh
      121 pllglsvpvt laltaawiva wagaarlhag rqfphdriar trvvampr
//
LOCUS       WP_175962911             308 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175962911
VERSION     WP_175962911.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34081
     Region          16..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          101..300
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(116..117,119..120,123,127,129..135,229..234,
                     240..241,243..244)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mmhpdlrrld lnlllafdal yrhrsvsaaa helamspsal shalarlrda igdalfvrlg
       61 nemqptvrad diatwagdal damskglara rrfdpaqsdr tfvfaatdyt afavlpafla
      121 riqhvaprlr irvvhsdrki svdelaagri dfalgyhees tadapgiedf dwfsddyvvi
      181 asaahpdirr rltldqylaa rhvvvtpwne argvvdyvld rlglarqvav qlptvlaapf
      241 viaesallmt vpnraaqalr haapirifpa pfeiprytlk vyshakhart dahrwiraql
      301 ldarpgpg
//
LOCUS       WP_175962950             239 aa            linear   BCT 11-JAN-2025
DEFINITION  thioesterase II family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175962950
VERSION     WP_175962950.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..239
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=26005
     Region          1..229
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mrlicfpyag gsaavyrglq allpgievrr helagrgsrl sepavrdmst lidallldld
       61 ncfdrpfall ghsmgaaiav elalrlpaqa qpnlrhlfvs graapgkerp vrrmqalddr
      121 afldalhemg gtpkpvldns elmallmpal radftmieny rpvpgrrlav ditafagrad
      181 eqvpvdsvag wgaettgqfd fhviegdhff mrsemramag iiaarlrrae hialsalqa
//
LOCUS       WP_175962964             270 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia
            pyrrocinia].
ACCESSION   WP_175962964
VERSION     WP_175962964.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..270
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29206
     Region          78..262
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mfamfsklgk vissagserf asdmhallve siplaitrmt ewtldepage vvhvqslgaf
       61 gapgddgrgs gpaahgerqp athsllnriv aacdrqlihi nplmrsgndr evapprgpeg
      121 gfqchlvsck anrryvislh rtashcdfsl hemsflknfa dtllplvewh astrrhgdle
      181 gttmpaveal rqefesrlar aavvlsares evclgllagk mlrelagelg vkestvetyi
      241 kraavklgis grhgltkwmi ddyvpcasaa
//
LOCUS       WP_175962986              62 aa            linear   BCT 11-JAN-2025
DEFINITION  CsbD family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175962986
VERSION     WP_175962986.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..62
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..62
                     /product="CsbD family protein"
                     /calculated_mol_wt=6544
     Region          1..60
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 mnkdqvkgva kkakgkvnev igratgnvkq eikgdaqqva gevqkkygdv keavkkqakk
       61 gh
//
LOCUS       WP_175963024             477 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175963024
VERSION     WP_175963024.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..477
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47855
     Region          34..420
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(40..41,44..45,48,80,130..131,133..135,138,160,
                     163..164,167,291,294..295,298..300,303,331,334,387..388,
                     392,396,412,415..416,419..420)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mserapaldc altaaapphr tslraifptv aaaslgfaiv qldvtvvnva ipslghsfgs
       61 svhglqwivd aytlsfaall ltsgtladrf gsrrlfaygl alfllaslgc alapslaali
      121 aarvaqgvga amilptslal ithacandaa arvkavawws atggaisaag ptlggllids
      181 lgwraiffin lpicaaglwl tlrrvqdsaa artrlfdpag qivavlvlgl ltggiiraga
      241 hgpgdpyaag aliasvvlga lfvaierrvt apmlqlaffr iarvpgvlai gaitnaafyg
      301 lifslslyfq nargftates glalapltii mlaniasarl avrygfratv ivglavslag
      361 yvclwqtlaa htpyallvpg laamaigggi aipaltstml gsvdagrsat asailntarq
      421 vgaavgvaal galvagqgaa ivagtsrafa vaaalvavci vlaarwpgga pdavara
//
LOCUS       WP_175963040             304 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia pyrrocinia].
ACCESSION   WP_175963040
VERSION     WP_175963040.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..304
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=33746
     Region          26..283
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mqnphslpdy llqsdavser farlkardvi ldvrhlgkrf rspqgevval ddisfrthrr
       61 efvcvigpsg cgkstliril aglesqtsgd vlldgkpvqg pgadrgmvfq gytlfpwltv
      121 kknvmfglkr ngsssgeaer ealqwldlvg ltrfadvyph qlsggmkqrv aiaralanrp
      181 rillmdepfg aldaqtrakm qahlldiwrn idvtvlfith dldeaillad rilvlkanpg
      241 nvqelievpv prprgysqfn tpefiatkar lealihpept gdasdedavr phmirmtdvt
      301 dnve
//
LOCUS       WP_175963056             505 aa            linear   BCT 11-JAN-2025
DEFINITION  S41 family peptidase [Burkholderia pyrrocinia].
ACCESSION   WP_175963056
VERSION     WP_175963056.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..505
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=53941
     Region          57..421
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mcvvrrlagc aavaavllpc assvgaqpas appaaappaa rppspcppdw epqicelkaa
       61 vevlkkqhlt dvdigallda athdgiktlp yarffnaker qeqldderra rdgtpgigiv
      121 fetrpdglhi idvipdapae kagvrpddlv vamndrsvvg idsselvkla kgdagvplkl
      181 tvqrgpnhaa lsfapvraiv kphpaiakrl dgdilytrls sfpepavgdf idavqaarra
      241 gppvkgmild lringggaln aaigiaalft grdrtamvtv ergdthrrrf stnwpdyelp
      301 vmhgqdplap lqaddwwrtv plvvlvdgqs asaaeataaa lkdlgrakll gmptygkgla
      361 qtgvdlidgt rlnftfarnl rpngcpmdgy gvvpdwlvpp rrdsdvdgvl lwyrevdlar
      421 apyadrlapd pfapvrkerq klrearvrak vdtsksaalp qrafgtaddw qlqqalaala
      481 grpvrtvdap aqlmpaqpvc erggn
//
LOCUS       WP_175963183             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175963183
VERSION     WP_175963183.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33348
     Region          8..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(104,108,151,165,167,226,243,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(105..106,110..111,113..114,117,121,123..129,194,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mddflsphla lfvdvvdqqs fsaaarrlgv aassvtrrid rleaqlgirl lhrtthalrp
       61 teagqllygr alrmlaelrg lqedlhsqhd epsgllrvdc papfgrlhlm avlaafmqrh
      121 palqvdlvlt dsmvdlqgar lgsdvdlavr igpledtrfv atvlapqrrv lcasaaylar
      181 rgepespdal aghdclawhg apppgawrfg drrhvpaqpr frsnhseall eaaidglgla
      241 hlptwlagda lrdgrlravl pqyaaapeha tihvlrqqar gsarasrlva flatwfaqpa
      301 wdaawa
//
LOCUS       WP_175963191             898 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175963191
VERSION     WP_175963191.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..898
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=97851
     Region          14..814
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnvtelaqai rggliqqdrl lkadipslpn nalvprravt hselgrdfsv tldlvstasd
       61 ielktliaqp itlwiqqanq sylpingyih tarrlgadgs lssyqltfss wmhflkfrsd
      121 mrywqdqsvd ailadvfdah pqakgryqfa lskplpsrsy crqsetdwnf vhrlmedegl
      181 fgfwrhsedg sahtlvitdd lhavdelspn lvrfdrsgtg setagftqwa asrtlqsslh
      241 ttrtfdyksp ssaanpngtt lptkagqgdl pnqteiyeyt gaytyagqdr gehlskirle
      301 ewesrakrff gvggvrgida grrftladhp ehdrdaaqdr efaalkvsry iennlpisdh
      361 eanfphslqd rlarvkaghg daaafevghd dgsagfylve veaqraavpy rspfehrkpa
      421 mqletavvvg pkgeevytde lnrikvmfvw drqsdgrena scwmrvvqsd tgggyggvhi
      481 prvgeevmig yiggdcdrpi vmhrvyngaa kpqwhsdgil sgfrskeyag sghnemvldd
      541 atgqnrarlf sssansllhl gylieqsgnt rgaylgsgfd lrtdaygavr aaqglyvtth
      601 pkqansqpld vseaqqqlan adgllesmsq vsemhqaesl gtghdalkqf tdatknsvag
      661 assggrtagg gtgsanafke pvmlfaspag igmasqqsth laadrhvnlv sgqstiiasg
      721 ksliasvadk isffvqnagm klfaakgkve vqahmgdiel taqkavkvls atenieiaak
      781 qeilltsgga yikikdgeik ihapgkidfk ggahsfsgpa qanypfphlp inhlydrpvw
      841 vvddqgfsip drpirvhlkn gktiagktdh dgvaqlaisd qadilrieil kklsgkni
//
LOCUS       WP_175963313             257 aa            linear   BCT 11-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175963313
VERSION     WP_175963313.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..257
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28571
     Region          12..248
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mssplqsesi raqvaelrer gfvvarglvg eqqcaalkri aerqlqeaae piefeadlry
       61 pgapeskhap gghtvrrlld aysrdpafae raiapeigaw mreyfgeepv lsrahhncmm
      121 tkhpaygslt gwhrdfrywa fersdmvsvw lalgpetnen galwlvpgsh taefgpeafd
      181 dakffrsdlp enrkmidaat cpslqagdvv ffhsntlhsa gqnrsnqvkf slvytyhgas
      241 nrpvpgtrsa akpevqf
//
LOCUS       WP_175963345             319 aa            linear   BCT 11-JAN-2025
DEFINITION  complex I NDUFA9 subunit family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175963345
VERSION     WP_175963345.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Parey,K., Wirth,C., Vonck,J. and Zickermann,V.
  TITLE     Respiratory complex I - structure, mechanism and evolution
  JOURNAL   Curr Opin Struct Biol 63, 1-9 (2020)
   PUBMED   32058886
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Babot,M., Birch,A., Labarbuta,P. and Galkin,A.
  TITLE     Characterisation of the active/de-active transition of
            mitochondrial complex I
  JOURNAL   Biochim Biophys Acta 1837 (7), 1083-1092 (2014)
   PUBMED   24569053
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..319
                     /product="complex I NDUFA9 subunit family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0010257 - NADH dehydrogenase complex
                     assembly [Evidence IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=33964
     Region          5..278
                     /region_name="NDUFA9_like_SDR_a"
                     /note="NADH dehydrogenase (ubiquinone) 1 alpha subcomplex,
                     subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs;
                     cd05271"
                     /db_xref="CDD:187579"
     Site            order(10,12..15,34..36,74..76,93,116..118,129,133,
                     156..159)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187579"
     Site            order(129,133)
                     /site_type="active"
                     /db_xref="CDD:187579"
ORIGIN      
        1 mdrqtvvllg gtgfigsrlv nalidagkhv rigtrrrdha rhlqmlpvei veldaldtrt
       61 larfvagaha ainlvgvlhg grgtpygpgf erahvalpav lasactevgv rrllhmsalg
      121 adshgasmyq rskgdgeaal haiaatdsle ltifrpsvvf gpgdsflntf anlqrtvpvl
      181 plampdarfq pvfvgdvvra fvntldlaaa hgktyelggp tvytleqlvr ycgtlvgrqa
      241 rivrlpdala rlqasvfecl pgepvltrdn lasmsvpnvl sgplapelgi spaslesiap
      301 aylgkaaars rfdwfrsrr
//
LOCUS       WP_175963376             372 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia
            pyrrocinia].
ACCESSION   WP_175963376
VERSION     WP_175963376.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..372
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40310
     Region          181..362
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mqrdhligdl yeaalrpdgf levfhqvses lganvfhmfs wdsarnapqf siyspraele
       61 svvalydqyy galdprrsfv eqaplgqfvc cqdhlteqdv arseffqdyq ipsgirylmg
      121 vrlarpggdd illgllracg rppyspeera alsgmaghlq rainlwqdan vlhrdaalga
      181 elmeelglav faldrharvv fvnraaesml rattclkleh ghlsaasaph ndalkaalar
      241 vaktrngesl alagsldgah eiflgiaala gpalhaafgg atmlvtarqr saaplvvaqq
      301 lrqafglssa eaavaealig gktpeecaas arvslatirt qlraiyekth srnqaeavgr
      361 mlwvlprrpr en
//
LOCUS       WP_175963404             210 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia pyrrocinia].
ACCESSION   WP_175963404
VERSION     WP_175963404.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..210
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23047
     Region          1..210
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mtrvlyiegs pnkahsasid vcqafldayr hahpdheirk ldiwdlampe fdaaalaaky
       61 aglsgtaltp eqaaawqqie qlaapfhead kflfgvplwn fsipyklkhl idaisqkdvl
      121 ftfdgsgfag klagkkaavv yarglsyesp gsftpaaefd lqrpymetwl kfvgvkditg
      181 ivvertlfgp dgkvdrsrai dearaiaraf
//
LOCUS       WP_175963415             190 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter small permease [Burkholderia pyrrocinia].
ACCESSION   WP_175963415
VERSION     WP_175963415.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..190
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=19840
     Region          37..185
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mtrrtslnga atagspaaap dgaaparpha apflrcvndv lfrvlavias aclavltvlv
       61 fyavvmryvf enapdfvepi alllviviam fgaamkvrdg ghigldslvr rlppnartvv
      121 vaiqhvslia faiaimvgcg smaaetmgdr ipiiglpegv rylitmpaav aiilfslehl
      181 lalrrsssgq
//
LOCUS       WP_175963463             302 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175963463
VERSION     WP_175963463.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32791
     Region          8..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..295
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(106,110,149,163,165,230,247,274)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(107..108,112..113,115..116,119,123,125..131,192,
                     223..224,226..228,235..236,239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 marrfdhlgd veafvtviek gsmtagaval gstpsvlsra itrletrlgv qllrrstrrl
       61 sltehgrlyl eqsraafali ddaeraiqgh ggtltghvrl svpttyghyr lppvlrrftq
      121 ehphvrveln ianrnvdlva egfdlairlg elpdsglvar kledaalclv aspgyvaaag
      181 mpenvadleq hlclpfmlps sgriapwvfr egdhdvdwlp psnvavsddv lgvvsmalsg
      241 agicqtydfi vqdrirdgkl vevlprlrgr trpfsviyap hrrlsaasra lidmliasaa
      301 aa
//
LOCUS       WP_175963480             234 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            pyrrocinia].
ACCESSION   WP_175963480
VERSION     WP_175963480.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..234
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24458
     Region          51..173
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkkrlepaph dvsapvepar aaaarasees sapvaaaaag vrrkkapdlv raqllaaase
       61 iathhgvaal tldavaerag vtkgalqyhf ankqglldal fgqaterfaa qmaarttadp
      121 ggdgaaaray lhavldaanp aastdvlrvl vasmiteqet rarwsvpmre wtrpdplple
      181 raatlmicrl aadglwisel ldsvevsael rseivrqlda mskgvfpkes ggaa
//
LOCUS       WP_175963484             225 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175963484
VERSION     WP_175963484.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..225
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24904
     Region          1..206
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mkiisgplsm fgakveiaah ekgidfelvl apfsqlrgyd pkhpdvlrin pkrqvpvlmd
       61 gtleifdstq ifeyledlkp dpalwpahpa araiarqleh csdeiyfphv irlmgleatp
      121 ddpaaqaara easeyyrrme hvlenrefla gtysyadiaf ymaqlfgarr gapmtaetps
      181 llawrarmta rpavrkvaga magylasige avpdflcgld qvslr
//
LOCUS       WP_175963632             244 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175963632
VERSION     WP_175963632.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..244
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26542
     Region          14..244
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 metgwselap dplsdtplyl qlarnlasai hggawragea lpserllsvs vgvsritarr
       61 alallveqgl itrargagsf itprvadpls rlvgftakmq qrgfmpdsvw lsrrlraasr
      121 deivhlglap gatvarlerl rradgivmav ehstlpaavv pdpqalgasl yeyleargmv
      181 vvralqhfra vnatreiakw mavkpgaall vitrigygad qraievtesy crddyydfva
      241 elkr
//
LOCUS       WP_175963683             786 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia pyrrocinia].
ACCESSION   WP_175963683
VERSION     WP_175963683.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 786)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 786)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..786
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85353
     Region          68..768
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mssnfaarss rgrlalacaa afawpaahaa spddarndpa rsgtdrsvga apasavaaas
       61 aatagdtlta vsvtaqrqpv dpdtpavves itreqidtht nvttedalky apnlmvrkry
      121 igdrnsvfag rdfnelqsar glvyadgvll snllgssyay pprwslippd diarvdvlyg
      181 pfsalypgns igstallatr rpekleasls tqfftqryhd gygfadsfgg nhqtarvanr
      241 vgrfwfalsl drlenngqpm qyaspnpayn pklgaavpvt gaatdigpng kprtivgaqt
      301 ierteqlnet vrmgyaftdh vdatltlghw enhyrqhget flrdaagnpv yggnvsiggr
      361 nmtiapnafa pqrgdqenwl yalglngrld sgwrlsgvvs aydvsrdvlr aastvqggag
      421 tlfqgdgtgw rtldlkaeap evkghtftfg yhydnyflrn vtyntadwla gpttslssvy
      481 rgdtrtqalf gqdawrfapg wlatlglrye rwdayggalg natgtlgyad rganalspkv
      541 alqwdatevw rfrlsfatgt rfptvgelfq gtisnnaivn nnpslrpeka idwdftaerd
      601 vgvgvvrasv fqsdlrdsiy sqttvsgast vtnisnvdrv rvrgvelafg genvglkgla
      661 idanvsasna qiladaanpa yvgsrfprip rmranllasy rfdehwlasv gvrysgrqfn
      721 tldnsdvnpd vyggtssftv vdlkaryrfd rhwtasvgid nltdrryyvf hpypgrtfyg
      781 elkwsl
//
LOCUS       WP_175963694             226 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175963694
VERSION     WP_175963694.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..226
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24912
     Region          10..225
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mnaltdvird rpaasaisla drayaliqrd iitmrlkpga alneadlvar tgigrtpvhq
       61 avhrlvlegl lsvmprkglm vqplslddiv avidvrrine ahcaelaarh atpddlarma
      121 aqlddgqacv dthdvegmme ldrafhqaia aaarnavlae ilralhersl rfwfvtlsep
      181 hhladvqheh relferlsar daagaraave rhidsfrstl lqhlrp
//
LOCUS       WP_175963717             315 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Burkholderia pyrrocinia].
ACCESSION   WP_175963717
VERSION     WP_175963717.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..315
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31901
     Region          2..314
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtilviaehd nasikaatln tvaaaaevgk fvggdihvlv aghnaqaaad aaakiagvsk
       61 vlladapqle aglaenveat alniakdysh ilapataygk niapriaakl dvaqisdita
      121 vdsadtferp iyagnaiatv qssdpikvit vratgfdpva aeggsasvek ieaaadagks
      181 qfvsrevtkl drpeltsasi ivsggrglgs genytkvlep ladklsaalg asraavdagy
      241 vpndyqvgqt gkivapqlyi avgisgaiqh lagmkdskvi vainkdpeap ifsvadyglv
      301 gdlftlvpel vaelg
//
LOCUS       WP_175963804             408 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: patatin-like phospholipase family protein
            [Burkholderia].
ACCESSION   WP_175963804
VERSION     WP_175963804.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..408
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43796
     Region          1..291
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mrlalvlmgg garaayqvgv lkalaeiale adpdrhtlpf avvcgssaga inatsiasha
       61 ddfshgvrrl lefwehlrpd yvyrtdwlgi aaagarwlat mtfgwaarrs prglldntpl
      121 ahllqrelsf hrieqmlear llhalavtal syssgrhltf yqaaepiqaw rraqrtarlv
      181 dlsashllas saipfvfpav plvldgqiey fgdgsirqia plspaihfga hrivvvgaad
      241 prpeipaang agrvrgypsl aqigqqvlas vfldsigsdi eriehinrmi ehlphqvevd
      301 sgwrhvdvla iapserieli aakhlkqmpa amrgllgavg gsqpagasfa syllfeeaft
      361 relielgygd graqrdtlag wiaqadggsa paagtppedg latgeirv
//
LOCUS       WP_175963827             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175963827
VERSION     WP_175963827.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33742
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..286
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdllaamrif vrvvergnls raakdlglgq ptvsdrvdrl erflgvklll rntravsctd
       61 egilfyqrsk ivldaadear avvtlgnkiv rgririaaph gfgevvlpei lavirehnpq
      121 lyidlvlnde itdpvtegvd islrlgqigd gnfvarrlgy vrrvlvaspl yiekhglpee
      181 ptdivghpfi rvtglfndgq lrlmspsksv rptpinvvis tshwrpvyel llngagigvl
      241 qehvcidale sgrlvrllpd ytvpgfdlha llpvtrpvps ktqvvvkiie eylpkamara
      301 angaldm
//
LOCUS       WP_175963886             329 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH:quinone oxidoreductase family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175963886
VERSION     WP_175963886.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Shimomura,Y., Kakuta,Y. and Fukuyama,K.
  TITLE     Crystal structures of the quinone oxidoreductase from Thermus
            thermophilus HB8 and its complex with NADPH: implication for NADPH
            and substrate recognition
  JOURNAL   J Bacteriol 185 (14), 4211-4218 (2003)
   PUBMED   12837796
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..329
                     /product="NADPH:quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=34101
     Region          1..322
                     /region_name="QOR1"
                     /note="Quinone oxidoreductase (QOR); cd08241"
                     /db_xref="CDD:176203"
     Site            order(40..41,122,126,147,150..152,171..172,176,191,215,
                     237..238,240..241,262..264,314,316,318)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176203"
ORIGIN      
        1 mkallctafg pidrlriedv aipepaagqv riqvkaasln fpdalivqgl yqvkpalpfs
       61 pgaefagvid avgegvsawr pgdsvvaftg hggfaqqcva dvhqiaalpp gmtfeqgaal
      121 vlaygtslha lqqrarlqqg etllvlgaag gvglaaieia kalgarviaa assadklalc
      181 raagadetid ystedlrrrv deltggrgad vvydpvggay seaalrataw hgrflvvgfa
      241 ageipkialn lallkerdil gvfwgdavrr npaqhvanmh llaewfaagk vrpaitervs
      301 lagaadaiar manrqvkgkv vilpdagps
//
LOCUS       WP_175963888             774 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia pyrrocinia].
ACCESSION   WP_175963888
VERSION     WP_175963888.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..774
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81541
     Region          <68..>194
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          203..764
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msapelsvrn esrralllgf asgglllafg vpslaraaap vqppvsanpq yggagmphgl
       61 rddphlfvai apdgtvtvtc irsemgqgvr tsvalvvade lgadwarvkv aqavgdepry
      121 gnqntdgsrs lrqsfaalrr agaaartmle qaaamawgvd alqvkvtvhe vvdtksgrkl
      181 gfgelaakaa alpvpdpatv mlkapaefry igkgktalid grdivggrah ygidtrldgm
      241 lyavvarppa ygdtvasfda saaeklpgvv kvvqlastal psgfqplggv avvardtwta
      301 iqaraqlkid wkhgpnasyd saayrktlea aaaqpgdvir ndgdaaaala gaakrvraty
      361 yiphlahatm eppaavarva dgrcevwtct qapqttrdei akalglpteh vtvnvtllgg
      421 gfgrkskpdy vveaallska vgapvkltft reddiahdyf havsleafdg gidasgkvva
      481 wqhrtvapsi qstfragvvh eqpgelaqgi adlpfaipnv rienpaaqah trigwfrsvy
      541 niphafgvqs fvselahaag rdpkdfllel igparrfeph itvknvnyge dpalypvdtg
      601 rlrrvvetva reagwgrklp kghglgiaah rsfvsytaav cevqvgadgk lsvprvdiai
      661 dcgpqvnper vrsqlegavv mglgialhge itfkdghpeq snfngfqvlr mneapreirv
      721 hlvapddfat plggvgepgl ppvapaltna ifaatgtrir slpvadqlak pqag
//
LOCUS       WP_175963900             265 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia pyrrocinia].
ACCESSION   WP_175963900
VERSION     WP_175963900.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..265
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=28304
     Region          11..>184
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(89..90,92..93,97,100,109,111,113,117..118,121,
                     123..124,126..127,131,134,143,145,147,151..152,155..157,
                     159..160,164,167)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          111..143
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          145..174
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mssnspskyf dgsylsaaka isdgdvaqlk svlsgidvnk pgrqemtllw faistknfpa
       61 iseliargsk pdaqiveglg samyftitne dtrylkamld gglspdtvds dgtsllqram
      121 egngamervr llvehhanin hrdsiggtal dsaldvgkpd iaiflvehga dvnahttngv
      181 svaysvqkdi dalqpgakqa tvtdisldke gqpvrttqtp papglspegk erlekferlr
      241 tlmiakgakf ppdppakvre qmskk
//
LOCUS       WP_175963902             703 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            pyrrocinia].
ACCESSION   WP_175963902
VERSION     WP_175963902.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..703
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=78106
     Region          11..703
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mqmseiasff qlqsnrlfti etplkgrsdl vlvdfhcteg lsqnfethvr lasqdkniel
       61 kkligqpvti tlqltdalas seeryfhgyv aafshldtdg gfamysatil pwlwmlsrrq
      121 dirifqeent eailsrvfre ygklasfefr lskgtknrsy ctqyretdla fverlmredg
      181 lfyyfehakd ghkliiadns vtakpidgrs pslqynqdep ldnlavvtsf qaqrhlapst
      241 vglktfdyki pqarrfasgg tevnqgevps yeiydylgeh gfadsdrgee ltrfrteala
      301 ahsktfsgat tsrrmmpcry felddhydhg stkqedrqfl lltvshtgtn nyepgegssa
      361 yscsftcirk kipyrpafeg erptivgpqt aivvgpkgee iytdslgrvk vqfhwdrlgk
      421 rdqgsscwvr vsqpwagsgf gmvqiprigd evvvsfldgn pdrplvtsrv ynsqnmppwe
      481 lpanatqsgi ltrstktgnv ntanairfed kkgeeevwlh aeknqrieve hdeshwvgnd
      541 rsknidhdet vhvghdrtet vdnnetihig vdrtetvgnn etltvggnrn etiqgmenll
      601 ialtstetvg lakaltvgga ytvtvagain taaglasaee vglskttmvg ktytvtagdr
      661 ielrtgkasi vlessghiti sgtsidilgs davkvdgktv dln
//
LOCUS       WP_175963919             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175963919
VERSION     WP_175963919.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46185
     Region          22..420
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,150,
                     153..154,157,245,248..249,252..254,257,285,289,347..348,
                     352,356,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 msehqtvpha pprirrgqri alallmasgi vnyldrgtla vassairgdl glslaqmgll
       61 lsafswsyal cqfpvgglvd rigprrllgi glivwsfaqa aggivstfgw fivarivlgi
      121 geapqfpsaa rvvsnwfplr srgtptgifn aasplgtala plllsilvaa fdwrwafiat
      181 gaaglvvavv wfalyrdpvr aqltvdersy ldadaqsvva apkltfgewr slfshgttwg
      241 mligffgsvy lnwvyltwlp gyltmerhms lirtgfaasv pflcgfvgsl vagwlsdvvt
      301 rrsrspvvsr rnavvvamlg mvaftipaal vqsnavalac isvviflana asasswalat
      361 aaappsrvas lgaiqnfggf iggalapilt giiaqkwsfv palltaaaia fagamaylll
      421 vrkpipeqaa naahgplpa
//
LOCUS       WP_175963948             310 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia pyrrocinia].
ACCESSION   WP_175963948
VERSION     WP_175963948.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..310
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33483
     Region          30..285
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(45,131,133,135..136,165,219,240,243,254,256,285)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 msqttrnvqp vianlgkegs gelvpsryav rvgnvdvvli sdgvlplpts tmstnvsead
       61 rnewfdgrfl qrdmfdwaln ialvrsgdrl ilidsgvgdg feyftragqs vmrlesagid
      121 latitdivit hmhmdhvggl nvdgvkaklr pdvrihvsaa evafwknpdf sktvmpetvp
      181 palrkaaakf velygenivq fdqtvevaag vsarvtgght pghcvvdvas ngekltfvgd
      241 aifevnfdnp ewqngfehdp easvdvrial ldeaaetgal laaahvafps ighiakngkg
      301 frfvpvlwdy
//
LOCUS       WP_175963964             343 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia pyrrocinia].
ACCESSION   WP_175963964
VERSION     WP_175963964.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..343
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37666
     Region          70..299
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 makdtskdkk ptgnlhlaag llrglaqena aletrlpepp aapnvvdatp tavppaavap
       61 agtpdlgapq kvlvkdcipn pfnprvfyse sslhelaltl kregqiepik vtrlpefpgk
      121 lvvidgqrrl ratsingdet inatfrtdht peqlytiayr anhdherqti fddavawkrl
      181 ldekvfqdqn tlaekigkdk asisktlsln alpntllerm asandvvglq aayflklife
      241 rlgeptadrl ltavidrkks vrdlenflra qsddnkkagr trysvrhdfa lesqaigqlk
      301 typdgrldlq lkgvdtshqe aladrlktvi dayvaelaaa tqk
//
LOCUS       WP_175964003             441 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia pyrrocinia].
ACCESSION   WP_175964003
VERSION     WP_175964003.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47608
     Region          33..435
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(46..47,50..51,54,86,136..137,139..141,144,164,
                     167..168,171,267,270..271,274..276,279,307,311,361..362,
                     366,370,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mrakypappv pgemlqrdda qtfeaatyak varrlipflm lcylgayldr vnvgfaklqm
       61 lndlrfsetv ygmgagiffl gyflfevpsn lilhrvgarr wlarimltwa visasfvfvr
      121 sptafyvlrf llgvaeagfa pgvilyltyw fpsarrakal slffmaipla giiggplsga
      181 imhslhgams magwkwlfll ealpsfvlgf aillylddgi tgakwltdae kallarnvsa
      241 daehttahls irsfvadrrl wlmaaiyfcv vlgqygltfw lptiirkagv adplwvglft
      301 aipyacaiia lpligmsadr rrerrfhlav pmliaaagfa tlptlgsvsa sivclsiasa
      361 gilasssqfw slptallggm saaagiaavn cfanlagffs paivgwlndl tgkstagllf
      421 isvaitvgal lvflvprsvn r
//
LOCUS       WP_175964023             290 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175964023
VERSION     WP_175964023.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..290
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32105
     Region          22..264
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mrnpnedpid phssglkkka hyrapalekg ldilellvdr qfgmaqadic ralkrsrsel
       61 yrmmqvleer gyiyrvdryd ryaltmklyf lgqhhaptrs igalvtpllq qfalqtvqsc
      121 yltvfdgdtm vviatagaet ewnlavrvgt rvplhgsavg emylafqded vrsrllrnig
      181 hdveswsqrr sdgalpahrg dghicrpner ipgitdiatp ivdksgsaia ilacpylals
      241 geagamsirq igialcetaq risatvdqrf mqsavempsr epartarrag
//
LOCUS       WP_175964064             176 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175964064
VERSION     WP_175964064.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..176
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=19340
     Region          47..172
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mttlndylaq krdawrakqd aarndpdfka tplkatvral grsgvreiri rdfqvisdsp
       61 pdfagynlgp aspelqlgvl gsclthitli qaaerglkid aievevtgdq hplaqqpgfe
      121 hvpvfphnlr ytldivspep pdairalhqa veavcpifnl lrlpqtidge lrhtra
//
LOCUS       WP_175964072             219 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia pyrrocinia].
ACCESSION   WP_175964072
VERSION     WP_175964072.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 219)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 219)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..219
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23158
     Region          38..123
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          137..216
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mkkrivllav lavagallav ygptllgfyr lqrhidetaq addadggpwp rttdvcmgch
       61 gvrgsslnda ypslagqpaq yvaarlhafa sgqranptms plattmseae ivrvagyyak
      121 qaplanryfk pdarlrakge qlvtggacva chgarlmgqt qfprlagqgy dylraqldaf
      181 angtrseatg tmqrvaqams addraavaty laslspvth
//
LOCUS       WP_175964100             325 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175964100
VERSION     WP_175964100.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..325
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35806
     Region          40..192
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <188..315
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 msaepssarh sslspsprnr krlaallrtl apdegynlta lpsvsilrsn ralsrtpvly
       61 dpgivivcqg rkrgyfgger ylydehhyla vsvpvpfsme tdatperpll alylhldftm
      121 aaelaaqidr egvaehvqap rsmmstpmda amhasvlrfv eamqqpleaa vlgpallrel
      181 yfrvltgaqg samrsalamr gqfgrigrsl rvihadyaqp ldvaqladaa gmsvpsfhsh
      241 fktitqvspm qylkstrlhq arllmvrqdl taeaagyavg ytspsqfsre fkrlfgltpa
      301 ketqrmresf aipeafedav fvssh
//
LOCUS       WP_175964109             174 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia
            pyrrocinia].
ACCESSION   WP_175964109
VERSION     WP_175964109.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..174
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19395
     Region          4..159
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 maqaeldvid rrilailqen grlsnqeiae rvnlspspcl rrirrleeig vitgyvalld
       61 pqklgldlla yvsvrlekrg glapvradet saragathae lfraavqtwp evvachamtg
      121 dmdyllrvqv edmahfsrfv qehllhhpsv idvktsfsle cfkettalpi rsvr
//
LOCUS       WP_175964119             213 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia pyrrocinia].
ACCESSION   WP_175964119
VERSION     WP_175964119.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..213
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22664
     Region          1..213
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mnlhtwwlfv atvfvvsaip gpnmllvmth garhglrrss stmagcltal vlmlsvsaag
       61 lgvfleawpa mfnalrfaga ayliylgvka wrarvgdaps aadvetvsrq aasasrwvlf
      121 rngflvagsn pkailfaaal lpqfinaaep tlpqfgvlvv tfavievswy lvyasfgtri
      181 gatlksqsva kifnrltggl fvgfgammal vrh
//
LOCUS       WP_175964124             384 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia].
ACCESSION   WP_175964124
VERSION     WP_175964124.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..384
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41335
     Region          18..184
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          128..382
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 myvlkliarn alrhrlrtll tvlgltiavl afgllhtvvd awyagaaaas sgrlvtrnai
       61 slvfplpvsy enrirgiegv tavvrsnwfg giyrdpknff asfavsenyl dlypefiipa
      121 qqradynrdr rgclvgrqla tqfgfrigdv iplkgtiypg twdfvvrgil dgrddstitr
      181 qlvfhwdyln etvrqrtpkq adqvgvfvlg vanpddgati arnvdavfkn slaetltete
      241 qafqlgfvam snqiiaairl vsyvviliim avmanamams arertaeyat lkalgfgpgf
      301 lalivfgesv viavaggglg ilatppaasl fkqaagsifp vfrvsaetvv lqaacsvavg
      361 vaaaivpawq aarvrvvegl raig
//
LOCUS       WP_175964125             388 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia pyrrocinia].
ACCESSION   WP_175964125
VERSION     WP_175964125.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..388
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41402
     Region          19..227
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          143..387
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mtipltyiar nlwtrrltta ltaggmalvi fvfatvqmld agltqtlvst gepdnavvir
       61 kgaeteiqss idhqqanale mhpavalgpd grplvskeav vlislvktss gkpsnvvirg
      121 vspsglalrp hvklvagrmf vpgsseiivg saiakgfsst qlgdrlhfaq rdwtivgifd
      181 aggsgfdsei wgdvdqlmqs frrtsyssmv lripsadgfa rfkadididp rltdeakreq
      241 tfygdqskal skfinilgit lstifsiaam igamitmyas vanrvaeigt lralgfkrms
      301 vlaaflleal llgfvggvag lacaslmqfa sfsttnfqtf adlsfrfvlt paivvktllf
      361 slvmglvggf lpamraarlk ivdalraq
//
LOCUS       WP_175964141             230 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia pyrrocinia].
ACCESSION   WP_175964141
VERSION     WP_175964141.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..230
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24206
     Region          1..227
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mtaqwidipt gndsfggyla lpkrgkgpav iiiqeifgvn shiravadqy asdgyvalap
       61 dvfwrtqprv eltyegadrd kgiellkktd vglavadiga aadalrarpe vagklaaigy
      121 cfggqlayra aaagkldaav ayygggiqna ldlagkvtqp ilfhyaendh giplaavdqv
      181 kaafagrgha sfhvypgaeh gfnctdrasy nqraaalahg rtltflaehl
//
LOCUS       WP_175964168             212 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia pyrrocinia].
ACCESSION   WP_175964168
VERSION     WP_175964168.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..212
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22319
     Region          1..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mslsallafa lilsvgvatp gptvllamsn gsryglrham vgmlgavtad vvlvvlvalv
       61 glglgvllda setafvtlkl lgaawlayvg irmlmssghs taaqepehpt pgrrtaflks
      121 ffvamsnpky ylfmsallpq fvdrshaiap qyailaativ aidvigmtgy allgvhsvrv
      181 wkaagerwln rvsgslllml agyvalyrkt tn
//
LOCUS       WP_175964247             120 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia pyrrocinia].
ACCESSION   WP_175964247
VERSION     WP_175964247.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..120
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=12133
     Region          48..>112
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mnktrhfstl lavgaaflls aaplasayaq dtsadngngn gmqaesnqpv tdtwittkvk
       61 tqlastdgvk sldigvktvd gvvtltgvlp skiavkkaia vsravkgvkh vdasglkaka
//
LOCUS       WP_175964249             315 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia pyrrocinia].
ACCESSION   WP_175964249
VERSION     WP_175964249.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..315
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34819
     Region          11..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrkfkipnmg alvafeaaar hesfthaake lfltesavsr qiatleaslg vrlfarvkqr
       61 vvltragkly gtqvrralea ldrdtlsiia hgsgggylel avlptfashw lipriksfyd
      121 rtpdvrvnmg srtdlfsfed thfeaaihyg kptwpgtssd ylfgeevvpi cspalldgpv
      181 ervedllayp llhsttrpga waqwfethgv edirtmqgvr yelhtmlisa aaaglgialv
      241 pkffveeqlq qlglvvpcda atvgdsayyl vyptefshsk plelfrgwll eqasayaapa
      301 rdmddvdaed dedve
//
LOCUS       WP_175964394             558 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia pyrrocinia].
ACCESSION   WP_175964394
VERSION     WP_175964394.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..558
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=60294
     Region          1..539
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mtydyiivga gsagcilanr lsesgrhsvl lleagerdas fwfkvpvgft ktyynrrynw
       61 myysepeaql adrelycprg kvvggsgsin amvyvrgqrs dyddwanagn pgwayddvlp
      121 yfrklethaa gaadpqhhgs tgpihitsmk advhpivhef lkgcaqlnlp rtddfngaqf
      181 egagiydlnt kngercsssf aylrpalgra nltlrsgvlv rrvtfdgtra tgvvvagang
      241 detlvaarev ilaagavdtp kllqlsgvgd pallarqrvp lvhalpavgr nlqdhlcvsf
      301 yfkanrptln demgtllgkm kiglrylltk rgplamsvnq aggffcgaed trepnlqlyf
      361 nplsyripks drasikpepy sgfliafnpc rptsrgtiei asnraedaak ihinalttqk
      421 dldeavqgsk viralmrapa lqsmtveeis pgpqvdsdea mlqyfreqsg siyhlcgsca
      481 mgpdaatsvv daalrvhglq alrivdasvf pnitsgnina ptmmvaekga dliladaahd
      541 etagaagtrp rereivap
//
LOCUS       WP_175964586             423 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter large permease [Escherichia coli].
ACCESSION   WP_175964586
VERSION     WP_175964586.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..423
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45378
     Region          1..423
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mswlliiplm ivclflnirv ylamfigiia yflffssvpi eiavqrliap tqspsllaip
       61 ffillgtlms ytgiaerilh ianvlvgkmr gglgvanilv stmmggvsas nladaamlsr
      121 mmvpemerkg ynrafaaait aggslvtpii ppgialiiyg lvadvsigkm fiaglvpgll
      181 cavvlmftvy lvarktnakp sreswptgke vvfslgqawp alflifavvg giraniftpt
      241 eagavavliv laigffiyre mrishvvkal getaratasv mlvimasaal gwifsmehag
      301 vavanfvtsl tenkymflli inillltlgm flegnailli lvpllkpvve hfgidpvhfg
      361 iimifnlsig aftppvgtvm llvcnitqvs vgnffkqslp rlaalllmlm lvtyipaisl
      421 flv
//
LOCUS       WP_175964600             393 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter permease [Escherichia coli].
ACCESSION   WP_175964600
VERSION     WP_175964600.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 393)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468467
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..393
                     /product="amino acid ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=43166
     Region          4..393
                     /region_name="BatB"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG4597"
                     /db_xref="CDD:443651"
ORIGIN      
        1 mshrrstvkg slsfanptvr awlfqilavv avvgiigwlf hntvtnlsnr gitsgfafld
       61 rgagfgivqh lidyqqgdty grvfivglln tllvsalciv fasvlgffig larlsdnwll
      121 rklstiyiei frnlppllqi ffwyfavlrn lpgprqavsa ldlvflsnrg lyipspqlgd
      181 rflafilavv iaivlsvglf rfnkthqikt gqlrrtwpia avliiglpll aqwlfgaalh
      241 wdvpalrgfn frggmvlipe laaltlalsv ytsafiaeii ragiqavpyg qheaarslgl
      301 pnpvtlrqvi ipqalrviip pltsqylniv knsslaaaig ypdmvslfag tvlnqtgqai
      361 etiamtmsvy liisltisll mniynrriai ver
//
LOCUS       WP_175964497             431 aa            linear   BCT 11-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Burkholderia pyrrocinia].
ACCESSION   WP_175964497
VERSION     WP_175964497.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia pyrrocinia
  ORGANISM  Burkholderia pyrrocinia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472037
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Burkholderia pyrrocinia"
                     /db_xref="taxon:60550"
     Protein         1..431
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=48681
     Region          2..132
                     /region_name="TadD"
                     /note="Flp pilus assembly protein TadD, contains TPR
                     repeats [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG5010"
                     /db_xref="CDD:444034"
     Region          28..55
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276808"
ORIGIN      
        1 makrpfrplq klltpaksva rlqarllela adfraalakg dyatgrtlae qalhetpsnm
       61 ailsdyalcl mrtgereqay qvymriynsp pdrqkqasst wldglaevcg wldkrdelrk
      121 fgnesltrad aafrngrqwq lpdgsppafe parpeqnvis yslfgadpry cesavaniha
      181 aaelfsgwtc riylddsvpl hvqqrlrdgg adlvqmkrda gdaippvmwr flvmedpdvs
      241 rflirdadal lserevpavq qwlesdrwfh hmrdyfthte lmlagmwggc tgvfpdiatl
      301 irqyvhdytg parfvdqyfl rttfwptvrn svlshdelfd fhgalvfpsh ppirwrtakf
      361 hvgsnasfqr itgqsglpdg atesvqlsrg eagpwtypai vrggqwelnl pfflvdelse
      421 grlrvecggg r
//
LOCUS       WP_175964669             269 aa            linear   BCT 11-JAN-2025
DEFINITION  KilA-N domain-containing protein [Escherichia coli].
ACCESSION   WP_175964669
VERSION     WP_175964669.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Iyer,L.M., Koonin,E.V. and Aravind,L.
  TITLE     Extensive domain shuffling in transcription regulators of DNA
            viruses and implications for the origin of fungal APSES
            transcription factors
  JOURNAL   Genome Biol 3 (3), RESEARCH0012 (2002)
   PUBMED   11897024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10516234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..269
                     /product="KilA-N domain-containing protein"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29690
     Region          4..110
                     /region_name="KilA-N"
                     /note="KilA-N domain; pfam04383"
                     /db_xref="CDD:367917"
ORIGIN      
        1 mnnlmvidgi evrrdaygry slndlhraav asganartke pgkflssqqt velvheltnt
       61 qnlgvdpvsv ihggnergty vckelvyaya mwispsfhlk virtfdmvts apeklsgqaa
      121 dkmqagvill dfmrrelnls nssvlgacqk lqeavglpnl apryaidapa dapdgssrpt
      181 lslsaplkqy girltanqay hqmaklgive qrerysrtai nnikkfwslt akgcmfgkni
      241 tspanpretq phffesrfpe llklldtvh
//
LOCUS       WP_175964972             393 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acetyl-CoA C-acetyltransferase [Burkholderia].
ACCESSION   WP_175964972
VERSION     WP_175964972.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 393)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..393
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40308
     Region          1..393
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mtdvvivsaa rtavgkfggs lakiaapelg atviravler agvkpeqvse vimgqvltag
       61 sgqnparqsl ikaglptavp gmtinkvcgs glkavmlaan aivagdaeiv iaggqenmsa
      121 sphvlpgsrd gfrmgdaklv dtmivdglwd vynqyhmgit aenvakeygi treeqdafaa
      181 lsqnkaeaaq kagrfddeiv pvaipqrkge plqfatdefv rhgvtaesls glkpafskdg
      241 svtaanasgl ndgaaavlvm saqkaaalgl tplarikaya nagvdpsvmg mgpvpasrrc
      301 leragwtpgd ldlmeineaf aaqalavhkq mgwdtskvnv nggaiaighp igasgcrilv
      361 tllhemakrd akrglaslci gggmgvalav erp
//
LOCUS       WP_175964982             712 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Burkholderia lata].
ACCESSION   WP_175964982
VERSION     WP_175964982.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia lata
  ORGANISM  Burkholderia lata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Burkholderia lata"
                     /db_xref="taxon:482957"
     Protein         1..712
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=77733
     Region          <9..154
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          464..707
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mrtkltvknp kpasptrapv rsgslvarka vrpaappagd kparpkkasp aaggertfkp
       61 raaagaerpg adrapakrap rdggaergtr apyrdnaage gakrsfgdrr tssdrpprrd
      121 ddarprragg eggarapyrd nasgegakrs fgdrrtssdr pprrdddsrp rraggeggar
      181 apyrdnasge gakrsfgdrr tssdrpprrd ddsrprragg eggartpyrd nasgegakrs
      241 fgdrrtssdr pprrdddsrp rraggeggar apyrdnasge gakrsfgdrr tssdrpprrd
      301 ddarprrags seggarapyr dnasgegakr sfgdrrtssd rpprrdddtr prragssegg
      361 arapyrdnas gegakrsfgd rrtssdrppr rndddrprra gaddgkrpsy rdkpagegak
      421 rsfadrparp ardgerrsfg avksaqpvkr aaadvdygde sglmrlskrm selgmcsrre
      481 adewiekgwv lvdgeridtl gtkvradqki eiderasaaq aaqvtillhk pvgyvsgqae
      541 dgyepaavli tranrwsgdh spvrfspqhl halapagrld idstgllvlt qngviakqli
      601 geqsdidkey lvrvrfgerl ididqhfpae slaklrhgle ldgvalkpam vswqngeqlr
      661 fvlregkkrq irrmcelvgl dviglkrvrm grvmlgalpq gqwrylsade tf
//
LOCUS       WP_175964987             117 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein, partial [Burkholderia lata].
ACCESSION   WP_175964987
VERSION     WP_175964987.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia lata
  ORGANISM  Burkholderia lata
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 117)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Burkholderia lata"
                     /db_xref="taxon:482957"
     Protein         <1..>117
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
     Region          <1..117
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 ralaaidlig ldgfenaypr elsggmrqrv gfaralvvdp tillmdepfs aldvltaetl
       61 rtdlldlwtq grmpiksvli vthnieeavf mcdrilvlss npgrviaeik vpfkhpr
//
LOCUS       WP_175965562             430 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Burkholderia].
ACCESSION   WP_175965562
VERSION     WP_175965562.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..430
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46537
     Region          17..419
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(31..32,35..36,39,71,121..122,124..126,129,149,
                     152..153,156,244,247..248,251..253,256,284,288,345..346,
                     350,354,370,373..374,377..378,381)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mqsavvgtvr avasryrwtv callffatvi nymdrqilgl lapmlqhdig wsqvqygriv
       61 mafsafyalg llgfgrivdr lgtrisyala mlvwsiaaml haavgsvmgf afvrallgig
      121 eggnfpaaik ttaewfprre ralatgifns ganigavfap aiipaiavay gwraafviig
      181 aiglvwlavw lvfyrqadtr alaaeydepr deaeamdaan anagaprwge lirkretwaf
      241 ligkfltdpv wwfylfwlpk wlnesrgmdm qhiglplvci yalttvgsig ggwlssmllr
      301 agwsvnrark tamlicaccv lpiafvsqvq slwvavlivg laaaahqgws anlfttasdl
      361 fprravasvv giggmagsig gvlfsevigq vlqrtghywv lfavgalayl ialavmhvlt
      421 pkmkpaqlda
//
LOCUS       WP_175966028             189 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LemA family protein [Acinetobacter].
ACCESSION   WP_175966028
VERSION     WP_175966028.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..189
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22150
     Region          2..164
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mgffvfviip llviitiimi rnsivrhhns tirawsdvas yerqklkild glqplveqys
       61 sfekgtlekv telrqnimnl niqdadiaql qrvenlnkel mrslnvvien ypelkaneiy
      121 lkmmneieeq nenvgaaiti ynrnvelfnn qiqifphnii nnmflkkkav rpfrdqtvsq
      181 nfdyrpnfh
//
LOCUS       WP_175966124             679 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: M3 family metallopeptidase [Acinetobacter].
ACCESSION   WP_175966124
VERSION     WP_175966124.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..679
                     /product="M3 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=77013
     Region          3..671
                     /region_name="Dcp"
                     /note="Zn-dependent oligopeptidase, M3 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0339"
                     /db_xref="CDD:440108"
ORIGIN      
        1 mtlekatlpv pqfdqitlad lkqkiegciq qglqflnelt qtpdtvqeql avlkqvdtle
       61 nnmseswgvl shlnavmnns etrdvyqall pglsdyytql gqhtalyqty qhvqdapvfn
      121 elpeaqqsai klalrdfkls gvalegeakk ryaeisahls qlssdfsnhv ldatqayfrp
      181 lkeeelagls esniellkqy gqqreldqpv atldfpsyla imthaedrgl reelykaytt
      241 rasdqseqte fdntaimeei lklrqemaal lgfnnyaeys laskmapnve avdeflrdla
      301 eharapaeqe vaelkaiaae dgitelkpwd ssyyseklkm qqfnlsqesl kpyfpapkil
      361 qglfsilkrl ydiqvverea pvwhpdaryf eledqgevig gfyfdlyarq gkrggawmsg
      421 frsrmqiaeg lqkpicymva nftppvgnrp allthdevit lfhefghglh hmltevdnia
      481 vagthgvdwd avelpsqfme fwawdqdsln llsehietke vlpadllkal ldarffqsgm
      541 qtlrqlefal fdlsihranp alnaeqiqat lneirekyav lpttpynrfq hsfshifagg
      601 yaagyysykw aevlasdafd rfeeegifnt etgkqfrqki lavggkdtal dafinfrgre
      661 pkidallrhq gwtnrskna
//
LOCUS       WP_175966161             272 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Acinetobacter].
ACCESSION   WP_175966161
VERSION     WP_175966161.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..272
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29747
     Region          8..248
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 mknqtaqdpq slievknlsf krgerviydd vslnirrgqi taimgpsgtg kttllrligg
       61 qltpeqgqvl ldgkdiakma rselfsarar mgmlfqsgal ftdmsvyenv afpirahtkl
      121 pehliaeiva lklesvglrg aeqmmpsels ggmnrrvala raialdpeli mydepfagqd
      181 pivmgvltrl irslrealdl ttiivshdva etlsiadyiy vvaegkiqge gtaeelknhp
      241 safvqqfltg svegpvdyqf shqaylsdev rs
//
LOCUS       WP_175966190             469 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FAD-binding oxidoreductase [Acinetobacter].
ACCESSION   WP_175966190
VERSION     WP_175966190.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..469
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=51903
     Region          7..468
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mnapvaltpe lltqltaivg enriktdads lqnwgrdhtk hfdpnpsviv fpssteqvqt
       61 ivklanqfnv avtpsggrtg lsagavaang eivvsmdkmn qileffpadr mvrvqagvvt
      121 eqlqnyaeeq gmyypvdfas sgssqiggni gtnaggikvi kygmtrnwvl gltvvtgkgd
      181 vlrlnkgmik natgyalqhl figgegtlgl vteaeikler qpqdlqvlvl gvpdfdaimp
      241 vlhafqakid ltafeffgel amqkvlangh vqrpfetecp fyvllefeap fepimdkame
      301 ifehcmeqgw vldgvmsqsl eqvhslwrlr edisesiapf ipykndisvl ithvpafike
      361 idsivnenyp dfeicwfghi gdgnlhlnil kpadlakdef fakcqvvnky vfdtvkkydg
      421 sisaehgvgm tkkpyleytr saeeieymka lkkvfdpngi mnpgklfdl
//
LOCUS       WP_175966379             942 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: type VI secretion system Vgr family protein
            [Acinetobacter].
ACCESSION   WP_175966379
VERSION     WP_175966379.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 942)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 942)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..942
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=106314
     Region          15..822
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mlqsiytvle glglssqkra lhlrfsneil nsqvliqrie grhwineglh aellclsthp
       61 yialkqfigc qvavdqvtdq gklfrttgii taakqghsdg alsvyqltle datslwhkrr
      121 nsrvflnksi kaiseilfte wqkrsglfak slsldlsgln reydvrplvi qsnesdydfl
      181 trlwrsegin wlidekelii pisaqtiqpq vlrlvdeqqy fqalkrrsir fhrshateqf
      241 dtitsliaer qlvpnsvalq rwqaidleqe qnqqlvniqq ssvqdhtsls ledvwnispa
      301 wtsdlkredq atssspaqld qlsqqlshyh amqskyfkas ssvrdaqvgy wfelhdhpei
      361 dqhphneref lilgkhfynq nnlpkdlllq ldqlmqsshw kvldderqgn elylirrdip
      421 vipkyhplqh rpmaypqrak vvgsegetiy vdewgrvkvr flftrsedhq hdggagandn
      481 dtdsawvdvl tpwagegyga rfhprigeiv vidffegdid rpfivgrihe aeryqtmfdk
      541 kgqlpftkkl sgirsqevdg egfnqirfdd ttgqisaqlq sshgasqlnl gnlshpkede
      601 asdgrgegfe lrtdqwgalr agaglllsty kqenananhl dtspaksqle snlnhskals
      661 eiaknqqtdp legldhlkkf ldqieqqdqs kaetfkqalm llcapnsial stnedlylsa
      721 dqqinhsaad ninfstqksl iahaqdkisl faaqqglkav aakgkvelqa qddaietiar
      781 hkvkiisted rieiispkei vltaggsqlk ingqgvfgvt ggkfeckagq hifkegakti
      841 yeipelpksg pyavdflfns lggsgiegae vtmfipenke ilwegktdsn gktqlsisqe
      901 wvayealvgf kqwsnifedl dnkdleeefd vgehgiqied iq
//
LOCUS       WP_175966389             132 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [Acinetobacter].
ACCESSION   WP_175966389
VERSION     WP_175966389.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..132
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=14804
     Region          15..132
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mariaiakiq sltipwqgei shgqhhyltd kpesfggqda gpapydlllg slisctmvtl
       61 rmyakhkdie lgdfqveaef fahkegqewi errlsfdith dsalqqkile icaktpvtkt
      121 llrsleirts li
//
LOCUS       WP_175966392             450 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GGDEF domain-containing protein [Acinetobacter].
ACCESSION   WP_175966392
VERSION     WP_175966392.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 450)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 450)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..450
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52049
     Region          139..409
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 msssneniys manmsfqnst tdrslklaec dlqnrqlied alvhraapip aqfqqyfyny
       61 lyvhrhqnlr qinymaqiaf llyffadifi ipdmfflsgl irvslviavm fccyylfnhq
      121 knirvldmil pvgttvaaat wigllllsss phvstyiyas aifilitnlc vqtefkgaly
      181 csifialfim igvthlmsls qafiftvvft plwafsiyin wnniinirrs flrtlldewn
      241 yqtlknlaht ddltqlfnrr hfvdmaersi hqwpkpastc llmfdvdyfk kindnyghdv
      301 gdrvlqliae itrkemrssd vlarfggeef ialledtqlq dclmiaerir csiqkqvmyi
      361 nsdkkiqfti sigiaelesp qqeledlikh adialyeakk agrnrirvyh pnmlqptkpl
      421 spnpwnvfkp lnkqeqsgah hkakqswsal
//
LOCUS       WP_175966517             232 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DsbC family protein [Acinetobacter].
ACCESSION   WP_175966517
VERSION     WP_175966517.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Shao,F., Bader,M.W., Jakob,U. and Bardwell,J.C.
  TITLE     DsbG, a protein disulfide isomerase with chaperone activity
  JOURNAL   J Biol Chem 275 (18), 13349-13352 (2000)
   PUBMED   10788443
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Chen,J., Song,J.L., Zhang,S., Wang,Y., Cui,D.F. and Wang,C.C.
  TITLE     Chaperone activity of DsbC
  JOURNAL   J Biol Chem 274 (28), 19601-19605 (1999)
   PUBMED   10391895
REFERENCE   5  (residues 1 to 232)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 232)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..232
                     /product="DsbC family protein"
                     /GO_function="GO:0003756 - protein disulfide isomerase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25742
     Region          35..225
                     /region_name="DsbA_DsbC_DsbG"
                     /note="DsbA family, DsbC and DsbG subfamily; V-shaped
                     homodimeric proteins containing a redox active CXXC motif
                     imbedded in a TRX fold. They function as protein disulfide
                     isomerases and chaperones in the bacterial periplasm to
                     correct non-native disulfide bonds...; cd03020"
                     /db_xref="CDD:239318"
     Site            order(35..43,46..73)
                     /site_type="other"
                     /note="dimerization domain [polypeptide binding]"
                     /db_xref="CDD:239318"
     Site            66..73
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239318"
     Site            order(122,125)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239318"
ORIGIN      
        1 mqirnmllal tlfpglsfan vdtvkanlak nspnlkieni qptemkgiys gsmqgqivyl
       61 nedaqhllag smfriqdqhn ltqdlllkqn svdwkklplq daiksvrgtg krqlaifsdp
      121 ncpyckqlev elkklkdvti ytfilplkqq siapskqvyc eknptqawed ligqgiqpks
      181 kkscanpier nkqlaqslgv ngtpaiifsn gfkvigaqpa eqieqgfkef gl
//
LOCUS       WP_175966521             321 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TerC family protein [Acinetobacter].
ACCESSION   WP_175966521
VERSION     WP_175966521.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..321
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=36233
     Region          6..315
                     /region_name="R_switched_Alx"
                     /note="integral membrane protein, TerC family; TIGR03718"
                     /db_xref="CDD:274743"
ORIGIN      
        1 metigtlwly lvffaivavm lvidfvgfkh qhgqevkvrt aaywsiawvs vatlfggglw
       61 lyleqtagaa iantkvmeyf agylleksla idnvfvwlmi faafaippal qrklllygvl
      121 gaivlrtifi figawfvqef swilylfgaf lvytgfkflr gqheedsnie dmailkwlrk
      181 hmritpqlrg dkffvrqngl lwatplflvl ilveasdvif avdsipaifa vttdpfivlt
      241 anlmailglr amffllsgaa skmhylpygl glilvfigfk mlmldvfhmp iwislsfivi
      301 vltvtailsi rhskkhnett l
//
LOCUS       WP_175966708             388 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA desaturase [Acinetobacter].
ACCESSION   WP_175966708
VERSION     WP_175966708.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Nakamura,M.T. and Nara,T.Y.
  TITLE     Structure, function, and dietary regulation of delta6, delta5, and
            delta9 desaturases
  JOURNAL   Annu Rev Nutr 24, 345-376 (2004)
   PUBMED   15189125
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Los,D.A. and Murata,N.
  TITLE     Structure and expression of fatty acid desaturases
  JOURNAL   Biochim Biophys Acta 1394 (1), 3-15 (1998)
   PUBMED   9767077
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..388
                     /product="acyl-CoA desaturase"
                     /EC_number="1.14.19.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016717 - oxidoreductase activity, acting
                     on paired donors, with oxidation of a pair of donors
                     resulting in the reduction of molecular oxygen to two
                     molecules of water [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0006636 - unsaturated fatty acid
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=44777
     Region          3..284
                     /region_name="OLE1"
                     /note="Fatty-acid desaturase [Lipid transport and
                     metabolism]; COG1398"
                     /db_xref="CDD:441008"
ORIGIN      
        1 mnaplpqapi nwvavfalvv lpivaviaip lyayhhdfsl aawismfvll gvsslgitag
       61 yhrlwahray eatlplkiil mimgtfavqn silywgsghr thhrhvddve kdpysinngf
      121 wyahlgwmlr dypaaepnyk napdlqndkv vmfqhkyyvp lviavhaail lpigwavgdv
      181 wgvlllgglv rlilshhvtf finslchmwg srpytdenta rdnfwlaiat wgegyhnyhh
      241 ifqydyrngv kwwqydptkw liwtcsklcl aknlrripsf nikkaelamk fkyaeqdlav
      301 yghnvnedii nvkskiaqey eaftqtlndw aklkeqeiqv kkaavaekih qmddklkvef
      361 qlveqrlshh retlnllvrn lkkapisq
//
LOCUS       WP_175966737             443 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: anthranilate synthase component I family protein
            [Acinetobacter].
ACCESSION   WP_175966737
VERSION     WP_175966737.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Kerbarh,O., Bulloch,E.M., Payne,R.J., Sahr,T., Rebeille,F. and
            Abell,C.
  TITLE     Mechanistic and inhibition studies of chorismate-utilizing enzymes
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 763-766 (2005)
   PUBMED   16042594
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Dosselaere,F. and Vanderleyden,J.
  TITLE     A metabolic node in action: chorismate-utilizing enzymes in
            microorganisms
  JOURNAL   Crit Rev Microbiol 27 (2), 75-131 (2001)
   PUBMED   11450855
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..443
                     /product="anthranilate synthase component I family
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=50187
     Region          40..436
                     /region_name="TrpE"
                     /note="Anthranilate/para-aminobenzoate synthases component
                     I [Amino acid transport and metabolism, Coenzyme transport
                     and metabolism]; COG0147"
                     /db_xref="CDD:439917"
ORIGIN      
        1 mneapyhcpl sfaslqlkdl lhalspldhl iylnnngqpf iaccaqkyfm vqdeqiqsfk
       61 rvdieqyqad iaelileleq tpdikanefy ggyvgfigyd yaarqhtqyp eraqpglfig
      121 qfdsyikfev dqwvfyshdl qaadifnhlq nllnqasipp kfqlktlcss rwdqsryaqa
      181 fqdiqdyila gdcyqinltq eftalaegsl letahafwtl tnapyagylr igdfellscs
      241 pelfidfeah rkivtkpikg tmprfsdpvl deqskqrlkd srkdqaenvm ivdllrndls
      301 vyaetgsvkt pklftiesfn qvhhmvseve atlkegvhpf dvllsalpgg sitgapkira
      361 mqiieelega prgaycgslg yfnfdgtgsw nilirsiqky qdevslwagg gitissdcda
      421 eyqecfdkve amldllntwy kpe
//
LOCUS       WP_175966796             234 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: energy transducer TonB [Acinetobacter].
ACCESSION   WP_175966796
VERSION     WP_175966796.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..234
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24802
     Region          155..233
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 msttfediek ssakkltgig vviflhilvg lvlmagmakd iikpseepve lmiiqdikpp
       61 epeppketpp eppkivekva qvpevkpvek vvpvqktqpt ptvtqpvaep tpvaaatpsp
      121 spvaapapvv aaapaappqp tgvtrgvsqg eagckrpdyp rdalmneeqg nvlisvfvnt
      181 dgkvkdakvk kssgsrsldr aaskafslct fkpamkngep qeswydipye fild
//
LOCUS       WP_175966803             382 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Acinetobacter].
ACCESSION   WP_175966803
VERSION     WP_175966803.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12124374
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..382
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41311
     Region          22..>44
                     /region_name="OppC_N"
                     /note="N-terminal TM domain of oligopeptide transport
                     permease C; pfam12911"
                     /db_xref="CDD:463747"
     Region          <162..378
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
ORIGIN      
        1 mlsaifkkeq hasavpesas tglwqlalrr lkrdriamfs lfvvlfyllm lllsmtgmia
       61 kdwnkevavs yappsfiytp svpgaagedq stesavvpvn pvdplkdvia elkaeiaaeq
      121 gagaidyygv vdplaedmka idqelggqll dqsselkqsl ffgadkwgqd vllktikgae
      181 tsilvgliaa lvavvigtvl gaiagyfggw vddvlnwfyn iftsipylll vlaiaavlqq
      241 kgilsiilil gltgwtgvfr lvraeymkht areyvlaaka igvsnmrrif vhifpnvshi
      301 alvqmsilav afiksevils flgfgvpigv vswgsmlnea qselilgkww qltaasvama
      361 vlvtafsmft dalrdaldpk lk
//
LOCUS       WP_175966306             618 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ferrous iron transporter B [Acinetobacter].
ACCESSION   WP_175966306
VERSION     WP_175966306.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Marlovits,T.C., Haase,W., Herrmann,C., Aller,S.G. and Unger,V.M.
  TITLE     The membrane protein FeoB contains an intramolecular G protein
            essential for Fe(II) uptake in bacteria
  JOURNAL   Proc Natl Acad Sci U S A 99 (25), 16243-16248 (2002)
   PUBMED   12446835
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     gene            1..618
                     /gene="feoB"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0015093 - ferrous iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
     Protein         1..618
                     /product="ferrous iron transporter B"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0015093 - ferrous iron transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=67638
     Region          4..614
                     /region_name="FeoB"
                     /note="Fe2+ transporter FeoB [Inorganic ion transport and
                     metabolism]; COG0370"
                     /db_xref="CDD:440139"
ORIGIN      
        1 msdtlrialv gnpncgktsl fnhltgsrqk vgnyagvtve rkvgnftlps gkpvrvldlp
       61 gtysldatsp deeitrnvvq gkiaeegqqd tflcvvdatn lklhlglvle miqlgrpmlv
      121 vlnmmdearr rgmqintqkl serlgvpvve tvavrtsgve nlknaldknk fsapqtelsg
      181 lngdhhhqia silkdvvnya dqedkrtdfl dkiflhpvlg llslaimmfv vfqavfawaa
      241 pfmdgietff gwlgeymggl iahpllnslv vdgiiagagg vvvflpqili lfffilvlee
      301 sgylpraafl ldklmfkagl sgrafiplls sfacavpgim asrtisdprd rlttifvapl
      361 mtcsarlpvy alliaafipk qtvwgfmnlq glvlfglyma gilsalivsf ilkffhkdks
      421 qhmllmelps yrfpdvknvw iglldrgrif lkrvggiifa lsillwflct fpqppegatl
      481 pdidysfagm lghvmqpifa plgfnwqici alipamaare vvvaalgtvy alsavdedam
      541 seglaalisg ggdlgwsiat glsllvwfiy aphclatlat vkretgswkt vsfmtfylfg
      601 layfmsflty qiashylg
//
LOCUS       WP_175967110            1147 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Acinetobacter sp. FDAARGOS_724].
ACCESSION   WP_175967110
VERSION     WP_175967110.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter sp. FDAARGOS_724
  ORGANISM  Acinetobacter sp. FDAARGOS_724
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae; Acinetobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1147
                     /organism="Acinetobacter sp. FDAARGOS_724"
                     /db_xref="taxon:2545797"
     Protein         1..1147
                     /product="DEAD/DEAH box helicase"
                     /calculated_mol_wt=132558
     Region          278..730
                     /region_name="BRR2"
                     /note="Replicative superfamily II helicase [Replication,
                     recombination and repair]; COG1204"
                     /db_xref="CDD:440817"
ORIGIN      
        1 mhkelieeli tkyldpefrg rlidrglars miwkngilpd naadfsdels ydilsygysl
       61 lslaiksvdn nvsevlrnqa fekaatalmt iiyngetsys nysfhalmca ssyhlahysa
      121 ksysllkkte eylsdnilek slrlllirdf ngllaniplw kislktdldl lindenneld
      181 easthlsyln svlidrylev iyeyidllei gnnsrldsin kklnenisis lkydfledww
      241 iyritfylln dlwertyhkv lpvendnrdw mryryefirq llkknnaeid lwpsqiegak
      301 kavndlenlv islptsagkt riaelcilra lskkkkviyi aplralsiqt eitlmnsfrd
      361 lgntvsslyg glslygyqrq qfsdsdilig tpekvdfllk hdpellndvg livideghmi
      421 gpgerevkfe vliqslvnrh dsdsrrivcl sailpsgkql ddfvswisrd eegkaisinw
      481 rptdlrfgiv ypnsssaafr ldyvlgtqnp fipqfinkit itkrskfpns qqelclaias
      541 kfihenqsil iycplkgsvn slakklieln nkdkldfkei ysdsqyfkna lriadelfgs
      601 nhyivlclkl gvvvhhgslp keyrtalell lknykvklii ssptlaqgln lqvnvvlfqs
      661 ihrmqklipq sefknvigra grsfvdlqgi vlyanydnsn ykakawedli hgkeqlslvs
      721 glkeivinli itllnslnee eiekyyeyiv ntnfgidltl knfeasiqee nelkqwrdkl
      781 nlldysiinl igdkdieife laeqidlalq kslfykqlqe fsdkeqlllk gfvkkraenl
      841 wlkttkesrk qlylsgvsle tidnsnsvie difrdlfliq silkyphlse dpitkyliel
      901 slrifsiqef rhnnalnddd irlilsnwlt gkkyfindki daivnfiekd vsytlvwale
      961 fiksrddmld kflieeetfd fisqaleygm idkcaivlmq lgmssrlqaq nlanylnfsd
     1021 pqqmalwise idldslqdql dseliaslrk ivnrinpfde akiiavlpde pvmwlvddpe
     1081 tylfsnlkli nidsetfils nraetigklk kyidlelikt lhihinddst vdiryqclnn
     1141 hllyrdl
//
LOCUS       WP_175967190             230 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: BON domain-containing protein [Acinetobacter].
ACCESSION   WP_175967190
VERSION     WP_175967190.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..230
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=24578
     Region          29..186
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mvkriaitml cvaslsgcas fisngtgtap vgtengartl gqvfidssiv rtakinlykl
       61 dsrfkqsrvn iesfhgnvll tgqvpdahlk qlaednvksm sdvkavhnfi tvgnqssytt
      121 imqdtavtan trglimkapv vsdskvhvht edgvlyvmgr lnsaeiddln qvlqqvgnit
      181 kivtlidnvd qrsgyntnqn faapasyaqs gveqtpvaid pdtveptdvp
//
LOCUS       WP_175967304             501 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: OmpA family protein [Acinetobacter].
ACCESSION   WP_175967304
VERSION     WP_175967304.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..501
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54311
     Region          377..479
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(381..382,415..416,419,423..424,427,469,473)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mvilmntdli erlksdvtai vlqgetehlf akdqslaqfy pvllsilrar pawieslgqq
       61 lnpkidelfn nnptlkqqfl aqldstapqd eieqtlnrai vptmnflqae agaptaeavg
      121 hlldthadsi qralpvwagp ilaslgvspl agqnlnrapg lasepeaepv lteekkavvf
      181 wpfillviia aiilfffrgc lrdddpdelr naqavseaaa tnpailkist gsqgeivncq
      241 vqmndpkymq ilqneikqif nysigcgava nenyhseftd qdtiptvlrt iqgmpnvsld
      301 wignqvsvra atnseaerla aqirslaknv tvvtqqplnr sdvintanse aeqalasikt
      361 dnvkaldvat alnlqiinfd tastevpevn klvldqaaal lqrapqvilk vkghadaqgs
      421 eaenkvlsvq raqaitsylv qkgvdpaqlq avgmgedqpv epnatpagqf qnrrvtfevv
      481 ntetgivrev dnegvvekka s
//
LOCUS       WP_175967401             156 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [unclassified Burkholderia].
ACCESSION   WP_175967401
VERSION     WP_175967401.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..156
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17579
     Region          1..138
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mdaidrklle llqsdatlpi aelaqrvnls qtpcwkrvqr lketgairaq valcdprklg
       61 vgttvfvair tnqhteewaq rftqavrdmp evvevyrmsg etdyllrvvv agiddydrly
      121 kqliravplf dvsssfameq ikystalpvr dlaepa
//
LOCUS       WP_175967444             206 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: regulatory protein RecX [Acinetobacter].
ACCESSION   WP_175967444
VERSION     WP_175967444.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Ragone,S., Maman,J.D., Furnham,N. and Pellegrini,L.
  TITLE     Structural basis for inhibition of homologous recombination by the
            RecX protein
  JOURNAL   EMBO J 27 (16), 2259-2269 (2008)
   PUBMED   18650935
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..206
                     /product="regulatory protein RecX"
                     /GO_process="GO:0006282 - regulation of DNA repair
                     [Evidence IEA]"
                     /calculated_mol_wt=23421
     Region          61..200
                     /region_name="RecX"
                     /note="SOS response regulatory protein OraA/RecX,
                     interacts with RecA [Posttranslational modification,
                     protein turnover, chaperones]; COG2137"
                     /db_xref="CDD:441740"
ORIGIN      
        1 msdakfskll dydaikqqfg daedsvtpap vesqalpefd pedslfgnsn keqkkpgltg
       61 srlrsyafav ltrkeyskae lieklalyae drnevvtlve elsrenyqsd qrvaeimlss
      121 qkrkgkgpnq ikmklkskki dtaliseelk etdwvqqaye lklrkygpev tkdpklkakq
      181 irflmyrgfe mdaimkaisr kakaea
//
LOCUS       WP_175967508             446 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TrkH family potassium uptake protein [Acinetobacter].
ACCESSION   WP_175967508
VERSION     WP_175967508.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..446
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=48397
     Region          16..429
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mkssnlnqnr ivnlsppsll algflglifi gslllmlpfs hqteiswlea iftatsavti
       61 tglsvvnvge aytpfgqvvi mfllqcgglg fmtfailafm slspklglrq qvmaqesigq
      121 tslkkvsfti kavflyslff eaigtliltl awledypfge alfyaafysv safnnggfsl
      181 fpnslmsfsg qyfvtftism lyiiggigfl vlmdvkqnks wrklspnskl ilttimglnl
      241 safivlwlle asnpqtlalm svgdqalnaw fhatvprssg fyslpmdqms dasslvtifl
      301 mfigggslst aggikvgtfi ivvisvisfl rredeirlfn hsisekttfk alavvcitag
      361 lvmtgfmsll ilepdhdfld llfeavsaac tvgltrgvtg elqpasliil mlmmyagrlg
      421 pltlayliat pkksrlkhpp seiqig
//
LOCUS       WP_175967538             211 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SOS response-associated peptidase [Acinetobacter].
ACCESSION   WP_175967538
VERSION     WP_175967538.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..211
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=24534
     Region          30..188
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mcsnyefpsk srlslldihe eqleldmkth vyplapapii mrgadefeld iarfglipsw
       61 akelkfgrht ynartetvas kasfrhawkn nqfalvpvdt fyepkyidgk shwyaisred
      121 gdpvtvaaiy ddaiiegekv rsfsmltina nqhpfmnqfh npndekrsit vipeesrqdw
      181 lhcnheease fffemwdefi aklrdsrlse n
//
LOCUS       WP_175967541             496 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: amidase [Acinetobacter].
ACCESSION   WP_175967541
VERSION     WP_175967541.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..496
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=54720
     Region          4..472
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mkfeeylqyd glglaelvkn kqvhssells valersanin peinaiiipm hehalqrtqq
       61 dlsgpfagvp flvkdlfqey agyptsygcq glkrigyiae tnaeivnrwe qagivtfgrt
      121 ntpefgikgi tepdawgsck npwnlrhnsg gssggsasav aasivpiaga gdgggsirip
      181 asycglfglk psrgrtpwgp qmseamhgaa iqhvltktvr dsaamldath gedrsslfti
      241 qrphthylev iqqppkklki afntrssidt pvsqdaikav eqtarllesl ghevvedqpq
      301 idgmqlakdf ittwfsqfsy mldeiqkgyp srsgdfelds lalaafgakt taieyiqnlt
      361 nwgqyvtqmn hffddydlyl tpatatvapk ngevktpnwq kpilkallkm nkahllaqgk
      421 lvdqivkenl qwvpftqlan itglpamsvp lywnednlpl gsqfiapfar edlllqlaaq
      481 leqaqpwfdq yskiri
//
LOCUS       WP_175967569             451 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: nucleobase:cation symporter-2 family protein
            [Acinetobacter].
ACCESSION   WP_175967569
VERSION     WP_175967569.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..451
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47254
     Region          24..431
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mteqstnisp eheylgagks aayglqhvlt myggiiappl ivgtaaglea tqiglliaaa
       61 lfvgglatil qtigvkyiga klplvqgvsf agvatmvaiv ttggglsavy gaviiaslig
      121 fflapyfsri irffppvvtg cvitiiglsl lpvavrwmmg gnknapewgs venislavmt
      181 laiviclnls rnasirrlsi llaivlgsvl aylfgfgdfs kvgngawvqf psffafgmpt
      241 felsaiisml ivtlvimtet tadiiavgei vgtqvdseri snglradmfs savapifgsf
      301 mqsafaqnvg lvaitgiksr fvvaaggmil vvlgllpimg rliaaipvpv lggaglvlfg
      361 tvaasgirtl akidyneqkn liivatsiaa gmipiidysf yanfpkwfqt lfhsgisstc
      421 lmaillnilf nhlpmfkskt evpeklaetl h
//
LOCUS       WP_175967603             309 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator
            [Acinetobacter].
ACCESSION   WP_175967603
VERSION     WP_175967603.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35033
     Region          1..>172
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          90..293
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(100,104,143,157,159,223,240,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(101..102,106..107,109..110,113,117,119..125,186,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mqlnalryfv mvattgsfsa takhfqvpss svsrfiskle qeigqqlfyr ntrsvrltdi
       61 gekyfvqike vldtldlane eisgknairg lirintaval grlhisrivn klhdsfpdls
      121 veliltdtfi dpvqegvdia irigslqdsa liarkvcdqk yvlcaspayl ekhgtphspy
      181 eiqnhqclvy kgvsgsqrwy frqqehdtpl liepqgplrs nnaevlvdaa legrgivlfp
      241 twifmedyfk thklvqllpd wistvepysi gihlvspenr irsqkvrtvl dfilkeigdp
      301 pywdnilkl
//
LOCUS       WP_175968191             250 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Acinetobacter].
ACCESSION   WP_175968191
VERSION     WP_175968191.1
KEYWORDS    RefSeq.
SOURCE      Acinetobacter
  ORGANISM  Acinetobacter
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Moraxellales; Moraxellaceae.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Acinetobacter"
                     /db_xref="taxon:469"
     Protein         1..250
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27289
     Region          8..238
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; pfam01925"
                     /db_xref="CDD:460386"
ORIGIN      
        1 mttwllfilg aiiagfvqgl tgfafaliam sfwvwglspl laaplvvfas vwshlislsn
       61 epklphlhra lylpyliagl igvplgtwll niveagtfri flgiflviwc plmllnpqik
      121 liqhsgktad agiglvggil gglggfcgsv psawlmlkql pkeqqryilr hfnfaiqvft
      181 laayllqgsl nqthlpymvv lilavsipai lgarlfhris elrfkqivlg llfssgcfll
      241 ikegidsfar
//
LOCUS       WP_175969450             174 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: gamma carbonic anhydrase family protein [unclassified
            Burkholderia].
ACCESSION   WP_175969450
VERSION     WP_175969450.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..174
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18071
     Region          1..170
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 mtiyklgdta ptihesvfva dtaaiigkvv leenasvwfg atirgdneti svgagsnvqe
       61 gavlhtdpgf pltiadnvti ghqamlhgct igegslvgiq avvlngavig rnclvgagav
      121 vtegktfpdn slilgapakv vrelsaedia rlrtnaktyv errahfkeql vrig
//
LOCUS       WP_175970809             162 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein, partial [Burkholderia sp.
            BCC0322].
ACCESSION   WP_175970809
VERSION     WP_175970809.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0322
  ORGANISM  Burkholderia sp. BCC0322
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 162)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Burkholderia sp. BCC0322"
                     /db_xref="taxon:2676296"
     Protein         1..>162
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          23..>162
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mqsipssaaa rqtqpapaar tqndafvrie nvvkkfgdst avdnvnltia knelfallgs
       61 sgcgkstllr mlagletats grifvdgedl aalppyrrpv nmmfqsyalf phmtvesnva
      121 fglkqegtpk neikervada lalvqmskya krkphqlsgg qq
//
LOCUS       WP_175971150             276 aa            linear   BCT 11-JAN-2025
DEFINITION  YncE family protein, partial [Mycobacterium tuberculosis].
ACCESSION   WP_175971150
VERSION     WP_175971150.1
KEYWORDS    RefSeq.
SOURCE      Mycobacterium tuberculosis (Mycobacterium tuberculosis variant
            tuberculosis)
  ORGANISM  Mycobacterium tuberculosis
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium
            tuberculosis complex.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Mycobacterium tuberculosis"
                     /db_xref="taxon:1773"
     Protein         <1..276
                     /product="YncE family protein"
     Region          <121..261
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 nggaggaggw lfgnggaggv ggaggagttf gvaggdggtg gvgghgglig vgghggdggt
       61 ggtggavsla ragtaggagg gpaggiggag gvggaggaag avttithasf ndphgvavnp
      121 ggniyvtnqg sntvsvidpv tntvtgsitd gngpsgvavs pvtglvfvtn fdsntvsvid
      181 pntntvtgsi pvgtgaygva vnpggniyvt nqfsntvsvi dpatntvtgs pipvgldptg
      241 vavnpvtgvv yvtnslddtv svitgepars vcsaai
//
LOCUS       WP_175972292             311 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Metamycoplasma hominis].
ACCESSION   WP_175972292
VERSION     WP_175972292.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma hominis (Mycoplasma hominis)
  ORGANISM  Metamycoplasma hominis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Metamycoplasma hominis"
                     /db_xref="taxon:2098"
     Protein         1..311
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=33711
     Region          7..309
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mennnlydvl iigagpaglt aaiylarndi nvafieggvp ggkvssqski enypgfsfis
       61 gfelskamlk qardngskfi ygnvkeinsi sdiekevile ngmsikskai iiatgmkeiv
      121 pldvkgieey rgkgvsycvi cdgplyknkp caiigggnsa feessylasi asevhifvrd
      181 giiaekklvn eamsksniyi henstikeil gnekveeiia nvngketkmn iscifpyvgf
      241 kpntafikgk ydeilnsrgf ievnenmetk ipnifaigdv iakdvrqitt atadgtiaar
      301 aisnkidkly k
//
LOCUS       WP_175972407             394 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: type II secretion system F family protein
            [Burkholderiaceae].
ACCESSION   WP_175972407
VERSION     WP_175972407.1
KEYWORDS    RefSeq.
SOURCE      Burkholderiaceae
  ORGANISM  Burkholderiaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Burkholderiaceae"
                     /db_xref="taxon:119060"
     Protein         1..394
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=42544
     Region          2..394
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 msrfrwrgid adgrrrrgtl valdarsale rirrdrivai elievrarws prvrhtdltr
       61 atrhlamllr sglslqpala lvaqhastpl rplfetvlqd itegstlsra lqrhshvfpa
      121 aywrlvelae htgsldtila qladtrdrva aqrarlrnal wyptlilala lglcalllvw
      181 vvptfeqvfa gfgsqlpkpt rivvalsrqw lthgpamvaa gglgiacgml awqrspqfrl
      241 rlhalllrap lvgpivqrtv iarwshalgq vldagialad gfdavdgisg naamdaatrd
      301 iaarvrvgas ladamrastc fppdvvatia laeqagtlgt tladigawnd qlvaerigll
      361 aqlaepliiv gpgaliaalv vamylpiiem gnvm
//
LOCUS       WP_175972371            1027 aa            linear   BCT 11-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Metamycoplasma hominis].
ACCESSION   WP_175972371
VERSION     WP_175972371.1
KEYWORDS    RefSeq.
SOURCE      Metamycoplasma hominis (Mycoplasma hominis)
  ORGANISM  Metamycoplasma hominis
            Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
            Metamycoplasmataceae; Metamycoplasma.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1027)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1027)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1027)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1027)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Metamycoplasma hominis"
                     /db_xref="taxon:2098"
     Protein         1..1027
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=120072
     Region          29..1025
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mekyniiven endtvvseyk plankakdyq teselesqfi smlksqgyey lnihneedli
       61 nnlrqqiell nkinfsdnew kkffnenian knfsikdksr iiqedyrqll trddgshkni
      121 ilidkdnihn nklqvinqye eetgnyknry dvtilvngip mvhielkrrg valkeafnqi
      181 iryqrdsfwa snglyeyvqv fvisngantk yysnttrlqh vnkksdmids ktsksfefth
      241 fwsdsknnpi hdlidftstf fskhtilnil tkyciftsee mllvmrpyqi vavekiinki
      301 nishnykkyg siaaggfiwh ttgsgktlts fktaklasql pyinkvifvv drrdldyqtm
      361 keydklekga ansnrstsil qrqlesndpn kkiiittiqk lsifiknnrn hpvfdkevvl
      421 ifdechrsqf gsmhtavikn fkkyylfgft gtpifaanin ksspeviktt eqafgqklht
      481 ytiinaindr nvlpfkieyi ktidvdksln dkedqkvrdi dresvfldqr riklvveyil
      541 khfdqktrrn sniiyshsis dnldktikrn vsgfnsimav ssiemakkyy lefknqlaqd
      601 pknnlkiali ysygvntees ygglideedn entlqlskpd rdflddaikd ynnmfntnfn
      661 segeqfqmyy kdvslklknk dldmlivvnm fltgfdaptl ntlwvdkklr ehgliqafsr
      721 tnrilndkkv ygnivcfrnl eketdqaisi fgdgeasgiv kiknfvdyyy gyndsqqvhh
      781 ngycdyiqkl nnefpldnwn viseqknkef iilfgkvlkl knilasfdef igkeilnvrd
      841 fqnysskyld ikdefkkiyk eeiasinddv ifetellkty evnidyilqk veefrgktit
      901 einnlrneis lasssspelr skkqliekfv stinnneqdi ptkfqefmel ekkkeldkii
      961 seenldfdkt hkfmdnsfel geiktagsei gdllpkmplf gskgkersik kkavlekfen
     1021 yfqkfyi
//
LOCUS       WP_175972549             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia stabilis].
ACCESSION   WP_175972549
VERSION     WP_175972549.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45728
     Region          21..426
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(34..35,38..39,42,81,139..140,142..144,147,167,
                     170..171,174,257,260..261,264..266,269,297,301,353..354,
                     358,362,378,381..382,385..386,389)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msaspptvah atgsagavsh rrivfasfig taiefydfyv yataaalvig pvffphgsat
       61 aqalsafvtf giafiarpig sflfghfgdr igrkstlvas llvmgvstta igfvpgydai
      121 galapvllcv lrfgqgiglg gewggaalla tehapqgkrg wfgmfpqlgp svgflmsngl
      181 ffalalslsd eqfrswgwri pflvsavlva lglyvrlkit etpafqaald rnervrvpva
      241 tlvtqhwqpt llgalamvvc ytlfyistvf slsygvsalh iprqsflgll cfavvfmgla
      301 tplsawasdr fgrkpvlvvg aiaallsgfa mepllgsgsm plvalfltie lflmgvtfap
      361 mgallpelfp tnvrytgagv aynlggilga siapyiaqll aargglswvg gyvsvaaais
      421 ligvllmret rdsslv
//
LOCUS       WP_175972575             260 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175972575
VERSION     WP_175972575.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..260
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=28523
     Region          28..233
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mthqaheava qangmielsh sfdanrflaa idrdelttla phlqlvhlks gqvlcepgdm
       61 laavylpvtt aislqyvssg gmtlevaeig nesvvcddvi ggsgrmpcra vacrdgfvyr
      121 ldrrvfaaaf daspvirhlv fvcvrllmaq vsqitfcsrh hvlkhqlcrw fllaydrtrs
      181 ieiqvthsml aqmlgvrret vtdaageiqk lglirqyrss ieladldgle rmscgcraiv
      241 rdemkrilsa dsgvpaasra
//
LOCUS       WP_175972578             450 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia stabilis].
ACCESSION   WP_175972578
VERSION     WP_175972578.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..450
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47864
     Region          36..426
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msaslaassp spqppslrll sadepaddah atnddariaa lldqlgpela adaarndvdg
       61 rfphenfarl hragliaqvv prehggagat laqasrivaa varadpatal vltmtylqhr
      121 algradnrwp arvrqavfds avaqgalina lrvepalgsp srgglpetva rrdgdgwrls
      181 ghklystgip alrwlavwar tdepeprlgv flvprdretd darirviesw nhlglrasgs
      241 hevvfddvrl padhavdvra pqawavsaat hadadaqadq qawmvallgs lydavarasr
      301 dwligfvttr apsglgapla tlprvqeavg eiegwlhanr vllddhiart dagaapsvtt
      361 sglvkrtvte hairvveqal klsgnhglsr gnplerhyrd vlcsrvhtpq ddaiavaagr
      421 avleaanrge tkaeaggtsr neaergrnda
//
LOCUS       WP_175972611             299 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175972611
VERSION     WP_175972611.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..299
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32049
     Region          41..290
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mtkmpvslal darratpadv sltdsigats tpldlaaqqa gtqtllrgla ileaiangar
       61 dmraigaalg ttrstthrlv sslvqarylr qvqggyllgp klielgtial eqmpltavar
      121 phlealaeat ldtihlgvrd gddvlyidki pgtrglemrs rvghrmplas tgigkammld
      181 ldpdlwrslf eaarralagv nfkpdnrpet saflqrmahy aaggytfdle eneasircva
      241 apirdasgav vaavsvasti pymphdrmde liplvqrear aisaelgwsp pqgtrrikr
//
LOCUS       WP_175972684             314 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175972684
VERSION     WP_175972684.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..314
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34528
     Region          14..72
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          102..303
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(112,116,155,169,171,235,252,279)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(113..114,118..119,121..122,125,129,131..137,198,
                     229..233,240..241,244)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mqqiaktggr mdrlramrif vqivdtgnfs gaaeslgipa atvtlavkdl ektlgvrlln
       61 rttrsssltq dgatyykvct rvlaeldeae alfhdrvnrp qgrlridvpp svgyrilipn
      121 lpkfrdaypd iqlsigmsdr pvdliqdavd lairvgrled ssliarqlgs fefvicgspn
      181 yfaknpppqt ladlsrhqgv ryfstqtgrq vdwtleidge sraldlidsv avndadaylq
      241 cglhglglim aprfmaephl akgelievls glepkhmpvs vvylqdttrs prirsfvdwv
      301 agvfasilpt gprk
//
LOCUS       WP_175972733             443 aa            linear   BCT 11-JAN-2025
DEFINITION  carotenoid oxygenase family protein [Burkholderia stabilis].
ACCESSION   WP_175972733
VERSION     WP_175972733.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Poliakov,E., Uppal,S., Rogozin,I.B., Gentleman,S. and Redmond,T.M.
  TITLE     Evolutionary aspects and enzymology of metazoan carotenoid cleavage
            oxygenases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1865 (11), 158665 (2020)
   PUBMED   32061750
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Sui,X., Kiser,P.D., Lintig,Jv. and Palczewski,K.
  TITLE     Structural basis of carotenoid cleavage: from bacteria to mammals
  JOURNAL   Arch Biochem Biophys 539 (2), 203-213 (2013)
   PUBMED   23827316
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Kloer,D.P. and Schulz,G.E.
  TITLE     Structural and biological aspects of carotenoid cleavage
  JOURNAL   Cell Mol Life Sci 63 (19-20), 2291-2303 (2006)
   PUBMED   16909205
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Wyss,A.
  TITLE     Carotene oxygenases: a new family of double bond cleavage enzymes
  JOURNAL   J Nutr 134 (1), 246S-250S (2004)
   PUBMED   14704328
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..443
                     /product="carotenoid oxygenase family protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006720 - isoprenoid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48842
     Region          10..439
                     /region_name="COG3670"
                     /note="Carotenoid cleavage dioxygenase or a related enzyme
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]"
                     /db_xref="CDD:442887"
ORIGIN      
        1 mtvfdlnsga iapvadevdl vdlrvtgsip reldgallrn gpnppggrfe ghdmlswwpe
       61 aamlhaiafe ggratgyrnr wartqrwaav hapeqaphlp dtnpnvnvlq hagellamae
      121 ggaplaitag ldslgvsrrh agfdggmtah pkvdpvtgel mtfradwrap wlrygvvdah
      181 gvqrvdiavd lpapsmmhdl aitetrslll dlnvgydfsm lkhghrmplr whddrparig
      241 viprhggdvr wfgiepcfvq hvvnaydcda scivldvvry pwflrldart grfddnpvge
      301 lwryvidtan glidegplad ggielprine srtgrryryl yaveqpnnae mrgvmrfdha
      361 rgtttryavp agdqnsepvf vprpggtded dgwllvmvyr aatessdvvi ldaraidagp
      421 vatvhlprrv pagfhgawvp rer
//
LOCUS       WP_175972728             729 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia stabilis].
ACCESSION   WP_175972728
VERSION     WP_175972728.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..729
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78223
     Region          36..721
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mssspfrits yisdtktgia iidaarhwag tsgvtwlyvf ktilaallal gvamklelpm
       61 prtamttvfv lmqpqsgmvl akslyricgt ivgllamlvl iglfgqapel flgatalwig
      121 ictagaarnr nfrtygfvla gytaaligip swqhpdaafl samtrvtevt igilssgavs
      181 alvfpqhvsk qisrvnrarf teftddvlsi lsgridrsfl ealsvrivde tvnaeaarsv
      241 avfegpdtrl rngrltrlna ermaastrlh alsqliarlr aaradvvlte iealmagiaa
      301 pirlewqdat haddidalvq sladtlehcr talpdrarla rnrlgsrasa ldfdtavdll
      361 drfldsyiay aqtylslsai ahereqwatp yeprtnplia avagvramll tlvlstfwia
      421 tawpsgallv lnggaicalv assarpsrta fqmaigtafa sviglivmfv aypvidgfpl
      481 lcvvlappla lgcwmttrps lagygvgyci yfcfltgpdn vvaydptsfm ndaialvlsm
      541 lmasvafelf lpptmrglrk hlladlrgqv vfactdsaat lrarfesrtr dlmyqvrsis
      601 rddpvanges vewflsvlei gsavvdlrga maieaarrgp datpawlddc asacraigll
      661 fetptptara aatravqaai atlqrtmqtt daagpavphl qtvlgslhfm hsalaapdsp
      721 lpapesdar
//
LOCUS       WP_175972798             187 aa            linear   BCT 11-JAN-2025
DEFINITION  GtrA family protein [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175972798
VERSION     WP_175972798.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..187
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20902
     Region          13..176
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 madlsfarfa snlgqfikfg lvggsgtlvn iatsivaakc glawfgatph dalfnlfgtq
       61 fhvrwfmlfs tiaflvantw nyqlnrmwtf ksvnkvswlr gffpflitgi gaylvtlavq
      121 yllmnptspl qlpphifdds tgfrtmyywa naisivvamp infifnklwt frstpkapvv
      181 vhetepa
//
LOCUS       WP_175972828            1023 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175972828
VERSION     WP_175972828.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..1023
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=114303
     Region          300..998
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 masyllhglw lpvsglslwi eqveghkiim psavpegtfp dvvdsilskk tfrnrarvsl
       61 rtpkgkdvsl mvpmamfapd eavetlakle yldtdsqaat peqratiapd llwlirayrg
      121 lyrfvragrv tirlsyqage wypmwqlasg lgerswlaem lasapgilsi nnralsddla
      181 delthwiayt qlrpqidapr aapwhdfaqa llrtspvkkg raqllrglne wkdsitsvdl
      241 qlvflveepp nenvsvedaa wpirllvrsg tdspmpvrqe qldrgsvekl revrrhafdv
      301 aprlkynsap asrnagdwdv yltteqlvdf vthdaaalrk agftvllpks wshmetkakl
      361 ettevrdpad aatkahigme klfsydwkls vgdtqltdae mhelissksg lirlrgewvm
      421 adtqalnkis qymreladta rkralkeleq laataemarq leqpgweelv aeverrrkef
      481 negeqeeavt ladlremalk smaedpvaft gsewhtsllg gldstapdrv eipdtvhael
      541 reyqrrgvdw lywmsrnnig avladdmglg ktlqllslla vekaaheteg eaeawkptlv
      601 vaptsvvgnw areakrfvpd fkvmvqhgtg rlkgeelvta aqnadivits ygtvsrdflt
      661 lskvewdrvv ldeaqaikna strsskavra ipsrhrvalt gtpienrlse mrsildycnp
      721 gilgsasffr nhfakaiere gsdvmaerlr lltgpfilrr lktdpniidd lpekseqiit
      781 vrmtdeqaal ykalvndveq alakkkegis rrglilaslt rikqicnhpa hfladgsavt
      841 ikgkhrsgkv eelmriidqa iesservlvf tqykafgdvl qpylseqlgc eipflhggvs
      901 knrrdqmvee fqaddgapvm llslkaggtg lnltaasivv hmdrwwnpav enqatdrafr
      961 igqqrnvqvy kmitagtlee siqdildgkt qlagavvgeg egwltelspe qladlmsyre
     1021 qek
//
LOCUS       WP_175972877             337 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175972877
VERSION     WP_175972877.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..337
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=35416
     Region          92..>176
                     /region_name="PRK11907"
                     /note="bifunctional 2',3'-cyclic-nucleotide
                     2'-phosphodiesterase/3'-nucleotidase"
                     /db_xref="CDD:237019"
     Region          168..307
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 msdktpdkat nfdddiptyt gpdsakasap eevetekpkk sslfqrpgra epqvikpkkv
       61 eepaaetaae paaeaktetf espsrgslsf dsaaaetett afpraeamae pdeqttampv
      121 sataasetqt epaatenyee vpstvavadp avdsetaave ekpeparrgt idfgllfvrl
      181 alsvyllvag astffklggn eglaglenef geytmaaala igvptvqlia gaflllglvt
      241 plaamfgliv tgfsaihgln aseagldvfa wnenvwlglv lfviavalqf tgpgfisldf
      301 nrswarrpla tswifvvigv aalvaiwwfg agvnpln
//
LOCUS       WP_175972861             319 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175972861
VERSION     WP_175972861.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..319
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32216
     Region          3..315
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mshvyvlveh eaeqlspvtg elitaaralg tvsavvvakd aataasfdae lgnlgaaqvv
       61 qataadyeqr ivtpevdalh alaannpapi vlastptnne iagrlaarlg sgalvnvdgi
      121 nadgsahhti fggsyetsst atgsvvytlr pgtataepqp vtaapapfel paatakdvtv
      181 tsftpaekta rpeltsakvv vaggrgvgdk fadvveplad algaavgatr davdegfydp
      241 afqigqtgat vspnlyiglg isgaiqhtsg mqtsetivvv nqdqdepffq iadlgvvgdl
      301 heiapalake lesrkgagn
//
LOCUS       WP_175972847             391 aa            linear   BCT 11-JAN-2025
DEFINITION  MraY family glycosyltransferase [Corynebacterium sp.
            Marseille-Q2823].
ACCESSION   WP_175972847
VERSION     WP_175972847.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Anderson,M.S., Eveland,S.S. and Price,N.P.
  TITLE     Conserved cytoplasmic motifs that distinguish sub-groups of the
            polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase
            family
  JOURNAL   FEMS Microbiol Lett 191 (2), 169-175 (2000)
   PUBMED   11024259
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Lehrman,M.A.
  TITLE     A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P
            transferases
  JOURNAL   Glycobiology 4 (6), 768-771 (1994)
   PUBMED   7734839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10160596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..391
                     /product="MraY family glycosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=40422
     Region          45..320
                     /region_name="GT_WecA_like"
                     /note="This subfamily contains Escherichia coli WecA,
                     Bacillus subtilis TagO and related proteins. WecA is an
                     UDP-N-acetylglucosamine (GlcNAc):undecaprenyl-phosphate
                     (Und-P) GlcNAc-1-phosphate transferase that catalyzes the
                     formation of a phosphodiester bond...; cd06853"
                     /db_xref="CDD:133463"
     Site            105..106
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133463"
     Site            234..237
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133463"
     Site            order(296,310..313)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133463"
ORIGIN      
        1 magtgvplre laliifvaaa ftylttglvr svlvrsgqva eirlrdshsq ptpqlggvam
       61 ftgfgaavyl agqlpaltrg fmpvtpemna vlwsaaaivi vgvvddlvel salvkligql
      121 vaaaimsglg ltwtllflpf gdgttvildq vqgtllttff tvllinainf vdgldglaag
      181 lgmiaggail vfsltvlhdq ggavsayppa iiaaalvgvc agflphnfep srifmgdsga
      241 mliglllaaa stsasgkinm slygtvdiva lmspvivvva avfipvldlv wavirrvsqg
      301 rspfaadkah ihhrllslgh thrrtvlvly lwvsavafga vsfsivpapv avvlaavalv
      361 vafgvtlipl rqgklgrqpr ptsvvvetdp s
//
LOCUS       WP_175972975             448 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1047].
ACCESSION   WP_175972975
VERSION     WP_175972975.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..448
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47560
     Region          9..414
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(22..23,26..27,30,69,127..128,130..132,135,155,
                     158..159,162,243,246..247,250..252,255,283,287,339..340,
                     344,348,364,367..368,371..372,375)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mgtsvkqpkr aalasfvgtt iewydfysya taaaivfgpl ffpgenrfis llasfgsfav
       61 gffarplggv mfgylgdrfg rkrsllatlm lmavstvaig llpthaqagv iapillvlmr
      121 vlqgiavgge wggavllage hapegkrtff asfaqlgsas glilsmlafg aistlskddm
      181 mswgwrvpfl assvllivgf virasvsesp efeevrksgn iaqkplreal kvwpllllai
      241 ganvygiagv yfsnifmisy atqflsldrs mvlhcmtiva vlqfvvqlaa aflaqrfgtt
      301 rvllitgawa mivpfvmlpl vhlgtpvsit vgvglatlae sgyysvvagf vsgifvarir
      361 ytaisiayqv cgalaggltp lvatiiaqnt apqwwplalq ytsaavlssl cvwlisrrvs
      421 iddagapgkt ddalprgtrt ahraprta
//
LOCUS       WP_175972980             154 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175972980
VERSION     WP_175972980.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..154
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17088
     Region          3..142
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mteldktdra ilaavqrdgr lpiarlaesv glsetpcarr lkrlendgyi eryraqlsrq
       61 algfgvvafv lvrfathdrk vadrferevl gierilachn vagtadyllq vvardlddyg
      121 tflrdslrml pgvtsiesal slrevkhdag lplp
//
LOCUS       WP_175973002             305 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175973002
VERSION     WP_175973002.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..305
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=33763
     Region          63..292
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mtpparrdgt pdkkkrdsdm ivsnakparh qhvkkkatad svardlgadw ladgkakkns
       61 qnqgerlqkv lakagvasrr haeilidegr vevngqviit qgtrvnpntd virvdgarin
      121 vneetqyfvl nkprgmqstm sddmgrpcvg dvvadrvvag qrlfhvgrld adtegllllt
      181 ndgelanrlm hpkyevtkty latvlgeadk rlvrqlregv eledgpakad yvqivdknqg
      241 yslvrlelhe grkhivrrml keagfpvqrl vrtklhtvql gdmkpgslra lnsneltsly
      301 kavgm
//
LOCUS       WP_175973025             743 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia sp. BCC1047].
ACCESSION   WP_175973025
VERSION     WP_175973025.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 743)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..743
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=81869
     Region          48..715
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mnrfvpflrd awlrcrarva plaaacrtrv ralgagalhr lrhptrrgva ltlaaipvlg
       61 llvllafvpf tpsigdirka ridrparvls adgqliaefr pvnrewvplk qisphmvdal
      121 iatedhrfya hhgidwrrtl aaglrtfsgd rqggstitqq larnlypdev graptltrkv
      181 kelitafkie avyskdeile tylntvpfly naygvemaar tyfgksadql ditesatlvg
      241 mlkgnsyynp vlnpdravqr rnivlgrmaq mgmlspqqla klqrrplhvd fepqtaqpgl
      301 aphfavqlrk wliawadrnn ydlyadglvv rttldarlqd matqaltrqt erlqaiadga
      361 wrgpsgcglr ndlfvgfmrq tpeyrqardt gltdvlalkq lganrefmra lcerktqvqa
      421 gfvaidprng airawvgspd fgsepfdhva qarrqpgstf kpfvygaafa dgmrpgdtfv
      481 drpvaipidg ravwhptdae pptgepmtlr dalalsrnri taqvmqhega akvaqlaram
      541 gvrdspldav pslalgtspv tlkemvsayg tianrgvyva pqmitriedr ngrvlaafgs
      601 apperalpap aaqtlvdamr gvvdygtgad irsrygirid vagktgttqd ntdgwfilmh
      661 pqlvagawvg fddgsvtlrs dywgagahsa lpivgsfyda alraraidph vqfspdfrpr
      721 sapapkrrap phsglfdwlr ffr
//
LOCUS       WP_175973030             148 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175973030
VERSION     WP_175973030.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..148
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15502
     Region          4..144
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mlsynviavg tdgsqtsmra vrsaasmara ydatliivsa fynhsgsmlg apnsedarvp
       61 vvseemsesf lnnaaeiahg egakrieiia ksgdpvnsll evgkdygvdm fvvgnkgihs
      121 vrgrvfgsva teltrkahtd vvvvnttd
//
LOCUS       WP_175973047             232 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia sp. BCC1047].
ACCESSION   WP_175973047
VERSION     WP_175973047.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 232)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 232)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..232
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23237
     Region          48..126
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          144..217
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mndavatrre psrrrfapll laaaallash ahaddtalgk tiatqgtatg vaacigchgs
       61 hgegnaaagf prlaganaay lsaqlaafad gsrqnavmqp lstllppher davsayfasl
      121 papagvftpd dasldpantg awlatrgrws qglpacaqch gsgglgvgta fpplagqpaa
      181 ylagqlhgwk hgtrppgpmg lmptiagkls dadidavaay yarggaaqgd kr
//
LOCUS       WP_175973077             438 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent RNA methyltransferase [Corynebacterium sp.
            Marseille-Q2823].
ACCESSION   WP_175973077
VERSION     WP_175973077.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..438
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=45953
     Region          23..435
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 mtatdhnsak dqsaaagsls kgqsfdttie rmghggvgig aapdgrvcfv sgafpgdhvt
       61 vtatkvkksf veaalssvvq pgpyrvesvc paaqrgagcc dfaeldpaae pdikvavlld
      121 qlrrvahied apdvetidva phrgwrtrvr lgvdkqgrag lrkrgstelv tdvacsqlip
      181 glvdglvgpd artfnpgaev iavmdsdgnr hvvetrkapr grrietirev ieaptenvvq
      241 radghefrfp ptafwqahvg apdvytslar ewlgaeghgn ggepeaadep avhavawdly
      301 ggvglfvpal advttpqggh tavysvdysp aaaapqpgla gidvhfrtak veqvasqlpq
      361 pasvildppr tgagndvvaa vaaakpqril higcdpatfa rdlaawsehg yrakrlamvn
      421 afpgthhfet lallvpla
//
LOCUS       WP_175973129             690 aa            linear   BCT 11-JAN-2025
DEFINITION  ribonuclease J [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175973129
VERSION     WP_175973129.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Li de la Sierra-Gallay,I., Zig,L., Jamalli,A. and Putzer,H.
  TITLE     Structural insights into the dual activity of RNase J
  JOURNAL   Nat Struct Mol Biol 15 (2), 206-212 (2008)
   PUBMED   18204464
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..690
                     /product="ribonuclease J"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0004534 - 5'-3' RNA exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=74970
     Region          123..669
                     /region_name="RnjA"
                     /note="mRNA degradation ribonuclease J1/J2 [Translation,
                     ribosomal structure and biogenesis]; COG0595"
                     /db_xref="CDD:440360"
ORIGIN      
        1 mtesrnrsrk vtrkagppae tetasneaas pvfqapnesa asgnnsnesn nsnnsnsedg
       61 nrrsrsrgsr ggrgrgrggn nnhnnggrnn nrnrnnnrgr rnvpksmqga dltkrlpepp
      121 kqqkdslriy alggiseigr nmtvfeyqde mliidcgvlf pssgepgvdl ilpdfgpiek
      181 kihkvkalvv thahedhiga ipwllklrpd ipivasrfti aliaakckeh rqkpkfvevn
      241 eksdvnygpf rcrfwavnhs vpdalgvmlg tpagniihtg dikldqtpld nrptdlpals
      301 rygdegvdlm lcdstnanip gvsasegdip atfkrlvaga kqrviiatfa snvyrvqaai
      361 daavaagrkv afngrsmmrn meiaekmgfl kvprgtiipi deaakmaphk vllittgtqg
      421 epmaalsrma rrehrqitvr dgdliifsss lipgneeavf gvinmlsqig aevitnkeak
      481 vhasghgygg ellflynaar pknampvhge wrhlrankel aistgvardr vvltqngvvv
      541 dlrngraevv gqipvgnlyv dgvsmgdvda dtladrtnlg aggvvsitcv idnrtsrlle
      601 hptvsttgfs dddrgivpev aemventmnd laaegendty rmvqklrrkv sklmdskykr
      661 epvilptivp tnsdvlmpdd devhasresl
//
LOCUS       WP_175973160             776 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia sp. BCC1047].
ACCESSION   WP_175973160
VERSION     WP_175973160.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..776
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=82023
     Region          60..739
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mirrpkaaar agatrrgrra rcigttvgal alfglppgsv raqqqadgsa iappepaivl
       61 pavvvvgttp llgigtplse vpanvqtvra aeldaqhrat ladffaanlq svtisdaqgn
      121 pyqtdvnyrg ftaspllgtp qglsvfvdgv rvnepfgdvv nwdilptqai drvqlipgsn
      181 pvyglntlgg alaittkngr sspggeaevs ggawgrktas ieqggtigpn ldyyasanva
      241 ndggwadhna srvrqafgkl rytdadttls iaaggadntl sgtqtiprsf ldnrkqayty
      301 pdrnrnsagy ltlsgerffg envelsgnay yrhlrntnts snnntdygsm dddgtvdtmq
      361 gsnarstivt dsyggsvqlt llgklggman rlvagvsadv anssyvassq dasftdaraa
      421 igigdfvpqt saktrnanvg vyvsdalslt phwtltlsgr ydwskaqigd esgvqplldg
      481 thvfsrfnpa vglnwnpvag ftayaayneg mrsptaiela cadpaapcsl pndfiadpal
      541 kpvisktfea gvrgrigaat twsaaayrtt laddiqfiss pasaqgyfrn vgdtrrqgie
      601 lagrtrfgpl rvglsyshvd atyrsswteh spansaadan gnvtvkpgdr ipgipahtvk
      661 lrldyaatsa wdiganvvwr sgvyargden ngdvngriag yvlvdldmry rvtkrfevfa
      721 svtnlfdkry asfgalgqnf fngpnhtfdg anpvnepfvg pgaprgawag mryawd
//
LOCUS       WP_175973130             255 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC1047].
ACCESSION   WP_175973130
VERSION     WP_175973130.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 255)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 255)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..255
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25853
     Region          55..254
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mttrgsmgpk rsalpayvar aaalalllvl llrpvwlqgl fapfadngap viydraslld
       61 ltlahlgtva lssligtiva vaagiavtrp fgadflpvar svvdigqtfp pvavlalavp
      121 avgfglkpvl ialvlygllp vfestiagie dvprdvvdaa rgmgmsgwqq lvsvelplaf
      181 pvivngirla vvinlgtati gstvaarglg dviiaglqts ntafvlqggv ivgllavlvs
      241 daigaiarva sarrt
//
LOCUS       WP_175973164             682 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Burkholderia sp. BCC1047].
ACCESSION   WP_175973164
VERSION     WP_175973164.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 682)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 682)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..682
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=73150
     Region          2..669
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mrddveqaag sraahpagwp apsiqkaher setfglqvsa rpdydvlsna alvlkreqsr
       61 vlcvhampvm etlheqivnt qsmivltdae glilhsigdd dflrraekva lrpganwaes
      121 rqgtnaigta laelcpmvvh gdqhflaanr fltcssvpil dpygdaigvl dvtgdhrsyh
      181 qhtmalakms vqmienhlft ttfqetlqvs fhgrpeflgt lmegivafta dgrflsanrs
      241 aqfqlgmpls alrahtlssl fditsaqlid rmrastdrhl mlnlgngavv carvhfrrat
      301 laegsrptdv hdagapaara navpapaagt saglsrlnyl dtgdaqvacv iakvrkvigk
      361 dipilitget gtgkellaqa ihndsprrda pfvavncasi petlieself gyeegaftga
      421 rrkgaigkll qanggtlfld eigdmpyplq vrllrvlqer lvnplgstkt iavdiaiica
      481 thrdlremia qnrfredlyy rlnglvvrlp plrdrtdlav vvqkmlqrea fagpggppls
      541 vapdvmelfv rctwpgnfrq lgnllrtaaa mvdddgeirr ehlpddffdd lrcgdavqtg
      601 qavpatpdsp aaastgagpg aadalpsvda rlqdvaasai aaalarhggn vsaaaralgv
      661 srntiyrkmp aadagrqpsd es
//
LOCUS       WP_175973179              98 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175973179
VERSION     WP_175973179.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 98)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002085
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..98
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10317
     Region          1..98
                     /region_name="ManC"
                     /note="Mannose-6-phosphate isomerase, cupin superfamily
                     [Carbohydrate transport and metabolism]; COG0662"
                     /db_xref="CDD:440426"
ORIGIN      
        1 mslidlksva naqacawqst ivgevgqari kvlrmdaqpy eaevhdyneg llvldgtlml
       61 eveaetvvvg agqmylarag trhavlpgsh gtlaiidv
//
LOCUS       WP_175973184             369 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease signature motif containing protein
            [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175973184
VERSION     WP_175973184.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10052677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..369
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39987
     Region          251..303
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(277,279..281,283,294..295,299..300,303)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 mgdietyirl rnsgialvea atstpeglra lgasagdaae laslhaiyfg dtrftgkqrt
       61 arqaaqrqgh dlatlslies ytaklkkqvd vwnlrvalas tpsermpsva aqrlkelkpk
      121 rvpspgvrlt yrkngphslt vtdsalnist mrsalesinp tdlldatrqv ffkegvgsrp
      181 avgtnvvvtl deldkiirhd gddieleltn ggrmsgaefl tykfaetgya tlvhptigpv
      241 wlhrlsrfas leqrimasae hptcaiedcn kpadycqvhh iipwqagget nppnltmlca
      301 yhngindddp tsptgrgyvf rlrgpvdyip pwgtpitaqp ayqkavkqla adkthaqppd
      361 ppngspppg
//
LOCUS       WP_175973262             284 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: phosphatidate cytidylyltransferase [Corynebacterium].
ACCESSION   WP_175973262
VERSION     WP_175973262.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium
  ORGANISM  Corynebacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Corynebacterium"
                     /db_xref="taxon:1716"
     Protein         1..284
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30243
     Region          12..279
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mpkpknsagr dmpaaiavgv glgalvvfav wagplvwylv vatalglamw evltrlrehs
       61 yyvprtlliv lgqamvwvsw flnasglvav yvvavlalmf grlfhngrhr ppinylrdms
      121 vgifvltwip lfgtfaamls rvetpfasga asivvfmlcv vasdtggfia gvmfgshpma
      181 pavspkkswe gfagsvvfgt ltgalsfafl lhhtpwvgal mglglvfcat lgdlvesqfk
      241 relgikdmsa llpghggimd rldgmlpsam vtwvamsflt tlap
//
LOCUS       WP_175973265             318 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia sp. BCC1047].
ACCESSION   WP_175973265
VERSION     WP_175973265.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..318
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33763
     Region          80..293
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mlepeiaafv aavdawypad aaarspdeqr qlydrfaaew tpaalpagiv qqdavwrapd
       61 graialrryt sahgtprgtv lffhgggfvv gsldshalit aqlaadtgld vvavdyrlap
      121 ehrapaaled cvavtraard arwtfgpcvh pltlagdsag gmlaaavata lrdagegsvd
      181 gialvypmlg fepqsparet eahapmltld dvrryralyw ggdlsdvlrn gnpllrasvp
      241 leagrfdglp pvlaigaehd plrddarvyv ervraaggva hywmgeglvh gcwralgtsp
      301 qaarmhrtvg sfllapha
//
LOCUS       WP_175973269             256 aa            linear   BCT 11-JAN-2025
DEFINITION  serine/threonine-protein kinase [Corynebacterium sp.
            Marseille-Q2823].
ACCESSION   WP_175973269
VERSION     WP_175973269.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..256
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=26367
     Region          22..>186
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(22,46..47,76,81,86..89,102)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(29..30,32..35,37,50,52,84,101..104,108,110,153,155,
                     157..158,160,181..182,185)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(29..30,32..35,37,50,52,84,101..104,108,155,157..158,
                     160,181..182)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mnsqptasgl pldlepelsa kgysqfhqig aggmgtivfa rkesldreva ikviaqhaae
       61 ddeevcrfma emrtvaaleh paivpiydgg itpggvpyfi mkflrgpsle ahinqrildn
      121 skftveetvq llapiaqald ylaalpspvi hrdvkpanii adstpsstah sdsegctvml
      181 adfgiained tslrparvhr vvasltalpt sasmtaqpsl slaaadrggl savlcaglla
      241 ggssaaggvg ggvega
//
LOCUS       WP_175973277             296 aa            linear   BCT 11-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Corynebacterium
            sp. Marseille-Q2823].
ACCESSION   WP_175973277
VERSION     WP_175973277.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     A novel family of ubiquitous heavy metal ion transport proteins
  JOURNAL   J Membr Biol 156 (2), 99-103 (1997)
   PUBMED   9075641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440813
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..296
                     /product="cation diffusion facilitator family transporter"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31496
     Region          16..290
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
ORIGIN      
        1 mahehhdhdh sstplralli alsitgtvff aeliggwlag smalmadamh mlsdaaglii
       61 avlavlvgrr qasaqatygy rrvevlaala navmvlaisv wivveavrrl qspaevqgtt
      121 mliiaviglv analsawvlh rhressinve gaflhvlvdm lgsvavivag ivvlttgfva
      181 adviaslmia amvlprawql mrlsasvlle qvpadfdasa iepalreveg vadihdlhlw
      241 sldgvnvltt vhivrdgtvd tgplldaaqq alrehgiehs tiqiehpehe shetvc
//
LOCUS       WP_175973346             282 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175973346
VERSION     WP_175973346.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..282
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30760
     Region          26..265
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mttkrevkrp ampehggenq dpaparseiv rstervaqil gavaigqdqg rrlsdiaeel
       61 alapatvhrl latlveqglv ekpagerryy igqevfllal srrnrfpvrt iasphldalr
      121 asfgetvflt arnaldsvci drragenpak ilyvdvgnrr plgvsiggia lmqtmarvef
      181 dalltrnarr favfgttvse iraraahcrr hgygcldvdl qnthyrgisv pivtdaeeti
      241 gaiglgaias rmtdgnikrf vrsmqkhaqq iaqayqaras sa
//
LOCUS       WP_175973422             225 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175973422
VERSION     WP_175973422.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..225
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23951
     Region          9..>121
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          80..220
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mktsnrterr adalskeriv eaaiaildha gegaltfral aahlatgsga iywhvadkhg
       61 llaaaadhvi aaaltdvpte pdgdaaqalr rialrlfdaf sahpwvgaql frepwqqavl
      121 rilervggql qalgvpepaq fnaasalmhy ifglagqyaa garlhpreag qpeivatvae
      181 rwaqlepaqy pfvrkvaeql aahderaqfl agidlilagi gaaar
//
LOCUS       WP_175973429             193 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Corynebacterium sp.
            Marseille-Q2823].
ACCESSION   WP_175973429
VERSION     WP_175973429.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..193
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21474
     Region          4..165
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mttprisviv gslrresfar kiahevltmi pedyeanive irdlplydfd yddpavtdkp
       61 tpaeytsfre tiknssgilf itpennrtip aclknavdig skpnsdvawk nlpagiishs
      121 vgrmggyssq knlrlalsyf dmplpgqpev flgqsptlfe esghlnqrta dfvkdyvmrf
      181 lqltddafra tng
//
LOCUS       WP_175973473             245 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175973473
VERSION     WP_175973473.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..245
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25030
     Region          1..245
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mlaliivagl waglqnalag ggsfvtlpal ivsgmsplaa nitstvalfp gqvttgwasr
       61 nmvsgvgrlp fralfaisva ggalggllll ktpssifshl vpwlvlfatv vfawgsffrk
      121 pragaqhlgp vaagvsqfli aiyggyfggg igflmmaalt maglpprham stknalagvm
      181 nasavvlfvt sphlhwreai algagaivgg llgawalhrv nervlriaiv cigalltvgl
      241 fvkpi
//
LOCUS       WP_175973500             251 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Corynebacterium sp.
            Marseille-Q2823].
ACCESSION   WP_175973500
VERSION     WP_175973500.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..251
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27927
     Region          9..239
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 malrrtqqhs miadylrnli rskklspgdf lpseaelceq fsssrgpvrq avaalrsegl
       61 issgrgrrsv vlgrftsesf dsiysvthwl rergfepgas tlwlgrcpat dreaeflrve
      121 tgspvifvhr vrsangmpia iermffpldv gsqilsfdad nesihdhlrk qgvdfdsvnr
      181 elslayasee darslnvepg iplwrlhldi sdhsghpvec tqilylgdrm tlgmtnvrgt
      241 tsplevklse g
//
LOCUS       WP_175973541             194 aa            linear   BCT 11-JAN-2025
DEFINITION  YdcF family protein [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175973541
VERSION     WP_175973541.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..194
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=21460
     Region          <3..149
                     /region_name="ElyC"
                     /note="Lipid carrier protein ElyC involved in cell wall
                     biogenesis, DUF218 family [Cell wall/membrane/envelope
                     biogenesis]; COG1434"
                     /db_xref="CDD:441043"
ORIGIN      
        1 mkyvivlgaa qydgrpsril agrvrfaaey aaahdlpiit vggnlpgdrf teagvartll
       61 ddeplkvtal eegldtrsel aaareklgvs eavivtdplh rlrtfliarq egiratvlgt
      121 pyypsprfsi pwwrylahel gglaylglrt llgeertegv raafyrierl irpnqalrhr
      181 vigarqtqed qdsa
//
LOCUS       WP_175973491             174 aa            linear   BCT 11-JAN-2025
DEFINITION  shikimate kinase [Burkholderia sp. BCC1047].
ACCESSION   WP_175973491
VERSION     WP_175973491.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Herrmann,K.M.
  TITLE     The shikimate pathway as an entry to aromatic secondary metabolism
  JOURNAL   Plant Physiol 107 (1), 7-12 (1995)
   PUBMED   7870841
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Bentley,R.
  TITLE     The shikimate pathway--a metabolic tree with many branches
  JOURNAL   Crit Rev Biochem Mol Biol 25 (5), 307-384 (1990)
   PUBMED   2279393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..174
                     /product="shikimate kinase"
                     /EC_number="2.7.1.71"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004765 - shikimate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=18199
     Region          12..160
                     /region_name="AroK"
                     /note="Shikimate kinase [Amino acid transport and
                     metabolism]; COG0703"
                     /db_xref="CDD:440467"
ORIGIN      
        1 mnprpqagpt rialvgmpga gkttigsala rtlalpfvda drelerrfga pvavqfnagd
       61 frareadvid altggpalvl atgggavlrd dtrarlgqrc fvihlatdld tlwhrtrdda
      121 srpllnvadp raalaalhda reslyracah cridtsgqsv aqtlaaalda laia
//
LOCUS       WP_175973592             434 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1047].
ACCESSION   WP_175973592
VERSION     WP_175973592.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45464
     Region          7..406
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mtspsssrpa wtyenrllli lfmtfgfvff drlalsflfp fmsaelhltn tqlgmvssal
       61 altwalsgaa tgawsdargt rkpllvaavl gfsvcsalsg lvggfaslia fralmgiaeg
      121 pvlplsqslm vesstpsrrg lnmgllqgsa agllgamigp pvvigiatay gwreafyvsc
      181 ipgfliafci wrwvrevppg gvrhaqadtt aipagsgaev srwallkern illcvliscf
      241 fltwfvviis fapvflvesr hlspsdmgvv mtclgaawvf wgfavpaisd rigrkptmiv
      301 falvaaacpl mlihvgsvwa lgalvfatyt glgcftlfma tipaetvppr aiasalglim
      361 gageliggfv aptvagfaad ryglqfamwt saagailacv lsfglvetap avlrkralag
      421 gaagrldtpn lggr
//
LOCUS       WP_175973608             333 aa            linear   BCT 11-JAN-2025
DEFINITION  FHA domain-containing protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175973608
VERSION     WP_175973608.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12874772
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..333
                     /product="FHA domain-containing protein"
                     /calculated_mol_wt=36035
     Region          14..86
                     /region_name="FHA"
                     /note="forkhead associated (FHA) domain superfamily;
                     cd00060"
                     /db_xref="CDD:438714"
     Region          21..>250
                     /region_name="COG3456"
                     /note="Predicted component of the type VI protein
                     secretion system, contains a FHA domain [Signal
                     transduction mechanisms, Intracellular trafficking,
                     secretion, and vesicular transport]"
                     /db_xref="CDD:442679"
     Site            order(22..23,38..39,41,59..60)
                     /site_type="other"
                     /note="phosphopeptide binding site [polypeptide binding]"
                     /db_xref="CDD:438714"
ORIGIN      
        1 mailkndasg eacllrayhm fgrddarcdt virdgsvsrv hahirwiggc welhdhssng
       61 tsvsgvslrd gehavlqqgd vvrfgragva pwrveslddp adtlwpirga aapivlaprq
      121 ilpppaaqpv tivrspagew lcddtlppra lhdgdevstg dfawrlalar hgstvmlaar
      181 adpavpaqll effvsrneeh vrmllhvrgg vvdlgerahh yglvtlarar sadmqagyda
      241 atqgwieldr larmlgidas hvnvqihrar sqfaalpglg asqlverrrg svrfgdvpfr
      301 imrgehlece svpavgprig lpravpapvv qcs
//
LOCUS       WP_175973622             273 aa            linear   BCT 11-JAN-2025
DEFINITION  siderophore-interacting protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175973622
VERSION     WP_175973622.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..273
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=29921
     Region          5..266
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mqntsertvt rvrhtlkfrl lqvlrvhtvt phllrvtlgg adladfesas fddhvkvffp
       61 ppgaerpalp tlgangpefp egepkpvard ftprrfdraa reldlefvln hpgpasqwaa
      121 qarvgqwlgi ggprgsfvvp tdfdwhllig ddtalpavar rleelpagar aavvlevadr
      181 taqisfetra dvheiwrfra eadtangdtl lnavrdlplp psgdgyvwaa gealsmravr
      241 qhltgergid ksriraaayw krgaaavhet led
//
LOCUS       WP_175973637             201 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175973637
VERSION     WP_175973637.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..201
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21829
     Region          14..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mntpldssge pgvrdrllda aealiysggi hatgvdaivk rsgaarksfy shfeskealv
       61 vaalerrdar wmrwfvdatl arghapraql lgmfdvlrdw fgqpdfhgca flnasgeipd
      121 addpvrvvar mhkarllafv rerfdayade tgvarrglar larqwlvlid gaigvalvsg
      181 dasaardara taellldtvs r
//
LOCUS       WP_175973705             235 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175973705
VERSION     WP_175973705.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..235
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25268
     Region          25..216
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mkktvktgaa tasgaararr qtqaershat rerviaaais llhkegysga ttlairread
       61 vsmgalqhqf ptkaelmaav qerltgdrfa qfehasrsat tpleridrml dvagaligtp
      121 lfaasmeiql arradkelde avahilkpfd egfralmdda vagfdraial kitqlqllag
      181 smirgltidv vtgsdpavar aafalwreia lrhmtdmaqs papaptktgk rrasr
//
LOCUS       WP_175973706             213 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175973706
VERSION     WP_175973706.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..213
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23873
     Region          7..211
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 meakldstad avaaslrdmi ingelaager lverdlaerf gisripmrea iqrleregll
       61 difrnrgavv rmlsasdvqe iydlrvlleg daiyrgvkrl ddetlarael vhrllgdata
      121 prrqgelnre fhallyaccg narqlksiae lrsqveryer lqatlladtp sfqvehddil
      181 qacrernara aramtvahle sarrivlrlv egg
//
LOCUS       WP_175973712             309 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175973712
VERSION     WP_175973712.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..309
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33653
     Region          8..301
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mtssstpryr gifpvvpttf sdtgeldlas qkravdfmid agsdglcila nfseqfaitd
       61 derdvltrti lehvagrvpv ivttshystq vcaarslraq qlgaamvmam ppyhgatfrv
      121 peaqifdffa rvsdaidipi miqdapasgt alsapflarm areieqvayf kietpgaank
      181 lrelirlggd aiegpwdgee aitlladlha gatgamtggg fpdgirpile awrdgrhdda
      241 fahyqtwlpl inhenrqsgi ltakalmrag gviacerprh pmpelhpdtr aellaiarrl
      301 dplvlrwar
//
LOCUS       WP_175973714             309 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175973714
VERSION     WP_175973714.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..309
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33384
     Region          4..256
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mshpislgvv gigkiardqh lpaiaaepgf altacasrha evdgvrnypd lnallaaepe
       61 ldavslcapp qvryaqaraa leagkhvmle kppgatlgev aaldalarer sltlfatwhs
      121 rcasavepar awlatrtira vqvrwkedvr rwhpgqqwiw epgglgvfdp ginalsivtr
      181 ilprelvlre atlivpsdaq mpiaaeldca dtdgvpvrae fdwrhgpveq weiavdtadg
      241 vlaisrggaq lsiagepvei gpereypaly ahfhaliarg esdvdvrplr lvadaflfgr
      301 rvqtdafgr
//
LOCUS       WP_175973737             460 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease signature motif containing protein
            [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175973737
VERSION     WP_175973737.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10052677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..460
                     /product="HNH endonuclease signature motif containing
                     protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49459
     Region          322..378
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cd00085"
                     /db_xref="CDD:238038"
     Site            order(348,350..352,354,365..366,370..371,374,378)
                     /site_type="active"
                     /db_xref="CDD:238038"
ORIGIN      
        1 mnlveahlrs qaagielvag vaglsfeqlr awgpesvvrs llalfdvyfa ptsftrkqar
       61 avsaarangh dlptlllier fagrlkkqre awdlrielcg iagdekavar yarkrirels
      121 pppapkpgvt irrgkelskl tltapaalie dlrpnideed pvgsftaafr egrlarpvaq
      181 tlavmelpey aiilgrlgdp sppppdsaap aadgtpptqp attstlrpds tgampptesa
      241 aaspsnvsde paidetsgrd staagdpaap dlgdiviqls ngakitgqel ierelaeegl
      301 vmlvdrvkgp velhrtqrva sekqrimasg eqptcawdrc lcgadysqih hitewrkgge
      361 tnpenltplc kyhnainglp grgrivredg kikwvpagpr dprepahphr apraqriren
      421 rqetvstvas pstsrraqta kpaesrtstr sepgspappd
//
LOCUS       WP_175973768             334 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175973768
VERSION     WP_175973768.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13300132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..334
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37388
     Region          29..>163
                     /region_name="PRK11242"
                     /note="DNA-binding transcriptional regulator CynR;
                     Provisional"
                     /db_xref="CDD:183051"
     Region          112..309
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(122,126,165,179,181,244,261,288)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(123..124,128..129,131..132,135,139,141..147,208,
                     238..242,249..250,253)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mpdtsiprpd addpfarsfs tcyagvvtfl avvtegsfar aadrlgvgrs svsrhvqrle
       61 drldarlfqr ttrsmsltre gelfyencrp giehlaqale dmrelrsgpp sghlrvgstp
      121 gfgrkviapl lrdfharypd itldlllndr padfsadrid vafrdgrmed saivarrlip
      181 mqmivcasps yahrhglprh vdelaqhrci nlctasgrvt ewefridgvt qrrqlaahht
      241 fndidlvvra vldglgiaql payqvcdlla dgrllsclgq hapddgghyl cylsrkhlpt
      301 rirvfidymi eqtrardlqc lttmttlapl etid
//
LOCUS       WP_175973801             330 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175973801
VERSION     WP_175973801.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..330
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35288
     Region          4..321
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtallevenl gvrftrkdap pidavngvsf sleagktlgi vgesgsgksq tvmallglla
       61 gngtttgaar yrgdnlldmd tralnavrgd riamifqdpm tslnpfltie rqmtetlqlh
      121 rklsrkeaik raiealesvr ipdaarrirm yphefsggmr qrvmiamall sepeiliade
      181 pttaldvtvq aqiidllrel nrergtaivl ithdmgvvag ladnvmvmya grtveyapae
      241 sifaapshpy tigllnalpr ltdaddaplv aipgnppmpg tapagcafak rctyaeercg
      301 aerpaletyg aagavrachr pladltgglr
//
LOCUS       WP_175973845            1043 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Burkholderia sp. BCC1047].
ACCESSION   WP_175973845
VERSION     WP_175973845.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   4  (residues 1 to 1043)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   5  (residues 1 to 1043)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   6  (residues 1 to 1043)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11534127
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..1043
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=105270
     Region          11..>174
                     /region_name="copA"
                     /note="copper-exporting P-type ATPase CopA; PRK10671"
                     /db_xref="CDD:182635"
     Region          216..276
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(222..224,227)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          298..1041
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mteplasaal qtielsvdgm hcggctgrvq ralaavpgvv daavdldaha atvtaqetva
       61 agqlvdavre agyraavret pvaagaaths ahasrdetps aasarppvaa tieldidgmt
      121 cascvsrvek alakvpgvtr asvnlatera tvdasagvsa aqladavkqa gygatptase
      181 ivvpaaatal ptapapapap apapapatat apasieldid gmtcascvsr vekalakvpg
      241 varasvnlat eratvdasna vsaaqlvdav kqagygatpa avaapaatsa atpastdvel
      301 diggmtcasc agrvekalaa vpgvaratvn laterasvhg agpldaatlv aavttagyha
      361 slpaaspaga pagadlqpas paqdadarkr reairernlv igaavlsapl vapmlaapfg
      421 idlmlpgwlq lvlasivqfg fgarfyraaw havkartgnm dllvalgtsa ayglslwmll
      481 rdpahpghly feasavivtl vrfgkwlesr akrqtteair alnalrpdra rvvedgverd
      541 vplsqvrvgt hvgirpgerv pvdgrivsgr shideslitg eslpvpkddg davtagsing
      601 egalvvetta igaettlari irlvesaqae kapiqrlvdr vsevfvpail giavltlvgw
      661 liagagmeta ilnavavlvi acpcalglat paaimagtgv aarhgvlikd aqalelaqrt
      721 tviafdktgt ltegkpsvta fdavgvprae alalaaavqr qsdhplarav vaahdadvaa
      781 qggaaepvva tdaravagrg veaqvggqrl algstrwrde lgiavppald araaelerag
      841 ntiswlmrad apravlalia fgdtvkpgar daiaalsarg vasalvtgdn rgsaaavaaa
      901 lgigevhaqv lpddkarvva elkrthggiv amvgdginda palaaadvgi amatgtdvam
      961 htagitlmrg dpalvadaid iskrtyrkiq qnlfwafvyn lvgvplaalg llnpviagaa
     1021 mafssvsvvt nalllrrwkg rar
//
LOCUS       WP_175973857             202 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Corynebacterium sp.
            Marseille-Q2823].
ACCESSION   WP_175973857
VERSION     WP_175973857.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22395
     Region          17..>119
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maekksrrnr psprsrlles atrlfttegi rvigidrilr eadvakasly slfgskdalv
       61 iayvealdee yradwqkrte datdpeskil affdkaieeq psmefrgshf lnaageyprp
      121 etdaergiva acvehrtwmh stvtallntk ngypseeqas eilifldggl agarltrdvv
      181 plvtakqlai rllsappady si
//
LOCUS       WP_175973862             276 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC1047].
ACCESSION   WP_175973862
VERSION     WP_175973862.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 276)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 276)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 276)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..276
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28633
     Region          3..275
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mqaslpergv lrrfgalpat allavcfvlp laalvdaaca gggrafaavw rdplvadaia
       61 rslalavgag tlsvavgvpv afalagqspa rrhwslallg vplafsglvi aygfilafgr
      121 agfvttllaa lgadptvvgg aiytmpglav ayayyliprv almiyptlan ldrrpleaal
      181 tlgarpwraw ldvawrelwp svasawclvt aialgtygta lalagtqini lpllmylkls
      241 dgqtdfsqaa vlsivltaic tcvlalgegl vrqrrh
//
LOCUS       WP_175973869              94 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175973869
VERSION     WP_175973869.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 94)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 94)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..94
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10452
     Region          26..91
                     /region_name="AF2118"
                     /note="Predicted transcriptional regulator, contains an
                     XRE-type HTH domain (archaeal members contain CBS pair)
                     [Transcription]; COG3620"
                     /db_xref="CDD:442838"
ORIGIN      
        1 mdkrynamsl pdqlalrrqa iedvlahpew slresvrhlk ktmrltsaem aklagvstkt
       61 iqdieqgrsd gtvqtmsrif gmlglklgvv rqda
//
LOCUS       WP_175973881             741 aa            linear   BCT 11-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Corynebacterium sp.
            Marseille-Q2823].
ACCESSION   WP_175973881
VERSION     WP_175973881.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..741
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=79771
     Region          35..647
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mteketsgrk sgnrkksash rsrrssgrtr rwpwivlavl fvivgipall fgyaytqydv
       61 pepkelqpsq istivagdge tqlaklvppe gnrrqvtlde ipdyvedsvl aaedrefwtn
      121 sgfsftglgr avlgkltgda sagggstitq qyvkntlvgd eysyvrkire liysvkmtne
      181 wskedilnay lntvyfgrna ygieaasnay fnkdakdltk eegallagvi qspsvldpwv
      241 deersqarwn yvmdglvemg dldqserdql vfpetrdpse ysayteapga yghiknqvid
      301 elsrvgited qlatgglkvt ttidmtvqna stdaahaqla vlqedaraaa vtidpatgav
      361 rgyfggddsn gwdyansplq tgstfkimal aaalqqgidl ntyyssapyq lpgsqtvtnv
      421 gggcgsctia ealknsynts flrlqddlen kmqdtadmah algvarslpg iektltengg
      481 tpyegvvlgq yqsrpldmat amatltnqgv whqphfvqkv enaagevlye nptdggerrv
      541 sanvannvis amqpiaawsn galaggrpsa sktgttqlgd tgtnkdawmv gstpqlatav
      601 wvgtadntsa ifnqwggimy gsdaptkiwk sildtslanv eqqpfpqayp vhygvgswgs
      661 gyvydpsqtt twnqtpaspe sdstegeeet pdeggehhde gqggspeqpa qpeqpeqpan
      721 pevpslddil ngdgldqllg q
//
LOCUS       WP_175973913             207 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175973913
VERSION     WP_175973913.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..207
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23128
     Region          1..207
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mlhvlgkips invrkvlwlc telnlpfeqe dwgagfrtth dpaylalnpn alvpvikddd
       61 fvlwesntii rylanryggd alypaepqar arvdqwidwq gsdlnrswvg aflglvrksp
      121 dhqdpdgiar siagwtthmr vlnaqlektg ayvagntftl adipiglsvn rwfgtpfehp
      181 dlpavsryie rlatregfkq yagsanp
//
LOCUS       WP_175973924             712 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia sp. BCC1047].
ACCESSION   WP_175973924
VERSION     WP_175973924.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..712
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=76579
     Region          40..642
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mtdptanppp ppappstppr rrrvwrtlag allgltlaca gigawtidri wtqlpsvehl
       61 avyrpalplr ifsrdgdlla eygverrefv pleripplmr hallaaedak fyehgpvdvg
      121 glaratfanv vtgqpgqggs titmqvarnf yltrdkvlsr klaeilmaak leraysknkl
      181 lelymneiyl geraygfaaa ahvyfgkpld alsageaavl aglpkapsaf npvvnparat
      241 arrnyvlgrm halgqlddaa yraavdapia lattpppgii aapyvaerar rmmverfhdd
      301 aytlgldvtt tismrdqraa eaaldrtlsr qsratrdarn glegalvsld aatgdmlalv
      361 ggadfnrnvf dhalqayrqp gssfkpfvys aalekgyfpg vlvddtqrtl thaetgarpw
      421 rprnfgnrye gfipvrrglv rsknlvavsl mqatdaryvq qhavhfgfda qrnpaslpla
      481 lgagavtple lasaysvfan ggtrmeprli lsvkqrhgga myeatvpage rvvsarnafv
      541 mdsmlrdvvr agtargalal rrddaagktg tsngskdvwf agyssgivav awlgydtprp
      601 mgratgatla lpvwldymkt avdgrtpvda tppqdvalvd gdfvyaeytr gtctadvpvy
      661 irsrfacgga aavdasdasd apagdgkrge pmpaavdaae rervldlfrt dd
//
LOCUS       WP_175973940             315 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175973940
VERSION     WP_175973940.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..315
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33987
     Region          2..315
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhtvavlalp dvvpfdlgva cdtfvrvrap hveqayrvrv fseqprvggd lfelrppfrl
       61 daladadtim vpgtsvplap tsrrvldalr aaaargcria sicsgafvla eaglldglra
      121 tthwlaaael arryptvdvd pnvlfvdngr iltsagaaag ldlclhmiqt dygaavavda
      181 arnavaprvr eggqaqfiap ewpvggdglh dlmdwlhanl rqpltldaia rkastsvrtl
      241 trrfqeqtgt spgqwlqtar vrhaqqllev telsiehvat eagfgsvtaf rerfarivgt
      301 spqryrqafr arada
//
LOCUS       WP_175973948             221 aa            linear   BCT 11-JAN-2025
DEFINITION  O-methyltransferase [Burkholderia sp. BCC1047].
ACCESSION   WP_175973948
VERSION     WP_175973948.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..221
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23636
     Region          65..221
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mttlmldpla sllarlfdea dasspatspa fanvsrdeqa rlmrsktdya dlyarlrdyp
       61 lpvsretgtl lymlarggga kaivefgtsf gistlhlaaa lrdngggrli tsefepskvv
      121 raqanlaagg ladlveireg dalrtlaadl pdsvdlllld gakalypeil alveprlrag
      181 afvvadnaey spdylayvra pengylsvpf gddvelsmrl r
//
LOCUS       WP_175973954             371 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia sp. BCC1047].
ACCESSION   WP_175973954
VERSION     WP_175973954.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..371
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39390
     Region          5..349
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,236,303,323,325..327)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,103,110,183,186,188,236,243,303,323,
                     325..326)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(27,103,183,186,188,326)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mtqdplfqpl rlgaltlpnr ivmppmtrsr asqpgdeane lmaayyaqra saglivsegt
       61 yiaplgkgya wtpgihtpsq vagwrkvtda vhaahgrmfa qlwhvgrlsh tsllggaqpv
      121 sssplqakgv nvfiagedgs tpgfvqasep ralsideire ivdqyrtaar haieagfdgv
      181 elhgangylv nqfidsnant rtdayggsle nrlrflrevt qalidgtgda srvgirlapl
      241 ttlngcvddd pettylaaak llgelgvgyl hiaeadwdda plmpvafkqq lraafpgvli
      301 yagaytaera reaiaagwad lvafgrpfva npdlperlrt gaalaphdrn tlfgggahgl
      361 tdyptlaqaa a
//
LOCUS       WP_175973977             178 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175973977
VERSION     WP_175973977.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..178
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18207
     Region          58..178
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msrlttirpe eatgaaaevf akikkavgkv pnayatigtq spealgaala fdaavaastl
       61 gkadieaikl avseyagcdy cvaahtlmgk lagltsdqmk qvragaatgd aardalvayv
      121 rtlvgthgtv pvavvdavre agyterqlie inlaiasitf tnlvnrvndt tldfpava
//
LOCUS       WP_175974001             412 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1047].
ACCESSION   WP_175974001
VERSION     WP_175974001.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..412
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42649
     Region          22..399
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(32..33,36..37,40,72,127..128,130..132,135,156,
                     159..160,163,235,238..239,242..244,247,271,275,328..329,
                     333,337,353,356..357,360..361,364)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mniatqagwv nrlfpalsea slrrylggqv asvlgswtqn vtlnlliyhl sgsaailall
       61 nfllygpqli vapvagsrig sanarrvtlc vltasllltg slftlsllgl lgvklilaha
      121 laigvssave tparqvlllt slqdathtsn avamntmvyn vgrmvgptva gfvyptlgpr
      181 tsfaiyalal cfmaacvrsi gtasadrpsr aesglrdavg yvlsdafsar ylpilacigl
      241 fagsyqtlvp lladqgfhda arftgvffac agagslsaav llssafgpra shrfiayapw
      301 tavgalavla attdaagsip afyalgfslt faatstnati qrqcpehvrg glvgmygmay
      361 ngtmpfgyll vgsasealgv rhtfaamaav lacgviavia wqrfthtrvg aq
//
LOCUS       WP_175974035             201 aa            linear   BCT 11-JAN-2025
DEFINITION  TlpA disulfide reductase family protein [Corynebacterium sp.
            Marseille-Q2823].
ACCESSION   WP_175974035
VERSION     WP_175974035.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..201
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=21817
     Region          1..>62
                     /region_name="MalE"
                     /note="Maltose-binding periplasmic protein MalE
                     [Carbohydrate transport and metabolism]; COG2182"
                     /db_xref="CDD:441785"
     Region          62..182
                     /region_name="TlpA_like_family"
                     /note="TlpA-like family; composed of TlpA, ResA, DsbE and
                     similar proteins. TlpA, ResA and DsbE are bacterial
                     protein disulfide reductases with important roles in
                     cytochrome maturation. They are membrane-anchored proteins
                     with a soluble TRX domain containing a...; cd02966"
                     /db_xref="CDD:239264"
     Site            order(94,97)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239264"
ORIGIN      
        1 mgrrtiraaa agvlavfala gcsqseenaq navasggtfe fispggqtti ryaeedrkpl
       61 kdfsgedlrd esttiklsdf kdqivvlnsw gqwcapcrse sddlqaihae lqkrqvgtvl
      121 ginvkdfnpe isrdfmadng leypsiydpp fktaaalggv ptsvvpttiv ldkqhrpaav
      181 flteitekdv levvdeleke q
//
LOCUS       WP_175974064             394 aa            linear   BCT 11-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175974064
VERSION     WP_175974064.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 394)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 394)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 394)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..394
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41068
     Region          39..392
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mtqlfdtlgf ieasavraga gvgaaahdet avpadgaavs leqvgkvfat prgqaaalrd
       61 vtldvrrgev fgiigrsgag kstllrllng lerpssgrvr vqgvdvgald edglvalrrr
      121 tgmvfqhfnl lsaktvfenv alplkiagvp kaervrkvda lldlvglaak rdaypaslsg
      181 gqkqrvgiar alvhdpevll cdeatsaldp ettqsilall adinrrlglt ivlithemev
      241 iravcdtvav ieqgevvetg pvwrvfgdpr hgatrallst lqhdlpaela arvrplpeqa
      301 alpdgaqivl dvrytgesgg epdvgalaaa lggsvrflhg giesiqghaq grlviaatpr
      361 addagpsatr ggavaaller arrhanhaev lgyv
//
LOCUS       WP_175974075             208 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC1047].
ACCESSION   WP_175974075
VERSION     WP_175974075.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..208
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21679
     Region          1..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mphvawlpfm atslliiltp gqdmvlvmsc tlsggtragl vtaagvsvgl lvhtmlatlg
       61 lgallqasew lftalkviga lyllylgitl lrssgeltla gsgaapesrl rtfaqgalsn
      121 vsnpkvalfy laflpqfvpa gaahpmlslf vlgatfaglt flvkgpvalf agllsasirr
      181 npriltrmhr vsgmvllalg vklalerr
//
LOCUS       WP_175974115             214 aa            linear   BCT 11-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Corynebacterium sp.
            Marseille-Q2823].
ACCESSION   WP_175974115
VERSION     WP_175974115.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..214
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=22873
     Region          6..160
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mksylksapa tlvlmvlcig awlvtaiqak tlstpyyrsl laqdwtlwgp evsehpptvi
       61 tagfmhldag hllvnmvmlf fvgreveral gsalyvaayl isivgssaav lwmdfgtptv
      121 gasgalfalm glligvyrsr gldlrapivl vvanviysfv aenvsvwghl gglftgllla
      181 pflfrqrawl rwlgiwliga iavvaaalga glwg
//
LOCUS       WP_175974127             450 aa            linear   BCT 11-JAN-2025
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Corynebacterium sp.
            Marseille-Q2823].
ACCESSION   WP_175974127
VERSION     WP_175974127.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..450
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=48082
     Region          62..429
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mskffsrgte fgllvlatvv faitlvslel srgnvltldv lcliggfigv favahlvlcf
       61 lapyadqlml pivavlngtg lillqrldla nggglavrqv mwtivglilf alvlvllrdh
      121 rsltrysyil galglillal plvwpqppgv dariwlwlgp fsiqpgefsk illilffaml
      181 ltqkrslftv agykflgisl prlrdlapil viwgiaivim gisndfgpal llfstvlgml
      241 fmatnrvswl ligvilvgig gfgiyqvsek iqqrfsnfld planydstgy qlsqalfgms
      301 sggitgtglg qghpdmvpva hsdfilagig eefglvglaa vlvlfamlvs rgfrtaltcr
      361 dtygklvssg laltlavqvf vvtggisall pmtglttpfm saggsslman ymllaillri
      421 snaarrpare lssnaptdts mfpavqeair
//
LOCUS       WP_175973725             298 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfate adenylyltransferase subunit CysD [Corynebacterium sp.
            Marseille-Q2823].
ACCESSION   WP_175973725
VERSION     WP_175973725.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Mougous,J.D., Lee,D.H., Hubbard,S.C., Schelle,M.W., Vocadlo,D.J.,
            Berger,J.M. and Bertozzi,C.R.
  TITLE     Molecular basis for G protein control of the prokaryotic ATP
            sulfurylase
  JOURNAL   Mol Cell 21 (1), 109-122 (2006)
   PUBMED   16387658
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Snoeck,C., Verreth,C., Hernandez-Lucas,I., Martinez-Romero,E. and
            Vanderleyden,J.
  TITLE     Identification of a third sulfate activation system in
            Sinorhizobium sp. strain BR816: the CysDN sulfate activation
            complex
  JOURNAL   Appl Environ Microbiol 69 (4), 2006-2014 (2003)
   PUBMED   12676676
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Malo,M.S. and Loughlin,R.E.
  TITLE     Promoter elements and regulation of expression of the cysD gene of
            Escherichia coli K-12
  JOURNAL   Gene 87 (1), 127-131 (1990)
   PUBMED   2185135
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Leyh,T.S., Taylor,J.C. and Markham,G.D.
  TITLE     The sulfate activation locus of Escherichia coli K12: cloning,
            genetic, and enzymatic characterization
  JOURNAL   J Biol Chem 263 (5), 2409-2416 (1988)
   PUBMED   2828368
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     gene            1..298
                     /gene="cysD"
     Protein         1..298
                     /product="sulfate adenylyltransferase subunit CysD"
                     /EC_number="2.7.7.4"
                     /GO_component="GO:0009336 - sulfate adenylyltransferase
                     complex (ATP) [Evidence IEA]"
                     /GO_function="GO:0004781 - sulfate adenylyltransferase
                     (ATP) activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0070814 - hydrogen sulfide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=33617
     Region          1..298
                     /region_name="PRK05253"
                     /note="sulfate adenylyltransferase subunit CysD"
                     /db_xref="CDD:235375"
ORIGIN      
        1 mtlspnlkdl eneslhilre vagqfdkvgl lfsggkdsvv vfelarrafa patvpfelih
       61 vdtghnfpev idfrdelvee tgarlhvalv qdwidrgdlq erpdgtrnpl qsvplvetia
      121 ergydavlgg arrdeerara kerifsirds fggwdprrqr pelwdlyngg kmagenvrvf
      181 pisnwtesdi weyigarnlq lpsiyyshqr evfnrngmwl tpgewggpre deqvetrtvr
      241 yrtvgdmsct gavestaasp devlaeisis tlsergatra ddklsesame drkkegyf
//
LOCUS       WP_175974144             234 aa            linear   BCT 11-JAN-2025
DEFINITION  MOSC domain-containing protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175974144
VERSION     WP_175974144.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12233312
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..234
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25670
     Region          30..183
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
     Region          180..219
                     /region_name="3-alpha"
                     /note="3-alpha domain; pfam03475"
                     /db_xref="CDD:460938"
ORIGIN      
        1 msdgarpaia aaidavrigt srplagtpha saidkqpvda rlwlgalgfa gdeqadarhh
       61 ggpdkavhhy ahdhyawwsg qigardvlar pgafgenlst rgiterdvcl gdvftlggav
      121 lqvsqsrqpc sklnarfdhp rmaalvqqsg rtgwyyrvlq egwvaagdvl alharrypqw
      181 plsavldvly rrtldmaald alcdvpllpp gwrkmlekrr terqvedwtk rleg
//
LOCUS       WP_175974183             333 aa            linear   BCT 11-JAN-2025
DEFINITION  bestrophin family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175974183
VERSION     WP_175974183.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..333
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37892
     Region          1..321
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 mhlgksykls efliwtrwni yalfvfgtvp vilykflcvt wlsipltivv llgtatsfiv
       61 gfknvqtynr atdaleiwte ivgksrrwgq lardfagdea isrtlidrhl gwltalryel
      121 rrprvwestt klynaeyrrf yrvpeweqdi revllkylsp settqalsst siatfvlnlq
      181 csalrtlhaa gqlnasfyie lhktigdfia lqsrserfkn fpyprqyatv sslfvrffcl
      241 slpfgllsef nrlndgvsgf mhgnmvwlvv pcsvavswmy tsldpvgest enpfeggand
      301 vpistlcvti erdlkamlgd padhpcdhti ial
//
LOCUS       WP_175974190             247 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia sp. BCC1047].
ACCESSION   WP_175974190
VERSION     WP_175974190.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 247)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 247)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..247
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=25678
     Region          2..201
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mkivviggsg ligsrvvtll eeaghqalaa spstgvntvt gegladaltd advvvdvana
       61 pswepqavld ffrtaarnlg kaevaagvrh hvalsivgcd rmpengyfla kvaqeqaiea
      121 agvpytivra tqfmefiggi adfstqdgtv rigdglfqpi aaedvsalva qialaaprng
      181 tveiagpdra pfaevvaryl ksvgdpravv tdrearyygg rveetslvpl gnarlgrigl
      241 dtwlarg
//
LOCUS       WP_175974202             465 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175974202
VERSION     WP_175974202.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..465
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49292
     Region          16..460
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mtttnnsvra qdvvasdnts addglqrgmk srhlqmiafg scigtglflg sgasiqeagp
       61 gviaayaigg fiiflimrml gemavehpva gsfsayarsy igpiagfvtg wnwwfttivv
      121 gmleltaagt imdfwfpgip hwltalvalv ivtainlvhv gafaeaefwl slikvvalil
      181 mivvgaaivf gltpepalgl snitehggff pngasgvlfs lvavifsfgg iisigtaage
      241 aqdpakslpk ainnviwril ifyvggigii vllapwneld tstspfvral stlgitaaat
      301 glnlivlvaa vsvfntmtfs garmlrdlsr ggqappffns vsakgvpvra llfnsllmgs
      361 avllnflfeg kilivllaii vgaeliswsa iavahlnfrk rcpdaafrap lypianylcl
      421 gffaliialm fmlpdyrtga ivlpcwivtl aliwlgkkrh darnt
//
LOCUS       WP_175974239             326 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH:quinone oxidoreductase family protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175974239
VERSION     WP_175974239.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Shimomura,Y., Kakuta,Y. and Fukuyama,K.
  TITLE     Crystal structures of the quinone oxidoreductase from Thermus
            thermophilus HB8 and its complex with NADPH: implication for NADPH
            and substrate recognition
  JOURNAL   J Bacteriol 185 (14), 4211-4218 (2003)
   PUBMED   12837796
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..326
                     /product="NADPH:quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=33968
     Region          1..322
                     /region_name="QOR1"
                     /note="Quinone oxidoreductase (QOR); cd08241"
                     /db_xref="CDD:176203"
     Site            order(40..41,122,126,147,150..152,171..172,176,191,215,
                     237..238,240..241,262..264,314,316,318)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176203"
ORIGIN      
        1 mkallctafg pidrlriedv aipepaagqv riqvkaasln fpdalivqgl yqvkpalpfs
       61 pgaefagvid avgdgvtawr pgdsvmaftg hggfaqqcva dahqlaalpp gmtfeqgaal
      121 vlaygtslha lqqrarlqag etllvlgaag gvgiaaieia kalgarviaa assadklalc
      181 reagadetid yatedlrrrv deltggrgad vvydpvggay seaalrataw rgrflvvgfa
      241 ageipklaln lallkerdil gvfwgdavrr dpaqhaanmr llaewfaagk vrptitervs
      301 ldgaadaiar manrqvkgkv vifpda
//
LOCUS       WP_175974235             774 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia sp. BCC1047].
ACCESSION   WP_175974235
VERSION     WP_175974235.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..774
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81568
     Region          <68..>194
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          203..764
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msapelsvhn esrralllgf asgglllafg vpslaqaaap aqppvsanpq yggagmphgl
       61 rddpnlfvai apdgtvtvtc irsemgqgvr tsvalvvade lgadwarvkv aqavgdepry
      121 gnqntdgsrs lrqsfaalrr agaaartmla qaaaavwgvd vrqvkvtvhe vvdtktgrkl
      181 gfgelaekaa alpvpdtksv alkapaefry igkgktalid grdivggrar ygidtrldgm
      241 lyavvarppa ygdtvasfda saaeklpgvv kvvqlastpl psgfqplggv aiiardtwta
      301 iqaraqlkid wkrgphagyd saayrktlea aaaqpgdvir ndgdaaaala gaakrvraty
      361 yvphlahatm eppaavarva dgrcevwtct qapqttrdei akalgvpaer vtvnvtllgg
      421 gfgrkskpdy vveaallska vgapvkltft reddiahdhf havsleafdg gidaagkvva
      481 wqhrtvapsi qstfragvvh eqpgelaqgi adlpfaipnv rienpaaqah trigwfrsvy
      541 niphafgiqs fvselahaag rdpkdflldl igpaqrfeph itvkntnyge dpalypvdtg
      601 rlrrvvetva reagwgrklp kghglgiaah rsfvsytaav cevqvdadgr isvprvdiai
      661 dcgpqvnper vrsqlegavv mglgialhge itfkdgrpeq snfngfqvlr mneaprdirv
      721 hlvapddyat plggvgepgl ppvapaltna ifaatgtrir slpvadqlak pqag
//
LOCUS       WP_175974212             454 aa            linear   BCT 11-JAN-2025
DEFINITION  TrkH family potassium uptake protein [Corynebacterium sp.
            Marseille-Q2823].
ACCESSION   WP_175974212
VERSION     WP_175974212.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..454
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47933
     Region          9..449
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mkrghflgpa rltavgfill ilvgtlllml pisanvpqwt pflpalftat savsltglvv
       61 edtgtywtpf gqaviialiq lgglgimsla slsgmlltgr isfkarrtma aegravasgg
      121 irhallltlm mtliceatva vfigvrlate hgvapgravw egifhaisaf nnagfstysd
      181 svisfaadgw iliplafali vgglgypmla efvrrararl trwrggtpri hrmsmtarmt
      241 lgataflllg gtvvfflseg sgvlhgmpld qklinaffms asprtagfna idygeahplt
      301 lmvtdilmfi gggsagtagg ikvttacvlg aamiseflgr edpsighrrl plstfrqala
      361 ltaagmivva vgvatlriwd peftadqvtf evmsafatvg lstgitasls apsqlmlcli
      421 myvgrvgptt fvaalaarti slryrypeer pfig
//
LOCUS       WP_175974290             331 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Corynebacterium sp.
            Marseille-Q2823].
ACCESSION   WP_175974290
VERSION     WP_175974290.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..331
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=33673
     Region          1..247
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mrsliliava gaaaqlvdgg igmgfgvtst tilllaglgp atasavvhas elgttlvsgi
       61 shwrfgnvhw ptvlklgvpg glsafigatv lsnlsleaaa pvtsailvvl ginlvwrfsr
      121 prsrtpketr qhstpllagl glvggfvdas ggggwgpist stlmavgreq prrivgtvnt
      181 aeflvtfgat agfivglwee ivanaaavva lliggvitap iaawlisrin ptllggfvgt
      241 aivtlnipra lgwalahqqi lllqvaalvl gvaltvwanq rrarsaqgae gdsasqerts
      301 srvvettept gregahagss adsedervgv d
//
LOCUS       WP_175974317             481 aa            linear   BCT 11-JAN-2025
DEFINITION  PucR family transcriptional regulator [Corynebacterium sp.
            Marseille-Q2823].
ACCESSION   WP_175974317
VERSION     WP_175974317.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12084760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..481
                     /product="PucR family transcriptional regulator"
                     /calculated_mol_wt=50962
     Region          <28..122
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          <365..476
                     /region_name="PucR"
                     /note="DNA-binding transcriptional regulator, PucR/PutR
                     family [Transcription]; COG2508"
                     /db_xref="CDD:441998"
ORIGIN      
        1 mseisfrwlt nqhslnlrpl vegkpafsti haseladpte ftspgalmlt lglvfrddpe
       61 gfehyaaala eagvhgigfg tglafaevpp altracsqhh ltlfeiprat rfvsittava
      121 qeqarlenna hftfhrqqer lnhaavsgiq alideasnql saavavasss gavlsqrdqe
      181 qlsaasaave ateqtgrgtg tststgatit stfgsagrrw avaarrsekf dsysralirh
      241 lsglasllld hpdgnnhail galaldaqla gvdspalhaa fhlidghdlv dvlyvtastp
      301 srlartvsei gkaephsfvr peqdsallml ppgtatshlf kkqsrylrvs alrgvawqel
      361 npallsslqs harslplgtv aafdsaaptw lvepgvseal garraatvsr laahdvqhnt
      421 ellaplrafl vgnanlataa aelgvhrhtv rarldkvenl cgvdlsnpvt raellllsid
      481 s
//
LOCUS       WP_175974414             246 aa            linear   BCT 11-JAN-2025
DEFINITION  RDD family protein [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175974414
VERSION     WP_175974414.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10533406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..246
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=26995
     Region          110..240
                     /region_name="RDD"
                     /note="RDD family; pfam06271"
                     /db_xref="CDD:428859"
ORIGIN      
        1 mlpasfapnl yehfsldsra tsrelgvqla aadahleglg ylpeaperee lavasrilce
       61 pasrasydqk vesgaqltwa qleeyantgr wdesthapts tpprddarra spgnrvlmav
      121 idyflaalvv sfivgfgftn pddnsvwivs issiftvayy icfevlagat pakmiagytv
      181 rdmttheklt wqqsirrnww rvaslvplig pliaffgaly vvttigaknn lrgqhdiman
      241 aevvkk
//
LOCUS       WP_175974406             390 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175974406
VERSION     WP_175974406.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..390
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42679
     Region          12..282
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 midgqillgh sirwgmvggg lgsqigyshr saalrdgsfq lvagafdidp ergrqfgvkl
       61 gvaaercypd yatmfdaear rpdgiravsi atpnnthfei craalnaglh vvcekplcft
      121 teeaealqrl sveknrivgv aygysghqmi eqaremiarg dlgeirivqm qfahgfhseg
      181 veaasaaarw rvdpkfagps yvlgdigthp lyisevmape lkikrlmcsr qsfvksrapl
      241 ednaftimey dtgaigyvws savnagsmhg qkvrvigska siewwdehpn qlryevqgqp
      301 aqvldrgmpy lhphalredr igaghpeglf dawsnlyarf alamdaadrg daagvkairi
      361 pdvhagvegv rwvencvrsa daggvwvdyr
//
LOCUS       WP_175974418             287 aa            linear   BCT 11-JAN-2025
DEFINITION  C40 family peptidase [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175974418
VERSION     WP_175974418.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..287
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=29768
     Region          <185..285
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mlesaiaqia rmqpaqlpdv slptvpdlta agplaeiahg dprtlldtar qatedlstar
       61 salnsargli saavreligl gfeliqrglp ialgllipnp aaqaaarsal qalameyvgk
      121 alqrlkhlag ellqaaaplv pigqravqps vrgpqeenta rhalvapaae ngattqgqaa
      181 aqaalsqvgt pygwggtgng sfdcsgltqw awrqagvelp rtaesqtvgr qvsaeelqpg
      241 dlivwdghva mysgdgqmve agspvqtnpl rtnnmgmafk gfwrptg
//
LOCUS       WP_175974347             409 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            sp. BCC1047].
ACCESSION   WP_175974347
VERSION     WP_175974347.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 409)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..409
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41264
     Region          32..313
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mhsralagga rwalfaacfa lpawlwphga vlgylaqtaa lvvlalsynl qlgttgllsf
       61 ghaafaglga faaahwfnri ggplpllplv ggvagagfgc vagllatrrs gtafamitlg
      121 lgecvaaaaw svpawfggig gvpidrasga pwgnahfgap ahayaliaaw cvvsawamht
      181 ltrtplarla navrdnparv aalgtdprrv rlamvacasf fagvagtltl idveiatpds
      241 vsmarsatvl iaaviggtga ffgpaagaav ltalsivvag vsrawalylg vlfvaivvaa
      301 pggiagiaqa fahalrreap aterwrllca igacafwgva ivcaaelgya wrfaqddgtg
      361 vafgawgida dtpigwavag saagigillw gwrarlghga aaatredar
//
LOCUS       WP_175974425             734 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175974425
VERSION     WP_175974425.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..734
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79726
     Region          33..717
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 msasspassr vdgpfaawta afgdwartdg aawlylfkal laafiatgvs mrldlpapkt
       61 amttvfivmq pqsgavlaks fyrvagtifg liatltfvgl fpqqpelfll avalwvalct
      121 agaarnrnfr sygfllagyt taliglpasq hpdgafmsam trvaeimvgi vsagvvsalv
      181 fprttgeqmr ttvrkrfgsf vdyvaaalsg kldrahieti htrfvadvvg feaarsmavf
      241 edpdtrmrsg rlarlnsefm sassrfhalh qlmnrlhaag aqaaidaiep yfreiaplll
      301 tpagepvrts adaghaaaql lawrdalprr iratraalet qpdfplldfd taaellyrfi
      361 tdlheyaaty aslssather erwieryepr tnatamviaa irtatvilvl gwfwietawp
      421 sgvtmtltaa atcalasstp rptamsaqmg mgtalavctg flltfgiyph idgfpllcva
      481 lapllaigif mtlkpklagy gmgyliffsf lagpdnithy dptsfmndsl alvlamlasa
      541 iafavlfppt apwhkkrlfa dlrhqvvaag harlaglrtr fesgardlmy qahtlsadqp
      601 dvqrdalrwm favleagnat idlrqelatl psdpryasam pwrraietmr salsalfstp
      661 saarfdatla atnaaidatr qtldavepsr derhrlqril shlhfvrtal ldpesplepl
      721 nrnrpvrpqp gass
//
LOCUS       WP_175974428             228 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Corynebacterium sp.
            Marseille-Q2823].
ACCESSION   WP_175974428
VERSION     WP_175974428.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 228)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..228
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23994
     Region          1..220
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mntvtisrvh kylgegaqrt hvlkgaslea degeflgisg ksgsgkttll ravagllpid
       61 egsitvfdtc vstaapkell alrrnkigfv hqddllmnel talenvmlvl aaagvdetta
      121 hdkasealaq vglaelaqrf paemsrgqcq rvgiaralsg nrrilladep saaldsensh
      181 gifqlfkkla stgttviats hdpimldycg ttytlidgql gkaaphaq
//
LOCUS       WP_175974432             473 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia sp. BCC1047].
ACCESSION   WP_175974432
VERSION     WP_175974432.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..473
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50373
     Region          2..473
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mmsseafvsa crdaigadhv ltdphdtepf ltdwrrrykg aacavlrpan taevaalvkl
       61 anahgvalvp qggntglagg atpdasgsqa vlsvarlnrv raldphnnti tveagvilad
      121 vqarareggr lfalslaaeg sctiggnlst naggtavlry gnarelclgl evvtpqgeiw
      181 dglrglrkdn tgydlrdlfi gaegtlgiit aavmklhplp aarvtalaal esphaaldfl
      241 alaqraagpl ltgfelmsdf cmqlvgkhyp qlrypfaqth aqtvllelsd neseaharal
      301 feklmeeafe aglvvdavva enlaqsrafw dlrehiplaq adeglnikhd iavpissiar
      361 fidetdaaiq qaapgarmvt fghlgdgnlh ynvqtpeggd pkaflatfqa pinrivydnv
      421 hrhhgtisae hgigqlkidd aqrykspvet tlmrtlktal dprglmnpgk vlr
//
LOCUS       WP_175974443             537 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA carboxylase subunit beta [Corynebacterium sp.
            Marseille-Q2823].
ACCESSION   WP_175974443
VERSION     WP_175974443.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..537
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58015
     Region          17..535
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mtisshlsel dslsadttag kiaelkrrre aaaqpmgeqa hekvraqgrl tardrldyll
       61 degsfvetdm lavhrttdfg mgkkrpvtdg ivtgwgtidg revcifsqdg tvfggalgev
      121 ygekmikime lsittgrpli glyegagari qdgavsldwi aktfyqnvka sgvvpqisvi
      181 mgacaggnay spaltdfvvm vdekskmfvt gpdviktvtg eeisqeelgg agvhmhksgt
      241 shytassdee aldwvhdllt ylpsnnrqlt paepyeelge etandlllde iipdspnqpy
      301 dvkevietlt ddgdyleiqa dradnvvtaf griegqtvgf vanqpqvfag cldidsseka
      361 arfvrtcdaf nipiimlvdv pgflpgadqe hdgilrrgak llyayaeatv pkitvtlrka
      421 yggaycvmgs kglgadvnla wptaqiavmg aagavgfiyr keikaahekg ldvaeltksf
      481 ereyedhmln pykaaergli davilpsetr saiaknlcff adknvarpar khgnipl
//
LOCUS       WP_175974433             286 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfurtransferase [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175974433
VERSION     WP_175974433.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..286
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=32034
     Region          25..285
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 maefdpnppf qeyahperlv sapwlsarlg inglhvievd edsllydigh iptairinvq
       61 telldsttrd iisaedftal lrskgierdd tvvlygdksn wwaafalwvf elyghedvrl
      121 ldggrdawms eerdtsfmvp epsassypev sreessrifv delrdssatv vdtrspeefc
      181 geaahktgag esaygttmth ghipgainle wdraiypngc fralselkvn ygelepatet
      241 vlyshvgaqa ahtwfvlkyl lgfeaprvyd gswaewgnmv rmpver
//
LOCUS       WP_175974486             148 aa            linear   BCT 11-JAN-2025
DEFINITION  TadE/TadG family type IV pilus assembly protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175974486
VERSION     WP_175974486.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..148
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=15928
     Region          10..120
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 mkrqsacpgw rrqrgatave faivfplffv ifyailsfgm ifviqqsltl aasegaragl
       61 ayapdlttrv anaktttqnv lgwlnssppn vaaqqcnysg tptpllyclt vtvsytpdsw
      121 mtimpflgai mtkpltgtav vqipqsml
//
LOCUS       WP_175974635             142 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175974635
VERSION     WP_175974635.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..142
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=15390
     Region          <40..138
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mstitkkysv dvtrvdtghy ratnaagvsl efgraeglls pvelllaava gcsavdvdvv
       61 tsrrtepeif dvhvegtrvd edgasrlsdv dvefslrfpd tdagrqaqsm verlvrisqe
      121 kdctvsrtve nptnvtfrtt ep
//
LOCUS       WP_175974726             201 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia sp. BCC1047].
ACCESSION   WP_175974726
VERSION     WP_175974726.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 201)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..201
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21281
     Region          2..72
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          85..185
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mqarvmgcaa chgahgegtd ndyfprlagk pagylynqli afrdggrsyp pmnyllaylp
       61 dvylkqiaef faherppypp ptapkvsaim lalgkslvtn gkssrkvpac vachgaaltg
      121 meptipglvg lraeyisaql gafrygtrra tspdcmhdva srlseqdiva iaswlaaqpa
      181 panstpkprs plplacgsvp q
//
LOCUS       WP_175974745             280 aa            linear   BCT 11-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175974745
VERSION     WP_175974745.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472037
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..280
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=29619
     Region          70..223
                     /region_name="TadD"
                     /note="Flp pilus assembly protein TadD, contains TPR
                     repeats [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG5010"
                     /db_xref="CDD:444034"
     Region          155..185
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          190..215
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkrigeavir agmlavalll gacatkesgy gvgaqteraa lmqaadqkqs vpdtpgmylg
       61 liqrmqaqgl yyaslahida ydktygvmpe sillradalr mtdqpaasaa vyaqllktpl
      121 aargyrglgl lagaagdfdr avqaltqase laptdpslls dlayaklrsg dvvgarvplm
      181 kaaeldqrnp kivsnlalyl faagraqdaq rlmnqqhlsp eirkdingda akiaaavraq
      241 qraiatppvv srpgattpit pmannfgydq tvpllqrfsq
//
LOCUS       WP_175974644             285 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175974644
VERSION     WP_175974644.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..285
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31868
     Region          13..280
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mevmsvpqtt fnddrempll glgtyklrge dlvrsvreai elgyrhfdta tlyeneeelg
       61 qalhdamkag dvtrdelfit skvwhdhhgk dkvgqafrts ldklqldyld lylihwpwpq
      121 gglyvetfee iarmqgmgqi asigvanfye etlqtlidet givpvlnqve lhpgftqpel
      181 rqfhdnhgiv teawsplarg vilnnpevia vaekhditpg qavlayllsk gisvipkssr
      241 rerlaenfaa aevelapedv aaldtldgqe gfgrmfkdpr efpga
//
LOCUS       WP_175974772             301 aa            linear   BCT 11-JAN-2025
DEFINITION  metallophosphoesterase [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175974772
VERSION     WP_175974772.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..301
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=33027
     Region          24..297
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mkifpvlggl aaaglgtaaw ahseltkfel keytlpllep gtlreesefr ilhvsdlhmi
       61 pgqrakiewv sgldaldphl vintgdnlsd kravpevlra lgpllsrpgm fcfgtndywa
      121 pripnpfnyl igkknepsyv nlpwkgmraa fvehgwhdan qarvefkvgd vrlaaagvdd
      181 phhdlddyse iagtpnedad lslallhspe prvlekfaad gyqlslsght hggqlclpfk
      241 vagsrsivtn cgidrvraeg lhrfgemymh vsnglgtskf vpfrvfcrps atllriteka
      301 a
//
LOCUS       WP_175974823             488 aa            linear   BCT 11-JAN-2025
DEFINITION  flippase [Burkholderia sp. BCC1047].
ACCESSION   WP_175974823
VERSION     WP_175974823.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..488
                     /product="flippase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52325
     Region          5..395
                     /region_name="MATE_Wzx_like"
                     /note="Wzx, a subfamily of the multidrug and toxic
                     compound extrusion (MATE)-like proteins; cd13128"
                     /db_xref="CDD:240533"
ORIGIN      
        1 mdkgilknvs infiglilpt fvslvtvpay ihalgveryg vvslvwtlig yfgildlgms
       61 maaqnhiska lasgnadesa rvfwsafwln lgtgivggll iyfgafvyta yftkvsaamq
      121 hevylalpwl alaiplanvs wvfagainga erfgvfntnq tigtflfqll plgaawwiap
      181 nlqtvlaaav varliaavml gqasikvlgi rridppqwgt akglfnfggw mliasttsmi
      241 adtldrvmlg agmgakfvty ytvpqnlvtr lnmlpnalvr tlfprlsavg rdhadtlarq
      301 sleflngvft pvgivaifal apfltlwvga dlaahsapvg rvlvisvwlv gqasvtrili
      361 qsqvnparaa faglvempff vgglwfgihh fgligaavvv aaralvdygv llylsairmr
      421 aivldmlahl afllaslfla qawpglvqsi gmcavvlvln vawsltmtpg lralvrdlfa
      481 rlnarrta
//
LOCUS       WP_175974831             157 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175974831
VERSION     WP_175974831.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..157
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17037
     Region          3..153
                     /region_name="COG3865"
                     /note="Glyoxalase superfamily enzyme, possible
                     3-demethylubiquinone-9 3-methyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:443074"
ORIGIN      
        1 mtiqkitpfl wysteaeeaa afyagifpds rivrvtavpg tdgtrmvefe lfgqpffams
       61 hprteafnhs isllvscadq aeldrywsal ldnggtadgc gwlrdrygvs wqivpealip
      121 mmadrdavka grvaaammqm tkfddaalka afagtag
//
LOCUS       WP_175974868             594 aa            linear   BCT 11-JAN-2025
DEFINITION  GspE/PulE family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175974868
VERSION     WP_175974868.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..594
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=63228
     Region          106..576
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 msssptppgk tpksvtplil sravkpietd psvtqvqpva paapalapva rprepvlsav
       61 aaaaaasvqp aqtasqsqpp gqalplaava rplsdsgefa asdeerkflc llddgtllva
      121 eghemnpfvl sycarlerln cryttrlval dairrsyqgp rrdgsaerid htqmqvvakn
      181 liaracdara sdihirvnrf steilfrihn elvrmseqtr eygerllatl yaamssvsdn
      241 tykpnerqda aigdrdklpd rlfgvriata ptsvgsvmvl rllyndagea taltelgftv
      301 aqanafella qqphgmniis gptgsgkstt lqrvltkqlr emagsihvit vedpveypie
      361 gavqtpvvna pteearslaf aaaianamrl dpdtimigev rdrasaqsal raamtghqvw
      421 ttvhangala ivdrlvdlgl piamvtdesl vtglisqrlv kllcphcsrp laesiaqldm
      481 glvarvkrav garfdavrva gpgcphckng tvgrtvvaev vrtdatfcel lragrkpdaq
      541 aywlgelagq tvaqhalekv aaglvdprma ervvgpfmpg sggrpqplgs gygt
//
LOCUS       WP_175974874             216 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Corynebacterium sp.
            Marseille-Q2823].
ACCESSION   WP_175974874
VERSION     WP_175974874.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 216)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..216
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23041
     Region          7..210
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtttasspal slrdivvtyp dgdsrvtald nvsldvkpge ltavigesgs gkstllsvaa
       61 gliepdsgtv ertgsrglif qqanllaalt areqlliidh megrkprqdr adellsfvgl
      121 egfgnrrmnq lsggqrqrvn iaralmgqps vlladeptsa ldsklsrdia kllrgvtedf
      181 dtatlfithd rslldyadtv vevkdgklse yselaa
//
LOCUS       WP_175974876             331 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175974876
VERSION     WP_175974876.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..331
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34427
     Region          116..329
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mflalreivt argrffligg vvalitlllv mlsgltqgls kqntsaleal geqtpnvtfs
       61 tedpsftese ifaedvpasg iplgtsqtkl eghggvavfg lpegtqipgs stvipeegmv
      121 lsqsideemn apsrgtlggv dldvtavved eyyshspvvw vstetwqqvs hspedmvgva
      181 vlsqeptdts vsmgkalsgl payssergsl ltmqaflygi salvtiafls iwtiqrtrdl
      241 silralgasv kyllkdaiaq aaiilaigvg vgalvgwllg laaqgavpfe vsamtvlvpa
      301 lgiwllgiag aflatrrvsk inpldalggn a
//
LOCUS       WP_175974903             446 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia sp. BCC1047].
ACCESSION   WP_175974903
VERSION     WP_175974903.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..446
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47897
     Region          5..435
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mqassssepv rlkrtlglps vllfglayma plivygtygv lakasddtaa layllaliai
       61 aftalsygkl arlypaagsa ytytrrtfnp ylgfmigwat lldyfflpmv iwligaayln
      121 aafphvptwi wivafivlts glnivgiela arfnivlmvv qlaivamfvv lcwhyasaaa
      181 gpggiamaep ffkphvpfga tmagaaiaay sylgfdavst lteetidpkk nmpraillia
      241 liggaifvia aytmqlahpg vefkdtdsaa fevakmiggd lfvtvflagl ilaqfasgis
      301 aqasvgrlly amgrdeilpk rifgfihprf ktpainiala gvvglialkl dvatstsfin
      361 fgaflaftav nlcvirlyls ghhrerrigv fgglvfplig avsdiwllvs lektalvlgv
      421 awfvlglvyl cwmtrlfrqa ppevai
//
LOCUS       WP_175974913             283 aa            linear   BCT 11-JAN-2025
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Corynebacterium sp.
            Marseille-Q2823].
ACCESSION   WP_175974913
VERSION     WP_175974913.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..283
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=29467
     Region          10..281
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mssvlqvpak vgvlgggrmg agiahaflaa gasvtvvdin ddavaaarer vhkairgsld
       61 rgaegtfesw derlslstaa safagfdlvv eavpesmdlk vaafkdiaea apqavvatnt
      121 sslsvsqlae sipndviglh ffnpvpaskl vevvvaestp ealvetakgw veglgktavv
      181 vkdapgfass rlgvaialea irmveegvas prdidnamvl gykfpigple ltdivgldvr
      241 lgiaeylesq lgerfsppql mrdmvargel grksgkgfyd yse
//
LOCUS       WP_175974908             191 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA-3-methyladenine glycosylase I [Burkholderia sp. BCC1047].
ACCESSION   WP_175974908
VERSION     WP_175974908.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..191
                     /product="DNA-3-methyladenine glycosylase I"
                     /EC_number="3.2.2.20"
                     /GO_function="GO:0008725 - DNA-3-methyladenine glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=21376
     Region          1..190
                     /region_name="Tag"
                     /note="3-methyladenine DNA glycosylase Tag [Replication,
                     recombination and repair]; COG2818"
                     /db_xref="CDD:442066"
ORIGIN      
        1 mndkrpvarc awadgdplmq ayhdhewgvp vrdsrllwem lmlegfqagl awiivlrkre
       61 afrhafagfd patvagyger dilrlmadpg iirsrakiea tiggariycd megrgerfsd
      121 fcwsftdgks vqgdgeswis ssplserisk dlkkkgfkfv gptivyawmq avgivndhsa
      181 acyrraavsr k
//
LOCUS       WP_175974925             111 aa            linear   BCT 11-JAN-2025
DEFINITION  putative quinol monooxygenase [Burkholderia sp. BCC1047].
ACCESSION   WP_175974925
VERSION     WP_175974925.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..111
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12397
     Region          8..96
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mnepylqvia hffakpgngd rvvellaela patrtepknl dyayfrspen pdhivilery
       61 seadgldvhr etphfqrigv gaimpllerr dvirymvqpd tgtatppggt r
//
LOCUS       WP_175974935             302 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175974935
VERSION     WP_175974935.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32919
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdllammriy vrvvergtms gaardldmgq pavseriekl ekhlgtrllm rsartlacte
       61 egrlfyersk alleaaelav asvsrtenal dgtirlaapq cfgevvlpav lmqirtaypk
      121 lhidlvlnde ivdpvtegvd isiragqlrd ggfvayalga vgrvlvaaps ylerhgpldt
      181 kadlanhpfi rvkgvfaneq vplrrdggav eyarirtvmt ashwrpmfdt iaagggigvv
      241 qhpacadala hgrlvrllph ydvpdfalnv lvhaqrplpp rvravvdllk rtlppllttp
      301 dr
//
LOCUS       WP_175974965             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1047].
ACCESSION   WP_175974965
VERSION     WP_175974965.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46881
     Region          28..433
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(39..40,43..44,47,86,144..145,147..149,152,172,
                     175..176,179,261,264..265,268..270,273,301,305,358..359,
                     363,367,383,386..387,390..391,394)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mqtrstldeh atiatpaper takhyllagw asmagttiew ydfflygtaa alvfnriffp
       61 sldpvvgtla afgtfavgfi grpmggivfg hfgdrigrks mlmitlllmg vpsmiiglip
      121 sydsigywaa alliamrflq gmavggewgg avlmavehap kgrkglfgsl pqtgvglgli
      181 lsslamaava alpeadmlsw gwrvpflasi alvglgwfir akvpespdfe kvrkqgkaek
      241 spvtaalrrh prevltivga raaentwfym vvtfalayat qqlhlpkaem lhaitagaal
      301 slvtmplcgh lsdrigqrrm faiglvlmca faapffmmlg tqqtsyawwa ivlglgvvfp
      361 ilyapesllf aqqfpaeiry sgislsvqla gvigggfapm iatsllkagg gqphyviayl
      421 vgfgvfalac talmrpara
//
LOCUS       WP_175975004             282 aa            linear   BCT 11-JAN-2025
DEFINITION  ParA family protein [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175975004
VERSION     WP_175975004.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..282
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30090
     Region          4..258
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mthprlitia nqkggvgktt savnlaaala eagkkvlvid ldpqgnasta vgaehtsgtk
       61 ssyevllgdc sadeamqhcp ddenlycipa tidlagaeie mvslvrrefr lydalyngfl
      121 eehgfdyvfi dcppslgllt inamtcaeev iipiqceyya legvgqllgn ismirehlne
      181 dlhisgvllt mfdartklae qvanevreqf gavvlgnvip rsvrvseapg ygktviaydp
      241 sstgaraysa aareldkrgd ytphpttgai gvspeifael eg
//
LOCUS       WP_175975011             388 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175975011
VERSION     WP_175975011.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..388
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41917
     Region          129..379
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mmsnrlwtvg lhtmfgfllv fgvlrawadd rldaralgls ialavvytgf aifgsrtitr
       61 pvpttlwlaa lcllwiglmv haqdfmwlef plvfvfihal pfwpgivasv vlwavaafvp
      121 awlhpqgwta aaaigpfigt cfavavyhaa rrvqaeaahh eavakqlret qeelaasehq
      181 agrleererl sreihdtvaq glssivllsr aakktstqqd vaeqlaliek vaqdnlaear
      241 rfvkelaapa ssidaelrsl vdelqaqakg lglrtrfglk ltgsadvpae fshvilraar
      301 egltnvmkha dadravvtlg sfedeitldv vddgrgiegp rgfgltgleq rvrsvggsvq
      361 vesspagtal avriptgsss ngqrdahr
//
LOCUS       WP_175975050             274 aa            linear   BCT 11-JAN-2025
DEFINITION  TatD family hydrolase [Corynebacterium sp. Marseille-Q2823].
ACCESSION   WP_175975050
VERSION     WP_175975050.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..274
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29741
     Region          19..273
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mskkkprpmp vpaeglsqli dahthlascr dadadlvera raagverivt vgdglaeaek
       61 alaaaqefdn vyaacaihpt kaheldeaar arlsemaadp rcvaigetgl dtywihhepe
      121 rtapldvqee alhwhaelaa kvgktlmihn readeelmrv lgecaeapkv mlhcfsspld
      181 vakealergy vlsfagnvtf krneemrqaa alapagqlli etdapymtpe lfrgarneps
      241 lightyrcva qargqevedl aaevaetfae vfgv
//
LOCUS       WP_175975099             213 aa            linear   BCT 11-JAN-2025
DEFINITION  CAP domain-containing protein [Corynebacterium sp.
            Marseille-Q2823].
ACCESSION   WP_175975099
VERSION     WP_175975099.1
KEYWORDS    RefSeq.
SOURCE      Corynebacterium sp. Marseille-Q2823
  ORGANISM  Corynebacterium sp. Marseille-Q2823
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Mycobacteriales; Corynebacteriaceae; Corynebacterium.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Gibbs,G.M., Roelants,K. and O'Bryan,M.K.
  TITLE     The CAP superfamily: cysteine-rich secretory proteins, antigen 5,
            and pathogenesis-related 1 proteins--roles in reproduction, cancer,
            and immune defense
  JOURNAL   Endocr Rev 29 (7), 865-897 (2008)
   PUBMED   18824526
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Corynebacterium sp. Marseille-Q2823"
                     /db_xref="taxon:2736606"
     Protein         1..213
                     /product="CAP domain-containing protein"
                     /calculated_mol_wt=23059
     Region          89..213
                     /region_name="YkwD"
                     /note="Spore germination protein YkwD and related proteins
                     with CAP (CSP/antigen 5/PR1) domain [Cell cycle control,
                     cell division, chromosome partitioning, General function
                     prediction only]; COG2340"
                     /db_xref="CDD:441910"
ORIGIN      
        1 mpnpqqlmqy agaaitvial ilglifgtgd lssssdngvq appsnsakps ntpapsngtr
       61 kpdsdgcvkn tpdyfkckqe nskigkknpp ltssdiqqar rsqfmqivew rsdskhlnpi
      121 tydlsleata qrfanelaqt pgdeiwhsny ntrglenvaf dtytyknffd ifagsvghas
      181 tmatngrapk vgigiaqdpv tghyfcvqhf adk
//
LOCUS       WP_175975115             239 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175975115
VERSION     WP_175975115.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..239
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=26717
     Region          13..218
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mqdnpplten hllaalpene rahlathltl vemplgtvly esggqlhhvy fpttsivsll
       61 yvmedgssae iaivghegmi gvslfmgget tpsravvqsa gqayrldasi lkeefrrgna
      121 mqrlllrytq alitqmaqta vcnrhhsidq qlcrwlllsl drlpsnqlrm tqelianmlg
      181 vrrsgvteaa lklqdaglir ynyghievld rpglekrvce cysvvkrefd rllpdlkrl
//
LOCUS       WP_175975118             665 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Burkholderia].
ACCESSION   WP_175975118
VERSION     WP_175975118.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 665)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..665
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=70690
     Region          27..378
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mfdfkelrpa rpaarieppe tpsvqglitl avgvtviaal yfareilipf tlaillsflv
       61 aplanllgri klghvasvll avtmsvsviv vlggiiatqi tdlavgipry qatidkkisv
      121 vhgltvgkln qlagtagqal qratvdqpkt iressssssg tqppaalpve vrepaqtpfq
      181 larrilspvv spletafivf vvtivillqr ddlrdrairl fgsrdlhrtt tamdeaarrl
      241 sryfvsqlgl nagvgvvigt glfiigvpsp vlwgilaall rlvpyvgiwi sailatalaa
      301 avspewsmai wslvlfvtve llagqavepl lyghstglsp fsvvvaaifw swiwgpigli
      361 lstpltlcll vlgrhvtrle fldvllgdqp alspvenfyq ralagdpdda veqarillrd
      421 rplssyydei vlkglqlaad dvlrggvtpa qlariettvn dliegldgfa dtdpatdaaa
      481 adwgapaapa agqkvscqpa rnasspgiea rpvrhadnqv lciagrgald elasailvql
      541 lgkhdldcrv vnhdaasrvr idgldvtavt ivcifylain gipshlryll rrvrqrlpda
      601 livvglwpag dtgqwpedlr saigadhyat svrdmvnaci vstgtasafg sepkpngvaa
      661 vtgir
//
LOCUS       WP_175975149             306 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175975149
VERSION     WP_175975149.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 306)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 306)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 306)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..306
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32942
     Region          2..182
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          214..297
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdplsevlsl letrdsfftg lraggawavd ipppdgikfn avvegscwlt vdgagppvrl
       61 rtgdcfllaa prafslasdp svppvpaadv yrhlergiah ygepadcfli ggrfayeegm
      121 plllgslppv vvvsgdsepa avlrwslqql arefgaaspg gslmvrhlgh mmlvqilrry
      181 vdagangdvg wlagfadarv saalaaihaa perrwtvdtl aacchvsrst falhfkrrlg
      241 fgpleyvlrw riqlamrelr rsnapisaia qrlgydsdsa fghafkrivg csprayrhdv
      301 akesgn
//
LOCUS       WP_175975156             244 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC1047].
ACCESSION   WP_175975156
VERSION     WP_175975156.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..244
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /note="The N-terminal region of this protein, as described
                     by TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc.; The
                     N-terminal region of this protein, as described by
                     TIGR01726, is a three transmembrane segment that
                     identifies a subfamily of ABC transporter permease
                     subunits, which specificities that include histidine,
                     arginine, glutamine, glutamate, L-cystine (sic), the
                     opines (in Agrobacterium) octopine and nopaline, etc."
                     /calculated_mol_wt=25505
     Region          6..242
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 magddsllal lafgdggygr vfagafaltf gvaaasfctg vllgiasalg klsryaalvw
       61 larlyttlvr alpellclll afyavapaie nalrgsgivs gdfafdpfvv aalslgfiqg
      121 ayltdifraa lvnvpvgeie aahaygmtpw qtfarirfpa aarlalpgvg nvwlnatkda
      181 sfisvlgsft dllkasqlaa gatrhyvffy lvtaalflll sitsaglfaa lerhanrgtr
      241 ratt
//
LOCUS       WP_175975170             556 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia sp. BCC1047].
ACCESSION   WP_175975170
VERSION     WP_175975170.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..556
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=61465
     Region          112..541
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 maadeplsvp tprgrdgrap dplrvggwsp mrmfrdddav dfvivgtgag ggtlacklae
       61 ygfsvvalda gawwrpleef asdethqhkl fwtdericdg adpltlgtnn sgraiggstv
      121 hfamvslrfr pewfrsrsal gygvdwpldw remwryyrev eqalkisgpv nypwgpprpr
      181 ypyrahelna aalvlargad amgidwtptp latlsaprgr ahpcvyrgfc iagcatnakq
      241 salitwipra vaagaevrdl amalridaeg drvtgvhyrr dgrtrfqrar nvvvagyaie
      301 tprllllsan grhpqglans sglvgrylma qlnqaswgtm ddevrwykgp pslsitehwn
      361 yaddgkdffg gycwmsqgpl piewarkvaa rglwgdalkh emarynfqag lkivgetlpr
      421 adnrvtlade rdafglpvar vtysyddndr rmirhalaqm arsleaagar diwheeddtc
      481 hlagtvrmgd dpatsvvdad crswdipnlw vcdgsvfptv ggvnpsltiq aiacrtadri
      541 ktlvargdah ararwr
//
LOCUS       WP_175975259             400 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175975259
VERSION     WP_175975259.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..400
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43058
     Region          5..362
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mssawsrarr ilcvrldsig dvlmttpalr alkesgadrq ltlltsrtga alaqhlpmvd
       61 dvwsydapwv khpdvrgdpv adldmidrll agrfdaavif tvysqnplpa ammcwlagip
      121 lrlahcrenp yelltdrvpe tepashvrhe varqlalvrt vgaktadwrm afepgdaarr
      181 avharlqaal qrfggarrpa aerprwlvvh pgataasrrw paerfgeaaa avaplfdgia
      241 vtgsaderal vdavceragp ramplagvlp lgelgaliet adlllsnnsg pvhlaaalgt
      301 pvvdlyaltn pqhtpwrvph rvlnvdvpcr ncyrsvcnqp ghpclrgvsv ddvaaavhal
      361 lrgsarhaqr taaraaahdd epvaahasnv ipfahvitrn
//
LOCUS       WP_175975265             401 aa            linear   BCT 11-JAN-2025
DEFINITION  zinc-dependent alcohol dehydrogenase [Burkholderia sp. BCC1047].
ACCESSION   WP_175975265
VERSION     WP_175975265.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..401
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41862
     Region          1..401
                     /region_name="FDH_like_1"
                     /note="Glutathione-dependent formaldehyde dehydrogenase
                     related proteins, child 1; cd08283"
                     /db_xref="CDD:176243"
     Site            order(38..40,43,86,162,166,185..186,188..190,209..211,215,
                     229,253..255,303,320..322,345..347,387)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176243"
     Site            order(38,40,60,162)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
     Site            order(90..91,93,96,104)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
ORIGIN      
        1 mkavvfhgig diridtvpdp evsaatdavv rltasaicgt dlhmvrgtlg gmkpgtilgh
       61 egvgiveavg rdvrnlrrgd rvlipstiac gscaycragy taqcdvanpg gpragtsffg
      121 gpaetgpvdg lqaeyartpl ahaslirlpd aidddrailm sdifptgyfg aqlaevkpgd
      181 tvavfgagpv gqfaiasakl mgagrviavd riasrlemac aqgaeivdfs eddpvdtilr
      241 ltggigvdrv idavgvdamr athgpaaadr daarafdaev daiaphrkpd grnwvpgdgp
      301 sqvlqwavra vakagtisvi gvypqaarvf pigeamnrnl tikmgncnhr tvtpplvelv
      361 rsgafdplsv ltrsepltna idayrafnvr epgwmkvklt p
//
LOCUS       WP_175975348             208 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175975348
VERSION     WP_175975348.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..208
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22596
     Region          15..169
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mtesthhyye psqghglphd plnaiigprp igwissrgsd gtlnlapysf fnafnyrppi
       61 igfssttakd svrnvqetge fvwnlatrdl aermnqtcaa vpydvnefel ggltavpsrl
      121 vdvprvaesg vnfeckvtdv irlrdhhgve tpatlvlgev vavhirqdll kdgifdtfga
      181 giilraggps ayvhvtpdsr fdiarpda
//
LOCUS       WP_175975369             257 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175975369
VERSION     WP_175975369.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..257
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28037
     Region          1..>240
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mnllelddlc iaydtphgrr tvvdglslal prgeigcllg asgcgkttvl raiagfepvr
       61 mgrivldgtp vaapsldvpp errrigmmfq dyalfphlsa vdnvafglrr mpkaerrlrv
      121 aemldlvgla dagdayphel sggqqqrval aralapspel llldepfsnl dvdtrerlaf
      181 elrdilkrtg htailvthnq aeafaiadri gvmkdgqlaq wdtpyalhhh paspfvadfv
      241 rrdaladera ralargr
//
LOCUS       WP_175975353             343 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175975353
VERSION     WP_175975353.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..343
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36618
     Region          8..343
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkldstpitl tgcaktfrgt rvlepldlsi gagetlvllg psgcgktttl rliagldtpd
       61 aggtiafgdd dvtalpierr qvgmvfqnya lfpnltvrgn vgyglkirkt epralrervd
      121 ellammrlda hadkpvdqls ggqrqrvala ralavrprvl lldepltald aklrdvlrrd
      181 mnallrelgv ttvyvthdqa eamelgdriv vmgagrieqi gtpreiyyqp anrtvaqfig
      241 tlnrlagqwr dgalettgga iatphaadew ffrpedaqla dpahaslrga vgacaflger
      301 trltiehaap dalvidvpgr valargtavg ltiapeglia lga
//
LOCUS       WP_175975352             300 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC1047].
ACCESSION   WP_175975352
VERSION     WP_175975352.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 300)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..300
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31588
     Region          34..263
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mqslsgssar spapapaplh akraarhapr vagaraiaal qwgvtlllca flivpvvmsv
       61 lagltvnyfr glssgltlrw leqvwqqyhg svalslyvaf atlaivlavg vpagyalars
      121 ksriaraiee alvlpvalpg lasalallvv yggftafrms lwfivvghvv ftlpfmvrav
      181 aavaagadlr tleegaaslg asfvtrfvti vlpnlrpgiv agalavltls igefnltwml
      241 htpdtktlpv gladtyaslr levgsaytil fllmtlpllv amqwlgvdps gtralkkrpr
//
LOCUS       WP_175975402             288 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175975402
VERSION     WP_175975402.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..288
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30647
     Region          12..278
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mkkiqgvysa prghwvgdgf pvrsmfsyqs hgthlspfll ldyagpatfe pasaprgvgq
       61 hphrgfetvt ivydgevahr dstgaggtig pgdvqwmtaa sgilheefhs eaftkrggpl
      121 emvqlwvnlp aadkmgapgy qtllnadipv velpdgagra riiagefdgr rgparthtpi
      181 dvwdvrlvag gharfpvaeg rtlavvvlsg tvlvngetva reaqfvqlgr dgsdveiean
      241 gdakllilsg epidepvvgy gpfvmnsqee irtaiddfns grfgqmpa
//
LOCUS       WP_175975427             295 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175975427
VERSION     WP_175975427.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 295)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 295)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 295)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..295
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32026
     Region          19..144
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Site            order(36,38,42,76)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:380405"
     Region          212..292
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 msatrlpdsa rywrtplvpd adlltatyrd hafaphwhda ytipvilega erftyrgngy
       61 vaetgtvpvi npgevhtgsr aadegwcyrv sympvefire lasavagrpq dapwfapgvi
      121 rdadlaarlt lahrmleags eralsshaad gpatdaprvy dplaaetaml dalstlivrh
      181 advrpqpapl aadeprvdam rerlaadlts avtlddvaqa vglspfhaar lftrttgmpp
      241 hawrnqlrlq ralaplragv pvadvaaasg fvdqshftrh fkrmfgvppg rwqas
//
LOCUS       WP_175975460             236 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175975460
VERSION     WP_175975460.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..236
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=24442
     Region          7..230
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          101..130
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(102,106..107,110..112,114..115,119,122,132,136..137,
                     140..142,144..145,149,152,161,163,165,169..170,173..175,
                     177..178,182,185,194)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          131..161
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          163..194
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mtkptnhlpk ralvaaafva sglfaaagah aesldaivka vkfddiadig kqlksgkldp
       61 ntiasngdpi lviaareksd kvaaaiaatp nvdlekedka genalmlasl ngdlnlvkll
      121 idkgaevskk gwaplhyaat ngqdavvkvl ldhdayidta spngttplmm aargnhastv
      181 tllldqgadp qvknqlgita lefakhynap daieilskrt trigaatpad aqksak
//
LOCUS       WP_175975542            1048 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia sp. BCC1047].
ACCESSION   WP_175975542
VERSION     WP_175975542.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1048)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1048)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1048
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..1048
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114586
     Region          11..1027
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msvsheegrf nlsawalrhq alvvyliala tlagilaytr laqsedppft frvmvirtfw
       61 pgasarqvqe qvtdrigrkl qetpaidflr sysrpgesli fftmkdsapv kdvpetwyqi
      121 rkkvgdigyt lppgvqgpff ndefgdvytn iwtlegdgft paqlhdyadq lrtvllrvpg
      181 vgkvdyfgdp dqrifievnn aqltrlgisp qqlgqainaq ndisstgvlt taddrvfvrp
      241 sgqfdnvdai antliringr tfrlgdlatv krgyddpqvt qmrtngkavl gigvtmqpgg
      301 dvirlgkald aeskalqaql paglkltevs smphavshsv ddfleavaea vaivlvvslv
      361 slglrtgmvv visipvvlav talfmylfdi glhkvslgtl vlalgllvdd aiiavemmav
      421 kleqgysrar aaafaytsta fpmltgtlvt vsgflpiala ksstgeytrs ifevsaiali
      481 aswfaavvli pllgfhmlpe rkrhaheahl pddhehdiyd trfyrrlrgw idwcierrfv
      541 vllitgvlfv vammgfslvp qqffpssdrp ellvdlrlpe gasfaatlre terlekaidk
      601 rpeidhavnf vgsgaprfyl pldqqlqlpn faqfvitaks vedreklatw lettlrdkfp
      661 avrwrlsrle ngppvgypvq frvsgdsiat vrsiaekvaa tmrgdartvn vqfdwdepae
      721 rsvrfeldqk karelnvtsq dvssflamtl sgttvtqyre rdkliavdlr apradrvdpa
      781 klaglalptp ngpvplgslg rftptleygv vwerdrqpti tvqsdvraga qgidvthavd
      841 aklnalraql pvgyqinigg sveesakaqt sinaqmplma iavftllmiq lqsfsrvlmv
      901 vltaplglig vaatlllfgq pfgfvamlgv iamfgiimrn svilvdqieq diaaghgrvd
      961 aiigatvrrf rpitltaaaa vlalipllrs nffgpmatal mggitsatvl tlfylpalya
     1021 twfrvkrder dpqdgpppgg tpaapsga
//
LOCUS       WP_175975547             297 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175975547
VERSION     WP_175975547.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31041
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mtpdqlitfa avaehlnisr aavalhlsqp avsgqlrllq defgeplyqr dgrgirltpv
       61 geqlaqyana qrdtfaqara frdavrglea gtlrigastt pasyllpyli aafqpraprv
      121 aiqtmsgnta dvvaalpsld laliegppge alppgtavha whedeivaiv paghplaapg
      181 ydagvtldal aahplvlrea gsavrqlver afahggapmr vafeiagvea vkeavragmg
      241 vgfvsamslr hddaalvlrs lapapltrhf silvphggap srvaaqflem slaqrla
//
LOCUS       WP_175975558             350 aa            linear   BCT 11-JAN-2025
DEFINITION  microcin C ABC transporter permease YejB [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175975558
VERSION     WP_175975558.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 350)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..350
                     /product="microcin C ABC transporter permease YejB"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042884 - microcin transport [Evidence
                     IEA]"
                     /calculated_mol_wt=38087
     Region          1..349
                     /region_name="YejB"
                     /note="ABC-type microcin C transport system, permease
                     component YejB [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4174"
                     /db_xref="CDD:443333"
ORIGIN      
        1 mlayilrrll lmiptligvv titfavtqfv pggpveqvlt qlrhgsaggg eaggggggyh
       61 gsqgvdpqqi eqirkqfgfd kppleryalm lksyatfdlg qsyfahrsvw avirsklpvs
      121 itlglwtvil tyfvsvplgi akavrngsrf dtvtsvlvla gyaipgfvlg vlllmlfggg
      181 tfwqvfpmrg ltsddfdelt ligkaldylw hialpvtasv vgnfaivtil tkntfldeig
      241 rqyvltarak gaperdvlwk hvlrnaaipl ltglpaafvg aflngnllie tlfsldgmgq
      301 lsydsvirrd ypvvlgslfl ftliglltkl iadvcyvlvd priqfnrldh
//
LOCUS       WP_175975710            1084 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia sp. BCC1047].
ACCESSION   WP_175975710
VERSION     WP_175975710.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..1084
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115203
     Region          3..1062
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mlkivrlala rpytfvvlal liliagplaa vrtpidifpd iripvisvvw nyaglqpddm
       61 agrvityyer tlgttvndvq hiesqsfrgy givkiffqpt vdirtataqv tsisqtvlkq
      121 mppgttppqi lnynastvpv lqialtsntl deqklgdyav nfirpqllsv pgvaiptpyg
      181 gktrevqidl dpqalqskgl saqdvahala qqnqiipagt qkigrfeyni klnnsplsld
      241 alndlpiksv dgttiyirdv ahvrdgfppq gnivrvdghr avlmsilkng sastldiiag
      301 vkaklplveq tlppglklvt mgdqstfvng avsgvaregi iaaaltslmi llflgswrst
      361 liiaasipla vlsaiallaa tgetlnvmtl gglalavgil vddatvtien vnwhleqgkd
      421 trtaivdgak qivmpalvsl lcicivfvpm lmldgisrfl fvpmakavif smassfvlsr
      481 tfvpmlaqyl lkphasagha sgelaavmdp haghagahdv ppsrnplvrf qraferrfea
      541 vrasyrillg laltrrkpfv vaflgivaas fllapslgrn ffptidsgei alhvrapvgt
      601 rveetaaeld rientirgvi ppaqlravid niglpnsgin ltynnsgtlg pqdgdilisl
      661 shdhaptady vhtlrerlpr aypgttfsfl padivsqiln fgapapvdlq vagpnqqanl
      721 ayarelyrkl rliagvadpr iqqastypqf tvtvdrtrad qlgiteqdvt nsvvatlagt
      781 sqvdptywln phngvsypiv aqtpqyrmtt lsalrnlpvt gangqsqllg glatitrgvg
      841 navvshynie plfdiyattq grdlgavaad idgivkatak dlpkgstvtl rgqvqtmnga
      901 faglllglvg aivliylliv vnfhswadaf vivsalpaal agivwmlftt htplsvpalt
      961 gailcmgvat anailvvsfa rerladtgna lasaleagft rfrpvlmtal amiigmapma
     1021 lglgdggeqn aplgravigg lacatiatlf fvpvvfslvh rrdalkhdas rasslsasga
     1081 shvh
//
LOCUS       WP_175975718             297 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175975718
VERSION     WP_175975718.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32400
     Region          1..>143
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..274
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrldairlf vrlvecgsfs avgreegigq ptvskqiaal eqylgaqlvl rtsrqvvita
       61 agqafyesak plmedfdsle ssvgtrqqsp qglvrlttap aygrlcvtpl lpgffrhyph
      121 velelsvser qvdlvgegvd lairhgplvd ssltarklse tesllvaspg yiaakgrpar
      181 ladldghtgv vfarnherrp wrfkvgretv hrvpqgsflt gdaeqvraav lhglgiaqap
      241 rwlfgaeidt gqvevllpef qpermathlv ypagrrvptr vrvvidylms algttst
//
LOCUS       WP_175975456             281 aa            linear   BCT 11-JAN-2025
DEFINITION  NRDE family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175975456
VERSION     WP_175975456.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Bard,F., Casano,L., Mallabiabarrena,A., Wallace,E., Saito,K.,
            Kitayama,H., Guizzunti,G., Hu,Y., Wendler,F., Dasgupta,R.,
            Perrimon,N. and Malhotra,V.
  TITLE     Functional genomics reveals genes involved in protein secretion and
            Golgi organization
  JOURNAL   Nature 439 (7076), 604-607 (2006)
   PUBMED   16452979
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..281
                     /product="NRDE family protein"
                     /GO_process="GO:0007030 - Golgi organization [Evidence
                     IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=30663
     Region          1..280
                     /region_name="Tango2"
                     /note="Uncharacterized stress-responsive protein, TANGO2
                     (Transport and Golgi organisation 2) family, contains NRDE
                     motif [General function prediction only]; COG3332"
                     /db_xref="CDD:442561"
ORIGIN      
        1 mcliafdwqp daaagpvftl vanrdeffrr tsaplswwed vpgvlagrdl eaggtwlgvs
       61 rdgrfaaltn yrapfdirag aptrgklvsd flggspvapl dylaqlaeha avyngfnllv
      121 gdwrrrelaw fcnrapeges rvaapvaiap gvhalsnarl dtpwpkvvrk raelgtlltd
      181 nptpsldeli almrdphvad ddalphtgip iereralsaa fietpeygtr gttalrvtmk
      241 egvrltvevk ersdddgshr tvrpgafera vtfdidaarp r
//
LOCUS       WP_175975794             403 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar ABC transporter permease [Burkholderia sp. BCC1047].
ACCESSION   WP_175975794
VERSION     WP_175975794.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..403
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42400
     Region          22..403
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mnselssstp atpdadarrp dgraprlplr hvftrykvla llfavvaiwa ffsvltdgaf
       61 vtprnvsnll rqmsitgmla cgmvfviiag eidlsvgsll gllggvaail dvnrhwpvaa
      121 tvpavlalgv liglfngwws tyrrvpsfiv glggmlafrg illgvtggst iapvsdgfvf
      181 igqgylprla gdglavllfv vatllvvrqr gtrrryrlsv aplwqdvaki vgagavlfaf
      241 vatldryggi pvpvllllvl lgvfswiatq tvfgrriyav gsnleatrls gvdtdrvklv
      301 ifalmglmca faglvntarl aagspsagsm geldaiaacf iggtsmrggs gtvygaliga
      361 lvmasldngm smldvdaywq mivkgavlvl avwidvvsrs nrr
//
LOCUS       WP_175975840             157 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175975840
VERSION     WP_175975840.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..157
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16663
     Region          1..144
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mytnimvavd gspsssqale eglkvarscg arvfavfvvd qsllityagr mnpdalldev
       61 rrdgaavlrs aeraishaav ngdteivete pgqdiaerlq ryvvdrsidl avvgthgrrg
      121 vrrlflgsva erflrgsrcp vllvrgddaa patvaaa
//
LOCUS       WP_175975844             371 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175975844
VERSION     WP_175975844.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..371
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38569
     Region          22..>224
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mgtpdtgrlk apaldaslvd wldanatqld tsaalkadvv prlataglfr agvpaslgga
       61 ggtttdaiag iaavaehslt aafvlwgqrs fieyllqspn talrerwlpa lldgrcagas
      121 glsnamkyls gieslqidat phaesaddwr ltgrmawvtn lrterfvvaa avafgdgrps
      181 aivaipddap gltrstdldl ialrgsntaa lhldgvptda awlihpdaqt flpavrpafl
      241 glqcglsigl arralaearr aaettrgilg peveacaggl aaacaqlssg iadgslrlhp
      301 nrlfelrial atyvatavnl eleasggrgy lrdaglgfer rwreaafipi vtpsvvqlka
      361 qlaartrsia a
//
LOCUS       WP_175975843             188 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175975843
VERSION     WP_175975843.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..188
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19664
     Region          40..178
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msrlplptve tapaasqpfl eksqrangfl pnlvrslana pvaletyltv aeinsraglt
       61 faereavqit aaavhgcafc vaghtaaalk kahvdradvd alrdgepvae prleavaaft
      121 raviatrggv tddaldafla agfteanale vvlgvslatl cnfannlsrn elnpelaayr
      181 weprtqaa
//
LOCUS       WP_175975930             215 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC1047].
ACCESSION   WP_175975930
VERSION     WP_175975930.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..215
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22281
     Region          6..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mhtsgslygf lviggmlavt pgpnmvyvms rsiaqgraag lvslagvmlg ylfymfaaaf
       61 gittlfmsvp yagsvlgavg atyllylawq avrpggrspf evktlpneqp lrllamgatt
      121 svlnpklaml fvsllpqfid ygqgsvfgqs lflgslliaa fasangmvav cssslakflh
      181 grptlllaqr wamgavlggl gvemmidask lagla
//
LOCUS       WP_175975974             339 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Burkholderia sp. BCC1047].
ACCESSION   WP_175975974
VERSION     WP_175975974.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..339
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36937
     Region          13..323
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(16..18,48,53,79,142..143,183..184,207,236..242,278,
                     295..298,303,306..307)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(48,53,79,142)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 mslkdklpgn kilgfgtapl gnmfrnipda eaaatveaaw qhgiryfdsa pfygaglaei
       61 rlgdalanhp rdeyvlstkv grlildeied vsardlgekg glfehgrpnr ivndysadat
      121 lrsiedslkr lrtdrldivw vhdiaqdfyg dewlaqfeva rkgafrvlsk lreegvinaw
      181 glgvnrvepi elvldlaepq pdgmllagry tlldheralq rvmpaaaaqn vgivvggpys
      241 sgvlaggthf eyqkaspdil akvdrikaia arydvpikaa alqfsmshpa tvavipgasr
      301 periaedqaa lnvaipadfw remreqglia adaplpter
//
LOCUS       WP_175975984             196 aa            linear   BCT 11-JAN-2025
DEFINITION  flavodoxin family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175975984
VERSION     WP_175975984.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..196
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=20669
     Region          <53..189
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mdqldppvkt vvvyhsgygh tqrmaaavad gagaalvaid adgnladdaw htlaaadail
       61 fgsptymggp swqfkkfada sskvwfdsgw qnkifggftn sasvngdkln tleyffllag
      121 qhggiwvsmd ikpanlkast rddlnrmgay iapmaqtpad aspeemspgd letarrygar
      181 vaaiagqlra gqsran
//
LOCUS       WP_175975987             315 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia sp. BCC1047].
ACCESSION   WP_175975987
VERSION     WP_175975987.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..315
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33077
     Region          1..261
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mmqteieatg pagplkgtll srgaedvpvv livpgsgptd rdgnnpygir astyrllaeg
       61 llaqgiasvr idkrgmygsa saitdaddvt iddyaadvra wvaairtrtg arrvwvlghs
      121 eggwvalsaa rqtadmcgli lvatpgrplg qvlaqqlqsn panagvlrna msilasleag
      181 ktvdaagidp almplfrpqv qrflmselai dpaalvtgyt kpvlivqgar diqvgvqdaq
      241 rlkdanprar ltivananhl lktvhtdald enlaaysnpd lplansvvea isafvrestg
      301 dgldhpalsq rknar
//
LOCUS       WP_175975991             281 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia sp. BCC1047].
ACCESSION   WP_175975991
VERSION     WP_175975991.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..281
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29898
     Region          9..257
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(24,105,107,109..110,138,189,210,213,226,228,257)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 msnvtfpgrr vgdftitais dgyltasldf lsnidatdaa gmqraagqqq psavhincyv
       61 vrgagrtili dagaggikew ggclpgnlrl agidpaaidt vllthahpdh vgglvnaagh
      121 aafpnaelva hrrevefwrd dgnlsraser argnfriarh afdaygdalr tfdegevlpg
      181 iaaiplpght dghtgyvles gdqgllvwgd ivhfphiqik rpdvsiafdq dasqaattrs
      241 rlldrvsaeg lliagmhlge pgfarirrtn geyglfyetd a
//
LOCUS       WP_175975999             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175975999
VERSION     WP_175975999.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33411
     Region          23..80
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          111..303
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(124..125,127..128,131,135,137..143,233..238,
                     244..245,247..248)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 misdqngese sqsirtnlps lmalrcfeaa arhehfsraa delcvthgav sravrlledd
       61 lgvalferrs rrvflteagr tlaqavhdgl glmrhaahal radaararrs vlsceptllm
      121 rwliprwpdf qarhagvdih laaaggpfsf dsgvdmairr ndfawpagyh aehlfaerig
      181 pvcrpdkvga wfasrrggrt lkpdaallht rtrpdawnaw agaanqpavn grgqkfdhfy
      241 fslqaavagl gvaigpwhlv rddiesgvlv apmgfvedgs dyylltpapv adgsaqaall
      301 gwlrgrv
//
LOCUS       WP_175976007             192 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter small permease [Burkholderia sp. BCC1047].
ACCESSION   WP_175976007
VERSION     WP_175976007.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..192
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=20201
     Region          33..187
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mtrrtslnga atvgspdaaa adgatpcrpr aaapvlrcvn dvlfrvlavi asaclavltv
       61 lvfyavvmry vfenapdfve pialllvivi amfgaamkvr dgghigldsl vrrlspkart
      121 vviaiqhlsl iafaimimig cgsmaaetmg dripiiglpe gvrylitmpa avaiiffsle
      181 hllalrrsss gq
//
LOCUS       WP_175976011             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC1047].
ACCESSION   WP_175976011
VERSION     WP_175976011.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..359
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37995
     Region          159..356
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mikvflilvr nellgylrsr sslfwtlvfp vfllsvmlfa fggsgslgta dvafdlpgga
       61 tpynqacqaq ivaslshsdt vkatfggrga padrvivvlg adertpatir ydfngslavk
      121 aasrvveial arcaaqrlgl paaqarfena aptrrpfdyg affatgilvm afmaiglnst
      181 ttaiaalrer ntfklyvcfp vsrgvflaal ivarmammal salvlltvar vafgialpia
      241 tpdglralpi vllgaamvls igvllasrtr slaaaelacn vtyypllffs dltipmhdap
      301 awlkaglafl ptnqfavalr galvdgapya qlapqllgmt actalflfaa arlfrwhda
//
LOCUS       WP_175976020             327 aa            linear   BCT 11-JAN-2025
DEFINITION  ferritin-like domain-containing protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175976020
VERSION     WP_175976020.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10090058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..327
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36640
     Region          98..228
                     /region_name="Ferritin_like"
                     /note="Ferritin-like superfamily of diiron-containing
                     four-helix-bundle proteins; cd00657"
                     /db_xref="CDD:153097"
     Site            order(107,137,140,187,217,220)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 mndtltvmqd tadirwsmpv dalmsndytl reealnrlye kakaaqwdva tdvdwnhdld
       61 panplgmpdp tlliygtelw gkladadkhe vrhhaqgwll sqilhgeqaa licasklasa
      121 englsarlca aaqmmdearh veayaklvne kldvsypmsr slkgllhdti tsnaldmtnl
      181 gmqvlvegia lsifqsvvay stdpfikdlf lriqrdearh favgritlcr vyaemsshel
      241 rereeficeg aavlyehlca ddiwepmgls krecsamvre spvsssirrs ifrrlvptir
      301 emglltptvq atfekldvld yaampln
//
LOCUS       WP_175976040             378 aa            linear   BCT 11-JAN-2025
DEFINITION  sialidase family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175976040
VERSION     WP_175976040.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 378)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 378)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..378
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41034
     Region          <40..>133
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Region          85..121
                     /region_name="Sialidase propeller 4"
                     /note="Sialidase propeller 4 [structural motif]"
                     /db_xref="CDD:271234"
ORIGIN      
        1 mtcaamvana asvpappgev iahspaatrv ylgspslall pngdyvasfd tfgaaaaqnr
       61 vsvfashdkg atwsrlagvp dqywsslfvl ngalylmgtn rsmgtpsirr sddggaswtt
      121 pvdastgllp ypgrfitgpv pvlvdrgrvw rayesvdggd lratvlsapv drdlldarnw
      181 rmsahlssdk rwldgtfqsw eegnvvgrqg aapvvmlrvn tangpekaal vttsddgrtl
      241 sfdptrdfvd lpgagkkfti rfdpqskqyw titnavpksv gpanlervrn tlvllsspdl
      301 rrwtarrill qhadkkrhgf qyvdwqfdgs dlvavlrvaf ddpeggaasq hdsnfitflr
      361 vrrfrdnaas taltqelq
//
LOCUS       WP_175976052             310 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia sp. BCC1047].
ACCESSION   WP_175976052
VERSION     WP_175976052.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..310
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33430
     Region          30..285
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(45,131,133,135..136,165,219,240,243,254,256,285)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mnapirnvqp vieslgneas gelvpsryav rigdvdvvli sdgvlplpts tmstnvsead
       61 rnawfdgrfl qrdmfdwaln ialvrsadrl ilidsgvgdg feyftragrs vmrlesagid
      121 laaitdivit hmhmdhvggl nvdgvkaklr pdvrihvsaa evafwkkpdf sktvmpetvp
      181 palrkaaatf velygenivp fdrtvevaag vsarvtgght pghcvvdias kgekltfagd
      241 aifevnfdnp dwqngfehdp daavdvrlal fneaadtgal laaahvafps ighvarhgdg
      301 frfvpvvwdy
//
LOCUS       WP_175976075             260 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_175976075
VERSION     WP_175976075.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..260
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=28479
     Region          28..233
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mthqatdava yangmielsh sfdanrflaa idrdelatlt phlqlvhlks gqvlcepgem
       61 laavylpvtt aislqyvssg gmtlevaeig sesvvcddvi ggsgrmpcra vacrdgfvyr
      121 ldrrvfataf easpvirhlv fvcvrllmaq vaqitfcsrh hvlkhqlcrw fllafdrtrs
      181 ieiqvthsml aqmlgvrret vtdaageiqk lglirqyrss ieladldgle kmscgcraiv
      241 rdemkrilsa dsgvpaasra
//
LOCUS       WP_175976120             182 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Burkholderia sp. BCC1047].
ACCESSION   WP_175976120
VERSION     WP_175976120.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..182
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19932
     Region          15..166
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtaaelsaml pamlprlwtf alrlsgdrhd aedlvqcacv ralerahqlr pgtvplswmf
       61 sivqstwlne lrarsvrrrs gmdwdddlle tisdpaaptl eqqaldaqiv ravqqlpeaq
      121 ravmllvsve glsyseaadv ldvpigtims rlsrarqaig alfadrperp vksaansedq
      181 ga
//
LOCUS       WP_175976153             221 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC1047].
ACCESSION   WP_175976153
VERSION     WP_175976153.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..221
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23452
     Region          1..218
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msfklylsfl aasvvliyap gpvnlltmnq alrtgwrral pcvwggtlav llqlaltalc
       61 lnslvhldeh altvlrwaga aylvwlgakq wlnrapvgad aapaeagitg agtaiaapdi
      121 dsgralfwrg vatsglnpkt llffpsffpq fisptadwsl ngqylllaat fallfaggva
      181 smalfshrls ralqrparmr amnrvtggll vgmgaimvgw n
//
LOCUS       WP_175976167             125 aa            linear   BCT 11-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175976167
VERSION     WP_175976167.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10577308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..125
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=14082
     Region          9..101
                     /region_name="SnoaL_2"
                     /note="SnoaL-like domain; pfam12680"
                     /db_xref="CDD:432716"
ORIGIN      
        1 mlqdpgdvar asyrayvdkd rdaiealiap dfhftspldn rldrdaylar cwpnsamlaa
       61 fefvdvavhg eyvyvvyeav ttagrrfrna erlrvhdgrl veaevyfgwy vphpapdggf
      121 iesgr
//
LOCUS       WP_175976204             341 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175976204
VERSION     WP_175976204.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..341
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36539
     Region          11..324
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mttsprrral iaaglgvlgv lgaparvrak prtvriskgy gvlylpllvm ekqrlferha
       61 arhgvrdvav ewvlldggns vndammagtl dfaaagapgf ielwarargi pnvevigisg
      121 lsttslslna nraglvslrd ftpsdriavp girtslsavv lqmvasrqlg pthfaqldsi
      181 tvnlphpqam qalirrengv tahftsppfs tlelrqpgih rvvnsvdvlg pltldvvfap
      241 krlvdaepal aaaflgalde anrmiaqdpr aaaalyasss gvgvshddvm rmlaapdtrf
      301 svlpnqlmdy veflylagti kakprawhem fapmlddyrs g
//
LOCUS       WP_175976226             343 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175976226
VERSION     WP_175976226.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..343
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=37895
     Region          33..92
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          123..323
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(138..139,141..142,145,149,151..157,249..254,
                     260..261,263..264)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mthsapgrpt arpepaphds datdglrvqd ldlnllktfr avyeerhvgr aalrlgvtqp
       61 svsyalgrlr lmfrdalfvr tgtgveptpr aqrlaisvdk alailqhvld egsrftpdst
      121 qrvfrlhmsd faasaflptl laafdrrapg avietlhvde cqlnvalesg ridfalghfa
      181 dasshfqrta llhercvllt prrtaqrvgl pddfvldgta pdalrfvavt shpqsmqlle
      241 rhelmprvra alpdfmvvpa llqdgdyali lpetiaitfa arqpcvlyei agagewavna
      301 ywhrrfdadp ghrwlralll elfnigeqap fdawlapqpp aca
//
LOCUS       WP_175976265             396 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175976265
VERSION     WP_175976265.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..396
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43508
     Region          68..333
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 msfplepdgp lsrdvappqf gvdgeqaerd wplithdeva avlaridgvg epvrltwhsp
       61 rqfaaavlvr madgrglfvk rhhaslrdva gleeehrfia hlrergmpvv dvladrhgat
      121 afasgewtye vhvlapgvdp yrgvmswqpf thashayaag ralaelhras agyaaparpv
      181 rtllssfrvl ssadlagale rwvdaqpllv ralgsrdwrg dvadaigpyh arlvpllptl
      241 tplwthgdwh asnllwtdag pgaqvrtvld fglsdrtcav mdvalaiern tvdwmapada
      301 rrveydqida lldgyeslep lsddayaalv allpivhtef alsevayfgc iidapgivdi
      361 aydgyligha rwfgerdgrq lldwlvqrrr akqgrv
//
LOCUS       WP_175976243             285 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175976243
VERSION     WP_175976243.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..285
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31132
     Region          29..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(32,57)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(39..40,51,54,58..59)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          105..270
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 madapdnllg aylrdrrakl dpaalglpat rrrtpglrre evaqrahvsa awytwleqgr
       61 ggapsadvld rlaralmlnd aerehlfllg vghppevryh apasvtprlq hvldsldasp
      121 aiirtatwdv aawndaaaat ltdyatlppa arnilrlifv dagvryaqpn wervarfavg
      181 afradvarsg atqsvqafvd emratsaefd amwrdhdirt hdegtkeirh pqagrialey
      241 safsvtgspd lslviftpvt padrarirel vaareqarav qapaa
//
LOCUS       WP_175976309             415 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175976309
VERSION     WP_175976309.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..415
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=45520
     Region          8..>119
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mnrqqswtrt aapgeiiyse gfagepvifl itdgkvelst rcddkrviva tlgrgeffge
       61 sallaaepra htakalsfcq ltvvpagild eeiervsall rhivrtmirr vkrkddqlat
      121 ythadfmpgv lsyahvlslm agadaresgd twarramqah aaetsvplae virkcraiag
      181 hsrphvlaml rrmeklnlvt ieaaqgdagg atdhatssda rqvvtfdaar vidraqqvad
      241 hdldvsinse lelieladle sligvdktll lnklsngeia eevfafrksk vlnyveqkgv
      301 ayfsrrngrr ggdvraledl vwidqrtlfd visafdtydl aklianlddr avadklfsvm
      361 tearrnevsw vmrrelkldp veiedieqrv ldavraakap aagaasvaat lssda
//
LOCUS       WP_175976275             241 aa            linear   BCT 11-JAN-2025
DEFINITION  ZIP family metal transporter [Burkholderia sp. BCC1047].
ACCESSION   WP_175976275
VERSION     WP_175976275.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Dempski,R.E.
  TITLE     The cation selectivity of the ZIP transporters
  JOURNAL   Curr Top Membr 69, 221-245 (2012)
   PUBMED   23046653
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Guerinot,M.L.
  TITLE     The ZIP family of metal transporters
  JOURNAL   Biochim Biophys Acta 1465 (1-2), 190-198 (2000)
   PUBMED   10748254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..241
                     /product="ZIP family metal transporter"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24377
     Region          27..235
                     /region_name="ZupT"
                     /note="Zinc transporter ZupT [Inorganic ion transport and
                     metabolism]; COG0428"
                     /db_xref="CDD:440197"
ORIGIN      
        1 mtptaklall tlppvlaacf galaaawrap gpitssviqh ftggivfaaa alellpqdra
       61 halfpvvvgf vlgialmlai ralsgaietr feqarlpvsl iivtaidlvv dglvlgiafs
      121 asdesgiilt valtlevlfl alsvsaalaa agigrmlsiv vpvalaalls vaavagnaaf
      181 aglpanvyav llglgtvall ylvteellve ahevpetpfa taaffigfiv ffliegsvka
      241 g
//
LOCUS       WP_175976375             337 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC1047].
ACCESSION   WP_175976375
VERSION     WP_175976375.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..337
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34354
     Region          23..337
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mnlpessstp sttlaatagn gdappprpmw aqlrrstlfy plvglivvci ammiaspsfl
       61 saanlenvlr qvsinaiiav gmtcviltgg idlsvgsvma lsgtlaaglm vagvnavaal
      121 aigiavglgf gflngvfvaf agmppiivtl atmgiargla liytggypid glpdwvaffg
      181 sgkvlgiqap vlimlvvyai awllldrmpf gryvyaiggn eqatrltgvr varvklivyt
      241 lagltsalaa ivltgrlmsg qpnagvgfel daiaavvmgg tsisggrgai lgtlvgalll
      301 gvlnnglnmi gvnpyvqnvi kggiillaiy isrersr
//
LOCUS       WP_175976404             243 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175976404
VERSION     WP_175976404.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..243
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27005
     Region          63..238
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <177..238
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mstlsaptdh apadwrralr acvdafdafa spsaivfyrl dqsgepadfe lfgmpesmhr
       61 tyvaryrmld plhpsrcaag ecavvtlasq lpderraasa ywtrflrrhd vadvveiwlr
      121 ddagrtvgaf sllrfgigda ngngtarrfa pgeidalarl qpvaeaalsp llrarrgihr
      181 idcaerltyr eeqiarlvrd grsnkeiard lalgpptikt hlmrmyrklg vsnrtelvga
      241 lfl
//
LOCUS       WP_175976423             784 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175976423
VERSION     WP_175976423.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 784)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 784)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..784
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=86556
     Region          19..737
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mrtiqdvlkh pnsvvtqplh leiaaldapv svlsfvltee mntrfladii vtsqdkridg
       61 ativgqpavf tieehasvps maavidpvrh aartvhgvvt qwtrvktsrd eatyqvhlkp
      121 rfslleevhd savlldrsfr ellsdmivdr nlfqsfdvef elegldgkle qtvmyeetva
      181 nfidrhcrra gvyyyfkqak keegpqrdtl vfgntprgym ralevplmph sgltswheai
      241 ltlevtralv pqtvrewdrn yrrpddplqv esivahddrs vygsvncsie hfhsveegqa
      301 ladarrdell trqvrltgts nvigmtpgmv vritndevhe aphgmvitkl vttgsrsqsv
      361 vntfeaipah qtyrpeyvpe khwrwiagml igvvesgdde pyawmdeygr yrvrllftrh
      421 sgkrgtnsmp lrvlrtsasy qgglhipllp rsevrvvatq gncdrlliag alhdharrdl
      481 vhgkegwysr avfrspllgn klrfedlkdh egirlatvfg qsslnmghlv drdknkrgqg
      541 felttqnwgt lrapkglfvs adaaggsetp hldmpaaiaq lktalqrvtd laaattqaka
      601 dpadratqta llegldqlrd agllasapgg iafvtpkslq qstgenvivt agrdmdvsiv
      661 rrlrmvagdl islcahklgl nfvaakgkvm maaltdgmdl fakqqlrvas qsadvqvsak
      721 skitlnsgga slviengnmt fhcpgaftik aasfsfhgpn nvttplpslp qanlkisdry
      781 sssh
//
LOCUS       WP_175976451             215 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175976451
VERSION     WP_175976451.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..215
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23286
     Region          7..203
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mtsthsltfy tadtpnghki aiyleeagla hdrvqvnlsa geqrspayla inpngkipai
       61 vdhdtglavf esgailsyla aktgclqpet laertavqqw lhfqiggigp mlgqlwwflr
      121 asktgnaeav dryrkealrl ygvvngrlse saylassrys iadiaafpwl rtadeldldi
      181 agfphverwl adiaarpavq rgliacrast aeaah
//
LOCUS       WP_175976447             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1047].
ACCESSION   WP_175976447
VERSION     WP_175976447.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46471
     Region          23..427
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(35..36,39..40,43,82,140..141,143..145,148,168,
                     171..172,175,258,261..262,265..267,270,298,302,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mpdtmstlaq paahaprrvr nsrlatasmi gtslewydft iyntlaalvf nhlffpsvdp
       61 lagtilafst yavgyvsrpl ggfvfgnlgd rigrravlml tlvlmgvtta lmgalptyaq
      121 agilspillv alrfvqgval ggewagavll svehgdqkrr glsaswtqig psfgtllgtg
      181 cialvtlstt sdnflswgwr vpfaasallv afgfwvrrgv detpqfeqla eshataevpv
      241 advlkyhwkr lliaggsrig sdvlyalivv ftltyvttvl hlsrpvalta vmigtacnal
      301 avpffgalsd rfgrrpvyla gamagivwaf vfftlldsar pvaivaavai glvihavmyg
      361 pqgafvteqf ptrvryagss laytlagivg ggfaplviaa lfrqtgttta vslyvtaalv
      421 vtsialvaar etahrpled
//
LOCUS       WP_175976459             207 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175976459
VERSION     WP_175976459.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22175
     Region          6..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maergrprsf dkeaaldram evfwrlgyeg asmtdltaam giaspslyaa fgskealfrq
       61 alehyrateg reiwggvera asahdavqsy lmdtarvftr rskpagcliv lsalhpaers
      121 dmvrqtliam regtvdalre rlaqgvaage isahanvdai aryyvtvqqg msiqardgas
      181 rrdleaiaqa alaawpalvg tsstasg
//
LOCUS       WP_175976496             269 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175976496
VERSION     WP_175976496.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..269
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29454
     Region          19..98
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(44,69)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(51..52,63,66,70..71)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          117..267
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 msqlssvpvp pldatparal gefirahrer lspqavglpp gprrrtpglr reevaqlcgv
       61 sptwytwieq grpvsasada lariavalql skaeraylfe laaqrdpaep dvaggdlppt
      121 laatvaaiat payvldrqwn alawnapaaa lfsgwldgeh drnllrftfm spaartlivd
      181 wetrarrlaa efradairhl tdaptralid altagsdafa qywasqdvfe regglrefdh
      241 padgrvvyqq itlkpahred lklvvlvrd
//
LOCUS       WP_175976500             780 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175976500
VERSION     WP_175976500.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 780)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 780)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..780
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=81878
     Region          49..777
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mrhagpgrpt aaplalaltl alralavcaq papvppaaas eaaaqadgly ldvslngept
       61 hriagfrqid grlyaasadl ndlgiatggp anapsntlva ldtlaglhyd ydagrqtldl
      121 rvpdalriph tfdtralaaa ppatsgrgfv lnydayaqtv ahaplavwse aryfdpagvf
      181 sstgiaylyd drrryvrydt swtrsnpgtl tttqvgdtis sslswtrslr lggvqwrsnf
      241 glrpdlvtfp vpalsgsavv ptsvdlyvnn vrqfsgnvps gpfvinsvpg itgagnatvv
      301 trdalgraia tsiplyvdtr llapglasys veagflrray gtdsfdyart paasaslryg
      361 iserltveah geatagvyna gagvlarlge rgvanaslal sapgrtgvqa gigyqyvtsr
      421 fsidaqtlra fgdyvdlgsr egvpvsratd rvtvsfpflr aqtlsfsyla lkypgvaasr
      481 igslaylvnl ggltsitfsg fqdfrqrdar gffvslsigl ggntsvsana grqngestyt
      541 lnasrppdyg ggfgwnvqag anagtrygqg qlqylgragq ltllaqsfdg rgnaaadvtg
      601 afvlmdgrvm tarrvddgfa lvstdtgrvp vlhqnrpiga tdragyllvp dlnayqnnrv
      661 aidgsalpad ariadttldv vpqarsgvla hfaitrysaa sialhasdgt plppglevrh
      721 vesgqrtivg ydgltfvdgl vetnhleisg ggrdctvefa yrrpddgtlp rigpltcspr
//
LOCUS       WP_175976530             309 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175976530
VERSION     WP_175976530.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33838
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..294
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdkldqvrif lqvaemgsfi kaahaldvpr atvsaavqql etalgtrllh rttrqvqlta
       61 dgalllergr rllaeadeld rlfrrrdrdv vgrlnvdvps riarrvvapa lpslfrrhpk
      121 lqlslgstdr aidlvqegvd cairvgrlad sslvvrplgq ftlincaspd ylrecgvpeh
      181 pdalahghwa igyaspttgr elgweycadg qrhmltlpsr vivnnaetyi ascvagmgli
      241 qiprfdvehl lasgalvdvm pghraapmdv savyphrrhr srrlnafiew fgalmadaln
      301 dadasgsgd
//
LOCUS       WP_175976533             238 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Burkholderia sp. BCC1047].
ACCESSION   WP_175976533
VERSION     WP_175976533.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..238
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=25756
     Region          6..224
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mdlesilytq gfgsrrqcrg lieagrvava gavapypdap fdtdglvftv ddtawpfhar
       61 aylalnkpag yecsrdpqhh asvfsllpap lvargvqcvg rldqdttgll llsddgqfvh
      121 aytspkrkvp ktyvatvrhp lddaqlhalr tgvqlhgepk piaavaadar aphtlaltvl
      181 egkyhqvkrm vaaasnrvel lhresiggft lpadlapgaw rwldeadlsm lrnpvqtl
//
LOCUS       WP_175976545             459 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia sp. BCC1047].
ACCESSION   WP_175976545
VERSION     WP_175976545.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..459
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48977
     Region          7..457
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mtrqqrsfda ivareqglrh altsgqmami aiggaigtgl flgsgfaigl agpsvlvsya
       61 igalialllm galaemtvah ptagsfgaya ehyvgplagf lvryaywfav vfaigteisa
      121 iavfmkywfp avpgwywvig fsalliavnl asvtlygtve yafsllkiaa ivvfivlgaf
      181 lvwsapaass igfanytahg gfmpkgpwgt wiavivaifs ymsieavaia ageardpqha
      241 vtrafrstvf rlvlfylltl almlaivpwt qagtdespfv kvmaathvpy aagvinfvll
      301 iaalsamnsq lyvttrmmfs lsraqlapav fgrlgangvp raalwistsg vavaavlval
      361 apdtaftvmm aiamfgalft wlmifvthlr fraqyrgpal afrmwghpfg sllgaglvaa
      421 illttaftre frmtmvvgvv favlltlaya lhyrhqhar
//
LOCUS       WP_175976572             252 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175976572
VERSION     WP_175976572.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..252
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27017
     Region          1..245
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mirleridks fgahrvlsgi dlalqpgsvt aligpsgsgk stllrcvnll evpeagalvv
       61 gdaridfvsa rrpsrdamfa vrkqtgmvfq nfqlfphlsv vqnvmeglvt vqrwpreqar
      121 qralalldkv giadkadawp atlsggqqqr vaiaralaps pqvllcdept saldpelsve
      181 vvevlrqlar egttmlmath dlrlaasiah davfladgci veagpsrdvf grprdprtak
      241 fvatlaqgvp vf
//
LOCUS       WP_175976603             349 aa            linear   BCT 11-JAN-2025
DEFINITION  M48 family metallopeptidase [Burkholderia sp. BCC1047].
ACCESSION   WP_175976603
VERSION     WP_175976603.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Lew,R.A.
  TITLE     The zinc metallopeptidase family: new faces, new functions
  JOURNAL   Protein Pept Lett 11 (5), 407-414 (2004)
   PUBMED   15544561
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..349
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37022
     Region          134..317
                     /region_name="M48C_Oma1_like"
                     /note="Peptidase M48C, integral membrane endopeptidase;
                     cd07331"
                     /db_xref="CDD:320690"
     Site            order(200..201,204,257,261,301)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320690"
     Site            order(200,204,257,301)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320690"
ORIGIN      
        1 mrgnrprrla haavalsvga aalaatlaha tdtgataags apaaaqtapp aaatsaapvp
       61 psaegaqptg aavpakaytp tppqvrygna iafrtlipsp lleqltaney aqivqtaads
      121 nrllpanqpr vkrlraivak lapysvkwnd rvkswawdvn virsrdirlt clpggkvlvy
      181 ggmldrvrln dddfgvllah giahalreha rsnfsvasqt slraaalppl fgvgdplpqa
      241 lnlgerlqsl hydptdetea dviggdiaar agfdpraait lwdklavatr anktsgfiyt
      301 hpystarrqd llnrlpdlmp lyakatgkrv eslpdyagis aqrrkivrr
//
LOCUS       WP_175976612             404 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent rRNA methyltransferase [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175976612
VERSION     WP_175976612.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..404
                     /product="class I SAM-dependent rRNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=43611
     Region          3..403
                     /region_name="RlmK"
                     /note="23S rRNA G2069 N7-methylase RlmK or C1962
                     C5-methylase RlmI [Translation, ribosomal structure and
                     biogenesis]; COG1092"
                     /db_xref="CDD:440709"
ORIGIN      
        1 mqtvtlkpsk eksllrrhpw iyanaidrvd gkpapgatvl vrahdgrfla rgayspqsqi
       61 rvrvwsfdeh epidhaffkr rvqravahrt tmvsdtgavr lvfgeadglp glivdyyvad
      121 taeagaaprg qlvcqfmaag veawkdaiva altgatgcpn vyersdvsir dkegleqttg
      181 vlagdappat lianengvry hvdvpnghkt gfyvdqrdnr alvaqyaadr dvlncfcytg
      241 gfslaalkgg akrvvsidss gdalalaqqn vvangfdaer atwldadafk tlrrlvdege
      301 rfdlivldpp kfaptrdsvd raaraykdin lsgfkllrpg gllftyscsg aidmdlfqki
      361 vagaaadakv darilkrlga gvdhpllaaf pegeylkgll lqiv
//
LOCUS       WP_175976619             257 aa            linear   BCT 11-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175976619
VERSION     WP_175976619.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..257
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28557
     Region          12..253
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mssplqsesi raqvaelrer gfvvarglvg eaqcaalrqi aerqlreaae piefeadlry
       61 pgapeskhap gghtvrrlld aysrdpafaa raiapeigaw mreyfgeepv lsrahhncmm
      121 tkhpaygslt gwhrdfrywa ferpdmvsvw lalgpetnen galwlvpgsh taefgpeafd
      181 dakffrsdlp enrrmidaat cpslqtgdvv ffhsntlhsa gqnrsdqvkf slvytyhgas
      241 nrplagtrsa skpevqf
//
LOCUS       WP_175976626             546 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia sp. BCC1047].
ACCESSION   WP_175976626
VERSION     WP_175976626.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..546
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58362
     Region          1..528
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mqydyiivgg gsggsslagr ladacpdati alieagshte rnllvnmpvg iaalvpfklg
       61 tnygyetvpq pglggrrgyq prgrgmggss ainamiytrg hptdydewaq lgatgwgwqd
      121 vlpyfrraeg nergadawhg adgplsvsdl rfrnpfserf iqaahaagyp lnddfngatq
      181 egvgfyqvth rdgsrcsvar ayiygrnrpn lhvvpdatvl rvgfdgkrav gvvvsrngrv
      241 etlgaraevi lsagafnspq llmcsgigpa dqlrrhgiav vqdapdvgan lidhidfiin
      301 trvnsselvg vcvrgiakmt palvryfssr tgmmtsnvae aggfiksdps larpdlqlhf
      361 ctalvddhnr kmhwgfgysl hvcalrpfsr gtvalasgda rdaplidprf fsdsrdldll
      421 vrgthamrri lsqaplasqg grelytrpdq seaelrativ ahadtiyhpv gtcrmgsdvr
      481 avvdpqlrvr gvdglrvvda svmptlvggn tnapsvmige raadfivapr kggvprgeaa
      541 aavhgr
//
LOCUS       WP_175976637             271 aa            linear   BCT 11-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Burkholderia
            sp. BCC1047].
ACCESSION   WP_175976637
VERSION     WP_175976637.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..271
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30005
     Region          13..268
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 msadalslpf aephaapdei tavswnlhkg rsplgftawn amrdwmqsth advyflqeam
       61 arrmprpmla pgfgapmddt vddvwhcqat eiaqaldwqi algpnvfkps wrhgnailsp
      121 hpldlggrwd isahrferrg llvaratlag arpvtllcah laltraarlr qmhwiahwie
      181 rnasdgplml agdfndwrnd svalfgeigl sevatllges grtfpafspa laldkmfvrg
      241 ltplewraps geaawlsdhl pyiarlrldp q
//
LOCUS       WP_175976639             371 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia sp. BCC1047].
ACCESSION   WP_175976639
VERSION     WP_175976639.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..371
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38982
     Region          1..366
                     /region_name="LhgO"
                     /note="L-2-hydroxyglutarate oxidase LhgO [Carbohydrate
                     transport and metabolism]; COG0579"
                     /db_xref="CDD:440344"
ORIGIN      
        1 meqtdcvvig agvvglaiar elaargreti vleaadaigt gtssrnsevi haglyyprgs
       61 lkatscvhgr dllyefcdth hvphrrtgkl ivatsaaqvk qlkaigaraa engvldllpl
      121 traeaqtlep alecvealfs pstgivdshq lmlallgdae rdgavcalqs pvesidvlrg
      181 grfivrtgga apteidascv insaglgaqv lahrtrgldp rwvpplylar gnyfslsgra
      241 pfshliypmp draglgvhlt fdlggqarfg pdvewcdalr yevdparaga fyasirafwp
      301 glpddalqpa yagirpkvag pgeppadfiv qgaaqhgvrg lvnlfgiesp gltaslalaq
      361 rvgdmvsvsr a
//
LOCUS       WP_175976655             381 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175976655
VERSION     WP_175976655.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..381
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40487
     Region          1..376
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfqhtedrr mladtlnrfi aeqyafpvrd riaqsaegfd ramwqrfael gtvgalfaea
       61 dggfggagfd iavvfeclgr glvvepflga llagralala ggdahrerla alidgsasaa
      121 fahdepgshy elttvrtrae rsgdgwvltg akgvvdqaaq aaffvvsarv sgndddaagi
      181 glfvvpadap gvslrdyrki dggraaevrf ervalpadaa lgapdaldge agaallervl
      241 gygllalsae algamdvaka htldylrtrk qfgmpigsfq alqhrmadll leveearsav
      301 inaaaqldap ravreralaa akysigrigt lvaeesiqlh ggigmtwelp lshyakrlvm
      361 idhqlgdedh hlaryialsk q
//
LOCUS       WP_175976667             383 aa            linear   BCT 11-JAN-2025
DEFINITION  VanZ family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175976667
VERSION     WP_175976667.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009512
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..383
                     /product="VanZ family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=41125
     Region          23..117
                     /region_name="VanZ"
                     /note="VanZ-like family protein (function unknown)
                     [Function unknown]; COG5652"
                     /db_xref="CDD:444373"
ORIGIN      
        1 mnvpgthras plarqafaay aalivyasly pfegwlslgi gpfdylfapm qryvttfdva
       61 tnvlgylpfg algvlalhpr wrgvaatlia galgvllsga mealqtylpt rvasnldlga
      121 nalgallgaa laapatgall drgalrrlrf awleadgstp lllaalwpfa ivfpspflfg
      181 igdwpaalwe radasmqdal lawlpaawrv sewpervdgw lsdsaweavl gglmlfaala
      241 iaslamrpra prirllialv vatlvlkaaa tfmqsatglv vvwatpgarl gielgfaaal
      301 valrvpatwr amlaalalla gvalvnllpv npffdftlsg wrqgryvhfn slarwlawiw
      361 pyaaliwlgq rvehawlpaa lrr
//
LOCUS       WP_175976736             261 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia sp. BCC1047].
ACCESSION   WP_175976736
VERSION     WP_175976736.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..261
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=27331
     Region          9..242
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 merkplvgit adltqigaha shtvgdkyva aivdgahala mvlpalgerq svgdildtvd
       61 gllftgsysn vephryggep sepgtkhdpa rdattlpllr aaivagvpvl avcrgfqeln
      121 vvcggtlhqr vhdvpgfadh redddapmdt qygpahvvrl tpggklhala ggrdeahvns
      181 lhkqgiaqlg sglaveafap dglieavsvv dapafalavq whpewrhaqd plssaifraf
      241 gdacrarrae rtramaaaal a
//
LOCUS       WP_175976748             204 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175976748
VERSION     WP_175976748.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..204
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22376
     Region          1..199
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mklyywpktr afralwmlee igvvyelvpi dlrsheqgsd afvqvnpmak lpalddgsap
       61 faesgavlly ladrcpaagl gvapddplrg rflqwmfftp tclepamaek ftgasgnpva
      121 fgwgniarvq ralaqalahs rwlvgerfta adlllastlk iafdahllph egvlgdyvar
      181 aedrdafrra vaieqreaar llha
//
LOCUS       WP_175976754             291 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175976754
VERSION     WP_175976754.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..291
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31838
     Region          52..285
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mlkpevdslv phvpfsrrkf mqaalggtfa aavlpvsaqt vttdsagldv dtieirsgda
       61 sipayraqpi dktnlpvviv iheifgvhah iadvcrrfak lgylaiapdl farqgnaaky
      121 ptmkelydhi iskvpdrqvt edldataawa gknggdlarl gvtgfcwggr qawlyaehnp
      181 hvlaavawyg fvegktdemt pfnpvdhasl lkvpvlglyg ekdqnitqas ladmrkaiqa
      241 sdskrarese ivvypdagha ffadyrpsyv kgdaedgwkr aiewfhkygv m
//
LOCUS       WP_175976755             444 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia sp. BCC1047].
ACCESSION   WP_175976755
VERSION     WP_175976755.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..444
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=48144
     Region          14..426
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mhriiivggg agglelatrl gdrygargnr paralvtlvd rnpthiwkpl lhevaagsmd
       61 pftqeleyaa qarwhgfefq qgeltgldra akrvtlspln dsdgeellpa releydtlvi
      121 aigstthffg vqgapenaia ldtvgeaerf rkrliaacmr aehqtpapta pgesaepriq
      181 vvivgggatg velsaelrnt aqvlsvyglh kldprhdvgi vliesgpril palqervsta
      241 taelleklgv rlmlservte vapgfvhtas gkavradltv waagikapsv lshldglqvn
      301 klgqldvrrt lqtftddnvf algdcaacaw pgnernvppr aqaahqqasf llkaigcrle
      361 grpqpeftyr dfgslvslgh fsavgnlmgg liggnmlieg lfarfmymsl yrlhiaalhg
      421 yprmmldtva hwlrrttlpr vklh
//
LOCUS       WP_175976775             235 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia sp. BCC1047].
ACCESSION   WP_175976775
VERSION     WP_175976775.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..235
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24662
     Region          51..149
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 msrpasaakf dpsraheyae qsrialagyd acheltacml asaigaadar ilvagaggtg
       61 qeicvaaale pgwrftavdp sapmlalars nveaagfgar ttfvedgvda lpdvaafdga
      121 tligvlhhvp gddakaallh aiarrlkpga plvlagnhrr yadhprllda wqqrwrmkga
      181 tpdavraqla kilqgadppa seeavfallr dagfdaplrf faslfwgawi avrha
//
LOCUS       WP_175976758             330 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175976758
VERSION     WP_175976758.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..330
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36259
     Region          6..330
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpliriwavd ralasgiaap tdiltaanhi assmppcrpa tpfrwrvesl ggrpvrtasg
       61 qvvpvdgaid ggsaadaiwl tgpfvadldr lldrpaslap lfdalrrqha rgtliatyct
      121 gafllaeagl ldgrvatthw skapsfrary pdvalrasdv lteqdgilcg gavtsyqnla
      181 lrvvdklana rvaasvarlm lidmnrdsqd sfidldrmgh hghhdpaiar aqrwmekhlr
      241 epfslarlsd hvamsertlh rrfrdavgap plrylqtlri evakrllaet klaietvcer
      301 vgyadisgfr qlfkretgts pseyrrrfar
//
LOCUS       WP_175976826             259 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Burkholderia sp. BCC1047].
ACCESSION   WP_175976826
VERSION     WP_175976826.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..259
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=28822
     Region          2..220
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mnvlivyahp eprslngalr dfavahleaa ghavqvsdly amnwkavlde ndvtdrapda
       61 rfdpaldskr afaegtqred iareqdklkw adavilqfpl wwfsmpaimk gwfervyayg
      121 faygvgehsd thwgdrygeg slagkramiv vttggwephy sprgingpid dllfpiqhgv
      181 lyypgfdvlp pfviyrtgkm ngarfdetcs algqrldelw ttppipfrrq nagdyeipal
      241 tlkdeiapgk vgfaahlaa
//
LOCUS       WP_175976856             261 aa            linear   BCT 11-JAN-2025
DEFINITION  peptidylprolyl isomerase [Burkholderia sp. BCC1047].
ACCESSION   WP_175976856
VERSION     WP_175976856.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..261
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=27783
     Region          100..247
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mndvrpeapa alringvaid gdavaaeaah hgdapdplda arralavrel lrqravslal
       61 lgedapldda avdallgrel thvpepdrad ceryyaqhsa rfrrndivya shvlfamtdr
      121 vplaplrqra eaaladvvaa pdtfeavara ssncpsaevg gslgqllrgd tvpefeaalf
      181 dtdglgvlpk lvntrfgfhi vrierrvpgd avpfdeaaaq iaaylservr qramrqyvai
      241 lagsarvegv afdgangplv q
//
LOCUS       WP_175976893             456 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia sp. BCC1047].
ACCESSION   WP_175976893
VERSION     WP_175976893.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..456
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47606
     Region          233..411
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mrsdlrfrva reqgrpaprg vhrfpigral lhgivaaacv agaqgaaaqa fhdavlaapa
       61 taettdlddv pffnaarttw gglhassapl dvayvshaln vsidagrgdp vahfgacvay
      121 rvlcetarda vergyasrfh yglasalpat galpalargp vdlasaepft laqpdrgtra
      181 gaivgslhas laradlppgv atqigrmlag rvdpkqrgah gdtfrvafep dhdaarpgrv
      241 rvtaldvrfr gqhvaavwfa pqagspgayy eldgmplaga rfampvaatr isspfgarvh
      301 pvsgarhvhs gvdlaapagr avhasergvv tfigtepsgy gkyvvirhdg gyasyyahls
      361 afeptlrtga rvmrgqrvga vgstgtatgp hlhfevrrha rlvdpielvq aanvaklkge
      421 qrvafnrvar dariqlasat faqpvamska vaphag
//
LOCUS       WP_175976894             289 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175976894
VERSION     WP_175976894.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..289
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31821
     Region          11..277
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mfldhlhper wtflwnalst lslklsagla llvagwwlsk rvgnwlnrll snkervddtl
       61 rpilcdvavw girivaivga lsqlgietas ivavlgaagl aiglalqgtm qniaagimll
      121 llrpfkvgdy idggsgvagt vdevglfmtr ltkpdgicey vpnsalwgsa irnytrnptr
      181 rldlevevsv hddieralda lralaaadpd vlqdpapdvm vmrfddstav anmrvwthtd
      241 tfwamrwrla rqvrktlaea dctlpirtre lhivhdaerr agdarvrvs
//
LOCUS       WP_175976904             452 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia sp. BCC1047].
ACCESSION   WP_175976904
VERSION     WP_175976904.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..452
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=48429
     Region          17..434
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mdnitpnlat araprlpriv ivgggagglq latrlgdtvg rrrhaeivlv drypthfwkp
       61 llheaasghr dpashtieya aqakrhgfrf vqgalqrvdr aartatiaav hdaegteilp
      121 qraldyddlv lavgsvtnff nvpgaerhal plenldqaed frrkflaact kanhaaeqqp
      181 arraapicin vigagatgve laaalrhaiq qlttyrfkal vsardvhirl ieggprilpa
      241 ldarlsgkmh aqlralnvdv lidtrvaevg adavttatge rlasditiwa agvagpamlr
      301 digdialnrs nqvivtdtlq tpddphvyaf gdcaacpsag asgclppraq vahqqavylv
      361 nafarriagk pvagftfhda gtvvslgqag avyqadigvr srslivdgla aiglykflyr
      421 khlfsvvgmk ralfqslshw lqsrnqpsik lh
//
LOCUS       WP_175976932             223 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia sp. BCC1047].
ACCESSION   WP_175976932
VERSION     WP_175976932.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 223)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 223)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..223
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23263
     Region          31..130
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          130..222
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mkrtwmigaa lvlaggmaag vlygpdlvdg mryqkalaai geadkangga wsqlqetcvf
       61 chgaqgqsrn awypslsgqp atyiaaqlra faadqrrnay mgplsreldd akidalatyf
      121 arqaparnea vpadaaldkr gmalvearsc rachgsaltg kdpaprlagq gqlyletqla
      181 afrsgerhdp tgamnalaat lsgddtrava hylaglapdg aak
//
LOCUS       WP_175976948             397 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175976948
VERSION     WP_175976948.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..397
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42776
     Region          1..364
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 marivchals khydggpavl hpldleiadg efivllgpsg cgkstmlrmi agleaitgge
       61 lvigdavvnd lpsrernvam vfqnyalyph mtvydniafg lrrlkvpade idrrvrdvar
      121 ilsldalldr rpramsggqq qraaiarami ktpavflfde plsnldaklr tqlrgdikrl
      181 hrqlktttly vthdqleamt ladrvvlmrg ghieqigtpa elygqphtvf aagfvgtpam
      241 nfadgtierv ganvwvdcng arwplassrf aglqhgqqvk aairpnhlrl vaerdpppgt
      301 laltgtvelv ellgaealvt ldwhgqpcaa lvpapmapap gavvafrfde ealhlfdagt
      361 ernvtlpdan piahavppta atratppaat swsmsrp
//
LOCUS       WP_175977143             265 aa            linear   BCT 11-JAN-2025
DEFINITION  ComF family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175977143
VERSION     WP_175977143.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..265
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=27699
     Region          17..235
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mvrgsaertm rvvlsqvral vvrvaavtlp nrcalcgnls htvicgacda aywnearlrc
       61 evcavplgvg harsrgggrs rvgsasayrc etcrtapppf datlaladyr apldglargl
      121 kfharlalgg efaarlarlv ddtrgasgfd lvapvplshr rlvargynqa waiarplarr
      181 lgvpaeaall arvadtapqs rldrharrdn vmaafavagg vagrhvalvd dvmtsgatla
      241 aaaqalkaag avrvtnlval rtard
//
LOCUS       WP_175977164             333 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia sp. BCC1047].
ACCESSION   WP_175977164
VERSION     WP_175977164.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..333
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35014
     Region          106..304
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mkdkpdgvvl psrvvpfpts isdearaalq rltgddgvpl nalhampavd didawmrvka
       61 sadahyatav aqfagslrsg vetirvgaad vhvatpeaap sgacaiidlh ggalivggga
      121 acragaqmqa drlgircygv dyrmppehpy paalddciaa yayvlqryap envviggrsa
      181 ggnlaaamvl rardeglplp aalvllspea dltesgdsfe tnrlvdvvlp aplmannlly
      241 angadlahpy lsplfgdfaa gfpptfiqsg trdlflsnav rlhralrraq vptelhifeg
      301 mphggfmgap edielsqeia rfvhahlhlh asn
//
LOCUS       WP_175977170             694 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia sp. BCC1047].
ACCESSION   WP_175977170
VERSION     WP_175977170.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..694
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=74606
     Region          44..683
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mrdlprlplr plsslslilf aaaahaqtdv paaadthtpa aaplapifvt anplgdteli
       61 aptvqlsgea ltrrqadslg etlnglpgvs tttygpmvgr piirgmdgdr irllqngvaa
      121 ydasslsydh avpedplsie rveivrgpaa llyggnavgg vvntidnrip reaiegvtga
      181 ldaryggans vragaaqveg gngrfafhvd afdretsklr ipgyarssqq raidgpdtpq
      241 pegnvpnsdg rvhggavgas ytwadgfagl sysgyesnyg svaesdvrlr mrqerlafas
      301 evrnlsgpft klkfdfaytd yrhkevdnge tattfrnrgy eariearhrk igpfegaigv
      361 qfgqntfsal gdemlvpstr tnsvalfgle ewqvvpalkl slggrfehvk vdpdpagiek
      421 fagarprdfn agslsagalf sltpvwsvaa nvayterapt fyelysngph datgqflign
      481 pnaskekavs tdlslryasg pnrgsvgvfy nrfsnyltey ntgrvvdddg apvapgtdgs
      541 lneaiyrgvr aefygieldg kwrafarrgh tvdleltady tharnvdtgq plpriaplra
      601 tlaadygygp fgaraqvtha wsqhrvpddd fstdgytslg vvltykfrvg pthwlaylrg
      661 dnltnqeiry stsvvrgfap qggrsvmagl rttf
//
LOCUS       WP_175977187             958 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia sp. BCC1047].
ACCESSION   WP_175977187
VERSION     WP_175977187.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 958)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..958
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..958
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=104029
     Region          42..957
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mknhglsrrg flkasvlagv avyvapigsr afaalfeekl ltpvkwdsvt giprfridgv
       61 akvtgskvfa rdvratdmph wpqqqshali lrvtqadrty egfdlsllgd elkpdrvvta
      121 ddlardgvaf pafygddmll pagktpaylg havailiyhd farfrfakna lkfrddviry
      181 gavtgplerd pwgtfryvrv ggktaydddv ysslkdapif psmmrkhlpv wpdgkehgkl
      241 deqgmflagq iaaeldqpsa dwlvfdreyn tqsvdtaale pdnancwyda atqslhlvvp
      301 tqsplevsen aaamvakcrf pvkklfvhpc ytvgygskdh fnvpfyglvc alyadgrpvr
      361 fandryeqfq tslkrhafkm hyriavdrnt gllqsfkgdf eangggrsnf spsvamvgat
      421 aaqsiyyfpk sdlaavaias raidagsarg ygtlqsmaat evavdeiaaq lnidpidfrl
      481 rnalrsgmkn tqgaipagal rvdevlerak qhplwtrraa rkaefeaahp gkrygvgfac
      541 vqkdfgtgae asfakvefda hgkvslhhta aeigtgmsts qavavakwlg rpatdvrval
      601 tewpdlpvet sgdpylmsqa dqdrlsanpr wspgyaspss atnsayyfth streaaravf
      661 ryglwpaams iwtrglgggq aapytiried arwvdgklta dglepltfeq lakqahalgl
      721 ptgavvhvfn rwqwtdaefe vggaverlpi dglslrvgap ktgddgplpg taapagatal
      781 rgtlpptang yrvldrkrvf ipptsrnnaa vtyytavgtl velavheatg kvellthhsi
      841 mecgnqispq lvsgqlqggl amgighalhe ylplyedgpg ngtwnfnryq lprasdvavw
      901 tqtgdvlppl setdppkgva evvmipvvga ivngiahaig hrftdlpvtp qkiqevla
//
LOCUS       WP_175977198             740 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia sp. BCC1047].
ACCESSION   WP_175977198
VERSION     WP_175977198.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..740
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=77834
     Region          60..>204
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          212..708
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msrglleagr vgagvsrrgf lklgmslgaa aggglllgfs lpaagddarr sviggdaaep
       61 apsgvfapna fvqidragki tlvmpkvemg qgvytalpml iaeelevpls svtldhappn
      121 eklfldpllg gqltggstsv ryaweplrra gatartllvs aaakqwnvdp ascraangev
      181 qhppsgrras ygqladaaak lpvpkdvalk qpadfkligt pakrldspek vdgtaqfgld
      241 vrlpgmlyav ivnspvfggt vasvddtaak kipgvrqvvr vdnavavvgd htwaakrgas
      301 alvvkwnega gakvstkdlf adlaqaaang kgavarkegd vgnafanakt rvdavyeqpl
      361 lahatmepvn ctvhvrgdgc eiwvgtqvpt rardtaqqlt glspdkivvh nhllgggfgr
      421 rletdmigqa vkvakqvnap vkviwtreed vqhdmyrpcy ydtisaglda ngkpvawrhr
      481 ivgssilarf appavkdgvd pdavevaael pydlpnqlvd yvrqeprhvp tafwrgvgpt
      541 rstfvvesfi delavqtktd pvqyrralld ktprarnvld vatkaagwgg pslpkgqgrg
      601 vsvmhafgsf fsividvavd ggevqvkrvv cavdcgmvvn pntieaqvqg giifgitgal
      661 ygeitiedgr vvqtnftdyr mmrinevppi evhlvksgea pggigepgta ataaalanai
      721 faatgtrlrk lpvgnqlkta
//
LOCUS       WP_175977210             766 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Burkholderia sp. BCC1047].
ACCESSION   WP_175977210
VERSION     WP_175977210.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..766
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=83959
     Region          170..765
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 msyvvavram ceftarrgdl dlrftpapta legiaghgav tskrgaryet eialtgtwgt
       61 ltvrgradgy dpvanrleei ktyrgsldam panhralhwa qakvyahlmc dardlkaidv
      121 alvyfdivse retvltetld aatlatffae qcacfvgwae retahraard talralafph
      181 gqfrsgqrel avavyraard ehclmaqapt gigktlgtvf pllkacgege ldhvffltak
      241 tpgralalea attlgagtpa lplrvlelva rakacehpdl achgescpla kgfydrlpaa
      301 rdaaieagll drdtvraaal ahdvcpyyla qelarwsdmm igdynyyydg samlhtlaqq
      361 nqwrvgvlvd eahnlldrar kmysasldpf afaaareaap aalrkafdrl arawgtlnra
      421 qaeryaaypd vpgpivsavq nlvaaigehl tdaprangda llrfhfeaiq fgvlaeafds
      481 asifdatlqg epmprqpald gvatagrrrr vqstlcvrnv ipagflapry eaaratvlfs
      541 gtlspfhfyr dtlglpgdtg wldvdgpfra eqltvrvash vstrwrdrdr slepiadlia
      601 aqyaarpgny lgflssfdyl grvvalmqtr hpdvpvwaqa pgmaenerda flarfdaggr
      661 gvgfavlgga fsegvdlvge rligafiatl glpqvndine qmrramdarf gngydymyly
      721 pglqkvvqaa grvirteqde gvvhliddry rrrevrnllp rwwrig
//
LOCUS       WP_175977218             136 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175977218
VERSION     WP_175977218.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..136
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=14520
     Region          51..>134
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mdatenprrd gtdgkpartr rrtpvvpias ilmlscawia tpryasades thaklasqas
       61 avggqirdat lasrvraalv aerglasgdi dvqvrdrvve ltgnvpderq ratairvahd
      121 vsgvsgvrdk lqirrk
//
LOCUS       WP_175977240             400 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid aminotransferase [Burkholderia sp. BCC1047].
ACCESSION   WP_175977240
VERSION     WP_175977240.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Alexander,F.W., Sandmeier,E., Mehta,P.K. and Christen,P.
  TITLE     Evolutionary relationships among pyridoxal-5'-phosphate-dependent
            enzymes. Regio-specific alpha, beta and gamma families
  JOURNAL   Eur J Biochem 219 (3), 953-960 (1994)
   PUBMED   8112347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..400
                     /product="amino acid aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43399
     Region          1..396
                     /region_name="PRK09257"
                     /note="aromatic amino acid transaminase"
                     /db_xref="CDD:181731"
     Site            order(102..104,130,183,214,243,245..246,254)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(105,140,207,252..254,290,293)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            246
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mfehidaypg dpiltlnenf qkdprdqkvn lsigiyfdae gripvlgavr eaetalqrds
       61 gpkpylpmvg laayrdavqa lvfgadhpar aagriatlqt lggsgalkvg adflkryfpe
      121 sqvwlsdpsw enhrfifera gftvntypyy deatgglkfd amlaaidalp arsivllhac
      181 chnptgvdld egqweklidv ieargllpfv dmayqgfgag ldadafavre larrgvptlv
      241 ansfsknfsl ygervgglsv vcedaaaaer vlgqlagavr snysnpqtyg akvvaavlgt
      301 palrkqweee lsamcrriar mrqsihdglr dhvsgealtr yvkqrgmfty tgltetqvda
      361 lrevhgvyil rsgrmcvagl ndsnvgivad aigkvlksgv
//
LOCUS       WP_175977301             222 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175977301
VERSION     WP_175977301.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..222
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23844
     Region          29..187
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpprhvqvpa ppgspaaqpa palrrrprqs raqassdalq qafvqlller gyakatirei
       61 aavagvsigt fyeyfgdkqs laalcihrrv laladrlrda vqrlrgvpra elaaalvdlq
      121 vesiaadaal wgalfalerq vspltayrrh ydayvalwrd alahaadppp aarldglarm
      181 ahticyggls qalltlgpal dftaqrrelr avllaylaaa da
//
LOCUS       WP_175977303             478 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia sp. BCC1047].
ACCESSION   WP_175977303
VERSION     WP_175977303.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..478
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49671
     Region          22..478
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mptpnpsaag sepggtplsl pddavdavla aelgdalvtr aadidphyft aynepagvrp
       61 ralvrprsvd dvsrtlalct rlgqpvvpqg gltglargav alggevvlsm erfagieald
      121 aaagtitvra gtplqtvqea aqaagftfgv dlgargscqi ggmlatnagg trairygmmr
      181 eqvlgleavl adgtvvssmn rmlknnagyd lkqlfigseg tlgvvtravl rlhpllaapa
      241 talcrvrdye avvalwnrvr tlpevvsfea mwpafydyva rhtpgvsapf vgdggfvvli
      301 ecatsapggd ahqaletgla agldaglidd avlatserqa rdlwtlregl aidalphlvn
      361 fdvslptgel gafaerceaa lrarwpaltc lffghvgdgn vhigvslaem tdadadaldh
      421 cvyavvrdmg gsvsaehgig vlkrpylaht rsdaeiglmr clkaaldplg ilnpgkvl
//
LOCUS       WP_175977311             294 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175977311
VERSION     WP_175977311.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..294
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32466
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="PBP2_CrgA_like_7"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08476"
                     /db_xref="CDD:176165"
     Site            order(101,105,144,158,160,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176165"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176165"
ORIGIN      
        1 menltgivaf vrtaealsfv aagrtlgisa savgktiakl eqslgvrlfn rttrrvtltd
       61 egrhfyercq riledfrdae atvtasaqrp rgklrvslpv igyrfllpvl pefrqrypdi
      121 eldldfndrm vdvveggfda virsgplsds slmsrrlgpf afvlcatpay laqagtprtp
      181 releahdcvr ycfpttgklq dwalaaddgt pltlrtamtc nnmealrgav laglgigymp
      241 dflardaleh galvtvlddy riapgqfsiv wpssrqlspk lrvfvdflce rlft
//
LOCUS       WP_175977320              94 aa            linear   BCT 11-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Burkholderia
            sp. BCC1047].
ACCESSION   WP_175977320
VERSION     WP_175977320.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 94)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 94)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 94)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..94
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=10597
     Region          5..94
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mtlalhwnpk ayedraaimd tiaeddplaa lelderleer aaalpahael yrqgrvagtr
       61 elviapnyav vyrirptegi veilrvlhar rqwp
//
LOCUS       WP_175977353             540 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175977353
VERSION     WP_175977353.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 540)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..540
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58901
     Region          9..537
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msdavvskad epllslerlh vrfgdtvavd dvtlaigrge rvalvgesgs gksvtalsil
       61 rllrdadvtg airfagqdla akseremrgl rgsdiamifq epmtalnply tigvqigeti
      121 vlhdgvsage arkraialla rtgiaepekr vdsyphqlsg gqrqramiam alacrprlll
      181 adepttaldv tiraqtvdll lelqreeaek rgmaillith dlnlvrhfaq rvavmehgrl
      241 vesgpverif aapehpytqr llnsrpqrav tpvmpiapvv ldarhvsvqf arkrpgfagw
      301 fgtvpvtava dvsvsvrqge tlgivgesgs gkstlamall glqktaggei efqgralsty
      361 rgreqtalrs nmqvvfqdpf sslsprhtie rivgeglelh rpdmtpdarr akslavlrev
      421 gldrtvlhry phefsggqrq riaiaralvl eprilildep tsaldvsiqq qvlkllanlq
      481 qkynlgyvfi shdlevigam ahrvavmqdg avvesgevsd iftrpshpyt qkllkavwka
//
LOCUS       WP_175977397             207 aa            linear   BCT 11-JAN-2025
DEFINITION  2'-5' RNA ligase family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175977397
VERSION     WP_175977397.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Remus,B.S., Jacewicz,A. and Shuman,S.
  TITLE     Structure and mechanism of E. coli RNA 2',3'-cyclic
            phosphodiesterase
  JOURNAL   RNA 20 (11), 1697-1705 (2014)
   PUBMED   25239919
  REMARK    Erratum:[RNA. 2014 Dec;20(12):2011]
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Arn,E.A. and Abelson,J.N.
  TITLE     The 2'-5' RNA ligase of Escherichia coli. Purification, cloning,
            and genomic disruption
  JOURNAL   J Biol Chem 271 (49), 31145-31153 (1996)
   PUBMED   8940112
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..207
                     /product="2'-5' RNA ligase family protein"
                     /EC_number="3.1.4.58"
                     /GO_function="GO:0004113 - 2',3'-cyclic-nucleotide
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0008664 - RNA 2',3'-cyclic
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=22861
     Region          30..201
                     /region_name="ThpR"
                     /note="RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA
                     ligase) [Translation, ribosomal structure and biogenesis];
                     COG1514"
                     /db_xref="CDD:441123"
ORIGIN      
        1 mksrsrpdgd aavtqltlpg fdapppvpvh rfffavmldp ataaritgla esmrlekdsp
       61 vsterlhitl gslgdfayvp daklararav adrmdvpsfs vrfdkiisfn rrsgrqplvl
      121 tgkagledli dfrrqlrdal kragvpvfps gftphvtlly gaqrldeyri epitwtvfdf
      181 vlidswlgks hydvlgrwpl ttgsppg
//
LOCUS       WP_175977360             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175977360
VERSION     WP_175977360.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32548
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrfkqietf aavaakgsls aaahaegvap aiigrrldal eerlgvkllv rttrkltltf
       61 egsafledcq riindmqnae asvsaggvka sghlrisapa gfgrrhvapl vpefsgahpd
      121 vsvtldlsdr mvdlvnegfd cavrlgelpd sslvslklge nrrvcvaspa ylarrgtpat
      181 laelarhncl alaananqqr gwafqegdkv vsirvngtme csdgavlhew claghglawr
      241 swwevgedva agrlvsvlda faappigiha vfpqrrhlpl rvrlfldylk htyerpgywg
      301 e
//
LOCUS       WP_175977399             294 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia sp. BCC1047].
ACCESSION   WP_175977399
VERSION     WP_175977399.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..294
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30346
     Region          3..286
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mqtavgfigl dvmgtpmaln laragtplva wsrshgsdda lrdagarvae nvdevftscr
       61 tvilmlandg aidatlargt agfaarvggh tivnmgtnap eysraladdi aaasgryvea
      121 pvsgsrkpae agqlvvmlag aptdvdavra lvkplcrdsf vcgdvpsalt mklavnlfli
      181 tmvtglaeat hfaqrhgidl arfadvlnag pmasdvsrvk lgklvandfs vqaaitdvlk
      241 narlvaesar gigiasplld ichalygete qaghgaadmv aviraierrt gdar
//
LOCUS       WP_175977414             233 aa            linear   BCT 11-JAN-2025
DEFINITION  TerC family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175977414
VERSION     WP_175977414.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..233
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24577
     Region          24..191
                     /region_name="R_switched_YjbE"
                     /note="integral membrane protein, YjbE family; TIGR03717"
                     /db_xref="CDD:163429"
ORIGIN      
        1 mlefltslhw gailqiiiid illggdnavv ialacrnlpa nqrlrgvvwg tagaillrva
       61 litfavalld vpflklgggl lllwigiklm apaadahdni kpadrlwdav ktiviadavm
      121 sldnviaiag aaeqadpshr ialvifglvv svpiivwgst lvlklldrfp vvvalgagll
      181 gwiagglivn dpvgdrwpvl dtpevvygas ivgalfviai gyalrkrrdv pqh
//
LOCUS       WP_175977444             260 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter permease [Burkholderia sp. BCC1047].
ACCESSION   WP_175977444
VERSION     WP_175977444.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..260
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26466
     Region          4..259
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mfeydfmina faasgivavl agivgyflvl rgqtfaghal shvgftgatg avllgispiw
       61 gmvgftlaag igmgalgekl agrdvaigvi lsgalgfgll flhfytsfat qvtallfgnv
      121 lavshdtlav lagigavsla alaliarpll faslqpelae akgvslrtvs mlflavcala
      181 vaaatqivgv llvftllvgp aaaaqnvstr lstgvllaal falseawagi vlayhtdwpt
      241 sfwitalsal vygasllrrn
//
LOCUS       WP_175977457             303 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175977457
VERSION     WP_175977457.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33009
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..295
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,224..229,
                     235..236,238..239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mtfdlrqlra fttivacgsl graadalhvt qpalsrilkr leeqvgaplf erhskgvqlt
       61 afgeallpha tllqheaeha reeldamrgf akgtikvgtv gsiaslvlpv avgrvldrwp
      121 nlrveiiegv wdrlaeglik heidlalsah gpdtdeivai pecrwedrsh ivaaphhplr
      181 algraptlad tlharwaipp rgtapfdhmr atfdahglpl pdiavetrsv ttlkslvaha
      241 gflcwmaepm ygaerragti dtlpvhevva vrtltafrrr hgilpgpagk lldelialtr
      301 egh
//
LOCUS       WP_175977474             520 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175977474
VERSION     WP_175977474.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..520
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54478
     Region          24..520
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 msspirsses ldvdallaal prriadvpah raaqspahpa liedarrlsy gelaqavdaa
       61 aarlaglgvq ggdrvmivae ncvaqivllf aaarldawal vsnarlsaae ldaiavharp
      121 kliafttdas adarahaerl gatpagvlpv digawsyrvd agapaepvaa dgagqcaali
      181 yttgttgapk gvmlshrnll fiaaisstlr rvspddvvyt vlpvshvygl asvcvgslya
      241 gatlrlaprf speavrvala degvtifqgv pamhaklleh lhthghawra prlrfaysgg
      301 spldanlkar verlygvplh ngygmtessp titqtpldap radssvgvpi pgvdmrivap
      361 dgtdvppgev geirvrgpnv mlgyyrdada traavspdgw lstgdlarqd adgavtivgr
      421 skeliirsgf nvypveveqv lnahpdvvqa avigraidgn eevlafverv pgaaadeaal
      481 hawcadrlta ykrpahirvl dalpaastgk vlkhrlrelv
//
LOCUS       WP_175977483             235 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175977483
VERSION     WP_175977483.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..235
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25200
     Region          34..228
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mpaslapylp qleanpwfaa lppalraali aratlrrlps ghalfrrgdp pcglyavlag
       61 sltigavdpq gketlltvae pvtwfgeial fdgqprthda ialddalllh vpqagllail
      121 ettpqywrqf allmaqklrl sfltvesmsv mpaaqrlaar llmiaegygg isagrthirl
      181 sqetlasmls ltrqttnqll kalqadgvvr lhvgeielvd idalrrasgl gdgpy
//
LOCUS       WP_175977521             163 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175977521
VERSION     WP_175977521.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..163
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17899
     Region          4..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 magitlddld lrilailqdd asvsnlqlae ralsspptcm rrvrrlteag virrqvavld
       61 pvaigtgvta lieisldrqt aedyeafeay vcaepavtqc yrvspgpdfv viadladvae
      121 ydefarrlft gasnvrnvrt ffsthrakfe anarvahamr krt
//
LOCUS       WP_175977524             177 aa            linear   BCT 11-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Burkholderia sp. BCC1047].
ACCESSION   WP_175977524
VERSION     WP_175977524.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..177
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18752
     Region          1..165
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtpahlipsp lgdiavried daltglyfvg qkyfpsvaiv readalarsp varrvaeeia
       61 eyfagardtf svpihlrgta fqqrvwkell aipfgelvsy gditervglp msgaravgga
      121 vgrnpvsiiv pchrvvgasg sltgyaggid rkrallsleg agfsrgayqp mqralaf
//
LOCUS       WP_175977538             318 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175977538
VERSION     WP_175977538.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..318
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35156
     Region          11..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrkfkipnmg alvafeaaar hesfthaake lfltesavsr qiatleaslg vrlfarvkqr
       61 vvltragkly gtqvrralea ldrdtlsiia hgsgggylel avlptfashw lipriksfyd
      121 rtpdvrvnmg srtdlfsfed thfeaaihyg kptwpgtssd ylfgeevvpi capallngpv
      181 ervedllayp llhsttrpga waqwfethgv edirtmqgvr yelhtmlisa aaaglgvalv
      241 pkffveeqlq qlglvvpcda atvgdsayyl vyptefshsk plesfrswll eqasayaape
      301 rdahnadaed eeddedve
//
LOCUS       WP_175977588             240 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD family hydrolase [Burkholderia sp. BCC1047].
ACCESSION   WP_175977588
VERSION     WP_175977588.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..240
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26254
     Region          6..233
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mrlakvsavs fdlddtlwpf gpsvvraeat lrawliehap ntervlptqq tlaalreeye
       61 rlrpdlasdy ramrigsirl aleranedvs lteraydvfy aarnrvefye dalpalawls
      121 arfpliavtn gnadlrltgg geffrttlsa rafgfakpep eifhaaadal gvrpaellhv
      181 gddfhldivg avnaglqaaw ivrepsaeea ptpphavtph lrlsdlamlc ralgapdtvs
//
LOCUS       WP_175977629             871 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC1047].
ACCESSION   WP_175977629
VERSION     WP_175977629.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 871)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 871)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 871)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 871)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 871)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 871)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 871)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..871
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..871
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=91710
     Region          35..871
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mkgpqhaaqp paghpghdgr thagrfglrd lihqaarmta rdwrageltl lvlalvlava
       61 altsvgflad rlrqglerda rqmlgadfvv radrpvdpsf drqaralglr tattaifpsm
      121 igsaargqaa daapsrlaav kavspgyplr gaveilpaga ttaqkasaip apgtvwadps
      181 lldalhlkag dtvrvglrtf tvaaaitrel drgfsfvnfs prlmmradel aatgltgygs
      241 rvtyrllvag daaavarfet yaharvdggk lrgvgleslq egqpqvrqtl drarhfltlv
      301 alltallaav aiamaaqrym rrhldgcatm rclgvsrrtl galfalefig vgivsgaaga
      361 vlgygghwal laalgslidv alppptlwpa ligmgaalvl llgfalpplv pltrvppvrv
      421 lrrewgdasr tawaayavgv vlfaglliva agnlklgliv aggfagalvg faliarlvlf
      481 aaaravrnar vaagvgwrya laslhrrgta salqitalal glmcllliai trndlvagwr
      541 qstppdapnq flidiqpdqr advaaylaah gvrdavpapm vrgrlvaing kpvnpdayps
      601 eearrlvdre fnlsyttelp sdnrivegdw fgaaatpqis ieaglaktln vkpgdtlrfd
      661 vtgltvdapi tsvrkldwgs frvnffvlmp ppvlkdfpav yltsfhlpas naalldplia
      721 rypnltaidv apilaqlqrm mlqvvgavqf lfaftlaagv lvlytalags rdervreaal
      781 lralgasraq vnavqraefv vvgalagvla sagaiavgwv lasrvfdfql avdpwlvpag
      841 iaagvvcaga agwlslhnvl rrpalqslrd a
//
LOCUS       WP_175977691             312 aa            linear   BCT 11-JAN-2025
DEFINITION  carbohydrate kinase family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175977691
VERSION     WP_175977691.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..312
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33727
     Region          4..290
                     /region_name="ribokinase_group_A"
                     /note="Ribokinase-like subgroup A. Found in bacteria and
                     archaea, this subgroup is part of the ribokinase/pfkB
                     superfamily. Its oligomerization state is unknown at this
                     time; cd01942"
                     /db_xref="CDD:238917"
     Site            order(52,250,253)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238917"
     Site            order(192,220,248,251..252,255,277,280)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238917"
ORIGIN      
        1 matlicgsia ydsimtfegr frehilpdqv hlinlsflvp tmrrefggca gnigyalhll
       61 ggdarimgtm galdaqpyld rldqlglrrd hvrvlpdtyt aqamittdld nnqiaafhpg
      121 ammqshlnha gdapdiklai vgpdgfdgmv qhveelakag vpfvfdpgqg lplfdgatlr
      181 rsielatyva vndyeaklvs dktgwsedei asrvdalvit rgehgatirh kqgaeqipvv
      241 paeriadptg cgdafrggll ygiehgldwa ttgrlaslmg slkiahqgpq tydltraeid
      301 arfetafgys lk
//
LOCUS       WP_175977721             251 aa            linear   BCT 11-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Burkholderia
            sp. BCC1047].
ACCESSION   WP_175977721
VERSION     WP_175977721.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..251
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26011
     Region          1..251
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlttqrkkai ldalardgqv laaelsvqfg vsedtvrrdl relaaegllq rvhggalpas
       61 pavapfaqre alettekrri arraaqmiap gqvaivdggt tsallvgqlp adlrativth
      121 spsvavalaa hpsidvilig grlykhsiva vgaaamegia rihadlyfmg vtgvhpvagl
      181 stgdfeeaai kralaeraae tvvlasqskl raasqfvigd itlaqtvvve ketdaaltkp
      241 ieaagvtvvr a
//
LOCUS       WP_175977744             418 aa            linear   BCT 11-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175977744
VERSION     WP_175977744.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..418
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45328
     Region          12..395
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mlkrfgnpdv akavanlvwl glerltqigv aiaisgllar yfgpdvfgkw qyantlllvl
       61 apltwvcgae ilvptivqrp paqlgavlgs afvlriavsv aalaatwiai aagafdplvg
      121 amlaglavtm vfrepfvgvi nawlqsmtys kpqlvtsmvt alakallvwl lvraaagpar
      181 fawlwaleaa aiglalllyy rhrnggtlgw tfdtslfrhf atagtvfwlg licmylflkf
      241 drlmlerhvs fadlgrysaa qqlnenwitl almlaqtiap afvyrvqdva rlrrnivrli
      301 amtaglmtag alvldaaapl ivgkvfgrgy easvdifrwa vwlsvpasie aignlivlky
      361 qakfvllskw llalaiavlv nlfaiprlgl ygalvglaag ylaaaavnfy yirfklrt
//
LOCUS       WP_175977757             442 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia sp. BCC1047].
ACCESSION   WP_175977757
VERSION     WP_175977757.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..442
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=48965
     Region          24..140
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
     Region          254..>332
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
ORIGIN      
        1 mdsfyrafed qhrgsrelik srlakyqpfi aplatlhpgg ktldlgcgrg ewlelmveag
       61 ftpvgvdlda dmleacrrrd lpvfqgdaie ylaaldsdnh alisafhvve hvpfeqvrri
      121 vsealrvlkp gglliletpn penivvagcn fyldpshkqp ipsellsfvg ehagfarvkr
      181 lrlqeppllq drsvrvrlld vlggvspdya ivsqkscsek earlfdeafd adyglslael
      241 aarfeeggar ehkavaeqtq rtqdevarlh gelglvhdel trtrseltqv vdelerirgd
      301 lgrvrddldq vsgdlervhd eaqhtagqlq avygstswrv tapmrsavty arsakgacks
      361 gmrrvlfrsv ayvnrnprlr rlavrvlgam pgvkqrlvri vvgaptqsvq rkpidddglt
      421 prareaymal ksalapetgd ie
//
LOCUS       WP_175977769             260 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC1047].
ACCESSION   WP_175977769
VERSION     WP_175977769.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..260
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29342
     Region          7..260
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mltlsladlk ksitawrlwt llgwleirqr yarsrlgpfw ltismgvmit slgvvygtlf
       61 gqkineylpf lacslvlwgt fsatiqegsv ayinsapyir qmatpkliyi lqvvwrnliv
      121 lahnfvivia lmvifgvkrw etlpmfipal llfvanatwi amvigllsar frdlpqivga
      181 llqvafyvtp iifrpdalnr fsfivewnpl aylidvvrsp ligqipsgts wavaigmavi
      241 gwpvalymtg rylkripywv
//
LOCUS       WP_175977784             243 aa            linear   BCT 11-JAN-2025
DEFINITION  DsbA family oxidoreductase [Burkholderia sp. BCC1047].
ACCESSION   WP_175977784
VERSION     WP_175977784.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..243
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25985
     Region          15..214
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(23,26)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 mttapiptar ptltveiwsd licpwcwigk hrfdealaaf ahadrvdval rayrlmpgqp
       61 vepveamlag kyrmapaqvd qmlrqvteaa asvglrydlp gtlvgdtldg hrlvklaqas
      121 grahalterl yrayfcehgs lfdhaaltef aveaglersa vevvlrgday rdeveadiar
      181 aaqiggrgvp lfvfggryav sgaqpadafa qaldhawrdg vvelggsdaa acgpdgcelp
      241 ars
//
LOCUS       WP_175977765             451 aa            linear   BCT 11-JAN-2025
DEFINITION  FkbM family methyltransferase [Burkholderia sp. BCC1047].
ACCESSION   WP_175977765
VERSION     WP_175977765.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Struck,A.W., Thompson,M.L., Wong,L.S. and Micklefield,J.
  TITLE     S-adenosyl-methionine-dependent methyltransferases: highly
            versatile enzymes in biocatalysis, biosynthesis and other
            biotechnological applications
  JOURNAL   Chembiochem 13 (18), 2642-2655 (2012)
   PUBMED   23180741
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523603
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..451
                     /product="FkbM family methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=51827
     Region          29..193
                     /region_name="Methyltransf_21"
                     /note="Methyltransferase FkbM domain; pfam05050"
                     /db_xref="CDD:428282"
     Region          <239..>427
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
ORIGIN      
        1 mkfvsyaqny edvmlrrala kvdrgfyidv gaaepyadsv taafyergwr giniepmpgp
       61 fdrlaqarpq dvnlqvaven kqtvaryfav dggngistgi qklaegyrna nwdisqvtva
      121 vttlrdicet yvgerpvhfl kidvegnere vlasadfntf rpwiilveat epnsqipshd
      181 dweallleae yhfvyfdgln rfyvsaekmd elkqafmvpp nwfdgfiras esdmirratd
      241 lerqlvesqr qlqeardgws lekgareele vrlntayhnm tdrvhdeqas qvvledasqd
      301 rgmknpeish eeidqlkarl agsegdlenh riqlaelrar lteseksgqa lsaerdtayq
      361 elfessrhaa wlsqervrlq eridessrhv vwvnqergrl qgkvdelerm vdtlrlqeer
      421 vsaalhavfq stswkltgpm rcikrmmhrr s
//
LOCUS       WP_175977815             286 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175977815
VERSION     WP_175977815.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..286
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31232
     Region          18..273
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mseplqhrqd adnakaeagy vvpglerglr ilaefsprep vlgapelskr lgiprttvfr
       61 llqtleslgf leradkdrny klgiavlrlg feylsslelt dlglpviesl rgatgftthi
      121 virdgrdvvf vakaqsqspv fssirvnvgt rlpahatthg hvlmgdlsln elhalypega
      181 lnrmtsatpe tvdalyevir edalrgygvs nssfergisv vtapvrndtq kivacitvtv
      241 prpeidaali adglidkvqr aaaelsrrln yrsddehtfl kalglr
//
LOCUS       WP_175977827             144 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175977827
VERSION     WP_175977827.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..144
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15721
     Region          1..143
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mlkllvpvgh sprslqavrh atflyrerca sevvlinvqa plestrleay hplsrlraie
       61 trfatddlam aerilrdadv kfsvvlkvgp vadtiaaaaa etgcdeivva aprrdplhal
      121 msvfrrsvma rlvrisnvpv tavq
//
LOCUS       WP_175977843             279 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175977843
VERSION     WP_175977843.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..279
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30306
     Region          19..239
                     /region_name="HTH_MerR-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     transcription regulators from the MerR superfamily;
                     cd04778"
                     /db_xref="CDD:133405"
     Site            order(21..23,37,53..55)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133405"
     Site            order(67,70,74..75,84,105,109,115,119,122..123)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133405"
ORIGIN      
        1 mskqthstpd eatpdsrney tvdelarvsd ttvrnvrayq drgllappek rgrvgiyddt
       61 hvarlklinh llargytlsn iqdlikaide ghdlrsilgl enaiggrwsh elpktyslaq
      121 laqmfgpqat tqlsrvtelg llerrglsfv akspalleaa aamtkegipp relldvisla
      181 rphfdaiarl lvdlvvkrld rydagtlppa tdvpelvdai wrlrplaavf vegetnrale
      241 taagaylggr vatildkkls deaarqsgts dtqgdgdng
//
LOCUS       WP_175977847             504 aa            linear   BCT 11-JAN-2025
DEFINITION  MDR family MFS transporter [Burkholderia sp. BCC1047].
ACCESSION   WP_175977847
VERSION     WP_175977847.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..504
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53170
     Region          38..422
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(39..40,43,74,124..125,127..129,132,152,155..156,159,
                     284,287..288,291..293,296,324,328,381..382,386,390,406,
                     409..410,413..414,417)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mttdtfltrp aadaarrdap tglivaalll vmllsaldqt ivstalptiv gelggldqls
       61 wvvtayllss tvvlplygkl gdlygrkivl qaaivlflag salcgvaqdm tqlivlralq
      121 glgggglmvv tmaaigdlvp pdrraryqgm fggvyglati vgpllggflv ehlswrwift
      181 inlpvgllal avigiafrph tahvkhridy mgaaflatal tcvilftseg gsllpwtspq
      241 lwmtlvlglv aiggfiyeer iaaepimple lfrhrtfvlv sligfvvgia lfgsvtfipl
      301 ylqvvkgstp sqagmqllpm mggmlvtsiv sgrlisqfgs yrpfpiagtl tggiamalls
      361 tltldtplht myaymallgi glgmvmpvlt lavqntvefr hmgvatsgat lfrsiggslg
      421 vagfgalfsh glqsrmmhal pagtelppal gpaavrqlpd avrdaylhaf agslhvvyla
      481 aaaiiaiafv fawfvedtpl rkhh
//
LOCUS       WP_175977863             426 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1047].
ACCESSION   WP_175977863
VERSION     WP_175977863.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..426
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45223
     Region          5..408
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(19..20,23..24,27,59,109..110,112..114,117,137,
                     140..141,144,232,235..236,239..241,244,272,276,334..335,
                     339,343,359,362..363,366..367,370)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtnirwrivl llfiagfiny ldraalsvaa pavmrelhms pgslgllfst ffigyaafnf
       61 iggwaadrwg gkrvfsgavl twsllcgatg lasgfgslla irtlfgmaeg plattinkiv
      121 nnwfphkesa tafgfancgl plggavagpv vglltaaygw rvafagiacf gllwlvfwvf
      181 matdkphqha rvsdderrli esdrsvpesp sdvqplgfyl kqpaivaami syfgysyilf
      241 ffltwfptfl tmdrhlslks mslatvlpwl lgfigyglsg vlsdrifrrt gnallarkrv
      301 liaclgtagv cvtlagavtt tlgalllmav avfalylsgs aywaliqdtv pgpklgsvgg
      361 cvhaiancag ivgpaatgfl vqeshtflsa fflaggiala svlavaillr pravaqrkss
      421 darvcg
//
LOCUS       WP_175977903             793 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia sp. BCC1047].
ACCESSION   WP_175977903
VERSION     WP_175977903.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 793)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..793
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85650
     Region          70..775
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msstlaarss rgrlalacaa afawpaaqaa stddaradaa rsggidrsaa aaapaavgva
       61 aaaatvgdtl tavsvtaqrq pvdpdtpavv asitreqida htnvttedal kyapnlmvrk
      121 ryigdrnsvf agrdfnelqs arglvyadgv llsnllgssy aypprwslip pddiarvdvl
      181 ygpfsavypg nsigstvllt trrpeqleas lstqfftqry rdgygfadsf ggnhqtaria
      241 nrvgrfwfal sldrlendgq pmqyaspnsa ynpklgaavp vtgaatdigp ngkprtivga
      301 qtierteqln etvrigyafa dhvdatltlg hwenhyrqhg etflrdatgn paagtpvygg
      361 nvsiggqnmt vapsafapqr gdqenwlyal glngrldsgw rlsgvvsayd vsrdvlraas
      421 tvqggagtlf qgdgtgwrtl dlkaeapavk ghtftfgyhy dnyflrnvty ntadwlagpt
      481 tslasvyrgd trtqalfgqd awrfapgwla tlglryerwd ayggalgnan gtlgyadrga
      541 nalspkvalq wdatqvwrfr lsfatgtrfp tvgelfqgti snnaivnnna nlrpekaidw
      601 dftaerdvgv gvmrasvfqs dlrdsiysqt tvsgattvtn isnvdrvrvr gvelafsgen
      661 vglrgldvda nvsasnaqil adaanpayvg scfpriprmr anllasyrfd ehwlasvgvr
      721 ysgrqfntld nsdvnpdvyg gtssftvvdl karyrfdrhw tasagidnlt drryyvfhpy
      781 pgrtfygelk wsl
//
LOCUS       WP_175977977            1059 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175977977
VERSION     WP_175977977.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..1059
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=112054
     Region          14..827
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnmqntvaal rggllqqdrl lkldtplgan vltvqravgr srigrayeft ldvlstdsdl
       61 elkkliaqpv tlwiqqgdrs yrpvngyvht arrlgadggl ttyqltfadf thflkfrrdq
      121 riwndttvdq iisdvldqhp qakghfrfal skplpsrsyt rqhdtdwhfv hrlmesegly
      181 ttwqqaddgk shtlvitdnl qafaplspqa vrfyhggaas eadaltqwsg trtlqsvtrt
      241 trtfdyknps qpsnpkgttl ptmagqgelp dqlevyeytg aytyldqtrg dhltkikmeq
      301 weseakrfhg vggvraidag rrftlaghpe hdrdpadqre fatigvewwi ennlpvasss
      361 adfpyslrda ltqaqegyga dpafrvphdd gsvgfylvev eaqrvsvpyr spfehekpkm
      421 hletaivvgp qgeevytdel nrirvqfvwd rlnpgnenas cwvrvvqsdt gggyggvhvp
      481 rigeevlidy vggdcdrpla vgrvynganq pqwhsdgils gyrskeysgg gynqlvmdda
      541 tgqnrvqlms ssansllhlg yiidqngnsr gsylgsgfdl rsdaygavra sqglyvtthp
      601 kaansqpldv keaqqqlvtg eslieamsgv seqhqaeslk eahdtmraft datqdsasgn
      661 asggrtaggg tgsanafkep vmlfgspsgi gmstqqslhi vandhvnvas gqsvhvaagk
      721 sligsigqkl slfvqnagmr lfagkgkvei qaqsdnvevt aqkavkvvsa tdrieiaadq
      781 gilltsgggy irikdgniei hapgavdvkg ashtfagpas mgyplpsprp dqpgqlelfh
      841 kyvngeavkg glftvkdvng avlkkgaldn sgntvvsglp pgavrvefgk dpresdqpan
      901 yfkqvkwpae pvqpsaeaaq aaasgqlasq lqgmapaatt aamglvgggs agaalgglas
      961 salpaaatal ggagvasalq tasslsgaak qvagmvqaar qgglaalaap aanaasgalq
     1021 salpgvagia gkgattvasa agatgmklpt sgfggplks
//
LOCUS       WP_175978190             310 aa            linear   BCT 11-JAN-2025
DEFINITION  thioesterase II family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175978190
VERSION     WP_175978190.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..310
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=34425
     Region          74..310
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mpgshvapri reqsrpggiv nlyrrtapva gpcdyaapss arrpgsdrgc dasrlplsig
       61 mpvkitpwfi lhrpqpaath rlfcfpyaga gsllyrrwal elpdwievva velpgrqtrf
      121 seapptslda mtdalataah glldkpfgtf gysfgsvvgi ewlreldrrr lrgpihafca
      181 ahraphvvpr plaihrlpep elidwlktmg gtpdallsep dwlrhflral radlalaegy
      241 ctdtpfalrc gltvfgglhd phvdidalre wrrysdgpfs lhrfdgdhff iharerelqd
      301 hvvatlaaha
//
LOCUS       WP_175978206             316 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175978206
VERSION     WP_175978206.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..316
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34526
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,161,163,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,190,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdtlqmmrif vrvaeegsft saaqrlditt ayasrsvaql ethlrtrlln rstrrialtd
       61 agqryldrcq rilgyideae aeaadaqvkp sgrlhvhatt sfgqsyvvpa vvryreryps
      121 vaveltlsqh vpdiidegyd vslqlsttel pdsglvsqrl gdvgsvlcas paylkargtp
      181 rtvsdlagha clrlvtslfp rdrwhldgpn gretfelsvp dfqvniadal gaalraglgi
      241 gplpmsaalp alasgalvrv lpdyrlqklt vytlyasrqy ldakirtfvd flrecvpeml
      301 aadeaalnac cvsrqs
//
LOCUS       WP_175978226             247 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175978226
VERSION     WP_175978226.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..247
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26810
     Region          3..243
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mdvklvartl dlfelfaaer rplpltelar llnvpasscl amartlvsrg ylyevrkrgg
       61 yyptrrlqtv aaaidatdpv vdivhphlva lrdasretav lgkiqgasvt yldvveseqa
      121 irytrqpgel rplhansigk aifaelasda qqalgaqlpf erltdatvad lpalvaqtar
      181 frelgwaenf gesapelsai avaltldgdw yglsvvgpte rirqhrdaha allvdakarl
      241 qaeharg
//
LOCUS       WP_175978252             282 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175978252
VERSION     WP_175978252.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..282
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29805
     Region          7..260
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtrstaalaa rglsvgyrdh vvidgldlsi aagrvtalcg pngcgkstll rtlaglqpar
       61 aghvevngkp lasfrrrala reltmlaqfn qipsgltvre lvaygryayg gflrglsrad
      121 haaidealdt sgladdaerd vgalsggerq rawiamalaq qapivlldep ttyldihhql
      181 dildalraln rargltivwv lhdlnqaaay sdeivlmrag rlvaqgtpda mleparlraa
      241 fgvemlklah pqtgapmcvp aygpstdgap qaagvfdrdl av
//
LOCUS       WP_175978245             754 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia sp. BCC1047].
ACCESSION   WP_175978245
VERSION     WP_175978245.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 754)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..754
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81622
     Region          71..754
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mkkveqkkme watgtrlrai aaaasvafgt aaaghayaqt apavnagaaa sastaqsgat
       61 tstsssaqng tlpaitvnaa sagdgtvglv akrsttgtkt dtplneipqt invvtaqqie
      121 mtgatdvnaa lryvpgfssy gsdnrsdwya alrgftptay vnglqvpnti nlaswrvdpy
      181 midsisvlrg ptsvlygagd pgaiidvhtk ladgervrea gvqignyark qfmidvgdkl
      241 dpdgkyayrf vgvardgnam tgpnndqrva lapsfrwrpd adtsltlsat ylqdwgdiss
      301 nflpaqgtvl pnpngqinkd iyegdgsfny yrkkqwsvgy qfernltpaw tfrqntrlmh
      361 lsldngsvfg ngfvdgsttd vsrwagvfqm nysrfdidnn legrfatgpl qhtlllgfqy
      421 nrqtatdsew laaapplniy npvyqpvtta vftpdatfrt ntyttlntfg lyaqdqikwn
      481 rwtltlggre dwvnmrqddr aagtstkadv taftgrvglt yqgdyglspy vsyatsfnpl
      541 igvnlvgggl pqptrgkqie aglrwqppgk nlmlnaaiyq inqtnvltsa lpsqdptgtk
      601 svqtgevrsr gielsatgkv trnlsviasy vyqdvknvqa ndvslnnwpv diprprqmas
      661 lwtdwtwytg plagfglggg iryqsasaga adnsltvssv tlfdaglhyd vrnwrfavng
      721 tnlfnrhyis gcqsnnvcif gtdrtviata kynw
//
LOCUS       WP_175978303             357 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia sp. BCC1047].
ACCESSION   WP_175978303
VERSION     WP_175978303.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..357
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=37578
     Region          23..357
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkktrqvvvr vagrrvvgtl gataiftagl vwtsggahad sgsqvqlygl igtyvgsikr
       61 sdtprttvlm gsgglttsfw girgkedlgg gvgaifvles ffqpangalg rsaadpfwsr
      121 nayvgfqgdf gqltfgrqrn paytaesvvn pfgsstvfsp lvlqtfvtny ggtiigdtvw
      181 nntvkyttpd fngfgatviy glggvagspg vgnlgvhlny rghgltavls gqrvrytaag
      241 pvgaqyayla gaaydfkivt lygawamtsd artptgshty eagvsiplsp adfllaewar
      301 tkrsgpteaa rslrntasvg ynhllskrtd iyaiysydkl sarptgntfa agirhtf
//
LOCUS       WP_175978390             199 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175978390
VERSION     WP_175978390.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..199
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22584
     Region          1..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrkgeqtraa ileaaldlas rdglegltig llaermqmsk sgvfahfgsr edlqvevvre
       61 yhhrfenevf fpslresrgl prlramlarw iekriqeltt gciyisgave yddrpdspvr
      121 eqliasvtaw raallraisq ameeghlrad tdpelmlfel ysftlglhhd arflhspdav
      181 rltwaalekt ivsyqsesr
//
LOCUS       WP_175978371             310 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1047].
ACCESSION   WP_175978371
VERSION     WP_175978371.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34414
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrlgdirlf veaaelgsls aagrklnltp aaasarlakl eakiatrlfe rstrqlrltd
       61 egklylnccr qalqalddad amlqegrnvv sgkvrlssts dfgrhqlldw lhefttlhpg
      121 vtfsltasds sanlwqdeid lairfaappd galiarrlat nrrvlcaaps fverhgvpad
      181 phdlarfpcn vitiasgpmn twhftrgdev qihtvpvsta fetndggltr ewtlrghgia
      241 lkslwdiadd vragrlrvll pdwrhqdapl haiyhskrym aprvrvlldf laerfareea
      301 alddllnacr
//
LOCUS       WP_175978411             673 aa            linear   BCT 11-JAN-2025
DEFINITION  BCCT family transporter [Burkholderia sp. BCC1047].
ACCESSION   WP_175978411
VERSION     WP_175978411.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..673
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73285
     Region          3..514
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mpdsrpsprt tfkpqvvlpa lvvigallvv calrpseaga lfsagqqwvi arfdwfyvla
       61 vtgflvflvl iaasdfgnir lgpddaepef sfvswtamlf aagmgiglmy fgvgepmqhf
      121 lkpptvdpgt saaareamlm tffhwgfhaw aiyglmglvl ayfgfrynlp ltlrsglypv
      181 lreringwig htvdafalvg tvagiattlg ygvmqlsagl htvagwdtgs nvfrvglvav
      241 vvilagvsaa tgldkgvrrl selnlllafl llafvvvagp tafllralgd nigqylsslv
      301 dlsfrtyaya ppreegwfgg wtilywawwv swspfvgmfi arisrgrtir qfvigvllvp
      361 tafnlvwmtv fgnsaiwldt haaagalaqt atnvdallfr ffdflplpql lsivaivlia
      421 vffvtsadsg afvidqiatr gsahspvwqr lfwaallgvt aavllvaggl galqamtlia
      481 alpvaiimla lcyglwrgla adrahysqdv apatsfwtgq hwrhrlthil rqtteaearq
      541 fiaetvepal rkvadelras gvdahvqhds ddavrltvpt aehrdfvygv rvtaksaaaf
      601 lvretaepde arahvygivt ffedgrlgyd veylrgdevi advlrqyery vslaadtrth
      661 llsrapghat eae
//
LOCUS       WP_175978413             282 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia sp. BCC1047].
ACCESSION   WP_175978413
VERSION     WP_175978413.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..282
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30060
     Region          52..146
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 meanrpneaq salwngpsgr awvdaqalld rmfepfetll adgaaassas svldvgcgtg
       61 avtlaiarrl ganaqctgid isarmidaar araertglra rfvcadgqth vfepasvdli
      121 vsrlgvmffd dpvrafanlr qaarpgapmr fvawrgaadn pfmttaeraa apllpslpar
      181 qsgvpgqfaf gdrqriasvl sdsgwadvai epvdracmlp tselddylar lgpvglalle
      241 tdeatrrrli dtmraafery vhgaevrfda acwlvtarap sa
//
LOCUS       WP_175978457             469 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia sp. BCC1047].
ACCESSION   WP_175978457
VERSION     WP_175978457.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..469
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50150
     Region          14..467
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mnhpappaat rrplppamld allaafgerv stadavrahh grdespfdpq lpdavvfars
       61 tddvrevvsl cslysvplip ygagsslegh llavrggvsl dlsemnrvls inaedltvtv
      121 epgitrkaln ealrdtglff pidpgadasi ggmtatrasg tnavrygtmr envlgltavl
      181 adgrvvktgs rarkssagyd ltrlfvgseg tlgviteitl rlhplpeavs aaictfptmg
      241 davrtvieti qigvpiarve fvdalavrsi nrhsnltlae aptlffefhg tdagvkeqae
      301 lvqalagqna gqgfewatrp edrtrlwsar hnayfamlql kpgcravttd vcvpisqlaa
      361 cveeteidlr asslpcpivg hvgdgnfhva ilidpdkpee laeaerindr iveralrlgg
      421 tctgehgvgl hkmrflpkeh gdnaidtmra iklaldprnl mnpgkiftc
//
LOCUS       WP_175978398             424 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia sp. BCC1047].
ACCESSION   WP_175978398
VERSION     WP_175978398.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..424
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41762
     Region          5..>328
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpshadspat hhagsltifq gaalyigavl gtgvialpal aaevagpasl lawaalvvls
       61 gplaatfaal garypdaggv styarrafgp kaaaivgwcf yfavpagapa aamfggayva
      121 avtggghatv ivtaaaliat vsaanafgvt vsgrmqlvls allvalllaa vlasaphart
      181 anlhpfaphg wlavgqaaal lvwsfagwea ithlaaefrr pahdmprsag iavvvvgfly
      241 lsvaaasvtv lgpsagasga plaeliaggi gghaqvlaaa aallltlgtm nayfagaakl
      301 gaalgrdgal pawlahgsqv ggvprrslgv iavlaavala atalsdvgpk plvlvtsgcf
      361 vmvyglgaaa alkllprggi ayrcawisli avaglfmttg wyflfpllla ggallylqia
      421 gprk
//
LOCUS       WP_175978516             317 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175978516
VERSION     WP_175978516.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..317
                     /product="VOC family protein"
                     /calculated_mol_wt=33947
     Region          <241..301
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 mssfnlrnll rmtaassavl aallagapaf adethlddia spaaaarspa iavgpqydtt
       61 hvcvapedfd rftdsfvatf ggkkskqgvf qvtptpsqtm sqlvltpvgt isvfgfktpi
      121 pypfceertg ylvtdmdvav ksarahgadi vvttfpdpig rdaivrwpgg vnmqlywhtq
      181 apnydplqtv penrvyvspe sasklarnfa afshgkivsd vrhapgieig rpndtyrrir
      241 iesgfgkmtv latdghlpyp fgremtgyev adlaatlkqa eaagvtvlvp pfksdgrdaa
      301 lvqfsggyva eiharsk
//
LOCUS       WP_175978551             423 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia sp. BCC1047].
ACCESSION   WP_175978551
VERSION     WP_175978551.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..423
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45574
     Region          91..415
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdqpqhvriv glprsrdaya irdflqrrmi aydwceltsd adcaqvlgia plhdirlpvv
       61 ifpdgsrlyq ptlteiaarl gwvarprfve ydvsiygagp aglsaavyaa seglravvie
      121 rgaiggqagt sslienymgf pdgipgaela erareqavkf gvelltmreg vhatfvdgki
      181 rveladgsil varanicatg ieyrslglpe epaflnaglf ygagsseapm ctgeqvfivg
      241 ggnsagqaam nfarharqvt ilvrgaslad tlsrylidri ertpnievry rssvaalhgd
      301 gwldaielrs adgtrerlpa trlfvcigga pntdwakdtd iirnpdgylv tggdlydcpa
      361 fervwplerr pyhletsvpg sfaagdvrsg svkrvasavg egamavtfvh rflgedahrl
      421 alv
//
LOCUS       WP_175978684             424 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175978684
VERSION     WP_175978684.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..424
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=43831
     Region          208..416
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(215,255,293,396,399)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(215,396,399)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(215,255,293)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 msfrssvaaa vlgaavfvsp laasaasgsp vgwvaawata lqpipdlaap pplyrapdva
       61 grtvrqvvyp tvsgpaarir vsnaygrapl vveaaslara gegaalagga vvpvrfggsa
      121 svtlapgqar esdpvsidvt aaqpyaislq mgpnqqmtvw hrvsnqfnyv svpgdhvgdp
      181 gagafrtrfi qyawvtelav evgsargsva aigdsitdgl rssvnrnrrw pdalarrlma
      241 sgadsigvvn lgisgnrlls dsacygtsla srferdalsr sgvkaaivli gindinfaam
      301 ppragldcdh phtqvtaasl idgyrrlida ahrqgvkvfg atltpaalpa greairlevn
      361 rwirsgggfd gvvdfdavlr dparpsvlqr rydsgdgihp sdagytamad avpieqlqaa
      421 vggk
//
LOCUS       WP_175978709             266 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175978709
VERSION     WP_175978709.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..266
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=27240
     Region          47..197
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mnqsrvkqtl vrttllaalt aglavslqgc vlgvvgaaag ggaliatdrr tlgaqtedre
       61 iqvksltqin nglpdqshvn vtvfnrrvll tgevpndask qraeeivrgi nnvngivnel
      121 svgpasslss randsylegr vkseliatkg isanyykvvs ergnlylmgl vtvdegnrga
      181 eaasqvpgve kvvkvfqyvk pqdaqalqda spasgasgaq aaaapadsat vgavpdasvq
      241 saplqppapi snssnvhpgn pkakaq
//
LOCUS       WP_175978697             212 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC1047].
ACCESSION   WP_175978697
VERSION     WP_175978697.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..212
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22279
     Region          1..212
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mnlhtwwlfv atvfvvsaip gpnmllvmth garhglrrss atmagclsal vlmlavsaag
       61 lgavleawpa tfdalrfaga ayliylgvka wrarvddapa advdavspqa astsrvalfr
      121 ngflvagsnp kailfaaall pqfinaaept lpqfgilvvt favievswyl vyaafgtrig
      181 atlksqsvak vfnrltgglf vgfgammalv rh
//
LOCUS       WP_175978713             405 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1047].
ACCESSION   WP_175978713
VERSION     WP_175978713.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..405
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40641
     Region          32..399
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(42..43,46..47,50,82,132..133,135..137,140,159,
                     162..163,166,234,237..238,241..243,246,274,278,327..328,
                     332,336,352,355..356,359..360,363)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 msespssesp spfaappdah rvlplparqr artasmalff vagmmyaswg vhvptvrdkf
       61 alspgllsia lfavaggsia amltiarwia rvgsrtacla gglvmsacaa lilvvpdywm
      121 llvvlalfgf smatldvamn aeasaveial gkpimsslhg mfsiggmaga aaggallsag
      181 mapvahlala aaasaavlva aspavlphvp hheqahgggn rwrspalwml ggialvalia
      241 egamydwatv ymrdvvaasp alasaayaaf sggmavarfa gdavrarfga pqlvfasasl
      301 acagmigall lpnpvavltg ftlmglglan mmpvlfaaaa rvkgihaaeg lahvaglayf
      361 gllfgpvvig avaqaanlti glsvvalcaa lvalvaprvl ahlki
//
LOCUS       WP_175978746             149 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia sp. BCC1047].
ACCESSION   WP_175978746
VERSION     WP_175978746.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 149)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..149
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16757
     Region          3..143
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 mtltflpvth adadalvair iaamrdslgr igrfdpqrar drflasfdpa lcrfieadhs
       61 ragfytlrpm adhwlldhly ivpahqrkgi gaavlraila dadehrmpvr vgalrgsdsn
      121 rfyerhgfvr tdeaewdity rrepgaatt
//
LOCUS       WP_175978717             233 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175978717
VERSION     WP_175978717.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..233
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26766
     Region          11..226
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mstsvmagre taaptrtglt vneiyeqlkq mavlyeirpg erfnelelae rfnvsrtpir
       61 ealnrlvaen llvfvpnrgf firelegkdv fdlfelrrsi ettavmlace rasdndikal
      121 rrfwkqvmkn aarmssaelv vkdeqfhlel aalsgnaeig rvlqginari hyvrwvdvdq
      181 rrneaftehl eildalaerd aercatltdt hirwrmeeit rvvqasvvkl yak
//
LOCUS       WP_175978751             200 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175978751
VERSION     WP_175978751.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21304
     Region          6..157
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkalgkkgaa treailaaar qaftqsgydv gvreiaekag vtamlvnryf gskeqlfeev
       61 vdavlsapgi ltrevmtnap dvstlcrdva aalvaktapd itsmdgflim lrsannrqat
      121 ailrtkfeth farplsellp geatsqraam flaviagfqv mrqvvemaal aqakpdqler
      181 qlqalfgvli ignpikdlag
//
LOCUS       WP_175978757             303 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175978757
VERSION     WP_175978757.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..303
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=33524
     Region          26..283
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mqnpqavpdy liqsdavrer fvrlkardvi ldvrhvgkrf atpqgecval ddisfrthrr
       61 efvcvigpsg cgkstliril agldaqtsge vlldgkpvdg pgadrgmvfq gytlfpwltv
      121 kknvmfglrm ngsssgvaer ealqwldlvg ltrfadvyph qlsggmkqrv aiaralanrp
      181 rillmdepfg aldaqtrarm qthlldiwrn idvtilfith dldeaiflad rilvlkanpg
      241 gvqelievpv prprdysqvn tpafiatkar lealihpkea ataeddgikp hmirmtdvad
      301 nve
//
LOCUS       WP_175978851             136 aa            linear   BCT 11-JAN-2025
DEFINITION  GFA family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175978851
VERSION     WP_175978851.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..136
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14958
     Region          5..131
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mahpepmegg cacgairyri advptdagfc hcrlcqrttg aavvasasvp idafeylqge
       61 ptvyassawg errfcgrcga qleyrradap rtveinyatl depsrlrpaw hvwygdrfpg
      121 ieidddlpky ddggre
//
LOCUS       WP_175978808             215 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175978808
VERSION     WP_175978808.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..215
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22672
     Region          29..129
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          80..209
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mkdkpaqgpr gldkdalvaa alalledvge aafsvrklaq svgcdpmsvl yhfkskdgls
       61 raianalsrs lvpvdpslpw rerlrdlarq yralalrypa afallqrhms tgpadlahie
      121 avhraltdag ipraalpsvc vgwyasvigl aaaeaggltr pandvelaem halsdaahpl
      181 vksaaplyaq ldpavvhdtm ldvlldgiaq rahta
//
LOCUS       WP_175978871             215 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC1047].
ACCESSION   WP_175978871
VERSION     WP_175978871.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122607
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..215
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23556
     Region          2..75
                     /region_name="GST_N_1"
                     /note="GST_N family, unknown subfamily 1; composed of
                     uncharacterized proteins, predominantly from bacteria,
                     with similarity to GSTs. GSTs are cytosolic dimeric
                     proteins involved in cellular detoxification by catalyzing
                     the conjugation of glutathione (GSH) with...; cd03043"
                     /db_xref="CDD:239341"
     Site            order(13,15..16,18..19,22..23,68,71..72)
                     /site_type="other"
                     /note="putative C-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(13,52..54,66..67)
                     /site_type="other"
                     /note="putative GSH binding site (G-site) [chemical
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(52,65..66,68..69,72)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239341"
     Region          88..200
                     /region_name="GST_C_3"
                     /note="C-terminal, alpha helical domain of an unknown
                     subfamily 3 of Glutathione S-transferases; cd03194"
                     /db_xref="CDD:198303"
     Site            order(91,98,158,161..162,165,169)
                     /site_type="other"
                     /note="putative N-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:198303"
     Site            order(91..92,95..96,99,135)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:198303"
     Site            order(98,102..103,106..107,166,169)
                     /site_type="other"
                     /note="putative substrate binding pocket (H-site)
                     [chemical binding]"
                     /db_xref="CDD:198303"
ORIGIN      
        1 mklvigdkny sswsmrpwll lvhfgipfde ivvelrrddt aarireyspt gkvpclvddh
       61 gaaiwdslai aetlaerypq fpmwpadpla raharcvsae mhsgfmalrt qmgmsirasm
      121 pgrgatpdal advaridalw secieasggp flfgefgiad amyapvvmrf ntyapalspe
      181 aagyaarvta lpavqrwida arretnvige yepqp
//
LOCUS       WP_175978951             290 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175978951
VERSION     WP_175978951.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..290
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31460
     Region          15..280
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mttarsldrt ypalrttegg gfvvhrpfpt rllmdfdpfl lldemgpvdy apgeavgapd
       61 hphrgfetvt yaldgrfrhr dssghagtlg pgdvqwmtag agvvhsempd pafaqtggrs
      121 hgfqlwvnlp rrdkmiapry qeipaaript atspdgrarv rviageafgv kaaietrtpi
      181 lyqhftlepg atvtqpvpag yrvfaypidg tglygpdrqa vdarhmivyg ddgdtvtfaa
      241 gdtsldllli ggvplnepiv rygpfvmnte eeirqavvdy qtgrmgriea
//
LOCUS       WP_175978962            1293 aa            linear   BCT 11-JAN-2025
DEFINITION  type I polyketide synthase [Burkholderia sp. BCC1047].
ACCESSION   WP_175978962
VERSION     WP_175978962.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1293)
  AUTHORS   Herbst,D.A., Townsend,C.A. and Maier,T.
  TITLE     The architectures of iterative type I PKS and FAS
  JOURNAL   Nat Prod Rep 35 (10), 1046-1069 (2018)
   PUBMED   30137093
REFERENCE   2  (residues 1 to 1293)
  AUTHORS   Keatinge-Clay,A.T.
  TITLE     The structures of type I polyketide synthases
  JOURNAL   Nat Prod Rep 29 (10), 1050-1073 (2012)
   PUBMED   22858605
REFERENCE   3  (residues 1 to 1293)
  AUTHORS   Staunton,J. and Weissman,K.J.
  TITLE     Polyketide biosynthesis: a millennium review
  JOURNAL   Nat Prod Rep 18 (4), 380-416 (2001)
   PUBMED   11548049
REFERENCE   4  (residues 1 to 1293)
  AUTHORS   Khosla,C., Gokhale,R.S., Jacobsen,J.R. and Cane,D.E.
  TITLE     Tolerance and specificity of polyketide synthases
  JOURNAL   Annu Rev Biochem 68, 219-253 (1999)
   PUBMED   10872449
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11462398
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1293
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..1293
                     /product="type I polyketide synthase"
                     /EC_number="2.3.1.-"
                     /EC_number="6.4.-.-"
                     /GO_component="GO:0034081 - polyketide synthase complex
                     [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0030639 - polyketide biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=136747
     Region          11..1290
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
ORIGIN      
        1 mdrsttdakr vaiigmscrf pggascassy wtllnsgrta iretprerfd idafyssdph
       61 epgttysrva gyvddpfffd rkffrtsaae amemdpqqrw mlelawsale nagiapgqlr
      121 grnvgvfmtt geadygrrtv wsgdperitt ysklgnlram apgrvahvlg lsgpaifvdt
      181 tcssslvaih laaqslqage cdvaiaggvn lilgpeetig varlqamsvs gqcrpfdana
      241 dgyirgeggg alvlkrldda rshgdridav lvgsavnsdg asngltapng aaqeavirra
      301 laragarpea vayveahgtg talgdpiels alrnvyarta trdkpvlvgs vkaqvghleg
      361 aagmagfika mlilrhryvp ahvnfatpnp rfqwegaqle ipregmplge ddslvgvsgf
      421 gitgtnvhli laapdrapda avhvarervl tlsgrspaal rrvasawraw ladtstplrd
      481 achtscvrrd hfdhrvalvg stkgdcvaal daflaadstg rwhagehprk arvaflipgq
      541 gawqpgigan lydengmfrk hadaclgqld aetaravlda ihdrtadavr hhpgqlahfi
      601 vcyalartwm dlgvrpnlli ghslgehvaa viggvmslgd glkaveargr lfdtatpaga
      661 mlavaagvde laarftfgtd lfvagingpg qtvvsgtkaa vtqvhdamva agkrvsllkt
      721 ydtpghspml rsmrdafrha leplkfasps ipiistltge ratdaiagve hwldlveqpv
      781 rfhealvaas dgktlflevg pgaalaklar aaaggdweca issladgpeg deetesagfa
      841 hacarlysvg qkiawsrlyg saprpaeapt ypfeaerfel pfpdragags khgrvqqrhd
      901 iaaneavpha vsqavdlgea aarayaepvl ttlraiaaav apdgvvladd valvgqglds
      961 laltelrvrl qqhfgrmppi tmlargasls slaawlgash hapdtepgar iaqpepaaad
     1021 drdlvvtlrt gagplvafvh pvggnvlcyq dlaavwpgdp tivavrhpya dlgraptyls
     1081 igqlasryra allaahgklp dllggwsfgg ivahemaaqw eaqglaappl tivdtplhdg
     1141 efatrlreld gefsaeevtq vveswladpr fvamldrdfy lgdvrrradp amfahiarlh
     1201 aasalalarh rpqqvhtria yalaartpgn lsgaqatqsl rllthgditv svfdddhnsi
     1261 vrepsarrva acfggdagtv haaadslara tst
//
LOCUS       WP_175978994             191 aa            linear   BCT 11-JAN-2025
DEFINITION  YbhB/YbcL family Raf kinase inhibitor-like protein [Burkholderia
            sp. BCC1047].
ACCESSION   WP_175978994
VERSION     WP_175978994.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..191
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=20165
     Region          51..186
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mrlgiflrss icstilcavm pavafadpla vkvddldhdg qfkgaqvyng fgcrgdnvsp
       61 rvswanvppg trsvvvtmyd pdaptgglgw thwevvnipp setsiqkgas gnvrlmpvga
      121 letltdfges kyggpcppqg eshryvvtvs alsipsvdvk stsspavvay qmhgnilgqa
      181 qyiatyhrss n
//
LOCUS       WP_175978995             373 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia sp. BCC1047].
ACCESSION   WP_175978995
VERSION     WP_175978995.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..373
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40280
     Region          4..354
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,55,97,231,308,328,330..332)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,55,97,99,106,179,182,184,231,238,308,328,
                     330..331)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,99,179,182,184,331)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            184
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mtqlfkpfdl ngipltnriv mapmtrsraa nniadertal yyaqratagl ivtegspisr
       61 egqgylfnps iysdeqvagw rlttdsvhav ggkifaqlwh vgrvshtslq pgggaprsat
      121 sriakdsivf aydenrkpgf vptstpsals tmevervved fvsaaaname agfdgveiha
      181 angylfeqfl nplvndrtdr ysatpgnqlr falevvdgva erigagkigi rispygqlfd
      241 mphypgildt ygalafelgm rriayihvmd qsnvsvapkd dtasedrtie llscikrvad
      301 ntsiilaggm tinrakvlid dglidlaafg qpfianpdlv hrlktglpla tadratyysg
      361 glkgyvdypp fga
//
LOCUS       WP_175979002             282 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia sp. BCC1047].
ACCESSION   WP_175979002
VERSION     WP_175979002.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..282
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29751
     Region          4..251
                     /region_name="17beta-HSD-like_SDR_c"
                     /note="17beta hydroxysteroid dehydrogenase-like, classical
                     (c) SDRs; cd05374"
                     /db_xref="CDD:187632"
     Site            order(9,11..14,34,58..60,86..89,109,136..138,151,155,184,
                     186..188)
                     /site_type="other"
                     /note="NADP binding site [chemical binding]"
                     /db_xref="CDD:187632"
     Site            order(110,138,151,155)
                     /site_type="active"
                     /db_xref="CDD:187632"
     Site            order(138..140,145,151,182..183,189,206,209)
                     /site_type="other"
                     /note="steroid binding site"
                     /db_xref="CDD:187632"
ORIGIN      
        1 mqetvlisgg nsgmglstal llaqrgyrvf agarseegla tirskarehd lpitplaldv
       61 qntdsvatav ndvlissdrl divvnnagyg lvasvedgtd eefvrqfdvn vfgvlrlira
      121 avpamrqarr gvlvnvgsfl ghmglpllth ynaskyaveg iteslrlels pfgirvhtva
      181 pglfrtgfvs rgltanprtt asdspyavva skllplvvsr inegpdpiav adavlsaieq
      241 pdaparipvg eeairadelk rslapaefea avcrlyglaa pa
//
LOCUS       WP_175979013             297 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia sp. BCC1047].
ACCESSION   WP_175979013
VERSION     WP_175979013.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..297
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30032
     Region          1..287
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mevgfcgpgl mgapmirhll aaghrvsvwn rsrdkadalv kdgaqvagtp relaervetv
       61 fvcvldgrav gdvvfgehgl lsgdanarrl qrivdhssip paatcdyaar aaalevgwvd
      121 apvsggvpga qagtlavmag graadldavr alidtyasri thmgdagagq taklcnqaiv
      181 tatvtaiaea vglaqasgid aarlaealag gwadsvllqt fvprmtsggh ppigalstfq
      241 kdvdaiadaa rdtgavmpvs atvqqvlrlg aaqglagadf aafidivrpg ngrqqas
//
LOCUS       WP_175979023             244 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia sp. BCC1047].
ACCESSION   WP_175979023
VERSION     WP_175979023.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..244
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25161
     Region          59..102
                     /region_name="LysM"
                     /note="Lysin Motif is a small domain involved in binding
                     peptidoglycan; cd00118"
                     /db_xref="CDD:212030"
     Region          <98..242
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
ORIGIN      
        1 mretipihda ltrwlpqaal vaaaialmgc tmtpwtdswq ptrqpastsa atpgviagyy
       61 rvnpgdtlag ianaygqrvq dvanwnrmap tdavspgqvl rvappqaats ygqppaaaaq
      121 pgslawpatg vvatpfsagk trgvviaasg pdhsvraaan grvvyagtgv kaygplvilk
      181 hdnglitayg hngkllvneg davrqgqpva emgadasgrs tfefevrqng kvvdpmnflp
      241 rngg
//
LOCUS       WP_175979031             472 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1047].
ACCESSION   WP_175979031
VERSION     WP_175979031.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..472
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48090
     Region          23..450
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,277,280..281,284..286,289,317,321,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msefaspaga hepavnwram savllavala tldtaianta lpaiatdlha spaasvwiin
       61 ayqlamvatl lpfaslgdiv ghkrvyvagl avftlaslgc slastlpmlt aarivqgfga
      121 saimsvnval irglfpahrl grgvgfnalv vgvsfavgpt iaslilsvaa wpwlfavnvp
      181 lgvfalavam pslpqtargk hafdpvaalf nvitfaslif algefaqrgp lsvvfaaaav
      241 afafgwllir rqaghpapml pvdlfrrpvf tlsaltavca faaqglafvs lpfyfetvlh
      301 rsavetgflm tpwsaivala apiagrlsdr yppgllgaig lallsagmvs laalpvspgv
      361 vdigwrmmlc gagfgffqsp nlkalmssap persggasgi iatarligqa tgaalvalsf
      421 giagrhgptl almlgagfag aasvasglrl fapshragap vvserveepa te
//
LOCUS       WP_175979065             117 aa            linear   BCT 11-JAN-2025
DEFINITION  FmdB family zinc ribbon protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175979065
VERSION     WP_175979065.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..117
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11127
     Region          1..73
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 mpiyayrcea cgfakdvlqk msdaplsqcp ecgkdafrkq vtaagfqlkg sgwyvtdfrg
       61 gsggasapat asgdaapaap aaeaapaaaa paatssagst tttsaapapa atpaags
//
LOCUS       WP_175979073             116 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF190 domain-containing protein [Burkholderia sp. BCC1047].
ACCESSION   WP_175979073
VERSION     WP_175979073.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..116
                     /product="DUF190 domain-containing protein"
                     /calculated_mol_wt=13213
     Region          5..103
                     /region_name="COG1993"
                     /note="PII-like signaling protein [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:441596"
ORIGIN      
        1 mdriflrfyv heqhrlhwkp lwewlleean rmgvaggsaf ramagfgqhh vlhedrffel
       61 qgslaievef ivtedeaqrl lerlshekvr vcyammpaqf gvidtlgapp aqgpaa
//
LOCUS       WP_175979091             581 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia sp. BCC1047].
ACCESSION   WP_175979091
VERSION     WP_175979091.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1047
  ORGANISM  Burkholderia sp. BCC1047
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Burkholderia sp. BCC1047"
                     /db_xref="taxon:2676299"
     Protein         1..581
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=61573
     Region          13..581
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mtlrrklhsp iylaililaa payaqslpna gsllneqkia pqprapqatt peevvpseap
       61 pgagepeagp tvtlksitfd gdkrvadaed lqsvtasmvg kklthaglqk iadtitqylr
      121 grgyalayay lapqdltagn lvitivegrl esgkdrvtik gntrssneri vaianaalpt
      181 drplkkedle ralllindrp gvsakavlqk gaqpgtskll vettptpivn gqlsidnygs
      241 rstgiergta tifvndplgm gdqvtlglsk sqgtevanlg yslpltptgl tlllggsylh
      301 yrvvqdaysa ldlrgsavtg svglnypiir trtqnlnatv mydhkylkds aldvslskrk
      361 ldnltfslsg nrydgllegg vtegraavtf ghvdlsgnpv dqladsmtar thgtftklaa
      421 nlsrlqtldp nwsvyggwag qlsntnldss ekfllggptg vrgypvgegs gdegwmgtve
      481 lrrfvnigvp svkvqalgfv dvgqirlhht tyagseineg htnkvtltsa glgvnvwsgr
      541 wnahaavart igrndgasla gnnadglnts wrawlqlgma f
//
LOCUS       WP_175979124             740 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: xanthine dehydrogenase family protein
            molybdopterin-binding subunit [Caballeronia].
ACCESSION   WP_175979124
VERSION     WP_175979124.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..740
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=79178
     Region          1..735
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mtvigkpldr tdgvlkvtgq arysadntda klahavivts tvahgriasi dtsraqsmpg
       61 vllvmtyrna mrlpnngvpd aqppavrklt llqtnevrys nepvavvvad slehaqgaar
      121 yvdvryeaam pnadftraka sayqpekmmg raittkrgdv daglkqgptr ldavyttpye
      181 hhnpmephat varwdgpnlt lydatqgvsg aksavakffg isdenvrvic pfvgggfgck
      241 gsvwshvvla amaskqtgrp vklvlerpqm fgmvgnrpft eqrfqvsard dgimtgmrhd
      301 vvsttstfed wtessaivtr mlyavpnqst shklvkldig tptfmrapge tsgsfalesa
      361 mdemayrlnm dplafriknh anmepqekkp wsekallecy rrgadtfgws krnhapksmr
      421 egntligwgv atatypanrs easavarilp dgtamvasgt qdlgtgtytv mtqvaadalg
      481 fpldyvrfal gdsslpkapv sggsqsaasv spavraasme ardqliamal adrgspvagl
      541 aredvtvsng wvvslsnpdk rdpaaaiiar nggkpieaia ttrpgdekkq ysfhsfgavf
      601 aevhvdadlg iirvprivgv ydvgtlfnek tahsqlmggi vwgvgsalle ksemdsrygr
      661 ytnanlaeyh vpvnadigml diafvgepdp hinphgargi geigitgvag algnavyhat
      721 gvrvrdlpit ldkilpptma
//
LOCUS       WP_175979149             207 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Caballeronia].
ACCESSION   WP_175979149
VERSION     WP_175979149.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..207
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21702
     Region          3..192
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mvsahllwvf vgalavvyal pgpdmalvlq tsgtrgfrhg lavaaglata rathvtlsal
       61 gvaallrsap wlydgvriag glylsyvaiq ifrspafgle aasghtastl rsaytkgils
      121 silnpkallf csvllpqfvr petgpvwsqv velgvvlvvv gvafdltlaa gavrisgwlr
      181 rhpkaqtvqr wtfsaallaf aarlsle
//
LOCUS       WP_175979192             224 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DUF799 domain-containing protein [Caballeronia].
ACCESSION   WP_175979192
VERSION     WP_175979192.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..224
                     /product="DUF799 domain-containing protein"
                     /calculated_mol_wt=23263
     Region          8..224
                     /region_name="COG4380"
                     /note="Uncharacterized conserved protein, DUF799 domain
                     [Function unknown]"
                     /db_xref="CDD:443506"
ORIGIN      
        1 mtfnisrkli avlsvlltmt acasrspsqt dytafrnskp rsilvlppvn dskdvgatyg
       61 mlsqmtmpla eggyyvvpva emeetfrhng lttandiqdv saaklrsifg adaalytkit
      121 aygssyqvva sttqvtaaak lvdlrsgetl wsgsatangn evgtnvsvgs gligalaqaa
      181 vthvvnvtsd kswavaglts qrllatggsn gllygprspk ygtd
//
LOCUS       WP_175979193             462 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FAD-binding oxidoreductase [Caballeronia].
ACCESSION   WP_175979193
VERSION     WP_175979193.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..462
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49910
     Region          7..461
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 msnisgeaid tlkasvrgrl itpsdsdyde arkvwnatid rrpalivrca gaadviaala
       61 fareqgvlvs irggshniag savsddalmi dlsalksvri dpqakrayve pgallsdfdh
      121 eaqafglatp lginsttgva gltlgggfgw isrkfgvtvd nlvaaeivta dgtwrrvsad
      181 sepdlfwalr ggggnfgvvt lfeyqlhevg pqiygglvvf pleqanevlp kyrefvaqcp
      241 deltvwavlr lapplpflpe dahgkpvvvl ascyvgpven geralapvrs fgtpygehlg
      301 ampfaawqka fdplltpger nywkshnfas lndatfdilt navkslpstq cevfigamgg
      361 qtnrvpvdat ayanrdsiyt inihgrwsev adddkctkwa rdmfsamtph aigsvyvnfm
      421 tgeegdrvra aygpnyerla evkrrydpdn lfrsnqnitp aa
//
LOCUS       WP_175979225             480 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Caballeronia].
ACCESSION   WP_175979225
VERSION     WP_175979225.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..480
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48384
     Region          26..446
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(33..34,37..38,41,73,123..124,126..128,131,153,
                     156..157,160,287,290..291,294..296,299,327,331,383..384,
                     388,392,408,411..412,415..416,419)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 magmnsnlss setrlsarqt ltvtatsvgf vvsqldvsiv nvalasighd lgasvaslqw
       61 tidsyalafa almlsagslg drfgarrmfv gglalfalas lacafsgdat qliaaralqg
      121 vgaaamlpns lallnaacgh drrlraravg lwtaagavsi aagpivggvl iaafgwrsif
      181 wvnlpicaag ivatlawien arpkdaghar gidlpgqala ivalasfvga vielrplgpm
      241 hplvigalll alaaggafia ieresrtpml plslfaertf saavafgigv nltyygmvfv
      301 lslylqrvlg htplqtglaf lpltggflis nlasgpvvar fgsrgpmifg alldaagfaa
      361 lafvdattpt aallvpflli psgmglavpa mttallgtvg qpragtasav lntarqaaga
      421 igvaafgala ahgdgaasah qivdavrwsa aisvalllca aliarhvnnp asanaeervt
//
LOCUS       WP_175979240             334 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Caballeronia].
ACCESSION   WP_175979240
VERSION     WP_175979240.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..334
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34702
     Region          1..324
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 makpdsalst tkrrplqwea mlaivlvvsl vagrvlsplf lstanisnml adfteialia
       61 lpmtliivaa eidlsvasvl gassalmgvl whmglpmplv ivlvlafgtl agllnglviv
      121 rfslpslavt igtlalfrgl ayvllgdqai adfpasytaf gidtvgdtfl pmpfvlviag
      181 aiiftvllqa tpfgrslfai ganptaaqfs gidvaktklk lfmmsgamaa lagivytlrf
      241 tsargdngeg felsviaavl fggvsifggr gsmigvllsl viigvlrnal tladvssetl
      301 tivtgallls svlipnlvar wraarekrlm aqal
//
LOCUS       WP_175979312             287 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Caballeronia].
ACCESSION   WP_175979312
VERSION     WP_175979312.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 287)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..287
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30794
     Region          1..271
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mialpaqrdp kgwlvapali filalfiypf ayglmlsfnp mngggiwany vtfftdssmw
       61 ptiivtlkla vpatiinvgv svpvafalrr tspwqkfatt llvvpvtlgt vliadgmlty
      121 fspngwfpqa lqalhlygde vrlthnywgv lislivsgfp faflltlsyv tgidptlara
      181 aatlganpwq qfrqiylpll lpgltmtacl sfvqafsvfp savllgapag ptrvisiaas
      241 eaafenydya lastiaivmg fvqllvvggm lgarrffytg pvtggkg
//
LOCUS       WP_175979332             308 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cation diffusion facilitator family transporter
            [Caballeronia].
ACCESSION   WP_175979332
VERSION     WP_175979332.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..308
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33102
     Region          7..297
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mkeespkaif yalaanfgia vckfgaaaft gsgamfaeai hstadcgnql lllfglkraq
       61 apanalhplg sgreiyfyal ivalllffvg gafsvyegah rlmhheplsn pivalvilgi
      121 svvleafsla gaireirkga pnktlwrwfr etresellvv agedvaallg laiafaavlm
      181 tmltgnpayd aagsigvgvl lmiiaflvar evksmivges aspevrkaid ahlrtrpeit
      241 riislitlqw gkhvvvavqa emidyasgra midainiied dlqrafpqvr wvffepdvar
      301 drgeptaa
//
LOCUS       WP_175979338             612 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glycoside hydrolase family 15 protein [Caballeronia].
ACCESSION   WP_175979338
VERSION     WP_175979338.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Sakaguchi,M.
  TITLE     Diverse and common features of trehalases and their contributions
            to microbial trehalose metabolism
  JOURNAL   Appl Microbiol Biotechnol 104 (5), 1837-1847 (2020)
   PUBMED   31925485
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..612
                     /product="glycoside hydrolase family 15 protein"
                     /calculated_mol_wt=68153
     Region          19..605
                     /region_name="SGA1"
                     /note="Glucoamylase (glucan-1,4-alpha-glucosidase), GH15
                     family [Carbohydrate transport and metabolism]; COG3387"
                     /db_xref="CDD:442614"
ORIGIN      
        1 mghhpeqipp aalpvdgrgm ignmktaalv slcgaidfmc fpridsptvf aalldgdrgg
       61 afaitprapn anvkqmylpe tnvlltrfmt gdgvcelldl mpvasnatra dalpncvlri
      121 vrlvfgrmtl dvrcdprfdy arakhtahav ekgvefmrdd gapslrlrsn vpltidgqsa
      181 catlnleega cacfvlgeae gladidanhd siltetidyw kewssrstyr gryrevvlrs
      241 altlkmlsse efgaivaapt fglpeaqdgs rrwdyrftwi rdaafsvyal lrlgytgeae
      301 rfmkwiaers rdcsahgqlr vmysvdgada peeselkslv gevpgrivig ngareqvqld
      361 vygalldsvy lynkygaais ydgwrhvtrt vdyvvehwre pdngiwefrn gtrallhsrl
      421 mcwvtvdral rlaekrslpa plarwfetrd eihrdiheqf wnddiesfvq tpgsdtldas
      481 almmplvrfi gpkdprwigt ldaigrelrv dplifrytrg stldglpgte ggfsacsfwy
      541 aealaragrv degrlvfekm layanhlglf seevatsgea lgnfpqalth lalisaayql
      601 drnldrvhvp wt
//
LOCUS       WP_175979340             242 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Caballeronia].
ACCESSION   WP_175979340
VERSION     WP_175979340.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..242
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26621
     Region          25..238
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mntsldtatt vstpydalhk igsgergslt daveaalrea ivtlalepgm midklavcer
       61 mgvsrfpvsa alarlehagl vevlpqrgtr vkpialedih qhlfirsale vetvrgvari
      121 reaatldala lnleqqrmml ktdqrlafht ldlafheill dainlprvke ivavsrsald
      181 rarqllaspe rlvhtldehe rifdairsgd adtaakamhd hldqvvaelr rsaqerpdqf
      241 ap
//
LOCUS       WP_175979354             210 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: response regulator transcription factor
            [Caballeronia].
ACCESSION   WP_175979354
VERSION     WP_175979354.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..210
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23083
     Region          7..201
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mnssapmvyi vdddngmrts lawlldsvgv ksegfanaad flrafdvsrp aclvldvrmp
       61 easgfdvqae lnrrgatlpi ifvsghgdip msvralqhga idfvekpyns qqmldrvqra
      121 mklamqrhak dqrqrelrer vdsltgreke vlrgviegka skriaadlqi svktvdvhra
      181 sikdklgaas iatlvrdvle vwspsgdera
//
LOCUS       WP_175979350             489 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sensor histidine kinase [Caballeronia].
ACCESSION   WP_175979350
VERSION     WP_175979350.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 489)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 489)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 489)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..489
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=54391
     Region          <26..>179
                     /region_name="PRK13560"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:106506"
     Region          126..484
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mnfpteddfh rlldaltqcv llhdaetkai vwanraacia lgfsveellp lkahdmtrdd
       61 iryrreiavn amdrsitegp qsyewcyrsr agvdmlseai atyvpltgre vvmvqfrdis
      121 aedamrqklr ryetrlreym qdlgegvavl tprgkvsfis esgrrvlgva ndaplgvald
      181 yctrsdrdrl vtqlrsatrq hstpaqryai trrdgakrwl ritcrridie dgtlvhfrdi
      241 sdevaieear rsearmleya grynamgema taiahelsqp laavrnfieg aiqrlaqpds
      301 idsaiwglra adrqaehaah iiksvrefiv krepaeaqtd lrdvladvay fiqlrardeg
      361 vtvriepshe plpircervl igqvilnlaf naveamsgmk psagtvtlaa mmngktaelh
      421 viddgpgvpd dalerlfdgf ssskaggngi glslcknivs rhegriwaqr aagggleccf
      481 alpllhhtd
//
LOCUS       WP_175979360             437 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Caballeronia].
ACCESSION   WP_175979360
VERSION     WP_175979360.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..437
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46634
     Region          22..425
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,154,
                     157..158,161,256,259..260,263..265,268,296,300,351..352,
                     356,360,376,379..380,383..384,387)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 msshspvayl tgdesstyak vtwrllpflf vcylcayldr invsfaklqm lndlhfsdav
       61 ygagagvffv gyllfevpsn lillrvgarr wiarimvtwg visagmmfvt tptsfyimrf
      121 mlgvaeagfi paillyltyw fpasrrskvt alfmtgipms gvvggplsgw imthmggahg
      181 iagwqwlfll eglptavlgv vayfylddkv adakwlndsq kamleanlrd eepahalhsv
      241 kdgllhpkvl llsvtyffft mglygvsfwl ptlvkasgvt dpldigllsa ipyaagaiam
      301 lavghssdkr gerrwhlaga gfvgalglfm svmyahstff gmigltlatm gvvttisqfw
      361 vlppailsgg aaaaglalan svgsisgvvs pwligviqtq sgstgsgvlg laascvigsl
      421 lvfavpaalv nsrrrsd
//
LOCUS       WP_175979388             421 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Caballeronia zhejiangensis].
ACCESSION   WP_175979388
VERSION     WP_175979388.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia zhejiangensis
  ORGANISM  Caballeronia zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Caballeronia zhejiangensis"
                     /db_xref="taxon:871203"
     Protein         1..421
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46718
     Region          <228..387
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 madidnirdm apldlirtlr aagraaeaca laaqlaasan pdcwlaqlgv dlsflgmhaq
       61 aekflklgle eplsqanrya lteelcmvqf algkfheanq ryrtirgrsy aevfhqlvle
      121 sdpdwagalp dkllgmdesv agkrifisae ggfgdfvqfs ryidallreg asmivseqfs
      181 gweevfrqse qvrlsmatqe qraaelaccd rvtfgfslya ryqrspyfpm enpaariaid
      241 pakrlsddan allnvettrp kigliwrsas gvrhepyrsm plqrlesllt nqacqfyslq
      301 vgelgddera imnrhgvtdi aphlstfgdt arvlekldll vtidtgtghl agalnrpvrv
      361 llsracdsrw ldcqrftpwy psmrlyrqte lgdwtqplad lcadlvsfsa ssapapsaes
      421 p
//
LOCUS       WP_175979370             297 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ketopantoate reductase family protein [Caballeronia].
ACCESSION   WP_175979370
VERSION     WP_175979370.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 297)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..297
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31277
     Region          1..295
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkvavmgaga vgcyyggmla rashevvlia rpqhveaver dglrldtqhf dervhvaast
       61 dasavkgaql vlfcvkstdt esaakalapy lehdalllsl qngvenaerl rellpqeaaa
      121 avvyvatema gpghvkhngr gelviepstk segvaralva agvpteisdn vrgalwaklv
      181 lncaynalsa itqlpygklv qgegitrtmr dvvdeclava kadnvtipgd vdaavrriae
      241 tmpnqfssta qdlargkkse idhlnglivr rgealgvptp anrvlhalvk aieskgs
//
LOCUS       WP_175979399             351 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Caballeronia].
ACCESSION   WP_175979399
VERSION     WP_175979399.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..351
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37733
     Region          10..325
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mepqseaikt dvliigagpv glfaafeagv iglscqivdt lgriggqcie lypdkpiydi
       61 paipsctare lvdrlleqir pfdvpihldq rvqsvtqrdd dhrwtvtten gmtfdcaail
      121 iaagngafvp qrlqlpeaaa legrdvhysv sraadfadke iivagggdsa ldwalalkdi
      181 arkltlvhrr ngfsaaansv atmkraveag emsfvvgmie sldapdgvlr garikqvegs
      241 tdlavdkiva lyglvselgp iatwnldvrg grievdtsny essrpgifav gdianypnkq
      301 klilsgfhea slalrkaysy aypekkrvhv hssydaklae rvsaahtadh a
//
LOCUS       WP_175979543             444 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: YihY/virulence factor BrkB family protein
            [Caballeronia].
ACCESSION   WP_175979543
VERSION     WP_175979543.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..444
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=45643
     Region          23..289
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mssvstqkie avvkkdaswa lgalkqfsed rcaamaasia fysafslapt lvmviavagw
       61 ifgpeaargq lfhqvnglig dqaaagvqsi venahrssgt giaaiisfvl lavgasatfs
      121 slntalnivw pmsgeqrssi mtlvrvrlvs fglvlgvafl livslvldta iqavgmwlwa
      181 nspfvivgdv vqlvvglail taafgalmkf lpdapvqwrd alvgglvsal lfsagkklfa
      241 lylthagtas afgaagslav llmwlyfsaa vlllgaefsa ararmhdprg awgqqnngrv
      301 ppgsrakigs llaastrtav pvagaasaaa pltpasapdd apatasarra igaraqhaqq
      361 ltgqarrkvs avaralalsr klaraestat ratalamvga grkashanaa vrrhpwravl
      421 vaagagmala llsrrdaare ndrg
//
LOCUS       WP_175979487             777 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Caballeronia zhejiangensis].
ACCESSION   WP_175979487
VERSION     WP_175979487.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia zhejiangensis
  ORGANISM  Caballeronia zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 777)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..777
                     /organism="Caballeronia zhejiangensis"
                     /db_xref="taxon:871203"
     Protein         1..777
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=85777
     Region          176..761
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mhtvsepayt vavralceft akqgdldlrf tptpsaqegv aghatvtnrr pdgyqkeisl
       61 setygpllvr gradgydpal nrleeikthr gklesmpenh rhlhwaqarv yghlmcrklg
      121 leaidialvy fdivdetesv lvetqtaaal avhfeaqcer fiawarqela hgaardealk
      181 tlafphadfr pgqralaeav yrsavskrcl aaqaptgigk tvgtlfpllk awpgqqldki
      241 yfltaksagr qlaldalttl aakplrvvel vardkaceyp drachgescp largfydrla
      301 daraaalqct qfdrasvaev arrhdicpyy lsqelsrwsd vivgdynyyf dtsamlfala
      361 eanrwrvavl vdeahnlver argmysatld qsafnamrrg apgvlrkalg rvarswseta
      421 seqhasgiey aahtepparf ltalgqavsl mtetlgeqpd aftpdtlrfy fdavhftria
      481 erfgshsifd itlsganana sanakkrnat lclrnvipap hlaprlarah svalfsatlt
      541 pahfyadtlg lpassvridv espfsadqld vraiadlstr yrdrersvdr iadliaaqyf
      601 raegnylsff ssfdyltqva aalaarhpsi pcwqqsrams eaaqreflar fvadgrgigf
      661 avlggafgea idlpgtrlig afvatlglpq lnpvnqqmka rmheafgegy aytylfpglq
      721 kvvqaagrvi rgpldrgvly liddrfarae vrrllpawwq vkvlrqrdls esrntti
//
LOCUS       WP_175979556             156 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: chemotaxis protein CheW [Caballeronia].
ACCESSION   WP_175979556
VERSION     WP_175979556.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..156
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=16776
     Region          1..145
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mlfvqftlda drylldsaqv ermlplaplk tlpgapawva gvldceganv pvidlaalal
       61 arashervst rlalvayprc gddgaikhhr lgllleqatr tvtfdaasft dagigtphar
      121 ylgplarder gllqwvrieh llpddvqtll fagsea
//
LOCUS       WP_175979526             520 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Caballeronia].
ACCESSION   WP_175979526
VERSION     WP_175979526.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..520
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52651
     Region          45..453
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(50..51,54..55,58,90,140..141,143..145,148,168,
                     171..172,175,300,303..304,307..309,312,340,344,397..398,
                     402,406,422,425..426,429..430,433)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mnnpqrvhav aspvspcdel airaqpvaad qpchrkrlal satilgssma fidgsvvnva
       61 lpsiqselga siaamqwvvn ayllflgalv lvggamgdkl grrkvfvagv aiftvasaac
      121 gfapgtgwli aaralqgiga allvpgslai igavfdgear graigtwagv gaitssvgpa
      181 aggwlvdafs wraifflnvp laaatialam asvpdshdad apptldwpga astaaglaml
      241 tyglteapsr gfadplvlgm igagivllaa fiaieaksrd pmvpldifrs rdfsganivt
      301 lllyfglggv lfflpytlir aygftateag aavlpmplii gllsrftggl tsrfgarall
      361 iagpcvaglg famlalpfva gsywmgflpa lvvlglgmti tvapltttvm asagseragi
      421 asginnavar vasllaiavl givfvwshda alsarldrlh vprdsmrald aqptseassa
      481 plaraqadai adalravaal saacafaaag aaaatiqrrk
//
LOCUS       WP_175979528             768 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: mechanosensitive ion channel family protein
            [Caballeronia].
ACCESSION   WP_175979528
VERSION     WP_175979528.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 768)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 768)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 768)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 768)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..768
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..768
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=82313
     Region          477..741
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 msaftrrida rrvlmalgvl igcscvfpam aapltgamqk fiapqtpada taasapssas
       61 qaemvrslnn ligtldndaq rsalvtqlka lrdatqsaap atpapanadl lgaiasgias
      121 vetnlseglt pmrfwtargs aaagelqavv tgakgesfgr ivsgmgatla gwglcaflli
      181 rvqrrifary grdvalapnp tstqllafal rqtgpwvvaf iavllfvram pdalgrtlgl
      241 viayaivags ifsaicmivf svfstahrrv avqqlltrtl wplfaigasg algdatanad
      301 vtrqlgpnla giistfagla aallcgyfal ayrrpvthli rnrpyarrrd hqfatealdi
      361 laslwhipil liavasvvai idgrgaegdv lrpsllsaal lvltlfasal llhltrrrdt
      421 raqrraphlt rllrfgctli vlliwlaylr felelwsgpi arlirhsamt pgfrhaliav
      481 vatvfgawfi wivldtvile algqnssrnk alspgvrart mlplvrngif vtvaslaaiv
      541 acaslginlt pllagagvig lavgfgaksl vtdlitglfi iveetisvgd wididgghag
      601 tvmdltirtv rlrdgqgavh tipfsqikiv knlsrdfana vfevrvpfsa kldditrmin
      661 evgadmmadf rfrneiigpv evwgldrfes ncivvkgqik tkplqqwsva rafnarlklk
      721 mdeagiemml pqmhiqtske sdersqaqtr haadgavqpd lrvlkesp
//
LOCUS       WP_175979562             683 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Caballeronia zhejiangensis].
ACCESSION   WP_175979562
VERSION     WP_175979562.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia zhejiangensis
  ORGANISM  Caballeronia zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Caballeronia zhejiangensis"
                     /db_xref="taxon:871203"
     Protein         1..683
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=74889
     Region          21..679
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mslqqarlsm rdwlvtdghv wlhlaktlla afiamsiamr lelpqprvam tttfvlmqpf
       61 sgmvlaksvy rfagtalgmi aalalgavfv qqpelhalal tiwvaactal avryrhfrwy
      121 gfvlagytaa ligipavtdp nslliatltr gaevmlgivc ssvvsalvfp rhasatltqs
      181 ldarrmrfaa faadvlrgrl sriarerrfa dfvdeivgfe atrgfatyes pamrqgngkl
      241 aqlnsafmda carlhaldqs mkrlrasdal apffeelaqn ferealkehl erykatlpkr
      301 lrdaqralph tdhatqldft tsaellyrfi adtirylsip nhrtapryda rtsrfvvvat
      361 fmrtgiviaa tawfwivtaw psggyaviga tlacalssal arpskfiaqm aagaalaivi
      421 gyaylcrvyp aidglallca mlapplaaga flamrpssag ygigfcvffc llaapdnriv
      481 ydpglllnng vavlvamlga aiacavivpp rtrwlvgktl aqlraqaala cegklaglge
      541 rfhsgthdlm sqlralltrr srehrhallw mlvtlevgqa midlrrdsra lhtacfpdal
      601 riawstslar vlrdiavlfr tpdsrtlrra iasvvasivi aedmlertrd ernarrevqr
      661 vlaclhfvrt alvdpdapfd ahr
//
LOCUS       WP_175979601             366 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Caballeronia].
ACCESSION   WP_175979601
VERSION     WP_175979601.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..366
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39151
     Region          1..364
                     /region_name="LhgO"
                     /note="L-2-hydroxyglutarate oxidase LhgO [Carbohydrate
                     transport and metabolism]; COG0579"
                     /db_xref="CDD:440344"
ORIGIN      
        1 mdriecvvig agvvglaiar alakrgrevi vleagegigi gtssrnsevv hagiyyprgs
       61 lkaelcvrgr dmlyafcqeh gvphrqcgkl lvatarnqvp qlaaleqkgi enrvkglvri
      121 sgaqaaemep qlqcveavws pltgivdshq ymlalqgeae nhganivfht pvtsidareg
      181 cfivetgges parfrasfli nsaglhanei arrirglddr hvpplyfakg nyfsvsgrap
      241 ferliypmpn eaglgvhlti dlggqakfgp dvewvqalny dvdprradsf yaairaywpg
      301 lpddalqpay agirpklsgp gqaaadfviq gksahgvpgl vnlfgiespg ltaslaiaer
      361 vadmar
//
LOCUS       WP_175979632             330 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Caballeronia].
ACCESSION   WP_175979632
VERSION     WP_175979632.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..330
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35660
     Region          4..318
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mndlltirnl qvtfggtqav dridlsvkpg evvgvvgesg sgksvtmmal mglidapgkv
       61 tadqvtfdgk dllkasarar rriigkdiam vfqdaltsln psytvgyqik evlklheglr
      121 gdaldkrale lldqvgipda knrinsfphq msggmnqrvm iamavacnpk lliadeptta
      181 ldvtiqaqim ellvklqker gmalvlishd lavvsevaqr vavmyageii etnhvptifs
      241 ephhpyteal laaipehsrg aerlaalpgm vpgkddrpsg clfaprckyv vddcrkarpn
      301 lyqldkndpa vrarcikpln idvvveggar
//
LOCUS       WP_175979668             558 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Caballeronia zhejiangensis].
ACCESSION   WP_175979668
VERSION     WP_175979668.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia zhejiangensis
  ORGANISM  Caballeronia zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Caballeronia zhejiangensis"
                     /db_xref="taxon:871203"
     Protein         1..558
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=61033
     Region          11..545
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mkqnarkleg efdyivvgag tagcvlanrl tedpdvnvll leaggkddyh wihipvgyly
       61 cignprtdwl yktqaepgln gralsyprgr vlggcssing miymrgqred yddwahvsgd
      121 pnwswdsvlp ifkrsedhhg ggnqwhgagg ewrvekqrlk wkiletfaka aqqsgipatd
      181 dfnrgdntgv gyfevnqrgg irwnaakafl reamkrpnlt titgahtqrl vfegarcvgv
      241 eyrggdvdyi ararcevils agavnspqil elsgigngar lqrlgidvvk slrgvgenlq
      301 dhlqlrmayk vngvrtlntl sahwwgklfi gmqyallrsg pmsmapsqlg afaksnpdda
      361 sikrpdvqyh vqplslerfg eplhafnaft asvcnlrpts rgsvhiespd ahaapliapn
      421 ylstdrdrev aanalrltrr iagapalary apeeilpgiq fqtqeelvea agkvgttifh
      481 pvgtcrmgtd ndpgavvdsr lrvigarglr vvdasvmpti tsgntnsptl miaerasdmi
      541 redrrsieaq eviatala
//
LOCUS       WP_175979663             300 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Caballeronia
            zhejiangensis].
ACCESSION   WP_175979663
VERSION     WP_175979663.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia zhejiangensis
  ORGANISM  Caballeronia zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Caballeronia zhejiangensis"
                     /db_xref="taxon:871203"
     Protein         1..300
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32065
     Region          29..290
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 msavmkkkgl grgldallgg svditeavrg egtpsvlsld klqagkyqpr trmdegalqe
       61 laasiraqgl mqpilvrsvg ddhyeiiage rrfraarlag ldevpvlvkn vpdqaaaama
      121 lieniqredl npleeaqgiq rlldefsfth eqaaesvgrs rsavsnllrl lnlatpvqtm
      181 llagdldmgh arallavdaa tqiqlanhvv nrrlsvrete rlvaattkea patkaraand
      241 ggrdtrrlee elsdllsanv kiklggrgrg kvtidfgtld slegiltklr gsieattpta
//
LOCUS       WP_175979713             304 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: M48 family metallopeptidase [Caballeronia].
ACCESSION   WP_175979713
VERSION     WP_175979713.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Lew,R.A.
  TITLE     The zinc metallopeptidase family: new faces, new functions
  JOURNAL   Protein Pept Lett 11 (5), 407-414 (2004)
   PUBMED   15544561
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..304
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=33963
     Region          92..275
                     /region_name="M48C_Oma1_like"
                     /note="Peptidase M48C, integral membrane endopeptidase;
                     cd07331"
                     /db_xref="CDD:320690"
     Site            order(158..159,162,215,219,258)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320690"
     Site            order(158,162,215,258)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320690"
ORIGIN      
        1 mtvsfklral vcawtwasla pssahaqdeq ktpppysapn nqirfgntal frnliapatl
       61 eaqaadeyaq vihdaernkt llpdtnplvk rvreianhei pfalkwndra kswkweinvi
      121 ksadermvcl pggkivvysg lidklhlndn eigmmighei ahalrehare rlgrqqaaql
      181 ssngmpqlfg fsnyasqqpd igdelltmry spadeteadv igseiasrag ydpraavtlw
      241 nkidsgtrra ddgfiwlhpy gpdrrqdllk rmpdmmplya kavgktidql pnyagmgrfk
      301 ksgr
//
LOCUS       WP_175979764             250 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SURF1 family protein [Caballeronia].
ACCESSION   WP_175979764
VERSION     WP_175979764.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Reeves,J.E. and Fried,M.
  TITLE     The surf-4 gene encodes a novel 30 kDa integral membrane protein
  JOURNAL   Mol Membr Biol 12 (2), 201-208 (1995)
   PUBMED   7540914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..250
                     /product="SURF1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0033617 - mitochondrial cytochrome c
                     oxidase assembly [Evidence IEA]"
                     /calculated_mol_wt=27871
     Region          6..237
                     /region_name="Shy1"
                     /note="Cytochrome oxidase assembly protein ShyY1
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3346"
                     /db_xref="CDD:442575"
ORIGIN      
        1 mkirfwpall ilivvaitvr lgfwqrdrah qkealnaqiv afenaparev gvepmplksi
       61 efhrvearge fmpervvyld nrpyndqpgf yvvmplkleg ggyvlvnrgw lprnmadrtg
      121 iepyetpkgv vevkgiaran asqafelgsg gsaahkeirq nldirsyaae tglafqpfvi
      181 qqtndtgdrl vrdwpaptlg vernygymfq wwgmaaaaig fglyaarraa kkrdatdigg
      241 esddeaehha
//
LOCUS       WP_175979860             262 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: metal ABC transporter permease [Caballeronia].
ACCESSION   WP_175979860
VERSION     WP_175979860.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 262)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 262)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..262
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26784
     Region          4..260
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mfeydfmvna faasgivavl sgivgyflvl rgqtfaghal shvgftgatg avllgmpplw
       61 gmvgftlaag vgmgalgerl sgrdvaigvi lslslgfgll flhfftayat qatallfgnv
      121 lgvshdtlvv laglavvslg alavimrpll faslqpelae akgvslrlvs vmflaitala
      181 vaactqivgv llvfalmvgp aaaaqnvttr lssglvlaal falaqawagl tlafytdwpt
      241 sfwitmlaav vygasllgkr gn
//
LOCUS       WP_175979876             457 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Caballeronia].
ACCESSION   WP_175979876
VERSION     WP_175979876.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..457
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47076
     Region          12..440
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(19..20,23..24,27,59,109..110,112..114,117,137,
                     140..141,144,266,269..270,273..275,278,306,310,362..363,
                     367,371,387,390..391,394..395,398)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtplerrgma aillsvalat ldtaiantal paiaadlhtt paasvwiina yqlamvatll
       61 pfaalggilg hrrvylggli vfliasavca fswslptlva arllqglgas aimsvnaali
      121 saifpphrlg rgvglnaliv giafaigptv asivlslgtw pwlfavnlpv gvfalmiawp
      181 slpqtkraah gfdrfaalln vvtfaslifa lgeaaqrapa htvlasfgva lvagflllrr
      241 erghpapmlp vdlfrrpmfa lstmtaicsf aaqglafvsl pfffesvlgr sqvetgflmt
      301 pwsalvalma piagrlsdrh apgllggvgl ailcvgmvsl amlpaephal eicirmaicg
      361 agfgffqspn lkafmssapr ersggasgmi atsrligqat gaalvalcfs iagkhgpala
      421 lslgaafaga gsiasglrlv trkqsseriv gdasrea
//
LOCUS       WP_175979926             244 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: (Fe-S)-binding protein [Caballeronia].
ACCESSION   WP_175979926
VERSION     WP_175979926.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..244
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26415
     Region          <2..237
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mrvglfvtcl idmmrpeigf sviklieqag fevvvppsqt ccgqpaynsg drplardlae
       61 ktlrefeqfd yvvvpsgscg gmirahygdl frddpqlmsr farlqprvfe ltdflvnvak
      121 armepgvfdg mvtyhdscsg lrelgvksqp rellaragvp vtemagcehc cgfggtfavk
      181 ygdistaivd ekcanikasg adtvvlgdlg cmlniegrlr rtgdtstrvl hiaqvlagda
      241 arra
//
LOCUS       WP_175979940             210 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Caballeronia].
ACCESSION   WP_175979940
VERSION     WP_175979940.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22147
     Region          1..207
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mslqtfslfl pacfainmaf gpnnvlslsn gardgvrasv lasfgrivaf aimiaiaglg
       61 lgalllasqt lftaikyaga aylvwigvkl irsgpslvvk eegaargpmn larlikqefw
      121 vaagnpkail vftaffpqfv drsayatsfa ilgatfllle lvaifiyaal garlgslsrg
      181 argftwfnrv sgalmigfgv mlafvrrpat
//
LOCUS       WP_175979946             733 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Caballeronia zhejiangensis].
ACCESSION   WP_175979946
VERSION     WP_175979946.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia zhejiangensis
  ORGANISM  Caballeronia zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 733)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..733
                     /organism="Caballeronia zhejiangensis"
                     /db_xref="taxon:871203"
     Protein         1..733
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80117
     Region          28..711
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mstpasligr qplkevvldw artdglawiy ifkavlaall slwiamrldm aqprtamttv
       61 fvvmqpqsgm vlaksfyrfc gtmvglvvmm ifislfsqqp vlflsatalw vgvctagaar
      121 nrnfrsygfv lagytaalig ipaaqhpeaa ylsaltrvge vtlgtvcsga vsalvfpqha
      181 geqvrttvrr rfaqfvdyvc ralsgnmera qiertnlafv sdivgfeaar svavfenpes
      241 rmrggrlarl nsefmsastr fhalhqlmnr lrenasatti aalepffrev pplfsvsgep
      301 vknaadaaha aaqlrdykaa lprrvratra aleadpdfaq lefdtatell yrfvddmlay
      361 aetyaslssp shererwiar yvpktnllaa aisglrgaiv mfvlsafwia tawpsggtmv
      421 lnaaavcala sssprptlms aqmalgtmla avagmivvfg vfphiegfam mcaalapall
      481 lgaylstrra lagvgigyci ffcflagpdn lvhydptgym ndalalvlsm ivaavafavl
      541 lptdapwlrr lllgdlrrev vsarhgrltr ltthfesrtr dllaqinala tgrpdlqrda
      601 lqwlfavlef gnavidlrre iaglsnapqy aasmpwrrsi datldaiarl fdrpnaqrfd
      661 atlaaterai ddtrdvlarf dlpreekhrl qriashlhfv rtalldhesp fapfvhgapv
      721 rkhtpegadh vpa
//
LOCUS       WP_175979970             548 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [Caballeronia].
ACCESSION   WP_175979970
VERSION     WP_175979970.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..548
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57966
     Region          39..441
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mtssftaspl dnlaanigit psadtpatda padkpagptf eslglsadiv saltaagyes
       61 ptpvqqraip aalagrdllv ssptgsgkta afmlpaiekf aqlqkleaqq praprdpnaa
      121 rgrrpqpiar pkllvltptr elamqvstaa ttygkhlrrl rtvsilggva ygqqlmllak
      181 npeilvatpg rlidhlergr idlselnmlv ldeadrmldm gfiedietiv datpasrqtl
      241 lfsatidski tsltgrllkd perieivqkl eaksniaqtv hyvddrdhkd rlldhllrge
      301 gldqaivfta tksdadlian rladagfesa alhgdlpqga rnrtiralre rrvrvlvatd
      361 vaargidipg ithvfnydlp kfaedyvhri grtgragrsg tavslvhyae mgalkrierf
      421 vraplpvnvv agfeprkapp kggfgggrgr pggngsgrrf ggngggsssg rgygpgnagg
      481 ygnksnagsr eggyrdgggy rggnsdggyr ggnsdggyrg gnreggygsr dgysarrndg
      541 praprrgs
//
LOCUS       WP_175979995             286 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Caballeronia].
ACCESSION   WP_175979995
VERSION     WP_175979995.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 286)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..286
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31129
     Region          7..277
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mpdalaeidg ldvafashdg vlmpavrgvs ltvrrgerlg ivgesgsgks ltgrallgll
       61 ppeakwsaka lrlegqdlla mrpkarrrlc gtrmsmilqd pkfslnpvmt vaqqmretfv
      121 rqgvkegrra lrerivaale avhirdpqrv adayphelsg gmgqrvmiam mvsagprlli
      181 adeptsaldv lvsmqvlavl demiarhdtg lvfishdlpl vmsfcdrvav myggrvvetc
      241 aardlvhath pytrgllean pplenppdel ptlrrdpawl degiar
//
LOCUS       WP_175979997             248 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Caballeronia zhejiangensis].
ACCESSION   WP_175979997
VERSION     WP_175979997.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia zhejiangensis
  ORGANISM  Caballeronia zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Caballeronia zhejiangensis"
                     /db_xref="taxon:871203"
     Protein         1..248
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26930
     Region          22..229
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 msdtkrsaas nvsdsapnga naesiaenir aailehrlap gaklteaqlc evfavkrgtv
       61 rqalaqlsne rlvdlepnrg afvaspslqe vhevfemrri ielavvdria qghgvrrlks
      121 isatigkerr afeshdfssw irlsgefhte laaltgntvl ceclsglvar stlisalyes
      181 lgksscsfed heailaalda gdaakarvlm aqhlrdvelk mlerpargav dlkevfmkpa
      241 ereraldm
//
LOCUS       WP_175980132             717 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Caballeronia].
ACCESSION   WP_175980132
VERSION     WP_175980132.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..717
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78921
     Region          31..710
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mrnaaiesrr tqrstlrlgl ahwaatdglv wlhlaktlta afiamgiamk ldiptprtam
       61 ttvfvlmqpq sgmvlsksfy rmvgtiigti vavmlgalfp qqpplyigal tlwvslctaa
      121 alryrnfrwy afvlagytsa ligipsvtdp nglfiaalnr saavllaivc sgvvsaivlp
      181 qwssarlkhi rrerfvsfsk faaqalrgei dnerfltkyg efidsvigfe atrafasfed
      241 pevrsrsrrl arlnaafmdl ctrlhalhrf latrrghavd vvaaycaela tlldvardag
      301 midedtisrr aalvsafgvr lnaraeadre elartvsapa lmdfdaavql lsdyvsswty
      361 yadayvslvn ekhvfeesdi krvfvtntsv iavtflmtca vlgtigawwl ssdwpaggya
      421 iigaaavsal gsnsptpirf slqmasgaav stlaaylvld yvypaidgfp llcfvltpll
      481 glgaflatrp kftgfglsfc iffcilggpd rviryapepl lnsgialtla mlacavawtf
      541 vfpvekpwrv aaltrdlrrq mnvactapld darqlfqsgt fdliaqiral lpqptaqyrq
      601 alswilvvle lghasiefrt dsrdvdavrm vaadwraste etmrrlmqll dtpshntrda
      661 slraidrqie vamhgieamr gadheilrmr sllarlhfmr svlmdvdspf lrsytha
//
LOCUS       WP_175980137             468 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cytochrome ubiquinol oxidase subunit I
            [Caballeronia].
ACCESSION   WP_175980137
VERSION     WP_175980137.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..468
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51601
     Region          5..452
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mldhaldlsr aqfamtaifh ilwpiltisl saflvlvevl wirtgdvayy rharfwskll
       61 vlnfavgvvs gipmefqfgt nwagfsqfsg qfignilgfe gamafmleag figvmllgwg
      121 rvsrgvhlfa tsmvalgssi safwimvans wmqtpagysi vdgkivvtdf laaifnpdmv
      181 wglghmwvaa ietgmfviag isawnlyrrr hpeffvrsfr lallvlvfva plqiwlgdss
      241 gvsvfetqpa kgaaieghwk tnapgtgasw sllawpdrea qrndwsievp gmlsvlgths
      301 lhgqvkgltd farddqppal pllyyafrvm agigfafmll afwtayalrk trgkldalla
      361 rrklllawvl ciplpyvave agwivrevgr qpwvvyglqr trdavssvpa ssvslsiamf
      421 lafyavllft ffvlarrwlr agpdldimpp aamagetars kanavtgy
//
LOCUS       WP_175980165             206 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FMN-dependent NADH-azoreductase [Caballeronia].
ACCESSION   WP_175980165
VERSION     WP_175980165.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..206
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22775
     Region          1..195
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mkvlfinasp hgdashgyrl alemidtlrk rarvdivkrd laatplpplt qdyaraitsr
       61 hpdeaqfdis eqlireiett dtliintpmh nftvpaalkl widyvlrihr tfvstpegkv
      121 glmrdrptfv ivgsggfhgg elarqrdflt pylryalgsi glqdlrfvtl qglvcgseav
      181 aqaldlared iarhalfasd gdtvtp
//
LOCUS       WP_175980188             381 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Caballeronia].
ACCESSION   WP_175980188
VERSION     WP_175980188.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..381
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41270
     Region          3..379
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mklsethqqi rdttrrfaqe virplaeeld reerfpaevy rqmgelglfg itvpeafgga
       61 gldaaayalv meelsrgyss vadqcgllel vgtllsvhgt eaqraqymep llraalrpay
      121 citesdagtd vsgirttatr tadgwelnga klwihnapva dvafvlartn paagkrgmsi
      181 fivdcdlegv skgpkehkmg qrasqvgelh fdrvklrhda llgeegrgfq immsvldkgr
      241 vgiaalavgi aqagleaald yaqtrkqfgs hiaefqgvqw mladmakdiq aarllvhdaa
      301 erldtgdras iacsmakcfa gdtavkhsan avqifggsgy irgyeverly rdakitqiye
      361 gtnqiqrtii ardlvangas l
//
LOCUS       WP_175980202             577 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ShlB/FhaC/HecB family hemolysin secretion/activation
            protein [Caballeronia].
ACCESSION   WP_175980202
VERSION     WP_175980202.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..577
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=61063
     Region          18..577
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mnhatkspcf ssrskaraag vgivcasafs awaqqvpmpg taqvpsagtl lneqprpsts
       61 apppggssal pappaaapev pdgkkftlks irfagnetlp sdtllalvsd rigqevsind
      121 lnamstkvaq ayrergypla qvvippqdvt ngdvtftvle gkigrvrltm apgapvkesm
      181 vrarlaaiep gkplrqnele rtmlllsdlp girvssalet gsapgtvdln vtveptrrwn
      241 favsvddyga apagrwrlga vgrlaspfgi gdnldinlla aeradtvygr igydapvdas
      301 gtrvgiaysh lyyylgeqfs slnahgdadv vtasvshpli rsrsqnlllr galeyrsltd
      361 kidsvsfdnp qklyvasvgl syesrdsflg ggfnsadvql afahlnidsa laeaidqgpf
      421 grntqgnsvr ltmqanrlna itrntsffig vsgqwanqnl dsssritlgg pravraysps
      481 esvvdeglia taqlryavip sltlstffdi gvgrynarsi pgqgantvtr sgvglgafws
      541 gpygitvdas vawrttradt tgddkvprvy vqvsksf
//
LOCUS       WP_175980225             387 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: phytanoyl-CoA dioxygenase family protein
            [Caballeronia].
ACCESSION   WP_175980225
VERSION     WP_175980225.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10529740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..387
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42877
     Region          59..282
                     /region_name="PhyH"
                     /note="Phytanoyl-CoA dioxygenase (PhyH); pfam05721"
                     /db_xref="CDD:399029"
ORIGIN      
        1 mnqtnwyaes dcsldefasl lerdarpklt fashiqrgip lydcgalapa lddsstcmal
       61 qaewatvlrd gagvfvlkha yadvdpidea aaifesiirq erergasaad hfakagandr
      121 iwnaqeklcl haprvfaryf anrfiecaal awlgpgfqmt sqvnvvrpgg daqqahrdyh
      181 lgfqtadevr rypahvhais pyltlqgava hrdmpvesgp tkllpfsqry aqgylawrra
      241 dfreyfeahh vqlplekgda lffspalfha aganrtrdvq rmanllqvss aygrametld
      301 rarmcesvyp vlldfkstes msdaeidavi aacaegyafp tnldrdppig glapksqqal
      361 lrqaldeaws vdalanalkd nawrrnt
//
LOCUS       WP_175980388             380 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Caballeronia].
ACCESSION   WP_175980388
VERSION     WP_175980388.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..380
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43190
     Region          21..378
                     /region_name="COG3146"
                     /note="Predicted N-acyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:442380"
ORIGIN      
        1 mnreveihvv daladiaadd wnrlagenpf vrhaflsalq etecavkrtg wrahhlilkr
       61 ggefagampl yikshsrgey vfdhawadaf erhglryypk alsavpfspv tgprliaahh
      121 edrvllarga ieltrrlels slhvlfphaq dvealtdagy mlregvqfhw enlpgdgyas
      181 fdaflatmsh dkrkkvkqdr rrvadagvty kwlrggeidd aaldffydcy dntyrehwna
      241 pyltreffgr ihadapdsml lviaeadger lacalnmigg dtmygrywgt refvsglhfe
      301 tcymqgiayc iehrlarfeg gaqgvhkmsr gllptptwsa hwiadqrfah aiaefldaet
      361 qamdqhieel eahtpfrkkt
//
LOCUS       WP_175980412             257 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Caballeronia
            zhejiangensis].
ACCESSION   WP_175980412
VERSION     WP_175980412.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia zhejiangensis
  ORGANISM  Caballeronia zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Caballeronia zhejiangensis"
                     /db_xref="taxon:871203"
     Protein         1..257
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=28776
     Region          8..87
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(41,52,55,59..60)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          104..257
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mtkasrsefg nflrsrrekl spesvglnnv rrrrtpglrr eevaelagig vdwyvrleqg
       61 rtvspsdttl ealaralqlg kveaahlral arsgdrqpft resvprpisn liatlelpay
      121 vtgkrwdlla wnaaaanllg fdrlaeadcn ilvfmfaepd srrlfgatwa nearrmialf
      181 rathdlyadd pafvelverl rahstefakw wnahdvrgga sgqkvlthpe rgaqrydyat
      241 fqanddpalk lsiytpa
//
LOCUS       WP_175980419             494 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Caballeronia
            zhejiangensis].
ACCESSION   WP_175980419
VERSION     WP_175980419.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia zhejiangensis
  ORGANISM  Caballeronia zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Caballeronia zhejiangensis"
                     /db_xref="taxon:871203"
     Protein         1..494
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=55758
     Region          335..413
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mfsfvkqlih pvsgsdlagl tpeetafarq fdnvrlvhpv egeaalpset iafigrnlet
       61 grgetnvcga wparrkaqpf kivsfytvdt qyeehamrlk etlerhtlsy hlepvetmgs
      121 wadncaykar filkmwqayd cpivwldada tvesypvlfs aidadfgmhk wnwdpaapgw
      181 efcsgtlyfg kseraerllk qwilrceadp stwdqvhlas awcdvsaeqp lrtvwlprey
      241 lqicdgevva ppvikhwqas rverkkpeah gtevvrftea gmrdratnrl wrtpeeafwv
      301 regkahikpe tgfsypegfd vgralhdavg gavpvleigc gvgriaslfd aneyvgvdvn
      361 pnalkqaret lpghrlkihd agiaypdapc vlfytvllhv adhvvdglla eaaegrerfi
      421 iaelmdrrwr regdppvfnr dpeeyilkma algfalsgfs kfeyeryave pwnvgrdsrl
      481 tvlvfhrngs patp
//
LOCUS       WP_175980428             269 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Caballeronia zhejiangensis].
ACCESSION   WP_175980428
VERSION     WP_175980428.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia zhejiangensis
  ORGANISM  Caballeronia zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Caballeronia zhejiangensis"
                     /db_xref="taxon:871203"
     Protein         1..269
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29768
     Region          33..215
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(36,38,121)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(67,120..121)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            119..121
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mnptsqstpl pkdwqvpgfd vrlwqgrshr yavvipvine garignller marlhistqg
       61 diilvdggst dgslsadlla rtnvrgllak tgpgklsaql rcayafalne gyegivtidg
      121 ndkddpdaip dfirkldegy dfvqasrfla ggvaentpks rdfairfiha pllslasgfh
      181 wtdttqgfra ysrkmmlske iapfrdvfkt yellaylsyr vpkvgfrcie iptsrrypvg
      241 evptkissvr gnwavmeill racagrynp
//
LOCUS       WP_175980433             263 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Caballeronia].
ACCESSION   WP_175980433
VERSION     WP_175980433.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 263)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 263)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..263
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30200
     Region          19..263
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mgridfrrne lwetaksphl wgllawydik qryrrsvlgp fwmtlstgil iatlgavwsl
       61 ifnmkiheyl pfyaigqvfw syystqines cvgftqfegv mkqtrlpvps yilrlvvrnl
      121 iilahnflvi vivisfvgpg wswtalvaip gvllatiaiy faslcvaipc trfrdlqpvv
      181 qnltmigfyv tpilwqpktl gerfawlvel npathlisvv rdpllgvlpt lqswmwvlgt
      241 ivffavmasl mlsryrhria ywl
//
LOCUS       WP_175980530             401 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: amino acid aminotransferase [Caballeronia].
ACCESSION   WP_175980530
VERSION     WP_175980530.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Alexander,F.W., Sandmeier,E., Mehta,P.K. and Christen,P.
  TITLE     Evolutionary relationships among pyridoxal-5'-phosphate-dependent
            enzymes. Regio-specific alpha, beta and gamma families
  JOURNAL   Eur J Biochem 219 (3), 953-960 (1994)
   PUBMED   8112347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..401
                     /product="amino acid aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43625
     Region          1..396
                     /region_name="PRK09257"
                     /note="aromatic amino acid transaminase"
                     /db_xref="CDD:181731"
     Site            order(102..104,130,183,214,243,245..246,254)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(105,140,207,252..254,290,293)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            246
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mfehidaypg dpilslnedf akdpradkvn lsigiyydde grlpvmravr eaeaqllaep
       61 aakpylpmag faayrdavqs lvfgddsaar iegriatvqt lggsgalkvg adfikryfpa
      121 shvwvsdptw dnhrfifera gftvgtypyy deasgglkfd amlsairdlp aksvvllhac
      181 chnptgvdln daqwamlida ikardllpfi dmayqgfgag ldadafaire lvrrnvpali
      241 ansfsknfsl ygercgalsv icesaeiaar vlgqltsavr anysnppthg arivarvltt
      301 palrqswqee lasmctriar mrsaiharls gnvpdamlar yveqrgmfty tglsaaqvdv
      361 lrerhgvyli rsgrmcvaal nernvdatas aigevlskai a
//
LOCUS       WP_175980534             394 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: benzoate/H(+) symporter BenE family transporter
            [Caballeronia].
ACCESSION   WP_175980534
VERSION     WP_175980534.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..394
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=40749
     Region          12..393
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 msipvsregs gsvsavsagl laviisyagp lailfqaaha ahvgndvias wvwsismgaa
       61 vsgialsvwl kqpiitawsa pgsallvtlf pgmpvseaig ayivagacif vlglsgwfde
      121 ivkripkgia cammagilfq fgtnvfksia vtpwlalgmi asflvfrrwa pryclilvla
      181 sgcalamalg lthfesvslh ltrpvftmpt wswqstvsla lplvivsltg qflpgfsilr
      241 vsgyqtptrp vlmttglasm lvafsggiti viaaitaalc tgpdahrdpa nryvagiang
      301 vfyliggcfa gtvvmlfaal pnafvavlag lallgaiaan vvglvqdeah reasfiafia
      361 tasnmsflgl gsafwgivlg tvahlvlgra rdrg
//
LOCUS       WP_175980558             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1630].
ACCESSION   WP_175980558
VERSION     WP_175980558.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1630
  ORGANISM  Burkholderia sp. BCC1630
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia sp. BCC1630"
                     /db_xref="taxon:2676304"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33600
     Region          9..>185
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
     Region          95..294
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(110..111,113..114,117,121,123..129,221..226,
                     232..233,235,237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrkllepsly yfsvvaqags ltsateklgl tvsalsrhma klegdigvpl ferhargmvl
       61 syagrlllrh aqrtlsdaqa vydeiqgder rrsrtitiac tegfafdflp vslaafcrdy
      121 pdvaiqlevv pserasqmll sgeasialtf sfkpepgvvv qftqrapvma lmheehalag
      181 kttvalkelt typvllqdkg ttnrqlfdia cnvesieiqp mmtsryvaal yrfalvvpda
      241 impsgyvsva krmsidglta vpfenplltq rrlqvltlag aqldelanec lrwiiedlkr
      301 tscgk
//
LOCUS       WP_175980602             308 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Caballeronia].
ACCESSION   WP_175980602
VERSION     WP_175980602.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..308
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=31958
     Region          29..307
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mkdivrsrli waavllaiva atlpwwltgy ilgvltvayy fgvfamswdl lfgfagevnf
       61 gptfliglga ysaailnaha aapipvcvma gglvalvggl llavpalrlr gpyfglvtlv
      121 avlllqnaiv ifagvtggei gmmvpdvmsv dashnywial aflivcaiil fglsrsaigl
      181 ilqasgqdtv gaqalgfnvv khklaafcis avfsgvagam lvfyqgtasv stvvdigigv
      241 qiiiaavlgg rrtilgavlg siflivagef lrplgqintf vvaavalavi lffpdgllgn
      301 ilrvrere
//
LOCUS       WP_175980608             326 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Caballeronia].
ACCESSION   WP_175980608
VERSION     WP_175980608.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..326
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33618
     Region          28..325
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 middtqraap ivqasakkkr gvaiqrevav llamivfnli ftqhfvslqt fnvnltqvvt
       61 ivivgigmtl vvatggidls vgasmaiaga lapmlfmnvd gplgivlaft lpivaaalcg
      121 vfngflvtrl nvqpivatlv lfiagrgiaq vvtdgslqaf tnpafqwial gkiagvpfqi
      181 llmlvlvalf twivrktlfg kfllvtggne daaylsgipt arvkmiaytv caalaglagl
      241 isisvnsssd anvvglgvel daiaavavgg taltggkayi tgtligalii qllrytllah
      301 gipdaaalvl kaaiiivavy vqrkrg
//
LOCUS       WP_175980613             278 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia].
ACCESSION   WP_175980613
VERSION     WP_175980613.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 278)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..278
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29859
     Region          13..254
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mfnfpayvtv wgrlgrlfhv gvslgvllfl vspvlvvmpl sfnsqpyfty plpgvslrwy
       61 hdflnspewm lalkntmivg vvstfiatvl gvtaslglmn pklkykalit gilvspmivp
      121 liitavgvyf afsplgltns ltglilahaa lgvpfvvvtv tatlagfnea lsragrslga
      181 spvrvfmqvk lpiiapgvis galfafatsf deivvalflt gtdqrtvprq mwagireqls
      241 ptilavatvl vvistlllvt lellrrrter lrgsanaf
//
LOCUS       WP_175980627             557 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Burkholderia sp. BCC1630].
ACCESSION   WP_175980627
VERSION     WP_175980627.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1630
  ORGANISM  Burkholderia sp. BCC1630
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Burkholderia sp. BCC1630"
                     /db_xref="taxon:2676304"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60777
     Region          25..384
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          453..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mntptlteqf gpresmeydv vivgggpagl saairlkqla rekggdvsvc vlekgsevga
       61 htlsgavmdp raleellpdw retgapldve vtedrflfls qtgakqvpnw llpdnfknhg
      121 nyvvslgnva rwlaqraeel gveifagfpa aevlygerge vtgvatgnmg vgkngeltgn
      181 fqlgmelhak ytlfaegarg hlgrqlmdry rlrdgadpqv yglgikelwe idpamhqagl
      241 vihtagwplg tdtyggsfly hlddnqvvvg fvvglgysnp ylspfeefqr ykthpeirkf
      301 leggkrisyg araitagglm slpkltfpgg aligceagfl nasrikgsha aiasgkmaae
      361 aayealqsgr qgdelveypq aferswlree lyrarnfkqw mskglyvgtl mvgveqkllg
      421 grvpwtlhhr hadhetlkpa aecqeivypk pdgkltfdrl ssvflsntnh eenqpahltl
      481 kdstvpvrvn lekyagpetr fcpagvyefs ssadgtghlv inaqncvhck tcdikdptqn
      541 ivwvtpeggg gpnypnm
//
LOCUS       WP_175980678             269 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Caballeronia
            zhejiangensis].
ACCESSION   WP_175980678
VERSION     WP_175980678.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia zhejiangensis
  ORGANISM  Caballeronia zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Caballeronia zhejiangensis"
                     /db_xref="taxon:871203"
     Protein         1..269
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=29475
     Region          15..261
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mqhsilggdv aepsilierd gdiatvvidr peklnamtkh lwrslgetie mlsgddtlrc
       61 ivlrgageka fspgndiaef rtdrsnveqa rtygaimhrt lhalrecrhp ivamihgicv
      121 gggleiaams dlricgessr fgvpiknlgl vmahaemegl vrlagpaval eillegrifd
      181 akealakglv trvvadgevt ahayetarri adgaplvarw hkqfvrrvme pqpltdeerd
      241 egfacfgted fhigyqafld kikpqfkgr
//
LOCUS       WP_175980721             123 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GFA family protein [Caballeronia].
ACCESSION   WP_175980721
VERSION     WP_175980721.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..123
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13435
     Region          4..109
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mnpttlkgac hcgaitfeve tspepaarcn csfcrrrgav msppfvkekl rilsgedelt
       61 lyqfntqvak hyfckrcgiy tfhrtrsnpa ewrvnlgcvd gvdaysldap vkdgasssvv
      121 gra
//
LOCUS       WP_175980693             647 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sigma-54-dependent Fis family transcriptional
            regulator [Caballeronia].
ACCESSION   WP_175980693
VERSION     WP_175980693.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..647
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=70510
     Region          10..639
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mqddiheiaa thderqsawl ipairkaher setfglnast rpdydvlteg elllkleqnr
       61 vlcahatpvm etlreqivnt qsmivltdaq glilhstgdd dflaraekva lraganwaee
      121 rqgtnaigta iaersptvvh gdqhylaanr fltcssvpil dpygdligvl dvtgdhrsyh
      181 rhtmalarms vqmienhlfs stfqgmlqia fhsrpeflgt lmegimaftc dgrflsanrs
      241 aqfqfglpls alrahtlssl fgltsaqlid rsqasraphm sldlnngavv carvrlnrap
      301 fvepastsvp mrsaprasaa idsssklasl dtgdpkvaav igkvrkvigk dipilitget
      361 gtgkellaqa ihsdsprrag pfvavncasi penlieself gyeegaftga rrkgaagkll
      421 qanggtlfld eigdmpyplq vrllrvlqer vvdplgssks ipvdvaiica thrnlremie
      481 qsrfredlyy rlnglvvklp plrertdlaa vitkmlhavs addgsgirls idddvmalfe
      541 ryawpgnfrq lcnllrtaaa mvdddscirr qhlpedffde pranvhrvse acapsalasg
      601 rlqevtasvi aaalaqhrgn vsaaaralgi srntiyrkmp acssmeq
//
LOCUS       WP_175980733             327 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: transketolase family protein [Caballeronia].
ACCESSION   WP_175980733
VERSION     WP_175980733.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..327
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35000
     Region          21..326
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mstrlktsam iasiasegqv trsapfghal veeartktni igmtadlgky tdlhifakaf
       61 peryyqmgma eqllmgaaag fahegaqpfv ttyavfatrr aydfihqtia ednldvkiva
      121 alpglttgyg pshqaaedla lmrampnmtv idpcdaldie qmvpaiaahk gpvyarllrg
      181 nvpavldeyd yrfelgkakl lrdgrdvlii ssgiltmral etakalqadn vdvavlhvpt
      241 ikpldtetiv regkrsgrlv vvaenhtvig glgeavatal ltagvapayr qialpdafld
      301 agalptlhdr ygistnvmsi tikgwla
//
LOCUS       WP_175980736             303 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: dihydrodipicolinate synthase family protein
            [Burkholderia].
ACCESSION   WP_175980736
VERSION     WP_175980736.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..303
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=32357
     Region          2..292
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mnfngiytpa itpltaegdi dhaafaevle yligagvhgi iiggstgeyy ahtmqeriel
       61 gayakqvigt rvplvigtga irtedsveya ksakkikada ilvgsppyal ptdqenaaha
      121 lavdraaglp vmlynyparm gvsmgreffr tvtaasknfv aikessgsta qlhmlarefr
      181 nisvscgwdd qaleffawga sswvcagsnf lpaehvalhq acvvendfrk grrimsammp
      241 lmdfledagk fvqsikygse laglrsggvr aplqplddan katlkqiiad vkreiagvtg
      301 gqg
//
LOCUS       WP_175980738             443 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1630].
ACCESSION   WP_175980738
VERSION     WP_175980738.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1630
  ORGANISM  Burkholderia sp. BCC1630
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Burkholderia sp. BCC1630"
                     /db_xref="taxon:2676304"
     Protein         1..443
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47311
     Region          21..424
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(31..32,35..36,39,71,121..122,124..126,129,149,
                     152..153,156,259,262..263,266..268,271,298,302,353..354,
                     358,362,378,381..382,385..386,389)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 makttvsied vplngfhqll tvrsgggwlm dgyvlsiigv amvqfsatln lssfwegmia
       61 asallgifvg gflggwltdr mgrrrpyffg pvlfivcsia qlwvqsgeal fvlrfitgig
      121 vgieypvags lltefmprky rgprlamlti iwffgaalay ivgnillaqg gpdawrwvla
      181 spavigvalf lvrlgtpesp rwllnkgrka eadavirevy gpsfsirnlp eepvdrkisl
      241 gallhsgygk rmlfvvlfwt csvipvfavy sfaprvlqal hlegdweafg svaitllfvv
      301 gcalatrvin tlgrralvih sflwsalall algacsngsa mlilvlfgay alliggaqvl
      361 qlvypneifp tdirafavgm gaslsrigaa igtwlvpial qnigigntmy aaaavsfvgl
      421 lasvalapet aslslqeaas lsh
//
LOCUS       WP_175980742             238 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175980742
VERSION     WP_175980742.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..238
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26567
     Region          12..220
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mppadrksal gdalrrrivn melapgalid eaaladefgm srppirelir qmaaegyiel
       61 epnraprvts mnfqslrsff iaapviyiat tqlaalnatp ddiarlrtiq anfraaiesg
      121 nvanrviynd efhleigria qndylmpslr rllidharlg kmfyrypatd tmqhtlesav
      181 vqhdqiidal erqdadaagq lirdhfelsr rrmteyaapq gmavsvnlgd pvlalvkr
//
LOCUS       WP_175980748             350 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Caballeronia].
ACCESSION   WP_175980748
VERSION     WP_175980748.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..350
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38497
     Region          <144..320
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          238..320
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpadsdppki sthfstracp rerqllawrd rvghvvdvvp dkdqiargfs gsidlhaagg
       61 lvfteartda lvlersiarv stdtrrdfaf hvyvegetgh vsglsvkrsa pgsvrgiial
      121 dlnqrfrver pacrvltmfv praivgahig dcdalhgrvl pdhaplvhfv fehfeatare
      181 lpvldrpdaa daldagarll leafadkpna asdsraalqt avksqvkryi etrlheadlt
      241 ptaivealgl kratvyrwfe qegglaayir lrrlreaade lalfpnlqia diafglgfks
      301 asdftrafrr afdvsplemr lralellrat sgdpvmrmra ahsrdlpesg
//
LOCUS       WP_175980757             337 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Caballeronia].
ACCESSION   WP_175980757
VERSION     WP_175980757.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..337
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37193
     Region          27..80
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          110..307
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(120,124,163,177,179,242,259,286)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(121..122,126..127,129..130,133,137,139..145,206,
                     236..240,247..248,251)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mpsdlvchsd dslaysfvas yagvvsflav anegsfakas drlgigrsav srnvqkleaq
       61 ldarlflrtt rstsltrege lfykncqpgv erivqaledm relrngaprg hlriasapgf
      121 grkvvaplla gfnarypdia lelllndrpc dftadrvdva frdghmedse vvakqlipmq
      181 mivcaspaya rehglprhvd dlddhrcinf rapagriaew efkvdglark rspaarqtfn
      241 didlmlqavl dgqgiaqlpa ylvcdslkag rlvtclaqya pddgghylcy lsrkhlparv
      301 rvfvdymteq traldlhclt tfitnpragv qqlvstd
//
LOCUS       WP_175980802             301 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC1630].
ACCESSION   WP_175980802
VERSION     WP_175980802.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1630
  ORGANISM  Burkholderia sp. BCC1630
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia sp. BCC1630"
                     /db_xref="taxon:2676304"
     Protein         1..301
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33485
     Region          1..301
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 miafthalea lrvanyvdrt ehyrwtvfsi dgepveassg iamrptqald vsgplpdvmi
       61 vcggtriret vdartllalr alagrritmg alcsgayalm aaglldryrc avhwadlhal
      121 raefpdveit nelfvidrdr itctggiapm dmmltlmskq igphlvvdvs khlvvnrlrg
      181 vnepqsipvr arltstrdel veavklmean veeplsfpei arlvglserq lqrvfkqfln
      241 asprdyyrsv rlghardllr rgsdfvgdvs vrcgfpsacs fskayrrefg hapiierrgp
      301 r
//
LOCUS       WP_175980825             419 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Caballeronia].
ACCESSION   WP_175980825
VERSION     WP_175980825.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..419
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43225
     Region          17..406
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(27..28,31..32,35,70,117..118,120..122,125,150,
                     153..154,157,236,239..240,243..245,248,278,282,332..333,
                     337,341,357,360..361,364..365,368)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 msslsttrsa tdrattwvli gaaalilsaa mgvrqtfglf igpfsfdrgm pvtliafaia
       61 lhnlvwgfaq pfagaaadry gaapvvatga atfaaglala aaassgwmlv lglgllvgig
      121 isctsfgvvl atvgrvaspq trsvamglas aggslgqvlm vpfaqevrvh agvpaslyal
      181 afvlllaapl gialdrasrr skassashet haqaaamplr etlayasrhr gyrlltlgff
      241 tcgfqlafia thlpgylmlc hmpvglgata laliglfnmi gswgcgwlgg rwrqhhvlaw
      301 lylirggaia lfvllpttsv svvvfaavmg ltwlgtvplt ngliakvfgt rhlgtlfgvv
      361 flshqlgsfl gawlggyvfd ttgsysliwa ataiaglvaa llhfpiddrp vaeaslaas
//
LOCUS       WP_175980860             130 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: VOC family protein [Caballeronia].
ACCESSION   WP_175980860
VERSION     WP_175980860.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..130
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14402
     Region          8..115
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 msatkayleh vaiwvkdihw hirffeevlg mtmrevdgpr deprqywtlg glqfisdpty
       61 dgpegrlahl gvmcedleaa laaaqpfgvt emtqgrnwlr lpdglaveli qarpatcvaq
      121 alsinpraea
//
LOCUS       WP_175980862             316 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ketopantoate reductase family protein [Caballeronia].
ACCESSION   WP_175980862
VERSION     WP_175980862.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..316
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33085
     Region          1..305
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkiaflgaga lgcaigaalt egghetwlvd kfaahveams rdglqvdder gtrrvkvrat
       61 mnpadvgpvd vvivlvksfh tdsamrgald ligpetlvls lqnglghedv lsdivgrerv
      121 lagktyvggv lrapghiqsg vtgkitiige ldgrvtpraq avaeafnsag ltttvsdnil
      181 gtmwdkllin vatgaitgit rltygqlyse pvlkatslaa ieeamaaaka agielsitra
      241 edawnmaaeg lpaafktsml qslekssvte idfingavvr wgerlgvptp vnstlvacik
      301 giergmtdrq neeraa
//
LOCUS       WP_175980863             356 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SDR family oxidoreductase [Caballeronia].
ACCESSION   WP_175980863
VERSION     WP_175980863.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Thorn,A., Egerer-Sieber,C., Jager,C.M., Herl,V., Muller-Uri,F.,
            Kreis,W. and Muller,Y.A.
  TITLE     The crystal structure of progesterone 5beta-reductase from
            Digitalis lanata defines a novel class of short chain
            dehydrogenases/reductases
  JOURNAL   J Biol Chem 283 (25), 17260-17269 (2008)
   PUBMED   18032383
REFERENCE   6  (residues 1 to 356)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..356
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=39311
     Region          5..312
                     /region_name="5beta-POR_like_SDR_a"
                     /note="progesterone 5-beta-reductase-like proteins
                     (5beta-POR), atypical (a) SDRs; cd08948"
                     /db_xref="CDD:187652"
     Site            order(9..14,34..36,49..51,72..74,110..111,146,169..170,
                     172,179..181,309)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187652"
     Site            order(114,146)
                     /site_type="active"
                     /db_xref="CDD:187652"
ORIGIN      
        1 mdkraliiga tgivggnlad hllasgdwhi tglsrgrsal rdgvesitad ltsaesvqra
       61 lsgkqfthvf ftawsrqate qenirvngam vrhvlealgp sgtlkhaalv tglkhylgpf
      121 eayakgsvpl tpfreeqgrq dvdnfyyeqe drlfdaarqf gfgwsvhrph tvigfavgna
      181 mnmgvtlavy atlckasgap fifpgsaaqw ngltdmtdar llarhlewaa tspnardeaf
      241 nvvngdvfrw kwmwslvany fgiepvefdg tmrpledrmq dageawreia arhhlaeadi
      301 gklaswwhad adlgrpmevl tdmsksrkag fldyqstpds fialfdrlkt lriips
//
LOCUS       WP_175980871             185 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: (2Fe-2S)-binding protein [Caballeronia].
ACCESSION   WP_175980871
VERSION     WP_175980871.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..185
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=19205
     Region          23..170
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mnttptatal dvgaphaqrv actlsinggt qtfdiepwtt lldllrercq ltgtkkgcdh
       61 gqcgactalv dgqrintcla lavsydgaei ttieglasgd tlhpmqqafi dcdafqcgyc
      121 tpgqicsavg mlaeghahda tevreamsgn icrcgaypni vqailqvssa ngvdetaven
      181 geths
//
LOCUS       WP_175980876             290 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Caballeronia].
ACCESSION   WP_175980876
VERSION     WP_175980876.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 290)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..290
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31169
     Region          7..284
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 matlddarpg aapwllsgpa lllftglllv pliltlvlsf rvfsdtagit saftlsnywe
       61 vvsdpyygti flrtaglatg vtllsivlgv petiilarmk kpwqslclli vlgpllisvv
      121 vrtlgwqill gnngvlnnvl qalhitdepi rlvftmtgmi ialthvlvpf mvmsvwanmq
      181 kldpqvewag rslggsplkv frrvvlpqim pgvlsgsiiv falsasafat paliggrrlk
      241 vvataaydef lgtlnwplga siavlllian vaivmgcsrl aerrfkhifd
//
LOCUS       WP_175980878             265 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Caballeronia].
ACCESSION   WP_175980878
VERSION     WP_175980878.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..265
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28367
     Region          6..255
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mkqngplalv fnalfltfil aplvvvmlvs ftdkgfismp fdgaslrwfh aiiengdivs
       61 afwlsiklaf aaatigvlla vpaalaiary rfpgraaltg fflspmmipa vvlgiaflrf
      121 lsmlnlsgsf wslvcahvvi vlpyalrlal ssavgldrda eraalscgas rftafrrvvl
      181 pmirtgvagg wvlsfiqsfd eltmtifvat pgtttlpvam ynqiaqtidp lvasvsavli
      241 vgtvllmill drmvgldril igear
//
LOCUS       WP_175980887             208 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC1630].
ACCESSION   WP_175980887
VERSION     WP_175980887.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1630
  ORGANISM  Burkholderia sp. BCC1630
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia sp. BCC1630"
                     /db_xref="taxon:2676304"
     Protein         1..208
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21768
     Region          1..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mphvawlpfm atslliiltp gqdmvlvmsr tlsggtragl vtaagvsvgl lvhtmlatlg
       61 lgallqasew lftalkmiga lyllylgitl lrssgeltla sgrdapasgl rtfaqgalsn
      121 vsnpkialfy laflpqfvpa gaahpmvslf vlgatfaglt flvkgpvalf agllstsirr
      181 npriltrmhr vsgvvllglg vklaferr
//
LOCUS       WP_175980902             259 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia sp. BCC1630].
ACCESSION   WP_175980902
VERSION     WP_175980902.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1630
  ORGANISM  Burkholderia sp. BCC1630
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Burkholderia sp. BCC1630"
                     /db_xref="taxon:2676304"
     Protein         1..259
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27496
     Region          8..206
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
     Region          <231..>256
                     /region_name="PHA03145"
                     /note="helicase-primase primase subunit; Provisional"
                     /db_xref="CDD:165416"
ORIGIN      
        1 mpdasaeass gvavldrafa ilhafgqtdd rlslaelsrr tglykstilr llaalehggf
       61 vrklddgqya vgheplrlaa lyqrsfrvgp vveplletls relgetasfy vrhgdmrsvl
      121 yrveptrtvr vsirvgeefp vqqgasgkvl laftephdar wndvreqlwa asygerdpet
      181 asasvpvfga agdcvgaltv sgptsrlaaa pamaaalaml lplaqkatva lggagaryda
      241 qavrdslarf aipdspaqp
//
LOCUS       WP_175980953             169 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: aromatic-ring-hydroxylating dioxygenase subunit beta
            [Caballeronia].
ACCESSION   WP_175980953
VERSION     WP_175980953.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10791045
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..169
                     /product="aromatic-ring-hydroxylating dioxygenase subunit
                     beta"
                     /EC_number="1.14.-.-"
                     /GO_process="GO:0008152 - metabolic process [Evidence
                     IEA]"
                     /GO_process="GO:0009056 - catabolic process [Evidence
                     IEA]"
                     /calculated_mol_wt=18944
     Region          15..169
                     /region_name="HcaF"
                     /note="3-phenylpropionate/cinnamic acid dioxygenase, small
                     subunit [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG5517"
                     /db_xref="CDD:444268"
ORIGIN      
        1 mlpgfekqni ahdkalvara avedfhaeyc aaldggdier wpefftencl yrvteyenaa
       61 ngfpvglvya egrdmlrdra vaiartqmfa prqmlhfvsn vrilnatdee ivaqsnymll
      121 qtlvegattl hqagrlfdrf arngnvlllk erqavydtam iandlaypv
//
LOCUS       WP_175980992             178 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: 2,4'-dihydroxyacetophenone dioxygenase family protein
            [Caballeronia].
ACCESSION   WP_175980992
VERSION     WP_175980992.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14449000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..178
                     /product="2,4'-dihydroxyacetophenone dioxygenase family
                     protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20200
     Region          42..161
                     /region_name="cupin_DAD"
                     /note="2,4'-Dihydroxyacetophenone dioxygenase (DAD), cupin
                     domain; cd20302"
                     /db_xref="CDD:380436"
     Site            order(54..55,58,64,66,83,85,87,89,102,105..109,111..113,
                     130,136,138,146,149,152)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:380436"
     Site            order(78,80,95,116,131)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380436"
ORIGIN      
        1 mqtevkpdeq viayqlpqvp ymskdlvhgg vmtdwleddn lwvpatetvs fkplilnasq
       61 gyyvnllrvr rsgvisrhrh sgavhamvlk grwyylehdw vaeqggyafe pagethtlfv
      121 pedvpemitw fhvtggytyv dpqgvaqgye dvftkieaar rhytsiglpa dyiesiir
//
LOCUS       WP_175981010             475 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1630].
ACCESSION   WP_175981010
VERSION     WP_175981010.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1630
  ORGANISM  Burkholderia sp. BCC1630
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Burkholderia sp. BCC1630"
                     /db_xref="taxon:2676304"
     Protein         1..475
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48086
     Region          23..450
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,277,280..281,284..286,289,317,321,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msefaspaga repagnwram savllavala tldtaianta lpaiatdlha spaasvwiin
       61 ayqlamvatl lpfaslgdiv ghkrvyvagl avftlaslgc slaatlpqlt aarivqgfga
      121 saimsvnval irnlfpahrl grgvgfnalv vgvsfavgpt iaslilsvaa wpwlfavnvp
      181 lgvlalavai pslpqtargk hafdplaalf nvitfaslif algefaqrgp lsvvfaaatv
      241 alafgallir rqaghpapml pvdlfrrpvf tlsaltavca faaqglafvs lpfyfetvlh
      301 rdavetgflm tpwsaivala apiagrlsdr yppgllgaig lallsagmvs laalpaapnv
      361 vdigwrmmlc gagfgffqsp nlkalmssap persggasgi iatarligqa tgaalvalsf
      421 giagrhgptl almlgagfag aasvasglrl fapshragap vasvaatpak epate
//
LOCUS       WP_175981019             295 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: dihydrodipicolinate synthase family protein
            [Caballeronia].
ACCESSION   WP_175981019
VERSION     WP_175981019.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..295
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=32040
     Region          3..290
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 msfegvhtpl vtpfkadgei dhdmlgkhaq slvgrvtgmg vggttgeyya lsfeervktl
       61 etvasavggk tyltaginat ttkevvrlgn eakragydal lvaapyyvqp tqdelldhll
      121 kvddaldmpi mlynfpartg taigdevldk llqrpnfaam kestgdiahl hhlatqlper
      181 fvlscgmddq aleffawgar swvagasnfl peahtdllea cvkrgdfgtg rklmtqllpv
      241 lellersgkf iqyvrygcel agtkvgiara plgtlndker safarlvqpl lrnaq
//
LOCUS       WP_175981022             220 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LemA family protein [Burkholderia].
ACCESSION   WP_175981022
VERSION     WP_175981022.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..220
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=23809
     Region          32..209
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mstnpaaisa rrslaralli aasaasllsl sgcgynaiqs edeqvkasws evlnqyqrra
       61 dlvpnlvntv kgyanqekev lvrvtearaq vgsiratpel iadpqafakf eaaqgqltss
      121 lsrllvvsen ypqlksdanf rdlqaqlegt enriavarnr yirsvqtynt tirsfpnnlt
      181 akafgylerp nfsvsneaei skpprvdfgs tpasagkasn
//
LOCUS       WP_175981043             228 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Caballeronia].
ACCESSION   WP_175981043
VERSION     WP_175981043.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..228
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25849
     Region          10..226
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mrgleriafd apkslaeite erlrqlivng elefgeqvte srlsdlfgls ktpvreallr
       61 lsiaglveik arsgtyvfsl tdknicdist lritleqaai rsamrenaar lmeelnrnld
      121 aaralhatfe latyraldhe fhqilvrhsd npylidcyst istkvlamrn rltfsreyin
      181 ksidehravt ralvendvdg aciilaehin cgftertrrl ltdiarmq
//
LOCUS       WP_175981047             423 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Caballeronia].
ACCESSION   WP_175981047
VERSION     WP_175981047.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..423
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45940
     Region          2..403
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(15..16,19..20,23,55,105..106,108..110,113,133,
                     136..137,140,237,240..241,244..246,249,278,282,332..333,
                     337,341,357,360..361,364..365,368)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mwkivpfafi lyffnyldrv nvgfaalqmn reldisptqf gtiasmffas yllcqipanf
       61 alqrmgarrw isfivivwga vtaltffaqt athvaiarll lgvfeagffp gmifylacwf
      121 parerakvts ffmmaiafss vvagpmsgwi vehvhmagyg gwrwlfaieg vptillggla
      181 ffilvdapad akwlnkdqra wlvaelqrer saqgadeqpt lkmvlgnsti wklalsymli
      241 qaasqasnyw lpgqvkgfaa sltdtqtgli malpyvcami smplwgahsd rtgerkwhaa
      301 lpmllagvgf fviasvpsms lrmagmalfg vgilsfygpy waippamlsp aglalsiafi
      361 nscsslggfl anqalghvsq aygsygvfmv eaalcvaafc vlvtmsiprq tpkvgpsaqt
      421 ana
//
LOCUS       WP_175981056             199 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Caballeronia].
ACCESSION   WP_175981056
VERSION     WP_175981056.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..199
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21062
     Region          20..197
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mhsssqaall llgiviilit pgptntllat aglrrgvrra tplmaaelag yliaisvwgy
       61 lvthaagflt wlptflrvac svyiaylavl mwrtavslpt saqktvgmrt lfvttllnpk
      121 amlfasaifp asafgnavvy lqtmsifaaa lipigflwit fgaalgtgrl awlspdrvqr
      181 gasivlatfs ialawtalh
//
LOCUS       WP_175981073             215 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: carbonic anhydrase [Caballeronia].
ACCESSION   WP_175981073
VERSION     WP_175981073.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Lindskog,S.
  TITLE     Structure and mechanism of carbonic anhydrase
  JOURNAL   Pharmacol Ther 74 (1), 1-20 (1997)
   PUBMED   9336012
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10096752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..215
                     /product="carbonic anhydrase"
                     /EC_number="4.2.1.1"
                     /GO_function="GO:0004089 - carbonate dehydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23694
     Region          11..191
                     /region_name="beta_CA_cladeA"
                     /note="Carbonic anhydrases (CA) are zinc-containing
                     enzymes that catalyze the reversible hydration of carbon
                     dioxide in a two-step mechanism in which the nucleophilic
                     attack of a zinc-bound hydroxide ion on carbon dioxide is
                     followed by the regeneration of an...; cd00883"
                     /db_xref="CDD:238448"
     Site            order(33,35,42,44..46,58,61,83,88,98,101,181)
                     /site_type="active"
                     /note="active site clefts [active]"
                     /db_xref="CDD:238448"
     Site            order(42,44,98,101)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238448"
     Site            order(43..46,48,50..51,53,58..60,62,64,78..79,82..83,121,
                     181,183..184,186,188)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238448"
ORIGIN      
        1 mnrpkrmlle niawaretah adaqffprla qgqspkvlwi gcadsrvpae tvtnanpgdl
       61 fvhrnianlf spsddntlsv leyavrvlkv dhvivcghyg cggvrasllp kssdlphvnr
      121 riaplcalge rhrheldsfg eldaranrla elnvleqvrl lrehaivreh dvpprvhgwi
      181 fglhdglikv lasgyaeesd srdiasaqvt slraa
//
LOCUS       WP_175981078             381 aa            linear   BCT 11-JAN-2025
DEFINITION  glycerate kinase [Burkholderia sp. BCC1630].
ACCESSION   WP_175981078
VERSION     WP_175981078.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1630
  ORGANISM  Burkholderia sp. BCC1630
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Burkholderia sp. BCC1630"
                     /db_xref="taxon:2676304"
     Protein         1..381
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38562
     Region          10..376
                     /region_name="GlxK"
                     /note="Glycerate kinase [Carbohydrate transport and
                     metabolism]; COG1929"
                     /db_xref="CDD:441532"
ORIGIN      
        1 mpqhpsapvv viapdsfkgs lsaeqvadai atgirrarpd avvrccpmad ggegtldaml
       61 asggtrrtvr vagaslaard aavgvidart aivetaeivg itdavgmsvp vdarstrgmg
      121 eairtlldeg vrrffvalgg sstndagagl laglglqcfd aagqpvepvp arladiarid
      181 asgldprlke tefigmsdvd npltgahgat avfgpqkgvt peqvatldaa lgrfadllea
      241 aldrrgrelp gagaagglgf alhmlgaqfe agaevvarqi gldaalagad wlitgegrsd
      301 vqtlhgkapf iacrharaag vpasllsgav dpaalprlse hfsgcfspap gpitldvair
      361 daanllanea eqltrlkyga h
//
LOCUS       WP_175981084             238 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: YdcF family protein [Caballeronia].
ACCESSION   WP_175981084
VERSION     WP_175981084.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..238
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27353
     Region          20..235
                     /region_name="ElyC"
                     /note="Lipid carrier protein ElyC involved in cell wall
                     biogenesis, DUF218 family [Cell wall/membrane/envelope
                     biogenesis]; COG1434"
                     /db_xref="CDD:441043"
ORIGIN      
        1 mvlisllllf ialflvwrkr rgmilvmtai vfwglgswfp gplvrlandh yasmkdptfg
       61 prtaiivlgg gtwydhnrrl vpkgdamtri dlaaslykrc vemekacfvi msggnpqhhe
      121 qseadlygsl lldagvkrqd lilenqsldt yenarnteki lrsrpydtsv litsslhmrr
      181 amlafeafgl hpqptvayvr pqfmwwrphr rgwfdsnsal helvgivrfy vwrwvgly
//
LOCUS       WP_175981088             215 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC1630].
ACCESSION   WP_175981088
VERSION     WP_175981088.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1630
  ORGANISM  Burkholderia sp. BCC1630
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14301956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia sp. BCC1630"
                     /db_xref="taxon:2676304"
     Protein         1..215
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22702
     Region          14..129
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          80..209
                     /region_name="TetR_C_33"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     cl38988"
                     /db_xref="CDD:476841"
ORIGIN      
        1 mkdkpaqgpr gldkdaivaa alalleevge aafsvrklaq svgcdpmsvl yhfkskegls
       61 raianalsrs lvpvdpslpw rerlrdlarq yralalrhpa afallqrhms tgpadlahie
      121 tvhraladag ipraalpsvc vgwyasvigl aaaeaggltr pandvelaem yalsdtahpl
      181 vksaaplyaq ldpaavhdtm ldvlldgiaq harat
//
LOCUS       WP_175981105             293 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Caballeronia].
ACCESSION   WP_175981105
VERSION     WP_175981105.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..293
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32579
     Region          1..292
                     /region_name="PenR_Burk_TF"
                     /note="beta-lactamase transcriptional regulator PenR;
                     NF041130"
                     /db_xref="CDD:469053"
ORIGIN      
        1 mramrphlpl nalrafeasa rhlsftraaq elnvtqaavs qqvraleerl gtplfrrvpr
       61 glsvtdegra llpvlsdafg rieavlkqfe gghfhevltv gvvgtfavgw lmprmkafre
      121 thpfvelrlf thnnlvdpas egldfairfg agvwpathna llldaplaal capdiarrly
      181 tpsdlvnevl lrsyraddws dwfdaaglda wtmngpvfds srlmveaavq gagvalappr
      241 mfvrelqagl lvrpfdvevr tgsywltwlk srrlshgmkl frdwivreaa eav
//
LOCUS       WP_175981122             301 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175981122
VERSION     WP_175981122.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32437
     Region          8..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(104,108,147,161,163,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(105..106,110..111,113..114,117,121,123..129,190,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mliddlpald tfarivsags lsaaareldl slsvvskrla hlesqlgvrl lhrttrqqtl
       61 tddgaqfhaq vlrilaevdr aetlmsdrrg tvsgvlrlta pgelgrlria plvaafqrqh
      121 pelivqlmlt dtivdllaqd idvavrigsl adstmiarel apnhrvlcas ssylavhglp
      181 ahpaelrahr civmgdqprt ewrfdgaqga vavevtaall tndggaartl alegagialk
      241 siwdvgadle agrlvrvlpt faapaaplha vypggrhvpl rvrafvdflr dqlretwrrs
      301 a
//
LOCUS       WP_175981156             387 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Caballeronia].
ACCESSION   WP_175981156
VERSION     WP_175981156.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..387
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42774
     Region          1..385
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 miestsdayq direavrdlc gqftgeyfrk ideargypea fvdaltkagw laalipqeyg
       61 gsglglteas vimeeinrsg gnsgachgqm ynmgtllrhg steqkkrylp kiasgelrlq
      121 smgvtepttg tdttkiktta erkgdryain gqkvwisrvq hsdlmillar ttpiadvkkk
      181 segmsifivd lreaignglt vqpilnmvnh etnelffdnl eipaenlige egmgfkyild
      241 glnaertlia aecigdgywf idkvtqyvnd rivfgrpigq nqgvqfpiar ayvnveaanl
      301 mrfkacerfd ahkpcgaqan makllaadas weaanaclqy hggfgfaaey dverkfretr
      361 lyqvapistn lilsyvaehi lglprsf
//
LOCUS       WP_175981170            1070 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit
            [Caballeronia].
ACCESSION   WP_175981170
VERSION     WP_175981170.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..1070
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114870
     Region          1..1036
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnishfcidr pifasvisii itlggaltml alptaqypdi tppqitisat ypgasadvva
       61 nnvaapieqq vngadnmiym sssssstgnl tinayfqigt npelaqvdvq nrvnlalpql
      121 pqsvtaqgvq vqkksqafmm viaiyspder ydatyianya nvyvldalkr ipganqsaif
      181 gtpdyamriw lkpdrmaqlg itaadvqrav anqnqqfavg rlgqsptgap veqsfavttt
      241 grltepaefe niiiraqsgg aaivrlkdvg raelgqkdys irsrfqgksa tvlavyqqpg
      301 analdvskqv raslaemkkt fpqgidyeia mdtteftras isdvvhtffe avvlvvivvf
      361 vflqslratl ipvlavpvsi vgtfmgmeal gfsinmltlf gmvlaigivv ddaivvienv
      421 ernmtvhkld pktaakkamd evagpvvaiv lvlcavfvpv aflsgitgqm ykqfaitiai
      481 svvisglval tlspalasll lkpghhekkg ffrwfdnqfa rmtrgythlv rlvikrfaia
      541 lllfvgmial avmmmrdipt aflppedqgy llgavimpda asldrtgavs drvteyfmkq
      601 pavgsittvd gfsildsqnk nnsstffvgf ksfedrytsa nirtqnarav lvdaykhlsq
      661 iregivvpln ppsipglgtt ggtemwiqsk gdatiaqfag ivddfvakak arpeltgvts
      721 tfnassqqll anvdrdkaet lgvpvedvys amqtmfgsly vsqfnrssrl wqvilqaepq
      781 yrlkpddltq ifvksksgem vplksvvntk yvtgpdlitr fnnfpavkit anaapgyasg
      841 qviaaledia kdlpsdygig wsgeayeakq sgsssalvfi fglimvflil aaqyekwslp
      901 fgvlmavpfa ifgallaill rglnndvyfq igltmlvala aknailifef avlnreagas
      961 vydaamtaae erlrpivmts lafilgcvpl aiatgasans rhsigtgvig gmlgatviav
     1021 ffipmffwgl etmssrskkk kgaeasapda kqthggsgqn aspsapdkgd
//
LOCUS       WP_175981204             403 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Caballeronia].
ACCESSION   WP_175981204
VERSION     WP_175981204.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..403
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42608
     Region          16..389
                     /region_name="MFS_MJ1317_like"
                     /note="MJ1317 and similar transporters of the Major
                     Facilitator Superfamily; cd17370"
                     /db_xref="CDD:340928"
     Site            order(26..27,30..31,34,67,118..119,121..123,126,146,
                     149..150,153,228,231..232,235..237,240,267,271,320..321,
                     325,329,345,348..349,352..353,356)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340928"
ORIGIN      
        1 mpspfatprp piprtvwalg lvslfmdlss elvhallpiy lvttmgmsvt algalegaae
       61 atamivkvfs galsdwlgrr kglllfgygl aaltkplfpl aetpalvvaa rlvdrfgkgi
      121 rgaprdalva dvappeirga afglrqsmdt igafagplla ivlmlafsdh irtvlwfatv
      181 pafiaviiil fgvrepesas argesfrspl hwrsmrefsg rywyvvaiga tftlarfsea
      241 flvlraqqtg ldiawipavm vvmslaysas aypagvlsdr wdrrallacg lalliaadvl
      301 lgagssmltl fagvalwglh mgftqgilaa mvaesappsl rgtafgvfnl asgvcmvlas
      361 aiagwiwdrh gapatfytga alaliplvmc faprradsas rka
//
LOCUS       WP_175981225             319 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Caballeronia].
ACCESSION   WP_175981225
VERSION     WP_175981225.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..319
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35787
     Region          7..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..294
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(110..111,113..114,117,121,123..129,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mreinqqrlr yfhevlthgt irgaadhlnt spsviarqik lleneldttl fereprgvrp
       61 teaafhllef wrgyrsqqek fedqlhalkg lqqgqirlav segyvdtlvd dvlapfcary
      121 prleidvqml avddlleeva qsrahiglay npppheriei rasspqpvvl larrdhplav
      181 rggvarirdl leyplalmpp tfgighvvkm lettddlair ptlttnslga lkrfvaaenf
      241 mtligefaay relasgeltt ipvahplfes aqakllvkag rplaagpqel ldwiltrmpm
      301 fahagaapvr rtrarerrk
//
LOCUS       WP_175981251             229 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC1630].
ACCESSION   WP_175981251
VERSION     WP_175981251.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1630
  ORGANISM  Burkholderia sp. BCC1630
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 229)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Burkholderia sp. BCC1630"
                     /db_xref="taxon:2676304"
     Protein         1..229
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24922
     Region          1..229
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 mflygfgpvl wagtvqtiel svlslaaava lgligavakl shnrvlraia tgyttlirsv
       61 pdlvlmlllf ysiqiwlnqf tdlvgwdqid idpfiagvlt lgfiygayft etfrgaflsv
      121 prgqleagaa ygmsgmrvfv rimfpqmmrf alpgignnwq vlvkatalvs iigladvvka
      181 aqdagkstfn mfffilvaal iylaittvsn lvliqlekry smgvrhael
//
LOCUS       WP_175981250             432 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Caballeronia].
ACCESSION   WP_175981250
VERSION     WP_175981250.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..432
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45170
     Region          23..426
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(37..38,41..42,45,77,127..128,130..132,135,155,
                     158..159,162,251,254..255,258..260,263,291,295,353..354,
                     357,361,377,380..381,384..385,388)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mesrieahta hdaassthat svrwrifgvv flitlinlvd rislsiampt iakefalspa
       61 mqglvlssff wsyallqipg gwlidklgpr kvvagatvlw glfqtlmgaa tggmsmlllr
      121 vglggaeapl fpagsklnal wlsrkerarg avlmdagspl gaaigglais nlilmfgswr
      181 tafvvaglat iacgwlawry lrddpakhpg vngaelahih dgappaskam hasqddaplp
      241 lrstiamcvg rmswamiffg lltwgpsylt qarglslsqi gaatffifla galgslsggf
      301 lcdalcgmnl srgkvvktmi avsgiatlav faalptitsp vvavavlcga sfllmwgsly
      361 wslpsllasp grvgllgacm ncagsvggis iplitgfilq rtgsfdavlh fygacalvyi
      421 fgsiaidlrr tr
//
LOCUS       WP_175981253             306 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: dihydrodipicolinate synthase family protein
            [Caballeronia].
ACCESSION   WP_175981253
VERSION     WP_175981253.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..306
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33109
     Region          6..298
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 maapvyrgvf pvaptifddq grldlegqkr aidfmidags hgvcilanfs eqfalsdaer
       61 dtvqrtvleh vagrvpvivt tthfssrica ersraaqdag aamvmimppy hgatirvger
      121 gihefyrevs naidipimiq dapvagtpls asflaklard vehvsyfkie taqaasklre
      181 lielggdaiv gpwdgeeait lmpdfdagat gamtgggypd girkivdayf agdtdnaael
      241 yqqwlpliny enrqcglaac ktlmkeggvi rsdavrhpla pmhpavregl lkvarkldpl
      301 vlrwgh
//
LOCUS       WP_175981458             570 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GMC family oxidoreductase [Caballeronia].
ACCESSION   WP_175981458
VERSION     WP_175981458.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..570
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=61009
     Region          1..553
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mfdflilggg sagcvlaarl sedaratvcl veagrdisar tmpdairsry pgrayldtrn
       61 iwqalkarms eraalrryeq arllgggsai nalmanrgsp sdydewealg adgwnwqacl
      121 pyfrkletdc dvtgplhgsd gplriqrtaw prispfvrtv lasladrgha lrddqngpwe
      181 dgtfigaiav sangeripts vcylddaara rdnltirtgd vvecilfdgk raigarivra
      241 dgtrqdlrah rvivsagaih spallmrsgi gpgdelaalg idvvadrpgv grnlmehpsi
      301 avsaflpraa rtpfpdehhe qaivrfssgl adtvqgdmhg ailsrsgwhs vgyrlgtiff
      361 wvnksysrgr vtlasanafd epnvdfamls dsrdlerlkl alrfgaatla sasmdaifps
      421 sysprvaava vpgtwnalqr galsalldia gplrgalikg vvtqgitide lladdrkmte
      481 fvmrhvggtw hpsgtcrmgs ssdplavtda rgavhgiegl hvcdaslmps ipcantnvpt
      541 imiaervada lrgtvldkhe paahavtqap
//
LOCUS       WP_175981460             114 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cupin domain-containing protein [Caballeronia].
ACCESSION   WP_175981460
VERSION     WP_175981460.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..114
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12421
     Region          <41..114
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 mkvqqlkqsi aiegledwgt aglpgtheik isgvqkvipg seaidtgvfe ctpgtyrrsv
       61 keaevmhfla grgrftpdge dtihftggdt lffaantegt wevdetmrkv yvif
//
LOCUS       WP_175981531             401 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1630].
ACCESSION   WP_175981531
VERSION     WP_175981531.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1630
  ORGANISM  Burkholderia sp. BCC1630
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024320
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Burkholderia sp. BCC1630"
                     /db_xref="taxon:2676304"
     Protein         1..401
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42338
     Region          17..385
                     /region_name="MFS_MJ1317_like"
                     /note="MJ1317 and similar transporters of the Major
                     Facilitator Superfamily; cd17370"
                     /db_xref="CDD:340928"
     Site            order(27..28,31..32,35,68,119..120,122..124,127,147,
                     150..151,154,228,231..232,235..237,240,267,271,320..321,
                     325,329,345,348..349,352..353,356)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340928"
ORIGIN      
        1 msapsptarr paiprtvwal glvslfmdls selihallpi ylvstmgmsv aalgvlegaa
       61 eatamivkvf sgaisdwlgr rkglllvgyg laaltkplfp lastpavvva arlldrvgkg
      121 irgaardalv adiappeirg acfglrqsmd tvgaifgpml aivlmlwfgd rirtvlwfav
      181 vpafvaiali vfgvrepeqs kpdrrfrspl rwnalrefpr sywfvvaaga tftlgrfsea
      241 flvlraqqtg ldaawipavm vamsvtysls awpagivsdr ldrrvllaag mvllivadll
      301 lgigtstlsm fagvavwglh mgftqgilaa svsetspatl rgtafgvfnl vsgicmllas
      361 siagalwthf gasttflaga alvvvplclc rfmprpgash a
//
LOCUS       WP_175981559             405 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Caballeronia
            zhejiangensis].
ACCESSION   WP_175981559
VERSION     WP_175981559.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia zhejiangensis
  ORGANISM  Caballeronia zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Caballeronia zhejiangensis"
                     /db_xref="taxon:871203"
     Protein         1..405
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43572
     Region          8..404
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(103..105,129,179,211,240,242..243,251)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(106,139,204,249..251,280,283)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            243
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mtapteglnr flaaarpsat ykvmdrvaar rasgatvisl sagepdfntp ehvcdagvaa
       61 iraghtrytq vaglralrea iatkfqreng ldvdwrhtlv csggkqvifn alaatlnegd
      121 evivpapfwv sypeivqlcg aqsvlvscea dsgfkltada lqaaitprtr wlilnspsnp
      181 tgavysrael qalaevllah pqvlvlsddi yehlifdnle fftiaqvepr lhervltmng
      241 vskayamtgw rigfgtgpgw lieameklqg qqtsgastis qyaalaaltg pqnsiehsrv
      301 afqrrrdlvv dqinrapglh cavpqgafyv fasckgligk ttpsgvrlds deavvnalld
      361 emgvatvhgs afghgpyfri ayalddesll ractairdfc rtltn
//
LOCUS       WP_175981566             375 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia sp. BCC1630].
ACCESSION   WP_175981566
VERSION     WP_175981566.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1630
  ORGANISM  Burkholderia sp. BCC1630
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Burkholderia sp. BCC1630"
                     /db_xref="taxon:2676304"
     Protein         1..375
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=42060
     Region          87..327
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 masplvflhr mlgfaaarrg rtlsgespqh ngerfsnvap rpvegfgktl giawnmlvnk
       61 prntvptgal pidsltreql daapdrslyr lghstlllkl rgefwltdpv faeraspfrr
      121 igpkrfhasp ialadlpplr gvllshdhyd hldrdtvlsl aaatgvfvtt lgvgdrliew
      181 gidakkvrql dwwqsvevdg ltltatpaqh fsgrslfdgn stlwaswviv dddlrvffsg
      241 dtgyfdgfrt igerlgpfdv tlietgaydp qwpyvhmqpe etvqahidlr grtlmpihng
      301 tfdlamhrwq epfervtala mvrgvelstp rmgerlnlda phrgerwwrt vdepakasat
      361 ktrrwqqlca sqatk
//
LOCUS       WP_175981613             380 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: amidase [Caballeronia].
ACCESSION   WP_175981613
VERSION     WP_175981613.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..380
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39027
     Region          21..380
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 msaflqqfdl athaaadapt iaikdsidia gypttaasra ladappaprh aqvvqrllda
       61 gwritgkanm helafgmtgl ndfsgtpvnp qdparipggs ssgsasavgl glvdaalgtd
      121 tggsvrcpaa ccgviglkpt fgrvsregia prqtsldcvg pfaramntvi dvmlaidpsf
      181 qggrarrdvt airvalpdvq aegrirdava savarsglas ravqlesiqd aftaglavin
      241 aetwrafghl vgsgklgpdi larlsaaant pvseldaaer irrdftdevd rvladadvli
      301 lptmpslpit ieaaragtpv iamsslirpf nlsghpaltl pvpvegaslk aglqivgrkg
      361 ddetvcavaa yieamlapha
//
LOCUS       WP_175981621             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Caballeronia].
ACCESSION   WP_175981621
VERSION     WP_175981621.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46596
     Region          21..427
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(34..35,38..39,42,82,140..141,143..145,148,168,
                     171..172,175,257,260..261,264..266,269,296,300,353..354,
                     358,362,378,381..382,385..386,389)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 matvhtstae tsaampdrtl rriviasvag namewydffv ygtaaalvfg slffpanadp
       61 ligtlgafaa famgfvarpl ggivfghigd rygrraslvw tllimgfatf gigllptydh
      121 vglwapvalv alrllqgias ggewgggvlm isenappekr gyyaawsqlg vgggfvlssa
      181 aflavqalph dqfiswgwrl pflasivifa lgvyirhslp esrdfanaee agktshmpvl
      241 eaikrhpkei lmamglrvae nggayiflaf slvygkfigi pnstmltgvm lamvvemiam
      301 llwgklsdri grkpvymiga aslaamafpf fwlldthstp liwlalvlgt avchgamigt
      361 lpalvgelfs tevrysgval ghevasifag glspllatal lshyhaswpv avflialslv
      421 tvvtlrfthe trhqsh
//
LOCUS       WP_175981676             270 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: enoyl-CoA hydratase/isomerase family protein
            [Caballeronia].
ACCESSION   WP_175981676
VERSION     WP_175981676.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..270
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28456
     Region          8..253
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mtndtlpvla sqhgalrllt lnradklnaf tpdmlaalea eiadaladda trvialtgsg
       61 akafaagndi erlvsldgvs ayrdmvagqr allrlhesak ptiamvngya lgggfelala
      121 cdfivassea sfafpeitln tmpgwggtql avakmglaca krfvmsgrrf sareceafgf
      181 iheiaapakl fdavraladt lasydpfaae makralnras dmplsagldf eaaqyavnfs
      241 segaraglrh fverkrarra aqadtapvtp
//
LOCUS       WP_175981674             387 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Caballeronia].
ACCESSION   WP_175981674
VERSION     WP_175981674.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..387
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41622
     Region          11..386
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mtttfnqphw lgeehtmmre avrrfaekei apqsetlweq eafpyaiwrq agelgftglp
       61 ypdefggggg dwlsfvivle elarvdcava nalmanstva sllnnygtpq qkarflrpil
      121 dgtqigaigl sepdagsdaa nigtravfdg erwiidgakt fisnsgteig gptviaavtg
      181 trpdgrkeis nfivpqgtpg ygkgrklrki gwrasithel ffeqcaipad qllgergagl
      241 rqtlaqistg riligalalg ilqgsldrsv aymkerrafg raiaefqalq fkiadmaada
      301 haarlmlyda aaskdagapf dvqasqaklf atehamkaah qalqihggyg vmaefpvara
      361 fgdakvleiv egtseiqrmi iartlla
//
LOCUS       WP_175981726             279 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: lytic transglycosylase domain-containing protein
            [Caballeronia].
ACCESSION   WP_175981726
VERSION     WP_175981726.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..279
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - lytic transglycosylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=30253
     Region          67..278
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 mnramrsasl riegrraiav llaigclalg eraraasmlr cesddntvty vstrienakc
       61 irvnmnwqwt ppaassasma saappaaplt rrqttariys yvedgvrhfv srkpagvaan
      121 vtvielrfme acnlcspadd vnvaglaldt rsygreidaa aasfnvdsal vravihaesa
      181 yranaisrag aqglmqlmpa tatrfnvgdp fdaaqnirgg vqylswllrr fnnnldlala
      241 aynsgeaavd ryngvppyne trtyvsrvkt laeryrdgr
//
LOCUS       WP_175981768             232 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CDP-alcohol phosphatidyltransferase family protein
            [Caballeronia].
ACCESSION   WP_175981768
VERSION     WP_175981768.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Sciara,G., Clarke,O.B., Tomasek,D., Kloss,B., Tabuso,S.,
            Byfield,R., Cohn,R., Banerjee,S., Rajashankar,K.R., Slavkovic,V.,
            Graziano,J.H., Shapiro,L. and Mancia,F.
  TITLE     Structural basis for catalysis in a CDP-alcohol phosphotransferase
  JOURNAL   Nat Commun 5, 4068 (2014)
   PUBMED   24923293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Koga,Y.
  TITLE     From promiscuity to the lipid divide: on the evolution of distinct
            membranes in Archaea and Bacteria
  JOURNAL   J Mol Evol 78 (3-4), 234-242 (2014)
   PUBMED   24573438
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Koga,Y.
  TITLE     Early evolution of membrane lipids: how did the lipid divide occur?
  JOURNAL   J Mol Evol 72 (3), 274-282 (2011)
   PUBMED   21259003
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..232
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25011
     Region          37..219
                     /region_name="PgsA"
                     /note="Phosphatidylglycerophosphate synthase [Lipid
                     transport and metabolism]; COG0558"
                     /db_xref="CDD:440324"
ORIGIN      
        1 mtkscppnpe avpepttwda rlarrlvtpl vgtpvtpnhl ttlrlaigla gawylslgqf
       61 wmctlgalli alsnfvdhtd gelarisgqs skighfydla cdalvtvllf lgigfyvavh
      121 hpsmivpaqw lggmagvava lifflrmrie smigksgtkq aslagfeted vlyllplvti
      181 lngmtpflia aaigaplfai yvavdyqrvv aqtkrraqat rakddkdfqa vr
//
LOCUS       WP_175981798             703 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC1630].
ACCESSION   WP_175981798
VERSION     WP_175981798.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1630
  ORGANISM  Burkholderia sp. BCC1630
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Burkholderia sp. BCC1630"
                     /db_xref="taxon:2676304"
     Protein         1..703
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=77898
     Region          12..703
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mqlsdipgff glqsnrlfti qtpmkgrsdl vfvdfqgteg lsqnfefrvr lasqdpniel
       61 kkligqpvtl tlqltdalas seeryfhgyv anfshldhdg sftvysatlv pwlwmlsrsr
      121 dirifqeent eailakvfre ygkiasfefr lskatknrsy ctqyretdle fverlmqedg
      181 lfyffehakd ghklvisdns iaakpisgrs pvlqytkgea ldnlavvtsf qasrqlesss
      241 vglktfdykv pharrfvsgg tevnqgevps yevydylgeh gfpdsdrgea ltrfrtqala
      301 ahskvfigts tsrrlspgqy felddhydhg aakaedrqfl lttvthsgtn nyqaseggat
      361 yqssfvcirk kipyrpafti erpsiigpqt avvvgpqgee iytdnlgrvk vqfhwdrlgk
      421 rdqgsscwvr vgqpwagrgf gmiqvprigd evvvifldgc pdrpliissv ynsanmppwv
      481 lpgnatqsgi ltrstktgnv ntanairfed kkgseevwlh aekdqrleve hdeshwvgnd
      541 rtknidhdet vhvkhdrtet vdnnetitig vdrtehvgnn etltvggnrn etikgmenll
      601 ialtstetvg lakaltvggg yqvtvvgavn ttaglasaee vglsktsivg ksysikagkv
      661 fevtvgkstf rmdedgnitl kgvklliegs gpveingkdv dvn
//
LOCUS       WP_175981811             232 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: pirin family protein [Caballeronia].
ACCESSION   WP_175981811
VERSION     WP_175981811.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..232
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25015
     Region          10..232
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mieirrsner ghanhgwlds yhsfsfadyy dpehmhfgal rvinedrvag gqgfgahghr
       61 dmeivsyvle galahrdsmg ngstirpgdv qrmsagtgvr hsefngsptd tahflqiwii
      121 pdapggapgy eekrfaddek rgrlrviasp egtdgsvkig anarifaglf dgderadfdv
      181 pagrrvyvhv argavtvnge algagdavkl edvskvtidk gdnaevllfd la
//
LOCUS       WP_175981883             378 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glycosyltransferase family 9 protein [Caballeronia].
ACCESSION   WP_175981883
VERSION     WP_175981883.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..378
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41189
     Region          51..376
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 msrlsgriri iaraipklaf kafrnkptdv ssiliahhll lgdtllltpl vaklrvrypq
       61 armaltcpka ivplyaghpy gaealpfdpr daasvsavlk sgpydlgivv gdnrhawlai
      121 aakcrwivgh gddtpawknw pldeshayps kpaawadiaa tlidgpapar yrpsdwpapv
      181 aasfapsdaa llaqpyvvlh pgastsvkrw phdrwralar hvetlgytpv wsggpgevel
      241 iraidpeary vsfagrvglg dlwhlfagsr alvcpdtgva hlgrmvsvpt ialfgpgnam
      301 ihgagefwrd arfrpvtivd mpcrdepdif rrkiawvrrc drnettcvaw rgdhaacmgl
      361 isldmvrgal eemlaegl
//
LOCUS       WP_175981954             284 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [Caballeronia].
ACCESSION   WP_175981954
VERSION     WP_175981954.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..284
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29331
     Region          7..279
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 msfeatfwlf ctglgasaag gmlgmasglf ivpiltmffh idmhaaigts ivsviacscg
       61 gaaaflrggl tnvrlavvle tattlgaltg vfvagvvpva aldflfagvl lvsawqmfir
      121 redpagtsrp ipsnglaaal glhssypdrt lrrdipyevr rvpvgltlmy aaglvsallg
      181 igsgilkipa mdnalrlpik vstatsnfmi gvtaaasasa yflrgeivsa iagpvalgsv
      241 igaiagarvl mkvrgerlrl lflsmlllva cqmfmqgigi dllr
//
LOCUS       WP_175982141             294 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SDR family oxidoreductase [Caballeronia].
ACCESSION   WP_175982141
VERSION     WP_175982141.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Bhatia,C., Oerum,S., Bray,J., Kavanagh,K.L., Shafqat,N., Yue,W. and
            Oppermann,U.
  TITLE     Towards a systematic analysis of human short-chain
            dehydrogenases/reductases (SDR): Ligand identification and
            structure-activity relationships
  JOURNAL   Chem Biol Interact 234, 114-125 (2015)
   PUBMED   25526675
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 294)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 294)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   7  (residues 1 to 294)
  AUTHORS   Jornvall,H., Persson,B., Krook,M., Atrian,S., Gonzalez-Duarte,R.,
            Jeffery,J. and Ghosh,D.
  TITLE     Short-chain dehydrogenases/reductases (SDR)
  JOURNAL   Biochemistry 34 (18), 6003-6013 (1995)
   PUBMED   7742302
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431150
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..294
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=32034
     Region          2..214
                     /region_name="YbjT"
                     /note="Uncharacterized conserved protein YbjT, contains
                     NAD(P)-binding and DUF2867 domains [General function
                     prediction only]; COG0702"
                     /db_xref="CDD:440466"
ORIGIN      
        1 mtilvtgatg rvgrqvvdql vrrnadvrvl vrdpskadfp savsvvqgem ldidslrraf
       61 agvrtlflln avsgdeftqa lialniares gvervvylsv mhaerfvnvp hfavksgaeh
      121 mieamgfsas ilrpayfmdn elmikdaiie hgvypmpigt kgvamvntrd iaevaaleli
      181 rrdeaaahlp levinlvgpd tltgpqlaai wtdvlgrpvg yggddptgfe qnlasfmpkw
      241 mayemrlmae ryvsdgmvpe lgdaerlvgi lgrplhayrd faadlaegqs qrti
//
LOCUS       WP_175982128             320 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: PDR/VanB family oxidoreductase [Caballeronia].
ACCESSION   WP_175982128
VERSION     WP_175982128.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..320
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35050
     Region          13..225
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(54..55,57,71..73,79,81..82,123,224)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(54,56..57)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(79,82,85,92)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(115,119..122,124)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(120..121,145..147,199..200)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          239..320
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 mndelsfrtl vvtkkdqvae gifrfelrdg aggklpafta gahltvrvpn ganrsyslcn
       61 dpaetdryvi avkrdaagrg gsvsmaddla qgdridvsep rnefvlnera rsfvfvaggi
      121 gitpilsmmr ylkaidgprf kliyvsrspe ttafidelsg pewkphvvih hdhgdlaqaf
      181 dfwpvfekpa sgahvyccgp ralmdgvrdm tghwptgsvh fesfgvdqsr aadnapfsvk
      241 lersgrsfei pkdrsileil rdngirapss cesgtcgscr ttlcageadh rdmvlgedek
      301 rdqimicvsr akseelvldl
//
LOCUS       WP_175982146             449 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: phenylacetate--CoA ligase family protein
            [Caballeronia].
ACCESSION   WP_175982146
VERSION     WP_175982146.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Luengo,J.M., Garcia,J.L. and Olivera,E.R.
  TITLE     The phenylacetyl-CoA catabolon: a complex catabolic unit with broad
            biotechnological applications
  JOURNAL   Mol Microbiol 39 (6), 1434-1442 (2001)
   PUBMED   11260461
REFERENCE   2  (residues 1 to 449)
  AUTHORS   El-Said Mohamed,M.
  TITLE     Biochemical and molecular characterization of
            phenylacetate-coenzyme A ligase, an enzyme catalyzing the first
            step in aerobic metabolism of phenylacetic acid in Azoarcus evansii
  JOURNAL   J Bacteriol 182 (2), 286-294 (2000)
   PUBMED   10629172
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Ferrandez,A., Minambres,B., Garcia,B., Olivera,E.R., Luengo,J.M.,
            Garcia,J.L. and Diaz,E.
  TITLE     Catabolism of phenylacetic acid in Escherichia coli.
            Characterization of a new aerobic hybrid pathway
  JOURNAL   J Biol Chem 273 (40), 25974-25986 (1998)
   PUBMED   9748275
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..449
                     /product="phenylacetate--CoA ligase family protein"
                     /EC_number="6.2.1.30"
                     /GO_function="GO:0047475 - phenylacetate-CoA ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0010124 - phenylacetate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49216
     Region          13..446
                     /region_name="PaaK"
                     /note="Phenylacetate-coenzyme A ligase PaaK,
                     adenylate-forming domain family [Coenzyme transport and
                     metabolism]; COG1541"
                     /db_xref="CDD:441150"
ORIGIN      
        1 mnvavhspar gvyfdeafet lpldevrrhq dalwashwpy lramsafyrt klerwagrdd
       61 itldtlqdmp ftekddlrvs qenaspygdy vactesgiar lhrtsgttgr plilansard
      121 aadiarvgar smwaaglrpe hrvvhclnyc mwtggftdht ileaagatvv pfgvgntrll
      181 idsilnlgid aisctpsypa lieqvlretg gpaprdlglk lglfggeagl dnpelraame
      241 ekwgfavrna nfglsevlsi lggqtdwttd llyhaadvvf aeiidphtla rlpieagttg
      301 elvcthlrkq cqplvryrtr dvvtvtatda gpdgrsawrf rvtgrtddmf nvrgvnvfpg
      361 avrlavealp qwasgmfriv lkgpgpydri amtveaangl pvarwndaaa rieaavreri
      421 gasaavtivp fehfprtegk trwidrepa
//
LOCUS       WP_175982197             785 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: type VI secretion system Vgr family protein
            [Caballeronia].
ACCESSION   WP_175982197
VERSION     WP_175982197.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 785)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 785)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..785
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..785
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=86078
     Region          5..773
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 masndavaqk plasvdtplg ddlrflslsa raelgrmpri eltlvskrad ldfsrilgkr
       61 vsvslnvpka kprvfagyvv gfrqagmrgr lhiyeaavrp wlwllsrrsn crifqnktve
      121 eivkavfadp vykglefgei kwkastrahp preycvqyre sdfnfvsrll edegiyywfq
      181 dkdgkeslil tdtlaahesv agceslpyga vqaaapdief vsewrthhai ethnwlltdy
      241 dfkhpsrplq kqaakhmqgf dafsglehfd ypggyveadh gesraksrad ewriegsvpd
      301 dpginwhqve artnsknvra gallkltrhp radqntqylv trtryeiela dyeafdgaqa
      361 nrcecwfsai dakqafapar tarkpfvqgp qtavvvgpgg deiytdqygr vkvqffwdrq
      421 gkrdensscw irvsqpwagk gwgaiaiprm gqevivdfle gdpdrpiitg rvynaeqmpp
      481 ydlpanmtqs giksrsskgg sgancnelrf edkkgaeqvl ihaeknqdie vendethwvg
      541 hdrkknidhd ettvvkhdrt etvgnnekid vvmnrtetvg vnesitigan rtktvkaset
      601 atvllqrths vginetitvg aaqevtigaf qvvtvgayht etigasqtvs vgsgqtvtvg
      661 sdqtvsvggn qatsvtgdqs lsvgggqtvs vakdasesid gaqsstvakg rttsvgedda
      721 lkvgktltin aeesislvtg dasivmkkdg tiqikgkdis lkgsgkisvt adsdvvmkgs
      781 kilqn
//
LOCUS       WP_175981820             132 aa            linear   BCT 11-JAN-2025
DEFINITION  GIY-YIG nuclease family protein [Burkholderia sp. BCC1630].
ACCESSION   WP_175981820
VERSION     WP_175981820.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1630
  ORGANISM  Burkholderia sp. BCC1630
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Dunin-Horkawicz,S., Feder,M. and Bujnicki,J.M.
  TITLE     Phylogenomic analysis of the GIY-YIG nuclease superfamily
  JOURNAL   BMC Genomics 7, 98 (2006)
   PUBMED   16646971
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Burkholderia sp. BCC1630"
                     /db_xref="taxon:2676304"
     Protein         1..132
                     /product="GIY-YIG nuclease family protein"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=15415
     Region          14..88
                     /region_name="YhbQ"
                     /note="Predicted endonuclease, GIY-YIG superfamily
                     [Replication, recombination and repair]; COG2827"
                     /db_xref="CDD:442075"
ORIGIN      
        1 mllkeedthm saawtyllvc segltylgst snlkrrlhah nsdnnsgwtk grkwrllaak
       61 rfetrqeafa yeallkvdvr rrnawkrkst arakivfarh giefdfakwa pkkrqrvlpa
      121 prpdywsqqn gr
//
LOCUS       WP_175982324             197 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: J domain-containing protein [Caballeronia].
ACCESSION   WP_175982324
VERSION     WP_175982324.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10446266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..197
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=22762
     Region          3..66
                     /region_name="DnaJ"
                     /note="DnaJ domain; pfam00226"
                     /db_xref="CDD:395170"
     Site            order(31..33,43,46..47,50..51)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
ORIGIN      
        1 matlyetlgv dehateeeik rayrkaamrc hpdrnvgned varakfleik eayailsdpa
       61 qrevydriyt eemrrweerv rqeeaerear etkerearea lyaqrvslam rfaskghnrd
      121 vvfgvllgaq cdestarqia dsaialhesr qereeskeke reeepvaakk eekepaaada
      181 snplgamwfq flnnlrf
//
LOCUS       WP_175982347             428 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Caballeronia].
ACCESSION   WP_175982347
VERSION     WP_175982347.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..428
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44593
     Region          16..>194
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mptddssrsa rpiphetaaa afvhivrdaf aalgrelvai rptparalfa tqamlsvgla
       61 valayafhls niwwaaisgf avmqskfsac aqrgvhrvvg tiagaligav agpiigdvpw
      121 lfvpllgaiv gmsvyralvs dagyawvlgg vtslmvtfea hrlesaaata sfallrvaev
      181 mvgtaacvav salvhagvqh yrksrgappv praqaastvd rvdgvnaqtv tvipsdaara
      241 vqaldathla raeqtalamr krlawqgaws vmilaaiaya wnlpgfaqam vtavavlilp
      301 tsalgkptrk piaermiqrf igcllagaas lallpllgdn afacmialcv gvwigchvqt
      361 gtqgasyvgr qfsiafimvf vqdhhwssdp mpalmrlegi lagivvlsav maagaawask
      421 rgphaamr
//
LOCUS       WP_175982354             348 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Caballeronia].
ACCESSION   WP_175982354
VERSION     WP_175982354.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..348
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37057
     Region          10..253
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msstqassvl rlgilggani arqftrdvrp servrvvava srsdenaqaf aqangiekwf
       61 gsydallasp didavyiplp nslhaewaik aadhgkhilc ekplaldrde aarmfeaadr
      121 ngvllleafp yyfqpqtatm maligegaig dvraiqanfg ftvgnpgani rmkpelggga
      181 lldagsypls lirlvmgsap qrvdaiatwa dsnvdislma tliyadgrra qvscsmdaan
      241 hrhatiigtq gtidteylnh tsaqtagdqy gylpsqmrvr rgipnsvpfe tvesdtgsgf
      301 ffaaesfarm vathdaaaie yyaqvsldna atlaaiiasa rsgkpvtl
//
LOCUS       WP_175982364             399 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DNA-binding protein [Caballeronia].
ACCESSION   WP_175982364
VERSION     WP_175982364.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13774834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..399
                     /product="DNA-binding protein"
                     /calculated_mol_wt=43819
     Region          29..141
                     /region_name="KfrA_N"
                     /note="Plasmid replication region DNA-binding N-term;
                     pfam11740"
                     /db_xref="CDD:432038"
     Region          <85..>323
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
ORIGIN      
        1 mdqstrdtlr qeieamratg arrqdlsqha ckrlffdlgv rpsvttvrel tqtgsasdip
       61 kdieafwagl rstlrvrida gampeslqer agellaalyd eaqtvaraal neekarldma
      121 iqaaqaqard adirreaier aqqraearae agaaqiaale aelktlrsqg tdaqaglrev
      181 iarwekenet lsarlqheqd aaarlrdrid elqnelrhst ehyaqqikda vkeaerrvhp
      241 mlveldslrg maatyqtsar easqkefdfi qqlsaarsra drlesqvraq sdeidalvle
      301 rdarrvqsga saevgalias laaqgrltsa eiarlgtqid ahvaaptscp aceagepelq
      361 rhedeyelsc pncertsgat asklaavdef irsarvstl
//
LOCUS       WP_175982375             362 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [Caballeronia].
ACCESSION   WP_175982375
VERSION     WP_175982375.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..362
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39600
     Region          20..343
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mnaaeslpps svdgqsksri rfgiillpnf tltafsgfvd llrlsadegd fsrpvrcsws
       61 vigetlapvr ascgiqitpw etydqaepfd yvvvvggllh sgpatsdatl qfirraaasn
      121 atlvgmctgv fslmragvle ghricvswfh ywdfverfph adeqslvadr lfvidrrrit
      181 csggrasidv aaaillrhfe tatvqkalri llvddmqkgn apqphppgla pathpkvkra
      241 illmeqhvgr sltldelahk ldlstrqler lfkaetgkap qayakqvrlr taawlltssd
      301 ktvadiassc gfsdashlgr efrkqfglpp mmyreqggap dapdanhamd ydetfpgraq
      361 ai
//
LOCUS       WP_175982415             386 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Caballeronia zhejiangensis].
ACCESSION   WP_175982415
VERSION     WP_175982415.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia zhejiangensis
  ORGANISM  Caballeronia zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Caballeronia zhejiangensis"
                     /db_xref="taxon:871203"
     Protein         1..386
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42060
     Region          26..373
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mkpmlapvve aharksaasq arewgadvkr ilcirldnlg dvlmttpalh alraaqpgrh
       61 ltllasragk atapfidaid dvieydapwv kqdapidala dlamrarlas ahfdaavifs
      121 vysqnplpaa mlchlagipl rlahcrenpy glltdwvqet epqhgtrhev erqlalvarv
      181 gakaddtrmr fsvrpadids ltqkliardv dmdapfivvh pgasaesrry pverfaetie
      241 rlgaqlewpi lvtgsrsesh lcraacgtsp yahdlsgvle lgelaaliqr arvlisnnsg
      301 pvhlasalga pvvdlyaltn pqhmpwqtsh rvlyhdvscr wcyrsvcpeg hhaclvgvev
      361 devvsaalel ieeehaspvh pitqas
//
LOCUS       WP_175982443             478 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Caballeronia zhejiangensis].
ACCESSION   WP_175982443
VERSION     WP_175982443.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia zhejiangensis
  ORGANISM  Caballeronia zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Caballeronia zhejiangensis"
                     /db_xref="taxon:871203"
     Protein         1..478
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49166
     Region          17..463
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(24..25,28..29,32,64,114..115,117..119,122,142,
                     145..146,149,279,282..283,286..288,291,319,323,379..380,
                     384,388,404,407..408,411..412,415)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mhmttsstrr wsafavllvg aflppldffi vnvalpsiqs tlhtsaaelq lvisgyaaay
       61 avflitggrl gdlfgrrsif ligvtgfglt svicglassp aililgrvlq glsaaamapq
      121 glasihalfp ekeraralgl ygaavglaav aaqalggali sadvfhlewr vvflinlpvv
      181 aavlifglpl lpdvrgdspa pvdrigvllc altlaflivp lvegreldwp wwacamlias
      241 pvagvgfcry emayarrggv plisvelirr pglmsgltgv lffyvvsaff ltfsvylqaa
      301 lgmspfetgl vflpfgvgaf igplttplai rlfgdrvpai gmmleaagci llaalvagap
      361 gqmpaqfpli gavallgfgq gwalptlvrs vinrapatgs gmiagitnsa lqisaalgva
      421 viggvffsva gtspdsvtla ralviammcv ggsltvsavl sivasrssih aaaraapr
//
LOCUS       WP_175982446             270 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MetQ/NlpA family ABC transporter substrate-binding
            protein [Caballeronia].
ACCESSION   WP_175982446
VERSION     WP_175982446.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 270)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..270
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29447
     Region          1..269
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkkfhplrag vlaiassami aslaqaadpn kpeirfgata gpysdqiryg ikpqlekegy
       61 kvtivefsdy vqpnlaladg aldanafqhe vylkkfsadh klalselvkv ptapiglysh
      121 khkrldelkd gatvslpndv tnqaraiill qqlgwvtlks gvdpvksser diasnphrik
      181 lvpleaaqlp rslddvdyaf vngnfalaag lklndallle kippyylnlv avrtadlnkp
      241 yvtdianayr sadfarvieq rfagfskpaq
//
LOCUS       WP_175982458             360 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Caballeronia].
ACCESSION   WP_175982458
VERSION     WP_175982458.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..360
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38438
     Region          1..356
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mthltlqavt krfhaayavd hvdlavpdgk lmcflgpsgc gkttllriia gletassgtv
       61 afagrdltdv panrrdfgmv fqslalfphm tvaqniaypl rlrrvgkaae asrvaelldl
      121 irlphmadrp vsrlsggqrq rvaiaraias spklllldep lsaldaklre amqveirllq
      181 qrlgittimv thdqreamtm adeivvmekg riaqvgkpld iyrnpvsefv adfiglgnil
      241 pvtleggdri alpggqqivv daappargaa gdvrllirpe dvcmrtavng avdpgpnmla
      301 gkvafirdvg asleatidca gftltaattt retpdlrtgm pvfaelppha ckliaartah
//
LOCUS       WP_175982459             280 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Caballeronia].
ACCESSION   WP_175982459
VERSION     WP_175982459.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 280)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..280
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30109
     Region          13..274
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 msalrlsaim pgrlsraasl latvvlflaa lpiltmvtms fgnsdtlqfp ppsfglrwyr
       61 aawhtfvspd asdvlsmgta lttslvvavs tmiiatavsv paayalsryr frgkavieql
      121 valplvyplv mlglslllvf nvlpvelgil rliiahvila lpftvkncaa svaaigpefe
      181 eaaclmgasp rraivdvvlp lmrpgilagm lfafivsfne ftvtfflygi dtmtlpiwly
      241 srtvssldpt vfsfavvivl idfaliwlle rligdegval
//
LOCUS       WP_175982491             252 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: enoyl-CoA hydratase/isomerase family protein
            [Caballeronia].
ACCESSION   WP_175982491
VERSION     WP_175982491.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..252
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=26790
     Region          4..247
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mghilsrred avlvlelsnp gkanaldfam laaldeqiaq inrddgirav vlrgtpggvf
       61 ssgadirews alspetfatq wvgegnavfr rferlrcptv avieglcfgg glelalccdl
      121 rlagtgarlr fpevsigaip gweggdrlqr iagrgralea vllsqeidas talqwgivna
      181 vctpqeveaq lqewtarlcr vspraaalak alivddhddp haaytsaala vrsspdaelg
      241 iraffaktaa vf
//
LOCUS       WP_175982496             435 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Caballeronia].
ACCESSION   WP_175982496
VERSION     WP_175982496.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46885
     Region          28..426
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(41..42,45..46,49,81,131..132,134..136,139,159,
                     162..163,166,261,264..265,268..270,273,300,304,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtsissnmta esavdttleq qavrkaawrf ipllalayff nyldrtsvgf aaltmnrdlg
       61 ltatqfgwga gimfagyclc evpsnlalyr fgarrwlari mitwgffaaa talavgptsf
      121 yvirlllgig eagffpgvif flavwfpasy rtrvlawftv stplsslvgg plstwllkmd
      181 gllglagwkw mfiveglpac ilgffvlkml adkpadakwl speerqalqs afdregtasq
      241 kkkdfgaalk dvrmyilami sfgftmgsyg igiwlpqmlk ahgmsvtqtg wvsavpyffa
      301 tiallwwakr vdrrgghian laaglfigav algistyfqq lvpaltgitl aligtiagrt
      361 ifytlparfl sgqaaaggla linsigalgg fagpylvgyl kdsfgtftag miglavvlaf
      421 ttlltlslya fnkgk
//
LOCUS       WP_175982501             208 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Caballeronia].
ACCESSION   WP_175982501
VERSION     WP_175982501.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..208
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22915
     Region          1..199
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 miligqydsp fvrrvgialk lydmafehrp wsvfgdadki apynplcrvp tlvldsgdtl
       61 iestmildyl daeagdaral ipsggperrq alkvcalatg ladkavalvy ervlhkeksq
      121 awldrctgqv ervlnalead raaratpywf gdaighadia vacalrfare ahpeifsstr
      181 wptlighsdr cetlpvfkai vqpfnppr
//
LOCUS       WP_175982519             522 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Caballeronia zhejiangensis].
ACCESSION   WP_175982519
VERSION     WP_175982519.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia zhejiangensis
  ORGANISM  Caballeronia zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Caballeronia zhejiangensis"
                     /db_xref="taxon:871203"
     Protein         1..522
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=56165
     Region          20..522
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 magstsadvv vvgsgvagsl vayrlakaga svilleagpr larwqivenf rraadkrdlc
       61 apyplvrhap rpepmnpgay lvdrgatsyq pqylrlvggt twhwagaawr llpsdfrvkt
      121 lygvgrdwpf pyetlepwyg qaeadlgvag pdidlgsprs tpypmdalpl swmdrrvaev
      181 lgaqsyrvvp epmarnsrpy darpaccgnn ncmpicpiga lyhaashadk aeragaalva
      241 qavayriean drgeivaihc kdpnglstrv tgrrfviaan giettrfpkg igngadqvgr
      301 nlmdhpaasv sflanealwp grgpvemssi vdfrdgpfra qqaakklhls naaptlavtr
      361 nlldkgltgg eldrqireqc arrltfgsfh eqrpssenrv mlsaqkdalg lprpeiaysi
      421 ddyvrksaad thaqfariag ifegteiehd dslgasshim gtaimgrdpn dsvvddecra
      481 hdhpnlfiag savmpaggsv nctltiaals lrlagtieas lr
//
LOCUS       WP_175982623             238 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Caballeronia].
ACCESSION   WP_175982623
VERSION     WP_175982623.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..238
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25557
     Region          14..238
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mtaivrrrda rvgspalavs vrglqrrygs rvvidaldld irkgefvall gesgcgkttl
       61 lralagldsp dagsiraper psvvfqehrl lpwstlwqnv algyentigr tgaaralaev
      121 glagreddwp rnlsggqaqr valaralihd palllldepf aaldaltrir mhglvkelva
      181 lhrpgvlivt hdvdealtla drilvmragr iaasfepgeh apqalrpall aelgvrsh
//
LOCUS       WP_175982662             265 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Caballeronia].
ACCESSION   WP_175982662
VERSION     WP_175982662.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..265
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28252
     Region          12..261
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mpsdtaslda akatgtaafs kfmavlqlia dagepptiar lttasgyprp tvyrivgali
       61 aeglvvesvr ggcyapgprl mslasrswer sdlriaatda lqalrdatqe tvhlavrsgs
      121 emvyiekles phavrmasri gtrvtlysss vgkaylstqs paerdallhg lkferftpnt
      181 itdraaldae ldathargys edreeneaqi fcygsaivga ngvtlgcvsi siplfrksat
      241 pletyveplk dasraiaerm spgtr
//
LOCUS       WP_175982670             180 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: universal stress protein [Caballeronia].
ACCESSION   WP_175982670
VERSION     WP_175982670.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..180
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18643
     Region          1..143
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mykhilvavg tslsesaltt aitrardcna rltalhivdq apwwaivtad snpgetldvi
       61 edharavthy aarlidsagi dgiarsvtqp ldgtsvgeli areakaagad livlggeaet
      121 gwrhgearlr dvvcshatcd vliaahasap lsagtdharv aassacagtr vshrqsaprk
//
LOCUS       WP_175982720             243 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alanyl-tRNA editing protein [Caballeronia].
ACCESSION   WP_175982720
VERSION     WP_175982720.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V.
  TITLE     Evolution of aminoacyl-tRNA synthetases--analysis of unique domain
            architectures and phylogenetic trees reveals a complex history of
            horizontal gene transfer events
  JOURNAL   Genome Res 9 (8), 689-710 (1999)
   PUBMED   10447505
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Cusack,S., Hartlein,M. and Leberman,R.
  TITLE     Sequence, structural and evolutionary relationships between class 2
            aminoacyl-tRNA synthetases
  JOURNAL   Nucleic Acids Res 19 (13), 3489-3498 (1991)
   PUBMED   1852601
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Schimmel,P.
  TITLE     Classes of aminoacyl-tRNA synthetases and the establishment of the
            genetic code
  JOURNAL   Trends Biochem Sci 16 (1), 1-3 (1991)
   PUBMED   2053131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..243
                     /product="alanyl-tRNA editing protein"
                     /GO_function="GO:0002161 - aminoacyl-tRNA editing activity
                     [Evidence IEA]"
                     /GO_function="GO:0002196 - Ser-tRNA(Ala) hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004813 - alanine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006419 - alanyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=26361
     Region          3..242
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
ORIGIN      
        1 mstralfred ayqtrcdatv taideqgihl dqtvfyplgg gqagdagtlt ladgtviaia
       61 dtrkakfega tpddavhvpa pgqedalakl ktgdkvgaei dwaqryrrmr lhtashlica
      121 vlpypvdgcs itteyarldl atvepierea veaklnalig gahgvqtewi tddemaarpe
      181 lvrtmsvkpp tglgrvrllr ienvdlqpcg gthvrnteei gelriaklek ksartrrlvl
      241 elv
//
LOCUS       WP_175982750             401 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Caballeronia
            zhejiangensis].
ACCESSION   WP_175982750
VERSION     WP_175982750.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia zhejiangensis
  ORGANISM  Caballeronia zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Caballeronia zhejiangensis"
                     /db_xref="taxon:871203"
     Protein         1..401
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=41602
     Region          9..401
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 mmndalelrf awrgmdsegq pmrgkiiaad alaaraslrr egvivtllet lgaapppkar
       61 tadvtvftrq lagllraglp lvgalellag sasasgmpri vralardiar gvpfsgalar
      121 hpaafgtlyc qlvsvgevag alptvlarla ddreraasqr arlraaltyp vmvlllslai
      181 taglligvvp tfktifdgfg aalpaptrfv lalsdgvanv gvpfgiaaas avfigwnwmk
      241 hspdaraaad haalrlplag kllrslavar wsralgtlls agtplsdafn slthatgnrv
      301 fdratvdiaa rlhngerlaa amravgcfpq dvvqpiavae esgsldamll dlatladrqv
      361 deriggfasl cepiviavlg alvgglviam ylpviqlgnv v
//
LOCUS       WP_175982797             305 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Caballeronia].
ACCESSION   WP_175982797
VERSION     WP_175982797.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32737
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..295
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,227..232,
                     238..239,241..242)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 melrllryfv tvaeemhfgr aaarlamtqp plsqairale eslgvalfvr tkrtveltpv
       61 gkdllpevrr llasadalrp laqslargea gvlslafvst adygllpall rdfgarhpgv
      121 rlqlteatsd vqidelvagr vdaglvippl ppryassley vpiareplmi amsekqaqel
      181 nsgedepvdl hdlaaaplvv fprrlapglh diimgcygaa gltprigqea iqmqtivslv
      241 sagmgvalvp qslrhlrrtg vvyrplldpg pfvetglvwr iaevspvlag fieivrsrae
      301 sagsv
//
LOCUS       WP_175982859             376 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Caballeronia].
ACCESSION   WP_175982859
VERSION     WP_175982859.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..376
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39270
     Region          224..>376
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mddeqpigda karladsslt ivqalvqrvq avlawldrvd pgthrrikgl rlvtayglaa
       61 algalqdvtq svpagvsvga laggfalwas vsearttrfe ssrdlvilcv aaafgaftft
      121 ffapmlretg rggaelilvt gaflagylkr fgmtgagvgs qlyigqllay gmdlrpgdsw
      181 aillalligm laaivprvls gpaehpvvlp alasepaygr daispafamg lqaacgalvv
      241 valnrlfgla esawaitacv yvvatsavgt aervrrriyg tlvgvpigiv clplaehwpl
      301 vvwilsafam iayamalper ydiacgafaf vlivtlaasg vhslelltar awetllggal
      361 gliasrvifp lrvvra
//
LOCUS       WP_175982812             454 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: mechanosensitive ion channel family protein
            [Caballeronia].
ACCESSION   WP_175982812
VERSION     WP_175982812.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..454
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=49423
     Region          161..435
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 mqnhflnels arlfrdfgep eviwqvaalv gllvvawwca rllrkkldar rqsrfeavrf
       61 gaeslnkalf pllgtvfvsi aqvvlapfih tsllrlalvp lcgitviytm lyvarrvfsr
      121 gqteheanal lylfeklvtv ivwvtmvltv mgiqddvvhw masvrfnfan ahmtllslas
      181 gvlwvcvtli vamwagalld drlmrarsld anlkvvlarv gralmilaai lvslsivgid
      241 itvlgvfgga lgvglgfglq kiasnyvsgf iilldrslrl gdminvsgnq gtvtqirtry
      301 tvvrgldgie tlipneklit dvvqnhssfl trgnakiavq vsyrcdvera mqllveatqg
      361 vervlqdpap aallasfgad ginlelsfwi eeaakgtggv kshvnravwr lfcehgieip
      421 yaqreiriid gvprpggesv lnagsggesa apaa
//
LOCUS       WP_175982879             509 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: class I adenylate-forming enzyme family protein
            [Caballeronia].
ACCESSION   WP_175982879
VERSION     WP_175982879.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..509
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54010
     Region          14..504
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mdtnkliasl paridaiisr gakahpdhia lhedaralty aqlddaidal aarlgaagvr
       61 agdrvmlige nsvllvaslf avsrldawvl ivnarlsave ldvirahakp rialytvdvs
      121 ddaahhaqrd gasvesldat pigafalsdi daaseqephg lssdrqcaal iyttgttgap
      181 kgvmlshrnl lfvaavsstl rrvgtsdrvy avlpishvfg lasmclgsly agatlrlaar
      241 fdparagrvl sdermtifqg vpamhaklid hftprgglna pslrfvycgg spldmtlkaa
      301 aeafygvplh ngygmtessp tvsntlldap apdssvgpli pgvearivpl ahqsdaddtg
      361 elwvrgpnvm layyrdaaqt aatvtedgwl ktgdlarfer gnlyivgrsk eliirsgfnv
      421 ypaeveqafn shpavlhsav igrsvqgned vlafvelrpg ctaseselae wvgerlapyk
      481 rpssirilda lpvsasgkvl khrlgklan
//
LOCUS       WP_175982930             160 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: thioesterase family protein [Caballeronia].
ACCESSION   WP_175982930
VERSION     WP_175982930.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10594194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..160
                     /product="thioesterase family protein"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17749
     Region          7..129
                     /region_name="4HBT_2"
                     /note="Thioesterase-like superfamily; pfam13279"
                     /db_xref="CDD:463826"
ORIGIN      
        1 mtyrdtvkpe wvdynghlrd afymliysla tdafmdrigl ddagrrarqr tlytleahvt
       61 ylreikegap vrvewrviah dkkrvhlyme mfegdateav caceqmlmhi dssgapksas
      121 fdddiaaria aepavapkda ryagrviglp arassaaapa
//
LOCUS       WP_175982941             374 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Caballeronia].
ACCESSION   WP_175982941
VERSION     WP_175982941.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..374
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40149
     Region          1..274
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mnrvrlgmvg ggegafigav hriaarlddr yelvagalss darraassaa aiglarsydd
       61 fremarieag rsdgieavai vtpnhlhapi atafleagih vicdkplavs ldegealakl
      121 arekdrvfav tytytgyplv rhargmvqrg llgdirvvqi eyaqdwlslp vetqanrqav
      181 wrtdpalagp agclgdigth ayqlaeyvtg mrpselaadv ttfvpnrrvd dhvqamlrye
      241 ngargmlwas qvaageenal rlrvygtkag iafdqqkpne lwftpiggas eritrgrvqs
      301 pealhatrvp aghpegylea faqvytdaaa ciasgttqgd dwlttvedgv aglrfveavl
      361 rsggrngewv glkn
//
LOCUS       WP_175982978             339 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Caballeronia zhejiangensis].
ACCESSION   WP_175982978
VERSION     WP_175982978.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia zhejiangensis
  ORGANISM  Caballeronia zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Caballeronia zhejiangensis"
                     /db_xref="taxon:871203"
     Protein         1..339
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34960
     Region          15..336
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mnkltaaptr qaastrttgt ptiskqalvr rfapllvlva lglcigalnh dffdpmnlsr
       61 iavgaaiplt ialgaafviq lgsidlsaeg ivavaaiavs tlvensyndn hfglwvlava
      121 laagailglv ngvlhvflri psfittlaig fvatgigtaw lsgntirvsd pslraisitr
      181 ylglplsvwi avlmlgvawf vykhtllgrh tlaigggedl arlsgvrvsr vriavfalag
      241 afygvagila vaqfgqghar iadgqlfvai taivvggtsl aggngtpmnt ligtlivivl
      301 gngmvllgvp pyvqqgiqgv liiaavtlal nrsrrrivk
//
LOCUS       WP_175982981             249 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Caballeronia zhejiangensis].
ACCESSION   WP_175982981
VERSION     WP_175982981.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia zhejiangensis
  ORGANISM  Caballeronia zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Caballeronia zhejiangensis"
                     /db_xref="taxon:871203"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26438
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkilvtvkrv vdynvkvrvk sdgsgvdian vkmsmnpfde iaveeavrlr eagvatevva
       61 vscgvtqcqe tlrtalaiga drailvesne elqplavakv lkalidkeqp qlvilgkqai
      121 dddsnqtgqm vaalaglpqa tfaskvvvad gkatvsrevd ggaetlsltl pavvtadlrl
      181 nepryvtlpn imkakkkple tvkpadlgvd vaprlrtlkv tepakrsagv mvpdvktlve
      241 klkneakvl
//
LOCUS       WP_175983032             742 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Caballeronia zhejiangensis].
ACCESSION   WP_175983032
VERSION     WP_175983032.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia zhejiangensis
  ORGANISM  Caballeronia zhejiangensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Caballeronia.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 742)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 742)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 742)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 742)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 742)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Caballeronia zhejiangensis"
                     /db_xref="taxon:871203"
     Protein         1..742
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=82877
     Region          1..702
                     /region_name="RloC"
                     /note="Wobble nucleotide-excising tRNase [Translation,
                     ribosomal structure and biogenesis]; COG4694"
                     /db_xref="CDD:443729"
ORIGIN      
        1 miksisisky ksyhptmptv ieidttkqat fiygsngagk saigevvhgr fvndpsfghc
       61 kvettgigpf rhlvynhafv arvigetmqg iftigeidta kqreidakei enaalraqlt
      121 plmegiatts kqveaentrg vddvwkgygl gkatklakll egygrdkrkf fdelrqyatd
      181 kgssldsier leqrwldass tetskslpha dltglaqiet dpiwaepiev stasklatli
      241 sllgngdwvd qgrkylkedq cpfcqqnlph dfqyelnkll egnrklkier vdslassyal
      301 rlerleqals gvfddaitrg tgldlawskl harmkenltl mrekqtkpge pvaieavvhs
      361 eltaalallk ekvsdfnqri ldrtaeraki ktmffqvlca draeayaiha salaplkerf
      421 ntesdeaaki ekqirtndll lqdlrraqtg vdasvesina slrdmgigsf wiarregdgh
      481 lyclarpdds dssthtlseg ektlisflyf ielikgshde tgavdvtktv vviddpissl
      541 sqnfvydvat iiqhqlvkpp igvakvkqvi vlthnlfffh elvlqlagnt lanasrkcqm
      601 lrvlknehsa vlpldpttfm ndydalwqvl qdakrglvpv rvvpntmrgi leqfftfttg
      661 medfdkalek mtivdrsqkf kalqrflnrg shkdgingpp vdwsqydvay yldklrallt
      721 acgnedhylr kmgepeeesd ag
//
LOCUS       WP_175983068             370 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: enoyl-CoA hydratase/isomerase family protein
            [Caballeronia].
ACCESSION   WP_175983068
VERSION     WP_175983068.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..370
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40919
     Region          21..356
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 mstlelsrda pevafevvnr vaivtldrph alnalshgmi ahlaerfaqc aaddsiaavv
       61 lrgagekafc aggdvrklyh aarndphhet pwlkffidey rldftvhrfa kpvialmdgi
      121 vmgggmglaq gaalriater trmampetri gllpdvgath flrvlprdla lyvgltgarl
      181 sgadarrvgl adecvpstwl rsfverleai rwddaqdtmt qvarvfvpsa nierhapldd
      241 mraqikrhfa vcatggveri vaslatdesd waratlalle shsptmlevt yhallrgrqm
      301 sladcfrmel gvvyraiddg dfvegvrali idkderprfa pttlaqvrae rvqhflsspw
      361 rremhpladl
//
LOCUS       WP_175983103             495 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Caballeronia].
ACCESSION   WP_175983103
VERSION     WP_175983103.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..495
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53665
     Region          44..470
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(54..55,58..59,62,96,146..147,149..151,154,174,
                     177..178,181,298,301..302,305..307,310,338,342,396..397,
                     401,405,421,424..425,428..429,433)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mnetatpret rlsdtasdrp aiietdlpgr ldrlpwgrfh tlivlalgit wlldglevtl
       61 agavasalks spalqfsnad vgiagsayia gavlgalgfg wltdrlgrrk lffitlflyv
      121 aataatafsw nlatfvlfrf ltgagiggey tainstiqef tparlrgwtd laingtfwvg
      181 agigaagsiv lldpallppd wgwracflig aalgltilfm rmwvpesprw lithnradea
      241 rhvveeieah frqhgieipd tpvkplrlha rdgtpirevv htlfkahrsr slvglvlmta
      301 qaffynaiff tyalvltdfy hvpgdhigwy vlpfaagnfl gpvllgrlfd vlgrrrmias
      361 tyaisgvllt vsgwmfmhgm ltvttqtiaw mvifffasaa assayltvse tfpleirala
      421 iavfyafgta lggiigptlf gqlidtherg pvfvgyligs llmiaaavva giwgvaaerk
      481 sledvarpls aadeh
//
LOCUS       WP_175983109             207 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: HAD family hydrolase [Caballeronia].
ACCESSION   WP_175983109
VERSION     WP_175983109.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..207
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23423
     Region          3..191
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mtikavvfdf ggvlidwnre ylykhlipdd terrwfldnv ckmewvvqqd ggqtiedgta
       61 eliavypehe alirafyarw pemvsgvlee gvalvdrlea agvplfgltn wsaetfpyaw
      121 erfdvlrkfr eivvsgrvgl vkpdpqifgl mraeierhlp gvqpnelvfi ddnpmnaqaa
      181 talgwhgvhy tgalqtetkl ralnlpi
//
LOCUS       WP_175983177             338 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NAD(P)H-quinone oxidoreductase [Caballeronia].
ACCESSION   WP_175983177
VERSION     WP_175983177.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..338
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=35858
     Region          1..332
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(40..41,126,130,133,156,159..161,180..181,185,200,
                     224..225,246..247,249,271..273,321,326)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mkaieitefg apevlklger ptpapgkcev likvaasgvn rpdvfqrkga yapppgasdl
       61 pglevageiv dgdfdpkhnp fglkegdrvc allagggyae yavapleqcl pvpkglsdie
      121 aaslpetfft vwsnvfergq lgagengeee tllvqggssg igvtaiqiak algfrvfata
      181 gtdekcrace algaerainy ktedfvevvk sltndrgvdv ildmvagdyl qrelkaladg
      241 gricviallg gakaeinlnd vlrrrlvitg stlrprpvaf kaklaaklke rvwpeieagr
      301 ikpvihqvfp ardaaaahal messthvgki vldwrdda
//
LOCUS       WP_175983205             328 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Caballeronia].
ACCESSION   WP_175983205
VERSION     WP_175983205.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..328
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33264
     Region          26..321
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mksqtsgeal anndtawerl kgvqapwaws fvgtvlvwfg ivgifgfgia snvaqtalty
       61 gvfmvlvglg qmlvitsgvg nidlsvpsti alagvvgmha mggsngqial gvaaalgvgv
      121 avgianymli rllrippiia tlsssfiiqs iaitqgrqlp ppppalgafa tsrlfnvpyi
      181 alvalalsvs lavllhravy grrlsaigqn araawlagvn vhrtrclayv lssmiaalta
      241 lllaatsgga sldmgveyml isiavvvigg tlvtggkati vgvwgasmfl fltnaalnav
      301 gadagvrsiv ygvliiavtv aaggkpar
//
LOCUS       WP_175983212             275 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Caballeronia].
ACCESSION   WP_175983212
VERSION     WP_175983212.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033773
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..275
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30318
     Region          21..>110
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          190..267
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mnlrapvlpp dwvrraepie gverieawfh gsaysmhrhd tyaigrtlag vqsfnyrrsq
       61 rnslpgntlv lhpdeahdgq agtdegfqyr mvyvepalfq evlggqalpf leggvttdrr
      121 levatvallq hvsytleple qsdalaelan alaavtgtpa rtakgdflaa rrardylhan
      181 csrvvaldel eavtgrdrws lshdfrrfyg tspyryltmr rldavrhmll agtslacaaa
      241 aagfadqshm trhfsktfgl tpgrwlqvag gvprg
//
LOCUS       WP_175983248             369 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: saccharopine dehydrogenase family protein
            [Caballeronia].
ACCESSION   WP_175983248
VERSION     WP_175983248.1
KEYWORDS    RefSeq.
SOURCE      Caballeronia
  ORGANISM  Caballeronia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Caballeronia"
                     /db_xref="taxon:1827195"
     Protein         1..369
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=40127
     Region          1..>34
                     /region_name="PRK06223"
                     /note="malate dehydrogenase; Reviewed"
                     /db_xref="CDD:180477"
     Region          25..355
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mkvalvgagl igqsiahllr etgdfdvvaf drdehalali daqgiptrrv dsadtpalrq
       61 aligfdalin alpyylainv asaakaagvh yfdltedvra thairaiadd selafmpqcg
      121 lapgfigiva hdlakrlddv revkmrvgal pefptnalky nltwsidgli neycqpceai
      181 regrtqwvqp legvehfsld gieyeafnts gglgtlcetl agkvetldyk svrypghrdl
      241 mkfllddlrm stdrdglktm lkravpstaq dvvlifvtvt gmrrgqlvqd vftrkifakd
      301 vcgvpmsaiq ittagaicae ldlfregvlp qsgfvrqeqv pldaflnnrf gklyeganav
      361 atarqlaaa
//
LOCUS       WP_175983359             522 aa            linear   BCT 11-JAN-2025
DEFINITION  S41 family peptidase [Burkholderia vietnamiensis].
ACCESSION   WP_175983359
VERSION     WP_175983359.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..522
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=55742
     Region          74..438
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mnpvmpairr vvasrtgait aavfiafafe lapaalaqtv pasattatta lpapaaaplp
       61 spcppdweaq lcelksaiev lkkqhltdvd igalldatvh agiktlpyar ffnaaerrqq
      121 lddegrardg tpgigivfet rpdglhiidv ipdapaekag vrpddlvvam ndqsvvglds
      181 advvklakgd agvplkltir rgpgqatlvv apvraivrph pasakrlagd ilytrlssfp
      241 epavgnyida veaarrngpp vkgvildlri ngggalnaai gitalfagre rtamvtlerd
      301 grnrrrittn wpdyelpvmh gqdplaplqa ddwwrtvplv vlvdgqsasa aeataaalrd
      361 lgrarllgmp tygkglaqtg vdlidgtrln ltfarnlrpn gcpmdgygvv pdwlvpprrd
      421 sdvdgvllwy revdlarapy adrlapdpfa tvrdarrklr darvrakvem sksaalpqre
      481 fgtaadwqlr qalaalagrp vqtvaapaql mpaqpvcerr dd
//
LOCUS       WP_175983366             241 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175983366
VERSION     WP_175983366.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..241
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26425
     Region          1..239
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 misiknvskw ygqfqvltdc ttevskgevv vvcgpsgsgk stliktvngl epfqqgeilv
       61 ngqsvgdkkt nlskprskvg mvfqhfelfp hlsitenltl aqikvlgrsk deatdkglkl
      121 ldrvglkaha hkfpgqlsgg qqqrvaiara lsmdpiamlf deptsaldpe minevldvmv
      181 elaqegmtmm vvthemgfak kvahrvifmd kgaiveddrk ddffsnpksd rakdflakil
      241 h
//
LOCUS       WP_175983380             473 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia vietnamiensis].
ACCESSION   WP_175983380
VERSION     WP_175983380.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..473
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50434
     Region          4..473
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mipseafvsa crdaigaahv ltdphdtepf ltdwrrrykg sacavlkpad taevaalvrl
       61 anthgvalvp qggntglagg atpdasgsqa vlsvarlnrv rafdphnnti tveagvilad
      121 vqarareggr lfalslaaeg sctiggnlst naggtavlry gnarelclgl evvtpqgeiw
      181 eglrglrkdn tgydlrdlfi gaegtlgiit aavmklhplp aaqvtalaal esphaaldfl
      241 alaqraagpl ltgfelmsdf cmqlvgkhyp qlrypferth aqtvllelsd neseahartl
      301 fetlmqqafd aglvvdavva enlaqsrafw dlrehiplaq adeglnikhd iavpissiar
      361 fidetdaaiq qaapgarmvt fghlgdgnlh ynvqtpaggd tkaflaqfqt pinrivydnv
      421 hrhhgtisae hgigqlkidd aqrykspvet almrtlktal dprglmnpgk vlr
//
LOCUS       WP_175983391             411 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            vietnamiensis].
ACCESSION   WP_175983391
VERSION     WP_175983391.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 411)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..411
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41759
     Region          32..310
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 manrmpngal rwtlfaacla lpawlwpqga vlgylaqtaa lvvlalsynl qlgttgllsf
       61 ghaavagvga faaahwfnrv gaplpllplv ggvagaafgc vagllatrra gtvfamitlg
      121 igecvaaaaw svpawfggvg gvpidraggt pwggwqfgap thayaliaaw cigsalamya
      181 ltrtplarla navrdnparv aalgteprhv rlamvtcasf fagvagtltl idveiatpds
      241 vsmarsatvl iaaviggtgt ffgpalgavv ltalsvvvag vsrawalylg vlfvavvvaa
      301 prgiagvaqa cahawrrgap averwrmlcg vgagafwaia ivcaaelgya wrfaqddggg
      361 safgvwrida dapagwavaa saagigmllw gwrarlagra hdvpdaredg r
//
LOCUS       WP_175983444             288 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175983444
VERSION     WP_175983444.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..288
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30606
     Region          12..278
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mkkirgvysa prghwvgdgf pvrsmfsyqs hgahlspfll ldyagpanfe pasaprgvgq
       61 hphrgfetvt ivydgevahr dstgaggvig pgdvqwmtaa sgilheefhs eaftkrggpl
      121 emvqlwvnlp aadkmggpgy qtllngdipv velpdgagra riiageldgr rgparthtpi
      181 dvwdvrlaag gharfpiaeg rtlavvvlsg tvlvngetva reaqfvqlgr egsdvdiean
      241 gdvkllilsg epidepvvgy gpfvmnsqee iraaiddfns grfgrmpa
//
LOCUS       WP_175983479             311 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia vietnamiensis].
ACCESSION   WP_175983479
VERSION     WP_175983479.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..311
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=32755
     Region          12..155
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          168..307
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 msstpsiptl arialavdpt pealsaaryt rtllrpgmql rivcaidnpr lvlpdiprvd
       61 alltsareem treaqatlar iaalfedsgv aveqaivdts vtggtvadal asdtsawqad
      121 vlvvganphh gllrlfegav sdtltaraqc allivpagya rpsdgplqrl mfavdgseps
      181 lhavrvglgf aapttllyaa yvvdrairlt divpvraled ayraegedal arvgpllhaa
      241 gnptkrgive trptsddvah almrdavhwr aellvvgthg rrgiaawlig svarriahva
      301 qvpvllvrga a
//
LOCUS       WP_175983494             673 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia vietnamiensis].
ACCESSION   WP_175983494
VERSION     WP_175983494.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..673
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=71997
     Region          23..662
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mlfaavtpah aadppatspp aplapifvta nplgdtdpia attqlsgdal trrqadslge
       61 tldglpgvst ttygpmvgrp iirgmdgdri rllqngvaay dasslsydha vpedplsier
      121 ieivrgpaal lyggnavggv vntidnripr eaiegvtgal darygganav ragaaqveag
      181 nghfafhvda fdretgklri pgyarssalr stddadtpqp sgsvpnsdgr vhggavgsay
      241 twadgfagls ysgyesnygs vaedgvrlrm rqervafase mrnldgpftk lkfdfaytdy
      301 rhkevddget atvfrnrgye ariearhrri gpfegalgvq fgqntfsalg demlvpstrt
      361 nsvalfglee wqvapalkls vggrfehvqv dpdpagiakf adarardfna gsvsagalls
      421 ltpvwsvaan vayteraptf yelysngphd atgqflignp naskekavst dlslryasgp
      481 nrgsvavfyn rfsnylaeyn tgrivddhgd pvapgtadal deaiyrgvra efygveldgk
      541 wrafaqrght idleltadyt harnvdtgqp lpriaplrat laadygygpf garaqvtraw
      601 aqhrvpdndf ptdgytslgv llsykfrvga thwlaflrgd nltnqeirya tsvvrgfapq
      661 ggrsvmaglr ttf
//
LOCUS       WP_175983423             622 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF262 domain-containing protein [Burkholderia vietnamiensis].
ACCESSION   WP_175983423
VERSION     WP_175983423.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 622)
  AUTHORS   Bair,C.L. and Black,L.W.
  TITLE     A type IV modification dependent restriction nuclease that targets
            glucosylated hydroxymethyl cytosine modified DNAs
  JOURNAL   J Mol Biol 366 (3), 768-778 (2007)
   PUBMED   17188297
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..622
                     /product="DUF262 domain-containing protein"
                     /calculated_mol_wt=70773
     Region          1..552
                     /region_name="GmrSD"
                     /note="DNAse/DNA nickase specific for phosphorothioated or
                     glycosylated phage DNA, GmrSD/DndB/SspE family, contains
                     DUF262 and HNH nuclease domains [Defense mechanisms];
                     COG1479"
                     /db_xref="CDD:441088"
ORIGIN      
        1 mrpytrsiie lfdgkkrylv plyqrqyawk vspdlellwe dieravarlk adrqtatphf
       61 mgaivisqik tfgkqvqafe vidgqqrltt fqlllaalrd vanaygsdyg qevnkllfnd
      121 gvmetpever fklwptltdr rafvhmidpv adldtigspp kdedgvvrpa iaahawfkar
      181 iekhvmldga fdlfkleklf ealrdglaav sielegaddp qtifetlnsr gvdlsaadlm
      241 rnfifqrakg lgqehgslki ddlyakhwlp ldrwfwreed trgrqtkqrl dwmlvdhlsm
      301 kraevvsvdh lfesyrrwil ndapfpsveq elisiansaa ihrriaeqsa ddvlgrfgrf
      361 arafdvstam plvlylatdg eagndlanal amieafilrr dvcglttkny nrlfidvldk
      421 vrssrlaplh glevqlslgd sdinrwpsdd ewkaawlahd qykssrqprl ryvfeaieka
      481 krsalseeie ikseltiehi mprkweqhwp vpgfdhvpeg evdldrlaae meraqainkl
      541 gnltlltral natvsngpfs vkmpavraha slalnrelng fdhwnegtil ergralfdva
      601 qklwrgpler ekalaadasi sa
//
LOCUS       WP_175983534             404 aa            linear   BCT 11-JAN-2025
DEFINITION  cation:proton antiporter [Burkholderia vietnamiensis].
ACCESSION   WP_175983534
VERSION     WP_175983534.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..404
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43649
     Region          13..390
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mksafsflpn wplapdavfw aglalfaagl cgelcyrawr lpritgyavi gliagslgfg
       61 vidastdets rllidvalgl llfelgsrld lkwirrnpwl iasslaeatl tfvlvlfvml
      121 algvsgmval vlsaiaiats psmviqlkte lraegqvsqr litltalnsv yaivltklvt
      181 swlhqeaygn vfatilqpvy liagsfivay lvaracnylf rhmtstmrde hsfvalfglv
      241 mlaiavaqal klstlltlll agiivknlea rpqlwpehfg tagwlltvvl fvltltsftw
      301 gdialgglla ivlivtrlva klagvvafak psglgmkqgv algialtpms alsyllvddt
      361 yqmypnfdph lraivmctvv vlqlvspfvv yrclsavser sdrn
//
LOCUS       WP_175983601             270 aa            linear   BCT 11-JAN-2025
DEFINITION  ComF family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175983601
VERSION     WP_175983601.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..270
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=28521
     Region          18..240
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mdgrssarvt rvvlsharml lthviaaalp nrcalcgnls hnvicdacda aywnearlrc
       61 evcalplgvg rastrrpggr hggadatsay ccdgcratpp pfdatlalad yrapldglar
      121 glkfrarlal gaefaarlas riddtdtlrr asgfdviapv plargrlvar gynqawaiar
      181 plarqlgvra daallervte tapqsrldrr arrdnvsaaf avtrelagrh valvddvmts
      241 gatlaaaaha lkaagavrvt nlvalrtard
//
LOCUS       WP_175983608             395 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia vietnamiensis].
ACCESSION   WP_175983608
VERSION     WP_175983608.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..395
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41064
     Region          22..389
                     /region_name="MFS_YajR_like"
                     /note="Escherichia coli inner membrane transport protein
                     YajR and similar multidrug-efflux transporters of the
                     Major Facilitator Superfamily; cd17472"
                     /db_xref="CDD:341025"
     Site            order(29..30,33..34,37,71,121..122,124..126,129,151,
                     154..155,158,221,224..225,228..230,233,260,264,308..309,
                     313,317,340,343..344,347..348,351)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341025"
ORIGIN      
        1 msnpsatssr mtapelrata slaaifalrm lglfmimpvf svyaktipgg dnvllvglal
       61 gaygvtqsll yifygwasdk fgrkpviatg llifalgsfv aafahditwi ivgrviqgmg
      121 avssavlafi adltseqnrt kamamvggsi gvsfavaivg apivfhwvgm sglftivgvl
      181 sivaigvvlw ivpdaarpvh vpapfgevlh ngellrlnfg vlvlhatqta lflvvprllv
      241 dgglpvashw kvylpvmgla fvmmvpaiiv aekrgkmkpv llggilaili gqlllgsaph
      301 tilivaailf vyflgfnile asqpslvskl apgsrkgaat gvynttqsig lalggiaggw
      361 llkhggantv fyacsglvaa wliiaasmka lprka
//
LOCUS       WP_175983665             156 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia vietnamiensis].
ACCESSION   WP_175983665
VERSION     WP_175983665.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..156
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16015
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 myrrifaald gsrgsrlald eaislaresg giviamcvvs daprltdvds gyveqrdpag
       61 ldadkaaiav adaetafqls gvrgiaqtve angqdisdvl araaaecdad livmgthgrr
      121 gvrravlgsv aeallreadr pvlvvregpg agagml
//
LOCUS       WP_175983785             377 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175983785
VERSION     WP_175983785.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..377
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39960
     Region          1..366
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfsftdeqq qfadalrryl geqygfdarq aivrsdagvs eaqwsafael gltalpvpda
       61 qggfgggpvd mlvamqelgr alvvepywat avavealrva gsgsgddaal leavaqghkr
      121 lavafhepha rydlyelgth aheqggacrl sgtksvvqhg aqahawivpa rvdgggiglf
      181 vverdaagvt ltdyrtidgq raatiafddt parqlaggvr daaaleqiad yatfllcaea
      241 vgaldelnra tveytktreq fgvpiarfqa lqhrmvdmli haeqarslty laavryagdd
      301 adarrkavsa akarvgaaar fvgqqavqlh ggmgvtneva aahlfkrlsi iettlgdtdh
      361 hlariaalpd faqadaa
//
LOCUS       WP_175983835             267 aa            linear   BCT 11-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175983835
VERSION     WP_175983835.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..267
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29575
     Region          94..248
                     /region_name="CE4_NodB_like_5s_6s"
                     /note="Putative catalytic NodB homology domain of PgaB,
                     IcaB, and similar proteins which consist of a deformed
                     (beta/alpha)8 barrel fold with 5- or 6-strands; cd10918"
                     /db_xref="CDD:213023"
     Site            order(100..101,156,160,204..206)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213023"
ORIGIN      
        1 malrmlvcll llscvpplra addagadapq pqpqrvlila yhrfattrvd smtvridtlr
       61 dqlqaidang yrivpladvv rwqrgdaval paravaitvd dghrsvydvl rpllaahpmp
      121 vtlfvypsai snagyamtwd qlralgqsad vaieshtywh pnfhterarq tpadyrrfvs
      181 fqlrrsrerl eaeigrpvtl lawpfgvhda qtdeqaaaeg yvaaftidar pvrrtdsama
      241 lprylmtdac dtrcmngllr saggshd
//
LOCUS       WP_175983892             375 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia vietnamiensis].
ACCESSION   WP_175983892
VERSION     WP_175983892.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..375
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39595
     Region          1..362
                     /region_name="LhgO"
                     /note="L-2-hydroxyglutarate oxidase LhgO [Carbohydrate
                     transport and metabolism]; COG0579"
                     /db_xref="CDD:440344"
ORIGIN      
        1 meqtdcvvig agvvglaiar elaardreti vleaadaigt gissrnsevi haglyyprgs
       61 lkatscvhgr dllyrfceth hvphrrvgkl lvatsaaqvk qlkaiaaraa engvldllpl
      121 traeaqtlep alecvealfs petgivdsrq lmlallgdaq rnaatcalqs pvesidvlrg
      181 grfvvrtgga apteieaacv vnsaglgaqa larrtrgldp rwvpplylar ghyfslaarv
      241 pfshlvypmp draglgihlt ldlagqarfg pdvewvdalr ydvdparaqg fyasiraywp
      301 glpdgalqpa yagirpklag pgeppadfvv qgpaqhgvrg lvnlfgiesp gltaalalaq
      361 rvgdiasrts rapha
//
LOCUS       WP_175983899             462 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia vietnamiensis].
ACCESSION   WP_175983899
VERSION     WP_175983899.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..462
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46122
     Region          25..450
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,151,
                     154..155,158,280,283..284,287..289,292,320,324,376..377,
                     381,385,401,404..405,408..409,412)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mpdtgkrtaa agrvatrrgv tlvtlciavl vaqvdtavvn latraigayf hagvgalqwv
       61 vdsynltyav lllsggllad lygrrrifia gaavfsvasl lcalapsvav liaaralagv
      121 gaalllpasl aivrvvwrdp vergralgvw aacngvamai gptlggvlir hfgwrsiffv
      181 vvplsvaail lairavpess dsrgrhfdgg aqvtgalalg slayaaivfr darigsaiag
      241 cvaiasfigf vaierrhrda alvpldlfra gafrgaiaat tgmtfgmygv lfllplmwqs
      301 tgrldstgag lallpmalvf vavspcsgrl serigtrttt aggvaviacg laaigasaas
      361 pqllgaeigl altglgmgia tgplmtvavg avdaarsgta salvnvarmt gatlgiavlg
      421 tlfavahggi aglrvamlgg aavqlagaag saiavrgver aa
//
LOCUS       WP_175983916             548 aa            linear   BCT 11-JAN-2025
DEFINITION  S8 family peptidase [Burkholderia vietnamiensis].
ACCESSION   WP_175983916
VERSION     WP_175983916.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..548
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=54574
     Region          235..514
                     /region_name="Peptidases_S8_13"
                     /note="Peptidase S8 family domain, uncharacterized
                     subfamily 13; cd07496"
                     /db_xref="CDD:173820"
     Site            order(242,310,314,381..383,409,411..412,482)
                     /site_type="active"
                     /db_xref="CDD:173820"
     Site            order(242,310,482)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173820"
ORIGIN      
        1 mranrfdfal artaharvla gmlsaaallp iagcgggggd gsspataapa paptpapapa
       61 papapaptng ttcaaqqaav qmaaqtvapt eppvdhlivr lkpstgtram aaldvgtrld
      121 aviqrsmtrw saptttgaar ayaaattsln vqvertlang aavlsigqri asddaaalaa
      181 afaadsdvdy aepdhpmhvr dtpsdpsysq qwylsdpavg intppawtrt kgaptvvtav
      241 ldtgyrphpd lvanllpgyn fisnantsnn gqarsndatd pgdwvtqqel ddatgpyyhc
      301 asepnnsswh gtrvmgviga ganngigvag vswlgrilpv rvlgkcggtt sdiadamrwa
      361 agipvngvpt nptpakvinl slggvgacst tfqqaiddvn akgvtvvvaa gndglstgld
      421 qpancrgvis vgatdatgrr asfsnfgadv slsapgvgil stansgttvp gadsygtasg
      481 tslatpqvsg ivslmlavng nltpvqiqqk lqggaraaml paattsctal pagagiadag
      541 aavtaaaq
//
LOCUS       WP_175983975             159 aa            linear   BCT 11-JAN-2025
DEFINITION  rubrerythrin family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175983975
VERSION     WP_175983975.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Cooley,R.B., Arp,D.J. and Karplus,P.A.
  TITLE     Symerythrin structures at atomic resolution and the origins of
            rubrerythrins and the ferritin-like superfamily
  JOURNAL   J Mol Biol 413 (1), 177-194 (2011)
   PUBMED   21872605
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Li,M., Liu,M.Y., LeGall,J., Gui,L.L., Liao,J., Jiang,T.,
            Zhang,J.P., Liang,D.C. and Chang,W.R.
  TITLE     Crystal structure studies on rubrerythrin: enzymatic activity in
            relation to the zinc movement
  JOURNAL   J Biol Inorg Chem 8 (1-2), 149-155 (2003)
   PUBMED   12459910
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   5  (residues 1 to 159)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099327
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..159
                     /product="rubrerythrin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17257
     Region          31..>143
                     /region_name="YotD"
                     /note="Rubrerythrin [Energy production and conversion];
                     COG1592"
                     /db_xref="CDD:441200"
ORIGIN      
        1 mkrfkqqmpv aalaalsfva apafadgplk dqtkqnleaa mhgeayahlk ylayaehark
       61 sghpeiaklf desanveane hfareaealn laksdeanla dgmagehyen tkmyvkfaeq
      121 adaagdkkva amfrqiaade gdhyaafrav seklrtask
//
LOCUS       WP_175984028             276 aa            linear   BCT 11-JAN-2025
DEFINITION  SH3 domain-containing protein [Burkholderia vietnamiensis].
ACCESSION   WP_175984028
VERSION     WP_175984028.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..276
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28135
     Region          5..96
                     /region_name="YraI"
                     /note="Uncharacterized conserved protein YraI [Function
                     unknown]; COG4991"
                     /db_xref="CDD:444015"
ORIGIN      
        1 msktmirslc vvlfgiaaap giaaaqssay tnsvaalyag papdypvvaq lppgtavdvf
       61 gclsdyswcd valpgvrgwi daeqldypyq gyyvplieyg aivgvpvtgf aigaywdryy
      121 rkrpwfhdrd rwehraepri gpgglppgqg hpqpggpiqr apggappaqh dtrpsatrgg
      181 wggpnrmpap qampqpapvp haapqpgpaa aphpapppgp apgsaivrpa pgpgggprmp
      241 ppqgnpgggg yggrsqgggn aggghgggvg ndefrr
//
LOCUS       WP_175984031             445 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia vietnamiensis].
ACCESSION   WP_175984031
VERSION     WP_175984031.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..445
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=47794
     Region          62..424
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 maaaaalvgi alsaapstra appettllag appsrvvgti gigtpqvagk idaatarfap
       61 dptlvalgrr iffdsrlsep rgmscagchd parafaptls aaalagpgvp egsrpgrfsr
      121 rnapsllyvr yvprrhfyqd ddapapapfg glfddgradt laeqirgplf dpnemnnrsp
      181 aallrkvdgt elagdlaarf gasvrrdpeq lvqalgsame aylqsdemap ftsrfdaflr
      241 traplapaem rglalfrnpd kgncmschtl setssrpers lftdfgydai avprnralaa
      301 nrdprhfdng lcdtaarlrw peptqwcgyl rtpglrnvav kqtfmhngvf rtlrdavafy
      361 ntrstdpafw yhgartfddv pvayrgninv nstplnrrpg tppaltdaei ddivaflgtl
      421 tdaryaelvp rggsdgvarg aartr
//
LOCUS       WP_175984072              96 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl carrier protein [Burkholderia vietnamiensis].
ACCESSION   WP_175984072
VERSION     WP_175984072.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 96)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..96
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=9963
     Region          3..78
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 msnetretvr tflqgltnlp fidaeenlfe rglltsltam avvhwiettf gfavegddlt
       61 qanlgsirai adyvdarltg aaavaaggsa catnaa
//
LOCUS       WP_175984112             343 aa            linear   BCT 11-JAN-2025
DEFINITION  C40 family peptidase [Burkholderia vietnamiensis].
ACCESSION   WP_175984112
VERSION     WP_175984112.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..343
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=35187
     Region          <6..175
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mlriwvpvav vsllaacssv ppqsasrsag mkittprafp apanfpnfvd hsvgqeeisi
       61 qamslvgvpy rwggntptsg fdcsglvryv lgraadvnlp rttadmssrg asidpdqiap
      121 gdliffnttg rphshvgiyv gklrfvnaps tggtvrldyl tnpywakrfd girrvapprg
      181 tptpfdapiy darrdapaaa tapvvaaaav rrpayasspa rataqaavpa vstttaaaaa
      241 pyepaprmsa pvssaggdtm amtpvlppag pseevgtqip ttaltaaqaa afdaeppsam
      301 papsspgsae pvqvlrastq aapvsprtst addpiarfan gsy
//
LOCUS       WP_175984123             431 aa            linear   BCT 11-JAN-2025
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175984123
VERSION     WP_175984123.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..431
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=46205
     Region          5..430
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 mtdqassnwr letiavhggy rpdpttrava vpiyqtvaya fddtqhgadl fdlkvqgniy
       61 trimnpttdv leqriaaleg gvgalalasg qaavtysiqt iaeagdnivs asslyggtyn
      121 lfahtlpqyg ittrfadprd pasfdalida rtkaifaesv gnplgnvtdi aaladiahrh
      181 giplivdntv pspyllrpfe hgadivvhsl tkylgghgts lggaivdsgk fpwaqhadrf
      241 krlnepdvsy hgvvyteafg aaayigrarv vplrnmgaai spfnafqilq gietlalrie
      301 risdnalkva qhlarhenve wvnyaglpdh pdhplvaryl sgrapgiltf gvkggrdgga
      361 kfqdalklft rlvnigdtks lathpastth rqlspselak agvkeetvrl sigiehiddl
      421 ladlnqalaq l
//
LOCUS       WP_175984167             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia vietnamiensis].
ACCESSION   WP_175984167
VERSION     WP_175984167.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33232
     Region          7..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..292
                     /region_name="PBP2_LTTR_like_4"
                     /note="TThe C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08440"
                     /db_xref="CDD:176131"
     Site            order(111..112,114..115,118,122,124..130,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176131"
ORIGIN      
        1 mginfdltdl qafravvelg sfrkaaesis isqpalsrri ekledalgvr lferttrsvt
       61 lttvgrvfap saeqllddld vallgirdvs ssrlghvtia cvpsvayyfl pnviasyhrr
      121 fprirvklld asanevlsav isgeadfgvs fmgsqepeve frlllqerfv aacrrdhpla
      181 gkkrvtwnel yaydyvsvdk tsgnrllldq altavapraa svcetrhvtt mlglieaglg
      241 vaavpsmamp grdhpvltsv plvepvvkrr vgivkrrgrt ltpaaeafhr avlnarrgaa
      301 agseaaa
//
LOCUS       WP_175984180             280 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia vietnamiensis].
ACCESSION   WP_175984180
VERSION     WP_175984180.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..280
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=31530
     Region          147..>233
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mqrrypggqg grsrssdwqe rderayrgvg rgitdepspw peeayesayh rfrsedvgpe
       61 dwgsewsera arspaeersa gwrdapagar epgrgygerr rdpqrtgger ggepqwrtgg
      121 yrgergydar dprdgrpgea pdlsrfggga mrartgpkgy trsdertred vcerlarale
      181 idvsdvsvev rdgcvvlegt vptrwmkhdi edlsddcmgv rdvenrvrvr rdgehdtgtv
      241 lrpsqrtvtp trpnpntrep epesgsarrd engadreprh
//
LOCUS       WP_175984219             448 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia vietnamiensis].
ACCESSION   WP_175984219
VERSION     WP_175984219.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..448
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48447
     Region          27..435
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(40..41,44..45,48,80,139..140,142..144,147,167,
                     170..171,174,268,271..272,275..277,280,308,312,363..364,
                     368,372,388,391..392,395..396,399)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mptitqtaaa paaadlseda vyrrvmrril pllllcyvva yldrvnvgfa klqmlddlsl
       61 sdgvyalgas iffwgyflfe mpsnlllhry garfwiarim itwgivsssm afivplaqff
      121 hvqtstmfya lrfllglcea gffpgvilym nywfparrqs vamsgflvai plsltlgsvv
      181 sgwlmeqthg lsgmsgwqwm llleglpsiv vafvvlaflg dgpqsakwls adekallarn
      241 lereaahksh svgvalrspr vwlltfillt fntgfyglaf wlpsiirasg vrsplhigll
      301 taipyltaif amlwnashsr ktgerrlhaa ipaliggvgl iasaacaqnv alsivfltia
      361 tcailalmpi ywtfpgqils gtaaaagial insvgnlsgf tgsmitgiak emtgninngt
      421 yalgacllis cvlilsiprs ilvppaer
//
LOCUS       WP_175984266             382 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia vietnamiensis].
ACCESSION   WP_175984266
VERSION     WP_175984266.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..382
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40914
     Region          1..370
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masismrrvq kaygehapvi rdvdldigah efcvflgpsg cgkstllrmi agledlsdge
       61 lsidgrrvnd vpaaergvam vfqsyalfph mtvyenmafg lklarvqkae idrkvrdaar
      121 ilqldtller kpkalsggqr qrvaigraiv repgvflfde plsnldaalr gqtrieiakl
      181 hrqferasvv yvthdqteam tladkivllh tgadtarhgs iaqvgapldl yhhpasrfva
      241 gfigsprmnf lpavvvacda rrttvtlvas gesftlprdg salapgaavt lgirpehltl
      301 gaapdattla rdvalverlg eqtyvhldqp ggtpliakvp gdaavhager vhvhaaaaac
      361 hlfnedgrav pacadlpvhh ya
//
LOCUS       WP_175984273             337 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Burkholderia vietnamiensis].
ACCESSION   WP_175984273
VERSION     WP_175984273.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..337
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=37688
     Region          31..304
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mslptcpdtp arpeekdlfn rgasdwivsp dtafdawlam qeyrrssadv yraqwgafla
       61 wlranqknla tvdtasianf vgelpirktq rmrylrlier vldhirqtel astnparfia
      121 qdgeatwrha rdneptgflt paerakllay lfspigvsgs aywkerrdra lvaaflgagv
      181 ktgearvlti scintsgtsl hipsthpdfa rethlasfai alleawlver khqniagdlv
      241 fpashagrpm hkatmlraid aivesaglas srtaraspqt lrntyaaelf ehdvppervg
      301 kwlgfvrpis snrlhrawkn wreellngde adrdeth
//
LOCUS       WP_175984279             320 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia vietnamiensis].
ACCESSION   WP_175984279
VERSION     WP_175984279.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..320
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34635
     Region          26..313
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mthtnvahsv deaegdvggr rsrksreigv vvfegfslla aaavcevfea aneiyapqaa
       61 slplydvrfy ssrggnvvws savsvrtfac daaladtfda vfvaggegar raardarvid
      121 wlrvvvpkag mvetisegrm lidaarsgah asdavvvdyd gygparaals lverdlggda
      181 vraiasrlal ndalvtaehd darhgapver vraaadwlrr ncdrsisvsd avrvaamser
      241 nflrhfkqei gttpsefllq vrlertvqll metdmpigti arqcgwgngd rlakifrrhl
      301 dvtpsqyrlq arsngdvrpi
//
LOCUS       WP_175984291             434 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia vietnamiensis].
ACCESSION   WP_175984291
VERSION     WP_175984291.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46914
     Region          24..425
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,156,
                     159..160,163,258,261..262,265..267,270,298,302,353..354,
                     358,362,378,381..382,385..386,389)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 matsthslpg ssgafeeaty rkvswrltpl lllcyvvayl drvnvgfakl qmasdlnlsd
       61 tvyglgagif ffgyflfevp sniilhkvga rvwiarimat wgvisiltmf vttpamfyvm
      121 rfllgvaeag ffpdvilylt ywypahrrgr mttffmtava lsgviggpls gfilkafngv
      181 sgwhgwqwlf llegipsvla gvlvffaldd riaraawltd eekallarnv daeeatkqdl
      241 algavmsspr vwlmaliyfs fvmglygvgf wlptiikatg vtdtlkigll saipyaaavv
      301 amiliarsad krrerrwhla ipaaigalgl vlsvmwahet alamlgltla tigilttlpl
      361 fwslptaflg gaaaaagiam insignlagf lspymmgwlk qatgandagm yllaaflvlg
      421 gllalsvpkr lvdk
//
LOCUS       WP_175984320             319 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia vietnamiensis].
ACCESSION   WP_175984320
VERSION     WP_175984320.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..319
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33675
     Region          54..292
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mslkvalavl svlvaaalla ahsplrllna ltptntfrlf adipygpger qvldvylpar
       61 vardwptepn agapvvvffy ggswqsgrrn dylfvgeala srgfvavvpd yrtypattfp
      121 gfiddaarav awarghaaaf ggdprrvflm ghsagaqiaa llatdgryla asemrsseia
      181 gviglagpyd flplrdatle rifpddrrga sqpirfvrgn eppmwlavae ndtvvepgnt
      241 drfaralqna gdsvvvtryr hlthaalvgv lgaplrraas vlddlsafvg ragrasnagv
      301 asgdakpraa tvaspvsaq
//
LOCUS       WP_175984327             317 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia vietnamiensis].
ACCESSION   WP_175984327
VERSION     WP_175984327.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..317
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34985
     Region          2..307
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mrriglvlvp qfqvmsllal svfdianlra grslyevsvi sedggpveas fgmcastrpa
       61 haaelhtvfv gaslskpplt dgmrqllldl sgkvermasi clgafllada glldgrratt
      121 hwayvdqfre rfpavsvekd cifvrdgriw ssagmstaid malamleedl gadaalevak
      181 dlvierwrrs gaqpqtsvll ehparsnrih dvityirqhl gtdltvekla dvarmskrqf
      241 trrfkdetgl tpakavdrir letardflts sswtidtiar etgyadperm rrsfvrafgq
      301 ppqalrrpaa tepvdsd
//
LOCUS       WP_175984337             190 aa            linear   BCT 11-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Burkholderia vietnamiensis].
ACCESSION   WP_175984337
VERSION     WP_175984337.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..190
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=20770
     Region          <27..116
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
     Region          43..73
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          78..101
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mennpssilc pddrmavlve amqssdesal halnnalerw pddyrlwflr gavhagsqhy
       61 eaarndfgvs qrltpdfpia gfmlgflhlt hghvdravea wgpldalsad dtlrvlktgl
      121 lnlvndrfal aseqlragia sntkyplinr yivdvlqhve sivgatpash apsektgilp
      181 eidsaystpr
//
LOCUS       WP_175984370             276 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia vietnamiensis].
ACCESSION   WP_175984370
VERSION     WP_175984370.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..276
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=29015
     Region          9..247
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mrarpivavs adrvlrgahq nhtagekylv avvdgagala fvlpalgarq pvdaivasld
       61 gllltgshsn vephhyggpa saadtlhdaa rdatvlplvr aaidagvpvl aicrgmqeln
      121 vayggtlhqr lhasvgfhdh rerdgdpler qygpahrvrf apggllqria rgahdamvns
      181 lhdqgiarlg aglaveasap dglieavsvr garafalgvq whpewrfaer plsrdifaaf
      241 gaacrarmth rlhaaggamp sreasdidtd tdtdtd
//
LOCUS       WP_175984384             194 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175984384
VERSION     WP_175984384.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 194)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 194)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..194
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=20983
     Region          4..135
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(9,11,72..73,76)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            11
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(71,116..117,119..120,124)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(77,82..83,112,115..116,119..120,123,126)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(101..103,112..113,116..117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(101,117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(125,131..132)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          147..188
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
     Site            order(148..150,182..183,185..187)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 msrtfayarv sttdqtatnq lreieaagfn vdkrrvvtes isgsvsadqr pgfadllrrl
       61 eegdvlivtk ldrlgrnamd vratvealae rgirihclal ggvdltsaag rmtmqvlnav
      121 aeferdllie rtqagiarak aegkamgrps altkqqrdev rqqlsggasv aslakaygts
      181 rqtimrvrdn thvl
//
LOCUS       WP_175984449             254 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175984449
VERSION     WP_175984449.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..254
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=27387
     Region          9..252
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mktdelictr idadvvqlti drppanalne plitalmsvf rdfarhdvpp givltgagek
       61 ffcaggdine vadhelalsr meafhafltq leqypsplvc avngyavgag femalhadyv
      121 vasaesrlgf peinhgllpa akgmrhaaal lgrraarsll fsgelitage alaigavdti
      181 sahdetlrda lakcralcak drqlfaaikr tlresprmsd eallqmtldd lrgylgnart
      241 adarsrflnr nkka
//
LOCUS       WP_175984464             147 aa            linear   BCT 11-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175984464
VERSION     WP_175984464.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..147
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=15596
     Region          <49..129
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mtkttvikri gkneivlsve neidsqsalt adiqysrrla daiqraassg vdfrnadfsk
       61 ldlrrlnltg ldlrgadlsg svldstllaf anladanlcg irmvsgslah anlrganlig
      121 acisltdmtg alfwpvdder kcaggkr
//
LOCUS       WP_175984480             345 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia vietnamiensis].
ACCESSION   WP_175984480
VERSION     WP_175984480.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 345)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 345)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18991652
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..345
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37718
     Region          21..137
                     /region_name="cupin_YkgD-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to Escherichia coli YkgD, N-terminal cupin domain;
                     cd06995"
                     /db_xref="CDD:380399"
     Region          <132..338
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          248..331
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqgeffnail aqihaqtshm dmldrllsmm pvtgrldvrc hfgspwridh pesnerelpy
       61 hillrgeavv egetggadep tlrmkagdiv vfpsgsahrl hdgsgdapra vqerhqnglt
      121 ittngsadas idvlcgrfvl pavpqqllrd hlprrlivss vaagdgqtrd aafaatrlar
      181 vielmreeal eqragsaavv dhlsgalfal tlrsasesgh aprgllalaq rhrlqpalta
      241 mfdepekpwt laqlaerchm sratfarhfd eaisrsatdv lteirmalag rklaqttmsv
      301 aeigetvgyr seaafqrvfk rqvgmtpakw rmqatriaap earaf
//
LOCUS       WP_175984516             955 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            stabilis].
ACCESSION   WP_175984516
VERSION     WP_175984516.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 955)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 955)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..955
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..955
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=103902
     Region          8..822
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mlrafvsald qnnrairfhw grhqealahv lvpqsvdlte glctgieghl tclssrpdlp
       61 lsaflglpls vqlvtdrgep ypvngiitdv ragqsdgslt cvqltlrdal nileqrvnsr
      121 tfrsmsvpdi leallhewqq rssalaqafd felvldrnqy pkreqtrqad esdaafirrl
      181 crrdgifwya ragkhdgast dtpvhtlvfc ddptklpqaa agrvsyhrga qsrerdsvtl
      241 wstarvltpg svrrsswdyk tgrmaqseqe tivdqgetgn dlaklladsv idvphagdsd
      301 adqerlakar ilahehraec vyassdvrdi spgfwftllg hpevdtrpde qrqfvvtslh
      361 hratnnfsks lderaqalfa asrwsfdalp aedgagvrye ntfmcvrrgv pltpaydprv
      421 dlppvhpfta kvvgqdgeev hcdelgrikv qilglraddh thaqgagasg terdsawvrw
      481 vspwagpnyg mdmlpragme vlidhlhgdp dkmvvtgvlh ggpnmpttfs htgslpgnry
      541 lsgiktkevk anrynqlrfd dtpgqissql asehtytqln lgylteprdd gkgaprgdgl
      601 eartdaqavi raakgvyvta qqqgraegkm lertalqtli eqlqdlvrnl gdasaandad
      661 ntdlarieki asqikgwdag snvdqgagag gapmvaiegp agvtvvsqda mvlgaqtnid
      721 avsagntqis agrrllmrvg dwmsafaakg mtlvtadgkl rieahkedvv vkaarriile
      781 ageeivfrsp kvstqasdea singgssysq wngggvvhgt sgvwrehaas hslvgpdnkp
      841 vkapdpltfk eleqqdslav vlrshpndgr playepytly kgaakiadgv tdehgqliis
      901 nhqkgtssyt vklhngheie vpvkeggltd ddqlaaqgwr avdgepesrq rhaeg
//
LOCUS       WP_175984532             734 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia stabilis].
ACCESSION   WP_175984532
VERSION     WP_175984532.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..734
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79976
     Region          33..717
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 msasssasth aggplaawya afgdwartdg aawlylfkal laafiatgvs mrldlpapkt
       61 alttvfivmq pqsgavlaks fyrvagtifg liatltfvgl fpqqpqlfll avalwvalct
      121 agaarnrnfr sygfllagyt taliglpasq hpdgafmsam trvaeimvgi vsagvvsalv
      181 fpqttgeqmr ttvrkrfgsf vdyvasalsg kldrahiesi htrfvadvvg feaarsmavf
      241 edpdtrmrsg rlarlnsefm sassrfhalh qwmnrlhaag aqaaidaiep yfreiaplll
      301 tpagepvrts tdagqaaeql lawrdalprr iratraalet qpdfplldfd taaellyrfi
      361 tdlheyaaty aslstather erwieryepr tnvtamviaa irtatvilll gwfwietawp
      421 sgvtltltaa atcalasstp rptamsaqmg mgtalavctg flltfgiyph idgfpllcva
      481 lapllaigiy mtlkpklagy gmgyliffcf lagpdsithy dptsfmndal alvlsmlvsa
      541 iafavlfppt apwlkkrlfa dlrhqavaac harlaglrtr fesgardlmy qahtlsadqp
      601 dvqrdalrwm favletgnaa idlrhelaal psdpryapam pwrraietmr aalstlftkp
      661 saerfdatla atnaaidatr qtldafepsr derhrlqril shlhfvrtal ldpesplepl
      721 nrnrpvrpqp gass
//
LOCUS       WP_175984550             305 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase, partial
            [Burkholderia vietnamiensis].
ACCESSION   WP_175984550
VERSION     WP_175984550.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         <1..305
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
     Region          <51..132
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          201..303
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 tyggsflyhm dnnqvvvgfv vglgytnpyl spfeefqryk thpsirafle ggkrvsygar
       61 aitaggllsl pktvfpggal igddagflna srikgshaai ktgmlaadaa fdavqagrqs
      121 delhaypdaf qqswlytely rarnfkqwma kglylgtlmv gleqkvmggn vpwtlhhkha
      181 dhemlkpasq ctpieypkpd gkltfdrlss vfisntnhee nqpahltlkd asvpvnvnlr
      241 tyagpegrfc paavyefvkn ddgsdrlvin aqncvhcktc dikdptqniv wvtpeggggp
      301 nypnm
//
LOCUS       WP_175984690             533 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia stabilis].
ACCESSION   WP_175984690
VERSION     WP_175984690.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..533
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57032
     Region          10..448
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msttsslnle gklrrdagii gllfasttsm vgsgwlfgay hasriagpls igswvlgaii
       61 imlialcfae laamfprsga lvhmshashg vglgriwcgl lflayvpvpa veaeaivtya
      121 nnylpwfiqp gsaglltaig fmacagllgi mallnlmvir wllsvnstit wwkilvpllt
      181 iaglmgasth wgvmqaapds yhlsgmftal paagivfsyl gfrtaidlgg esanphrnip
      241 lavigavlla aviyillqia fiyalapadl vagwnhlsfk gemgpfagla atlgmgwmat
      301 llyidayvsp ggtglmyvtg gsrilfaage ldagprmltr lnankipwva vlimwavgvl
      361 fllpfpawqq mvsyitsitv ltyglgpval lvlrrnmpdl qrpfrmsgag liapiafvcs
      421 nlviywtgfk tnnflfslva igfvlyalhh hvvlrrsard fgwkhiawll pwfgglwlls
      481 wmggiggglg vigfgwdill vavwslvvla lamrsaldag etsemmgrmn ets
//
LOCUS       WP_175984706             392 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia stabilis].
ACCESSION   WP_175984706
VERSION     WP_175984706.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..392
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=41676
     Region          50..343
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mtqghgiaiv gagpagcaaa ialmqagagp vllidaagrd dsggareaga rrprfgeslp
       61 pdirlvfaal glqpafdaqg fdpccgsass wgadalgynd flfnphgfgw hverrrfdal
      121 lrdcairagv qwktgrvehc satgngvrlq lalpggdtec fdaafvvdas ghaacvaram
      181 gaerldgdrl vcvsacvpld adsglgqrsl leaveygwwy aarfapdeai vvvatdaqml
      241 crhalqqpas whaclrgtrh vaaalgdgvr dapstltvrq arsarlsrca gprwlaigda
      301 aasfdplssq gvikamldgv aaareiagdr dgraiaarhe qrigerfady trmrddfydq
      361 errwanapfw lhrrhrdttt pagvlhatet qp
//
LOCUS       WP_175984772             386 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein, partial [Burkholderia
            aenigmatica].
ACCESSION   WP_175984772
VERSION     WP_175984772.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia aenigmatica
  ORGANISM  Burkholderia aenigmatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Burkholderia aenigmatica"
                     /db_xref="taxon:2015348"
     Protein         <1..386
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
     Region          <1..346
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 hhgkqytsqa eesadaqhgt yygyeavlvp ddaewraepl phpridgpqp avvvgpegee
       61 iytdeygrvk vqfpwdrqgq hnehsscwir vaqnwagalw ghmaiprigq evivdffdgd
      121 pdqpvitgrt ynclqlppye lprhktrmti ksqthkgegf nelrfedeag qeeiyvhaqr
      181 dqnihvnhde ttfvgndrse qvehdetiai gndrketvgh deqvtigrdr rhdigqdgfl
      241 tigcnhtitt gkdrteevgn hrrdktaanh tvdigghleq rvqgrvevea gqaiqhrtkv
      301 yeirsaetvv ikgpggtlri dssgitlngv airvkgpmtq qgggaspipa pvgvpapgqp
      361 fdvlcmkrtd gscprsdcpc gnfrgn
//
LOCUS       WP_175984785             249 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Burkholderia aenigmatica].
ACCESSION   WP_175984785
VERSION     WP_175984785.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia aenigmatica
  ORGANISM  Burkholderia aenigmatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia aenigmatica"
                     /db_xref="taxon:2015348"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26365
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkilvpvkrv vdynvkvrvk sdntgvdian vkmsmnpfde iaveeavrlk eagvatevia
       61 vsvgvaqaqe tlrtalaiga drailvestd gveplgvaki lkalvdkeqp qlvilgkqai
      121 dddsnqtgqm laalaglpqa tfaskvtvad gkatvarevd ggaetlsltl pavittdlrl
      181 nepryvtlpn imkakkkple tvkpedlgvd vaprlktlkv veppkraagv kvpdvktlve
      241 klkteakvl
//
LOCUS       WP_175984786             311 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Burkholderia aenigmatica].
ACCESSION   WP_175984786
VERSION     WP_175984786.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia aenigmatica
  ORGANISM  Burkholderia aenigmatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia aenigmatica"
                     /db_xref="taxon:2015348"
     Protein         1..311
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31538
     Region          2..310
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtilviaehd nasikaatln tvaaaakigg dihvlvaghn aqaaadaaak iagvskvlla
       61 dapqlevgla enveatalni akdyshilap ataygkniap riaakldvaq isditavdsa
      121 dtferpiyag naiatvqssd pikvitvrst gfdpvaaegg sasvekieaa adagksqfvs
      181 revtkldrpe ltsakiivsg grglgsgeny tkvlepladk lsaalgasra avdagyvpnd
      241 yqvgqtgkiv apqlyiavgi sgaiqhlagm kdskvivain kdpeapifsv adyglvgdlf
      301 alvpelvael g
//
LOCUS       WP_175984805             315 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: electron transfer flavoprotein subunit alpha/FixB
            family protein [Burkholderia].
ACCESSION   WP_175984805
VERSION     WP_175984805.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..315
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31960
     Region          2..314
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtilviaehd nasikaatln tvaaaaeigk cvggdihvlv aghnaqaaad aaakiagvsk
       61 vlladapqma dglaenveat vmniaknysh ilapataygk niapriaakl dvaqisdita
      121 vdsadtferp iyagnavatv qssdpikvit vratgfdpva aeggsavvek ieaaadagks
      181 qfvsrevtkl drpeltsaki ivsggrglgs genytkvlep ladklsaalg asraavdagy
      241 vpndyqvgqt gkivapqlyi avgisgaiqh lagmkdskvi vainkdpeap ifsvadyglv
      301 gdlfseipel aaqla
//
LOCUS       WP_175984831             244 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: O-methyltransferase [Burkholderia].
ACCESSION   WP_175984831
VERSION     WP_175984831.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..244
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26805
     Region          78..238
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 maspttvllr rlheesrtei vararaqfqg snedflslae eyeaiaprlr grfletfgls
       61 sddfaspegs plslavspet ggflrnlvls qrparilelg sscgvstlyf aealrtlgsg
      121 vvvaterdal kctrlrdhvs tagldayvdv regdvfetva eldgtfdmvf idvwadvylk
      181 vfkeierllr pgsvvladnm ytaedavrpy khyldddprf stttldfesg ieftvvvsqa
      241 gmss
//
LOCUS       WP_175984837             275 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Burkholderia].
ACCESSION   WP_175984837
VERSION     WP_175984837.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..275
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29197
     Region          66..269
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mtilyrgmdr aaldaaylnt kvvpdfpall asmqarsavl yeavsgrrdl rygaqpaqrf
       61 dwlscgqpda plfvfihggy wqhcakedfa yaasgplarg fdvilaeytl apiatmtdiv
      121 geigalldyl andpdglgta krpihlsghs agghltavhr ahpavvsala isplvdlepi
      181 slcclndklq ltahevdays plrhlgpgap tvvavgdael pelvrqardy ataceaager
      241 tahvglpdmk hfdvlddlak pdgamlaalq siapr
//
LOCUS       WP_175984865             247 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [Burkholderia].
ACCESSION   WP_175984865
VERSION     WP_175984865.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..247
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26903
     Region          3..240
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mdvklvartl dlfelfaaer rplpltelar llnvpasscl amartlvsrg ylyevrkrgg
       61 yyptrrlqti aaaidatdpv vdivhphlva lrdasretav lgkiqgvsvt yldvveseqa
      121 irytrapgel rplhansigk aifaelagda qqvlgtqlpf erftdttvan lpalvaqtaq
      181 frelgwaenf gesapelsai avaltldgdw yglsvvgpte rirqhrdmha allvdakarl
      241 laeharg
//
LOCUS       WP_175984880             338 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Burkholderia].
ACCESSION   WP_175984880
VERSION     WP_175984880.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..338
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37965
     Region          171..316
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 medtltkpag tadavegeva aaldgaahgq alavaehtld awrpddspdr llaafvalfn
       61 tdtrydaati svplggadaa avasyvarav regvidgarv agdtlrvtvs ratfwqnprp
      121 wlkapasggm plrhvitngh rhpvrppspa geiyarympq vgmtfslhtv didehaqlfs
      181 dwmnldrvah fwdqrgtrde haaylaerla dphmhpmigy fddtpfgyfe fywakedrla
      241 pfydahdydr glhlligdsr fqsagklhaw wsgvlhymfv deprtqrlvg eprvdhvrhi
      301 aymhrlgfyt lkefdfphkr aaltvierdt ffdtfrlp
//
LOCUS       WP_175984885             387 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: pyridoxal phosphate-dependent aminotransferase
            [Burkholderia].
ACCESSION   WP_175984885
VERSION     WP_175984885.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..387
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=41480
     Region          17..369
                     /region_name="AspB"
                     /note="Aspartate/methionine/tyrosine aminotransferase
                     [Amino acid transport and metabolism]; COG0436"
                     /db_xref="CDD:440205"
ORIGIN      
        1 mrhrrparlq eiagigvdrm gsiadhagrd vlrlenldtd ipphadalar traaasedaa
       61 nsylpfvgqd rlrasvaahv tvqtgvnyra dnvivsaggl sgilnvllav levgdevilt
      121 dptyagllnr vrlaggspvq ipfsfhpgae wkldreamaa acgpktraml lmspsmpsga
      181 vldeedwvfv aglcvqhdll livdsamerl lfdgrevvhp arlpgmaert itvgsaskel
      241 rmigwrvgwi vapdalipdl vavslanvvv pvgiaqeaaa ialerstidl pdyvaelqrr
      301 rdaiaaelhg lpfgmpaggw smllrvsdfg ltgeqmserl leldvcatam tgwgrqhgga
      361 yirfvfanep vnryagfgkk vieafgm
//
LOCUS       WP_175984894             347 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia aenigmatica].
ACCESSION   WP_175984894
VERSION     WP_175984894.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia aenigmatica
  ORGANISM  Burkholderia aenigmatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia aenigmatica"
                     /db_xref="taxon:2015348"
     Protein         1..347
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37795
     Region          180..326
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mlaevrpdgf tmldtyrlaf adglfavrdg aeirvaqgdg igaqllraql gddgalrlva
       61 ynhraapadq rrallaalaa afsdsarhaa irldpaawpa valdalrasg vladggrcmr
      121 egwaqqadlw lvgphlpcat lpmltdgrrh prrppaprge vyardlpalg vrftlrgwqp
      181 aedpgrlarw fdeprvrdgw pgaqpvqagp dgvqgaapdt dphvtplvgc fdgepfayfe
      241 aywlkedvla phvgardydr glrmlvgesr wrgphcvagw lpsvvhylfl ddprteavgc
      301 avpagharva dhlarhglar qrrlaladaq plwmralret ffsgrhv
//
LOCUS       WP_175984900             282 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia aenigmatica].
ACCESSION   WP_175984900
VERSION     WP_175984900.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia aenigmatica
  ORGANISM  Burkholderia aenigmatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia aenigmatica"
                     /db_xref="taxon:2015348"
     Protein         1..282
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29719
     Region          7..260
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtrstaalaa rglavgyrdh vvidgldlsi aagrvtalcg pngcgkstll rtlaglqpar
       61 aghvevngqp lasfrrrala reltmlaqfn qipsgltvre lvaygryayg gflrglsrad
      121 haaidealet sgladdasrd vgalsggerq rawiamalaq qapivlldep ttyldihhql
      181 dildalraln rargltivwv lhdlnqaaay sdeivlmrag rlvaqgspda mleparlraa
      241 fgvemlklah pqtgapmcvp aygpstdgap qaagvfdqdl av
//
LOCUS       WP_175984901             335 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TauD/TfdA family dioxygenase [Burkholderia].
ACCESSION   WP_175984901
VERSION     WP_175984901.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Islam,M.S., Leissing,T.M., Chowdhury,R., Hopkinson,R.J. and
            Schofield,C.J.
  TITLE     2-Oxoglutarate-Dependent Oxygenases
  JOURNAL   Annu Rev Biochem 87, 585-620 (2018)
   PUBMED   29494239
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Schofield,C.J. and Zhang,Z.
  TITLE     Structural and mechanistic studies on 2-oxoglutarate-dependent
            oxygenases and related enzymes
  JOURNAL   Curr Opin Struct Biol 9 (6), 722-731 (1999)
   PUBMED   10607676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10496218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..335
                     /product="TauD/TfdA family dioxygenase"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37196
     Region          13..321
                     /region_name="TauD"
                     /note="Taurine catabolism dioxygenase TauD, TfdA family;
                     pfam02668"
                     /db_xref="CDD:367137"
ORIGIN      
        1 mtlltlptld dlriepglpt vvsprgsegm siddvaplar eiaadtlera ggvlftgfhv
       61 psidafqqfa asfgdpligy eyastprsqv egavytstey pphraiplhn eqsytsewpl
      121 riwfhcalaa pkggatpiad sravyraldp alvarfekre llyvrnfgqg ldlpwqqsfg
      181 tdepaeverm caargiecaw rtdddgelll rtrercqava rhprtgdrvw fnqanlfhls
      241 aldddmqeal vdavglenvp rnvyygdgep leadalaeir gvldqqrivf pwrtgdvlml
      301 dnmltahard pfegprkvvv amaqsytvpr drted
//
LOCUS       WP_175984906             311 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Burkholderia aenigmatica].
ACCESSION   WP_175984906
VERSION     WP_175984906.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia aenigmatica
  ORGANISM  Burkholderia aenigmatica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia aenigmatica"
                     /db_xref="taxon:2015348"
     Protein         1..311
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31569
     Region          2..311
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtilviaehd nasikaatln tvaaaakigg dihvlvaghn aqaaadaaak iagvskvlla
       61 dapqleagla enveatalni akdyshilap ataygkniap riaakldvaq isditavdsa
      121 dtferliyag naiatvqssd pikvitvrat sfdpvaaegg sasvekieaa adagksqfvs
      181 revtkldrpe ltsakiivsg grglgsgeny tkvlepladk lsaalgasra avdagyvpnd
      241 yqvgqtgkiv apqlyiavgi sgaiqhlagm kdskvivain kdpeapifsv adyglvgdlf
      301 alvpelgeal q
//
LOCUS       WP_175985143             463 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54 dependent transcriptional regulator [Burkholderia sp.
            BCC0506].
ACCESSION   WP_175985143
VERSION     WP_175985143.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0506
  ORGANISM  Burkholderia sp. BCC0506
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia sp. BCC0506"
                     /db_xref="taxon:2676290"
     Protein         1..463
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=51097
     Region          <36..130
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <151..454
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mnmpitrdks agvgsgngqr pliywtqsps vmlrkelsrr dwkvsvvaha selrdtsgei
       61 tcgildlsgg hadaigsias tcasmrdvvw valvdagqta spnvrallrd ycfdyvtlpa
      121 shqriadtvg haygmeclfa rdreqlesde kgivgtcsam lrlfdtvrrf artdapvfvf
      181 getgtgkelt avaihrhser rngpfvavnc gaipphllqs elfgyergaf tganarkigy
      241 veaanggtll ldeigdlphe sqasllrflq eraihrlggs dpvpvdvriv sathvdlrea
      301 meegrfradl fhrlcvmrid qpplrargkd iellahhmle rfrgdarhrv rgfstdaita
      361 lykhdwpgnv relinrvrra vvmtegrlit aqdleleycl daaspsvadi rksiereaie
      421 tallrtrgrv aasarelgvs ratlyrwmea ygierprgtg ssd
//
LOCUS       WP_175985183             257 aa            linear   BCT 11-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Burkholderia sp.
            BCC0506].
ACCESSION   WP_175985183
VERSION     WP_175985183.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0506
  ORGANISM  Burkholderia sp. BCC0506
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia sp. BCC0506"
                     /db_xref="taxon:2676290"
     Protein         1..257
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28615
     Region          12..253
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mssplqsesi raqvaelrer gfvvarglvd eaqcaalrqi aqrqlqeaae piefeadlry
       61 pgapeskhap gghtvrrlld aysrdpafae raiapeigaw mrayfgeepv lsrahhncmm
      121 tkhpaygslt gwhrdfrywa fersdmvsvw lalgpetden galwlvpgsh taefgpeafd
      181 dakffrsdlp enrrmidaat cpplqtgdvv ffhcntlhsa gqnrsdqvkf slvytyhgas
      241 nrpvpgtrsa skpevqf
//
LOCUS       WP_175985191             606 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia sp. BCC0506].
ACCESSION   WP_175985191
VERSION     WP_175985191.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0506
  ORGANISM  Burkholderia sp. BCC0506
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Burkholderia sp. BCC0506"
                     /db_xref="taxon:2676290"
     Protein         1..606
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67024
     Region          <140..585
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 madmshlpea fdalqgrlpe gytaserlld pvvvidrigg ktiarlggtr tvrgqrrilh
       61 aptnrhswvn dgntlrplpr dsvqifkell gsadandlpy dvairlirns gaaiktepae
      121 gfldagktva aslhdsisip dlranlfpyq argvqwmhet irytggvila demglgktlq
      181 viallllerp qssapaliic ptslianwlr eierfapdlt vmvhrgpert gvykglqvas
      241 vvvttyetmv ndisivssfk wswvicdeaq avknpesnrr ralvtiprrr aiaitgtpve
      301 nslldlwslg dfvipgllgs rrefedhypd ttdsaqlvgr itdpivlrrr vkevaddlpe
      361 rvdidlplel ddnltdyylq vrnetiakyp vagplvatlq lqllcahpwl rlandaelgs
      421 edanlepskt valmtakler teallqeafy nkqkvilfsi fnkvgdlvrt acpnpdnvfw
      481 gtingstpqd erqqiiddfs ahagpgclil npkaagagln itaatvvihf tpvwnpalea
      541 qasarahrrg qtrpvtiyrl fyqdtveqvm iersawkrel anesipvatr datdmkrald
      601 mkpgks
//
LOCUS       WP_175985817             188 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LemA family protein [Microbacterium].
ACCESSION   WP_175985817
VERSION     WP_175985817.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium
  ORGANISM  Microbacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Microbacterium"
                     /db_xref="taxon:33882"
     Protein         1..188
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=20780
     Region          18..188
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mewlipvliv vavlvlvgiy lwatynslvq lnvrvdeaws gitvqlkrra dlipnlietv
       61 kgyashekav fenvtrarae tlaatspgea giaeghlqqa lkslfavaea ypqlqasqnf
      121 lqvqhslvdt edkiqaarrf ynggvrelnt kikvfpnnlf arslgftere ffevadgaai
      181 aepprvqf
//
LOCUS       WP_175986196             205 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: M23 family metallopeptidase [Microbacteriaceae].
ACCESSION   WP_175986196
VERSION     WP_175986196.1
KEYWORDS    RefSeq.
SOURCE      Microbacteriaceae
  ORGANISM  Microbacteriaceae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Microbacteriaceae"
                     /db_xref="taxon:85023"
     Protein         1..205
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21804
     Region          <112..173
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 matsidleyp ftgrwlvqns panrvpshgt allatsyaid fvpaddagrt apitfrslir
       61 pepaekfpgf grmllspveg ivvathdtep dhpayrglps lgyaltqqrr aragwialag
      121 nhvlietggv vvalchlqqd slgvrtgqrv qigaelagcg nsgnstephv hiqaittldi
      181 eraiavpltf rgtlprngnv idise
//
LOCUS       WP_175986200             222 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Microbacteriaceae].
ACCESSION   WP_175986200
VERSION     WP_175986200.1
KEYWORDS    RefSeq.
SOURCE      Microbacteriaceae
  ORGANISM  Microbacteriaceae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Microbacteriaceae"
                     /db_xref="taxon:85023"
     Protein         1..222
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24303
     Region          16..184
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msrgqdsadp kerpprstrv dkrralldga llvfaedgyt rasidtiarr agvstrtiyn
       61 qfgdkaalfe avivdsarrt adeqiatvrr ylgkivdied dliefgrvwa spapehaphf
      121 alvrqihada ghiaettlra wqevgplrvr keiaehlsri ataghltvtd adlaavhlvq
      181 liagdittrt yhgaiplpva elhrlsdagv raflhghisa rh
//
LOCUS       WP_175986342             199 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175986342
VERSION     WP_175986342.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..199
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=22254
     Region          10..199
                     /region_name="RsmC"
                     /note="16S rRNA G1207 methylase RsmC [Translation,
                     ribosomal structure and biogenesis]; COG2813"
                     /db_xref="CDD:442062"
ORIGIN      
        1 mtnhyysskp evesnpqiiq felrghsfrf ktdqgvfskk evdfgsrali esfelpeteg
       61 dlldvgcgyg piglalakdf ddrivhmvdv neralslase nakangveni siyqsdryhn
      121 vkeksfaail tnppiragke tvhsilsesy dyladkgelw vviqkkqgap samdkmeelf
      181 snveiaarkk gyyilrsvk
//
LOCUS       WP_175986426             286 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175986426
VERSION     WP_175986426.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..286
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32628
     Region          7..256
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 medkinlike kiphldikey hqnkqgqnnd vliinnewvf rfpkyragie qlkketvild
       61 yassklsipv pqpayqfffp eepgmvftgy rilpgsplwk ndmtdldrtr rqqaavdlav
      121 flkelhsisp dsslgsiqqs eptcfdemkd lherlktkiy pfmkqeside vddrfteyfg
      181 scqsvsacii hgdfgcsnil wdkdrvsgii dfggagfsdp aydvagllas ygeefiqmmi
      241 phypeitsfl nrvhfykstf alqealfgie ngdqeafeng magykk
//
LOCUS       WP_175986431             370 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175986431
VERSION     WP_175986431.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..370
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42299
     Region          158..352
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 maaiiirtif lgllwsayiy dssqdsismi flmllcslsf acffitpvsr nrlflyicqt
       61 llllisslvs pepllawgif cyfhleastq lspekyqmfm ytailfsgie aflfwdsysp
      121 avipffamff fmtwklnerc hdlkeqrvly deligeyrkl krilyvtern skaeertria
      181 reihdsvghn ltallmkiqm lsiehghslf keiknlaaes ldetreavka lkegevegiq
      241 svihlirkle sessvmvelt tqqgvlstrl snkqniavyr ciqegitnam khssvkevkv
      301 tlgktalghl hfkiinqlnq ldnirpfqmg fgltnmkeri eelggnleih qtdkefilgg
      361 afpveevaka
//
LOCUS       WP_175986456             391 aa            linear   BCT 11-JAN-2025
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175986456
VERSION     WP_175986456.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..391
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=43587
     Region          6..386
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 metrqrfadk fdwglvfllm mffivsalgi ssaqtsgqyg tnfvirqafw yvvggiiiag
       61 alffdseqyk rlawymygag illllvllis pesiapyrng akswfmlgpl gsiqpsefmk
      121 tflilalarv itnhnevttr ktlqtdfqll lkigfttlvp lafimkqpdl gtslvilaim
      181 tgiilvsgit wklivpiyaf lgvvggills lviwapefle kytgfepyqf griyawldpy
      241 nysklegfhl inslnaigsg qifgkgysdg evyipenhtd fifsvigeey gfigasvvis
      301 lfflliyhlt ktaldtkepf nayvcagiis mitfhvfqni gmtiqllpit giplpfisyg
      361 gsslmgnmla lgivfsmrfh hktymfssed s
//
LOCUS       WP_175986506             247 aa            linear   BCT 11-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175986506
VERSION     WP_175986506.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..247
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=27333
     Region          129..220
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mkkhfgyili ayivmqlssi vgvpllykig vdvlgepadq vkqlvpgywl misftltliv
       61 vwailrkset stnlersapl nagssigwai agifiaffaq siaiqieyal gikmgsentq
      121 miigiiekvp ltmlvaavig pileeivfrk iifgvlyekm nfffaalvss iifalahfep
      181 ehvilysamg ftfaflyvkt krilvpifah vamntsvvli qsiykdeiqk imkeaeqiqg
      241 figglfs
//
LOCUS       WP_175986511             153 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175986511
VERSION     WP_175986511.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..153
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=16568
     Region          12..146
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 msqqlinvat kgkwvegmkt nvqardfafi vdepealggt dqganpveyv laalsgctsv
       61 vialiakeld fkyedatfen egtldlrgln gvegvsphfq tvtfdvtivt deseerldel
      121 kskvekrcpv ynllkdagia lesnwvkkat vsa
//
LOCUS       WP_175986570             290 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175986570
VERSION     WP_175986570.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..290
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33962
     Region          3..155
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnnrkrkvad ialslfiekg fqqtsiqeii ekaniskgtf ynyfsskndc iadileylry
       61 dasqqrvamq igkdakdrnv lveqitilik lnkernlnvl feailssnea elkklvmqhr
      121 miemewlsnr fievmgdeir evsfegtvlf ygmlqyllft mkvtnssspl erlvevvmsy
      181 ieliipymlk hdtsmlshsa idllqsnidk htvtktevle laerfqkhsa fneeqqdlfd
      241 aimnelqrdr irkivlkpll kpfqqlfnet dneshahkft nmlwyylksv
//
LOCUS       WP_175986669             131 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175986669
VERSION     WP_175986669.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..131
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=14798
     Region          2..114
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mfeldlrsrk piyeqlvekl kelminevmk pdeqlpsvrt laqqltinpn tiqkayrele
       61 sqgyiysvkg rgsfvnpssh iqnaekimkv keelskllse alylgitaed lkemiaeiea
      121 svggnqaddr d
//
LOCUS       WP_175986678             108 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175986678
VERSION     WP_175986678.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..108
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=12141
     Region          8..95
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(29,32)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mkeqhtledi kntiekenmv llyisrpdcs vchallpqvk evlkkypgie avhadadeip
       61 eiageysift vpvlivfveg kemmrkarfv pideldsgls rlvtmled
//
LOCUS       WP_175986723             518 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175986723
VERSION     WP_175986723.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..518
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59093
     Region          6..508
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 msllsvknlt hgfgdraifn dvsfrllkge higligange gkstfmniit gklepdegkv
       61 ewakririgy ldqhaqlkqg mtirdvlkta fqylfdmeae mnelfgkmgd asteeleell
      121 eetgtlqdal tnndfyiida kveeigrglg lddigldkdv hdlsggqrtk vllaklllek
      181 pdillldept nyldeqhiew lkrylqeyen afilishdip flnsvinliy hmenqelnry
      241 agdyhefkkv hemkkqqlea aykkqqqemk dlkdfvarnk arvstrnmam srqkkldkmd
      301 vielaaekpk pefnfkmart agrvifetkd lvigydtpls kplnlkmerg qkialsgang
      361 igkttllrsi lgeirpisgs velgdylhig yfeqeiktqn yntcieevwn efpsfnqaev
      421 raalakcglt tkhieskvev lsggekakvr lcklmnkesn vlvfdeptnh ldveakeelk
      481 ralkeykgtv llishepefy ndvatevwnc eswttklf
//
LOCUS       WP_175986725             441 aa            linear   BCT 11-JAN-2025
DEFINITION  phenylacetate--CoA ligase family protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175986725
VERSION     WP_175986725.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Luengo,J.M., Garcia,J.L. and Olivera,E.R.
  TITLE     The phenylacetyl-CoA catabolon: a complex catabolic unit with broad
            biotechnological applications
  JOURNAL   Mol Microbiol 39 (6), 1434-1442 (2001)
   PUBMED   11260461
REFERENCE   2  (residues 1 to 441)
  AUTHORS   El-Said Mohamed,M.
  TITLE     Biochemical and molecular characterization of
            phenylacetate-coenzyme A ligase, an enzyme catalyzing the first
            step in aerobic metabolism of phenylacetic acid in Azoarcus evansii
  JOURNAL   J Bacteriol 182 (2), 286-294 (2000)
   PUBMED   10629172
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Ferrandez,A., Minambres,B., Garcia,B., Olivera,E.R., Luengo,J.M.,
            Garcia,J.L. and Diaz,E.
  TITLE     Catabolism of phenylacetic acid in Escherichia coli.
            Characterization of a new aerobic hybrid pathway
  JOURNAL   J Biol Chem 273 (40), 25974-25986 (1998)
   PUBMED   9748275
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..441
                     /product="phenylacetate--CoA ligase family protein"
                     /EC_number="6.2.1.30"
                     /GO_function="GO:0047475 - phenylacetate-CoA ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0010124 - phenylacetate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48693
     Region          1..434
                     /region_name="PaaK"
                     /note="Phenylacetate-coenzyme A ligase PaaK,
                     adenylate-forming domain family [Coenzyme transport and
                     metabolism]; COG1541"
                     /db_xref="CDD:441150"
ORIGIN      
        1 milheietag rdqmeslqle rlqktaslvy hsvpfyrnhf eqrnlhpddi rslkdikmlp
       61 lttkkdlrdh ypfgmfavkq eemvrvhass gtsgkptvvg ytqndidmwg nivaraiama
      121 ggrqgsvlhn aygyglftgg lglhygsekl gmitvpvsgg nmdrqitlie dfkpsvicgt
      181 psyvlnlaet iagqgkdpas lslqagifga epwsnrmrdt legilgikac diyglsevig
      241 pgvamecpea qdglhiaedh flvevihpdt lepvpegetg elvftsltke afpiiryrtg
      301 diasiqhgtc scgrttvkms rvkgrvddml iirgvnvfps emehhllelk elaphyqlhv
      361 kkkgaldtve lhveinpdfy aglsgdiqhe kvfeltskik rvmkngclvs mdvkvrapke
      421 iprsegkavr ivdlreeaif p
//
LOCUS       WP_175986745             342 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175986745
VERSION     WP_175986745.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..342
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36204
     Region          1..317
                     /region_name="COG4120"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443296"
ORIGIN      
        1 mptaifasfe sgiiyaimal gvylsfrild fpdltvdgsf vtgaavaatm ivsgvnpiia
       61 titaivigfi agcitgllht fgkinallsg ilmmialysi nlrimgrsnv pllsqettft
      121 gvesmwaplg idaalnklwm avglgeplpg twsilfimii itlaikfltd aflkteigla
      181 lratgdnqrm irsfsantnl miilglgisn gmvalsgali aqysrfadvg mgigmiiigl
      241 asviigealf gtktiarttl aviggaiiyr lvvsmalrvd fletgdmkli tativilali
      301 mpkvmdrykd kkrkaqrmae rlgktsiteg kgdngaaiks ns
//
LOCUS       WP_175986755             397 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrolipoamide acetyltransferase family protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175986755
VERSION     WP_175986755.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..397
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43757
     Region          2..395
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mevklhdige gmteanvnhf lvkagdtvka dqplvevqtd kmtaeipapf sgrikeltvg
       61 egetipvgtt vllmekeegm teavtapkkp qgirarrvla spytrkiare ngvdldevsg
      121 sgsggrilde dvyafiqgge qsrpeesvsv etavktkgvq psvsdhdsnt iplrgrrkqi
      181 askmthslrt iahcthfeei dvtnllewke amknnhqsis mgayfikvis vclkefpifn
      241 avldeknecv rlkpehhigi atdteegliv pvirnvetks mkeihhemke ltlkaqennl
      301 sikditggtf tvsnvgplng sigatpiine pevgllafhk tkkrpmvndq deivirsmmn
      361 vsmsfdhrvv dggtavrftn rlrdlieepq tllleli
//
LOCUS       WP_175986906             552 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175986906
VERSION     WP_175986906.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..552
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=60307
     Region          1..534
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 malkkrlmil gfiplilsti iigyvvsqli slqssanedv kilveteklr sdlivtkqal
       61 anysvntsde nkqmaetllt dtssqidelg klisvkeqde tlaiietkfs elksvsgkal
      121 nannkaeikr qslrisgvln dmhllnkqts dwyqnllken eqqitfivwa tiigfltali
      181 lsigasails nrivkplnam vhnaermarg dltisfeess kknnkfevyk lqeafqhmvm
      241 nlrntvqsvn eigvnveqft rdvqgqmanl sesssqvavs teelakgsqa isedvqstas
      301 lmtvmgeefa snvrssqess anskvalqsv ehgrtslikq kefaesinds sasieqsvls
      361 farytgeieq aaqavkeiae qtnllalnaa ieaaragdag kgfavvaqev rklaedssva
      421 terigsmvgs ikegihsime asqkgsslsn rqmesmsvte safeeiagnv ssiyeklsel
      481 etgmmasner tnnviaaven isaiteetaa gteeiysste eqlryfeqlt gqvselnamt
      541 vkmkkelekf tl
//
LOCUS       WP_175986972             408 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175986972
VERSION     WP_175986972.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..408
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44095
     Region          11..389
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(19..20,23..24,27,59,109..110,112..114,117,137,
                     140..141,144,220,223..224,227..229,232,260,264,317..318,
                     322,326,342,345..346,349..350,353)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mlmmrwkdpi lllmgiglsn vgawiflial nlivldewgs alavgilyvl kplaalftna
       61 wagsvidrmn krrvmvfldl fravlvavlp fissitlmya vvfvinmgsa vfypasltym
      121 tklvprenrq rfnalrsvig sgafiigpav agilfilgtp ttalylnaaa lflsglitll
      181 lpdlegdsft gakklsfemi kadwrvvrnf srrytyvmav yllfscmivm taaidsleaa
      241 fskevlglsn stygylvsia gagflagaiv ntviankvre vhliafgsvm vsagymvysf
      301 sgefaaaaig fsllsfslaf aqtgfetfiq eripvevmgr vssvygwieg ilviaatili
      361 gvgaellsir gmviagsivm vtitvflfvy smgrgevktv eknpieis
//
LOCUS       WP_175987025             393 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175987025
VERSION     WP_175987025.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..393
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43067
     Region          12..378
                     /region_name="MFS_YcaD_like"
                     /note="YcaD and similar transporters of the Major
                     Facilitator Superfamily; cd17477"
                     /db_xref="CDD:341030"
     Site            order(19..20,23..24,27,59,109..110,112..114,117,137,
                     140..141,144,218,221..222,225..227,230,254,258,308..309,
                     313,317,333,336..337,340..341,344)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341030"
ORIGIN      
        1 mnqslsfrfw vlvaivaisg fsqgmllpli aiifeqdgls sslnglnata lyigillasp
       61 lmekplqkig ykpmiiiggi vvalslflfp lwksfwfwfa lrlfigigdh mlhfatqtwi
      121 tsfspkehrg rnisiygvsf gigfavgplm aqlieysqal pfmissalsl lvwsfvfklk
      181 nefpeqqnig sasflgsfqr fgkvlkyawv allpplgygf leaslngnfp vfalrngisv
      241 eavsillpaf avgsiisqvp lgvmsdkygr qnvllivmmi gflcftaagf vsestiglft
      301 cftlagmavg stfslgisym tdllpkellp agnimcgiff sfgsmmgpfi ggiviewfsg
      361 psffymislm mlvifvsllv fsvqnrrrev tqn
//
LOCUS       WP_175987058             246 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175987058
VERSION     WP_175987058.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..246
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28600
     Region          106..155
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mdrgktcsic gehisiknfa kkdkqrwrsy ckscrmlrne mlkarqietp elekgtqiev
       61 rgnmsnghry ssfvsyekav qmvdekvayi vnpklirkyf dretfrklvf rrygncciyc
      121 edeattidhv ipksqggiss fancvpacsq cneakgsmnv eeflyyydls ttipgmsrva
      181 tvryglmeim eklhnihiyl nmclqkieie eivfndlvev eelekkvnev netikmykkl
      241 nkqslv
//
LOCUS       WP_175987076             241 aa            linear   BCT 11-JAN-2025
DEFINITION  M48 family metallopeptidase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175987076
VERSION     WP_175987076.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..241
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=28677
     Region          2..236
                     /region_name="YgjP"
                     /note="UTP pyrophosphatase, metal-dependent hydrolase
                     family [General function prediction only]; COG1451"
                     /db_xref="CDD:441060"
ORIGIN      
        1 mekhqieyan nvidfiikrk qvknvnlnvk pdmtievtan drvpldfisd fvkskgswil
       61 knvgnfndvq plkqsereyv sgetfkylgk qyrlrvqqsm eeevvkyfrg fiylyvkktd
      121 nvsrksklmd ewyrekaqmt fneslekmyp lvqkygvekp eidirlmkar wgsalteknt
      181 vllntelika pkycidyvvl helihfkynd hsdnfyqmlf slmpdwekrk aildeevvkd
      241 l
//
LOCUS       WP_175987125             377 aa            linear   BCT 11-JAN-2025
DEFINITION  zinc-dependent alcohol dehydrogenase [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175987125
VERSION     WP_175987125.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..377
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41610
     Region          1..377
                     /region_name="FDH_like_1"
                     /note="Glutathione-dependent formaldehyde dehydrogenase
                     related proteins, child 1; cd08283"
                     /db_xref="CDD:176243"
     Site            order(38..40,43,85,161,165,184..185,187..189,208..210,214,
                     229,253..255,279,296..298,321..323,363)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176243"
     Site            order(38,40,59,161)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
     Site            order(89..90,92,95,103)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
ORIGIN      
        1 mkavtyqgkn svavkkvddp riedpqdviv ritstaicgs dlhlyqgnfp lpigyvighe
       61 pmgiveevgh dvtkvkkgdr viipftvacg tchycnhhle sqcdnsnphy dsgglfgyse
      121 kfgnypggqa eylrvpygny tpflvpsdce ledeqllmls dvmptaywsv enagvkkgdt
      181 vivlgcgpvg lmaqqfawkk gaerviavdy fdyrlqhskk mnstetfdft qyddmgetlk
      241 eltkggadvv idcvgmdgkk splefveqkl klqggtigpi qiatkavrkc gtvqltgvyg
      301 glynmfplga ffsrnitlkm gqahargyme plykqvvnne idstsiithk lkledaakgy
      361 elfnkkeddc ikvilkp
//
LOCUS       WP_175987203             122 aa            linear   BCT 11-JAN-2025
DEFINITION  PH domain-containing protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175987203
VERSION     WP_175987203.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10547098
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..122
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=13381
     Region          10..120
                     /region_name="bPH_1"
                     /note="Bacterial PH domain; pfam08000"
                     /db_xref="CDD:462337"
ORIGIN      
        1 maattgilew tlisecpipd dvtallvtge eavaayktfr dsaiftnkrl ivrdsqgltg
       61 kkvemyslpy ssitmwsten agsfldvnae velwtksghi kvklkkgidv rkfdkliaea
      121 ll
//
LOCUS       WP_175987295             595 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175987295
VERSION     WP_175987295.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 595)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 595)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 595)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 595)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 595)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..595
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=67515
     Region          143..580
                     /region_name="YesM"
                     /note="Sensor histidine kinase YesM [Signal transduction
                     mechanisms]; COG2972"
                     /db_xref="CDD:442211"
ORIGIN      
        1 mffslrnrlf miftllltfp flvlsilipn wftsimeert tsstiemmeq yslyidsits
       61 qaedlgkqvl vnpttqewik seendreags aerllmknql kaelssmmin nsksmsvsvf
      121 lndgtgtagn lpplektiwf ddfykndqrw lrshndlmad hvnsyllplf dintldlsgv
      181 ikvnfpssll ekalskiklg ekgrvylldr hgrnvltgsi dtpekvlkes lntiktepkk
      241 sglievpfek eeymlfyqka rvgewilvse itkselfsri nelqknlllt sgwiflltim
      301 asyllsstiv kplgkltgam klvetgdfkk akqlipfikt andeigyvvd vfgqttnrld
      361 tlieteyean irrrdaeyka lllqinphfl nntletiggl aaqgknkevi dvtihlgrim
      421 ryslntesdt vtlgeemtyi rrfleilklr yeealsvsie edpkasalpi ikfviqplve
      481 nsvkysfiek teavlristk kvddwveiki edngigipes ivkelkrdlg ghesravwvs
      541 kgrsiglknv lgrlklyyge nftyhitsee nqgttislci ksgegdhhae gdsgr
//
LOCUS       WP_175987353              67 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175987353
VERSION     WP_175987353.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..67
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7889
     Region          1..64
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mknkikelra erkmtqdqla arldvsrqti islererynp sinlafkiar vfqcsiedif
       61 iyeedne
//
LOCUS       WP_175987370             213 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175987370
VERSION     WP_175987370.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..213
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24547
     Region          15..176
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtqsdqqkka pgrprlnkev akgellrsat klfstkgfee tslreiasda dvnmalikyh
       61 fgskmdlwka vilklseevl efndfdleev rnysdmrqml gdlfdrmvdm tfehpefslf
      121 vmnesiqkge rfdhlferli tpfheqsypf iikgielgvl adqdpeeliv mllssvsyqq
      181 aaphilanft pvtndeaqwk evikhslran fik
//
LOCUS       WP_175987404             347 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175987404
VERSION     WP_175987404.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..347
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38991
     Region          32..335
                     /region_name="AKR_unchar"
                     /note="uncharacterized aldo-keto reductase (AKR)
                     superfamily protein; cd19099"
                     /db_xref="CDD:381325"
     Site            order(36..38,66,71,103,173..174,213..214,251,290..296,305,
                     322..326,330,333..334)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381325"
     Site            order(66,71,103,173)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381325"
ORIGIN      
        1 misgyatlkg tseyliksgm pyrkspgfca ppiamgthlg emneedsaly regieyglln
       61 glnfidtain yrgmrserdv ghvlksliqr gtikreeviv stkagiipgd ieanlvpady
      121 lkkvlldggi iresdlnivd thrhvlepdy yrfaierskk hlhletidly yihnpeislm
      181 tlgsarfyqq lellfsffee qvqtgnlnyy gfatwsglln apnedgyisi eetvntakrv
      241 ageahhfkfi qfplnkqmnk aiknqnqrvh gkwltiieaa qelgihstts apfnlgkvfd
      301 dgsdpqssli dvartngvfs tmvgmkkveh ikenigvfkh npvvkrr
//
LOCUS       WP_175987431             140 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175987431
VERSION     WP_175987431.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..140
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16381
     Region          14..129
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mqeltlkngm tykirefeea dfecvhqlna eeewnnlvkk kedtknawmh stirflvfdg
       61 dalagyvrgf tdenvttyic ellinkryrg qgigseliks vhhlypktrv ellgsqtsks
      121 fyeandyraf ygfrktieey
//
LOCUS       WP_175987556             145 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175987556
VERSION     WP_175987556.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 145)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10120901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..145
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=16073
     Region          4..113
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cd02883"
                     /db_xref="CDD:467528"
ORIGIN      
        1 mfivnveaai hrddkwllir rsekedhapg mlslvggkcd aegvsndile rtlirevdee
       61 vgikvgglty vnscsfvtdt gidvidivfl ckvedgepya kspdevgevl wmstseilae
      121 eeipeylkan vqlaekrlqe gffvk
//
LOCUS       WP_175987614            1019 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175987614
VERSION     WP_175987614.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..1019
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=111190
     Region          1..997
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnllkfivnr kilvglmvll vlviggysvf kldkellppi qfdaayvdin agdmsaieve
       61 rtitnpleqq ingiegvekt esttyigrss imvtfergkg delskeveal anaaaadnta
      121 ikevvagqag lsqsyeffmd vsgedmgeit afsrdilepr lealpevsdv llsgieekev
      181 aiefnrdkvs elgidisqta avisgaggee tlgelsgead sptirwstkl entedvknil
      241 iptstgfvrl eevasvsvqp ldtssivwkn gtkdfifiqv grvsevtqie maeavrkeiq
      301 airdeglvdg ftvnevvsqa dyvkesldgv tgniviggii avvilflflr nlratfiigl
      361 siptsvfltf atmflfdysf nmltlvglgl gigmmvdssi vilesiykkk eqgmekfeav
      421 iagtkevasa vfasmlttiv vflpiglvgg emgqfmills avvaitliss vvvaftlips
      481 lsenflklre ktkarkegri tglysrmvsw tvkkkrtsfa viglffmmfa aslflitkvp
      541 mtimpdmfnr yaelmvkvet glslqekedv vgemtdalag ipdvetsyvl dngsmlytii
      601 nmtkgddite eqekvneqif sslrdleest pienvasamn ggggypvqvn isgddfeglr
      661 etadnftkel eeiegitgvt tsidrtsleq vvdvkedeie aagltqsqik qfiqqaflev
      721 pvgemsidnd afpllvkwne ktdmnselln livstpkgee klssfielrs vdtpneisha
      781 dgdrfisvfa dikdkdlgai nrevqkmike frapagytva vagdleqqqe liqemilvla
      841 iaiflvyfvm avqfnnlsqp ivvmsvipmt itgvilglfi tqrelsvmsg mgivmligiv
      901 lnnaillidr tnqlrkeglt veealvragk drvrpifmtt lttaggmlpl alasgtsgny
      961 qapmatviis gllfatlitl vlipsvyklf aslgagfkra grrkkkyqts taekletln
//
LOCUS       WP_175987618             206 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175987618
VERSION     WP_175987618.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23719
     Region          7..172
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mspkvsqehk eqrrnqllqa aeevfieqgy enttmkhvmd kagvsrggly qyfdnkedlf
       61 ealigeqqke imddslqami eqqgscweal lmtflgeekr atddmdplap skleyfitgr
      121 nekrrrehak kryhhaygft ekiikagiea gefaprfdpe viaryiisyv dglavdhaiv
      181 gsesiklkeq tellieylrw glnvke
//
LOCUS       WP_175987643             254 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175987643
VERSION     WP_175987643.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..254
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29352
     Region          3..105
                     /region_name="HTH_TipAL-Mta"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators TipAL, Mta, and SkgA; cd01106"
                     /db_xref="CDD:133381"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133381"
     Site            order(51,54,58..59,68,80,84,90,94,97..98)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133381"
     Region          135..249
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 meytvkklgq laavsprtlr yydeigilkp arinssgyri ygekeidklq qilfykelgv
       61 sleqikdild dptfdlasal aehreqllek rkqldllian vdktiavkeg rmtmsdkekf
      121 egfkkdmide nerkfgkeir ekygddtvnq snaklqnmsq edyeranrla edihetlaea
      181 fktgdpsset aqkaaelhkq wismywpqys keahaglgdm yvaderfray ydkeqdgvae
      241 flrdaiyvyt gmkk
//
LOCUS       WP_175987650             384 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175987650
VERSION     WP_175987650.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..384
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42703
     Region          1..376
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
ORIGIN      
        1 mlrriflkem kdsfrdrrtl flivllpilm msgltffyen mlkddkgdsy tlavnqdade
       61 eilarfssye nvkiekssdp ekmvsdgdal aglmvaydfm etveqgeqae vtvvgdsfsq
      121 kassliaivt nefttlekei taqrleaqgt elsviqpftv kqeelsedls vnmlallvpl
      181 ilaiaigiga spaaaelfag ekekktmeal lmtpvnrstl ilakwlaist lstimgfitl
      241 lvmmieitff teklkeaisf genlyliagi sllvilvyav fnssilmits imgktvkeaq
      301 syytpvsmls mfpamiigsl gvnelevhhf aipilnlfsq mkellfgivd yqhlaitiss
      361 nllvmivvfi igrilfmkdk wvln
//
LOCUS       WP_175987672              91 aa            linear   BCT 11-JAN-2025
DEFINITION  glutaredoxin family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175987672
VERSION     WP_175987672.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Shelton,M.D., Chock,P.B. and Mieyal,J.J.
  TITLE     Glutaredoxin: role in reversible protein s-glutathionylation and
            regulation of redox signal transduction and protein translocation
  JOURNAL   Antioxid Redox Signal 7 (3-4), 348-366 (2005)
   PUBMED   15706083
REFERENCE   3  (residues 1 to 91)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   4  (residues 1 to 91)
  AUTHORS   Fernandes,A.P. and Holmgren,A.
  TITLE     Glutaredoxins: glutathione-dependent redox enzymes with functions
            far beyond a simple thioredoxin backup system
  JOURNAL   Antioxid Redox Signal 6 (1), 63-74 (2004)
   PUBMED   14713336
REFERENCE   5  (residues 1 to 91)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002164
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..91
                     /product="glutaredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=10332
     Region          7..>57
                     /region_name="GrxC"
                     /note="Glutaredoxin [Posttranslational modification,
                     protein turnover, chaperones]; COG0695"
                     /db_xref="CDD:440459"
ORIGIN      
        1 mnkelilely trptcsdcqa akeylaehdi dyvhknvged amlekelidi agsrivpsfv
       61 fykkgllgkk kfvknligfe nnreeiekll g
//
LOCUS       WP_175987697             485 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase [Bacillus
            sp. Marseille-Q1617].
ACCESSION   WP_175987697
VERSION     WP_175987697.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..485
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=52877
     Region          9..485
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(66,68,72,75,79,112,115..116,125..132,137,140,143,
                     236,240,243,246,248,421,423..424,426..427,430,433..434,
                     436,438..441,450,454,456,470,477..482,484..485)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(152..155,163,178,181,211,228..231,234,252..254,286,
                     386,388,414)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(155,252,283,286)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 matattntlk nfingkwvda ktdhyqsvpn patgeelaqv pisskqdvdd avntakeafq
       61 swsrtpvpkr arilfkyqql lvenwdelak liteengksf keaygevqrg iecvefaaga
      121 pslmmgkqlp diatniesgm yrypvgvvgg itpfnfpmmv pcwmfplaia cgntfvlkps
      181 ertpllanrl aelfqeaglp dgvlnvvhga hdvvnglleh kdvpaisfvg sqpvaeyiyk
      241 taagngkrvq alagaknhsi vmpnadldaa vkeiiaaayg sagercmacs vvvavgdvad
      301 tlikklneqa daikigngmd edvflgpvir ddhkkktesy iesgvdegat lvrdgrndea
      361 ykdngyfigp tifdnvtssm kiwkdeifap vlsvvrvetl edaikltnes dfgngaclft
      421 kdgsdvryfr efievgmlgv nigvpapmaf fpfsgwknsf ygdlhangsd gvefytrrkm
      481 ltarw
//
LOCUS       WP_175987706             253 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175987706
VERSION     WP_175987706.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..253
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27952
     Region          2..224
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mtileavklh ksygnkfnkq evlkgidlqi tkgefvgimg psgsgkttll nvlssidkvs
       61 egsikienne mtrmkekkla efrknhlgfi fqdynlldtl tvkenillpl sitktpkkea
      121 eskfdtlasq lgilelkdky pneisggqkq rtsaarafih epsiifadep tgaldsksas
      181 dllnklgeln vqlestivmv thdpvaasyc srvifikdgr iytqlnkgdq srqaffkdvm
      241 ktqgvlggvq ner
//
LOCUS       WP_175987718             231 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175987718
VERSION     WP_175987718.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..231
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=26591
     Region          17..227
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mlkkeeikkh lqtvplfkel sdeelqpiis isssriynar siifmqeepl drvffihsgi
       61 vkiyktdatg keqivsvled gemfphagff rqgtfpanae vikkaqlivt pikdfekili
      121 qhpelciklf rvlggkivdl qsrleekilh ntyeqvimll lrlsksngvk qenlykitth
      181 ftnrelanmi gtsretvsrt lnqlrkkdli eldtsgfyvi dpdklkeeii h
//
LOCUS       WP_175987783             238 aa            linear   BCT 11-JAN-2025
DEFINITION  (Fe-S)-binding protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175987783
VERSION     WP_175987783.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..238
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26051
     Region          <2..235
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mkvslfvtcl idifqtdvgr dtvellerlg cevdfpekqt ccgqpaynsg hvekakesmk
       61 hmisvfeesd yvvtpsgscg tmfreyphlf kgdpqweera kslagktyel tqfivevlgv
      121 edvgaklngn atyhtschmt rllgvteapm kllskvdglk mnplphnync cgfggtfsvk
      181 mspiseqmvd ekvtsveetg adiligadcg clmniggrid rkgkpikvmh iasvlnsq
//
LOCUS       WP_175987851             318 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175987851
VERSION     WP_175987851.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..318
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35851
     Region          12..223
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(56..57,59,72..74,80,82..83,124,222)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(56,58..59)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(80,83,86,93)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(116,120..123,125)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(121..122,145..147,195..196)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          236..310
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 mkrhntipvs vasikqeckd vkvftlrpek gsvlppfggg ahittyieke eeviarsysl
       61 tnhaddreyr iairlnehsr ggsacwhhhi ktgdrlrisf pknyfplsfr akhhvlyaag
      121 igitpflamm kelakkgssf elhyvskara scpfytylke nyphqcsfyf seehkklhvt
      181 sllhhpigth vyfcgpqsfi eefreaaksy gypsssihfe rfaapeikes hpfhvvltsg
      241 kvvhvgkdqs lldalleegi papyscrmgr cgtcelkvih grvehydsfl sveekkshgl
      301 ilpcvsrags kgllldie
//
LOCUS       WP_175987892             281 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175987892
VERSION     WP_175987892.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..281
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31046
     Region          3..255
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mvrlytneln igygdhlivk dlsvqipdkk ittiigsngc gkstllkait riishqsgsv
       61 lldgenisrg ntkelakkma ilpqtpesas gltvgelvsy grfphqkgmg rmskkdyevi
      121 nwalevtgts dfkyrqvdal sggqrqrvwi amalaqetdi ifldepttyl dmahqlevle
      181 llqklnieqe rtivmvlhdl nqaarfadyi valkegeivk agdceevith dvlkkvfqid
      241 aaigrdprtn kpmcitynll kgedqhekmd astyaavgai g
//
LOCUS       WP_175987918              68 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Microbacterium].
ACCESSION   WP_175987918
VERSION     WP_175987918.1
KEYWORDS    RefSeq.
SOURCE      Microbacterium
  ORGANISM  Microbacterium
            Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Microbacterium"
                     /db_xref="taxon:33882"
     Protein         1..68
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7321
     Region          4..68
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mstqgtvkwf nsekgfgfis pddggadvfa hysaieatgy rsldenqrve fdvaqgpkgl
       61 qaenirpl
//
LOCUS       WP_175987930             712 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175987930
VERSION     WP_175987930.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 712)
  AUTHORS   Ingmer,H., Vogensen,F.K., Hammer,K. and Kilstrup,M.
  TITLE     Disruption and analysis of the clpB, clpC, and clpE genes in
            Lactococcus lactis: ClpE, a new Clp family in gram-positive
            bacteria
  JOURNAL   J Bacteriol 181 (7), 2075-2083 (1999)
   PUBMED   10094684
REFERENCE   4  (residues 1 to 712)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11909043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..712
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=79015
     Region          1..>71
                     /region_name="McsA"
                     /note="Protein-arginine kinase activator protein McsA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3880"
                     /db_xref="CDD:443088"
     Region          87..710
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mkcqvcqqnq atvevfkrvn nhktrmhmcs acfqqqqskm psglnggfpf delfkgmntg
       61 ghqpqafggq phgpetqtgg sggngildqf grnvtqaaka glidpvigrd kevervieil
      121 nrrnknnpvl igepgvgkta iaeglalkit aedvpsklln kevyvmdvas ltagtgvrgs
      181 feerlkaiis elqnrknvml fideihqlvg agsaegsmda gnilkpalar gelqvigatt
      241 lkeyrqiekd aalerrfqpv mvneptpeqa idilkglrdk yesyhgvtft detieacvkl
      301 shryiqdrfl pdkaidlmde agskmnlqse gkdtsalhkk lnevkaekdr ateeeryeea
      361 aklrdkekei ekqlqngnsk eksvvepeli qsiieaktgi pvgklqsddk krmkeletnl
      421 snkvigqaea vkkvakairr sraglkakhr pigtflfvgp tgvgkteltk tlaeelfgsk
      481 dsmlrldmse ymekhsvskl igsppgyvgh eesgqltekv rrnpysilll deiekahpdv
      541 qhmflqiled grltdsqgrt vsfkdtviim tsnagvtdkk eavvgfdtvg tdavketnil
      601 kslgayfkpe flnrfdsiie fqslekeell qildlmiadl qaelndqkit vtvekdakek
      661 laelgyhpef garplrrviq eqvedkiadl lleeedinem ivslendeiv vk
//
LOCUS       WP_175987941             166 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175987941
VERSION     WP_175987941.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..166
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=18456
     Region          10..145
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mkwwhnekvs viwtvfriwl gikwfeagwh kvndgfdasg flqgamakat gehpavqgwy
       61 aaflegfavp nvelfnilip wgevlvglgl itglmtipal lagafmnlnf lmagtistnp
      121 illtvavill ftgkgayywg adhwvmpylk qnllhnknqh kkafvv
//
LOCUS       WP_175988040             164 aa            linear   BCT 11-JAN-2025
DEFINITION  STAS domain-containing protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175988040
VERSION     WP_175988040.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..164
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18603
     Region          33..147
                     /region_name="STAS_RsbR_RsbS_like"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist domain of the 'stressosome' complex proteins
                     RsbS and RsbR, regulators of the bacterial stress
                     activated alternative sigma factor sigma-B by
                     phosphorylation; cd07041"
                     /db_xref="CDD:132912"
ORIGIN      
        1 mtndstlihe lkeeisqlkk qlaeseelir disapiipsi vpetilvpit grlfperfem
       61 iitrilnesy redihtiiid fsaisekeic eldvfgtyid nmakaislmg vevifvgftp
      121 sltqiivnsg lqqilevksf lsfrtalqyl mqqrglqfqn indq
//
LOCUS       WP_175988007             603 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175988007
VERSION     WP_175988007.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 603)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 603)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 603)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..603
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=68915
     Region          150..594
                     /region_name="YesM"
                     /note="Sensor histidine kinase YesM [Signal transduction
                     mechanisms]; COG2972"
                     /db_xref="CDD:442211"
ORIGIN      
        1 mlknsirnkl ivllmittiv pfgssivity lytknsiedq vvaesrnlly qgkinlesyi
       61 nelndltlsl ynnpdfinym rnpgqendyl tigivknvvq tilytadtit gvkisfened
      121 rvisatkrsn vvfssekket kkeaflraer spynmyiept fpqkeneikr skniitvhra
      181 frnipddevl ayisleispe kiidlsrnly taeteefyil tpqgemiyss dldvsddqnn
      241 qkwikriveg kelagtlewk edefngvimy dqlpvsaggw ilakrvsyan lyesafsvak
      301 inilfgilgl tlvvlatlfv sfkitspirv llkniqqvek gnmnvqlpsf gpdeigllgf
      361 rfqqmiervn mlinreykle lenknnqlkv lqsqinphfl ynalqsigtv alknkvpqvy
      421 tlitylskim rygmnmeedm vpldkeisyt kaflllqker fgenldytik vdervreaav
      481 pkmilqpiie nyfkhgfdir egigkielnc mskddqlvit iedngigvtg erleevfahf
      541 kaaalnnige dtniglknvf vrlklyyddd aalllenpae ggfkvtmklp ikmegeanes
      601 nhh
//
LOCUS       WP_175988090             276 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175988090
VERSION     WP_175988090.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..276
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31528
     Region          13..272
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 mlknlqskkt lhngieipyv glgvfqmkdp retveavksa ietgylsvdt aavyeneesv
       61 gqgvkessar redlfitskv wnsdqgydtt lkafetslkk ldmdymdlyl ihwpvegkyk
      121 dtwkalerly seglvksigv snfhqhhled lmsssnekpv inqiechprl nqeklraycq
      181 deniaveaws piaqgrvlde tilkqiaekh gksaaqvilr whlqndvvii pksvhsnrik
      241 enadlfnfel stdemnqind lnqderfgpd pdnfdf
//
LOCUS       WP_175988114             180 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175988114
VERSION     WP_175988114.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..180
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19304
     Region          1..153
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mniviingsp rkrgrtgiaa rfmartynad lidlsdgtlp lytgeqeqae vssvqslkqk
       61 vkkadavila speyhsgmsg alknaldfls seqfahkpva llacagggkg ginclnnlri
      121 vargvyanvv pkqlvldphc fdydhdglle epaklvddmv qelkvyvkaa eivqneapak
//
LOCUS       WP_175988137             299 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175988137
VERSION     WP_175988137.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..299
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=34823
     Region          26..275
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 midllpnwnl ekvniislqs nimkvtsggn tfylkkrngt ssterleeyl itqylvrkgf
       61 pvetplltnk gevfinsdes fyslyasldg tsfynssfvt sqhsfslgvy larfhqaler
      121 ypykketavw nvygylkswl svpnpelnew gkrvyagiaq herlyeqlpp qlvhsdlhlr
      181 nflwqgqdis glvdferiri aprvadiayl itsilrdtgr qsdpthslkk ihqilkgytk
      241 nkklrkreil sipplvilff lqytlfysqr ghmkeveyhv nkvdfmisdt rylesltdf
//
LOCUS       WP_175988180             365 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175988180
VERSION     WP_175988180.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 365)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..365
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40797
     Region          1..364
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 maelkleniy kiydnkvtav ndfnlhindk efivfvgpsg cgksttlrmi agleeiskgd
       61 fsidgkrvnd vapkdrdiam vfqnyalyph msvydnmafg lklrkfdkke idrrvqqaak
      121 ilglealldr kpkalsggqr qrvalgraiv rdakvflmde plsnldaklr vqmraeiakl
      181 hqrlqtttiy vthdqteamt matrivvmkd gviqqvgspk evydkpenvf vggfigspam
      241 nffhgkieeg sfvigkskva vpegkmkvlr dqgyvgkdii lgvrpedihd epifidtaqg
      301 akitakievs eltgaetmly sqiegqdfva rvdsrtdina gqtielafdm nkahffdses
      361 efrir
//
LOCUS       WP_175988242             247 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175988242
VERSION     WP_175988242.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 247)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..247
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27626
     Region          4..244
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 malleinhli ggytrkpvlk disfsinsre ivgliglnga gksttikhii glmepkqggi
       61 ainghtlken adqyrkqfsy ipetpilyde ltleehlklt amayglteee ykgrvgkllk
      121 afrmekklgw fpahfskgmk qkvmimcafl iqpslyiide pfvgldplgi qslldwmeem
      181 kqsgagilms thilataery cdsfvilhdg kirakgtlke lqsefsmpga tlddiyiqlt
      241 keesdde
//
LOCUS       WP_175988318             391 aa            linear   BCT 11-JAN-2025
DEFINITION  thiolase family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175988318
VERSION     WP_175988318.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 391)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..391
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=41462
     Region          1..391
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mrnvvitsal rtpvgafgga fkdllptdli vpvmkeaakq snlhsseide vilghciqrt
       61 dqpntartaa llsgfddttt gftiqrqcas gmqaiisaal qiqtglseiv laggveamss
      121 spyilkqhrf gqrlqhgevr dsvwevledp ihgimmgeta enlaeshdis reeqdqfaml
      181 shqravnaie kgyfdsqivp vtikgrkgek vigtdesprp gltadklanl kpafreggtv
      241 tagnssslnd ggaalilmse eeaekkglqp lariagysva gvdpkimgig pvpaiqdgih
      301 kgnwtldeid lfeineafaa qylavekelg ldrnkvnvng sgisighpvg ctgariavsl
      361 vhelkrqnlk kgiaslcvgg gmgasvlles l
//
LOCUS       WP_175988383             284 aa            linear   BCT 11-JAN-2025
DEFINITION  YitT family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175988383
VERSION     WP_175988383.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..284
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=31327
     Region          9..284
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mnrdhvhlea kkfvvvliga ilgaiamnff lipanvyasg ftgmaqllss iikeftqfnv
       61 stgillfiln ipvtiigwfk vgksftvysf isvfltsffl evipvihlsp dillnavfgg
      121 viaavgvglt lkwgastggm diiamilsrm kdrpvgsyff vmnaviiisa gflygwekal
      181 ytlvtlyast rvidaihtrh ekltamiitk ksqelreaih sklmrgittv pakgafsgea
      241 kemmiivisr yelyelehti kevdpnaftn ivqttgifgf frrd
//
LOCUS       WP_175988494             141 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175988494
VERSION     WP_175988494.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..141
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15884
     Region          9..141
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mkvviakses qleevfqvrk tvfvneqnvp leeeidefen qsihfilyed dqpagagrfr
       61 vldgvgkver icvlknirgk gagrelmlai eqyaynhsis klklnaqtya ipfyeglgyq
      121 tvseefmdag iphktmvktl s
//
LOCUS       WP_175988516             384 aa            linear   BCT 11-JAN-2025
DEFINITION  thiolase family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175988516
VERSION     WP_175988516.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 384)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..384
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40836
     Region          1..382
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 mrevvivegi rsavgrrnga lksmrpddla geilkglmkk sgvdpgsvdd vilgcvtqsg
       61 eqagdiarva aliagfpvev pgttidrqcg ssqqavhfaa qailsgdmdi viaggvenms
      121 rvpiasnygk agfseklkeq heiihqglsa eriaekygfs reeldrfasq shqkalqaqe
      181 dqrfegeihp idipteeggt fifskdegpr qgttvdvlst lkpafkedgi ihagnasqis
      241 dgaaalllms rekadelglk arfkvhtrvv tgsdptlmlt gpipatkkal kksglsledi
      301 dvfevneafa pvalawlkem radparlnpn ggaialghpl gasgarimvt mmhelertgg
      361 hfglqtmceg hgmanatiie rles
//
LOCUS       WP_175988544             357 aa            linear   BCT 11-JAN-2025
DEFINITION  GGDEF domain-containing protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175988544
VERSION     WP_175988544.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..357
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41020
     Region          190..337
                     /region_name="GGDEF"
                     /note="Diguanylate-cyclase (DGC) or GGDEF domain; cd01949"
                     /db_xref="CDD:143635"
     Site            order(223,267)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143635"
     Site            order(228,231..232,236,240,263,265..268)
                     /site_type="active"
                     /db_xref="CDD:143635"
     Site            order(259,287)
                     /site_type="active"
                     /note="I-site [active]"
                     /db_xref="CDD:143635"
ORIGIN      
        1 mkislylndy eteklfsylr wlfllvsvmi fyvppfsinl psqkelfpyl ltagiiymlv
       61 tqvalygmrd nkknlhyilk agilfdyial iwlmalsggi hsplypisil fvlhatiywr
      121 tkgavislfa fniayigmgl lsvdvflfkh yftvlmnlff lciigvfgal imlrershyv
      181 qkeayhylvh qdylsglsnh rsfqeklken aasgnyfslf lgdiddfkkv ndkyghqkgd
      241 evikevgeif qavslrykgq afryggeefa lmlpdideed lnsllddlyd qmrdarslsi
      301 smsfgqscsk egndpaelll fadqrlykak qagknrvflq sgevyigkfd qdmklak
//
LOCUS       WP_175988557            1028 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175988557
VERSION     WP_175988557.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..1028
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112983
     Region          1..1018
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mkisdfsirr pvftivtmll ililggvsll riplklipdl nppvgvvvtn ypgaspdevv
       61 ekvtkpleen lstlpgmkni qstsregsnf illefswtts ideiendvlq ridqsplpdg
      121 aqeprflkfd laqfpiiqvs lreegdgnnl kalseklkle ltrvegvanv nvsgsfndev
      181 vieldqqalr enrmkqadiv nairannits pgdtietdgq tlttrvisql ksadeikklv
      241 vgvnpqtgkd ltledvatve rkeestntst ranqepavlf svlqqsdant asvskefqee
      301 larlleqeqy qsikanilfd qgdyisdaig nitnslligg afamlvlflf lrnvksplii
      361 gvaipysviv tfvlmffadf tlnimtlgal algigmlvdn aivvieniyr hlslgkdpkt
      421 sasegakevg aaitastltt vavflpvvfi sgllgelfte faltisfsli aslvvaltvi
      481 pmlasrllkk pkgnlearrr rsktrkrfiq sikwslrhrf vilmitvvtl vaggyglttv
      541 gtqflpptde gffnmrvele ngssiketnk tvkaieknlk gqkevdvfvs lvgttqeesf
      601 rgsekgniae iyvkmkplee rgrsifefad dikpeiekaa qsvndsaeis fnlqstsgts
      661 pqtltfnvrd tdperldksv drlfdslkdm knvtalstdk metvkeiqmn vnedealkqg
      721 ltpaqigstv qditrgvmat qivtkesdvl svfvqydrni tenldslkkl lipngrgeyi
      781 aldsvvdfsi edgpvsiqri dqqhavqfdl kyssstnlgt isqsvdekie elnlpdatqv
      841 sfsgdrelle dsiddmalal glaivlvylv maaqfesfky pfvimftvpl mvigvalslt
      901 itrtpisisa iigvivlagi vvnnaivivd yinqrketap nsfeaiveav qdrtrpilmt
      961 alttilgllp lalgigegte inqpmgiavi gglvsstllt iyvipvvysf fdketrrmkr
     1021 knkytyky
//
LOCUS       WP_175988569             450 aa            linear   BCT 11-JAN-2025
DEFINITION  TrkH family potassium uptake protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175988569
VERSION     WP_175988569.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..450
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49489
     Region          14..445
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mwlllrskln kltpaqvivt yyllavtvat illslpaahk pgvdwkfida lftsvsavsv
       61 tgltvvstad tfsttgifll ifvlqfggig vmavgtffwl lvgkkiglke rrlimtdqnq
      121 tnlaglvnll kqillliiii eiiggltlgv yflsyyptwq eafiqglfas vsattnagfd
      181 itgqsmipfk hdyfvqfiti ilitmgaigf pvlietkdfl mnskrskhhf slftkittlt
      241 facllvfgtv miiileynhf fngmvwhesf fyalfqsast rsgglatmnv aefstttlll
      301 lsglmfigas pssvgggirt ttfalnllfl fhfargnqti kifrreiheq diikslvvti
      361 vatilcfcsi lilslteshs lieiifevss afgttglslg itselstigk cvimilmfig
      421 rvgilsflfm iggkektany hypkerviig
//
LOCUS       WP_175988626             260 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175988626
VERSION     WP_175988626.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001272
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..260
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28703
     Region          4..260
                     /region_name="FetB"
                     /note="ABC-type iron transport system FetAB, permease
                     component [Inorganic ion transport and metabolism];
                     COG0390"
                     /db_xref="CDD:440159"
ORIGIN      
        1 mekgiiniel wrfiaayafi lilliivklr gisrekqiii aslrmtiqli iagyiltyif
       61 dnpspwltll iilvmevfai rnvfkqvkhe lskqlkatvs iamtagtlgc lfyfnivvih
      121 ftpwyepryf ipiagmivgn smtgitlgln tllgglkdqr evvegalmlg atpkaaskky
      181 vdnafdsail ptlnnmigmg iiflpgmmtg qilsgvsplv aieyqiaill givgsvaltv
      241 ilfiylgykf lftkhcqlni
//
LOCUS       WP_175988834             270 aa            linear   BCT 11-JAN-2025
DEFINITION  cell division protein FtsQ/DivIB [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175988834
VERSION     WP_175988834.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..270
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=30582
     Region          13..239
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mrkenvvsie eripklkqhr kkkanrrllf lltlflimil sviyfqspls hvktievkgn
       61 eivssetils esklkpgmnl wsvnknetae rlnklpevks aevklsfpns fvievdelgk
      121 kayllkdnkf liilengkvl nkgtesipvd apllrgfked ktlkkmisel gelpkevqhl
      181 iseinlvpkk tdqyhltlfm ndgyevsati rtfsekmehy psivsqldps kkgiidlevg
      241 syfrsyetea eaeseaqeqg egddgdeseg
//
LOCUS       WP_175988891             892 aa            linear   BCT 11-JAN-2025
DEFINITION  cation-translocating P-type ATPase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175988891
VERSION     WP_175988891.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 892)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 892)
  AUTHORS   Cross,R.L. and Muller,V.
  TITLE     The evolution of A-, F-, and V-type ATP synthases and ATPases:
            reversals in function and changes in the H+/ATP coupling ratio
  JOURNAL   FEBS Lett 576 (1-2), 1-4 (2004)
   PUBMED   15473999
REFERENCE   3  (residues 1 to 892)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   4  (residues 1 to 892)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..892
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..892
                     /product="cation-translocating P-type ATPase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=97112
     Region          2..882
                     /region_name="MgtA"
                     /note="Magnesium-transporting ATPase (P-type) [Inorganic
                     ion transport and metabolism]; COG0474"
                     /db_xref="CDD:440242"
ORIGIN      
        1 mkyhemrqed iekslntdyt nglseedvsk rrkqfgynql eeaekqsnll lffsqfkdfm
       61 vlvllaatli sgllgeyida vaiiaivlin gflgffqerk aekslqalke lsapqvtvlr
      121 egswvkvlsr evivgdimrf gsgdrigadv rlidannlei eesaltgesv pvskstspva
      181 gdhislgdle nmafmgtmvt rgngvgvvta igmktamgqi admlqkaesm vtplqrrlee
      241 lgkilitval iltalvvgvg viqghdiytm flagvslava aipeglpaiv tvalslgvqr
      301 mikkkaivrk lpavetlgca svicsdktgt ltqnkmtvth lwsggrnwsv tgtgyepdgq
      361 fysgeervsp hnqkalnqll tfgmlcnhae lvtrddsfav dgdptegall vagikaglnr
      421 eallqkfkiv kefpfdstrk mmsvividqn gkqfsvtkga pdvlaanses ilwddklqfk
      481 tgdlsqrvdn aisemssnal rniaigykpl ngvkaeslse kdveegitfi glqgmidppr
      541 pevkqavrec kaagiktvmi tgdhlltaka iaaqlgilkr ndkvldgkal nemdveelqe
      601 vvedvsvfar vspehklkiv kalqnrghvv amtgdgvnda paiksadigv amgitgtdva
      661 kessslvlld dnfatiksai qegrniyeni rkfiryllas nvgeilvmlf amllalplpl
      721 vpiqilwvnl vtdglpamal gldkpeddvm krkprnmneg vfarglgwkv vsrgfliglv
      781 tllafilayk ahpdhlayaq tvafatlvma qlihvfdcrs evsvfsrnpf gnmylvwavi
      841 sslvlmllvi yipslqpifh tvpielkdwm lilglsslpt fllagsffar kk
//
LOCUS       WP_175988767             161 aa            linear   BCT 11-JAN-2025
DEFINITION  PaaI family thioesterase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175988767
VERSION     WP_175988767.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Song,F., Zhuang,Z., Finci,L., Dunaway-Mariano,D., Kniewel,R.,
            Buglino,J.A., Solorzano,V., Wu,J. and Lima,C.D.
  TITLE     Structure, function, and mechanism of the phenylacetate pathway hot
            dog-fold thioesterase PaaI
  JOURNAL   J Biol Chem 281 (16), 11028-11038 (2006)
   PUBMED   16464851
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..161
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=17089
     Region          55..157
                     /region_name="PaaI_thioesterase"
                     /note="PaaI_thioesterase is a tetrameric acyl-CoA
                     thioesterase with a hot dog fold and one of several
                     proteins responsible for phenylacetic acid (PA)
                     degradation in bacteria. Although orthologs of PaaI exist
                     in archaea and eukaryotes, their function has not...;
                     cd03443"
                     /db_xref="CDD:239527"
     Site            order(75,104,111..114)
                     /site_type="other"
                     /note="CoenzymeA binding site [chemical binding]"
                     /db_xref="CDD:239527"
     Site            order(76,78,81,105..109,111)
                     /site_type="other"
                     /note="subunit interaction site [polypeptide binding]"
                     /db_xref="CDD:239527"
     Site            order(77,85..86,89..90,104)
                     /site_type="active"
                     /note="PHB binding site [active]"
                     /db_xref="CDD:239527"
ORIGIN      
        1 mqeelhklld evleradeee lisirqllng vkrkqnkqne siiggifame kssvdgifti
       61 sipitavthn slqivhggvt atlvdtamgt lanmmlpegy gavttnlnvh ylapgigegl
      121 tasativhqg sktmvvdgkv vnssgkvvah stgsffifkk d
//
LOCUS       WP_175989066             555 aa            linear   BCT 11-JAN-2025
DEFINITION  ribonuclease J [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989066
VERSION     WP_175989066.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Li de la Sierra-Gallay,I., Zig,L., Jamalli,A. and Putzer,H.
  TITLE     Structural insights into the dual activity of RNase J
  JOURNAL   Nat Struct Mol Biol 15 (2), 206-212 (2008)
   PUBMED   18204464
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426779
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..555
                     /product="ribonuclease J"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0004521 - RNA endonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0004534 - 5'-3' RNA exonuclease activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /GO_process="GO:0006396 - RNA processing [Evidence IEA]"
                     /calculated_mol_wt=61536
     Region          4..555
                     /region_name="RnjA"
                     /note="mRNA degradation ribonuclease J1/J2 [Translation,
                     ribosomal structure and biogenesis]; COG0595"
                     /db_xref="CDD:440360"
ORIGIN      
        1 msktknevir iiplggvgei gknmyvvevd heifiidagl mfpenemlgi divipdiqyl
       61 iehkdrvkgi flthghedsi gaisyvlnri kapvygtklt nalvkarlkd ahveedvkff
      121 nvhsdsllnf dgvqvsffrt thsipdsvgv cihtsegviv htgefkfdqs akhlyrpdlg
      181 kmaaigdkgv lcllsdstea erpgyttsea viasqltetf rtakgriiva cfasnlirlq
      241 qvfdaaeqnn rkvavvgksl krvydvalkl gylhirdeim itldeienhp ndeiviiatg
      301 nqgepfealq rmakkshrlv niesgdtvli tatpspgmev iigrtvdmlf ragaevltan
      361 kkvhvsghgs qedlkfmlni mkpkhfipiq geykmlvahs kvahdiglpy kkifildkgd
      421 vleykggkmk msgrvqagnv lidgsgvgdv gnivlrdrkl lsedgvftvv vtinrrskti
      481 vagpeiisrg fvyvreseel iegasgivsd vvqtylqkgs fewsaikqdi rdqlnyylfn
      541 ktrrrpmilp iimev
//
LOCUS       WP_175989084             307 aa            linear   BCT 11-JAN-2025
DEFINITION  dipeptidase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989084
VERSION     WP_175989084.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..307
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=34605
     Region          1..301
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 mifdahcdvl mklyidpdnl sfqskqdmhi typqlneggs kvqlfaiyip sylkpgqrfh
       61 aalnmvnlfh rkildphhnv klvtskqdid nlsqneigam ltlegaeaie edlekletly
      121 rlgvrsvglt wnwanaaadg aleprggglt nfgfemvnfl nekkmwtdvs hlcekafwdt
      181 leaslypias hsnaysicpn prnlkndqie alikkdsvmg vtfvppflnk ngsavltdiv
      241 rhvehicslg gedhvgfgsd fdgidqtvkg lssyqqydnl igtlqryysd kqikkflfgn
      301 fhkriqf
//
LOCUS       WP_175989071             349 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989071
VERSION     WP_175989071.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 349)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 349)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..349
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37489
     Region          3..349
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 msnrltnili pvisvllgii vgtiimlvsg ydpiagytal wqgifgeiyy vgetirqvtp
       61 yilaglavaf afrtglfnig vegqlivgwm aavwvgiafd dlpkiihlpm aiiaaalaga
      121 iwgfipgllk akyrvheviv timmnyialh vtnsiirdvl terkdrtdyi adsasltspf
      181 fesitdysrl hwgifvalac vfimwfllek ttrgyelrsv gfnqhasqya gmnvngniil
      241 smvisgafag lagameglgt fgyasikggf tgvgfdgiav allggnvaig vvfaallfgg
      301 lkvgalnmpl eagipnelvd iiialiiffv asgymiryli qrfskkgvk
//
LOCUS       WP_175989092             171 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175989092
VERSION     WP_175989092.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..171
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18263
     Region          <9..161
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(38,40,44..45,48..50,52..53,57,60,69,71,79,83,86..88,
                     90,93,97,100,109,111,113,117..118,121..123,125..126,130,
                     133,142)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          38..69
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          71..109
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          111..142
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mtpvtvkgff aaiqngdidv veqslqadtn lcnaedengl ialgvaahyg qmgivqllln
       61 ygadiksvsn skvsyipsns alhaaiagka pkelveflli egadihgids egytplhvaa
      121 fegdedlvtl llefsadpdf rndanqtpfd iaedrgnmdf isacerystr l
//
LOCUS       WP_175989106             213 aa            linear   BCT 11-JAN-2025
DEFINITION  DedA family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989106
VERSION     WP_175989106.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..213
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23521
     Region          1..194
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mlefiinair elgmwgllag naieasslpf pgvlvtltyg ylldpswgkl islaifssli
       61 ytvfsyipyv igfkikhtik dktndkntrk vekaqkwfrk ygvwsialsr plgignyisy
      121 asgiskvnki kfgvltfigi fpvtfimliv gknghlesvq almssvqnyi figgavllil
      181 yiaykflysa kkkkggdssq enitpktakq ges
//
LOCUS       WP_175989113             202 aa            linear   BCT 11-JAN-2025
DEFINITION  trimeric intracellular cation channel family protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175989113
VERSION     WP_175989113.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..202
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=21628
     Region          1..195
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mtwevlsiig tiafavsgai iameeeydil gvyilgivta fgggairnll igvpvsalwe
       61 qgmlfqiall aitavfifpn nllkhwrrwg nffdavglsa faiqgalyas emshplsavi
      121 vaavltgsgg giirdllagr kplvlrseiy avwavlcgaa vglgiasssf elytlfiltt
      181 alrvlsylyk wrlpnrslra hg
//
LOCUS       WP_175989155             281 aa            linear   BCT 11-JAN-2025
DEFINITION  STAS domain-containing protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989155
VERSION     WP_175989155.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..281
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32442
     Region          165..273
                     /region_name="STAS_RsbR_RsbS_like"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist domain of the 'stressosome' complex proteins
                     RsbS and RsbR, regulators of the bacterial stress
                     activated alternative sigma factor sigma-B by
                     phosphorylation; cd07041"
                     /db_xref="CDD:132912"
ORIGIN      
        1 mhinkdlhsf llskarelte awyntidknk asgvysssdp kvienlknqn fefhqlfcev
       61 fmidkqtfnk rlddwvltia edkhhletpt hniiqefmrv rnqyldfvne faqnypeeni
      121 fdqmrmwedi viesfdraml rfmelqnqvv ekqlhsqqqi ihelstplis lnedtalvpl
      181 ignidptrak lilentleqc vqkevsylfi dlsgvvmidt mvahqlfqli daleligvkp
      241 ilsglrpeia qtavqlglnf drltitstla qaitinskah s
//
LOCUS       WP_175989235             160 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989235
VERSION     WP_175989235.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 160)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..160
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=18151
     Region          8..128
                     /region_name="YjhB"
                     /note="ADP-ribose pyrophosphatase YjhB, NUDIX family
                     [Nucleotide transport and metabolism]; COG1051"
                     /db_xref="CDD:440671"
ORIGIN      
        1 mqmpthivav ggivedkkgn illvrtvhrg wetpggqvea genlmdalmr eikeesgidv
       61 evsqmigvys ntgtyiwhdg etevptkvmf dflcyergge lgvseettds rwvekdkvle
      121 fiespalrtr yqayldfkgn ihymeyvtkp efelkvkrsv
//
LOCUS       WP_175989240             279 aa            linear   BCT 11-JAN-2025
DEFINITION  STAS domain-containing protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989240
VERSION     WP_175989240.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..279
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32010
     Region          160..269
                     /region_name="STAS_RsbR_RsbS_like"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist domain of the 'stressosome' complex proteins
                     RsbS and RsbR, regulators of the bacterial stress
                     activated alternative sigma factor sigma-B by
                     phosphorylation; cd07041"
                     /db_xref="CDD:132912"
ORIGIN      
        1 mnttfenked isqfivenrk nfqekllsea invgskindi lekgnidllk naerlalyva
       61 eskeeelvef akvegvawae hsltlsfkle wvqairrtlw hflykyeqir eaelnrerff
      121 elekrindhv dhflnsffis ysdykdeqls sqrklvehls vpiipisssi avlpligkid
      181 syriqaieek ilmniaslki qtliidmsgv admeidvivh lqrllgginm mgceavltgl
      241 rvdlvrkmih sgvsfeqnal tkgtlqqtlk eylvlepge
//
LOCUS       WP_175989306             435 aa            linear   BCT 11-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175989306
VERSION     WP_175989306.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..435
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=48240
     Region          9..422
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mkrvrlhqkl sitiisfmal ssfgsvvhge skakinadaa ilvnadtgki vdkynedell
       61 giasmtkmmt eylvleaidk gkikwsdtyt vsdkvyqlan apglsnvplr adekysikel
      121 yeamviksgn gaaialsevv agsegefvkq mnakakdlgm erfqfvnssg lsnydmlgmh
      181 pegtdvnden mvsaedmatl ayylikdype vlktsganyk yfrkgtdeey lmkntnamlk
      241 drahfyegad glktgttpfa gstftgtaer dgvryisvil dakdqygqps saerfiqtga
      301 lldygftqvq taqfslddav kkktlpvkdg kefevemavd kplkvripkd eisnvnvrfn
      361 vdkgklnkng elqapiekge kigelvlvnk kkdeyildel eketkvdvya dssvekanwf
      421 vrsarnigef fgklf
//
LOCUS       WP_175989312             146 aa            linear   BCT 11-JAN-2025
DEFINITION  HIT family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989312
VERSION     WP_175989312.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..146
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16903
     Region          5..137
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 msnhsclgcr lankeekvyl vhensllsci ldhepyntgh vmilpkqhve egvefneeln
       61 lsvmkaiqii sktiqalynp dgiticqngg ifsdlthyhm hviprykgqd faefyqedes
      121 iwepdepfev ttekmkeyie rlmeke
//
LOCUS       WP_175989313             132 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989313
VERSION     WP_175989313.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..132
                     /product="VOC family protein"
                     /calculated_mol_wt=14921
     Region          7..112
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 miyemtiqvr vpnmkegqsw yetllsrgpd fvphdgfaew ellpgcwlqv aegspapgsg
       61 pirlgvadle aekerlmgll evedfcihsr eevpvkwatf kdpwgngigl fqyldqqeiq
      121 nrivtilgrh iq
//
LOCUS       WP_175989318             186 aa            linear   BCT 11-JAN-2025
DEFINITION  glycerol-3-phosphate responsive antiterminator [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175989318
VERSION     WP_175989318.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..186
                     /product="glycerol-3-phosphate responsive antiterminator"
                     /calculated_mol_wt=20915
     Region          3..180
                     /region_name="GlpP"
                     /note="Glycerol-3-phosphate responsive antiterminator
                     (mRNA-binding) [Transcription]; COG1954"
                     /db_xref="CDD:441557"
ORIGIN      
        1 msfegqkilp airsmkdfdk mletsfkygv fldlhvgmlk svfqyakqqn rnmflhidli
       61 hglsndeyga eyicqevkpy giistkgnvi kkarqkgvya tqrmfvidss amkrsielih
      121 ktepdyievl pgvvpkiite irektgkpif agglidtiee veaaidagat aittsdralw
      181 khfdqk
//
LOCUS       WP_175989319             276 aa            linear   BCT 11-JAN-2025
DEFINITION  MIP/aquaporin family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989319
VERSION     WP_175989319.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..276
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28984
     Region          1..234
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mtaflgevig talliifgag vcanvnlkes faynsgwivi tfgwglgvam svyavgqfsg
       61 ahinpavtlg lafngdfpws qvpqyilaqm lgaiigaiit ylhflphwha tkdpgvklgv
      121 fatgpaiphv fsnllseiig tfvlvvglls igantftdgl npfivgflii aigislggtt
      181 gyainpardl gpriahfllp ipgkgpsnwg yswipvlgpv lggsfgglfy kavftgqvtt
      241 sfwvvlfitl svlgaaylsd rkltlsqkve klsaen
//
LOCUS       WP_175989368              60 aa            linear   BCT 11-JAN-2025
DEFINITION  CsbD family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989368
VERSION     WP_175989368.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..60
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..60
                     /product="CsbD family protein"
                     /calculated_mol_wt=6859
     Region          4..58
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 mrenkdqikg krkqtkgdlk ktwgkltmdd qkiaegersk dkgkiqekvg dvkeslkksw
//
LOCUS       WP_175989355             385 aa            linear   BCT 11-JAN-2025
DEFINITION  CapA family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989355
VERSION     WP_175989355.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..385
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=42991
     Region          57..346
                     /region_name="CapA"
                     /note="Poly-gamma-glutamate biosynthesis protein CapA/YwtB
                     (capsule formation), metallophosphatase superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2843"
                     /db_xref="CDD:442091"
ORIGIN      
        1 mnrklyvtsl ilviplmlit gylmmdqyks wnsdkqpekg tsllhatrev qaegktmkst
       61 asiaaigdil lhntvyndak sgsqydflpm fapvrdilse pdflianqes tpggseigls
      121 syplfnspke ivkslqevgv davttannhs ldqgeeglls aidyyeeism pyvgafkspe
      181 dkekirtfnv ngikfallsy tygtngipvp egkdylvnll deqkmvaeik kartmdidlv
      241 vmslhwgney qrfpteeqqr lakvltenga diifghhphv lqpiqtykts dgrdavviys
      301 lgnflsgqkd dfkdiggvae vqvekqrnpa gavitypsie fhptfvaenn yknyriypld
      361 faqkngfity tedemvshmm dgvpq
//
LOCUS       WP_175989366             150 aa            linear   BCT 11-JAN-2025
DEFINITION  PH domain-containing protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989366
VERSION     WP_175989366.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 150)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10535482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..150
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16733
     Region          67..140
                     /region_name="bPH_4"
                     /note="Bacterial PH domain; pfam06713"
                     /db_xref="CDD:369049"
ORIGIN      
        1 mrfyskkgkv lfpvlimvli lmagssltsy ldwdfvkhip gidesdrvsl fvtvpvmvli
       61 lwliagtyye ingevlkvaa gpirytihih tisaikasnn plsspalsld rlkitynhgn
      121 tvlispkdkq efineilkvn pnikvnlkkk
//
LOCUS       WP_175989369              60 aa            linear   BCT 11-JAN-2025
DEFINITION  CsbD family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989369
VERSION     WP_175989369.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..60
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..60
                     /product="CsbD family protein"
                     /calculated_mol_wt=6884
     Region          4..58
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 mkenkdqmkg krkqtegdlk ktwgkltmdd qkvgegerdk dkgkiqenfg dvkesikksw
//
LOCUS       WP_175989382             376 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989382
VERSION     WP_175989382.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..376
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41528
     Region          1..115
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
     Region          121..296
                     /region_name="POD-like_MBL-fold"
                     /note="ETHE1 (PDO type I), persulfide dioxygenase A (PDOA,
                     PDO type II) and related proteins; MBL-fold
                     metallo-hydrolase domain; cd07724"
                     /db_xref="CDD:293810"
     Site            order(173,177,233,251,254,258..260)
                     /site_type="active"
                     /db_xref="CDD:293810"
ORIGIN      
        1 msvksisvke iaqkviknek afildvrkkg dfndwkvegk sievlntpys dlvdgidpiv
       61 dhlpkdepiy vicskgnssk kaaeqiaghg ydnvysiegg mqawsehlep ikvgdlksgg
      121 tiyqfvrigk gclsyfiesn gegavvdttr mtevfenfak ekgvkikali dthlhadhis
      181 ggrkladssg aeyflppkda eevifgftpl eegndikigd svisihplys pghtigstsl
      241 iidesylltg dilfidsigr pdlagkagdw andlrhslye rykalddeli vlpahfmtik
      301 emnedgsvae klgvlykenh glniedesef rkavsedlpp qpnayqeire tnmgkitpdd
      361 dkqremeigp nrcaik
//
LOCUS       WP_175989440             215 aa            linear   BCT 11-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175989440
VERSION     WP_175989440.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..215
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=24535
     Region          32..214
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mtnrlkidkp kiqpnlkkaq fedvyyeedp llaeceirna fvegeelekl hvssvyfksv
       61 rllnssfrka dltdvvfdnc dlsntrfeeg ifhrvtfkdc kllgldlsqa hlknvsfenc
      121 ilnissfiea rlkqvlfeks tlhssnfyqs rlekttfdqc dlndidftvt nlkgidisss
      181 ffekinvead nlrgcivspq qavsfasllg lkvke
//
LOCUS       WP_175989510             249 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989510
VERSION     WP_175989510.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..249
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26896
     Region          52..248
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mnsntrvlfg rlmrtilhsp dtiitvavtp immlllfvyv fggaietgtd syvnyllpgi
       61 llitiasgva ytslrlftdm ksglmarfmt mpikrssvlw ahvltslvsn alavavvila
      121 avlmgfrsga dilewlavvg vlllftislt wlavipglta dsmegatays ypliflpfis
      181 safvptetmp avvrvfaenq pvtsivnsir allyqgsvgs diwtslawci gimviayfia
      241 ntvfkrklg
//
LOCUS       WP_175989632             178 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA thioesterase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989632
VERSION     WP_175989632.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..178
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20234
     Region          7..152
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mqetkhpres lvvntdqvmi ndlnnyntlf ggvlmkkldn natlsarrha rvkecvtast
       61 dsidflypih qtdsvcvesf vsyvghksme ifckviaedm itgerrmaat afltfvalde
      121 nkkpikvpei lpeteeekfl fesgkeraen rrirrkhskt lteiiklekp wnmggeas
//
LOCUS       WP_175989644             150 aa            linear   BCT 11-JAN-2025
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175989644
VERSION     WP_175989644.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..150
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=17194
     Region          1..139
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 melfevksep lsleeitkkv erreagaitt figtvrewtk dkrtlyleyq ayepmaakml
       61 aqigkeaeek wpgtkmaish rigrleisdi aviiavssph rkaayeaney aierikdivp
      121 iwkkehwesg eewignqket vpypsgrphl
//
LOCUS       WP_175989661             244 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175989661
VERSION     WP_175989661.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..244
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27121
     Region          1..243
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 misikglkkr fddlevlkgm dvevkkgevi vligpsgsgk ttflrclnal etpnegsvsi
       61 ggmtvdfsek vstaellkfr rrtgmvfqty nlfphmtale nvmegpvvvq gkkkaevren
      121 airllekvgl gdkidyypfq lsggqqqrvg iaralaiepq vmlfdeptsa ldpelvgevl
      181 kvmkdlaeeg mtmvvvthem rfakeaadkv ifmdggyile egtprevfen pkhdrtrqfl
      241 nlir
//
LOCUS       WP_175989702             285 aa            linear   BCT 11-JAN-2025
DEFINITION  YitT family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989702
VERSION     WP_175989702.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..285
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=31129
     Region          1..284
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mhrkiprkem akrvilitlg aiimgvglei flvpnnvidg givgisiils hltglklgly
       61 ifilnipfff igykqigktf afstlygiii lsvttiflhp vpaftqdill aslfggivlg
      121 igvgmviryg gsldgteila ilsskklpfs vgeiimivnl filssagfvf swdramysll
      181 ayyvafkmid itikgldesk svwiisdnye kigdallhrl grgvtylkge gafsgddkkv
      241 ifcvitrled aklkdivseh dpaaflaiad iaevrggrfk kvdih
//
LOCUS       WP_175989722             340 aa            linear   BCT 11-JAN-2025
DEFINITION  inorganic phosphate transporter [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989722
VERSION     WP_175989722.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..340
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=35468
     Region          1..301
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 mnigasgaaa smgvaygaga vksmrtalli csagvllgav lgggevvkti ssgiipqdil
       61 ttkivviill sstlslflan mlgiplstse vtvgavvgag vayqvliies llviimfwil
      121 vplaaflitw ltgkilylle mkgyqfkrrw mgavlvitgf feafsagmnn vanavgplvg
      181 agmlsagkgi wlgglfvalg vvllgsrvve tngkkivqlt kmegivisst gaillmissl
      241 yglpmpltqv tsssiiglga akrgrvmlkk kivskiikiw vvsplislsm syfmiklliq
      301 ldlysivvpf sviiatigal slmkiineek rsvheegggi
//
LOCUS       WP_175989793             379 aa            linear   BCT 11-JAN-2025
DEFINITION  glycerate kinase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989793
VERSION     WP_175989793.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..379
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40089
     Region          2..373
                     /region_name="GlxK"
                     /note="Glycerate kinase [Carbohydrate transport and
                     metabolism]; COG1929"
                     /db_xref="CDD:441532"
ORIGIN      
        1 mkiviapdsf kgsmtsieaa daiqrgveqv nsswettlvp madggegtve aimsilggek
       61 idrrvrdplg rqiqasfgwl setktaviet aaasglpllt yselnpedss tygtgelvec
      121 aldlgvrrii iglggsatvd ggtgflqalg ihfldekrve lsqggkilgh ihtidssnld
      181 prlndvewvv asdvtnpllg eegavsifgp qkgvtkdksm ifeagmkhya qkvrehtgid
      241 cstdkgsgaa ggfgfalkaf fnpsfqsgfs liaelgglhk eikeaslvlt gegkmdaqsl
      301 ygkvpvgigr iakeyhiptv aftgklegtt qnvssegisl vfpivdspms lddamkngsk
      361 llekaaerlm ramtlnnkk
//
LOCUS       WP_175989792             161 aa            linear   BCT 11-JAN-2025
DEFINITION  PaaI family thioesterase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989792
VERSION     WP_175989792.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..161
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=17343
     Region          34..154
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 meeikhaiqd dypddfawcy gcgrlnkdgn hfrtgidgek tvtiytpqpe htalpgfvyg
       61 gliaslidch gtgsaaielh rlnggtvgdg qepprfvtas lhvdfmkptp hgvplkavgt
      121 vekihpkkfk vvtevfaege icakgevvav vmpetflnsl k
//
LOCUS       WP_175989832             309 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175989832
VERSION     WP_175989832.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..309
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34521
     Region          24..292
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 manttpedvk ktvddtvdki idndlwvtlg tntlkiaaim lityialklg rtairnifrv
       61 rskaplkfte rreatllkll envltyvvyf islmtilstl gidikgliag agivglaigf
      121 gaqnlvrdii tgffiifedq fsvgdyvrig saegtveeig lrttkikswt gelhifpngn
      181 itevtnfsih nsiavvdvsi ayeenideae kviqdllitl pqkyedlvnp pellgvqtlg
      241 asdvviriva etvpmrhwyi armirkdvkl vldkhgieip fprmvmysrn edihaqpyhd
      301 kkrlgqeeg
//
LOCUS       WP_175989838             691 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989838
VERSION     WP_175989838.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12036995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..691
                     /product="methyl-accepting chemotaxis protein"
                     /calculated_mol_wt=76522
     Region          56..296
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          <293..690
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mkreklkkkh pkskdkkgsl klssirakli mvfsilfvas liaiiaitsw qtrmktedqv
       61 igqtqgvvke lnssvqlfle qyekslnqys vsnvlknysk aqldpetdaa rdtelyadiq
      121 sdfknylgly qeatsiyias pnkelkivpa vdlpddfdpt srewyqeave aksgavwsep
      181 yidtateeyi itasravvsd nkiigvigvd vnltkltdsv sdmelgyegy pflfgldgta
      241 ivhptlrgen lsdrpfikem leseneqgti hyeldgekkv lvyntvpktn wkvgsayemd
      301 allqsskeie rlllltgavt lvvmlimvvf vsdkmtkpik elqktvteva tgdlsiqssi
      361 kskdetglla sdfnkmiesm retikivqes vlnvrqsaes lsavseetna sseematvvn
      421 eiahgasqsa adsenaqqks ellgtrinev ydnskamaem agrademnqt gllqveelvs
      481 ayhssneyis smekvimsle skvktiesvm etitdissqt nllalnasie aaragehgkg
      541 favvadevrk ladqsvqate qvkstineiq qgsnqavdem aktketfetq yvviqktnev
      601 fdqtsalmkt mqneieqmyk qvgqinldkd evvnviqlma ataeqtaasc eemnasseeq
      661 lraihsvtea aevltdlsqe lqdsiqrfki k
//
LOCUS       WP_175989881             157 aa            linear   BCT 11-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase [Bacillus
            sp. Marseille-Q1617].
ACCESSION   WP_175989881
VERSION     WP_175989881.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..157
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=17690
     Region          4..157
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mtklynklyr spiglidiqg tderitsilf ieeqeaddcg decplvleec ekqldeyfkg
       61 krrtftfpyq ldgtlfqkkv wealtgvsya ktstykdiav tignekavrg vgsangrnrl
      121 sivvpchrii gsngkltgya gglwrkewll rhergli
//
LOCUS       WP_175989861             326 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989861
VERSION     WP_175989861.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..326
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36219
     Region          4..258
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkfdkvrwgi igcgdvtekk sgpafqkvey selvavmrrt gelardyaer hqvpkwydda
       61 dalindpevd avyiatppgs hkeytlkaaa agkpvyvekp marnfkecse mvaackeagv
      121 plyvayyrra qerflkikel ldqkaigdvr yvsttqyqka gddvkdpdnl pwrvqpelag
      181 gglffdlash tldildfllg piqeakgfss nqagyyeaed mvtgtylfqs gvhgvgkwcf
      241 tafenvdrne ivgskgkisf stfgndpvil ttcegqqqws ferpehvqqp lvttivkelt
      301 evgswcpstg esgartnrvm devvgk
//
LOCUS       WP_175989893             302 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989893
VERSION     WP_175989893.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..302
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34273
     Region          1..300
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkiaiiglgd iakkaylpvl sqkegielvl ctrnletlnt ladkyrieek vqsidelitk
       61 eidaafista teahfeiaek llergihvyi dkpismnlge tdrivslake qnkiamvgfn
      121 rrfiprvhel kehgkaslil mqknrfaspd hvrrfvvedf ihvvdtlrfl mntdvrnvkv
      181 eclkdgdelh hlviqllgdg ctaigimnrn ggvteetiey htghhkyvvn slvetthyhn
      241 kdisitkfgd weptlhkrgf yqlvdhfidc aannrtpdps iedslithei cerivksids
      301 qa
//
LOCUS       WP_175989982             406 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175989982
VERSION     WP_175989982.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..406
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44944
     Region          8..387
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(18..19,22..23,26,58,115..116,118..120,123,143,
                     146..147,150,227,230..231,234..236,239,263,267,317..318,
                     322,326,342,345..346,349..350,353)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mkkfsksfka lwagevisef ggaaggiing lllfeltgsk ewmgilwlvy fipslvlqgi
       61 sapflnhvvk ekmlkriqli rafayllpla ghltgspngi itglvllqcl lglmqpiyas
      121 lsfsllpdic keeeladanv lldgtirlms flapgatsll lvvspmhfiy gfscvmflas
      181 yfalsripqt stkkaaawtk kfwweemkeg yntffqyprl lrltilssav qfavgaalvl
      241 svpfirsdln gdawhygifs gafpvgyalg mflltrvskn aqtmylglig gglsfvffyf
      301 vqsiplawlc elfgglifpl fnaqnaaqfq keaprdrlsq lsavrllfir ltmplgilfa
      361 ssavlgtrqt ymvvglaivi pglyyfftsf frrdsrlpvk enqkig
//
LOCUS       WP_175990012             429 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175990012
VERSION     WP_175990012.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..429
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=46457
     Region          <59..429
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mgkerryksg lrkklvffit ilalvtysts affiyfikpt fapdmneflf tsvtlgmgvf
       61 wsavlaffaa gfivkplqrl eqaalkaaeg diavevevpk sddeiralgl afnrmlhnlr
      121 dmvssieenf tktnsnvvdl skasemasqq adaisrtise isagaessam siqttaesve
      181 dviqiaqevq nhsksseqls knmvtelqgs kevihslveg ittlakgned slvvvrrled
      241 nakkveqiiq lvgdianqtn llalnasiea aragehgkgf avvaeevrkl adesgkavqg
      301 isdlikniqt evgnvvgqit nqvttankea ekgsetnevi etmtntihev adsvqkisgl
      361 vdrqmesirl tsqqsqevaa iaeetsagae evseatreqa avmgnvedlt lnlkkqaesl
      421 kgtitrfhl
//
LOCUS       WP_175990160             304 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175990160
VERSION     WP_175990160.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..304
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33538
     Region          1..289
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkdlkigmvg ldtshasvft rllndsgeeh hvrggkvvka fpggspdfel slkridrfte
       61 evrrygieiv etleeaaegt daillesvdg gthleqlrrl ivykkpifid kpfslssvea
      121 eemaelakty gtpimstsal rfsegltnvl srsdkgeiig adcfgpmdfq dgqgyfwygi
      181 havemlfail gggteavtth snedhdcivg wwkdgrigtv rgnrtgsqqf galvhfekgt
      241 eyvnvaadak pfyaslleev idffkegdpg vklsetleii rfleaanesk sredglkmve
      301 ckrk
//
LOCUS       WP_175990163             351 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175990163
VERSION     WP_175990163.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..351
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=38971
     Region          16..328
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mlnpavknsl hegafipahp laitegkeld eksqraltry yidsgvggla vgvhttqfei
       61 rdpefnlyqr vlrlaieemn ragvpdsfik vagicgpvdq avkeaqfskd agydlgllsm
      121 gglqdhseeq llertkkvae iipvfgfylq pavggrvlsy efwealadip nvhaiklapf
      181 drylttevvr avchssrgde ialytgnddn ivndllttyk fkvggevkek kivggllghw
      241 svwtkravel fhelkqlkph dcvpdrmltl aqeitdanga ffdaknqfkg siaginqvla
      301 aqglmkgrwc lidkeelspg qleeidrvra ayphlhddsf veknlerwlg s
//
LOCUS       WP_175990164             352 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175990164
VERSION     WP_175990164.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..352
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38858
     Region          5..349
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkndvnigli gigsiaessh ipnlkaadgv rlaavadvdl drarvisqkh dipqffktad
       61 emfetsqlda vmictpnqth isiavkaaek gihvfmekpi gtdlkevkdy lqlakeknvl
      121 tmvgmphrfr rdarilkgya trgtfgdvyy vkaklfrrrg tpkgwftnka lagggalmdi
      181 gvhvldlaww ligkpearsi tgktitglgn yethyvsswe ssnkqlnsgr ifdvddfgaa
      241 wirfrngavl sletawavng eqdegihiei lgnkggavls plsifteeeg llskhqpvfe
      301 knepfkdeid hfihcirtgs pplidgedgy evlkllmgiy essnlgkeic fn
//
LOCUS       WP_175990198             647 aa            linear   BCT 11-JAN-2025
DEFINITION  beta-galactosidase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175990198
VERSION     WP_175990198.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 647)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 647)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448998
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..647
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=74370
     Region          1..613
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
ORIGIN      
        1 mylgvdyype hwdkslided ltrmkemgvn mirigefawh lmekqegtfd fsffdhvikk
       61 akrqgisvmf gtptatfpaw laknhpdili edingnkkaf ggrrqycfns etyeayslri
      121 veklvdhykd eeaivswqid nefghegsdm cycgqcqdaf qrflekkyds idelnerwgt
      181 ifwgqtyndf seipvpkvtv tvhnpammld warfrsasla gfahkhielv nrlkgnhqtv
      241 ttnlpggffd kwfdhnefsr eldfvsydny pvwgglkepi spahlsmtld yvrglkkenf
      301 wiveelmgaq ghdiigylpr pnqakawawh afahgcsnml ffrwrgmnkg aeqyclgild
      361 snnrttrkyk evqqffsevk ehkalfdapv kadvalvydf dtiwswrnqq qnasidytee
      421 ilrlyepfhk qntsidviky dqdfsdykvl llpvakvmdp elagrleeft rnggtvvmsy
      481 ragvkdrdnn lvfgkmvpge lsgllgieve eseslqages apvvpvdgge ateavywrdl
      541 vkpltartlh ryddrfyney scvtendfgk gkayyigagv qqeimhslak tiasssglht
      601 vesnpgveii trtaegkdyq vivnhngyee tfngielqpy ecrivev
//
LOCUS       WP_175990268             431 aa            linear   BCT 11-JAN-2025
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175990268
VERSION     WP_175990268.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..431
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=46346
     Region          1..425
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 mtksfdvetl llhggqepdp ttgsravpiy qttsyvfdns ehaaklfgle eegniysrim
       61 nptvdvlekr ialleggiga lgvssgmaai slsilniaga gdeivaatnl yggtynlfst
      121 tlpkygikvh fvdpsdpenf rnaitpktka vfaetignps lhvldieava kvahdneipl
      181 iidntfatpy lckpiewgad ivihsatkwi gghgtaiggi vvdggkfdwn nkkfpgfvde
      241 drsyngirya vdvgeaafit klrvqllrdf gaclspqnaf lllqgletlh lrierhtena
      301 lkiaehldqh sgvawvsypg laqhpshtla qkylkkgags ivvfgikggr dagrkvvdni
      361 tlwshvanvg daksliihpa stthqqlneq elrttgvtee lvrlsvgles skdliedlds
      421 aieaalaasp v
//
LOCUS       WP_175990292             341 aa            linear   BCT 11-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175990292
VERSION     WP_175990292.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..341
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37967
     Region          1..336
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mirvqnvtki fetkdgpfta lknvsfqvkk geiygvigfs gagkstlvrc lnylekpssg
       61 difieeqslk eqsavdlrke rhrigmifqh fnlfqsrtva gniayplkla kwpkekiner
      121 vkellafvgl edkakhypde lsggqkqrvg iaralatsps illcdeatsa ldpqttesil
      181 nllkrinaey gitivmithe mqvireicdk vavmengeiv eegsvfdifs npqtattknf
      241 vksvmndqlp ssvldklngs gegricrlif kgdstgapil setakkfnah invlfgqite
      301 lqgkpfgnli vqiigseret teilrywqqr lfvsevekra s
//
LOCUS       WP_175990350             522 aa            linear   BCT 11-JAN-2025
DEFINITION  alkaline phosphatase family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175990350
VERSION     WP_175990350.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 522)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..522
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=58276
     Region          36..>307
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 mikrlvfifs flifvigctg ssqvpsldtk kplplqtgse phpkvillvi dslmeeplnk
       61 aiedgkapal eflkkngqys tdlvssyptm svtidsslit gtypdqhkip glvwfddker
      121 riitygngff eilklgvsdf aknglyaynn qdlssnvkti hedldnagfk tasinaliyr
      181 gnhphtlkvp gfisavaklp deiqtmgpet lslgvfsren qenhhivnri glndsfaaee
      241 ltyllktntl psftilylpe ndftvhrkgp saikgiedad kqlqnvlnsf pdwnealdnl
      301 vwvimgdsnq slvksnkkea lidlrkelse ynilklgeav rakdeivita nermayvyml
      361 kediqqrgma eklqkesria wiawkdnegi kmispdhqge lsfkpggpyr dqyhqtwsvk
      421 gnidildmkv nentisfgdy pdalarlyga aesqngrfli tdakpgyefi gesspehsgg
      481 gahgsmhkad skvplivsgt dknienlriv dlkgwimeii qr
//
LOCUS       WP_175990419             366 aa            linear   BCT 11-JAN-2025
DEFINITION  Ger(x)C family spore germination protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175990419
VERSION     WP_175990419.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Cooper,G.R. and Moir,A.
  TITLE     Amino acid residues in the GerAB protein important in the function
            and assembly of the alanine spore germination receptor of Bacillus
            subtilis 168
  JOURNAL   J Bacteriol 193 (9), 2261-2267 (2011)
   PUBMED   21378181
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Li,Y., Setlow,B., Setlow,P. and Hao,B.
  TITLE     Crystal structure of the GerBC component of a Bacillus subtilis
            spore germinant receptor
  JOURNAL   J Mol Biol 402 (1), 8-16 (2010)
   PUBMED   20654628
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Hudson,K.D., Corfe,B.M., Kemp,E.H., Feavers,I.M., Coote,P.J. and
            Moir,A.
  TITLE     Localization of GerAA and GerAC germination proteins in the
            Bacillus subtilis spore
  JOURNAL   J Bacteriol 183 (14), 4317-4322 (2001)
   PUBMED   11418573
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..366
                     /product="Ger(x)C family spore germination protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=41162
     Region          1..360
                     /region_name="GerAC"
                     /note="Spore germination receptor GerABC, GerC subunit
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG5903"
                     /db_xref="CDD:444605"
ORIGIN      
        1 mkkvlvcwia mvlsvlssgc vereilddly ietgkgydli dentirgtam fpiykpdksi
       61 enmtlsaeat strevletla rmsqqplvrg gldavvigeg laqkgvidia dslqrdpsig
      121 arvfmmvsrg dakdilqgqy girgngmyis nllrqnikrr elpetnlhmf lfdyyqlgqt
      181 pylpiirkis dstlkvdgia lfqkdkmvdt ipaedmfffk ilvdkisegs hvvrlddekk
      241 rdgqkveasi tslkakhkik vtykkkpvkv tikikikgii keytgerltp kkiteieknm
      301 eediedkame mltkfqkigv dpigigqiqk hgvrgfdike wegtlypnaq fnvepdvkiv
      361 eggtve
//
LOCUS       WP_175990441             340 aa            linear   BCT 11-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175990441
VERSION     WP_175990441.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 340)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 340)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 340)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..340
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=36963
     Region          1..339
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mitisdvkki yqsksgpisa vdgvnlsvke geifgvigys gagkstlirm lnglevpteg
       61 ainvggqavs tirgkklrea rqsigmifqh fnllwsrtvi eniqfpleia gvpkkernkr
      121 anellalvgl egrgdsypaq lsggqkqrvg iaralannps vllcdeatsa ldpqttdsil
      181 dllvdinkrl gltivlithe mhvikkichr vavmengkva elgdvlevfr npqqqvtkrf
      241 vkevsqdqds devieqliqd ystgkvlkft fvgestgqpl itslirkfdl evnilqgqis
      301 qtqkgaygtl fvhldgaesq lkealafaes qlvkvevmag
//
LOCUS       WP_175990443             275 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175990443
VERSION     WP_175990443.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 275)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..275
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30264
     Region          1..272
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mkkwlagava aasifglaac gndsgagsde kelvvgasnv phaeileqvk pileekgidl
       61 qietyqdyil pnkdldngdi danyfqtipy melqmkdneg ydfvnaggih iepigvyskk
      121 yksledlpeg atilmsnsvs dhgrilslle kkglitlkdg ventqaqied ieenprnlkf
      181 dyeyeagmlp qmyeneegda vvinsnyaid aglkpledsi aiedtdspyv nvitvnkgde
      241 dkeevkelvk alrskeiqdf inkewdgavv pvsee
//
LOCUS       WP_175990486             187 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175990486
VERSION     WP_175990486.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 187)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18951323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..187
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=21250
     Region          2..126
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(7,9,64..65,68)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            9
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(63,107..108,110..111,115)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(69,74..75,103,106..107,110..111,114,117)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(92..94,103..104,107..108,111,115,118,122)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(92,108,111,115,118,122)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(116,122..123)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          138..179
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
ORIGIN      
        1 mkigyarvst qdqsldlqmd alqkagcekv ysekvsgmkd drqklkelid yaregdvlvv
       61 ykldrlgrst kklieltdel enrgielvsi rdnidtttav gkamfrmlav lsemerdlis
      121 ertraglesa rargrkggrp rkdskiinka iklyesrqys vreiedltgv skatlyrelk
      181 eknmnnd
//
LOCUS       WP_175990513             246 aa            linear   BCT 11-JAN-2025
DEFINITION  peptidylprolyl isomerase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175990513
VERSION     WP_175990513.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..246
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=26983
     Region          61..246
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mkrlvllslc liglilagcg qtekdnssee kpaeteenkt tdaesggddk mtypqlttdv
       61 aenekvvemk tsmgtikikl fpeqapktve nfithsengy ydglkfhrvi kdfmiqggdp
      121 ngngtggesi wgesfedefs kqlfnirgal smanagpdtn gsqffivqns emnpgfeekm
      181 keagfpqeii daymerggtp hldfkhtvfg qviegmdvvd kiadvevgqn dapkedvtie
      241 kitvvk
//
LOCUS       WP_175990559             273 aa            linear   BCT 11-JAN-2025
DEFINITION  Cof-type HAD-IIB family hydrolase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175990559
VERSION     WP_175990559.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..273
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30490
     Region          20..264
                     /region_name="HAD_Pase"
                     /note="phosphatase, similar to Escherichia coli Cof and
                     Thermotoga maritima TM0651; belongs to the haloacid
                     dehalogenase-like superfamily; cd07516"
                     /db_xref="CDD:319818"
ORIGIN      
        1 msykmivldl ddtllrddqt isertkkalm eaqesgvkvv lasgrptygm rwvekelkld
       61 dygsyilsfn gskiincrtn detysrtlsa eaahrlydls kregvgilty seeailveep
      121 seyadiesrl tglpvkvvws fkeavqgpvv kvlmlkeaer lvevekklqt eldgelsvmr
      181 skpyfleftq lgvtkgasld ylikplgihr eeviaigdsy ndqtmiefag lgvamgnape
      241 dikekadyva asnmedgvae vvekfvlnrl trv
//
LOCUS       WP_175990569             514 aa            linear   BCT 11-JAN-2025
DEFINITION  C40 family peptidase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175990569
VERSION     WP_175990569.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..514
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=56100
     Region          <20..167
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
     Region          <173..304
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
     Region          297..512
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mkklmttavc tvaltfssvs ippvqqanae tasqqpeveq kadniistak sligkatyer
       61 yvynpphqfg csgfiyyafk qngidlatrd tnvqaqlgey vpkdqlqkgd lvffdsnpnd
      121 ndpvthngiy igdnkiihma deendilisd ldgkdyyknn yktarrvlps fmydeatsst
      181 aekvveiaeg ligkasygtp yneetltfng agltyytykq vgidlkskta seqsklgepv
      241 krqdlqkgdl vflsnnssng kivhvgvyag ndqivhaags dsgikksvil ngyydehyvt
      301 arrvidvdaa atedtaente tqtpsasqek petetdvqpe tpaakpetet dvqaekpaet
      361 psesdvqpqa padkpented kpaapqnkgt evsglaedlm gkaqygrsyd estmsfnsag
      421 layyvfkqng idlqdktaag qstkgqyvsk sqlkegdlvf fsnsssdgei vntaiyagnn
      481 evimsagktl gvvkrnldrs wyqenyvtar riie
//
LOCUS       WP_175990581             334 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175990581
VERSION     WP_175990581.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..334
                     /product="phosphotransferase family protein"
                     /EC_number="2.7.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=38242
     Region          15..281
                     /region_name="YcbJ"
                     /note="Predicted kinase, aminoglycoside phosphotransferase
                     (APT) family [General function prediction only]; COG3173"
                     /db_xref="CDD:442406"
ORIGIN      
        1 mkagwersne wimpdldevr nmlkpyfkdr fvkeierldg glnnsnikik tnlneyfvlr
       61 iynkrsnnmk ieteiarllq grvpvpqtvy adsscsvfky pfllmnwmeg eqfsemiyrk
      121 nhkdirkaah aagaaladih kirfpdsgff ddelnikehv einastfigf ilemvekgfv
      181 skylgktlcs svvkfvqehv ylmddpgvqn slvhsdfnpl nvlveekggg vkitildwey
      241 afsgsplmdi gnmlryegtt apgmlkpfiq sylenggglp enwlqkakll dlialldlln
      301 kekcgevrvk dikglimkmm dewegyeavq rafe
//
LOCUS       WP_175990571             250 aa            linear   BCT 11-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175990571
VERSION     WP_175990571.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..250
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27470
     Region          1..242
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlteerhrii ldllkekeai kiqeiaeqtn asestirrdl tqleqekflk rvhggaarlq
       61 gklkeltvse ktskslhekn aiaryaaslv eegdciflda gtttlgmief lpeidivivt
      121 nglthvdsll qkgfktyivg gsvkpttkam igsgaieslq kyrfdkaflg tngvhpqygy
      181 ttpdpeeaqi kktaielsre amvladdtkf geiafskiad lekaivitng ttndldpayk
      241 kqttvkvvtt
//
LOCUS       WP_175990603             258 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175990603
VERSION     WP_175990603.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..258
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29054
     Region          1..251
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mnflsldtih htyfspktat nalsnisfdv negefisfig psgcgkttll siiaglikpt
       61 egkvllhgkp vnseknqmgy mlqqdylfpw ktieenifig lkimesltke kkreayelle
      121 klglsgvass yprelsggmr qrvalirtli tepkilllde pfsaldyqtk lkledliftt
      181 lkslnktall vthdigeaia msdriilfas kpgrvhrvfe vprelreltp ltvrnheayp
      241 pyfqtiwkel enlesgnp
//
LOCUS       WP_175990626             104 aa            linear   BCT 11-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175990626
VERSION     WP_175990626.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..104
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=11620
     Region          3..104
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mteiktittd elnkklqnge dlllvdvred eevaegmipg arhikmgdip esldkfdkdk
       61 eyificrsgn rsgnvahymk dqgykvvnme ggmmnwgget apkk
//
LOCUS       WP_175990630             238 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175990630
VERSION     WP_175990630.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..238
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=27020
     Region          1..226
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mridkllanm gygsrkevkk llkdgglqvn gevikdgkvh vdtekdtvml ygdkveyref
       61 iylmmnkppg lisatedane etvidilqme dqifnpfpvg rldkdtegll litndgqlsh
      121 qllspkrhvp ktyfaviege vterdieafk egvtledgyh tkpgdlvilk agitsdielt
      181 itegkfhqvk rmfesvgkrv vylkrlsmgp leldedlelg eyreltdeev emlkeyrp
//
LOCUS       WP_175990646             497 aa            linear   BCT 11-JAN-2025
DEFINITION  peptide MFS transporter [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175990646
VERSION     WP_175990646.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 497)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..497
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54135
     Region          12..497
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mssinkqkiv dsvpqkgffg hpkglftlff tefwerfsyy gmrailvyym yyevskgglg
       61 leegtalaim siygslvyms gviggwladr ifgtskavfy ggilimfghi alsfpgslsm
      121 ffvsmvlivi gtgllkpnvs tvvgemyaen dtrrdaafsi fymginlgaf laplltgalm
      181 ksygfhwgfa laaigmffgl vvfmvtkkks lglagtyvpn plnaaekkky gslsalvvva
      241 vaivlgitip ngwftldlfi nlvgifgila ptiyfivmyk spkttaters rvlayiplfi
      301 aavmfwaiqe qgstilaaya dkrtqldflg leispawfqs lnplfiiila pmfagmwvkl
      361 gdrqptipqk fslgllfagl sflvillpgy ftgedalvsp lwlvlsyfiv vlgelmispv
      421 glsattklap eafsaqtmsl wflasagaqa lnaqlvrfys adsemlyfgs iggaaivlsi
      481 ilfllapkiq vfmkgik
//
LOCUS       WP_175990869             403 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175990869
VERSION     WP_175990869.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..403
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=44580
     Region          2..401
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 mtrfkyegrd rsgrkrgvit apsrkeammr lknqgirvis aeevpetllt keitlgnpvk
       61 lqqmvvflrq fstllkagvt vvdatrilsa qtsskalakv lgevelelke gnplseafak
      121 hrkvfeplfi nmlkageatg sldetlerlg dhyekqhttr qkviaalsyp avvgmiaigv
      181 viflllavvp tfvdmfadmg selplitrav lgasemvqky wyillllvil aavgitllrr
      241 kketkyyldy ailripifgs liqkavlarm trtfsslfss svpilqsmvi lekvvgnevi
      301 arvimesrds lesggsltep mkdhwaippl vshmisigee tgsldgmlsk vadfyekeve
      361 nttdqlksli eplmivvlag lvgtivtaim vpmfemfnnv qnf
//
LOCUS       WP_175991014             435 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175991014
VERSION     WP_175991014.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..435
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49474
     Region          6..411
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mkknlfldyd fqpfivqaie elgfyeptei qkkmiplilk gqsaigqsqt gtgkthsyll
       61 piiekvdaas eqvqavitap trelaqqiyh eilkltknsg itsrcfiggt dkqrtieklk
      121 tqphivvgtp grvndlvkeq alfvhtssil vvdeadlmld mgfiedvdqi atkmpeklqm
      181 lvfsatipek lkpfmkkyme npqfahvepe risakniqhi iipkksrekv nvlydllvei
      241 npylgivftn tkakadevad aliakglkvg rihgdlspre rkkmmkqtrn ldyqyivatd
      301 laargidieg vshiinfelp qdldfyvhrs grtaragnsg iaytiyepsd edalnrlekm
      361 gisfshmelk kgewielpal nkrksrqktt adeidvkaks lvrkpknvkp gykkkmkykm
      421 eqikkkerrk knrnk
//
LOCUS       WP_175991020             138 aa            linear   BCT 11-JAN-2025
DEFINITION  Fur family transcriptional regulator [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175991020
VERSION     WP_175991020.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..138
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15892
     Region          1..138
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mnvteamdll ksegykhtgk reellqlfsd snkyltakdv lehmksdypg lsfdtiyrnl
       61 slfvdlgile etelsgerhf rftcesdhhh hhficmdcgk tkeihtcpmd vlkesieetg
      121 ydisghkfei ygkcpqcq
//
LOCUS       WP_175991102             466 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrolipoamide acetyltransferase family protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175991102
VERSION     WP_175991102.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..466
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49957
     Region          2..457
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mgienmkmpq lgesvtegti skwlvspgdt vnkydpiaev qtdkvnaevp ssftgtikel
       61 iaeegdtlev geiicsieve gagsapseea pkeekketae ssqaaakssq qaakpsqpaa
      121 kpsqpaakps qpaakpsqpa kkeagnkary spavlklsqe hdidlnqveg tgndgritrk
      181 dlkkiiesgn ipkagdapas qpaeaapapv keqaqpaaaq kqaapapnvp vmpgdieipv
      241 tgvrkaiasn mvrskheaph awtmmevdvt nlveyrnslk tefkqregfn ltffaffvka
      301 vsqalkefpq insmwagdki iqkkdinisi avatddalfv pviknadekt ikgiareitd
      361 lagkvrsgkl ksedmqggtf tvnntgsfgs vqsmgiinyp qaailqvesi vkrpvvmnng
      421 miavrdmvnl cmsldhrvld glvcgrflqr ikeilentsk ettsvy
//
LOCUS       WP_175990935             216 aa            linear   BCT 11-JAN-2025
DEFINITION  O-methyltransferase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175990935
VERSION     WP_175990935.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..216
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24401
     Region          36..213
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mineqvinyi esitrkrspl leemkqyaee hhvpimelvg ieallgilsi qqparileig
       61 taigysairm aeslpgteit tierdeeryg aaqaflsrse hssrihtlfg dalelqeeve
      121 kygpydaifi daakgqyqkf fdlysamlsg ngvvysdnvl fkglvaeeei eqkrirnmvk
      181 klqkynawlm shedyetail pvgdgiaisk krgdrk
//
LOCUS       WP_175991111             328 aa            linear   BCT 11-JAN-2025
DEFINITION  aromatic acid exporter family protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175991111
VERSION     WP_175991111.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10532842
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..328
                     /product="aromatic acid exporter family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37660
     Region          2..142
                     /region_name="ArAE_1"
                     /note="Aromatic acid exporter family member 1; pfam06081"
                     /db_xref="CDD:428756"
     Region          148..306
                     /region_name="ArAE_1_C"
                     /note="Putative aromatic acid exporter C-terminal domain;
                     pfam11728"
                     /db_xref="CDD:432028"
ORIGIN      
        1 mfrigyrtlk tgigtalais iaqlfqldnf vsagiltilc iqntkkksvq asssrfiacv
       61 igmlfsgaff efiayhpivi gllllvfipv tvslrikegi vtssviilhv ysagnvtlgl
      121 frnemgiivi gigialimnl ympsvenkla eyqekieenf ykifcelinh lktnqsdwdg
      181 keitetetll keaktlafkd venhflrhed lyylyfkmre kqfeilqril piaasislrv
      241 eqgkkiaqfl eelsqhihpg ntalfylkkl ydlkvefeqm dlpktreefe vraalyqfvq
      301 emeqylliks sfkgiqknek skrevhyt
//
LOCUS       WP_175990667             986 aa            linear   BCT 11-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175990667
VERSION     WP_175990667.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 986)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..986
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..986
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=108606
     Region          26..740
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
     Region          <836..>911
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
ORIGIN      
        1 mretwnklle kldpvirfft ntgvqkrari tygvfwnlal itivvlvlgt afaggvgagy
       61 faslvkeepi rsydqmkkdi ynyeetsqly faddvylgkl rtdlereevk ledvsehlrn
      121 aviatedeyf kehngvvpka imravlqeft nsstqsggst ltqqliknqi ltnevsferk
      181 akeillalrl erffekdeil eaylnvatlg rnssgrnigg vqsaaqgifg vdakdltlpq
      241 safiaglpqa pfsytpfmnn gelkenlepg msrkntvlyr mhregyitdk eyedavaydl
      301 tkdfiepkas psenypwlta elesraidim tgvlaekdgy skqdlennde leekyhtlad
      361 rnvrqsgyei hstidkkiyd qmqktknayd mygpsktvtt tdpetgeevq veepvqvgai
      421 mienktgrii sfiggrdfkl eqlnhatssy rsngstmkpl layapaleyg yispgsplpd
      481 vgvningwtp enyslkergl fparfalaes lnltavrtya niydrnpfne flmkmdfakl
      541 grvdnnlsla lgattqgvtv eenvnaystf anggkfvday midkivdqdg nivfehksep
      601 vevyspqtay ltidmmrdtl dhslgtgrya krflnfssdw agksgtsqdy kdhwfvasnp
      661 sitfgtwfgy dtpsdlntaa sraqyghygl rnirlwsfll ndtrdlapnl idpegsfkep
      721 ggivrrsfcs isgllpseac tkaglvksdl fnakfvptkt ddsllmsryv mvngkkylal
      781 pntpeefsqp gvilnpdfvk nvfgkvpgda sklipqeder fknvliaenk isddgaapgt
      841 vkasvngnki twtssgsgdv vgyrvysksg skvgsvksgd nysvsvgnge yfvkavdvag
      901 kesspsntvq vgkpepkpek pkpepkppgg dkptdpkppe pdkpepppad gggdgggdgg
      961 gdggttpepp gddeptdpkp peegte
//
LOCUS       WP_175991017             293 aa            linear   BCT 11-JAN-2025
DEFINITION  YitT family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175991017
VERSION     WP_175991017.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..293
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=32200
     Region          6..290
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 makrvhkkes pfhfiyrlff itigaalagv sielflipnn iidggiigvs lildylvsdr
       61 ipllnfstll vllnlpflys gykqigktfv vsslfavval aviegflhhf dpfikeeila
      121 tvfgglilgt gvglvirhgg sldgteilgi lltkklpfsv gefvmfinif ifgwaafvfg
      181 ieeamysvmt yyiafktidt viqgmdetka viivsdeyae vseailnrlg rgttmlkgrg
      241 gytdhdkevi yvvvtrlevt klksvvsdid pnafitimst qetkgarfks aih
//
LOCUS       WP_175991112             167 aa            linear   BCT 11-JAN-2025
DEFINITION  L,D-transpeptidase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175991112
VERSION     WP_175991112.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Mainardi,J.L., Villet,R., Bugg,T.D., Mayer,C. and Arthur,M.
  TITLE     Evolution of peptidoglycan biosynthesis under the selective
            pressure of antibiotics in Gram-positive bacteria
  JOURNAL   FEMS Microbiol Rev 32 (2), 386-408 (2008)
   PUBMED   18266857
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..167
                     /product="L,D-transpeptidase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=18215
     Region          28..149
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mrillaimlm aspiwplgrn plpgdpflii nkesnqlsfi negkvvgtyg vatgkttdlt
       61 peglftvtvk aknpyyrkkn ipggdprnpl gsrwigfdae gtdgriygvh gtnqpssigk
      121 yisngcirml nknvefiydr vpigtkvlvv ktsksfqelg keygalk
//
LOCUS       WP_175991236             396 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175991236
VERSION     WP_175991236.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481629
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..396
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43124
     Region          5..391
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Site            order(100..102,126,176,207,236,238..239,247)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(103,136,200,245..247,276,279)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            239
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mnlslakrvs altpsttlai takakemkaq gidviglgag epdfntpqhi iqaaydslie
       61 ghtkytpsgg taqlkdavin kfkqdqnlty kpseiivtsg akhalytlfq vllndgdevi
      121 iptpywvsyp eqvklaggnp vivegkqens ykitpeqlse sitektkavi inspsnptgm
      181 iyssdelkai gqvcleknil ivsdeiyekl vydgnghtsi aeisdelkeq tiiingvsks
      241 hsmtgwrigy aagnetiika mtnlashsts nptttsqyga vaaymgdqqp veemrksfee
      301 rlnivfskln nipgfdcikp qgafylfpnv keaarltgye svdifvqall eeakvavipg
      361 sgfgsednir lsyatslesm eqaiermhef vvkksq
//
LOCUS       WP_175991160             243 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175991160
VERSION     WP_175991160.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..243
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=27360
     Region          1..226
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 merlqkviah sgvasrrkae qliiegrvkv ngnvvkelgt kvsssdkvev ngvqierenk
       61 vyymlykprg visavtddkn rqvvtdffpe ieeriypvgr ldydtsglll ltndgefanl
      121 lmhpsnqiek tyvarlkgip pkfkirelek gvklddgmta pakvkvlsid kkqgkaiaei
      181 tihegrnrqv rrmfeaigfp vqklkrerfa fltlhglnag egreltphev kqlrtlaetg
      241 sir
//
LOCUS       WP_175991262             277 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfurtransferase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175991262
VERSION     WP_175991262.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..277
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31244
     Region          10..273
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mrfiksvdwl kkhlndrnvr vidcsfslgd psagktsylk ehipgavyfd lekdlsghvk
       61 ehggrhplpn mknllrkven agidnqsaii aydqgegafa srcwwlfryl ghenvfvlng
      121 gfkawkergf etqasipeyg eksytpsfne dmlaslgeve risegesqav lldsrseerf
      181 lgleepidri pghipkaina pwtqcihkgf frdtdvqnqr fanldrnspi ivycgsgvta
      241 tpniiallea gfhdvklyag sysdwvsyeh hkvdkqq
//
LOCUS       WP_175991271             432 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter permease [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175991271
VERSION     WP_175991271.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 432)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..432
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47439
     Region          15..280
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mnhlwqsllh dgntqwvlls tlllgiasgv lgsfallrkq sligdavaha alpgicfafm
       61 figeknffvl ligaastgll aaytiqlitn ttrikedtai clvlsvffgl givmltkvaq
      121 mptgnqsgld dfifgqaasl vgrdvqlmgl taavlivitt llfkefkvst fdpqfargig
      181 lpvgflnflf vsllvitvvi giqavgvilm aamlitpais arywtdslrt mvfisgivgg
      241 lsgaagtlis tmgkglstgp fivltatvif ifsllfspkr glisiilrra rnderlairf
      301 vlkkvyamrk eriyekslye etnismfryt rvmkhlvkng yivktdgavs itdwgamkae
      361 qfrfvdeive lkemypselg sldinwieeq eeevlskdql kklqskmsei ysqnpflnik
      421 vnadrggqgy el
//
LOCUS       WP_175991272             292 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter permease [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175991272
VERSION     WP_175991272.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 292)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 292)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..292
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30862
     Region          1..277
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 msyelwillt gslvglscgv igcflilrkm smladaisht vllglvmafi vsqsmngfnm
       61 ligaaaagll ttfivqllns sgiqedaaig vvftslfalg vilislfakn vhldvehalm
      121 geiafvpwnt islpflgaip ksvvmlgsil iidtavilll fkefkltsfd pnmaaaigip
      181 vlaihyilmg lvsvttvsaf dsvgailvva mliapgatay lltdrykvml llsgvigifd
      241 svagyygakl ldvsisgsma vaagivfliv wmlspkyglv skflnhrrls ee
//
LOCUS       WP_175991278             287 aa            linear   BCT 11-JAN-2025
DEFINITION  DegV family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175991278
VERSION     WP_175991278.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..287
                     /product="DegV family protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=32070
     Region          1..280
                     /region_name="DegV"
                     /note="Fatty acid-binding protein DegV (function unknown)
                     [Lipid transport and metabolism]; COG1307"
                     /db_xref="CDD:440918"
ORIGIN      
        1 mriawvtdst ayiedlsack eknvfvvpmn ilfgekeykd gidlspqdlf eklkeekvev
       61 ktsqpsigtf kelyeelagr ydhifsihvs shfsgtmssa yqaaellsdt fpsitcidsk
      121 tltyplteli eygqtlhekg ksieemtksi eekiktrevy vmvgsleqlh ksgrmnglsf
      181 flgsvlnikp ilsivdgkle vydkvrsink glskmskqls eslktkkikk vsilhglnhe
      241 eaaewmeelk ksypdiefga yplgavidvh agantigisw sedigqa
//
LOCUS       WP_175991275             225 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175991275
VERSION     WP_175991275.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10549394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..225
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25471
     Region          53..144
                     /region_name="Methyltransf_11"
                     /note="Methyltransferase domain; pfam08241"
                     /db_xref="CDD:462406"
ORIGIN      
        1 msksewhena ksrwdinadn whsrsaemws tgsrkaiipf flknvnegkk vgdlgcgdgy
       61 gsyllhqngf kvtgmdfsek mveianqlek ehlqfvqgdl vrppfkdnaf davmainsie
      121 wtesplqaln elervtakng ficigllgpt ahprenafpr lhgenaicnt mmpwelerls
      181 eekgwkkide ewiykkgvng slaaslsnel kqaltfmtlf mfrls
//
LOCUS       WP_175991286             161 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrofolate reductase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175991286
VERSION     WP_175991286.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11087044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..161
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=18432
     Region          1..160
                     /region_name="DHFR_1"
                     /note="Dihydrofolate reductase; pfam00186"
                     /db_xref="CDD:425512"
     Site            order(5,22,27,57,96,102,115)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(7,14,44..46,64,97..100)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 misfivamds ksaigknnel pwhlpadlaf fkrvtmgnpi vmgrktfesi gralpgrenv
       61 ivtrdrqyra kdctiihsve kiseiqsstt eemfviggae ifkevfpiad rlyitlieee
      121 fggdtffpsf nqdewelisk ekgptddknp ydyyfltydr k
//
LOCUS       WP_175991313             191 aa            linear   BCT 11-JAN-2025
DEFINITION  YitT family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175991313
VERSION     WP_175991313.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..191
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=21110
     Region          20..>173
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mfkgffilvi gsiligigin lffvpyhfld ggmigiglif hywfgfkpgl tiillsiply
       61 vivffkdrpl fynsihglwl ssfmidffyq wydfyilppl fsalvggafv gvgiglmlra
      121 dsatggtdll aqlisksfgf nagklifvid slvlligwsv iglesflysl faistvgfft
      181 tilthhkdsd g
//
LOCUS       WP_175991340             429 aa            linear   BCT 11-JAN-2025
DEFINITION  NCS2 family permease [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175991340
VERSION     WP_175991340.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..429
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46410
     Region          8..428
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mkerkgifql kdhdtsfkqe imagaigyft ivyiiavnal ilseagipfe gavmatilas
       61 fvgclvmafw anapillvpg mginamftft lvkssgltwq ealavvvvsg ilfmiiaftk
      121 lskvlseaip ktlkeaitvg lgmflmfigl ekggliqrgd salitigdfg elkvlatvlt
      181 flvtiflfir nvkgqflwsi afgtmlgfif giepsisgst fhlseygqvf gqisfdavle
      241 ipfwiavfsv tmvlvfenig lihghvdmig qpqkypkafq anafsaftsg ffgtsptvst
      301 vesaaamtag grtgltsltt gvlflgsvlf ipylkwipdh aiapiliiig glmiqnirhm
      361 dlrdlteafp aifiiamipf tysiadgiai gfimypilkm atgkarevsi plyiiaglfl
      421 mnffvhsih
//
LOCUS       WP_175991355             212 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphoribosylanthranilate isomerase [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175991355
VERSION     WP_175991355.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785047
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..212
                     /product="phosphoribosylanthranilate isomerase"
                     /EC_number="5.3.1.24"
                     /GO_function="GO:0004640 - phosphoribosylanthranilate
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23043
     Region          1..201
                     /region_name="TrpF"
                     /note="Phosphoribosylanthranilate isomerase [Amino acid
                     transport and metabolism]; COG0135"
                     /db_xref="CDD:439905"
ORIGIN      
        1 mtkvkvcgiq dlkaaqwavd agadavgfif aesrrrisve kaaaisnsih egilkigvfv
       61 naskeeledi vekvkldyvq lhgdespafc nslnvpyika vavteerdln ilpeysgefv
      121 lvdsgkgpyr ggngtsfdwe ylkdyqssnh klilagglkk dnvrmavsia kpymvdvssg
      181 vesggikdke kildfinevr aiktdsesge lq
//
LOCUS       WP_175991359             121 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175991359
VERSION     WP_175991359.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..121
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13643
     Region          5..120
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mivnkintvf ipvadlrksv dwygqtlglr idqqqyreid dlpvytfsmg dtsltleree
       61 sfipspstvp icnihtadie kvredflssg vaveseiitf pdfsyfnfrd lngnllmict
      121 g
//
LOCUS       WP_175991365             280 aa            linear   BCT 11-JAN-2025
DEFINITION  STAS domain-containing protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175991365
VERSION     WP_175991365.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..280
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31679
     Region          165..273
                     /region_name="STAS_RsbR_RsbS_like"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist domain of the 'stressosome' complex proteins
                     RsbS and RsbR, regulators of the bacterial stress
                     activated alternative sigma factor sigma-B by
                     phosphorylation; cd07041"
                     /db_xref="CDD:132912"
ORIGIN      
        1 mnenfkkigq aiinkkseia kevheerfsk ipaeerekia siekeileir agfihifgea
       61 lidfqnkehy ldvltqwgkd tgeriynmga pldealkdtn qyrrgiwkei khqaqkynms
      121 ldtvfeaqei ldplldqavy sfsltyvtyh ketldraksa flelsvpvvp litgvavlpl
      181 ignidtqrar limeeallqa nklkltklfi dlsgvaivdt mvadrifmvi salkllgvkt
      241 iltgirpeia qtitqiginf nqveiranlq qaieemkalv
//
LOCUS       WP_175991374             368 aa            linear   BCT 11-JAN-2025
DEFINITION  Ger(x)C family spore germination protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175991374
VERSION     WP_175991374.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Cooper,G.R. and Moir,A.
  TITLE     Amino acid residues in the GerAB protein important in the function
            and assembly of the alanine spore germination receptor of Bacillus
            subtilis 168
  JOURNAL   J Bacteriol 193 (9), 2261-2267 (2011)
   PUBMED   21378181
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Li,Y., Setlow,B., Setlow,P. and Hao,B.
  TITLE     Crystal structure of the GerBC component of a Bacillus subtilis
            spore germinant receptor
  JOURNAL   J Mol Biol 402 (1), 8-16 (2010)
   PUBMED   20654628
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Hudson,K.D., Corfe,B.M., Kemp,E.H., Feavers,I.M., Coote,P.J. and
            Moir,A.
  TITLE     Localization of GerAA and GerAC germination proteins in the
            Bacillus subtilis spore
  JOURNAL   J Bacteriol 183 (14), 4317-4322 (2001)
   PUBMED   11418573
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18824267
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..368
                     /product="Ger(x)C family spore germination protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_process="GO:0009847 - spore germination [Evidence
                     IEA]"
                     /calculated_mol_wt=41803
     Region          3..362
                     /region_name="GerAC"
                     /note="Spore germination receptor GerABC, GerC subunit
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG5903"
                     /db_xref="CDD:444605"
ORIGIN      
        1 mskkfriagv lllfhlaltg cwdqrllkds rliysssfdl ieddkiftta itrdfhgemg
       61 anveitgegk tiretrmsmd rkingnfeps knrvfllged lakkdiyqfl dvfyrdpsss
      121 isakiavaeg rgsdflsklr ekntfisefl teaiesaega teveeqnlqt ictlmfdpgk
      181 dfilplftle deeinlegna ifhkhsmtgk lsimqstlyl vladkkakra rfiseveken
      241 ksplddyisy niikpkakmk ilsdspddik veislkagit iseypadklk dkknikkink
      301 kiekdlvkrs kklvetiqta nadlfgigre liafhpktwe klnweedyke itiipkiete
      361 ivgngiin
//
LOCUS       WP_175991377             198 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175991377
VERSION     WP_175991377.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22942
     Region          5..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkhgnknrik kaalrlfgqk gyedtslhei assvgikkps iynhfanked ifsavlddll
       61 itettayhql qqemeqglpk anlkrlfdly csrlmtteea llwkrvtffp ppqfkefiee
      121 kffqfedait gilsaiyeda leldilqkvd kkdfvasflc lvdgiflehh yysedifkqr
      181 mnavwrvytl gifngkge
//
LOCUS       WP_175991388             218 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD family hydrolase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175991388
VERSION     WP_175991388.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..218
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25221
     Region          1..214
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mkailfdlde tllnrersll nfirdqydrl faeydvnkee fcskfmewdq rgyvwkdvvy
       61 eqiikffsld hfcteelvrd yvlnfashaa afpglhhvls tlkregyylg litngrvdlq
      121 tstiealkia pffdiilise sfgikkpdpr ifkhalnqlg vepssavyvg dhpindvkaa
      181 kqcgmkgiwr ktahwdgegi qyeieelpdl leliknik
//
LOCUS       WP_175991415             241 aa            linear   BCT 11-JAN-2025
DEFINITION  ZIP family metal transporter [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175991415
VERSION     WP_175991415.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Dempski,R.E.
  TITLE     The cation selectivity of the ZIP transporters
  JOURNAL   Curr Top Membr 69, 221-245 (2012)
   PUBMED   23046653
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Guerinot,M.L.
  TITLE     The ZIP family of metal transporters
  JOURNAL   Biochim Biophys Acta 1465 (1-2), 190-198 (2000)
   PUBMED   10748254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..241
                     /product="ZIP family metal transporter"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25412
     Region          1..241
                     /region_name="ZupT"
                     /note="Zinc transporter ZupT [Inorganic ion transport and
                     metabolism]; COG0428"
                     /db_xref="CDD:440197"
ORIGIN      
        1 mfqaalwgga aslslflgal igiffkipkr itafimafgt gliigsatfd llseaagnan
       61 iihitamfll gaaiftafel wiskkggsqr krskknphdh sglaiyigtl mdaipesiii
      121 gvsflgsqsi qwvfiaaifi snfpealsss iglkldryst kkililwgsv vvvsslssll
      181 gytflqdape steyiigafg aggllamvss tmlpeafedg gplvgflsaa giilsyiftn
      241 l
//
LOCUS       WP_175991442             375 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175991442
VERSION     WP_175991442.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10893456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..375
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41782
     Region          6..105
                     /region_name="RHOD"
                     /note="Rhodanese Homology Domain (RHOD); an alpha beta
                     fold domain found duplicated in the rhodanese protein. The
                     cysteine containing enzymatically active version of the
                     domain is also found in the Cdc25 class of protein
                     phosphatases and a variety of proteins...; cl00125"
                     /db_xref="CDD:444705"
     Site            73
                     /site_type="active"
                     /note="active site residue [active]"
                     /db_xref="CDD:238089"
     Region          120..295
                     /region_name="POD-like_MBL-fold"
                     /note="ETHE1 (PDO type I), persulfide dioxygenase A (PDOA,
                     PDO type II) and related proteins; MBL-fold
                     metallo-hydrolase domain; cd07724"
                     /db_xref="CDD:293810"
     Site            order(172,176,232,250,253,257..259)
                     /site_type="active"
                     /db_xref="CDD:293810"
ORIGIN      
        1 mavkamspke vakkvmnked lfildvrntd afedwkidgh tfeylnipyf dlldgveeim
       61 dklpndkdil vvcakegssv mvaemlseeg kdvayleggm kawsehlepv kvgdltdgge
      121 lyqfvrlgkg clsymvvsng eaavvdatrm tdifidfake knaeitnvfd thlhadhisg
      181 grkiaeatna aywlppkdae evtfeyaalq dgnkvvigns tidinalysp ghtigstsfv
      241 idekyllsgd ilfidsigrp dlagkaedwv adlreslykr yknlsmeltv lpahfmiide
      301 lnedgtvgek lgtlfaknhg lniedeeefr klvsenlppq pnayqeiret nmgkvtpdee
      361 kqremeigpn rcavr
//
LOCUS       WP_175991447              98 aa            linear   BCT 11-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175991447
VERSION     WP_175991447.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..98
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=10905
     Region          1..94
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mnritpaelq kklengdvln iidvretdev rtgkipdavn iplgllefrm neldktnqyf
       61 ivcqsggrss qavrfleyqg fdvvnmdggm sawegtlq
//
LOCUS       WP_175991512             278 aa            linear   BCT 11-JAN-2025
DEFINITION  YitT family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175991512
VERSION     WP_175991512.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..278
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=30368
     Region          3..277
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 mnkttvkeit liivgslffa lgvnlfaipn elgeggvtgi smtlyyvlgw spgitnfvmn
       61 gallaigykv lnkrvtwytm laifftslfi kftegmgesv dimlgtvfag vfiglglglv
      121 lrsggttggs tiiarmlnqh fgwavsttmf vfdilvvlgs sfvigientm ytgisiyist
      181 kildylidgf dtrkavtiis ahtddiaekv saemdrgvtv inarghyske skdilyvvin
      241 kqelfllkkm iqkidekafv vvhdvrdvfg egftfpkt
//
LOCUS       WP_175991508             355 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175991508
VERSION     WP_175991508.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..355
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38299
     Region          134..351
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mflafkelkh skvrytlial imtavlflvf fisglanglg fgdsaavrnl eadyvvlnee
       61 addaivgssl sekqvhqide svdgevspls itmmssfkgs dkeevdvtyf svdtdaypem
      121 divegknise leaheviade slqqegyqln dkvvdqstsk eltiagfskd qmysnipvvy
      181 tdlstglqek rgsetmynav lysgpeaald gvdiltidea vggipgytet qgslrmivvf
      241 lfiisafvtt vffyvitihk lhqlgvlkai gattgyiars imtqvslltv iglvfsgalv
      301 ygmtrviped mpfrltpgll agtaglflll nllgallsvr qvaktdalea igrvg
//
LOCUS       WP_175991543             376 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175991543
VERSION     WP_175991543.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..376
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41742
     Region          5..368
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 msdqkvkiav agagsftdlw ylpilkklps vilkaicsqn gtnadrlaak ygipsscrsy
       61 remleedidg icivtpnvsh heiallaaek qihvmcekpl amearqakam weaaernnii
      121 hgvnftyren pavvrlkeli eggligkvye gkfeysgdyg lsgppgwrgt ssvggrggvl
      181 adlgshlida vhyilgenie hvsaslsyle ggsmkraadl edkdrsadsa ffqasfpsgi
      241 qgsfytswvs tqgdrnqtid lmvkggkgal qllsselgir lryapvngpw ediklaniyp
      301 wddaaepsee rfrpwrftek neiwkwvdai nekkeldrpt frdgyvvqrv idsvllsdql
      361 rkevavkele kmeesq
//
LOCUS       WP_175991614             763 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Bacillus sp. Marseille-Q1617].
ACCESSION   WP_175991614
VERSION     WP_175991614.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 763)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 763)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440013
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..763
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..763
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=85807
     Region          6..757
                     /region_name="YprA"
                     /note="ATP-dependent helicase YprA, contains C-terminal
                     metal-binding DUF1998 domain [Replication, recombination
                     and repair]; COG1205"
                     /db_xref="CDD:440818"
ORIGIN      
        1 mfrknnlqel ieqfkkdeqf nkqiihwhti dekpaaytdi peeidkrikk alrgrgiekl
       61 yshqhdafqh avkgksftav tptasgktlc ynlpvlqtim kdpnaralyi fptkalaqdq
      121 kselneiise agasinsyty dgdtsanirq kvrkaghivi tnpdmlhsai lphhtkwvsl
      181 fenlkyviid elhiyrgvfg shvsnvirrl kricefygas pvfictsati anpkelseql
      241 tgskmelidn ngapsakkhf vfynppivnk plnirrsatl evrriagell rnriqtivfa
      301 rsrvrveiil tylqelvkgq lgaksirgyr ggylptqrre iekglrsgei ygvvstnale
      361 lgvdigqlqv cimtgypgti asawqqagra grrhgeslvi mvassspldq fiidhpdyff
      421 dqtpetarin pdnliilidh lkcaayelpf kdgeqfgshe vedileflae ekllhkngdk
      481 wywmndvfpa hnislrsasq enviiidqtd iaavkvigem drfsamtllh deaiylhqgi
      541 qyqvemldwe ekkafvrevd vdyftdanla vqlrvletdk erstgsceia ygdvtvqama
      601 tifkkikfdt henigsgpih lpeeelhtns swislsdsss ftqerleegl igaaqslksi
      661 iplyvmcdps difvvpqvka ahndkptifi ydrypggigl sekvyeqieq vlsearklie
      721 scpcqtgcps cigtehsmkt akadtlklla lfhggreege svs
//
LOCUS       WP_175991638             313 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Bacillus sp.
            Marseille-Q1617].
ACCESSION   WP_175991638
VERSION     WP_175991638.1
KEYWORDS    RefSeq.
SOURCE      Bacillus sp. Marseille-Q1617
  ORGANISM  Bacillus sp. Marseille-Q1617
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Bacillus.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427633
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Bacillus sp. Marseille-Q1617"
                     /db_xref="taxon:2736887"
     Protein         1..313
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34441
     Region          61..311
                     /region_name="FepB"
                     /note="ABC-type Fe3+-hydroxamate transport system,
                     periplasmic component [Inorganic ion transport and
                     metabolism]; COG0614"
                     /db_xref="CDD:440379"
ORIGIN      
        1 mkkissliii lmlsvlftaa cgndsdnqka gegteeksvd qsihvkdalg deitleskpe
       61 riislipsnt eilfelglgg evvgvtdfdn ypeeaaakek iggmefnvek iisldpdlvl
      121 ahestavsak eglnqlrdsg isvfvvkdtq kidevytiie nigkltdtek kaeklvsgmk
      181 kdlqelkska eeveqkrkvy vevapapdiy stgnntfine mlelinaena lkdqegwiav
      241 nqeeviaanp dviittygdn eqimtrdgwq dinavknehv ydvhtdlvtr tgprlvegve
      301 eiaksvypei fte
//
LOCUS       WP_175991722             817 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia
            stagnalis].
ACCESSION   WP_175991722
VERSION     WP_175991722.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stagnalis
  ORGANISM  Burkholderia stagnalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 817)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 817)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 817)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Burkholderia stagnalis"
                     /db_xref="taxon:1503054"
     Protein         1..817
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=86978
     Region          1..803
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mlavssqsqa tefnssflsi dgasnvdlsq faqadftlpg eylldvqvnd lfyglqtief
       61 iagdasgagk pclppelvaq fglkpslaka lprfqggrcv dlaaiegvsv ryqkgegrlk
      121 isipqaalef tdayylpper wtegipgaml dyrviantnr nfgsagsqtn svqaygtvga
      181 nwgawrfrgd yqaqsnagnt vyadrtfrfs rlyafralps iestvsfgdd ylssdifdtf
      241 altgatirsd drmlppslrg yaplvsgvar tnatvtvsqq grvlyvtrvs pgafalqnin
      301 tsvqgtldva veeedgtvqr fqvttasvpf larqgqlryk aavgkprlfg gagitpffgf
      361 geaayglpld ftvyggfiaa sgytsialgv grdfgafgal sadvtharar lwwngatrng
      421 nsyrinyskh fdaldadvrf fgyrfserdy tnfsqfsgdp tayglanskq rysatmskrf
      481 getstyfsyd qttywarqsd qrvgltltra fslgalrrvn vsvsafrtmg agsggnqfsv
      541 tatlpigdrq tvtsslttgg gntsvnagyi yddpagrtyq iaagttggrg aanasfrqrt
      601 ssyqltaqas tvanayaaas lelggslvat qygvtahang nagdtrllvs tdgvpdvpls
      661 gslartnarg ytvldsispf nvydatvnve klplevqvsn piqrmvltdg aigfvkfsaa
      721 hgrnlfvtls dasgkalpfg asvqdgangk elgivgedga ayltqvqpks slvvragert
      781 lctldvlpdq lqlegtpipv tcrppgesha atgrier
//
LOCUS       WP_175991742             308 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stagnalis].
ACCESSION   WP_175991742
VERSION     WP_175991742.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stagnalis
  ORGANISM  Burkholderia stagnalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia stagnalis"
                     /db_xref="taxon:1503054"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34099
     Region          16..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          101..300
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(116..117,119..120,123,127,129..135,229..234,
                     240..241,243..244)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mmhpdlrrld lnlllvfdal yrhrsvaaaa helamspsal shalarlrta igdalfvrlg
       61 nemqptvrad diaawagdal damskglara rrfdpahser tfvfaatdyt afavlpalia
      121 riqhvapqlr lrvvhsdrki atdelaagri dfalgyhedt aadtpgieef dwfsddyvvi
      181 asashpsihr rltleqylaa rhvvvtpwne trgvvdyvld rlglarqvav qlptvlaapf
      241 iiaesgllmt vpnraaqalr haapirifpa pfeiprytvk iyshakhart dahrwlrtql
      301 learpdga
//
LOCUS       WP_175991768             277 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia stagnalis].
ACCESSION   WP_175991768
VERSION     WP_175991768.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stagnalis
  ORGANISM  Burkholderia stagnalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Burkholderia stagnalis"
                     /db_xref="taxon:1503054"
     Protein         1..277
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30581
     Region          3..135
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          153..275
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 msyktllvhl ddsercnkrv alaldlagrw nahliglyvv cqdlfeplmr pdeplklavy
       61 erlceerrkq aeirfleaae ragrsvewra pagpatetat lharhadllv lgqtdphdrm
      121 thiahhfved vvmgsgrpai vvpyagrvrt lgenilvawd ggreaarava dalpllmrar
      181 fvnvetvvrk rpdpdktpag vdvaaylerh gvrssfsttp rdadigsgvt llnrasdlha
      241 dllvmgaysh trmhervlgg atrtiletmt vpvlmsh
//
LOCUS       WP_175991792             704 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein, partial [Burkholderia
            stagnalis].
ACCESSION   WP_175991792
VERSION     WP_175991792.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stagnalis
  ORGANISM  Burkholderia stagnalis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 704)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 704)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..704
                     /organism="Burkholderia stagnalis"
                     /db_xref="taxon:1503054"
     Protein         <1..>704
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
     Region          2..704
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 psvtanldld kivgtevtvs iqlegigqfi pglagnaglg nigagtreit glvtaarvag
       61 edrhsilyel elrpwlyrat ltqdcrifqd msvieitdav lakypypvdk rlagafrgiy
      121 pkrdvqrqaf etdwaflqrl weewgiwwwf ehegghqrlv lcdtmgghhp hgaayetvry
      181 lspdgkride ehihalsvts rltsgsvtvv dydytrpran ltvteenprk tassdgavyd
      241 wgdysqplag aqgvegqpnd teqesrhlar vqlearrcag lrangrgnlr gltvgrtfal
      301 tgypqqaanr eyvvlsttld ieevgdrtga satyrceaqf ellpanepfr lersvrkpvm
      361 sgpekaivvg pagqevwtdk ygrvkvqfgw drqgkldehs giwlrvvspw qgadmgatfl
      421 prighevavm hyygdpdlpv itgspvnefr qptlelpanq avavlrgref qgtasghvai
      481 ddtqgqiqtq iasdagssvl algnirrivk ktgradargk gfdlrtdywg vvralmglfi
      541 stdgqpngag qtkeakaavg rltrarelqe slsglaqqhe aqqrdadqse vakaikarnd
      601 airgdtpage ndfpelkepd lvlasaagvs vaaersahva snediavtsg rhvgiavghs
      661 lfasvsnafs lfvhkagmkl iaaagkvrie aqtdgidmka kqsv
//
LOCUS       WP_175991814             223 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease [Escherichia coli].
ACCESSION   WP_175991814
VERSION     WP_175991814.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..223
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25929
     Region          <33..79
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mfnvtrnipa pqclsrkvyn hktvvnalde ifhgkcylce qgnlmdpeie hfiphrdlde
       61 lkydwnnlfl acsrcnsiks dsfenlldct ksdvdvfsei vhlagnaits gvqvyprrkr
      121 psrkvlntvk lldkcfnsss tglrgitran lseklqdklf yftgwrmklv sdrsteqeiq
      181 eaknklkpmc nvsypfsvfw rwhlltdirv mkkfprirde lgf
//
LOCUS       WP_175991942             335 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Sphingobacterium sp. CZ-UAM].
ACCESSION   WP_175991942
VERSION     WP_175991942.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. CZ-UAM
  ORGANISM  Sphingobacterium sp. CZ-UAM
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Sphingobacterium sp. CZ-UAM"
                     /db_xref="taxon:1933868"
     Protein         1..335
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37604
     Region          1..315
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mmlkiavfra lqlgdllcam paitalkyny pesrlyfigl phmrpllqrf dcvdefiafp
       61 ghpelpelpc hplaladfvk rmqaekfdll lqlqgngtiv ndflknfgak rlvgfrpsgs
      121 aedsgwleyp dklhevdrhl alidflglqi pnrtmyyplf ssdwsgfevi knrlaypfvi
      181 vhvgsrdtnr qwplenfvql aehlhakgyq ivltgvsaek qriatfenll tfkvlnlcaq
      241 ldlgvlgclv qqaflvicnc tgishiaaal etrsivlsmd geperwgpqn kcihktfdar
      301 kpiqltdifs aidslhefqs pvgqnvaatp kisrg
//
LOCUS       WP_175991963             260 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Sphingobacterium sp. CZ-UAM].
ACCESSION   WP_175991963
VERSION     WP_175991963.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. CZ-UAM
  ORGANISM  Sphingobacterium sp. CZ-UAM
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Sphingobacterium sp. CZ-UAM"
                     /db_xref="taxon:1933868"
     Protein         1..260
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006644 - phospholipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=28608
     Region          128..225
                     /region_name="PAP2_like_5"
                     /note="PAP2_like_5 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03394"
                     /db_xref="CDD:239488"
     Site            order(142,149,160..162,199,205,209)
                     /site_type="active"
                     /db_xref="CDD:239488"
ORIGIN      
        1 mmrfllllll pftvsaqtds lrslpkydgl tiqdnntdsl fnsslfklka kqfivpaali
       61 gygllatdak ffkninldir neivanhpnf stkiddytri vpgaavfalq afgikgessv
      121 kkeavvyams vgistatvfs tkrltrqerp dgsdrrsfps ghatlafasa eflrreywqv
      181 spwigvggya vatgtgilrl ynnkhwlgdv aagagigils ttlsywlydk ihiggddqrt
      241 islfpgysnr qftvgfvkqf
//
LOCUS       WP_175992092             388 aa            linear   BCT 11-JAN-2025
DEFINITION  ROK family protein [Sphingobacterium sp. CZ-UAM].
ACCESSION   WP_175992092
VERSION     WP_175992092.1
KEYWORDS    RefSeq.
SOURCE      Sphingobacterium sp. CZ-UAM
  ORGANISM  Sphingobacterium sp. CZ-UAM
            Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
            Sphingobacteriales; Sphingobacteriaceae; Sphingobacterium.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Sphingobacterium sp. CZ-UAM"
                     /db_xref="taxon:1933868"
     Protein         1..388
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=42059
     Region          70..379
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 mkekilvyly ylkelsiagl skslakstpi vtkainelle qhvivdkgla astggrraal
       61 yalndhadql iisvsvdqfy tsihlsnlkq evlaetvdir ldlrdestgn divehirkfi
      121 nahklksski igigismpgf vnaslgvnds fadnnplhhl khniekklni ptiidndshc
      181 vawaekefgs gvdsthtlvi nlnwgvglgi iingeiftga tgfagefshi plsntnslcs
      241 cgkrgcleve aslksaieqt elaiqqgeys iystliktms nknnalieaa kigdqlviyn
      301 igkigfmigk gistllhiln pnkvvisgrg aeighilgpq iqnainefsi priakmteie
      361 isglhktaqq kgtaalvveh yinriltn
//
LOCUS       WP_175992278             229 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175992278
VERSION     WP_175992278.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..229
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25722
     Region          8..204
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mstlqyhlvs hvlcpyvqra vivltekgvp fertdvdlsn kpdwflrisp lgktpvlvvd
       61 gapifesavi cdyldetlap plhpdapler arhrawvefa sarlsaiagf ytapdeatla
      121 gktrdirarf qqledtlgag pyfsgthfsi vdaafgpvfr yfdvfeqidd fgffaalpkv
      181 tawrqrlaer psvraavrad ypqllmefll krgsmlstri rehvlrvqd
//
LOCUS       WP_175992422             434 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia vietnamiensis].
ACCESSION   WP_175992422
VERSION     WP_175992422.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10150691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43426
     Region          10..396
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cd06174"
                     /db_xref="CDD:349949"
     Site            order(14..15,18..19,22,54,105..106,108..110,113,133,
                     136..137,140,238,241..242,245..247,250,278,282,332..333,
                     337,342,358,361..362,365..366,369)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:349949"
ORIGIN      
        1 mrparpleal nffiadvqag igpfagvill srgwsadaig svmtlaglaa maatpaagal
       61 vdalrakrll ivcataatal asmtlrfadg yaavaasqvv aavcgaalap aiagmtlgia
      121 rrqgfdrqfg rnqmanhagn vvgaalagwl gwhagfdalf alvaafavla ivsacaipar
      181 aidhacargl ampddaagra rgepasdrgr sgggaappar awrsvaanrp lvllgaslal
      241 fhlgnaamlp lygmgvvaah rsdpsvftaq tiviaqcvmi aaawcaprli rahgywcvll
      301 lsylalplrg vlaaalmsea gvwpvqildg igaglqsvvv palvvrlldg tghvnagqga
      361 vatvqgigaa lspalggvla qhygypvafv vlgavstgsl alwlgyarsl raacgkppgg
      421 adggepadlp vasr
//
LOCUS       WP_175992577             346 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-binding protein [Burkholderia vietnamiensis].
ACCESSION   WP_175992577
VERSION     WP_175992577.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 346)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 346)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 346)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10598562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..346
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37820
     Region          53..170
                     /region_name="AAA_22"
                     /note="AAA domain; pfam13401"
                     /db_xref="CDD:379165"
ORIGIN      
        1 mvtttgtpdp lvaahvprdh pvvtrdyslf tiaihdmaeh igswlddqid gatifgpsrf
       61 gkssavdhwl qrllserhgg fvplviwsht dsgssqavgs fyahlldasg hrlaqarrsp
      121 lerqtmlver wielaaqggg rflvlvidea qgmsqrewlw lvelhsllek qrirlcvfsi
      181 aslqffdepf glalagsahv aarfmlaaep fhgvqttdel ayvmrgyddg sewppgsgks
      241 ftaglaprpw aggfrmehqa aalmqamldt lppryagpid fpmktvaqac rhvllriagg
      301 advdavttad vwdttvrdcg hrelmalisa tamlrgshar eegpha
//
LOCUS       WP_175992662             654 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Burkholderia vietnamiensis].
ACCESSION   WP_175992662
VERSION     WP_175992662.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 654)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 654)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 654)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 654)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 654)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 654)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 654)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19997826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..654
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=72241
     Region          1..391
                     /region_name="AAA_15"
                     /note="AAA ATPase domain; pfam13175"
                     /db_xref="CDD:433011"
     Region          <232..532
                     /region_name="YbjD"
                     /note="Predicted ATP-dependent endonuclease of the OLD
                     family, contains P-loop ATPase and TOPRIM domains
                     [Replication, recombination and repair]; COG3593"
                     /db_xref="CDD:442812"
ORIGIN      
        1 mklksarvtd frsvedsgef kvgdltclvg kneagktall salyglnpya afaydktrdy
       61 prrfvnkfee rsngttskvi dtvwtlddad lkavtdlfge kalatrevrv hrgigydgai
      121 wtlsvnaaec lvflvkehtt ddterkivkd ckdaaqaita ieavaqrsag ldalhaalkk
      181 crgedfelai qdilatrmpk lfltshferm sgevsinaln haranntlts sdrifldfle
      241 yagtsieelq astrleelka kcegasneit deifefwtqn dalqvaidia egrpgdpppf
      301 nagtvvtari hnsnhrvtvp lsersagfiw ffsflaqfkq lrkvagnaii lldepgltlh
      361 gkaqadllry iekrllpthq viysthspfm vpsdrlsdvl ivedvvrrde rnrpivegtk
      421 vrddvlsvdk dtlfplqgal gydmtqslfv gkntllvegp sdilylqals aalqqrkgig
      481 ldprwtmcps ggidkiapfa slfganrlni aalcdvangd kakidrlrks qilqaghvlt
      541 igdftgqdes dvedlfppak yaellnasyg ltgenemtvn rlhdaapktq rvvkqaeaaf
      601 rvlpveiaef dhftpsswli rnprfldgad egilallera erlfttvnal lvkv
//
LOCUS       WP_175992747             200 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175992747
VERSION     WP_175992747.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18951323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..200
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=21341
     Region          16..140
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(21,23,78..79,82)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            23
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(77,121..122,124..125,129)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(83,88..89,117,120..121,124..125,128,131)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(106..108,117..118,121..122,125,129,132,136)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(106,122,125,129,132,136)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(130,136..137)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          152..194
                     /region_name="HTH_CRP"
                     /note="helix_turn_helix, cAMP Regulatory protein
                     C-terminus; DNA binding domain of prokaryotic regulatory
                     proteins belonging to the catabolite activator protein
                     family; cl46859"
                     /db_xref="CDD:481199"
     Site            order(153..155,188..189,191..193)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 mrdpadhytr dlaghvigya rvstadqdaa mqrealiaag aakvfedvas gakadrpglt
       61 aalaylregd tltvwkldrl grslphlvqt vaeleqrgvg frsltesidt ttpggrlvfh
      121 lfaaladfer dlirertrag lavakargsa agrrpvvtad klararmlid akgltvreaa
      181 arvkvgktal ykalavpkev
//
LOCUS       WP_175992751             170 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175992751
VERSION     WP_175992751.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..170
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18121
     Region          55..157
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(60..61,93..94,97,101..102,105,147,151)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mrttmgiavm saavllvgca sepalnrdqe vaanqavgit vepsakgglv rlpetvlfdf
       61 dksnlradag pvvdrsvvll srsdrpievn gytdnvgtre ynqhlseara emvadaliqr
      121 giaasrvtth gfafdnpvvt ndtaqgraln rrteivlpge hlenimgpqk
//
LOCUS       WP_175992786             261 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia vietnamiensis].
ACCESSION   WP_175992786
VERSION     WP_175992786.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..261
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28775
     Region          6..237
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mtlvredats lyeqiattlr deidrgvyep tgklpseaql serfevsrvt vrlaldrlad
       61 ariverkqgk gtfaakqrlr hrldvlrglh dsiagqgara rmellrmetc dvppglrqvf
      121 aadvtrciyl erlhwvddep ialaqtcllp eardvayaqa dsmptyelle qvlgwriada
      181 dmsvtavaap ddiaallktg kqgpllalrr tsrladgrtc estlfhirpe rfdlvvrsgv
      241 earfvacgap svvdhgdgaa q
//
LOCUS       WP_175992844              91 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: putative quinol monooxygenase [Salinivibrio].
ACCESSION   WP_175992844
VERSION     WP_175992844.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio
  ORGANISM  Salinivibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Salinivibrio"
                     /db_xref="taxon:51366"
     Protein         1..91
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10504
     Region          4..>70
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mskvilegfi lvpdadlqav trelvnhekl tleepgclif kvqqhsenpl rfdvyeefvd
       61 rsafdkhqer vkssywgavt qnvtrhyqis e
//
LOCUS       WP_175992940             213 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Salinivibrio sp. EAGSL].
ACCESSION   WP_175992940
VERSION     WP_175992940.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..213
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22259
     Region          6..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtdalslvsi gfaffvvavs pgpanisnat iamskgrkvs lvygaglsig llfwgivaas
       61 glgvvlqgsv yllmllkivg gvyllwlayl sfkssfnaaa tvstndsqev gyrkwfvrgv
      121 vlnssnpktv vawmaalsvg mgsssdglfl vaavltcmlv gflvngmysl lfsingvmnv
      181 yqkvahwver vvsgifalag lgllrsafsr npa
//
LOCUS       WP_175992987             235 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SURF1 family protein [unclassified Salinivibrio].
ACCESSION   WP_175992987
VERSION     WP_175992987.1
KEYWORDS    RefSeq.
SOURCE      unclassified Salinivibrio
  ORGANISM  unclassified Salinivibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Reeves,J.E. and Fried,M.
  TITLE     The surf-4 gene encodes a novel 30 kDa integral membrane protein
  JOURNAL   Mol Membr Biol 12 (2), 201-208 (1995)
   PUBMED   7540914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="unclassified Salinivibrio"
                     /db_xref="taxon:2636825"
     Protein         1..235
                     /product="SURF1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0033617 - mitochondrial cytochrome c
                     oxidase assembly [Evidence IEA]"
                     /calculated_mol_wt=26615
     Region          20..233
                     /region_name="Shy1"
                     /note="Cytochrome oxidase assembly protein ShyY1
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3346"
                     /db_xref="CDD:442575"
ORIGIN      
        1 mgfliltvvv vlllvklshw qwtrgaqkaq hlarfdanqt pqsltgsvqk gqylvidgqf
       61 rpefavwldn qihqgrvgyr lflpfipsqq psqwwlvelg wmaapalral pdvptlasry
      121 qlfgfadtps krvvlkqqte tqtwpvrvqr idlptlqarl palevqwlir aeklvdvtap
      181 srdalaqagv rpvwqpvvmp ptkhygyalq walmalavgi gagiwwhktq rkece
//
LOCUS       WP_175993045             284 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Salinivibrio sp. EAGSL].
ACCESSION   WP_175993045
VERSION     WP_175993045.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..284
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30165
     Region          6..243
                     /region_name="SDR_a4"
                     /note="atypical (a) SDRs, subgroup 4; cd05266"
                     /db_xref="CDD:187576"
     Site            order(10,12..14,33..35,75..77,110..112,135,139,159..162)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187576"
ORIGIN      
        1 msglkvgicg cgwlgtplas hllaaghqvv gtkrqsdaaq awsqslgapm vpfdvmapdy
       61 hhaqplldcd ivviniaagr rnadfdayrs amtafidhla qagvehvlfi sttsvygelk
      121 gqvteqtpta attasgqahe aieahvdrvy gergsvlrla gliggerhps tmlsgrtgls
      181 ggsepvnlih rsdvmaaisa mihqrqwghv fhlsadlhps ksvyyswaar emgltppeyh
      241 psagdgkwid ashtlaqlgl tlryaspyqm iangqvtsdd papk
//
LOCUS       WP_175993108             213 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Salinivibrio sp. EAGSL].
ACCESSION   WP_175993108
VERSION     WP_175993108.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..213
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23332
     Region          33..168
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mslsvyekea ivamekryra tfvnslsgfk sanllgtsdt nqqtnlcivs safhlganpa
       61 lmgviirpdt vprdtlenir atgfytlnhv qkemivaahq tsaryphdis efdqvgltpl
      121 wrekfgapfv qeaairlglv lreehtmain gthllvgeii eahvpdscvs edgfvdieqa
      181 gtvalsgldc yhtasrvgrl syakpdcqpe wld
//
LOCUS       WP_175993165             179 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Salinivibrio sp. EAGSL].
ACCESSION   WP_175993165
VERSION     WP_175993165.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 179)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10120901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..179
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20344
     Region          25..134
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cd02883"
                     /db_xref="CDD:467528"
ORIGIN      
        1 mqiiathidq rvrplesktv ikrdaaraia lqgdeillmy taryddyslp gggidqgetq
       61 eqgmirelqe etgargirdi epfgcfeeyr pwhrdgadvm hmlsycfycq vdrelgtptf
      121 ehyelnngmr pvwvrlnhai ahnkavmans ekagqslvre tmllemiaqq rdstqqata
//
LOCUS       WP_175993185             423 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system ImpA family N-terminal domain-containing
            protein [Salinivibrio sp. EAGSL].
ACCESSION   WP_175993185
VERSION     WP_175993185.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10536173
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..423
                     /product="type VI secretion system ImpA family N-terminal
                     domain-containing protein"
                     /calculated_mol_wt=48132
     Region          19..117
                     /region_name="ImpA_N"
                     /note="ImpA, N-terminal, type VI secretion system;
                     pfam06812"
                     /db_xref="CDD:429132"
ORIGIN      
        1 msfilsidnq pfriiqdvqp lrdderyqai rdqinkrhsp lsggtdwqfv kdncqalase
       61 qgidlllsgy ytvaalkigg laglanglel ilaclnneda vsekrarark ealewvnarv
      121 qgelnqikpd qqalrelyrc eklcdtlyhv leqqqpkyvv dyegiayvlf ehidrietrf
      181 hsalkqqqrd envnptisir vsrirtllag vvgacltavi wlgypyipyf qtpfqvdapa
      241 pslnhadata afakthqpst lvrwesqfvp lyaqsttqel eqsiesskvl akahlnalat
      301 lyadnkqtre lltrydmerk ealentakyi dkfravrtkm anmallaeqn rwwalqkqtr
      361 sledfaisls piygradyva tlvkqgdmdk anaelavlte rlnylswkvv qlqekinvhq
      421 ttq
//
LOCUS       WP_175993193             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Salinivibrio sp. EAGSL].
ACCESSION   WP_175993193
VERSION     WP_175993193.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33181
     Region          11..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,214..219,
                     225..226,228..229)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176159"
ORIGIN      
        1 maphweglne flsvaehgsf tqaankldit vvsvsrrvaa leaylgvklf hrttrkvslt
       61 degelyyqrc rpllaalvda eqtitqsqal psglvrvtap vnfgeqyiap llapfltayp
      121 qvsidlhltn rrvdltdtgt dvairighlp dsslkakrlg srqlticasp gylaahgspd
      181 spsalsrhtc lvgsnehwhy qssgkirtlt vsgklrcnsg valldaakhg lglaqlphyy
      241 vqaalandel vevltdyrvd degiwalyps grqlqpkvaa wlefladhlp dhqlrtstsa
      301 smaar
//
LOCUS       WP_175993194             534 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Salinivibrio sp. EAGSL].
ACCESSION   WP_175993194
VERSION     WP_175993194.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..534
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=56858
     Region          11..519
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mkklilivvc amfavaaias itattfishd eidsiilkrs qaqaelladr aeyilensst
       61 ptadlqdmvs dlkgrddisy avmidknika iahsdrqkid kvysdnytva gagqgqpqhs
      121 rwyadvqdvw vydimmpvyv dgrlwgafdv gipitevdaa angiaiaqlt aiglifigct
      181 lvlvwllgrl faplkgleha ladiskgdgd ltvrlpvtgn neitriseaf ntfvdkidqi
      241 ianvvetgee lgrsagslrd kaaqslkrge sqseqallvv tsmnemiati neisqsassa
      301 adsassanse teagkqtlte atatinqldt emdnmstvit slaertqsiv sildvirgis
      361 eqtnllalna aieaaragea grgfavvade vrslatktsq steeiqstid qlqqeaknav
      421 damdtskalt tegnrateqa ltalesiatq vstildmnth vatateeqss vaneinvnmd
      481 nvnqaaqagl edshsleass qdlaglaqtl dqhvgafkis aikpttgtlr asrh
//
LOCUS       WP_175993222             226 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Salinivibrio sp. EAGSL].
ACCESSION   WP_175993222
VERSION     WP_175993222.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..226
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25832
     Region          1..225
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mkvyghplsi nvqkvmwlie eldlsialee vdirhshrda qaiaercpmq qtpvledgpn
       61 svweshtilr ylvacygnkm wypdcafqrs cyerwmdwcl ssfqpvikra lfssasdhph
      121 amssqamssq amssqamssr dmssrekale qcryhlerid evlaeqkyla sdritladia
      181 igslihslhn easltlppni srwyqqladl pgyqrwimqa estlpa
//
LOCUS       WP_175993248             663 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Salinivibrio sp. EAGSL].
ACCESSION   WP_175993248
VERSION     WP_175993248.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..663
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=73870
     Region          131..663
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mrgsvlirmy lgfsflvvlf ivavvllifn mknmysdfea vseesfplvl ksneartnll
       61 hlekvvknyi nenevkkldg ikdnffkakd vfdkklseie dsarflsmeg shnnplivfd
      121 seyssiasli mssykktlis enrfsqlmrd fqrlnmkltv glkeyvakkn dialtlmadg
      181 ffsqlhnlqn dtsdalssrd layvdqvikk nrkslvhlny afkllssqap dlkdkfdspl
      241 keftkhigmn dgvleeykiv lrdkkelder virldmmark asfelgeisk vaksnldksl
      301 ylastkykdg vvhtfavgli ltiiaagvgi nvsrnvrrpl sdivkvlegl sdgdlkgrll
      361 nnysnefsii grhinhmadr lqelilkigs asedmnkaam knsdaisdtn sklseqnalv
      421 lkanssmrgi efsvskvnds vnvtsnkvis akrasdssln mmndnmemmg vledrlassv
      481 vavtdlkrsc dhiglmldvi hnvsektsll alnaaieaar agengrgfav vadevrelar
      541 ktsestieie dkvqylksra sethcvilnc vedmkksksy algtskavkv iqcslqeian
      601 eskdiescmk eqnsmttdta mrlnaikels desnlaisnm tevsaglsti akeqfdlvkq
      661 fdl
//
LOCUS       WP_175993276             517 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Salinivibrio sp. EAGSL].
ACCESSION   WP_175993276
VERSION     WP_175993276.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..517
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=56060
     Region          28..517
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mfkslkaifv tqvviavsiv lgissyidyq stkkelssal ettvanatnr mnlslpkaiw
       61 dfdleaakls isaelkapdi kavrvldkqg eaivflrlgq dngkdgerqa ktigdgeksm
      121 yesmmlkene lsfteygetn lvgtlqvfyn terleaalad tlkrsvielv vldiviivfl
      181 ilaltatvvk plndltarvr elasgdgdls kvipapkyke faqitehinh ftaslreivn
      241 evtqasinla svsaesgqma rtnaerleqq kqslstvaaa atqmnqsiat vadtandaat
      301 haanatdlvn qvygtiessa seiinmrtem envntemhkl leegekisdv vnvindiseq
      361 tnllalnaai eaarageqgr gfavvadevr slsvktsest ekiqsniksl sdatesveke
      421 inrissiles tagrvsesqe svsqvretit disersgqis qatdeqrqai devsqainea
      481 seatnqvteg aqdnatrtdk vltlsedikg qmekfkt
//
LOCUS       WP_175993285             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Salinivibrio sp. EAGSL].
ACCESSION   WP_175993285
VERSION     WP_175993285.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32634
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..286
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,221,238,265)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     215..219,226..227,230)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdtltaarvl idvgltqsft ataerlemsr pmvtrhveal edwlgvrllq rttrkvslts
       61 ageqslpqle qwveqanvlt qqwqqeaglt gkvrvatsms fgfaqlipav kpfmaahpgv
      121 dvdievqdka vdliaeridi airiasnpdp sligrpiaac dsvlvaapdy laahtpirsp
      181 ddltahscls ykqfdrpiwh ldkgeehaav evqgklsane attllsaaiq gmgvsmqpvy
      241 lahsaiargq levvlpdwqp kamdiyalyp srrnqppavr alldaliahf adskwapvai
//
LOCUS       WP_175993380             252 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Salinivibrio sp. EAGSL].
ACCESSION   WP_175993380
VERSION     WP_175993380.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..252
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26247
     Region          9..244
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 maisleysfi lvilgviagi intlagggsn ltlpalmvmg mpadvanatn rvavwlqcas
       61 gmsgfrqhdk ldtqdiipvl ipnligglcg alaaawlpts wvkplllgtl ltmtvvmlvk
      121 patfgppagt pvkkvadtpt awfglmlagf yggfvqagvg fvllaalcgt lhydlvrgna
      181 lklactlaft slsllvfiad dlvrwapgli laigtmvgar iavrfaisan pkllklflfv
      241 mtlvgclaay lf
//
LOCUS       WP_175993419             371 aa            linear   BCT 11-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Salinivibrio
            sp. EAGSL].
ACCESSION   WP_175993419
VERSION     WP_175993419.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10505910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..371
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40657
     Region          <2..370
                     /region_name="YafD"
                     /note="Uncharacterized conserved protein YafD,
                     endonuclease/exonuclease/phosphatase (EEP) superfamily
                     [General function prediction only]; COG3021"
                     /db_xref="CDD:442257"
ORIGIN      
        1 mtapstlrfa qfnlslagrk agdiksqmqa ptpsrqiknl aatlqrvrpd vvvlcefdhp
       61 gdggddgala afcerhlaks qdgappidyp yrylpatntg lkltvpvsah prltdaqqch
      121 gfgdyhgqfg fviisrypie dtaictwqhf awhqlphhqi psdyyteaak kklrlasknl
      181 vsvpisigeq qirlvachpt ppvfdgpekr nwrrnsdeih qliglldnad wlvddkgvhg
      241 glsseipfvv igdlnadpsy gdgdkqaiga llnhprmhpd vatgaqvpks eaaqshafrf
      301 idgkgraiat hngglrldyv lpsrelavlv sgvfwpapdd adyplicdkn gqeharahsd
      361 hrlvwvdval n
//
LOCUS       WP_175993442            1042 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Salinivibrio sp. EAGSL].
ACCESSION   WP_175993442
VERSION     WP_175993442.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..1042
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114721
     Region          11..1025
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mneaptpprg liayfahnpv aanlimifvl imgiasyffi qrqmfpniei nyihitadyp
       61 gaspqevees ilvkveeaik dvtgiesvvs tarrgfgrve ievdvgedln vvldrvnqkv
      121 daisnlpasm eplnvsqvef rqtvirmavv gdkpltelkp vaqniedell qlndvtlvel
      181 sapnyeiaie vapqqlrkyd ltlgqvsdai arysanfsag evrtdsgmia irvenqryrg
      241 defrqipiki gpngsrlrlq diatikdgft egeryfkysg qnaiflsvna tasqnmvtva
      301 savkdyietk nntlpaglal ksvvdmthyl narldmmlkn llqgavlval lltlflrfkl
      361 amwvlvglpv cflgavmlmp vigvsinivs lfafimvlgi vvddaivige svytevehkg
      421 ggvnnvvaga qrvatpatfg vlttiavfap flmssgpera fffgiaaivi lclvfslies
      481 klilpahlah thfstpkpns lrqrfnrrfq qfihgpyrrt vtrathwrws vltvfialla
      541 isialvvash vrmvptpkvp hdfpnirlem nnnasseqti aalkaiermv ydvdnntqae
      601 tgqamiketl vfnegrtagq lviplvddav rpfttfelsr rwrdampdip gvkkltiqdd
      661 vnggeqgdef gyllfgpdid tlnaagralm srlnqqpglf disssmdsgs qeilisltpv
      721 ahdlgldltt iaqqvggsfy ggeaqrlird geeikvmvry pkrtretfss lryavittpt
      781 gqqvmlgdvv nfeqqpgiss lrreagfrtv yvygaideeq vepnqvveti rqsvipdvla
      841 dypevtsels gsieeqqaqq seqllffiag mivvyallav plksytqpli imsvipfslt
      901 gaiwghywfd idlslmstfg liaaagvvvn dslvmtdyin rarqagvavk qavidagcar
      961 fraitltsit tfagvlpimf etslqarfvi pmavalgfav mfatlltlil vpclylilqd
     1021 igrvlqrlmq rvlptasedq lr
//
LOCUS       WP_175993594             280 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Salinivibrio sp. EAGSL].
ACCESSION   WP_175993594
VERSION     WP_175993594.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5), 4725 (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10897914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..280
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=30167
     Region          3..149
                     /region_name="AANH_superfamily"
                     /note="Adenine nucleotide alpha hydrolase (AANH)
                     superfamily; cl00292"
                     /db_xref="CDD:469708"
     Region          166..279
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mnkiiacidg asytqsvtdl siwaasrlsa pltflhvlek passdselsg siglgsrdql
       61 mselteldek raklalqhgk allheceeva lskgltevtr lqqhghlles llalestmrv
      121 lvigrsgdlh qndakaigsq lesvvrrihn hiliatgdvt ppdsyllafd gsevseklve
      181 kalntpllkg mtchlvmvdn dahseafera aqrltaqgvd vvqarlsgep aqallayqaq
      241 qnvglitmga yghtklrqlf vgstttrivi dspvplllir
//
LOCUS       WP_175993599             557 aa            linear   BCT 11-JAN-2025
DEFINITION  BCCT family transporter [Salinivibrio sp. EAGSL].
ACCESSION   WP_175993599
VERSION     WP_175993599.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..557
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59919
     Region          25..543
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 msarstsdas nastlqhpfa dcvtqtgpfk gvhknmmiaa tllvfvfvff tgfnthlaas
       61 vfaaargwve stfgwyymlv lvlllaasfi iavtrfgnir lgddddrpef stfswlsmlf
      121 sagvgvgilf fgvaeptlyf dtsgafgypn npyadmagat tmgfdraaaa lrvtyfhwgf
      181 hgwavyvivg lalayfsfrk klplalrsti ypligdriyg pighitdilg vlgcvfgvat
      241 slglgvsqia vgldrlfgid pgvmtqvili vlisvasims slsgvgkgir iisewniivs
      301 alviayflfg gpttwlihvf gaslsdylvg fipmglwfpe tpgpaawqna wtifywgwwi
      361 gwapfiglfi arisrgrtlr efvvcvlcap tlmifawlai fggnalhqel vaemgvgtag
      421 iidlvngwdl paalfatadg itgggiwgwi lnammifllf swfitssdss tlvlttilsm
      481 gnddppkrfr vfwgtmigav aavllvaggl ralqtanmvt alpisvlvil mtisvmksll
      541 aepvgkptas tpsqanr
//
LOCUS       WP_175993625             455 aa            linear   BCT 11-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Salinivibrio sp. EAGSL].
ACCESSION   WP_175993625
VERSION     WP_175993625.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..455
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=47685
     Region          2..454
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mirttlstla naigatvyya dhasgtppid aittdtrelr agalfvalkg drfdghdfae
       61 qakasgaaam vvsreldidi pqllvddtrl algqlgawvk qqcqvptiai tgscgkttvk
      121 qmlatilaqk gptlstagnf nndigvpltl frltpahhya vielganhig eiayttslvk
      181 pdiamvtnla aahlegfgsl egvavakgei yqglpeggia lvnqgshggd twgdvladkq
      241 viavtdtqaa pltlidsalt taggyqltls dgqsqqsvml plpgkhniin almagcaamq
      301 lpdvslvdvv tglesvenva grtqvseprp glrliddtyn asvpamksai dvlasypger
      361 wlivgdmael geyseqmhre vgehaaqaav nrvfttgrds rvisercggd hfdskealia
      421 hvvamiktqt pdtilikgar gmameavvta ikeac
//
LOCUS       WP_175993699             337 aa            linear   BCT 11-JAN-2025
DEFINITION  permease [Salinivibrio sp. EAGSL].
ACCESSION   WP_175993699
VERSION     WP_175993699.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..337
                     /product="permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=36669
     Region          22..332
                     /region_name="YraQ"
                     /note="Uncharacterized membrane protein YraQ, UPF0718
                     family [Function unknown]; COG0701"
                     /db_xref="CDD:440465"
ORIGIN      
        1 mfdvftyfad wlayqligls pdtqlgeaih ffiedttkil allvvmiyvi allraslkve
       61 rvrdylagkk rffgyasgsf fgaitpfcsc ssipvflgft sagiplgitm aflitsplin
      121 evailllfsl lgweftlayv algitigivs gwfldaigaq rwlqpfaana mekaqaqpas
      181 pttsstpasp ssasaislna rhqfakqemk divgriwkwv figvgigaal hgfvpdgwie
      241 shlgagqwws vpasvfigip lysnatgvip imesllrngl plgttlafcm stvaasvpef
      301 vmlkqvmqwr llailfalll tgftvtgwvf nlpfwqf
//
LOCUS       WP_175993728             213 aa            linear   BCT 11-JAN-2025
DEFINITION  potassium channel family protein [Salinivibrio sp. EAGSL].
ACCESSION   WP_175993728
VERSION     WP_175993728.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 213)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10545436
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..213
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_function="GO:0005267 - potassium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=24161
     Region          128..201
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
ORIGIN      
        1 mnfklivtgt ielllsptyf fadykkskyg senknispli krfnsiylli aslialglff
       61 ypptevykte lgdaffwfam fivwvyplsr aneiiyafyr daieklngep srsdlkyger
      121 iqlavksyie liinfasiym llppcyfdnk insyidalyf sgvtittlgy gdispryafp
      181 qflsvyevlc gftlivvsfa vytgrgieas gsa
//
LOCUS       WP_175993773             317 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Salinivibrio sp. EAGSL].
ACCESSION   WP_175993773
VERSION     WP_175993773.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..317
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34840
     Region          4..316
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 msnlleinnl cvdyvspngl aravncanls iskgetigla gesgcgkstl afaisrlhka
       61 palisegeii ynkkdvlkmn dkelrkfrwn dvsivfqsam nslnpvitig eqltdvlqah
      121 kdipyklaye kgiellntvg mhgdrmesyp hqlsggmrqr vviaialale pkliimdept
      181 taldvvvere ilnelyelke kfgfsilfis hdlslmgeia driavmyagn iveigtaekv
      241 fsepqhpytk glissfptih gpkerlygip gnpvnlldlp kgcnfqarcn ecfsrckese
      301 pelvsasngs yvschli
//
LOCUS       WP_175993865             337 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Salinivibrio sp. EAGSL].
ACCESSION   WP_175993865
VERSION     WP_175993865.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..337
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39033
     Region          1..221
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mitilmpvfn askflnesig svlaqdyknw eliciddqss ddslsmlydf srkdarikvy
       61 tkenegpaqa rklglqhssg dyvtlldadd alspdflsqt lavatetdad vvmpvliqnw
      121 ksdnrsdydf nlknglmfkq eiaprvaflk tmpwrvhgln lykaehfkky alseisninn
      181 ynadeyltrf lllyankivv segkyfyran nksitttfsl rrigllktne alfnlakker
      241 fndeelkmia lhflrlaaal kyqllknknk lnysemtnai aeinknyswh nylgndfktv
      301 lmrlfvlfyp sffssllsmf vsikmfftnq rhykkpl
//
LOCUS       WP_175993815             654 aa            linear   BCT 11-JAN-2025
DEFINITION  beta-N-acetylhexosaminidase [Salinivibrio sp. EAGSL].
ACCESSION   WP_175993815
VERSION     WP_175993815.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 654)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 654)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 654)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 654)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 654)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 654)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         1..654
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=73985
     Region          127..649
                     /region_name="Chb"
                     /note="N-acetyl-beta-hexosaminidase [Carbohydrate
                     transport and metabolism]; COG3525"
                     /db_xref="CDD:442747"
ORIGIN      
        1 mtyrldlsvi neypndtppr srmgltlhnl tdcllnqlsi avlfdrfinp ntlsqgsieq
       61 vgsycvitpa hqtldanqsl yiefdahtpp lrflcagfkd allyangeqy svmltpinla
      121 hthttrssip dvhpaehaii pvpksvrhqp gyftlspttp liavdpqalp aaqwlsnewv
      181 rmypqadial dprhqdavtg dhaillrplp dsalrdithr deayqltvtd qgvviqacae
      241 rgfihgcasl lqlcqeqdtq lripaikisd aprfayrgmm ldcarhfhsv dtvkrlinql
      301 ayfkfntfhw hltddegwrl eikalpeltr ygsqrgpntr lapqfshiae rhegyyrqee
      361 vrdvieyaaa rgitvipeid ipghcraaik alpdwlhddd drstyrsvqh ytdnvlspvl
      421 dgtyrfldtv lsevaelfpa swvhigadev pdgvwtdspi yrdrrmnget taslqgqilt
      481 yaeqklralg krmvgweevq hgdkvskntv iyswqsedaa lhcaqhgfdv iltpgqatyl
      541 dmvqdyaate pgldwagvtp lekayqyepl aslasddpar ehmlgvqcal wselitnqdr
      601 ldymvfprlt aiaeaawshs errdwldyla rlkaqlprld kfgiqyrspw asnk
//
LOCUS       WP_175993923             333 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein, partial [Salinivibrio
            sp. EAGSL].
ACCESSION   WP_175993923
VERSION     WP_175993923.1
KEYWORDS    RefSeq.
SOURCE      Salinivibrio sp. EAGSL
  ORGANISM  Salinivibrio sp. EAGSL
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Salinivibrio.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Salinivibrio sp. EAGSL"
                     /db_xref="taxon:2738468"
     Protein         <1..333
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
     Region          <1..313
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 dehgrvkvhf pwdrysngdd ksscwirvaq gwagsqygmm aiprighevi vsflhgdpdq
       61 piitgrtyha tnvppytlpa hktktvwrse shqgegynel tfedqsgseq vylhaqkdwh
      121 tevendrvte ighdnhhqvh ndqfhrvmgn ahhtvegesr triggnhsnl vkasehykvg
      181 kvhaveagsd ihlktgaklv ieagaevtls aggsfvkvda agvhasgaav nlnsggsags
      241 gpgfngqmak rpktidalad peaaplpdiq avdvmttset qqgaptliav pataslvqqv
      301 iadvkseipi tqaclkqpdg scplsdcpcg nnv
//
LOCUS       WP_175993948             197 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Actinomyces marmotae].
ACCESSION   WP_175993948
VERSION     WP_175993948.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces marmotae
  ORGANISM  Actinomyces marmotae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Actinomyces marmotae"
                     /db_xref="taxon:2737173"
     Protein         1..197
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20623
     Region          11..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 messaprggg rprdpridgr iltaaarlma sgglgalrad alataagvpk stiyrrwgtl
       61 ldlavdavda algprhlpat eepladlath vqrahtilat pplgpaviqi ahellgrpea
      121 aasyrqrvia plrdgaidav sraikagqwd gpeavlsidm vigtvlyrlt ylgiettlee
      181 afelvetiag rplprpa
//
LOCUS       WP_175993979             824 aa            linear   BCT 11-JAN-2025
DEFINITION  (Fe-S)-binding protein [Actinomyces marmotae].
ACCESSION   WP_175993979
VERSION     WP_175993979.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces marmotae
  ORGANISM  Actinomyces marmotae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 824)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Actinomyces marmotae"
                     /db_xref="taxon:2737173"
     Protein         1..824
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=87211
     Region          69..>135
                     /region_name="FdnI"
                     /note="Cytochrome b subunit of formate dehydrogenase
                     [Energy production and conversion]; COG2864"
                     /db_xref="CDD:442111"
     Region          331..818
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mtslevlqav caavvlvsti vgvtvfgrac ltiarrlrvg rpvprerlrp igrrawlsls
       61 salnhrafrr rpwiraahwl vmisfpllfl tlvtgygqvl ggaaftlpll ghaawwgwvv
      121 diiawlslag iihlvavrrr ltrrgaaepp yaadseggar prtsrfagst tsqahfveai
      181 iaavvacvla lrmleharla aspdaaeral atwtrfplta wavpaleplg ftglaaaiti
      241 vatikvvvsm twfvvvgrqp smgvawhrfl afiniyarre vdgskalgpl tpialpdgrp
      301 ltaetmddld aameaadege gpevrlgvgr ieeftwkgll dfstctecgr cqdlcpawnt
      361 gkplspklft lalrdhaaaa apylraaael gvapeevddd alpargvssp tgsaglapgs
      421 ahtgdvlgal laakaaptes gvatrpapla gdvipadvlw acttcgacve qcpvdiehld
      481 hvvdvrrqqv lmesafpkel ggmfrklesk gnpwglaark rmdwakgldf dvpvigddve
      541 saadvdylfw vgcagafedr akkttravae llhiagvsfa vlgdaesctg dparragnei
      601 lfqmlaaqnv etlseagatr ivvtcahcfn tlareypqvg gqyevlhhtq llnrlvregr
      661 lrpapptpgs gdpgsgaads aggapgngas pidpssapna apstaptvty hdacylgrhn
      721 rvyspprell eatgatavem prhreeafcc ggggarafme esigtriave rsreaigtga
      781 qviatacpfc ttmlsdgvas egadvrvadv atlmleavhr gqra
//
LOCUS       WP_175994003             292 aa            linear   BCT 11-JAN-2025
DEFINITION  ComF family protein [Actinomyces marmotae].
ACCESSION   WP_175994003
VERSION     WP_175994003.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces marmotae
  ORGANISM  Actinomyces marmotae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Actinomyces marmotae"
                     /db_xref="taxon:2737173"
     Protein         1..292
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=28913
     Region          35..263
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mtslprpapa gsprpgppaw laalpaalgl alpkscagcg rwetalcpgc aalldaplte
       61 vtgapaaeel rvhavlayag pgralilnwk ngaredlapv maavgarage qwaalaqwpg
      121 ggpgagapar livvpapsgi arrargrlva aaladavaqg iarapapppg gagspgpliv
      181 sadilrreng rafrgahqag lsaaqrrrnr qapprvlada sgwdalivdd vvttgstlrs
      241 catalrgaga rplgalvlaa tppparatar lpgpvgppgg agrrgrtaak rl
//
LOCUS       WP_175993981             370 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Actinomyces marmotae].
ACCESSION   WP_175993981
VERSION     WP_175993981.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces marmotae
  ORGANISM  Actinomyces marmotae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Actinomyces marmotae"
                     /db_xref="taxon:2737173"
     Protein         1..370
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37217
     Region          5..369
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mrdglsidgl rvvypggrga gpvvavdgvg lgipsgrita llgasgsgks sllravagle
       61 pvaagtirwd grdvvatpvh krgfglmfqe gqlfpfrdva gnvgygltgm traqrarrva
      121 emlelvglpg yaarpittls ggqaqrvala ralaprprll lldeplsald ralreqlagd
      181 lrailteqgt talyvthdqd eamtvadevg vmeagrlsrl aapealwadp gsvgvaaflg
      241 fspilvreea ealgwgslld agrpgaragg gagvglalap galsivgpqe gapgadgtgg
      301 rgcaelpgas gtvlarrvrr ggvevdvsld vpggravvaa gvsggdgaan gvgervrlgl
      361 dasrtaiief
//
LOCUS       WP_175994026             552 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC-F family ATP-binding cassette domain-containing
            protein [Actinomyces].
ACCESSION   WP_175994026
VERSION     WP_175994026.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces
  ORGANISM  Actinomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Actinomyces"
                     /db_xref="taxon:1654"
     Protein         1..552
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59325
     Region          4..547
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 minvqdltlr igarrlvaga gfrvdkgmri glvgrngagk ttmtkllaaa svaqgtsqav
       61 adgderhgld avehegtisc ngtvgylpqd tkvgdlgeia rdrilsargi dsllarirka
      121 eeristtegd amakaldryt rldheftmag gyaaaseaar iaaalslpdr vldqpigtls
      181 ggqrrrvela rvlfahpdtl lldeptnhld hdsivwlrdh lraysggfiv ishdvellrd
      241 tvnqvmhlda nrgaldvyhl gwdaylkqra ddehrrrrer anaekkaatl raqgekmrak
      301 atkavaaqqm lkraerlmag leaeqqadkv ahlrfpdpap cgktplkaag lskaygslev
      361 fagvdlaidr gsrvvvlgln gagkttllrl lagvetpdsg evlpghglki gyyaqeheti
      421 dndrtvvenl rsaapemddt qvrgvlgsfl fsgadadkpa rvlsggektr lalailvvss
      481 anvllldept nnldpasree ilralstftg avvlvthdeg avtalnpdrv lllpdgdedl
      541 wgddylelva ma
//
LOCUS       WP_175994056             450 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: hemolysin family protein [Actinomyces].
ACCESSION   WP_175994056
VERSION     WP_175994056.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces
  ORGANISM  Actinomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Actinomyces"
                     /db_xref="taxon:1654"
     Protein         1..450
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=46672
     Region          1..431
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mrdalmilvg illtagtavf vagefslval dpstvetraa agdrraervr lalgrlstll
       61 sgaqvgitlt tillgytmqd alanildgll sgwvaqsvaa gaavtlalvl vnafsmivge
      121 lipknatlsd plraaglvtp flsgfttils pvirvlnata nivlrrlgit paeelsgars
      181 agelaalvrh sakegaldas tatlltrsil vaelsavdvm tdrgrlhtlp arataadvvd
      241 laratghsrf pvtgddvddi qgivhlrrai gvphakraev pvtssslmtp aprvpetmpl
      301 asllvelraq gvqmavvvde yggtagvvtl edaveeivgd vadehdrrrg gahleasgdw
      361 ivpgwmrpde latragvhvp ddgpyetlgg lvmtelarip aigdrlalpr aeliveameg
      421 rritrlrvrp vgaagasgag edpaeggara
//
LOCUS       WP_175994066             630 aa            linear   BCT 11-JAN-2025
DEFINITION  FHA domain-containing protein [Actinomyces marmotae].
ACCESSION   WP_175994066
VERSION     WP_175994066.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces marmotae
  ORGANISM  Actinomyces marmotae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Li,J., Lee,G.I., Van Doren,S.R. and Walker,J.C.
  TITLE     The FHA domain mediates phosphoprotein interactions
  JOURNAL   J Cell Sci 113 Pt 23, 4143-4149 (2000)
   PUBMED   11069759
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Durocher,D., Henckel,J., Fersht,A.R. and Jackson,S.P.
  TITLE     The FHA domain is a modular phosphopeptide recognition motif
  JOURNAL   Mol Cell 4 (3), 387-394 (1999)
   PUBMED   10518219
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Hofmann,K. and Bucher,P.
  TITLE     The FHA domain: a putative nuclear signalling domain found in
            protein kinases and transcription factors
  JOURNAL   Trends Biochem Sci 20 (9), 347-349 (1995)
   PUBMED   7482699
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Actinomyces marmotae"
                     /db_xref="taxon:2737173"
     Protein         1..630
                     /product="FHA domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=62940
     Region          519..630
                     /region_name="FHA"
                     /note="Forkhead associated (FHA) domain, binds pSer, pThr,
                     pTyr [Signal transduction mechanisms]; COG1716"
                     /db_xref="CDD:441322"
ORIGIN      
        1 mreaagtige arwgagdwhg iitpraslil ppvipmpive rlwrdlhgdg lttaavlwdv
       61 issvvartge rpdfafvlle pdgnrhvavr grgivrtshg diasgptstw tetivepsdt
      121 lvlltpdtgd gimrpladgi apvsvvalpa laeeerpega stvhdaaslp rraeasgpsp
      181 atsrptadvl agapapsaap vapsvapvap saapvapsaa pvapsaapva ppaaptppta
      241 psapagrpet lpepavestl avpfdpaail agidqqaaps adgvpetlpe pavestlavp
      301 fdpaailagm nqgstpaeae gwtasgpavt agsvpapsag sapllpasaa sgpaapsapi
      361 aasapaafsa pgapsapiaa sapaafsapg apsapgafsa dlpaqtgpgi taapnfavgp
      421 estgesslts paplrrgdhd gstvaelpgd lleeirsars elaelptpdr sglvpshgar
      481 vlsafcansh pnpthlvacr vceaplegpv rlaprpvlgs lilsdgrvls lggpivlgrr
      541 psadrvatfd agfptcikvs spdrqisrnh llididewsv lardlsntng tvllregsap
      601 vhlsrvetti lrsgdvlelg egvtarfeaa
//
LOCUS       WP_175994067             491 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NCS2 family permease [Actinomyces].
ACCESSION   WP_175994067
VERSION     WP_175994067.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces
  ORGANISM  Actinomyces
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Actinomyces"
                     /db_xref="taxon:1654"
     Protein         1..491
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=50633
     Region          22..484
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 msttspgraa psrptpstal paldrffrit ergstvarel rggvvtfftm syilvlnpli
       61 lggalagdgd vtsakakiaa gtaliagvmt ilmgvvanyp lamaaglgin amvaytivgn
      121 hgmtfadamg ivviegviil ilvltgfrea vfravppflr taisvgiglf ialiglvdak
      181 vvraggtple lglggslkgw pvvvfllglf ltiilhirkv rgailigivs atllaviiea
      241 iqglgafeeg snptgwalsv pslsgspvsv pnlsglghfs llgsfekagv vsivllvfsm
      301 mladffdtmg tmvaigaead lldengnppr treilvvdsv gaivggvgav ssntsyvesa
      361 agvgegartg lanvvtgalf lasvflsplv amvpyeaatp alvvvgflmm tqvadidwkr
      421 pelgipafmt iimmpfsysi tngigagflt yvlvetavgr arrihplmwl taalfavyft
      481 tapikeilgl s
//
LOCUS       WP_175994085             336 aa            linear   BCT 11-JAN-2025
DEFINITION  ParA family protein [Actinomyces marmotae].
ACCESSION   WP_175994085
VERSION     WP_175994085.1
KEYWORDS    RefSeq.
SOURCE      Actinomyces marmotae
  ORGANISM  Actinomyces marmotae
            Bacteria; Bacillati; Actinomycetota; Actinomycetes;
            Actinomycetales; Actinomycetaceae; Actinomyces.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Actinomyces marmotae"
                     /db_xref="taxon:2737173"
     Protein         1..336
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36163
     Region          30..289
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mpgsifdqvr adhstlsela eggfqppeqt rviavanqkg gvgktstavn vaaalaeagl
       61 hvllidadsq gnastalgvp hdeehasiyd vlvdgmpfnd vvvqtrfapt lyclpatidv
      121 aaveielint ssresklrla ledylrsrye dgqprmdyii idcppslgim tinafvaane
      181 vlipmqaeyy aleglallsr sieriakihn palavsmivl tmfdgrttla rdveaevrty
      241 fpdatldtki prsirvaeap sfgspvvfwd prasgaiayk rlaweiadrg iagwqtrrvv
      301 rettegshnp qvedagitgn vnsndagtad nnskea
//
LOCUS       WP_175994163             548 aa            linear   BCT 11-JAN-2025
DEFINITION  S8 family peptidase [Burkholderia vietnamiensis].
ACCESSION   WP_175994163
VERSION     WP_175994163.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10165821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..548
                     /product="S8 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=54548
     Region          235..514
                     /region_name="Peptidases_S8_13"
                     /note="Peptidase S8 family domain, uncharacterized
                     subfamily 13; cd07496"
                     /db_xref="CDD:173820"
     Site            order(242,310,314,381..383,409,411..412,482)
                     /site_type="active"
                     /db_xref="CDD:173820"
     Site            order(242,310,482)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173820"
ORIGIN      
        1 mranrfdfal arsaharvla gmlsaaallp iagcgggggd gsspataapa paptpapapa
       61 papapaptng ttcaaqqaav qmaaqtvapt eppvdhlivr lkpstgtram aaldvgtrld
      121 aviqrsmtrw saptttgaar ayaaattsln vqvertlang aavlsigqri asddaaalaa
      181 afaadsdvdy aepdhpmhvr dtpsdpsysq qwylsdpavg intppawtrt kgaptvvtav
      241 ldtgyrphpd lvanllpgyn fisnantsnn gqsrsndatd pgdwvtqqel ddatgpyyhc
      301 asepnnsswh gtrvmgviga ganngigvag vswlgrilpv rvlgkcggtt sdiadamrwa
      361 agipvngvpt nptpakvinl slggvgacst tfqqaiddvn akgvtvvvaa gndglstgld
      421 qpancrgvis vgatdatgrr asfsnfgadv slsapgvgil stansgttvp gadsygtasg
      481 tslatpqvsg ivslmlavng nltpaqiqqk lqggaraaml paattsctal pagagiadag
      541 aavtaaaq
//
LOCUS       WP_175994207             843 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia vietnamiensis].
ACCESSION   WP_175994207
VERSION     WP_175994207.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 843)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 843)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..843
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=90863
     Region          54..697
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mssvrellak waaraqpvaa aaavpvkrvl asawrhlrhp trrgalraaa avpvlfllyv
       61 lalipftpgi gdirkarvdq paqvlsadgk vlaefkpsnr ewvslkqisp hmvdaliate
      121 dhrfyehhgl dwkrtasaal htfsgdrqgg stitqqlarn lypdeigrap tltrkvkeai
      181 talkiealys keqiletyln tvpflynayg vemaartyfd ksadeldvld aatlvgmlkg
      241 nsyynpvlnp eralqrrntv laqmvkygkl saaqfaqlqr rplridferq keppgpaphf
      301 aqqlrkwlig wadrndyniy sdglivrtti dsrlqqiatq altqqanqlq giannawsgs
      361 dgcgtdnevf rtfmrespey kaaqdagknn aaamkqlaad rgfmralcka ktdvqagfva
      421 idprdgqira wvgsrdftse pfdhvaqarr qpgstfkpfv ygaafasgmt pddtfidqpv
      481 eiplkggeiw rpnddvppsg kpmtlrdala lsrnritaqv mekvgpaava rlardmgvre
      541 splervpsla lgtspvtlke mvasyatian gglytepqmv trienrqgdv laeyapappe
      601 raldgetdkt lldvmrdvvt rgtgssirtr fgvrgdvagk tgttqdnadg wfilmqpglv
      661 agawvgfddg rvtlrsdywg qgahsalpiv geffqraqra rivdaklkfd tepspgwfas
      721 vrervtdlfd gwfgpepkka ptrvrtqrie rqpdadaaaa saasaasape aasggiveqw
      781 ipasevaasa aamsggasqa pvlpppaags agnaggagpg aasgvapgpa papaspesas
      841 ssq
//
LOCUS       WP_175994233             316 aa            linear   BCT 11-JAN-2025
DEFINITION  ketopantoate reductase family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175994233
VERSION     WP_175994233.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..316
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32771
     Region          1..307
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkiailgaga lgcaigaalt eggnevwlln rsaahveamr rdglrvddrn gsrhvkvhat
       61 traaeagvvd lvivlvksfd tdaamrgave ligpetlvls lqnglghedv ladivgrerv
      121 lagktyvggv mrnpghiesg vvgkathige ldgritpran aiadtfnasg ldttvsaniv
      181 gtmwdkllvn vatgaltgat gltygqlyde pllkatalsa vaeamavaha agvtlstddp
      241 erawtlageg lspgfktsml qslekgsite idfingavvr wgrrhgvptp vnatlvacik
      301 giergmadrk kqetta
//
LOCUS       WP_175994248             274 aa            linear   BCT 11-JAN-2025
DEFINITION  SH3 domain-containing protein [Burkholderia vietnamiensis].
ACCESSION   WP_175994248
VERSION     WP_175994248.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..274
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28005
     Region          5..96
                     /region_name="YraI"
                     /note="Uncharacterized conserved protein YraI [Function
                     unknown]; COG4991"
                     /db_xref="CDD:444015"
ORIGIN      
        1 msktmirslc vvlfgiaaap giaaaqssay tnsvaalyag papdypvvaq lppgtavdvf
       61 gclsdyswcd valpgvrgwi daeqldypyq gyyvplieyg aivgvpvtgf aigaywdryy
      121 rkrpwfhdrd rwehraepri gpgglppgqg hpqpggpiqr apggapppqh dtrpsatrgg
      181 wggpnrmpap qampqpapvp haapqpgpaa aphpapppgp gpavvrpapg pgggprmlpp
      241 qgnpggggyg grsqgggnag gghgggvgnd efrr
//
LOCUS       WP_175994344             216 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            vietnamiensis].
ACCESSION   WP_175994344
VERSION     WP_175994344.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..216
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24983
     Region          3..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mlpedrekei ieesvrffae vgfegtlrel alrlgithqn lfryfstkea lidrvyqevy
       61 lsrwqpewea mlrqpgksle arlidfykay lhaifrydwv rifvfaglkg vgisqrylal
      121 iqtrliepla ielrslsgdt ptrkalsade levawglhge lfylavrrwv ydmpvpddld
      181 rvietaiarf lhgapaamqa vardrasakp lrqrgr
//
LOCUS       WP_175994369             298 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia vietnamiensis].
ACCESSION   WP_175994369
VERSION     WP_175994369.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..298
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31132
     Region          37..284
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mqslsgssap spapapsdar gttlraprvs gacaiaalqw svtlllcafl ivpvvmsvla
       61 gvtvdyfrgl ssgltlrwle qvwqqyqgsv alslgvafat laivlvtgvp agyalarsns
      121 rvaraieeal vlpvalpgla salallvvyg gftafrmslw fivvghvvft lpfmvravaa
      181 vaagaelrtl eegaaslgas fvtrfvtivl pnlrpgivag alavltlsig efnltwmlht
      241 pdtktlpvgl adtyaslrle vgsaytivfl lmtlpllvam qwlgvdpsgt raarrrar
//
LOCUS       WP_175994357             346 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia vietnamiensis].
ACCESSION   WP_175994357
VERSION     WP_175994357.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..346
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38160
     Region          15..323
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mvpvsrpaga trttqvaiva lppvsmsgvg pivdalnlan eidgrllyrw qvcswdgrpv
       61 plaggaqwha daafndaiac dwlivvserf qqfadyrlfl aslarvgqrt pvvsgihhgv
      121 wwlamagqls gyrvsvnwet yqqfaeqfer sivtqqifei drdratcagg qatvdfmlam
      181 igrehgadla eriadalgag tlrsgeerqr ipfvtapger hprlndalll meaniedplt
      241 tdeiaglvgv srrqlerlfr qylgampsky ylnlrllkar tqlqrtsksv vqvslacgfs
      301 saahfsnayr erfgvtpred rrawlekqtg ggsepragal verhgd
//
LOCUS       WP_175994510             259 aa            linear   BCT 11-JAN-2025
DEFINITION  TatD family hydrolase [Burkholderia vietnamiensis].
ACCESSION   WP_175994510
VERSION     WP_175994510.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..259
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28866
     Region          2..257
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mfvdshchin fkgladrlpa vlenmrehdv thalcvsvdf etlpevlaia qahdnvyasv
       61 gvhpdhedah dptlaeliel aahpkvvaig etgldyyrle grsiadmewq rerfrthira
      121 atatmkpliv htrsssedtl rimaeerahv pggvmhcfie pwpvaeqala qnfhislsgi
      181 vtfknatdvq dvarrvpler llietdspyl apvpyrgkpn epayvshvgr fiaaqrgiav
      241 ealadattqn ffrlfriar
//
LOCUS       WP_175994575             254 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF899 domain-containing protein [Burkholderia vietnamiensis].
ACCESSION   WP_175994575
VERSION     WP_175994575.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..254
                     /product="DUF899 domain-containing protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=28502
     Region          1..251
                     /region_name="COG4312"
                     /note="Predicted dithiol-disulfide oxidoreductase, DUF899
                     family [General function prediction only]"
                     /db_xref="CDD:443453"
ORIGIN      
        1 mtthltgtrd ewltarrall daektltrhs dalarrreal pwvrvdktyr fdtehgaatl
       61 ddlfdgrsql lvyhfmfgpd ykagcpscsa ladgfdgfav hlanhdvtla avsraplakl
      121 layrqrmgwr fpwassegga fnfdfnvsft eaqqrtgdve ynyaraaham dvdpppaava
      181 qfaatcgtda atyardrpgm safvredsvv yhtystyarg ldalwgmyaw ldraplgrne
      241 tgvwwrrhde yard
//
LOCUS       WP_175994667             402 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175994667
VERSION     WP_175994667.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..402
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43624
     Region          74..339
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mtfplepdar avrgeadthd vappqfgvdg eqaerdwplm tldevagvla ridgagapar
       61 lawhsprpfs aavlvhttse ralfvkrhha slrdvaalae ehrfiahlra rgvpvadvla
      121 ardgasafas gewtyevhal apgvdayrgv mswkpfahps hayaagrala elhrasagyd
      181 aparpvrtll ssfcvlscad ltgalarwvd aqplltralg trdwrgdvak wigpyharlv
      241 pllgalpplw thgdwhasnl lwtdaapgal vrtvldfgla drtcavmdla lalernaidw
      301 lapaaarrve ydqigalldg yesiaplsdd ayaalvamlp ivhtefalse vayfgcivaa
      361 peivdvaydg ylighaqwfg erdgrrlldw lgerrltkrr sl
//
LOCUS       WP_175994656             317 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia vietnamiensis].
ACCESSION   WP_175994656
VERSION     WP_175994656.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..317
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34186
     Region          11..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..291
                     /region_name="PBP2_CrgA_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08475"
                     /db_xref="CDD:176164"
     Site            order(103,107,146,161,163,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176164"
     Site            order(104..105,109..110,112..113,116,120,122..128,190,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176164"
ORIGIN      
        1 mderlrgvae fvdvvesgsf aaaalragkt rsavakivar leqrlgarll rrttrqlglt
       61 degliyyeqc rrllaelget eaaldagrre pagrvrisvp vlfgrqcvap vvrrlveryp
      121 klevdlsfsd riadlvndgf dvavrigela dtsalvgrkl gvqrmgicaa paylsrhgrp
      181 sgldelashv giaysrggqp spwrvigadg tvrehrpagr lrlddllaia daaaagagla
      241 wlpcwlmapy vrdgrlalvm dsnsvsgaev favrpasrhv pskvrvvvda lvdeipqmla
      301 sddadgerap rrasrtr
//
LOCUS       WP_175994689             483 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia vietnamiensis].
ACCESSION   WP_175994689
VERSION     WP_175994689.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..483
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48959
     Region          20..420
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(27..28,31..32,35,67,117..118,120..122,125,147,
                     150..151,154,284,287..288,291..293,296,324,328,380..381,
                     385,389,405,408..409,412..413,416)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mdtsrspalp palarvvatv svgfvvtqld vtivnialah fagdlhlpva alqwvvdayt
       61 lafavlmltg galgdrfgar rlyvaglvlf svaslacgaa vspamliaar aaqgigaaam
      121 lpnslallnd acrhdprlra ravgawtaag sisiaagpvv gglliaawgw rgiflvnlpl
      181 caaglaatfa wvparradaa pppaaarlld vrgqliaiam ltaltaavie wrplgfvhpv
      241 vaggfavaal aalafvavea rstapmlpls lfrrrtfsaa vlfgvcvnlt yygtvfvlal
      301 ylqrvrgeta lqaglaflpl tggfllsnla sgravahdgp rmpmlagalv aavgygslhf
      361 vdaqtplpll lvpfllipag mgfavpamtt avlasvepar agiasavlnt arqaggamgv
      421 aafgaltgag gaaqtvhglr vetavsvall iaaallatlv rrdahrdphr daaaarrpvs
      481 aad
//
LOCUS       WP_175994738             516 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia vietnamiensis].
ACCESSION   WP_175994738
VERSION     WP_175994738.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..516
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54333
     Region          10..441
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(17..18,21..22,25,57,108..109,111..113,116,136,
                     139..140,143,267,270..271,274..276,279,307,311,363..364,
                     368,372,388,391..392,395..396,399)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mkkwivlfsi giclllanld mtivnlalpa fstefgasmq qiqliivsyl taaaaffclf
       61 gkmadsvgrk rvfmfgavlf mvsslylgaw sstvteiiva rfvqgagfaa tlglalvlia
      121 nafppdqkgf atgvavtitg vgmalgpltg gfilqylgwr wifllnvplg llsivltwif
      181 vsddaagarr plaldvagvp fylfalgcli yvsnmlstaa tatlaaiava gllsaaifvr
      241 rslrkpapli nvtlltsrgy ltvilirmif nytmasflfv lplfmqnvld ysklksgmwl
      301 lcmtiavafi aplagkvidr vgfriptlvs msllfvscaa fcvlgpatss aifvvglfcf
      361 gvsngmltta tingvttqvp akdagtaigl fftlvmvgsm fgvsvaglvl drvshaevva
      421 rlahaalpla eparaalfma angsrniaes glqndaptfa aatqiahaay ysalgklmtg
      481 nalltlvgvg lsimllkkqp srsmsgatha ieiper
//
LOCUS       WP_175994742             206 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia vietnamiensis].
ACCESSION   WP_175994742
VERSION     WP_175994742.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..206
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21482
     Region          3..194
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtyvaqlvav ggvmllacvs pgpdliavts halakrragl yatagistsh alwaalaifg
       61 lglilaklaw lyeviriaga vyllylggkt laglrkpmqq tevdaqsaks dgqayrrgll
      121 vgltnpkaaa ffgslfitvl pahaplwvhg atlaivtavs ltwfgamail fstervqvgy
      181 arirkpidav mgavllglga klaldr
//
LOCUS       WP_175994744             411 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia vietnamiensis].
ACCESSION   WP_175994744
VERSION     WP_175994744.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..411
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44082
     Region          11..393
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(25..26,29..30,33,65,115..116,118..120,123,143,
                     146..147,150,225,228..229,232..234,237,265,269,321..322,
                     326,330,346,349..350,353..354,357)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 midpnksrra sfavfallyl gycisyidrs aialslvaig kefhvgsaal gvvmstfyis
       61 yaamqipggw iadrwgskkv ivvsvafwsl ftlmtglaws lasliairfi fglgeggypg
      121 aavkgvtesv aradrpkmsa llmssnyvgs fiaplaiapl illlgwrhaf fvsgcaglvf
      181 alfylfavkd thqkrdsngr aaridgdatr allkmplmwk illtwfgmgi vnkgldawmp
      241 ayllterhld lkavgmltpl pfvaasista lggwiltrwf dgrekwlmaa ccaisgffly
      301 qmytaqtvtg viayqsivyf fksfvfagvf alpakflptn ligtgagmvn fggqvagfva
      361 paiigllvsa tgnydavfgf livatafalv tslsirlvpe atphvgatke a
//
LOCUS       WP_175994779             666 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Burkholderia vietnamiensis].
ACCESSION   WP_175994779
VERSION     WP_175994779.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..666
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71192
     Region          1..460
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          598..662
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(620,629..631,638)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            630
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mfdkilianr geiacrvaat ckrlgiasva vysdadanak hvaacdeavh iggsaaadsy
       61 lrieriidaa ratgaqaihp gygflsened faqachaagi afigppvdai aamgskaaak
      121 almhaaavpl vpgyhgddqt pahlhreadr igypvllkas aggggkgmrv versedfpaa
      181 lascqreaas sfgndrvlie kyltrprhve vqvfgdthgn tvylfdrdcs vqrrhqkvle
      241 eapapglhdd vrqamgeaav aaaravgyvg agtvefimtg dafyfmemnt rlqvehpvte
      301 mvtgldlvew qlrvaagepl plqqhelrvq ghaiearlya enpargflps tgtlrhlrlp
      361 dgvefaigap vrvdsgvreg daitpfydpm iaklivhgad raealgrmlr alracevvgl
      421 ytnaaflqri vacepftmpd ldtgliernh dalfaprkpp raalalacaa lfarerdaaa
      481 hasrspwcal pdwrlnagyr rtlewheper evdltvvydd dggrarlaig daaaqpfewt
      541 rgatpldfdv tlggvrssgr vyadgdtfhv ftqgaaetfe wrnllahagd aehgggrlta
      601 pmpgkviavl vepgqkveag tplivmeamk mehtigapgp gvvaevlygv gdqvadgaql
      661 lmmaeg
//
LOCUS       WP_175994782             731 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia vietnamiensis].
ACCESSION   WP_175994782
VERSION     WP_175994782.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..731
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78188
     Region          62..731
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 msfrrplrra ralrpwragl palitlcvag gahaqaqraa pasaasaada aspaappaae
       61 relpaisvsa savadptvgy qprtssiagg ddralkdipq siavvssavm edqhansldd
      121 vlgnvsgitq tntlggtrda fikrgfgsnn dgsvlvdgvr tpvlhsylat idrvevlkgp
      181 asllygmqdp ggvinlvtrk peaefggsis asrtshggss aqfdltgplg kpgqvaggtl
      241 afrltgeydt srywrsfgre rdaliapals whdantsidv ayqyvdyttp fdrgtvlvng
      301 rpddalryrr yeeawsqsgg iqetlrarie hrfsdawrvr atygwgrdry dqyltraaaf
      361 nsktgaltrs sdanlgrnda dqiatlgllg nltlagmhha lyiggeyerq rsfrgdtirg
      421 tatkgfdlyd pvygllapgg tvsakqsdsl skvhaysmiv qdtvklterl tasaglrwed
      481 wqqesgmgrp fvfadrshgn vwlpqfglay altpsltaya nvsrsfkpnv asnvaaplap
      541 efgrvleagl kfsmtpaisg tlaayqidkr nvavtvgdlt stigtarsrg ieldvagqlt
      601 rhlsligsya ytnandrdsd tplvnvarht gslfavydta ianlpgrwrf gggarlvgar
      661 pgdtansftl pgyvtvdafa ayetmvgkfp triqlnvknl ldktyypssn snlivavgep
      721 rlvtltttvs f
//
LOCUS       WP_175994785             731 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia vietnamiensis].
ACCESSION   WP_175994785
VERSION     WP_175994785.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..731
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=80765
     Region          58..692
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mnrfvpslrn lwlrcrdrar alcagawqrl rhptrrgvvl alaalpllgl lvllafvpft
       61 psigdirrar idrparvlsa dgqliaefrp vnrewvplrq isphmvdali atedhrfyah
      121 hgidlrrtia aglhtfsgsr qggstitqql arnlypdeig raptltrkvk elitafkiet
      181 vyskdeilet ylntvpflyn aygvemaart yfgksadqld ivesatlvgm lkgnsyynpv
      241 lnperavqrr nlvlarmaal hmlspqqlaq lqrrplrvdf epqtaqpgpa phfavqlrkw
      301 litwadrnny dlysdglvvr ttldaqlqqm atralaqqte rlqavadgaw rgasgcglrn
      361 dlfrgfvrqs adyraardag ladavalkql ganrafmral cerktrvqag fvaldprdga
      421 irawvgspdf dsepfdhvaq arrqpgstfk pfvygaafad gmrpddtfvd rpvaipigah
      481 aqwrptdaep ptdapmtlrd alalsrnrit aqvmqregaa rvaqlaramg vrdspldavp
      541 slalgtspvt lkemvsaygt ianrgvyvap qmitriedrd gkvlatfgsa pperalpvaa
      601 aqtlidvmrg vvdygtgadi rerygiridv agktgttqdn tdgwfilmhp qlvagawvgf
      661 ddgsvtlrsd ywgagahsal pivgtffdaa lraraidprv qfspdfrprs apapkrraph
      721 sglfdwlkff r
//
LOCUS       WP_175994939             241 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175994939
VERSION     WP_175994939.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..241
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26440
     Region          1..239
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 misiknvskw ygqfqvltdc ttevskgevv vvcgpsgsgk stliktvngl epfqqgeilv
       61 ngqsvgdkkt nlsklrskvg mvfqhfelfp hlsitenltl aqikvlgrsk deatdkglkl
      121 ldrvglkaha hkfpgqlsgg qqqrvaiara lsmdpiamlf deptsalnpe minevldvmv
      181 elaqegmtmm vvthemgfak kvahrvifmd kgaiveddrk ddffsnpksd rakdflakil
      241 h
//
LOCUS       WP_175994998             561 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia vietnamiensis].
ACCESSION   WP_175994998
VERSION     WP_175994998.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..561
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=61230
     Region          10..546
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mttqrtlege fdyvivgagt agcvlanrlt edpdirvlll eaggkddyhw ihipvgylyc
       61 ignprtdwly ktqpeaalng ralsyprgrv lggcssingm iymrgqredy dgwaqetgda
      121 gwswdsvlpi fkrsedhhag asdahgaggy wrvekqrlrw eilesfaqaa qqtgipatdd
      181 fnrgdntgvg yfevnqkrgv rwntskaflr pamarpnltv itgahaqrvv fdgrravgve
      241 yhgggvdyva harievllts gavnspqlle lsgigagarl qalgidvvhd lpavgenlqd
      301 hlqlrmafrv dgvrtlntrs anwwgklmig aeyallqrgp msmapsqlga faksdpddpa
      361 ltrpdleyhv qplslerfge plhrfnafta svcqlrpssr gsvhiasvdp gvapsiapny
      421 lstdhdrhva analrltrri asapalaryr pqeilpgtry qteaelveaa gaigttifhp
      481 vgtcrmgrad deravvdsrl rvrgiaglri vdasvmpfit sgntnsptlm iaerasdmir
      541 edrraacdat qvrteaammp a
//
LOCUS       WP_175995018             234 aa            linear   BCT 11-JAN-2025
DEFINITION  TerC family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175995018
VERSION     WP_175995018.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..234
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24572
     Region          12..191
                     /region_name="R_switched_YjbE"
                     /note="integral membrane protein, YjbE family; TIGR03717"
                     /db_xref="CDD:163429"
ORIGIN      
        1 mpefltslhw gavlqivvid illggdnavv ialacrnlpa nqrlrgvvwg tagaimlrva
       61 liafavtlld vpflkfgggl lllwigiklm apaadahdsv kpadrlwdav kmivladavm
      121 sldnviaiag aaeqadpqhr lalvifgliv svpiivwgst lvlrlldrfp iivafgagll
      181 gwiagglmvh dpvgdgwpvl dtpaaiygas iagalfvvaa gfllrrrrgi pqah
//
LOCUS       WP_175995075             207 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175995075
VERSION     WP_175995075.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..207
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23172
     Region          1..207
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mlqilgkips invrkvlwlc aeldlpfeqe dwgsgfrstn dpaylalnpn glvpvikddd
       61 fvlwesntii rylanrygdd alypadprar arvdqwidwq asdlnrswvg aflglvrksp
      121 qhqdpaaiaq siagwtnhmq vlnahldatd afvagehftl adipiglsvn rwfgtpferp
      181 dlpavqryve rlatregfkk yagsanp
//
LOCUS       WP_175995106             166 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein,
            partial [Burkholderia vietnamiensis].
ACCESSION   WP_175995106
VERSION     WP_175995106.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..>166
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
     Region          1..>166
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkilvavkrv vdanvkvgvk sdntgvdian vkmsmnpfde iaveeavrlk eagvatevva
       61 vsvgvtqaqe tlrtalaiga drailvestd gveplavani lkalvdkeqp qlvilgkqai
      121 dddsnqtgqm laalaglpqa tfaskvtvad gkatvarevd ggaetl
//
LOCUS       WP_175995124             579 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Burkholderia vietnamiensis].
ACCESSION   WP_175995124
VERSION     WP_175995124.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 579)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 579)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 579)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 579)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 579)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 579)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..579
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62883
     Region          3..338
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 melqavevlg fkrlekiell tpsmtvlvgg nnsgkssllq aihfgitvlq sarlsadggk
       61 pmntlgfdqf iykptgdlik lnhggpitsk agpeftftyt dagadghqqf klklrrgkna
      121 niaitfedes tfffraanrs qpfsvfvpgl agvplreelr tpsivangia qgdsnvylrn
      181 vlyricende kltrfhevia svfpgltist afdpeahlyi disvhhdgrt vplemvgtgv
      241 lqaiqlvayv taydpallll depdahlhps nqkllaltlq kiaeagrtkv ilathsrhmf
      301 dalardeatq ivwlkgggkq egaersnlsv lldlgaldsf ellhagqrri viltedtkva
      361 rlkvflsang lnedeyflqp lhgvnnlaaa vpvadyftrq gdnthvlvhr dgdcmtdvek
      421 twwleqeskk lpdratafit pltdiehtfl kaehiaavyg isqddaeail aaviaantpv
      481 faaefaqkrt slkdtalkkm ngvpsatdml vegvkfehvk gkrllshvlt aiqqaghnpm
      541 rltdtpsaal vhaplrdkia aikaevaaad avgpapvda
//
LOCUS       WP_175995264             276 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Burkholderia vietnamiensis].
ACCESSION   WP_175995264
VERSION     WP_175995264.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 276)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..276
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29782
     Region          30..276
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mlhavfsarf spgraarvla aallgvvlln garadtaplk vglstspqie alkiaakeak
       61 aqgldvrive ftdwntpnaa lankdidvny fqhipflena kkqggydfva iapgtimkig
      121 lyskkvkrfd elkdgarvai andpvnggrg llllqraglv tlkpgvdyra ttrdivsnpk
      181 hlkiipleas qlarslddvd laqgypsfik lagtadpnga llfdgtenks falqwvvrpd
      241 svndprirkf iaiyqhspav rralddafgs lyaiaw
//
LOCUS       WP_175995283             443 aa            linear   BCT 11-JAN-2025
DEFINITION  carotenoid oxygenase family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175995283
VERSION     WP_175995283.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Poliakov,E., Uppal,S., Rogozin,I.B., Gentleman,S. and Redmond,T.M.
  TITLE     Evolutionary aspects and enzymology of metazoan carotenoid cleavage
            oxygenases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1865 (11), 158665 (2020)
   PUBMED   32061750
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Sui,X., Kiser,P.D., Lintig,Jv. and Palczewski,K.
  TITLE     Structural basis of carotenoid cleavage: from bacteria to mammals
  JOURNAL   Arch Biochem Biophys 539 (2), 203-213 (2013)
   PUBMED   23827316
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Kloer,D.P. and Schulz,G.E.
  TITLE     Structural and biological aspects of carotenoid cleavage
  JOURNAL   Cell Mol Life Sci 63 (19-20), 2291-2303 (2006)
   PUBMED   16909205
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Wyss,A.
  TITLE     Carotene oxygenases: a new family of double bond cleavage enzymes
  JOURNAL   J Nutr 134 (1), 246S-250S (2004)
   PUBMED   14704328
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..443
                     /product="carotenoid oxygenase family protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006720 - isoprenoid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48882
     Region          8..438
                     /region_name="COG3670"
                     /note="Carotenoid cleavage dioxygenase or a related enzyme
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]"
                     /db_xref="CDD:442887"
ORIGIN      
        1 mptfdlnrga lapvadeadl vdlrvtgaip peldgtllrn gpnppagrfe gndvlswwpe
       61 aamlhaisfe rgratgyrnr wlrtqrwarv hapeqaphlp danpnvsvlr hagellalae
      121 ggaplaitaa ldtlgeparh aglggamtah pkldpvtgel ilfradwrep wlrygvaday
      181 gvqrvdmvvd vrapsmmhdl aitetrslll dlnvgydfam lkqghrmplr whderdarig
      241 vlprhggdvr wfgiepcfiq hvvnaydcdp scivldvvry pwflrldart grfadnpvge
      301 lwryvidtan glidegplad ggielpride srtgrsyryl yaaeqpdsae mrgvvrydhv
      361 rgtstryalp vgdqngepvf vprpgrsaed dgwllvvvhr aatdtsavvi ldasaidalp
      421 vatvhlprrv pagfhgawlp rer
//
LOCUS       WP_175995387             145 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175995387
VERSION     WP_175995387.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..145
                     /product="RidA family protein"
                     /calculated_mol_wt=16179
     Region          28..137
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 msqpthtrir mfntkdtypn qtldndlcqa vragntvyvr gqvgtdfegn liglgdpraq
       61 aeqamknvkq lleeagsdlt hivktttyli dpryrepvyq evgkwlkgvy pistglvvsa
      121 lgqpqwlmei dviavipdhw qpnra
//
LOCUS       WP_175995411             336 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia vietnamiensis].
ACCESSION   WP_175995411
VERSION     WP_175995411.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 336)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..336
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36145
     Region          16..334
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtprtndapy esdnllldvr dlrvtfgdaq rtvtavdgvn fsvrpgtifg lvgesgsgks
       61 vtcrslvqlf ggarplrteg slrfagrelv gatedtladv rgreiamifq dpmtalnptm
      121 rvgaqieegl rrhwkltarq araqaidllk svgvtaperr ihdyphalsg gmrqrvliai
      181 alacrpklli adepttaldv tiqdqilklv vqlrdetgma vllvthdlgv vaqtcdqvav
      241 myagriveha atvelferps hpytrallna lptharragr lepiagappd lsappsgcrf
      301 hprcthavpa caegqppfvg vaaghtsaci rieeiv
//
LOCUS       WP_175995419             928 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175995419
VERSION     WP_175995419.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 928)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 928)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..928
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..928
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=101205
     Region          25..840
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mdirssalgd lklrelyeai sngvlqqgrl lmldtplgkn alvplrargs arigrdysyt
       61 idvastrddt allslmhqpv tlqvqqvtap faipvyrpvh gfvhrvaylg gngglstyqi
      121 efssalvfle kthneegwle kdareiisdv ldrypqlrgq yrfsllsdpa krswcrqses
      181 dlhfvnrlae aegwyfywih envaegdapk talvivdhvs tlpdakavef irandsnesd
      241 gfahwtgvqt mqstryisra fdykrpasdf qaesglaats yvteerrqkv ersvpdvpmt
      301 vyestaygys ssdtgearar rlveawdara sryfgvggvr wldagsrfvl nghprheggd
      361 akkreflvie arwfiennvp igqqtaefpq slratlaeqq aihrerfktp ghaadgsagf
      421 fvieveaqpt tveyrspldh pkpimsieha lvvtpdgaea wtndrnqirv hfawdrknpp
      481 daftssplls slqsdtgngy gavhvprare wvivgywngd cdkpfvlgri nggatpspwh
      541 snallsgfks egfgktgayn sfvhddstnq ggtrlvsytg ksyaaltqgy likhegntrg
      601 kylgagfilh adefgavras kglsisahsk syddeqmgvd earsqlqqag mlveslssas
      661 ttaqaeslqt gqdalkalsk diqhpvsgdt sggvtagggt gsangfsqpn ilvstpkdia
      721 lvadnsthiv aekeinvvsn entyvatgks lvvaaaekvs ffaqklgaff vtakgpikls
      781 antddvnvna gkdvtvkakr ivldadeiii kaggsytrwv aagiedgtqg prtiksasls
      841 rqgpssiaqh mnslpqakfn dpyvlrdris gevlknhpye lvrsdgtrik gmtnelghva
      901 eqknedietl klhalrpelp assgngse
//
LOCUS       WP_175995420             209 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175995420
VERSION     WP_175995420.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..209
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=23235
     Region          14..>186
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(61,63,67..68,71..73,75..76,80,83,92,94,97..98,
                     101..103,105..106,110,113,121,123,127..128,131..133,
                     135..136,140,143,152)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          61..92
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          94..120
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          121..152
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mkpkiviksg vqqwnylhag mrnnnpdfaa dldrrlelat kkgnfdrvke liehgadlhi
       61 nddaplvial rnrhtqiady lidrganvga hdnfpvfyca megnlstlrk lvengadpha
      121 ngeqplrkaa skgflpivry lvekgayina enseaiklss eedhlpvvkl liehgacpnt
      181 ahlyggqkvr kyieafhaha vsnhqrlsh
//
LOCUS       WP_175995469              99 aa            linear   BCT 11-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Burkholderia
            stabilis].
ACCESSION   WP_175995469
VERSION     WP_175995469.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..99
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=11218
     Region          1..98
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 msvrlsdfai aeleaiadfi ardnpqravt fvreirdkcl glagmplafp lvprferhgv
       61 rhrvygnyqi fyrvvgdppa ridilyilhg ardyasilf
//
LOCUS       WP_175995484             196 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia stabilis].
ACCESSION   WP_175995484
VERSION     WP_175995484.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008163
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..196
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=21022
     Region          11..184
                     /region_name="COG3963"
                     /note="Phosphatidylethanolamine N-methyltransferase [Lipid
                     transport and metabolism]"
                     /db_xref="CDD:443163"
ORIGIN      
        1 miwpnawrvs alfvrewvgr paavgalcps srhlaremad avpdgdglvv elgggtgait
       61 aallergvap rrlvvversp afvqhlrrrf pdvsvvwgda rqlerllppg arvdaivscl
      121 plrtlprddv taivdqcrrv lpadgvliqf tydlrppgrh plgdpafvas gsrivwanip
      181 parivtvrga taeadg
//
LOCUS       WP_175995504             108 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Burkholderia stabilis].
ACCESSION   WP_175995504
VERSION     WP_175995504.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..108
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11302
     Region          21..101
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(33,36)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mdteqrytan aptraevdal agttviefga nwcgicasaq paiaasfsah pavrhlkied
       61 gpgrplgrsf gvklwptlvf lrdgvevarv vrpadakqie adgfaala
//
LOCUS       WP_175995507             480 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia stabilis].
ACCESSION   WP_175995507
VERSION     WP_175995507.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..480
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47652
     Region          31..435
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,157,
                     160..161,164,286,289..290,293..295,298,326,330,388..389,
                     393,397,413,416..417,420..421,424)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msptirnapt gtaiaadave parhrlvlpa lciavliaqi dtaivnlatq pigaafgarv
       61 galqwviday nlayavlllt gglvgdlygr rrafilgaav lsgasvvcal aptlgvliag
      121 ralagagaal lipaslaivr viwrdpaers ralgiwaacg giamivgptl ggvlihafgw
      181 qsifwvvipf gvaaivlaaa vvpesadphg rrfdpaaqml gafaiacvvf atidarhdap
      241 raallvatga aavalfvrie rrlgtaalvp ldlfanrpfr gmliangamt fggygmlfvl
      301 plawqshhvl datgaglall pmsvlfalvs fgsgavaarf ggraagaggv almgvglaai
      361 gigaagstda hapllgwaet glaltgtglg lavgalaata vgavdaarag taaslmnvmr
      421 migavfgvav lgalydacgg gaaglriamm vgstvqlaca alawrtsgsa kragsprpig
//
LOCUS       WP_175995513             340 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia stabilis].
ACCESSION   WP_175995513
VERSION     WP_175995513.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..340
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=35495
     Region          180..340
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mqrfsytcll vtvfampglv wgqcttrpsg gedttdpfvy empgfdpgsf npnvpngtvi
       61 dkrsvlvtnf vqgtytclpe igtvtfrgtt tpigvtpdgk grtyssgigg iglrfqltgp
      121 aphypgywpv yqvyrpgtit aplgtlpiti nvelvkvgki taggiitgev agwfsvsqfv
      181 sirlsggivv qprvptcrvm tpaitvplgs mpastftgvg svspskpfni vlqcsdgdpg
      241 tvtnvyttlt dhadpgnvsd tlsltsdata tgigiqvlng stvikygpds satgntnqwk
      301 agttengtft ipltaryiqt apkvtpgtan glatftmsyq
//
LOCUS       WP_175995551             457 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia stabilis].
ACCESSION   WP_175995551
VERSION     WP_175995551.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..457
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47792
     Region          213..412
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mrfdlrfsla reqgqparrg vrcvpirral lrgvvatvcv agaqgaaaqa vhdavpfapa
       61 taettdlvdv pffsvarttw gglrasaaap ldvthasham nvpartdrdd paahfgacva
      121 yrvlceaarg averayaarf dyglasalpa mgalpafeqg fvdlasaepf tlaepdrgtr
      181 agpiagtlra slaraelppg vaaqvmrlla aridtkqrga igdtfrvafe pddgatlpgg
      241 vrvtafdvrf rgqrvagvwf apdagaqgay ydlagvplag trfampvaat risshfgtrv
      301 hpvtgarhvh sgvdlaapag ravhasergv vsfigtepsg ygkyvvirha ggyasyyahl
      361 safeptlrtg arvvrgqrvg avgstgtatg phlhfevrrh arlvdpielv qaaqaarlkg
      421 erriafnrva raartqlaaa twtqpvamsa avaphag
//
LOCUS       WP_175995167             107 aa            linear   BCT 11-JAN-2025
DEFINITION  transcriptional coactivator p15/PC4 family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175995167
VERSION     WP_175995167.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Calvo,O. and Manley,J.L.
  TITLE     The transcriptional coactivator PC4/Sub1 has multiple functions in
            RNA polymerase II transcription
  JOURNAL   EMBO J 24 (5), 1009-1020 (2005)
   PUBMED   15692559
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Kaiser,K., Stelzer,G. and Meisterernst,M.
  TITLE     The coactivator p15 (PC4) initiates transcriptional activation
            during TFIIA-TFIID-promoter complex formation
  JOURNAL   EMBO J 14 (14), 3520-3527 (1995)
   PUBMED   7628453
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Kretzschmar,M., Kaiser,K., Lottspeich,F. and Meisterernst,M.
  TITLE     A novel mediator of class II gene transcription with homology to
            viral immediate-early transcriptional regulators
  JOURNAL   Cell 78 (3), 525-534 (1994)
   PUBMED   8062392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10491384
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..107
                     /product="transcriptional coactivator p15/PC4 family
                     protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0003713 - transcription coactivator
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0140297 - DNA-binding transcription
                     factor binding [Evidence IEA]"
                     /GO_process="GO:0060261 - positive regulation of
                     transcription initiation by RNA polymerase II [Evidence
                     IEA]"
                     /calculated_mol_wt=11672
     Region          44..86
                     /region_name="PC4"
                     /note="Transcriptional Coactivator p15 (PC4); pfam02229"
                     /db_xref="CDD:460501"
ORIGIN      
        1 mtfpttqnek grdsgksatq ttrrndtsav dhstcfldar rsdserlrvt vseyrgralv
       61 dlriwfstes gefkpgragv slrpeqvgev mqalrlaaqa adpkgvs
//
LOCUS       WP_175995561             452 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia stabilis].
ACCESSION   WP_175995561
VERSION     WP_175995561.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..452
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=48321
     Region          16..434
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mdnitpnlat draprmpriv ivgggagglq latrlgdtvg rrgqaevvlv drypthfwkp
       61 llheaasghr dpashtieya aqakrhgfrf vqgalqqvdr aartatiaav qdadgteilp
      121 qrelgyddlv lavgsvtnff nvpgaarhal plenldqaed frrkflaact kanhlaeqhp
      181 arraapicin vigagatgve laaalrhaiq qlttyrfkal vsardvhirl ieggprilpa
      241 ldqrlsgkmh aqlralnvdv ltdtrvaevg adavttatge rlasditiwa agvagpailr
      301 eigdialnrs nqvivtdtlq tpddphvyaf gdcaacpsag asgflppraq vahqqavylv
      361 nafahrvagk pvagftfrda gtvvslgqag avyqadvgar srslivdgla aiglykflyr
      421 khlfsvvglk ralfqslshw lqsrnqpsik lh
//
LOCUS       WP_175995584             363 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF917 domain-containing protein [Burkholderia stabilis].
ACCESSION   WP_175995584
VERSION     WP_175995584.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..363
                     /product="DUF917 domain-containing protein"
                     /calculated_mol_wt=37308
     Region          1..360
                     /region_name="COG3535"
                     /note="Uncharacterized conserved protein, DUF917 family
                     [Function unknown]"
                     /db_xref="CDD:442756"
ORIGIN      
        1 mgrilsskdv eaavkggsvf acggggwadh grelgtlavt igrpelvtid elpddawiat
       61 aaaigapggl tdwqmlgady vkaaqlvqea lgaplaglii gqngmsstln awlpsallgt
      121 kvvdavgdir ahptgdmgsl glasstaqmi qaaaggnrar haymevvvrg atakvspvlr
      181 kaadmaggfi ascrnpiras yvrqhaalgg isralalgea iidaerrggs avidaicaat
      241 hgeiiasgkv erntleytre afdvglvylg sgarravihv mnehmavdda hgeriatypd
      301 vittldaegr pvsagqlkeg meihvlrvak ahiplsssvf dpavyppvea algisiadya
      361 lar
//
LOCUS       WP_175995617             205 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia stabilis].
ACCESSION   WP_175995617
VERSION     WP_175995617.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..205
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22227
     Region          4..200
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mefltlsalp agmlfalvts itpgpnntml lasgvnfgfr rtmphlfgis igvailmlcv
       61 gfglgeafkr lpllytilea asvayllyla wrigtsgevk ahgakprpmt fieaaafqwv
      121 npkawmmvlt aattvrlsad ygmnaawmav vfiligfpci clwaafglgl rrflsnsral
      181 rifnvtmavl lilslyplia hllpq
//
LOCUS       WP_175995628             521 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia stabilis].
ACCESSION   WP_175995628
VERSION     WP_175995628.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..521
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=55451
     Region          1..521
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 metydhivvg ggsagctvah rlvkagrrvl lledgpkdds lfiripatfi rvlgtqrtvt
       61 fesepqpgaa grktyvpqgr tlgggssvna mlyvrgtrdd yddwaalgct gwgwddvlpv
      121 fkraeshlrl sepfhgtdgp lkvgdtrfrh plslafvkaa qeagiayndd fngaaqhgvg
      181 fyhttifdgq rgstaatyla daighpnlrv ltgcrvtrvr fdgrratgve wrtesgatgs
      241 aaaradvvla agalstpkll mlsgigpgah lrahgidvlh dsrdvganyq dhlevsiygr
      301 shapvsllge drglkalrhg lqwmlcrtgl ltsnvvesga fvdttgsgrp diqfhvlptl
      361 vgdvdreplp ghglsinpcl lrprsrgsvq lrgndpaapi lfdsgalsdp advaglvrgv
      421 alareiirap slarivreae tlndaalady vrhraktvyh pagtcrmgnd ahavvtprla
      481 vqgvdglric dasvmprivs gntnaptimi aercaafmla d
//
LOCUS       WP_175995683             298 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia
            stabilis].
ACCESSION   WP_175995683
VERSION     WP_175995683.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..298
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=31045
     Region          5..292
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 msillkgiia ypvtpfsadg gvdlkaldal ierliadgvh aiaplgstge saylsdaewe
       61 avatasirav rrrvptvvgi sdlttagavr rarfaeqaga davmvlpvsy wklgsdeiva
      121 hyraigdaig ipvmlynnpa tsgvdmspdl iaticrtvdn vtmvkestgd igrmhrlaql
      181 sdgtipfyng snpmalaala agaagwctaa pnlnaalpla lydamqsgdv araravfhaq
      241 lpllqfivng glpvtvkagl rlrgfdagep rkpllplgda rtrelerlla alpgdvta
//
LOCUS       WP_175995747             557 aa            linear   BCT 11-JAN-2025
DEFINITION  alkaline phosphatase family protein [Burkholderia stabilis].
ACCESSION   WP_175995747
VERSION     WP_175995747.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 557)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 557)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..557
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=58263
     Region          42..535
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 misffgkqrk mavmvagala lasagahaaq dgngqgedgg hasrvvkhvl lisvdglheq
       61 dlarcigant cpniavlaks gvtyanaytp glsdsfpgla alvtggspkt aglfydvsyd
      121 rnlyapgdtt csgkqgwnvv fdettgidaf nggklahldg ggafnpqaip harvngqcvp
      181 vyphnyvktn tvfeavkagv pnahtawadk hawgydwlng psgtgvddlm rteinsidpa
      241 tntdytdiys htarfdnlhv qalinqiegr dstgtksapv ptlfgadfqt lsvaqkspva
      301 kgggyldadf tpngqvanai tyvdnsighi vaalkqanly tstavivtsk hgqsptdhtk
      361 lvkngdtltk lleannyldp ngnfgqnntt tgnlndgsgl vgtgfvqtdd vgliwlrdrs
      421 qrtavvqtlk anlgcnapgi cadgsqayvl ygaaladrfg dpangrtpdi ivqpnpgviy
      481 tsstkkdeeh ggnapddshl gllvsypgih rartvtdlvg tkqvaptile llgadprllh
      541 avvaentrvl pglgigr
//
LOCUS       WP_175995749             469 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Burkholderia stabilis].
ACCESSION   WP_175995749
VERSION     WP_175995749.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..469
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51996
     Region          5..445
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mdtalsaldl arlqfaftvs fhivfpalsi glasfiavle yrwlktgkqy yktlclfwsk
       61 ifavafgmgv vsgvvmsyqf gtnwsgfssf agavtgpllm yevmtaffle agflgimlfg
      121 wnrvsprahf gatlmvaigt listfwilas nswmqtpqgf eivdgrvvpt dwfaiifnps
      181 fpyrlfhmai aafivaalvv aatgawhllk grrdkgvkkm fsmalwlllv laplqavigd
      241 qhgintlkhq pakiaaiegl wetekggtpl nlfgipdmka ettryavkvp hlgslilths
      301 wdgeirglke fppedrpnst vvfwsfrimv glgfamigla alawflrrrg rlyeskwfqr
      361 falvmgptgf vsllagwvtt eagrqpwvvy gvmrtaqavs plsvqqvsls mmtfvivyfl
      421 vfgtgvyyml klmkagpalp dvkhdmpdtr pdhtarrpls avdepletv
//
LOCUS       WP_175995753             219 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia stabilis].
ACCESSION   WP_175995753
VERSION     WP_175995753.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..219
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24763
     Region          1..207
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 miptlyahpf ssycqkvlta lyengtpfay rvlahddpkp mqeltalwpl krfpvlvdag
       61 rtvveasiii eylglnhpgp vrllpddpha alevrmmdrf fdnyvstpqq kvvydalrpe
      121 aerdargvad aramldtsya wldkkmadre waagdrfsla dcgaapflfy adwthridpa
      181 fanviayrqr llarpsfara vdearpyraf fplgapdrd
//
LOCUS       WP_175995772             705 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia stabilis].
ACCESSION   WP_175995772
VERSION     WP_175995772.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 705)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 705)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..705
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=76311
     Region          20..638
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mtdhtasppp ppaprrrrrm wrtlagallg ltfacagiga wtihriwtql psvehlavyr
       61 palplrifsr dgdllaeygv errefvpler iptlmrqall aaedakfyqh gpidfgglar
      121 atfanvvtgq pgqggstitm qvarnfyltr dkvlsrklae ilmaaklere yskdkllely
      181 mneiylgera ygfaaaanvy fgkpldalna geaavlaglp kapsafnpvv nparatarrn
      241 yvlgrmhalg qlddatyhaa vdapialatt pppgivaapy vaerarrmmv erfhddaytl
      301 gldvtttism rdqraaeaal qrtlrrqppa kretrngleg alvsldaatg dmlalvggad
      361 fnrnvfdhal qayrqpgssf kpfvysaale kgyfpgvlvd dtqrtlthae tgarpwrprn
      421 fgnryegfip vrrglvrskn lvavslmqat daryvqqhav hfgfdaqrnp aslplalgag
      481 avtplelasa ysvfanggtr meprliqsvk qrhggamyea ttpegarvvs arnafmmdsm
      541 lrdvvkagta rgalalrrdd aagktgtsng skdvwfagys sgvvavawlg ydtprpmgra
      601 tgatlalpvw ldymktavdg rtpvdatppq dvalvdgdfv yaeytrgtct advpsyirsr
      661 facggtaapd aadtpagsgk pdepmpaavd aaerervldl frtdd
//
LOCUS       WP_175995780             268 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Burkholderia stabilis].
ACCESSION   WP_175995780
VERSION     WP_175995780.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 268)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..268
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28529
     Region          25..268
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mrrslltglg alaaalafaa pgahadpqtl kigtmsgpda qiwtevtkva areglaikvi
       61 efndyvqpna aldsgdldan gfqhqpflds qikqrgykiv nvgltytapm gfyskkiksl
      121 kdlpvgakvg iqndpsngnr allllqkygv iklkpgvgtn gvnatpldva enpkkikive
      181 ldsaqlpral pdvdaasint dyavkagltp vkdaiaiedl rgpyanliav raqdkdkpwv
      241 kklvaayese dvrkfidqkf ggaivpaf
//
LOCUS       WP_175995804             198 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175995804
VERSION     WP_175995804.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21536
     Region          6..158
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrysvehkhe trarildaas rlfrqegygg sgigpltkaa gvtngafygh fkskgeafrs
       61 vvldgldqlr qgvarfkaeh garwrrpfvs fylgprrtce lgescalpsl spevmradde
      121 trdayeqalr qivdevasgl gdtsdddrai aflallsggv tlaravrdpv laeriadavg
      181 ryavviaert dvqpeqqa
//
LOCUS       WP_175995815             391 aa            linear   BCT 11-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Burkholderia
            stabilis].
ACCESSION   WP_175995815
VERSION     WP_175995815.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..391
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40637
     Region          38..389
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mtqlfdtlgf ieasavhaga gsaahdaavv pvgaaavsle hvgkvfatpr gqsaalrdvt
       61 ldvrrgevfg iigrsgagks tllrlvngle rpssgrvcvq gvdvgalded glvalrrrtg
      121 mvfqhfnlls aktvfenval plkiagvpka ertrkaeall elvglaakrd aypaslsggq
      181 kqrvgiaral vhdpevllcd eatsaldpet tqsilallad inrrlgltiv lithemevir
      241 avcdtvavie qgevvetgpv wrvfgdpkhg atrallstlv hdlpaelaar vqplpeqdal
      301 pdgaqvvldv rytgesggep dvgalaaalg gsvrflhggi eriqghaqgr lviaaapgag
      361 eaghaharga vaallerarr hanhaevlgy v
//
LOCUS       WP_175995892             469 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia stabilis].
ACCESSION   WP_175995892
VERSION     WP_175995892.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..469
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50273
     Region          14..467
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mnhpappaat rrplppamld alraafgerv stadavrahh grdespfdpq lpdavvfahs
       61 addvrevvsl cslysvplip ygagsslegh llavrggisl dlsemnrvls inaedltvtv
      121 epgitrkaln ealrdtglff pidpgadasi ggmtatrasg tnavrygtmr envlgltavl
      181 adgrvvktgt rarkssagyd ltrlfvgseg tlgviteitl rlhplpeavs aaictfptms
      241 davrtvieti qigvpiarve fvdslavrsi nrhsnltlte aptlffefhg teagvkeqae
      301 lvqalagqnn gqgfewatrp edrtrlwsar hnayfamlql kpgcravttd vcvpisqlaa
      361 cveetevdlr asslpcpivg hvgdgnfhva ilidpdkpee iaeaehindr iveralrlgg
      421 tctgehgvgl hkmrflpkeh gdnaidtmra iklaldprnl mnpgkiftc
//
LOCUS       WP_175995934             327 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175995934
VERSION     WP_175995934.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..327
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35443
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,161,163,226,243,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,190,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mnqiqtmrvf vcvaeqqsfr raahhlgvsn alvtrsiaml eghlntrlih rttrnlslte
       61 agaryldgcr alleefdhle ssvahavrep ggtlrvvasg llsplaltpl vssfrhrfpe
      121 lrvqltvteg pldvldsgyd vgivtgnrld gnpslighal apnpfvacaa paylerrgep
      181 rspddlpghd wvtlaphqha sawqlvghdg vvhsvtvrpa ctvnqlalvq aaalagagia
      241 vlpepcvada lnhgtlvrll ptyriddpdt qlslvypnrq yvpartrsfv ehaldhfgaq
      301 aareradysf lrqprgpera divtglq
//
LOCUS       WP_175995996             116 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF190 domain-containing protein [Burkholderia stabilis].
ACCESSION   WP_175995996
VERSION     WP_175995996.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..116
                     /product="DUF190 domain-containing protein"
                     /calculated_mol_wt=13205
     Region          4..103
                     /region_name="COG1993"
                     /note="PII-like signaling protein [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:441596"
ORIGIN      
        1 mdkvflrfyv heqhrlrwkp lwewlldean rmgvaggsaf ramagfgqhr vlhedrffel
       61 qgslaievef ivtedeaqrl lerlshekvr vcyamiparf gvidtlgapp aqgpaa
//
LOCUS       WP_175996073             555 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia stabilis].
ACCESSION   WP_175996073
VERSION     WP_175996073.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Kane,E.I. and Spratt,D.E.
  TITLE     Structural Insights into Ankyrin Repeat-Containing Proteins and
            Their Influence in Ubiquitylation
  JOURNAL   Int J Mol Sci 22 (2), 609 (2021)
   PUBMED   33435370
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Mosavi,L.K., Cammett,T.J., Desrosiers,D.C. and Peng,Z.Y.
  TITLE     The ankyrin repeat as molecular architecture for protein
            recognition
  JOURNAL   Protein Sci 13 (6), 1435-1448 (2004)
   PUBMED   15152081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19763717
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..555
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=58281
     Region          92..380
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          219..249
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          412..466
                     /region_name="Ank_4"
                     /note="Ankyrin repeats (many copies); pfam13637"
                     /db_xref="CDD:372654"
ORIGIN      
        1 mkklppranp dqlkkqakel lrlyrqgdah avarfvqflp aaanrthdqa lalglrlhda
       61 qsciareygf aswadlgafv etqalaqqqr pllirrwlgl ayggdvtggf daprprvaaq
      121 llrdhpdlva ddatiacaag dldalkaaia adpgwiarag galklpplva vthsrlgqlp
      181 efavrlraca rhlldagadp nqrignrfpp aslaapdesg plsalygaag vnrdpvltam
      241 lleagadpnd geslyhslen pvctrvlleh garvggtnal rraldmrdaa alelllahgg
      301 dpnepagegp tkmwgapllr aiavrcsarh iaallaagad prartaagvs ayrlamqtgl
      361 tdvaallraa gaeetlgaed afvaacarad addarriqar hpelpgalpe drlrllpdaa
      421 awgsadavkv mvelgwpiaa rggdwdasal nqavfrgdak llafllahga swremhgygs
      481 dalgtlswas vnepadlgep dweacarvll ahgvpqaard psnpegvlvd gramrfseav
      541 tdvllgiesg qpgsq
//
LOCUS       WP_175996082             396 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia stabilis].
ACCESSION   WP_175996082
VERSION     WP_175996082.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..396
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41335
     Region          13..376
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 msapeksenr gdpvvivgtg lagytvarew rkldgdtplv misrddgcfy skpalsnala
       61 qrktpeqlam sdartmegql rasiwtrcsv qairadahei vlddarvlry ralvlatgad
      121 arrvpcegdg aadvlsvndl adyarlrnal hdcrsvailg agligcefan dlvaagltvt
      181 vidpadapls rllppeagqv fahalgdagv hlrlgagvrs iarlargyrl altdgghlda
      241 dlvisaiglv prtalareaa levadgivtd awcrtsapdi falgdcaaid grvrpyvlpi
      301 mhaaralaqc lrgtparvaf pvmpvvvktp aiptvvvtad ggghwttetg vgdvpratra
      361 lcsdpesgrl tgfalldaat aekaallkam tdtast
//
LOCUS       WP_175996194             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175996194
VERSION     WP_175996194.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32794
     Region          11..69
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          100..295
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(115..116,118..119,122,126,128..134,226..231,
                     237..238,240..241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrnrineeit frklevllaf meagslakaa ealgvstvsv hralhtleeg mhcalfrheg
       61 rnliptdaal vlaevagevl ktmadgirst reaagygagq lkigslyslt irtvpevvia
      121 lkerrpelqa elvlgsnadl ldklrqgaid atlmalpdpd aeiesialfe demffaapid
      181 spyaqrnaid ldacrdvpfv slgegfathh gfteafraag vtpnvvmrvg difslinlvs
      241 ggvgcsllpg rvrdlfahki alvplagpti rqtiglsflh rrerdpnlla latvcrltvk
      301 gpnar
//
LOCUS       WP_175996208             381 aa            linear   BCT 11-JAN-2025
DEFINITION  metallophosphoesterase [Burkholderia stabilis].
ACCESSION   WP_175996208
VERSION     WP_175996208.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..381
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=40752
     Region          113..381
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mrsffvrfia igvlfhlyvg iriipdafas pvartvaalv lasfvvlipv gmfsrrfdeg
       61 waatlvgwvg slvmgffssl laltllrefv llgvvvwrqf vhagawsgas gdtavgvlaa
      121 avlvtaigfv garrtaavkr vsipvaglpa gldgltivql sdihvgptik rpyierivra
      181 vnaldadvvv vtgdvvdgsv krlrehtapl grmksrhgsf lvtgnheyya gahawidefr
      241 rigltvllne hvlierggar avlagvtdft aggfdpahrs dpeqalagap hdvgtkilla
      301 hqprsaeaan ragftvqlsg hthggqflpw ppfvrlqqpv igglsrfgdl wlytsrgtgy
      361 wgppnrfgvp seitlirltr g
//
LOCUS       WP_175996261             282 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175996261
VERSION     WP_175996261.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140973
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..282
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30670
     Region          19..239
                     /region_name="HTH_MerR-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     transcription regulators from the MerR superfamily;
                     cd04778"
                     /db_xref="CDD:133405"
     Site            order(21..23,37,53..55)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133405"
     Site            order(67,70,74..75,84,105,109,115,119,122..123)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133405"
ORIGIN      
        1 mskqtqpipd eaavdsqney tvdelarvsd ttvrnvrayq drgllappek rgrvgiyddt
       61 hvarlklinh llargytlsn iqdlikaide ghdlrsilgl enaiggrwsh elpktyslaa
      121 lvqmfgpqap tqlsrvtelg llerrglsfv akspalleaa aamtkegipp relldvisla
      181 rphfdaiarl lvdlvvkrld rydegtlppa tdvpalvdai wrlrplaavf vegetnrale
      241 taasaylggr vatildkkls deaarqsgtp dtpdtqddgd ka
//
LOCUS       WP_175996277             729 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia stabilis].
ACCESSION   WP_175996277
VERSION     WP_175996277.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..729
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78199
     Region          36..721
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mpsspfrits yisdtkagia iidaarhwag tsgvtwlyvf ktilaallal gvamklelpm
       61 prtamttvfv lmqpqsgmvl akslyricgt ivgllamlvl iglfgqapel flgatalwig
      121 vctagaarnr nfrtygfvla gytaaligip swqhpdaafl samtrvtevt igilssgavs
      181 alvfpqhvsk qisrvnrarf teftddvlsi lsgridrsfl ealsvrivde tvnaeaarsv
      241 avfegpdtrl rngrltrlna ermaastrlh alsqliarlr saradvvlte iealmagiaa
      301 pirlewqdat haddidalvq sladtlehcr talpdrarla rnrlgsrasa ldfdtavdll
      361 drfldsyiay aqtylslsai ahereqwatp yeprtnplia avagvramll tlvlstfwia
      421 tawpsgallv lnggaicalv assarpsrta fqmaigtafa sviglivmfv aypvidgfpl
      481 lcvvlappla lgcwmttrps lagygvgyci yfcfltgpdn vvaydptsfm ndaialvlsm
      541 lmasvafelf lpptmrglrk hlladlreqv vfactdsaat lrarfesrtr dlmyqvrsis
      601 rddpvanges vewflsvlei gsavvdlrga maieaarrgp daapawlddc asacraigll
      661 fetptptara aatravqaai atlqrtmqtt daagpavphl qtvlgslhfm hsalaapdsp
      721 lpapapdar
//
LOCUS       WP_175996304             304 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia stabilis].
ACCESSION   WP_175996304
VERSION     WP_175996304.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..304
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32624
     Region          14..296
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mpmnsatapa plceidglri gfrghdgvvt davrdlsltl spgerlgivg esgsgksltg
       61 rallgllpda arwsartmrf aghdllamsp rerrrlcgsq mgmilqdpky slnpvmtvak
      121 qmgeafrlhe pglrgralre rivdalaavq irdparvada yphelsggmg qrvmiammvs
      181 tgprlliade ptsaldvavs mqvlavldam iarhgtglmf ishdlplvms fcdrvavmya
      241 grvvetcaar dlrdashpyt rgllaanppl anppdelpvl rrdpawldpa phaippadrq
      301 eaar
//
LOCUS       WP_175996311             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175996311
VERSION     WP_175996311.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33699
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,223,240,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdfesirifl rvvergnfta aatqldmpls rvsrkvkqle ddlgvqllyr ttrrvsvtea
       61 grdyyerclr aedilldadr laralrtepe gtlrvlvpys iglfelepal aefrrryplv
      121 qlvliydnsa ldlvehgfdv alrtgvltds gyvarslgws haklaasphy ldragrpqtp
      181 qdlahhdilf vgrdtpgltl rltnaagdva dvpvrpvlis nesvtvlrqa ssgggialis
      241 thftarrlek neleivlpdw hrtddvelhv lyprratlds kvrafveflt evftawrstp
//
LOCUS       WP_175996312             673 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia stabilis].
ACCESSION   WP_175996312
VERSION     WP_175996312.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..673
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=71181
     Region          30..658
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mkfafpslpp faavraalrd arptlppgal afalrntaas llalyiafrm nlddpkwaas
       61 tvwivaqgsr gmglsksqyr ilgtaigaav alaltgafaq tpelflaala vwiglcagva
      121 tfqrnfraya avlagytaai iamdavsapl hafdiavarf lyvvvgilcc alfdtvfapg
      181 aplndvrtrl kryldrsvav gagalrrepn gaavhrlfad aleldtaaey aatgappvrn
      241 aighlraaal gvlaaqaagq airehavrag dapdplvdev arvldgiaas gdaghelaal
      301 rervdvalha etvgpdtsrl ltldrlaall agfdrayasq aqldrpeppp srvryafhhd
      361 pviawhnair aflavmtasa iwiftawpsg agfvtitavv galfstrpns vraavgflkg
      421 tacaavagvv cnfillpavs gfemlayilg vfliaagiai rhprtaamgs aftiffwnft
      481 spdntarigd aaflnsalat mlgiafgalv falvfpddpg tsrqrlhrav rrdlagiard
      541 prawsastwl srtadrlare lgfagslpqt lierdmrdll aiwglgdsll slaelaahep
      601 aarraatvvr grcaraefae ldrtcdmaar vllrrvaard gddarallrg vvllrriada
      661 aaehggflrg rrd
//
LOCUS       WP_175996384             310 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia
            stabilis].
ACCESSION   WP_175996384
VERSION     WP_175996384.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..310
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33230
     Region          9..302
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mqsnhssary rgvfpvvpti faddgrldld gqrrcvdfmi dagsnglcvl anfseqfsla
       61 dderdavmhc vlehvagrvp vivttshfgt tvcaqrsrra qdagaamvmv mppyhgatfr
      121 ageaaiveff rsvsdaidip imiqdapasg thlraallar maieipnvsy fkievpqaaa
      181 klrelialgg daivgpwdge eaitlladle agatgamtgg aypdgirriv dawaagrade
      241 aereygrwlp linhenrqgg iatakvlmka ggviasdavr hplpsmhpdt rasllriara
      301 ldplvlrwgr
//
LOCUS       WP_175996389             282 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia stabilis].
ACCESSION   WP_175996389
VERSION     WP_175996389.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..282
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28505
     Region          20..261
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mihfnltegv lvsslqgltp fdlagiaval llggmvkgvt gigvpliamp ilsqflpirh
       61 avlllsmpii lgnipqaleg gqvlatarki aapiagtvig nivgvaills lnpghaqaas
      121 gallivaatl mlaapklnlp dawqkpvgfv lgfgaalmes iasvpgplla tylissgatg
      181 rvftkqiaii lvvsivtlit tfsgaahasa adlaisaaas lpaiagmwlv rplrdkmspk
      241 vfrmvvllfv liaasqmiwk sgalrhggsp aaqtngahaa gk
//
LOCUS       WP_175996431             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia stabilis].
ACCESSION   WP_175996431
VERSION     WP_175996431.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21467
     Region          2..205
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mlfiksvvmg lsialpvgpi gmlciqrsls rgfqagfatg igaacadaiy gllgalgiag
       61 ivtafpmltv glkigggafl vwlawtiarq apaasamqrd lprttvlrdf lttfgltlsn
      121 pmtilsfvgi faalgplsga regamwpsvs lmvagvfigs atwwlclssa saalrtkmsf
      181 afmhglsrvs avviaafgai qlaagvrgvi
//
LOCUS       WP_175996640             297 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia stabilis].
ACCESSION   WP_175996640
VERSION     WP_175996640.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 297)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..297
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31839
     Region          23..263
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 mnasnesaah aapvgtppaa aeadlvievr nltkrygrni ihqkldfdvr rgeivaivgg
       61 sgsgkttlvr qilglerpts gtikvfgedt atiddasarm mrtrsgmlfq qgalfssmtv
      121 fdnvaqplre lgrvppdllh divmlklemv glpckhaskm paalsggmvk rvgiaraial
      181 epellfldep tagldpqasd efveliatlh rtlgltvvmv thdldtmval strvavladr
      241 kvlvaapvee aanvdhpfih eyflglrgrr alqalpperr aklpkaalep alssvel
//
LOCUS       WP_175996657             503 aa            linear   BCT 11-JAN-2025
DEFINITION  ammonium transporter [Burkholderia stabilis].
ACCESSION   WP_175996657
VERSION     WP_175996657.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..503
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50769
     Region          96..500
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mrkllmsllm agsliaagvg paladdaasa aaasapaata sdassaaapa asasattdas
       61 aaaaaapasg aadasaaaaa sapaapaapt apfsvdsski sagdtawmlt stalvlfmti
      121 pglalfyagm vrkknvlatv mqsfaitavi tvlwtvvgys laftpgngfi gglsraflhg
      181 mnyihgdkat tltvshlapt ipesvyfvyq mtfaiitpal icgafadrmk fsamlvfmtl
      241 wslivyvpia hmvweptgwl ssdgvldfag gtvvhinagi aglvsclvlg krvgygresm
      301 aphnlvltmi ggsmlwvgwf gfnagsavaa dgragfamlt tqvatacaal gwmfaewiak
      361 gkpsvlgivs gavaglvait paagfvgvtg alvigiaagv vcfwsatwlk sklgyddsld
      421 afgvhgvggi lgalltgvfa vkdiggadgs lllqakgvli tlvysgvlsf vllklidltm
      481 glrvseeeer egldvilhge hve
//
LOCUS       WP_175996789             459 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia stabilis].
ACCESSION   WP_175996789
VERSION     WP_175996789.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..459
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49049
     Region          7..457
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mtqqqrsfds ivareqglrh altsgqmami aiggaigtgl flgsgfaigl agpsvlvsya
       61 igalialllm galaemtvah ptagsfgaya ehyvgplagf lvryaywfav vfaigteisa
      121 iavfmkywfp avpgwywvig fsalliavnl asvtlygsve yafsllkiaa iivfivlgay
      181 lvwsapaasg igfanytahg gfmpkgpwgt wvavivaifs ymsieavaia ageardpqha
      241 vtrafrstvf rlvlfylltl slmlaivpwt qagtdespfv kvmaathvpy aagvinfvll
      301 iaalsamnsq lyvttrmmfs lsrarlapav fgrlgtngvp raalwistsg vavaavlval
      361 apdtaftvmm aiamfgalft wlmifvthlr frsrysgpal afrmwghpfg sllgaglvaa
      421 ilfttaftre frmtmvvgvv fvvlltlaya lhyrhehar
//
LOCUS       WP_175996796             238 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Burkholderia stabilis].
ACCESSION   WP_175996796
VERSION     WP_175996796.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..238
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=25695
     Region          6..224
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mdlesilytq gfgsrrqcrg lieagrvava gagatdpdat fdtdglvfsv ddtawpfhar
       61 aylalnkpag yecsrdpqhh asvfsllpap lvargvqcvg rldqdttgll llsddgqfvh
      121 aytspkrkvp ktyvatvrhp lddtqlealr tgvqlhgepk piaavaaaar dthalaltvl
      181 egkyhqvkrm vaavsnrvel lhresiggfa lpddlepgaw rwlddadlsa lrhsvktl
//
LOCUS       WP_175996834             204 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175996834
VERSION     WP_175996834.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..204
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22187
     Region          6..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maergrprsf dkeaaldram evfwrlgyeg asmadltvam giaspslyaa fgsketlfrq
       61 alehysateg reiwngveha gsahdavrny lmdtarvftr rskpagcliv lsalhpaers
      121 dtvrqtliam rertvdalre rlregvatge iaahanldai aryyvtvqqg msiqardgan
      181 rrdleaiaqa alaawpalvg arga
//
LOCUS       WP_175996845             140 aa            linear   BCT 11-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Burkholderia stabilis].
ACCESSION   WP_175996845
VERSION     WP_175996845.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..140
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=14457
     Region          35..135
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mtfftdytnl aliaillvsg gllawpalrr grgglsaaea tqlinrrnav vidvraasdf
       61 aaghlpsarq vaageigaki aqvaknkstp vllvcqngqq sqkaarevea agyaevhvle
      121 ggvvawqqag mpvvkqgvak
//
LOCUS       WP_175996852             308 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175996852
VERSION     WP_175996852.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34051
     Region          16..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          101..300
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(116..117,119..120,123,127,129..135,229..234,
                     240..241,243..244)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mmhpdlrrld lnlllvfdal yrhrsvaaaa helamspsal shalarlrda igdalfvrlg
       61 nemqptvrad diaawagdal damskglara rrfdpaqsdr tfvfaatdyt afavlpafla
      121 riqhvapqlr irvvhsdrki svdalaagri dfalgyhees aadapgiedf dwfsddyvvi
      181 asaahpdirr rltldqylaa rhvvvtpwne srgvvdyvld rlglarqvav qlpsvlaapf
      241 viaesallmt vpnraaqalr haapirifpa pfeiprytvk vyshakhart dahrwiraql
      301 ldarpdpd
//
LOCUS       WP_175996877             859 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia stabilis].
ACCESSION   WP_175996877
VERSION     WP_175996877.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 859)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..859
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=93142
     Region          74..712
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mhpfqpsstr vnrrnvssvr dfcarwiara qpvaaaaavr vkplaaaawh hlrhptrrgv
       61 llaaaavpal falyvvvlip ftpgigdirk arvdqpaqvl sadgkllaef kpsnrewvpl
      121 kqisphmvda liatedhrfy ehhgldwkrt asaalhtfsg srqggstitq qlarnlypde
      181 igraptltrk vkeaitalki eavyskdqil etylntvpfl ynaygvemaa rtyfdksade
      241 ldvldsatlv gmlkgnsyyn pvlnperalq rrntvlgqmv kygklspaqf aqlqrrplri
      301 dferqkeppg paphfaqqlr kwliawadrn dyniysdgli vrttidsrlq qmatqaltqq
      361 gnqlqgiang awsgrdgcgt dnevfrtfmr espeyktaqd agkddaaamk llaadrgfmr
      421 alcktktdvq agflaidprd gqirawvgsr dftnepfdhv aqarrqpgst fkpfvygvaf
      481 asgmkpddtf idqpveiplk ggeiwrpndd vpptgkpmtl rdavalsrnr itaqvmekvg
      541 paavarlard mgvrespler vpslalgtsp vtlkemvasy atiangglyv epqmvtrien
      601 rqgdvlaeya papperalda etdktllsvm rdvvtrgtgg sirtrfgirg dvagktgttq
      661 dnadgwfilm qpglvagawv gfddgrvtlr sdywgqgahs alpivgdffq raqrariidt
      721 kakfdtepsp gwfaslrerv tdlydtwfpp etkkapasar tqrverppea degasaaesa
      781 asapeaasgg iveewipase vaasaaalss gasqpqpaqp paagaspasg gnagvgaeps
      841 tapapppapa spdttdasq
//
LOCUS       WP_175996923             356 aa            linear   BCT 11-JAN-2025
DEFINITION  AI-2E family transporter [Burkholderia stabilis].
ACCESSION   WP_175996923
VERSION     WP_175996923.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..356
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37741
     Region          35..355
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mgahvpsshd saarprtqqi aravlyaall vlalwvirdf lpaivwacvi aiamwpllkr
       61 feshrlfrgr ptvialvita aisllvvlpv avaatqaigq ahdlrvwlht iqdngiplpd
      121 vvgrlpygsa qitewwqanl ghplhaasam hsvngekfia fgrqfgtkla hallefgfml
      181 vtlfvilrag hklsgalleg arrafgrnga eliermvaav ygtvtglvvv glgegallgi
      241 ayalagvpha allglvtava amlpfcapiv fcgaalwlfv qgatmwavav avigfvvvfv
      301 aehfvrpvli ggstrlpfll vlfgilggae tfglvglfvg palmtvltml waewia
//
LOCUS       WP_175996886             473 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia stabilis].
ACCESSION   WP_175996886
VERSION     WP_175996886.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..473
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=51064
     Region          83..470
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mtarpafpsp dasgtpapra psrllrrtaf vlgaavlgyg afaiafpaqv paaigtvvad
       61 wtganphpvv lqrpaaqpls avaqlgralf ldpslsasgk qscaschspd haygppnald
      121 vqpgglamtq qgyrpppslm ylyrqpnfsi gpdagendaa psvaqqaasa agvvkaqkva
      181 gtsaapqlvp qggmfwdgra dtlqqqafgp llnpvemant siddvahkla qsahrtqfek
      241 lfgarvfdss qltvseamfa iaryqvedps fhpydskydr wlegrarlsq aelrglrlfn
      301 dpdkancagc hlskpgkdgl ppmftdyqye algaprnkql aqnhnaafyd lgvcgpfrdd
      361 lkdqtqycgm fltptlrnsa trhvffhngv fhtldqvmaf ynersispqk fysrgadgkv
      421 deyddippky ranvdvtdap fdrkpgdtpa mtaqdikdie aflgtlndep vrh
//
LOCUS       WP_175996937             344 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia stabilis].
ACCESSION   WP_175996937
VERSION     WP_175996937.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 344)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..344
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37108
     Region          42..328
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mtrttapaps dahddkrrkl lraagaaala apaitlgrka wsapplkklt fawnqnafcl
       61 tpivvaqerg ffeknglkvd linysgstdq llesiatgka daavgmihrw lkpleagfdv
      121 kiigsshggc vrlvgakaag vttlqalkgk tvgvsdlaap gkhffsilla kngidperdi
      181 twrqypadll gvavdkgeih aiadgdpnly llekrsngay telatnlsge yarkvccvig
      241 argdlvrndr paaaglarsi vqateythdn pneaakvfak yspkispedl rklyatltyt
      301 hhptnvdlqq eiafyaddfr risvlkkstd pqrfaqqvya nvlg
//
LOCUS       WP_175996942             288 aa            linear   BCT 11-JAN-2025
DEFINITION  MOSC domain-containing protein [Burkholderia stabilis].
ACCESSION   WP_175996942
VERSION     WP_175996942.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..288
                     /product="MOSC domain-containing protein"
                     /EC_number="1.7.-.-"
                     /GO_function="GO:0016661 - oxidoreductase activity, acting
                     on other nitrogenous compounds as donors [Evidence IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=31092
     Region          1..281
                     /region_name="YcbX"
                     /note="N-hydroxylaminopurine reductase subunit YcbX,
                     contains MOSC domain [Nucleotide transport and metabolism,
                     Defense mechanisms]; COG3217"
                     /db_xref="CDD:442450"
ORIGIN      
        1 mpaiaelfvy pikscagial sraqlletgl aydrhwlitd pdgqmitqrt hprlalirta
       61 ldtdalvlna pgmreirtpl dgdatpatpa maaavwrdtv daidtgaeta awlteflgtp
      121 aklarfgada rrgcnrkwtg eidthtqfad gypllvigqs slddlnarla akgapaipmn
      181 rfrpnivvsd ldayeedfve hldtdgatpv rlrlvklctr cpmptidqat gapdpawphe
      241 ptdtmqayra npnyedaltf ginaivvega gawleigqsl eaeigfgd
//
LOCUS       WP_175996958             592 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia stabilis].
ACCESSION   WP_175996958
VERSION     WP_175996958.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..592
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=64862
     Region          7..585
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 maaekkphvd avivgfgwtg ailakeltea glkvvalerg eyrdtypdga ypntidelty
       61 nirkklfldl skttvsirhg lqdtalpyrq laaflpgegv ggaglhwsgv hfritpeelr
      121 lrshyeeryg kkfipagmti qdtgvtydel ephfdfaekv fgtsgqaykv ggkvvgdgnv
      181 feanrsdnfp lpaqlntysa qrffdaaqsl glhpyrlpsa ntsgpytnpy gvqmgpcnfc
      241 gycsgyacym yskaspnlni lpalkqtpnf elrskchvlr vdlddtkkra tgvtyvdpag
      301 revhqpadlv ivaafqyhnv hllllsgigk pydpitgegv vgrnfayqnl stikaffdkd
      361 tftnpfigag gngvavddfn adnfdhgplg fvggsplwvn qagvkpisgi atppgtpqwg
      421 sawkkavkdn yahtismdah gtnmsyrdvy ldldptyrds ygqpllrmtf dwkdndikma
      481 qyvtgqmkki aeamgpkaig vstrefgkhf dsrayqtthl vggavmgtdp ktsvlnrylq
      541 cwdvhnvfvm gasalpqgig ynptgiiaal aywsaraire qylknpaplv tv
//
LOCUS       WP_175997004             673 aa            linear   BCT 11-JAN-2025
DEFINITION  BCCT family transporter [Burkholderia stabilis].
ACCESSION   WP_175997004
VERSION     WP_175997004.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..673
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73292
     Region          3..514
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mpesrpsprt tfkpqvvlpa lavigallvv callpseaga lfaagqqwvi arfdwfyvla
       61 vtaflvflvl iaasdfgnir lgpddaepef sfvswtamlf aagmgiglmy fgvgepmqhf
      121 lkpptvdpgt paaareamlm tffhwgfhaw aiyglmglvl ayfgfrynlp ltlrsglypv
      181 lreringwig htvdafalvg tvagiattlg ygvmqlsagl htvagwdtgs nvfriglvav
      241 vvilagvsaa tgldkgvrrl selnlllafl llafvvvagp tlflfralgd nigqylsslv
      301 alsfrtyaya ppreegwfgg wtilywawwv swspfvgmfi arisrgrtir qfvigvllvp
      361 tafnlvwmtv fgnsaiwldt hgaagalaqt atnvdallfr ffdflplsqs lsiaaivlia
      421 vffvtsadsg afvidqiatr gnehspvwqr lfwaallgvt aavllvaggl galqamtlia
      481 alpvaiimla lcyglwrgla adrahysqdv apattfwtgq hwrhrlthil rqtteaearq
      541 fvaetiepal rkvadelras gvdahvqrds ddavrltvpt aehrdfvygv rvtvksaaaf
      601 lvreaaepes arahvygivt ffedgrlgyd veylrgdevi advlrqyery vslaadtrth
      661 llsrapghat eae
//
LOCUS       WP_175997066             227 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia stabilis].
ACCESSION   WP_175997066
VERSION     WP_175997066.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..227
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23751
     Region          23..223
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mtdvlplttd pdsglqyrlr ptagrpaarl lllhgvggne tnllnvagai dprieiaflr
       61 apltfgpgqh awfpvrfgpn gpeidparad asrvkliall ralraqdgtg palptviagf
      121 sqggimsasv altspgdvta favlcgrilp eidpliaprd alaplhaliv hgrfddklpv
      181 swadtadakl talgvahdtr lyaaghelta emagdfgrwv gertgln
//
LOCUS       WP_175997091             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia stabilis].
ACCESSION   WP_175997091
VERSION     WP_175997091.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46786
     Region          28..433
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(39..40,43..44,47,86,144..145,147..149,152,172,
                     175..176,179,261,264..265,268..270,273,301,305,358..359,
                     363,367,383,386..387,390..391,394)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mqtrstldeh atvaapapar takhyllagw asmagttiew ydfflygtaa alvfnriffp
       61 sldpvvgtla afgtfavgfi grpmggivfg hfgdrigrks mlmitlllmg vpsmiiglip
      121 sydsigywaa alliamrflq gmavggewgg avlmavehap kgrkglfgsl pqtgvglgli
      181 msslamaava alpeadmlsw gwrvpflasi alvglgwfir akvpespdfe kiqrqgkaek
      241 spvtaalrrh prevltivga raaentwfym vvtfalayat qqlhlpkaem lhaitagavl
      301 slvtmplcgh lsdkigqrrm faiglvlmca faapffmmlg tqqtsyawwa ivlglgvvfp
      361 ilyapesllf aqqfpaeiry sgislsvqla gvigggfapm iatsllkagg gqphyviayl
      421 vgfgvfalvc talmrpaca
//
LOCUS       WP_175997166             468 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia stabilis].
ACCESSION   WP_175997166
VERSION     WP_175997166.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..468
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47679
     Region          23..450
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,277,280..281,284..286,289,317,321,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msefapaagi aepavnwram savllavala tldtaianta lpaiaadlha spaasvwiin
       61 ayqlamvatl lpfaslgdiv ghkrvyiagl avftlaslgc slastlpmlt aarivqgfga
      121 saimsvnval irglfpahrl grgvgfnalv vgvsfaigpt iaslilsvaa wpwlfavnvp
      181 lgvfalavai pslpqtargk hafdpvaalf nvitfaslif algefaqrgp lrvvlaaaav
      241 alafgwllir rqaghpapml pvdlfrrpvf tlsaltavca faaqglafvs lpfyfetvlh
      301 rsavetgflm tpwsaivala apiagrlsdr yppgllgaig lallsagmvs laalpatpnv
      361 fdigwrmmlc gagfgffqsp nlkalmssap persggasgi iatarligqa tgaalvalsf
      421 giagrhgptl almlgagfag aasvasglrl fapshragva aaperare
//
LOCUS       WP_175997179             511 aa            linear   BCT 11-JAN-2025
DEFINITION  catalase [Burkholderia stabilis].
ACCESSION   WP_175997179
VERSION     WP_175997179.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..511
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56963
     Region          22..504
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 msspshrvlr havaaicval saspyaaelt rdtgapvgdn qnsqtagpag pvllqdsali
       61 eklqrfdrer ipervvharg tgafgefvps aditdltkak vftpgtrtpv fvrfstvmgy
      121 rgspeqardp rgfavkfytq qgnwdmvgin wpvffirdgi kfpdfvhank psavtgvqdp
      181 nlafdffant peatnmltml ytnagmpdsy rhmdgfavha fkfvnahgdv hyvkfhwksq
      241 qgvhglrpqd iaasigrdwn mmtndlygal kqgdypkwdl yvqvltpkdl nrfdfdaldd
      301 tkvwsgvper kigtmtlnrv pdnyfqstee safapsrlvp giepsedrml qdrlfayadt
      361 qmyrlganym dlpvnrpvvp vvnnnqdgkm nagdrkgevn yepstlhela qdpqyksvrt
      421 tlggttqqea ihkkllfrqa geyyrglsqq dkddlvtals gdlgkvtnah nqyamlsyfy
      481 kadadygtrl tqavhanlqq vqslaaklne n
//
LOCUS       WP_175997180             203 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia stabilis].
ACCESSION   WP_175997180
VERSION     WP_175997180.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..203
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=21509
     Region          <49..202
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(77,79,83..84,87..89,91..92,96,99,108,110,112,
                     116..117,120..122,124..125,129,132,141,143,145,149..150,
                     153..155,157..158,162,165,174)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          77..108
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          110..141
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          143..174
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          176..201
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mrperftrai raaaaalala aiagcvhlpd rpaygkadpa alrrydgdwf daarigrvdi
       61 lralhdagyp vdatnsrgft avilasydgq paaldyllsa ganacagdrh gntalmgalf
      121 knepdiarrl idtrcpidqt ngagetalgf atlfnrfeli pllvahganp shvdrrgqsl
      181 lqlalshdnt eaadalrqag arr
//
LOCUS       WP_175997270             223 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175997270
VERSION     WP_175997270.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..223
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24230
     Region          38..192
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mepksaspdd iraepasdta agdvpraltq rgrntvgril esaieifivd gyggltmrkv
       61 aagaglalsn lqhyfpsred lfaaiiseti aeysktydsv rtdetlspea rlekvvrmli
      121 edaklprtqs lfvniwalah ahefarqame dsylfqrqmi agfvtavnpg ltplhlarrs
      181 alitaqiegl svlipqrnrf psdikgmede vvkavlavaa lpg
//
LOCUS       WP_175997291             482 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia stabilis].
ACCESSION   WP_175997291
VERSION     WP_175997291.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..482
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50566
     Region          25..478
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mshpatpaqa lpvpdgaaqa gglrrnylsl peliaqsigl vgvsggigvl ipavfatagn
       61 gtwlaylfai vallfsswsi svfardaasp galyayvsag igpiwgaicg wslliayava
      121 aagilqgtin tflvlgretg llggatpvgt vlgltivtaf aawyiafrdi rlstrftlfv
      181 elatllliav vviatiafgg hpvdraqltl egvkptqlql gmvlaffsft gfesatvlga
      241 eardpfraip ravlisvvgp ailfvigayg mvsafhgqtp pldrvdgpla vlahrlgagw
      301 vgvlidagva lsffaaffss inaaarivyt fgrqgvlhas tgrahernat phvavaliaa
      361 lalitalvft argtalldsy gylssiatyg wllayvlvai gaplylrrqr klrprhvais
      421 vvavvllaip ligsvypvpd gvyawlpyvf vallaiglgw fvllrirfpe rlreleaelq
      481 tk
//
LOCUS       WP_175997249             237 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia stabilis].
ACCESSION   WP_175997249
VERSION     WP_175997249.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..237
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25956
     Region          6..229
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 msqtsgsmit frrpdgqelq gylatpakke gapavvviqe wwglndqirg vadrlarcgy
       61 falvpdlyrg kstveeeeah hlmtgldfgd aasqdipgav tylktlaprv avtgycmgga
      121 ltllslqyad adagvtwygl ppldyidpak lkvplmghwa tqdaffaidq vdalekkltd
      181 akvgfefhry lahhafanee avgpgriagt qfdpvwsqta wdrtltffgr tlwtkqg
//
LOCUS       WP_175997300             215 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia stabilis].
ACCESSION   WP_175997300
VERSION     WP_175997300.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..215
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24410
     Region          1..210
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mltvwgrrna fnvqkvmwlv gelalahrhv paggqfgvld tpeflamnph grvpviddgg
       61 tvvweshsil rylaarhgra hfwrddpaeq sradrwmdws qttlqpvflt gvfrgyyrtp
      121 peqrdtarve qsvaqcaqhf qtldavlagq pflagdaitl adiaagthly ryfeldiarp
      181 rvphvqawye rlkarpayrt hvmipfddlr grldg
//
LOCUS       WP_175997332             471 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia stabilis].
ACCESSION   WP_175997332
VERSION     WP_175997332.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..471
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50386
     Region          9..456
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mnqrqgfdai verekglhrg lstaqlsmia iggaigtglf lgsgfaigfa gpsvlvsyai
       61 galialllmg claemtvahp tsgsfgayae hyvspwagfl vryaywasiv favgtevtai
      121 avymkywfpa vpgwywiigf saaligvnlv svkvfgavey vfsmlkiaai vafialgavv
      181 vfgapagsgi gfanytahgg ffpkgvwgmw vavivsifsy lsiemiavaa geardphkai
      241 trafratmlr lvffylltla lmlaivpwta agsdespfvk vmaathvpga agvinfvilv
      301 aalsamnsql yittrmmfsl sragyapkal grltghgvpa aalglsaigi alatvlnvly
      361 pdtsfvmmms vsmfgamftw lmifvthlff rrrhrgqtlt frmwgfpvts llgavlmfaa
      421 lvttyftref rmtlfcgvpf mialsvvyav wyrgrgeapa geregvhapg q
//
LOCUS       WP_175997336             555 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia stabilis].
ACCESSION   WP_175997336
VERSION     WP_175997336.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..555
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60123
     Region          4..550
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mqasatsaap vtvftarril tmnpaqpsat hvavrdgril avgdaddata wparfgtcaa
       61 ddslrdkvlm pglveghchl megamwdavy vgyydrrgpd gtlwpglrsl davlerlava
      121 eramtddgpl lawgfdpiff gtsrltvrel drvssrrpia ilhasvhlmn vngamlarag
      181 idedtdidgv srdadgrptg elqefaamlp vyqtiggkla isasekphai wnfgrvaqla
      241 gvttatdlvn dlsldgnrtl hevtadadyp vrivpafapq rnparsadsv laeierntdk
      301 lhfgpvkfiv dgsiqgftar vrwpgyaggq pnglwlippa qlvdvfepfh raglqlhvht
      361 ngdeatevvl damatllarh prpdhrhtlq hcqmadaaql rriralglcv nffanhlyyw
      421 gdahytqtig adranrmdaa gsarrlgipf alhsdapitp lnplftawca mqretasgrv
      481 lgegerlald dalhaitlga aytlrmdhlv gsievgkyad favldedpsa caparlkela
      541 vwgtvlggrv frspr
//
LOCUS       WP_175997356             463 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia stabilis].
ACCESSION   WP_175997356
VERSION     WP_175997356.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..463
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49702
     Region          36..451
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mdndrpgrsa svaamndigt rmhrddadgr rkphllglst lvifglayml pmtvfttygl
       61 vtsetnghlt aayavtlvam lftarsyghm arlmpsagsa ytfasrnfgt sagfmvgwal
      121 lmdylfipmi sylaigiymk qlfplvpasv wivasivlit glnivgirlv nrvnlilias
      181 qlvfiaifvi asarvaageg lslavalpas gdasaifags ailclsflgf davttlseet
      241 reprrtvpra illctlasgl lfmliayvgq vvfpdwhafk dldsaslelm rrigggalsa
      301 lfvavyvagc fasamagqas vtrvlfamgr drvlpervfg hlharlrtpv ratlavgavs
      361 lsalfitldl astmisfgal vafaivnlcv mrsylcraen rhvagwitfg vmpaigfamn
      421 vwlwsglsrq tfyvgigwlv lglcqlvwlt rgftrpaptl smn
//
LOCUS       WP_175997374             220 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia stabilis].
ACCESSION   WP_175997374
VERSION     WP_175997374.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Kane,E.I. and Spratt,D.E.
  TITLE     Structural Insights into Ankyrin Repeat-Containing Proteins and
            Their Influence in Ubiquitylation
  JOURNAL   Int J Mol Sci 22 (2), 609 (2021)
   PUBMED   33435370
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Mosavi,L.K., Cammett,T.J., Desrosiers,D.C. and Peng,Z.Y.
  TITLE     The ankyrin repeat as molecular architecture for protein
            recognition
  JOURNAL   Protein Sci 13 (6), 1435-1448 (2004)
   PUBMED   15152081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12158766
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..220
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=23702
     Site            order(22,26..27,30..32,34..35,39,42,52,54,59,63..64,
                     67..69,72..73,77,80,89,91,93,97..98,101..103,105..106,110)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          22..52
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <24..111
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          54..89
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 msitwdgitg agvlgdaeva rrhaladaak ggnwatmldl vakdsalvna trpggtslyt
       61 plhqaaygga prevaaellr lgawrtlrda hreravdiav arghrhlvdl ltpqlkrfvp
      121 dgtlreiqrh fhamivgria hlrvdalrlp elepllefdt qadhmwfavp gmyggfgyal
      181 rtdgdaavlv ssswsrvvgg sgqrheitan gctlveegfv
//
LOCUS       WP_175997401             229 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia stabilis].
ACCESSION   WP_175997401
VERSION     WP_175997401.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..229
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24856
     Region          25..229
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 merkpaekia vdagsdpgts tldvfafatp nsvkvpiale dmgveyrlvp vdlrrgeqkt
       61 daframnpda kvpvlvdrsa hgdgdivvse saailvylae ktgqllpasg pqrgkvfeql
      121 ffhasgvspa flqafrvamh aspepdakar alaevdrtlg vldrvlersr yvagdtysia
      181 diahfgwlwr hqaigatldr fpsvvrwyde msarptvvta vektlalar
//
LOCUS       WP_175997444             127 aa            linear   BCT 11-JAN-2025
DEFINITION  GtrA family protein [Burkholderia stabilis].
ACCESSION   WP_175997444
VERSION     WP_175997444.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..127
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=13823
     Region          11..127
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 midllctert rlvrfglsgl cstaihtlva aamfalfdat pvtanavafi catvfsylan
       61 tlwsfsstvr trnllrflav tlagfietll laraaellev srgmsvvaia llippttfll
      121 hrlwtyr
//
LOCUS       WP_175997445             347 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Burkholderia stabilis].
ACCESSION   WP_175997445
VERSION     WP_175997445.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..347
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39031
     Region          12..194
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(15,17,102)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(49,101..102)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            100..102
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mrephytplv slvvpfyneg eaverffdvv iplltaidai rfeivcvndg srddtlerli
       61 ristaerrvr vidltrnfgk eaaltaglde algdavipld adlqdppsli pvmiehwrdg
      121 aevvaakrss racdsfakrt aaaiyyrvhn llsdvklpen vgdfrlmdrk vvnalrslpe
      181 rhrfmkglfa wvgyrtvive yqrdprsagh skfsgwklwn falegitsfs tvplrswtyi
      241 gvgiaalafv ygafivlrtl lfgnpvfgya slisvtlfig gielvgigvv geyigriyde
      301 skqrpvylir rryqahgkvi elpvardarr qlarrraqpa rvrigtr
//
LOCUS       WP_175997452             147 aa            linear   BCT 11-JAN-2025
DEFINITION  TadE/TadG family type IV pilus assembly protein [Burkholderia
            stabilis].
ACCESSION   WP_175997452
VERSION     WP_175997452.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..147
                     /product="TadE/TadG family type IV pilus assembly protein"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=15458
     Region          2..>94
                     /region_name="TadG"
                     /note="Flp pilus assembly protein TadG, includes
                     N-terminal TadE domain [Intracellular trafficking,
                     secretion, and vesicular transport, Extracellular
                     structures]; COG4961"
                     /db_xref="CDD:443987"
ORIGIN      
        1 msarhfplsr rraqrgsaiv efgliasvlv mlligifefg rvlfywntas eavrlgarta
       61 vvcdvnaagv akrvtalmpl lssanvavsy spascdvnsc afvtvsvtnv tvktmipfvn
      121 vtlkmppftt tlpresltsa tggsacn
//
LOCUS       WP_175997454             729 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia stabilis].
ACCESSION   WP_175997454
VERSION     WP_175997454.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..729
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78346
     Region          35..729
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 matgtgaarr araiaaggal caaaaggaha qasnaarlqa dpaaavlpai gvkgradgss
       61 aglvglrtaa gtktdtpvae ipqtinivta qqiemtgaad lnqalryvpg fatfgadsrt
      121 dwyaalrgft ptlyvdgvpa pntavianwr vdpytidsia vlrgptsvly gagepgaivd
      181 ahtkladger vreagveign darkqfmldv gdrldpdgry ayrfigvard gnavtgpngd
      241 rrvalapsfr wrpnadtslt lsasflqdsg dissnflpas gtvlpnpngr lsqdiymgdp
      301 sfndyrkkqw slgytlehhv naiwtlhqdv rwshlsldda tvfgngfapr sttnmmrfag
      361 lfqlnysrld idnhaqarfg tgplehtllf glqfdrqttt nsvwlalaps lnlynpvypp
      421 vtaaifsgpt slghvdqyta mnafgayaqd qirwrrwtlt lggredrvna rfddrtagtq
      481 aqqdvsafsg rvgltyqgda glspyvsyst sfdpvigvrm fggglpkptr gtqteaglrw
      541 qppgrnlmln aavyqinqtn vvtptpvnld atgttsvqtg evrsrgiels algkltrels
      601 ivasyvyqdv rnvkandasl nhwpvavplp rqmasmwadw twhagvlsgl gigggvryqs
      661 asagapdnsl tvpsvtlvdl amhyemrhwr falnvanlfd rryvsgcqsy avcvfgnert
      721 mlasakynw
//
LOCUS       WP_175997466             428 aa            linear   BCT 11-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Burkholderia stabilis].
ACCESSION   WP_175997466
VERSION     WP_175997466.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..428
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46092
     Region          1..422
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 mdttdsmlrr qnnlgpayrl fydepvhars aegvwlhdvd grryldvynn vpsighahpg
       61 vmaaisgqma vlathtryve erileysdrl lalfpaeldk vmftctgsea ndlalrvara
      121 atngtgiivt rlayhgvtss iaeispsfga gvplghhvrt vpapdtyrty taeqvasgfa
      181 esvaaavadm krhgiqpaal ivdtifssdg ifgdpagflg pavdlirreg glfiadevqa
      241 gfgrtgsamw gferhgvvpd ivtlgkpmgn gypvagivar tplidafagr tryfntfggn
      301 pvacaaglav lnairdeglm lnvqstghyf rsrlhdlqdr cpligdirga gffigvdlvk
      361 drqtraplsd dtpkvvndmr rkgilisatg phgnvlklrp qlifqpdhvd lfmtnleavl
      421 sdvmrsla
//
LOCUS       WP_175997493             972 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia stabilis].
ACCESSION   WP_175997493
VERSION     WP_175997493.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 972)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..972
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..972
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=105050
     Region          498..787
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          517..548
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(550,552,556..557,560..562,564..565,569,572,581,583,
                     585,589..590,593..595,597..598,602,605,614,616,618,
                     622..623,626..628,630..631,635,638,647)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          550..581
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          583..614
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          616..647
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          649..680
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          669..954
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          717..747
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(718,722..723,726..728,730..731,735,738,747,749,751,
                     755..756,759..761,763..764,768,771,780,782,784,788..789,
                     792..794,796..797,801)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          749..780
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          816..847
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          850..880
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(851,855..856,859..861,863..864,868,871,880,882,884,
                     888..889,892..894,896..897,902,905,914,916,918,922..923,
                     926..928,930..931,935,938,947)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          882..914
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          916..947
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mariefhrnl dwgsekpaad kapsgeekri sydplehgpl aafdrspqga alraqyreni
       61 gklseflrnr dpvnqravrs leafdgkiaq gadgpystal halygpgkha ldnvaaride
      121 gghsgealea givelangld vcapgvashl imtdqtinag qdgidghakm iwetlfdsvl
      181 rdfvahvhga eenyqgeeih lvnqyrnlla pdfhvaprpd dfkppqagan gllegcrryl
      241 qrhvtpdrll rvmaeeclqt vrehfaayqd rpldtnevwa lrqaydkslg aslamkygei
      301 dagvlvnehn geqvqpdnne dshywlidnp tllmraiskn lytaaiiges ykpvrlfgqk
      361 gedgvvkqvg gggiytktgh ayrplrvdew gelagrspea dqngtvmavl lrtalantrs
      421 pellakvppe rvwhaiaqgi dsvnaltrla qpeirryrqv skdhdtflvn eaaravgers
      481 pserqralli vsaggesalg vriaetldtv sgkdaagrsa lhhavlngdm qlldvlipks
      541 alfidvpdrn glaplmaaar ngdteaidrl igagaivdne neagivalmv aaqhnradvi
      601 drllekgasi didnragfta lmtaaqygsv aaidqlvaag aaiditdlkg htalmvaady
      661 gradaidrll sanpevdktn hdgytalmla aqngrveaid rlltkarpei dktlakgfta
      721 lilaaqnghd kaierllnan pevdktneyg ftalmlaaqk ghdkavgqll narpeidktn
      781 pegftalmla ayhgrdtvie qlltkarpei dktdpkgfta lmlaafhgrd kaieqllnah
      841 pnvdktdpkg ytalmlaarn ghdkavgqll nakpeidktn pkgftalmla ahqgqdkaid
      901 qlltkakpei dkentkghta lmlaaasgai hvvdrlldng akvdkrdkng vtaiqfaqrg
      961 gfsavvdrlk sv
//
LOCUS       WP_175997520             330 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175997520
VERSION     WP_175997520.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..330
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36647
     Region          9..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..296
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,231,248,275)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     225..229,236..237,240)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mdpsqlpsla wfvhiahhls ftkaaaemgv sraalsqnlk alerqlnvkl lyrttrdmsl
       61 tedgqrlydt lrpafgsiel airnlhevrh epsgllrint srvaarnlve phlgefmary
      121 pllrvelvmd dglsniiadg ydagirlges laehmvavpi tpmlemavag spdyfarhgt
      181 patpadligh nclcyrhtts gaiyrwefts peieghafev ephgsvvtnd ddgmiraalq
      241 gigliqhqdv alrehldagt lvrvlepwck pfpgyylytp sreqmpakvr almdflvekr
      301 ehlavdsarr aasptkpaep kprkpratra
//
LOCUS       WP_175997541             310 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: electron transfer flavoprotein subunit alpha/FixB
            family protein [Burkholderia cepacia complex].
ACCESSION   WP_175997541
VERSION     WP_175997541.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..310
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31450
     Region          2..310
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtilviaehd nasvkaatln tvaaaakigg dihvlvaghn aqaaadaaak iagvskvlla
       61 dapqleagla enveatalni akdyshilap ataygkniap riaakldvaq isditavdsa
      121 dtferpiyag naiatvqssd pikvitvrat gfdpvaaegg saavekieaa adagksqfvs
      181 revtkldrpe ltsakiivsg grglgsgeny tkvlepladk lsaalgasra avdagyvpnd
      241 yqvgqtgkiv apqlyiavgi sgaiqhlagm kdskvivain kdpeapifsv adyglvgdlf
      301 alvpelvnel
//
LOCUS       WP_175997580             320 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia stabilis].
ACCESSION   WP_175997580
VERSION     WP_175997580.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..320
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34570
     Region          10..223
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(51..52,54,68..70,76,78..79,120,222)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(51,53..54)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(76,79,82,89)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(112,116..119,121)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(117..118,141..143,195..196)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          237..320
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 midglivrva akhdeaadic sfelvradgl plppfsagsh idvivpggpt rqyslcnapd
       61 enhryriavl rdpksrggsa gmhdrvnagd tltisvprnh falahdaahs lllaggigvt
      121 pilcmaerla ridvpfdmhy ctrsrsrtaf ldhiasapya gqvqvhfdde denqrfdiaa
      181 rlavpepgth lyvcgpkgfm davltaaras gwpeaqlhye ffaadarqtd qdgrfeveia
      241 ssgrvivvek nesvvralak agieietsce qgvcgtcatr vlagepehfd lcltpderaa
      301 ndqflpccsr sksarlvldl
//
LOCUS       WP_175997661             278 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175997661
VERSION     WP_175997661.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..278
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30647
     Region          111..275
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          217..274
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mrilqpdpaa rghyligvrp dtlgstlrav gtpgfvgavt efvndsidad avhlerwrad
       61 tgstsghvve wlgsgslrfa adtlrvmdly yqdychadpl vaplrgqagt llvqrhvdgi
      121 aqgefrrrif depgiaqecl lvhgnahvqy alglartvgr aafttdelfh frqmvdllfp
      181 mfelhartca arrvtsgsga anaasqagfd arlerqdvql srreheicrl mlcgrsvpea
      241 aqqldvklst aesyvkrafa klgvrtrrel fdwvlvdc
//
LOCUS       WP_175997662             574 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Burkholderia stabilis].
ACCESSION   WP_175997662
VERSION     WP_175997662.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..574
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=62760
     Region          7..560
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mqiqpthaaa tpadfvltna kvytvdphkp waqavavrdg rivhvgdtaa vqayigaqtk
       61 vvdaagrlvl pgfveshwhf ettafafqaf vnyedpqkvl aalrayvdth pdepaitgmg
      121 wvqatippal lrketldaic adrpvcllst dfhtmwvnsk aleiagidas tppvqegasw
      181 fekdavtgep tglivdgaay sllmqrisaa gllptgidly lksippwqkk lcaagvttvf
      241 dagffdpsgd qsllyetlqt meragdlklr vvgsvavige iddpvgtlvr yreqydsplv
      301 karalklfld gteanhtayl lepyadrpdt cgaptmpadt fnrylveadr ananvmvhcv
      361 gdaavrmald gfdevnrtnp prdrrhvith aflthpddip rfrragvman tqlqwgvvda
      421 yteqlrdhyg herwsnmykf rtfldegvtv sigmdglacq crcqhkpleh iesghtrqla
      481 gepdaavfpd iaerlsipql iaaytihgay qlgmeheigs ltpgkradlv vlendlfevg
      541 qydigridva ltmmdgdvth vgddfgartg igar
//
LOCUS       WP_175997678             486 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia stabilis].
ACCESSION   WP_175997678
VERSION     WP_175997678.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..486
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52432
     Region          72..450
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mthlaispri gaavvvlafl agcttfskdg gfdavstaas erigkdavvv rtdadraavd
       61 qrtkallakp lsiddavqva llnnrglqas yaelglsead lvqagrlpnp rfsfsrtrag
      121 dgelslgrtf sanvfalltl platniehrr fertkletad amlkvaadar rayveavaae
      181 qaahyarqvr daagaaaela lrmrqagnfs rldyareqaf hadavaqqak arqqavaare
      241 kltramglwg eraqyalper lpdlpaarpq lpdlerfamt nrldiqaakl qtqgvasslg
      301 lskatrfvna vdlgyvnnye tdkghehgye isveiplfdw ggakvaraea vymqsanrla
      361 ktaidarsdv resyaayvts ydvakhyrde vvplrktisd elllryngml asvfelltda
      421 reqvgavngy idslkdywla etdlqmavgg rlpaaphsie pepaaapqpa sspaaqpapa
      481 thpegh
//
LOCUS       WP_175997719             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia stabilis].
ACCESSION   WP_175997719
VERSION     WP_175997719.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21550
     Region          9..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msahgffsan lllaytayfi gtaspgpsnl aimsvaanqg rkaalafalg visgsmfwas
       61 vaalgvsaal lawskllvai kifgglyllw lafksgrtaw sgkaaaspna ahgqrlsrfy
      121 vrgamlhltn pkailvwvsi valssngaga shgavvpgcl vigclvfggy alvfsmdgar
      181 rlyvrgrram eaclavvfga agirllvsna
//
LOCUS       WP_175997721             316 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175997721
VERSION     WP_175997721.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..316
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34862
     Region          11..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrkfkipnmg alvafeaaar hesfthaake lfltesavsr qiatleaslg vrlfarvkqr
       61 vvltragkly gtqvrralet ldrdtlsiia hgsgggylel avlptfashw lipriksfyd
      121 rtpdvrvnmg srtdlfsfed thfeaaihyg kptwpgtssd ylfgeevvpi cspalldgpv
      181 ervedllayp llhsttrpga waqwfethgv edirtmqgvr yelhtmlisa aaaglgialv
      241 pkffveeqlq qlglivpcda atvgdsayyl vyptelshsk plelfrgwll eqasayaapd
      301 adganaeyde ddedve
//
LOCUS       WP_175997757             204 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia stabilis].
ACCESSION   WP_175997757
VERSION     WP_175997757.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..204
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20822
     Region          19..204
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msttvntllp lagvlllsva spgpnfvivt stavvsrrag vmtglglaaa sgtwaaiaia
       61 glsllvthva wvhtalrlag aayliwlglk miltarkplp asapavatdw naarkgyvvs
      121 mtnpksvafy gsifalmvpa qapasldlav valsiaisaa wyctmallas hpsvrrllvr
      181 rkavldttag lllvgvggrm lagr
//
LOCUS       WP_175997785             197 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175997785
VERSION     WP_175997785.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..197
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22058
     Region          8..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkkgtdtqas apdtrerilq tasalfyreg travgvdliv aqagvaktsl yrhfatkddl
       61 ieafllreda dfwahwdvva qqykrtpree ldaqlqwige riarpgyrgc pqiniaaeya
      121 ddnhparkva vahkqelrrr ltelagamrv depetfalrl atvidgalss gralhehgpv
      181 yflqeiaqll lpkkgrk
//
LOCUS       WP_175997765             358 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia stabilis].
ACCESSION   WP_175997765
VERSION     WP_175997765.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..358
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39032
     Region          12..335
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 msntasynvr siwytrcpvp tplgiaahlg wldsefagdg itvralqesq haalhhahvd
       61 hsldnafrqg gsipalwara agadtrvval twvdeaqaiv alpetgltrp kdlrgrrigl
      121 prrdgeridi fraaalrgfv salsldglgp gdvewvdvpa snlrapvstp ltrdaafshp
      181 asltsrrlya aeaaalvrgd vdaiyvkgsl gletahliga qpvvdigfhp dpqirinngs
      241 prpltvnast lerhpdivsr flarvtdveg warehedevl gylgretgsg hdwlrlayga
      301 dvhrrlrtdl deasiaaldd fkrflvdwqf lpadfdvraw idrraldgia tlsrdaar
//
LOCUS       WP_175997795             481 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia stabilis].
ACCESSION   WP_175997795
VERSION     WP_175997795.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..481
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52156
     Region          28..419
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,156,
                     159..160,163,282,285..286,289..291,294,322,326,375..376,
                     380,384,400,403..404,407..408,411)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mktshpietd alarldnlpw trfhtlmlva lgvgwaldsf etniigsvfg vlkshwhlsa
       61 aqgslavsiw vfgmlvgaia fgyladrygr krlflatllw yaffsvatvl swnyesflff
      121 ramtalavgg eysavtatmg efipkrhrgr tdalilsgfp vgallsaavs ylvlnqlpae
      181 wawrvgfglg ttmalvffwi rrvipesprw liqqgrvaea daiveqivas aardpraqad
      241 raqlaqrytp trfehqapaf wrnvgelfga yrarcalaga lnfsqaavvy gvlslmalvi
      301 lpylkvsstd mpiyymigna aalaggivaa vlveawgrra slfasytftv aaivfiyamh
      361 alpgmvlgyc liqfgvtway isgyvvssei lptriratgl gvsvaigrlg aviaplmltn
      421 vyamsgspsa alivllvlal pgplaaglww ingretrris leecsteldv eptvdaspri
      481 a
//
LOCUS       WP_175997803             603 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia stabilis].
ACCESSION   WP_175997803
VERSION     WP_175997803.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 603)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12379621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..603
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62735
     Region          1..289
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
     Region          329..603
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 maswldytln glivgniyal lavglalifg vshlinfahg svymvgafig wlcltrfglp
       61 lpvalaavvv gcgalgvaie riglrplrha ariapllati gisfildqla qlafgadpra
      121 vptplpdwhl riagatlgsl dlliagigia aaallygflr ftrlgwavra taqdrdaalq
      181 mgvdvdrvnq tvfaiacalg gvsgllvgmy ynsidpamgf qatlkgvval ligglgnvpg
      241 aiagslllgl vesygvalfg tsyrdlfafg llivflvrrp nglfsakral ppepmtgtfl
      301 aaakavrvpr pvlvaliala avlpwlgasp yvlqtltnaw lygllalslt lvagtvgqis
      361 lghaallvig ayasallssd lgwspavtip cagvitavlg tllvypafrl rghyvsiatl
      421 gigevvslvi lnwdgltrgp lgitgiaplp wastaraayw ftlavlvvla lvqvrllrsh
      481 lgrtlravre ddvaarahgi apnrykaiaf avggvaagvs ggiaahlysy inhqtfdsqv
      541 silaltmvil gglgnvlggi vgavaliglp elfrwaadyr mliygvvlll lvrfrpqgll
      601 gtv
//
LOCUS       WP_175997823             517 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Burkholderia stabilis].
ACCESSION   WP_175997823
VERSION     WP_175997823.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 517)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 517)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 517)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..517
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=56675
     Region          <55..>204
                     /region_name="PRK13560"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:106506"
     Region          148..513
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mratragaml virprdaarl hpnpimsfpd eddfhrllda lttcvllhda htkaivwanr
       61 aacialgfsv eellplkard mtrpepkyrr eigvgamdra mtdgpqvyew cyrsrtgvdm
      121 lseaiatyvp lhgrdvvmvq frdisaeeai rqqlrryear lrefmqdlde gvavvtphgg
      181 aqfisesgrr vlglapdeal gevldyctea drdrlvaqlr dapstcpsep qryrivrrdg
      241 stcwlritcr qveiegdldg llvqfrdvsd evaiedarra earmleyagr ynamgematv
      301 iahelsqpla avrnfiegav qrlngrgnvd daiwglrsad rqaehaalii ksvrefivkr
      361 epavaladlr diladvayfi elrakeagvt vaivqadapl pircervlig qvilnlafna
      421 ieafascerv prtltlgtan vdgyaelrai dngpgieega hgrlfdgfss skvggngigl
      481 slcksivtrh ggrigaspas gggldcrvtl plagera
//
LOCUS       WP_175997846             220 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175997846
VERSION     WP_175997846.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..220
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23859
     Region          27..182
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msnsgmekal etekrgrsyg gvapevraae rrealiraat rvfgtvgfrk atvrsicqea
       61 klndryfyaa fdstedllrc tylhhaqqlh eavaqavaar ggdpresvda glaaffaflr
      121 dpcaarvlll evmgvsadtd mtyqrmlidf gklimaigap geattpvert eqrliglalv
      181 gamtnvgaaw llteyrdpea qmiascrkvl lgtlraiget
//
LOCUS       WP_175997847             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175997847
VERSION     WP_175997847.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33027
     Region          9..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..294
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,229,246,273)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,193,
                     223..227,234..235,238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 madlrdvnln rlaifvavvd agsltaaaer lglaktvvst hmqrlesevg anllvrttrr
       61 lsvtdagrtf ydacrsivra tenaldavss dagplrgtlr vsvpidygal vvapavvalr
      121 dthpgldvel iandrvvdlv adnldvairi grladsnyra vqlgtyekwl vaspafvarh
      181 glprdpdala alpfvmlstl prphtleldh arggntsvrc aapvvsntat acraivlagg
      241 gfglltdfst addvaagrlv rllpawgsap agihavypst rlpspkvraf idamkarige
      301 arpvpaaknr rsr
//
LOCUS       WP_175997850             402 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Burkholderia stabilis].
ACCESSION   WP_175997850
VERSION     WP_175997850.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..402
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43842
     Region          74..339
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 msfplepdgp aprdaadard vappqfgvdg eqaerdwplm thdevaavla ridgvgapar
       61 ltwhsprpfs aavlvrtsdg ralfvkrhhv slrdvaglee ehcfiahlre rgvpvadvla
      121 grdgatafaa gdwtyevhvv apgvdayrgv mswkpfthps hayaagrala mlhrasagyd
      181 aparpvrtll ssfrvlssad ltgalerwvd aqpllvralg ardwrddvad aigpyharlv
      241 pllpalaplw thgdwhasnl lwteagpgaq vqtvldfgls drtcavmdla lalernaidw
      301 mapadarrie yaqidalldg yesleplsdd ayaalvallp ivhtefalse vayfgcivda
      361 pdivdiaydg yligharwfg erdgrqlldw laqrrrekqg ra
//
LOCUS       WP_175997852            1070 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia stabilis].
ACCESSION   WP_175997852
VERSION     WP_175997852.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..1070
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=114941
     Region          1..1040
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mferlirfai ahrwlvmlai aavaaigvfs yqklpidavp ditnvqvqin taapgysple
       61 aeqritypve tvmaglpgle qtrsisrygl sqvtvifkdg tdiyfarqlv neriqeakdk
      121 lppgiapamg ptstglgeiy lwtveadaaa rkpdgtryta adlrelqdwv vrpqlrnvrg
      181 vtevnsiggy vkeyrvapnp aklmsygltl advvralern ndnvgagyie krgeqylvrv
      241 pgqartvddi anivltnvgg vpvrmkdvgi vdisrelrtg aatsngdevv lgtvfmlmge
      301 nsrtvstava akmedvnrtl pagvkaipvy drtvlvekav atvkknlleg ailviavlfl
      361 flgniraali talviplsml mtftgmvnak vsanlmslga ldfgiivdga vvivencvrr
      421 lahaqatagr pltrderfae vfgasqearr alifgqliim vvylpifalt gvegkmfhpm
      481 aitvvmalaa amvltvtfip aavalfiger veekenrlmg warrayepvl aafmtrparv
      541 migagaivlv tlglatrlgs efipslnegd lavsalripg tslsqsvemq ksiektlkar
      601 fpeiervfar tgtaeiaadp mppnlsdgyi mlkpadqwpn pkkprdtlvr eieealaelp
      661 gnayefsqpi qlrfnelisg vrsdvavkvf gddmavlnqt geqiaaalqk vpgasevkve
      721 qttglpvltv nldrdklary gvsvadlqdt vaaavggqka gtlfqgdrrf divvrlpdel
      781 rtdieaikrl pialpapaag asgpraaapy vplaelatie vapgpnqisr edgkrrvvvs
      841 anvrgrdvgs fvadareqlq qdvrvpagyw vswggqfeql qsaserlklv vplalfmvfv
      901 llfvmfnnvk dgllvftgip falsggvvsl wlrgiplsit aavgfialsg vavlnglvmi
      961 sfirnlrdeg vpldaavhdg altrlrpvlm talvaslgfl pmafatgtga evqrplatvv
     1021 iggilsstal tllvlpvlyr vshsvswraa frggfgagll rrlgflkgna
//
LOCUS       WP_175997889             331 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia stabilis].
ACCESSION   WP_175997889
VERSION     WP_175997889.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..331
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33425
     Region          14..330
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msstpistha apdasrarra qfvrlvqarg aiailvlvcl iagrvfphfl sapnlldiva
       61 aaafvaliti gqsfviilgg fdlsvgslvg lgtviaayaa pygwgaalaa pvcaglvvgl
      121 angwliarar mapfivtlaa llglkglslv lasqdmlian pgffatiang slfgvgnlvw
      181 ivvvaylvaa fvlnhtryga gvfaiggnee aarmlgvnve glkivtygls galaglagal
      241 lasrldsglp gagnsyelqs iaaaviggvl ltggvgtlfg plagvlllgv ienvinqvgt
      301 lspyyqnlas gaflllavia qtlltgkrrk r
//
LOCUS       WP_175997893             414 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175997893
VERSION     WP_175997893.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..414
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=45565
     Region          8..202
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mnrqqswtrt aapgeiiyse gfagepvifl itdgkvelst rcedkrviva tlgrgeffge
       61 sallaaepra htakalsfcq ltvvpagmld eeiervsall rhivrtmirr vkrkddqlat
      121 ythadfmpgv lsyahvlalm agadardstd awarrpmqah asevsvplae virkcraiag
      181 hsrphvlaml rrmeklnlvt ieaaqadlag sasdyaassd arqvvtfdaa rvidraqqva
      241 dhdldlsins elelieladl esligvektl llnklshgei aeevfafrks kvlsyveqkg
      301 vayfsrrnar rggdvqalad lvwvdqrtlf dvisafdtyd laklianldd ravadklfsv
      361 mtearrnevs wvmrrelkld pveiedierr vldavraaka pvtgaasvps atda
//
LOCUS       WP_175997903             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175997903
VERSION     WP_175997903.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33597
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdyidklrif rsvvemrsft raadmhglar pvvsravadl earfgsrllh rttrqvslte
       61 taeriyerca avldeldale vqaqaqtrep egllrlvaht taalnrlvpl iagfksahpk
      121 vrldvtlter pvdlvgegyd igivvpymlt sestvvrlve ripvvivatp aylsahtrpe
      181 tpadladhpf vpispslrrp alsfrvdgnt ltvpfrfdis snspvfnrem vmhdfgigvv
      241 prtlveaela sgalvqlleg adlidafvei klayanrall pakvkafidy taaycdregw
      301 svpaaa
//
LOCUS       WP_175997944             323 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Burkholderia stabilis].
ACCESSION   WP_175997944
VERSION     WP_175997944.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10627418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..323
                     /product="phosphatase PAP2 family protein"
                     /calculated_mol_wt=35376
     Region          111..293
                     /region_name="PAP2_3"
                     /note="PAP2 superfamily; pfam14378"
                     /db_xref="CDD:433919"
ORIGIN      
        1 msknsrkiyl vawlvtilli lvdliwayhv dfriekgslv qsarmlsvvf avalafwlis
       61 ripykvpark afyenvahsl qwiavlavft hvalvfqylc vttnfplvgd alvavdaalg
      121 fhwleiyrwv tmhhwmqavl glayvsgdaq llaipvilai tsnsqdyaef vvqfivaviv
      181 silisvflpa esaflhfniq dpgtvstvsd farlrsgaar evifasaqgl isfpslhvml
      241 alsfayslrh vrfvfpigia lnalmivstp tqgghylsdv lsglvigvlv iyvvriwfag
      301 grapgvaapn pgvrdgrkgl ths
//
LOCUS       WP_175997953             565 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia stabilis].
ACCESSION   WP_175997953
VERSION     WP_175997953.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 565)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..565
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=60848
     Region          27..565
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mrtvsagrll saanllafav aaaaqtpqag aqpqsaqrhq aqqldelkqq mldqpdvlsa
       61 ksssdsdtlr fpeetpcfdi heiewrgada fpwlrdaipl ehacigqkgl sllrewvgkr
      121 lvargyitsl vsipsqdlst grliiellpg rigaindasg rigwapilfp rgahallnvr
      181 dldqalenvr rlpgqsataf dlvpgaslgd tdivvrhpdd arrvrfiata dnggldatgr
      241 nqlgaivaid splrlydqli vtyntdaalg nkslgsqaks aawnvpvgya sfslgisewt
      301 srqalvpelp gevmpplgqr trryeagvsy vpyrsghgkt tlrfrlarre drswfgpvel
      361 dvfrhdivsy evgashrekl aratvdasig mraslaglsa fpgrvngqpe wdgryrvysa
      421 slgadapfri gtrafgyrgs lqlqyapgal psteylqigg rytvrgfdgn qtlagdsgwf
      481 wrnelatpvf gaheayaald agvvtgagsr egagrdgrtl lgaalgvrgg yrmlgydial
      541 gvplrkpgal htarptvdvs lfarf
//
LOCUS       WP_175997978             330 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175997978
VERSION     WP_175997978.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..330
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36257
     Region          6..330
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpliriwave halasgiaap tdiltaanrl aptlpqgrta apfrwrvesi ggrpvrtasg
       61 qvipvdgaid ggstadaiwl tgpfvsdldr lldrpaslap lldalrrqha rgtliatyct
      121 gafllaeagl ldgriatthw skassfrary pdvalrasdv lteqdgilcs gavtsyqnla
      181 lrvvdklana rlaasvarlm lidmhrvsqd sfidldrmgh dghddpaiar aqrwmekhlr
      241 epfslarlse hvamsertlh rrfrdavgap plrylqtlri evakrllaet klaidavcer
      301 vgyadisgfr qlfkretgis pgeyrrrftr
//
LOCUS       WP_175998057             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175998057
VERSION     WP_175998057.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33656
     Region          15..74
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          103..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(113,117,156,170,172,231,248,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(114..115,119..120,122..123,126,130,132..138,199,
                     225..229,236..237,240)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mssdpvpcpn kpldlldval fvraallanv taagrefgvs aavasariaq lerqlgarll
       61 hrttrrislt qdgeifmara dallsaadaa rasvghgrse pygrlkvsms ssfgrqhvap
      121 visaflrryp svsldlrlsd eivdlvddgy dvairlgalk dstlvarkla anrrvlccsp
      181 aylaergtpr hpadlaqhec vilgdqrdws fttpqgpltv rvggrlvasn geairealvd
      241 gfgiaikstw dvgpllasga lvtvlddypf addvaiwavy psrahvplkt lvfiaflaeh
      301 fgdppywdhv dgr
//
LOCUS       WP_175998006             584 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia stabilis].
ACCESSION   WP_175998006
VERSION     WP_175998006.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..584
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=63905
     Region          9..584
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mkrfafwslf fvfipcvtea qqapmspdqa aaarasaeqn qqvqqrrdaq qrdatvqapg
       61 vrsdvprpea ypvlptetpc fridrfaldv pdslpaaska qgasalpmdr fafardwlth
      121 yagqcvgkqg vdlivkglsq ailargyitt rvlvpeqdls tgtlklalip gvirhvrfvd
      181 eklrgtwkta fptrdgdvln lrdieqgleq mkrvssqdvt mqiapgnvpg esdvvldvkr
      241 gkpwtvvasi dnsgtratgk lqgnvslgid nplglndifn vgfnqdlefg dkrfgshgwn
      301 afysvpwgyw tgtlsaytst yfqplaavnq tfvasgnmkt vdfrlnrvlm rsqddvfgaq
      361 vrltrrfgds yiegttipss hqnatflefg lndrhyfgss qfdgslayrq glgwlgstds
      421 mfaaeggqty rfkmvvldan lstpfvigtq pfkyvttfhg qytgntvsyl dsitigsryt
      481 vrgfdgetll agsrglywrn elqvpiaqtg laayagldyg rvwgpepval vgtqlagavi
      541 gvkgsvatrf gayaydlfag tpvykpsgfe tarvtlgfql taqf
//
LOCUS       WP_175998158             304 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia stabilis].
ACCESSION   WP_175998158
VERSION     WP_175998158.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..304
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31691
     Region          38..290
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mssprlsrrh ftiacasasl aactsfgdks rpntaqsqek pvkigialgg gaargfshig
       61 vlkaleargi pveivagtsa gsvvgalyas gmsalqinki aldmdqaais dwalpfrsrg
      121 llqgvalqnf lnktlnnrpi ekmakplgiv atdlqsgqpi lfqqgntgla vrascsvpsv
      181 fepvkignre yvdgglvspv pasyarkmga sfviavdisa rpdgaatnnp iemllqtfti
      241 mgqtiktyel dkyadvvirp nlaamggsdf nqrnaailag eeavarimpe lqrklaaarg
      301 vaaa
//
LOCUS       WP_175998128             330 aa            linear   BCT 11-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Burkholderia stabilis].
ACCESSION   WP_175998128
VERSION     WP_175998128.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..330
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=35032
     Region          <9..324
                     /region_name="FAD_binding_2"
                     /note="FAD binding domain; cl46878"
                     /db_xref="CDD:481218"
     Site            order(34..35,38,41..42,66..67,70,73..74,97..98,101,
                     104..105,108,128..129,132,135..136,159..160,163,166)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          48..74
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          79..109
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          113..136
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          140..166
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          174..199
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          206..236
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          299..325
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mivsspavpl pgaldpdhda lvarlaapda svrriallel adledpdlvp sfvaalhddp
       61 sadvrgeaar vlgaweqpdv vdalcralld pdddvratva qslselkdat sgtvlcgwae
      121 rpepfvrgav lrglrelrdp dafapalral dadtstvrae avavlgwlrd rralsplari
      181 vtadvdadvr rvavgalgfa tpddttvita llaalrdaew qvreesagtl gklrvalard
      241 plvaaldddy wqvrlravra lgqlrdavaa pavaallaht isnlrkeaal algelrdagt
      301 lpalhdaled rdpevrkavr iairqigetq
//
LOCUS       WP_175998176             262 aa            linear   BCT 11-JAN-2025
DEFINITION  TatD family hydrolase [Burkholderia stabilis].
ACCESSION   WP_175998176
VERSION     WP_175998176.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..262
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28675
     Region          2..247
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mwidthchld aaefdadrda vaqaahaagv srivipsigr dnfttvrela hrtpgavyal
       61 gihpmytpha rdedldrlrm eieaslddpr fvaigeigld yfvpgldedr qqffylgqlk
      121 larefdlpvl chvrksqdrv laglrrfgvr rgiahafngs fqqadaylah gmhlgfggnv
      181 tfaralqirr latelpldai vvetdapdia pewayksrnt pdqvprigdv laelrgldag
      241 tvslcttana laalprlals sa
//
LOCUS       WP_175998235             328 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175998235
VERSION     WP_175998235.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..328
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=36293
     Region          24..82
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          114..315
                     /region_name="PBP2_DntR_NahR_LinR_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators that are involved in
                     the catabolism of dinitrotoluene, naphthalene and
                     gamma-hexachlorohexane; contains the type 2 periplasmic
                     binding fold; cd08459"
                     /db_xref="CDD:176148"
     Site            order(120,122..123,127,185,223,291)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176148"
     Site            order(121,124..125,128..129,132..133,135..136,139..140,
                     142..146,148,212,240..244,247..248,251..252,255,270)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 miacinnisi icimkmahdd dfdlnllmvl dallreqhlt raaselglsq sgmshalarl
       61 refyddplfi rsangmqpta ralelaapva salgtirhqv lsrahfdpkt anrtftlclt
      121 dlgeiaflpe lmshfqreap nctlrsihvp saelaqtles gaadlaigar snvsdqlyqq
      181 llftqpfvtl astrntrvsg dtltldlfth sqhiavdlgd plheafdqvi eaagierrif
      241 lrtphflsvp lllernpcml atvpralgvl fsrygnvkvf appvtlpema lrqywhiryh
      301 rdaanlwlrg tikelyggng qyvgelag
//
LOCUS       WP_175998250             264 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175998250
VERSION     WP_175998250.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..264
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28392
     Region          12..256
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mekeresaae draggiqvia rtakilnalg dtpdgmslae iakavdlprs tvqrivsals
       61 qeniiqadrs dgvrlgpall rlvarvhtdv vsivtpyleq lsrevdetvt laringrgla
      121 fvhvvvaehi lrvmppvggd lpmhstsggr allamhsdse vkallgqhyk rltdrtvhsi
      181 tellaiveea rklgyawesd etvhgvssla faidtilgry avsivlptar aaekrarvae
      241 calrtkeala aeighplepn essr
//
LOCUS       WP_175998258             135 aa            linear   BCT 11-JAN-2025
DEFINITION  PaaI family thioesterase [Burkholderia stabilis].
ACCESSION   WP_175998258
VERSION     WP_175998258.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..135
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14276
     Region          5..135
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mddfavremm nrllppwarl yglvpvsiss sgialrlpys sglchlddai snqvlatvad
       61 vamiiavsva igevrpmspv ymnahyvrri rsgsvlvsah msrlltstga gevemldasg
      121 svavhataty tmraa
//
LOCUS       WP_175998268             252 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease [Burkholderia stabilis].
ACCESSION   WP_175998268
VERSION     WP_175998268.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..252
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27953
     Region          <8..53
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mrnkgfknkt cvycgresvs etadhviare ffreherdnl pkvpacticn naksqlehyv
       61 lsvlpmggvh pdaaativdq varrigknek lrrrlavgqr vrlvrgpdgv wregmaipfe
      121 geklaalacy ialglawhhw qiqiaphava sarifsatgt qdfegmwati paehrisqvy
      181 erdviayrgg yiatnknvtl wqirffggve lgdskqaget artmfvatnd evswiarhse
      241 rapgclapis vd
//
LOCUS       WP_175998299             194 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Burkholderia stabilis].
ACCESSION   WP_175998299
VERSION     WP_175998299.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..194
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22255
     Region          18..185
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mespptsrtm tdpdrditai vtrertrlvs firrrirdpd daedilqdvf hefvqayrlp
       61 apieqvsawl fraarnrivd rfrkkkeqpl tdlfeaddea nseyrldlal pahdagpeal
      121 yartlllkal qdaldelpan qrevfvahel dgqsfkemaa qsgvaintll arkryavlhl
      181 rarlqliyde ldnt
//
LOCUS       WP_175998330             388 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia stabilis].
ACCESSION   WP_175998330
VERSION     WP_175998330.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..388
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42177
     Region          1..386
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mqfdltddqr aiesaiekic arfgddywle rdraggfpad fhaalaeagw lgiamdpahg
       61 gaglgmteaa lmmrtisasg aglsgasavh mnifglnpvq vfgndtqkar flppliagrd
      121 kacfavtepd agldtthlst qarrdgnhyv lsgrkiwist aqvankmlii arttpldqva
      181 kptdglslfy tdldrsrvev reiekmgrka vdsnmlfidn lrvsrddlig negegfryll
      241 hglnperili aaeaiglgqa alrratqyac ervvfgrpig qnqsiqhpla qawmqleaaw
      301 lmvmkaatry dagqscgaea naakylgaea afqacqtava thggmgyake yhverylrec
      361 miprlapvsp qlilcyiaek vlglpksy
//
LOCUS       WP_175998310             289 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia stabilis].
ACCESSION   WP_175998310
VERSION     WP_175998310.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 289)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 289)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 289)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..289
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30742
     Region          5..287
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mstlaastpr dakawlvtpa lafivalfiy pfayglvlsf qpmngggala nyvqfftdta
       61 mwptvlvtlk laapatlinv gisvpvafal rrhspyqkfv ttllvipvtl gtvlvadgml
      121 tyfgpngwfp qalqglhlyt devrlthnyw gvllslivsg fpfafllmls yisgidptla
      181 raaatlganp wqqfrqiylp llvpgltmaa clsfvqafsv fpsavllgap agptrvisia
      241 aaeaafesyd yslasaiaiv mgfvqllvva smlgarrffy tgavtggkg
//
LOCUS       WP_175998343             753 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia stabilis].
ACCESSION   WP_175998343
VERSION     WP_175998343.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..753
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81419
     Region          70..753
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mkkveqrkme watgtrlrai aaaasvafga aagqayaqta pavnagaats assaqngaaa
       61 nasasaqngt lpainvnaas agdgtvglva krsrtgtktd tpineipqti nivtaqqiem
      121 tgatdvnaal ryvpgfssyg sdnrsdwyaa lrgftptayv nglqvpntin laswrvdpym
      181 idsisvlrgp tsvlygagdp gaiidvqtkl adgervreag vqignyarkq fmidvgdkld
      241 pdgkyayrfv gvardgnalt gpnndqrval apsfrwrpna dtsltlsaty lqdwgdissn
      301 flpavgtvlp npngqinkdv yegdpnfnyy rkkqwsvgyq fernltqawt frqnvrlmhl
      361 sldngsvfgn gfvdgsttdv srwagvfqmn ysrfdidnnv egrfatgplq htlllgfqyn
      421 rqtatdsewl aaapplniyn pvylpvttav fdpastfrtn tytamntfgl yaqdqikwnr
      481 wtltlggred wvnmrqddra ggtstkanvt aftgrvglty qgdyglspyi syatsfnpli
      541 gvnllggglp qptrgkqiea glrwqppgkn lmlnaaiyqi nqtngitpal psqddtgtks
      601 vqtgeirsrg ielsatgkvt pnlsliasyv yqdvknvkan dvslnnwpvd iprprqmasm
      661 wadwtwhtgp lagfglgggv ryqsasagaa dnsltvssvt lfdagvhydt rnwrfavngt
      721 nlanrhyisg cqsynvcvfg tdrtviatak ynw
//
LOCUS       WP_175998344             341 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia stabilis].
ACCESSION   WP_175998344
VERSION     WP_175998344.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..341
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37165
     Region          180..320
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mlaevrpdgf tmldtyrlaf adglvaardg teirvaqgdg isaqllraql addgtlrlva
       61 ynhraaavdq rrallaalaa afsdgahhav irldpaawpa valdalrasg vladggrcmr
      121 dgwaqqadmw lvgthlpcat lpmltdgrrh prrppaprgd vyardlpalg vrftlrgwqp
      181 gddaervarw fdaprvrdgw pgaqpgadga apdadphvtp lvgcfdgepf ayfeafwlke
      241 dalaphvaar dydrglrmlv geprwrgphc vagwlpcvvh ylflddprte avgcavpagh
      301 arvadhlarh gfarqrrlal adaqplwmrt lretffsgrh v
//
LOCUS       WP_175998418             137 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175998418
VERSION     WP_175998418.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..137
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15361
     Region          19..100
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(20..22,36,53..55)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mtttvekvvl ppipakryft igevselcgv kphvlryweq eftqlrpvkr rgnrryyqhh
       61 evllirrire llyeqgftin garnrldspg garaaavpde hevqavdara agkpgatvdv
      121 valrqalldv ldglkhd
//
LOCUS       WP_175998421             557 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Burkholderia stabilis].
ACCESSION   WP_175998421
VERSION     WP_175998421.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60496
     Region          25..384
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          453..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mtpaslieqy gpresmeydv vivgggpagl saairlkqla aekgteigvc vlekgseiga
       61 hilsgavmdp rainelfpdw kergapldve vtedrflfls eksavttpnw alpanfqnhg
      121 nyvislgnvt rwlgaqaeal gveifpgfpa aeilynddgs vkgvatgnmg vgkdgepten
      181 fqlgmelhak ytlfaegcrg hlgrqliskf kldanadpqa ygigikelwe idpakhkpgl
      241 vihtagwplk sdtyggsfly hmdnnqvvvg fvvglgytnp ylspfeefqr ykthpsiraf
      301 leggkrvsyg araitaggll slpktvfpgg aligddagfl nasrikgsha aiktgmlaad
      361 aafdavqagr qsdelnaypd afkqswlyte lyrarnfkqw makglylgtl mvgleqkvmg
      421 gnvpwtlrhk hadhemlkpa sqcepieypk pdgkltfdrl ssvfisntnh eenqpahltl
      481 kdanvpvnvn lhtyagpegr fcpaavyefv knddgsdrlv inaqncvhck tcdikdptqn
      541 ivwvtpeggg gpnypnm
//
LOCUS       WP_175998448             461 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia stabilis].
ACCESSION   WP_175998448
VERSION     WP_175998448.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..461
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=49801
     Region          92..452
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mkprqptaga farswlhltg alalattlat lagcdgqpga gtppaqaasa asaphaakmd
       61 asatvfasaa vvatnqpqtr aqvyegvrrm talgkqlffd ptlsgsgkla caschspeha
      121 fgppnalavq fggddmkrag fravpslkyl qgvpqftehf hdsddegdes vdagptgglt
      181 wdgrvdtgae qaripltspf emnsspakva qavkaapyad efravfgvkv ldddaatfka
      241 vlraletfeq tpelfspyts kydaylagha qltpaelrgl qlfndekkgn caschisqra
      301 ldgtppqfsd fgliaiavpr nralpvnrdp rfydlgacgp ertdlkgrde fcglfrtpsl
      361 rnvalrktff hngvyhsled vmrfyverdi hpekfypvvh gkaqiyddlp krywpninre
      421 ppfdrkrgeq palnaaeikd viaflgtltd gyqpgstqaa r
//
LOCUS       WP_175998452             151 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia stabilis].
ACCESSION   WP_175998452
VERSION     WP_175998452.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..151
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15773
     Region          22..139
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mavptrsggf gnpawirall sqpwvlplvr lalvsaylig gvakaldfdg avaeqahfgl
       61 hpaalwaala iaveiagslc vvlrrftwlg agslgmltlv ammvandfwn htgaerfmal
      121 nsffehlgli aalvlatvla dakhpagdsr a
//
LOCUS       WP_175998455             130 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Burkholderia stabilis].
ACCESSION   WP_175998455
VERSION     WP_175998455.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..130
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=13701
     Region          14..129
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mselsveasi gsvdylvhfs dgvhqwrade paplgggdaa ptpvalllss lgactaitlk
       61 myaqrkgwpl aevhvklahe sgnagstivr ritlegdlss eqrerllqia nacpvhkilt
      121 hpitidtaia
//
LOCUS       WP_175998485             258 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia stabilis].
ACCESSION   WP_175998485
VERSION     WP_175998485.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 258)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..258
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27752
     Region          4..254
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mthmleidrv swspggaiav ldsvtlsvaa gefvglvgpn gsgktsllrc vfryarpgag
       61 svaldaqdvw rmrpravaqr iavlqqetpd dfgltvdelv gmgrtphkra fdaesaddrr
      121 ivdsalqdvg laarraqrfa slsggekqra llaralaqqp elllldeptn hldlrhqlel
      181 larvrrlgia tlatihdlnl aaaycdrlhv lshgrivasg asadvlteal lrdvfgvaal
      241 vdrhpvtgrp ritplhpe
//
LOCUS       WP_175998487             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175998487
VERSION     WP_175998487.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34015
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdkwtqieff vqvaelgsls kaaerlgmss aaasrclnal eerlaarlve rttrrlwltd
       61 agheyhrrcv ailtemaead aavneasvnp agtlrvtasv sfasiyiapa lpefhrrypn
      121 lnvqivaanr ypdfieagid vairtrehea dsgitvrrla etrrvlaasp gylakhgapa
      181 tpdalcdhql lvynlandpy vlhfrhgakk qsitiksvld anegqviraa alaglgiliq
      241 plyiihddiv agklvpvltd wqlpaltvni ayqsrrhqpa kirvftefli erferlglar
      301 kwkevsr
//
LOCUS       WP_175998494             178 aa            linear   BCT 11-JAN-2025
DEFINITION  PadR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175998494
VERSION     WP_175998494.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..178
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20368
     Region          1..84
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          91..174
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 mslphallta laerpgsgse ladrfdrsig yfwqathqqi yrelgrleet gwieslpaes
       61 grgrkrayri lpagkkelrr wiaeqedptp lrealmvrlr aeavlgpagl edeirrrial
      121 hqekldlylq ieardfsees asrakrlqhl vlqagianer fwvefsqdal dtlrlpkd
//
LOCUS       WP_175998495             138 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia stabilis].
ACCESSION   WP_175998495
VERSION     WP_175998495.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..138
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14416
     Region          6..129
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mdrykylpll griligapfl msglsklaah attvgyiasv glpapslafv vavlveaggg
       61 llllsgyrar pvalamalfs lvtavffhhn fadqnqmihf lknvmmaggl lqiayfgaga
      121 fsldarigrt alriapaa
//
LOCUS       WP_175998496             326 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH:quinone oxidoreductase family protein [Burkholderia
            stabilis].
ACCESSION   WP_175998496
VERSION     WP_175998496.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Shimomura,Y., Kakuta,Y. and Fukuyama,K.
  TITLE     Crystal structures of the quinone oxidoreductase from Thermus
            thermophilus HB8 and its complex with NADPH: implication for NADPH
            and substrate recognition
  JOURNAL   J Bacteriol 185 (14), 4211-4218 (2003)
   PUBMED   12837796
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169523
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..326
                     /product="NADPH:quinone oxidoreductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=33866
     Region          1..322
                     /region_name="QOR1"
                     /note="Quinone oxidoreductase (QOR); cd08241"
                     /db_xref="CDD:176203"
     Site            order(40..41,122,126,147,150..152,171..172,176,191,215,
                     237..238,240..241,262..264,314,316,318)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176203"
ORIGIN      
        1 mkallctafg pidslriedv aipepaagqv rvqvkaasln fpdalivqgl yqvkpalpfs
       61 pgaefagvid avgegvtawr pgdsvvaftg hggfaqqcva dahqiaalpp gmtfeqgaal
      121 vlaygtslha lqqrarlqsg etllvlgaag gvglaaieia kalgarviaa assadklalc
      181 rdagadetid yvtedlrrrv deltggrgad vvydpvggay teaalrataw rgrflvvgfa
      241 ageipkialn lallkerdil gvfwgdavrr dpaqhranmq qlaewfaagk vrpaitehvp
      301 lagaadaiar manrqvkgkv vilpda
//
LOCUS       WP_175998520             156 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia stabilis].
ACCESSION   WP_175998520
VERSION     WP_175998520.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 156)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..156
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17014
     Region          1..153
                     /region_name="MutT"
                     /note="8-oxo-dGTP pyrophosphatase MutT and related
                     house-cleaning NTP pyrophosphohydrolases, NUDIX family
                     [Defense mechanisms]; COG0494"
                     /db_xref="CDD:440260"
ORIGIN      
        1 mkrggaprtv scgvvildaa grvflahatd tthwdipkgq gepgetpada alrelleetg
       61 iefaqarlld lgrfayrhdk dlhlfavqva dgeidpahct ctslfpsrrd gsmipemday
      121 rwtvpgdida yasrslarlf rtklsladlh rrlsgv
//
LOCUS       WP_175998503             539 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA synthetase [Burkholderia stabilis].
ACCESSION   WP_175998503
VERSION     WP_175998503.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..539
                     /product="acyl-CoA synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016405 - CoA-ligase activity [Evidence
                     IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57604
     Region          48..538
                     /region_name="MACS_like_3"
                     /note="Uncharacterized subfamily of medium-chain acyl-CoA
                     synthetase (MACS); cd05971"
                     /db_xref="CDD:341275"
     Site            order(111,241..243,267,287,289,293,314..317,336..341,
                     344..345,361,421,433,436,442,444..447,476,505,510..511,
                     513,515)
                     /site_type="active"
                     /db_xref="CDD:341275"
     Site            order(192,195..200,202..203)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341275"
     Site            order(237,289..290,293,314,444..446,505,511)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341275"
     Site            order(314..317,336..341,361,421,433,436,442,447)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341275"
ORIGIN      
        1 mlpaadrydd llsrfawdvp arynigvdvc dkwadgsgrl alihetaqgd vsrftfddlr
       61 nasnrlansf araglrrgdr igiflaqgpe taiahlaayk lgaiavplft lfgvdaleyr
      121 lanseaaalv tdaagyakia plhaqlpalr tvycvgddap dapgvlryda alaaespefv
      181 padtaaddpa viiytsgttg kpkgalhahr vlpghlpgve msqqcfprda rlfwtpadwa
      241 wigglldvll pswhhgvpvl arrfekfdge aafalmarhg vthaflppta lklmrtvpap
      301 reryalslks vasggeslgt eltawgrdal gvtinefygq tecnmvlssc aalfdaqpga
      361 igkavpghav aivdadgtpl ppgvegriav rrpdpvmfle ywrnpgatrd kfagdylltg
      421 dtgtidadgf vrfvgrdddv itsagyrigp gpiedcllth pavrmaavvg vpdatrteiv
      481 kafvvlnpgy tgddslvral qahvrtrlaa heypraiafv dslpmtatgk ivrralrda
//
LOCUS       WP_175998548             218 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175998548
VERSION     WP_175998548.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..218
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24303
     Region          28..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnedlkayaa pgadqagham kttprrgrkr dgesrerllq aartifaekg yeatsiesia
       61 laagytrgaf ysnfrdktvv llellrrdhe dverelmriv qagndreame ramhayfrqr
      121 yrqpdacvmw meaallsvhd rpfrvqfaaf lnarrdrgsa cagarlplpi elltlgltgl
      181 gddvlpdgas grwhltdawv daavtrvfag cpcdetme
//
LOCUS       WP_175998554             277 aa            linear   BCT 11-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Burkholderia stabilis].
ACCESSION   WP_175998554
VERSION     WP_175998554.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..277
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30480
     Region          1..237
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mddlkrkafa edgavliegv lneeqlarcr lafdwgienp gpmasslldg tefrshvdna
       61 npyakerlde lvatlplgrl fadlwgseha wffaeelflk rggkgarslw hqdtsylpwa
      121 gmhfgnawis feavpkrnal eivrgshrgv rhdgttfqnv ddpteplhgg gvwprmpdie
      181 aerradpgky diiswatkpg dvlllhpgvl hgggvvdpaf pdrhtlvlrf fgddatfspl
      241 pdnsasgftp agvlfvdela slkagdpfra pcfrqlv
//
LOCUS       WP_175998580             750 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia stabilis].
ACCESSION   WP_175998580
VERSION     WP_175998580.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..750
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=79934
     Region          50..>203
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          211..744
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mrhsarspqs adlpesaddv aspsrrsflg nlaaltlavg fggeiavaas vnpatarvpf
       61 evnafiriga dgivnvvsey lemgqgtftg vatlaaeeld igldkvrvvp apadvkryan
      121 pmfakmgwki qatggstamt gswtvmreaa asaramllsa aarkwkvdps slrvedgtii
      181 haasgrragy gqfaadaare pvpskvavkq radfrligkr dtrrvdipak vdgsaiytqd
      241 vklpgmlvav iahpprmwgk vrhvdaskak aipgvvavvq vpgddnlqgg vavlarntwv
      301 arqgrdalki twdethalav gsaeiaqryr aaldkpgvia ltrgevasea psggkfidav
      361 yeqpylshap meplncvvhl hadrceiwng eqwhtgdqvi vakevglkpe qvtinqlyag
      421 gsfgrranpv sdyvceaari arlaraqgid apiklvwmre ddmragfyrp atvhrvrlav
      481 dksgnlvswn qnvvgqsffa plpsgvdptl vegsadipyd ipnvkvtqhi qklavktqwm
      541 rsvghthaaf vgetmmdeaa raagkdpytf rrallakqlr hrgvldlvaq kagwstplra
      601 gapgtkrgrg ialqfafgty vaqvaevtvl qdgtftvdri vcavdcgsvv npdivasqve
      661 ggigfgltfl raaitlengr vqqgnfndyp vlrmngmprv evhtvpsqea psgigepgvp
      721 paapavanal taatgttfrs lpmrgtlrpa
//
LOCUS       WP_175998586             297 aa            linear   BCT 11-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Burkholderia
            stabilis].
ACCESSION   WP_175998586
VERSION     WP_175998586.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..297
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=30977
     Region          70..276
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 makrslaala acmlistval dalvvpqqaf aeasgpvava atasapqaaa depspppapa
       61 atkavenpyg lgalwkngdf varfvlillv imsmgswyim iakfleqfra nrrakladeq
      121 lwsapslsag aslldeaspf rfiaetaiea gehhdealle avdrntwidv sveraitnvs
      181 nrlqdglafl atvgstapfv glfgtvwgiy haltaigiag qasidkvagp vgealimtai
      241 glavavpavl gynflvrrnk svmervrnfg aqlhtvllag skrpvraaga ptaslvh
//
LOCUS       WP_175998597             434 aa            linear   BCT 11-JAN-2025
DEFINITION  replication-associated recombination protein A [Burkholderia
            stabilis].
ACCESSION   WP_175998597
VERSION     WP_175998597.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..434
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=47391
     Region          1..432
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 msdlfhtdpr rplaealrpt tladvigqsh llgegkplwr afesgkphsm ilwgppgvgk
       61 ttlarltaqa fdcefivlsa vlgsmkdira amaraqdare rngrrtilfv deihrfnkgq
      121 qeallpfvqs glvtligatt enpsfevsra llshaqvhvl tpltddelrr lferargtvp
      181 gelafdgqav dtlisyadgd arrllnlleq awsaataadv ttidaafvtg altvgarrfd
      241 kggenfydqi salhksvrgs npdaalywlc rmldggcdrk ylarrivaia wddigladpr
      301 glrmanaave acerlgapdg dlalaqavly lacaaksnag gmafmqaraf vrqdlprnvp
      361 qhlrdapaqv lralghtyrd phdephgyaa getylpdgmy ephwyqpvpr gveariaerl
      421 awlgtldrga grrd
//
LOCUS       WP_175998600            1058 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia stabilis].
ACCESSION   WP_175998600
VERSION     WP_175998600.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..1058
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113437
     Region          1..1041
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mdfskffidr pifavvlsii ifaigliaip mlptgeypev vppsvvvrat ypganpkeia
       61 esvaepleea ingvegimym ksvagsdgsl qvvvtfmpsv dadtaavrvq nrvsqalsrl
      121 pdevrqygvt tqkqsptplm yiglispdgs rdplylrnyl tlhvkdelsr ipgigdvslh
      181 gsgdyamriw ldpnrlasrg ltagdviaav reqnvqvsag qlgaepspka tdflmsinvr
      241 grlrttqefg divlkngadg qvvklsdvar ielgagdytl rahldqsdaa tvgiflapga
      301 nalavakavy akldelakrf ppgltykpmw dptvfvresi ravqhtliea vvlvvlvvil
      361 flqtwrasii plvavpvsvv gtfawllllg ysintltlfg lvlaigivvd daivvvenve
      421 rnieqglspr daahqamkev sgpiiaialv lcavfvpmaf lsgvtgqfyk qfavtiaist
      481 visainsltl spalaakllr phdappdals rvlerlfgrl frgfnrfflr ssdryhgvvg
      541 rtfqrrgavf vvyvgllaat allfktvpgg fipiqdklyl fagaklpega slsrtdavvr
      601 qmvkiahete gvemmpafag mnalqvvntp nitssyillk pfdqrkrsaa qinadlnarf
      661 agikggfaya lmpppiqglg ngsgyalyle draglgygvl qnavnafqva vaktpgmhyp
      721 vstyqsnipq levkvdrlka kaqgvaltdl fealqvylgs vyvndfnvfg rvyrvmaqad
      781 aahrqsvedi anlrvrnang emvpigsmvt vtptfgpdpv vryngypaag ligeadpavl
      841 ssaqaiaklq qiakdvlppg itlewtdlsy qqvtqsnaai vvfplavmlv flvlaalyes
      901 wtlplavili vpvcmaaalf gvwlsggdnn vfvqvglvvl mglacknail ivefarelei
      961 hgkgiveaal eacrlrlrpi vmtsvafiag svplmigsga gsevraatgv tvfagmlgvt
     1021 lfglfltpvf yvvirtlagg rqstawveqp vtlegelq
//
LOCUS       WP_175998603             519 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia stabilis].
ACCESSION   WP_175998603
VERSION     WP_175998603.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..519
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53801
     Region          16..465
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,142,
                     145..146,149,273,276..277,280..282,285,313,317,371..372,
                     376,380,396,399..400,403..404,407)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msvdvslknk ialaaiclsa vmlgleitsv psilptlehv lpadfkqlqw imnaytiamc
       61 sslvamgala drfgrkrvft igivvfgias licglassap lliaarflqg vsaaamlscq
      121 vavlshqfqg gpergvafaw wgvvfglglg fgpivgglia sfanwewvfl ihvliavlav
      181 slaragvves sdphalkidi ggmatlslav fclvylitqg qkpeagnpvg mgalaiavvs
      241 filfvvvenr varpmfdfka frvrnfsgal lgacgmnfsf wpfviyfpiy lqavlgyssv
      301 aagltvlayt lptvvvppva erlllkrgpn fvipvglfti aagfllihlv ataghaswit
      361 llpgclvagi glgltntpvt ntatgslppe ragmasgmef sarmislain iaimgfvlvk
      421 gvsagvadal palaqsrhlv davsagnfva adaggipvav graaltrgfg wvtlygtiap
      481 lllgfaaaiv fgrkkpapva tndersgadd kqpaltsid
//
LOCUS       WP_175998626             700 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia stabilis].
ACCESSION   WP_175998626
VERSION     WP_175998626.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..700
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73132
     Region          38..689
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mhdaadqtst vaaspgrlsr aaaallarid iftprgayva rsviaaalal gvayllelet
       61 pysaastvll vinpvqgavi gkgvwrvvgt vagmvvafvl mgcfaqkpll filgfafwlg
      121 tcvagmtllr hfrasgtvva gytiglatyg amqhpeltfe hvigrgstva vgvlclslvs
      181 mllgtrdvhv klealvtrvt advarviaaq rnglaaapgd dkrhalfagi ygiddllalg
      241 kaesedlaqr aaavrhgmas lfgalaggmp plpadspgar aiaplqprla aaweaaadal
      301 rdgrggatqa fgllgdardh lrdaldgial gdprddaall iagerlieqi ddyraaldgl
      361 velqrprprs rpapvrfhrd tgaavrngvr sacaivisga fwlatgwdqg dmmllvvapy
      421 callatagnp aagaqafikg tilavpaafv cafgilphle gfpllvvala lfwmpgiyat
      481 svprtalagl aylvafntlt aatnpwhpdv alflnqsvaw vlatfltlls frlilprnla
      541 tdaarlrrti rddalalvag krataagwqq rqqhriaqlg allagqpaam tqasiealaa
      601 lhvgkellri rrgtardglp dvakqcarag laglarhaaa paraarharr aahtlaglaa
      661 aqpgnpelkr lmaafadvhv llhtyaayft avpepardaq
//
LOCUS       WP_175998643             461 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia stabilis].
ACCESSION   WP_175998643
VERSION     WP_175998643.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..461
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48287
     Region          16..449
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,141,
                     144..145,148,275,278..279,282..284,287,315,319,371..372,
                     376,380,396,399..400,403..404,407)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mhrsprrarw lalagvaias flgcidftiv ntaipdirsa fevgidqvqw vvtafvials
       61 sctipvgqla drhgrrrvml asmavfggas lgaglasglv alvlwrvvqg iacaglytas
      121 aalvatmfpe sergkalgll fsvnglglal gpvaggllvd algwrwiflv nvplivtsfl
      181 lcagrltqda aapmqrrarf dwpgvalllt ilpcglvavv rggewgwtsp atlglllval
      241 lsaaaltrve rhaaapllql alfrqrpfvl avcataglaf fycaaflfmp lylgelrgqd
      301 saatgwlllp ttavmamvsp pagrgydrfg avaimalgfv allvsalmqa tfgattawww
      361 vlagfacmgf gwgcvlgpsl taalaavpea lagtalgmat mvhnvggsmg laaatvlyrf
      421 satpdggfit gyrsvmlmlv ivcivvlwil avehrrdlra r
//
LOCUS       WP_175998670             323 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175998670
VERSION     WP_175998670.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..323
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35698
     Region          38..190
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <186..313
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 msieppaapp pslsprnrkr lvallrtlap degynltalp svrilrsnra lsrtpvlydp
       61 givivcqgck rgyfggeryl ydehhylavs vpvpfsmetd atperpllal ylhldftmaa
      121 elaaqidreg vaehvqaprs mmstpmdeam hasvlrfvea mrqpleaavl gpallrelyf
      181 rvltgaqgsa mrsalamrgq fgrigrslrv ihadyaqpld vpllageagm svpsfhshfk
      241 aitqvspmqy lkstrlhqar llmvrqdlta eaagyavgyt spsqfsrefk rlfgltpake
      301 tqrmresfsi peafedatfv ssh
//
LOCUS       WP_175998687             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia stabilis].
ACCESSION   WP_175998687
VERSION     WP_175998687.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..359
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38545
     Region          1..359
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masvslkqir kryddgadvi kdvsldiedg efmvfvgpsg cgkstmlrml agleeitsgd
       61 llidgrrvnd vpaakrglam vfqnyalyph mtvfenmafg lkltgvdaae trarvgqaae
      121 alrlsaller kpkalsggqr qrvaigraiv rkpgvflfde plsnldaalr ggmrlelarl
      181 hrelgstmiy vthdqveamt lgdriavfng grieqvgspl slyeqpanhf vasflgspsm
      241 nflpcrahvg adamrfdvpg gslaatpdas rawpsgslql girpenvavg apgtgldgrv
      301 thaehlgdat ivyvelaghd rplsvrqnrd aytvaagqpv gvrfdmrhah ffddagral
//
LOCUS       WP_175998693             159 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia stabilis].
ACCESSION   WP_175998693
VERSION     WP_175998693.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..159
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16804
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 myekimvavd gsasskqala eavkvalagd ahvsvvyvvd ksvlftyagr idphalveei
       61 rddgrkvlre agqiialaga kgeaeliete sigediaerl qryvkergid lavvgthgrr
      121 girrvllgsv aerfvrgskc pvllirgdda depaaaaaa
//
LOCUS       WP_175998781             288 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175998781
VERSION     WP_175998781.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..288
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31520
     Region          <148..282
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <217..280
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 msaspesppp arphdawlaa apslvdalge psfmatlddv lsrivefdlt cvlmyehaha
       61 plllhdnlkn vsepdamrny ltgtylldpv ysacagaiaa glyrmeelap daffdsdyyh
      121 splvhpcism tsgslaeeiv figaptperr vayslmrsng rarftdgdva alraiqplln
      181 allcrhasat aparpdgqrv eqpeqdvrgy leaafadfat dvltlreqei vslilrghss
      241 lsiahlldia egtvknhrkh ihaklgissq selfhrfveh lfsrrivs
//
LOCUS       WP_175998717             306 aa            linear   BCT 11-JAN-2025
DEFINITION  bestrophin family protein [Burkholderia stabilis].
ACCESSION   WP_175998717
VERSION     WP_175998717.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..306
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34110
     Region          1..304
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 mivrprqnwl rmlfvwngsv lqsiipqlvf maivstlavf tngrifgeki plntapftlf
       61 glalaiflaf rnnasferfk earhlwgnll iaartltsql hrylpdsvdd eqrgrladll
      121 iaftyalkhq lrhtdptedl trilgaerag alarkcfkpv aildelrggi vralgrapgs
      181 ettcwmfetq ldelgksvgg cerilstpip fsysvllhrt vyaycvllpf glvdstefft
      241 plicvfisyt lialeaiane vaepfglapn alaldamtrt iersvlelgn rempeefvpa
      301 ssyqit
//
LOCUS       WP_175998807             499 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Burkholderia stabilis].
ACCESSION   WP_175998807
VERSION     WP_175998807.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..499
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53445
     Region          5..471
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mnlhslnsls avdarrliag rqispvelld aciaqmehvn phvnalaatr fdlarseara
       61 aeqavmrget lgllhglplg vkdleetagm lttygsphfr nnvpshdnal varlraagai
      121 ltaktntpem gagantrnav wgatgnpfaa elnaggssgg savalatdml pvctgsdtgg
      181 slripaalcg vvgfrpspgl vpsdtrllgw spltvagpmg rtvadtrlql aamvglhrge
      241 plgiecdsrs ildaqgidps tlrvgytedf gacdvsndtr qtfrakiaal shhvgvcepv
      301 nfelgevdrc fdvvraqnfi aglkdiyerd pdllgqntra nyemglamsi sdvvwahaeq
      361 trifrrfqpi fddydvivsp tcsvspfpwq qaslteidgr plenyyrwlg vtyvvslvtn
      421 pslslpagtd hadmpfglqf igpqrsdrrv ldiaqaleev fardeslkrp apdiarlmas
      481 haalksivtd ppddsvayr
//
LOCUS       WP_175998836             441 aa            linear   BCT 11-JAN-2025
DEFINITION  leucine-rich repeat-containing protein kinase family protein
            [Burkholderia stabilis].
ACCESSION   WP_175998836
VERSION     WP_175998836.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Johnson,L.N.
  TITLE     The regulation of protein phosphorylation
  JOURNAL   Biochem Soc Trans 37 (Pt 4), 627-641 (2009)
   PUBMED   19614568
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Shen,K., Hines,A.C., Schwarzer,D., Pickin,K.A. and Cole,P.A.
  TITLE     Protein kinase structure and function analysis with chemical tools
  JOURNAL   Biochim Biophys Acta 1754 (1-2), 65-78 (2005)
   PUBMED   16213197
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
REFERENCE   7  (residues 1 to 441)
  AUTHORS   Hanks,S.K. and Hunter,T.
  TITLE     Protein kinases 6. The eukaryotic protein kinase superfamily:
            kinase (catalytic) domain structure and classification
  JOURNAL   FASEB J 9 (8), 576-596 (1995)
   PUBMED   7768349
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..441
                     /product="leucine-rich repeat-containing protein kinase
                     family protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006468 - protein phosphorylation
                     [Evidence IEA]"
                     /calculated_mol_wt=47065
     Region          <9..>186
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          39..61
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          62..81
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          82..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..175
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          214..432
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(214..217,220,222,238,240,269,287..290,345,349..350,
                     352,362..363)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270622"
ORIGIN      
        1 mtstleqlqa ghlsgarqlk lacgltefpr eifdladtle vldltgnalt alpddlprlh
       61 rlrilfasgn rftelpdvlg actqldmigf kanrirtvpr rslpralrwl iltdneidal
      121 paeigacsrl qklmlagnrl ralpaemaac ralelvrlsa nrlddlpdwl lrlprlawla
      181 aagnpfgaap eaaasagpdi vdvewvslac eqklgegasg viyraqwtad grapravavk
      241 lfkgavtsdg lpdcemaacl hagqhpnvip vigkvrghpd gthglvmelv dpaltnlagp
      301 psfatctrdv yaadagfepa aavriahgia svaghlherg imhgdlyahn ilhdgeggal
      361 lgdfgaasly dvndrmrgag ferlevrafg yllgellerc eprawagrha ldvlaaacln
      421 edvdarpsfa eitaalavne i
//
LOCUS       WP_175998857             433 aa            linear   BCT 11-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Burkholderia stabilis].
ACCESSION   WP_175998857
VERSION     WP_175998857.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..433
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46332
     Region          5..431
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 mslnddatfw rnarqhlvry ggtfepmiie raqgsfvyda dgraildfts gqmsavlghs
       61 hpeivsvise yagkldhlfs gmlsrpvvdl atrladitpd gldralllst gaesneaair
      121 maklvtgkye ivgfaqswhg mtgaaasaty sagrkgvgpa avgsfaipap ftyrprfern
      181 gaydylaeld yafdlidrqs sgnlaafiae pilssggiie lpegymaalk rkceergmll
      241 ildeaqtgvg rtgtmfacqr dgvtpdiltl sktlgaglpl aaivtsaaie erahelgylf
      301 ytthvsdplp aavglrvldv vqrdglvara nvmgdrlrrg lldlmekfdc igdvrgrgll
      361 lgveivkdrr tkepadglga kitrecmnlg lsmnivqlpg mggvfriapp ltvseaeidl
      421 glsllgqaie rav
//
LOCUS       WP_175998890             955 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            stabilis].
ACCESSION   WP_175998890
VERSION     WP_175998890.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 955)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 955)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..955
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..955
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=102340
     Region          77..828
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mlnplagqla sgamsglqga tasalpaasa aasadaapsv ddhplagqpl sdlasapqff
       61 mpgqtpaqpg thasvlpfse ttrllrlqss ltgnralsia aikggealse mprytldlit
      121 qnpsidlkdv lnqavtvnia lqdgserqih gylvrfgfer ndggiahyrg elvpwlwylg
      181 krvnsriyqq vtvldvlrkv fadygalvdy qthikqepkp edyvvqfqes dlnfvsrlle
      241 rhglfyyfey rqdghtlvia ddsascpdqa hdpvvtynaa sgvqqadrlt alsasretqp
      301 gvvalhtfdy khpksrpyve lptladqgna pklevydgss afaykdtsdg eaeakrrlev
      361 fewqakvfrg esgcrgltvg rkfkidghfw fdpakqddnq flvvgleida knnfddasaq
      421 pgsfrntltl irskipyrpv rrhdkpvmpg pqsaivvgpk gqeihtdgmg rikvhfpwdr
      481 ygkndqessc wirvsqpwag rgwgtvaipr vnqevivdfl ngdpdrpiiv grmfnaeqtp
      541 pyalpdgahq mgfhsnstpg gggfcevvih dkkgeelvni hsqkdmattv qnnhvtvvng
      601 pnqtnvvtqg qhasivrkai svqsqdehiq htaktavilh aqeqhmalka kgpvqiesdt
      661 qhvhvkgsqs ivlecgkaki tlsangeivl dgtrvvvlgs qsvdlnpdga tgpaspplvp
      721 vtdpaapaqd laapaagggg gggggggaaa apahgkkhak gapkkavatg lgagvdqlaa
      781 ksptlerdia klqkdgwhiq ygpanqgsst nksgqpptiv idgsergnpq avvqglahet
      841 ghalyqgvpd ystktnyvns eladegaatm nnikvqreiv thggpdihia gdpanapayn
      901 aaynqfvqng danaaraaig hvygtgehas vpvngqyvny qtyygswydr nypsh
//
LOCUS       WP_175998898             322 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia stabilis].
ACCESSION   WP_175998898
VERSION     WP_175998898.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..322
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33999
     Region          80..297
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mlepeiaafv tavdawypad aaarsaaeqr rlydrfaaew tpaalppgiv qqdavwhapd
       61 graialrryt asygaprgtv lffhgggfvv gsldshalit aqlaadtgld viavdyrlap
      121 ehrapaaldd clavtravrd trgpfgpcvh pltlagdsag gmlaaavata lrdageggid
      181 gialvypmlg fepqsparet eahapmltld dvhryralyw dgpldsdasd alldgnpllr
      241 asvpleaarf dglppvlaig aehdplrdda rvyveriraa ggaahywmge glvhgcwral
      301 gtspqaarlh rmvggfllap ha
//
LOCUS       WP_175998929             388 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Burkholderia stabilis].
ACCESSION   WP_175998929
VERSION     WP_175998929.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..388
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39811
     Region          60..368
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mntikridpr rpfiitaagl kritlgeegs adasaahwsa hghaaaaklp ravqdpkhvm
       61 lvvahserga lddharqaia aaalladsht evallafgel kddvaelgvd klvelagfdr
      121 rafdpeselq alqacvaala pkhvfvpdna tgdgdlgrry aaaagasvat nvveidakhv
      181 gayaqagraf atrglpdvil laqnavdakl pfvgagerla adfirpagda aqpyrdlgle
      241 eidaaqvale eadfivsagn gvsdigafer lagafgaaig asrvavdngh ftrdkqvgat
      301 gktveasvyi afgisgavqh lqgikdcrhv iavnldgsap iakranltvv gdaqatiaal
      361 ieqvqaaraa rgqspasvga repegvaa
//
LOCUS       WP_175999031             441 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia stabilis].
ACCESSION   WP_175999031
VERSION     WP_175999031.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46713
     Region          9..414
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(22..23,26..27,30,69,127..128,130..132,135,155,
                     158..159,162,243,246..247,250..252,255,283,287,339..340,
                     344,348,364,367..368,371..372,375)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mgtsvkqpkr aalasfvgtt iewydfysya taaaivfgpl ffpgenrfis llasfgsfav
       61 gffarplggv mfgylgdrfg rkrsllatlm lmavstvaig llpthaqagv iapillvlmr
      121 vlqgiavgge wggavllage hapegkrtff asfaqlgsas glilsmlafg aistlskddm
      181 mswgwrvpfl assvllvigf virasvsesp efeeikksgn taqnpvreal kywpllllai
      241 ganvygiagv yfsnifmisy atqflsldrs mvlhcmtiva vlqfvvqlaa aflaqrfgtt
      301 rvllitgawa aivpfvmlpl vhvgtplsvt vgvglatlae sgyysvvagf vsgifiarir
      361 ytaisiayqv cgalaggltp lvatiiaqnt apqwwplaiq ytsaallssl cvwlisrrvs
      421 iddagapgkq daplprgart a
//
LOCUS       WP_175998969             355 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia stabilis].
ACCESSION   WP_175998969
VERSION     WP_175998969.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..355
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38135
     Region          3..332
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,226,287,308,310..312)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,174,177,179,226,233,287,308,
                     310..311)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,174,177,179,311)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            179
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mdalftparv grytlqnrlv mapmtrsraa fdgtpgelaa eyyaqraglg livtegtqps
       61 ddgqgylttp giytdahvag wktvsdrvha rggrlfiqlm hvgrmshpdn tphhrqgvap
      121 saiapgvpmf tlkgmqeipa pralttaevr dtvndfrfaa rraieagadg veihgangyl
      181 vqqffapnan trsdayggsi enrtrfaiev aeaivdeiga drtairlspg salwgidega
      241 qgpdlyrhla tqldrlglay lhvmhqgdep lladlrerws gtlivnrpgr trdaigtdva
      301 tgiadleayg qmvlanpdfv trlrtgapmn daqhatffgg dargyvdypa lsgaa
//
LOCUS       WP_175999057             136 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Burkholderia stabilis].
ACCESSION   WP_175999057
VERSION     WP_175999057.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..136
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=14843
     Region          32..134
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mytnptlaer htsavhpaaa eaarrpvvtp avdivedarg vtlqadlpgv prenldvkvh
       61 dntltieadt ridtpadlrv ryaearapry artfvlspdl dtskidanlr dgvltltipr
      121 reetrprrid vtagna
//
LOCUS       WP_175999074             437 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrolipoamide acetyltransferase family protein [Burkholderia
            stabilis].
ACCESSION   WP_175999074
VERSION     WP_175999074.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..437
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46910
     Region          2..437
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mgihvikmpd igegiaevel vawhvevgqt ikedqpladv mtdkaaveip spvtgkviel
       61 ggrigemmav gselirleve gdgnlkagap vretkvetap vaatpskpaa dvpaekpaap
      121 rdakrapaap hraepaaqpr aalapgerpl aspavrqraw dmgielryvr gsgeagrvlh
      181 edldayarts gsaarpsqah gyderndetd vpviglrrai arkmqeakrr iphfsyveei
      241 dvteleslrt elnrrygdtr gkltplplli ramvialrdf pqinarfdde agvvtrygav
      301 hmgvatqtdg gltvpvlrha eakdvwsisa eiarladavr anraqrdels gstitisslg
      361 alggivstpv inhpevgivg vnriverpmi rdgavvarkm mnlsssfdhr vvdgadaaef
      421 iqavravler pallfve
//
LOCUS       WP_175999090             455 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia stabilis].
ACCESSION   WP_175999090
VERSION     WP_175999090.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..455
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48642
     Region          2..449
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mknlqrhlsa rhirflalgs aigtglfygs ataiqlagpa vilayilgga avymvmralg
       61 emavrepvag sfghyatenl gpfagfvtgw tytlemviva iaditafgiy mgfwfpdvpq
      121 wiwvlgvvai icglnlchvk vfgelefwls iikvgaiiam igggvaillt gmhfghsadv
      181 ptfanlwnhg gflpngvggl iaslsvvifa yggievigms ageakdperv iprainavpa
      241 rillfyvltm vvlmsispwt gvgsdgspfv qifsalgvks aatilnlvvi saaisainsd
      301 ifgagrmmfg marqgqaprv lmttsrhgvp wvtvlvmaga llfgvllnyl mpkdvflmva
      361 aiatfatvwv wlmillsqva mrrrlsstei aalkfkvplw pvapaltiaf mgfvivmlgw
      421 fedtrvalyv gaawlallai vfyarirpkf apasr
//
LOCUS       WP_175999092             257 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia stabilis].
ACCESSION   WP_175999092
VERSION     WP_175999092.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..257
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28031
     Region          1..>240
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mnllelddlc laydtphgrr tvvdglslal prgdigcllg asgcgkttvl raiagfepvr
       61 mgrimldgtp vaapsldvpp errrigmmfq dyalfphlsa adnvafglrr mpkaerrmrv
      121 aemlelvgla dsagayphel sggqqqrval aralapspel llldepfsnl dvdtrerlaf
      181 elrdilkrtg htailvthnq aeafaiadri gvmkdgqlaq wdtpyalhhh paspfvadfv
      241 rrdaladera ralargr
//
LOCUS       WP_175999129             166 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrofolate reductase [Burkholderia stabilis].
ACCESSION   WP_175999129
VERSION     WP_175999129.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11087044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..166
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=18024
     Region          3..163
                     /region_name="DHFR_1"
                     /note="Dihydrofolate reductase; pfam00186"
                     /db_xref="CDD:425512"
     Site            order(7,24,29,59,99,105,118)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(9,16,46..48,66,100..103)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 mttltlivar arngiigrdn qlpwklpedl affkrttmga pivmgrkthe sigrplpgrr
       61 nivvtrdttr rfdgcdtvts ladalalaar dgvpeaflig gaqlyaegll ladklvvtei
      121 dadfdgdasf papdaahwqe vsrdaheaaa pntfgyafvv yerkrd
//
LOCUS       WP_175999175             782 aa            linear   BCT 11-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Burkholderia stabilis].
ACCESSION   WP_175999175
VERSION     WP_175999175.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 782)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18771781
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..782
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=84437
     Region          19..133
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Site            order(30..31,33,57,60..61,64..65,67..68,91,94..95,98..99,
                     102)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          55..85
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          181..757
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          214..240
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          248..274
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(250..251,254..255,257,281,284..285,288..289,
                     291..292,315,318..319,322..323,326)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          279..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..342
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mlsfelsasa tltpeqqlaq dialvldnal erqragafdd aralyeaild ampahgdahy
       61 nlavlladtg raadavphfe aalgvspdng yywvsyihal hrsgqtaaaw iaveiaqqrg
      121 vhgpalnsli aqlaspdivl ataavataps gidaaivlet aagtggksds gksarrpnqt
      181 llqkhaalyt knrhaestal aqklvadype dgacwralsa slhregrfae mieagfrtve
      241 llpdevlvri lladtlramn rlseadeqct rlyqlqpdhp eamrirglvl falrrtdeal
      301 aacrravela pgaaapcgtl gfvllelgat qeaigwlkra ieinptdsvt hssmlfciah
      361 stefdpqalv aehrkfgery dnqkrkraav fsnprdpark lqvgfvsgdl lshavasyav
      421 pviehlaadt giamhfyhnh feedytserf kahattwrnv agmsdqafle rvrndridiv
      481 idlsghtgrn rlvalaqraa pvqaswigyp attglaamdy yltdrfvaph gafddqfveq
      541 lvrlpaiapf mpapncppvn vlpalhngyt tyasfnrlnk lsphvievws rvlhadptar
      601 malgaigsdg dqqtltewfa aagidagrlt fhrrsnipvy mqqhhgvdlc ldafpytgst
      661 ttlnalwmgv ptvtipgatm agrgsagwlq hvgldayiat deddfvtral algrdtaalq
      721 alraglrarc gesaafrpav vaaglssalr tmwtrwcage pvtafdtplf ddtataqaaa
      781 ea
//
LOCUS       WP_175999191             294 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175999191
VERSION     WP_175999191.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..294
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32529
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="PBP2_CrgA_like_7"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08476"
                     /db_xref="CDD:176165"
     Site            order(101,105,144,158,160,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176165"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176165"
ORIGIN      
        1 menltgivaf vrtaealsfv aagralgisa savgktiakl eqslgvrlfn rttrrvtltd
       61 egrhfyercq riledfrdae atvtasaqrp rgklrvslpv igyrfllpvl pefqqrypdv
      121 eldldfndrm vdvveggfda virsgplsds rlmsrrlgpf afvlcatpay laqagmprtp
      181 hdleahacvr ycfpttgklq dwalaaddgt plklrtamtc nnmealrgav laglgigymp
      241 dflardaleh gtlvtvlddy riapgqfsiv wpssrqlspk lrvfvdflce rlfr
//
LOCUS       WP_175999197             476 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia stabilis].
ACCESSION   WP_175999197
VERSION     WP_175999197.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..476
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49598
     Region          27..476
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mqtrdtaaps geqgdaplag daletvlvae lgealvtrsa dvdpryftay nepagvrpra
       61 lvrprsvddv sralalcarl gqpvvpqggl tglargaval ggevvlsmer fagiealdaa
      121 agtmtvragt plqtvqeaae aagftfgvdl gargscqigg mlatnaggtr airygmmreq
      181 vlgleavlad gtvvssmnrm lknnagydlk qlfigsegtl gvvtravlrl hpllaapata
      241 lcrvrdydav lglwnrvrtl pevvsfeamw pafydyvarh tpgvvapfag dggfavliec
      301 atsapggdah ealetglaag idaglvedav latserqard lwtlreglai dalphlvnfd
      361 vslptgelga faerceaalr arwpdvvclf fghvgdgnvh igvslagmtd adadaldhcv
      421 yavvrdmggs vsaehgigal krpylahtrs daeiglmrrl kaaldprgil npgkvl
//
LOCUS       WP_175999199             222 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_175999199
VERSION     WP_175999199.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..222
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23737
     Region          37..187
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpprhvqvpa ppgqpaaqpa palrrrprqq raqassdalq qafvqlller gyakatirei
       61 aavagvsigt fyeyfgdkqs laalcihrrv lamadrlrdv agrlrgapra elaaalvdvq
      121 vdaiaadaal wsaffalerq vsplaayrrh ydayvalwrd alaqaadppp aarldrlarm
      181 ahtvcyggls qalltlgpal dfaalrgelr avllaylaaa gv
//
LOCUS       WP_175999201             503 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Burkholderia
            stabilis].
ACCESSION   WP_175999201
VERSION     WP_175999201.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..503
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54335
     Region          3..498
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mnlvaaldra aratpdkpfl vneyatitya darershraa avlsalgvga gdrvaamcfn
       61 tpafvdlmfg awrlgavfvp inhklqapev dyvlehsrsk ailfdvtlap vlerivhpar
      121 rlvtegeldg vprfdtmcaa mdgvagiepa dgdiaqilyt sgttgrpkgc vhshrtvtfa
      181 amaaalatgi grnertlmam piwhssplnn wfggtlyagg tvvllreyhp lrflqtiere
      241 rvtlyfgapv sytlpldtid gfaafdlssv rawlygggpi gtaqaerlar ayrtdaffqv
      301 ygmtetgpag ttlypdeqva kagsigrqgg pgvdlrvvrm dgidarpgei geiwlkadsm
      361 mlgylddaaa traafapdgw yrtgdiarid qdgylfivdr lkdmivtgge nvyskevedv
      421 lgahpdiaea avvgvphpdw getvvahvvm ragattdada lrafcgerla aykipreftf
      481 aqalprtptg klqkfllrvr ged
//
LOCUS       WP_175999214             561 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia stabilis].
ACCESSION   WP_175999214
VERSION     WP_175999214.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..561
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=61124
     Region          10..539
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mttqrtlege fdyvivgagt ggcvlanrlt edpdisvlll eaggkddyhw ihipvgylyc
       61 ignprtdwly ktqpeaalng ralsyprgrv lggcssingm iymrgqredy dswaqetgda
      121 gwswdsvlpi fkrsedhhag esdvhgaggy wrvekqrlrw eilesfaqaa qqtgipatdd
      181 fnrgdnsgvg yfevnqkrgv rwntskaflr pamarpnltv itgaqaqrvi fdgrravgve
      241 yhgggtdyva raraevllts gavnspqlle lsgigcgrrl qalgidvvqd lpgvgenlqd
      301 hlqlrmafrv egvrtlntms ahwwgklmig aeyallqrgp msmapsqlga faksdpddpa
      361 ltrpdleyhv qplslerfge plhsfnafta svchlrptsr gsvhiasadp glapaiapny
      421 lstdhdrhva analrltrri asapalaryr peeilpgaqy rteaelieaa gavgttifhp
      481 vgtcrmgrad deravvdsrl rvrgiaglri vdasvmpfit sgntnsptlm iaerasdmir
      541 adrraareat pvrteaaata v
//
LOCUS       WP_175999216             176 aa            linear   BCT 11-JAN-2025
DEFINITION  SET domain-containing protein [Burkholderia stabilis].
ACCESSION   WP_175999216
VERSION     WP_175999216.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Qian,C. and Zhou,M.M.
  TITLE     SET domain protein lysine methyltransferases: Structure,
            specificity and catalysis
  JOURNAL   Cell Mol Life Sci 63 (23), 2755-2763 (2006)
   PUBMED   17013555
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Dillon,S.C., Zhang,X., Trievel,R.C. and Cheng,X.
  TITLE     The SET-domain protein superfamily: protein lysine
            methyltransferases
  JOURNAL   Genome Biol 6 (8), 227 (2005)
   PUBMED   16086857
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Yeates,T.O.
  TITLE     Structures of SET domain proteins: protein lysine
            methyltransferases make their mark
  JOURNAL   Cell 111 (1), 5-7 (2002)
   PUBMED   12372294
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459262
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..176
                     /product="SET domain-containing protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19622
     Region          1..143
                     /region_name="SET"
                     /note="SET domain-containing protein (function unknown)
                     [General function prediction only]; COG2940"
                     /db_xref="CDD:442183"
ORIGIN      
        1 mssrriavrr sgvhgkgvfa veqikagerv veykgerisw kealrrhphd psepnhtfyf
       61 aldeggvidg kidgnsarwi nhscapncea eevkgrvyih alrdigpeee lfydyglvid
      121 akltkklkre yachcgaasc rgtllatsdg adkkkkkkdk kdgkpesrak dkkskk
//
LOCUS       WP_175999277             191 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Burkholderia stabilis].
ACCESSION   WP_175999277
VERSION     WP_175999277.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..191
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=20653
     Region          4..135
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(9,11,72..73,76)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            11
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(71,116..117,119..120,124)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(77,82..83,112,115..116,119..120,123,126)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(101..103,112..113,116..117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(101,117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(125,131..132)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          147..188
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
     Site            order(148..150,182..183,185..187)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 msrtfayarv sttdqtaanq lheieaagfa vdrrrvvtes isgsvsadqr pgfaelllrm
       61 eegdvlivtk ldrlgrnamd vratvdvlan rgirihclal ggvdltsaag rmtmqvlnav
      121 aeferdllie rtqagiarak aegkalgrps altmqqraev rreldqgasv aglakrysts
      181 rqtimriras v
//
LOCUS       WP_175999296             892 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            stabilis].
ACCESSION   WP_175999296
VERSION     WP_175999296.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 892)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 892)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..892
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..892
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=96983
     Region          14..828
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnvteiaqai rggliqqdrl lktdipslpn nalvprravt cselgrdfsv vldlvstasd
       61 velktliaqp itlwiqqadk sylpingyih tarrlgadgs lssyqlcfas wmhflkfrsd
      121 mrywqdksvd ailadvfdah pqarghyqfa lskplpsrsy crqsetdwnf vhrlmedegl
      181 fgfwrhsedg kahtlvitdd lhavdalpek tvrfdrsgtg tetagftqwa asrtlqstlh
      241 ttrtfdyksp ssagnpngtt lptkagqgdl pdqaeiyeyt gaytyagqdr gehlskirle
      301 ewesrakrff gvggvrgida grrftladhp ehdrdsaqdr efaalkvlry iennlpisdh
      361 eanfphslqd plaqakaghg eaaafevghd dgsagfylve veaqranvpy rspfehrkpe
      421 mrletavvvg pkgeevytde lnrikvmfvw drqsegreta scwvrvvqsd sgggyggvhi
      481 prvgeevmig ylggdcdrpi vmhrvyngaa spqwhsdgil sgfrskeyag sghnemvldd
      541 atgqnrtrlf sssansllhl gylieqngnt rgaylgsgfd lrtdaygavr agqgmyvtth
      601 pkqassqpld vneaqqqlag aggviesmsq vseshqaesl gvghdalkqf tdatrnsvag
      661 essggrtagg gtgnanafke pvmlfaspag igmasqqsth laadrqvnlv sgqsthvvsg
      721 kslvasvkdk lslfvqnagm klfagkgpvq iqahndnvem taqktvkvvs atasiegvak
      781 eeilltsgga yvrikggnie lhapgkidvk ggehafsgpt smhktfkteg rkadmriryv
      841 dadgnvphge pikfatedga ehsvaldaeg raelknidfd efvasqvkrt ge
//
LOCUS       WP_175999311             427 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia stabilis].
ACCESSION   WP_175999311
VERSION     WP_175999311.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..427
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45411
     Region          15..415
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(26..27,30..31,34,69,116..117,119..121,124,148,
                     151..152,155,243,246..247,250..252,255,286,290,341..342,
                     346,350,366,369..370,373..374,377)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mnwavtrigg rfhygwlaaa vvflillaaa gtratpsvlm vplerelgws ratislaisv
       61 nialygltgp faaaamqrfg lrptiltalv tmsagvalss mmtqswqmvl iwglmvgcst
      121 gvvaltlsat fvtrwfharr glimgiltas tatgqlvflp mlaaiaqhhg wrpvvlvvav
      181 aaaiviplva fllperpadv qlrpygepad apaapeatke nplavafrtl lmasrsrdfw
      241 llffsfficg astngyvgth liamcsdygm tevqgaslla amgvfdlfgt tlsgwlsdry
      301 dnrvllfwyy glrglsliyl phafgidffg lplfamfygl dwiatvpptv rlatdvfgka
      361 aapvvfgwiv aghqlgaafa algagllras lgtytiasmi sgglcivgal ivlrinrgps
      421 rataqaa
//
LOCUS       WP_175999341             198 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia stabilis].
ACCESSION   WP_175999341
VERSION     WP_175999341.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..198
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20826
     Region          1..188
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mttilqinsa arsqgaqstl laneltaklq qsnpganvvv rdlladalph ldesvlgaff
       61 tpadkrtaeq naivaksdal iaelqaadii vigapmynfg issqlktyfd wiaragvtfr
      121 ytengpegli kgkrvhvvta rggkyagtpn dsqtpylrtf lgfvgmtdvs fifaeglnlg
      181 pdaqnaalas areaiaaa
//
LOCUS       WP_175999383             360 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia stabilis].
ACCESSION   WP_175999383
VERSION     WP_175999383.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..360
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40625
     Region          5..333
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mangnptqri lviridflgd mlcttaflda lkerwpgael hvvanrynaa alvgnpvvha
       61 vhsyvysrqc erndrpgrmr affdrlrlvr rlrrlrfdlv vvpnggmhrs smqfarqlga
      121 kdcrwhdaet efddrkpehv aqrpmcheal sgfrlvpelg radidrlals vhpdrtlqda
      181 whhllgartk prvglfvsnk aaerrwpadr wrdlgerlap fadvivfrdp alrhpaeddp
      241 wrdvgarhva pssvadlvaa aslldtivsa dsapvhlasa lrvpvaalfe drpekylrwh
      301 plgvphmilr agltvdaiev daveravrhl lpqaghrdlp aadasrawpr rpqrlqclrs
//
LOCUS       WP_175999434             397 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia stabilis].
ACCESSION   WP_175999434
VERSION     WP_175999434.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..397
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=42292
     Region          163..394
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 msettpspag lpgtfsassd sprpdpaktp dapaaqaaaq svavdgaspv taasepgapg
       61 stgstitagd gaaaplkpga pppgfgappd fdtqrpppas aqnappaylk qsdtpwsvfg
      121 rivaararrl fdragqritq rtlrigvsar ifhpepgakg lrgktlqyle esiahwvmsr
      181 dvlvfmiptv ghqgmihpsn irlrdyakhl dglllqggad vspqtyaasd vrpewpgdrv
      241 rdmyelellh efvesgkpvl gvcrgcqlin vafggslyqd iatdvptana hvsehydqhr
      301 hairfpdtst lasmfpgrse aivnsihhqa irdlgrdlni eavsagdgii egirhrrspf
      361 vvgvqwhpef hraggaelld ctplldaflr aaretrl
//
LOCUS       WP_175999443             419 aa            linear   BCT 11-JAN-2025
DEFINITION  sialidase family protein [Burkholderia stabilis].
ACCESSION   WP_175999443
VERSION     WP_175999443.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 419)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..419
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44701
     Region          54..>241
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Region          101..150
                     /region_name="Sialidase propeller 2"
                     /note="Sialidase propeller 2 [structural motif]"
                     /db_xref="CDD:271234"
     Region          161..214
                     /region_name="Sialidase propeller 3"
                     /note="Sialidase propeller 3 [structural motif]"
                     /db_xref="CDD:271234"
     Region          281..>407
                     /region_name="COG4692"
                     /note="Predicted neuraminidase (sialidase) [Carbohydrate
                     transport and metabolism, Cell wall/membrane/envelope
                     biogenesis]"
                     /db_xref="CDD:443727"
     Region          <367..>415
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
ORIGIN      
        1 mvavksfaag calwlaalsp agahdapkaa dphaahmgmq aapaqqkqpl atgaafdarh
       61 rlwvawvega hvvvahsdda grtlsapvtv nampepvyts aenrpkiats pdgravyvsw
      121 smpldapytg mvrfsrsldg gatwsvpvtv hrdrqaithr fdmmavdpag niaiawidkr
      181 dlvaakaagq ayegaavyya vshdggasfe perkvtdhtc eccriamaid paghieaawr
      241 nvfpgqirdh alavlpvsas epvvpvratf snwhveacpe hgpalaitpd gtrhlawfgv
      301 vdgradvfys rigadgqprg tpwafganpv vpgeqashaa lvargdvvwl awkafdgdam
      361 qiklrrsddr gehwsaprvi astsgasdnp qllddagrly lswrtrndgy rliavegaq
//
LOCUS       WP_175999486             151 aa            linear   BCT 11-JAN-2025
DEFINITION  porin, partial [Burkholderia stabilis].
ACCESSION   WP_175999486
VERSION     WP_175999486.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         <1..>151
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
     Region          <1..>151
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 grltthlfls tilfnpfyds ytfspmvyhv flglgtfpty psdqgavgds gwnnalsyts
       61 psfgglnfga myalgnqagd nrskkwsaqf nyangpfaat amyqyvnfnn gpqdlsalvt
      121 gmksqgialv gatydlklvk lfgqymytkn d
//
LOCUS       WP_175999514             504 aa            linear   BCT 11-JAN-2025
DEFINITION  MDR family MFS transporter [Burkholderia vietnamiensis].
ACCESSION   WP_175999514
VERSION     WP_175999514.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..504
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52558
     Region          38..422
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(39..40,43,74,124..125,127..129,132,152,155..156,159,
                     284,287..288,291..293,296,324,328,381..382,386,390,406,
                     409..410,413..414,417)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 metntlvavp ptaaagrdap sgpivaalll vmllsaldqt ivstalptiv gelggldrls
       61 wvvtayllss tvvlplygkl gdlygrkvvl qaaialflag salcgiaqdm pqlivlralq
      121 glgggglmvv tmaaigdlvp pdrraryqgm fggvyglati vgpllggflv ehlswrwift
      181 inlplgalal avigvafrpq aapvkhridy mgaaflatal tcvilftseg gsllpwsspq
      241 lwltlvlgai aiggfvyeer laaepimple lfrqrtfvlm sligfvvgia lfgsvtfipl
      301 ylqvvkgstp sqaglqllpm mggmltmsva sgrliarfgt yrpfpiagtl lggvamalls
      361 tlsldtslht iyaymallgi glgmvmpvlt lavqnavefr hmgvatsgat lfrsiggslg
      421 vaafgalfsh glqsrleqal padatlpaal gptavqqlpa avrdaylhaf agslhgvyla
      481 atgviaiafv lawfverapl rtrr
//
LOCUS       WP_175999565             739 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia vietnamiensis].
ACCESSION   WP_175999565
VERSION     WP_175999565.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..739
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=77974
     Region          <59..>203
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          210..707
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msrglieagr vgarvsrrsf lkagmslgaa aggglllgfs mpaaggearr sviggdadep
       61 arpgvfapna fvqidragqv tlvmpkvemg qgvytalpml iaeelevpls svtldhappn
      121 eklfsdpllg gqltggstsv ryaweplrra gatartllvs aaakqwsvdp aacraengev
      181 rhppsgrras ygqladaaak lpvpkdvalk kptdfkligk pvkrldspek vdgtaqfgld
      241 vrlpgmlyav ivnspvfggt vasvdataak kipgvrqvvr addavavvgd htwaakrgas
      301 alvvkwnega dakvstqdiv adlahaaang kgavarkegd vgnafahakt ridavyeqpl
      361 lahatmepvn ctvhvrgdgc dvwvgtqvpt rvrdtvhglt glaperivvh nhllgggfgr
      421 rletdmvaqa vkiakqvnap vkvvwtreed iqhdmyrpyy ydkisaglda ngkpvawqhr
      481 ivgssilarf appafrngvd pdavevaadl pydlpnqlvd yvrqeprhvp tafwrgvgpt
      541 rstfvvesfi delaaqtstd paqyrrallg ktprarnvld vatkaagwgs plpkgqgrgv
      601 svmhafgsff sividvaved gevqvkravc avdcgmvvnp stieaqvqgg iifgitgaly
      661 geitikdgrv vqsnfndyrv lrinetppie vhlvrsaeap ggigepgtaa taaavanaif
      721 aatgkrlrkl pvgaqlkta
//
LOCUS       WP_175999574             138 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia vietnamiensis].
ACCESSION   WP_175999574
VERSION     WP_175999574.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..138
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=14503
     Region          58..>136
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mkrsnytqrd giggrpahrm rmrmrpaaqi igawllscac vatpraaaad esvghklase
       61 asavggqlrd atlasriraa lvaerglasd didvqvhgrv aeltgsvpde pqhaaairvm
      121 rdvsgvsgvq drlkvgrk
//
LOCUS       WP_175999576             843 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia vietnamiensis].
ACCESSION   WP_175999576
VERSION     WP_175999576.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 843)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 843)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..843
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..843
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=90866
     Region          54..697
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mssvrellak waaraqpvaa aaavpvkrvl asawrhlrhp trrgalraaa avpvlfllyv
       61 lalipftpgi gdirkarvdq paqvlsadgk vlaefkpsnr ewvslkqisp hmvdaliate
      121 dhrfyehhgl dwkrtasaal htfsgdrqgg stitqqlarn lypdeigrap tltrkvkeai
      181 talkieavys keqiletyln tvpflynayg vemaartyfd ksadeldvld aatlvgmlkg
      241 nsyynpvlnp eralqrrntv laqmvkygkl saaqfaqlqr rplridferq keppgpaphf
      301 aqqlrkwlig wadrndyniy sdglivrtti dsrlqqiatq altqqanqlq giannawsgs
      361 dgcgtdnevf rtfmrespey kaaqdagknd aaamkqlaad rgfmralcka ktdvqagfva
      421 idprdgqira wvgsrdftse pfdhvaqarr qpgstfkpfv ygaafasgmt pddtfidqpv
      481 eiplkggeiw rpnddvppsg kpmtlrdala lsrnritaqv mekvgpaava rlardmgvre
      541 splervpsla lgtspvtlke mvasyatian gglytepqmv trienrqgdv laeyapappe
      601 raldgetdkt lldvmrdvvt rgtgssirtr fgvrgdvagk tgttqdnadg wfilmqpglv
      661 agawvgfddg rvtlrsdywg qgahsalpiv geffqraqra rivdaklkfd tepspgwfas
      721 vrervtdlfd gwfgpepkka ptrvrtqrie rqpdadaaaa saasaasape aasggiveqw
      781 ipasevaasa aamsggasqa pvllppaags agnaggagpg aasgvapgpa papaspesas
      841 ssq
//
LOCUS       WP_175999580             548 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 32 protein [Burkholderia vietnamiensis].
ACCESSION   WP_175999580
VERSION     WP_175999580.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 548)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446838
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..548
                     /product="glycoside hydrolase family 32 protein"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58850
     Region          38..533
                     /region_name="SacC"
                     /note="Sucrose-6-phosphate hydrolase SacC, GH32 family
                     [Carbohydrate transport and metabolism]; COG1621"
                     /db_xref="CDD:441228"
ORIGIN      
        1 mtstfpcffl rlaglllacs agvqaasaac taapadgtpq wrpafhytpq rnwmndpngl
       61 vyengryhlf yqynplgadw gnmswghats tdlvhwheqp vamhanatee ifsgsivadp
      121 hntsglgtpg dtpliavyts vykegsghpp gtqaqsiays ldhgaswqpy ahnpvltldp
      181 eskafrdpkv swyapgrywl mttvvadaqv vklyrsddli hwsflsdftl pgvphtgalw
      241 empdlvslpv dddprhikwv mivnvnpwsi aggsgamyfv gefdgrtfvp drvapagsdp
      301 aqfrwvdhga dfyaagtfsg apgrrplaia wmsnwdyaak sptapwrgam tlprelalka
      361 idgeptlvvt paaaftgwad rrpevhvgtl evdsaaralp sathgvaqri evtiapgqaa
      421 ragvvvrgsa dgsigtrivy dtaartltld rsrsgtpdfa atfsrqhiva lplengllrl
      481 diivdrgsve vfanggrtvl tdvvfppada drvsvfaerg tatfsgltvt plgardrage
      541 gdcvasar
//
LOCUS       WP_175999617             503 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia vietnamiensis].
ACCESSION   WP_175999617
VERSION     WP_175999617.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..503
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53069
     Region          27..474
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mkhvserapa kaggaqprda erdamfashe agyeqklkpr hvqmiamgga igtglflgag
       61 grlqsagpal alvylvcgaf aflimralge lvmhrptsgs fvsyarefmg erasfvagwm
      121 yylnwattgi vditavaiym kywavftdvp qwvfalgalg ivsvmnmigv kvfgemefwf
      181 sivkvgtlal flavgavfla sghpvagqmp glhlvadhgg ifphgilpav livqgvvfay
      241 asielvgvaa getadarkvl pkainsvmwr ialfyvgsvv lltmllpwta ysahespfvt
      301 ffsklgvpyv gtvmnvvvlt aalsslnsgl ystgrvlrsl amggsaprfv srmnargvpy
      361 ggilvtvavn algvplnyiv paqafeivln maslgivttw gfivmcqilf rravdrgels
      421 pvsfrmpgap ftswltlgfl vsvlvlmafd ypggtwtvam ipvvvlalvv gwklakrgaa
      481 rdaaaaaaaq aaapiaadpa gsv
//
LOCUS       WP_175999624             205 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Burkholderia vietnamiensis].
ACCESSION   WP_175999624
VERSION     WP_175999624.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..205
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21345
     Region          1..>184
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkilvavkrv vdanvkvgvk sdntgvdian vkmsmnpfde iaveeavrlk eagvatevva
       61 vsvgvtqaqe tlrtalaiga drailvestd gveplavaki lkalvdkeqp qlvilgkqai
      121 dddsnqtgqm laalaglpqa tfaskvtvad gkatvarevd ggaetlsltl pavvttdlrl
      181 neprcvkvpd vktlveklkt eakvl
//
LOCUS       WP_175999666             431 aa            linear   BCT 11-JAN-2025
DEFINITION  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase
            family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175999666
VERSION     WP_175999666.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kulikova,V.V., Revtovich,S.V., Bazhulina,N.P., Anufrieva,N.V.,
            Kotlov,M.I., Koval,V.S., Morozova,E.A., Hayashi,H., Belyi,Y.F. and
            Demidkina,T.V.
  TITLE     Identification of O-acetylhomoserine sulfhydrylase, a putative
            enzyme responsible for methionine biosynthesis in Clostridioides
            difficile: Gene cloning and biochemical characterizations
  JOURNAL   IUBMB Life 71 (11), 1815-1823 (2019)
   PUBMED   31359602
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..431
                     /product="O-acetylhomoserine
                     aminocarboxypropyltransferase/cysteine synthase family
                     protein"
                     /GO_function="GO:0016765 - transferase activity,
                     transferring alkyl or aryl (other than methyl) groups
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019346 - transsulfuration [Evidence IEA]"
                     /calculated_mol_wt=46218
     Region          5..430
                     /region_name="MET17"
                     /note="O-acetylhomoserine/O-acetylserine sulfhydrylase,
                     pyridoxal phosphate-dependent [Amino acid transport and
                     metabolism]; COG2873"
                     /db_xref="CDD:442120"
ORIGIN      
        1 mtdqassnwr letiavhggy rpdpttrava vpiyqtvaya fddtqhgadl fdlkvqgniy
       61 trimnpttdv leqriaaleg gvgalalasg qaavtysiqt iaeagdnivs asslyggtyn
      121 lfahtlpqyg ittrfadprd pvsfdalida rtkaifaesv gnplgnvtdi aaladiahrh
      181 giplivdntv pspyllrpfe hgadivvhsl tkylgghgts lggaivdsgk fpwaqhadrf
      241 krlnepdvsy hgvvyteafg aaayigrarv vplrnmgaai spfnafqilq gietlalrie
      301 risdnalkva qhlarhenve wvnyaglpdh pdhplvaryl sgrapgiltf gvkggrdgga
      361 kfqdalklft rlvnigdtks lathpastth rqlspaelak agvkeetvrl sigiehiddl
      421 ladldqalaq l
//
LOCUS       WP_175999691             472 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia vietnamiensis].
ACCESSION   WP_175999691
VERSION     WP_175999691.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..472
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49164
     Region          26..453
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(32..33,36..37,40,73,123..124,126..128,131,151,
                     154..155,158,283,286..287,290..292,295,323,327,381..382,
                     386,390,406,409..410,413..414,417)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msapsvpasq aqpnsispwp vfwiasvsvf lvsidvtvly aafpalrraf pgtdsgglsw
       61 vlnaytlvfa allvpagrla dlcgrkrmfl lglamfvggs fgcgiasrie mlwmmravqg
      121 agaalllpas lsillaafpv tkraiavslw gavsgvagal gpsvgsflvd rfgwpwaffl
      181 nlplgalalw qgwrvldesr dpergapldl vgvvllivgv gaiafglvqs ealgwaspkv
      241 alaiagglam laafvawart arapaidlsl fqdrtyryin laslcfaigf ammffqtflf
      301 ttgvwsyslt raglagspgp llvvptaivc grfaaraghr lllvtgslis maaslwfalv
      361 pgvtpdylya wlpgalltgl gvgmvmpsls aaavahlppa rfgvgsavnq airqmgsvfg
      421 valtvaitgn aitrlaefht lcylqialal atailcapvd trprvlasaa ar
//
LOCUS       WP_175999738             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia vietnamiensis].
ACCESSION   WP_175999738
VERSION     WP_175999738.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32949
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..295
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,190,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mqnldallif arvaemtsft raaeslgiqk grasmvvrql erdvgvallh rttrsvqlte
       61 dgrafyarar dllaevqelq smfsgsgtrl rgrlrvdmpt elarsvvvpa lpqlmaahpe
      121 lelelsstdr rvdlvqegfd cvvrlgpiid dtliarplgr lrminaaspd ylarhgvpht
      181 lddllgqghr mvhysltlga rhagweypkg dgyatlalps amqvnnvqty haaglagigl
      241 iqagysgvap hiasgalvev lpnlrpepla aslvvahrrn lsprvrafmd wiervlqpyf
      301 d
//
LOCUS       WP_175999638             825 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_175999638
VERSION     WP_175999638.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 825)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..825
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87525
     Region          507..793
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mrhfllgwll aavvsiahaa apasapaaas aasgavpalt pqqaqqalsv lqnprereqv
       61 ettlraiaav gvlstpalpa saaapasaas aaapaalttn glasmlvrqg shwageigda
      121 lneslrslld vasvgnwwhe rlvraderad llhalltiva vlvpalgaew larrllrrtl
      181 ralgarraes srradaappd teppelpesi dhaastplaa gtpsassvss tsatpetqsr
      241 gharrhttll hrmpralvsl vvravpllvf agvasltmsv ldgdgtptdt algslidiyv
      301 icrlvtivsr lffqpdarql rllhisdawa ayaqraiari aivvgictaa ielaasfgls
      361 eaghvallka valvghlmis alilrcrqpv aariratgde hrafamfsha ladawapvav
      421 favmalwfvw aldvhngyrv lialggrsia vmigmrivsi vvfgalarlf qrrdddrtlv
      481 hlhayryypl lrrivstvia ivtvvlllqi wgvpifhafk tgtighrlas almtiaiaal
      541 valfvweaan iaierrlqqw tregnlvraa rlrtllpmlr slllimialv vvltglsqig
      601 vnigpllaga sifgvalgfg sqklvqdfit gifllmenam qvgdwvtlag vsgtveylsi
      661 rtvrlrggdg slytipfssv ttvnntnrgl gnaavkvsia ygqdidpaia tlkeigaalr
      721 ddpnykdgil sdfsywgvdq vdgatvtlag qiqckdsarw gvqrefnrri avlfrergir
      781 ianpqrsvva ydagaqrgga dgaegpdtaa apsaavnppp rpapq
//
LOCUS       WP_175999757             257 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            vietnamiensis].
ACCESSION   WP_175999757
VERSION     WP_175999757.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..257
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29223
     Region          30..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtetkrkaas rpsrtaaaep aatpgrrltp earerqivek avehfathgf sgstrelarq
       61 igvtqpllyr yfpskealid rvydevytwn pdwekliadr tiplqqrlva fyrsyaqtil
      121 rrawirtfif aglsregfnt rylsrlrerv flpvlrelrh eydiptpasd aqrnaeielv
      181 wslhasifyl gvrkwvyglp vpddvdaeie rqidaflngt paalkrvaad tppttttpap
      241 tptptpaptp tprrkrg
//
LOCUS       WP_175999823             139 aa            linear   BCT 11-JAN-2025
DEFINITION  HIT family protein [Burkholderia vietnamiensis].
ACCESSION   WP_175999823
VERSION     WP_175999823.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..139
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15001
     Region          5..136
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 msydnnnpfa rilrgelpcv kiaeddatva imdvmpqadg hvlvipkepa aqlfelsgda
       61 aaasirmtqr vaaavrdalg pdgmfigqfn gaaagqtvph vhfhviprwe dvelrmhard
      121 fadaatleal aqrirarfv
//
LOCUS       WP_175999825             927 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Burkholderia
            vietnamiensis].
ACCESSION   WP_175999825
VERSION     WP_175999825.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 927)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 927)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 927)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 927)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 927)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11534155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..927
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..927
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=94577
     Region          12..78
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          101..163
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(107..109,112)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          180..925
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mteslastat htieldidgm tcascagrve kalakvpgvt rasvnlater asvdaapdvs
       61 asrlvdavrq agygatpvaa kpaasaqpaa apqaqapasi eldidgmtca scagrvekal
      121 akvpgvtras vnlaterasv daapdvsasr lvdavrqagy gatpvaatpt adragpasfe
      181 ldiggmtcas cagrvekala avpgvarasv nlaterasvq aagtldaaal iaavtsagyq
      241 aslaaeaqaa aaapaapdpa qatdarkrrd airernlvig aavlstpliv pmlvaplgid
      301 amlpgwlqlv lasivqfgfg arfyraawha vkartgnmdl lvalgtsaaf glslwmllre
      361 pahpghlyfe asavivtlvr fgkwlearak rqttdairal nalrpdrari vehgverdvp
      421 laqvrvgttv airpgervpv dgrivsgrsh vdeslitges lpvpkddgdp vtagsingeg
      481 alvvattaig aettlariir lvesaqaeka piqrlvdrvs evfvpsilgi avltligwli
      541 agagaetail navavlviac pcalglatpa aimagtgvaa rrgvlikdaq alelaqratv
      601 iafdktgtlt egkpsvtafd avdipreqal avaaavqrhs dhplaravva aydadvaarg
      661 gaavaadaav atdaravagr gvearvdgwl valgssrwrd elgiavppel garaaelera
      721 gntiswlmra dapraprall aliafgdtvk pgardaiaal sargvasvlv tgdnrgsaaa
      781 vaaalgidev haqvlpddka rvvaelkrth ggvvamvgdg indapalaaa dvgiamatgt
      841 dvamhtagit lmrgdptlva daidiskrty rkiqqnlfwa fvynligvpl aalgwlnpvi
      901 agaamafssv svvtnalllr rwkgkar
//
LOCUS       WP_175999884             391 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Burkholderia vietnamiensis].
ACCESSION   WP_175999884
VERSION     WP_175999884.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 391)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..391
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42033
     Region          4..386
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 mtalktlaia nyrslreliv plaaltvvtg pngsgkssvy ralrlladta qgrvipslar
       61 egglpstlwa gperfsraml agdtpvtgtv rnrpvslklg facadfgyai dlglpvpsss
      121 qftldpvvkr eciwsgallr pstllverqg aqirtrttsg dwrtvpqpva sfdsmmtefa
      181 dpvgapemia vrerirswrf ydhfrtdara parqshigth tpvladdgad laaalqtire
      241 igdaavldat iddafpgasi didnpggrgr fdvlmrqpwl lrplaaaels dgtlryllla
      301 aalltprppa lmvlnepets lhpdllpalg rliaqaarrs qvlvvshaar liatlereag
      361 ceslvldkql gatalvdada rdlppwkwpa r
//
LOCUS       WP_175999894             841 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia vietnamiensis].
ACCESSION   WP_175999894
VERSION     WP_175999894.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 841)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 841)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..841
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..841
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=91324
     Region          59..779
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mpiikrpsss sdrkephysl rrspsgayyp dddepdddrr asrrgggrdg dgrrsfgsrv
       61 alwfvglfat laivgalivg yalvvmapql psldaltnyq pkvplrvysa dhvllgefge
      121 errslvrfqd ipdvmkkavl aiedyrfyeh ggvdflgilr agvadllhgg arqgastitm
      181 qvarnfflss ektytrkiye mllaykiera ltkdqilely mnqiylgqrs ygfaaaarvy
      241 fgkdlkditl aeaamlaglp kapsaynpvv npkrakvrqe yilkrmleig yitqpqydqa
      301 vkeeihvrtp gnqyavhgey vaemvrqmmy eqykdetytr gltvtttina adqeaayqav
      361 rrgildyerr hgyrgpegsi nlpaagddrd eavddaladh pdngdlqsav vlsaspnavd
      421 vqfvggattt igpaglrfvs aalspranat lrikpgsivr vlkdgktgwq vvqlpqvega
      481 lvaitpqdga irslvggfdf nkskfnhvtq awrqpgssfk pfiysasldk gmgpatiind
      541 aplyfppsvp ggtawepkdd dqpdgpmsmr talqrsknlv sirilasigt qyaqqyvtqr
      601 fgfdpaktpp ylpmalgagl vtplqlatgy avfanggykv dpyliaevdd argqplqksq
      661 pavagstapr tiegrnayvm nsllhsvata gtgagtnalg rsdlqgktgt tndakdgwfa
      721 gyqqslvava wmgfdqpksl gsrefgaqla lpiwvnymrt alngvpeqqm pmpdglttid
      781 gelyyadrtp gngfvasvdi npaenaisan dalgsagaag lapppvtqqe kqqimdmfes
      841 k
//
LOCUS       WP_175999925             339 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia vietnamiensis].
ACCESSION   WP_175999925
VERSION     WP_175999925.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..339
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34848
     Region          36..338
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtqlpvspsd agaqqdltgr rartlsgtrl gvsnylglag alvamvalfs alsshfltyd
       61 tfstianqip dlvvmsvgmt fvliiagidl svgsvlalaa smvsvaalkw qwaplpaals
      121 giavatvtgs ltgavtvgwr ipsfivslgv legarglayq ltnsrtayig dafdflsnpi
      181 algispafli avavmiaaqf vltrtvfgry lvgigtneea vrlagvnprp ykilvfalmg
      241 alaglaslfq isrleaadpn agvglelqvi aavviggtsl mggrgsvist ffgvliisvl
      301 aaglaqigan eptkriitga vivvavvldt yrsrrsrar
//
LOCUS       WP_175999951             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia vietnamiensis].
ACCESSION   WP_175999951
VERSION     WP_175999951.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45841
     Region          22..420
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,150,
                     153..154,157,245,248..249,252..254,257,285,289,347..348,
                     352,356,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnenhavpaa ppgirrgqri alallmvsgi vnyldrgtla vassairadl glslsqmgll
       61 lsafswsyal cqfpvgglvd rigprrllgi glivwsiaqa aggmvstfgw fivarivlgi
      121 geapqfpsaa rvvsnwfplr argtptgifn aasplgtala plllsvlvas fdwrlafvat
      181 galglvvavv wfalyrdpar aqlsavergy ldadaqtaaa apkltfadwr slfshgttwg
      241 mligffgsvy lnwvyltwlp gyltmerhms lirtgfaasv pflcgfvgsl vagwlsdfvt
      301 rrsrspvvsr rnavvvamlg mvaftipaal vqsntvalac isvviflana asacswalat
      361 aaappsrvas lgaiqnfggf iggalapilt gviaqkwsfv palltaaaia fagamaylll
      421 vrkpipeqaa saapgplpa
//
LOCUS       WP_175999993             266 aa            linear   BCT 11-JAN-2025
DEFINITION  (Fe-S)-binding protein [Burkholderia vietnamiensis].
ACCESSION   WP_175999993
VERSION     WP_175999993.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..266
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28090
     Region          <5..256
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mnprpypava pahvylfatc lvdlfvpeag ldavrllere gltvhyprgq sccgqpayss
       61 gnpdearrva aaqldlfgda wpvivpsgsc agmirhhwpt lfaddpvhgp karaiakrty
      121 elaeflvnvl hvrldaiapp agpdervvlh tscaarremg trahgvalvd alpgvtrveh
      181 ereseccgfg gtfslkhpdi sgamvqdkva sacatgcdrl vsadcgclln ighaadkaga
      241 klavehlasf lwrrtagaas lsgdaq
//
LOCUS       WP_176000002             244 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator [Burkholderia].
ACCESSION   WP_176000002
VERSION     WP_176000002.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..244
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26478
     Region          16..244
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 metgcselap dplddtplyl qlarnlasai hagawragea lpserllsdt vgvsritarr
       61 alallveqgl irrvrgagsf itprvadpls rlvgftekmr qrgfipdsvw lartlrvasr
      121 deiahlglap gatvarlerl rradgtvmav ehstlpaavl pdpqalgasl ydylaargss
      181 vvralqhfra anatheiakw mgvkpgaall virrigygad qralevtesy crddyydfva
      241 elkr
//
LOCUS       WP_176000019             398 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia vietnamiensis].
ACCESSION   WP_176000019
VERSION     WP_176000019.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..398
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42548
     Region          5..360
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mstawdrarr ilcvrldslg dvlmttpalr alkdggrgrq ltlltsrsga alaghlpmvd
       61 dvwtydapwv khpeargdpv adldmvdrll agrfdaavif tvysqsplpa ammcwlagip
      121 lrlahcrenp yelltdrvpe tepeshvrhe varqlalvrs vgattsdwrm afepgdaarr
      181 alharlraal qrlggprdpa rarwlvvhpg asaasrrwpa erfgeaaarl aplfdgiavt
      241 gsasehalve avceragpra vplagalplg elgalietad lllsnnsgpv hlaaalgtpv
      301 vdlyaltnpq htpwrvphrv lnvdvpcrnc yrsvcdqpgh pcllgvsvdd vvavthallr
      361 gserhalhaa araaahgaap vavnasnvip fahaitrs
//
LOCUS       WP_176000038             529 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxylesterase/lipase family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_176000038
VERSION     WP_176000038.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..529
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=57634
     Region          13..515
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mneqthisei dhrhagsdcv ltlahgrlrg srshgvarfl gipygmpatg srrfappvap
       61 lawdgtrdcr aygdacpqvn ddlpawrfdg dhsanclnln vwtpaaampg drlpvmvwlh
      121 ggaylsgsan lplydgrtla deqqvvvvsi nhrlnafgyl ylgdrdehga qaanvgqqdi
      181 vlalvwiaan iaafggdagn vtlfgesggg gkicaltmmp sadglfhkai iqsgafvtml
      241 sraqarkrtd allsllgadv rsldaiddar llgatrrlid rygytafwpv ddgnvvdasr
      301 rraasmpmli gttrheaayf lppqllarsp ldstdyrdal eegmrplcig addvraaaat
      361 aarlhalgpr slgrdltdvm frmpalalae rnaehadtfv yrfdwafpcc ggryaihgae
      421 ipfvfgtldy alpawdsadl prdryrddph gdrfrlaarv rrawagfarc gdpsagdasi
      481 wrrytrdqpa trifdricri etdpdgprrh alfaadsnaf ssstlidke
//
LOCUS       WP_176000045             263 aa            linear   BCT 11-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_176000045
VERSION     WP_176000045.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..263
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28210
     Region          22..254
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 malstqpapp pdivtsdaap asaprghdlr iatynihggy gawparaver ivavirelda
       61 dvialqevpl ggtrapdvla hlrdatgmha vagptidtpe rrygnavlsr cpiraartld
      121 lsfhqreprg aldadidcsa gpirvvathl glsanersaq vqrllaafdt gampvilmgd
      181 inewfvrgra lqalttrfrr apaprtfpta wpvfsldriw ihpgellvdv avhrsmlarh
      241 asdhyplvaq mrvepgagtp lag
//
LOCUS       WP_176000082             430 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia vietnamiensis].
ACCESSION   WP_176000082
VERSION     WP_176000082.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..430
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=47055
     Region          16..345
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mnemksnsvd vaiigagpsg avaaallrna grsvlvlerq hfprfsiges llpqsmryle
       61 eagmlqavve agfqfkngay fvhrdrmssf dfrdkfsdgw gtayqveraa fddllircae
      121 kqgaqvrfgh avrafhagdt prldvvdeag heysvqasfv ldasgfgrvl prllgleapt
      181 glptraaifs hvedrlpags tdrdkiciav hperrdvwfw mipltngrss vgcvadaafl
      241 dvpeaeqeal lrellqtept lsrlvgskpf vmpvrricgy asnveslhgh gyallgnage
      301 fldpifssgv tialrsahla vatlerqlrg etvdwardyd valrkgidtf rafverwysg
      361 alqdivfhed kasdvkrmvc silagyawde tnpfvrepar gldilaqlcc ptvasgnaaq
      421 aatpdgarrr
//
LOCUS       WP_176000372             466 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-mobile-trio recombinase GmtY [Burkholderia vietnamiensis].
ACCESSION   WP_176000372
VERSION     WP_176000372.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Mahata,T., Kanarek,K., Goren,M.G., Marimuthu Ragavan,R., Bosis,E.,
            Qimron,U. and Salomon,D.
  TITLE     Gamma-Mobile-Trio systems are mobile elements rich in bacterial
            defensive and offensive tools
  JOURNAL   Nat Microbiol 9 (12), 3268-3283 (2024)
   PUBMED   39443754
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Hurley,C.C., Quirke,A., Reen,F.J. and Boyd,E.F.
  TITLE     Four genomic islands that mark post-1995 pandemic Vibrio
            parahaemolyticus isolates
  JOURNAL   BMC Genomics 7, 104 (2006)
   PUBMED   16672049
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF040693.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     gene            1..466
                     /gene="gmtY"
     Protein         1..466
                     /product="gamma-mobile-trio recombinase GmtY"
                     /calculated_mol_wt=52975
     Region          3..432
                     /region_name="recomb_GmtY"
                     /note="gamma-mobile-trio recombinase GmtY; NF040693"
                     /db_xref="CDD:468657"
ORIGIN      
        1 mfvtvkakvy tdatgvstel pvlltpagvl eplldyclhr shdrsltwms kvarsvrmfl
       61 eylqtnpaeh gtyrlfqnfa qrlhtgtfdr etgfdpsglc waprspqdas hvithltdff
      121 dwlgemrpea aqinpryagg afdrqtdeia yqhrrsrafl ghtwaanasp aetghrvrgr
      181 rlprvekgep pafpeerfee llvtgfcaag rcdyrgmlvt lllhgagfre sepfhlyisd
      241 vfpdpanprq akvlihhpsh gaapadwrde rgrprkanra eylahkfgla prtdvmdrrh
      301 agwkggthdg pyykqaywft peygewflqi wrryleqvar ierdhpfafv nlgrepvgam
      361 ytltqynkah aaacerigik vskslgttph ghrhaygrrl rqagvdkali rrfmhhasme
      421 sqegytqast realaaldaa aqrlrdkyte pqpalrlvlp gielnn
//
LOCUS       WP_176000387             145 aa            linear   BCT 11-JAN-2025
DEFINITION  SET domain-containing protein [Burkholderia vietnamiensis].
ACCESSION   WP_176000387
VERSION     WP_176000387.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Qian,C. and Zhou,M.M.
  TITLE     SET domain protein lysine methyltransferases: Structure,
            specificity and catalysis
  JOURNAL   Cell Mol Life Sci 63 (23), 2755-2763 (2006)
   PUBMED   17013555
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Dillon,S.C., Zhang,X., Trievel,R.C. and Cheng,X.
  TITLE     The SET-domain protein superfamily: protein lysine
            methyltransferases
  JOURNAL   Genome Biol 6 (8), 227 (2005)
   PUBMED   16086857
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Yeates,T.O.
  TITLE     Structures of SET domain proteins: protein lysine
            methyltransferases make their mark
  JOURNAL   Cell 111 (1), 5-7 (2002)
   PUBMED   12372294
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459262
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..145
                     /product="SET domain-containing protein"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15745
     Region          1..141
                     /region_name="SET"
                     /note="SET domain-containing protein (function unknown)
                     [General function prediction only]; COG2940"
                     /db_xref="CDD:442183"
ORIGIN      
        1 mrriavrqss vhgrgvfalr diasgeriie ykgrvmswrs aiagqqklas edghtfffgl
       61 tdgrvidgga ggnsarwinh actpnciaee degrvfifas hairagdeis idyqlsvdgr
      121 htaavrasya crcqslecrg tmlar
//
LOCUS       WP_176000426             546 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia vietnamiensis].
ACCESSION   WP_176000426
VERSION     WP_176000426.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..546
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58219
     Region          1..530
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mqydyiivga gsggsslagr ladacpdati alieagshte rnllvnmpvg iaalvpfklg
       61 tnygyetvpq pglggrrgyq prgrgmggss ainamiytrg hpgdydewaa lgatgwgwqe
      121 vlpyfrraeg nqrgadawhg adgpltvsdl rfrnpfserf vqaahaagyp lnddfngatq
      181 egvgfyqvth rdgsrcsvar ayiygrnrpn lhvitdatvl rvgfdgkrav gvvvsrdgrv
      241 etlgaraevi lsagafnspq llmcsgigpv eqlrrhgiav vhdapevgtn lsdhidfivn
      301 trvnsselvg iclrgiakmt palarylssr tgimtsnvae aggfiksdps ldrpdlqlhf
      361 caalvddhnr kmhwgfgysl hvcalrpfsr gtvalasgda rdaplidprf fsdtrdldll
      421 vrgahamrri lsqaplasqg grelytrpdq sdaelrativ ahadtiyhpv gtcrmgsdar
      481 avvdpqlrvr gvdglrvvda svmptliggn tnapsvmige raadfivaar tgsasrsaav
      541 aavhgr
//
LOCUS       WP_176000498             459 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia vietnamiensis].
ACCESSION   WP_176000498
VERSION     WP_176000498.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..459
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48947
     Region          13..457
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mtrqqrsfdn ivareqglrh altsgqmami aiggaigtgl flgsgfaigl tgpsvlvsya
       61 igalialllm galaemtvah ptagsfgaya ehyvgplagf lvryaywfav vfaigteisa
      121 iavfmkywfp avpgwywvig fsalliavnl asvtlygsve yafsllkiaa iivfivlgay
      181 lvwsappasg igfanytghg gfmpkgpwgt wvavivaifs ymsieavaia ageardpqya
      241 vtrafcstvf rlvlfylltl almlaivpwt qagtdespfv kvmaathvpy aagvinfvll
      301 iaalsamnsq lyvttrmmfs lsrarlapav fgrvgdngvp raalwistsg vavaavlval
      361 spgtaftvmm aiamfgalft wlmifvthlr frarysgpal afrmwahpfg sllgaalvga
      421 illttaftha frmtmvvgvv fvvlltlaya lhyrhqhar
//
LOCUS       WP_176000462             298 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia vietnamiensis].
ACCESSION   WP_176000462
VERSION     WP_176000462.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..298
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31114
     Region          32..284
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mqslsgssas spapapsdar gatlraprvs garaiaalqw svtlllcafl ivpvvmsvla
       61 gvtvnyfrgl ssgltlrwle qvwqqyqgsv alslgvafat laivlvtgvp agyalargns
      121 rvaraieeal vlpvalpgla salallvvyg gftafrmslw fivvghvvft lpfmvravaa
      181 vaagaelrtl eegaaslgas fvtrfvtivl pnlrpgivag alavltlsig efnltwmlht
      241 pdtktlpvgl adtyaslrle vgsaytivfl lmtlpllvam qwlgvdpsgt raarrrar
//
LOCUS       WP_176000585             339 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-quinone oxidoreductase [Burkholderia vietnamiensis].
ACCESSION   WP_176000585
VERSION     WP_176000585.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..339
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=35421
     Region          1..333
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(40..41,127,131,134,157,160..162,181..182,186,201,
                     225..226,247..248,250,272..274,322,327)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mkaieitefg apdvlklter vrpepargev likvaasgvn rpdvfqrkga yapppgasdl
       61 pglevageiv ggdlsdpaln pfglklgdrv callagggya eyavapllqc lpvpggltdi
      121 eaaslpetff tvwsnvfdra llgageggeq etllvqggss gigvtaiqia halgfrvfat
      181 agtadkcrac ealgaerain yktedfvevv kslthdrgvd vildmvgaay lprelsalad
      241 ggrivliall ggakaeinlg eilrrrltvt gstlrprpve fkariaaqlk arvwplladg
      301 rikpviyrvl pagdaaqaha lmesgehigk ivldwgaia
//
LOCUS       WP_176000696             399 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia vietnamiensis].
ACCESSION   WP_176000696
VERSION     WP_176000696.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..399
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /note="Members of this family of hydrolases with an active
                     site Cys residue belong to MEROPS family C26."
                     /calculated_mol_wt=42596
     Region          <56..>123
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          165..396
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 msettpspag lpgtfsaspd srrseppraa dvpaapaaqa aaahdvaddr aspvtaasep
       61 gaagtpgtag eaapskpgaa ppgfgaqpdf dtprpppasa qnaqnappay lkqsdtpwsv
      121 vgriiaarar rlfdragqri tqrtlrigvs arifhpepga kglrgktlqy leesiahwvm
      181 srdvlvfmip tvghqgmlhp snirlrdyak hldglllqgg advspqtyaa sdarpewpgd
      241 rvrdmyelel fhefvesgkp vlgvcrgcql invafggsly qdiasdvpta nahvsehydq
      301 hrhairfpds stlasmfpgr seaivnsihh qairdlgrdl sieavsagdg iiegiryrra
      361 pfvvgvqwhp efhraggael ldctplldaf lraardtrl
//
LOCUS       WP_176000697             425 aa            linear   BCT 11-JAN-2025
DEFINITION  sialidase family protein [Burkholderia vietnamiensis].
ACCESSION   WP_176000697
VERSION     WP_176000697.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 425)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 425)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..425
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45768
     Region          60..>247
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Region          107..156
                     /region_name="Sialidase propeller 2"
                     /note="Sialidase propeller 2 [structural motif]"
                     /db_xref="CDD:271234"
     Region          167..220
                     /region_name="Sialidase propeller 3"
                     /note="Sialidase propeller 3 [structural motif]"
                     /db_xref="CDD:271234"
     Region          287..>415
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Region          287..332
                     /region_name="Sialidase propeller 1"
                     /note="Sialidase propeller 1 [structural motif]"
                     /db_xref="CDD:271234"
     Region          342..386
                     /region_name="Sialidase propeller 2"
                     /note="Sialidase propeller 2 [structural motif]"
                     /db_xref="CDD:271234"
ORIGIN      
        1 mvavksfaaa calwlatlsc aaahdlrdth aapqaadpha ahmsmqpapa qqkpplatgt
       61 afdarhrlwv awvegahvvv ahsddagrtl sapvtvnamp epiytsaenr pklatspdgr
      121 avyvswsmpl dapytgmvrf srsldggatw svpitvhrdr qaithrfdmm avdpagniai
      181 awidkrdlva akaagqsydg aavyyavsrd ggasfeaerk vtdhtceccr iamavdpagr
      241 ieavwrnvfp gqirdhalav lpiaasepvv plratfsnwr vdacpehgpa laitpdgtrh
      301 iawfgvvdgr advfysrida dgrprgapwa fganpaapde qashaalvar gdvvwlawka
      361 fdgdtmhirl rrsddrgehw saprdiasts gasdnpqlld dagriyvswr trndgyrlip
      421 vegvq
//
LOCUS       WP_176000708             273 aa            linear   BCT 11-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Burkholderia
            vietnamiensis].
ACCESSION   WP_176000708
VERSION     WP_176000708.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..273
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=30481
     Region          65..161
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 mspgeraenl iaefgitapd eldvrafayd aglevefddl egceatlvgv gnrgiatirp
       61 snvvgrerfs ighelghwem hrgksfrcrv ddpsdnlasn seqekhadey ashllmprpl
      121 lqpmvksvgc pgfkhinefa eifqtsrtat cirlaqidtl piiaacyrgn dlrwlsrapd
      181 kwflkrrlde dsfaydvlqh greaqgkqpa evwfdddgad kyevmehsar grdgevlvlv
      241 yltdvemmts rsnrsrdaeg awgarggyss gtr
//
LOCUS       WP_176000725             252 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome c1 [Burkholderia vietnamiensis].
ACCESSION   WP_176000725
VERSION     WP_176000725.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 252)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458269
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..252
                     /product="cytochrome c1"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28328
     Region          26..252
                     /region_name="CYT1"
                     /note="Cytochrome c1 [Energy production and conversion];
                     COG2857"
                     /db_xref="CDD:442105"
ORIGIN      
        1 mkkllstlal igatavalla apavraegnf pldrapdnte nlvslqhgaq lfvnyclnch
       61 saslmrynrl tdlgisqkei eknllfttdk vgntmsvamr pedaknwlgt mppdlsveer
      121 argrdwlyty lrsfyrddtr ptgwnnavfe nvgmphvlwq lqgqrtakfe dktneetgek
      181 vhtlvgfqqv tpgtlsspdy daavadlvay mtwmsepaqq trkrlgvwvl iflgvltfla
      241 wrlnaaywkd ik
//
LOCUS       WP_176000764             714 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia vietnamiensis].
ACCESSION   WP_176000764
VERSION     WP_176000764.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..714
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=77357
     Region          9..697
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mtfpslrdwl fsgktfaasm lalylglyfq lprpywamas vyivsnpfvg atrskalyra
       61 lgtalgaaaa ilfvppfvet pilfsiivat wcgtllylai sdrtarsyvf mlagytmpli
      121 alptvadpst ifdvaiarte eivlgivcas vvgstvfpnr laptliertd awfkdaafyg
      181 retlsghlag kalsacrqrl aatitglefl lsqlsydhah prvleraqal agrmqlflpl
      241 mssladplva lmrelkvrpp gldalladaa kwfdaplpav kadtggemah dpaaddlrar
      301 iaalqppdsa laswdgalls nalwrlrqvi diwqdcrslr alianesgiw qprfrhwrlg
      361 gterffdrgm mlfstltvag aivfacwlwi asgwhdgaga vtlaavacsf faaldepapl
      421 vfkfflataa svvfaglylf avlphvhdfa mlvlmfagpf iligtllprp qfnmvtmlva
      481 vntatfisiq saydadffvf lnsnlagvag llfaylwtra trpfgaelav rrllrsgwed
      541 varsastqpl ddqrnhasrm ldrvtqllpr lgasddhrhp siesfrdlri alnaldlrra
      601 rrrlsgdvpd aidrvlagvt dhyarcaaan arqpappall asiddalrrv agrtrppaas
      661 agaveagatp gaptsraahr rlrntlhalv glrlslypaa aaqppqatad gara
//
LOCUS       WP_176000780             459 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Burkholderia vietnamiensis].
ACCESSION   WP_176000780
VERSION     WP_176000780.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..459
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=51596
     Region          10..422
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mseiastkar krcavycrvs sderldqefn sidaqkeagh ayvasqrseg wipvaddydd
       61 pgfsggntdr pglkrlmadi ergqidivvv ykidrltrsl adfskmvevf erhgvsfvsv
      121 tqqfntttsm grlmlnvlls faqferevtg erirdkiaaa krkgmwmggv pplgydvdnr
      181 llvineaeaa vvrrifeeml tigsptqiav nltadgittk awttqegqtr sgtridkkyl
      241 hkllrnriyl gelshkgnwy pgahppiidq elwdkvhtvl ardghtrsve tkirsrtdal
      301 lrgllyapsg ermyptysrk ngrkyhyyvs ksesrfgapg ksyerlpape ieaavvaqir
      361 tvltspesia avvrhiqrng gqideattvm amgrlndvwd qlfpverhri anlmieridl
      421 vyvgevqgik vkwrelgwda ligefaprgi gaelvevea
//
LOCUS       WP_176000817             343 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia vietnamiensis].
ACCESSION   WP_176000817
VERSION     WP_176000817.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10859374
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..343
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38793
     Region          3..98
                     /region_name="HTH_NolA-AlbR"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators NolA and AlbR; cd04788"
                     /db_xref="CDD:133415"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133415"
     Site            order(51,54,58..59,68,80,84,90,94,97..98)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133415"
     Region          131..>187
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
     Region          <259..>305
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 mrlkvgelak rsgltvrtlh hyhaigvlap saradngyrl ydrddiarlh qiqalrrfgl
       61 slaeigdyln qpgtplvelv akqiaslerq laqaaqlrer lvqlhaqlaa gtepeladwl
      121 ttlelmtvyd kyfseeelar mpmyrksqtg daewvalvad vralhdagvp pederarala
      181 erwmtllvrd tnndprllak lnlmhereps mqskigista lrdyvlkama etkmrvfeky
      241 lapdeirfmr ahygeramew pqliadvrda idagktpasp egralarrwl elfcsyagtd
      301 pathakfrha matepallkn awtdetllgf mrdamaqlqt arh
//
LOCUS       WP_176000858             265 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_176000858
VERSION     WP_176000858.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..265
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=28199
     Region          11..>184
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(88..90,92..93,97,100,109,111,113,117..118,121,
                     123..124,126..127,131,134,143,145,147,151..152,155..157,
                     159..160,164,167)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          111..143
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          145..174
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 msanspskyf dgsylsaaka isdgdvaqlk salseidvnk pgrqemtllw faistknfsa
       61 iseliahgsk pdaqiveglg samyfaitne dtrylkamld gglspdtvds dgtsllqram
      121 egngamervk llvehhanin hrdsiggtal dsaldvakpd iaiflvehga dvnahttngv
      181 svaysvqkdi dalqpeakqa tvtdisldkd gqpvrtaqtp papglspegk arlekferlr
      241 almiakgakf ppdppakvre qmskk
//
LOCUS       WP_176000904             210 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease, partial
            [Paraburkholderia caledonica].
ACCESSION   WP_176000904
VERSION     WP_176000904.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caledonica
  ORGANISM  Paraburkholderia caledonica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 210)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Paraburkholderia caledonica"
                     /db_xref="taxon:134536"
     Protein         1..>210
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
     Region          1..>208
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 msiflqllvn glllggayai isigltlifg vvrvvnfahg ellmvgmyav wmlaqhlgwh
       61 pyisavpval mlfaagallq rfviqpllss eahiqifatv gvstallnla lmifgadvhp
      121 vdvtfgtehl qlgslnvstg qvitfvvail vasglhvflq qtftgrafra vaqhryaasl
      181 mgvnvkatyi lafgfgaalv glasgllavq
//
LOCUS       WP_176000914             271 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease, partial
            [Paraburkholderia caledonica].
ACCESSION   WP_176000914
VERSION     WP_176000914.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caledonica
  ORGANISM  Paraburkholderia caledonica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Paraburkholderia caledonica"
                     /db_xref="taxon:134536"
     Protein         1..>271
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
     Region          1..271
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mdtlvqqiln glvlgsvyai ialgytmvyg ilgiinfahg dvlmvgamva lsaigvlqnh
       61 fpglgnvptl cialaiaavv cavvgytier vayrplrkap rlaplitaig vsillqtlam
      121 miwsrnplpf pqllptdpln vikatdttpg avismteivi ivvaflvmag llllvhktkl
      181 gramraiaen pgvaslmgvn pnfvisatfm igsalaalag vmiaseygna hfymgfipgl
      241 kaftaavlgg ignlggamvg gvilglieql g
//
LOCUS       WP_176004115             466 aa            linear   BCT 11-JAN-2025
DEFINITION  GspE/PulE family protein [Flavobacterium agri].
ACCESSION   WP_176004115
VERSION     WP_176004115.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..466
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=52623
     Region          1..463
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mdeiiitedn rhaisnyman sykilpqevy pealvlycae ktdytditde lelllgkkvt
       61 ftpypshlve kalsryyrqe rqelsrtlnl ekgdfleell aeakslkssd ihcevyensa
      121 rvrlrvdgql ldrykldrds yqelvnkiki maklnitekr lpqdgrittp afdirvsilp
      181 tlfgekivmr llgqdaskid ldtlgfepea lkeyleairk pngiilisgp tgsgktttly
      241 atlrllndsr rniltvedpi eyilkginqv qlkedigltf saalrsflrq dpdiimlgei
      301 rdaetalmai rasltghlvl stihtnsalg tvsrlvdmgv payliaetln lsvaqrlirk
      361 lcpdckeeip yqpedfpggf ripyepdrlf rakgcnncfh tgykgrraly eivritpqvs
      421 daiktgaldt flenkeeyks lsekafdvlg agetsleeiy sillna
//
LOCUS       WP_176004128              63 aa            linear   BCT 11-JAN-2025
DEFINITION  cold-shock protein [Flavobacterium agri].
ACCESSION   WP_176004128
VERSION     WP_176004128.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 63)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 63)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..63
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..63
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6728
     Region          1..63
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mkegtikffn eakgfgfitp dnggddvfvh esglngrvre ndkvtysveq gkkgpnavnv
       61 tvi
//
LOCUS       WP_176004135              49 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Flavobacterium agri].
ACCESSION   WP_176004135
VERSION     WP_176004135.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 49)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 49)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..49
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..49
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=5320
     Region          6..>45
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mkqpalakkv aslriekglt qaelaemcnv tvrtiqries aevepealr
//
LOCUS       WP_176004158             488 aa            linear   BCT 11-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Flavobacterium agri].
ACCESSION   WP_176004158
VERSION     WP_176004158.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..488
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=55014
     Region          5..404
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mgivikqsis ntvityvgfa igaantlfmy philgkdfyg ltgyvlsaan vimplmafgv
       61 hntlvkffsg yrseqekdrf ltyllllpll vavpllilsl vfyepvaall skknpiifdy
      121 cwqipliglf mayfeifyaw vkvhlksvfg sfareillrl litaglftvf fkwisagtfv
      181 nltvliygvi tivmgisafk vrqfkadlrf penrkavfny siyiilsgsi anmlldldkf
      241 mmgfyihidn iafynvaifi atvisvpsra mhqiaypita klmaedkyie lnelykktsi
      301 slqlvgglvf vgilvnikqv ylllpaeygq gmftvfvigl skyldlilgn nnaiifnsky
      361 yravlllgll laalmiglnm flipkmgidg aalatlasia lyslskllfv vfkmklypfs
      421 kqtlysfail tatfcmfyyw dfpfhpipni alksilvtvf figinywlri spdvnsvidk
      481 gfallrrk
//
LOCUS       WP_176004164             194 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Flavobacterium agri].
ACCESSION   WP_176004164
VERSION     WP_176004164.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..194
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22377
     Region          8..190
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 matvnipdal lvknyvagde nalatlisrh qskiygfiys kvtdrdisdd ifqdtfikvi
       61 ktlksnsyne egkflpwvmr iahnlivdhf rrtkkmpmfr eteefsifsi msddapnveg
      121 qmittqvedd lkklilelpk dqkevlemri yqdlsfkeis eitgvsinta lgrmryalmn
      181 lrkvidkhqi iltn
//
LOCUS       WP_176004209             343 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Flavobacterium agri].
ACCESSION   WP_176004209
VERSION     WP_176004209.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..343
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=38549
     Region          50..333
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mkrlfvlafi gltacspdda sytdvpfais kpsnfpdfay nfeanmptqa gfelgkkify
       61 dgrlssdgti scgfchiqqh afthhghsls hgvnnevgfr ntpaiqnlaf qnvfmydgst
      121 dnldlqplip itsevemhgn ltsivtmmqs daqyrklfkr afpdaeidte hllkalgqfm
      181 vmlqssnsrf dkwrrnetga nfsgdetegy qifqqkcasc httdlqtdhs frnnglavnq
      241 qlydtgrerv thlpsdkykf kvpslrnvek tapymhdgrf ytleavlehy asgvqtsetl
      301 dpilqqngsp gialtdeqks kiiaflktlt ddeflsnpkf sef
//
LOCUS       WP_176004216             273 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Flavobacterium agri].
ACCESSION   WP_176004216
VERSION     WP_176004216.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..273
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30419
     Region          37..270
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mkkvivivlf lalgatgcaq kdlrnlmyga hkqqnldlfl pakidsktpv limlhggaws
       61 lggkeytdkt ardlrdrgfv vanvdyryvn envhakdlld dineavkymq shaseygfas
      121 kgyhfsgisa gahlamlysy trnagvksva vlcgptqfdt denkkhiekl lltqvleqla
      181 dskyekdkkp nakftaispy arisniptll fhgdkdelvl ysqsvlmlqe lkkanveskl
      241 itlegkghdc gmnqpdsekm vldnienwvr ihs
//
LOCUS       WP_176004286             601 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Flavobacterium agri].
ACCESSION   WP_176004286
VERSION     WP_176004286.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..601
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=65920
     Region          30..428
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mepaiekdvt rggqflvket ksediftped fseeqrmmrd svkefcdkkl waqkekfekk
       61 dygyteeamr kagemgflsv svpeeygglg mgfvdtvlvc dyisgatgsf stafgahtgi
      121 gtmpitlygt eeqkkkyvpk lasgewfgay cltepgagsd ansgktkavl sedgkyysit
      181 gqkmwisnag fcslfivfar ieddknitgf ivendasngi algeeehklg irasstrqvf
      241 fsetkvpven mlsergngfk iamnalnvgr iklgaaclda qrritteaak yanervqfnt
      301 piasfgairs klaematncy agesatyraa hdiqnriaar eadgaghqea elkgveeyai
      361 ecsiikvavs edaqncadeg iqifggmgfs edtpmesawr darisriyeg tneinrmlsv
      421 gmlvkkamkg hvdllgpamk vqeelmgipd fntpdyself seekemiakl kktflmvagg
      481 avqkygpdld shqqllmaaa dilieiylae stilrteklv ksigeqaaeg qiamaklyly
      541 kavdivtakg kegiasfaeg deqrvmmmgl rrftkyinmp nvvalretia ekvvsangya
      601 f
//
LOCUS       WP_176004304             157 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Flavobacterium agri].
ACCESSION   WP_176004304
VERSION     WP_176004304.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..157
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=18444
     Region          3..155
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mvfdtiyqty wnkifrlcrg ylgdddwakd vaqdtfvsvy nnlsnfrqes aistwiyria
       61 vnhclrqlek dkrlaktdvq dnladhaetr ndaqidllyr figelkeidr iiisleledv
      121 kqaeiasvtg lsesnvrvri hrikeqlsqk fkkyehd
//
LOCUS       WP_176004318             256 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Flavobacterium agri].
ACCESSION   WP_176004318
VERSION     WP_176004318.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..256
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27886
     Region          41..251
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mrkialtlfa milatsmnaq lkavsysdgs qklnglfias akpsagkpgv lilpawmgiq
       61 ehekevaqql skmgynafia diygegnypk nydeagkiag nyktkyqdyq rriqlaleql
      121 vksgananni vaigycfggt gvlemarakm nvkgvvsfhg glgkdasren gaittkvlic
      181 hgaddpyvpk edieavqkel rdgktdwqmn fyanavhaft eksvgndnsk gaaynekadk
      241 rswkaledfl netltk
//
LOCUS       WP_176004330             127 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator [Flavobacterium agri].
ACCESSION   WP_176004330
VERSION     WP_176004330.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..127
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=14097
     Region          2..127
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 masprrclfi dddaddqeff cdaalsidpq iecifadngi eamtklndsa ftpdfifidm
       61 nmpqmngret lseirkmdrl nmaavymyst aaapriteei malgatdfli kpssvkglqe
      121 mlgkilk
//
LOCUS       WP_176004397             837 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA translocase FtsK [Flavobacterium agri].
ACCESSION   WP_176004397
VERSION     WP_176004397.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12144184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..837
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=93139
     Region          46..172
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          287..825
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 martkktaet adekkdikkk rkisrrheil igsllvllsv alllsfvsff iywredqstl
       61 vswadrslka rnwlgkfgaw ladffifkgf gaasflfvkl ffltgaflvl dvplrklksi
      121 wfwdlfaliv lsvlfgffad slpelggtvg yemnvflqdy igstgtllvl vfgiiiyliy
      181 kikvspdkik gfferkksei neelakmnta tpavsdnagd aynleefate eqpnedlkfn
      241 pfpeedeedi pepvlkvask feidkealrp tiehpseisl thdpkheavl eslptptpap
      301 qiittddeaf viekapeedi veenlaarlv edfglfdptl elsnykfpti dmlkeyaggg
      361 itinqeelee nknrivetlr nykidiaqik atvgpsvtly eivpeagiri skiksleddi
      421 alslsalgir iiapipgkgt igievpnqkp tivsmknvig sskfqeaeme lpialgktis
      481 netfvadlak mphllmagat gqgksvglna vltsllykkh paevkfvlvd pkkveltlfn
      541 kierhylakl pdtedaiitd ntkvintlns lcvemdnrys llkdamvrni keyndkfknr
      601 klnpeaghrf lpyivlvvde fadlimtagk evetpiarla qlaraigihl iiatqrpsvn
      661 vitgiikanf pariafrvts kidsrtildt qgadqligrg dllysngndv trvqcafvdt
      721 pevekitefi gsqkaypnay llpeyvpege tginldidis erdalfreaa evivssqqgs
      781 asllqrklkl gynragrlid qleaagivgp fegskarsvn vpdlqaldqf faneqne
//
LOCUS       WP_176004422              66 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Flavobacterium agri].
ACCESSION   WP_176004422
VERSION     WP_176004422.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..66
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7267
     Region          1..64
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mtnnlkvqra ikdisqeela kqigvsrqti namekakyvp stvlalkiak ffgvaveeif
       61 tleetd
//
LOCUS       WP_176004427             197 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Flavobacterium agri].
ACCESSION   WP_176004427
VERSION     WP_176004427.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..197
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21626
     Region          2..184
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrkitvlsmi tldgvmqapg gpeedrsngf eyggwtasyg deaygkaieq elkpadyllg
       61 rktfeiweny wpehgdfwpg inegtkyvls gtrndsdwkn tefltnieqi eklknsdgpn
      121 iqvwgsseli qlllshdlvd elrlkihplt lgkgkklfgd agipaafslt essitskgvl
      181 lvsydragdv ktgnaga
//
LOCUS       WP_176004467             360 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Flavobacterium agri].
ACCESSION   WP_176004467
VERSION     WP_176004467.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..360
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38338
     Region          1..267
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkktrigiig anpergwasm ahipalkslp gyeisalsnr naanteilsk tfgvanivag
       61 seelakspdv dmilvairvp lhfdavrtai engksvfsew plgknlqete kltalaeekn
      121 vkgyiglqsr svpairfikd yidqgnigev lstsmigsgi iygeftpkan dytvdpvnga
      181 gminvtfgna adalcyvlge fselnattat rratttived gdiipmkiad qvavtgklls
      241 gavasihfrg gmfpgtnffw eingtkgdiq isaaggslav fepeirisag lngpmeptpv
      301 pqsynlvsdy gldyipasvg qnymliqsge aptfedallr hkmidaveka ardgssqsyl
//
LOCUS       WP_176004481             158 aa            linear   BCT 11-JAN-2025
DEFINITION  Dps family protein [Flavobacterium agri].
ACCESSION   WP_176004481
VERSION     WP_176004481.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 158)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..158
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=18154
     Region          3..157
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 mkttsigita pskdqvaqkl shiladefll ytktrnahwn iegrdfhamh iffesqykel
       61 damvdmiaer irtighyapa slqtflnlth lteriyqenn gegfmrella dhetvviklr
      121 elvdffsgkl hdqgsadfit glmerhekla wtlrahlv
//
LOCUS       WP_176004627             261 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Flavobacterium agri].
ACCESSION   WP_176004627
VERSION     WP_176004627.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..261
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28932
     Region          8..232
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 mnakeehtgn vveindlhig fggneilkgl dltlakqenl vvlgksgtgk svtikcivgl
       61 lrpdsgsvkv fgkeitamkk selddtrkdv gflfqsgaly dsmtvrenle fplrrirkel
      121 seeeierkvv ealenvslpd aidkmpsels ggmrkrvgla rtiivdpeii lydepttgld
      181 pitsdeisql ilelqkklkt ssiiithdie caktvadriv mlkdgkvykd gtledfvddd
      241 defvssffys pnqlktkkqk s
//
LOCUS       WP_176004628             395 aa            linear   BCT 11-JAN-2025
DEFINITION  AI-2E family transporter [Flavobacterium agri].
ACCESSION   WP_176004628
VERSION     WP_176004628.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..395
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=43795
     Region          28..338
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 manitklpfn aklaytllci slllgltyva qdiimpvlla llfaillrpv arffrtklkf
       61 phviasmasv avmvllilgi fillsyqiad ivndwdkikk ncsvhmanlq dyvhdtfnls
      121 kreqnkmidd atkdsmetgk sivgstltsf sdmllnlili piytflflly rthflrflak
      181 lipndkrdvl edilvrikvs vqsyiiglmi emvlvsvltg agymiigley aimlgvltgl
      241 lnlipyigit iagvlavvas ittntdfslv igvvvvnivv qlidnnllvp livsskvein
      301 afisivgiii ggalggisgm flaipmiail kvifdrirpl epwgylfgdd lpktyswhrl
      361 rlprydhdtm ettlevsgds kkakplftet ttqnq
//
LOCUS       WP_176004642             176 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Flavobacterium agri].
ACCESSION   WP_176004642
VERSION     WP_176004642.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..176
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20489
     Region          2..175
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtqeqllami vqkeerayth mynmyskslf avisnmikdk eeaedvlqes fvkiwknids
       61 yteskgrfyt wilnvtrnta idklrskgfn nskknlpsdn fvhlledssr mtyridaigl
      121 rdfvkklkpk cieiinllff kgytqqeasd elgiplgtvk tqnrncindl rnflqv
//
LOCUS       WP_176004654             170 aa            linear   BCT 11-JAN-2025
DEFINITION  PH domain-containing protein [Flavobacterium agri].
ACCESSION   WP_176004654
VERSION     WP_176004654.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Scheffzek,K. and Welti,S.
  TITLE     Pleckstrin homology (PH) like domains - versatile modules in
            protein-protein interaction platforms
  JOURNAL   FEBS Lett 586 (17), 2662-2673 (2012)
   PUBMED   22728242
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Xu,Q., Bateman,A., Finn,R.D., Abdubek,P., Astakhova,T.,
            Axelrod,H.L., Bakolitsa,C., Carlton,D., Chen,C., Chiu,H.J.,
            Chiu,M., Clayton,T., Das,D., Deller,M.C., Duan,L., Ellrott,K.,
            Ernst,D., Farr,C.L., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Han,G.W., Jaroszewski,L., Jin,K.K., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Krishna,S.S., Kumar,A., Marciano,D., McMullan,D.,
            Miller,M.D., Morse,A.T., Nigoghossian,E., Nopakun,A., Okach,L.,
            Puckett,C., Reyes,R., Rife,C.L., Sefcovic,N., Tien,H.J.,
            Trame,C.B., van den Bedem,H., Weekes,D., Wooten,T., Hodgson,K.O.,
            Wooley,J., Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S.A. and
            Wilson,I.A.
  TITLE     Bacterial pleckstrin homology domains: a prokaryotic origin for the
            PH domain
  JOURNAL   J Mol Biol 396 (1), 31-46 (2010)
   PUBMED   19913036
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology (PH) domains and phosphoinositides
  JOURNAL   Biochem Soc Symp (74), 81-93 (2007)
   PUBMED   17233582
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Lemmon,M.A.
  TITLE     Pleckstrin homology domains: not just for phosphoinositides
  JOURNAL   Biochem Soc Trans 32 (Pt 5), 707-711 (2004)
   PUBMED   15493994
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..170
                     /product="PH domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=19415
     Region          24..166
                     /region_name="YdbS"
                     /note="Uncharacterized membrane protein YdbS, contains
                     bPH2 (bacterial pleckstrin homology) domain [Function
                     unknown]; COG3402"
                     /db_xref="CDD:442629"
ORIGIN      
        1 meftnntldv tslprfeevk fnkihsdywk viliveaiif lvvgialglv yyfqqefrgy
       61 asyfglsyvv liliavwfsr lsfskkgfaf rehdvlyrdg viathtmvip ynrvqhvalh
      121 egaisrifgl akieiftagg hqsdieipgi ekeqaenikq llmgkirkel
//
LOCUS       WP_176004660             261 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Flavobacterium agri].
ACCESSION   WP_176004660
VERSION     WP_176004660.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..261
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29286
     Region          8..260
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mktidsktvv fvtgafvthk gwepwkeyfe skgyttynpa wphkegtake lrdkapndip
       61 larltlteli dhyanfikql pekpiiighs lggmitqili nkglgvagia ihpvppqpvi
      121 pyelsflrag ykvlglftsl dktytmslsd wqyaftngmt leeqkkswee nvipesktva
      181 rggltsaakv dfkkphvpll ivsgstdnii pasmnlrnfk ayktpgsvtd ykefkgknhf
      241 vlslptwkee adyildwidr n
//
LOCUS       WP_176004691             122 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator [Flavobacterium agri].
ACCESSION   WP_176004691
VERSION     WP_176004691.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..122
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=13505
     Region          1..121
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mekkkilvvd ddsrnifals avlksrnfec issstakeai dllrsdmpln yvlldmmmpe
       61 mdgyeaisii kalpnrqklp viavtaqamv gdrekcllag adeyiskpvd idklvqllsk
      121 fk
//
LOCUS       WP_176004718             125 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Flavobacterium agri].
ACCESSION   WP_176004718
VERSION     WP_176004718.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..125
                     /product="VOC family protein"
                     /calculated_mol_wt=14544
     Region          4..125
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 mkrvtgiggi ffkckdpqkm newykthlgi nvspygaqfh wkqqiesden gytlwspfpd
       61 ttkyfepssr efminytven lvalveelkk egveivdeia vyeygkfvhi rdcegnkiel
      121 wepak
//
LOCUS       WP_176004739             307 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD:protein FMN transferase [Flavobacterium agri].
ACCESSION   WP_176004739
VERSION     WP_176004739.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..307
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=33765
     Region          11..304
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mkafkrsmrl mgntfsfsav sddektaqhh ideaigeikr ieallttfda nsqtnainem
       61 agkrpvkvds evfsliersl aisritqgaf disygsldks lwnfdrnmtr lpdletakkm
      121 vhlidyrnie ldrenetvfl kregmrigfg gigkgyaaec akrlvrkngl engiinasgd
      181 ltawgfqadg kpwtigvanp dkpdfpfsyl eisgkavats gnyekfvmin gkkyshtidp
      241 ktglpisgik svtvicdnae fadamatpia vmginagmdl vnqipglyai viddynkiyt
      301 skninln
//
LOCUS       WP_176004746             453 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Flavobacterium agri].
ACCESSION   WP_176004746
VERSION     WP_176004746.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..453
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=49849
     Region          172..453
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          349..443
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(355..356,389..390,393,397..398,401,443)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mrkelllltf gllafgqvsa qteeadskev siedtynkwt ieagvgqarg mrpytegyys
       61 snpnsvlgsi rlnsyslgvr ymispkfgfk idgnydkfen nddteskpfe vqqlrfqvqg
      121 vinasrllnl eevinrfgll ahgglsygri tpkldtgidp vggpsnegrt ennlgvvfgl
      181 tpqfrildrl aiyldvssiy nfrqhfawdg hysnedqnlq gqmltgslgl syslgsnplh
      241 gdwgliedkk edeiaaldkr igdletmmnd adkdgvpdyl dvennsipgv avdtkgrmvd
      301 mnqngvpdel ekyvntsvke gatqaaqqav tdaaqngeiv kelindgyia vffdfgsvkp
      361 tpsstenvaf ilnylrnnps ttaditgyad eiggtefnks lsgkraeyir nvlikagidg
      421 srlnivpage dtsvdkdsdm arrlvrkaif hik
//
LOCUS       WP_176004765             131 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Flavobacterium agri].
ACCESSION   WP_176004765
VERSION     WP_176004765.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..131
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=14337
     Region          16..131
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mastttkigr ekykmtivss sgntliadep vhlggknsgf spfellasal gtctsatlrm
       61 yadrkgwdle evitqvsfer ddkadkatfi rhiafsgnld qeqcsrllei aekcpvhrtl
      121 egqisietil e
//
LOCUS       WP_176004780             511 aa            linear   BCT 11-JAN-2025
DEFINITION  T9SS type A sorting domain-containing protein [Flavobacterium
            agri].
ACCESSION   WP_176004780
VERSION     WP_176004780.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Veith,P.D., Nor Muhammad,N.A., Dashper,S.G., Likic,V.A.,
            Gorasia,D.G., Chen,D., Byrne,S.J., Catmull,D.V. and Reynolds,E.C.
  TITLE     Protein substrates of a novel secretion system are numerous in the
            Bacteroidetes phylum and have in common a cleavable C-terminal
            secretion signal, extensive post-translational modification, and
            cell-surface attachment
  JOURNAL   J Proteome Res 12 (10), 4449-4461 (2013)
   PUBMED   24007199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10024511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..511
                     /product="T9SS type A sorting domain-containing protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=54514
     Region          441..511
                     /region_name="Por_Secre_tail"
                     /note="Por secretion system C-terminal sorting domain;
                     TIGR04183"
                     /db_xref="CDD:275036"
ORIGIN      
        1 mikkllylll pacalgqapv vqwnrtlgts svdigmdiae tndggivvmg dawsqtsavq
       61 nahgdnemwl vklnpdgtta wnrafggals dhgrkviptq dgnyiiagtt yssngdvsqs
      121 hgmgdywiak vsasantgnv fwqksfggth ndfldqviet pdagyvlfgh srstdgqvgt
      181 nhgiedlwii kidasanivw qhvyggsged iihkaistsd ggylalgytn sndgdltqnh
      241 giedgyalki aadgtlqwsk qyggslfdvf ysavevdgay ilagttasdd gdvnqqhdvh
      301 dgwllkigmd gqileshlyg gegsdsfesi elasngdivv agntlsntgd vsgnhgqfdv
      361 wlvrfdpnld iiwqkcigas ssdvayglcl tsdggyatig ytesnneydv qpnhgiydfy
      421 vtklvpeala vdhpdpisve lfpnpvatel qlrfrdgmta dsvtitdmtg ktvlsenpvs
      481 nsvdvsslas gtyliaisag nksftskfik k
//
LOCUS       WP_176004643             194 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione peroxidase [Flavobacterium agri].
ACCESSION   WP_176004643
VERSION     WP_176004643.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Arthur,J.R.
  TITLE     The glutathione peroxidases
  JOURNAL   Cell Mol Life Sci 57 (13-14), 1825-1835 (2000)
   PUBMED   11215509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785352
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..194
                     /product="glutathione peroxidase"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004602 - glutathione peroxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043295 - glutathione binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21728
     Region          33..191
                     /region_name="BtuE"
                     /note="Thioredoxin/glutathione peroxidase BtuE, reduces
                     lipid peroxides [Defense mechanisms, Lipid transport and
                     metabolism]; COG0386"
                     /db_xref="CDD:440155"
ORIGIN      
        1 mskkiiaafv clfglcvsaq klespsqkkm nipsiydqnf kvetltgepf dlkslkgkkv
       61 mivntaskcg ltpqyeqlee lynkfkgkdf viigfpannf aeqepgtnae iaefckknyg
      121 vtfpmmskis vkgddmspiy kfltqkskng vqdsevewnf qkfllnekge lvkvvspktl
      181 ptdekiadwi ksks
//
LOCUS       WP_176004782             440 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Flavobacterium agri].
ACCESSION   WP_176004782
VERSION     WP_176004782.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..440
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47326
     Region          1..436
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 msanpnnklq kvlglgfgia ifvggtigvg ilrtpgeiat ylddgwliva cwligglyil
       61 mgcgaysela tsipkaggsy nyikrafgdy agflsgwfdy itnaiapaff civiseyiai
      121 lipeikgqtt vvavgfligf mlihvsgvrn gsivqqitsi ikvaffvali vacfwysdia
      181 vkripieprl mplgvvigff kslqmalgay dgwyavcffa eedenpnkni pkslytgaii
      241 viaiyvvinm aflhvlpaaa iadsplaasd vaktvfgqkg stivtviaif siigilnaym
      301 mipprilygl srdgffvksg tkvnkggtpi vtllcssaft lglilvgsfe vlfalatfms
      361 vivwglaycs liklrisepd lirpykawgy pftaillvgf slavflgfay sdrnsflvia
      421 aiavvsypif rliqpktnst
//
LOCUS       WP_176004802             140 aa            linear   BCT 11-JAN-2025
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Flavobacterium
            agri].
ACCESSION   WP_176004802
VERSION     WP_176004802.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..140
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=16034
     Region          5..134
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mklselpkgk kiilfdgvcn lcdsfvqfvi krdkkdefrf vplqselgek ilehigidre
       61 hidsmvlyep gvayfykssa aieiakslgg lmslsvsfkl ipnflrnkiy dyvaknrykw
      121 ygkkdscmip tpelkakfle
//
LOCUS       WP_176004813             263 aa            linear   BCT 11-JAN-2025
DEFINITION  (Fe-S)-binding protein [Flavobacterium agri].
ACCESSION   WP_176004813
VERSION     WP_176004813.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..263
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28821
     Region          <14..260
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mseelkvptm adfmaqgksp evlfwvgcsg sfddrakkit kafvrllnra gvefavlgte
       61 esctgdpakr agneflfqmq ammniellna yevkkivtac phcfntikne ypglggsyev
      121 vhhtqflksl lddgrltieg gtfkgkkivf hdpcylgran niyeapreli qkldaelvem
      181 krsrtnglcc gaggaqmfkd aepgdkeini erseealdtg skiiaaacpf cntmltdgvk
      241 nkekeaevkv ldvaeliana hdl
//
LOCUS       WP_176004857             278 aa            linear   BCT 11-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Flavobacterium
            agri].
ACCESSION   WP_176004857
VERSION     WP_176004857.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..278
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31867
     Region          23..276
                     /region_name="EEP-1"
                     /note="Exonuclease-Endonuclease-Phosphatase domain;
                     uncharacterized family 1; cd09083"
                     /db_xref="CDD:197317"
     Site            order(28,64,156,191,193,240,268..269)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197317"
     Site            order(64,268)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197317"
     Site            order(156,193,269)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197317"
ORIGIN      
        1 mklrfffpml lllmnnvqsq avkvmsynir vdfggdgenn wefrrdflad qisynnpdfi
       61 gtqegklhql kyldsalvdh ewigrgrdns etqgeysaif ynkkkfklis qntfwlsetp
      121 dvpeskswet ayprictygl fedlkskkrf yvvnthldhi separengtk lileriskln
      181 tkrlpviltg dfnsemssga yktivsqmnd arnisktkpf gpsgtfsgfk fhepvtllid
      241 yiftskgnie vlkfavlsds knckypsdhl pvlaelki
//
LOCUS       WP_176004860             361 aa            linear   BCT 11-JAN-2025
DEFINITION  inorganic phosphate transporter [Flavobacterium agri].
ACCESSION   WP_176004860
VERSION     WP_176004860.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..361
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38896
     Region          16..361
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 mdltlliiii vlalifdyin gfhdaansia tivatkvltp fqavlwaamf nfaayfiskf
       61 wigefkignt iaksvdehfi tlevilaglv aaiiwnlatw klgipssssh tllggfmgaa
      121 lahagalsdm vdgkeidvin yakvvptflf ifcaplvgmi mayfitvlil nvcrkanpnr
      181 aekwfkklql vssalfslgh ggndaqkvmg iigaavicyk ldmgdaafva adsserfklf
      241 vndgfwwwvp lasfvviglg tlsggwkivk tmgskitkvt plegvaaeta gaatlylteh
      301 lgipvsttht itgsiigvgi tkrisavrwg vtinllwawi ltipvsavia gifyyilkif
      361 i
//
LOCUS       WP_176004883             270 aa            linear   BCT 11-JAN-2025
DEFINITION  M48 family metallopeptidase [Flavobacterium agri].
ACCESSION   WP_176004883
VERSION     WP_176004883.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Lew,R.A.
  TITLE     The zinc metallopeptidase family: new faces, new functions
  JOURNAL   Protein Pept Lett 11 (5), 407-414 (2004)
   PUBMED   15544561
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..270
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=28712
     Region          64..259
                     /region_name="M48C_Oma1_like"
                     /note="Peptidase M48C, integral membrane endopeptidase;
                     cd07331"
                     /db_xref="CDD:320690"
     Site            order(135..136,139,198,202,242)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320690"
     Site            order(135,139,198,242)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320690"
ORIGIN      
        1 mknklilavs allivaacst naltgkkefn ivsndqlfps afaeynsfls qnkviatgad
       61 aqlvqkvgsk iraavekyya skgissslqg yqweyklvdd kavnawcmpg gkivvytgil
      121 pvtkdeagla tvlghevaha llnhgaqrms aaqaqaigaa glalatsgqs eerqqmyqqy
      181 ygigsqvgvm lpfsrkhese adeigltlma iagynpdnal tfwqrmsaqs ggastpeils
      241 thpsdntria dikklipqak anaaklgvky
//
LOCUS       WP_176004887             102 aa            linear   BCT 11-JAN-2025
DEFINITION  GIY-YIG nuclease family protein [Flavobacterium agri].
ACCESSION   WP_176004887
VERSION     WP_176004887.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Dunin-Horkawicz,S., Feder,M. and Bujnicki,J.M.
  TITLE     Phylogenomic analysis of the GIY-YIG nuclease superfamily
  JOURNAL   BMC Genomics 7, 98 (2006)
   PUBMED   16646971
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..102
                     /product="GIY-YIG nuclease family protein"
                     /GO_function="GO:0004518 - nuclease activity [Evidence
                     IEA]"
                     /calculated_mol_wt=12123
     Region          1..82
                     /region_name="YhbQ"
                     /note="Predicted endonuclease, GIY-YIG superfamily
                     [Replication, recombination and repair]; COG2827"
                     /db_xref="CDD:442075"
ORIGIN      
        1 mfhyvfilrc kdgrfytgit tdlakemdyh qkginrksyt yyrrpvtlew yqsfsnyqqa
       61 iaikkklsgw sgqkkaafle knfehiqtla ecrnathhky ks
//
LOCUS       WP_176005022             170 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA thioesterase [Flavobacterium agri].
ACCESSION   WP_176005022
VERSION     WP_176005022.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..170
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18765
     Region          6..150
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mlpkhpsesl ttltdlvlps etnplnnlfg gellarmdra asitarrhsr rvcvtasvnh
       61 vafnrsiplg svvtieskvs rsfkssmeif idvwiedres gvrtkaneai ytfvavddtg
      121 rpvevapilp etelekeryd aalrrkqlsl vlagkmkpde atelkalfns
//
LOCUS       WP_176005081             297 aa            linear   BCT 11-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Flavobacterium
            agri].
ACCESSION   WP_176005081
VERSION     WP_176005081.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..297
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32231
     Region          8..290
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mqtkaeqavk ttylsivgnl glalvkgavg ylgnsyalia daiestsdvf asllvlfglk
       61 yssrpadenh pyghgkaeal vtfavvgflv vsatviayes idhirtphkt papytlivlg
      121 viviikevfy rivskksddt nssslkadaw hhrsdaitsa mafigiaiav fmgpgyetad
      181 dwaalfasgf iiynaylifr palgeildeh lhhevvaqir viaqtvpgvi dteklhvrkt
      241 gmnylvdlhl tvngditvte ghdiahclkd kiqqempeva dvlihvephh laqkipt
//
LOCUS       WP_176005083             111 aa            linear   BCT 11-JAN-2025
DEFINITION  single-stranded DNA-binding protein [Flavobacterium agri].
ACCESSION   WP_176005083
VERSION     WP_176005083.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Bianco,P.R.
  TITLE     The tale of SSB
  JOURNAL   Prog Biophys Mol Biol 127, 111-118 (2017)
   PUBMED   27838363
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..111
                     /product="single-stranded DNA-binding protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=12632
     Region          6..111
                     /region_name="Ssb"
                     /note="Single-stranded DNA-binding protein [Replication,
                     recombination and repair]; COG0629"
                     /db_xref="CDD:440394"
ORIGIN      
        1 mnalrnrvql ighvgqdpei knfendkkka nfnlatsevy knergekvee tqwhriiawg
       61 knaeiiekyv gkgkeiaieg klvhrqyddk ngekkyitev vandllllgg k
//
LOCUS       WP_176005114            1053 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Flavobacterium agri].
ACCESSION   WP_176005114
VERSION     WP_176005114.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..1053
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115184
     Region          1..1035
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mfnrfiqrpv lsivisliiv flgvlaliql pvtqfpsisp pkvnvtveyp gannelliks
       61 aiiplerain gvpgmkymas dagndgegti qvvfnlgtdp nvaslnvqnr vasvtnklpp
      121 lviregvkit reesnmlmyv nlystdkntd qkflfnyadi nilpelkrvd gvgyadilgn
      181 reyamriwlk pdrmlaykis aeevmealss qsleaspgkt gessgkrsqs feyvlkysgr
      241 fttkeqyqnv vlrstpdgei lrlkdvadie fgssmydiys nlngkpsaai vlkqsygsna
      301 qqviedvkak laeikgnsfp kgmdyeisyd vskfldasid kvlhtlveaf ilvglvvflf
      361 lgdwrstiip alavpvslig tfffmqffgi tinlitlfal vlaigvvvdd aivvieavha
      421 kmeeehlkpr katqkamkei agaiiaitfl maavfipvaf msgpvgifyr qfsitmatai
      481 ilsgivaltl tpalcamilk nnhghakkkt pidkfldgfn rgfnnmagky dnilrkivsr
      541 rvvtfgvlgv fcvltyflsg svptgfipge dqgmiyaviq tppgsslert nqisqhlqki
      601 cegidgvssv sslagyeilt egtgansgtc linlkdwner kenareiiee leekskdiag
      661 aqieffqppa vpgygaaggf elrlldktgt ndykkmeqvs ndflkelksr kelqsvfsff
      721 sasfpqymlh vdndiaqqkg vsidnamntl stlvgsnyei sfikfgrayk vivqaapnyr
      781 alpsdilkly vkndrdemvp fsafmrmdkv yglseitrqn mytaseisgs papgyssqqa
      841 invinevaak tlprgygidw agiskdqvaq gnqaiwifli clgfvylils aqyesfvlpf
      901 avilslpigi fgaffllqlt glenniyaqi amvmligllg knavlivefa vqkhsegatv
      961 leaamegaav rfrpilmtsf afiagliplc lasgpgavgn rtigtaaagg mlfgtvfgvv
     1021 iipglyyifg kiaaktqfvk neeesplteq ien
//
LOCUS       WP_176005116             271 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Flavobacterium agri].
ACCESSION   WP_176005116
VERSION     WP_176005116.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..271
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29863
     Region          18..265
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 meeffndlvk niegyynqiv avtpklllgl vvivimwlia arikmfadvr lkkrmhdpll
       61 atfianlvka vliiigifmm friigltava ssilagagis afvigfalkd igenflagil
      121 lafkrpftvg diiesngvrg kvmalnlrdt qiksdgkdiy ipnallvknt linfnrggyl
      181 lqdftfgley gsdyracidl vkqilndekd vvsegknsiv vlsgivatap qvnvrywvkt
      241 dslstdgrvr sevlikvfta lkengfvlkk e
//
LOCUS       WP_176005161             934 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Flavobacterium agri].
ACCESSION   WP_176005161
VERSION     WP_176005161.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 934)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20710189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..934
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..934
                     /product="TonB-dependent receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=102474
     Region          22..106
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          81..897
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mkiylfilsl lfcgmtyaqt tisgtvsesg tglpvpgani kvtgdsaatv sdadgkfslt
       61 vskkppftve ismvsytaqt vnvtsanqtv nvslvgeetk leeivvsasr tpervmqspv
      121 tiermtaaqv kntsaptfyd glenlkevhf ntsslsfksi ntrgfatvan trflqlvdgm
      181 dnsspalnfv lgnlvglsel dvasvellpg assalygana fngilfmnsk spftnqgist
      241 yfkygktyqd aagtndyydf gfraatafsk hfagkinfty lratewiaad ersmttggvg
      301 hdinqnydgl nfygdevttf ipnvgqvsrt gyaekdlnnn kiesvkadis lhfkpfandf
      361 eiilqekvgl gttiyqganr yalknflmnq vrvevrnrnf flrgymtses agdsydmrfa
      421 awnvnraaks dtgwftdyat afqlgsafyg ldaqqagiya rkfadyndnt spvnglpalp
      481 ltphgnprli pgtpefkaal ntvtnnpdlt rgakfldnsk lyhvdgnynf kellkvvevm
      541 vggsfrqyal dsqgtiftdy dgvlrydeyg ayvqaignpt drlkltgslr ydksqnfdgf
      601 vspriaavys agdhkehnfr isyqtgfrnp ttqdqyigld lgpfaligsa pdnltryvet
      661 lpvsaagqaa gqpssvtlsg vdaynnsytl asvqafaasg npadlqvaki glvkpervqa
      721 feagyravin ndisvdingy ynlyndflnq srvitpyygv vgtdssdpnv qlgyqalgfg
      781 drrvyqvytn srtevtslgf gvglskkffk tlelganyny aefeydeked psfipgfntp
      841 khrvkayvss pniykglgfs fnyrwsdeyl yqgsfadgvv pensvidaqi sytipkwktm
      901 fkvgaanlfg edyiqvigag migqqwyaqi tinp
//
LOCUS       WP_176005179             550 aa            linear   BCT 11-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Flavobacterium agri].
ACCESSION   WP_176005179
VERSION     WP_176005179.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18640651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..550
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=63317
     Region          <66..284
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          71..97
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(73..74,77..78,80,104,113..114,117..118,120..121,144,
                     153..154,157..158,161)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          102..138
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          143..176
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <451..550
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mpfirvvlsf vfacllaqta awgqtrqdcd slivkgvkam qnqqhaksle llaeaksiah
       61 kqnwpeqefl ainniganyy illeygeald hyleaytlai rklqpkfemi vlnniailys
      121 kekkfdkade yfgkayniak enndklkigl yamnlgnvan evhkpqiard yfleaipllk
      181 nqpefsamak vgmaeseyqq grwseartsa lqiydsikns afedaktssl iiagksflke
      241 nnlpqaekyl nlliaskpnl etkitlfdml sdlhfrakrf dkalvckdsi ikinsqleai
      301 kngklletnk akfeiknyqn elvlkeakit nerrifysit aiilvilalv iwslrnrsik
      361 hkqkkliaer nqqilylele keknehllle klskenetta lleqerlkne learnrklsa
      421 kalylsgrne mieevlsels kipqlsedkv lstridslkk hlksdgqwdd fithfeevnh
      481 tflnalktkh anltandirf lsyiymnlsn keiasmlnit veacrkrker lsdkmsipeh
      541 vnlydylatl
//
LOCUS       WP_176005196             150 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Flavobacterium
            agri].
ACCESSION   WP_176005196
VERSION     WP_176005196.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..150
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16777
     Region          13..137
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mktrlnifek gkdalrplfg vgayinksti daslrhlvev rvsqingcay cldmhykear
       61 aigeteqrly glsswkeapy ytereraala waealtktkv sektyalasa hfseqelidl
      121 tivvtgintw nriqlafpsv agsyqpgqfn
//
LOCUS       WP_176005221             456 aa            linear   BCT 11-JAN-2025
DEFINITION  NADH-quinone oxidoreductase subunit N [Flavobacterium agri].
ACCESSION   WP_176005221
VERSION     WP_176005221.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..456
                     /product="NADH-quinone oxidoreductase subunit N"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=49253
     Region          4..455
                     /region_name="NuoN"
                     /note="NADH:ubiquinone oxidoreductase subunit 2 (chain N)
                     [Energy production and conversion]; COG1007"
                     /db_xref="CDD:440631"
ORIGIN      
        1 mntllaitgi gvlcllfeia nlrkaivpft vvallgtlgi tlsdygtvhs hynnmivtnn
       61 fsvsfsalfi vltiflvals gdfyrkteak isdfvsikif llagavamvs fgnlsmfflg
      121 ievlsislyi laasqrlnir sneagmkyfl mgsfasgiil fgicliygam gtfdiqeise
      181 ltgsaelpew ffigivllti gmlfkiaavp fhfwapdvye gsptlttavm stltkvvama
      241 afyklltgmn anisyeyemv imvvsiasmt vgnimalrqt nakrmlafsg ishagfmlmt
      301 llnitssagt llyyasayal agiaafavil yvcrdkened iynfnglgkt rpvlaavlta
      361 allsmagipi fagffakfal fsqtikagyl vmviaavins iisvgyyfkl ilamytkdst
      421 eeatkvpvvf yavgvlsili niaiglypsf vinlik
//
LOCUS       WP_176005278             426 aa            linear   BCT 11-JAN-2025
DEFINITION  epoxide hydrolase family protein [Flavobacterium agri].
ACCESSION   WP_176005278
VERSION     WP_176005278.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..426
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47041
     Region          30..134
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          101..>225
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mktkvskgli igvliaaapv saqkkaddsi rpyevhiade klsdlkqris atkwpdqelv
       61 kdetqgvqla tmkaladywa nqydwrkmea klnalpqfvt tidgvdihfi hvrskhknal
      121 pviithgwpg siieqmkiig pltdptkygg kaedafdvvi pslpghgfsg kptelgwnpv
      181 hvakvwiklm drlgykkyva qggdwgnavs enmaviapag llgihtnmaa tvpaeiskal
      241 aegkmpngls adeqnaykql dffykkglgy asemslrpqt lygiddspig laawmldhdd
      301 rsqkliarvf egkqegltrd dildnitlyw ltntgissar fyweasqnat ggffdprglk
      361 ipvavsafpd eiyavpkswa eraypkliyy naldkgghfa aweqpkafte elraafkplr
      421 sglnvk
//
LOCUS       WP_176005281             323 aa            linear   BCT 11-JAN-2025
DEFINITION  fasciclin domain-containing protein [Flavobacterium agri].
ACCESSION   WP_176005281
VERSION     WP_176005281.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Clout,N.J., Tisi,D. and Hohenester,E.
  TITLE     Novel fold revealed by the structure of a FAS1 domain pair from the
            insect cell adhesion molecule fasciclin I
  JOURNAL   Structure 11 (2), 197-203 (2003)
   PUBMED   12575939
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..323
                     /product="fasciclin domain-containing protein"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=33039
     Region          1..175
                     /region_name="FAS1"
                     /note="Uncaracterized surface protein containing fasciclin
                     (FAS1) repeats [General function prediction only];
                     COG2335"
                     /db_xref="CDD:441906"
     Region          178..321
                     /region_name="FAS1"
                     /note="Uncaracterized surface protein containing fasciclin
                     (FAS1) repeats [General function prediction only];
                     COG2335"
                     /db_xref="CDD:441906"
ORIGIN      
        1 mktqlkkiam lclavcawsc ssdddgsnns gqtiaeiasa nanlsvlvda ldradlvatl
       61 dgntqytvfa ptnaafnafl qangyanvda vpvaalkeil lnhvisgett ssqlatgyvk
      121 tlakgsastt ntlsmyints sgvvinggta nggatvttad vqasngvihi vdgviglptv
      181 vnhavananf svlvqaltrd dqpdfvgils gsanspftvf aptntafasl ltelslagln
      241 dipqatlekt lkyhvvtnan vlssaltdgm mvdtfagdsf tigltggpki tdfngrvsni
      301 tvtdvqasng vihvidkvll psl
//
LOCUS       WP_176005299             169 aa            linear   BCT 11-JAN-2025
DEFINITION  2'-5' RNA ligase family protein [Flavobacterium agri].
ACCESSION   WP_176005299
VERSION     WP_176005299.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Remus,B.S., Jacewicz,A. and Shuman,S.
  TITLE     Structure and mechanism of E. coli RNA 2',3'-cyclic
            phosphodiesterase
  JOURNAL   RNA 20 (11), 1697-1705 (2014)
   PUBMED   25239919
  REMARK    Erratum:[RNA. 2014 Dec;20(12):2011]
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Arn,E.A. and Abelson,J.N.
  TITLE     The 2'-5' RNA ligase of Escherichia coli. Purification, cloning,
            and genomic disruption
  JOURNAL   J Biol Chem 271 (49), 31145-31153 (1996)
   PUBMED   8940112
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..169
                     /product="2'-5' RNA ligase family protein"
                     /EC_number="3.1.4.58"
                     /GO_function="GO:0004113 - 2',3'-cyclic-nucleotide
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0008664 - RNA 2',3'-cyclic
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=18978
     Region          7..158
                     /region_name="ThpR"
                     /note="RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA
                     ligase) [Translation, ribosomal structure and biogenesis];
                     COG1514"
                     /db_xref="CDD:441123"
ORIGIN      
        1 mkywasfiav ffdadvadni lgygkanwgd hlsaykiekg anlhmtlfyl gwsdskdlet
       61 iknillgapa lpklevtgki ltfntsedcr yvtlevrhtp eiaalysyle rsllqadiff
      121 kaqgfvphit ilkmpkdlil dfhdapfplt vtgdrlslss tqstfyeph
//
LOCUS       WP_176005297             153 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator [Flavobacterium agri].
ACCESSION   WP_176005297
VERSION     WP_176005297.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..153
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=17794
     Region          2..122
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mifyadddye dleifreiad elnvelvtfn dglslierlk nppptpslif ldinmpghng
       61 lqilemirsn dhwkdvpvir fttsvgedvi rrslflgaty ylpknpdyqg vkqsvkfvig
      121 hewkdflpee ktfvhqkssm fdlpyefknd qth
//
LOCUS       WP_176005329             599 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 15 protein [Flavobacterium agri].
ACCESSION   WP_176005329
VERSION     WP_176005329.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Sakaguchi,M.
  TITLE     Diverse and common features of trehalases and their contributions
            to microbial trehalose metabolism
  JOURNAL   Appl Microbiol Biotechnol 104 (5), 1837-1847 (2020)
   PUBMED   31925485
REFERENCE   2  (residues 1 to 599)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..599
                     /product="glycoside hydrolase family 15 protein"
                     /calculated_mol_wt=69261
     Region          2..586
                     /region_name="SGA1"
                     /note="Glucoamylase (glucan-1,4-alpha-glucosidase), GH15
                     family [Carbohydrate transport and metabolism]; COG3387"
                     /db_xref="CDD:442614"
ORIGIN      
        1 mkslnygiig ncrsaalvse kgaidwcclp rfdspsvfar lldeengghf siltdrsyri
       61 eqhyientsi lstrfdngsd afevldfmpr ylnesgdsyt ppeiirhirl lrgspifrvk
      121 ydprleyase etftymkdaf iisltntkkf dslflysdfd leaittgkei alrkdgfflm
      181 gynekifvpt lerirlefer tkvywlnwsd ntpsyqnyda einrsaitlk llsyektgav
      241 laaattslpe tigevrnwdy rfcwirdasm vvkvltsigh rqqakdylrf vldllpdkde
      301 klqimygihg ekklteefle hlsgyegsrp vrignaayeq rqhdiygilm dvihqqltlf
      361 sndiengeei wnitkgivwv vgqhwqepdk giwefrteer hftfskvlcw taidravkva
      421 lllgkrekar kwqpladair kdildnawnd dieaftqsyg ssdldasvll menygfiepw
      481 npqyvstvka igrdlsndgl lyryknrddf glpsssftic tfwyinslfk igetdeaeal
      541 fekllsysnh lglfsedldf ktkrllgnfp qayshlalie tainlstltk eekiidalr
//
LOCUS       WP_176004889             642 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha-1,4-glucan--maltose-1-phosphate maltosyltransferase
            [Flavobacterium agri].
ACCESSION   WP_176004889
VERSION     WP_176004889.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Kumar,V.
  TITLE     Identification of the sequence motif of glycoside hydrolase 13
            family members
  JOURNAL   Bioinformation 6 (2), 61-63 (2011)
   PUBMED   21544166
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Stam,M.R., Danchin,E.G., Rancurel,C., Coutinho,P.M. and
            Henrissat,B.
  TITLE     Dividing the large glycoside hydrolase family 13 into subfamilies:
            towards improved functional annotations of alpha-amylase-related
            proteins
  JOURNAL   Protein Eng Des Sel 19 (12), 555-562 (2006)
   PUBMED   17085431
REFERENCE   3  (residues 1 to 642)
  AUTHORS   MacGregor,E.A., Janecek,S. and Svensson,B.
  TITLE     Relationship of sequence and structure to specificity in the
            alpha-amylase family of enzymes
  JOURNAL   Biochim Biophys Acta 1546 (1), 1-20 (2001)
   PUBMED   11257505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10571012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..642
                     /product="alpha-1,4-glucan--maltose-1-phosphate
                     maltosyltransferase"
                     /EC_number="2.4.99.16"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_function="GO:0016758 - hexosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009313 - oligosaccharide catabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0030979 - alpha-glucan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=75143
     Region          6..188
                     /region_name="GlgE_dom_N_S"
                     /note="Alpha-1,4-glucan:maltose-1-phosphate
                     maltosyltransferase, domain N/S; pfam11896"
                     /db_xref="CDD:463388"
     Region          193..548
                     /region_name="AmyAc_GlgE_like"
                     /note="Alpha amylase catalytic domain found in GlgE-like
                     proteins; cd11344"
                     /db_xref="CDD:200482"
     Site            order(246,250,261,263,306,338..339,341..342,376,378..379,
                     407,465,519..520)
                     /site_type="active"
                     /db_xref="CDD:200482"
     Site            order(324..326,333..335,348,381..384,386,389,411,413..414,
                     417,421)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200482"
     Site            order(378,407,465)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200482"
     Site            order(410..412,429,432..433)
                     /site_type="other"
                     /note="acceptor binding site [chemical binding]"
                     /db_xref="CDD:200482"
ORIGIN      
        1 mqkqtriiie nvkpqldsga ffikrvsgqi vhvtadvfsd ghdviaccvk ykhekdrkwn
       61 evrmvptand ewqaefkvek qghysylveg wvdyalnwqh gierkiqdnq hvksellegv
      121 eyvnevltia dksekeylkk iaqwftdenr yddavkeavs qelheiftky pirqlenqsa
      181 elkvyvdrpk alfstwyeff prsassedgk hgtfkdcekl lprvaqmgfd tlyfppihpi
      241 gevnrkgknn atnaetgdvg spwgigsrfg ghkathpdlg tvedfkslvk aaknlgieva
      301 mdyalqaapd hpyvkehpkw fkwrpdgtvq yaenppkkyq diqpiyfese dwknlwkell
      361 dvalfwveec dikvfrvdnp htkpfyfwgw lisevkkkhp dvlflaeaft rpkimhelak
      421 qgftqsytyf twrnskaeli eyvteltkte qkefyrpnfw pntpdinpfp lqhgneaihl
      481 iryflaatls ssvgiygpvy eymvsepltn keeykdseky qvvkwdwniq nklialiaki
      541 nfirkehasl qqtnniefcd tqtdqiiayy kwnddysdkt lmvvnldshn rqntwvklpq
      601 rfagqgvnvn dlitgnsyfw dqewnfveld pslpfhlfki sk
//
LOCUS       WP_176005404             433 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Flavobacterium agri].
ACCESSION   WP_176005404
VERSION     WP_176005404.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..433
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48096
     Region          1..426
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 mdnldaarlq maftlmfhiv facigmvmpf fmvvshfkwl ktrnpiyltl tkawqkgvai
       61 ffvtgavsgt alsfelgllw pgfmkhagpi igmpfslega affvealaig fylygwnkin
      121 ekfhwltgvi vgvsgvasgi lvvsanswmn apsgfdying qyvnidpvka llndawfsqa
      181 lhmtlaafaa tgfavagiha wqvyrkhnpa vhakafhiai ifggiaallq plsgdiaakd
      241 vakrqpvkla ameahyetek gaplyiggiv deknktvshk ieitkglsfl sfgdfdaevk
      301 glndfpkdel ppvaiphyaf qvmvgmggim alaalfyfis vrkrkwwens kfwllfaila
      361 ptgyialeag wvvtevgrqp wiihkvmrtk davtpmpgmi ysfwfyvlly tiltltviwl
      421 mrrqikvlnq kvd
//
LOCUS       WP_176005424             756 aa            linear   BCT 11-JAN-2025
DEFINITION  cation:proton antiporter [Flavobacterium agri].
ACCESSION   WP_176005424
VERSION     WP_176005424.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001476
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..756
                     /product="cation:proton antiporter"
                     /calculated_mol_wt=83288
     Region          61..467
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
     Region          481..595
                     /region_name="AANH_superfamily"
                     /note="Adenine nucleotide alpha hydrolase (AANH)
                     superfamily; cl00292"
                     /db_xref="CDD:469708"
ORIGIN      
        1 mgkirnaify vatiggfgal mywiigtgks leagrtlaqk svatahwddf vasmihnleh
       61 plaillaqii tiifvarffg wvsrkigqps vvgeiiagvv lgpslvgmyw pevsthlfpk
      121 eslgnlqfls qigliffmfv igmeldlkvl rnkahdavvi shasiifpfs lgvglayfiy
      181 erfapagvdf lsfalfcgvs msitafpvla rivqergihk trlgaiaitc aaadditawc
      241 ilavviaivk agsitsafyv iamaivyvil minvvrpflk rvgelnstre slskpvvaif
      301 lltliisayv seiigihalf gafmagvimp esgkfrnifi ekiedvsviv llplffvftg
      361 lrtqigllsd vsllstacwi vaiavigkfv gstiaakfvg qnwkdalsig almntrglme
      421 lvalnigydl gvltpeiftm mvlmalittf mtgpsldlin yfwrqpksiv pqeiemkgky
      481 rilisfansq sgktllrlas altkkqsgnt gitalhlsls semhsfdlkd yekkvfapil
      541 veseileqpv stdfkvsndi nhdithqanh gdydllligl gqsifegtil gkvlgfttqi
      601 inpdrlidkf igkeglfens pfdertrhiv lsakmpvgif ldkkneefnr iflpvfsped
      661 aflveyaqkf ihnngaqvtv ldatgdsknt temretvrhi eqiapnhiam rsdkiinkef
      721 lgeqdlmlis leswkklvds hsvwltdtps vliikp
//
LOCUS       WP_176005433             207 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Flavobacterium agri].
ACCESSION   WP_176005433
VERSION     WP_176005433.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 207)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 207)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629959
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..207
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=23428
     Region          33..162
                     /region_name="Thioredoxin_9"
                     /note="pfam14595"
                     /db_xref="CDD:434059"
ORIGIN      
        1 mkmaiaeglf rshtylkyrn iitklfadgk vtgnsqteal lgytklnesr mnrldkklvv
       61 pedlikrlla lkqkyvwlvi segwcgdsaq vvpvmnklat lspnielklv frdendalmn
      121 tfltngsrsi pklivldaet nevkgtwgpr pkgaadfiks yksqygvide taktelhlwy
      181 thdkglstqn elielmeeme vslyakr
//
LOCUS       WP_176005472             809 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Flavobacterium agri].
ACCESSION   WP_176005472
VERSION     WP_176005472.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 809)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 809)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 809)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 809)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..809
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=92701
     Region          13..379
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
     Region          425..809
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 miknwikvfi yhlrqnklfs ilntlglaig isgiifavly wneehsydaw npekdhvfql
       61 intvssdmsw pysnepagry lkavspeles ycytetgyhk dvvrfqdkki liekvfeaqq
      121 lffnyfpfqf legsadsalk densmaieen takklfgnek algkqvfmsk kayvvrgvyr
      181 lpgkssmapd litrkieqyl rdnkdqwgnf nfnlllklkn pddkekvekq leqvylvnrt
      241 akyakeegip ldefikkngt tkvlleplsm arlhstvegy pegkgnykfl limsglsvli
      301 lllsivnyvn latasaikra kevgvrriig asksnivwqf ltetvittvf sillalaive
      361 lalpfyndfl gkqlqmngse fflkivgifi vvvivagifp avyvsnfetl kvlkgnfgrs
      421 ksgvwlrngm lvlqfaiatf fvigshivyq qvhymstkdl gfkgeqvvdi iyrndydwkq
      481 pdyqkklrnr ysmlkqeilk vpgvqsltgg afsfgndans ssgftyndhq vqaknmaadf
      541 efldmmqikm legrklsaey ssdtissvlv nqtalrqmqe kqplgkkfkw ngkeftivgv
      601 vndfhiagpq qeippmiffh yktvdwmlnn tnhifvkidp ekmepalasi ekfwvknidn
      661 eypftydfvd knfartyksf vnqrnlfell navvilialf glfalasfsi errmkeiair
      721 ktlgaetssl lkelskqyla fciigfaiaf fptrmflskw ledfayqiei ttmpfilgfl
      781 ilctltlvvv vakaykatrv dvlkylkye
//
LOCUS       WP_176005546             532 aa            linear   BCT 11-JAN-2025
DEFINITION  RagB/SusD family nutrient uptake outer membrane protein
            [Flavobacterium agri].
ACCESSION   WP_176005546
VERSION     WP_176005546.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Mystkowska,A.A., Robb,C., Vidal-Melgosa,S., Vanni,C.,
            Fernandez-Guerra,A., Hohne,M. and Hehemann,J.H.
  TITLE     Molecular recognition of the beta-glucans laminarin and pustulan by
            a SusD-like glycan-binding protein of a marine Bacteroidetes
  JOURNAL   FEBS J 285 (23), 4465-4481 (2018)
   PUBMED   30300505
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Bolam,D.N. and Koropatkin,N.M.
  TITLE     Glycan recognition by the Bacteroidetes Sus-like systems
  JOURNAL   Curr Opin Struct Biol 22 (5), 563-569 (2012)
   PUBMED   22819666
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Gilbert,H.J.
  TITLE     Sus out sugars in
  JOURNAL   Structure 16 (7), 987-989 (2008)
   PUBMED   18611370
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Cho,K.H. and Salyers,A.A.
  TITLE     Biochemical analysis of interactions between outer membrane
            proteins that contribute to starch utilization by Bacteroides
            thetaiotaomicron
  JOURNAL   J Bacteriol 183 (24), 7224-7230 (2001)
   PUBMED   11717282
REFERENCE   5  (residues 1 to 532)
  AUTHORS   Shipman,J.A., Berleman,J.E. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins involved in
            binding starch to the cell surface of Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 182 (19), 5365-5372 (2000)
   PUBMED   10986238
REFERENCE   6  (residues 1 to 532)
  AUTHORS   Reeves,A.R., Wang,G.R. and Salyers,A.A.
  TITLE     Characterization of four outer membrane proteins that play a role
            in utilization of starch by Bacteroides thetaiotaomicron
  JOURNAL   J Bacteriol 179 (3), 643-649 (1997)
   PUBMED   9006015
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..532
                     /product="RagB/SusD family nutrient uptake outer membrane
                     protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=58691
     Region          43..485
                     /region_name="SusD"
                     /note="starch binding outer membrane protein SusD;
                     cd08977"
                     /db_xref="CDD:185760"
ORIGIN      
        1 mkklrfsilf iaamfsmtsc vddlnvtped ddtflseeff asspnsykqa lagvygnlsl
       61 tgatgsgssn lqgidagtsq ygrclwylqd lttdeviwsy endagtrelq rniwtadnpi
      121 llgmfsrtml svsfsneylr qttdeklqar gvtdtqllad iatyrnevra lrayayyvlm
      181 dlfgkapmvt endpinfrap qaerqelfsf ietelnevlp nlkpahsney grldqafahm
      241 vlakmylnae vyiganrynd citecnaiig anaytlesny ldnfnadnht ssemiftlqs
      301 dgivtqnyga ttvmvngevg sieqngaslg vstggwggal rlrkqfvqkf dggafdfdtr
      361 ktiisgdrpi ditsianqgq gfvitkfsnk tsagvngsnq tfvdtdfplf ryadvllmya
      421 eatlrggngs attaldyvnq lreranggts gnissgeltl dfllderare lhweahrrqd
      481 lirfgkytgg tynwawkgns lngvaipshl svfplpnqsi aanpnliqns gy
//
LOCUS       WP_176005685             774 aa            linear   BCT 11-JAN-2025
DEFINITION  T9SS type A sorting domain-containing protein [Flavobacterium
            agri].
ACCESSION   WP_176005685
VERSION     WP_176005685.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Veith,P.D., Nor Muhammad,N.A., Dashper,S.G., Likic,V.A.,
            Gorasia,D.G., Chen,D., Byrne,S.J., Catmull,D.V. and Reynolds,E.C.
  TITLE     Protein substrates of a novel secretion system are numerous in the
            Bacteroidetes phylum and have in common a cleavable C-terminal
            secretion signal, extensive post-translational modification, and
            cell-surface attachment
  JOURNAL   J Proteome Res 12 (10), 4449-4461 (2013)
   PUBMED   24007199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10024511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..774
                     /product="T9SS type A sorting domain-containing protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=85126
     Region          63..>318
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          142..162
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          163..193
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          222..246
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          704..774
                     /region_name="Por_Secre_tail"
                     /note="Por secretion system C-terminal sorting domain;
                     TIGR04183"
                     /db_xref="CDD:275036"
ORIGIN      
        1 mrnlyflffv lcyaglsaqi vnipdpafkq illehfdfdn dgeimapdet ycqcfidvdn
       61 paitdltgis afsasewhis ntsitsiytn npqgndgisn lnfiltdnpl lqsvdlsess
      121 fqylriwdsp lmttlnlnps qmhsldlnnt glsvlnltgf pdlidlwcvn nvqlasvvid
      181 aplhtlecnf npnleslsmm ntfisilnch hnklhtltvn saetinandn elvelnivqd
      241 yylsslyldv snnnlthldl sqagtlflld asnnqlesin lkngreeypw swvlsgnpnf
      301 kylcvdanel egfvnltngd cmvntycsft pggeyntiag sftfdgandg cdasdahfsn
      361 vklqvangts tedvftnnng efgffvntgn ytlspvlenp eyftvspnsa tvnftdvnnv
      421 sdhdfcvtan gnhpdlevlt yanilepgfd tnrsviiknk gnqvlsgtat lsfddtrldy
      481 vsatpaysnl atgsiswdya nlqpfesrhy tvvlnvnspm etpavnigdv fefnassaia
      541 ndetpndntf tyietavgsf dpndktcleg avvspekige ylhylirfen tgtavahniv
      601 vkdvidatkf dvsslqvldn shavntring qnvefifegi elgaeadgyv lfktktlptl
      661 tegttvsnka diffdynfpv etndaettfq alstddfnva svalypnptk neftvkstsd
      721 lksvqifdvq grllethvgs ssemqvslys kskgvyfvka isekgsavik ivke
//
LOCUS       WP_176005681             545 aa            linear   BCT 11-JAN-2025
DEFINITION  T9SS type A sorting domain-containing protein [Flavobacterium
            agri].
ACCESSION   WP_176005681
VERSION     WP_176005681.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Veith,P.D., Nor Muhammad,N.A., Dashper,S.G., Likic,V.A.,
            Gorasia,D.G., Chen,D., Byrne,S.J., Catmull,D.V. and Reynolds,E.C.
  TITLE     Protein substrates of a novel secretion system are numerous in the
            Bacteroidetes phylum and have in common a cleavable C-terminal
            secretion signal, extensive post-translational modification, and
            cell-surface attachment
  JOURNAL   J Proteome Res 12 (10), 4449-4461 (2013)
   PUBMED   24007199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10024511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..545
                     /product="T9SS type A sorting domain-containing protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=58846
     Region          308..>399
                     /region_name="COG4719"
                     /note="Uncharacterized conserved protein, UCP014979 family
                     [Function unknown]"
                     /db_xref="CDD:443754"
     Region          475..545
                     /region_name="Por_Secre_tail"
                     /note="Por secretion system C-terminal sorting domain;
                     TIGR04183"
                     /db_xref="CDD:275036"
ORIGIN      
        1 mtlpylpvlh nlivagnqit tldvsqcpsl fylnaggnpm esvfakngsi etflsvfsid
       61 pttlkficvd edqlasvqqq yydpewadlv issyctftpg gtfntisgqa kididangcd
      121 asdpampslk ikiddgsqvg ysfvnseggf sfyvgegdht ltpifenpty fnaapasatv
      181 nfpaqdgtvn tqdfcitang shqdlevtfv piggarpgfe afyqvvlrnk gnqsmsgnva
      241 isfeenvldf veasetliqn pgnltwnftg lqpfgsqvvg mmfnvnapta tppvnindvl
      301 tftavaypla sdempqdnts vldqvvvgsf dpndkqcveg nvvsaqkigd ylhyvinfen
      361 tgtfpaenvv vadlidtakf dlstfqllsa shpnstritg akvefifegi dlgvnehgnv
      421 vfkiktkntl ttgstvtnka niffdynypi etnlasttfq nlqtgdfvqd asvvvspnpt
      481 sgmvrikads dihsvsvydm qgrivsaelp sandfvldmg rnqsgiyflk iitakgisie
      541 kvmkk
//
LOCUS       WP_176005708             503 aa            linear   BCT 11-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Flavobacterium agri].
ACCESSION   WP_176005708
VERSION     WP_176005708.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..503
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=55754
     Region          1..414
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 msqlkkgaal syvtiiltng igllltpfii khlgdseygl ytligsligt isvldfglnn
       61 tivrfvakfr akqdrqaedn flatvmiiyg iisaviaivg iglyfnladv fekltpaele
      121 kakimfsili fnlaitlpgg aftaicsaye hfvypralni ikycvrslmv vglllwggds
      181 vsivvldtvi nvivismnay yvlrilkarf klysfemqlv reifkysiwi fifamvgqfq
      241 wragqlilgd migpkavgiy gvgillgtyy gafstaisgv flpratkmtv leakadeltd
      301 qmtrigrfsl iillmilggf llygrqfvhl wvgdnyrdsf ivaiiimfsy tlplvqsfan
      361 silearsmfs fkavtyisli aigtgigawl tqfyglvgii ygsaggwils qiimniyykr
      421 virleigrff kelfggllpa flvilligyg idflpgknwl nlvlkisafg ivycalvykf
      481 gmnaseravi sssipflkkk sha
//
LOCUS       WP_176005496            1011 aa            linear   BCT 11-JAN-2025
DEFINITION  leucine--tRNA ligase [Flavobacterium agri].
ACCESSION   WP_176005496
VERSION     WP_176005496.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   ALLEN,E.H., GLASSMAN,E. and SCHWEET,R.S.
  TITLE     Incorporation of amino acids into ribonucleic acid. I. The role of
            activating enzymes
  JOURNAL   J Biol Chem 235, 1061-1067 (1960)
   PUBMED   13792726
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423059
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..1011
                     /product="leucine--tRNA ligase"
                     /EC_number="6.1.1.4"
                     /GO_function="GO:0002161 - aminoacyl-tRNA editing activity
                     [Evidence IEA]"
                     /GO_function="GO:0004823 - leucine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006429 - leucyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=115498
     Region          1..1010
                     /region_name="LeuS"
                     /note="Leucyl-tRNA synthetase [Translation, ribosomal
                     structure and biogenesis]; COG0495"
                     /db_xref="CDD:440261"
ORIGIN      
        1 mkynpneiea rwqkywaenn tfaasnhsek pkyyvldmfp ypsgaglhvg hplgyiasdi
       61 yarykrhqgf nvlhpqgyds fglpaeqyai qtgqhpektt keniaryreq ldkigfsfdw
      121 erevrtsnpd yykwtqwifi qlfnswynfd snraesictl idkfekegna nvnaasddni
      181 eifdaafwns lspkaqdril lkyrltylae tevnwcpglg tvlandeivn gvserggfpv
      241 irkkmtqwsm risayaerll qglndidwtq slkdaqtnwi gksvgasvkf qvvgyeaemv
      301 adpddpiiev fttrpdtifg vtfltlapeh elvskivtee qkaeidayid atskrserer
      361 madvktisga ftgayaihpf tglpipiwig dyvlagygtg avmavpagdq rdydfathfk
      421 ipienifegi diskeayask dnvklknsdf lngldyksat kkvveeleqi nagkgktnyr
      481 lrdavfsrqr ywgepfpvyy keglpqmidl qhlpivlpev ekylptedgs pplgnasvwa
      541 wntetnqvvs ndlidektif plelntmpgw agsswywlry mdahnnerfv seqaeqywqn
      601 vdlyiggseh atghllysrf wnkflfdrgf iskdepfkkl inqgmilgms afaysvilrn
      661 etagsvtisr pekpllvsyr yyekiqkkld eriskgglna yvdpedliwk eehyevvrkl
      721 eernpsvfeg hepdfslqkl hvdvslligt sdeldvekfk lwrdefaead flfedgkyit
      781 grevekmsks kynvvnpddi ceeygadtlr lyemflgple qakpwntagi tgvfgflkkl
      841 wklyfddngl vvtsneaskd alktlhktik kvqddiegfs fntsvsqfmi avneltamnc
      901 hertilepla ilispyaphi aeelwhqlgh qtsistapfp tfnpehlies skeypvsfng
      961 ktkfsielgl dlnpkqieei ilkdertitq lggnapkkvi vvpgriiniv l
//
LOCUS       WP_176005725             288 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Flavobacterium agri].
ACCESSION   WP_176005725
VERSION     WP_176005725.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 288)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..288
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32796
     Region          25..288
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mdsrakdenw dlvikghssl fdlkfrdvwr yrdllrmfvk rdfisfykqt vlgplwfflq
       61 pmfttivytf vfgsvagist dglpkplfyl cgitawqyfs ecltktstvf rdnasifgkv
      121 yfprlimpls ivvsnlvrfg vqlllllccm vyfylkgydf gftsaillfp ilvvmmallg
      181 lgtgliital ttkyrdltfl vgfgvqllmy gttvvyplht vqqkhpdfaw ivelnpmtgi
      241 ieayryaflg sgafdyaslf ysavvtlvll lagvlifnkt ernfvdti
//
LOCUS       WP_176005712             241 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 32 protein [Flavobacterium agri].
ACCESSION   WP_176005712
VERSION     WP_176005712.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Yoko-o,T., Tsukahara,K., Watanabe,T., Hata-Sugi,N., Yoshimatsu,K.,
            Nagasu,T. and Jigami,Y.
  TITLE     Schizosaccharomyces pombe och1(+) encodes
            alpha-1,6-mannosyltransferase that is involved in outer chain
            elongation of N-linked oligosaccharides
  JOURNAL   FEBS Lett 489 (1), 75-80 (2001)
   PUBMED   11231017
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467330
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..241
                     /product="glycosyltransferase family 32 protein"
                     /EC_number="2.4.-.-"
                     /calculated_mol_wt=28001
     Region          1..127
                     /region_name="OCH1"
                     /note="Mannosyltransferase OCH1 or related enzyme [Cell
                     wall/membrane/envelope biogenesis]; COG3774"
                     /db_xref="CDD:442988"
ORIGIN      
        1 mipkvihycw fgrnplppla ekciaswkkf lpeyeiiewn ednfpiddfi ftkqalenrk
       61 fafvsdvarl yamdkmggiy mdtdvevlkp ldeflhhtaf sgfenddfvp tgimasekgg
      121 awvkelltyy ddkpfvnadg smettsntfi itqmmkkkgf kmtntfqeie gyvtfypndy
      181 fcpksyktgk leltensaci hhfakswipa karwrnnfkm kvmnivgpkp vqfvidiikr
      241 r
//
LOCUS       WP_176005843             299 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Flavobacterium agri].
ACCESSION   WP_176005843
VERSION     WP_176005843.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..299
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33327
     Region          35..297
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 maqaikkqal grglsallkd penniqsadd knadkvigni ieleldliei npfqprsnfn
       61 eealqelavs irelgviqpi tvrktdfnky qlisgerrlr askiagltti payiriandn
      121 dsltmalven iqrhdldpie ialsyqrlid eisltqeqms ervgkkrsti anylrllkld
      181 piiqtgirdg fismghgrai iniedhdaqt diyhkiisqn lsvretealv knyhesllpk
      241 sakskssgfs vdieqkkaia syfgtkvdvk vaangkgkit ipfhseedfn rivkliqgs
//
LOCUS       WP_176005904             519 aa            linear   BCT 11-JAN-2025
DEFINITION  T9SS type A sorting domain-containing protein [Flavobacterium
            agri].
ACCESSION   WP_176005904
VERSION     WP_176005904.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Veith,P.D., Nor Muhammad,N.A., Dashper,S.G., Likic,V.A.,
            Gorasia,D.G., Chen,D., Byrne,S.J., Catmull,D.V. and Reynolds,E.C.
  TITLE     Protein substrates of a novel secretion system are numerous in the
            Bacteroidetes phylum and have in common a cleavable C-terminal
            secretion signal, extensive post-translational modification, and
            cell-surface attachment
  JOURNAL   J Proteome Res 12 (10), 4449-4461 (2013)
   PUBMED   24007199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10024511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..519
                     /product="T9SS type A sorting domain-containing protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=55144
     Region          457..518
                     /region_name="Por_Secre_tail"
                     /note="Por secretion system C-terminal sorting domain;
                     TIGR04183"
                     /db_xref="CDD:275036"
ORIGIN      
        1 mkkklllfaa mllfssnsha tryyvnasat gngngltwvn aftslqaais atiagdeiwa
       61 atgtykpgts rsasfvmkng vnlyggfagt etmlsernia tapttlsgdi gtlgnnndns
      121 ykvmkienit igitldgfri vsgynqndgs egagafiqdn pgiitiknci fydnyaygyg
      181 gglfidqsdv nfenceflyn snfdygggai yasnvsgsni tlikckfvgn tsrsgaaisf
      241 dgpnliidrt vfcgnaatsy siigvgptqt fkmtnclvvg nqfggsygtl msisppnans
      301 cylvnntich nksttpdaml ypgirtlnng ahfrnciiyd nhtsgayqlp stnytannil
      361 sgslptgtnn vftdplfanp gslagapfds safdysltss spginsgnat yliagyntld
      421 lngneriqqg vvdrgaiesp flstpehvlg aadyifsdgv ltfkniddfa gkdltiynmr
      481 gqsvhsvrie engirlnlts glyfvsidnk siakkiivp
//
LOCUS       WP_176005928             257 aa            linear   BCT 11-JAN-2025
DEFINITION  O-methyltransferase [Flavobacterium agri].
ACCESSION   WP_176005928
VERSION     WP_176005928.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..257
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29156
     Region          93..247
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mwtqvksylr flskstnehg vhspfvfdlv tkcfydrsdy peyttlgnyr ksllqnhkti
       61 svtdfgagsr vfksnerkvs diaknagisa kraellfris ryfkpetile igtslglats
      121 alalgnssak vislegcant aseakrqlek sgisnaeitv defesglnrl sdkkfdliyf
      181 dgnhqkdatl ryfetllkta sndsvwifdd ihwsegmtea weiikkhpkv tvaidtfqwg
      241 fvffrkeqek edfvira
//
LOCUS       WP_176005935             203 aa            linear   BCT 11-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Flavobacterium agri].
ACCESSION   WP_176005935
VERSION     WP_176005935.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..203
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22884
     Region          2..193
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mkiicigrny ashiaelqne rpdepviflk pdtavlpkqf pfvipefsqd vhhevellvk
       61 inkvgkyida kfahkyydei glgidftard vqqrlkekgl pwekakafdg savigdflsk
      121 kifsshesit feltnngktv qkgdsasmlw kideiisyvs qyftlrtgdi iftgtpegva
      181 kvstgdvleg fiedkklfri qik
//
LOCUS       WP_176006006             194 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Flavobacterium agri].
ACCESSION   WP_176006006
VERSION     WP_176006006.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..194
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21667
     Region          4..168
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 magrnktfde kdviakaalv fwekgydgss addllkamgi gkgsfylffk ggkrelyeka
       61 mrqyvdqllg rirkdllgsd driqylkdff msiptaefgq ivkgclmgnv laemsakdev
      121 irdlasrllm eledvftqvi aeakasgklk ttasaellgr hlinlwngln ltdrmypnda
      181 lmqelvaknl elln
//
LOCUS       WP_176006037             201 aa            linear   BCT 11-JAN-2025
DEFINITION  trimeric intracellular cation channel family protein
            [Flavobacterium agri].
ACCESSION   WP_176006037
VERSION     WP_176006037.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..201
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22193
     Region          1..195
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mfyylnvigt mafavsaslt amnkkldpfg vfviafatsv gggtlrdvli gytpvgwmrd
       61 lnvvyfiiag falavifrkk ldklrvslfl fdtiglgvft ligiergiat glhpvicval
      121 gtmtacfggv irdilcneip vifrkeiyat lcivggiiff tirnnfdinq dllyilvsai
      181 iivlrllavr ykwylapldr y
//
LOCUS       WP_176005813             262 aa            linear   BCT 11-JAN-2025
DEFINITION  zinc ribbon domain-containing protein [Flavobacterium agri].
ACCESSION   WP_176005813
VERSION     WP_176005813.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Rigden,D.J.
  TITLE     Ab initio modeling led annotation suggests nucleic acid binding
            function for many DUFs
  JOURNAL   OMICS 15 (7-8), 431-438 (2011)
   PUBMED   21348639
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446337
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..262
                     /product="zinc ribbon domain-containing protein"
                     /calculated_mol_wt=30087
     Region          9..242
                     /region_name="DR0291"
                     /note="Predicted nucleic acid-binding protein DR0291,
                     contains C4-type Zn-ribbon domain [General function
                     prediction only]; COG1579"
                     /db_xref="CDD:441187"
ORIGIN      
        1 matsvkelsv edklralydl qlidtridei rnvrgelple vedledevtg lstrldkfks
       61 eleviedsik srktaiedhk eaikkytkqq etvrnnrefn altkevefqe leiqlaekqi
      121 kemkasiehk kevisqskek letksshlkh kkseledima etakeegfla eksaeyraqi
      181 edrllmaydr irtsvrngla vvsiergasa gsfftippqt qveiaarkki itdehsgril
      241 idnvlaaeer ekmdqlfsef kh
//
LOCUS       WP_176006094             242 aa            linear   BCT 11-JAN-2025
DEFINITION  metallophosphoesterase family protein [Flavobacterium agri].
ACCESSION   WP_176006094
VERSION     WP_176006094.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10065661
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..242
                     /product="metallophosphoesterase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=28005
     Region          6..219
                     /region_name="MPP_PPP_family"
                     /note="phosphoprotein phosphatases of the
                     metallophosphatase superfamily, metallophosphatase domain;
                     cd00144"
                     /db_xref="CDD:277316"
     Site            order(9,11,37,41,67..68,128,158,184)
                     /site_type="active"
                     /db_xref="CDD:277316"
     Site            order(9,11,37,67,128,184)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277316"
ORIGIN      
        1 mnrtlvigdi hgglraleqv feradvstdd kliflgdyvd gwsespqvld ylmalsqthe
       61 ciflrgnhdd llmewlrgke nklwhqhgge atilaysilp etikehhiaf ldslrnyyld
      121 gqkrlfvhag ftnlhgvdye yyprllfwer tlwetalald pkigpdhily pkrftvynei
      181 yightpvtri dettpqnran vwnidtgaaf kgklsvldie tkqfwqsdcl pdlypneigr
      241 nk
//
LOCUS       WP_176006146            1057 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Flavobacterium agri].
ACCESSION   WP_176006146
VERSION     WP_176006146.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..1057
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115498
     Region          1..1036
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mlktfiqrpv lstvisilit ilgilgllsl pveqypeiap ptvqvtatyt ganaetvlns
       61 vvipleeein gvegmtymts saandgsaki tvffelginp diaavnvqnr vsratsklpq
      121 avvqtgvttf ksqtsalmfl sifsnnpeyd gtyvqnyaki nlvpklqrvk gvgqvnvfgg
      181 kdysmriwid pekmaaykvs pkdvqaalne qnveaapgkf genaegvyey vikykgrlsk
      241 teeyenivvk atgngqfvrl kdvadielga fnyaqknygm gqqgvamgvf qtsgsnandi
      301 ieevesimte akadfpegid yvipfntktf ldasiekvis tlieafilvf ivvfiflqdl
      361 rstlipaiav pvaivgtfff lnvfgfsinl ltlfalvlai givvddaivv veavhskmdq
      421 geksakkati samseitgai isitlvmaav fipvsflkgp sgvfytqfai tlavailisa
      481 vnaltlspal calflkphde hehekkknfk drffiafnsg fdrmndryvk slgflfkrkw
      541 itvlglavfa gaiillfkst psgfipnedr giimaditlp pgttleqtdk viqkfdsilk
      601 tmplvearmn ivgfsllnsv nggsyafsvi klkdwkerke dnqsvdaivg elfaktagfn
      661 darmlfftpp svqgfgtadg felkiqdkgd ddwqkvnqvt geflgalnqr peiayamtnf
      721 npnfpqyrmd invekakdag vsvsdifntm qgyygglytt dfnrfgkqfr vmiqskpear
      781 adensinhiy vknangeqva isqfitlsri ygpeavarfn mlkavningk akpgfssgda
      841 ikavqevaeq hlpktygyef sgmtreeiia gnqaagvfll slifvyflls aqyesylipl
      901 avilslpvgi agaigfvkla glenniyfqv alimliglla knailivefa mqrrkhgmei
      961 wqaaiegaka rlrpilmtsf afifglmpla langvgavgn rsigmgavgg mlvgtifgvf
     1021 aipvlyvife slqerisgqp hdadydedqd qpktvte
//
LOCUS       WP_176006148             618 aa            linear   BCT 11-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Flavobacterium agri].
ACCESSION   WP_176006148
VERSION     WP_176006148.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 618)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..618
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=70968
     Region          <168..249
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          210..354
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
ORIGIN      
        1 mkrfqhliis lfliasmnak adswidptwr kmldnsdvva lveyvssgdf nakakivsmy
       61 kgalkvgdvi eisefsnryg pidkmekgdr yvvflnrrdk sdqvlsyyvq sptsgdlkvk
      121 gknvqydlts ttfhqnqhfh slkqfeefle ayydrkkapk lisqlrprll sdadpevvaq
      181 hlmklyflgf defeevydef adygsvttky alaqllgnvr ndqsrevlfk llkddsslvq
      241 geavrqlkke pieivgpllv ehlktassrn ygpinlmdpv mnrsdggkne iiralgemry
      301 kaavpallpl lntndpdqfk lvveslkaig skeyipyfns nllqkneela stiatfivsd
      361 slneclpslk yfisncnrns rrdqswmitn lsalkssdik nfllfdyqrf qtyadtlesr
      421 kqlkwnaayi esftrlktke arpyiyasiy dwmgispdfv rnpalfdlkk seeralsekf
      481 nslpdfknyk lshdiafire seestgkkva vyhmievvip seeepksarq riaklleiap
      541 knvyirfdsg ayynesqdrf dekrpnnpan lfieyakaip nqkdaaflqa lidngyisep
      601 yykeraldai ksikvalp
//
LOCUS       WP_176006306             462 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Flavobacterium agri].
ACCESSION   WP_176006306
VERSION     WP_176006306.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..462
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51828
     Region          115..452
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 msklqnlmfl llltavsgsa qiltmpeaiq tgvanygtvk akenyakasg etvkqtrrdy
       61 lpnlvlsgqq dygtvngqng plygyggygv assgipldhq nwnaafgaly lanvnwefft
      121 fgryrerinl akadlarnqa dyqqelfqhq irvaaaylnl lasqrlvrsq qknldrakvf
      181 lntsgarvkn glnpgvdstl asaevsraki elnrvldlvk eqnnrlaflm gtdvrdfqld
      241 tslvtkipnn vlalqtsads vnpilkyyks rldfsdqqvk lyrknyypsf slfgvfqtra
      301 sgfepeytqd qtqfsrnyfd gispdrqnyl vgvgvtwnlt nilrtskqvs aqkfvseglk
      361 neydvidkql ktqsdaadak iryamdnyne sprqvaaakq aylqrttlyk nglttltdvt
      421 qalyilnrae tdndviftnv wqslllksaa tgdfnlflte fq
//
LOCUS       WP_176006307            1078 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Flavobacterium agri].
ACCESSION   WP_176006307
VERSION     WP_176006307.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 1078)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1078)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1078
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..1078
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=117856
     Region          1..1049
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnlirfalrk pisilvlvag lfffgigavr dikvdilpkm nlpviyiahp fggytpdqme
       61 ayyaknyini llfangiksi etkniqglml mkltyypgtn maqaaselsa lsnriqaifp
      121 pgsqppfiir fdasslpvgq lvlsspirsn nelqdmaniy vrasftqipg llapapfggs
      181 prtilvdvdp yllrshnltp dqiveairln nqtappgnvr igdknyltpt nftireiadf
      241 ekiplfknnv qnlylgdvak vrdgadvvag yalvngkrsv ymsiaksada stwdvvknlk
      301 aalpkikstl pedvqlsyef dqsvyvmnsv kslvtegiig ailtglmvll flgdrraali
      361 viltipisii sgvlflqlfg ftinlmtlsg lalaigilvd estvtienih qhfdmgkpka
      421 laiwdackei alpkllillc ilavfapaft magipgslfl plalaigfsm itsfllsqtf
      481 vpvmanwlmk thhkekefpa hsadtfeshs ilverddfnd dgkisrferf rnrfmklidr
      541 lftirkkval vyllgvtala vvalnligqd vfpkvnasqf qlrmrapagt rverteekan
      601 avlaeikkla genhvsvtsv yvgqhpslfs inpiylftag pheavfqigf kdneldldkf
      661 kdnlrnslak klpdvklsfe pieltdkvls qgsttpieir isgkvkklne eyaqklvekl
      721 qktpylrdvq iaqpvkypsl nididrvraa qlgvdmsdis rslvastsss rlteknnwid
      781 ektglsysvq vqvpldqmrt endikeipva rnqarpvlgd vatispsfth gendnlgaip
      841 yvsvtanisd kdlgtavkdv rkdiaslgel prglfvepvg mgivleetmg slqsgllvai
      901 vviflmlaan fqsfkvsfvv lttvpavvlg sllmlfitgs tlnlqsymgi imsvgvsian
      961 avllvtnaeh lrrvngnamq sareaaglrl rpiimtsiam iagmlpmaig hgeggdqvsp
     1021 lgraviggll fstfavlvil pmifawvqgn attqsvsldp edeqskfyva pntpdnek
//
LOCUS       WP_176006320             586 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Flavobacterium agri].
ACCESSION   WP_176006320
VERSION     WP_176006320.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..586
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=65809
     Region          15..559
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mkrsllivll fcafssiaqt adlivfngki atmhkpnefv qavavkdgli ldigkssdil
       61 kkhsgnatqk idakgktvip glndshihvi reglnynael rwdgvktlkr amemlreqaa
      121 rtpqgvwikv vggwneyqfa ekrqptieei naavpdrpvf isylygkafv nkkglevlgy
      181 dnntkyegsl lekdangnlt gvmyaketpk aiyttlgltt klspeeklns siqfnrelnr
      241 fgltsaidaa gggqnfpady atslelakqn kltlrisyyl faqqkgkelq dyekwvyetk
      301 inkndnlfva ngyseegage nlvasaadfe nfleprivls demeqdlepi irllvknrwp
      361 frlhatyges iermltvfek vnkeipfdgl rwlfdhaeti tpaqmervkk lgggiavqfr
      421 myfqgelyek mygaptvqip pinqmlkigi pvgmgtdatr istynpwmam hwlltgktlg
      481 gmqfwpvses ldkfdalkly tsgsawfsge envkgklikg myadfavldh dyfsiapddv
      541 rqiesvltvv ngkvvyatde fktlqpvvpv vipdwspvky fggyqk
//
LOCUS       WP_176006322             275 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Flavobacterium agri].
ACCESSION   WP_176006322
VERSION     WP_176006322.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..275
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31294
     Region          3..259
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mlpnanktil fitgafighs swnnwiayfe ehgyttitpa wpgkdaspdi lrkrhpdaqv
       61 aairlrdlie fyedicdkqp eppivighsi ggliaqllav kkkasmavai hsvpprgift
      121 frfsfykagw gplgfftspk ktffmslkqw kyaftngmpe dwqeasyfsy aipesklvvr
      181 dtitkdasvd fssehapllf iagendntip aslnednyrk ysdldsitdf klfpgrnhfv
      241 lgqpgweeia syisdwikeq erlqynhktl knqyl
//
LOCUS       WP_176006330             526 aa            linear   BCT 11-JAN-2025
DEFINITION  S41 family peptidase [Flavobacterium agri].
ACCESSION   WP_176006330
VERSION     WP_176006330.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..526
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=58894
     Region          42..355
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mknnlkylpi llfgtlalgi liggmlnfpt qsltpkaslh knkldrlidf idneyvdkvn
       61 tdsivdvtvn silgqldphs vyispdeqee vaqsmkgdfv gigvnfymyk dtvavimpve
      121 ngpsekagil pgdrilyagk tklfgrklpt dslftklkga egsavqltvf rkstnktfkv
      181 nvtrdivpik svdvatmlna tvgyirinrf aettydefed glqrlkkrga keividlrdn
      241 gggylekave iaddflsdkk livftknkkg rtdrtyatsg gsfengkidi linensasas
      301 eilagaiqdn drgtiigrrs fgkglvqrem dfedgsavrl tiaryytptg rsiqkaydkg
      361 kddyfkdfdk rfesgelyek dsihiadtlk frtpkgkivy ggggivpdvf vplevehgde
      421 gvaylmqsga vsyfvfeqld mhrndfkgls feqfkdkmek devyyvnfqk ylqrnglelk
      481 idknrslvkr ylaaefarql fgeekyfdiv lpgdamikav legktn
//
LOCUS       WP_176006337             130 aa            linear   BCT 11-JAN-2025
DEFINITION  HIT family protein [Flavobacterium agri].
ACCESSION   WP_176006337
VERSION     WP_176006337.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..130
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=14861
     Region          1..126
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 msifskiisg elpaykited ehylafldin pnakghtlci pkkevdkifd ldsdeyiglm
       61 kfsrrvakal ekavpckrvg maviglevph ahvhliplnh mdemrfeqkv klqpeefeki
      121 vhdireklll
//
LOCUS       WP_176006340             759 aa            linear   BCT 11-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Flavobacterium agri].
ACCESSION   WP_176006340
VERSION     WP_176006340.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..759
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=86058
     Region          5..755
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mfkkiafllf tisassqmvn eitdpvewvn pligtqsnpg fsngntypai ampwamnfws
       61 pqtnkmghgw mygytdmkir gfkqthqpsp wmndygqfsi mptvgkikvk eddresffsh
      121 kaeiakpyyy svyladydmt teiapteraa mfrfsfkktd sanviidgfd kgsyvkiias
      181 enkiigyttk nsggvpanfk nyfvikfdrk fdasgtfsgd vfsagnteiq adhagavltf
      241 kiregeqlva rvassfispe qaelnlkevg nrsfesiknq gkqqwndvlg kvkvsggtid
      301 qmrtfyscly rsvlfprkfy efdkegnpfh yspyngqvlp gymftdtgfw dtfralfpfv
      361 nlvypemgak mqeglvnayk eggwlpewas pgyrdimvgn nsasivseay lkglrgydie
      421 klyeallkga nnagpmeavg rfgadyyktl gyvpydvkin enaartieya yddfaiyqla
      481 kllkkpkkei efyknrslny kklfdkssgl mrgknkdgkf qspfnpfkwg daftegnswh
      541 ytwcvfhdvn glaelmggke kfamkldsvf slapvfddsy yggtiheire mqvanmgqya
      601 hgnqpiqhmp ylynyagkpw ktqywvreim nrmylptpdg ycgdedngqt sawyvfsalg
      661 fypvtpasne yvlgaplfrk aeisldggkk isisaeanss enryiksatk ngqpftenfl
      721 rhdeiikgve lkfdmsnepn tkkgttdeda pyslslekn
//
LOCUS       WP_176006365             109 aa            linear   BCT 11-JAN-2025
DEFINITION  YegP family protein [Flavobacterium agri].
ACCESSION   WP_176006365
VERSION     WP_176006365.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007345
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..109
                     /product="YegP family protein"
                     /calculated_mol_wt=11710
     Region          1..56
                     /region_name="YegP"
                     /note="Uncharacterized conserved protein YegP, UPF0339
                     family [Function unknown]; COG3422"
                     /db_xref="CDD:442648"
     Region          55..109
                     /region_name="YegP"
                     /note="Uncharacterized conserved protein YegP, UPF0339
                     family [Function unknown]; COG3422"
                     /db_xref="CDD:442648"
ORIGIN      
        1 mgkfviskrs ngqfqfslka gngqeilsse syttksacen gvesvrknaq nedmfdkkls
       61 aggkpyfnlk asngqvigts emyetdnard ngirsvmena psatvddqs
//
LOCUS       WP_176006371             170 aa            linear   BCT 11-JAN-2025
DEFINITION  RDD family protein [Flavobacterium agri].
ACCESSION   WP_176006371
VERSION     WP_176006371.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..170
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=19375
     Region          1..147
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 meyalrelei pdhllassgq rfanyivdyi aenamnfgii iilgyfmdti sassdgfffw
       61 rstsllqvfi glfwsltyyt mfelltgrtl gkfvtgtivv sktaqkptal qilgrslsrl
      121 ipldafsflf msagwhdrip ktrvvrksdy eqyirqvdel deigknqesl
//
LOCUS       WP_176006428             227 aa            linear   BCT 11-JAN-2025
DEFINITION  SCO family protein [Flavobacterium agri].
ACCESSION   WP_176006428
VERSION     WP_176006428.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..227
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25481
     Region          62..227
                     /region_name="Sco1"
                     /note="Cytochrome oxidase Cu insertion factor,
                     SCO1/SenC/PrrC family [Posttranslational modification,
                     protein turnover, chaperones]; COG1999"
                     /db_xref="CDD:441602"
ORIGIN      
        1 mknksyiwvs lvvlvfgiiv ipnivdrfkr gdvvrgrdld kvdnhvegeg elftlakapk
       61 feltdqngkk itnadydgkv yvlefffttc pticpkmnqn mlelqkkfyg npnfgiasis
      121 inpehdtpqv lkehaealgv tssnwhmmtg nrdyiynlan kgfnlyagtd pnseagfehs
      181 gmfalidkng nircrkdqyg nptayydgie kagvqaimqd iqillke
//
LOCUS       WP_176006434             414 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Flavobacterium agri].
ACCESSION   WP_176006434
VERSION     WP_176006434.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 414)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..414
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45755
     Region          5..414
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mfnierwqei feaisknklr tfltgisvas gifilvillg agkglqngie kqfardaegi
       61 ievwsgvttk eykglnpgry vqmhnsdyel alqklgdqmv lksagaglwq tqfaykketg
      121 syqirganad mqgienmtlt ngrfvnqndl lnrekvavig eklrltlfkg inpigeifti
      181 ngipfkvigv ftdpggeree sraflpfttt qnvfglgqni nnmfytlkra dnydkalaes
      241 ekfkndlqsm lkaknivapd degaiqvhns vedakkfydl nlyirlffww vgictivagv
      301 vgvsnimlii vkertkeigi rkalgaspfs ivvmilhesi fittiagfig llaslallef
      361 vgpmitseff vnpqvdfnva ittlvllvia gagagffpay raakikpiia lree
//
LOCUS       WP_176006435             421 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Flavobacterium agri].
ACCESSION   WP_176006435
VERSION     WP_176006435.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 421)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..421
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45670
     Region          5..421
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mfdrdkwgei lqalsanpvr taltafgvfw gifilvilla agkglengvk kgfsgiatnt
       61 mfiwtqvssk pykglpigrd fnfknddvpa lkatfpdlly vsprnqlggy qgannvvrgd
      121 ktgafgiygd ypeltsqesm siirgrfvnh ndinakrkva vigegvinlm ykpgeevigs
      181 yikingvtfm vvgvyksrnn dgggieeaqk nifipfttfq qafnfgdtvg wmaitakdga
      241 sitdlkkdiv nflkarhtih pdderaignf dlyeeyskvt glfmilrfia yfvgtlvlls
      301 gvigisniml ivvkertkei girralgatp gtirrqilte sifltiiagm agiafatgll
      361 aglnaildsm psedmmfanp svdllvvfva lmilvgsgll agfipaqiav svkpvdalrt
      421 e
//
LOCUS       WP_176006439             284 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Flavobacterium agri].
ACCESSION   WP_176006439
VERSION     WP_176006439.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..284
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31604
     Region          14..274
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 menlenvekk eitselhslt dylhqlvnwi ieytprlisa fillfiglwa irlinrlikr
       61 lmikreldpt lskfladill wamrvllfit visrlgiets sfvailgamg lavglslqgs
      121 lsnfaggmli imfkpfrvgd tieaqgvtgt vseiqifvtk lttgnnqtif vpngalsngt
      181 itnfsmeglr radltftvsy dtnikqvrei llevlkknkk vlkkpepsiv vrdltdhain
      241 iavrawsktp dygdmvseil eegkeafeaa gisiqpvvke rsvq
//
LOCUS       WP_176006496             188 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Flavobacterium agri].
ACCESSION   WP_176006496
VERSION     WP_176006496.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14388723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..188
                     /product="cupin domain-containing protein"
                     /calculated_mol_wt=20728
     Region          40..178
                     /region_name="cupin_BLL6423-like"
                     /note="Bradyrhizobium japonicum BLL6423 and related
                     proteins, cupin domain; cd02231"
                     /db_xref="CDD:380359"
ORIGIN      
        1 metnntfrri vtghdtdrka iilsdaapdr tfmvggpnga kfheiwntrq tpalidsqsg
       61 epeeaglvla ppksgtrirv idfppegdei rnlteeearg hfktmsgeys skaandaphp
      121 lmhrtqtidy givlegeltl ivdkgetvih agdiviqrgt nhawanrtnk ncrvafilid
      181 gefeqslr
//
LOCUS       WP_176006520             255 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Flavobacterium agri].
ACCESSION   WP_176006520
VERSION     WP_176006520.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18109313
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..255
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29753
     Region          112..224
                     /region_name="COG4627"
                     /note="Predicted SAM-depedendent methyltransferase
                     [General function prediction only]"
                     /db_xref="CDD:443666"
     Region          <121..173
                     /region_name="Methyltransf_11"
                     /note="Methyltransferase domain; pfam08241"
                     /db_xref="CDD:462406"
ORIGIN      
        1 mkkifkfiln tiprpilirl syvarplisi llsgdkftdp idgksfrkfl pygygkqren
       61 vlspstlsle rhrllwlylk eetdfftapk kvlhfapeqa fyklfreqkn ldytttdlfs
      121 pladvkadic dlpfndnqyd lilcnhvleh ipddtkamqe lfrvmkpggm gifqipqdlk
      181 rehtfeddsi tdpkqraeif gqydhvrvyg rdyfdklrsi gftvveedyt kkispemver
      241 yclapgeiip vvfkp
//
LOCUS       WP_176006522             205 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Flavobacterium agri].
ACCESSION   WP_176006522
VERSION     WP_176006522.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..205
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22922
     Region          96..188
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(101,104)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mkkllffaas lliigckttq kttqrvktpe vtsqkpstgl latttegdll gqgevqdllr
       61 tpfrnwfapg ydnykpdaat vtklrdltng isikifmgtw cedsqnqvpk ffkilhdagf
      121 dkqdvtlifv dkdkttpekl eaglnitnvp tfifykttqs ggkkgpkgep ktkelnrive
      181 spretlekdm lkilsnqgyk hsyle
//
LOCUS       WP_176006542             186 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Flavobacterium agri].
ACCESSION   WP_176006542
VERSION     WP_176006542.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..186
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21558
     Region          8..175
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mkvialhqeq heiialaven nrhaqqkiyt qyapkmlsvc rqyakdvhha edlmitafmk
       61 vfanlrnfkh egsfegwirr imvneciswl rvqkkvsfme dsfykeegfn dvesglsvdd
      121 iqnlidglpd gyrmifnlya iegykhkeia emlginegts ksqlsharri lqekiveskn
      181 yengte
//
LOCUS       WP_176006563             239 aa            linear   BCT 11-JAN-2025
DEFINITION  cell division protein FtsQ/DivIB [Flavobacterium agri].
ACCESSION   WP_176006563
VERSION     WP_176006563.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..239
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=27342
     Region          10..239
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mkrfnwenir lvlifivvgf lfafsanrne hralkkseva feqtenlflt peavnkllie
       61 knrasetvak enldlnklen avnahemvek sqvyvsvdgv lkakvkqktp vvrvfdgsgs
      121 fyidyqgkkm plstlytarv plvsgtmdan npelikvfrs ihdddflkkn iigikmlpng
      181 alvmknrnya yeidfgrpih idrkfknyka ffqkaaldst innykrinli ftqqvvcsk
//
LOCUS       WP_176006567             193 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Flavobacterium agri].
ACCESSION   WP_176006567
VERSION     WP_176006567.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..193
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=22183
     Region          11..191
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mesfinylqs hnlsahsids lvssanpeaf kkgefvlrqg evcrhkvfve kgllrtfglt
       61 tdgnehilqf spentwtldv esydrqipal ynisaiektd vliwerndfe rlrselpelq
      121 slsqqlisrn iynsrhrllt algetpeqky enfvhtsgdl lsrlplrmia sflgislktl
      181 trirkaqlhr qsk
//
LOCUS       WP_176006575             738 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Flavobacterium agri].
ACCESSION   WP_176006575
VERSION     WP_176006575.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 738)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 738)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 738)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 738)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 738)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..738
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=86003
     Region          1..727
                     /region_name="RloC"
                     /note="Wobble nucleotide-excising tRNase [Translation,
                     ribosomal structure and biogenesis]; COG4694"
                     /db_xref="CDD:443729"
ORIGIN      
        1 mitkihlnkv asyttsatle tdkkvnliyg lngtgkstfs nylhkkmddr ykccsieglt
       61 ddhdllvynq sfiqenffed dslkgiftls kenkeaetki analeeikkl qsnrdikake
      121 ldtekkslnk kldiaketlw kiktdysggd rvlefcldgy kgskdnlfnh vialpkpsvk
      181 plknisdlkn dlqsisgdna ekyiellhid fsyqntqtkn lldkqivgne hssvsqlikh
      241 lgnsdwvkqg lqyipqeten stcpfcqedt iskalldsir dyfdasyead italkeflkv
      301 ysdgiqnlps ksvlesnprl edyrrdfeik faaftkvlen nkklieekik tpsvsislad
      361 ssklleelne iigrinlsir ehnknidqkd ivksnikkvf wdimrwdydq tvssinadks
      421 tsqikihsle tslkvnsesi atqhaiisee qkqtvniesa iekirnglnd lgitdfeikk
      481 hsenlykivr renedkvfhs lsegekmiis flyflelcrg kkeatdagkr kvvviddpis
      541 slshiyvfni grlikneflg kkktstdket geqkieleyn yeqvfilths lyffyemtet
      601 nhdfrkesqn lfrlikneng srfipmkyee vqndyqaywf iikdeeqhps liancmrnii
      661 eyffnfvekk dlnnyfqqep lkankfqafy ryinreshsl gqnifdikef nyqdfrdafr
      721 elfkvsgyee hykkmirk
//
LOCUS       WP_176006650             110 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Flavobacterium agri].
ACCESSION   WP_176006650
VERSION     WP_176006650.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..110
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12642
     Region          12..110
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(13..15,29,46..48)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mhielspdkr yysigevaka fnvnaslirf wdkefdilkp kknakgnrlf tpedvknlql
       61 iyhlvkergf tlegakthlk egqkktldkf eiiskleaik kqltdlkngl
//
LOCUS       WP_176006651             325 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Flavobacterium agri].
ACCESSION   WP_176006651
VERSION     WP_176006651.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..325
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36658
     Region          139..300
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mkkvkyyyds enlafrkiki kkrtkvayaa lfllasalfg tlafivllnt pyfetpkdrl
       61 lsrevdnfki qysilnkkmd qidevlanie erdnniyrty fntspipdeq rkagfggvnr
      121 ykelegydns elvvntskrv dviskqlaiq sksldeilkl akeknkllaa ipaiqpvkne
      181 nlravasgfg yrtdpftkvr kfhagmdfss rtgtpiyatg dgiveradnt asgygnhivi
      241 rhgygyetly ghlskynvra gkrvkrgdli gfvgstgrse aphlhyevhk ngevvnplny
      301 yygnisaaey iqiakvanqe nqsld
//
LOCUS       WP_176006717             636 aa            linear   BCT 11-JAN-2025
DEFINITION  T9SS type A sorting domain-containing protein [Flavobacterium
            agri].
ACCESSION   WP_176006717
VERSION     WP_176006717.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Veith,P.D., Nor Muhammad,N.A., Dashper,S.G., Likic,V.A.,
            Gorasia,D.G., Chen,D., Byrne,S.J., Catmull,D.V. and Reynolds,E.C.
  TITLE     Protein substrates of a novel secretion system are numerous in the
            Bacteroidetes phylum and have in common a cleavable C-terminal
            secretion signal, extensive post-translational modification, and
            cell-surface attachment
  JOURNAL   J Proteome Res 12 (10), 4449-4461 (2013)
   PUBMED   24007199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10024511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..636
                     /product="T9SS type A sorting domain-containing protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /calculated_mol_wt=68458
     Region          560..631
                     /region_name="Por_Secre_tail"
                     /note="Por secretion system C-terminal sorting domain;
                     TIGR04183"
                     /db_xref="CDD:275036"
ORIGIN      
        1 mtsfrtlrnw lpvcglllpl smqsqdiqwe ksyggrhady lfdavptady gfilagssls
       61 gktgnkassn kgnldywvwk mdehgelvwq ksfggsgidm lhavrltndg gfflagtsds
      121 pksddkkedt hggrdfwvik ldagggerwq ktlggladee lvgvavskdg gcllagstys
      181 dasgdvtqks kggldfwlvk ldyegtikwq ktvggalsde lrsviatadg gylvggtsns
      241 pegydktskc ngandfwvlk ldkdgniewq rtmgaekddq lqsliqtndg gyvasgnsns
      301 gagfnktsas rggsdfwvvr ldqsgnplwq etynfgkydv ltslventdg tlliagtaks
      361 esvvnkdkeg tndyialktd aegkelwsrt igsegedvlr klietrdggy llagtsnpea
      421 vkpgkrkknk nglngissgg rlaaaenaqr emdktvaqgr dtandfykeq tasaskavnd
      481 algqkegspl kmgvgepgnl lqsgngsggk kgshrdtnpt nakklpasrq ksnnpgrsdf
      541 wvvklkdkdk kekakqnvea fpnpahgytn vvvgyeyekg tatvfdingr qlqsfaiter
      601 tipvsleglp egiyiinikt dksndsvkvm kasrtn
//
LOCUS       WP_176006734             179 aa            linear   BCT 11-JAN-2025
DEFINITION  toll/interleukin-1 receptor domain-containing protein
            [Flavobacterium agri].
ACCESSION   WP_176006734
VERSION     WP_176006734.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Nimma,S., Gu,W., Maruta,N., Li,Y., Pan,M., Saikot,F.K., Lim,B.Y.J.,
            McGuinness,H.Y., Zaoti,Z.F., Li,S., Desa,S., Manik,M.K.,
            Nanson,J.D. and Kobe,B.
  TITLE     Structural Evolution of TIR-Domain Signalosomes
  JOURNAL   Front Immunol 12, 784484 (2021)
   PUBMED   34868065
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Essuman,K., Summers,D.W., Sasaki,Y., Mao,X., Yim,A.K.Y.,
            DiAntonio,A. and Milbrandt,J.
  TITLE     TIR Domain Proteins Are an Ancient Family of NAD+-Consuming Enzymes
  JOURNAL   Curr Biol 28 (3), 421-430 (2018)
   PUBMED   29395922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10615567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..179
                     /product="toll/interleukin-1 receptor domain-containing
                     protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=20518
     Region          35..>127
                     /region_name="TIR_2"
                     /note="TIR domain; pfam13676"
                     /db_xref="CDD:463954"
     Region          <152..>174
                     /region_name="PRK08566"
                     /note="DNA-directed RNA polymerase subunit A'; Validated"
                     /db_xref="CDD:236292"
ORIGIN      
        1 mayltfnqls ttttlrksst lneslrarty tetnvflsyr rkdrqyveai vkflkgigin
       61 lyvdyldetl edktnenvaa ilrdrikscn kfisvatpds gnskwmpwel glgdriinyk
      121 nvailpltns avtwndqeyg kiygrvegsn syvsngpddw yviypdgski klkewflkn
//
LOCUS       WP_176006827             379 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Flavobacterium agri].
ACCESSION   WP_176006827
VERSION     WP_176006827.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427633
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..379
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41928
     Region          95..368
                     /region_name="FepB"
                     /note="ABC-type Fe3+-hydroxamate transport system,
                     periplasmic component [Inorganic ion transport and
                     metabolism]; COG0614"
                     /db_xref="CDD:440379"
ORIGIN      
        1 mktfrfsvfs lilalvfvgc kksettekps aavqnsikya kglsifdygd ysvvkvsnpw
       61 pnatqdytyv lkekdakipd slqkftsvnv pvksiivtst thipslemlg venslvafpq
      121 ldyissekvr aridakkike lgsnqslnte vvidlspdvi igygidnnnk aidnlqksgl
      181 kvvlngdwne tsslgkaewi klfgalygle dkadkifsdi ekeynstlel akkatkkptv
      241 iagamfenkw ylpqgnswga eliaqgagqy lwadskgtgs lslpfesvle kgvdadfwig
      301 pgqftslaem taanahydqf kafktknvys fsskkgktgg iiyfelapnr pdlvlkdivk
      361 ilhpellpdh elyffeklk
//
LOCUS       WP_176006769             475 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Flavobacterium agri].
ACCESSION   WP_176006769
VERSION     WP_176006769.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 475)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10396022
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..475
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=53135
     Region          3..295
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Site            order(7,9..10,12,31..33,73..75,109..111,121,125,144..147)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187535"
     Site            order(87,111,121,125)
                     /site_type="active"
                     /db_xref="CDD:187535"
     Region          331..467
                     /region_name="DUF2867"
                     /note="Protein of unknown function (DUF2867); pfam11066"
                     /db_xref="CDD:431633"
ORIGIN      
        1 mkilltgatg yiaqrllpvl ldqghevvcc vrdvrrfnte ayqdknisvv eadlvkkdtl
       61 sslprdidaa yylvhsmstq gdfgkseers aknfveyiat gsatqiiyls givnerelsa
      121 hlssrknves ilgqataklt tlraaiivgs gsasfeiird lveklpvmva pkwlytkcqp
      181 iairnvvqfl sgvlakestf gkhfdiygpa iltykemllg faevrglkrt ivtvpvmtpr
      241 lssywlyfvt stsytlaknl vdsmkidvia tpndlagsig iqlidyktai gmafdkieqn
      301 lvlsswsgam hdkgsefdfd klvkvprfgc fkdrktrkii daasavdril aiggdsgwyy
      361 anwlwefrgf ldklfggvgl nrgrknrnvl dagdvldfwr vvyvnkdegr lllyaemklp
      421 geawlefkvs gdrselvqta tfrplglagr lywyavlpfh yfifngmirr itkgl
//
LOCUS       WP_176006836             123 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Flavobacterium agri].
ACCESSION   WP_176006836
VERSION     WP_176006836.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..123
                     /product="VOC family protein"
                     /calculated_mol_wt=13741
     Region          14..119
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 mknilglrta iykvtdikaa tdwyakafqt epyfnepfyv gfniagyelg lqseesviln
       61 kaetvltywg vndieseyar fldlgasehe kptnvggeiv vasvkdlwgn iigliynpef
      121 rlp
//
LOCUS       WP_176006829             261 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Flavobacterium agri].
ACCESSION   WP_176006829
VERSION     WP_176006829.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..261
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28613
     Region          5..250
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtdpilhtrd lsigyqskkh ttvvasgidl slgsaklvsl vgangvgkst llrtltgiqk
       61 pisgqvllen kivtdyspsq lskklslvlt eklppsnltv felvalgrqp ytnwvgkltp
      121 ediskvneal hltdtfhlsa kkhfqisdgq lqnvlvaral aqdtplivld eptthldfqh
      181 kvalfrllkk lssetekcil fsthdiemai elsdeiiamn dgkaiqdtps kliesggfdr
      241 lfaddnivfd kqkgrfvfrg i
//
LOCUS       WP_176006873             318 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Flavobacterium agri].
ACCESSION   WP_176006873
VERSION     WP_176006873.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..318
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35995
     Region          5..187
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(8,10,94)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(41,93..94)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            92..94
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mnlsivipll neeeslhelh nwivsvmekn sysyeilfid dgstdnswpi ietlshenan
       61 vkgirfmknf gksqalhagf aaakgdvvit mdadlqddpe eipelyamia ndkydlvsgw
      121 kkkrydnvvm knlpsklfnw aarmtsgvkl hdfncglksy qnrvvknvev sgemhryipv
      181 laknagfkki gekvvkhrar kygetkfgmn rfingfldli tiwflsrfgk qpmhlfgalg
      241 simfvigfla agyigaskli rlydheptil vtenpwfyis latmiigtql flagflgeii
      301 lrarqgndry kvsdtvnl
//
LOCUS       WP_176006974             198 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Flavobacterium agri].
ACCESSION   WP_176006974
VERSION     WP_176006974.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 198)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..198
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23112
     Region          70..195
                     /region_name="NUDIX_Ap6A_hydrolase"
                     /note="diadenosine hexaphosphate (Ap6A) hydrolase;
                     cd03673"
                     /db_xref="CDD:467541"
ORIGIN      
        1 mykvfvndkp lfltdeihke tdfqlflleg idfaqliskm fsnkvkkayl yhpdekemlr
       61 tikdtipvqk aggglvynkk gqvlfifrng kwdlpkggie kgekieytal reveeetgvg
      121 klsiirklqk tyhvfrrngr yklkvthwfe mksdfdgplh pqleegiekv awlnpedieq
      181 allnsyenik llfeeqlt
//
LOCUS       WP_176006987             208 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Flavobacterium agri].
ACCESSION   WP_176006987
VERSION     WP_176006987.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..208
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24456
     Region          10..159
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtelnekqvq illvaeklfa ekgfdgtsir disreakini amvsyyfgsk dkmlealivw
       61 rtsdmalqle nllkmqvdpw ekmerlidly itrvnknrci ykiihsevln thrsiniqqf
      121 nevklrnlgm irqiveegqk tgqfrndipv ellpttvlgt yfhfhntrpf yedmlnlksd
      181 rdfdnyvknn lipyikqvik allknenq
//
LOCUS       WP_176006986             443 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Flavobacterium agri].
ACCESSION   WP_176006986
VERSION     WP_176006986.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..443
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49162
     Region          113..438
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkiskilala llflgasqlq aqkkslslne avkmavtqsn qsvladtkvn tanfetqsvk
       61 mnqypdlkis gqylrltnad itlkssgnsn neegegnstp kvnqlilgqa slsmpiysgg
      121 klrnsikase nrskaelata ahskeevame vvqyyvdlyk vqksiellre slksqqqrvk
      181 dftgmeengl iarndllkaq laesrvqlsl deaeknervi nyylvtllkl pagtqmqisp
      241 dnidrdifam tlntedqalq nrkdlealny skkasedqik vakadyypsl sltggyiaad
      301 lenvvrvena mnigvglsyn lssifkngka vkaaksrtae leqqqailtd eikeevmksn
      361 enyqlslkqd kvyneavgqa denyrivkdk yengladtnd lleadvddln akinvayska
      421 nivlkyyell eangqltqsf kfn
//
LOCUS       WP_176006993             466 aa            linear   BCT 11-JAN-2025
DEFINITION  anthranilate synthase component I family protein [Flavobacterium
            agri].
ACCESSION   WP_176006993
VERSION     WP_176006993.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Kerbarh,O., Bulloch,E.M., Payne,R.J., Sahr,T., Rebeille,F. and
            Abell,C.
  TITLE     Mechanistic and inhibition studies of chorismate-utilizing enzymes
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 763-766 (2005)
   PUBMED   16042594
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Dosselaere,F. and Vanderleyden,J.
  TITLE     A metabolic node in action: chorismate-utilizing enzymes in
            microorganisms
  JOURNAL   Crit Rev Microbiol 27 (2), 75-131 (2001)
   PUBMED   11450855
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..466
                     /product="anthranilate synthase component I family
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52424
     Region          8..462
                     /region_name="TrpE"
                     /note="Anthranilate/para-aminobenzoate synthases component
                     I [Amino acid transport and metabolism, Coenzyme transport
                     and metabolism]; COG0147"
                     /db_xref="CDD:439917"
ORIGIN      
        1 mntydfhtfh qdiladtltp vgvylrlrdk fadsvlless dfqagknsfs yiccnpiasf
       61 kvadgkisqq fpndeafsea iddktdvmqn lqtfasrfkm sktdhkciqg glfgyiayda
      121 vryfesvdil kktdnldipd lhyaffknvi ainhfkneay lfchsldgks nldeilgllq
      181 nsslpkykfe rsgektanis eddylnlvgk akshcqrgdv fqlvlsrrfs qrfkgddfnv
      241 yrtlrsinps pylfyfdygn fkifgsspea qlvvdnakae ihpiagtfkr sgndeqdail
      301 artlsedpke naehvmlvdl arndlsrnat qvtvekyael qffshvihlv skvtgklrdk
      361 nqtlqavadt fpagtlsgap khramqliee lenrnrsfyg gaigfidfdg nfnhaimirt
      421 flsknntlhf qagagltaas dekkelqety nklgalekai alaeti
//
LOCUS       WP_176006999             103 aa            linear   BCT 11-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Flavobacterium agri].
ACCESSION   WP_176006999
VERSION     WP_176006999.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..103
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=11453
     Region          7..99
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mdlsqhdwld qlsndpnavi ldvrtddewn egiipgavni diykgqgfiy evdqldknkn
       61 yyvyckaggr saqacaimnq lgfantynlv ggfmqwqget amp
//
LOCUS       WP_176006998             201 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Flavobacterium agri].
ACCESSION   WP_176006998
VERSION     WP_176006998.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   6  (residues 1 to 201)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   7  (residues 1 to 201)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   8  (residues 1 to 201)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..201
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22177
     Region          29..200
                     /region_name="PRX_like1"
                     /note="Peroxiredoxin (PRX)-like 1 family; hypothetical
                     proteins that show sequence similarity to PRXs. Members of
                     this group contain a conserved cysteine that aligns to the
                     first cysteine in the CXXC motif of TRX. This does not
                     correspond to the peroxidatic...; cd02969"
                     /db_xref="CDD:239267"
     Site            65
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239267"
ORIGIN      
        1 mktmkilaav aivafmsaft tpgtgykvgd iatdfklknv dgknvslsdy ksakgfivif
       61 tcnhcpfaka yedriialdk kyskqgypvi ainpnnpekq kedsfdlmkk ratekgftfp
      121 ylfdegqkiy pqygatktph vyilqktakg nevkyigaid dnyeeptavk ekyvenavda
      181 llkgqsvkvt etkaigcsik a
//
LOCUS       WP_176007201             185 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Flavobacterium agri].
ACCESSION   WP_176007201
VERSION     WP_176007201.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..185
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20834
     Region          2..179
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mrkliaginm tldgfcdhta inpddeiheh yngllrnsgt llygrityql mesywpsvvk
       61 npsgnapmde faliidniek ivfsrtlqhv dwnnsilknq vikdeilelk rqtgkdmlvg
      121 spsliitmir lglvdefqlm vhpvvagsgl alfahiddri elkllrtktf ssgaillcye
      181 pklre
//
LOCUS       WP_176006981             350 aa            linear   BCT 11-JAN-2025
DEFINITION  RluA family pseudouridine synthase [Flavobacterium agri].
ACCESSION   WP_176006981
VERSION     WP_176006981.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Rintala-Dempsey,A.C. and Kothe,U.
  TITLE     Eukaryotic stand-alone pseudouridine synthases - RNA modifying
            enzymes and emerging regulators of gene expression?
  JOURNAL   RNA Biol 14 (9), 1185-1196 (2017)
   PUBMED   28045575
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Hamma,T. and Ferre-D'Amare,A.R.
  TITLE     Pseudouridine synthases
  JOURNAL   Chem Biol 13 (11), 1125-1135 (2006)
   PUBMED   17113994
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Ofengand,J.
  TITLE     Ribosomal RNA pseudouridines and pseudouridine synthases
  JOURNAL   FEBS Lett 514 (1), 17-25 (2002)
   PUBMED   11904174
  REMARK    Erratum:[FEBS Lett 2002 Apr 24;517(1-3):287]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12393452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..350
                     /product="RluA family pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /calculated_mol_wt=40067
     Region          33..111
                     /region_name="S4"
                     /note="S4/Hsp/ tRNA synthetase RNA-binding domain; The
                     domain surface is populated by conserved, charged residues
                     that define a likely RNA-binding site; Found in stress
                     proteins, ribosomal proteins and tRNA synthetases; This
                     may imply a hitherto unrecognized...; cd00165"
                     /db_xref="CDD:238095"
     Site            order(33,45..46,48..49,51..52,55..56,58,65..66,67..71,73)
                     /site_type="other"
                     /note="RNA binding surface [nucleotide binding]"
                     /db_xref="CDD:238095"
     Region          100..335
                     /region_name="RluA"
                     /note="Pseudouridine synthase RluA, 23S rRNA- or
                     tRNA-specific [Translation, ribosomal structure and
                     biogenesis]; COG0564"
                     /db_xref="CDD:440330"
ORIGIN      
        1 mnnedfdles qeesqelfeh yrfevpkgqa llridkyvty lipnatrnki qnaadngdiy
       61 vndvpvksny rikpfdviri llshppfenr idpedipidi vyeddalivl nkppglvvhp
      121 ghgnytgtlv nalvyhfqhl pmnsskrpgl vhridkdtsg llvvakteha lanlaaqfef
      181 ktsereyval vwgnvkedsg tiegnisrhl kdrmqmavfe dpeigkpait hykvlerfgy
      241 vtlvscrlet grthqirahm kyightlfnd eryggdqilk gttfakykqf vencfkacpr
      301 qalhaktlgf khpetgemmr fdteipadmk avidkwrtys sakemeeeed
//
LOCUS       WP_176007255             123 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF805 domain-containing protein [Flavobacterium agri].
ACCESSION   WP_176007255
VERSION     WP_176007255.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..123
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=13862
     Region          1..105
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 mfrnpfsfsg rirrleygfs llvvlgvvmf gsllmfglat lsvwflvvsp flifgtmwfr
       61 iaqavkrshd tgysgwcili pffglyllfa dsqygenryg ynpknignhk gemddigsds
      121 ysa
//
LOCUS       WP_176007355             552 aa            linear   BCT 11-JAN-2025
DEFINITION  peptide MFS transporter [Flavobacterium agri].
ACCESSION   WP_176007355
VERSION     WP_176007355.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 552)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..552
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=61687
     Region          4..548
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mwnkhpkalp ylflsemwer fgyylmigif tlylkdvekg famtekeaad lygtfialvf
       61 ltpfigglia drylgyrksi ilggilmgvg yfmmgihslp ilytamtlvi lgngffkpni
      121 stllgnfynn deykakkdeg ynifymginv gaficnffga alynlfgwqq afmaagvgmf
      181 igvitfmvgi khygthdqkk gvqegdmpfs kivmfillps ivfgiigwll kgtasdanpd
      241 syifgsdstd afifacipvi lfysslyfka rpedkrpiga lltifavvil fwgvfklngs
      301 alntwgdryt nrhitgttes vfhnlklsdk laykkdsvgv ydeqfrlqkv dgkvvkevny
      361 pvyfrnvpkd klpkeneeis lwspnlsqsi npfwvivltp lviaffsflr vrqkepttpt
      421 kiafgllisa lsvlvmvaav kagsngtekv svwwlvanyg vitigelfls pmglsvvskl
      481 spakitslmm ggwflatsig nklsgvlasm wdsyedktnf fwvnfcllla atalmfvvlk
      541 nlnkvmaekg ir
//
LOCUS       WP_176007392             322 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Flavobacterium agri].
ACCESSION   WP_176007392
VERSION     WP_176007392.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..322
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=33600
     Region          2..318
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 msiliyaess dgkfkkvafe lasygkkvae slgttvtavt vnannvsels kygvdkvlkv
       61 tndklsafna kayadvikqa aqkegtklvl lssttdslyl aplvavglsa gyasnvvglp
      121 vstspfqvkr nafsnkafni teiatdvkvl glaknsygvf enmgsaseed fspalndadf
      181 niktesvdkt agkltiadae vvvsggrglk gpenwglied lasalgaata cskpvsdlgw
      241 rphsehvgqt gkpvatnlyv avgisgaiqh iaginaskvk lvinsdaeap ffkvadygvv
      301 gdafeivpkl tekikefkan na
//
LOCUS       WP_176007366             385 aa            linear   BCT 11-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Flavobacterium agri].
ACCESSION   WP_176007366
VERSION     WP_176007366.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..385
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=41748
     Region          1..379
                     /region_name="ArgD"
                     /note="Acetylornithine/succinyldiaminopimelate/putrescine
                     aminotransferase [Amino acid transport and metabolism];
                     COG4992"
                     /db_xref="CDD:444016"
ORIGIN      
        1 mknlfdvypl yditpvkafg skvfdesgre yldfygghgv isighshpny vkavsdqvsk
       61 igfysnsiqn piqtglaekl cafsgypdys lflcnsgaea nenalklasf htkkskviaf
      121 kkafhgrtsa avastdnpsi vapinahkvi flelndqksv ldelqkgdva cviiegiqgv
      181 ggldeattef fqflssetkk ygvvlildei qsgygrsgkf fahqhhdikp diisvakgmg
      241 ngfpiggili spefkashgl lgttfggnhl acaaalsvle viesenliqn vnevsdyfkq
      301 qaseipqikn vkgrglmlgl efdfeianlr ksliydfgif tgnasqknll rilpplsitk
      361 aevdfffvgl kkaigkivep qisvp
//
LOCUS       WP_176007393             248 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Flavobacterium agri].
ACCESSION   WP_176007393
VERSION     WP_176007393.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..248
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26216
     Region          1..247
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkilvcishv pdttskinft ngdaefdtng vqfvinpnde fgltravwfq eqqganvtvv
       61 nvgaadteat lrkalaigan eairvnatpt dgffvakqla evvknggydl vicgkesldy
      121 nggmvpgmla altganfvns cigltvdgsn vkatreidgg ketlstslpl ivggqkglve
      181 ekdlripnmr gimtartkal qvlepvsadq ttkavkfekp aakgpvklft vdnldelvna
      241 lhneakvi
//
LOCUS       WP_176007400             741 aa            linear   BCT 11-JAN-2025
DEFINITION  beta-N-acetylhexosaminidase [Flavobacterium agri].
ACCESSION   WP_176007400
VERSION     WP_176007400.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 741)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 741)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 741)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 741)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 741)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..741
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=83197
     Region          5..571
                     /region_name="Chb"
                     /note="N-acetyl-beta-hexosaminidase [Carbohydrate
                     transport and metabolism]; COG3525"
                     /db_xref="CDD:442747"
ORIGIN      
        1 mfkkilfall isqslfsqel plipqpqslr llggevktia fapedlfsdl dglnaffdkk
       61 spsvyslgnp gsieirksan fkkeayslki ladkpiqiea sdasgafyal qtlfqmtsaq
      121 nattlpclei vdepkfqwrg mhldcsrhfw svhfvkkyid ylamykmntf hwhltddqgw
      181 rieikkypkl teigskrkgt maghyneqrw ddipyggfyt qeqikdvvay akarhitivp
      241 eiempghava alsaypelac tfgpfevekt wgvfddvfcp kentfkfled vltevmalfp
      301 seyihiggde cpktrwktca hcqglikekg lkdehelqsy fiqriekfvn skgrriigwd
      361 eilegglapn aavmswrgid ggiaaakqkh yvvmtpesnl yfdryqgdpk neplgfggfv
      421 piekvynfnp ipealsvees kyilgaqanl wteyiatekh aeymvfprla alaevdwgta
      481 qpgnfgqfqk rlvnhmklld kkgvnysrsm fglsakvspf grnqimleft sadknpeiry
      541 ttdgseptse splfpgkivi pdseifkaar feygkkiset ttqefkfgks tarsvslknq
      601 pspkysgdga ftltngifgd knrfgrdwlg fsgtdleavi dlsekqkves vtasflqsag
      661 swiyfpaeve ifvskdnldf ksvgkisasd iekaggtiti kfkkqktqyv kviaknttki
      721 adgkpgagna awlfadeilv n
//
LOCUS       WP_176007435             433 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Flavobacterium agri].
ACCESSION   WP_176007435
VERSION     WP_176007435.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..433
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=48715
     Region          4..395
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 msnkkriaii gagfgglrla qdlrksdydi wlfdkhnyhq fqplmyqvas arlepasisf
       61 plrkvfqyck nvhiritsvt svnpetktvh teigdypydy lvlaqgcntn yfgnkqleky
      121 afpmksvpea mqlrnrilet feqalitppd qlqsllnfvi vgggptgvel agalaemkkn
      181 ilpkdypdqd fskltvylle glpnllnams adskrmsrky ledlgvvvkt dtivdnydge
      241 tvtlksgemi kaknviwaag iagvqipgip tenytrgnrl ivnryselek lkdvyavgdi
      301 symetnkypk ghpqlaavai eqatvlaknf irmsnattlk pyeyhdkgsm atvgkrkavv
      361 dlpqfsfqgr lawftwmfvh lmlilsvknk isifvnwmys yfskdstlrv llkaadkeve
      421 nsvgdriean nas
//
LOCUS       WP_176007501             317 aa            linear   BCT 11-JAN-2025
DEFINITION  transketolase family protein [Flavobacterium agri].
ACCESSION   WP_176007501
VERSION     WP_176007501.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..317
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33819
     Region          7..314
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mkkyentgsk dtrsgfgagl telgqknenv valcadligs lkmddfkknh perffqigia
       61 eanmigiaag ltiggkipyt gtfanfstgr vydqirqsva ysdknvkica shagltlged
      121 gathqiledi glmkmlpgmt vintcdynqt kaatiaiadh hgpvylrfgr pvvpnftpad
      181 qkfeigkavl lnegtdvtiv atghlvweal laaetleakg isaeviniht ikpldeeail
      241 tslkktgciv taeehnilgg lgesvsrvla lknpapqefv avfdsfgesg tpeqlmekyk
      301 lnataivaaa ekavsrk
//
LOCUS       WP_176007443             262 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Flavobacterium agri].
ACCESSION   WP_176007443
VERSION     WP_176007443.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..262
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28898
     Region          191..256
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mkldllrqqw ldivfegknk lygayqlrkq nprttmlall fgavifaflv stpmlarlip
       61 egksedasld tkivtikipp kqkppenlpp ppppppkvdq ikfvkpvvak aeevveeppk
      121 mdkiedkkvg tenikgdpda pvtidepvgn gpkdvvednn iynaagievk pefpggiekf
      181 ykfvrdnyrt pedavggrmi vsfvvekdgs ltdikvprpa gpgtaeeair mlkrspkwtp
      241 aeqngkkvrc aftlpitiqa pe
//
LOCUS       WP_176007505             172 aa            linear   BCT 11-JAN-2025
DEFINITION  shikimate kinase [Flavobacterium agri].
ACCESSION   WP_176007505
VERSION     WP_176007505.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Herrmann,K.M.
  TITLE     The shikimate pathway as an entry to aromatic secondary metabolism
  JOURNAL   Plant Physiol 107 (1), 7-12 (1995)
   PUBMED   7870841
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Bentley,R.
  TITLE     The shikimate pathway--a metabolic tree with many branches
  JOURNAL   Crit Rev Biochem Mol Biol 25 (5), 307-384 (1990)
   PUBMED   2279393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         1..172
                     /product="shikimate kinase"
                     /EC_number="2.7.1.71"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004765 - shikimate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=19225
     Region          6..172
                     /region_name="AroK"
                     /note="Shikimate kinase [Amino acid transport and
                     metabolism]; COG0703"
                     /db_xref="CDD:440467"
ORIGIN      
        1 mkkvllcgym gcgkstvaqi lshktdlpqf dlddliekne gmsipeifek ngevyfrkle
       61 hrlftqlmgs pddfilalgg gtpayannhl lmngegvtsf flrasietlh drlidenenr
      121 plvagkasde lkehiakhlf drnyyynqat ytvvvdgksa eqvadeilek la
//
LOCUS       WP_176007593             643 aa            linear   BCT 11-JAN-2025
DEFINITION  RHS repeat domain-containing protein, partial [Flavobacterium
            agri].
ACCESSION   WP_176007593
VERSION     WP_176007593.1
KEYWORDS    RefSeq.
SOURCE      Flavobacterium agri
  ORGANISM  Flavobacterium agri
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Flavobacterium.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Flavobacterium agri"
                     /db_xref="taxon:2743471"
     Protein         <1..643
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
     Region          <106..497
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 qvnggtneri flnayddlgq lvekqvgqig tgalqhvdyk ynirgwltdi ndvdpghasg
       61 dlfsfrinyd tvgddlddev splyngnise tfwrsssdgf qrkygykydg lnrllhayyq
      121 rpyenvprsr sydewmaydr ngnitslgrn gdyedltavq piddlvytye phtnklvdvd
      181 dleahasgfn dgntgddygy dtygnmtadk nkdigtityn hlnlplkily fdgsfityqy
      241 nasgtkvrkl vskqvgsnqe qtttvyqqgf qyenntlqfi ahpegyikat kvgnayqfny
      301 vyqykdhlgn irmnyaldps dnevkilned hyypfglkht nynsdvknfq edpgfstlri
      361 iqvssegnty rykyngkewq delglnfydy garnydpaig rwmnidplae tsrrwspydy
      421 aynnpivfvd pdgmqakwip gvdgkaityt tdkngnltvs qnatedtkti vagineskse
      481 kaksqfkgia dsegkvnlvi dkentgangs klyglhqphd asgkalnwnk dtqsfdgtpe
      541 tivdskgnti ykeatitifd knfddlsnnk favlgktgiw dsgltksdam tgtvsheidh
      601 nlnpysieai idrangrtnn yeveppayqv qkkvheeika arq
//
LOCUS       WP_176007647             254 aa            linear   BCT 11-JAN-2025
DEFINITION  TatD family hydrolase [Paenalkalicoccus suaedae].
ACCESSION   WP_176007647
VERSION     WP_176007647.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..254
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28723
     Region          1..253
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 midthvhlna dqyeedveev iarareagvq emvvvgfdtk tihkamqlan dydfiyasvg
       61 whpvdakdfd deklawleel aahpkvvaig etgldyywdt stkeqqheaf kkqialakkv
      121 klpliihdrd ahddvlrilq eenaaeaggi mhcfqgdvem akacldinfy isfggpvtfk
      181 naklpkevak tipndrllie tdapylaphp yrgkrnepay vklvleqlae lrevsyeelr
      241 tqttqnakkl fsls
//
LOCUS       WP_176007752             239 aa            linear   BCT 11-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Paenalkalicoccus
            suaedae].
ACCESSION   WP_176007752
VERSION     WP_176007752.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..239
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=26926
     Region          98..189
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mavilpqnln tfnvygiyly ltiflwiylf fkkhnisfke ltigntrkvp wlkigitttl
       61 myvlstaitv agilylmylf psfitdagsg gpvveetllr vlihilltvl tapiveellf
      121 rgilqnklsf kygrvigivl tallfavihp lsmlsafiis iflsilyiry qtiivpilah
      181 vffnflsiiq tyglapssee paitvpnvea lwiisgiilf lcmliiplvy vffvretar
//
LOCUS       WP_176007760            1054 aa            linear   BCT 11-JAN-2025
DEFINITION  type I restriction endonuclease subunit R [Paenalkalicoccus
            suaedae].
ACCESSION   WP_176007760
VERSION     WP_176007760.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Gao,Y., Cao,D., Zhu,J., Feng,H., Luo,X., Liu,S., Yan,X.X., Zhang,X.
            and Gao,P.
  TITLE     Structural insights into assembly, operation and inhibition of a
            type I restriction-modification system
  JOURNAL   Nat Microbiol 5 (9), 1107-1118 (2020)
   PUBMED   32483229
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Loenen,W.A., Dryden,D.T., Raleigh,E.A. and Wilson,G.G.
  TITLE     Type I restriction enzymes and their relatives
  JOURNAL   Nucleic Acids Res 42 (1), 20-44 (2014)
   PUBMED   24068554
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   4  (residues 1 to 1054)
  AUTHORS   Roberts,R.J., Belfort,M., Bestor,T., Bhagwat,A.S., Bickle,T.A.,
            Bitinaite,J., Blumenthal,R.M., Degtyarev,S.Kh., Dryden,D.T.,
            Dybvig,K., Firman,K., Gromova,E.S., Gumport,R.I., Halford,S.E.,
            Hattman,S., Heitman,J., Hornby,D.P., Janulaitis,A., Jeltsch,A.,
            Josephsen,J., Kiss,A., Klaenhammer,T.R., Kobayashi,I., Kong,H.,
            Kruger,D.H., Lacks,S., Marinus,M.G., Miyahara,M., Morgan,R.D.,
            Murray,N.E., Nagaraja,V., Piekarowicz,A., Pingoud,A., Raleigh,E.,
            Rao,D.N., Reich,N., Repin,V.E., Selker,E.U., Shaw,P.C., Stein,D.C.,
            Stoddard,B.L., Szybalski,W., Trautner,T.A., Van Etten,J.L.,
            Vitor,J.M., Wilson,G.G. and Xu,S.Y.
  TITLE     A nomenclature for restriction enzymes, DNA methyltransferases,
            homing endonucleases and their genes
  JOURNAL   Nucleic Acids Res 31 (7), 1805-1812 (2003)
   PUBMED   12654995
REFERENCE   5  (residues 1 to 1054)
  AUTHORS   Piekarowicz,A., Klyz,A., Kwiatek,A. and Stein,D.C.
  TITLE     Analysis of type I restriction modification systems in the
            Neisseriaceae: genetic organization and properties of the gene
            products
  JOURNAL   Mol Microbiol 41 (5), 1199-1210 (2001)
   PUBMED   11555298
REFERENCE   6  (residues 1 to 1054)
  AUTHORS   Makovets,S., Doronina,V.A. and Murray,N.E.
  TITLE     Regulation of endonuclease activity by proteolysis prevents
            breakage of unmodified bacterial chromosomes by type I restriction
            enzymes
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9757-9762 (1999)
   PUBMED   10449767
REFERENCE   7  (residues 1 to 1054)
  AUTHORS   Murray,N.E., Daniel,A.S., Cowan,G.M. and Sharp,P.M.
  TITLE     Conservation of motifs within the unusually variable polypeptide
            sequences of type I restriction and modification enzymes
  JOURNAL   Mol Microbiol 9 (1), 133-143 (1993)
   PUBMED   8412658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..1054
                     /product="type I restriction endonuclease subunit R"
                     /EC_number="3.1.21.3"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0009035 - type I site-specific
                     deoxyribonuclease activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009307 - DNA restriction-modification
                     system [Evidence IEA]"
                     /calculated_mol_wt=120561
     Region          5..973
                     /region_name="COG0610"
                     /note="Type I site-specific restriction-modification
                     system, R (restriction) subunit and related helicases ...
                     [Defense mechanisms]"
                     /db_xref="CDD:440375"
ORIGIN      
        1 mhqlshrsea eieshlievl gdghnqwtyr ndlkseedlw qnlrqkitqn nlselgdqpl
       61 tdkefeaikt elllrtqtpf daakwlkgen giaritiere ndqagfvsli lysnqdiggg
      121 issyevvnqi akkrdqsegr drrfdvtlli nglpivqiel kkvtardgvy qafnqvkkya
      181 eegvfrnnif stlqlfvvsn eqttryiant mpknmhkkfm fswrtkdnkk vdnlyefckq
      241 alnipdahrl iahytvvsed qdnktlmvlh pyqihaieal ftaanknksg yvwhatgsgk
      301 tltsfvstkl lakksgidrt imlvdrkdld nqttseftkf asefntgiss gttpansliv
      361 gtgsaqelsk tlladansnv viittrqkld aalkhakkve eqkgtnryek ligqhivfvv
      421 dechralsae nmeeikaffp rstwfgftgt pifeenkkqa kgklarttfd qygevlhtyt
      481 iknaledgav lgfqveheat ieptsidnmi hqklrqvdky atkpgaeinr videmtgvek
      541 ekyiesstye sdehvkqviq kvlrpdnayt kfdfkngkpt ksailttssi amakryyrai
      601 kemtqqddwm tsvfpdlpir egrtmddpdf priaitysle ennedsadqq kemqgiiddy
      661 ntyygtawsl qdieryngdi nnrlarkrae fkqpgrqvdi vivvdrlltg fdaptiqtlf
      721 vdrnleyagl iqafsrtnrt ypdktkgliv tfrkpstmeq nvekatklys qaneetgliy
      781 ptyeeakkrf kkahkefsai vesegnvdeq ssvetrvdyv kafqemnnay ealvtydtyn
      841 qdigtssalq dqvgvlkeev gvyetvkgsl vhidedddgg ndsdfseltf ysdstkrlyd
      901 idssyidqll gvyqannpdv reeiekalqk lnkveivkdv yrsilnaide egikegqdif
      961 avkrhfftqk kdqliegfst ywcisinelh asaiqytvgm daipnmrsii eskdyetfka
     1021 qhpevkpfqy pqmmkrewkh mldeqivpld delr
//
LOCUS       WP_176007767             242 aa            linear   BCT 11-JAN-2025
DEFINITION  (Fe-S)-binding protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176007767
VERSION     WP_176007767.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..242
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26732
     Region          <2..235
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mkvslfitcl advfypgvgq dtvevlerlg cevdfptgqt ccgqpaynsg ykkdtvnvak
       61 htittfahae yvvlpsgsca smiheyphlf esdpewrera ealvkktyef tqflvhvlkv
      121 edvgaklsar atyhtschmt rllgekeapl kllenvegld lqplpnresc cgfggtfsvk
      181 mgqiseqmvd ekvehiketk asiligadcg clmniggrme rkeepvkamh iaqvlnsrge
      241 ee
//
LOCUS       WP_176007850             317 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paenalkalicoccus suaedae].
ACCESSION   WP_176007850
VERSION     WP_176007850.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..317
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=34439
     Region          2..303
                     /region_name="CeuB"
                     /note="ABC-type enterochelin transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG4606"
                     /db_xref="CDD:443656"
ORIGIN      
        1 mklflslcgl lvlafaslfv gvsslspadl fqlteaqqqi lwtsrvprll sillagvgms
       61 iaglimqqlt qnkfvsptta gtmdsarlgi lismiffaga hplfrislsm lfaiagtllf
      121 mqilnrikmk dpifiplvgl mfgsiigsit tffayqrdli qnmtawlqgn fstvitgsye
      181 mlylvlplvi lcyifanrft vagmgedfak nlgvsyktvv ntglilvavv tatvvltvgm
      241 ipflglvvpn lvtiflgdnl kknlpytaia gavfvlicdi fgrliiypye ipigmtvgvi
      301 gsglflylll rrrqhas
//
LOCUS       WP_176007888             308 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176007888
VERSION     WP_176007888.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..308
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34593
     Region          5..235
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mefavqvkda sksyrkrkss vdvlhnlslr vtkgkitall gpngsgkttl mkgmcgllkl
       61 dsgeitvnni passkkvlge vgcilegern vyyyltvydn lyyfgklnrl prkrlipmid
      121 tvleqlgllh kkhtyvsels rgmqqkvala vllikdppvf lldeptlgld vratlelcdy
      181 lkelsheqgk tvlltthqle iaekiadeii ffdkgevilh enketifshy qgenrwtiqt
      241 qtpveasvra eiqgwsaise dglqlevane hvfkviavle qqgvqiisle nskrnlqdif
      301 leitkvmt
//
LOCUS       WP_176007901             236 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Paenalkalicoccus suaedae].
ACCESSION   WP_176007901
VERSION     WP_176007901.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..236
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27078
     Region          1..230
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mlkyqqiald iermieteql krgvklpvle almkefevsk stitkaldll ekkgviyqvr
       61 gsgifvrghk rkgflslisn qgfkdsleef ditsevlelk ivqperyvrd aldlpegaea
      121 hyvkriryin gktlcvensy yskelipyln keivtgsifh yiteglklqi gfsdmylqvg
      181 klteeeagyl qlksgdpkls aetifhlnng kpfdysmity nyeqsqfyvq sgsylr
//
LOCUS       WP_176007928             332 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paenalkalicoccus suaedae].
ACCESSION   WP_176007928
VERSION     WP_176007928.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..332
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35029
     Region          7..330
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mstkeasaka gattfdfvsf lyrygtiili vllvalfasl npaflqpanl lsilrsisiv
       61 tliavgitis lsvggfdlsv gsvaslanav vismfvwysq ptlialavgf avalcvglfn
      121 awmivkirip dllltlavmf iiqgvaltyt rgatisqnmi msdgsyatgq ipaffsqlgr
      181 lpyiiiimvv avivvhiflt ytkhgrymym iggneeaarl sgipvnrykv layslsalfa
      241 alggivlasr vmtaeinagg pylmdavaaa figfavlgag kpnafgtfvg avligilang
      301 limmnvpyya mdivkgsvla lalavtyykq tn
//
LOCUS       WP_176007946             212 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Paenalkalicoccus suaedae].
ACCESSION   WP_176007946
VERSION     WP_176007946.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 212)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..212
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24259
     Region          5..192
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          <129..203
                     /region_name="ArgA"
                     /note="N-acetylglutamate synthase or related
                     acetyltransferase, GNAT family [Amino acid transport and
                     metabolism]; COG1246"
                     /db_xref="CDD:440859"
ORIGIN      
        1 mtveirevrq edisevkrlv artwgidgvf ddrtslevaa slfvntflhn gtfgrvavln
       61 eeivgliigs argdaprlrm lteepielia galgleeadv triqgylsti ftsyekllsp
      121 hkenyqgcle lfvvdtkarg nqvgkrllqe lttyfykhrv etyylftdtn ctygfydhng
      181 ftrrekeelt lpftidhqpa kmtnflydyt lh
//
LOCUS       WP_176007979             112 aa            linear   BCT 11-JAN-2025
DEFINITION  PadR family transcriptional regulator [Paenalkalicoccus suaedae].
ACCESSION   WP_176007979
VERSION     WP_176007979.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 112)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 112)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..112
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12560
     Region          1..103
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 mkerlikkyv pasetayyim lvlhespkhg ygiskrvevl tggrirlgsg tiygtitkml
       61 kdglivmyan eerkkiyelt eigeailqte ivritelhrh aaeiggdkde rg
//
LOCUS       WP_176008057             177 aa            linear   BCT 11-JAN-2025
DEFINITION  PadR family transcriptional regulator [Paenalkalicoccus suaedae].
ACCESSION   WP_176008057
VERSION     WP_176008057.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 177)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..177
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20503
     Region          7..86
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          94..176
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 mpktnrtrva vlgllttsck tgydmkqfid qslayfwkis ygqiyptlkq lvedgavrik
       61 nenadkkeye itsvgreelt nwlselpdal ptqknelllk lffsknqeve ksvallrhqq
      121 elleeklaay eaieemires deesedelyw mmtldhgkrl arasyewcea siktlrg
//
LOCUS       WP_176008072             325 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176008072
VERSION     WP_176008072.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..325
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35964
     Region          1..250
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mnigtigtgf ivdrfieash nvphmnvtas fsrqeetaks fthkhniasy ytdieallgd
       61 tsidaiyvas pnslhytytv qalehgkhvf cekpftsnsr eaqhvielak ernlflfeai
      121 ttihlpnyal irehiaslgp irlvqanysq yssrydkfla getpnvfsph ysggalqdin
      181 vynlhfvigl fgkpesvtya anvqrdidts gialltydgy vascagakdt asdgfvymqg
      241 ekgfihvvqg angcrevvik vgnsesrlna qtednvlyye iaawqklman ndfdacykll
      301 dhslhvmqtl ekarasagvr fegdn
//
LOCUS       WP_176008076             327 aa            linear   BCT 11-JAN-2025
DEFINITION  ring-cleaving dioxygenase [Paenalkalicoccus suaedae].
ACCESSION   WP_176008076
VERSION     WP_176008076.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10327061
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..327
                     /product="ring-cleaving dioxygenase"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37255
     Region          6..130
                     /region_name="VOC"
                     /note="vicinal oxygen chelate (VOC) family; cl14632"
                     /db_xref="CDD:472697"
     Region          157..313
                     /region_name="PcpA_C_like"
                     /note="C-terminal domain of Sphingobium chlorophenolicum
                     2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and
                     similar proteins; cd08347"
                     /db_xref="CDD:319935"
ORIGIN      
        1 mnglkgihhv taitssaekn yefftyvlgm rlvkktvnqd diqtyhlffa ddegsagtdm
       61 tffdfpgipk gshgtdeifk tgfrvpsdaa leywvkrfdh yevkhtgike rfgkqtlsfv
      121 dfdeqqyqlv sdeknegvpa gkpwqdgpvp lefaitglgp ihirtahfdf fqevlekvme
      181 fkeigtegsi hlfevgeggn gaqilleknv vlpqarqgfg tvhhvafrve nkevleewis
      241 rfgkfgfqts gyvnrfyfes myvnvapqvl felatdgpgf mddepyetlg eklalppkle
      301 pqreqieqyv reidtvrstk tiekeyy
//
LOCUS       WP_176008129             406 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paenalkalicoccus suaedae].
ACCESSION   WP_176008129
VERSION     WP_176008129.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 406)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..406
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44972
     Region          1..403
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
ORIGIN      
        1 mrnslkvakw elkrnlknks flislfltpa lfavfffvgf lfssgdsmpg dpfdqeitly
       61 iqddvgieee lseqlsddps ltyefgtyee esirgeelsv flpiteegva qgsityyatp
      121 dvsnfsflqp veqvmkqeql eqfdlateei eiaaspiafe gvpveeeiae geeaaefdif
      181 trlipggfaa lilfsviitg mmifqsasqe kkekvaemvl ssvtptelmq gkiigyfglg
      241 mvqvsvwfti ilplltlrtd ipifsylfvp qtivlvliai lgylmfasiy vaigatiedt
      301 tassnfqgll fiipwipfml agpiltnpsg tiaqvatfip ltapgvllfr lsfleewpwi
      361 eiigaiavla vaivlfmkla gkifktgill ygknasvkei lkwlry
//
LOCUS       WP_176008145             424 aa            linear   BCT 11-JAN-2025
DEFINITION  CapA family protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176008145
VERSION     WP_176008145.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..424
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=47277
     Region          54..377
                     /region_name="CapA"
                     /note="Poly-gamma-glutamate biosynthesis protein CapA/YwtB
                     (capsule formation), metallophosphatase superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2843"
                     /db_xref="CDD:442091"
ORIGIN      
        1 mndkldfkdr lklmqvnhkk kalphslial ailavpflgh nifanstvpt dtrpddvtyr
       61 msmvgdmmlg rhvadaarqa nepidrvfny vtpffeesdy vtgnfetpii ddsipeieae
      121 iedaelhnkd ihlyatpdag dalinagfds vtlannhmld ygdlslqqsl dyfrdadidi
      181 igmgdamnls eeeiaegaid aagvktfeld ddtrvgilgf tdvfvqgfsa qdfvggvftr
      241 eyaglgelrn rlieaklpee egglgvdimv vhihwgdeyq igsnaeqeer aqylanygvd
      301 ivighhshvl epvtilegfe gnrmlsmnsl gnfvfdqgwt rtkesviaql dfldngskel
      361 sfvpmflnqs qpqetagimk pyrdfrifrt lrkelprelw evrdgrlvid ldaagilegv
      421 dvtp
//
LOCUS       WP_176008187             251 aa            linear   BCT 11-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator
            [Paenalkalicoccus suaedae].
ACCESSION   WP_176008187
VERSION     WP_176008187.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..251
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27471
     Region          1..242
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mltlerheri lallkqqkia klhelveatg asestirrdl sileddhklk rihggasfls
       61 rkseepslle kktqhttekd aigkhaaslv enndciyvda gstteailph itaknvtvvt
      121 nglniieaal lqnlkvyvla gyvktgtraf vgkaaaesik qyrfdlafig tngidvsfgy
      181 stpdpeeasi kaaaiaqsnl aymvsdpskf rqtsftkiad lneaslitid ygdddyleel
      241 seytrveavk q
//
LOCUS       WP_176008193             487 aa            linear   BCT 11-JAN-2025
DEFINITION  catalase [Paenalkalicoccus suaedae].
ACCESSION   WP_176008193
VERSION     WP_176008193.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..487
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55991
     Region          3..479
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 mskklttnqg vpirdnqnsr tagengpill edyqllekia hfdrekvper vvhargfgah
       61 gvfkvknsmk rytkakflqe egqetpiftr fstvihghhs petlrdprgf svkfyteegn
      121 ydfvgnnlpv ffirdtmkfp dvihslkpdp rtnvqdgnry wdfmsltpes tnmllhlfsd
      181 egiprsyrtm rgssvhafkw vnahgnyvyv kyrwvpklgi qslsaeeaee iqgkdfnhas
      241 vdtfnaieeg dfpewdlyvq flqpedldey dfnpldatke wfeddfpyhh vgtmtlnknv
      301 enffaetesv gfnpgvlvpg iepsedkmlq grlfsysdtq ryrigtnylq lpincpyaqv
      361 annqrdgamp yaqqkstiny epnshegepe edpsqlehqa pvhgvtgrqp iekkndfgha
      421 gqvwntftde ykeslvknlt delgaideki amrqlcnfyr aseelgkrvs dnlnidiesy
      481 lqsmhnn
//
LOCUS       WP_176008225             352 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176008225
VERSION     WP_176008225.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..352
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38709
     Region          1..351
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msflqlenis kvfagagkpa vnglkltinq geivsllgps gcgktttlrm iagfenpseg
       61 tikidgativ kdafalppek rgigmvfqdy alfphmtilk nvmfglnkws srdkkkrake
      121 vlelvgleef adryptqisg gqqqrvalar alaprphvvl mdepfsnlda glrekmrfei
      181 tnilrrantt aiivthdqkd afavsdrvvv mnegeiqqia apkemyrcpk ncfvaqfvgk
      241 tnlltgkmdq dlrsihthig rvtlpeeskq lledvtlsvr pegcmlseqg aycgkvervt
      301 ysgeyqelhv hlqndgglap apmliyapve qdievgtvvs fdikpelval vd
//
LOCUS       WP_176008234             118 aa            linear   BCT 11-JAN-2025
DEFINITION  STAS domain-containing protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176008234
VERSION     WP_176008234.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..118
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12822
     Region          2..109
                     /region_name="STAS_RsbR_RsbS_like"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist domain of the 'stressosome' complex proteins
                     RsbS and RsbR, regulators of the bacterial stress
                     activated alternative sigma factor sigma-B by
                     phosphorylation; cd07041"
                     /db_xref="CDD:132912"
ORIGIN      
        1 mripilklhd yllisvqvel ddqtalqfqe dvlekihqeg srgvvidlts vdmidsfiak
       61 vlgdvvdmsn lmgakvvltg iqpavaitli dmgivlddvp taldleqgle rlqleleg
//
LOCUS       WP_176008236             109 aa            linear   BCT 11-JAN-2025
DEFINITION  STAS domain-containing protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176008236
VERSION     WP_176008236.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..109
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=11898
     Region          5..103
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(21,23..25,31,54,56..58,60..62,65..66,88,92..93,95)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            57
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 mnleinvtes enqnlaqvsg evdvytaskl ketlhplaeq pnkhlivdls dvnyidstgl
       61 gifigtlkst eksgstltlt glnervrrlf eitglnevie idatkreea
//
LOCUS       WP_176008253             481 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176008253
VERSION     WP_176008253.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..481
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=56438
     Region          1..394
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mrtgiyirvs tdeqvkegfs iraqherlnn fadsqdwsvv dyyieegvsa kdtkrqelnr
       61 lmkdiedgki dvvlvyrldr ltrsvrdlye lldfferync kfksatevyd tttamgrlfi
      121 tlvaalaqwe renlgervrm gqermieekq ypggpppfgy synkdtkqle vdpveakvve
      181 kmfdlyfdgf geqriadrln eqgyktrrgn nwrakavrdt lkrtlmtgef swggnmyndy
      241 tdaiipkerf esamklrtsr rgahprtirs sypfsgfarc arcgapmkgh skhgrkkldg
      301 tapfyrtyic trkrdgctsk qineesidre llkeirklss eyreisedks likreddhtq
      361 elkqltreln kvqgrrkkwq vayaegvisl delrshtemd qealsnlkmy isklesksmq
      421 ldyrsmanvl adfernwiel dhmekksmls mliksfdvds ddlkphkare rkvwvsnvef
      481 h
//
LOCUS       WP_176008384             332 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Paenalkalicoccus suaedae].
ACCESSION   WP_176008384
VERSION     WP_176008384.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..332
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36576
     Region          11..316
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(15..17,47,52,78,135..136,176..177,200,229..235,271,
                     288..291,296,299..300)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(47,52,78,135)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 msflktflnq pigygtaplg nmfrdvpeee aqatiesvwn egiryfdtap fygaglaetr
       61 lgeflkdkpr deyiistkvg rlisdekedk sgtglfeygn qnkiiqdyta egtrksieds
      121 lerlqtdyld ivyvhdispd fhgdewislf dearkgafkv lqemkeegvi rdwglgvnlp
      181 lpievalgle etvptlslqa thytlmnhhs alnslmplae ekgsgivvgg pynsgallgg
      241 dhydyapase etkqhaqelk kianqhgvsl kaaalqfsta hpavaavipg strpdriked
      301 iaalketipe afwnelrekn liskdaplpg sn
//
LOCUS       WP_176008378             188 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paenalkalicoccus
            suaedae].
ACCESSION   WP_176008378
VERSION     WP_176008378.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..188
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21852
     Region          8..155
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
     Region          86..182
                     /region_name="TetR_C_8"
                     /note="Transcriptional regulator C-terminal region;
                     pfam14278"
                     /db_xref="CDD:464123"
ORIGIN      
        1 mskkldhrkr ytrkvlkdsl itlmaekkia aitvkeical akvnrstfya hfkdpfdlld
       61 hieeeisedm qrylenipln sdevaqemte qilhylkehr miietllnhe gaptfekklm
      121 tltrqymvkg alrdaevddt elrylttfvl sgaihvikdw ieqdmvqspa eiarminsfv
      181 tsgfsylr
//
LOCUS       WP_176008469             421 aa            linear   BCT 11-JAN-2025
DEFINITION  hemolysin family protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176008469
VERSION     WP_176008469.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..421
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=46765
     Region          8..416
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mdsipygsil llgaflflsa yfsasetait sankvrlrtl aeennprakr slaltenfdr
       61 slstilignn vvnigltamg taiatsifgg tattlllttv vitvvvltfg eilpksfakq
      121 rpeklllgvs wslqtvlvvl tpvtwlfvql kkglnrliks emepsvtded vkalvtigee
      181 egtfeiqere llhnaiefdd tivrdiltpr pditavgvda dieevkdifi rekfsripiy
      241 eesvdnivgv lsyrdfmtky venepfalkd tmrapyfvig tvkisgllkd lqnnkvhlai
      301 vldeyggtag iisiedilee ivgdiwdehd dkellieald asrfrmdgsi sledfcesvd
      361 islpatdsyt lggwiselfg ylpkkgesvv yehirihvee vrrrrvksvi ievdtpvyvg
      421 i
//
LOCUS       WP_176008393             373 aa            linear   BCT 11-JAN-2025
DEFINITION  GGDEF domain-containing protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176008393
VERSION     WP_176008393.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..373
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41704
     Region          5..>196
                     /region_name="KinB"
                     /note="Sporulation sensor histidine kinase B [Cell cycle
                     control, cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG5806"
                     /db_xref="CDD:444508"
     Region          <171..357
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mldlvkella niaiitsglf vysqltkdkp lnrhssflrk mfvgltggml atvlmtyslr
       61 ldealldlrf ipviilvyyg gaipalfsmi piiigrflie vseaafyspi llilvvllgl
      121 litklpvsql vkvflmisst ffwfsfllie vnmetnells vlaffacmsy iagflafyti
      181 dyvrnaqkim reyrkaaltd pltglhnirq fdqlfnswsk qaqlskssla ilfididhfk
      241 kvndtyghpe gdivlktlsq liekevrsdd ivsrnggeef tvllrtisls qsmqlaerir
      301 qlvertpfal sngtkisitv sigfahypet tacgdrilkd adaalyvakn sgrnrvvkat
      361 gvtlfspgke dek
//
LOCUS       WP_176008492             314 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176008492
VERSION     WP_176008492.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..314
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34547
     Region          6..227
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mekpvlqvke ltkrvsgmkk ivddvsfevn kgeivgllgp ngagkttiir migglinktn
       61 gsviingqda drdpeacree igaivenpsf ydfmsgyknl qqyarlsret itkeridevv
      121 alvklenaik dkvrkyslgm kqrlgvaqai lhkpsllild eptngldpkg irelrdylre
      181 manegtavlv sshllsemql mcdrfivveh gklidstvls dqsveevsth vsiqisqeqq
      241 klavaaieel evaelvraek amltvslpyd sipklneflv gkgvrifglq sqkesledrf
      301 laltaektag gsaq
//
LOCUS       WP_176008501             316 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Paenalkalicoccus suaedae].
ACCESSION   WP_176008501
VERSION     WP_176008501.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..316
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34486
     Region          11..310
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mtkdklsrvv kvakmyyqld ysqqtiakel gisrpsvsrl lhaakekgiv kitivdpdeg
       61 vaeladvika rfglkeciia dapvnenqvi keelgrkaae ylhgivkdgd iigttwgttl
      121 yevarhmqpk sihnvtvtql nggvsysetn tyaaeilhfl gnafhtspyf lplpavvdhl
      181 vvkqaivsdr hirhvlelgk katialltvg erhedsalvk anyyteedkh vlksrqavgd
      241 icsrmitidg dicdadindr tigieleslr didhsilvvg gltkvegilg alhggyanvl
      301 iidqyaaqal admgan
//
LOCUS       WP_176008498             419 aa            linear   BCT 11-JAN-2025
DEFINITION  NupC/NupG family nucleoside CNT transporter [Paenalkalicoccus
            suaedae].
ACCESSION   WP_176008498
VERSION     WP_176008498.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Hirschi,M., Johnson,Z.L. and Lee,S.Y.
  TITLE     Visualizing multistep elevator-like transitions of a nucleoside
            transporter
  JOURNAL   Nature 545 (7652), 66-70 (2017)
   PUBMED   28424521
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Johnson,Z.L., Lee,J.H., Lee,K., Lee,M., Kwon,D.Y., Hong,J. and
            Lee,S.Y.
  TITLE     Structural basis of nucleoside and nucleoside drug selectivity by
            concentrative nucleoside transporters
  JOURNAL   Elife 3, e03604 (2014)
   PUBMED   25082345
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Munch-Petersen,A., Mygind,B., Nicolaisen,A. and Pihl,N.J.
  TITLE     Nucleoside transport in cells and membrane vesicles from
            Escherichia coli K12
  JOURNAL   J Biol Chem 254 (10), 3730-3737 (1979)
   PUBMED   374403
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..419
                     /product="NupC/NupG family nucleoside CNT transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005337 - nucleoside transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:1901642 - nucleoside transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=43778
     Region          1..418
                     /region_name="NupC"
                     /note="Nucleoside permease NupC [Nucleotide transport and
                     metabolism]; COG1972"
                     /db_xref="CDD:441575"
ORIGIN      
        1 mnilwglmgi aivvgigill stdrkaikpr tilaglalqi tfaflvlvsd vgraalqglt
       61 nvvnsivgft deginflfgg lfeaegigmv fafqvltvvi ffsslisvly ylgimqwivr
      121 liggalakll gtsrteslsa aanifvgqte aplvvkpfln hmtrselfav mtgglasvag
      181 svligysllg vpleyllaas fmaapsglvm aklmlpeteh dktsdkldie meddkesfnv
      241 idaaargast gmtlalniaa mllafiaiia llngilgavq sgvnglvdfi pgidftlsgf
      301 tlenifgfif aplafaigvp wgeavqagsf igqklilnef vaysnfapvi gdlsektali
      361 itfalcgfan vsslgillgg lgklapnrrq diaqlgirav aagmlaslln aaiagmffi
//
LOCUS       WP_176008532             200 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176008532
VERSION     WP_176008532.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14449023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..200
                     /product="cupin domain-containing protein"
                     /calculated_mol_wt=22326
     Region          16..167
                     /region_name="cupin_OxDC-like"
                     /note="Oxalate decarboxylase (OxDC)-like cupin domain;
                     cd20306"
                     /db_xref="CDD:380440"
ORIGIN      
        1 mvsnmdyisp naqftfdmnq splfvkdsqn yinvlgvkql ntlqgsslld iflstnnvve
       61 phyhqnaael vycisgsatv nilnpftkql qsytitpgqv anvpqgwwhy evalvdrthl
      121 laifdaptpe vvlgsdilrf tpssvmahty cmdeqtwkda iapvkpstyi gpytdcdqpp
      181 sppaqahtyy pmphqhypty
//
LOCUS       WP_176008556             222 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Paenalkalicoccus
            suaedae].
ACCESSION   WP_176008556
VERSION     WP_176008556.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..222
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24967
     Region          18..212
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mknyinqfel dklfpphvqa smrlhtfkqg dvifdqadea ttmlflvkgk ikiytssseg
       61 ktllltfktp lsvigdvefv qqvplintve avsdvemlgi sydvlrkemr envefisfll
      121 hviagkfysr smmsntaqly pvnvrlasyl vshatagsdl iptgtlhdta nligtsyrhl
      181 nrviqqfeed glvkrtkqgi kitglnglre rsdeasyewe ea
//
LOCUS       WP_176008727             325 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Paenalkalicoccus suaedae].
ACCESSION   WP_176008727
VERSION     WP_176008727.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..325
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36560
     Region          9..295
                     /region_name="AKR_AKR11C1"
                     /note="AKR11C family of aldo-keto reductase (AKR);
                     cd19086"
                     /db_xref="CDD:381312"
     Site            order(17..19,49,54,79,119..120,150..151,170,198..204,263,
                     280..285,288,291..292)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381312"
     Site            order(49,54,79,119)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381312"
ORIGIN      
        1 mnyrtlgdlk iselsfgtwa iggawgktnd eeavrglkqa meqgvnffdt advygdghae
       61 rlireatkgq edqiyvaskf cragdihdpv tyqeesvrhy lektlknlgr eqldlyqihc
      121 ppleiikdgs vfevldklqq egkirhygvs vetveeglea mtyknvralq vifnifrqkp
      181 vhelfpiake kevgilarvp lasglltgkf keshqfeedd hrnfnadgqq fnvgetfagl
      241 pfakgvalsq eldwikegre smakaalkwi lehdavssvi pgfkttkqve dslgavdvpa
      301 ftgeemqrle tfyqahvneh irgpy
//
LOCUS       WP_176008679             621 aa            linear   BCT 11-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Paenalkalicoccus
            suaedae].
ACCESSION   WP_176008679
VERSION     WP_176008679.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..621
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=69591
     Region          4..619
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mrlfagsllt vffigtffll ftqtskelss aqtlhevlde qirfteidlp ansvmtdrng
       61 niisdiysdq nrvfieyddi pqsmidlfia vedklfyehe gfdvsgiara livnlqsdgi
      121 eqgastitqq varnlylshe qsyerkitel lyayqlerem skedilelyi ntiyfangvy
      181 gfeaasqyyf sksvhdltla etaflgaipn nptvynpltn ednthsrkef mlnrmlnegf
      241 iaeeerdaal qesivfsske kvdeypdyvt yiyheldali aesegyrdql kqattpeare
      301 ainetirerr qtilragvti etaldqqiqr hlvttintrl dgspveaaas vvdhqsneiv
      361 altggknyrk fdfhrgyqak rqpgsaikpl lsfapfieat gqtrtsivda gpfsrngysp
      421 tnfgggvygl vtmeqafvqs yntaavrmld sigidsgfsy lnqfdfssiv nddyrlpaal
      481 ggftngmsvn emtqaytvfq tegnylspra ikrvvdlegn elyswskspk avysadtatq
      541 ikrmmqenvn rgtgreagrg vagyvggktg ttntyhdlwf vgateahtvg lwigqdqptp
      601 lqsessgqlh trlwnqlvrg f
//
LOCUS       WP_176008733             318 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Paenalkalicoccus suaedae].
ACCESSION   WP_176008733
VERSION     WP_176008733.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..318
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35570
     Region          60..316
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 maghipvepl yapkpkrpfr wlvrllvflv vmltivilgi svyvglnmtr tdtkplmgtp
       61 edvdlpyedm syfsadgets lsgwliepes datatiimsh gyrgnreeen vgflslanef
      121 reegyrvily dfrnagdsag sittigdmeq ddlagtvewa nerfddpvil ygismgaatt
      181 lgyagredse diasivvdsp fsslrsylet nmsvwtnlpd fpftpiilyt aplytgidvd
      241 rlepieavns iyptpilfih siddplipyt esermhalhp dafdiwlpeg pdhvqtypdm
      301 peeylervlp fiedalan
//
LOCUS       WP_176008734             278 aa            linear   BCT 11-JAN-2025
DEFINITION  STAS domain-containing protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176008734
VERSION     WP_176008734.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..278
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30879
     Region          162..270
                     /region_name="STAS_RsbR_RsbS_like"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist domain of the 'stressosome' complex proteins
                     RsbS and RsbR, regulators of the bacterial stress
                     activated alternative sigma factor sigma-B by
                     phosphorylation; cd07041"
                     /db_xref="CDD:132912"
ORIGIN      
        1 mvnplissig ealqhsketi ahdiyqsfrt khdvqfskip qdsflkklea yveilgselk
       61 ehatedtnla arewgkefgn haaslglsae kamlvvpilr rtlyeiirae fgrevhdvkd
      121 yyeiadaidp ildrtiyaft qeyveeneks laqvqaevme lsvpvvpltq evailpiigt
      181 instrsqlll tqaldrgrel klshlivdls gvhvmdtyva qnlfnlhdal kvvgikaifs
      241 glrpslaqtl vhlgisfehv avvsnlkqal kmadlsls
//
LOCUS       WP_176008743             290 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176008743
VERSION     WP_176008743.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..290
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32481
     Region          3..217
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mkvqhlskii hnkeilkdie fevetgniig ivgrngagkt tllrtmagil sptkgdvlve
       61 dksifeqhkl keqilfvpds sealknystk eilklykaiy pnfdtdyfha lmgkfalpqv
      121 skigtyskgm kalfsiiiaf atkahyilld eptdgldviv kkqvlqllve evadkersvi
      181 isshrldele fmandiimik dgrvdthyel dalksqyika qvvfeadmpd elhehvtiva
      241 qtgrvytill drqnevasna ihshspllfe elslsledif vaklggesdv
//
LOCUS       WP_176008836             215 aa            linear   BCT 11-JAN-2025
DEFINITION  O-methyltransferase [Paenalkalicoccus suaedae].
ACCESSION   WP_176008836
VERSION     WP_176008836.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..215
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24313
     Region          36..214
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mnndkthqyi tslippregl llqmeeyale nnvpimdveg mhvllellkl qkpsrilevg
       61 taigysgirm lkachgaslv sierdeervr lakenilkak ledrftiieg dalevfsqva
      121 nhspydvlfi daakgqyekf fqlyeplvae dgvilsdntl frgyvaneve pesrrmrsma
      181 kklaeynasl mnhdrfssml lpvgdgllvt rkekq
//
LOCUS       WP_176008920             291 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter permease [Paenalkalicoccus suaedae].
ACCESSION   WP_176008920
VERSION     WP_176008920.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 291)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..291
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31040
     Region          14..273
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mrsiqlfidq lmnytylqna lvaailvgvi cgvigcfiil rgmalmgdai shavlpgvvv
       61 symisgsffi gavftgvlta laigfisrns kikedsaigi mftgmfalgi vlmtalrgss
      121 idlnhilfgn vlavssqdfl itlvigiivl lsififyrpl llstfdetma qatghpvrai
      181 hyllmlllsl vtvaslqtvg iilvvamlit pgatayllte rfsvmlflsa lfgvlsavig
      241 lffsviydva sgasivlaas sffvlaflfa pkqgylskml rspkkseqia n
//
LOCUS       WP_176008924             272 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Paenalkalicoccus
            suaedae].
ACCESSION   WP_176008924
VERSION     WP_176008924.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..272
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30383
     Region          1..250
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mketnfvvev egvsfayrqq tvledihmri pagsflglcg pngsgkstli klllglnrpv
       61 dgqvklfgts vksfknwski gfvsqkansf nsgfpatvfe vvsmglygkv glfrfltkkh
      121 kekvkeaikq vdmqdfmyan igelsggqqq rvfiaralvs dpellildep tvgvdaksvs
      181 nfytmlrdln tnkgitlilv thdigamtdy vtdvaclnkc lhfhgnksdf eenqeemlsa
      241 myghdvsmie hnhdhhhhdh hhdhdhvrge vr
//
LOCUS       WP_176008944             202 aa            linear   BCT 11-JAN-2025
DEFINITION  superoxide dismutase [Paenalkalicoccus suaedae].
ACCESSION   WP_176008944
VERSION     WP_176008944.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..202
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22527
     Region          4..197
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mafslpelpy ahnalephid eetmkihhgk hhqtyvtkln daleghsdlq sksieelltd
       61 ldalpesvrg pvrnnggghf nhtlfwqlms pngggapsge laeaiestfg sfdsfkedfk
      121 nagltrfgsg wawlvvnngk leitstpnqd tpisegktpi lgvdvwehay ylkyqnkrpd
      181 yvdaffnvvn wdevakryne ak
//
LOCUS       WP_176008978             123 aa            linear   BCT 11-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Paenalkalicoccus
            suaedae].
ACCESSION   WP_176008978
VERSION     WP_176008978.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..123
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=14348
     Region          26..118
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mlwvyigitl llvafilfrl kkpsflttie qeeftknyrk aqlidvreer efqtghilga
       61 rniplsqlrm rnteirpdkp vylycqngsr svqaskiink krgaediyml kggfrkwsgk
      121 ikk
//
LOCUS       WP_176009049             261 aa            linear   BCT 11-JAN-2025
DEFINITION  carotenoid biosynthesis protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176009049
VERSION     WP_176009049.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..261
                     /product="carotenoid biosynthesis protein"
                     /calculated_mol_wt=29627
     Region          2..252
                     /region_name="COG2324"
                     /note="Uncharacterized membrane protein [Function
                     unknown]"
                     /db_xref="CDD:441898"
ORIGIN      
        1 mpstfdlylf rfflvwygvg villsfdlvp pwlewanvvf litagllamv ylirsqlkiv
       61 gvflvilifa lsmaiesfgv htglffgdys yqadfgpkvi gvpitigfaw vmviatshvl
      121 aapiihmvgr fkrliytiyg aliatsldli idpvaydvkq ywvwneggly ydipfsnfyg
      181 wfilsfvlhg visllvyrgg ewrnrfsefw rskmvflyva malmfvival vnglvlapiv
      241 svstvllfvg lyflferkla r
//
LOCUS       WP_176009064             389 aa            linear   BCT 11-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein
            [Paenalkalicoccus suaedae].
ACCESSION   WP_176009064
VERSION     WP_176009064.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..389
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=42921
     Region          1..364
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mkkwilimlv istlfptsaf aeevmqesri mleartgtvl meqaadvqrq pasmtkmmtm
       61 lliieaienh sldwedsvti senaasmggs qifleageqm tvkdlmkgia iasgndatva
      121 maeklagsee afvtmmnera kelgavstvf kntnglpeeg hvstardmai igqelvkhee
      181 ildftstyed ylrtetdkpf wlvntnklir typgvdglkt gftreakygi tvsalrdnmr
      241 litvvmgaes akernkqias mldtgfdtyt vepyleaaeh vsdmyisrga kqviaataqd
      301 slaevrkkse efeeatavve ldqvsapiak gqtiglmqlk rgeeviastp lisneeveea
      361 sfwqfftrsf smltkgnvet skqttsfde
//
LOCUS       WP_176009070             145 aa            linear   BCT 11-JAN-2025
DEFINITION  peptidylprolyl isomerase [Paenalkalicoccus suaedae].
ACCESSION   WP_176009070
VERSION     WP_176009070.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..145
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=15590
     Region          14..137
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mkkgeiifgn gekivieffp eaapghvenf eklasdgfyn glnfhrvipg fvaqggcpng
       61 tgtggpgyti kcetegnphk hqkgtlsmah agrdtggsqf flvfdpqphl dgvhtvfgqv
      121 iegldvmdri kqgdvmeevk vydve
//
LOCUS       WP_176009149             290 aa            linear   BCT 11-JAN-2025
DEFINITION  YitT family protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176009149
VERSION     WP_176009149.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..290
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=31936
     Region          6..284
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 myppikirhi llillgtail sfglvyfnme nnladggftg itlilffmfe fnpaytnlll
       61 niplfiigwk ilgrnvfiyt vigtvgvsvf lwlfqaypim slplqddmtl aalfagvfig
      121 vglgivfrvg gttggvdiia klgfnyfgws mgrtmfvfda vvitasliyl dyreamytiv
      181 avfvaakvid fmqqgaysgk aamiisdhvp eiataileem drgatmlkgr gsftgndrev
      241 lycvvgrnem vrlkktiarv dphafvtlqd vqdvmgegft ldenkrplgv
//
LOCUS       WP_176009175             185 aa            linear   BCT 11-JAN-2025
DEFINITION  cysteine hydrolase family protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176009175
VERSION     WP_176009175.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..185
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20778
     Region          3..178
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mralividyt ydfvapdgkl tcgergqaie drlteitkgf merqdytila idahkendsf
       61 hpesklfpph nvigtkgrel ygklqplveg snnyewfdkt rysafagtei emklrerkit
      121 evhlvgvctd icvlhtavda ynkgfsivvh edavdsfnpe ghewalghfk dtlgatvvsa
      181 wtped
//
LOCUS       WP_176009200             308 aa            linear   BCT 11-JAN-2025
DEFINITION  dipeptidase [Paenalkalicoccus suaedae].
ACCESSION   WP_176009200
VERSION     WP_176009200.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..308
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=34396
     Region          1..308
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 mnvidlhcda llrldelsda sfidderlev nlnrlkqgkv kvqffaifie pdipsdqkfy
       61 ealkqadlfh khvltapgir fitswdqinq lkedeigavl tlegadpigq dlvklstlyh
      121 lgvrsfgltw nqanlvadgi geprggglte fgfdvvkfnn ehrmltdvsh lsiagfydvm
      181 ktaaypiath snatsinphr rnlndeqidt likakgiigi vynppfvgks ddtasieeli
      241 ehidyilnrg gedcialgsd fdgietyves lehagkhqnl idallnkyer slvekiahkn
      301 vraylnri
//
LOCUS       WP_176009213             258 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paenalkalicoccus suaedae].
ACCESSION   WP_176009213
VERSION     WP_176009213.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Beis,K.
  TITLE     Structural basis for the mechanism of ABC transporters
  JOURNAL   Biochem Soc Trans 43 (5), 889-893 (2015)
   PUBMED   26517899
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Saurin,W., Hofnung,M. and Dassa,E.
  TITLE     Getting in or out: early segregation between importers and
            exporters in the evolution of ATP-binding cassette (ABC)
            transporters
  JOURNAL   J Mol Evol 48 (1), 22-41 (1999)
   PUBMED   9873074
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..258
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=27131
     Region          58..249
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mspflahtyv ltkrsvivll rnpftvipnl fismffllvy sgglsgiasl pafegadyls
       61 filpvsivsa aiggaggagq slirdlesgy farllqtpvs rlaivlgpii agmlqllvqt
      121 giilavafll glrveagvgg vlvlllfaig wglafagysv aialktknaq aaqagtliff
      181 pllflsttfv plelieatwl rvaavmnptt ylfdamravl idgwvwqpil igasviaiac
      241 aitiglsvrs aktafsrd
//
LOCUS       WP_176009220             360 aa            linear   BCT 11-JAN-2025
DEFINITION  AI-2E family transporter [Paenalkalicoccus suaedae].
ACCESSION   WP_176009220
VERSION     WP_176009220.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..360
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39424
     Region          37..355
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mpkskwflfl ysvvlilvti nlavevpfif rpigialgsi apviilggvl yyilrplvhl
       61 lnkklpkvvs illifaafag llallirvvg piiveqttel vnnfpsiirq verwinetla
      121 sdwvqviqne pifeqfdpsv itdnlsnila saggsilsgi gmlfsvvtvi vlipfvlffl
      181 lkdgnkfpds vlkilpsdqh kegrkimsdm dntisayiqg qaivsvfvgv fayiayliig
      241 ldyslilalv amftnlipfi gpfigtapav vvgffndplt avwvivaivi iqqiesnlis
      301 pnvmghklqm hpltiilllv iagnlaglig lifaiptyai skvlvqniyr llklkypnln
//
LOCUS       WP_176009234             375 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176009234
VERSION     WP_176009234.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..375
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40976
     Region          7..375
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msikttqlie eahilkekfa draafydesa mlpeenirdl knafflsmtv servgghglt
       61 lvpmleiltt laegdaptal sfgwhagycl elsedsispk tekllttiak eqvllnlaqt
      121 ekatgsparg gaptvsaarr dsgwvingtk tftsfakald yavisatvke tgekgffvid
      181 mtkpgvtiee twdsvsmrat rsddlvltdv fveedallkt ealtspkprg wyllvpavyl
      241 gvakaaraya kefansyqps tlphpiaevp evqrkfgeie lalfeaetll hatarkweet
      301 dlqsrddlrg dlgatkkivt ekaniivdla mkvvgaksls qscplqrhfr dvraglhnpp
      361 aedlvisqlg knilk
//
LOCUS       WP_176009235             534 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Paenalkalicoccus suaedae].
ACCESSION   WP_176009235
VERSION     WP_176009235.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..534
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59898
     Region          4..527
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mlqatdvslr fgdkklfeev nikfnpgncy gligangagk stflkilsge lepqtgnvsl
       61 gknerlavlk qdhfayedev vldtvmighe rlyevmkekd aiymkpdfsd edgmraaele
      121 gefaemngye aesdaavllq glgiadelhq akmseltegq kvkvllaqal fgspdvllld
      181 eptngldiea itwledflas fentvivvsh drhflnnvct hiadldfski qiyvgnydfw
      241 yessqlaqkm aqernkkkee kidelksfva rfsanasksk qatsrkklld kieledirps
      301 srkypyiafk pereigndvl vvenisktvd gkqllnnvsf slnredkval vgsneqaktl
      361 lmqilmgeve pdsgsfkwgl tttqsyfpkd nseffensnd pslidwlrpy spedqsesfi
      421 rgflgrmlfs geeakkspsv lsggekvrcm lskmmlsgsn vllldeptnh ldlesitaln
      481 ngliqfkgvl mfashdhqfn qsianriidi qdegvidkem tydeyvaskl qttk
//
LOCUS       WP_176009244             277 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Paenalkalicoccus suaedae].
ACCESSION   WP_176009244
VERSION     WP_176009244.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..277
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31536
     Region          1..>173
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mrditfkysd kkslplyykq akeftntavl cihgvtsemd awdtastiis ekanvdcymp
       61 ilrgyddapv gdlkkkgqfd sdihdlltyl ynrytnviai ghsmgsgnll rylstyndtr
      121 lkhtiftapf fhpalntfyk eeeqdrpedm tytvyynkvm aigildrlkl plfhtttvve
      181 iphrkvpydv nsktsvkkls frlmisrfie npakipsvpl dhstvlvgrf dqivhpellt
      241 tywtssvgrd vtiaegadhn silsskelle tvkkyag
//
LOCUS       WP_176009268             877 aa            linear   BCT 11-JAN-2025
DEFINITION  RHS repeat domain-containing protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176009268
VERSION     WP_176009268.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 877)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..877
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..877
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=98103
     Region          <106..789
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mlndagiepk gasfisaple piragktyta ssvvsgkelg datafiaiel ysstgaklgr
       61 eeiqrpinkl dywtplyvqm seqrakqiha sathmrvvvg skgrftgtml vdnvrlddqi
      121 srdsyaydak gnylieetdg lgrkvtytnd argnitrinf sksgvftnyv ydeldrvtsv
      181 sdhrlrfdls hdangnisqi qyrpsasssv fssvsqhhde ldrltrtvdq lgaetrfaye
      241 pngtlkqvty ptggqihyay nafdeltrvs yggtdtltwd yeydksgnqt katqngslvt
      301 tytydsldrv tkeeypavng trntltytyn edgdvetyth srvgqvrfah dasgksnsae
      361 gpqgqrmdym ydesggikka flklnaesfs tyydynpvgq psrirqenkh gdlvsdeqlt
      421 fdenghitev rslsgarvty eydndyqlrk ethrnaagai tldqsyeydf lgnrlsktvg
      481 aarttytydk anhlhhqgsl tythdhvgnt tsrgdtnfvy ntdreltevk ragatiatyd
      541 ynhhgmrtkk vagsrtehyy ytgkdlayit daqnrirssf vrdalgqlmt ytdhtgaspk
      601 tylyvlnhrg dvlglrdedg imvvtytyda ygniisqsgt gltgdgrllr eanpfryasy
      661 vydeetslyy vqtryydadt grfltrdiva dtnlyiyadn npvnfvdpdg rvpipliifl
      721 akagfkayta ystykaiknd psmknillsl mpggkitrmg gkkilafakg tksvgiigks
      781 ygkngrfgtv vknpkikiss fsghavnqai trgvktkeiq stvnkpiavl sqwggkkfay
      841 vskkavvvmd nkgriitiwg kkqfddvvkq vikdsrr
//
LOCUS       WP_176009283             131 aa            linear   BCT 11-JAN-2025
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Paenalkalicoccus
            suaedae].
ACCESSION   WP_176009283
VERSION     WP_176009283.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..131
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14849
     Region          1..124
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mptsiilfdg ychvcdasiq fimkhdkkdt ftfaslqgek gaqlkkdydi qvdsvvliep
       61 sgrvytksda alrickqlsg fpkilqigll lprflrdavy eliaknryrf fgkrdtcrlp
      121 tpeerakfld g
//
LOCUS       WP_176009349             311 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Paenalkalicoccus suaedae].
ACCESSION   WP_176009349
VERSION     WP_176009349.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..311
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36072
     Region          48..308
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mekwiehiqk htlsldesnp hlhnedllay lsfysfhmdr vhtyrcgfvp sahfriftql
       61 fsrkkakglv vlvhgyldha gglsktvnhl ledgydvltl dlpghgmteg gngsirtfde
      121 yvqaiidvce tstyyvkqtt iigmghstga amlfhtacqn kikfdrlifv aplfmpfrwt
      181 lvkgiikaag kvrprsrrrf krnsadrtyh sfikkdplqs kwlhadwlla meawqssien
      241 clvyknpvyl iqgtkdttve wpvnirffrk kckniqvmll pegrhqllne rglyreiime
      301 risqflrqsv k
//
LOCUS       WP_176009287             131 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Paenalkalicoccus suaedae].
ACCESSION   WP_176009287
VERSION     WP_176009287.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..131
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=14485
     Region          3..116
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mlitlnfesd eaiysqivkq viigiakkql qpndplpsvr slaadiginl htvnkayqql
       61 kqegyilihr qkgvvvhpeg vgkatekyve svkdtlrpii aeglckqlsd esilaifket
      121 ldefspkede s
//
LOCUS       WP_176009624             370 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Paenalkalicoccus
            suaedae].
ACCESSION   WP_176009624
VERSION     WP_176009624.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..370
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41701
     Region          70..350
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 meevaqqfsw qelliavgif flflvfrklf ttyvfkmivs lsrkiptdli tnillaferp
       61 mrsfmvfigl fiafvyfplp dtyqaiftqi frsiiivhva wglfnlasss ssiltsvgkr
      121 fdvaeddilm pfvsklirfa ivamglsivl sewgfevggf vaglglggla falaaqeslg
      181 nffggvviit ekpfavgdwi stpsvegive dinfrstlvr tfsdslitvp nstlsnepie
      241 nwsqmgkrrv sfnlgveygt pvarlrslmt kldtylrnhe dvdqelimvk fsefqdssle
      301 ilvyyftkpt gwvdhlnike siniaiihml eeedvkiafp tstlhvendd eiaflndlek
      361 ntqqskende
//
LOCUS       WP_176009635              66 aa            linear   BCT 11-JAN-2025
DEFINITION  cold-shock protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176009635
VERSION     WP_176009635.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 66)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 66)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..66
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..66
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7148
     Region          1..63
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mtqgtvkwfn aekgfgfiev egqddvfvhf saiqgdgfkt leegqavtfd ieqgqrgpqa
       61 anvnkq
//
LOCUS       WP_176009670             501 aa            linear   BCT 11-JAN-2025
DEFINITION  HD-GYP domain-containing protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176009670
VERSION     WP_176009670.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..501
                     /product="HD-GYP domain-containing protein"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=56617
     Region          184..495
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 meqtiiqrfq rqiiisyvlg svlavfgvgs vfifrtlils asevlyllii mvlsatimis
       61 aelvlykkht ksiynvfiks npsykeleea fitayrfpkl tfiriigphl fglgipatil
      121 tivfiemnil sfpyyyigya wvgailiaim hgfiefflca rpsrelgqqi nlyakrmynr
      181 piflngryfl sirtklflsi iftatfpvvl mllalqirti aasnnmldsy wswssvilvv
      241 ilavslacsv llymsikepi erlssqftra segtfekmeq tyadefddlv sgfntmvtgi
      301 nlrderneel ldglfavfat tldardeyta ghsfrvadys vkiaetlnme edqidvvrrs
      361 allhdigkig isdsillktg kltkeefdvi kehpglgarm lediglpdel lpilpgvkyh
      421 herydgrgyp eglrgddipl lgrllgvada fdamtsdrpy vkgksfdeal aiidaekgsq
      481 fdpyfadvfi qlmneekklr a
//
LOCUS       WP_176009779             126 aa            linear   BCT 11-JAN-2025
DEFINITION  rhodanese-like domain-containing protein [Paenalkalicoccus
            suaedae].
ACCESSION   WP_176009779
VERSION     WP_176009779.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..126
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=14017
     Region          6..101
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 msyeldgvkq yskeelkell vnpgnkviid vreeeeytng hipsvplapm gtipdlisgf
       61 qddkeyvfvc rsgnrsqrvs qflqqqgltn vanyeggmlv wdgdtlqgde kqlqsaeela
      121 dysgke
//
LOCUS       WP_176009901             127 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease [Paenalkalicoccus suaedae].
ACCESSION   WP_176009901
VERSION     WP_176009901.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..127
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14710
     Region          44..109
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mpikpkkkcs vvscnvltse rfcpdhkkey yrrldkergt ahergynsrw rkarlfylrr
       61 hplckrcadn gqdvpaqvvd hiiphkgdak lfwaevnwqs lckschdtkt akedggfgre
      121 ainepkq
//
LOCUS       WP_176009781             436 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar ABC transporter permease [Paenalkalicoccus suaedae].
ACCESSION   WP_176009781
VERSION     WP_176009781.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 436)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   5  (residues 1 to 436)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15767475
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..436
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49169
     Region          16..>113
                     /region_name="DUF5683"
                     /note="Family of unknown function (DUF5683); pfam18935"
                     /db_xref="CDD:465918"
     Region          120..428
                     /region_name="UgpA"
                     /note="ABC-type sugar transport system, permease component
                     [Carbohydrate transport and metabolism]; COG1175"
                     /db_xref="CDD:440788"
ORIGIN      
        1 maatnkndkh dllvnkkhnp tvaallsiip glgqaynkrf lkgaalfilf aafvvaftel
       61 isaglqglvt lgevpredds riflsngils liftafflsf yilniqdafk dakriqlgwk
      121 vpniregfrn awdnsfpyll igpglfllif vvifpllfmv flaftnynly napprnllew
      181 vgfenfvtlf tinewrttff nvlswtliwt fvattlqigl alflavlvnd prvrfkklir
      241 tvlilpwavp gfvtiiifsa lfndnfgain lqiieplfgq rvpwltdata trvaiimiqv
      301 wlgfpfvyal ftgvlqgisa dwyeaadmdg anrwqkfrni tfphvmfata pllimqyagn
      361 fnnfniiylf nqggpavrgq taggtdilis wiygltftnq qfnmaaaisi ilgilvagfa
      421 ffqfrrsrsf keegtf
//
LOCUS       WP_176009783             576 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176009783
VERSION     WP_176009783.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..576
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=63769
     Region          12..554
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mgkkgvkrgr qslvrllygv icitllvtic sggliyyfnn evqtqtntld evadfqqsyn
       61 dllsninevs slklqlvstg yrenqvsrme sllvnsaeev eglrqrasdr egidhyfdti
      121 esainaysiq yetyfssifv gdeieqirtr ivpvvtrtee qlinvdermq nylltereea
      181 nlalqeamsm sqlvtgiglv iivvipfvtl vlfaqvfkkg vrhilarvra ykggefgfhh
      241 vsnrrdelah vdaelanmgr elhhllgead risnqvmdva ngtaiksaeq fkamqaiqlt
      301 tdellsgike qsdhttsisa tteevsasaq diyeaiayms ekmraldqts qeglvtvksl
      361 edhmeelank tvqtatdmtt mqkqmqemts flagidsiad qtnlvainas ieaakagsfg
      421 nsfavvanei rklskqasdf sdqtkqtlsa llvetteave gfnkfseqtt vmkehtskts
      481 slfrtilden mevtrsqmes keavndinha legvvgdigk ladsatvlle ksgkvrvivh
      541 dqterqqala nevgsleeta gmlkkhkkra nsmqas
//
LOCUS       WP_176010077             103 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176010077
VERSION     WP_176010077.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 103)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..103
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11989
     Region          11..100
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(28,31)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mkkiesieql ekikqeenav flftagwcpd ctfiepflpe leekhsdkaf ysinrdefie
       61 vcqdmdifgi psfvvfkdgk evdrfvskdr ktkeeidsfl lqa
//
LOCUS       WP_176010112             269 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Paenalkalicoccus suaedae].
ACCESSION   WP_176010112
VERSION     WP_176010112.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..269
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30844
     Region          10..246
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
ORIGIN      
        1 mfrfettdkk pkgvfvvvhg ageyharyrf vveklnefgy hvimgdlpgq gttqgprghi
       61 tsfqqyidti rlwlsearqf klpvvllghs mgglastrtl mqlsekelpd avvlsspcfg
      121 lynktplnkr alvkilnkva pgtlfptnle agsgtrdkwm ndrdasdelm ikkvsvrwyr
      181 eltssinyvh entelfpevp lyimqggtdk ivdkysvkdw fnqvdvldkh ykewpnlyhe
      241 vlneperhlv fahmmgfvtt qlafrregf
//
LOCUS       WP_176010134             549 aa            linear   BCT 11-JAN-2025
DEFINITION  PucR family transcriptional regulator [Paenalkalicoccus suaedae].
ACCESSION   WP_176010134
VERSION     WP_176010134.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..549
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=62669
     Region          6..125
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          226..535
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 mtvaaeilqa pifehakvra gtsflaqnyi ewisvmelpv enfvrenefv lttgigchgd
       61 yvlleqfvrd vidsgasmlg iatgrfifti pdsiltlane hefiiveipw evrfgdaiqa
      121 vlhvinhqkr sereeserir rqfinivlqt tdvqaicell hdhtslspii idnketvrah
      181 iksnppvlsv ndlplaeses pisdhplypy iesynyqdtv ystiqieash rklgyiwfph
      241 psstlswfhl tilehaltac alffvqedav etaeirlkdt fllelargiv tedstlsska
      301 qklgydlnlt ylcivgdihl rkkvgdfpsf kqdspttssl qnvnyyiqre vanaaqflsk
      361 rvmvtfdege viiyletdhh llaesanqfl dtvdrrlnel ltevglnwgi aakrdsfkqs
      421 yveakaaldi glrssvertf ykdtrikrll ltmldkpevf dvmedtiqpl ldydakrqtd
      481 lvhtfmmynk hngnvsqtar elhlhrqsll yrlrnieslt qlslvdaddv fllelcirls
      541 mlkngvdhd
//
LOCUS       WP_176010158             191 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter small permease [Paenalkalicoccus suaedae].
ACCESSION   WP_176010158
VERSION     WP_176010158.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..191
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=21372
     Region          19..183
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mpttqnetkq kgpfagvvkv vkvldaalht vekfilswam imiafltagn visreltgvs
       61 wffsaelsrl alivasfigi syaarkgrhi smsaffdmap kkpkkflaif nplltatilf
      121 vvayyaalyt idvyesgrtt aalrfpfwlm vvaipigcfl gglqylrnmw mnikhkevyl
      181 aqdkkdyteq l
//
LOCUS       WP_176010230             341 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar-binding transcriptional regulator [Paenalkalicoccus suaedae].
ACCESSION   WP_176010230
VERSION     WP_176010230.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   de Sanctis,D., McVey,C.E., Enguita,F.J. and Carrondo,M.A.
  TITLE     Crystal structure of the full-length sorbitol operon regulator SorC
            from Klebsiella pneumoniae: structural evidence for a novel
            transcriptional regulation mechanism
  JOURNAL   J Mol Biol 387 (3), 759-770 (2009)
   PUBMED   19232357
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..341
                     /product="sugar-binding transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37400
     Region          25..339
                     /region_name="DeoR"
                     /note="DNA-binding transcriptional regulator LsrR, DeoR
                     family [Transcription]; COG2390"
                     /db_xref="CDD:441955"
ORIGIN      
        1 mnmlldlqkk llpdlvevlg lrfrilryir lmqpigrrtl atnlemserv lrsevtflks
       61 qglvefatsg mtlteegqnl lsqlevvmke vfntrsmeee lqaklgvkev hvvpgdsdqf
      121 pwvkkemgrt cvnvikrnla mqgniiavtg gttiaavaem lvpdsdlkes lfvpargglg
      181 eqvenqanti catmarkamg tyrllhvpdq vskdayeslv lepsiqsilk lihsatmvih
      241 gigeaqtmad rrdteedvla klkekeavae afgyyfnksg eivhkvptig lhlndlesin
      301 tiiavaggas kaeaiqayli kspsqvlitd egaakeilak l
//
LOCUS       WP_176010280             229 aa            linear   BCT 11-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Paenalkalicoccus
            suaedae].
ACCESSION   WP_176010280
VERSION     WP_176010280.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..229
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=25420
     Region          128..223
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mrfsvrdvlk tmiisltwii llsiptiiil advthalefs lsiisiivls tvilsinkym
       61 lrknglswea lgfrrlnkqq liklawqipl lwflmvatqv lflmiyfgnd mqnlsspqng
      121 taslnitift ffaaliaiaf vtpiieeiif rggilealsn kfsvpiaili ssilfvlahp
      181 itlimpgliv aglslgylyq kynsiyapll hhmfintinv lavssaalv
//
LOCUS       WP_176010275             157 aa            linear   BCT 11-JAN-2025
DEFINITION  single-stranded DNA-binding protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176010275
VERSION     WP_176010275.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Bianco,P.R.
  TITLE     The tale of SSB
  JOURNAL   Prog Biophys Mol Biol 127, 111-118 (2017)
   PUBMED   27838363
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..157
                     /product="single-stranded DNA-binding protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=17407
     Region          1..102
                     /region_name="Ssb"
                     /note="Single-stranded DNA-binding protein [Replication,
                     recombination and repair]; COG0629"
                     /db_xref="CDD:440394"
ORIGIN      
        1 mnqfafvgri vrtpdlmktk dgthftryal avrrpfkntk gqydtdfihi vswnklaerv
       61 atyctkgsmv svtgriqmrq lelgqerqyt ipdiigetvs flklnresvp aisapvppet
      121 qpkppasevv esdvmsdplk qapisekidv saiatae
//
LOCUS       WP_176010305             508 aa            linear   BCT 11-JAN-2025
DEFINITION  RHS repeat domain-containing protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176010305
VERSION     WP_176010305.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..508
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=57664
     Region          <27..414
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mdymydesgg ikkaflklna esfstyydyn pvgqpsrirq enkhgdvvsd eqltfdengh
       61 itevrslsga rvtyeydndy qlrkekhrna agaitldqsy eydflgnrls kivgaartty
      121 tydkanhllq qgsltythdh vgnttsrgdt nfvyntdrel tevkragati atydynhhgm
      181 rtkkvagsrt ehyyytgkdl ayitdaqnri rssfvrdalg qlmtytdhtg aspktylyvl
      241 nhrgdvlglr deggimvvty tydaygtiig qtgngltgdg rllreanpfr yasyvydeet
      301 slyyvqtryy dadtgrfltr divadtnlyi yadnnpvnfv dpdgrvpipl iiflakagfk
      361 aytaystyka ikndpsmkni llslmpggki trmggkkila fakgnkgvvk aadkklfrrf
      421 dyhfekhvlg khggkkefrn itrqqylnra ldlatsrtns dvvrrtlsgg reatyrhstk
      481 elvivhngkd igtffkpdkg fkyfqnlk
//
LOCUS       WP_176010324             537 aa            linear   BCT 11-JAN-2025
DEFINITION  PucR family transcriptional regulator [Paenalkalicoccus suaedae].
ACCESSION   WP_176010324
VERSION     WP_176010324.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Beier,L., Nygaard,P., Jarmer,H. and Saxild,H.H.
  TITLE     Transcription analysis of the Bacillus subtilis PucR regulon and
            identification of a cis-acting sequence required for PucR-regulated
            expression of genes involved in purine catabolism
  JOURNAL   J Bacteriol 184 (12), 3232-3241 (2002)
   PUBMED   12029039
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20581820
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..537
                     /product="PucR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006144 - purine nucleobase metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=62131
     Region          7..126
                     /region_name="PucR"
                     /note="Purine catabolism regulatory protein-like family;
                     pfam07905"
                     /db_xref="CDD:462312"
     Region          222..530
                     /region_name="CdaR"
                     /note="Sugar diacid utilization regulator CdaR
                     [Transcription, Signal transduction mechanisms]; COG3835"
                     /db_xref="CDD:443046"
ORIGIN      
        1 maitveqamk ieglnechir agykgisklv khvtimevpd ivqwlkgeel mltslysiyd
       61 dekaqgelik qlhekgtsal aikphrfiad ipeiilkean kydfpiieip keipyidils
      121 pvmkriysnr dvlyedlqga yqlmnetsln rggiqrlqqi lsdfikhdvf iesfvpyvgi
      181 segqeslapl etwkkdeleh mqrptsverv drttgeavsc ivapividnv lygtitsvds
      241 delqidvala ilerastlla lefmrkkvth eleqqyksdf fydlffsqiq seslmvekgq
      301 lygfdlnkky lcmaiqfrfd kqgglkpiah tvdqlelics qrekdaiigs fkngvyvlyp
      361 tagkkvdrih qeitllyrel drivqatfym gigrpyfeig nlresldqae rsvvlgrtff
      421 eekrlvfyed lgvyrlfaei knteemhqff getvnalvey drdhdlelme tlrvyfthne
      481 slnqtskalf ihvntlkyrl qriklltgls vqssedklml hlglkvfdfi kndyryq
//
LOCUS       WP_176010355             306 aa            linear   BCT 11-JAN-2025
DEFINITION  ROK family protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176010355
VERSION     WP_176010355.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..306
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=32929
     Region          8..290
                     /region_name="ASKHA_NBD_ROK_FnNanK-like"
                     /note="nucleotide-binding domain (NBD) of Fusobacterium
                     nucleatum N-acetylmannosamine kinase and similar proteins;
                     cd24068"
                     /db_xref="CDD:466918"
ORIGIN      
        1 mnvltkpyia fdiggtnvkw gllskegell qhdlfsskdg dsetilagmr kilrevdvag
       61 iavsmpgfih adtgyiefgg aivgfhhfpl kdtleaefgi pvtvendvnc valaekwkgn
      121 aqdltdfvci tvgtgiggam ylnndlyrgh ayrggevgfi itadrpgtrp ldnclsmigs
      181 mrglllnyak lrgttlenvt geacfadydn gdpevialvd dfysnltkgl fnigailnpq
      241 killgggits rgaflgemrk hladmndmkl diplelcsfg ntagmigalh yhlqqvpvap
      301 ekklsl
//
LOCUS       WP_176010391             671 aa            linear   BCT 11-JAN-2025
DEFINITION  beta-galactosidase [Paenalkalicoccus suaedae].
ACCESSION   WP_176010391
VERSION     WP_176010391.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 671)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 671)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 671)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448998
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..671
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=76728
     Region          1..617
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
ORIGIN      
        1 mfigvdyype qwprerwetd lklmkelgin virisefgwt lmepeegtyd fslyddaikl
       61 itsygmkvvl gtptatppaw liqkypevlp adengvtigf garrhytvns ktyhllskri
      121 veamakhygd hpdvigwqtd neygheksdr sysevdqeaf qewllqkygs leelnhrwgt
      181 vfwsqtydnw sqipvprkvy qehnpsllld fnrfcadayt aynrmqvetl rehiredqfi
      241 thnfvytgla qdqkaiaedl dfisfdnypv wgglaepikp aaiarqhdlc rgtkngkgyw
      301 vmeelsgaqg wsqigylprp ghlklwtyqa iargaeaivy frwraarfgt eqfchgildh
      361 dgvprrkyke vkdvidslkr rgddliaadf paevgfyhdp endwawqiqp qsdqfdfiqe
      421 flrfyepaha lqvqgniird dvdlsaykvi vvpiyfltkk gfnekleqfa rqggtvifsy
      481 rtgvkdqdnv vsektlpgel snmcgievhe ydslrgsrsa tvkgtaaple glsaessvwc
      541 dfiepteaev latyeddewf sgraaitrny vgrgqvyyig tgvdrsmllp lyeaifkeag
      601 iettdtpepv emvtrvgddv tyvtvlnhsv eesfdvklpa gkwidasnge etfegtltlk
      661 plqsiiless n
//
LOCUS       WP_176010402             243 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Paenalkalicoccus
            suaedae].
ACCESSION   WP_176010402
VERSION     WP_176010402.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..243
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26344
     Region          2..243
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mllelffifl illagsfiqg vsgfgfglla msflpllftv kdstllvvsl alivstsiav
       61 qlykhikwra llvmlaaafv grigaffils nygelpimrd flgaflilvv iylffgkglt
      121 ryvprvtapl aitlgalggf vggiyavggp ffvfllmlmf kddkyaysan lqvtfvftnt
      181 itvllhalng dftsswllyf avgvvtvlig trlgvacfty vsqentkria gvivaiaain
      241 fll
//
LOCUS       WP_176010430             530 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paenalkalicoccus suaedae].
ACCESSION   WP_176010430
VERSION     WP_176010430.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 530)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007556
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..530
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57031
     Region          1..530
                     /region_name="NodJ"
                     /note="Putative exporter of oligosaccharides and
                     polyketide antibiotics DrrB/NodJ, ABC-2 family
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG3559"
                     /db_xref="CDD:442780"
ORIGIN      
        1 mnayvantwq ltkfflktvk lrafiwilsi itltvatpls fvglydseae inamaqtmen
       61 pamiamlgpa dlnnytigvm tahqmllfta vavgamsill ttfltradee dgrmellhal
      121 sigraaplva amivmiainv ilgittaagl yalqietmgl egsllyglal tgtglvftgi
      181 taifaqvsen trgtsgmafa vlltsylvra vtdisnpdls wasplgwvsk aeayaannwl
      241 pfilmvclfl lassasfvfy vrrdlgrgmi asrsgksygs allrnplgli irlqrtsfti
      301 wilvlfvtga sygsvlgdld affaeneafs qmlaaegsls lieafmpmli ivlvllsaip
      361 timsfnrlrg eekkerldll larplarvkl ilsfilvaal taffmmsaaa lglyttgnav
      421 vegglalsti ygatlayypa mlvliglsal lvgvlpkata fiwaflaytf vvaylgdifq
      481 lpdwagyatp fsfvgdvple svstltlili stvalllasv gmwrfkerdi
//
LOCUS       WP_176010460             308 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Paenalkalicoccus
            suaedae].
ACCESSION   WP_176010460
VERSION     WP_176010460.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..308
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=34741
     Region          109..305
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mtgaflvgas vilfligmmy lldfraqkkl wkrkvttwft atgkrksaiv llgdrfdqsk
       61 yakkmeaklr kanigltpse fygmlivgam altlvianvl gsslllslvi agallwvmqi
      121 ilfslrknky qdqlnqqlae icrmlsnatr sgmtiqqgid lvaremnypa seefarvsqe
      181 mrlgvdfdra liklqdrvds rdfklfiatl qiqkraggnl sevleemsmt leerkilqqt
      241 iktmtaeqky iawilplmpi fivfvmntiv dgflepiftl vggilvtifl vctiatffli
      301 rkvtdirv
//
LOCUS       WP_176010493             594 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Paenalkalicoccus suaedae].
ACCESSION   WP_176010493
VERSION     WP_176010493.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 594)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 594)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 594)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 594)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..594
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=67834
     Region          141..579
                     /region_name="YesM"
                     /note="Sensor histidine kinase YesM [Signal transduction
                     mechanisms]; COG2972"
                     /db_xref="CDD:442211"
ORIGIN      
        1 mktmkqklre qslfwklfvl tvvivvsvtl attyqtirma eslfidtfsi tnekvlnqit
       61 gtldsynysv irtsnqlqns vnmrnmlsqa qsnsdmmnvy ydlynrleav kttldpyevt
      121 lrvtgvngvt lstgrplwed teqslqlqgm ienrreeprr mhydyiesen epreqlivas
      181 tqimdritgv iygavyltir eedfrefysr ftspgndvfm ldqsgiivss nrteligtqs
      241 iellqhvrgm ngadyvnaef lgeehiivqe eipafdmhiv ntidrsvvte gvidrsriif
      301 tsgaialvai liiyifsrrw tgalsrlvtq igdtskyefd qkvsvvgtye tkqiglafnh
      361 mldelhayvd qlvttqkqkr naeleslqqq inphflyntl tsvkfmisqg skeeaaatit
      421 slisllqnti anvnemntvn qeidnlkhyv finhrryger vtvnyfiadd ckeipvpklf
      481 lqpfvenaff hgfnekksgt invmvwkean klfaevmdng dgmvlqkdsa fpekrqkrqq
      541 fsgvgirnvh eriqliygds fgvqltsepq egtrvrielg vlegqdqqqs ppap
//
LOCUS       WP_176010534             573 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Paenalkalicoccus suaedae].
ACCESSION   WP_176010534
VERSION     WP_176010534.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 573)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 573)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 573)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 573)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459466
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..573
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=65808
     Region          133..565
                     /region_name="YesM"
                     /note="Sensor histidine kinase YesM [Signal transduction
                     mechanisms]; COG2972"
                     /db_xref="CDD:442211"
ORIGIN      
        1 mpqttslkek vrkafmrytl ipllivavav saffyfnssq ilirqteeag qalaadlsem
       61 hesyaqfiee taqsaividy ldfmqgessl fqafyefntq qiiqsdfflf dkneslvlsn
      121 aidvdqlapd ladyfltskr lldrqespvi nrvnqipyhn grlssylyga qivdeneekg
      181 yvfyllheed fltllfqhpv nlsvitdpyd tiiatsnnsv rdflnkyrpd veegmnvqir
      241 dndfvqakeq ipgsalsvyt lnpvqqysst laiitgfflv lslfifivlr vlssklsdkl
      301 tesinnmtes inqfkigsnd yylkssdeee mnvlagqfnd mldeikqlir ekeelskrqr
      361 eseikhlelq fnphfvfnvl esirysilie pknaeksila lskllrysvq ksdqevllvd
      421 elnqlqhyid lhqlrfedsl hyvvevdpml qlhqhvillp rlliqplven aikhadpkge
      481 alqihvqmrl kqnqllctvi dngktctfek vdlltkelqd ensseiglgl ynvhrriqll
      541 fpdnkgldva vnngglrvsf emplilther svg
//
LOCUS       WP_176010548             402 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paenalkalicoccus suaedae].
ACCESSION   WP_176010548
VERSION     WP_176010548.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..402
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43149
     Region          7..387
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(16..17,20..21,24,56,106..107,109..111,114,134,
                     137..138,141,222,225..226,229..231,234,258,262,315..316,
                     320,324,340,343..344,347..348,351)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mnwkapflll vgvgisniga wvyllalnil vftmtgspfa vavlymlipl aslatdvwag
       61 sfidrlnkrt mmigldvvra glilcvafvd slvviyvlvf linmassife stslvymtkl
      121 vpgenrqrfn slrnfiqssg fiigpsvagi lfvvsspeta ivvnavallv safiiillpd
      181 ldprkedevf ervtfavvke dlrtvlafgr sngyvtwvyv lfgmfgvfla gidslevafa
      241 tsvllfsesa ygflvgiagl gmvvgslvna gfaarlrvsv lmgvgavvtp vgylvfafae
      301 sflvaaigff vltfamtfah vgfltfyqar ipveilgrft nlvgmieavg aivvvfgvgv
      361 laewlgirav yvgssvafla lgvyvcrvvi gvreeervrv sa
//
LOCUS       WP_176010581             214 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar transferase [Paenalkalicoccus suaedae].
ACCESSION   WP_176010581
VERSION     WP_176010581.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..214
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=24483
     Region          <9..193
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mertkgglyr rffkrpmdiv lsslaiivls pvllivavlv rtklgspilf kqqrpglnek
       61 ifmmykfrtm tderdelgql radhvrltkf grilratsld elpelfnilk gdmsiigprp
      121 llvqylslyn dhqkrrhevr pglsglaqis grnaisweek fdldviyvks vsliedwkii
      181 cltikkvlvr egissqttvt mepfkgnlke rigs
//
LOCUS       WP_176010565             375 aa            linear   BCT 11-JAN-2025
DEFINITION  S-layer homology domain-containing protein [Paenalkalicoccus
            suaedae].
ACCESSION   WP_176010565
VERSION     WP_176010565.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Gerbino,E., Carasi,P., Mobili,P., Serradell,M.A. and
            Gomez-Zavaglia,A.
  TITLE     Role of S-layer proteins in bacteria
  JOURNAL   World J Microbiol Biotechnol 31 (12), 1877-1887 (2015)
   PUBMED   26410425
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Mesnage,S., Fontaine,T., Mignot,T., Delepierre,M., Mock,M. and
            Fouet,A.
  TITLE     Bacterial SLH domain proteins are non-covalently anchored to the
            cell surface via a conserved mechanism involving wall
            polysaccharide pyruvylation
  JOURNAL   EMBO J 19 (17), 4473-4484 (2000)
   PUBMED   10970841
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Engelhardt,H. and Peters,J.
  TITLE     Structural research on surface layers: a focus on stability,
            surface layer homology domains, and surface layer-cell wall
            interactions
  JOURNAL   J Struct Biol 124 (2-3), 276-302 (1998)
   PUBMED   10049812
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Lupas,A.
  TITLE     A circular permutation event in the evolution of the SLH domain?
  JOURNAL   Mol Microbiol 20 (4), 897-898 (1996)
   PUBMED   8793886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10448992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..375
                     /product="S-layer homology domain-containing protein"
                     /GO_component="GO:0030115 - S-layer [Evidence IEA]"
                     /calculated_mol_wt=41281
     Region          26..66
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
     Region          84..125
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
     Region          149..191
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
ORIGIN      
        1 mrkvwsimlf vvmmvgmatn vaasgftdvr dtwyetevna laskgviagt sattfspgqd
       61 vtrgqfaafv araldlpfgg rnnfndidat npfyielnel gqagimtgdq qgnsnwnspi
      121 trveataiid rmlqvegikt dsykkplffr dnhaipawan esvgnmvgle ivagmpdgsf
      181 sgnvkvsrat aavllyrafe vidsgegnte dsvggvrylg psvqhgtvhm dffarklvsg
      241 dwkesvyntg alvyvpevgy dhvsgrfdls sdeantlvfe nwigfdygad kqlrvelyly
      301 kredlfsgcg egdcfvydgv ltspyatvnl naqdrvefdv seeefdlvdf rvvltsnrni
      361 ldgirdvnmr fsfkd
//
LOCUS       WP_176010589             373 aa            linear   BCT 11-JAN-2025
DEFINITION  S-layer homology domain-containing protein [Paenalkalicoccus
            suaedae].
ACCESSION   WP_176010589
VERSION     WP_176010589.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Gerbino,E., Carasi,P., Mobili,P., Serradell,M.A. and
            Gomez-Zavaglia,A.
  TITLE     Role of S-layer proteins in bacteria
  JOURNAL   World J Microbiol Biotechnol 31 (12), 1877-1887 (2015)
   PUBMED   26410425
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Mesnage,S., Fontaine,T., Mignot,T., Delepierre,M., Mock,M. and
            Fouet,A.
  TITLE     Bacterial SLH domain proteins are non-covalently anchored to the
            cell surface via a conserved mechanism involving wall
            polysaccharide pyruvylation
  JOURNAL   EMBO J 19 (17), 4473-4484 (2000)
   PUBMED   10970841
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Engelhardt,H. and Peters,J.
  TITLE     Structural research on surface layers: a focus on stability,
            surface layer homology domains, and surface layer-cell wall
            interactions
  JOURNAL   J Struct Biol 124 (2-3), 276-302 (1998)
   PUBMED   10049812
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Lupas,A.
  TITLE     A circular permutation event in the evolution of the SLH domain?
  JOURNAL   Mol Microbiol 20 (4), 897-898 (1996)
   PUBMED   8793886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10448992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..373
                     /product="S-layer homology domain-containing protein"
                     /GO_component="GO:0030115 - S-layer [Evidence IEA]"
                     /calculated_mol_wt=39119
     Region          27..67
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
     Region          87..128
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
     Region          154..189
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
ORIGIN      
        1 mktamrllla svlilslfat pasaanfsdm kqgdfghsev talveksiig gmpngtfapr
       61 anvsradtai mftralgltr tssnnpfrdt draayyfnda maavdagift gdalqrfnpr
      121 dtltreqmas vivraynlqp tstqvslndl navhqahidd vrtlaqngit agrangnydp
      181 kapvtrvefa ifldrtikqn pdvgaptptp eqpgtpeqpa ptpdpedptn pedpvdgpep
      241 tppgggggap apsepsvita aslttangtt itgsvsngtt vrfnlsnlpd sttfrsgtis
      301 vteaatlttf dgpvadldvt qqlkagennl tvaevlgnaq iqlgtirlfg dftlpgtlts
      361 ngqttnvqvi fqf
//
LOCUS       WP_176010651             244 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Paenalkalicoccus
            suaedae].
ACCESSION   WP_176010651
VERSION     WP_176010651.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..244
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=28857
     Region          20..225
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mmyqsvidtt ffhsiihrnd relveqafie rcyerehtiy hegddgesmf ivksgsvkil
       61 resdsqeiil ghqlpgetfg eleifhydkk rtasvrtled tvvwsttrer lqpilekypk
      121 lynriiyvls erlvqanrki dylaflnarv rvanllmdmy ynfkgtkkgi pfinrkithq
      181 yvadmigisr esasrvltel qqkkiidvrq kliyidnyaq lkqmarsskh eedeariwhr
      241 sytv
//
LOCUS       WP_176010685             182 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Paenalkalicoccus suaedae].
ACCESSION   WP_176010685
VERSION     WP_176010685.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..182
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21077
     Region          2..169
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtdeelitla lddnedalks lheryfdviy nyvylqtrnh hdteevvqdc fckmafnlhs
       61 fdnkstfktw ffticrhtll dfhrkkkkks aapttglytn iasnsrsaed eafrhkspvi
      121 daiyvlkkdy qdvlllrfvq dlslaetaev igksvfavks lqkravkkll tivnervedy
      181 ge
//
LOCUS       WP_176010693             285 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Paenalkalicoccus
            suaedae].
ACCESSION   WP_176010693
VERSION     WP_176010693.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..285
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31727
     Region          12..284
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 msqfdqglck hrikasyhef rakekviady imehpekiih ssisqvadnl nvaeatvfrf
       61 ckrigfkgyq amkialasev vndvkdihek ihedddeksi aekvfksnir tledtlsvmd
      121 adkmkqavdi lcnaqriefy gnggsgviaq dahhkfirtg ipsaaysdsh lqmmsasqlt
      181 skdavvlish sganrdilqt levaqehgvp tigitslaks plseqvdval ftlseeteyr
      241 sealasrlaq lslidalyvn vsirkkeqmq esvtkmrqai srtrm
//
LOCUS       WP_176010694             507 aa            linear   BCT 11-JAN-2025
DEFINITION  gluconokinase [Paenalkalicoccus suaedae].
ACCESSION   WP_176010694
VERSION     WP_176010694.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..507
                     /product="gluconokinase"
                     /EC_number="2.7.1.12"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046316 - gluconokinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /GO_process="GO:0046177 - D-gluconate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=54881
     Region          5..494
                     /region_name="ASKHA_NBD_FGGY_GntK"
                     /note="nucleotide-binding domain (NBD) of gluconate kinase
                     (GntK) and similar proteins; cd07770"
                     /db_xref="CDD:466790"
ORIGIN      
        1 mskqyvmgld igttsakavi ftkhgdvvse aevgyatlhp apgwceqdpl eieaaaieai
       61 htamtrsaid keaiisvgls samhslicvd aantplspsi twadgrsaal adelratdig
      121 eriylatgtp lhpmspllkl lwmqenkyep ylkaakflsi kefltsrwfg edavdysias
      181 atglfniytr qwheealsla sirenqlsrp vpathlftgl dvdiaeqmrl dpntpfvagg
      241 sdgplanlgi gainpgetai tigtsgairq msaaphtdsr qevfcyaftd dlwvlggptn
      301 nggnvlewlk ntighaelta aletqqdpfd vlidaanqva pgadqllflp ylngeraphw
      361 dasargafig lcsthtshhm araglegvly ailsvaesle altgetekly anggfarsei
      421 wvqmladmfg revhlpvshq ssawgaawvs lyavgevtdl raikqsipmk gvvvpdmekh
      481 evyrkmfevf remygvvggs vrklqrv
//
LOCUS       WP_176010767             148 aa            linear   BCT 11-JAN-2025
DEFINITION  nucleoside deaminase [Paenalkalicoccus suaedae].
ACCESSION   WP_176010767
VERSION     WP_176010767.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..148
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16319
     Region          1..>102
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mkheelvkrc vklaernvrd gqapfaaivt rggevvseav ndgkatfdpt ahgeiraiqm
       61 agtklettdl sdcelytnce pcpmclaaih wsgikqvyyg lsigqqaefd empqelyeaf
      121 rtgehsvklh dysgkvdgaa pfrleere
//
LOCUS       WP_176010780             690 aa            linear   BCT 11-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Paenalkalicoccus
            suaedae].
ACCESSION   WP_176010780
VERSION     WP_176010780.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..690
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=76679
     Region          1..622
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 mnprrnkhkr rlrlwtipif filtcallag gvvfyayqme applqvaqtt tlyaqdaspi
       61 gefehseqry wipidemgta iqeatlaved rrfyshpgld pvritraiit nlqtgrkseg
      121 astitqqyar nlylyhdktw erklheafya lrlelhyske eilegylnti yyghgvygiq
      181 aaadayfskp aqeltyaeaa mlagipkgps vyspfideea arerqrivla sltaagftsp
      241 eeertyvnes lsftqkdrak tfaphfkdav raelmragid eevinrgglk iyttldvemq
      301 ehaealvqeq lteanveval taqdprtgav vamiggkdyd esafnravqa rrhsgstmkp
      361 flyyaalehg lhpnsmlkse ettfvydegr eeykpsnfnh qyandyitml qalalsdniy
      421 amkthfllgf drlgetaref gitselratp slalgtaevg vlemgnayap fanggsrvap
      481 qlvtqvdaad gttilevspr keevlnpayt ammtnmmqgm fepslnasya svtgasisea
      541 ldrpvagksg stladswmig ftpqllttvw tgyddgssle rgdsqyakkl waefmkrsld
      601 aelklafhvp envhevdinp angllasdsc pvsrttlfyn gteptdlcts hladasgave
      661 eageslphqh eggrerswlg rltewtqded
//
LOCUS       WP_176010824             123 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF423 domain-containing protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176010824
VERSION     WP_176010824.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..123
                     /product="DUF423 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=12584
     Region          1..121
                     /region_name="YgdD"
                     /note="Uncharacterized membrane protein YgdD,
                     TMEM256/DUF423 family [Function unknown]; COG2363"
                     /db_xref="CDD:441930"
ORIGIN      
        1 mklflvlggi lgflfvsiga fgahalaarl estgyaaqfq tgvqyhmiha iaivgvailm
       61 nhlpstgllt gagwsffigi ilfsgslyal sltgirvlga itpigglafl vgwvlivaaa
      121 iid
//
LOCUS       WP_176010590             684 aa            linear   BCT 11-JAN-2025
DEFINITION  S-layer homology domain-containing protein [Paenalkalicoccus
            suaedae].
ACCESSION   WP_176010590
VERSION     WP_176010590.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Gerbino,E., Carasi,P., Mobili,P., Serradell,M.A. and
            Gomez-Zavaglia,A.
  TITLE     Role of S-layer proteins in bacteria
  JOURNAL   World J Microbiol Biotechnol 31 (12), 1877-1887 (2015)
   PUBMED   26410425
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Mesnage,S., Fontaine,T., Mignot,T., Delepierre,M., Mock,M. and
            Fouet,A.
  TITLE     Bacterial SLH domain proteins are non-covalently anchored to the
            cell surface via a conserved mechanism involving wall
            polysaccharide pyruvylation
  JOURNAL   EMBO J 19 (17), 4473-4484 (2000)
   PUBMED   10970841
REFERENCE   3  (residues 1 to 684)
  AUTHORS   Engelhardt,H. and Peters,J.
  TITLE     Structural research on surface layers: a focus on stability,
            surface layer homology domains, and surface layer-cell wall
            interactions
  JOURNAL   J Struct Biol 124 (2-3), 276-302 (1998)
   PUBMED   10049812
REFERENCE   4  (residues 1 to 684)
  AUTHORS   Lupas,A.
  TITLE     A circular permutation event in the evolution of the SLH domain?
  JOURNAL   Mol Microbiol 20 (4), 897-898 (1996)
   PUBMED   8793886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10448992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..684
                     /product="S-layer homology domain-containing protein"
                     /GO_component="GO:0030115 - S-layer [Evidence IEA]"
                     /calculated_mol_wt=74239
     Region          499..540
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
     Region          560..601
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
     Region          627..669
                     /region_name="SLH"
                     /note="S-layer homology domain; pfam00395"
                     /db_xref="CDD:459798"
ORIGIN      
        1 mkkypiskka iavaivttma itpfatlapl agdsstayas evevaevrse vrelagkvtt
       61 iystfradts tngvqsritf dairdnvrdt dlaewqeivn atngeileld gdagellfsa
      121 rfvqglaeif tnsnptslee dledfiaefe dgftnvfpdi siadlfvian qleaefrlnk
      181 pfatdlsrnn iraylearvn avaarndnel qamldilsdy gitrdgvasm fielrdtvap
      241 adnqtfsntr mqqlaitlfr aaqafeeqpp vvqppggggg vppvdpedpe epetpiddee
      301 vtvpddttse ervtdpvtgq vtvittvnae qlaalldgee fdrvsfnltp adgeyavlrl
      361 sddvldvira anpdaiieva tlegsfaipv aeldytsvdi svnevdfdas enqvtpvapv
      421 veflvvatin gqeveitrfn apvertitan ddlsnnsvvv rlntngtitg vatkrdgdta
      481 tftgftnsly tvvensvsys dvpsslwsse vinklstqyi lrgfssgdfr ptgtasraef
      541 aaiisrglsl tggstymgqf tdivgnewfm gdlvavtdyd lirgyenntf rgnnevtrqe
      601 aatiivrame llgydfdlde svsytdfsds advapyares vtilsqagli egrpgnnfap
      661 ranisrqeva alverflvka dfld
//
LOCUS       WP_176010886             194 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Paenalkalicoccus suaedae].
ACCESSION   WP_176010886
VERSION     WP_176010886.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..194
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21651
     Region          2..194
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mlyvtanpkp lhqsnslqig qafletytsl hpgekieqld lfdvtvptme gqalaawerg
       61 gsvtvtnplv eqllthdklv lvtplwnmgi papmkayvdq ivvpnktfrf aekgmegllg
      121 elkvlhiqsr ggiysegkla afehgdsylr tifklvgvkh yehlfiegts typeqveeml
      181 kekvkeakvl aerf
//
LOCUS       WP_176010889             264 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paenalkalicoccus suaedae].
ACCESSION   WP_176010889
VERSION     WP_176010889.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..264
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29128
     Region          21..254
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mskrvlqmim llllivlfvl pvgfmfiksf tfslrwpsli pdtftlrawa viwqdpqlts
       61 alqttliigv svvvlnmila tpaayvlshf yfrgkavvet iillpllipv laiamgmhla
      121 mirvgladsi mgvilihllp tlpysvrvlk agfdrisptw ieqgavlgvn gwksfitgil
      181 pmmlpslrtm avltfvisls qyvltaiigg grvatlpliy ypyfsstnea vvagfsvlfa
      241 llpivflllm eatmllymrv lrra
//
LOCUS       WP_176010898             178 aa            linear   BCT 11-JAN-2025
DEFINITION  PadR family transcriptional regulator [Paenalkalicoccus suaedae].
ACCESSION   WP_176010898
VERSION     WP_176010898.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447737
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..178
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20498
     Region          3..81
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
ORIGIN      
        1 myeliilstl mtgqahgysi aqtinsiigp iakasngriy pllaklekqg fvknvvkqin
       61 grqqkvftlt ptgkerffal mldtesnpke yqelfsfkvt vfdllqqekr lqltehyvey
      121 ceahiehlkk gveasssylf gedkpsylnk vmthrinqwq vekewaltik kqleedlq
//
LOCUS       WP_176010928             245 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Paenalkalicoccus suaedae].
ACCESSION   WP_176010928
VERSION     WP_176010928.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..245
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28585
     Region          1..207
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mqpsygkpkq siresiykmm rdkiltmele pgrklsekew sqklevsrtp vreaflklse
       61 eglldivpqs gsvvaridla iveegrfvre qletaivrea chslppefar kieenlllqd
      121 fnhvedprtm ftldeafhql lflaskkgrs wemskqmntq ferirmlrlr sesldwgnlv
      181 edhkeifrli lekdeiaaae rmkqhlrlvd fekgaimsey pnyfithieg aegkseydsk
      241 vvwps
//
LOCUS       WP_176010982             375 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Paenalkalicoccus suaedae].
ACCESSION   WP_176010982
VERSION     WP_176010982.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10893456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..375
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=41793
     Region          8..104
                     /region_name="RHOD"
                     /note="Rhodanese Homology Domain (RHOD); an alpha beta
                     fold domain found duplicated in the rhodanese protein. The
                     cysteine containing enzymatically active version of the
                     domain is also found in the Cdc25 class of protein
                     phosphatases and a variety of proteins...; cl00125"
                     /db_xref="CDD:444705"
     Site            73
                     /site_type="active"
                     /note="active site residue [active]"
                     /db_xref="CDD:238089"
     Region          120..295
                     /region_name="POD-like_MBL-fold"
                     /note="ETHE1 (PDO type I), persulfide dioxygenase A (PDOA,
                     PDO type II) and related proteins; MBL-fold
                     metallo-hydrolase domain; cd07724"
                     /db_xref="CDD:293810"
     Site            order(172,176,232,250,253,257..259)
                     /site_type="active"
                     /db_xref="CDD:293810"
ORIGIN      
        1 mtvhtwkaed iakkvinred lfildvrned afadwkiegh nfsymnvpyf dlldgveeil
       61 kdipedkevl vvcakegssi mvaemlsdeg rdaayleggm kswssylepi kvsdltngge
      121 lyqfvrlgkg clsymviseg eaavidavrf advytsfadk kgvtithvfd thlhadhisg
      181 grdiaeatga tyhlppkdae evifeyeplt dethvtigas nidvnalysp ghtigstsfv
      241 idnqylltgd ilfidsigrp dlaglaedwv gdlretlytr yrdlaedliv lpahfmiiee
      301 lnedgtvakr lgdlfaenhg lniedeaefr smvtdnlppq pnayeqirhv nmgklspdhe
      361 eqtemeigpn rcavr
//
LOCUS       WP_176010966             248 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Paenalkalicoccus suaedae].
ACCESSION   WP_176010966
VERSION     WP_176010966.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..248
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28346
     Region          3..105
                     /region_name="HTH_TipAL-Mta"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators TipAL, Mta, and SkgA; cd01106"
                     /db_xref="CDD:133381"
     Site            order(4..6,20,37..39)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133381"
     Site            order(51,54,58..59,68,80,84,90,94,97..98)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133381"
     Region          130..244
                     /region_name="TipAS"
                     /note="TipAS antibiotic-recognition domain; pfam07739"
                     /db_xref="CDD:462248"
ORIGIN      
        1 mglqvkelan ltgisvrtlh hydhigllvp stttdagyrl yadadiaklq qilffraldf
       61 plkeikrila spdystleal dvqrsmlmer raqlnemiet idktirskkg efamsneerf
      121 kgmafkddty eqearerwgd apieeskrrv eslsdaeqqa lgeeweriyr klaevmqtes
      181 pesarsqeai aewfhylnan fgtyskaafa glgemyvade rftknidayg dglavfmaka
      241 mkefgrlr
//
LOCUS       WP_176010387             176 aa            linear   BCT 11-JAN-2025
DEFINITION  NfeD family protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176010387
VERSION     WP_176010387.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Green,J.B., Lower,R.P. and Young,J.P.
  TITLE     The NfeD protein family and its conserved gene neighbours
            throughout prokaryotes: functional implications for stomatin-like
            proteins
  JOURNAL   J Mol Evol 69 (6), 657-667 (2009)
   PUBMED   20012272
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Kuwahara,Y., Ohno,A., Morii,T., Yokoyama,H., Matsui,I., Tochio,H.,
            Shirakawa,M. and Hiroaki,H.
  TITLE     The solution structure of the C-terminal domain of NfeD reveals a
            novel membrane-anchored OB-fold
  JOURNAL   Protein Sci 17 (11), 1915-1924 (2008)
   PUBMED   18687870
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..176
                     /product="NfeD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=18772
     Region          16..163
                     /region_name="YbbJ"
                     /note="Membrane protein implicated in regulation of
                     membrane protease activity [Posttranslational
                     modification, protein turnover, chaperones]; COG1585"
                     /db_xref="CDD:441193"
ORIGIN      
        1 meiagipitt iyltllvvgv altilyifvg evlegildig dgainpvtai gfvtllggag
       61 yilelvlpis sglvlglafi lssilivlvn yfiilpvkrs eknmsfsird ligrvgevyt
      121 svpahgygev iirrthgtis kpaksfddvp lpegtkvliv dideegvflv seyeee
//
LOCUS       WP_176011098             211 aa            linear   BCT 11-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176011098
VERSION     WP_176011098.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..211
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=23490
     Region          24..210
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mkidvpkipa klealsfhdi wededrtlst ceiqqsdfsn etlervrihd avikncqftn
       61 tdfsqidltd vhfqncdfsn vnmarasihr vtfttcklvg cefpesslgn vtfsdcilhl
      121 aafgnsklvk vrfkesslkq adfydctfkk vaydqcqldg anfeqtplng idiststfdt
      181 ltvsladlkg civsshqaiq latlmgvvik d
//
LOCUS       WP_176011105             132 aa            linear   BCT 11-JAN-2025
DEFINITION  HIT family protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176011105
VERSION     WP_176011105.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..132
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=14920
     Region          2..128
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mngcifcqve lvpdqnvvls nehcmflqvd eaqirgvqle gaglivpkvh rettfdltae
       61 ewqgtysllh evkkyidevh qpdgynlgwn cgeeagqhvf hahfhvipry adeplagkgi
      121 rylfkskenn rg
//
LOCUS       WP_176011107             164 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Paenalkalicoccus suaedae].
ACCESSION   WP_176011107
VERSION     WP_176011107.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..164
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19288
     Region          7..162
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mrevlseeel halyedmkgp lysflfryth eeqfsidlvq etfervkkye gnynqekgsm
       61 knylfqvayr llitklnrrk tfrrilpfly tsqektldta dqmtvrdavl alpdkqravi
      121 iltyyhdltq veigsileip vgtvksrlhk atatlkealk edfr
//
LOCUS       WP_176011158             350 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paenalkalicoccus suaedae].
ACCESSION   WP_176011158
VERSION     WP_176011158.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 350)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 350)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 350)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..350
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37825
     Region          5..350
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 mlkgrffgli vpliaitfgf iagaiimlls gnnpitgyva lfqgvfgdty yfgetlqrmt
       61 plifsglava fafragllni gvegqlivgw ftsvyvgftf dlpmiihlpm alaagalaga
      121 lwgfvpgllk arfevheviv timmnyiamh vvnsiirtyf idsaqrteii aptaslasdw
      181 lmqitqfsrl hwgfllaiaa cfvmwfilwk tkrgfelrsv gynknasays gmsvkgniil
      241 smsisgafag vggamlglgt yqyanilpsf tnygfdgiav allgassslg iffsaflfga
      301 lkegannmqa aagiapelve iiiafiiffv assylirwiy srlqskkgak
//
LOCUS       WP_176011174             147 aa            linear   BCT 11-JAN-2025
DEFINITION  GatB/YqeY domain-containing protein [Paenalkalicoccus suaedae].
ACCESSION   WP_176011174
VERSION     WP_176011174.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..147
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=16324
     Region          1..147
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 mhildqlnqd mkdamrkkdk qrlsvirgvk stlqneaink gselsedevl tvlnremkqr
       61 reslhefeqa erqdlvektk aevsilseym paqldeaeld aivaetvtev gatskadmgk
      121 vmgaimpkvk gradgtavkk rveqals
//
LOCUS       WP_176011411             165 aa            linear   BCT 11-JAN-2025
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Paracoccus
            saliphilus].
ACCESSION   WP_176011411
VERSION     WP_176011411.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus saliphilus
  ORGANISM  Paracoccus saliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Paracoccus saliphilus"
                     /db_xref="taxon:405559"
     Protein         1..165
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=19063
     Region          32..159
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mtstpsseer iplsklnfpk fhyrsnerlv gkfpedrllf vydgvcvlcs ggakmvakrd
       61 kfdrvrfvsg qselgkeffk hyglpsteft aqlviadgea ftgfdgfaet irrlpiswlh
      121 lgrllrylpf kekiyswlar nryrvfgrrs ncmippvelk krfia
//
LOCUS       WP_176011294             415 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paenalkalicoccus suaedae].
ACCESSION   WP_176011294
VERSION     WP_176011294.1
KEYWORDS    RefSeq.
SOURCE      Paenalkalicoccus suaedae
  ORGANISM  Paenalkalicoccus suaedae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Paenalkalicoccus.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Paenalkalicoccus suaedae"
                     /db_xref="taxon:2592382"
     Protein         1..415
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44696
     Region          12..394
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(22..23,26..27,30,62,117..118,120..122,125,145,
                     148..149,152,228,231..232,235..237,240,264,268,320..321,
                     325,329,345,348..349,352..353,356)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mtqqsifknr tfifimvagf laimgytmff mtttwfvisd lgsseslgiv liaitvprlg
       61 mmvfggvlad rfkkstimfs tslsqgimll aiyllsstds mtmtyllvfg mlfgtldacs
      121 gpagasllpk vvatsqiqqa nafyqgaaqi gvivgpilag avmeasgvta syliativvl
      181 lsaffmfppf lkegdventi kqtpfkdlre gfsyikssaf lttgilvlit lnffafgaiq
      241 igipilvdlh ggspinlsyi evslgigmll ssgligsiki krrgvtsivg lvatlavava
      301 fsqvpnlyil tglaffigfs mtfvyipffs saqektdari mgrvmsvifl amngfdplay
      361 agvtlfvsng yniqhimlaf altglviami iswrgksyrq dysdvqenev erkal
//
LOCUS       WP_176011434             366 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paracoccus saliphilus].
ACCESSION   WP_176011434
VERSION     WP_176011434.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus saliphilus
  ORGANISM  Paracoccus saliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 366)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Paracoccus saliphilus"
                     /db_xref="taxon:405559"
     Protein         1..366
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40101
     Region          1..366
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 miecrdvqky ygdyhalrgi dlsiregeff sllgpsgcgk ttllrviagf edissgavli
       61 dgkhmedvpa nrrptnmvfq syaifphlsv aenvafglrr dprsktekta mvdealemvg
      121 lkgygaraah alsggqrqrv alaralilkp kvllldepls aldrkmreqm qveliklqrq
      181 vgitfvlvth dqeealvmsd riavmfegei aqldepemly arpasrrvad figvmnflpa
      241 rvlnepgdga tvdvpglgvv dlpegqisra daddsgpmvg frpetmtllg pgqssqqare
      301 tgavidevvy ygdmtyydlr ldgsarldgk artvrismrn vfgrdvpcvg tavrlawspg
      361 slvlfr
//
LOCUS       WP_176011478             174 aa            linear   BCT 11-JAN-2025
DEFINITION  SH3 domain-containing protein [Paracoccus saliphilus].
ACCESSION   WP_176011478
VERSION     WP_176011478.1
KEYWORDS    RefSeq.
SOURCE      Paracoccus saliphilus
  ORGANISM  Paracoccus saliphilus
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodobacterales; Paracoccaceae; Paracoccus.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459669
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Paracoccus saliphilus"
                     /db_xref="taxon:405559"
     Protein         1..174
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17942
     Region          113..>174
                     /region_name="YgiM"
                     /note="Uncharacterized conserved protein YgiM, contains
                     N-terminal SH3 domain, DUF1202 family [General function
                     prediction only]; COG3103"
                     /db_xref="CDD:442337"
ORIGIN      
        1 mffllvttla viliglsvyg tgnlrtenqp seteqaasqe sgiatdllpd lskapesnga
       61 dgappadlvq aaaqtpervq kfpgpelrps peyagetpdq aappadaegp ilyitgsrvn
      121 frsgpstgdr vigalnggaa vealgpndgd wvhirdmdgr igymsgqfls pdap
//
LOCUS       WP_176011570             741 aa            linear   BCT 11-JAN-2025
DEFINITION  right-handed parallel beta-helix repeat-containing protein
            [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176011570
VERSION     WP_176011570.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Burnim,A.A., Dufault-Thompson,K. and Jiang,X.
  TITLE     The three-sided right-handed beta-helix is a versatile fold for
            glycan interactions
  JOURNAL   Glycobiology 34 (7) (2024)
   PUBMED   38767844
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12131601
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..741
                     /product="right-handed parallel beta-helix
                     repeat-containing protein"
                     /calculated_mol_wt=83154
     Region          521..689
                     /region_name="Beta_helix"
                     /note="Right handed beta helix region; pfam13229"
                     /db_xref="CDD:463811"
ORIGIN      
        1 mrintrtsdr ewqcvwriaa gvlsagkryr valslrvlea aedsllqvlv rqpdrpdlvr
       61 ydtklplehl efsvevpadg tgyqlqlhar kqilaqidri eitemencei eypipaapve
      121 pfagelaglp tgapefeiel pcpggaaatv raadfgvspa aadnvaalnr alaycretga
      181 arlelspgiy rftsddfihl erlkdftlag ngatlvwhkk tgdlihvdec erirladfqv
      241 dwdwetdpla sfvrveavna aagwvdlhfi dydefprrdv rvadleeldp gtmsvgveng
      301 lnagfewtrg vspafgkrwl sgnllrvnla gqpgfldrlr vgqlfrmrha vydmngivlw
      361 qnrhltlenv tvhsapghaf liggkqqywq flrthvrppr egrrrpvtst adhchvansr
      421 gyfkmigcef tlggddclnv hdnsafvtrh serevklwrd gmleefqigd pielrhadya
      481 ptgfraplag trrdetgayl vfdrelpaqp tdgfvafnwk ydtanilird cffhdnrarg
      541 llllgrnitv encrfvhnqm gaikietgyt fnlwsegyga rnivvrgnsf dtvnpsgtay
      601 ggkerdiyig vylkqdptle rtnypiirdi lfennrfsds fglvayvssa anvtfrgnsf
      661 rnptsrrrnq pyraaifaay adgvtvvnnr weaspwvepr llcdpettrn illagnavvp
      721 avpgenasit adepswqtel q
//
LOCUS       WP_176011636             205 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176011636
VERSION     WP_176011636.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..205
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22157
     Region          25..182
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mktpsspanr frkvvwpgst qlapvppvlv acagpdggrp nlltiawtgi lcsrppmlsi
       61 avrperysyp lleasgefsv nlptpqlaka vdwcgvvsgr dhdkfresgl tplpasriqa
      121 pivaecvval ecrivqkltp gihhlflaei vavqvsehli asdgklqidr dgllayahgh
      181 yyelgrclgh fgfsvrrkag plirq
//
LOCUS       WP_176011618             418 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176011618
VERSION     WP_176011618.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..418
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46207
     Region          152..417
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mkkvvsvlic cfclcwagig engrnaaaag aaaaaelpva anddgrparv taangfvqld
       61 ltkqedvkwf frhktelarf gvgfvlsvla vfvfnfligr lvrfccnrsg nndllvrliv
      121 rglfwpiglc vfatgmrysf eqltfvdpen ilaakisgff vvlsviwalf slgnsmcryg
      181 etraraknnm mgfllitmvr rginvisfai lllfilkdvl dininailas agvaglaiaf
      241 aaqstianff gsvmilidhp ftvgdrvkin avdgvveavg frstrirsld gnlytlpnst
      301 vadavvenvt erpfikyafd iglvystsaa qmrkacalld eifkrhpgfy tekhppvirf
      361 tefrdwslni avvvwydpad wgqflierea vnleilerfn aeklefafps ttnylqqg
//
LOCUS       WP_176011650             352 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176011650
VERSION     WP_176011650.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..352
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40062
     Region          2..251
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mknkikvglw glgragwnmh ceeiakfnde felvagcdll pdrcrefeer yrrpaypaeq
       61 aflndseiel vsiatysqdh vkdtrlaleh gklvflekpv alsvaegeel rrldrqypnr
      121 lfirqnrrfe aafqhvleim rrgilgnvye iklcrhnfmr rddwqtlvnc gggqlnnwgp
      181 hlidhglrfl espcveihsd lkliaacgda edhlkillkg angrvidiei sggvaipgdv
      241 yqvygtrgtl vsrdekelvl kyldpavtlp alrphagspa rnsgygnpge lkwleetipt
      301 rpsngydmsd iyhylylalr enqpfpvtle ealevvrvta evkrqsaver mr
//
LOCUS       WP_176011684             472 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176011684
VERSION     WP_176011684.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..472
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52246
     Region          55..463
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mktptvicsl iggillfggc ytpppagrli eetsfqaavv rsgdlklldg istltladak
       61 rialannpty qaaffavrsa kmryyqamga yspalsgafa igdqlydgrd ngssqqdtvf
      121 ytfttvqasw vvfdglaref qllaarhgvk mqehlsenag rlllqavsla yddiriaqaq
      181 qriaradadf qqeqyrqaei rhrvgevsrs dvlnfagrlk qaemqivkar nryelglyal
      241 avllgypegt fspqlqfapl erevkpplpi dvlldsalqq rpdlnavren lavlkyqlyr
      301 syssfsptms vftnysyssn stqnsgnnpt gfgnfyeagn sfnygglasw nlfegfgryn
      361 ksreakaeld qayltgtnew lkavqeirda ysscvhnrkl aelaaagrdi mreqrdlvvk
      421 eyqvgevdiv rlnaaqenyv vsenelaeal vnahrakvql eaaaaldmap rp
//
LOCUS       WP_176011808             450 aa            linear   BCT 11-JAN-2025
DEFINITION  ADP-ribosylglycohydrolase family protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176011808
VERSION     WP_176011808.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..450
                     /product="ADP-ribosylglycohydrolase family protein"
                     /calculated_mol_wt=50063
     Region          100..413
                     /region_name="DraG"
                     /note="ADP-ribosylglycohydrolase [Posttranslational
                     modification, protein turnover, chaperones]; COG1397"
                     /db_xref="CDD:441007"
ORIGIN      
        1 mlptiqhlrs ilqnviaqry kqgydtaglq nelrklpesy dalaafaekl eslprrndfg
       61 yeqpetlaei faacppnftr qrigrrlsga eaaararsaf lgavagcilg kpvecdptle
      121 elrkalestg dwplrdyfsl rtldalgrrh dsaatccret iryveldddm nyivtglrml
      181 elhgldftrc hlakywlenl plyctfgper kflldaglnw nwspdapvne etidrmrrrw
      241 vandeacgaa irvdsygyac pglpalaael awrdaslthr ftgvyasmyi aaavaaapvl
      301 ddpmaifeya iscvpqqsyf aevmrdafdl vgkaadyleg yagihakyge yrhcalyqec
      361 allintakfa rnteeaicmq vsqgcdtdcf gkiagsimgg ffgpgslper wiavfnddfr
      421 vcppefters lskvadriaa lpaltldlpc
//
LOCUS       WP_176011795             252 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176011795
VERSION     WP_176011795.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..252
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26771
     Region          17..209
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mvkdgeksll kllqlleavg sapegigsre laaelgmpps slfrmlkflt atgyaakngr
       61 lytlgigvqr lgwraevqnp lrtlalpalq rlaretletv hlakldggrm iyvakveger
      121 alrmrslvgr ssplhctgig kavlaflped drqrrlnsle lnaytpatlt sgaalrqela
      181 eircrgyavd deeheegvyc vaapvlnrng gvvaavsvag aalylrgrtv elaglvgaaa
      241 rdigkaidgt ad
//
LOCUS       WP_176011812             355 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176011812
VERSION     WP_176011812.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..355
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=39392
     Region          1..354
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 maklkagvig lgmgwghlag yashpdvevv avadrieakr eaakkefnlp kiyaegidmi
       61 rqekldilsv avpnnqhkel tvagleagah vlcekpmamn taeaeemlaa akkhnlklgi
      121 dfsyrfspqs ramktlvedg rlgeiyyars vwlrrrgvpg fvagfntqga sgswffdksq
      181 sgggplidlg vhrldlalwl mgypepdwvm gstycklape makyynqnyt vedlacamik
      241 fkngatleld aswaaniken eqmstrllgd kgglyqynln egytydveyy qeidrkqfdc
      301 tlhppvpevk safhmfvdav rddkpflvqp eegvcvmrll daiyksaatg qpvqc
//
LOCUS       WP_176011842             444 aa            linear   BCT 11-JAN-2025
DEFINITION  phenylacetate--CoA ligase family protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176011842
VERSION     WP_176011842.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Luengo,J.M., Garcia,J.L. and Olivera,E.R.
  TITLE     The phenylacetyl-CoA catabolon: a complex catabolic unit with broad
            biotechnological applications
  JOURNAL   Mol Microbiol 39 (6), 1434-1442 (2001)
   PUBMED   11260461
REFERENCE   2  (residues 1 to 444)
  AUTHORS   El-Said Mohamed,M.
  TITLE     Biochemical and molecular characterization of
            phenylacetate-coenzyme A ligase, an enzyme catalyzing the first
            step in aerobic metabolism of phenylacetic acid in Azoarcus evansii
  JOURNAL   J Bacteriol 182 (2), 286-294 (2000)
   PUBMED   10629172
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Ferrandez,A., Minambres,B., Garcia,B., Olivera,E.R., Luengo,J.M.,
            Garcia,J.L. and Diaz,E.
  TITLE     Catabolism of phenylacetic acid in Escherichia coli.
            Characterization of a new aerobic hybrid pathway
  JOURNAL   J Biol Chem 273 (40), 25974-25986 (1998)
   PUBMED   9748275
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..444
                     /product="phenylacetate--CoA ligase family protein"
                     /EC_number="6.2.1.30"
                     /GO_function="GO:0047475 - phenylacetate-CoA ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0010124 - phenylacetate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=49832
     Region          11..438
                     /region_name="PaaK"
                     /note="Phenylacetate-coenzyme A ligase PaaK,
                     adenylate-forming domain family [Coenzyme transport and
                     metabolism]; COG1541"
                     /db_xref="CDD:441150"
ORIGIN      
        1 mselvienrl wnpaaetmpp ediralqlak lkktvdyaas hvefyrreyr arhlsaasiq
       61 slddlrrfpf ttkqdlrdny pfgffavpka qlarihassg ttgkptfvgy thndlelwse
      121 lcarfltagg ltsdqvaqia fgyglftggf glhygiekvg aaivpassgn tqrqimllkd
      181 vgintlictp syalniaeti eriglkpadf alrfahfgge qwteamrrni eealhihafn
      241 nyglseiigp gvsgecaarq gmhiqedhfl veclnpetle pvpdgeegel vitalskeac
      301 piiryrtrdl ariypghdcp cgrttrrmsr ikgrtddmmi irgvnvfpsq leeallrvgg
      361 taphyliely rpnnldeavl kvemreqefs dkmdemqrlr dridreissi tgikfrielv
      421 apnsiersvg kakrvadhrn lkve
//
LOCUS       WP_176011866             448 aa            linear   BCT 11-JAN-2025
DEFINITION  flippase [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176011866
VERSION     WP_176011866.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..448
                     /product="flippase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50505
     Region          30..418
                     /region_name="MATE_Wzx_like"
                     /note="Wzx, a subfamily of the multidrug and toxic
                     compound extrusion (MATE)-like proteins; cd13128"
                     /db_xref="CDD:240533"
ORIGIN      
        1 mwrgvqlkek vvafftrllr qvgfrqygvn llwlfaekfl rmavgfsvgt yvarqlgtte
       61 fgvlsyslsy caiwgvmcgl glepvvvrel vlrpaardri lgsawllkfa awlpaflivg
      121 ilmavskqdw etkslilllm ggycsqtllv ldsyfqakve sryvaiaqmt allamsavrl
      181 llawnncpvi cfaaaevgnm vltqagycff yyrrvrqwsw scrwgemgyl lrqtwplwva
      241 atagisamri dqvmlknmlg dsevgcymaa vrlveifyfv gialsgtlfp pilqakrdsi
      301 dgyqrrlkgf fsllfylnlg lvlgmaclgh laiglygaay aasypifmiy iwrilfcamg
      361 vggsnyylse nlqhysmwfs lvvmglnvlf nyiligrfgv lgaaatavlt nliavyllpl
      421 ssrttrrlav lqlaaldprw lwrwrtqr
//
LOCUS       WP_176011856             292 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176011856
VERSION     WP_176011856.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 292)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..292
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33478
     Region          23..285
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          <170..>285
                     /region_name="AdaA"
                     /note="Methylphosphotriester-DNA--protein-cysteine
                     methyltransferase (N-terminal fragment of Ada), contains
                     Zn-binding and two AraC-type DNA-binding domains
                     [Replication, recombination and repair]; COG2169"
                     /db_xref="CDD:441772"
ORIGIN      
        1 mpivfdaval nadwpvriia sdrqddrpid flhahslpel gycyegagif midnrmipyq
       61 agdvslidar qlhlaqslpn scsrwdwiyv dlpklfcrlt rqtalsnfhf cwradfpgil
      121 pasrypaisr rlrqiavgmq eehryrwekt iaefcllmid lqalfpsspe tpsrqispel
      181 lerlspalhy lnghyhenfq vsdlarlcnl sethfrrlfr rftgasplgy qrqlqlagil
      241 aqladrnrsi geiafgsgfn slssfnrlfk aavgcsprew rqrnacdvny cl
//
LOCUS       WP_176011918             335 aa            linear   BCT 11-JAN-2025
DEFINITION  ROK family protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176011918
VERSION     WP_176011918.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..335
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=36665
     Region          93..323
                     /region_name="ASKHA_ATPase_ROK"
                     /note="ATPase-like domain of the ROK (Repressor, ORF,
                     Kinase) domain family; cd23763"
                     /db_xref="CDD:466849"
ORIGIN      
        1 mrkinnsqvr gnntnlirqf llsgavhtke slaaatglsa atcrnilmem lqtaeveala
       61 pgrpaggrpp cryrynagfv swllcriknv ptgkqleilv adaagkvvar resgllavla
      121 pdillefivd aakdfshvga iavsypgvvl dgktscwgdi eelngfdlkk lieehtripv
      181 liendinlaa egylirhpee nirdlvyigf ppqnlpgcgl iaeghllhgt rgfageilyi
      241 qdqtreeqwn tmnaphglae mlpavlravt alldpalivv aspdlpasee llrekirkma
      301 hpdflpelri ipdylpdnfa gllnlarnsf yqrgf
//
LOCUS       WP_176011925             251 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176011925
VERSION     WP_176011925.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..251
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=27183
     Region          6..227
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 msdsgekiyl akflsvngaa srrraaelvr agrvavngvt vdnpadpvpp aaevrldgrv
       61 vaplgrrhyv mlnkprgyvc tnedihaark aldlialpgv rlvsagrldk esdglllfsd
      121 dgdfiyrvah pkfeilkvye vatgrplpdr alrrlrggiv dageflqphs lepvgpavyr
      181 vvlnegrkre irrliaaagg kvvrltrlsv ghltlgglpa gcwrelssre veealrpglp
      241 elgrsdrvae s
//
LOCUS       WP_176011933             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176011933
VERSION     WP_176011933.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..359
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39981
     Region          1..359
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 maevilenvw kiyeddgyqa vkgvsldird refmvlvgps gcgksttlrm iagledicrg
       61 tirigdtvvn dippkqrdia mvfqnyalyp hmsvfdnmaf glklrkfpka eiqkrvmeaa
      121 rilglepyld rrpkalsggq rqrvavgrai vrkpkaflfd eplsnldakm rvqmrieisk
      181 lhhqlestmi yvthdqteam tmgdricvmk dgviqqvadp ltlysrpanq fvggfigtpp
      241 mnffngrleq sgerlcfase gmtftlpeaw kdkaakaagp dvvfgirpen lviaddgmaa
      301 vievrelmga etylhlrlgg htfvarvape tgfhagdtvk frfdtakahl feqesgral
//
LOCUS       WP_176012119             241 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176012119
VERSION     WP_176012119.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..241
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=26682
     Region          1..88
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mkkrftliel lvviaiiail asmllpalgk akaqaqkikc lgnvkqlglg tvmyagdnad
       61 ylpigqqhna kgdawlywhn llnpyiggqe mtsmyemeki advmfcpttv srglkedisy
      121 glnlyimhwn gfidpglpet isckmtsvpd pastimmgdn algsplcvwg srqwlyfpee
      181 sirlddggsg qdyiltatrh sngknlawvd ghadyrsfta linkwndgre wwsfkgvtgn
      241 p
//
LOCUS       WP_176012137             866 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176012137
VERSION     WP_176012137.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 866)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 866)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..866
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..866
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=97738
     Region          60..>409
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 melknyqrkv mddlnrflda frstpivaea yrkhwenqgv pvngldgmkp ytnllgevph
       61 vcfkvptggg ktflacnalr pvfdafpftr tkvvvwlvps dailqqtvkn lsnpdhgyrh
      121 kinvdfsnrv evyaksqlla gqnfnpvavq eqlsililsy dsfrsktkeg rkgfqengnl
      181 aqfvrvfgpp dhpidgadet sliqivnqln pvvivdeshh aisdlsieml rnfnpkfvld
      241 ltatpksnsn iisfvdaael kaesmvklpv ivynrpgked vlydaitfrn rleatainer
      301 aatgryirpi vlfqaqprns edsttfekik eglllagipa sqiaiktaek delknvdlls
      361 esteiryiit vnalkegwdc pfayilatia nktsvvdveq ivgrilrqph trqcgnplln
      421 yayvftsssh fsdtvnkvvd glnkagfgkw ecrevetlpt aparqpdmpe qgklslpdee
      481 aadsgfdpea lrkrlavaap ettpaddpia atalaqgeey taaiaatenq svpmevrnrm
      541 khyamrpefa eqaramqipq fhlkqppslf saedsclldk khltkgftlk nkdseidfaq
      601 lqidayavdi tgqgreqqvq rkvlddaerr rfqeylnsqp pesrvrhckg ailqllsryd
      661 evesvelkgy vdriidnlss dqltaletdy tlyarkirek idqlleehre rnffewlnld
      721 kivvkpswtf ptqisplqts pgiagslyss egsmnsletr vadlfsslpn iiwwhrnler
      781 sgfgingfln hypdfivctr ngrilliesk geqlrnddsa akvrlgkswa nasgqqfryl
      841 mvfdqfpldm dgaykfddfs rmmrel
//
LOCUS       WP_176012220              72 aa            linear   BCT 11-JAN-2025
DEFINITION  flavodoxin family protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176012220
VERSION     WP_176012220.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..72
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..72
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=7788
     Region          8..>68
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mkglnrknvl iisstprsgg nsdvlcdefa rgardsgnav ekirpkdlkl hfctgcgvcn
       61 hthkcvqney di
//
LOCUS       WP_176012224             485 aa            linear   BCT 11-JAN-2025
DEFINITION  MATE family efflux transporter [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176012224
VERSION     WP_176012224.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Claxton,D.P., Jagessar,K.L. and Mchaourab,H.S.
  TITLE     Principles of Alternating Access in Multidrug and Toxin Extrusion
            (MATE) Transporters
  JOURNAL   J Mol Biol 433 (16), 166959 (2021)
   PUBMED   33774036
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Kusakizako,T., Miyauchi,H., Ishitani,R. and Nureki,O.
  TITLE     Structural biology of the multidrug and toxic compound extrusion
            superfamily transporters
  JOURNAL   Biochim Biophys Acta Biomembr 1862 (12), 183154 (2020)
   PUBMED   31866287
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Radchenko,M., Symersky,J., Nie,R. and Lu,M.
  TITLE     Structural basis for the blockade of MATE multidrug efflux pumps
  JOURNAL   Nat Commun 6, 7995 (2015)
   PUBMED   26246409
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Kaatz,G.W., DeMarco,C.E. and Seo,S.M.
  TITLE     MepR, a repressor of the Staphylococcus aureus MATE family
            multidrug efflux pump MepA, is a substrate-responsive regulatory
            protein
  JOURNAL   Antimicrob Agents Chemother 50 (4), 1276-1281 (2006)
   PUBMED   16569840
REFERENCE   5  (residues 1 to 485)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..485
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0042910 - xenobiotic transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006855 - xenobiotic transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53436
     Region          16..443
                     /region_name="MATE_MepA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Streptococcus
                     aureus MepA; cd13143"
                     /db_xref="CDD:240548"
ORIGIN      
        1 mttaaiqtte elghdsifkl llkfsipaai snfmfttynv vdrifistal gteafagvgi
       61 tfylfmicia vglmfgiggg tlvslrlgen dqpaaerilg nvimifligg vlttalgflf
      121 lkpllywfga deatypyaaa ymnvllwfma pdflslgvsn liraegspkf smwniaagcl
      181 anivldylfi fvldwgiaga awatgiskll stllmfwhft lspfrlltlr lrnlridwpl
      241 vkamaaigls plilqsiisv inalinqslr ahggtqavaa mtivstviml mmiptfgvim
      301 gyqpivgfny garqfrrvad tlkgafllsi astsvlylpv miftaplval fskddpavvq
      361 lathglrlfv lllplwpifg igsnffqatg rprntiwltl frnvfcfisl vlilphflgl
      421 ngiwltapia dasagavtlw llyrefgklr qleirerret rslrrreppp sadyepelgl
      481 pdlql
//
LOCUS       WP_176012279            1042 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176012279
VERSION     WP_176012279.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..1042
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113380
     Region          1..1028
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 miskvfidrp kfaivisvvm vlagticlfk mpvaeypeva pptivvnasy pgasaqviad
       61 tvaapiesei ngvedliyys sqsdnsgnys lsitfksgid sdmaqvnvqn aiqraepslp
      121 qevkalgvnv ykrsgdilgm laftsengkl sklfmsnyvs mnvkdalari dgvsqaviwg
      181 elnysmrlwl dplrmtalgv thedvknais tqniqaaaga vgteessefm qyklnaegrl
      241 kevgdfeqii vksgsdgrqi rlsdiariel gaetyngtny fngepcvmma lfrnndanav
      301 avidniksem aklaqnfpeg lswhlgydst efvritmeei vvtliltfvl vvaityiflq
      361 dwratlipsi tipvsllgtf iflypmgfsa nvltmfalil vigsvvddai vvvencmrli
      421 eeehlspyea avkgmgqitg aviattlvil aiyapvafyg gmvgtiykqf avtmcialvl
      481 ssvnaltlsp alcaivlrpq kqargpfkwf niglnfsrdg yvslsgilvr rglltailfa
      541 gvlylnyhlf nkvptsflpd edkgaifcdv qlapgstlyr tgqalgkisg iirgidgvkd
      601 mlvisghsmt agsgenvgmv ivvlkdwser ktpelqvkyi qqqimqkcat ipeanvrafl
      661 ppaiiglgat ggvsfalqat gdqtpqelaq avrsligqim atgkavyats sfeantpqle
      721 lvidrakaea lnipvsrifg tlqsqlaayy indfnlngyt fqvkmqadsd yrkninmieq
      781 lnvqtdagqm vplstiaqlk witgprqier fnqfssasmn tqslpsvssg emmntvqqlv
      841 ndtlpkdyqi swtdmsyqeq nnqgqiiylm alalifgylf lvaqyeswtv pisvilsvav
      901 atlgamvall vtdmplsiyc qlglimligl asknailmve fskqereagr tieeaalnga
      961 rtrfravmmt alsfvigvfp mviasgagag srraigvttf wgmvaatavg iffipalyaf
     1021 fqrgrealqr lrgthpdgkt qr
//
LOCUS       WP_176012293             227 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176012293
VERSION     WP_176012293.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..227
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=25773
     Region          8..>64
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mkqqktnftl iellvviaii ailasmllpa lgkakgaaqr iscvsnnkqm glyyafyand
       61 fddwqwackd gsnrqikphw fdvlwelgys geryndvvsc paaehakdhn nsrmistgps
      121 rllirpwkis kipspttfft fgdfafksed vvtsfwgftw rddqsvdvtp gfrhpgntcv
      181 rthgdghvav yrenehtsyd sielypqmwp hydtngniii pssswmp
//
LOCUS       WP_176012295              67 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176012295
VERSION     WP_176012295.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..67
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7627
     Region          1..66
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 meqfvchlkk yrqlagltqe elavlvgvrr etiirleaak ynpslklaid isravrkpie
       61 vifqfes
//
LOCUS       WP_176012302             218 aa            linear   BCT 11-JAN-2025
DEFINITION  HD domain-containing protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176012302
VERSION     WP_176012302.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..218
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24374
     Region          11..216
                     /region_name="RnaY"
                     /note="HD superfamily phosphodieaserase, includes HD
                     domain of RNase Y [Translation, ribosomal structure and
                     biogenesis, General function prediction only]; COG1418"
                     /db_xref="CDD:441028"
ORIGIN      
        1 mmcdvdwvnn faelakqvrr hleeapgchd fdhtqrvlrn aelllpecad advqvvrfas
       61 llhdiarpee lamkgeicha algaklaaql lrrydlpeaf vcavadaveh hryrsssppt
      121 tvearivyda dkldslgatg vgraflfagr vgarlhntse eafdgeaygr edtayreflv
      181 klrylpsqml tapgrrlaae rlkvmeaffe qlnrevyg
//
LOCUS       WP_176012313             284 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD-IIA family hydrolase [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176012313
VERSION     WP_176012313.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428959
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..284
                     /product="HAD-IIA family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31998
     Region          12..283
                     /region_name="NagD"
                     /note="Ribonucleotide monophosphatase NagD, HAD
                     superfamily [Nucleotide transport and metabolism];
                     COG0647"
                     /db_xref="CDD:440412"
ORIGIN      
        1 mkfldfwvkn qeryqallfd idgtliagrh lmpgadqmlr wlrenrypff lltndgnhst
       61 leksmllasn glkiapeeil scadalvevv eerrlhdqkf filgdlgnpc yafraglqpt
      121 relaeldsct gvicgegryd wydhiqavfn ffrrhpdrlf ivpnpdgcwp gapngdfgig
      181 aggvarfias llaemnldip ihylgkpypa iydyalhrlr qkfqlqlndr rrvmmlgdsl
      241 lsdirganws glesgllltg itspelaaaa taefkpnlqf esfi
//
LOCUS       WP_176012361             237 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176012361
VERSION     WP_176012361.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..237
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=26244
     Region          8..>64
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mkkhfsnftl iellvviaii ailasmllpa lgkakqkavg itcvsnlkqn llgaqlyand
       61 nkdlmmayyy dgkieltwsk aldenkyvdr avffcpsvkq ldynngnidw tfrtygvinl
      121 kddltfyndh keewgdfatf gnpswyygfy tfsrmkqptn ipiladtcaa sgahmgegfy
      181 gfypyataen saastnhgst gnvafgdgha aaltigqfrd ldfttlvvdg vvktytn
//
LOCUS       WP_176012385             254 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176012385
VERSION     WP_176012385.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..254
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=28340
     Region          1..95
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mkrniekcrw ssrnftliel lvviaiiail asmllpalgk akaaaqaikc vsnlkqlglg
       61 hafyqndndd wcmpaeftgi npwggegtrv wgwelidnyg faaelyecps sekgivsqdd
      121 llknmanysy glnmnsfgvt swtnvyytph klsdfdrfgn ttnlvwsada tpteivqnat
      181 gtwapsyfls fdrgcyplre lsfyqpnarh nnkvnaaild ghvesipavq ldsvtkywap
      241 yntgdgtllw pswl
//
LOCUS       WP_176012389             252 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176012389
VERSION     WP_176012389.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..252
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=27957
     Region          1..>69
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mmlpvchrsg knftliellv viaiiailas mllpalgrak aaaqsikcvn nlkqfglgna
       61 fyqndhdnwv lpaeiageca kgnncrvwge elignygfgf nsfncpsaes naadadqlli
      121 dgeysygvnr nsfglntwyd gwflphklnd fdafpgavsk lmwagdtlpt svqekvsgsw
      181 apsyfmqldh gvypysgnkf yqivarhgga qkcnavildg hvesihykqv dwvseywapy
      241 nydgkllwpn wl
//
LOCUS       WP_176012413             545 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176012413
VERSION     WP_176012413.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..545
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=61482
     Region          55..465
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mlkdfrvlsg ltiavllagg crsaeeyeae rfskvpqaie kitngkvlpe gtvltlqdcm
       61 rmaiennrdl rvyeqkqkva kekiyaevmg mlpdltvtnd itgrnntpas ssenvtggtg
      121 gtysasqssd rnvnnlkvem alsaldfgls ylnaaqaedy sliedqqlrr akqnlmldvv
      181 rtyyrvaatq daiettnall ekckqveval edlaqnrtls plrlsdeakr fyrlekqlme
      241 yrrnynnaci elralmgylp isdikvdtsl iknmqikelp dinllekial tqrpelyqld
      301 iqtnimvnes rktllmmfpn vkafvdwnns nnsflyhqsw weigavaayn llklpqniyr
      361 yraqreqvne idertlalsi gvmsqvriah aniievkeqf elddkiaqkf amhakmares
      421 ykaggaltql eldrleleaa eaeidrmlsl snyyvayqrl inavgvdnid petvgllekk
      481 iaeaeakeha lserekqaia nvqnsvkdng qvmfkgvvvg entlspemrd rlnalvpqee
      541 adaal
//
LOCUS       WP_176012448             393 aa            linear   BCT 11-JAN-2025
DEFINITION  FtsW/RodA/SpoVE family cell cycle protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176012448
VERSION     WP_176012448.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Ikeda,M., Sato,T., Wachi,M., Jung,H.K., Ishino,F., Kobayashi,Y. and
            Matsuhashi,M.
  TITLE     Structural similarity among Escherichia coli FtsW and RodA proteins
            and Bacillus subtilis SpoVE protein, which function in cell
            division, cell elongation, and spore formation, respectively
  JOURNAL   J Bacteriol 171 (11), 6375-6378 (1989)
   PUBMED   2509435
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002381
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..393
                     /product="FtsW/RodA/SpoVE family cell cycle protein"
                     /EC_number="2.4.99.28"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0015648 - lipid-linked peptidoglycan
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=42993
     Region          24..393
                     /region_name="FtsW"
                     /note="Peptodoglycan polymerase FtsW/RodA/SpoVE [Cell
                     cycle control, cell division, chromosome partitioning];
                     COG0772"
                     /db_xref="CDD:440535"
ORIGIN      
        1 mkirtiqaea pqegalwpav rgylagydwl qiaamlfllg vgltfiwstd qqsgnsffqr
       61 qirwivmgts lwvmaaginy rqwlpiswlg yllalgalmv vllfgvevng avnwfeikpl
      121 glrlqpsefa kpvvivalaa llsnhlfhin kfthfllfgv vfavpfllia kedigtaavl
      181 vpvaagmvfv selrwrtiia ivvtlvvlvg gvvanemlsi kpilpelkky qrerilifld
      241 perdptnygy nqhqsrlavg sgglwgkgvg rgtqnvlgfl prtvsnndfi fsvvaeeigf
      301 agvmaliaaq llliysilrt ayltpdpfgr yigvgvamvf ithgfinmgm sigltpvtgi
      361 plpfisyggs ftmagmaslg lvqsiyrngl ree
//
LOCUS       WP_176012469             148 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176012469
VERSION     WP_176012469.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..148
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=16739
     Region          50..147
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mlaklndnwg vltpwrtvne lqkgfwglld elgdsvnrrl vsypritlde nedstvakfv
       61 lpgykaaeid vsvvgdfltv kaerqceels dnerylhrer acgrfeetvk lpsrvkaaev
      121 sakyadgilt vtlprqeeek pmtikinq
//
LOCUS       WP_176012488             268 aa            linear   BCT 11-JAN-2025
DEFINITION  creatininase family protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176012488
VERSION     WP_176012488.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Yoshimoto,T., Tanaka,N., Kanada,N., Inoue,T., Nakajima,Y.,
            Haratake,M., Nakamura,K.T., Xu,Y. and Ito,K.
  TITLE     Crystal structures of creatininase reveal the substrate binding
            site and provide an insight into the catalytic mechanism
  JOURNAL   J Mol Biol 337 (2), 399-416 (2004)
   PUBMED   15003455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..268
                     /product="creatininase family protein"
                     /EC_number="3.5.2.10"
                     /calculated_mol_wt=29908
     Region          3..246
                     /region_name="ArfB"
                     /note="Creatinine amidohydrolase/Fe(II)-dependent FAPy
                     formamide hydrolase (riboflavin and F420 biosynthesis)
                     [Coenzyme transport and metabolism]; COG1402"
                     /db_xref="CDD:441012"
ORIGIN      
        1 mnwekltare feqgvkdceg vcllpigvle rhgdhlplgq dvitiheqcv raaelepamv
       61 fpfyflgkia egrhlpgtia lkcellipvl enicdeisrn glkkiiicng hggngaflaf
      121 fldmmleksk dymiyntfpy apavearael irakvdghgg evetsmtmdi apelvkeprp
      181 adfglplgrl aafqklrirt tvdwyadhpw hlaadqtpgs aekgrqinra laeyladvir
      241 lvkrddtpie lyrkclaqqq aprcdfpa
//
LOCUS       WP_176012548             236 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphoribosylanthranilate isomerase [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176012548
VERSION     WP_176012548.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785047
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..236
                     /product="phosphoribosylanthranilate isomerase"
                     /EC_number="5.3.1.24"
                     /GO_function="GO:0004640 - phosphoribosylanthranilate
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000162 - tryptophan biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25522
     Region          1..215
                     /region_name="TrpF"
                     /note="Phosphoribosylanthranilate isomerase [Amino acid
                     transport and metabolism]; COG0135"
                     /db_xref="CDD:439905"
ORIGIN      
        1 mrikicgiqn etemaaairc gadvlgfqvg qiyqsksfil pstagrlaae lppyvtpviv
       61 thlsepeaiv dilnksaift vqlhkvtpvq vavlrdllpa nakiiltfyl npgrydwtld
      121 eylslidavn ldafnldlsr vgldtadkvy qweraaefva qcprpvmlsg glnaanvaqa
      181 ietvhpfgvd acnqlkapdq fcdpavchqf vqaarlagma lnpppeipdg kvsnli
//
LOCUS       WP_176012605             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176012605
VERSION     WP_176012605.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33523
     Region          1..57
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          86..284
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(101..102,104..105,108,112,114..120,214..219,
                     225..226,228..229)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mkifhlasvl hnftetaaal gmsqpnvtqq iaqleaelgt plferdgrrl rltpggralq
       61 aecesllaae dqlirqvqya asairhyrlg atmtaggyvl pgflaaysel hprcnlslyi
      121 antdeiadrl kkhqldlalv egpfdrnyff aepwvqdelv aagqpgfaaa efslaeaiaa
      181 grrlilrepg sgtrycfdrf laerglpapd iravqevngf ealkqlvklg fgftvisela
      241 ireelaagtl aaarftegrl lrtmhfiymp henlkfaerf iafcrrrlps ddrvdrrqlr
      301 s
//
LOCUS       WP_176012683             273 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176012683
VERSION     WP_176012683.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..273
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31362
     Region          22..249
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mavnatieew gvdtkesgfv laqelllkkl lsgevaagqa lkesvlakef glnrpsvrea
       61 lsqavgwgva eyvpycgyrv knftlkdmld wnelregiep iaarrlaehr sdlvlerler
      121 lvtlfgeavm nkdrnqsifa dlnfhmeiin scgnsrfasp nnlcyftvlf rltvkvcfel
      181 efrlsqqknn crfpklyspe qfmtynneia ldnhrqildc irrraveeae qvsrrhirdq
      241 vksaheliel cgdaglplns dfelicrrkq lfw
//
LOCUS       WP_176012689             233 aa            linear   BCT 11-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176012689
VERSION     WP_176012689.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..233
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=25597
     Region          3..198
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mlflqlmndg gpvmwlilvc sliamyvfle kwlqfhreqi nvrellkgln nvlkrngfve
       61 aislcdntpg pvarvlsaai layergdedl eraiedanle evpklerhln ilgtvgyiap
      121 llgllgtvlg mmrafqtihd tqsvylnatq lsgsinmali ttaaglavai pcyvahnyll
      181 arvntmtldm ekaestilgf fqyhskndea ltrvsnlsta sennvdllsg eea
//
LOCUS       WP_176012696             417 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176012696
VERSION     WP_176012696.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..417
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47341
     Region          3..361
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 merkitlgvf gggrgaaval carsagfeiv avcdafepll rhaeasinde svvyytdfdr
       61 flehdgmeav lianyatqhv waavkalnag khvmsecmam ftmaeavelv eaveasgrvy
      121 mfaenypfta erlemkrlyd sgemgefryg eaeyihpvtp rvkasltsgp dhwrcwlpvn
      181 fyysthsmgp vmhitgtrpt tvnglaipyd fndpvltgql rksdlaslli crmdngalak
      241 impcaflrdh geryrfccsr gtmemnqgnp elrvhhelfd fdppkpvnlf ykpnfpeefr
      301 llaekcghng gdfftsyffa kairdggrpm idvyqaidmt sigilgyrsa lqggipieip
      361 dfrdrtvreq yrhddwnpdp arrregmpys svlgdielpa ktledfyryr reyreql
//
LOCUS       WP_176012699             254 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176012699
VERSION     WP_176012699.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..254
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=27918
     Region          1..>59
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mktsrnftli ellvviaiia ilasmllpal gkakqaaqii kctnnmkqlg lgillysnda
       61 ddsapiqens wlqewdygrn rkfwmgelia nygvsyaslq cpsntawsdp nangdyepqi
      121 gwvnhlydwg sgaswetnys fnnyglilsk tedkpgiggk lskadspsqv amlleaewpg
      181 glnavtfynn gvsrfgstay trdhggaacl ftaldghvlk skwsngaidl yltplsaywl
      241 ngnwrfgsff yptl
//
LOCUS       WP_176012724             592 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 2 protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176012724
VERSION     WP_176012724.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 592)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..592
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=67234
     Region          24..>574
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mnsiprseyp rpqlvrqdwl nlngtwsyef dpgksgvarg laaskgfagk itvpfcpesk
       61 lsgvghtdfi eamfyhrqlv vpadwsgkri ilhfggvdye cegfidgksv grhfggsvsf
      121 efditgfvtp gqthdlvlkv lddtrsgvqs vgkqsteyhs hacsytrvtg iwqtvwlepv
      181 amaglqrcri tpdvdndsfv ftpqfyaeqr grkmrvkvsa agklvgetvt aaasgvsfav
      241 kvaaphlwsp edpflydisy eltdaagnvl etleayaglr kihiegnrif lnnreiflrl
      301 vldqgyyedg iwtapsddal rrdielsmaa gfngarlhqk vfeerfhywa drlgyltwge
      361 saswgnafgn sshqkpapey wqslfnflae wreiierdyn hpsiiawtpa necwpgndla
      421 lyrrslseiy dvtrqldptr pcnessgyhh aktdlwtvhf yrptakelhe alvpadypvg
      481 rwnaelecey rgqpylndef ggfmfippdr rkfaentwgy ygmsipdede fcrildeeve
      541 tmlnidslsg ycltqltdve qeqngvynyd rtpkvaperl kaifgrqpkr ls
//
LOCUS       WP_176012792             214 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176012792
VERSION     WP_176012792.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Upton,C. and Buckley,J.T.
  TITLE     A new family of lipolytic enzymes?
  JOURNAL   Trends Biochem Sci 20 (5), 178-179 (1995)
   PUBMED   7610479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..214
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=23682
     Region          5..204
                     /region_name="SGNH_hydrolase_like_2"
                     /note="SGNH_hydrolase subfamily. SGNH hydrolases are a
                     diverse family of lipases and esterases. The tertiary fold
                     of the enzyme is substantially different from that of the
                     alpha/beta hydrolase family and unique among all known
                     hydrolases; its active site...; cd01834"
                     /db_xref="CDD:238872"
     Site            order(11,58,87,188,191)
                     /site_type="active"
                     /db_xref="CDD:238872"
     Site            order(11,188,191)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238872"
     Site            order(11,58,87)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238872"
ORIGIN      
        1 mieiivfqgd svtdcgrsye akeanqglgg gypllaagrl lrelpaknlr cynrgisgnr
       61 vvdlyarwki dtlnlkpdfi siligvndiw hefanhngve terfervyre llswtlevlp
      121 svrllliepf alecgavsaa wrpelagkqq vvrklaaefk tlflpaqell naavkeapss
      181 gpeywladgv hptiaghtvl adawcelvkp lcev
//
LOCUS       WP_176012799             435 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA recombination protein RmuC [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176012799
VERSION     WP_176012799.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13487459
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..435
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=49107
     Region          1..>150
                     /region_name="PRK12704"
                     /note="phosphodiesterase; Provisional"
                     /db_xref="CDD:237177"
     Region          91..434
                     /region_name="RmuC"
                     /note="DNA anti-recombination protein (rearrangement
                     mutator) RmuC [Replication, recombination and repair];
                     COG1322"
                     /db_xref="CDD:440933"
ORIGIN      
        1 meiaivilav illvsvgtvf lllrrlaava glesevarlr gvemqaekag aeltelagrn
       61 nalqlevvql kmelqhqqel ardriaflen sekrqqtefa nlanrlleek grqlseqhre
      121 klsqlvtpfk eqlkefreri drvheeelkq gatlltqirq mqetsnkvsa eannlaaaik
      181 gdkkkqgnwg eliierlfes sglergreye aqvsleteng grlqpdfvvy lpndravivd
      241 skvsllayeq fcnaateeer qaalaahhqa vknhiqglrs knyqdllknn tldfvimcip
      301 iepayqlaly pdhtmlyeqs hlnvvltgps tllitlklin qiwrrekenr naaqmavesg
      361 kmfdtfmaml dnlaeldral gaargcydqv lkrinsgnnn ilrqmerirs lgaktsrqls
      421 vkagtllenr desls
//
LOCUS       WP_176012852             247 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176012852
VERSION     WP_176012852.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..247
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=26596
     Region          3..93
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mtkknftlie llvviaiiai lasmllpalg kakakaiaik cvgnlkqvtl gahmyggdnd
       61 drfpansywd nttggalyyp yylssyvggn sddlflqgmq attaevfwcp vtydwmdsta
      121 rkynwgvpvd gkkmcsgpgy gvnwaldsyf sslwfdnayp gkfsavrnps gqlyfiethn
      181 ndiadtdpdy stslkhvatt gsaaydahgq ratgshvdgs vqsfnqgasd asnggllipw
      241 dadcdgi
//
LOCUS       WP_176012855             102 aa            linear   BCT 11-JAN-2025
DEFINITION  putative quinol monooxygenase [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176012855
VERSION     WP_176012855.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..102
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=11122
     Region          2..91
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mihviariev kegkldefla ifkanipnvi aekgchgytp cldvatglpp qvnynagcvt
       61 ilecwesreh laahlatphm irygeavkel vknmeltvvt pa
//
LOCUS       WP_176012860            1982 aa            linear   BCT 11-JAN-2025
DEFINITION  RHS repeat domain-containing protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176012860
VERSION     WP_176012860.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 1982)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1982
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..1982
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=219864
     Region          327..1021
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
     Region          811..1805
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mtdnislrss ssapangaef vpaynslleg fqargfltdr takqdgdtvs qtdlknlrta
       61 lnnmcssfvn wdeiepllng pypnlfnehp mkindgkgfl avpaeynsgk vdlytsdgvn
      121 idnlpileeh lqdicknlnk mqyqkvasqq kreisnhrty hnysgelyvs tvipptpkee
      181 nlsdtadiiy qfgnysipmq ayqggiwdsk vinesteklq sylfhahtvq emlqpdskwl
      241 sigqgatmsf ngspitnypq lqpptttity tvcqmvslky hsksvsipsv dkmldssdnd
      301 ltkpgclpct lrsikeqfdl dgqaaqwplg isngseglka yayytdwtfa gfsgthlsld
      361 tvftpnvqng qatkdgqtvy wkfsrlqrpq garplmywdd wtgstpacak tvnggsytls
      421 lvtndsnqaq kydvkfadev hhvfnaagtf veawqkvkde ilrvsssfpg lstsatnndg
      481 fvndvscplg rtvvnytpae ystmgkliqp lkitsldsyd pngnplglvn rsdrtetdpv
      541 tgitrnrrih evrdgsnlli ekygtmkdpe sgavvhtvyq psapetvyqt ttilprvfee
      601 sgnyyedetr mvgsdsqttr rvyrrypwgd elfqeirdag getersvkqe yytdstvpaa
      661 yhqlryrqea dgswqyfqyd gqgrqakvis pfgnyalpvd esgavlvpdp ahcqvveydy
      721 alldsdeety agdnrprriv rkicgvevgr syalyftnea hdivcraaga awnaagnlvt
      781 krfssvsgdf agrhwktefp dgqlelttye avagggrret vvqgianaak tavtdgirtv
      841 ttfdgnddvi rrqrfdivsg lalsdetytl dhlgrvsrvd yldgsfevte ygccgpvslt
      901 drdgvvtnyg ytpdkrrdwe srdglitfyt ynadgrvltt tvrkavgvel vtansynaag
      961 elvsvtqpdg avtgyaesrv ngnrtvtttd atggtriety nrdgspasvs gtavhpvrye
     1021 ygvendelft keirlgenda agewmkqyrn fngqvyktlh adgreelvef dawnrpvkqt
     1081 gadgvvtltv ynakgevfrq gidldgdggl slsgsdrite ivnevatkng dtvrrqtvkv
     1141 yptansnavq tvsireqsvd glrqwntvyg rttqtamtrn gsgrvttvtt npdgststev
     1201 klngrilsvn hsvlglttyg ydnfnriasa thtengvsrv lsytydaagr vltetetagt
     1261 ssrmttksyd aqgrvssetr pggrtveydy fatgelkavs gaetypqsys ydrqgriktl
     1321 ttyrnhpaqp evttwhyhaa sgqlisktya dgsavsyqyn sqgrlskrtw argvetsyty
     1381 neagelgsvs ysdgtagvsy sydrqgrrst itdaagtrnf qynldhtlas eeipyisnnt
     1441 lltrnydaqg rnsemklsag ttgyiqatya yddmsrlsqv safgqtavys rvsganrlas
     1501 tvfqagsatv ftalrsydnf nrltsvggyg yvyddrdqra rltlpdsqnw nytydqlgqv
     1561 tggvkktaag tavsgqnyay afdtignrqt mtangtatay tandvnqyta igsvtpsydq
     1621 dgnlltgynd wmlewngenc lkaiynastk lefdydyngr rfskkvyaks ggnwvlskes
     1681 lfvydnfkqi aeftvsggak tlaksyvwqp etsgdfdvpl wqkvdgnvyt cvvdgnknvr
     1741 rllntagtev anydydpfgs vtasgtasag nafrfssefl deetglvyyn yryysptlgr
     1801 wisrdfinel vfirqeyvyn esinlllkrk sffpdylflc nntindidfl gldrwineaf
     1861 hvsvsvdvws ddctqkigve siefgpdhgn igipipllgt vseleiiakg fwvrglvtit
     1921 egeaigvdil yletcciddk alatwareql vdarmgdlky nmyayncyhf afdavmimgf
     1981 gi
//
LOCUS       WP_176012867             590 aa            linear   BCT 11-JAN-2025
DEFINITION  RHS repeat domain-containing protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176012867
VERSION     WP_176012867.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..590
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=65693
     Region          <8..372
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mseyiqvtya ydgmsrlsqv sasgqtaays rvsganrlas tvfqagtalv ftasrnydhf
       61 nrlttiggys yvyndqdqrt rltlpdsrnw nytydelgqv tggekrtaag vavtgqnyay
      121 afdtignrqt mtangtatay tandvnqyta igsvtpsydq dgnlltgynd wtlewngenr
      181 lkaiynastk lefdydyngr rfskkvyaks ggnwvlskes lfvydnfkqi aeftvsggak
      241 tlaksyvwqp etsgdfdvpl wqkvdgnvyt cvvdgnknvr rllntagtev anydydpfgg
      301 vtasgtasag npfrfssefl deetglvyyn yryysptlgr wisrdpigek gglnlygfir
      361 nsiplltdkq glkvaegccg vdvtaklvrl mqnvekviai pgvfdkvckk nniydpnygw
      421 diveffeagq ainpntfscn kkkeghecek tvtylggchk vfainyllwg vanracklds
      481 qdaldavpsy rvvsigrtda seneswiqgt nsrynwavvg ikgeyhkppe atsknctpct
      541 qkyvgtltar lrfsatqhif itsdtlynrp emhlidtstd ypprerfgek
//
LOCUS       WP_176012875             875 aa            linear   BCT 11-JAN-2025
DEFINITION  beta-N-acetylhexosaminidase [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176012875
VERSION     WP_176012875.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 875)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 875)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 875)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 875)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 875)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 875)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..875
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..875
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=99322
     Region          358..870
                     /region_name="Chb"
                     /note="N-acetyl-beta-hexosaminidase [Carbohydrate
                     transport and metabolism]; COG3525"
                     /db_xref="CDD:442747"
ORIGIN      
        1 mkfwsalmmm avtwsamafd dfenypdsga mrqvyrefda nnpypdrlel gerdgnhfml
       61 menrdrnysv vfrevvlpeg erhsairfrv rggndqgtpq tfnvvlrprn gmpdsvgqti
      121 eltdawqtvt vgdlelaeld rfilvfglhk qpgeamfvev ddlefaedpa wqwvqedrkr
      181 llddygaysd aaalrqkylt reteaaapvl dlttydnraa lqldsgpeam eticlreyan
      241 pfgaaaagve idvadvsrqp esglvyvavr atpdgpdlgr vkidelprgf etyrvlapgl
      301 gkldkfflvl qtarrdreey aemkylndfc gvpsvpvstk igypvsaafa sprlmlkeqm
      361 vniipavkel eigdglfqll pksaivlsdg seaarpvaeq lrallapstg ftlpivdpvr
      421 gasyprrivl tlapeqagtt gkegyeleva adtirltaae naglfyamqs lrqlfrpeie
      481 srqfryldwv ipqvkivdrp eytwrsvhfd tarhffpkey lfrlidllal qklntfhwhy
      541 ndgtawrves dafpkltevg awwgdsaggf ytkedvkaiv dyarerfitv vpevempaha
      601 naalyaypdn acqkeqlleg khgdantasw flrpywvaty casreetydf idrliaetve
      661 lfpdskiihi ggdelpsgaw eacprckafm qekgfageve lqnyftrrve eivarhgrra
      721 lgweqvmadn lrpdtmihay lsqemvaraa aagyevfsnn agcnyfdyyq gsqadeplai
      781 tsgmttvkqt ytfdpmarvp eelrskvlgg qgalwtefis tpaqadymff prmtamsekv
      841 wsapercgwq eferrlnffy prlsqfdvhy kdyrk
//
LOCUS       WP_176012925             221 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176012925
VERSION     WP_176012925.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..221
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=24597
     Region          7..>66
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mkrlqlftli ellvviaiia ilasmllpal skakaaavri kctsqqkqig lgliiygsdn
       61 redlpscnsy nyryakvtae erfldlvcgr vfydrgetgd hddcnliepa llycpgngga
      121 irsggdlpyn qisyitfhgs aydlysplkl tddpgmllla dlvvkdeqll ganwesylnh
      181 gglgsnalyl dghvewhnrg elkvgfdpyd hywaiperrk r
//
LOCUS       WP_176012938             305 aa            linear   BCT 11-JAN-2025
DEFINITION  AEC family transporter [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176012938
VERSION     WP_176012938.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..305
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33162
     Region          4..305
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mdlmlnvfla ivetflafgl galamryqfl qpgdlprlgr ltldlmfplm vfssitrnfd
       61 psrlndlwlm pvlgfalmaf galagfglrr gmrgrtparl atfhhfcavn nyvflplivl
      121 dkiwgehyvs llllmnvgst igfwtigvlt lggsglsqsi knifsinlla vaaalfvsfl
      181 glpiptvlan tarsigdasv pvmllligaa iynsagkifh ykfdvfylsa vrlvllplli
      241 vlalkllplp revyevtfvv almpvssssv litqryggct dfagqaivvt tvlslfsipl
      301 mlnll
//
LOCUS       WP_176013038             110 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176013038
VERSION     WP_176013038.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..110
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=12254
     Region          17..>97
                     /region_name="AF2118"
                     /note="Predicted transcriptional regulator, contains an
                     XRE-type HTH domain (archaeal members contain CBS pair)
                     [Transcription]; COG3620"
                     /db_xref="CDD:442838"
ORIGIN      
        1 mtedkynpvp hdhekfmkkv msteegrqay aeaqrefail dalreaiaes gltqvelarr
       61 mgtrqsnisr llngsvipgw ktvnkvfrat graivkietk piadtpvtsr
//
LOCUS       WP_176013092             135 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176013092
VERSION     WP_176013092.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10545315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..135
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14364
     Region          52..124
                     /region_name="Cupin_2"
                     /note="Cupin domain; pfam07883"
                     /db_xref="CDD:462300"
ORIGIN      
        1 mtttlflsgd gqthrkmttp chggegewyf rdllaplaas evlfikfihd diippgstfg
       61 ahchggdagg peeewyycls grgvmmldgr ehemtagdla vcyaggchgl rntgseamri
      121 ivicaspcrt agqea
//
LOCUS       WP_176013099             246 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176013099
VERSION     WP_176013099.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..246
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=26701
     Region          1..90
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mkrrrnftli ellvviaiia ilasmllpal skakaaaqsi kcvanlkqig lgcfmyaddh
       61 qdwalavypi tgnawipwlk tlrddyvtsp ealqcplapk dcfekeketg eiangqhyla
      121 qnatyglnid sfgyrmgddn pwfqkthkfa efanggasgl nmigdtpava eiidgfhsdq
      181 glmctanggi mptiadggwy plylrhgsrl nvlkadghae qlnsgqadee rawlprsgsp
      241 ggalvf
//
LOCUS       WP_176013183             238 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176013183
VERSION     WP_176013183.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..238
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=26766
     Region          1..>61
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mkrkqftlie llvviaiiai lasmllpalg rakaaaqaik clsnlkqigt gimlyandyd
       61 dcivpyqdag dfpdlwpayl crdygfseel fscpsastsn twgwdesnln ssktywitdw
      121 sedvnkgngy gapqfcsyai svltmasnkg varpmkmtsq pdnlgsseiv ivledsvyny
      181 winwndantn riwdiatdrh lgkqgmlyad ghvqrnqrey kfdeprthaf rnladlyn
//
LOCUS       WP_176013216             516 aa            linear   BCT 11-JAN-2025
DEFINITION  RHS repeat domain-containing protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176013216
VERSION     WP_176013216.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..516
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=57683
     Region          <7..374
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mihcsfhtat rgydhfnrlt gvngygysyn ardqrtkqtl sdgqyweysy delgqvisgv
       61 kktaagvvvn gqnyayaydt vgnrettaad avatnytanq lnqytaignv ipsydvngnl
      121 ltgysgwtme wngenrlkai yntttrlefa ydyngrrfsk ktyaksgadw vlssekkfiy
      181 dgfkqiaeyn gttlaqayvw qpagsgdfdv plwmksgsnv ytyvtdgnkn irqlknaagt
      241 vvatydydpf gnvaatgsvs nnpwqfssef rdtetgliyy nyryyapsig rwisrdpiwe
      301 eggvnlyimi anslissyds wgygfwsrvf nviggalqat aggvliatgg pagwvlgglm
      361 liqglanvva gfradesnfg illsqriaea vgldpqtgal vyvgieavtg lisissggkt
      421 clqivfkgek yvrqsvnyvr qypffgqvvt rivplfhyse yvrihwsirv lvggqtvfda
      481 yteyesvrdf frrmdpenkd dlelrdvfyq nieyqe
//
LOCUS       WP_176013238             247 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176013238
VERSION     WP_176013238.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..247
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=27126
     Region          1..>63
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mkqkihftli ellvviaiia ilasmllpal skakakaqmi ncrsnlrqii yaslfyagdy
       61 ddylmpafty nteeaangvg psvswcywpg emkysygmgd kvflcpaasg adfeflewsn
      121 yrskvpyghn sttfgysgle sgspkryeav lnagrkngsd piafadcyit gespvgpryp
      181 twggeiaphq tacenpdmva snialrhdmt tnlafyngsv iglrgaeiva kqkqlcwpiw
      241 qnggwvd
//
LOCUS       WP_176013243             152 aa            linear   BCT 11-JAN-2025
DEFINITION  tRNA (cytidine(34)-2'-O)-methyltransferase [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176013243
VERSION     WP_176013243.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..152
                     /product="tRNA (cytidine(34)-2'-O)-methyltransferase"
                     /EC_number="2.1.1.207"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0141098 - tRNA
                     (cytidine(34)-2'-O)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=17581
     Region          4..150
                     /region_name="TrmL"
                     /note="tRNA(Leu) C34 or U34 (ribose-2'-O)-methylase TrmL,
                     contains SPOUT domain [Translation, ribosomal structure
                     and biogenesis]; COG0219"
                     /db_xref="CDD:439989"
ORIGIN      
        1 maqfnivlvh peipqntgni grlcvstdsr lhlvkplgfs ledkylkrsg mdywphldlh
       61 vyetweaflt vntpetlffl strgrrsfwd crypdgcylv fgneghglpp efyeryqhsl
      121 ltipmrgqfh rsfnlansva itlfealrqq eg
//
LOCUS       WP_176013339             208 aa            linear   BCT 11-JAN-2025
DEFINITION  flavodoxin family protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176013339
VERSION     WP_176013339.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..208
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=22514
     Region          2..183
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mkvlllngsp hrdgcvftal sevaealrsn gveseffqig nravqgcigc lhcadgndgc
       61 vfkeplytel vaqcrgcdgi vigapvyyag ppgslcalld rlffsagkyl kykpgacvvn
      121 crrggasaaf drlnkyftin qmpvassqyw nsthgftpde vrrdleglqt mrtlgnnlay
      181 llksvakaev vrpepeepvy tnfigttq
//
LOCUS       WP_176013344             354 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176013344
VERSION     WP_176013344.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11575100
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..354
                     /product="GntR family transcriptional regulator"
                     /calculated_mol_wt=39698
     Region          10..70
                     /region_name="WHTH_GntR"
                     /note="Winged helix-turn-helix (WHTH) DNA-binding domain
                     of the GntR family of transcriptional regulators; cd07377"
                     /db_xref="CDD:153418"
     Site            order(31,33..34,42..46,48..49,52,62..63,65..68)
                     /site_type="DNA binding"
                     /note="DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:153418"
     Region          73..352
                     /region_name="PurR"
                     /note="DNA-binding transcriptional regulator, LacI/PurR
                     family [Transcription]; COG1609"
                     /db_xref="CDD:441217"
ORIGIN      
        1 mnnsktdctq qtrqqifdqy irgrlpgeri ptekqlskey qvsvttvrra vslledsgfl
       61 krrhgsgtfi gealrirkvg llvpeadysq ffhtmairms pelrqrgysp tlfvtggdhf
      121 elatmesdlr smdalilcgy gaeagelrri gvpyvvlgne fpredtyvat dmisgmmmam
      181 rhlyatgcrk iiylgnfhwn splaqehlet smrylgfrla lhelglefsp gqalaagyss
      241 lhgyervlrl vdesefdall catdqlaqga iqallgrnlr ipeevsvvgc nnllpeteyl
      301 vpltaidfnl dqfaaqavyl lnrkldgtpe edvfslflrp klvcrastrp lsgr
//
LOCUS       WP_176013357             230 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176013357
VERSION     WP_176013357.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..230
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=25495
     Region          6..85
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mkkwkftlie llvviaiiai lasmllpalg kakakaqeik ctnnlkqagv vynlylndnd
       61 dwtlpdgwaa gpgywfldlg wwysgkqiys geglgelnnl lqcptnsvgs iwgdpnaeng
      121 ykinyvhsry liaikstept npsdvvlfgd vaaadgsqfi fcsvaangny tehaergnty
      181 awgfglihnk kanclkldgh vegvngdqfe ndeiifdkpe nkwyryghrp
//
LOCUS       WP_176013492             492 aa            linear   BCT 11-JAN-2025
DEFINITION  anthranilate synthase component I family protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176013492
VERSION     WP_176013492.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Kerbarh,O., Bulloch,E.M., Payne,R.J., Sahr,T., Rebeille,F. and
            Abell,C.
  TITLE     Mechanistic and inhibition studies of chorismate-utilizing enzymes
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 763-766 (2005)
   PUBMED   16042594
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Dosselaere,F. and Vanderleyden,J.
  TITLE     A metabolic node in action: chorismate-utilizing enzymes in
            microorganisms
  JOURNAL   Crit Rev Microbiol 27 (2), 75-131 (2001)
   PUBMED   11450855
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..492
                     /product="anthranilate synthase component I family
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=53988
     Region          20..484
                     /region_name="TrpE"
                     /note="Anthranilate/para-aminobenzoate synthases component
                     I [Amino acid transport and metabolism, Coenzyme transport
                     and metabolism]; COG0147"
                     /db_xref="CDD:439917"
ORIGIN      
        1 mntkpdfkef eklyrphcii plyrelladl etpvsilskl agrdqiflle sveggerhgr
       61 ysfialnpya tftveagrpy ltdragrrpl agaangfaal rqvlgdavmv rqpglpplag
      121 gaigclnfea aglfeelppp kdhperpvaq fmltdemitf dnmrhtllls valhsddyps
      181 araaydtgle rlkalagqlg gaghpapavt dmvqfqanms keefcrmver gkaeiaagea
      241 iqlvlsqrfq apltvdpvcl yralrlvnps pymyfcknfd ryligsspet mvklqqrtag
      301 lrpiagtrrr sgdeatdrql adellrdeke raehlmlvdl grndlgrvaa pgsvqvrdfm
      361 qveryshvmh lvsnleaqld dsfdafdlvr safpagtlsg apkirameli relepesrga
      421 yggavgyisy dgnldlaiti rtmliedgvl siqagagiva dsvpeteyqe tlnkamamfk
      481 avelaanglk ln
//
LOCUS       WP_176013574             182 aa            linear   BCT 11-JAN-2025
DEFINITION  LemA family protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176013574
VERSION     WP_176013574.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..182
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=20271
     Region          19..179
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mlgvvlviaa vavivgvclw yiavvnrfrv llvkieetds gievaltkry dlltkmvalc
       61 rkyaereaga lsslvelrrg mdvngrslac rrmdevsrqi aelveaypdl rssanfkelq
      121 tavreteerl raarrlyngn vsvfnrllat fpagwvggkl hlrpraffta eeaekanvem
      181 al
//
LOCUS       WP_176013586             333 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-dependent glycerol-3-phosphate dehydrogenase [Victivallis
            sp. Marseille-Q1083].
ACCESSION   WP_176013586
VERSION     WP_176013586.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..333
                     /product="NAD(P)H-dependent glycerol-3-phosphate
                     dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0047952 - glycerol-3-phosphate
                     dehydrogenase [NAD(P)+] activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0046167 - glycerol-3-phosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=35984
     Region          1..328
                     /region_name="GpsA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0240"
                     /db_xref="CDD:440010"
ORIGIN      
        1 mkisvlsdga wgsalamvlc gnghqltiwg pfpdylaqme atrsnprflp girypdgirf
       61 eadmktavag aelillatpt qylrgvlqqf kpffqpdrql vvnvakgied gswrrvsevv
      121 qselgdsryv vlsgpshaee vsrqvptavv aaarqpewas qaqqlfmndy frvysgddpi
      181 gvelggalkn vmaiaagiid gmqlgdnpka alitrgiaem srlgealggr aetfaglsgi
      241 gdlivtccsg hsrnrhvgee lgrgrklpei ieamglvvae gvrtargayt larsrqvetp
      301 iidqiygily enrepalair elmtrsakae rfg
//
LOCUS       WP_176013611             103 aa            linear   BCT 11-JAN-2025
DEFINITION  glycogen-binding domain-containing protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176013611
VERSION     WP_176013611.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10120552
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..103
                     /product="glycogen-binding domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11203
     Region          21..102
                     /region_name="E_set_AMPKbeta_like_N"
                     /note="N-terminal Early set domain, a glycogen binding
                     domain, associated with the catalytic domain of
                     AMP-activated protein kinase beta subunit; cd02859"
                     /db_xref="CDD:199889"
     Site            order(42,72,79,91..93,95,97)
                     /site_type="other"
                     /note="glycogen binding site [chemical binding]"
                     /db_xref="CDD:199889"
ORIGIN      
        1 mvkmtkkntc adgaepkkrr vnfvidagpg kvvsvagsfn dwdpeakila drnndgvyrg
       61 almlkpgqye ykfvidgvwc vdaqnpnfsp ndlgtlnsll ive
//
LOCUS       WP_176013621             239 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176013621
VERSION     WP_176013621.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..239
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=26857
     Region          1..78
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mrkkftliel lvviaiiail asmllpalak akakamgvkc isnqkqlgla mwmygddydd
       61 ytlcilpydn flwpwpyllk dykyvtakdi yfcpssssky tvdenfdtrn eftyglfqrl
      121 vgekasntgn ppmkraaidr ygnssreiwm adtangsdvt gfgnyygswa iewgsvfpgn
      181 eggknyypva arhrqnaanc lifdghveav pvyellnyne rrwvpgtnwv ggledggll
//
LOCUS       WP_176013665             290 aa            linear   BCT 11-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Victivallis
            sp. Marseille-Q1083].
ACCESSION   WP_176013665
VERSION     WP_176013665.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10173375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..290
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31961
     Region          32..287
                     /region_name="EEP-1"
                     /note="Exonuclease-Endonuclease-Phosphatase domain;
                     uncharacterized family 1; cd09083"
                     /db_xref="CDD:197317"
     Site            order(37,73,164,198,200,251,279..280)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197317"
     Site            order(73,279)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197317"
     Site            order(164,200,280)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197317"
ORIGIN      
        1 mkfilgmvlg allamadgas reaadqpags irvvscnlrg aliddgpdsw eyrkesclei
       61 lkeidadimc fqelqtpnre aleeafpdyc ffgaldrpag ghpmngilyr rsafkllgsg
      121 gyalsdhphl sgsidwnhsc prfvnylile ekttgrrfri vnthldhesq iarekgaali
      181 neesavydpa mpqilagdmn cmvsnpavra llaaswqdsf flatgqeepg rtfhafqgre
      241 ctvdsfpgki dfilvrgale vtgaeivdrv gkngrypsdh ffveavvrfr
//
LOCUS       WP_176013702             311 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF523 and DUF1722 domain-containing protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176013702
VERSION     WP_176013702.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..311
                     /product="DUF523 and DUF1722 domain-containing protein"
                     /calculated_mol_wt=35482
     Region          1..150
                     /region_name="YbbK"
                     /note="Uncharacterized conserved protein YbbK, DUF523
                     family [Function unknown]; COG1683"
                     /db_xref="CDD:441289"
     Region          65..301
                     /region_name="YbgA"
                     /note="Uncharacterized conserved protein YbgA, DUF1722
                     family [Function unknown]; COG3272"
                     /db_xref="CDD:442503"
ORIGIN      
        1 miklgisscl lgqrvrydgg hkldyflrdg lkdrvewvpv cpetecglav prepmhlvad
       61 asgyrlrtvd sqrdytelmr hyinrrvtql sqsglygyvf kgkspscglr evpcyrpdge
      121 aagvagglfa eavrralpll pviddasihn vwlretfgnq iltlrrwhqf vaadgsaagl
      181 aefnrrhrll imlhspgmtp llsylvlhat sdkltatceq yfrtlmavma tpvslrkhqk
      241 vlffvfeelk nhldnwerle lqnmlhhlpe qpdtrsavaa lllhyirkfr ladwldqyyf
      301 qggeqifspq s
//
LOCUS       WP_176013711             323 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176013711
VERSION     WP_176013711.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 323)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..323
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35713
     Region          4..306
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mfriilllmi gccrlagaea aplrlylqwr pqaqfagyyl aeelgfyrea glqlelhhla
       61 ahrtpvqlla dgkadfvsdw lpsavsrraa gvpvvsvgql mrrsgmllvg skargvetla
      121 dlagrrvgvw vndfrlgplc mllrekiafe tvpssgdiel flwggcdama amiyseyfsl
      181 lnaglepedl svfclddygv plpgdgiyal eetcrqrpde cralveatrr gweaafadpe
      241 kaleavrrac rqgdvyynea eqrwmlehlk alydppgaaa rsqlsreeye fvgqmlrdng
      301 fitgplpdfa efaplaagag ere
//
LOCUS       WP_176013719             389 aa            linear   BCT 11-JAN-2025
DEFINITION  ROK family protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176013719
VERSION     WP_176013719.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..389
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=42239
     Region          70..376
                     /region_name="NagC"
                     /note="Sugar kinase of the NBD/HSP70 family, may contain
                     an N-terminal HTH domain [Carbohydrate transport and
                     metabolism, Transcription]; COG1940"
                     /db_xref="CDD:441543"
ORIGIN      
        1 misnqllqqe flrrllqcgt ltrseftaag nyraatvlka vdelkalgll lepdrngsrt
       61 grrsprlrin pdagrfigle vtsdhlygvv cdatgqptat aslepgwrfh asdlpqllna
      121 llrklcrepa ecysgialad pglvdtrrqv slrsvaiagw ngletgkllr qlshleqtlv
      181 ipecgarsyl eysercrhfd gslfhlrldd gigagfiqng tlfsgdscca melghlvlip
      241 dgplcqcgnr gcleaiagla girrriaele ansvrtilrt dgfqlkdlpa avrsgdrpaq
      301 llasdiceqi apvfaiiatl lnpgcivisg alkelgelll dtirrslrer clqatlaglr
      361 lelssldefa galgaarllr drlllqkir
//
LOCUS       WP_176013759             236 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176013759
VERSION     WP_176013759.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..236
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=25799
     Region          1..>62
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mrksrftlie llvviaiisi lasmllpalg kakstalraa csnnlrqvai gasiygqenk
       61 nwvspvadgf awsvlltgkh anganadkvg gnyleggvfv cpmsmddewt edtatyamyd
      121 alndgnydnk vkncgdfvnh kvfndnniay rttkikmpst mvmfseslnp keqsmyyrfs
      181 pnavvngasi htyhdnftna vffdshvasm rpgelsqtat eitnviddqg nqigmk
//
LOCUS       WP_176013771              98 aa            linear   BCT 11-JAN-2025
DEFINITION  glycogen-binding domain-containing protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176013771
VERSION     WP_176013771.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10120552
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..98
                     /product="glycogen-binding domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11120
     Region          16..81
                     /region_name="E_set_AMPKbeta_like_N"
                     /note="N-terminal Early set domain, a glycogen binding
                     domain, associated with the catalytic domain of
                     AMP-activated protein kinase beta subunit; cd02859"
                     /db_xref="CDD:199889"
ORIGIN      
        1 mkmiqlkkpv agsrrvafrv kaatgrrvrl igsfngwnep arpmvdwrhd giyrgmlsll
       61 pgvyeynfii dgqwysdaan pnrkswqpgk srsilkvs
//
LOCUS       WP_176013802             393 aa            linear   BCT 11-JAN-2025
DEFINITION  sialidase family protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176013802
VERSION     WP_176013802.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..393
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=43218
     Region          60..380
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Site            order(84,245,261,328,357,374)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:271234"
     Region          117..167
                     /region_name="Sialidase propeller 2"
                     /note="Sialidase propeller 2 [structural motif]"
                     /db_xref="CDD:271234"
     Region          173..235
                     /region_name="Sialidase propeller 3"
                     /note="Sialidase propeller 3 [structural motif]"
                     /db_xref="CDD:271234"
     Region          244..282
                     /region_name="Sialidase propeller 4"
                     /note="Sialidase propeller 4 [structural motif]"
                     /db_xref="CDD:271234"
     Region          292..349
                     /region_name="Sialidase propeller 5"
                     /note="Sialidase propeller 5 [structural motif]"
                     /db_xref="CDD:271234"
ORIGIN      
        1 mksgvallfa avgglsfflp apaaatagsl paaskgdvsm eqktvlelph qagnprnseg
       61 afitlkdgri mfiytkfygd swsdhaaacl aarysddngd swtaedeivv pnegqnvmsv
      121 sllrladgrl amvylrkalt adgyldcrpq lrhsadegkt wsepvsiipt pgyyvgnndr
      181 lvqlksgrll ypvalhraht dddgrkgvdi rgiglvyysd dngdswreap qwllppsrlg
      241 sgfqepgvve lsggrlmiwf rtndgaqyta csgdqgltwe tavknnrfrs sespmsikrd
      301 pehgdliavw ndhsprwaie rrdaswgrtp lvlarsadeg etwhdhqlle sepdhgycyi
      361 aiefvpdgll layccgggrd avlqdlrikk iyr
//
LOCUS       WP_176013857             250 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 3 protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176013857
VERSION     WP_176013857.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 250)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444753
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..250
                     /product="glycoside hydrolase family 3 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27040
     Region          14..>243
                     /region_name="BglX"
                     /note="Periplasmic beta-glucosidase and related
                     glycosidases [Carbohydrate transport and metabolism];
                     COG1472"
                     /db_xref="CDD:441081"
ORIGIN      
        1 mledfgsrgv etfdgpagvr laeaatawpc avaiasswdp dlaeqigrav aaeaglngld
       61 iwlapgmnih rnplcgrnfe yysedpvlsg kiaagltrga qsngvgvtlk hlvannkenn
      121 rtnsdsrvse ralreiylkg friaiqeaap wcimssynkv ngretaenre lltgilrqew
      181 hydglvmtdw gnnslqtlei kagsdvkmpn gqpdgllaal hageltrtdl ergakrvlel
      241 vlkreaagtq
//
LOCUS       WP_176013864             371 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176013864
VERSION     WP_176013864.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..371
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42593
     Region          5..224
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkipftivvp acnvagyaae miasvkaqtf pefeaiivne eskdgtrqvl heaiagdgrf
       61 elvtlprsgs asvsrnygid haggeyivfl dgddwlepea larfdrlire adhpdivmaa
      121 vrcwycradg vwepreclgl gregerfasg vdamladgkl ehwipgswln ifrtgllren
      181 rlyqvpgrmh qddewtyrvf lvagktaate yshynyrcne qsitntqsrk siadraanae
      241 svlqywrthd iparikrpla dyycknflhh sfftrsrlgr lnpnrpscae rremfrrcfg
      301 pserfaayla varaakrser lmipvmrlar crygfkpael ffnfiyypai fvfwrklkna
      361 gwlhrkapda k
//
LOCUS       WP_176013876             414 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176013876
VERSION     WP_176013876.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..414
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=45446
     Region          218..411
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 mmkwsggiwv gigvfglllq lplaagsvfe eqmadsvawg gdenalvane tldgrpvlkf
       61 tlpgrrhcqf ngnavgknal kleiqrldtd fwltirlgsr pyydcfsamv piagegwqtv
      121 ivpfeqflpg fdvvysspsp lapeavirgk iggailplee lntvtfgsyw qishrnepia
      181 pysflvrnie laaigegerp agavepersr tldevvkkma ageavtidci gdsitagtsv
      241 eqpernayps llqaqlrqaf dneqivvrnl gvggafsfel rlwaqrdlte fpadlvtvmv
      301 gfndriynvd reiyrqamld yvdrvrhsaa vapalvlltp spglgdryht qdelaeairt
      361 igvekqlpvv dvsaafqalp meefeslmad fahpnkrgqa liadrlaalf rqar
//
LOCUS       WP_176013865             518 aa            linear   BCT 11-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176013865
VERSION     WP_176013865.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..518
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=59275
     Region          6..419
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mikipivknt ltnylsmgvk llqgvlvtrw liaylgeeyy glwallwsff cysllldfgf
       61 gvtaqkytsi gifqqdlkry nriistifsf havmsliila ctvaasffvv tlfhlddtpa
      121 erieycrrcf llfgigsali fpsgifpeim vglhkiyqrn yviivsklle laglllvfac
      181 kgellllisf tlvlnlltnl amlfyirpai pgfrlrlwis revfreifqf sgfvylcsva
      241 rllwgrvspl lisifcglqe vgffqigsrl pnlmnqltgp yqenitpisa sfyaqgkhra
      301 lsrilvnsmr wnsflssgmm vgifvfaael irflfkvdqp lvlaicqlmv vslyigllfr
      361 siperfllma ekhkllswit iwesvanfaa civllqffni tcvvwaalii kvfttvffia
      421 ppmlrylkig vwkllyeicf rqlaaalplv giallletfa agslsdfwll viggssggla
      481 yvgcsywwvl sadekrffrr kyltrwrqiw rqwkggrr
//
LOCUS       WP_176013981             236 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176013981
VERSION     WP_176013981.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..236
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=26046
     Region          1..78
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mkqrftliel lvviaiiail asmllpalgr akakaqqikc tsnqkqigta tilystdfdd
       61 dlplagngnp adyanffywh wlltgyignt tdgsagsdyg kvflcptggs detfknagge
      121 iisnysynkv ignlmqgyqv kktstcpmps tmavlvdgkc tsgtangnfe iwdvygdnpn
      181 nhdkyftirh drnrsnhlyv dghvefsnft gldrydtlvr yafvdtsngg wknlwn
//
LOCUS       WP_176014014             324 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176014014
VERSION     WP_176014014.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..324
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35106
     Region          89..297
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mksnlpssqs pwltvetqqf idalnanpgp plytltpega rqvlseaqai pvaspaaeva
       61 dlvlpvgptg kvevrlvrpe gaaanlpalf yfhgggwvmg nkdthdrlvr elavgagvav
      121 ifvnytpspe aqypvpveqa yaaveyvcah pekfhidpkr lavagdsvgg nmtavmtlla
      181 kqhgrpefaa qllfypvtda afdtasyref adgpwltlka mewfwdaylp dktrrcevtv
      241 splqatveql eglpealvit dqndvlrdeg eayarklqqa gvkvtavryn gtihdfmmln
      301 alagstptra avrqavdflk nifs
//
LOCUS       WP_176014024             517 aa            linear   BCT 11-JAN-2025
DEFINITION  RHS repeat domain-containing protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176014024
VERSION     WP_176014024.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..517
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=57955
     Region          <5..395
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mtmmrsfnsa hrltgvstta gsltknygyt lnikdqrikt tladgsywdy aydnygqvin
       61 avrknasggi agqsfnysfd qvgnrqsafq gttgsdsqws ytanavnqys litepngtty
      121 aqvhdadgnl tgsyttqyty daenrlktad vgtyrheyty dyqgrrirqk vilksgatgq
      181 tqsevayvyd gwnvvgvydt mtaaptfqkg ylwgedlsgs lqgaggvggl laekrggqty
      241 lpvydgngni msylnastka svaeyvydaf grtisssgte adnftyrfst kpmdgnglyy
      301 ygyryydpqh grwisrdple eeggvnlygf iqnngvkfid vnglwgwdgd yietiwimms
      361 ddsadgdavr eaffmeawdr gnatadaltf datkalrqkl ncdivfdees yekqrcfasc
      421 weritasalt agildkrtnw pavsdslgir divnywqddn mlgvsgsatl mglghyariy
      481 errsreqqei ferlrvsarr nqhkkkqpne fceieek
//
LOCUS       WP_176014051             355 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF805 domain-containing protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176014051
VERSION     WP_176014051.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..355
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=41273
     Region          3..114
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 mfkyvvhffk hyfdfsgras kkemiigvsi vifillisre llinalirns sevkwyillv
       61 ffimlilfpa hfaimirrmh digrpgseaf ipfvgcfrif epsqkgpnqy gdepilwdmk
      121 rnmsfnlsgn kfilkskknn nhivlngsff vliflsllfv lslllllsif wfdlpqtfim
      181 lvleiitlgf vlhniikcfi kkkslyqhpi iyyeskykyi kllknkyfkl ycfqgnciei
      241 avsskkifhi ahnnfddvkg efftlstiin nnnviiatgn ywdiiklasi inyictlssn
      301 dasikllynd dfyppkdlrs mkdlpndtkc nsssevqgps vqaddvnyfq cnmrc
//
LOCUS       WP_176014072             243 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar transferase [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176014072
VERSION     WP_176014072.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..243
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27557
     Region          <46..242
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mteyqqpnhk lrkelinlll erasyaqgdy prrkvklwhf tvgsayllkr tfdlvlcivg
       61 livlspllav ialwikldsa gpiiytqtrv gkngrhfhfy kfrsmytdad qrraelagan
      121 esadgvlfkm kndpritrsg rflrkfslde lpqlfnvilg dmslvgprpp lpsevalytl
      181 edrkrlhitp gitglwqvsg rsdlpfkqqv eldkayiqsq sfgqdllill ktipavltgr
      241 gay
//
LOCUS       WP_176014118             245 aa            linear   BCT 11-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Victivallis
            sp. Marseille-Q1083].
ACCESSION   WP_176014118
VERSION     WP_176014118.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..245
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27650
     Region          1..243
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 mrfltyniay gtgspgserg rlltthrylk tsrlwlariv rfirqqspdv vglietdlgs
       61 srtdgvnqve mvaehlryqh faaakygphs llrrlpylqy qanallstge ihepfqhflp
      121 hgvkklvltg esggvnfmll hlslyyrtrc kqlrhltelv ppglpviiag dfntfrgste
      181 iqafcdaadl rsanaahlpt ypswgprkel dfilvspqik ilnfsipdte lsdhrplvld
      241 feldn
//
LOCUS       WP_176014138             184 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176014138
VERSION     WP_176014138.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..184
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=20153
     Region          64..184
                     /region_name="SoxW"
                     /note="Thioredoxin-related protein SoxW [Posttranslational
                     modification, protein turnover, chaperones]; COG2143"
                     /db_xref="CDD:441746"
ORIGIN      
        1 meakfnwqkt grtigwavga vivlgilsws amtgkcpfal ckpaapnata tdvppqtida
       61 eafwltdfpa aqvrakqenk pllllfhgsd wcgwcikldk evfsqpefid wakqnavlfs
      121 adfpqnipqs aalekqnskl aeqyqvegfp tvvllspdgr eiartgyqag gatnylkhle
      181 sllk
//
LOCUS       WP_176014214             176 aa            linear   BCT 11-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase [Victivallis
            sp. Marseille-Q1083].
ACCESSION   WP_176014214
VERSION     WP_176014214.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..176
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18541
     Region          <30..157
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 mrntpvqyrw ttgkepkive irlgvvagtp pppalagagr slerrlagel pawdmaqfal
       61 agvgdwarkv ltllfalvpa grvvgygqla alagrpggar avggvmrsnp lplvypchrv
      121 vaadgklngf mcssdaagaa lrlkrwllet egvefdaagr vkkaffltdp vdilpe
//
LOCUS       WP_176014200             125 aa            linear   BCT 11-JAN-2025
DEFINITION  BlaI/MecI/CopY family transcriptional regulator [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176014200
VERSION     WP_176014200.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..125
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=14152
     Region          5..123
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 msdlqisdae levmkvlwqq sprtsaelvk tlqqttdwaa ptiksllvrl vkkgavlqsg
       61 egrcfqyrpl vdyetyterq svdfldkffg gapqrmlsff veknklsand lkllqelied
      121 agkhe
//
LOCUS       WP_176014228             236 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176014228
VERSION     WP_176014228.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..236
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=25751
     Region          3..>62
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mekkgftlie llvviaiiai lasmllpalg kakaaaqsik cvsnlkqigv gtalyvdend
       61 dtmcpaymad avfdnytqkg nsyypallsn fcprdiwlcp sasgqeggln ppfadpqnds
      121 qknwiinygm nqcgstanas tkrfdkgiki tsipnptgti mfscdanyws gpyaigdfts
      181 lldyqvpipa vldgtdswte gtriayihnl kcnhlwvdgh vsnqkitkyr dwsttd
//
LOCUS       WP_176014252             378 aa            linear   BCT 11-JAN-2025
DEFINITION  MraY family glycosyltransferase [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176014252
VERSION     WP_176014252.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Anderson,M.S., Eveland,S.S. and Price,N.P.
  TITLE     Conserved cytoplasmic motifs that distinguish sub-groups of the
            polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase
            family
  JOURNAL   FEMS Microbiol Lett 191 (2), 169-175 (2000)
   PUBMED   11024259
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Lehrman,M.A.
  TITLE     A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P
            transferases
  JOURNAL   Glycobiology 4 (6), 768-771 (1994)
   PUBMED   7734839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10160596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..378
                     /product="MraY family glycosyltransferase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=41192
     Region          44..308
                     /region_name="GT_WecA_like"
                     /note="This subfamily contains Escherichia coli WecA,
                     Bacillus subtilis TagO and related proteins. WecA is an
                     UDP-N-acetylglucosamine (GlcNAc):undecaprenyl-phosphate
                     (Und-P) GlcNAc-1-phosphate transferase that catalyzes the
                     formation of a phosphodiester bond...; cd06853"
                     /db_xref="CDD:133463"
     Site            117..118
                     /site_type="other"
                     /note="Mg++ binding site [ion binding]"
                     /db_xref="CDD:133463"
     Site            229..232
                     /site_type="active"
                     /note="putative catalytic motif [active]"
                     /db_xref="CDD:133463"
     Site            order(284,298..301)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133463"
ORIGIN      
        1 milwphlyfi tllggagltl iatplfqrla ekldfmdrpk gekhkghgkp vallggaamf
       61 sawlccflfa flaldsglat qisqaiaaht aglahvsvkl lfiilgaala mllgladdrc
      121 hlqaapkfag qflvaliavq fagirisifl dvpvltwlat vfwfmlmmns inffdnmdgl
      181 avgtvtiaml ffaivagiqq qyfvatlasl scgvglgfwf fnhspatifm gdsgshflgy
      241 liavvsasvt yyspefslsr fpvllplfil siplfdtlsv ivirslrrqp fwigdhnhls
      301 hrfvrlgmsr kravlllhtl mfvinlsvlp llwgtfqtav vilvqllfll sfltlllnag
      361 ktlpaasgpp tdqpakkp
//
LOCUS       WP_176014293             189 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176014293
VERSION     WP_176014293.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..189
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21101
     Region          35..171
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mmkdfltdia peefncrifq llskrwmlla agdlaagkfn amtvgwgmmg tmwnlpvvta
       61 avrpqrhtle fmneyetftl safpescrai lafcgshsgr dedkfaacnl tlaaasrvaa
      121 pafaeaelvi ecrkiyidkl lgknfleksi lkdcypqrdf hhlfigsvvh isgteayrhn
      181 rendekaga
//
LOCUS       WP_176014314             317 aa            linear   BCT 11-JAN-2025
DEFINITION  serine/threonine-protein kinase [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176014314
VERSION     WP_176014314.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..317
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=35441
     Region          43..304
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(49..50,52..55,57,70,72,104,121..124,128,130,168,170,
                     172..173,175,186..187,190,204..207)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(49..50,52..55,57,70,72,104,121..124,128,170,
                     172..173,175,186..187)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(53,128,130,168,170,172,190,204..207)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(66..67,96,101,106..109,122)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(186..194,200..207)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mlyrcsfcrr qsdstspefs tgrcphcgee lagefsggri geftvlaelg rgnngvvyla
       61 rqqilnreva lkilpperfe epatrqaffr eskvtaklsh pnivqawaag vtehgygffa
      121 melvagksld dwllafgalt yaealkigar isdalayawe kygmthgdik pgniiirqsd
      181 kcpkladlgl akfanepyqd evmatplyap pevinfdfeh mgyksdiysf gatlyelfag
      241 eapfpsddqq wvldqhrftv peplkergcf dpqlsdfias mlaknpddrp ewrdiadflq
      301 qlerrlphaq pavtsaf
//
LOCUS       WP_176014327             286 aa            linear   BCT 11-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176014327
VERSION     WP_176014327.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..286
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=31981
     Region          15..180
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
     Region          <246..277
                     /region_name="DUF6576"
                     /note="Family of unknown function (DUF6576); pfam20216"
                     /db_xref="CDD:466367"
ORIGIN      
        1 mrpssggqel sgrtmifili giniflylif paprtmqqlv dpdfpyyrlv lssrgiasgq
       61 iwqlvtamfm hadfyhilfn myglylfgml laplmngyki lwlyliggls gnlifllfnw
      121 gnpfylmgas galfgimaav allrpnvqfi mllppipvka ktlvivyavi ellfqfgngg
      181 qsdgiahlah lggllggyly ikflfgpnla wdilprrrvr pgetpppgag prmwrqpdft
      241 vkpgskiksq didylldkis ktginsltpe eteilrrare qmrgkh
//
LOCUS       WP_176014357             773 aa            linear   BCT 11-JAN-2025
DEFINITION  right-handed parallel beta-helix repeat-containing protein
            [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176014357
VERSION     WP_176014357.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Burnim,A.A., Dufault-Thompson,K. and Jiang,X.
  TITLE     The three-sided right-handed beta-helix is a versatile fold for
            glycan interactions
  JOURNAL   Glycobiology 34 (7) (2024)
   PUBMED   38767844
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12131601
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..773
                     /product="right-handed parallel beta-helix
                     repeat-containing protein"
                     /calculated_mol_wt=87521
     Region          571..712
                     /region_name="Beta_helix"
                     /note="Right handed beta helix region; pfam13229"
                     /db_xref="CDD:463811"
ORIGIN      
        1 mifkfhsgkr lrlwlvvadl lcamfsavaa enffqddtcg ilnashatiq lqpdgsaall
       61 vdtrqsdgew nvcwrtapgv lkperhyeat frsrilenpg dsgllflvrp essidnysdv
      121 isqwqnrgek lqrirfktpa epqdyafqih thnrlkalis sfqlrelesp eqsvaldrpf
      181 ssggsaatda eptgapefti krpepaagap vlsvadfgas pdnpdnfaaf qqaidacaaq
      241 qaaqltvppg tyrfrtnqsl qfrrlhnfrf dgngallifl kesaammeiq gceqvefanf
      301 aidwdwqvdp lasfvevaai dpaqdsvdlr fidyekfpve kikirdieei dpatmsvgve
      361 hsvnrwfqqp nyrwlkpnll rlsgtgqmtr dmavgqlfrm rhyvydmagi clsdnrhltv
      421 envtvhsvps hafviggkqq ywqllnthvr ppagerrpit ctadhchvaq scgyfkmigc
      481 efmlggddcl nvhdissfcq raddhelqia rpgmqyyykv gdelelrhed ysptgyrgki
      541 tgiwekdgql hltmdavlpe mkqegfivfn waydssnill rdnyfhdnra rgilllgrni
      601 tvennrffhn qmgaikietg ytfdswsegy gagnivirrn rfeqtnpqgt vndgmerdif
      661 igvylksdps sektsypilh diliednqfi dsygllayis saanvtlrgn riqqwtprqr
      721 aqpyrgsiya vytdgltied nlwqrsklap pprlifdrps vhnitvrgns lvd
//
LOCUS       WP_176014383             248 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176014383
VERSION     WP_176014383.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..248
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=26994
     Region          1..>61
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mkksftliel lvvvaiiail asmllpalar aktaaqrisc isnlkqcslg qqlyavdadn
       61 yvlvyswdgt neltwggall ygaylgtadv lncpaltytk gltwehgykn swdqwenyga
      121 shtregdwdn yydkmaarwg sffsaisfhe agqgahlwam skmiapsdtf mivdsiknng
      181 hgstnfhpri fwgnetamgi hhggtsgnla fadghaaavs knaligeyyf kylnggagvl
      241 sfdpvvsq
//
LOCUS       WP_176014406             382 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176014406
VERSION     WP_176014406.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..382
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=43248
     Region          9..>97
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 miretgksqt iyrelrariv sgrlepgrql pkesdfcref gvaretlrra lerleaenli
       61 drrrslgtfv aerrerppvi nfllpcsdfl srrgvvpvfn rqlfegvmte cyqrncrvst
      121 iavsadndnr hidlrqlryl epesrvviqs awfepvfpyl eslncrmvfv ggyivetpll
      181 ngmprprppa takkvifndr yafelaatel ykagcrkval aapayvddly npprngylea
      241 agrfgqkqpl ifplpdaapr wpwlpgilsr rhaetgfdgl vlcprdgdep dsgvyfnytl
      301 glpdsvkvvi gwlmpersfq esclpsvvfd tpaigriaak allderfvad eivisphfrk
      361 pppgdvpaaw sredmpslnp nn
//
LOCUS       WP_176014409             224 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176014409
VERSION     WP_176014409.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..224
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=25061
     Region          1..>73
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mkqrftliel lvviaiiail asmllpalar akrtaqlikc tnnqkqlgly inlygndnad
       61 liphqrqnln vdpytntdag gqvdtsvirv gsgwysglgl lisaeyipfv wdqkptelff
      121 cplsesvvds whanwegtwy ssylyfggfh nsltwtydkg srarlsdngg calmvdyptv
      181 dsatesshgl ykanvlyldg hvesrtqkeg yygrgysyst nwed
//
LOCUS       WP_176014437             430 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-binding protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176014437
VERSION     WP_176014437.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Miller,J.M. and Enemark,E.J.
  TITLE     Fundamental Characteristics of AAA+ Protein Family Structure and
            Function
  JOURNAL   Archaea 2016, 9294307 (2016)
   PUBMED   27703410
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..430
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=49780
     Region          1..424
                     /region_name="COG1373"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440984"
ORIGIN      
        1 miikrdqylq klinrqwngl ikvitgirrc gksyllrnif keyllsqgvk peqiihleld
       61 ltsniryrnp lelaqyvhdr idgknekfyl fideiqmsep vknpylpdgk kitfydtlnd
      121 fkamqnldvy vtgsnskmls tdiltefrgr gdeirihpls faefysaigg dkqeafkqya
      181 yyggmplvlm qkddgeksay ltslfsevyl kdiierkkie ypdelsqild llcssigsls
      241 npskiadtir srkgvkvsan tlksyleylk daflfceckr ydvkgkayfe ypmkyycedi
      301 glrnartgfr qmemthiven micselrqrd fnidvgivyk ngkskngsni kisreidfia
      361 skgnrkfyiq safampdeek rvtelkpfsl tgdsfpkivv rqdignpwyd dsgflnigli
      421 dflldtsyln
//
LOCUS       WP_176014504             560 aa            linear   BCT 11-JAN-2025
DEFINITION  RHS repeat domain-containing protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176014504
VERSION     WP_176014504.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..560
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=61541
     Region          <9..385
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mnldagcegr pmahythnaa gqlstlrlat apanqtvsta trsfdsahrl tgvsttagsl
       61 tknygytlni kdqrikttla dgsywdyayd nygqvinavr knasggiagq sfdysfdqig
      121 nrqsafqgtt gsdsqwsyta navnqyslit epngttyaqv hdadgnltgs yttqytydae
      181 nrlktadvgt yryeytydyl srrirqkvil ksgatgqtqs evayvydgwn vvgvydttta
      241 tptfqkgylw gedlsgdlqg aggvggllae krggqtylpv ydgngnimsc lnastkasva
      301 eyiydafgrt isssgaeadn ftyrfstkpl dgsglyyygy ryydpqhgrw isrdpieeng
      361 gvnlygfvgn nginkkeylg ldiwvensta vhgwhkricv tvwkensaef ygprrtccgn
      421 dgreyipagk ycisfgmrkr avlgflggaf adggifdfds ggedgsssva ephlepdfen
      481 pipfppgfeg ptadgngeiy sdmiaateki rqhaqtecne dfetlkymks legkraeysi
      541 lgqncrdfsd mmfdyltsek
//
LOCUS       WP_176014657             420 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176014657
VERSION     WP_176014657.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..420
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=44587
     Region          <47..245
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          71..103
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          108..137
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(111..112,115..117,120..121,125,128,137,141,144,
                     148..149,152..154,157..158,162,165,174,176,178,182..183,
                     186..188,191..192,196,199,208)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          141..174
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          163..417
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          176..208
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          316..348
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          350..382
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mttsrkmqmi vaivavtlai gtaysqqart epdpaetapl enfsvfarta tadevaaalq
       61 kgadpaeidd iyntalinaa kfnpdvkvir lllqsgaevd argmynytal iagaemaene
      121 eiikalldag aqtdlrsgpr sgsqsalhla aianpnekvv evllnagmpv nilnregqtp
      181 lmlaawrnpn pkvistllrh gadaklqdpq ghtawdyand naarvgseal aqleaiiqpa
      241 nkpnnpsgip ygtqleellr ngsladiqka idagvnlerr nirgipafca vatnpdmkav
      301 slvinsginp nlafadgwtv lmtaaqhgns peiikilada gadinhqdag gwtpliaaif
      361 hnsdaamiea llkagadptl aakngqtpld farrifepen engqkiyhlv eqavkkkaqk
//
LOCUS       WP_176014675             168 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176014675
VERSION     WP_176014675.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 168)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12226222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..168
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19268
     Region          25..160
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 mptadfqlra aesdaelrri ealarriwpk tydgilspeq leymlhmmyd lpvlrrelae
       61 gvcfrilydg espigffscg pyregvaklh klyldydyhh lglgsymlqa akqllreagy
      121 rhmllnvnkn nrnalrayer nglvleqavv ndigngfvmd dyvfgcdl
//
LOCUS       WP_176014780             221 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176014780
VERSION     WP_176014780.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..221
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=24872
     Region          1..93
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mkrrkiftli ellvviaiia ilasmllpal skakaaatni kcinnskqlg lawfmygndy
       61 ddvalgpgwd anetfwpdrm anylaakwwn nsdgvdhasf fathgcpars vgdngnapwi
      121 aplrfldesd dtwqprvskf sqfkrpskqv llaestwyny cwgswlaphg qnanytfsdg
      181 hvsamrsmlk drvtpapnpe ngydpgfpdt dgyrwfdyse f
//
LOCUS       WP_176014833             447 aa            linear   BCT 11-JAN-2025
DEFINITION  MATE family efflux transporter [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176014833
VERSION     WP_176014833.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..447
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47064
     Region          13..444
                     /region_name="MATE_yoeA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Bacillus
                     subtilis yoeA; cd13138"
                     /db_xref="CDD:240543"
ORIGIN      
        1 mkefaqnltv gkvskqlfrf tvplffanll qafynitdmi vvgrfvgstg laavsnasvl
       61 cfiiagigqg itiggtvlva rtrgagdrrg eretigtlft ltalaalpvt vaglmlsrqi
      121 fvwlelpdea lpeavaymdi lsggtiaifg ynavcallrg rgdsrrplqf vavaavvnvv
      181 ldlllvgwlq lgtsgaawat vtaqgvalsv alghlkqref fcgfrlrslv mrpdkvagil
      241 qtgipsalqm lvvnlafllv tgmfnrygva vaaaagiglk istlagmpcw avgqavtama
      301 aqnlganqia rtaetalagi rlsllstgta vvliqlfaaq vigcfnsdpe virtgvvylr
      361 ifcsfsglay avmytcdafa tgtgaaslal fnalleavll rlllcwlfgm vwgggfvgvc
      421 wgmalstlpp aliglgyyrr gswrrls
//
LOCUS       WP_176014836             358 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176014836
VERSION     WP_176014836.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..358
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39043
     Region          1..356
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtataidlkg ickayqpgkr vlepidlsiq pgelffllgp sgcgkstllr ilagliapde
       61 geiffnaari dqlppekrqa amvfqsyalw phlsvfenva fglrasgvkg aelnrrvaea
      121 leivqlgelr drkipslsgg qqqrvalara lavepavlll deplsnldar lrdimrleir
      181 rickerrqta iyvthdrkea lsmadriavl nqgklqqigt pqeiyrqpcn rfvgaflgea
      241 nfipatitav tavrirvacg wgelsvpspa kplaagdcve llirpesirp aadeelensf
      301 eavltegtfl gesgswslka gdgsrlvmne lsprprlpgd tlrvqvaped ivileaer
//
LOCUS       WP_176014799             404 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176014799
VERSION     WP_176014799.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..404
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44925
     Region          13..341
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mglqtrfqai flprsgalaf fvsiliwgig igcfaatlnn ylveihsvde fqrglieffr
       61 eipglllvil lafmhrisdw rimrigtlis mvgisallip vdkvvvtlli miwstgehlv
      121 mpvrssiamq vaapgkagqs lgfvtgamng gtvagsilva lifwigvhwl hweraelyni
      181 vwgmifvlml islictftrn apnypshrpr lyfnwkfkkf ymlelfygar kqifltfapy
      241 vliinyhltt admalllgic aainifgspl igrltdrigy rnvmiydtvi lffvclaygy
      301 agelfraeva fwvvcvnfif davisttsla tnlyvreiag sqdeltstls tgisinhlis
      361 ilsaplggwi wqrygvgvlf sfaavmavan slfawtlpkp gtae
//
LOCUS       WP_176014839             436 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176014839
VERSION     WP_176014839.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..436
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=49606
     Region          85..397
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 maiqkikldi gtvyqkeegg vyyfryqvng arkaislktr nqkealkean kqipllkats
       61 teviaahvqh arglitpekn lplseawavy eksperatsa tvaeaqsyra tfqefldwlg
      121 apqknvrdit peigeqyaey mrnqkiavst hnrkikrlrr ifhvlreyws gsnpfhsatq
      181 lrrereereq dvrrlsftre qeqllqavld ddkytvmnkp evrvvyylgm ftgqrlkdcv
      241 llrwnkinfn lkriwvkqfk tgkevtipia pkllevlqga lawkagetdy vcpniaaryn
      301 ktdargknvg nnlvnidmlr virwigleps vavpgrdkkv tvygfhslrh sfasycaeag
      361 vpqatvlsil gadseivskf ythigdeaqr qaiaaisgei sgksaqqrin ealelirtst
      421 etsdevlkki railek
//
LOCUS       WP_176014887             509 aa            linear   BCT 11-JAN-2025
DEFINITION  excinuclease ABC subunit UvrC [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176014887
VERSION     WP_176014887.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Truglio,J.J., Croteau,D.L., Van Houten,B. and Kisker,C.
  TITLE     Prokaryotic nucleotide excision repair: the UvrABC system
  JOURNAL   Chem Rev 106 (2), 233-252 (2006)
   PUBMED   16464004
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Grossman,L. and Yeung,A.T.
  TITLE     The UvrABC endonuclease system of Escherichia coli--a view from
            Baltimore
  JOURNAL   Mutat Res 236 (2-3), 213-221 (1990)
   PUBMED   2144612
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417185
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..509
                     /product="excinuclease ABC subunit UvrC"
                     /GO_component="GO:0009380 - excinuclease repair complex
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0009381 - excinuclease ABC activity
                     [Evidence IEA]"
                     /GO_process="GO:0006289 - nucleotide-excision repair
                     [Evidence IEA]"
                     /calculated_mol_wt=58003
     Region          10..488
                     /region_name="UvrC"
                     /note="Excinuclease UvrABC, nuclease subunit [Replication,
                     recombination and repair]; COG0322"
                     /db_xref="CDD:440091"
ORIGIN      
        1 mselqkefhp gdvpqtpgvy vfrdrfakvi yvgkavnlrr rlsqyfqpsr tryadaklrs
       61 lintianwdf ypvrteneal ilesrlikey apyynilmrd dkrylmlkin lnepfptltl
      121 arvrkddryr yfgpfpngga lkstleflls hfglrtcrta qpddetrkrc lkrivkdcca
      181 pctgqvtpee yrqkvdqmls vlngnikels ailqqrmkea aaaqrfekaa hwrdvltnle
      241 tvfgeknrsf sraflpvesg eaavlalqea lrlpkpprhm ecfdisnilg tlavgsmvcf
      301 engkpardqy rrfriktvhq sddfammhev itrrykrcle enrplpdllv vdggkgqlss
      361 aiaalvecgc ppfpviglak qqekffgpgr pqsvrldrhn palrmlqamr deahrfaigy
      421 hrelrnkrlq qslldeiegi gpqrkkqlle tfgsvrelrk asvaevvqkv pgigetfaak
      481 vlaqlnrkap prtqppatkp eppaaapsq
//
LOCUS       WP_176014916             317 aa            linear   BCT 11-JAN-2025
DEFINITION  RHS repeat domain-containing protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176014916
VERSION     WP_176014916.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..317
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35627
     Region          <57..166
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mklinslkdw klhikqifkt gkntfilfgi mnlhktkspv mldaapltvf daaanktyfy
       61 qtdanknvtd ltdsagtiva hyeyspfgql vkssgayant nvftwsseyt dretgliyyn
      121 freydpklgr wlsrdpihkq gglnlyayis nktinhidkl glqnfgegfl pttidllpqi
      181 aeqetggegn sentscstqe ahlnkylfyf llmfkscaqf vgmeigpeqp pprpayeqti
      241 epanppsgss gpdpdpdpdp tpkptdpnpp kkppispgti diffipiphw wfqmqiyniq
      301 eqerrnnpch gnppyta
//
LOCUS       WP_176014950             253 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176014950
VERSION     WP_176014950.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..253
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27579
     Region          1..243
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mikvldkala mlemavvasp epvaisefek alginkatct riakeltaad yleqvsrkdg
       61 yragiralaf ggavryetel lrtaapllre caaawqasvm lcalrhgqry ilwhenpnpd
      121 lkiripalal rdlrgtaagl mllafagdae rravlqapfs egeeilkral ypddsleefl
      181 dgvkrrrelc fespfgwgvc sspvfrdgsc vaavslgmta aafeavdrsr lqeqvgriar
      241 eiscrisshv sig
//
LOCUS       WP_176014923             991 aa            linear   BCT 11-JAN-2025
DEFINITION  RHS repeat domain-containing protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176014923
VERSION     WP_176014923.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 991)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..991
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..991
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=110362
     Region          <21..820
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mkkssnamny yntkgqlikp vtpggvmtly tynvrgqlis eivdmdrdgt qstgdiatty
       61 tysfgtktld gqsvtvqvmt vttssgansv evrkteqtld glcswvtefg ktafsrteyl
      121 gdgevrltet davgvkkvtt qenglvtkee lfnsdgtagn vttytydqfd rlstvtekrg
      181 atvvntlann sydangnvls rtvngqsvsm aydnlnrlyn yllpgnrivn yefhltgelk
      241 kvsgaetytq eftynnfggm atlktwrtnt tpqvtswnyd trqrvkekiy adsrkvsyty
      301 tadnqplkrt wargvtttys ydnggrqtgi dysdatpdvs itydflsrpv tvtdgagtrt
      361 ytydntknll taetvpylad ttlnytyday grrtgqmlkt gstthqqany tygtdgryat
      421 isdggytahy thnaagqlst lrlatasnnq tvstatrsfn sahrltgvst tagsltknyg
      481 ytlnikdqri kttladgsyw dyaydnygqv inavrknasg giagqsfdys fdqignrqsa
      541 fqgttgsdsq wsytanavnq yslitepngt tyaqvhdadg nltgsyttqy tydaenrlkt
      601 advgtyryey tydylsrrir qkvilksgat gqtqsevayv ydgwnvvgvy dittatptfq
      661 kgylwgedls gnlqgaggvg gllaerrggq tylpvydgng nimsclnast kasvaeyiyd
      721 afgrtisssg aeadnftyrf stkpldgsgl yyygyryydp qhgrwisrdp ieenggvnly
      781 gfvgnngvde ydiyglkkcy rwmlitfyng qkkvapgqtp eppldefsaa vanqrytppp
      841 ensnkrnpdf lgndhpvnqp yptgtifhir rgrknndrrv vrdtgkgwam prspkssegg
      901 ltnneryalp kgvdpdewld lwtkkpdgrd pewdivilei gedcscpskw sendpppepd
      961 nmkkykegqk ekaeydkrka terwkkrnpg k
//
LOCUS       WP_176014911             431 aa            linear   BCT 11-JAN-2025
DEFINITION  S41 family peptidase [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176014911
VERSION     WP_176014911.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..431
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47620
     Region          54..418
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mttfgsflrp mpsagrvfll sllltaanll raepaaavae tafqkedpyp qimlltnvme
       61 ilrdnyvden kvtyerliag alrgmlreld pysaydtpee hrrnsddlng qqvglgvmvr
      121 kndyeavkvm avipnssaaq agiqagdwlv evdgfstlda tleecmrrls gpvdsevqlk
      181 vyreeedelh evtvtrcafa rnsvpsngie mlpggygyir iesftsntpa eldralkqln
      241 qksmhalvld lrnnpgglld aalavcdrfl gaselllfie grresdrevf yagdstvkyl
      301 nlplailvng hsasaaeivs gclkdhrraa ligektfgkg svqrvhqlnn agairftiak
      361 yytpsrnlih gvgiepdlev elpeeeelpl kllrepaglr mtledgsewn dtqlqealfy
      421 leketgansd r
//
LOCUS       WP_176014967             455 aa            linear   BCT 11-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176014967
VERSION     WP_176014967.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..455
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=50669
     Region          27..448
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 mgqynpapyq ldltqyphlv tetipgpksa alhrratryy rglsgqvrlf pvafergsgc
       61 sledadgnry idfssgiyvt tlghchpkis eavanyarql mnahdfttei kvrllekmae
      121 clpgdlknfq lydsgttave aglrtcraat gkhefiscfm dfhgksghsi glarmtrfsg
      181 sgrpegfyla prpdtyrpww trpdgsldte qylefydkfi resttgqvaa fvvepiqgwg
      241 gsimppddff pklrkflder gillfadevl tgmgrtgkyl cmehwqvlpd ivtlgkgfgn
      301 gfpvtamvvr tpyadavdki sastsyggnp macaaalacf evieeeglle haqeleklfr
      361 rrmsgwtsry rivgdtrvkg cllgvelvkd kqtkepyeea grlvyqkafr rglawipagh
      421 ilrmsppivm peevalkgmd lieaaiaete kellg
//
LOCUS       WP_176015021            1757 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-binding protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176015021
VERSION     WP_176015021.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 1757)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1757)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 1757)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 1757)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 1757)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 1757)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 1757)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418077
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1757
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..1757
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=200139
     Region          1386..1748
                     /region_name="HerA"
                     /note="Archaeal DNA helicase HerA or a related bacterial
                     ATPase, contains HAS-barrel and ATPase domains
                     [Replication, recombination and repair]; COG0433"
                     /db_xref="CDD:440202"
ORIGIN      
        1 mkyyiksvvn yidgqlkaip gtgnrfqmmi pslpaketle lanrldkycs gndihldfkv
       61 ahelaeewta qeqadvkvng ywvsgsltgl rnaintsdkn sllilvgsak vtdkgslsdf
      121 hqcdfynlwn aqlkqsfagw lddffnehni qfgeaeleqa dnilkelsar ydilkisafl
      181 enaeidgtsa keairellaq ldsfglpnls ncvyqskrke sfryysssak dffsynsfle
      241 pskredalkr idkfiseaqk diqpeqiasf eseeeffdal klyiaendag skqllnkcdf
      301 vfiwedilky kpkkektdkq tvkklygspl evflhaiyia lgkakthnit kvvltgkkfr
      361 hdccaddmnq sekaqqlltq mlggldafle kyiqifqnkd gdtteiscel lndtiayess
      421 ktgepyfefq vtleqlssed mdedfnfalc lpeihpyrla sdlitlahkn iaehnadwly
      481 pipvfhlnyy qelmaakded eicrillhci ndsdshpgat pfmenlftet wrtqhpdelk
      541 idlekiafdy kqfisnaknn gfysalreka salidsyhqa aehfvkeeky qnstklaaml
      601 fraflvigdh rnqdidiwgv rpyekdavit ilhpsliemv haqcvfltra fstlvneala
      661 sdkpsfkenr wqyyvdmaei qmplgglltd angvlsidvr gknllhriln khtdptssia
      721 trlitrydhi deddisdtei fketreskll lrilndyrvm hphardgicl avyrnddiqp
      781 vlsalnsylk kwinpdqmkn gqkyavslvl fsdfaddtgi anyleewqer weaaenedkl
      841 kyysycslsv ahrivsttnn raqfekilre dfdcdifvfy nfiaagqden kfkpvaaydn
      901 trdvlkfpil eksfcsqatp dekltrtqii snrqfrinad hteimarlkn qytktdqyhv
      961 ilgtgnfaew qriidaahea aewivcidan iddkllkeis ptykdqgker eligfgsgvg
     1021 vhgesnytis tqqfsfadlk inlrnnfknt fsygskaedi viveqlvgea qklsglsmir
     1081 algpsyyrcd llaysliykl lpltsgehlc nqifsidayr hwfdlsspdd kthpdllwmr
     1141 aditpsgkfa fkmtmieckm vkensavldk akeqiqngld vlikafrprv ngqevpdgry
     1201 wylqlhrlia csaknvqnee iflaamerls agdfeiswta gvfafwtdsk qpgmdeiecw
     1261 diesnnenye vqvysigyqf iknicngmes pirdwdgkmv tlkpssstat dieerpqdei
     1321 epeeeeeviv appviepvip edeppvssgn dsiddsasta dgndedgkti eqppavpgpq
     1381 heipqriflg kengrdfywe fghpklnnrh llifgssgmg ktyaiqtilc efgrqkqnsl
     1441 ivdytngflp nqlesatsna lrpgqrfvka nklpldpflk qkqdvgggyf iennsmdvak
     1501 rvtsifnsvy nmgdqqasil idaiydgves gqmnlerlmp iwesylddgv hkkgtvqtvi
     1561 sklkpfvseh pftneqnssw qgifddkqhl chvfqlagvd ketsrilief ilwdlyayac
     1621 nsstektpkv ivldevqnld qkleaplgki ltegrkfglc liaatqtlsn ldkdqqarlf
     1681 qaghklffgp napeanqyae lvmqvansgt keqwkaklms lqkgeclsig pvlnektgem
     1741 rvevhkikis slaergf
//
LOCUS       WP_176015039             654 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176015039
VERSION     WP_176015039.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 654)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 654)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..654
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=73247
     Region          7..533
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          578..643
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 midfaeiskg ygeqqlldav sfrinpgdri gvvgpngagk stlfgiitge lspdrgkvtl
       61 pkgqrigylh qqlpdyspgq tlldftadsm pelrrigeel heleqrlheg gvtdtetllk
      121 rhgelqtqfe hlggyhmrsd aesalcglgf attdferplk sfsggwqmrs mlartliarp
      181 dillldepsn yldipavewl crflngfrgt mllishdrfl lnkltditle inagqvtryp
      241 gnydfyrser enrrvsleaa krnidrkkke lqrnidrfrs ksskasqaqs wqkqldriqd
      301 vvvpdelsys gsirlpeppp cgaeaarleq vtfaypgkep tivdttlqid hgdkiaivgy
      361 ngtgkstllk lltgrnipqs grvvighnvv igyqaqefad llepeqsayd vvrgaarrdf
      421 plnmipgvlg sfgfsgddsh klckvlsgge kirlcfarif vnppnllvld eptthldiaa
      481 realqkvlqa yrgtlclvsh diefvrqvat tivamrppti kkyfgnydyy lqktaeenap
      541 aatagkaaek enivfdnsre krreraqkrq alaadkrrae qevtrlekql etleqeqkai
      601 iaqlssqasg ldfaelnkkl nglkleteqt tarweqafek leellalnaq ihqd
//
LOCUS       WP_176015054            1036 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176015054
VERSION     WP_176015054.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..1036
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=116577
     Region          <569..1017
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 maqsfegkll eassaevlka akqllkssrl acayrdetgs inavfqegnh yahtvvqlge
       61 pptavcscgn hgdslcahav asimycgrfr steiapindg varyagikde sleslagrgt
      121 apaeaqlfiq aesdfphvps kwenvaltvk lragnrdyvg nvnnlrqlyf dkalaitlkl
      181 nqfslqdrqi ihflavnaea ensqlllnse vtaeffhsli gfdrfsrngr rlivhrehae
      241 pvvlkkrign evmlspgivv ggaplsihsa kvivgrsgcw igrqgeywwm patldigwlr
      301 nffrtgeqkr qyneyqklia dggfpvrlld vesfepekkp ctvllsgnls lenglrlktn
      361 ylydnviypa dhgrlsrdgr kfwlrdeeme qsfanelkmf gfaehgaelq lddsetigvf
      421 ldqvlpmwlt qrpnccltae larlcrggsg lpgammqctl aktlsdryvl nyqlecygqg
      481 igfqqalkav knhrrylqla nnhmalldes fgnfllaaen viqkvdekkm tfelprcavh
      541 ywkhiarntp evipeefqll aspgaaapqe lpdppaaefk gelrgyqqeg vnwmrqlldn
      601 sfnvvladem glgktvqlla llagrktkkd apiliicpas lvenwkrecg kfvpgfrvav
      661 lncggrdeiw qhamdydliv gsysitrlda ealkslkfsy lildeaqhik npntanaqnc
      721 kairadhrlv ltgtplenss edlwsifdfl hpgllgsfns fkkyygnlrd npalqqdlaa
      781 rvtpfikrrt kahvcqelpp kqeytlmcem eveqrrlyde ilrhgreqlk alpkndnran
      841 feilttllrl rqvcchpdll peagknvvsa kfellkelin qhidsgnkml lfsqftslls
      901 lirdwldaeg iryeyldgat rnrqqrvdsf nntpeiplfl lslkaggtgl nltsadtvii
      961 fdpwwnpave lqaadrthri gqtkpvtsik llvkdsieek ilalqdkkqe ifdniienpa
     1021 anadklslee lkflfq
//
LOCUS       WP_176015070             533 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176015070
VERSION     WP_176015070.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..533
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=60515
     Region          54..464
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkicrtlvgv gaagmvllag cksfdeyqdd riayavkhfe raqysnidse kvltlnkcva
       61 lavqnnldlk vfgleenvak emrtsemlgm lpelnvsnnl tgrtntpass sqqlhgegsg
      121 tysysqsqar nvnylnvdla lsvldfglaf fntqqandrm llrqqiprra eqnlvldtvr
      181 vyfqvaaaqr aidittrlle dckdryelie qmgesgqisp frafdevrqf idmekrltny
      241 irsydnscve lrsllglypn trikvddsil dqvpeftlpe melmeqialm krpelyeidm
      301 qkhinvlecr ktiammfpnv rmfvdftnsd nsflyhsaww elgiraaynl lrlpqqisry
      361 qaysaqvdae earsyaqaig viaqvriaha dlvsvkeryn idvrvnaayr knlakaeasd
      421 eisgelsqle lahmrlatte teiekylslg nyyvsyfrll ntlgiedlha atveglknql
      481 deeriraeae leearaeyes eqanveadse qaeiteaeeq ldvavsppte par
//
LOCUS       WP_176015136             399 aa            linear   BCT 11-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176015136
VERSION     WP_176015136.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..399
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=43642
     Region          7..397
                     /region_name="ArgD"
                     /note="Acetylornithine/succinyldiaminopimelate/putrescine
                     aminotransferase [Amino acid transport and metabolism];
                     COG4992"
                     /db_xref="CDD:444016"
ORIGIN      
        1 msgslyqtiv ekyqhyimpt yapktllvrg egawlydadn rryldfacgi svcnlghchp
       61 avteaiqrqa aklvhisnly fnevtpilae kliragmdgv vffcnsgaea negmikfark
      121 wgseqgkhei ismhdsfhgr tlatlaatgr skyrkgfapd mpgfrqvtfn dfaeleaavn
      181 ehtcaillep vqgeggiipa dreylkkvra lcdarkilll fdevqcgmgr tgnlfayqtf
      241 gvepdalsma kaianglpmg afivkrqyan tlqpgmhast fggtplvsaa alavlevier
      301 enilancrkm aaflqenlek ltqkyafvka vrscglmigi vldreaaavl plllkngmia
      361 ltagetvirl lprlnltqee aeyglailek sldeyaagl
//
LOCUS       WP_176015177             231 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176015177
VERSION     WP_176015177.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..231
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=24995
     Region          5..88
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mkptftlvel lvviaviail aslllpalqt arskavtihc lgnlkqqgma yfsytadwnf
       61 tppvsksgvr wvdllvpylt akseqsagnv fvcaadsrpe drkvvygssd vnklsyginq
      121 cyskgyenqn ayklwygina gliatpsefv tvadagayyi gttiasplfg dvggetgvad
      181 gfcknlsfrh pgaahnfnaa fadghvstlk fesapyrywd crnawdgtfd d
//
LOCUS       WP_176015181             256 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176015181
VERSION     WP_176015181.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..256
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=27783
     Region          3..>62
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 mtkknftlie llvviaiiai lasmllpalg kakataqmik crsnlrqcal fanmyqldyd
       61 dyligywtyp aeafggqpas awiswqvtlq hfygapkelf lcpssssasw deadnpiapk
      121 qpnttiglnf gtfgysfshg darhvkaatv lsnckdgnmp lyfadtpsss lngsgthyag
      181 dyfnvtsvnt slgndsfftg gnqcdrwypm aaihsgmrvn aafmdgsvng ltpaeicadw
      241 qkycrpvqvg gawmae
//
LOCUS       WP_176015151             435 aa            linear   BCT 11-JAN-2025
DEFINITION  S41 family peptidase [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176015151
VERSION     WP_176015151.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..435
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47397
     Region          35..426
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mkikgifrva wlvcwlalpg maagaasvrq eraqrvldev wsqlaaqnfe pdfnekfrep
       61 vyekfqpevl saaddaelag vldrmvhqlg vshlkvlppl giqafsalea arrpprndgt
      121 enwdlsvpgd pglklieaen avavwrvwpe saaaeakiet gelvlaidgi plladkdtpl
      181 gwamigqall tgppgssvav rlrnaagaer evtltrqrmg tkflefgimp rafldywsew
      241 lpgdilyihf safypeavkr lrydvskryp garglivdvr nnaggiltmg qwvvswcapk
      301 vlplgemtia qtslkleswp qqqtfrgpva vllnrdsyst aeifagclqd aagavlfget
      361 sagmclpsnf vllesgfrlq tvvgsyvrpa ggeieglgve pdrvvpvrld slrsgkddvv
      421 daaaeylrse lgtqp
//
LOCUS       WP_176015228             430 aa            linear   BCT 11-JAN-2025
DEFINITION  ammonium transporter [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176015228
VERSION     WP_176015228.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..430
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45551
     Region          22..425
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mkilallfls vavlplaate tadtvavfta dnlwimiagm lvfmmhlgfa avesglsrak
       61 nctnilfknt lvppigilty alcgfslmyp gsnwvvghvl gfqglgiadp gsgmaynghy
      121 tywtdfffqa mfaataativ sgavaerikl nvfliftliy vsivypvvgs wgwgggwlae
      181 lhfhdfagst fvhsvggwaa lagviligpr lgkyvgnhsm pfmghsmpla tigvfllwfg
      241 wfgfnggsvf saapdqvslv lvtttlgaca giiaamltaw tllkkpdlsm tlngclaglv
      301 gvtaaadcit paaaviigav sglivipavl ffdrrhlddp vgalsvhlvc giwgtlavgl
      361 fstnpeysfk iqllgviavg vvtfpsafli fyllkrtigi rvseeeelrg ldlgehgmea
      421 yagfqifsnq
//
LOCUS       WP_176015264             219 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Victivallis sp.
            Marseille-Q1083].
ACCESSION   WP_176015264
VERSION     WP_176015264.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Upton,C. and Buckley,J.T.
  TITLE     A new family of lipolytic enzymes?
  JOURNAL   Trends Biochem Sci 20 (5), 178-179 (1995)
   PUBMED   7610479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..219
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=24168
     Region          6..212
                     /region_name="SGNH_hydrolase_like_2"
                     /note="SGNH_hydrolase subfamily. SGNH hydrolases are a
                     diverse family of lipases and esterases. The tertiary fold
                     of the enzyme is substantially different from that of the
                     alpha/beta hydrolase family and unique among all known
                     hydrolases; its active site...; cd01834"
                     /db_xref="CDD:238872"
     Site            order(15,64,93,193,196)
                     /site_type="active"
                     /db_xref="CDD:238872"
     Site            order(15,193,196)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238872"
     Site            order(15,64,93)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238872"
ORIGIN      
        1 mklkqgerlv fagdsvtdag rnhpvaagtl fdplgkgypn ivsgwinavy palginvina
       61 gtggntsrdl rqrwdneils vrpdwlsimi gindiwrqfd spaqpelhih pteyeanlda
      121 mlaaakskvq ggiivmapfy lelnradaml altlqyaaia ramaqkhetl fidtqahfdr
      181 llasrhpnfi awdrvhpnnv ghtllarafl eaidfdfka
//
LOCUS       WP_176015278             505 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176015278
VERSION     WP_176015278.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..505
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56815
     Region          93..474
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mltslknrir swlgiaqpav ptvgtarpav knrpaagkss knkrteepat rpprrsvrsg
       61 ekkprqlpal gqktrilpvk paallevpev egktrfldlp ihqdilfglq emgfqyctpi
      121 qaqslpvlla grdlagkaqt gtgktaafli aaftrllnqp lperaagycr vlvmaptrel
      181 aiqihkdaek iaafanlnnv vvfggmdhek qrrsldqpvd vligtpgrii dfargrslnl
      241 skteiliide adrmldmgfi pdvrriiaql pgrekrqtmf fsatlddsil rlaqswlreq
      301 tfiesepeev vgktieqify taaireklpl llyfirtqhf drmlvfgnrk dsnlslqhql
      361 srygvkaall sgdipqekrl riledfrsgk ekiviatdva argihvddvs vvinydlpeh
      421 pedyvhrigr tgraghlgks isfvceygay vlpeiekfid mqfhcvwped emlvlpegqe
      481 nwdrpepaap rkrssrsprr srarr
//
LOCUS       WP_176015282             194 aa            linear   BCT 11-JAN-2025
DEFINITION  flavodoxin family protein [Victivallis sp. Marseille-Q1083].
ACCESSION   WP_176015282
VERSION     WP_176015282.1
KEYWORDS    RefSeq.
SOURCE      Victivallis sp. Marseille-Q1083
  ORGANISM  Victivallis sp. Marseille-Q1083
            Bacteria; Pseudomonadati; Lentisphaerota; Lentisphaeria;
            Victivallales; Victivallaceae; Victivallis.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Victivallis sp. Marseille-Q1083"
                     /db_xref="taxon:2717288"
     Protein         1..194
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=20939
     Region          3..>141
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mkkmlvlygs grangntatl tklvlsqlpa gsveveeidl rklenkfggc sscygcqkvg
       61 nyrcvqkdet aalinrlpef dlvlfaspvy ffnfsaqtka fmdrlmallk headgsmstp
      121 larmkfayvm tsggdendsg vetakvcagy laefaamppp qffyrgncvd iareiagdps
      181 laaaaaqfae elvk
//
LOCUS       WP_176015344             282 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: class I SAM-dependent methyltransferase
            [Burkholderia].
ACCESSION   WP_176015344
VERSION     WP_176015344.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..282
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29862
     Region          52..146
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 meanrpneaq salwngpsgr awvdaqalld rmfepfetll adgaaassas svldvgcgtg
       61 avtlaiarrl ganaqctgid isarmidaar gragrsglpa rfvcadvqth afepasvdli
      121 vsrlgvmffd dpvrafanlr haarpgaqmr fvawrgaadn pfmttaeraa apllpnlpar
      181 qpgapgqfaf gdrqriasvl sdggwadvai epveracvls esalddylar lgpvglalle
      241 tdeatrrrvi dtmraafery vhgaevrfda acwlvtarap sa
//
LOCUS       WP_176015372             227 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia sp. BCC0398].
ACCESSION   WP_176015372
VERSION     WP_176015372.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..227
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23986
     Region          23..225
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mtdvlsltte pesglqyrlr patgraaarl lllhgvggne tnllnvadti dprieiaflr
       61 gpltfgpnqh awfpvrfgpn gpeidaarad esrmqlitll hafrardgaa palptviagf
      121 sqggimsasv gltspgdvna favlcgrvlp eidpliaprd alstlhalvm hgrfddklpi
      181 awadtadakl talgvahdtr lyaaghelta emagdfgrwv geragln
//
LOCUS       WP_176015386             135 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF427 domain-containing protein [Burkholderia sp. BCC0398].
ACCESSION   WP_176015386
VERSION     WP_176015386.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Lupas,A.N., Zhu,H. and Korycinski,M.
  TITLE     The thalidomide-binding domain of cereblon defines the CULT domain
            family and is a new member of the beta-tent fold
  JOURNAL   PLoS Comput Biol 11 (1), e1004023 (2015)
   PUBMED   25569776
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..135
                     /product="DUF427 domain-containing protein"
                     /calculated_mol_wt=14768
     Region          9..129
                     /region_name="COG2343"
                     /note="Uncharacterized conserved protein, DUF427 family
                     [Function unknown]"
                     /db_xref="CDD:441912"
ORIGIN      
        1 msinpdtpsr pvkspgpdhp iliephssrv ivqvagkvva dtrhalvlre asypavlyip
       61 redadmslle rtdhatycpy kgdcayysip aggerstnav wtyehpnpav esirghlafy
      121 pdrvdsiees llvta
//
LOCUS       WP_176015442             138 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC0398].
ACCESSION   WP_176015442
VERSION     WP_176015442.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..138
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14846
     Region          1..125
                     /region_name="COG3607"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]"
                     /db_xref="CDD:442825"
ORIGIN      
        1 mhkmvfinlp vadlpraktf yqalgfevvp aytneqaaci kisdtifaml lvrpffqtft
       61 dktiidpath iqvlsclscd sraevgtlva kalaaggaap qapreypnmy ghgftdpdgh
      121 twelmample asaqgqas
//
LOCUS       WP_176015460             783 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC0398].
ACCESSION   WP_176015460
VERSION     WP_176015460.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 783)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..783
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=86254
     Region          1..733
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msmilpsqay elklaphpap fsilkfsgld rvsqlyrydi eftspaagip mdqvlgrpak
       61 fvvdpvdpdm dylrkmfgen aaqfsakpsa ytvhgvitqf deletsadet ryrvvleptl
      121 adlargvtsr lfqkqsvdei vtgtlrhygy ragvdfrfql rgqykrreyv tqyhettfaf
      181 iqricaeegi wfrweqkkdr avvvfgddld ayarkqrtvp yrresglesv gsdaiktlgr
      241 emkrvpeavr lhdynhrqag vsllveenaa rddttthsvd yrwgehyetp eegkriarlr
      301 heaylagqit fkgtgnpfwl eagevmrvep kpadakhgvf vtsveshggr nesywvafeg
      361 ipsdrvwrts mgsisrpvvd gilparitsp gnykyaylte qgwyviklpf dldewspggt
      421 srpvrfakpy sgdnyghhfp lidgaevaiv htdgdpnrpv iigamhdsvh pdlvnnlnht
      481 rnlirtaarn elrmedkegv ehihlttptq tselnlghmv ddarhergqg aelrtdghla
      541 argpkgmlls teaqvgaagh qldmkdahaq lqraidrmes lseavraaea tvaelqqqks
      601 fyaealdglk raailasaps gigltsgehl qlnadrnlia taggnfdvgv mrnftvaagk
      661 qvslfaqaqg vrvtaakqdv vvqartgama lsaskdlnft ssegailaas rgaltlasgg
      721 aylkidggni elgcpgditl kcgnfhwtgp asldtrlpnm pigpckecll dahrgveamt
      781 eva
//
LOCUS       WP_176015481             220 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC0398].
ACCESSION   WP_176015481
VERSION     WP_176015481.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122607
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..220
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24761
     Region          8..79
                     /region_name="GST_N_1"
                     /note="GST_N family, unknown subfamily 1; composed of
                     uncharacterized proteins, predominantly from bacteria,
                     with similarity to GSTs. GSTs are cytosolic dimeric
                     proteins involved in cellular detoxification by catalyzing
                     the conjugation of glutathione (GSH) with...; cd03043"
                     /db_xref="CDD:239341"
     Site            order(19,21..22,24..25,28..29,72,75..76)
                     /site_type="other"
                     /note="putative C-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(19,57..59,70..71)
                     /site_type="other"
                     /note="putative GSH binding site (G-site) [chemical
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(57,69..70,72..73,76)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239341"
     Region          92..205
                     /region_name="GST_C_3"
                     /note="C-terminal, alpha helical domain of an unknown
                     subfamily 3 of Glutathione S-transferases; cd03194"
                     /db_xref="CDD:198303"
     Site            order(95,102,163,166..167,170,174)
                     /site_type="other"
                     /note="putative N-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:198303"
     Site            order(95..96,99..100,103,139)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:198303"
     Site            order(102,106..107,110..111,171,174)
                     /site_type="other"
                     /note="putative substrate binding pocket (H-site)
                     [chemical binding]"
                     /db_xref="CDD:198303"
ORIGIN      
        1 mesnarttlt issrnyssws mrgwllakls glafetisvp idatsraell llspsilvpc
       61 lthdgnavwd tlaiaeylne irpqarllpd erharahcrs icgemhsgfs alrsalpmnl
      121 rghfpgfriw sraqhdieri vtiwreclae yggpwlfgae igiadamyap vvtrfltydv
      181 klepdvteyc mrvlahpfva ewidaakaeh edideldmef
//
LOCUS       WP_176015506             285 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Burkholderia].
ACCESSION   WP_176015506
VERSION     WP_176015506.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..285
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31196
     Region          9..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(32,57)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(39..40,51,54,58..59)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          105..270
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 madasdnllg aylrdrrekl dptalglpat rrrtpglrre evaqrahvsa awytwleqgr
       61 ggapsadvld rlaralmlnd aerehlfllg vghppevryh apasvtprlq hvldsldasp
      121 aivrtatwdv aawndaaaat ltdyatlppa arnilrlifv dagvryaqpn wervarfavg
      181 afradvarsg atqsvqafvd emratsaefd amwrdhdirt hdegtkeirh pqagrialey
      241 safsvtgspd lslviftpvt padrarirel vaareqarav qapaa
//
LOCUS       WP_176015517             418 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia].
ACCESSION   WP_176015517
VERSION     WP_176015517.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 418)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 418)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..418
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45062
     Region          <195..412
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mtiapsspst aalkrelkaa esrkrtmall liaplaifll lifvvpigtl ltravqnpei
       61 atalpntvaa lsgwdrktpp adaayvalaa dmtkvadsea mgalarrlnt eipgyrslva
      121 ktaramplkg dndaaltpaq trakfidlda rwgdvaywqs iakngsqvsp fyllaaldhk
      181 qdgfghivqa dpdqsiyvai fgrtfvigva vtlfalllgy playwistls erranlvmil
      241 vlipfwtsvl vrvaawivll qseglintal lgsglishpl tllfnrvgvy ismthillpf
      301 milplysvmk sipptyqraa vslgshpfaa fwrvyvpqty pgvgagallv filaigyyit
      361 pallggpndq mvsyyvayft nvtinwgmac algglllaat lvlyavygrf trtnvslg
//
LOCUS       WP_176015704             280 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [Burkholderia].
ACCESSION   WP_176015704
VERSION     WP_176015704.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472037
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..280
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=29607
     Region          70..223
                     /region_name="TadD"
                     /note="Flp pilus assembly protein TadD, contains TPR
                     repeats [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG5010"
                     /db_xref="CDD:444034"
     Region          155..185
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          190..215
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mkrigeavtr agmlavalll gacatkesgy gvgaqteraa lmqaadqkqs vpdtpgmylg
       61 liqrmqaqgl yyaslahida ydktygvmpe sillradalr mtdqpaasaa vyaqllktpl
      121 aargyrglgl lagaagdfdr avqaltqase laptdpslls dlayaklrsg dvvgarvplm
      181 kaaeldqrnp kivsnlalyl faagraqdaq rlmnqqhlsp eirkdingda akiaaavraq
      241 qraiatppvv srpgattpit pmannfgydq tvpllqrfsq
//
LOCUS       WP_176015640             332 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: phosphotransferase enzyme family protein
            [unclassified Burkholderia].
ACCESSION   WP_176015640
VERSION     WP_176015640.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..332
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=36798
     Region          9..287
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mdslavtfde irdayglgrg gpptqvserv whlptssgag vavkryapeh haralketav
       61 lahlethgdt rfhvqtlkrt tsgeslwsgq hshamltrwe agqfktydtf sppewdvlga
      121 slaalhlsle qlplpsldti rarltaidad avrrslldal dradanaada tnlrryvdla
      181 lrmldryypg svdafpaddp qhpihndynq fnylftgtlp plivdweasi gapreyelvr
      241 clnhlpleap hlaqafvray lrvrpanpay iawavdaacv qhalklwivq gwlddpsrfa
      301 shlngamtma samvdardrl idffsrcvea gs
//
LOCUS       WP_176015721             817 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia sp.
            BCC0398].
ACCESSION   WP_176015721
VERSION     WP_176015721.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 817)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 817)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 817)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..817
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=87070
     Region          1..803
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mlvvgsqsqa tefnssfldi dgtrnvdlsq fsqadftlpg eymldlqvnd lylglqpief
       61 vavdatgagk pclrpelvar fglkpslvkd lprfrggscv dlaaiegatv rylksdgrlk
      121 itipqaalef tdstylppeh wsegipgaml dyrviantnr nfgagggqtn aiqaygtvga
      181 nwdawrfrgd yqaqsnvgnt ayadrtfrfs rlyafralps iqstvtfgdd yltsdifdtf
      241 altgasirsd drmlppslrg yaplisgvar tnatvtvsqa grvlyvtrvs pgafalqnin
      301 tsvqgtldva veeedgsvqr fqvttaavpf lartgqlryk aavgkprlfg gagitpffgf
      361 geiayglpfd vtayggfiaa sgytsialgv grdfgafgav sadvtharar lwwngatrng
      421 nsyrinyskh fdgldadvrf fgyrfserey tsfaqfsgdp tayglanskq rysatlskrf
      481 gdtstyfsyd qttywarase qrvgltltra fsigtlrnln vsvsafrtqs agasgnqfsv
      541 tatlpiggrh tvtsnlttgn gstsvnagyi yddpagrtyq vnagetdgra sanasfrqrt
      601 sayqltaqas tlanayaaas levdgsfvat qygvsahang nagdtrllvs tdgvpdvpls
      661 gtlthtdsrg yavldgispy nvydatvnve klplevqvtn piqrmvltdg aigfvkfsaa
      721 rgsnlyltlt daaghalpfg asvqdaangk elgivgegga afltqvqpks alavragert
      781 lctidalpnq lqlegtpipv tcrtpgesha aaarver
//
LOCUS       WP_176015729             222 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: (2Fe-2S)-binding protein [unclassified Burkholderia].
ACCESSION   WP_176015729
VERSION     WP_176015729.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..222
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=23568
     Region          46..216
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mttaqtaasa asagaasaas asvpvapaal aaapverplv rfqqkplsln ingksvgpmq
       61 vpeglmmief lheylgltgs rlgcgqgich acvvivdkpd gtsdemrtci tgahffhgrs
      121 irtieghakr neagevvels piqqkflehf sfqcgyctpg fvnaatvlie rlkrepiaka
      181 dvertitdal dahlcrctgy vryyeavkdv vlttpglvke aq
//
LOCUS       WP_176015749             909 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: type VI secretion system Vgr family protein
            [unclassified Burkholderia].
ACCESSION   WP_176015749
VERSION     WP_176015749.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 909)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 909)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..909
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..909
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=98872
     Region          1..801
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 malfdaprtl svsgaalply agqsiltpvk ltggetvgel feytlelktp dalgfsqsia
       61 anvkldtlig tevtvsiqle gkgrfipgla gnagmanlga gareitgivs hatlvredgr
      121 sivyaltlrp wlwqatkncd crifqdmsvv eitdavlssy pfpvekrltt prpnnawpkr
      181 diqrqhfesd wtflqrlwee wgiyyffehg egkhrlvlcd smgalkplgd ayaalryepp
      241 tgrrldeehi qdfsvshalt agavtsvdyd ytlpradlkv tredprdtgl ahqehytwgd
      301 yaqpqagaag lsgdhneprt eaeyltlvqm earrcqglra ygkgnlrgmv agqtfvlshy
      361 pqdaanreya viackltiee igeasgsgqr yrceadftvq ptiepfrllr tiakprvngv
      421 eyavvtcpen qeiwtdaygr vklqflwdrl gnndersscw vrvagawhgd qfggiflprr
      481 ghevevafvn gdpdlpiivg raanafnmpp falpknqtla gyrsrevggr rantlafddt
      541 ngkiqahlss degtsqlnlg yitriagnag rqdergrgae lrtdgkaavr gaeglllttf
      601 srpaangdaf svdeidaqls esqelaegla htaqsvhahd geqttivtsl kaqanairgg
      661 gklnqfrdpq lvlaspagiv astpeqihls sgraaavtvg tdmsvstggg lfasmrkalr
      721 lfvyqagmrl vaaagdidlk alkdsinlla klnvtvvadr irisaqqeve isgggsytrw
      781 rageitsgtn gnfevhsagr iftgpdnkss plvldapelp enlhftlgal pgaanryvde
      841 pyelfkgtak igegvtdefg rvivmnhqpg tsayrvklsn ggefnlkvrd alnhdpehvd
      901 lrsnrgerv
//
LOCUS       WP_176015791            1613 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD-glutamate dehydrogenase [Burkholderia sp. BCC0398].
ACCESSION   WP_176015791
VERSION     WP_176015791.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1613)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1613
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..1613
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=179114
     Region          4..1610
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 meakneevva hllsdvvefa rarlpdatfr ivelflrhyy dfvdaddlqs rgiadlygaa
       61 mahwqtaqkf vpgserlrvy npileqhgwh sdhtvieivn ddmpflvdsv tmainrlgla
      121 lhsalhpvfr iwrgagggie rvdaggatsg dgqsqlasfi hfevdrcgda alldtlredi
      181 arvlgdvras vedwpkivdi aratikemka restaediea raflewmaad hftflgqrdy
      241 alvsdgtgfg lrgiegsgfg ilreslrtsg aadvtplppa aadiitgawp ifvtkansra
      301 tvhrpgyldy vgvklvgadg kvtgerrfig lytstayfgs yteipivrrk canivrragf
      361 lpkghlgksl vtvletyprd elfqadedrl ydialgilrl qehqrtrlfv rrdrfdrfvs
      421 clvfvprdky ntdlrrriak llvdayngvn veftpllses alarihfvvh aepgtmpdvd
      481 treletrlvq vtrrwqddla dalldafgee qgnrllqrya dsfpagyrdd ypartavrdi
      541 eliervkdsg qlamnlyrpi eaeprafrfk vyragdpial srslpmlehl gvrvdeerpy
      601 riqtqdaaha wvhdfglela ddtefdierv kglfedafdr iwsgriendd fnrlvlrahl
      661 sarevtilra yakylrqvgs tfsdayiera ltgnpaiarq lvelfllrfd prigdtrdvq
      721 aerllkaieg aldqvpnlde drilrqflgv inatertnyf ladangeskp ylsfkfnpak
      781 vpglpepkpm feiwvysprv egvhlrggrv argglrwsdr redfrtevlg lmkaqmvknv
      841 vivpvgskgg fvvknpppqs dreawmregi acyqtflrgl ldltdnlagn aivpppdvvr
      901 hdaddpylvv aadkgtatfs dyanaishey gfwlddafas ggsvgydhkk maitargawe
      961 svkrhfremg vdtqatdftv vgvgdmsgdv fgngmllsph irlvaafdhr hvfldpnpdp
     1021 atsfaerqrm falersswad ydtsvispgg gvyprtakti plspavqsal gidahalppt
     1081 elirailqap vdllynggig tyvkaareth tqvgdranda vrvngadlrc kvvgeggnlg
     1141 ctqfgriefa qrggrintda idnsagvdcs dhevnikill glvvsdgemt ekqrnallae
     1201 mtdevgllvl rdnyyqtqal siagryavel ldaearlmrw leragrlnrv ieflptddev
     1261 aerqaaklgl tsperavlla yskmwlydal lesdvpedpl vaamlvdyfp kplqqrfsep
     1321 mrrhplrrei lathltnalv nrvgcafvhr lmeetdaqpg divracimar dvfdldavwr
     1381 didaldnrva ddvqarmfvd varlleraal wflrhlqsga vadggvagli arcrdavqri
     1441 apqlpsllpa ddlealserq rvlvdagvds alavrvasgd isaalldiae vaatcnrsle
     1501 lvagvyfslg tllnygwige raanlptpth wdmlaraaal aevarlkrtl atsalaespd
     1561 sttpdtivga wrvrreaala ryehlladlr asggtslavl lvvvremavl era
//
LOCUS       WP_176015814             486 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC0398].
ACCESSION   WP_176015814
VERSION     WP_176015814.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..486
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50465
     Region          31..475
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,156,
                     159..160,163,226,229..230,233,301..302,305,333,337,
                     390..391,395,399,415,418..419,422..423,426)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtnhtlapca pagaaaaatp rshhgwalvv llvgailppl dyfivnlalp airdgigarq
       61 aelqlvvsay acanavvqit ggrlgdlygr krmfmvgmag fvlastlcgl adngtvlvgg
      121 rvlqglfaai lapqvlatir svfspqeqvr vmgfygfafg laavigqlgg galislhpfg
      181 lgwraiflvn lpigilalig swrfipenra prgqridvpg tvlmslfllm ivyplthgre
      241 agwplwmiac gigalpmlga llavearrla rghdplldvr lfrnpvvalg lllaflfyml
      301 safflsygiy lqgclnwspl asgfailplg lgflaspllt trlvarfggy rvltlgfaml
      361 aagvasaaal ardgapgpgf yagiaaigig qglvlpsvvr ivlaevdaar agvasgmvsa
      421 mlqigaavga atiggvffar lgvhpaaldy vqgfrasmft ltivlvgcia lsmalgpmhr
      481 rlhada
//
LOCUS       WP_176015851             393 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC0398].
ACCESSION   WP_176015851
VERSION     WP_176015851.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..393
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42629
     Region          1..383
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mtyeltddqi qirdlirrva rervaprade idrtaeyphd ifallkelgl ftlpfpeayg
       61 gagsvmsaci aveefgrvcy ntgyllvvqw tpfgailegg teeqkarllp glacgdlrga
      121 lsiteaqsgs dvsgirttar rknggyvlng skiwctnshi adfilvaakt ldeqgqplgi
      181 nlfivdrhtp gltigneedk mgargvpscp lyfddafira ddrlgpegsq gfkvamealn
      241 tsrpivaara vgiaqgaidh avkfiqdrva fgqaisdfqg vrwmiadmvt qteaarqlvy
      301 rtaslvdagv sgrelapmaa makmfasdva mkvatdavql fgaagisney pinryfrdak
      361 vvqiiegtnq iqrnivadnv lgrirknqer qpg
//
LOCUS       WP_176015856             509 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Burkholderia sp.
            BCC0398].
ACCESSION   WP_176015856
VERSION     WP_176015856.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..509
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=55942
     Region          4..509
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mrtlgemier narlhgdhta lvyaerrlth aqlaerarrl sgalyerglr rqdrvailam
       61 ncaeyyetyr acewagfila tvnfrlapae ilyilqdaap kalvfeaqya tvvdglraql
      121 pgieqyicig dtpawavsfe avmeagsveg ppirsnpedy aylmytsgtt grpkgvvrtq
      181 qamcvtaesc alvsefsgnt rvlqttpafh vggigfvnsv awmggttvvh rgfepkqmle
      241 tiaqeritft fmvaamlqav ldvpelstyd vssienivta aapvppplla rgidalgpvf
      301 svqygmtesn acwlpahevk phgspeevrr lasvgrpcpg idlrivddhg ndlpqgqtge
      361 vwlrsktqls gywnnsvatv ealrdgwyrs gdmgyqdkdg yiflvdrkkd miisggeniy
      421 srevedvlaq hpavvdvavi gvphaqwgec vkaivvlrrg eqaseaqlie fcraliasyk
      481 cpksiafvde lprlptgkis kvmlrkqfa
//
LOCUS       WP_176015872             363 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia sp.
            BCC0398].
ACCESSION   WP_176015872
VERSION     WP_176015872.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..363
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39537
     Region          178..362
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mqmngvvpst widdvyaaal gdqrweavld glrlsvgvrm atllsfddaa rlpaieraag
       61 ddpswvaach rryntefyly dpvvpvaadw qagrwfedvr hlsvrqrthg vfyreflqpf
      121 glgsisglyi hrgagasafl svqsglesqg lsdeqrrtie imgahisral riharigele
      181 arvaaaesal davpvpvfll gaqrelrytn raaeqliaae palrilngrf apegcvddaq
      241 wrhafarggl llrratgepl plalipvpeq srlarerpgv aalmtaadlr spsaraqrlr
      301 vfyglssaea dlavllccdg rspqecaalr gvsigtvraq iksiytktdv araaqltslv
      361 mqt
//
LOCUS       WP_176015906             193 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC0398].
ACCESSION   WP_176015906
VERSION     WP_176015906.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..193
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20535
     Region          1..138
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtrktdarar aiataerlfr iqgytatglt qileesgapk gsfyfhfprg kaqlaeeaid
       61 qyvtnriavl qnisaettgh aldfvrrlfs tfaaemvaad fqygclmqnl anelpaldae
      121 ltervargfa dsteviaahf rgcgfasara ssaaaalvaa legartiarl erspavfaal
      181 advsgqgwga tee
//
LOCUS       WP_176015947             343 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC0398].
ACCESSION   WP_176015947
VERSION     WP_176015947.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..343
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34947
     Region          11..342
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mlemtsdrsq aderaarqrr rdliqkfaal gslvvlvfaf sissaaffsv dnlmtvglqv
       61 tsiaylgvaa tcviitggid lsvgsvlala gvcaallvka gvpvpaamaa gilvgalcgl
      121 vngicvtqmg lppfiatlgm mlvargialq itgarpvsdl gdafgalgng allrishiga
      181 dgfpdttfpg ipypvvimvv lfvvvsvlls rtslgrhiya vgsnaeaarl sgvnvqgvkl
      241 ftyvlsgala gvtgcvlmsr lvtgqpnegv myeldaiass viggtslmgg vgtisgtaig
      301 afvigvlrng lnmngvssfi qqiiigvvil gtvwtdqlrn rrp
//
LOCUS       WP_176015990             751 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Burkholderia sp. BCC0398].
ACCESSION   WP_176015990
VERSION     WP_176015990.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 751)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..751
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..751
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=81464
     Region          43..744
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mnspleatpd arrdttsagr arapegtfel srkrvdeldt ifgvggllar aldgyrprts
       61 qiemaravas ameasarrmp epeifetrkr parrlgdadk pggpaaehaa atesdsdagd
      121 ntliveagtg tgktyaylvp amlwggkviv stgtkhlqdq lfqrdiptvr nalavpvtva
      181 mlkgranylc hyylqrtadn grlpsrqdta ylqeivrfak itksgdkael asvpenapvw
      241 smvtstrdnc lgqecphyke cfvmqarrea qqadvvvvnh hlffadimlr dtgmaellpn
      301 antiifdeah qlpetatlff getlsttqil elardtvaeg lshardavew vklggdlera
      361 ardlrlafan dqivrmslaq lgddhpmfga ldaldaalda lasalagqae raeslgaclr
      421 rarelqdlla gwvapgatea aaqadaaaag dkaaaegdpn ekvrwvevfa htvqlhetpl
      481 svapifakqr agvprawvft satlsvrgdf thyaaqmgls srrsmtlasp fdyqsqglly
      541 vprnlpqpss paftdavfda alpaieasgg gvfmlcttlr avdriasklr dviesrgwnt
      601 pllvqgdasr telldrfray gnailvgsqs fwegvdvrgd alslvvidkl pfappddpvl
      661 aarldaltkk glspfavhql pqavitlkqg agrliraetd rgvlmicdtr lvdkpygrri
      721 wqslppfkrt reiavvqdff derrsdkgag a
//
LOCUS       WP_176016003             281 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NRDE family protein [Burkholderia].
ACCESSION   WP_176016003
VERSION     WP_176016003.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Bard,F., Casano,L., Mallabiabarrena,A., Wallace,E., Saito,K.,
            Kitayama,H., Guizzunti,G., Hu,Y., Wendler,F., Dasgupta,R.,
            Perrimon,N. and Malhotra,V.
  TITLE     Functional genomics reveals genes involved in protein secretion and
            Golgi organization
  JOURNAL   Nature 439 (7076), 604-607 (2006)
   PUBMED   16452979
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..281
                     /product="NRDE family protein"
                     /GO_process="GO:0007030 - Golgi organization [Evidence
                     IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=30637
     Region          1..280
                     /region_name="Tango2"
                     /note="Uncharacterized stress-responsive protein, TANGO2
                     (Transport and Golgi organisation 2) family, contains NRDE
                     motif [General function prediction only]; COG3332"
                     /db_xref="CDD:442561"
ORIGIN      
        1 mcliafdwqp daaagpvftl vanrdeffrr tsaplswwed vpgvlagrdl eaggtwlgvs
       61 rdgrfaaltn yrapfdirag aptrgklvsd flggasvapl dylaqlaeha avyngfnllv
      121 gdwrrrelaw fcnrapeges rvaapvaiap gvhalsnarl dtpwpkvvrk raelgtlltd
      181 nptpsldeli almrdphvad ddalphtgip iereralsaa fietpeygtr gttalrvtmk
      241 egvrltvevk ersdddgshr tvrpgafera vtfdidaarp r
//
LOCUS       WP_176016084             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0398].
ACCESSION   WP_176016084
VERSION     WP_176016084.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32752
     Region          13..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..295
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(106,110,149,163,165,230,247,274)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(107..108,112..113,115..116,119,123,125..131,193,
                     224..228,235..236,239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mgfdsrllsg igvlsaviea gtfarageam gltqpavsra varleervgi rifnrtarai
       61 tltdegrrfy eavapllagi eeaaldagqs karvrgrlrv nvdgtfghyv laprmaefld
      121 rfpdlsveis vrdrmgdlva dgfdvavrfg ipepssyrar llletrvltc asaayvarhg
      181 eprhprdlad ahrcvlirdp vtgrpyewef hrgkevvpvd asgrltvndt ggllgaclgg
      241 vgiaqllely ardvladgrl vqllpewade tfplyayhha snlvsakvrv fldfvrelma
//
LOCUS       WP_176016091             538 aa            linear   BCT 11-JAN-2025
DEFINITION  multicopper oxidase family protein [Burkholderia sp. BCC0398].
ACCESSION   WP_176016091
VERSION     WP_176016091.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..538
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=58390
     Region          88..538
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mrrrtflsrt igvaaaslfa rtawaqhagh agmagmdsmd dmpgmtgmsg msahaqhgkl
       61 apdalaaada lpagaplatl rtlanesrep gtfratlvaq pvarpllrga rptafwqfga
      121 gtqgpvvgpl idvregdtve irfvnklpqp stihwhglpv ppdqdgnpsd pvapgasrvy
      181 rftlpkgsag tywyhphphm mtaeqvfrgl agpfvvraad dplagwperh lfvsdlklar
      241 dgtiapndmm dwmngregqf vlvngarrpr idvagderwr vwnacsaryl riafddgraf
      301 ehvgtdgglf daprrvtsll iapgeraell vragdrasra vlqaaeydrr kmamshddgh
      361 gslppdpala ladvafapaa aralpatlra vravrplgep aahktvafge emdmdammkg
      421 gahgrpagmr ftingdtyap hratltsrrg dverweirnt tdmdhpfhlh gtqfqviera
      481 sggsrtsepf rawrdtvnvr sgetvsilvt qdmpgermfh chilehedlg mmgtlkvv
//
LOCUS       WP_176016108             458 aa            linear   BCT 11-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Burkholderia sp.
            BCC0398].
ACCESSION   WP_176016108
VERSION     WP_176016108.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..458
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47722
     Region          22..430
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mqsntvhpcd evlptgklvt lglqhvlvmy agavavpliv gaalklpkdq iaflisadlf
       61 scgiatliqt lglwifgirl pvimgctfaa vgpmiaigtn pglgildifg stiaagiigi
      121 vlaptigkll rffppvvvgt viaviglslm evginwaagg vgnpeygspv ylglslvvlt
      181 lillinkfgr gfianisvll givagfviaf aigrvntegv slapwvgfvm pfhfgwphfd
      241 plsivtmvtv mfvtfiestg mflavgdmvd rpvnqerlvr glrvdglgtl iggifnsfph
      301 tsfsqnvgli gvtgvksrfv catggvilvl lglfpkmaqv vasvppfvlg gagivmfgmv
      361 aangikvlsk vdfvnnshnl fivavsvgmg lvpvvsphff sklppalapi lhsgillasa
      421 savilnivfn gvkgekdarc eirraghdfd grpadvhh
//
LOCUS       WP_176016146             475 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia sp. BCC0398].
ACCESSION   WP_176016146
VERSION     WP_176016146.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454817
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..475
                     /product="MBL fold metallo-hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51402
     Region          159..>350
                     /region_name="UlaG"
                     /note="L-ascorbate lactonase UlaG, metallo-beta-lactamase
                     superfamily [Carbohydrate transport and metabolism];
                     COG2220"
                     /db_xref="CDD:441822"
ORIGIN      
        1 msvddrlgvf lntgilasra hdlgllierq dalmqqfmea kfepaacaal lrdaiarypf
       61 laelfdpdsv aaggciasra llydlhqrrd rwtlalapqg gepivldtaa gdvpqlanal
      121 rdalqrnrwq plselyadpr llgcerpkgd aglawpafdg pgiqrlehas lliasettrl
      181 ltdpislaig gnvglpdldr apsnlarqid gmlvthghld hwhiptilrh ggdgsvpviv
      241 phipvaslla qddmqqslrd vgqtvlapgw getvrigdie idilpfygeq ptigaavpph
      301 dvrnwgncyr vttpqfsvil lvdsgddakg svmdvidrsv arrgrpdlvl sccremrkap
      361 fwqglftfwm vlpmtdlqrl prvaeagdgp sitlgpsgig elcaragaha fapyangfcg
      421 iaaeiddigw ingepaeadt ldqidarldt lgattrvirw lpgdvlrhng dwqvs
//
LOCUS       WP_176016232             157 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia sp. BCC0398].
ACCESSION   WP_176016232
VERSION     WP_176016232.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 157)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..157
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17230
     Region          22..139
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04667"
                     /db_xref="CDD:467552"
ORIGIN      
        1 mtlrdpsdfp vravplapla kerativcvr nrrvllvarg rssrwtlpgg virrgesald
       61 aahrelreet glvdlelayf fyvdgsvkrh hvfvaslprg ahacpgreie lcrwvgidav
      121 shwpasaptq riirqfaglc iasglqpdav trlsssr
//
LOCUS       WP_176016259             279 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Burkholderia sp. BCC0398].
ACCESSION   WP_176016259
VERSION     WP_176016259.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 279)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..279
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30164
     Region          41..279
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mlhpvfsarf sagrvarlar lltaallgvv llngaradia plkvgistsp qiealkiaak
       61 eakeqgldvk iveftdwntp naalankdid vnyfqhipfl enakkqggyn fisiapgtim
      121 kiglyskkvk sfaelkdgar vaiandpvng grgllllqra glitlkpgad yratthdiva
      181 npkhlkiipl easqlarsld dvdlaqgyps fiklagttdp nsallfdgte nknfaiqwvv
      241 rpesandpri rkfisiyqhs pavrkaldna fgslyaiaw
//
LOCUS       WP_176016272             276 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia sp. BCC0398].
ACCESSION   WP_176016272
VERSION     WP_176016272.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..276
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29546
     Region          17..271
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mekiartkkt aaaerdrrqr vqsastgllv lkelaacggr atltalaarl denpakvhry
       61 laslmeeafi tqeratqqyv lgpqcisigl aairmadpir laepslvrvr erlevtcfva
      121 imgnrgptim rfeepglpvt vnvragsvms llwsatgrlf lalldeprvr qlaedelasa
      181 paelraqldr rdpvgqlqre iraaglatvr dtnlkgisav saplfdangh mcaaitalga
      241 tggfdasidg pvatalrhea alisgelgyr adpdsr
//
LOCUS       WP_176016291             347 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC0398].
ACCESSION   WP_176016291
VERSION     WP_176016291.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..347
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37458
     Region          2..342
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mslefehvsf qypgarhgvd ditlsaaqge llavmgrsgs gkstllrlaa glldgwrgri
       61 aiggddvagv pvwrrevgmv fqhyalfpnl svvdnvaygl rmrgvaadvr rrraldmler
      121 vglsahatrg iamlsggqqq rvalaralvi epklllldep laaldagirh qlrdeiralq
      181 racgattlfv thdqdealsm adrvaivdgg rvlqagtprd lyerpataqv arfvghstll
      241 rgrvlahgtv dvrfatlrae tgehrpgaei evlvrpehvq adppghsanr idgrrgdvry
      301 fgatqrydfi pdgsadvllc egrepasrsi aidprhllvl paspaaq
//
LOCUS       WP_176016332             637 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Burkholderia sp. BCC0398].
ACCESSION   WP_176016332
VERSION     WP_176016332.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 637)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 637)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..637
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=67941
     Region          8..637
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mpqpfvlpat agrtdllaqa harstavglr aherpdfapl srvalrelld tnhtlfshar
       61 pvmedlhaqi aetqslvllt dadgvilhsi gdadfiekan rvalcngvsw aegargtnai
      121 gtalasgqav vvhgaehflr anhiltcaca pivdpfgrtl gtldvsgdpr gssphtlalv
      181 rmsaqlienh lfanqcgeal rlrfhahedc vdslfaglva fgpdggliaa nrsaqfqlga
      241 sfdalqhqas dalfgmrfaq laqqaarapg atfrltlstg vrvlarcefp eaqkttvavt
      301 ppapaarvra pdpdaitfat ldtgdarmaa vlervakirg rdlpllilgq tgtgkewlar
      361 alhqasprad gpfvavncaa lpdslieael fgyedgaftg arkrgspgki aqadggtlfl
      421 deigdmplaq qvrlmrvlqe ravmplggar avpvdvrvvc athrdlrami adgtfredlf
      481 yringlavtl palaartdlp alverilarl arsepmprrl aadvldafar hrwpgnlrqm
      541 tnvlrtagml aedeaeitla hlpddfwldc ddaattsaaa ipvasipsag kregttlhsh
      601 qaamidavla rhggnvsaaa relglarntv yrylrrh
//
LOCUS       WP_176016293            1025 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Burkholderia sp. BCC0398].
ACCESSION   WP_176016293
VERSION     WP_176016293.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 1025)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 1025)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11534155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..1025
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=103854
     Region          11..79
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          113..175
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(119..121,124)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          198..258
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(204..206,209)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          280..1023
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mteplasaal qtielsvdgm hcggctgrvq ralaavpgvv daavdldtha atvtaqdtva
       61 agqlvgavre agyraavrea aieagaaths ahasrdetps aasglppaaa tieldidgmt
      121 cascvsrvek alakvpgvtr asvnlatera tvdasagvsa tqladavrqa gygatptasd
      181 tvvpaaatal ptaptsield idgmtcascv srvekalakv pgvtrasvnl ateratvdas
      241 navsaaqlvd avkqagygat paavaappat saatpastvv eldiggmtca scagrvekal
      301 aavpgvtrat vnlaterasv hgagaldaat liaavttagy haslpaaspa gapagadlqp
      361 sgpaqdpdar krreairern lvigaamlss plvapmlaap fgidlmlpgw lqlvlasivq
      421 fgfgarfyra awhavkartg nmdllvalgt saayglslwm llrdpahpgh lyfeasaviv
      481 tlvrfgkwle srakrqttea iralnalrpd rarvvedgve rdvplsqvrv gthvsirpge
      541 rvpvdgrivs grshidesli tgeslpvpkd dgdavtagsi ngegalvvet taigaettla
      601 riirlvesaq aekapiqrlv drvsevfvpa ilgiavltlv gwliagagme tailnavavl
      661 viacpcalgl atpaaimagt gvaarhgvli kdaqalelaq rttviafdkt gtltegkpsv
      721 tafdavgvpr gealalaaav qrqsdhplar avvaaheadv aaqvgaaepa vatdaravag
      781 rgveahvggq rlalgstrwr delgiavppa ldaraaeler agntiswlmr adapravlal
      841 iafgdtvkpg ardaiaalaa rgvasalvtg dnrgsaaava aalgigevha qvlpddkarv
      901 vaelkrthgg ivamvgdgin dapalaaadv giamatgtdv amhtagitlm rgdpalvada
      961 idiskrtyrk iqqnlfwafv ynlvgvplaa lgllnpviag aamafssvsv vtnalllrrw
     1021 kgrar
//
LOCUS       WP_176016347             389 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: electron transfer flavoprotein subunit alpha/FixB
            family protein [unclassified Burkholderia].
ACCESSION   WP_176016347
VERSION     WP_176016347.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..389
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40200
     Region          61..369
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mntikridpr rpfiitaagl kritlgeegs adanaaqwsa hghgvatakp rralqdpkhv
       61 mlvvahserg alddhsrqai aaaavladaq tevallafge lkddvaelgv dklleltgfd
      121 rrafdpesel qalqacvaal apkhvfvpdn atgdgdlgrr yaaaagasva thvveidakh
      181 vgtyaqagra fatralpdvi llaqnavdak lpfvgagerv asdfirpahd aaqpyrdlgl
      241 deidaaqval eeadfivsag ngvsdigafe rlagvfgaai gasrvavdng hftrdkqvga
      301 tgktveasvy iafgisgavq hlqgikdcrh viavnldgsa piakranltv vgdaqatiaa
      361 lieqvqaara argespaavg trepegvaa
//
LOCUS       WP_176016374             666 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Burkholderia sp. BCC0398].
ACCESSION   WP_176016374
VERSION     WP_176016374.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..666
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70775
     Region          1..460
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          598..662
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(620,629..631,638)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            630
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mfdkilianr geiacrvaat ckrlgiasva vysdadanak hvaacdeavh iggsaaadsy
       61 lrieriidaa ratgaqaihp gygflsened fahaceeagi vfigppvdai aamgskaaak
      121 almhaaavpl vpgyhgddqd aanlhgeadr igypvllkas aggggkgmrv versddfpaa
      181 lascqreaas sfgndrvlie kylmrprhve vqvfgdthgn tvylfdrdcs vqrrhqkvle
      241 eapapglhad vrqamgeaav aaaravgyvg agtvefimtg eafyfmemnt rlqvehpvte
      301 mvtgldlvew qlrvasgepl plkqeelrvh ghalearlya enpargflps tgtlkhlrlp
      361 agvefdigaa vrvdsgvreg daitpfydpm iaklivhgad raealglmqr alracevvgl
      421 htnaaflqri vacepfaipd ldtgliernh ealfapqqpp ratlalacaa llarergaaa
      481 qegawpwcsl pdwrlnggyr rtlewhater eadvtvtyeh dgagtriaig daaaqpfawt
      541 rgatpldfdv tlggvrssgr vyadgdtfhv ftqgaaetfe wrnllahagd aeqgggrlta
      601 pmpgkviavl vepgqkveag tplivmeamk mehtigapsa gvvaevlygv gdqvadgaql
      661 lmmaeg
//
LOCUS       WP_176016375             248 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_176016375
VERSION     WP_176016375.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..248
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27233
     Region          27..184
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtaapadtmt atakadradt prapagrksq qrvqdilrag revfaekgye hataaeiaqr
       61 vgvseatvfs yfrgkrelca rviadwydei iaafehgmpr dasvqqqfaf ivrthlrlml
      121 vngtglcalv lsegrakqha lsdeltalqr rytaplmdvl argqaagqvr adlplsllrs
      181 mvfgpmehvl wdailghrkl dtettatqli dmlwaamqpp apeqaalvrf rnevaeavrr
      241 legkasra
//
LOCUS       WP_176016371             208 aa            linear   BCT 11-JAN-2025
DEFINITION  trimeric intracellular cation channel family protein [Burkholderia
            sp. BCC0398].
ACCESSION   WP_176016371
VERSION     WP_176016371.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..208
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=20938
     Region          6..204
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mrrieqvvla adlagtgvfa ieganaaiga gldlfgvmvl slvvalgggv irdlligarp
       61 psavsdwryp alafaaglfa fvfharvasf spsllttlda aglalfavag avkalefrvh
      121 pfiatlmgav tgcgggvvrd lllaripvvl vtdiyasaal lgavvvvlcr rlgcpsvvaa
      181 vlggvacfal rmaavrfgwq lpkiagga
//
LOCUS       WP_176016376             143 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GFA family protein [unclassified Burkholderia].
ACCESSION   WP_176016376
VERSION     WP_176016376.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..143
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15286
     Region          3..130
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mtrtlsahcl cgavtvtlrg epaaranchc atcrdfygtp mlsatawppe qvtidgghat
       61 fphpsksmar twcaacgeiv fgtnrlgmrv vpnsltaray ggplpgdlqp tmhlfyrqrv
      121 ldvvdalpky vdgwdgptld pan
//
LOCUS       WP_176016464             937 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC0398].
ACCESSION   WP_176016464
VERSION     WP_176016464.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 937)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..937
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=100912
     Region          33..747
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 marerdtqrs vaqwitgrqs yflevpsapv apdlsimsfv lderlgepyr ievtltspvs
       61 laradylnrp aiftieppgt nvatdairrf agcitafgqi rktrdfvsyr ivvepfvarl
      121 rlveatriyq qqsvpeives ilrrhefrah qfsfklrray prlafrmqyr msdwdyirll
      181 meqtglfcff ragqhgdelh fgddvdaysy rpqvvipyre asglesghea vlsleslset
      241 iprsikvady npekaddrfn aeatiaredp ttwgasyvyg thhadgdear reaqlrreaa
      301 lawqvtysgk ssvvdfapgl vakldeqpad aphgivivsv rhaggrdasy intfdaipcg
      361 rpfrlklder rwpaiagtls arvttpgasp yahltsdgyy tvrfdfdfdt wpaggecvpl
      421 rlakpfagsh qtgfhfplla dtevavafag gnpnrpyiah ahhhsqavdl vtsrdgfntr
      481 nvirtrannk lrfedrkgre siklstdygg ktqvnlghfv dsrqqtrgeg fevrtdergv
      541 lragkglfls adaqssaggh afdmtvarrq ldaarsrmrs lsdavekara tmaaceaqqa
      601 lleaqvhdle aavllasaph gvavtsgehm qlaadghlft ttggnadaai ggnytvaagn
      661 avslyanahg mklyagagkv dvqaqadale ltalkgvtia stsdavtlna qkalvlmcgg
      721 ayikleggtv eigsageirl rgpvsagpsa trrqalplmp aqeqtgmqlw haypngepvr
      781 nakyrvtfpd gswregrlda dgrgtvadmp rgggsvqyfe edhdlqdtth kwgdpqgtpp
      841 fspasgdagh tvpslvgasm taaipiaesa gqalgaaalv reaasggaan vangdaaala
      901 rasldavgkp vanstsnhaa asmpgaapgl vkttvsr
//
LOCUS       WP_176016469             240 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD family hydrolase [Burkholderia sp. BCC0398].
ACCESSION   WP_176016469
VERSION     WP_176016469.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..240
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26287
     Region          6..233
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mrlakvsavs fdlddtlwpf gpsvvraeat lrawliehap ntervlptqq tlaalreeye
       61 rlrpdlasdy ramrigsirl aleranedvs lteraydvfy aarnrvefye dalpalawls
      121 arfpliavtn gnadlrltgg geffrttlsa rafgfakpep eifhaaadal gvrpaellhv
      181 gddfhldivg avnaglqaaw ivrepvsage yapgyaaaph lrlrdlsmlc rvlggpddvs
//
LOCUS       WP_176016471             304 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia sp. BCC0398].
ACCESSION   WP_176016471
VERSION     WP_176016471.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..304
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32146
     Region          5..298
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdthhevivi ggsfaglsaa mqlararrrv lvidagrprn rfaehahgff gqdgkppari
       61 iaeasaqlaa yptvqridge vraaerdade rfhvtladgs rasadrlila tgirdelpal
      121 pglaerwgis vlhcpychgy evsgqrlgvl athplsvhqa ilipdwgptt wftqrvvean
      181 eeeaallaar gvrierspvv eivgdaprid alrladgqvv pidalfvgar tdmasdlaqq
      241 lgcafdegpl gtairvdawk rtsvagvyaa gdasslmtna tfasasgvaa gvgvhrslif
      301 glda
//
LOCUS       WP_176016530             862 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC0398].
ACCESSION   WP_176016530
VERSION     WP_176016530.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 862)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..862
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=94119
     Region          40..735
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 maefdrvtsy ltgrqsahlt lmrrkskrdp etgelppmpt vsvvswvvre aicepysvka
       61 vvaapvaipr ktvlgqlakf svrpedgrak refagfvtqf dsvsesrdgy tyrivmrqhl
      121 avmdgpsnca tyqgmaswei ikeilarydl rfwiqvefnl rrehprhpfr fqynigdwdy
      181 iklemeqagl ycytrtgehg dvlviaddvd gymrpaipvl drptaglatf eesifsfkvr
      241 srvvpesyvv adynpeqawe rfraedravs ddesmigkpy vwgthhddak gakrdaqlrh
      301 eaarasqiry svestvlair pgsivqsdra ledagaamfv tavvhrgarn asyvnsftai
      361 padrpyrrei derrwpkipg tlgatitspd kykfayltdk geyvarfhcd fgnwpkgges
      421 vplrlakpfa grnhtgmhmp aldgdealig fregnpnkpf iaafihnsec pdlinssrrr
      481 msrneirtqs gntfwmddwd nqegielgtq hsgrsqlhlg hmvdralnqr gagaelrtsg
      541 havarggagv mvtaydrpgg agkqldmaet iaqlkemlal aeslaksaea skaspadtqa
      601 qkaisdglde lkrpgavvta pgpvgvvsgd gvqlaadgsi igtakkgvhf salkritaaa
      661 ggrlslfark gmsliasage vivqaqrgrm qlaaqedmtv etvngvlhvk spkevllsvg
      721 gsyirvnpeg iemgsrgrvh frtsglkktg paqldlsgaa fapafvpfkt ecevwrtnpn
      781 fvqapalale pnpaqwesqg nrggvppvra sdtgatvpps slgdifggks sanagvssdr
      841 gltvndpdne qqkssglirf sy
//
LOCUS       WP_176016532             842 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Burkholderia sp. BCC0398].
ACCESSION   WP_176016532
VERSION     WP_176016532.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 842)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 842)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 842)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 842)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 842)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10833107
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..842
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..842
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87671
     Region          136..192
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(141..143,146)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          234..829
                     /region_name="Haloacid Dehalogenase-like Hydrolases"
                     /note="The haloacid dehalogenase (HAD) superfamily
                     includes carbon and phosphorus hydrolases such as
                     2-haloalkonoate dehalogenase, epoxide hydrolase,
                     phosphoserine phosphatase, phosphomannomutase,
                     phosphoglycolate phosphatase, P-type ATPase, among others.
                     These...; cl21460"
                     /db_xref="CDD:473868"
     Site            order(525..529,679..680,707,726..727,730..731)
                     /site_type="active"
                     /db_xref="CDD:319763"
ORIGIN      
        1 mtdaqrphdp rhrhaggadt ccadardtqt atvadaapaa gerahghdhd hghghaahgd
       61 aghdhdhdea htdthrhgas cshdhaahdh agrdhdhdhd hdhdhaagdc capaaltlap
      121 lpvaqatasg hvrsafrimq mdcpteetli rkklggmqqv salefnlmqr mltvehvpga
      181 qpalesairs lgmtpeaasa dapaaptapp pakpwwplal agvaaiaseg atwaglpvwl
      241 saalalaavl acglttykkg wiairngnln inalmsiavt gamaigqwpe aamvmvlfti
      301 aelieaksld rarnaiqglm qlapdtatvq qadgawrtie aaqvalgavv rvkpgerigl
      361 dgevvagrst vnqapitges lpvekasgda vyagtinesg sfdyrvtava anstlariih
      421 aveeaqgaka ptqrfvdqfa rvytpivfav allvavappl vmggawhdwi yralvllvia
      481 cpcalvistp vtivsglaaa arrgilvkgg vyleegrkla wlaldktgti thgkpvqtdf
      541 dvhadgadaa rvrhlgasla arsdhpvsqa iaaaardagt tafadvqdfe aivgrgvcgt
      601 idgtrywlgn hrlveelerc saaleaklda lerqgksvvv lvdatrvlgi favadtikdt
      661 srdaiadlha lgirtamltg dnphtaqaia rqagiddarg nqlpedklaa veelsaggag
      721 avgmvgdgin dapalaradi gfamgamgtd taietadval mdddlrkipa fvrlsrathr
      781 vlvqnigfal gvkvvflglt vaglgtmwma vfadagasli vvanglrlls sswafgdvpa
      841 kr
//
LOCUS       WP_176016570             507 aa            linear   BCT 11-JAN-2025
DEFINITION  ammonium transporter [Burkholderia sp. BCC0398].
ACCESSION   WP_176016570
VERSION     WP_176016570.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..507
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51145
     Region          100..504
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mrkllmsllm agsliaagvg saladdaasa aagstaaasa paatasdasa aaapaasapa
       61 adasataaaa pasgatdasa aaaasapaap aaptapfsvd sskisagdta wmltstalvl
      121 fmtipglalf yagmvrkknv latvmqsfai tavitvlwtv vgyslaftpg ngfigglsrv
      181 flhgmnyikg dkattltvsh lastipesvy fvyqmtfaii tpalicgafa drmkfsamlv
      241 fmtlwslivy vpiahmvwep sgwlsadgvl dfaggtvvhi nagiaglvsc lvlgkrvgyg
      301 resmaphnlv ltmiggsmlw vgwfgfnags avaadgragf amlttqvata caalgwmfae
      361 wiakgkpsvl givsgavagl vaitpaagfv gvpgalvigi aagvicfwsa twlksklgyd
      421 dsldafgvhg iggilgallt gvfavkdigg fdgslllqak gvlitlvysg vlsfvllkli
      481 dltiglrvte eeeregldvi lhgehve
//
LOCUS       WP_176016604             503 aa            linear   BCT 11-JAN-2025
DEFINITION  HDOD domain-containing protein [Burkholderia sp. BCC0398].
ACCESSION   WP_176016604
VERSION     WP_176016604.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..503
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=54714
     Region          18..213
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 mstteylprt alldklwarm nergdfplls eslratmaam knddldftal vrvvlsdfal
       61 tqkvlrlans amymafggni ttvtralmvl gmdavghlvv glklvdhfhq stprridakl
      121 elnrallsgc varkltehae lrggeeaivc tlmrqvgkll vvcyldsewd rirrraaeln
      181 gdeaaacvdv lgvgfdeigv eaaarwrlpe vicggmaddd ratradafdn edgdarhagp
      241 agddgsadri rwlravsrcs tdvagalvmp aspqrdaria alaqhygael dmeadalvei
      301 adrlareeas dtmmreivel ranadaiara qaapeaclea gladlralps ehvltpvlal
      361 asesllagla ftrtvmfvrh ddgtfaarlg fgpgvdtald rlhfderfep dvfhlaisns
      421 vgifieqaqd pkmtkrlpaw yldafddara fvllpvrvgt tsvallygdw agaqparkis
      481 qqemavlnel arelgrffaa qpg
//
LOCUS       WP_176016696             204 aa            linear   BCT 11-JAN-2025
DEFINITION  CGNR zinc finger domain-containing protein [Burkholderia sp.
            BCC0398].
ACCESSION   WP_176016696
VERSION     WP_176016696.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..204
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22652
     Region          12..204
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mvtrsdparh ehewraadfv gghpaldfln tvadtgktrd eeklvdwpav rawaakaggl
       61 apddlarllr hprqdgpdel aalhrfrdda yvaiahltte gggsagaraa drlavtirea
      121 igrsafdavg grfawrldar tasrwidava lgfehlmrsd dfarvrqcgr ctwffvdrgr
      181 gvgrrwcdmr tcgnrakvea frer
//
LOCUS       WP_176016726             456 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia sp. BCC0398].
ACCESSION   WP_176016726
VERSION     WP_176016726.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..456
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47520
     Region          233..409
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mrsdlrfrva reqgqpaprg vhrfpmgral lrgivaaacv agaqgaaaqa fhdaaqlapa
       61 taettdlddv pffnaarttw gglhassapl dvayvspaln vstgagrgdp varfgacvay
      121 rvlcetarda vergyasrfh yglasalpat gaqpafarga vdlasaepft laqpdrgtra
      181 gaivgslras laradlptgv aeqivrmlag rvdpkqrgah gdtfrvafep dhdavrpgra
      241 rvtaldvrfr gqrvaavwfa pqagspgayy eldgmplagt rfampvaatr vssqfgtrvh
      301 pvsgarhvhs gvdlaapagr avhasergvv tfigtepngy gkyvvighdg gyasyyahls
      361 afeptlrtga rvvrgqrvga vgstgtatgp hlhfevrrha rlvdpielvh aakaaklkga
      421 qrvafnrvar dartqlasaa faqpvamsta vapqag
//
LOCUS       WP_176016739             329 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_176016739
VERSION     WP_176016739.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..329
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35302
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,146,160,162,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     222..225,232..233,236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdmlenmrtf vrvvqagsfs avakqtdvat aqvsravasl eayaqirlln rttrkialtd
       61 sgrryferlq silgdvdqan aearnalvrp ygrlrvhtmp glgqshvtal avayrarfpe
      121 vaiemtysqr mpnlveegyd vsvvtaaslp dsaciahscg tsfsvlvasp aylarhgvps
      181 apadlarhtc lrldtpaean dewllhgpgg qtashavtaa pfhanapeal sialraglgi
      241 gslaiysaid dlrsgrlvrv lpdyrltmld vyamfasrrf vdakvrtfve hlrlglspal
      301 kadaraldal aaprgrerar aravagvta
//
LOCUS       WP_176016743             311 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC0398].
ACCESSION   WP_176016743
VERSION     WP_176016743.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 311)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 311)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401161
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..311
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35338
     Region          14..95
                     /region_name="cupin_MtlR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to MtlR, N-terminal cupin domain; cd06976"
                     /db_xref="CDD:380381"
     Region          31..284
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnpdleivpt hrdesfrawv hdyphsvakw hfhpeyeihl iqasrgkvfv gdhigdfapg
       61 nlivtgpnlp hnwvseladg ervpsrdvvl qfsrdaiekm vgafselqpv idliddaarg
      121 vqfpdrvgve vaplmlelad ahgcrrveil mslfdrlssc rerrvlagpg yrsdaqhyms
      181 stinqvlsyl qqnlpgmlre tdvaafagms vstftrffrr htgssfvryl nrlrineace
      241 llmfsdltvt dicyrvgfnn lsnfnrqfla mkqvppskfr alhrlnephg rddappprrv
      301 pprapdrmlh t
//
LOCUS       WP_176016745             351 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia sp. BCC0398].
ACCESSION   WP_176016745
VERSION     WP_176016745.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..351
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36677
     Region          11..109
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(55,58,62..63,72,91,95,101,105,108..109)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
ORIGIN      
        1 mgtdtlrlna saaaarlgis ikalrlyerh glvmpertpa gyraygpddl araadiaalr
       61 klglglaqia nvlggdarsl daalaaheaa ldrgiqdlvg kldsvramra glargrmptd
      121 seltrlvdpg sagvafdlpw pwggerfecr dirplnyiig slgsgktrla lrladalpgt
      181 vfvgldrldd dcaaafdalr adpelksrvd rtaallagng aapsaaltal lvsleaagpr
      241 vlivdmieqd ldqatqrali ahlracaaag mrplflltrs aaildlaavg pdetillcpa
      301 nhspparvap ypgapgyeav atclaapavr eriarppear ammlgtarem n
//
LOCUS       WP_176016764             927 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC0398].
ACCESSION   WP_176016764
VERSION     WP_176016764.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 927)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 927)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..927
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..927
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=98890
     Region          14..813
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mniresfrnf vsgidanrrp vvlnwgkaqh algskialqh asiresmmtg isghltcisq
       61 qgdlppklfi gapvsigivt drgqvhaina iisavqvgrt dgeltvyqfa vtdalnllhk
      121 rtnsrifrnv svvdvlgvvl sewrqrsval aqafefdlsq ldrsrypvrs fvrqvnesda
      181 rfisriarrd gitlfvragr vsgetkdgds pvhalvfcdd prklgesaag ivrvhprdag
      241 teqrdtital tmrqqlisge sgrpswdyry arvdqssast ridqgesgnd laklltdivi
      301 dvphmadswa dhermtedri laheaqavry dgvsgirdla vgawitiage dewgalpsdk
      361 qqfvitslhh eiwnnlpkgl seraqalfat shtlqqpqsl sdgdpsgqdt ryentfscvp
      421 rgtpltppyd pktdlpptpl itgrvvgadg eevscdengc vfvqilgqds rdhahaqgag
      481 tnsnesdsap irvasslagp nfgetflprv gtevllgslg gdpdrlviig vlanganmpa
      541 sfthtgslpg nrflsgiktk eikgqrynql rlddtpqqis aqlasehahs qlnlgyltqp
      601 rdngqgadrg qgaelrtdaa aalraaqgml lttyartqas ggqldrdelv ellgecaelf
      661 kalgdyagqh ggtatdatgq qavvtafkgw tpgghasggd rapnadagds qalmafgaka
      721 galnitpkty vtyagenidq iaqqnlqfag gqrvittagk gihlfgrgeg vraiagegpv
      781 vlqaqqdtla ataqkgiqim svgdevlisg ksirfvaedg syvkvgggve vgsdgaftah
      841 taghdfvgpk tdhvappafn rggadqkfrl rypgtdgddg thpvpnrpyk itlrngqvin
      901 gvsdahglte lassdamhia hiqvfda
//
LOCUS       WP_176016775             194 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia sp. BCC0398].
ACCESSION   WP_176016775
VERSION     WP_176016775.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..194
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21118
     Region          7..161
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mdshiapval nkayrllnhg ptvlvsarhd gvdnvmaaaw acaldflppk ltvvldksak
       61 trelversgt fviqvptaaq lqlthavgsh slaqrpdklr eagvtlfdvd ghdlpfvagc
      121 sgwlacrlip ephnqqtydl figevigaws dtrvfrdghw yfesadpalr slhyiaggnf
      181 yaigeslyvd pdaq
//
LOCUS       WP_176016776             141 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC0398].
ACCESSION   WP_176016776
VERSION     WP_176016776.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..141
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15713
     Region          1..141
                     /region_name="COG3565"
                     /note="Predicted dioxygenase of extradiol dioxygenase
                     family [General function prediction only]"
                     /db_xref="CDD:442786"
ORIGIN      
        1 mslspfhlai pvydlpaard fygrvfglee grssaqwvdf nfyghqlvih ehpktasqeg
       61 ahtnavdghd vpvphfgtvl dwaswealae rlrgfgvtfv iepyvrfqgq vgeqatmflf
      121 dpcgnalefk afrdigqlfa k
//
LOCUS       WP_176016803             703 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC0398].
ACCESSION   WP_176016803
VERSION     WP_176016803.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..703
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=78315
     Region          11..703
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mqmseiasff qlqsnrlfti etplkgrsdl vlvdfhcteg lsqnfemhvr lasqdkniel
       61 kkligqpvti tlqltdalas seeryfhgyv aafshldtdg gfamysatil pwlwmlsrrq
      121 dirifqeent eailarvfre ygklasfefr lskgtknrsy ctqyrendla fverlmredg
      181 lfyyfehakd ghkliiadns vtakpidgrs pslqynqgea mdnlavitsf qaqrqlapdt
      241 vglktfdyki pharrfvsgg tevnqgdvps yeiydylgeh gfadsdrgee ltrfrteala
      301 ahsktfvgvt tgrrmmpcry felddhydha stkqedrqfl lltvshtgtn nyepgegssa
      361 yscsftcirk kipyrpafeg erptivgpqt aivvgpkgee iytdslgrvk vqfhwdrlgk
      421 rdqgsscwvr vsqpwagsgf gmiqiprigd evvvsfldgn pdrplvtsrv ynsqnmppwt
      481 lpanatqsgi ltrstrtgnv ntanairfed kkgeeevwlh aekdqrieve hdeshwvgnd
      541 rtknidhdet vhvghdrtet vdnnetihvg vdrtetvgnn etltvggnrn etiqgmenll
      601 ialtstetvg lakaltvggg yqvtvagavn tsaglasaee vglskttmvg ktytitagdr
      661 ielktgssvl imesnghitl rgtqlliegs gpvqingkdv dvn
//
LOCUS       WP_176016859             926 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: type VI secretion system Vgr family protein
            [Burkholderia].
ACCESSION   WP_176016859
VERSION     WP_176016859.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 926)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 926)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..926
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..926
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=98776
     Region          28..829
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 msisetlssf asgavdwnrr pvalnfgrlq gtlgrllalq hanvheglmt gihghltcvs
       61 prhdlpptlf igvpvsvrlv tdrgqlhtin aiiqnvqigq sdgelcvyql ticdalslmd
      121 krtnsrvfrk qsvvdilavm fnewrqrspa larafefdls flnrdryppr eltrqvnesd
      181 aafvrrlvrr egisifaksg pakgsssgqd dtpihtlicc dnpdslqesv agtvrlhprd
      241 agteerdtvt lfalharlvp gtasrpswdy kkaridestv agsvdqgdag ndlaklltdv
      301 aidvphagds wddhdrltrs rmlahqfeae qydgasgird lavgtwitlt gdpeldmqaa
      361 dkrqfvitsi rhdvsnnlpk gltervqmlf aasknlvsps paqlapsste sdtryentft
      421 cvrrgvpitp aydpkidlpp vhlltgvivt rdgdevvtde lgrvyvrihg ldpadhshaq
      481 gagtndnagd sapvrvassl agtqfgasfl prigmevllg aiggdpdrlv iiavlgngan
      541 ppaafthtgs lpgnryvsgi ktkeikgqry nqlrlddtpg qissqlaseh ahsqlnlgyl
      601 tqprqdgqgk drgegaelrt daaaalraaq gillttyars qasggqldrd ellqllgect
      661 elfkslgdya gehggqatdt agqqavasaf kswtpaggas gtgageaggs qalmafgaqa
      721 gsvaitpkth vtyagenidq vaqqhvqlts gqrinlhggr gvamfahsdg vsaianqgkv
      781 ilqsqaddtq idsakniqfs aadgkitgma ndqvvfttsg gaylklhgsd ielgcpgkft
      841 vksaghswqg pasmstdmpk fdhaplgrvp klvrasdgnp iegyvgevhk asgeivngqt
      901 dsagtmppid hnqfeqvvvk ffkkda
//
LOCUS       WP_176016861             246 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CPBP family intramembrane glutamic endopeptidase
            [Burkholderia].
ACCESSION   WP_176016861
VERSION     WP_176016861.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..246
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=27469
     Region          139..228
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 mattitepsy ppprsakafa kswrwallfg ffvywgyrll elvllgvvve qfgltseaks
       61 ytilfayvpa lvflggmfyv hrrlvfpdiq fvgafkrrdv vtgialvtlv yllgyglawl
      121 thqprepima slfqsktslq ivvmigamll lppvveelaf rhfllsmlpf raswwvaava
      181 vcatglffsy vhayqywttn ltiflvgvvf avarirsngm tlpimlhaya vvlalvldql
      241 maaaig
//
LOCUS       WP_176016888             263 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: IclR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_176016888
VERSION     WP_176016888.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..263
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28841
     Region          13..260
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 metspdqand llfnqslekg lnvlrafsak rrtmtlaeva daagmtkssa qrmvytlekl
       61 gyirkhpvtr ryqltphvmr igfnylaadt lidvanpfls eltnltgett nltepdedem
      121 vyvarfvstk fvpihmpigs ripmyctgsg raflsalape earvrldgma rtphtprtvt
      181 alddlvalld sarregyatn qeelfigdms iaapvlgsqg qpvaavhvva ptsrwtfdda
      241 rrklapavid cargisnsir tle
//
LOCUS       WP_176016944             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC0398].
ACCESSION   WP_176016944
VERSION     WP_176016944.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32709
     Region          1..>157
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          91..286
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,221,238,265)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     215..219,226..227,230)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 melndlrifv atvdagsfta aadqlmlskq fvsrrtmale aslgvrllhr ntrnlavtes
       61 gqefyaraqr ilaeiadaeq amsvrstelh gslkisapls fgithvspli aeflsahpav
      121 rlnldltdrr vdligegfdl vlrigsleds tliarplgaw rmiacaslay lkrhgtpqtp
      181 adlaghtcvl ygrerrvgwe frvdgaartf dvqgplvann gevvrdaaia glgiallphf
      241 ivgaaldsga lvpvldayvp ppitlnavfp qhregfvtlr tfigflaerl gepagaeasa
      301 agrvr
//
LOCUS       WP_176016947             214 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [unclassified Burkholderia].
ACCESSION   WP_176016947
VERSION     WP_176016947.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..214
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24428
     Region          1..210
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mltvwgrrna fnvqkvmwlv delalahrhv paggqfgvld tpeflamnph gripvidddg
       61 tvvweshsil rylaarhgrp gfwrdnpaeq sradrwmdwa qttlqpafln gvfrdyyrtp
      121 peqrdtvrve qsiaqcaqyf rlldtvlagq pflagdaitl adiaagthly ryfeldiarp
      181 dvphvvawye rlkarpayrt nvmipfedlr gklg
//
LOCUS       WP_176016977             575 aa            linear   BCT 11-JAN-2025
DEFINITION  WD40 repeat domain-containing protein [Burkholderia sp. BCC0398].
ACCESSION   WP_176016977
VERSION     WP_176016977.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Jain,B.P. and Pandey,S.
  TITLE     WD40 Repeat Proteins: Signalling Scaffold with Diverse Functions
  JOURNAL   Protein J 37 (5), 391-406 (2018)
   PUBMED   30069656
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Schapira,M., Tyers,M., Torrent,M. and Arrowsmith,C.H.
  TITLE     WD40 repeat domain proteins: a novel target class?
  JOURNAL   Nat Rev Drug Discov 16 (11), 773-786 (2017)
   PUBMED   29026209
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Smith,T.F., Gaitatzes,C., Saxena,K. and Neer,E.J.
  TITLE     The WD repeat: a common architecture for diverse functions
  JOURNAL   Trends Biochem Sci 24 (5), 181-185 (1999)
   PUBMED   10322433
REFERENCE   4  (residues 1 to 575)
  AUTHORS   Neer,E.J., Schmidt,C.J., Nambudripad,R. and Smith,T.F.
  TITLE     The ancient regulatory-protein family of WD-repeat proteins
  JOURNAL   Nature 371 (6495), 297-300 (1994)
   PUBMED   8090199
  REMARK    Erratum:[Nature 1994 Oct 27;371(6500):812]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12822048
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..575
                     /product="WD40 repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=61781
     Region          4..307
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          8..45
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          49..85
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          79..552
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(86,104,108,114..115,126..127,145,149,155..156,
                     206..207,224,229,235..236,292,340,345,358,373,385,407,465,
                     469,475,486..487,504,509,515..516,528..529,548,551)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          90..125
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          132..167
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          211..248
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          255..278
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          296..359
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          367..405
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          421..475
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          491..530
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          533..559
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
ORIGIN      
        1 miahrspisg vaafggrfva tagydnqvil wdaltqralg rglhdhlanq vefspdgryl
       61 vsassdhtar vwmlpdmklh avlsdhvddv emavfhpdre liatasrdqr imvynltgnl
      121 vrcfnghrad visvvwsscg dylisssddg tvkrwsldtg elvtdvdvgg vetdtiaida
      181 aggiyagnde gnivvirsgr vetirahaag ikrlvynsra kllvslsydr tlcvwhvget
      241 ldkiatallp aeiwarscaf idratlafat fgnsyavyhi dtgswdltrv gptagvnava
      301 lhdghrltvg dsgvfaidgq pvthlgslcn fitptdghil tggqlgqvmn altgrvlyqh
      361 hsplncgvaf trdghahali gtytgeglvf rmaqdsgavl vgilrlhtna vksvavsdgv
      421 ifsvcadrga awfsvdtlde igrvddahdr iangaaplpd rrfvsvsrdr kmriwreqhv
      481 ealdtphehs ikcvatsrdg ryiasgsysg vvavfdvida rwvatvrptt sgissicngp
      541 atgtflmssy dghvyeldva aeivqgesha qsela
//
LOCUS       WP_176016987             107 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia sp.
            BCC0398].
ACCESSION   WP_176016987
VERSION     WP_176016987.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..107
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11880
     Region          19..83
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mlyamstkpr trdrrnavat aigkrvkacr ieaeksqeel ayeacldrtr vsaiergign
       61 ptvetlatic yvlgitlsdl feplkmalkp tgehrgeapq prrrplr
//
LOCUS       WP_176017007             174 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: shikimate kinase [unclassified Burkholderia].
ACCESSION   WP_176017007
VERSION     WP_176017007.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Herrmann,K.M.
  TITLE     The shikimate pathway as an entry to aromatic secondary metabolism
  JOURNAL   Plant Physiol 107 (1), 7-12 (1995)
   PUBMED   7870841
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Bentley,R.
  TITLE     The shikimate pathway--a metabolic tree with many branches
  JOURNAL   Crit Rev Biochem Mol Biol 25 (5), 307-384 (1990)
   PUBMED   2279393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..174
                     /product="shikimate kinase"
                     /EC_number="2.7.1.71"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004765 - shikimate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=18180
     Region          12..160
                     /region_name="AroK"
                     /note="Shikimate kinase [Amino acid transport and
                     metabolism]; COG0703"
                     /db_xref="CDD:440467"
ORIGIN      
        1 mnprpqagpt rialvgmpga gkttigsala ralalpfvda drelerrfga pvavqfhagd
       61 frareadvid altcgpalvl atgggavlrd dtrarlgqrc fvihlatdld tlwhrtrgda
      121 srpllnvadp raalaalhda reslyracah cridtsgqsv aqtlaaalda laia
//
LOCUS       WP_176017072             460 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia sp. BCC0398].
ACCESSION   WP_176017072
VERSION     WP_176017072.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..460
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49497
     Region          3..451
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mkqpedqlhr gleerhinlm algatigvgl flgsatairt agpailltyl lgglaiflim
       61 rglgemaitn pvagafsrya rdylgplagy ltgwtywfvw ivtcmaeita vgvymhmwfp
      121 gvpnwiwala allamgsvnf iavklygefe fwfalikivt ivlmivgggl miafgigngg
      181 iatgisnlws hggfmpngin gviaalpivm faylgvemlg ltagearnpe ksltkavnsv
      241 fwrvlifyig alfvimslyp wdqigtqgsp fvmtfsrlgi paaagiinfv vltaalsscn
      301 sglfstarml ynlaqqgqap aalgrvnrsg vpvygvavsv allligvlln ylapqhvftw
      361 ltsvstfgai wtwcviliaq mrfrrtlsad qiarlpirvp lfplgsfval gflvlvvvlm
      421 aftpdtrval vigpvwivll giaytlfyan rpaasmptks
//
LOCUS       WP_176017027             449 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia sp. BCC0398].
ACCESSION   WP_176017027
VERSION     WP_176017027.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..449
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=48179
     Region          76..440
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mhtllksfaf arslipaaat lavagalaal agcdaqpgtt asaasvvpaa qaapaspava
       61 pagqpqtraq vfegvkqmta lgkqlffdps lsgsgklaca schsaehafg ppnalsvqlg
      121 gddmhrtgfr avpslkylrg ippfsehfhd spdegdesid agptggltwd grvdtrdaqa
      181 ripltspfem sssparvana vraapyadaf rkafgetvlg ddqatfgavl raldafqqqp
      241 alfdpytsky daylaghaql tpaelhglql fndekkgnca schisqrtle ggppqfsdfg
      301 liaiavprnr alpvnrdprf hdlgacgper tdlkgrdefc glfrtpslrn valrktffhn
      361 gvyhsledvm rfyverdihp ekfypvvhgk vqiyddlpkr ywpninrepp fdrkrgdppa
      421 lnaaeiedvi aflgtltdgy qqtaasakp
//
LOCUS       WP_176017075             786 aa            linear   BCT 11-JAN-2025
DEFINITION  LPS-assembly protein LptD [Burkholderia sp. BCC0398].
ACCESSION   WP_176017075
VERSION     WP_176017075.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC0398
  ORGANISM  Burkholderia sp. BCC0398
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Burkholderia sp. BCC0398"
                     /db_xref="taxon:2676297"
     Protein         1..786
                     /product="LPS-assembly protein LptD"
                     /GO_process="GO:0015920 - lipopolysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86715
     Region          76..757
                     /region_name="LptD"
                     /note="LPS assembly outer membrane protein LptD (organic
                     solvent tolerance protein OstA) [Cell
                     wall/membrane/envelope biogenesis]; COG1452"
                     /db_xref="CDD:441061"
ORIGIN      
        1 mppkplfpnv fpgdgaprkr rlalallavp glvpavsyaq lsgaaaqpqp ldspwdlrla
       61 pqledhplkd gakpaafvia dhtsgtaeqd laakgsaelr rgdavvkada ihydqdtdma
      121 daygqvkvvn ggtsfagpea hlkieanqgf mtapkyhfnv tggsgsaerv dmvdnersvf
      181 vngtytacqc stnpawyikg srfdfdtgad egtarngvlf fqgvpifasp wmtfplsger
      241 rsgllpptfs vnsnngfels lpyyfniapn rdltltprii srrgvmteat frylspsysg
      301 tftanylpdd rlahrnryai ywqhqqnfgg gfggyvyfnk vsdntypedl gsanqfingt
      361 qtlyqqeagl tynngpwsvl aryqhwqtlp psiapysrep qlnvkytkyn vggfdfgaea
      421 dysrfritta datqgdravf npyisygvyg pgyfavpkvq yhlasydlny lssatpnspk
      481 rftesiptvs fdsglifdrs vrlfgqdfiq tleprlyyvy tpyrdqsnap lfdtaesdfg
      541 laeiyqpntf vgndriadan ritagltsrf idprtgdera rfviaqqyyf adqrvtlnpg
      601 qsavlarhsd livgaalklg sgfmsetafq ynqnnnqlvk ssigfgyspg errvinvgyr
      661 ytrtnttldn qpinqflvsa qwpltrrlya igrfnydfag drvvdglvgl qydadcwalg
      721 vgvqraangi nssgqqnsst rfmmqltlkg lstidnglvs afragvpgyt plppppppms
      781 rfsnye
//
LOCUS       WP_176017132             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Pantoea ananatis].
ACCESSION   WP_176017132
VERSION     WP_176017132.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22581
     Region          1..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mlissimaia avlimgvisp gpsfiyvarn avvhsrlhgi vtalgtgvga aifalvamlg
       61 lqrllllvpe lfvvmkvagg fyllwlafni fkgasqpvhl alngqnghsk twlktfrdgl
      121 ltqlsnpkta iifasifsal lpknipllfy vviplmsfli dfvwysivsv alsaekprqv
      181 ylriktsvdr vssavlgilg iklisssftk
//
LOCUS       WP_176017175             190 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Pantoea ananatis].
ACCESSION   WP_176017175
VERSION     WP_176017175.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449350
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..190
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=21001
     Region          6..>188
                     /region_name="SpoIVCA"
                     /note="Site-specific DNA recombinase SpoIVCA/DNA invertase
                     PinE [Replication, recombination and repair]; COG1961"
                     /db_xref="CDD:441564"
ORIGIN      
        1 mteirigyar cstdrqdlta qqealvklgv tpdriyidkg ltgsnrqrpg ldqalaavrs
       61 gdtlvvpkld rlarsvpdar eiadalqarg vklalgtniy dpadpmgkmf fnvlatfaef
      121 evdlirlrtr egmaiarakg klrgkqpkls dkqqkelcrm hgsgeysisd laelfsvsrp
      181 tvyrtltrhk
//
LOCUS       WP_176017209             292 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Pantoea ananatis].
ACCESSION   WP_176017209
VERSION     WP_176017209.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..292
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31809
     Region          10..287
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mqtksrvdiv gerirsrehq lsprllavah yinsnretvl dstamdiada nhtsdatvir
       61 aiqalgfsgl rdlkkvlqaw fgpgmsseek mtttvndvtr dvtssidfvl qghlhachvl
      121 sseqnrqala eatglmiear qvaifginas giladysarl lnriglvsfs lnragialae
      181 qmlalqrgdv limmaqksah regstvvrea krlgvpiill tnatdsffar eadvvinvpr
      241 ggekgriplh gtvmvclemm ilsvasslpd rtvktmkrlq dlyrglkpaa kk
//
LOCUS       WP_176017210             709 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Pantoea ananatis].
ACCESSION   WP_176017210
VERSION     WP_176017210.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..709
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78335
     Region          15..709
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mkkrsneikn lgiqqavmla mcsgallasg kglaavsdnt vtvtsdaerh dgytipttsv
       61 askapvarld eaqsvstvtq qqlddyqans lsdamrfvsg vseantlagt edgfvrrgfg
      121 snsdgsvyrd girssqglnl dattervevl kgsasllygi qnpggiinvi skkpqyswhs
      181 avsgryaseg ggagtldvtg plgngvafrl iaekqrqdyw rnfgsdehsl lapslqwyge
      241 kasllisysd yrydipydrg tafingspls lpykqrlddk anhawgrnqa lnahydwqfn
      301 dswstrltlg wnqrrydnne vrvtaidpas gvvtrradan rgfnqktkyv swdvlgnpel
      361 fgmthalvfg tdyemnqtyr ahqyqgkndr rfnyfnpvyd mfspvtdstt entanannln
      421 rihsrsvyvk nsisltsdwi avvggryqhy eqraskgfnp vvqtlddegn kflpqagliy
      481 kitpdislyt sisksftpst dvddagnvsq peqgttweag skwqitprlf asvafynide
      541 rqmslsingt prpinkarsq gvelevngev apdwdisany sydnaeivdd rinpannghr
      601 lqnapehaga lylshnlvir slpgdfrvgg garyvgsrag dpdnsfslpd yvvadgfiaw
      661 nnqllgtktq lrlnlnnlfn khyytssggn lrvregetrn lmvqarvef
//
LOCUS       WP_176017317             112 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Pantoea ananatis].
ACCESSION   WP_176017317
VERSION     WP_176017317.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 112)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10657338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..112
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13037
     Region          14..79
                     /region_name="Trans_reg_C"
                     /note="Transcriptional regulatory protein, C terminal;
                     smart00862"
                     /db_xref="CDD:214866"
ORIGIN      
        1 mliinngkvs fkkkrvsltk yeykffefli knmessnyes lldfvwgqrk cvvsyntvsq
       61 layrlrvklr asgiplviri sqkegpclkf dekiivlkkg gsiwswrini lk
//
LOCUS       WP_176017213             778 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Pantoea ananatis].
ACCESSION   WP_176017213
VERSION     WP_176017213.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..778
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=83583
     Region          28..778
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mthdqndllh sgnavdskgd hneryrrapa slsglgtprt rgdgevkvtg karyaiehtp
       61 enavhgvviq stvasgrirh mdttkaesaa gviavythln slkihqptai adggaaqtty
      121 tpiqddviih ngqniglvva etfeqatyaa slveidydtt palisptdeg vepkplppqd
      181 iemgdaqsam nqsevrinqr yttpreynmp mephgciaqw endhmivwep sqwvmgaqve
      241 iaewmgispk qvriispyvg ggfgskpvpy thvalacvas ralnrpvrvs ltrpqtftgl
      301 ggrpatsqql emgatregki qsvilrsfse tslidvfaen cskvtgrmya ienlsaqhqv
      361 rpintvtpgw mrapgenpsa fglevamdem ayaldldpla frllnwadrd yqkdlpwssr
      421 rlkeayqkga eafgwdkrvm aprsmregre ligwgmasgt ypvntmpaea killspqgqf
      481 vvqcagadig tgtytilaqt aadilgvdsq ridvelgdtq lpragvaggs qlagnltaav
      541 dvtakklrar llalasqtsg splagishdq ltlaqggihl takpsqaidl gallklanln
      601 glsveggtfs pnmsaqerds vtgslnemsr pdtvsahsws aqfvevrvde dfgtirlkrm
      661 vaafdsgrly npklarsqwv ggmimgvgqa lleggiidpr ngrvinnnla dylipvnadi
      721 peittidvge pdyqatsmgg ktvgelgivg vaaaisnavy hatgkrvrdl pitldkil
//
LOCUS       WP_176017322             153 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Pantoea ananatis].
ACCESSION   WP_176017322
VERSION     WP_176017322.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..153
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17460
     Region          1..140
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mldkkdkell rllqrdcslc lqelaaaidl tpnpcwkrik rledegfitg rvallskdkl
       61 hlsltaflmi ktqnhshdwy kqfvsqvnsm pevigffrtt geydyllqvv vsdmkaydrf
      121 ykklassvsg lsdvtssfsm edikyttqlp llg
//
LOCUS       WP_176017380              98 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Pantoea ananatis].
ACCESSION   WP_176017380
VERSION     WP_176017380.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..98
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=10964
     Region          17..69
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mknfytvktl sqlrplliaf rkekgltqkd iserlgvtqq tyarmeanpa sagierlyrv
       61 ltllgveinl sseasssdve rmeettslsd sparlekw
//
LOCUS       WP_176017414             297 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Pantoea ananatis].
ACCESSION   WP_176017414
VERSION     WP_176017414.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..297
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=31919
     Region          1..297
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mfkglsafpl tpfmsgspde ksflrilrrl tdakvgslgv lgstgsyaym treqreqiar
       61 lavdnadnip vmvcvgavsa devlrladda qeagasalll pplsyqalye eevyelfemv
      121 arnvsvplcv ydnpgkthft fsdnlhrkia tlpavhslki ppvpsdmeaa asrvrnlrai
      181 lpadvtigis gdssaangli agcevwysvf gglfpdvakk itdaavagdh tavrehhgrl
      241 splwelfhqh gggfriiaaa asilgmaden clprpllpir gerfaelkhv isslelt
//
LOCUS       WP_176017428             406 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Pantoea ananatis].
ACCESSION   WP_176017428
VERSION     WP_176017428.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..406
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43229
     Region          23..395
                     /region_name="MFS_MdtG_SLC18_like"
                     /note="bacterial MdtG-like and eukaryotic solute carrier
                     18 (SLC18) family of the Major Facilitator Superfamily of
                     transporters; cd17325"
                     /db_xref="CDD:340883"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,229,232..233,236..238,241,268,272,324..325,
                     329,333,349,352..353,356..357,360)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340883"
ORIGIN      
        1 mntsplnats esthdnrrmq lllctavfll vsgtgiiapl lapyagtmgi styaigflfs
       61 gfyivrliig tpvgffseky garttlivsl vvypfvslty ffagdavtll garllhgias
      121 ammlpmamay mgnislrgke gyyigilntv ilsagafgpv aggfiaqywg fraafsclff
      181 lslisllvvi llprenptpd rsrnsvtsds apqtnatltr gvivlamfnt viavfdifii
      241 sffplyalkm nlspsvlgtl iavnslimag lqipfgrlvd rhsrqacili svigmsvsll
      301 ltpvisgyaa waglcffvct tavsvalcma gvsalsvetg kkngmgrimg flgsassfgm
      361 vigpmlnafl vdrvsydsif yvtaalwllt gavfvcvtrg shhdhh
//
LOCUS       WP_176017431             707 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Pantoea ananatis].
ACCESSION   WP_176017431
VERSION     WP_176017431.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..707
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=79753
     Region          241..600
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 msphtpiess wrpfdmneyw lersltsaer ttlassgsrs amlrmkpapd lirpltdiaa
       61 gsgcgskvta liiarllrem htsgtpcwcw pqerwlticr evregrplma aftwhlagfy
      121 dplslpdirk palyasaifg qdfyhqeldr ltdtltslgy apasqknhvs gilatlmivn
      181 rdprletftp ellwqvqsgm eagtsryvgr vshalaalgi isapmrmrny tkwyekpveg
      241 idpawvhwcr rwretsvlrp rtretqysfa lrcglwlare hpvvrepadw tmetcasfia
      301 avgrmnvdel qlgtergtrk smrsgepmmp hsranfiysl rrfmidyenw gwgrlrfspa
      361 rhlstpdtpl frrgvnprvi ddpvwlkliw asmnlrqedl lteihyplsm lqamaviwth
      421 aglrksellr lttgciapqa deivkedgsi itagtlcylh ipagktskaf vkpvaavvkk
      481 yvdiwlderp aeqamlader tgekvrllfq yrgkpaggti lnrtvipmlc aragvpveds
      541 ggmitshrgr asavtalasv pqgmslyelm qwtghstpqs tlhylrirpt qlaasfvkad
      601 rvahmisvli dhdpeaaslt gpatyydlgd syctnpfwss cqhrmacigc dfnllkqsar
      661 glvleskvsv rryleevpit pderaiveqd aekieqaler ltlkper
//
LOCUS       WP_176017523             412 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Pantoea ananatis].
ACCESSION   WP_176017523
VERSION     WP_176017523.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..412
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44240
     Region          18..381
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(28..29,32..33,36,68,123..124,126..128,131,151,
                     154..155,158,230,233..234,237..239,242,266,270,323..324,
                     328,332,348,351..352,355..356,359)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mhkgvstged allqhrsfva fwlartcssf gfqmfsvavs wqiyaithsa malgmiglmq
       61 flpsvllalp aghladqfdr rrivvigqli ewaallalva ltllhwadki eiwglvflia
      121 lakalewpai tsmlpalvpp silaramaas svggqaaviv gptlggllyv agpevvygvs
      181 alfyllslil vsrlryerpp qermpmtlsn mfmgvrfire rkdvlgvisl dlfavllgga
      241 tallpifaqd ilhtgpwglg llrgapsvga llvgvwlsrn klekhvgmim fgsvagfgla
      301 tllfalstkl wlsllalaal ggfdmvsmvi rgalvqldtp dmmrgrvnav naifintsnq
      361 lgefesglla awmgavpaav iggvgtlvvv glwmtlfpnl rkrqklenet ve
//
LOCUS       WP_176017633             424 aa            linear   BCT 11-JAN-2025
DEFINITION  YeaH/YhbH family protein [Pantoea ananatis].
ACCESSION   WP_176017633
VERSION     WP_176017633.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Ruggeri,Z.M.
  TITLE     Von Willebrand factor
  JOURNAL   Curr Opin Hematol 10 (2), 142-149 (2003)
   PUBMED   12579041
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Whittaker,C.A. and Hynes,R.O.
  TITLE     Distribution and evolution of von Willebrand/integrin A domains:
            widely dispersed domains with roles in cell adhesion and elsewhere
  JOURNAL   Mol Biol Cell 13 (10), 3369-3387 (2002)
   PUBMED   12388743
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Tuckwell,D.
  TITLE     Evolution of von Willebrand factor A (VWA) domains
  JOURNAL   Biochem Soc Trans 27 (6), 835-840 (1999)
   PUBMED   10830113
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11148708
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..424
                     /product="YeaH/YhbH family protein"
                     /calculated_mol_wt=48925
     Region          13..420
                     /region_name="DUF444"
                     /note="Protein of unknown function (DUF444); pfam04285"
                     /db_xref="CDD:427839"
ORIGIN      
        1 mayfidrrln gknksavnrq rflrryksqi kqsiseaink rsvtdvssge svsiptddis
       61 epifhqgrgg qrhrvhpgnd hfvqndrver pqggggsgsg qgnagqdgeg qdefvfqisk
      121 deyldllfed lalpnlrknq hrqlneykth ragftsngvp anisvvrslq nslarrtamt
      181 agkrrqlhel edalttveks epaqlleeer lrkeiaelra ridrvpfidt fdlryknfek
      241 rpepssqavm fclmdvsgsm dqatkdmakr fyillylfls rtyknvevvy irhhtqakev
      301 deqeffysqe tggtivssal klmddvvker ydpaqwniya aqasdgdnwa ddsplcheil
      361 aknilpvvry ytyieitrra hqtlwreyeh lqsvfdnfai qhirepediy pvfrelfhkq
      421 amea
//
LOCUS       WP_176017685             144 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Pantoea ananatis].
ACCESSION   WP_176017685
VERSION     WP_176017685.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..144
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15629
     Region          33..137
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mfsginqlfi rmtdhpdlgk lllrltlggl llfhgefklv hgvgwiaqll hqhglpgfla
       61 wgawigeiia plmlivglmt rpaafivavn mvvatllvkt galwhrtgvg awsletealf
      121 llgalvimll gsgrftlird srlq
//
LOCUS       WP_176017711             153 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Pantoea ananatis].
ACCESSION   WP_176017711
VERSION     WP_176017711.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 153)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140385
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..153
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17079
     Region          5..143
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04685"
                     /db_xref="CDD:467568"
ORIGIN      
        1 mrtrrsarll ilnashnlll frfvhtqdal aghaywatpg ggveegesfe qaalrelyee
       61 tgirrndpgp srrercfvmt lpsgervqah erffiinvsg deidtlgwse neksviasyq
      121 wwsisalnat tetvypgnlv emltsmdsds sgk
//
LOCUS       WP_176017736             194 aa            linear   BCT 11-JAN-2025
DEFINITION  YceI family protein [Pantoea ananatis].
ACCESSION   WP_176017736
VERSION     WP_176017736.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..194
                     /product="YceI family protein"
                     /calculated_mol_wt=21179
     Region          19..194
                     /region_name="YceI"
                     /note="Polyisoprenoid-binding periplasmic protein YceI
                     [General function prediction only]; COG2353"
                     /db_xref="CDD:441920"
ORIGIN      
        1 mknvkrftlp llaaaalyvp vsqaeamhyq ldpqhtsvvv swehfgfshp tadipdttgs
       61 lvfdsskpeq srvdvtlpvs kidshvpalt refkgaeyfd vakypsatfr stkviakgdn
      121 kfdvegnltl kgitkpvtlh atlnkqgehp mvkkqaigfd atgtikrsdf kldkyvpavs
      181 ddvtltiste ayak
//
LOCUS       WP_176017740             340 aa            linear   BCT 11-JAN-2025
DEFINITION  dipeptidase [Pantoea ananatis].
ACCESSION   WP_176017740
VERSION     WP_176017740.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..340
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36706
     Region          1..337
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 mlvfdghndl llnlwlyhrd apaeafyagv pkghldfprm qqggfagglf avfvppqdyl
       61 aqvaparaaq epydpltimw qqlailqqia aqsagrarlc hsaaeieacr vegvlalvah
      121 iegadaldae getlnafyqa gvrsigpfwn lknrfgegvn gsfpgspdtg pgltaegeal
      181 irqaaalnmm idvshmneka fwdtvrlsaa plvashsnah vlcaqprnlt dnqlkaihas
      241 gglvginfgn aflradgkrd sdtdlteivk hcdhlinimg edhvafgsdf dgisppealg
      301 dvsglprlla vfrdsgydqr mlekltwgnw lrvlqhtglh
//
LOCUS       WP_176017745             391 aa            linear   BCT 11-JAN-2025
DEFINITION  benzoate/H(+) symporter BenE family transporter [Pantoea ananatis].
ACCESSION   WP_176017745
VERSION     WP_176017745.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Collier,L.S., Gaines,G.L. 3rd and Neidle,E.L.
  TITLE     Regulation of benzoate degradation in Acinetobacter sp. strain ADP1
            by BenM, a LysR-type transcriptional activator
  JOURNAL   J Bacteriol 180 (9), 2493-2501 (1998)
   PUBMED   9573203
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Neidle,E.L., Hartnett,C., Ornston,L.N., Bairoch,A., Rekik,M. and
            Harayama,S.
  TITLE     Nucleotide sequences of the Acinetobacter calcoaceticus benABC
            genes for benzoate 1,2-dioxygenase reveal evolutionary
            relationships among multicomponent oxygenases
  JOURNAL   J Bacteriol 173 (17), 5385-5395 (1991)
   PUBMED   1885518
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459726
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..391
                     /product="benzoate/H(+) symporter BenE family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042925 - benzoate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0042919 - benzoate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=40157
     Region          3..389
                     /region_name="BenE"
                     /note="Predicted benzoate:H+ symporter BenE [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3135"
                     /db_xref="CDD:442369"
ORIGIN      
        1 msarrapfpv tlpmavsglv avlvgysstg aiiyqvalsa gassaqiagw lsviglamgi
       61 asaglslayr mpilaawstp gaallatslq gasireavgv fvfanalivl cgvtglfarl
      121 mnyipaslaa amlagillrf glqtfsdlav nftlagamcc vwllarrwla ryailialla
      181 glavaygqns lhfpahaasf slpgpvwptf swpvligvgl pyflvtmasq napgiatlha
      241 hgyrppvsal mswtgllalv lspfggfsvc vaaitaaicm gedvdvdprr rwiaaalagf
      301 fyllagfsga liavlfsalp avmvqvlagl allatlggsl qraleqpeer dsaliaflit
      361 asgvtlcgig aafwglvggv vahlllkrkt a
//
LOCUS       WP_176017762             455 aa            linear   BCT 11-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Pantoea ananatis].
ACCESSION   WP_176017762
VERSION     WP_176017762.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..455
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=48724
     Region          22..443
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 mksttdlnmv nayipgqvdv gpvtaamiqr rdallgpayr lmyehplhiv rgegvwlfdp
       61 egrryldiyn nvtslghchp avteaicqqv qtlatntryl hdtilelaer llatvpetal
      121 ahlmltctgs eandlayria kvrtggtgii vtetayhgit davsqfspsl gtsvdlgahv
      181 rlipaprlyh aegadlsesf trdvenaiad lqrhgikpaa livdslftsd gilpgpvgfm
      241 kgaveaikra ggvfiadevq pgfgrtgetm wgfqrhgvip dmvtlgkpmg ngqpiaglla
      301 tadvlaefgq rsryfntfag ntvscaaala vlktierdgl vahardvgkq lldgitalgk
      361 rheaigdvrg aglfvgvelv sdrlsrtpdr wltsqvvnrm rqkgvllsac amghnvlkir
      421 pplvltadqa gmiidvldqs lteataaras qsvlr
//
LOCUS       WP_176017781             213 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Pantoea ananatis].
ACCESSION   WP_176017781
VERSION     WP_176017781.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..213
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23433
     Region          24..188
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mspftlvvmn sqlstackhr ergrprefnm eqaldkamiv frqkgyhaas ladlgeamnl
       61 svgsiykafq dkrslfllvf qryiavrnad lrerlaqydt graklsellq fyldssrgge
      121 grtgclvvgs aielqvldae lsqlvaqvin rnkhflmsll eegqhdgsis adldietaag
      181 lilriafgmr vtgkvadvan eqatialalk ild
//
LOCUS       WP_176017797             273 aa            linear   BCT 11-JAN-2025
DEFINITION  C40 family peptidase [Pantoea ananatis].
ACCESSION   WP_176017797
VERSION     WP_176017797.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..273
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=30537
     Region          48..266
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mrsiitllil afaqlffnva saspqapvka slhkvekksa rederrkrrt vkasakksrs
       61 saeqkssktl ktsknpshav ashktltkat dshkkltkkv aanatskkry ghqravkvak
      121 adskdigtik msnahrqryq karetamakl mgqlgkryqw ggksphtgfd csglvwyayk
      181 dvvkfkiprt anemyhlrda apvnrealek gdlvffring rgtadhvgvy lgngkfiqsp
      241 rtgkdiqisa lsedywqrhy igarrvmtpk tvr
//
LOCUS       WP_176017805             478 aa            linear   BCT 11-JAN-2025
DEFINITION  protein adenylyltransferase SelO [Pantoea ananatis].
ACCESSION   WP_176017805
VERSION     WP_176017805.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Dudkiewicz,M., Szczepinska,T., Grynberg,M. and Pawlowski,K.
  TITLE     A novel protein kinase-like domain in a selenoprotein, widespread
            in the tree of life
  JOURNAL   PLoS One 7 (2), e32138 (2012)
   PUBMED   22359664
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10011099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..478
                     /product="protein adenylyltransferase SelO"
                     /EC_number="2.7.7.108"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0070733 - AMPylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53836
     Region          3..478
                     /region_name="PRK00029"
                     /note="YdiU family protein"
                     /db_xref="CDD:234583"
ORIGIN      
        1 mifdnswfre lpgsytalnp tplaggrlly hnaplakama ldsalfsgqg hgvwygaall
       61 pgmaplaqvy sghqfgvwag qlgdgrgill geqrledgrr ldwhlkgagl tpysrmgdgr
      121 avvrstvref lasealhhlg ipttraltla vsdepvyret aergamlmri apshlrfghf
      181 ehffysqqpe qvkqladyai hhhwpqlvde adryqlwfad ivlrtarlia qwqsvgfahg
      241 vmntdnmsil gltldygpyg flddyqpdyi cnhsdyqgry sfenqpmigl wnlnrlahal
      301 sglmsteqlk qalsgyenal mrvwgermra klglltadag dneiltells lmsqersdyt
      361 ltfrllsdtq qaesrsplrd efidrsafdr wyqryrqrll qeqvgdaerq qvmkaanpav
      421 vlrnylaqqv ideaekgesg alarlhqalq qpfsdaaaae yrqrppdwgk tlevscss
//
LOCUS       WP_176017849             248 aa            linear   BCT 11-JAN-2025
DEFINITION  YoaK family protein [Pantoea ananatis].
ACCESSION   WP_176017849
VERSION     WP_176017849.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..248
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=27190
     Region          1..216
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mlvrkkrmrs hsedrhlalt mattagmlnt malcafgifp shmsgntsqi paevfssnfs
       61 kltlliglia aflagctmar litllgemlk irtifciili legvilatas lfeslfyspl
      121 hnsgllatma fmmglhntts tqlsngrvrs thitgtitdv gialgtyiws fiipktlcnr
      181 yfaykqlcth litivcflsg citgmllfkg yaframlaia iiliiyatta ivmtlhnvrn
      241 fkkrstit
//
LOCUS       WP_176017850             140 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Pantoea ananatis].
ACCESSION   WP_176017850
VERSION     WP_176017850.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..140
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15079
     Region          9..135
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mikgitvfnk ltnhpdagkl llrltfgilv mfhgiakilh gtqwistile tkgipgfiay
       61 gvfageiiap ifiilglmtr paaliyafni liatllvgid rfftvtkvga wgletealff
      121 fgaisimlig sgkysmttds
//
LOCUS       WP_176017869             265 aa            linear   BCT 11-JAN-2025
DEFINITION  inositol monophosphatase family protein [Pantoea ananatis].
ACCESSION   WP_176017869
VERSION     WP_176017869.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Neuwald,A.F., York,J.D. and Majerus,P.W.
  TITLE     Diverse proteins homologous to inositol monophosphatase
  JOURNAL   FEBS Lett 294 (1-2), 16-18 (1991)
   PUBMED   1660408
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001594
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..265
                     /product="inositol monophosphatase family protein"
                     /calculated_mol_wt=28306
     Region          25..257
                     /region_name="SuhB"
                     /note="Archaeal fructose-1,6-bisphosphatase or related
                     enzyme, inositol monophosphatase family [Carbohydrate
                     transport and metabolism]; COG0483"
                     /db_xref="CDD:440251"
ORIGIN      
        1 mtkndldkpr lllaakraar aggaelvkrf gsledtdisk kgtadyasaa dlaaesiifs
       61 rlnedapgfg flgeetgftr ghhsqywvvd pldgtsnfiw gipyfavsia lcddegeilg
      121 vvydplreec ftairghgar ldgmplpglt aktpaealcs vslpvpgqlk vidqavlfng
      181 ltrlmaesag vrrlgsaald layvasgrld affedglsyy diaagkliaq engiqvrqfs
      241 geeahegsvv aarpelyswf hgsfs
//
LOCUS       WP_176017906             306 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Pantoea ananatis].
ACCESSION   WP_176017906
VERSION     WP_176017906.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..306
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33628
     Region          1..305
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtirigvvgl ggiaqkawlp vlsqarawql vgafspnqan aqvvceryri pcfstlnala
       61 aacdavfvht stashyevvh allqagkdvc vdkplaenls qaealvtlae kkqrrlmvaf
      121 nrrfapayqq lkdemasvas lrvekhrsds vgpqdlrftl lddylhvvdt alwlaggrsl
      181 prqghistne qgqmlyaehh fnagqlqvtt smhrragsqr ervsaigdgq cidihdmrdg
      241 qvergagvvi tpspswqshl aqrgfvgaae hfiqcvenqt kpetsgeqal laqrvvesmw
      301 rdaere
//
LOCUS       WP_176017505             487 aa            linear   BCT 11-JAN-2025
DEFINITION  serine/threonine protein kinase [Pantoea ananatis].
ACCESSION   WP_176017505
VERSION     WP_176017505.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Hanks,S.K., Quinn,A.M. and Hunter,T.
  TITLE     The protein kinase family: conserved features and deduced phylogeny
            of the catalytic domains
  JOURNAL   Science 241 (4861), 42-52 (1988)
   PUBMED   3291115
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424655
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..487
                     /product="serine/threonine protein kinase"
                     /EC_number="2.7.11.1"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=52683
     Region          36..455
                     /region_name="SPS1"
                     /note="Serine/threonine protein kinase [Signal
                     transduction mechanisms]; COG0515"
                     /db_xref="CDD:440281"
ORIGIN      
        1 msendnhqnv pnalpigyrf nefeikdvig gggfgivyra wdhqlerdia ikefmpasla
       61 vrsddlnlvl rserfsktfh aglnsfiqea rllarfnhpn llhvlrfwvq ndtaymgtvf
      121 ysgttlsnmr erhphliden wirrllppll gaiktihdag ylhrdisldn iqiqsngdpv
      181 lldfgsarkt ignlsdeset mlrpgyapie qysdndeseq gawtdiyalg avlhtlitga
      241 pppvsvvrsi ednyqplvqr apagysatll aavdsalslk pedrpqsida faasmvlpek
      301 apeplpevkh sgpgtmlvpi qeedeaaaaa atplkklmrn rfvlpglvaa gvlvgvcvgl
      361 lmaggdkdgd apanvaqtet apatqapaeq paatpvqtqt aqaepekpqe pvapppepva
      421 qvyiklqpge rvqvngkpqa vvpaangfaa lqlapgnytf svtgqggere qtltinqqgv
      481 wlldphi
//
LOCUS       WP_176018017             397 aa            linear   BCT 11-JAN-2025
DEFINITION  zinc-dependent alcohol dehydrogenase [Pantoea ananatis].
ACCESSION   WP_176018017
VERSION     WP_176018017.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 397)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..397
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42454
     Region          1..388
                     /region_name="FDH_like_1"
                     /note="Glutathione-dependent formaldehyde dehydrogenase
                     related proteins, child 1; cd08283"
                     /db_xref="CDD:176243"
     Site            order(38..40,43,86,170,174,193..194,196..198,217..219,223,
                     238,264..266,290,307..309,332..334,374)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176243"
     Site            order(38,40,60,170)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
     Site            order(90..91,93,96,104)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
ORIGIN      
        1 mkaltyhgph kvsvdnvadp gleaaddiil rvtataicgs dlhlyrgkip gtdhgdifgh
       61 efmgevveag savtavakgd rvvipfviac gdcffchlhq yaacentnsg kgaalnrksi
      121 tppaalfgys klyggvpggq aeyvrvpkan agpfkvpntl sdekvlflsd ilptawqavk
      181 naeikqgssv aifgagpvgl lsaacarqeg aeqiymvdhn dyrlnfarer ygvipinfdn
      241 nddpaawiie hsaghrgvda vidavgfeak gsmtetvltn lklegssgka lrqciaavrr
      301 ggivsvpgvy agfihgflfg dafdkgltfk mgqthvhayl pdllnliekg hltpeeivth
      361 hmpledaarg yeifekreea crkvilvpgm mptqatl
//
LOCUS       WP_176018173             237 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF2076 domain-containing protein [Pantoea ananatis].
ACCESSION   WP_176018173
VERSION     WP_176018173.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007341
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..237
                     /product="DUF2076 domain-containing protein"
                     /calculated_mol_wt=25435
     Region          1..236
                     /region_name="COG3416"
                     /note="Uncharacterized conserved protein, DUF2076 domain
                     [Function unknown]"
                     /db_xref="CDD:442642"
ORIGIN      
        1 mqreeqelie nlfsrlkqae sqtaardaaa eqlikqhlqa qpgapyymaq ailiqeaalk
       61 klnervqele nhlaqqqaqq qqqpkssggf lsslfgggsq qaqpaqpspq wnsapqqpqp
      121 yasapaprgs gflggalqta vgvaggvvma dmltsmfhhs qpeeivniin epqslpqvdd
      181 slntfnggnd qsflgqgtga dnqsfldqsn gwsdtyadng dlndfggndy ddddsfv
//
LOCUS       WP_176018211             290 aa            linear   BCT 11-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Pantoea ananatis].
ACCESSION   WP_176018211
VERSION     WP_176018211.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..290
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31956
     Region          1..252
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mieqwqvdqy hqqgflvveh vltseeiaal qhdfdqwvee srsqsapwgn tqdgrsrfdi
       61 esdhsadhps lrrvsspndi saayrhaalq srmaqiagql iggcgaryhh skinsklpht
      121 atkvewhqdf lftphsnddi vtallmvsev tpengplnvv pgshrgplys hwqdgrftga
      181 vepavvkeqc qqpsacfgps gsvcfmhtrl lhasspnete wprtlfiavy aaedalpfge
      241 nplpspdagt lvygdesgmv rstpnelrlp qkprgasffv qqagqdlanv
//
LOCUS       WP_176018266             149 aa            linear   BCT 11-JAN-2025
DEFINITION  GGDEF domain-containing protein [Pantoea ananatis].
ACCESSION   WP_176018266
VERSION     WP_176018266.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 149)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 149)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 149)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..149
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16223
     Region          <15..139
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mtlrcllnpw rfkqcviaid idhfknindt fghdkgdlvl vslasllkqs crpndivsrs
       61 ggeefilllp nmplaegmat aerirqavys aifpgvgkmt isagvavfng pdgareeglh
      121 yadkalyqsk rngrnrvsis etggiyltl
//
LOCUS       WP_176018323            1046 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Pantoea ananatis].
ACCESSION   WP_176018323
VERSION     WP_176018323.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..1046
                     /product="DEAD/DEAH box helicase"
                     /calculated_mol_wt=116054
     Region          237..>663
                     /region_name="BRR2"
                     /note="Replicative superfamily II helicase [Replication,
                     recombination and repair]; COG1204"
                     /db_xref="CDD:440817"
ORIGIN      
        1 mkagfnskrl fgitrskgkm yefgldeslh lrvpegsdpl qlfvmtvatl gdvtgvlael
       61 shpltplppe tqaelnfcas ffdavldsgf ahgleritll lasaayyvar rpgsslvlar
      121 rieyraegnk vehflqwllk adwstywpld dvrygsllss isnsvithfa egtqlqhies
      181 llkhlrsevy kmgtaeelly advaisvcrm rlaasawstl pqysglsvey wrpviqrghf
      241 pkelwpsqll lgakgiysgv sgliqmptsa gktrsielvl rsafmsartr lavvvapfra
      301 lcheialslr qdlagddikv neltdalqid fveqiaellg stppsisnvl vltpekflyv
      361 lrqssqvlkh vglvvydegh qfdtggrgit yelllteikk llpgtaqtll isavmqnpla
      421 iaswlmgadk aqvidgatll ptsrsvafas wteslgqlmf hengydredy fvpriieaae
      481 lsrlkadsam fptrakssdv slylglrvvg kgsvaifcgt kiiangiakr avqiaeagyn
      541 tvwpsayanl eeinalktli egnfgsdall skaaklgiyt hhsntpqgir lalehgmqkg
      601 linfiactst laqgvnlpir ylivqgvnqg agrvkvrdfq nligragrag mhtegvvifa
      661 dstvwdrrnn rqeswrfqsa vellspdhae gvtsslllll kpfalprnqe wtfkggdlld
      721 fmeketewds wahhvankfp rlkksqkdal vrsllrslae rkkmtdtles ylmanctttd
      781 tvafeqrage laretlaysl asaeeadkle eyfrlvarri esiesspvkq affgktlmga
      841 kqtkrietws dehrdvlltl dssdawltav wplltelcdn rffrsvepvd agfqialmwm
      901 sgtsygeifr qalqmkvkkk vgnlerkvsd ddilqfvest lafdcalila alaqflftqe
      961 dltgepgasl anfqkslkyg lpdklsmnvf eagfadrfis qavrdallqd gyegsvfdea
     1021 rknhlsaiey viqaapayfk yvlssy
//
LOCUS       WP_176018361             814 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Pantoea ananatis].
ACCESSION   WP_176018361
VERSION     WP_176018361.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 814)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 814)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 814)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 814)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..814
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..814
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=88337
     Region          3..782
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mmsfsphpva laiaglcclt pgsvwaetft slppppavdn saagqrymle lvvnqqargd
       61 ivpveqqngh flvragdlqr agippekyqg qqqvdvnqla evkvdyddrr qrllltvppg
      121 wlpeqtiges ntgprfpgrv spgalinydl yatrtdvagt rlaawnelrl fgdaghissn
      181 gvwqqqlegq nryqddgyir ydtwwsnene nailswrvgd lttdalawts svrlggiqva
      241 rdfsvrpdlv typlpafsgq aavpstvdlf vngyrstqan vqpgpwsltn vpfvngagna
      301 vitttdavgr qvvttlpfyv ssnllkpgls dyafsagamr qnygiknady gaaamsgswr
      361 ygmtdwltle thgegsnhlg mggagaqfkv gswgvingaa aqsqmdgqsg aqyswgyqyn
      421 nsrfslgtqh qvrnagfgnl allsnqrngg sdyryslarr taqysasisl nrygslgaay
      481 idisggdnqr ttlwnlswsk nlwgnaslyv sasrdrqqge wsgavslvip fgensnasls
      541 verdqqgrhn qraylsramp sdggfawdas wanqggnsgd yrqgslryrn nkidtsggfy
      601 gddgnttqwa dlsgalvlmd nqvfaantin dafvvvktny pdvnvryenq smgrtdskgy
      661 llvpsissyy aakydidtld lpadmttpkv eqrfavkrqs gfllnfpver lraasvilyd
      721 shnqplpvss qvirpgqatg yvgwdgiawl ddlsehnpik viapdgrtck teltlaggqp
      781 qalktygplt cplpplpdga papnpenata gitp
//
LOCUS       WP_176018413             324 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Pantoea ananatis].
ACCESSION   WP_176018413
VERSION     WP_176018413.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Xun,L., Belchik,S.M., Xun,R., Huang,Y., Zhou,H., Sanchez,E.,
            Kang,C. and Board,P.G.
  TITLE     S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of
            glutathione transferases
  JOURNAL   Biochem J 428 (3), 419-427 (2010)
   PUBMED   20388120
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418207
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..324
                     /product="glutathione S-transferase family protein"
                     /EC_number="1.8.5.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36732
     Region          1..324
                     /region_name="ECM4"
                     /note="Glutathionyl-hydroquinone reductase [Energy
                     production and conversion]; COG0435"
                     /db_xref="CDD:440204"
ORIGIN      
        1 mgqlidgvwh dtwydtkstg grfkrsesaw rnwvtpdgsa glsgkaafta erdryhlyvs
       61 lacpwahrtl lmrqlkglds midvsvvhpl mlengwtfdd sfpdatgdkl hqneflyqly
      121 lhadadysgr vtvpvlwdkq qntivsnesa diirmfnsaf davgaragdy ypadlrekid
      181 alngwiydni nngvykagfa tsqsaydeav talfhslsrv eqilgqhryl agdrlteadl
      241 rlwttlvrfd pvyvthfkcd rhrisdylnl sgflrdiyqm pgiadtvnlp hirhhyycsh
      301 ktinphgvis vgpafdwdap hgrg
//
LOCUS       WP_176018523             333 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Pantoea ananatis].
ACCESSION   WP_176018523
VERSION     WP_176018523.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..333
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35109
     Region          16..325
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mrdflprfih thecrllaim tlmivfltvf ttefatlqnl ldvsgatafi gimaagllvv
       61 iitggidlsf aatasitqyv altlannmgl gwvgifavai glgivlgfin gvlvnvlrts
      121 aliitiatln vffgilltvt sgqdifmlpd wfnagfelvf ytdaqgatya lnfqiialvl
      181 afvltwllln rsntgrqiya tggnpdaaqr vgfnvfklnm lvygymgala glaslvqaql
      241 aqsvsptalv greldvvaav viggasltgg kgtvlgtvlg vvliavmqng lillgvssyw
      301 slfstglvii aamimmaret rkqnklvdeg ais
//
LOCUS       WP_176018281             300 aa            linear   BCT 11-JAN-2025
DEFINITION  homoserine O-succinyltransferase [Pantoea ananatis].
ACCESSION   WP_176018281
VERSION     WP_176018281.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Raushel,F.M., Thoden,J.B. and Holden,H.M.
  TITLE     The amidotransferase family of enzymes: molecular machines for the
            production and delivery of ammonia
  JOURNAL   Biochemistry 38 (25), 7891-7899 (1999)
   PUBMED   10387030
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012359
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..300
                     /product="homoserine O-succinyltransferase"
                     /EC_number="2.3.1.46"
                     /GO_function="GO:0004414 - homoserine O-acetyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008899 - homoserine
                     O-succinyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0019281 - L-methionine biosynthetic
                     process from homoserine via O-succinyl-L-homoserine and
                     cystathionine [Evidence IEA]"
                     /calculated_mol_wt=35040
     Region          1..295
                     /region_name="PRK05368"
                     /note="homoserine O-succinyltransferase; Provisional"
                     /db_xref="CDD:235433"
     Site            47
                     /site_type="active"
                     /note="proposed active site lysine [active]"
                     /db_xref="CDD:153225"
     Site            142
                     /site_type="active"
                     /note="conserved cys residue [active]"
                     /db_xref="CDD:153225"
ORIGIN      
        1 mpiyfhdelp sakkirnfhi ksfndkelsv inqssislli lnlmpdkiet eyqilnllsq
       61 lpthididfl rldhiehknt sklhinkfyl pfnlikdnky dglivtgapl evidfekikf
      121 wdqlvkiinw aknnvgsslf icwavqaaln ilydtpkkhr knklsgvfth hltdnedglv
      181 qgfdevfyai hsryadypvs ylkentdlrv laetvthday ffssydkrfv fvtghpeydr
      241 ltlsneylrd tlrglsptlp enyfpnddvl rnphftwrsh gvlvfsnwin fcllqkistk
//
LOCUS       WP_176018529             186 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA-3-methyladenine glycosylase I [Pantoea ananatis].
ACCESSION   WP_176018529
VERSION     WP_176018529.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..186
                     /product="DNA-3-methyladenine glycosylase I"
                     /EC_number="3.2.2.20"
                     /GO_function="GO:0008725 - DNA-3-methyladenine glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=20987
     Region          1..185
                     /region_name="Tag"
                     /note="3-methyladenine DNA glycosylase Tag [Replication,
                     recombination and repair]; COG2818"
                     /db_xref="CDD:442066"
ORIGIN      
        1 mqrcgwvtqd pvylayhdde wgrpqrdkqa lfemlclegq qaglswitvl kkrqnyraaf
       61 hqfepqtiaq mdaqdiaqlm qnsgiirhpg kiaaiianar amlameakge dfahfvwqfv
      121 dnqpvvnhvv dykkspttsa qaialskalk trgfkfigpt icysfmqacg lindhqtncf
      181 chpdni
//
LOCUS       WP_176018592             163 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Pantoea ananatis].
ACCESSION   WP_176018592
VERSION     WP_176018592.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..163
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17655
     Region          5..142
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mthvddydlk iltllqsngr ltnqelsdlv glsasqcsrr rinleqanli lgyharlspd
       61 avglgmvgli evrlinhtad yvesfhqmve reeaivdayk ttgdadyllk vavadltsls
      121 alisqllagh qsvshvktsv vlgrlkengl mmsaepaarq ksa
//
LOCUS       WP_176018649             791 aa            linear   BCT 11-JAN-2025
DEFINITION  beta-N-acetylhexosaminidase [Pantoea ananatis].
ACCESSION   WP_176018649
VERSION     WP_176018649.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 791)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 791)
  AUTHORS   Intra,J., Pavesi,G. and Horner,D.S.
  TITLE     Phylogenetic analyses suggest multiple changes of substrate
            specificity within the glycosyl hydrolase 20 family
  JOURNAL   BMC Evol Biol 8, 214 (2008)
   PUBMED   18647384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 791)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 791)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..791
                     /product="beta-N-acetylhexosaminidase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004563 - beta-N-acetylhexosaminidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=88323
     Region          1..602
                     /region_name="Chb"
                     /note="N-acetyl-beta-hexosaminidase [Carbohydrate
                     transport and metabolism]; COG3525"
                     /db_xref="CDD:442747"
ORIGIN      
        1 mplrrnvlic ccaltfsaaa dtlplmpwpq qveqparagw ltltpqltlq ivgdtlpgae
       61 trwlsriarq tgwpllpadq pvehptiria isqavnpvpq pdsdesyqld vnrdgvllka
      121 nsrfgamrgm etllqliens aegtripwit ihdkprfawr gilidsarhf mpvrtlkrqi
      181 dgiaaarmnv lhwhltddqg wrfaslrypq lqqkasdglf ytqaemrevv qyaaergvrv
      241 vpeldipgha salavampel isapgpyqme rgwgvfkpll dpsneqvyqv idalvgemaa
      301 ifpdpylhig gdevdpsqwq asaavqqfmr drgladphal qawfnqrvek ilekhqrrmv
      361 gwdeiahpdl phsiliqswq gqdalgtvak ngyrgilstg fyldqsqpas yhyrneiypq
      421 glngkdvvqs geqaqswsft mprlkgspvt gsftlikgrd gwrgfidfag ksrrlvnaid
      481 wlsanrltft vdtwmgpfkp vvtlannqls gymlvgnvry aaegqrldav pkgiqpvlpd
      541 arqmqqnllg geaalwaenv nsaiidtklw prafvvaerl wsaqdvtepd smyqrlaamd
      601 rwttvsvglq qhyqadrqmt rlanstdiqp lrvlaqalep aqyytrqhlk fqaghynyfe
      661 plnrladvlp aesdtvrmle kqvvalvedr snvaaaaair sqlqrwhdna aqvapllngs
      721 aplkalessa kqadelsvmg idmvnayvrn qafgasemaq mhakldaaaq vqdetvialv
      781 rpleallraf k
//
LOCUS       WP_176018654             322 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Pantoea ananatis].
ACCESSION   WP_176018654
VERSION     WP_176018654.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..322
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35535
     Region          5..321
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mppstiavla fngispfhls vpclvfenra geglpafdlr vcavdadena klrtvagftl
       61 hsdltledam qaevlivpsw rsaterppks mlnavrtawq rgatvvglcl gayvlaeagl
      121 ldgqqatthw stvadfsqry pqitllpdvl yldahdgrlv tsagtaagld cclhlvrrwy
      181 gaevanqiar rlvvaphrqg gqgqyieqpl hhqpggdrls dllnwmvanl aeqhtldala
      241 qrvsmsrrnf trrfreltgm tvnqwllgqr layaqrlles trqpienvaq qsgfgsavsl
      301 rqhfnrtfkt spgawrnlfs rd
//
LOCUS       WP_176018706             442 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Pantoea ananatis].
ACCESSION   WP_176018706
VERSION     WP_176018706.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..442
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48426
     Region          16..438
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(30..31,34..35,38,70,120..121,123..125,128,148,
                     151..152,155,267,270..271,274..276,279,307,311,364..365,
                     369,373,389,392..393,396..397,400)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mktspmsqgk patnfrwvvl alifavyavn yadrsnigsv lpfiteefnm tnfeagqias
       61 mfflgyalcq ipagfllakr gvrgivtlsi lgfsaftwli gtassalsik wmrlglgite
      121 aptpvgltst innwfppkek atatgiyias tmfapiivpp lvvwisltlg wrwvfflfai
      181 pglflaviwy llvkskpees qfvspseley irasetasgn evnvenivqh trfatldkli
      241 rvreikplds aakifrsrnv wgntiayfmm vsimygiltw ipsylvtekg fsfvkmgfva
      301 ampfvggfig sifggwisdk ifgrrrkptm iftalativm mvvmihvpqs tamvagalfm
      361 vglllnigwp aftaypmgvv drknypiais lvnsggnlgg fvspmaagyl ldktgqfssv
      421 ftyfgicavi glvllliide pk
//
LOCUS       WP_176018742             322 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pantoea ananatis].
ACCESSION   WP_176018742
VERSION     WP_176018742.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444071
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..322
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36070
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_GltC_like"
                     /note="The substrate binding domain of LysR-type
                     transcriptional regulator GltC, which activates gltA
                     expression of glutamate synthase operon, contains type 2
                     periplasmic binding fold; cd08434"
                     /db_xref="CDD:176125"
     Site            order(107..108,110..111,114,120,122..128,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176125"
ORIGIN      
        1 mklkqlyyfk rlsetehyte aasslfitqp slshaiaele kelgvslffr qgrnvrises
       61 gkcflpyvet alsalengre rlkknhllcr enirigfiyt mgeyvipqii nnysqhfrhn
      121 dvtfsfkqgt svallqslka dkvdmvicsr igddpdiefi pvieqelvvv takdhplarl
      181 hesdvdlaet ihypyvyfse ssglrpfidd ifhqqtlspd iacyveedla maglvsigyg
      241 iaimpriaal thynlhilti knslppryic latiktkmls paalrlknfi ithsdvarkh
      301 aqsaalgmsa arkaspsspa vv
//
LOCUS       WP_176018721             840 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Pantoea ananatis].
ACCESSION   WP_176018721
VERSION     WP_176018721.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 840)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 840)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 840)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 840)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..840
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..840
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=91438
     Region          26..839
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mnkatlllff assliaaras qaadaqsdyt fdpaliremm pgqvampvds qdawfqpgry
       61 dvdlylngkf qqstalqivr aegplsvclt spfyrafgvk tpylsalkae dcarpeaflp
      121 gatvnvntas lrvdvtipqa mlvqrpvgyi apenltagdt mafvnynlnq fysdyknaqr
      181 festylgins gmnvgmwrfr qqgnfthdef gnrwqsaraw vqralptlrs eagigelfsn
      241 gdlftavsfn gvsldsddrm lpdsvrgyap vvrgvansna rvtiwqgkqr iyqttvppgp
      301 fiindlspvs yggdlsvevq esdgslhrfs vpyavlpqsl rpgrtdynfa agkvrdyskd
      361 nafteltvkh gltnaitlng gvrlgqryha llaggvwasd igavgfnsay seadlngges
      421 tqgwryalsy srtfqptntt ltfagyqyst qgyrdlndvi alnnaetpgr nlinseymqr
      481 nrlqmtlnqt lgqwgnvyls gskqnyydgr srttqfqvgy gtvlpknial nislsrqysr
      541 raystdprma vmaqhaddtf ykdtqlqvsl svplgsdats pylalggtrg sqngsnynas
      601 lsglsgesgt sysvnvnrdq qqrdttlsgs lgkkfseasv tgtastssrf dqmsvnamga
      661 avihsggvtl gnylgdtfal veakgarnah vlnsqgteid rfgyalvpsl npyhyntisl
      721 gaggsdshve iqdsekivap yagamvkvsf rtlrgyplml ktrtnrdntv pmgadlldes
      781 gnrvgtfgqg gnawlrvakt qgqlkavwge gaqssclidy ripkpkpdav ityadavcrf
//
LOCUS       WP_176018735             352 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Pantoea ananatis].
ACCESSION   WP_176018735
VERSION     WP_176018735.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Thorn,A., Egerer-Sieber,C., Jager,C.M., Herl,V., Muller-Uri,F.,
            Kreis,W. and Muller,Y.A.
  TITLE     The crystal structure of progesterone 5beta-reductase from
            Digitalis lanata defines a novel class of short chain
            dehydrogenases/reductases
  JOURNAL   J Biol Chem 283 (25), 17260-17269 (2008)
   PUBMED   18032383
REFERENCE   6  (residues 1 to 352)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..352
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=39465
     Region          9..295
                     /region_name="5beta-POR_like_SDR_a"
                     /note="progesterone 5-beta-reductase-like proteins
                     (5beta-POR), atypical (a) SDRs; cd08948"
                     /db_xref="CDD:187652"
     Site            order(14..19,38..39,53..55,77..79,115..116,145,168..169,
                     171,178..180)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187652"
     Site            order(119,145)
                     /site_type="active"
                     /db_xref="CDD:187652"
ORIGIN      
        1 msqkpqskva lvagasgivg sklvktllqn ewqviglsra ggahrgtvqf vnvdllnekd
       61 taralkplrh vthifysawl naaswremve pnvtmlrnlv tqvenvaple tvslmqgyki
      121 ygahlgpfkt paresdaaip gaefntaqqd wlcrfqhhkt whwhalrpgi vgsaltgntm
      181 nlalsiaiya slckaqnlpl rfpgsqrtwh siidhtddsl lsaatlwast assarnqafn
      241 inngdiwrwc elwpliagwf eletappval sfqqlfgdyr rtwhalaekk qlveadimrl
      301 sdgqfadfvf swdydmfgdg sklrragfte fcatdemfir lftqfrmani ip
//
LOCUS       WP_176018767             308 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pantoea ananatis].
ACCESSION   WP_176018767
VERSION     WP_176018767.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..308
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34247
     Region          5..233
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtyalelsrl tktypgsvqa lkgidlnvea gdfyallgpn gagksttigi isslvnkseg
       61 svrvfgydle kdvvnakrql glvpqefnfn pfetvmqivv nqagyygver realqraekh
      121 lkqldlwekr nerarmlsgg mkrrlmiara lmhapkllil deptagvdie lrrsmwvflk
      181 dlnaqgttii ltthyleeae mlcrnigiiq ngelventsm ksllsklkse tfildlaprs
      241 plpslegfqy rlvdtstlev evlreqglns vfsqlsaqgv qvlsmrnkan rleelfvglt
      301 qgktgaka
//
LOCUS       WP_176018790             226 aa            linear   BCT 11-JAN-2025
DEFINITION  tRNA-uridine aminocarboxypropyltransferase [Pantoea ananatis].
ACCESSION   WP_176018790
VERSION     WP_176018790.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Funk,H.M., Zhao,R., Thomas,M., Spigelmyer,S.M., Sebree,N.J.,
            Bales,R.O., Burchett,J.B., Mamaril,J.B., Limbach,P.A. and Guy,M.P.
  TITLE     Identification of the enzymes responsible for m2,2G and acp3U
            formation on cytosolic tRNA from insects and plants
  JOURNAL   PLoS One 15 (11), e0242737 (2020)
   PUBMED   33253256
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Meyer,B., Immer,C., Kaiser,S., Sharma,S., Yang,J., Watzinger,P.,
            Weiss,L., Kotter,A., Helm,M., Seitz,H.M., Kotter,P., Kellner,S.,
            Entian,K.D. and Wohnert,J.
  TITLE     Identification of the 3-amino-3-carboxypropyl (acp) transferase
            enzyme responsible for acp3U formation at position 47 in
            Escherichia coli tRNAs
  JOURNAL   Nucleic Acids Res 48 (3), 1435-1450 (2020)
   PUBMED   31863583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006970
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..226
                     /product="tRNA-uridine aminocarboxypropyltransferase"
                     /EC_number="2.5.1.25"
                     /GO_function="GO:0016432 - tRNA-uridine
                     aminocarboxypropyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0006400 - tRNA modification [Evidence
                     IEA]"
                     /calculated_mol_wt=25136
     Region          23..225
                     /region_name="TapT"
                     /note="tRNA U47 aminocarboxypropyltransferaseTapT/TuaA/
                     YfiP, DTW domain [Translation, ribosomal structure and
                     biogenesis]; COG3148"
                     /db_xref="CDD:442382"
ORIGIN      
        1 msenavlrlr aqrlaratrp flargnrvlr cqgcllpeqq clcasirvqs arsrfclvmf
       61 dtepmkpsnt grliadvlpd tqafgwsrte pdplllqava seayqplvvf pasyadegrk
      121 ivhspplsgk pplfimldgt wnearkmfrk spwldrfpvi slnvtapsry rlreahgegq
      181 hctaeiaaal lhqagdraag ealtlhfeqf rqaylagkph hpgqek
//
LOCUS       WP_176018808             310 aa            linear   BCT 11-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Pantoea ananatis].
ACCESSION   WP_176018808
VERSION     WP_176018808.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..310
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34106
     Region          44..299
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mmclttpevr qtsvftrlpd rfrapdrhna watanrggql tdsflegpvw hpsgclyltd
       61 ipygrifrvd magnwdivvq ydgepngmkl vgsetllitd yrhglmklcl ktqkitpwls
      121 rrnsesfrgv ndltpdsrgn lyftdqgqtg lhdptgrvyr lsqegrldil ldncpspngl
      181 vlspdekvly vamtrgnaiw rvplqrdgsv skvgqyftsh gpsgpdglam nahgellian
      241 pglgrvwlln dlaepaeilt spagrsttnl cfggenlqql fitesvsgsi ltcsmktpgh
      301 plpflstdfl
//
LOCUS       WP_176018887             369 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Pantoea ananatis].
ACCESSION   WP_176018887
VERSION     WP_176018887.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..369
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40300
     Region          1..348
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masitlnnvt knwgetqvlk pinltienge fvailgpsgc gksttlflla glyapssgei
       61 afdghnvnri dardrnvgiv fqsyalypnl tvreniafpl rfkkldrdqi arrveeaasl
      121 vqisalldrr psqlsggqqq rvalaralvk epnillldep lsnldatlri tmrtelknlq
      181 krlgfttliv thdqmeaitm adriicmnqg eivqigtped lyrrpddlfv agfigsppmn
      241 lvkgqalgrf lqlgqmslel nhgydgpvcf glrpedislv apddaplcge vmtvepigre
      301 vfytidtpag rlhaleygea vrhapgsrig iacqsaltli fnssgkrivd lhanlsvfch
      361 pgkhvhaas
//
LOCUS       WP_176018844             339 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Pantoea ananatis].
ACCESSION   WP_176018844
VERSION     WP_176018844.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..339
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36337
     Region          104..311
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mnvkltagal llasqitsaw aspvenapep tvgvaaflka lnsgggkpie tltpkearav
       61 ltgaqqgatl ppaqvsekti talgkplklt ivkpehatgv lpvfmffhgg gwvlgdfpth
      121 erlvrdlvne sgaaavfvny epspeahypv aitqayeatk wvaehgaeig vdgkrlalvg
      181 nsvggnmvaa valqakqhkt pairydvmlw pvtdarfdda syqqfangyf ltrnmmkwfw
      241 dnyttsdkdr nnilasplra teaqlaglpp tliqtaeldv lrdegeafgr kldaagvpvt
      301 vtryngmihd fgllnalske ptvrtaitqa saelkehlk
//
LOCUS       WP_176018810             238 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Pantoea ananatis].
ACCESSION   WP_176018810
VERSION     WP_176018810.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..238
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25783
     Region          5..226
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mgnegvnave kalalldcfk pgeeslsltt lsqlsgyhkt tvyrlmnsle rmsyvvrrdn
       61 giytlgprll ylgklyeqsf hlasvvqpel qtlasatkes aswyvidsgq rlcvfraess
      121 dglrhtrlpg slypldnsai gqvlrhwgmg etlfddaadl plytsgardp htaafaipvf
      181 gegdqlaaal altgpssrlt ldrkeaglge lmresaarls aqlgarkafc dvvyahna
//
LOCUS       WP_176018937             384 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Pantoea ananatis].
ACCESSION   WP_176018937
VERSION     WP_176018937.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..384
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40332
     Region          19..363
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(27..28,31..32,35,67,117..118,120..122,125,144,
                     147..148,151,217,220..221,224..226,229,257,261,310..311,
                     315,319,335,338..339,342..343,346)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 mtaldaakst psdrrlsggt riiflinglg msawaplvpy ardrlhldga slgalllclg
       61 igsllampvt gtlvarfgcr tvmifstllv lcmmpllatv qthlfmaaal mlfgaglgml
      121 dvamnyqave vekaagkpmm sgfhaffslg gilgagavsl llslgltpll svlivmavmm
      181 vlllwqmptf mnqrlhqpdq pwlviprgrv aflgmlcfil flaegavldw gallllqnpv
      241 mttahaglgy alfsvamtvg rfsgdkiihr fgrypvmlvg alaaasgmal avllpwpeas
      301 llafllvgfg lsntvpmlfn aagnqndmpa nlaisamttl gyagilsgpa ligfisqwis
      361 lsgafllial lllavavsar nvar
//
LOCUS       WP_176018946             250 aa            linear   BCT 11-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Pantoea ananatis].
ACCESSION   WP_176018946
VERSION     WP_176018946.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..250
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=26761
     Region          5..216
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mnefgiehvw eqgdiitrsv aiillimsvm swsvivikci qgagmkkiah rtkhlfwsqk
       61 tlpaaidtlg angnnpfrdl aiaghaamsh qytieagisn nldisdwlar alknsiddst
      121 anlqsglgil asigstapfv gllgtvwgiy halqsismad qpdlahvagp vgealimtaf
      181 glfvaipavl gfntisrrnr alqhaiarfa ndlhayyltg sritsnveel haadkaqssp
      241 vqpfrasqpv
//
LOCUS       WP_176018977             460 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Pantoea ananatis].
ACCESSION   WP_176018977
VERSION     WP_176018977.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..460
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50574
     Region          36..445
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(45..46,49..50,53,85,135..136,138..140,143,163,
                     166..167,170,278,281..282,285..287,290,318,322,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mstqviasha hpadasvlla rlerlpitrr lmairvvvgl stffdaytii aiafalpqlt
       61 qewgltptfv gliiaasyig qlvgalffgt laekigrigv lritivmfvi mdaaclfawn
      121 gwsiliirfl qglgigaevp vasayinefv gakkrgrffl lyevifpvgm mcagligffl
      181 vpiygwkimf liglipsala aplrwfmpes prwlvskgrh qqaekvvqsf eaealrrgms
      241 lpepvikpvp vmpasssgvk alfsgiyksr tfmlwglwlt vytvnngmit wfptmyrtlf
      301 hlpletslay gwitstcgvi asvicafeid qvgrkrwytw afmlaiipli vlcvlgantp
      361 wqililgsma yailqtiafs lylysaelyp trlratgtaf ssawlragss vgpqmvgfiv
      421 sgfgirfvfi afavialigg mitllfaiet kgksleelsp
//
LOCUS       WP_176018995             305 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Pantoea ananatis].
ACCESSION   WP_176018995
VERSION     WP_176018995.1
KEYWORDS    RefSeq.
SOURCE      Pantoea ananatis
  ORGANISM  Pantoea ananatis
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Pantoea ananatis"
                     /db_xref="taxon:553"
     Protein         1..305
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34687
     Region          5..202
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 mkdirfsivi paynasesiv ttldcvkaqt yrhfeviivd dksadaaala evvrseryqd
       61 ldinlvlsev klngagarnk gielatgdyv sfldaddewr adkllqvsek iaeleaqgqh
      121 ntiifsqvni yqdgaflkvm pmqppaknet vaeylfgcyg fiqtstivlk redaakiqfd
      181 arfirhqdyd fciradrmgy rfemiaapla nyhlvtkfgs khkgesvkys lfwldtmkph
      241 ltardihtyk afklplrykm dgnslmasvs faryflltnk dnrtyflnrv kdklkarlgg
      301 ekals
//
LOCUS       WP_176019171             268 aa            linear   BCT 11-JAN-2025
DEFINITION  M48 family metallopeptidase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019171
VERSION     WP_176019171.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Lew,R.A.
  TITLE     The zinc metallopeptidase family: new faces, new functions
  JOURNAL   Protein Pept Lett 11 (5), 407-414 (2004)
   PUBMED   15544561
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..268
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=28159
     Region          65..249
                     /region_name="M48C_Oma1_like"
                     /note="Peptidase M48C, integral membrane endopeptidase;
                     cd07331"
                     /db_xref="CDD:320690"
     Site            order(127..128,131,191,195,234)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320690"
     Site            order(127,131,191,234)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320690"
ORIGIN      
        1 mkqlllaivi ttlvsacatt tsptgrrqmv ggvsqaqldq lgaqafaetk qkekissdgr
       61 qngyvqcvvn alvaqlppqy rgvrwetavf vdkepnafal pggkvgvntg ifsvarnqdq
      121 laavigheig hviarhheer itrqmgaqtg lavlgalaga yggegaastv nqlggmgaqt
      181 afllpgsrtq eseadvigqr lmaeagfnpa qavdlwqnmm aasggrspqw lsthpdpanr
      241 irelqrdapa lgpvyqqaqa agrrpkcg
//
LOCUS       WP_176019179             236 aa            linear   BCT 11-JAN-2025
DEFINITION  2OG-Fe(II) oxygenase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019179
VERSION     WP_176019179.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..236
                     /product="2OG-Fe(II) oxygenase"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /calculated_mol_wt=26189
     Region          134..224
                     /region_name="2OG-FeII_Oxy_3"
                     /note="2OG-Fe(II) oxygenase superfamily; pfam13640"
                     /db_xref="CDD:463943"
ORIGIN      
        1 mqqsgpvdfi evihnavpsd vcaaivarmr asqglkpgav gsgvfpelkh skdlrisgle
       61 gwqdvdqqlq qavfaglqty lrrypqalia plmlqiqdsn gqprrlsaed fpdmapeqla
      121 dlartclrpg ainlqwyaag eggypywhce lypkdaqadt lhrhvlwtly lnddfdeget
      181 eflfqgrkia prtgslliap tafththrgn rpqggdkfia tswilfqsaq qlfrgs
//
LOCUS       WP_176019210             756 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019210
VERSION     WP_176019210.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 756)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..756
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=82356
     Region          43..737
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msptrtsrgr spvarplvva lsallplvaa aqetpaakdp valdalqvta qrrvenakdv
       61 pvaisaiqge kldvlgsagd dirflaarvp slniessygr afprfyirgl gntdfdlnas
      121 qpvslvyddv vqespllkgf plfdlagvev lrgpqgtlfg rntpagvvkf dsarpsqdad
      181 gyvrvgygsy nswnvqgayg gpltdrwsar vsaiyqrrdd wvdnthagap nsgfegydea
      241 agrvqflyeg ddfealfnlh krklngtarl franiiekgg nslvenfdrd kvandgvnfs
      301 dletwggsar lqwnlgsvtl hsitgyetae slnrgdidgg ygaaflgagn sgpglipfss
      361 esadglphhr qwtqefrves newgrfdwqa gvfyfdedvt innfnydslt pgnpqtghvv
      421 qqqrnkawav fasgdfdvtd rfklragvry tqdkkdfsas vlqavpfgtp vsgpylantd
      481 vndvswdvsg vykltdnvna yarvakgfra psiqgrlafa pglsqadsek visyeagika
      541 dlferrarlg fsvfrydvdg qqliavggtn ntatllnadk tigqgveldl eayladnvll
      601 tfgssyndte ikdknlavai cgggctitdp ttiinggtya lvngnplpqa pkwihnatlr
      661 vgfplsdgse lyaytdwayr savnffiyes pefrgrssle gglrlgynwd ygqydvavfg
      721 rnltnqtrvv gaidfnnltg flneprtwgv eftakf
//
LOCUS       WP_176019256             544 aa            linear   BCT 11-JAN-2025
DEFINITION  TldD/PmbA family protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019256
VERSION     WP_176019256.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..544
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=58617
     Region          42..538
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 mhrrdflalt gltagglivp sffgkaiaae qlqssldpal kkrladaalq aarsagatyc
       61 dvrigrylrq fvitredkvq nvvntestgv girvivngaw gfaatnalst advaraaqqa
      121 aaiakanagv qtapvqlaka pgvgevswkt pirknamevp ikekvdllld vnaaamgaga
      181 sfvnsmlflv neqkyfastd gsyidqdvhr iwapmtitai dkasgkfrtr eglsapmglg
      241 yeyldgaaag kvltpngvvn ygssydmked aiaaakqaqe klkapsvkpg kydlildpsh
      301 twltihesig hpleldrvlg yeanyagtsf atldkreqhf qygsdkvnif adktqpgslg
      361 avayddegvk ckrwdlisng klvdyqtird qahilgktes dgccyadsws svqfqrmanv
      421 smapgktpls vsdmikdven giyiigdgsf sidqqrynaq fggqlfyeik ngkitrmled
      481 vayqirtpef wnacsavade rdyrlggsff dgkgqpgqvs avshgsstar fnginvinta
      541 rslg
//
LOCUS       WP_176019257             543 aa            linear   BCT 11-JAN-2025
DEFINITION  TldD/PmbA family protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019257
VERSION     WP_176019257.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..543
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=58939
     Region          56..536
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 mqrreflafs glglaglvlp hsrliaaeql lapvdptqrr rlaevalaaa raakasycdv
       61 rigrylnqsv itrehqvgnv tnressgvgv rvivngawgf aathqqteaa vrtaveqata
      121 iaranasiqt rpvqlaptps vgevrwqtpi rrnamevpiq dkvelllsln aaalnagady
      181 instlflvne qkyfassdgs fidqdihriw lpftataidk asgkfrtrag lsspmgmgye
      241 fldgdasgkv qlpggitayr dsydpvedai aaarharekl kapsvkpgky dlvldpsnlf
      301 ltihenvghp leldrvlgye anyagtsfat ldkrdagfrw gsdivtvfad ktqpgslgav
      361 gyddegvktq rwdlvrdgvl vdyqatrdea hilgrdashg csyadswssv qfqrmanvsl
      421 apgkaalsve emvkdvengi yihgrgsysi dqqrynaqfg gqlyyqikng kitgmvedaa
      481 yqirtpefwn actaicderd frlggsffdg kgqpgqvsav shgssttrfn giniintars
      541 lga
//
LOCUS       WP_176019275             476 aa            linear   BCT 11-JAN-2025
DEFINITION  ammonium transporter [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019275
VERSION     WP_176019275.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..476
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49047
     Region          73..475
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mkmrlltgwq arfhlvcllm lfsalaagvw pgnahaqaqv tplqseavav eplqdptaaa
       61 paaaeavaap aydhgdvawm ltstllvllm vvpglalfyg glvrsknvls vlsqilvvfs
      121 lvlllwvayg ysavfsagnp ffgsftefaf lkgftpesvg ntpikglpdy lfvafqstfa
      181 gittalivga faerikfrav llfsalwftl syipmahivw gggylgelga idfaggtvvh
      241 inagvaglva awfvgkrlgy gqtalkphnv pftyigamll wvgwfgfnag saaaadtvas
      301 laflntvlat aaavlgwtlv eaiskgkpsa lgaasgavag lvgitpacgt vgplgaivig
      361 fvagvvcvwg vtglkrllkv ddtadvfgvh gvggivgail tgvfsaqslg gtkadldigh
      421 qvwvqvvsvg ltvvwsavvt aailllvkvv vglrvteeae rtgldvtshg esayea
//
LOCUS       WP_176019279             502 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019279
VERSION     WP_176019279.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..502
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53304
     Region          84..>274
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
     Region          <408..474
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mtrsactsss rfqvrrpvva atlaalslal aaalpaqasp aalafepytl qtkghgdipa
       61 eiatlevprr hsepdgprlh lkvvrlrata gngraapvvy laggpggsgi dtargprwpv
      121 fdqvrresdv llldqrgagq sepppecphe srfddaqplq rdaalavlqa ttakcvafwr
      181 qagvdlgayt taesagdldd lrraldvpki slwgmsygth lalatvrlhg gglervvlmg
      241 segpddtlkl plssdallqe lavlarkdgf ddlagsvtrv lqalreqprq grshmhegkq
      301 vtiglydaqi vianmlgqrv pqqwlplvlr eaergnydpl admvligraq fakfpamgla
      361 mdvasgqspq rralaeaqar qslfgdglnf pfpaigeglg ladlgegfrs plhsevpvlf
      421 isgtldgrtp panaaallpg fsnghallvr nashhnelwt gnpaiarsiv dflagrvvnd
      481 tvldvpppvf athssellgg kr
//
LOCUS       WP_176019308             725 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019308
VERSION     WP_176019308.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 725)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..725
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79403
     Region          29..723
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mnrclrptll alalcaalpl yaseagtdtv dapssptela avrvqagkpa tdtsrlsafg
       61 ggswkdtpas vnvlgrdyld rrqvrslsel asndaslgda yapvgyyqni airgfaldaa
      121 tgyrfngmsi ageqrlalen iqdvqilkge aglaagvmap ggiinyvgkr paevrtvtlg
      181 tdsegsryaa vdvghwltpr fgvrfnaawd asdsyvehad grrnfyslat dwligehgkl
      241 evdanyqtss qrsvsgfqll gardlprgvd rerllgyqpw qrpvdiastn italhtydfn
      301 dawqsrlsig hsrsviddnv afaygcyyta gcadgsvpgn yfapngdydi ydyrspddtr
      361 rnqqaraelr gsfdtgsish qlsigadyfr rtvdkrpsvn eyvgsanihd aqvpvfepsp
      421 kmpgasarrl dsrqtaffal drmsfgddwq wlaggrfvrl deraydkrgt pqrhsrlsrf
      481 lpqtalvwka tdqlnayasy vrgislgqea pfwtsnadtf lpsmqsrqle vgvkympvda
      541 ltlgaavfrt tqpyqyakpd gsdagytfve egqqthtgle ltangqltda lqivasasvl
      601 qarardtgtp ayeghqlvnv pkvrasvhla yalpfvegld vtggwryaaa nvaradgavr
      661 apdysvfdag lrfqhrlher avtwnlsvdn lfnrfywrdt gssggdyylf pgaprqarls
      721 vtfal
//
LOCUS       WP_176019282             681 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019282
VERSION     WP_176019282.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 681)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..681
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75294
     Region          42..656
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mktstlvaal aaapfapeaf aqsadaaltl gkvdvhqhse gqlsahqvlt svdvlgadqi
       61 esrnvshswe llgqmpgiql tetrqgaesg kvsfrafnge gylnaiktli dgipsnvnsg
      121 nqrfidmlfp leisyievvr gtndpryglh niggnvnfgt rqggtytdar laygsyntrd
      181 aqlavgread gfaqnyfvgt qasdgyrdhd sskkyslggk wffgsledgl rigltarayh
      241 headepgfmt aeelhagrrr sdlrnandgd drdmrqfaah ldmklsdalt fgtrlyynry
      301 eddrrvtfsd lptgslprqr rlwderqtgl lgtltwkasa tltveggvny eqqdngyire
      361 ryayaeptdf srpparvqnn drhsfdnwgt yvqaiyqpad awkivpayrv drfsghtrlm
      421 ngitgrlqdy gsigqpklsv ihslgehthv yanwgrtfqv ltgstapayl tagqapmqps
      481 tntgmelglk fqpfagsqar lavwqqdaen evsnmpatgt tvtlgktrrr gvdmqisaql
      541 gdawtlwash ayqeakitrd drapgvslqg revaatprhi snlgldyqas dalqlglqar
      601 aqgdyyleer nvagkfggfa vldlsakyqi tpawsvdlql knvtgreyay awydsffwds
      661 arpmfspapg rsvfvglnmk l
//
LOCUS       WP_176019318             159 aa            linear   BCT 11-JAN-2025
DEFINITION  tRNA (cytidine(34)-2'-O)-methyltransferase [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176019318
VERSION     WP_176019318.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..159
                     /product="tRNA (cytidine(34)-2'-O)-methyltransferase"
                     /EC_number="2.1.1.207"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0141098 - tRNA
                     (cytidine(34)-2'-O)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=17546
     Region          7..159
                     /region_name="TrmL"
                     /note="tRNA(Leu) C34 or U34 (ribose-2'-O)-methylase TrmL,
                     contains SPOUT domain [Translation, ribosomal structure
                     and biogenesis]; COG0219"
                     /db_xref="CDD:439989"
ORIGIN      
        1 mnaapqfhvi lfqpeippnt gnvirlcant gaqlhlvepl gfaledkqlk ragldyheys
       61 rlqvhpdldt alariapkrl falstrasvr ydsvsfedgd aflfgpesrg lpqdvldalp
      121 dgrrlrlpmr pdnrslnlsn tvavvmyeaw rqhgfagga
//
LOCUS       WP_176019331             203 aa            linear   BCT 11-JAN-2025
DEFINITION  PIG-L deacetylase family protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019331
VERSION     WP_176019331.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..203
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=22291
     Region          4..196
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mahdilaiga hpddielgcg gslaklafag arihalvlsr ggrgchdgad rsdeshralr
       61 qlgarqvlqh dfpdtcfpsc rnaiisaleq aceaiqprrv ymmcgedhhq dhrtvheasi
      121 vacrsvpqil cyespstlpq fapqvfedis vqlelkiral rehasqggrh ymqeshlrch
      181 aqfrgqqvgi gpsegflphr lvl
//
LOCUS       WP_176019353             223 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019353
VERSION     WP_176019353.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789896
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..223
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23968
     Region          16..217
                     /region_name="COG2945"
                     /note="Alpha/beta superfamily hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:442188"
ORIGIN      
        1 mhkpsfpvap getaclvldg pagplevvvd lpkadasvqp ivaiichpls teggtlhnkv
       61 vtmtattlre lgiatvrfnf rsvggsagef dhgvgeqedl kavtawvrqq rpddrlwlag
      121 fsfgalvslk aaaelqpeal isiappagrw dfggitppar wlviqgeqde ivdpqavyqw
      181 ldtldaphel vrmpdtshff hrklidlrga lthgvkhwlg taa
//
LOCUS       WP_176019356             211 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019356
VERSION     WP_176019356.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..211
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22313
     Region          4..210
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mpatsdllaf alvslamvlt pgpnmiyvis rsicqgrvag lislggvalg fvfymlcaal
       61 gitallmtvp faydalrigg alyllylawq avkpggrspf avrdlpvdgp rklfamgflt
      121 nvlnpkvavm ylsllpqflh pdsegsvlmq slvlgftqia vsvsvngmia lmagsiagfl
      181 aarptwqavq rwfmgtvlag lavrmamdgr r
//
LOCUS       WP_176019365             501 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019365
VERSION     WP_176019365.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..501
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53225
     Region          8..484
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(65,67,71,74,78,111,114..115,124..131,136,139,142,
                     235,239,242,245,247,420,422..423,425..426,429,432..433,
                     435,437..440,449,453,455,469,476..481,483..484)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(151..154,162,177,180,210,227..230,233,251..253,285,
                     385,387,413)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(154,251,282,285)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mtvaaprirm lidgqfvesa tshwqdvinp atqdvlaqvp fattaevdaa vaaakeafkt
       61 wrktpigtra riflkyqqli renmselahi ltaeqgktlp daegdvfrgl evvehaaaig
      121 nlqlgelann vangvdtysi mqplgvcagi tpfnfpamip lwmfpmaiat gntfilkpse
      181 qdpmvtmrlv elaleagipk gvlnvvhgge evvnaicdhp dikavsfvgs trvgthvynr
      241 aslagkrvqc mmgaknhavv lpdankeqtl namvgaafga agqrcmaast lvlvgeargw
      301 vqdlvdkakt lkvsggtvag tdvgpviscs ardrveglia sgveqgaklv ldgrkpqvdg
      361 fekgnfvgpt ifagvttdmr iyqeeifgpv lvileaetld eaiamvnsnp ngngtalftq
      421 sgaaarrfqe didvgqvgin vpipvpvplf sftgsraskl gdlgpygkqv vlfytqtktv
      481 tarwfddetl shgvnttisl k
//
LOCUS       WP_176019368             389 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176019368
VERSION     WP_176019368.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..389
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41210
     Region          23..365
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 mttvadeapv lfeeraagng vrigiatlna prtlngfslp mahlllkqln awadddgial
       61 vvlegageka fcaggdlhsl yqsmiafrea ghgdirenay aaeffdveyr vdylihtyak
      121 pilcwghgiv mgggiglmsg ashrvvsers klafpeitvg lfpdvggswl lprvpgkagl
      181 flaltgalln pgdaiyagla dvhvaeerrs avfdallqva wsadaarnhe rlsqlllsfa
      241 sdaatgplla haaqvdalce gddlvaiver istlqtddaw lqaaqktlaa gapgsarlaf
      301 elqrrsagqd lasvyrleyi talhcaahgd faegiralli dkdrnpswnp atlaeashaw
      361 adtffaspwa daahpladlg tpvaersla
//
LOCUS       WP_176019389             444 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019389
VERSION     WP_176019389.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024287
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..444
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48297
     Region          24..434
                     /region_name="MFS_KgtP"
                     /note="Alpha-ketoglutarate permease of the Major
                     Facilitator Superfamily of transporters; cd17367"
                     /db_xref="CDD:340925"
     Site            order(34..35,38..39,42,79,137..138,140..142,145,165,
                     168..169,172,258,261..262,265..267,270,299,303,356..357,
                     361,365,381,384..385,388..389,392)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340925"
ORIGIN      
        1 msttsqpavp asdgaalrrs isntlkgsag nlvewydvyv ysvfavyfes qffspedkns
       61 tmyvwaifaa tflmrpigaw ffgrfadrhg rrlaltvsvt lmafcsfiia itptaasigi
      121 waaiillfar llqgfatgge ygasatymse aaipgrrgfl ssfhyvtlvg ghvlaqltlf
      181 vmltfwakpe isefgwriaf giggiaavvv fwlrrgmdes lsessieaar egkdkksgsm
      241 yelfvhqwrp lllcflitag gtiafytysv ngpkmiqsaf agndpmtgtl inlgvlaflm
      301 vlqpvggwls diigrksllv ffgvggvlys wylitqlphq hdatlafltl algfviltgy
      361 tsinavvkae lfpthiralg vgfgyalans lfggtaplly qgalktghvd wfaiyvtati
      421 avslvvyvff ltnkgpnwld gtrk
//
LOCUS       WP_176019393             438 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019393
VERSION     WP_176019393.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 438)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12118482
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..438
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46073
     Region          86..278
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          191..437
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mnklkkwlgn avtvlllgvg lavwialpwi gvlaiavlvg lwlaltrsgr lalaatrigi
       61 aslpqrwgas svivvgiagv vgvlvamlam gegfqatlnn tgddttaivl rggsqaetns
      121 vitreqvptl stlpgitrda qgrpllspel sqvvnlvska dgtdvnaqfr gvgpqawavh
      181 dkvkivegrr faaglreivv gqgaksqfrd mdvgktltlg nqtwtvvgvf atgdahdsel
      241 wtdadtlatt yqrsawqsis vrtdgkagfe qfkaavaadp rlkldvettr vyyskqgggl
      301 tklidilgkv igtimavgav fgalntmyaa vatrareiat mraigfrglp vvtavmletm
      361 llallggllg cavawllfng ysvstigsnf savvfkfhvs pellwsglkw algiglvggl
      421 fpalraarlp ittalret
//
LOCUS       WP_176019394             385 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019394
VERSION     WP_176019394.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 385)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..385
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42337
     Region          132..>313
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mkyfslvwaq lfrsrtrtll tllsvvaafl lfgmldsvrv afssggsveg anrlvvasrl
       61 sitqslpirl eaqvrqvsgv rdvaygmwfg giyqdpknff pnfsvspnyf dvyrelqidp
      121 aqledwkqtr tgaivgetla kqfgwkigdt iplqatifpr ggsndwplel kgiyrskdra
      181 laaneerqlm mnwkyfdesn dyiknqvswy tvtldnpdqs srvaqaidai sansdhetkt
      241 qtesafqqaf vkqfadigmi vtsimgavff tlllltgntm aqavreripe latlktlgfk
      301 dstvltlvmv esvlliglgg ligmglaali lpaispksmg mlpphvptpt wlvgivlivv
      361 igivvgllpa lrakrlkivd alagr
//
LOCUS       WP_176019396             298 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019396
VERSION     WP_176019396.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..298
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32350
     Region          10..220
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mdpiapslar lqqvqvryrd htalhgidlq vragqvlall grngagksta isvllglrra
       61 dagqvellgg dpkqrdhrlg lgvmlqstsl ppmlqvdelv aqasacypdp lplgevlqrv
      121 glqdlarrry gqlsggqqrc vqfaiaicgr prvlfldept tgldiqarqa mwqaiqqlva
      181 egcgvlltth yleeaealaq rvvvleqgrv vadaplselr ladrprrirc rstlaadevq
      241 hwpgvqqvqr egehlqllas paepvvarll atdvqlrele vqgaaladaf ldltreaa
//
LOCUS       WP_176019530             434 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019530
VERSION     WP_176019530.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..434
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47960
     Region          4..>359
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mfayyarlav rsfrrnkvlt almvvaialg igasmttltv fhvlsgdpip dksdrlfyvq
       61 vdprprsgyl tgeepetqmt rfdaetllre krgerqamms agdvtvepeg stlkpfnidt
      121 rwtsadffpm fnvpmlygra wtasdddgra rvvvlskvin dklfqgadsv grqvrvdghs
      181 lrvigvmdtw npephffdlt vgnygreedl mmplstamdl kfgsngnmnc frdgapddds
      241 nsinapctwv qywveldpsk aedyrrylvn ysdqqraagr ferpanvrlr tvmewltfnn
      301 avpsdvrlqm wlalgflgvc lvntvgllla kflrrsgeig vrralgasrg qiflqclvea
      361 gavgvvggvl giglallgly avrqqpvdya klahldgsml llslgltlla siaagflpaw
      421 ramqvtpaiq lksq
//
LOCUS       WP_176019398             405 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019398
VERSION     WP_176019398.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..405
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=44341
     Region          161..389
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 migsdrprle ssvppswlas llrpapdsav adnlrrgkpv wadaihllwt vwvfmtpvfs
       61 ggytlrwall tlgsyplfll lyvrlllspr hhapryalam valatllvpw ypsgisyfif
      121 gcvmlrvcgr gswwvyllql aalnavfctv allshypwqs lvwipavsfi igmvvnveav
      181 nkdkdaalql sqeevrrlat taererisrd lhdllghtls litlklelar klydrndara
      241 rqeigeaedi arealsqvrs avtgirasdl agelasarll lecqqvhlqy avpppmpvdv
      301 erglalvlre aatniarhaq atqarvdfmm egrqlamqir ddgrggvqae gnglcgmrer
      361 vvalggqlav qsargegtvl tvrvplaaat splpptapqv qdgva
//
LOCUS       WP_176019627             146 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019627
VERSION     WP_176019627.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..146
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15738
     Region          1..141
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mfntllvald ggpqhdrvld laaamagprs rlhllcvldp efalaanttd adrreypaaa
       61 kqqahaeavl adalaelrer gvdaiaqlpc gdpgevisaq arrlqcdliv ighrhlsrlq
      121 rlfepsvgqw tidhapcpvl vetrdp
//
LOCUS       WP_176019564             642 aa            linear   BCT 11-JAN-2025
DEFINITION  M1 family metallopeptidase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019564
VERSION     WP_176019564.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Evnouchidou,I., Koumantou,D., Nugue,M. and Saveanu,L.
  TITLE     M1-aminopeptidase family - beyond antigen-trimming activities
  JOURNAL   Curr Opin Immunol 83, 102337 (2023)
   PUBMED   37216842
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Peer,W.A.
  TITLE     The role of multifunctional M1 metallopeptidases in cell cycle
            progression
  JOURNAL   Ann Bot 107 (7), 1171-1181 (2011)
   PUBMED   21258033
REFERENCE   4  (residues 1 to 642)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   5  (residues 1 to 642)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..642
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=70463
     Region          47..483
                     /region_name="M1_LTA4H"
                     /note="Peptidase M1 family including Leukotriene A4
                     hydrolase catalytic domain; cd09599"
                     /db_xref="CDD:341062"
     Site            order(175,177..178,303..307,328,331..332,335,350,354,361,
                     413,418)
                     /site_type="active"
                     /db_xref="CDD:341062"
     Region          525..636
                     /region_name="Leuk-A4-hydro_C"
                     /note="Leukotriene A4 hydrolase, C-terminal; pfam09127"
                     /db_xref="CDD:462686"
ORIGIN      
        1 mrnplmllpl avalaagcsq eaaapaaapt aqkapaapvn aenrshdess yaepdkvvvk
       61 dialdlkldf dqkqiggtat ytlewkqkda kqlvldtrel siakveaiaa dgarsplqfv
      121 lapadkvfgs kltietpeqp akvevtyhta ptasglqwla psmtegkklp fmfsqsqaih
      181 arswvplqdt psvrftysah vvsrpdvmvl msadndpkaa rdgdytfkmp qpipsyllai
      241 aagdlvfepi sgrsgvwaep tmvnkaakef edtekmigaa eklygeyrwg rydmlvlpps
      301 fpfggmenpr ltfatptviv gdkslvslva helahswsgn lvtnaswkdi wlnegfttyv
      361 qgritealyg kemaemekqi dqtdllaevk dmspadqala lpplnerdpd ealsqvayvk
      421 gswflefleq rfgretfdpf lrgwfddhaf qsantdqfve ylkknllpkn psavteaelk
      481 awldepgipa faakaqsrnf ssvdtariaf asagtvpssq viadwstqew vrfidglgat
      541 qpldklatld kafhftgtpn geiamrwypl tirsgyeqan egaaafierv grrklilpiy
      601 aelvktpkgl elakqafeka kpgyhpitta svqdmlakae ak
//
LOCUS       WP_176019628             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176019628
VERSION     WP_176019628.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444099
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33447
     Region          17..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..297
                     /region_name="PBP2_DntR_like_1"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     similar to DntR, which is involved in the catabolism of
                     dinitrotoluene; contains the type 2 periplasmic binding
                     fold; cd08460"
                     /db_xref="CDD:176149"
     Site            order(102,104..105,109,166,203,272)
                     /site_type="other"
                     /note="putative substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:176149"
     Site            order(103,106..107,110..111,114..115,117..118,121..122,
                     124..128,130,192,220..224,227..228,231..232,235,249)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176149"
ORIGIN      
        1 mplpdlnlll aldvlidecs vaaaarrmnl sapamsrtlg rvrvalgdpv lvragrglap
       61 tpralelreq vrdvieqahr vfnagrevdm atlertfsvr andvfigsyg grlrevfrqq
      121 aprcmlrfvp egdtdddamv qgridlyist agkhsaetkv qhlfttsllg aaredhplfd
      181 gdisaerfaa cdhiavsrrg lahgpideel aalglqrrva vviptfhgai faaadsdlvl
      241 pqmpsvmldr ithmglplrm fplpvpvrtv alvqawhprm dsdpahqwlr raikgmcdsv
      301 eaarh
//
LOCUS       WP_176019736             299 aa            linear   BCT 11-JAN-2025
DEFINITION  PilN domain-containing protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019736
VERSION     WP_176019736.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..299
                     /product="PilN domain-containing protein"
                     /GO_process="GO:0043107 - type IV pilus-dependent motility
                     [Evidence IEA]"
                     /GO_process="GO:0043683 - type IV pilus assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=31836
     Region          1..198
                     /region_name="PilN"
                     /note="Type IV pilus assembly protein PilN [Cell motility,
                     Extracellular structures]; COG3166"
                     /db_xref="CDD:442399"
ORIGIN      
        1 marinllpwr aerrkqrqre fgimlgmaal ggvllslmiw fyydlqvsgq gdrnaylqte
       61 idkvkeqnke idrldaqrdr llarkevieq lqakrsqmvh lfdalvrtip dgvvltalqq
      121 egdvltlegr tqsnarvsay mrnlevsgwm tnpelaiiea repdkdkdgr atgpvvdika
      181 lpyvfkvkvk lpaqseeatt tsglnpdgsv astapvaptv aplsagpdaa apaaaasqpg
      241 tspapaappa tapsqvpppp paatpapaap atkpatkteg srlaqppqaf hapllgdra
//
LOCUS       WP_176019716             124 aa            linear   BCT 11-JAN-2025
DEFINITION  PilZ domain-containing protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019716
VERSION     WP_176019716.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..124
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13703
     Region          8..112
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mstqppvdtr raprrqvsdl vpvtdqmrds vvgrlgnvse tgmlmlasat lrddalyqlr
       61 fplpladgrs elidvgvhll wsepahapgq swagfrfltl srehrqllrr wigedsdeap
      121 vstg
//
LOCUS       WP_176019803             593 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 15 protein [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176019803
VERSION     WP_176019803.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Sakaguchi,M.
  TITLE     Diverse and common features of trehalases and their contributions
            to microbial trehalose metabolism
  JOURNAL   Appl Microbiol Biotechnol 104 (5), 1837-1847 (2020)
   PUBMED   31925485
REFERENCE   2  (residues 1 to 593)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465339
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..593
                     /product="glycoside hydrolase family 15 protein"
                     /calculated_mol_wt=67192
     Region          1..589
                     /region_name="SGA1"
                     /note="Glucoamylase (glucan-1,4-alpha-glucosidase), GH15
                     family [Carbohydrate transport and metabolism]; COG3387"
                     /db_xref="CDD:442614"
ORIGIN      
        1 mtqpdldlgv vgngsfgalv dkharvvwsc lptfdgdptf callspnqqt ggdfaieled
       61 fadseqeylt ntailrtvlr dahggaleil dfaprwrqnd rfyrpvslir qvrplsgspr
      121 ivirarplad wgarvpestw gsnhvrwilp ehvlrlttdv pvrfvrdglp fvlnhpihli
      181 lgvdeslnrs isgyvqeafq rtrdywrewv rylsiplewq davirsaitl klcqyedsga
      241 iiaamttsip eapgsvrnwd yrycwlrdaa fvvralnrlg atrtmeqflg yifnlattdg
      301 tlqplygigf eakldedevp slsgyrgmgp vrrgnlawvq rqhdvygsvv lastqlffdr
      361 rlqdpgdsht farleplgeq afalhdvpda glwefrgrte vhtytsamcw aacdrlckia
      421 vrlkrddrar ywreradtih arimekawse elghftdtfd ghrldaslll ladigfidan
      481 darfvatvea igrdlkhgna lyryiapddf gepetsftic tfwyidalaa igrmdearem
      541 feallrqrnh lgllsedlaf dggeawgnfp qtyshvglit aamrlsrswq eas
//
LOCUS       WP_176019800             141 aa            linear   BCT 11-JAN-2025
DEFINITION  thiol-disulfide oxidoreductase DCC family protein [Stenotrophomonas
            sp. NA06056].
ACCESSION   WP_176019800
VERSION     WP_176019800.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Ginalski,K., Kinch,L., Rychlewski,L. and Grishin,N.V.
  TITLE     DCC proteins: a novel family of thiol-disulfide oxidoreductases
  JOURNAL   Trends Biochem Sci 29 (7), 339-342 (2004)
   PUBMED   15236740
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006848
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..141
                     /product="thiol-disulfide oxidoreductase DCC family
                     protein"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15722
     Region          14..135
                     /region_name="YuxK"
                     /note="Predicted thiol-disulfide oxidoreductase YuxK, DCC
                     family [General function prediction only]; COG3011"
                     /db_xref="CDD:442248"
ORIGIN      
        1 mrgdhaagae pggvivfdgv calcsrwvrf llrfdrrerf rfaamqgaqg sallrahgld
       61 ahdptsflll daqgawtdtd ailrvltglg ggwrlaavlr vlprrwrdga yrvlarnryr
      121 wfgrhvachl pdpqqaarfl d
//
LOCUS       WP_176019845             311 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019845
VERSION     WP_176019845.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..311
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34178
     Region          41..298
                     /region_name="YbbA"
                     /note="Predicted hydrolase of the alpha/beta superfamily
                     [General function prediction only]; COG2819"
                     /db_xref="CDD:442067"
ORIGIN      
        1 mqrvrgwsvl aclalagcam svappatqne akdaatavqg vvlpdteslr vhdpigrdya
       61 lwvalpagya aqpqkrypvl yvtdalysfp lvrsvrnlvg qqginiedfi lvglppqegl
      121 tskqsrsrdy tpsepvrdrp gyysddvtyg gaahyrdfva dhvlpmidar yrtdparraf
      181 aghsygalfg ayvlttrpdm frtyilssps lwfdqhllpr mqdeakapan ptrvllsvgs
      241 yetvkpgpry stgndmlrqa adftaqlers grtlqvdnvv idgedhltvy prvitrallq
      301 vfpgegpytg g
//
LOCUS       WP_176019881             144 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NfeD family protein [Stenotrophomonas].
ACCESSION   WP_176019881
VERSION     WP_176019881.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Green,J.B., Lower,R.P. and Young,J.P.
  TITLE     The NfeD protein family and its conserved gene neighbours
            throughout prokaryotes: functional implications for stomatin-like
            proteins
  JOURNAL   J Mol Evol 69 (6), 657-667 (2009)
   PUBMED   20012272
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Kuwahara,Y., Ohno,A., Morii,T., Yokoyama,H., Matsui,I., Tochio,H.,
            Shirakawa,M. and Hiroaki,H.
  TITLE     The solution structure of the C-terminal domain of NfeD reveals a
            novel membrane-anchored OB-fold
  JOURNAL   Protein Sci 17 (11), 1915-1924 (2008)
   PUBMED   18687870
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..144
                     /product="NfeD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=15161
     Region          23..144
                     /region_name="YbbJ"
                     /note="Membrane protein implicated in regulation of
                     membrane protease activity [Posttranslational
                     modification, protein turnover, chaperones]; COG1585"
                     /db_xref="CDD:441193"
ORIGIN      
        1 mrwevvawga lalllfaaea lapgafmlwi gigaaavfal vavfadipvl wqvvafvvls
       61 vlsiqcyrhw gkprarqsda pllnrraeql vgrvvplqqa iiggqgrvsi ddaswqvsgp
      121 elpagtlvrv vavqgsalvv eava
//
LOCUS       WP_176019894             214 aa            linear   BCT 11-JAN-2025
DEFINITION  2OG-Fe(II) oxygenase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019894
VERSION     WP_176019894.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The DNA-repair protein AlkB, EGL-9, and leprecan define new
            families of 2-oxoglutarate- and iron-dependent dioxygenases
  JOURNAL   Genome Biol 2 (3), RESEARCH0007 (2001)
   PUBMED   11276424
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..214
                     /product="2OG-Fe(II) oxygenase"
                     /EC_number="1.14.11.-"
                     /GO_function="GO:0008198 - ferrous iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016705 - oxidoreductase activity, acting
                     on paired donors, with incorporation or reduction of
                     molecular oxygen [Evidence IEA]"
                     /calculated_mol_wt=23667
     Region          21..>71
                     /region_name="Herpes_UL46"
                     /note="Herpesvirus UL46 protein; cl28045"
                     /db_xref="CDD:355696"
     Region          118..203
                     /region_name="2OG-FeII_Oxy_3"
                     /note="2OG-Fe(II) oxygenase superfamily; pfam13640"
                     /db_xref="CDD:463943"
ORIGIN      
        1 mseavateat tlfqqyaeel qrtgstlipa glvfteeeit rleglqaqip eeavtngdag
       61 dthdiyvrri mldlagempt lvnqpfsgai tdilsaeprr sclaelfqsn dpyfirrcqm
      121 nrmtansfig lhldaasnpd yeysvivqlg rafeggafvv htdddqqhay masyasvlvt
      181 ncryrhevst vlsgernslv yfyskhggvn rrsa
//
LOCUS       WP_176019923             153 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019923
VERSION     WP_176019923.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..153
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=16271
     Region          15..153
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 msswrclfav psprrgmeaf llllarivag vmfsvsgwnk vftdagrerm vhtlveagip
       61 fpalsapvlg aiewiaggll vlgllsrpsa lllaaicava altdgiarip aglslpdwls
      121 wffylsevpl gvlllwiaav gsgrfaiear war
//
LOCUS       WP_176019984             391 aa            linear   BCT 11-JAN-2025
DEFINITION  thiolase family protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176019984
VERSION     WP_176019984.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 391)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..391
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40073
     Region          1..391
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 msniviaaak rtaigsflgq fngvptptlg aaaiaaaleq sgvpasdvse vlmgcvlpan
       61 lgqaparqaa iaagiplsvg attlnkvcgs gmkaimlghd likagsariv vaggmesmsn
      121 aphllpnsrt gnrfgnfqav dhmahdglvn aydgkamgef aecavdkyqf treeqdaysi
      181 esvkraqaaq angafadeiv avkvatrkge vevtsdeqpg rsdiakiptl rpafkkdgsv
      241 taassssisd gaaavvllte edavarglqp larivghath sqepewftta pigaihtlle
      301 ktgwsldqid lfevneafav vamapmrelg iphdklnvng gacalghpig asgarlvvtl
      361 vnalrtrggk rgiatlcigg geataiaiel i
//
LOCUS       WP_176020063             216 aa            linear   BCT 11-JAN-2025
DEFINITION  SCO family protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020063
VERSION     WP_176020063.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..216
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23202
     Region          48..212
                     /region_name="Sco1"
                     /note="Cytochrome oxidase Cu insertion factor,
                     SCO1/SenC/PrrC family [Posttranslational modification,
                     protein turnover, chaperones]; COG1999"
                     /db_xref="CDD:441602"
ORIGIN      
        1 mfnrnvgiil lialaaglgl laaqqvfapk ppagqpatea itlypqpral pdynlaqsdg
       61 trlipgelkg hwtlvflgft fcpdvcpttl aelagaqnqw ealpdglrpr vlfvsvdper
      121 dtatrlgeya hgfhkdtlaa tadvpslerf atslgfvfqk vpgkhfdenp edytlehsas
      181 lavldpqgrl aglvrppfna paiardlqkl teksap
//
LOCUS       WP_176020052             701 aa            linear   BCT 11-JAN-2025
DEFINITION  M13 family metallopeptidase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020052
VERSION     WP_176020052.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Bland,N.D., Pinney,J.W., Thomas,J.E., Turner,A.J. and Isaac,R.E.
  TITLE     Bioinformatic analysis of the neprilysin (M13) family of peptidases
            reveals complex evolutionary and functional relationships
  JOURNAL   BMC Evol Biol 8, 16 (2008)
   PUBMED   18215274
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466452
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..701
                     /product="M13 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=76158
     Region          48..701
                     /region_name="PepO"
                     /note="Predicted metalloendopeptidase [Posttranslational
                     modification, protein turnover, chaperones]; COG3590"
                     /db_xref="CDD:442809"
ORIGIN      
        1 mtrtpkivll tlavsaalvg cgknetpakd atastpaaad aattykldes klpaynafqa
       61 sdldsnldac tafgdyvngk wlaaneipgd rtswgaftil dersvavqhq laeqvaqvkn
      121 pagiekivgd lwatgmdeak vnaqgieplk adlaaidglq dkaaianylr tsaakgenvl
      181 fgfgaeadfk nsavnmayas qgglglpdkt fytdaskadk lkayqahvak vlelsgvaaa
      241 daakqaeevv kfetrlakas kssvelsrdv slyyhpvsla eadaltpnfs wteffksqnv
      301 aapekfslai pafhqevska lgdtdpsvwr aylrfhtvds aspyladafv qesyefygkt
      361 lngqkeqkpr wkrvlgties dageafgqly vkvafspeak akmeelvknl aaslkeriqg
      421 ltwmspetka kaiakwetft pkigypdkwr dwsglqtnrd sylgnvraat afnyqynlak
      481 igkpvdktew gmtpqtvnay ynplqneivf paailqppff dakaddalny ggigavighe
      541 mthgyddqgs rfgptgnfen wwtegdsknf agltgklvkq fdqykvdgqa vnghltlgen
      601 iadlgglata ydalqkasag kedakidgft rdqrfffnwa tvwrtkytpe nakvrlatdp
      661 hapaqfraig apsnlptfta afqckpgtpm srtgdsqvvi w
//
LOCUS       WP_176020116             190 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176020116
VERSION     WP_176020116.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..190
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20948
     Region          10..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpespprsrr kapdsvrqal lhatahtigq nglaaltvqd vadaagvskg alfhhfsskq
       61 dlveatlssl iadfenrvre vlrqsparhg gfsrayvqvn fehllqqeqi ndigltmgnm
      121 lepallvhwr twmrgmlaef pdeacdprly aarcvadgyw ataygrplde derqnaqama
      181 lealklcepa
//
LOCUS       WP_176020210             138 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020210
VERSION     WP_176020210.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..138
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=13949
     Region          41..119
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mnvrllslsl laatslagcg tseppaapaa aptevaavkt pppqyplela ctgvggtstf
       61 kvvigtdgkp sevtlltgag npqldelakt avqgwqfkaa trngeavpat iqvpvsfnpp
      121 qpkpdqcfai eeslrrgg
//
LOCUS       WP_176020162             415 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020162
VERSION     WP_176020162.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..415
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43602
     Region          20..402
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(30..31,34..35,38,70,127..128,130..132,135,155,
                     158..159,162,236,239..240,243..245,248,272,276,329..330,
                     334,338,354,357..358,361..362,365)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 msepataedt algllsrpgf arllayrifa mlsyqvvavt vgwhiyevtr npfslgligl
       61 aevlpffcva pfagylvdhl prrrlgmvac sgliatalvl tsvakgwlpv egvwpiyaai
      121 altgmvrafl spiynalfar vlprehfarg aglgavvfqt gmiagpalgg vlvgfggkgl
      181 ayavatvfal vamgclatlk veepvhagpa apifksiaeg arfvvgnrim vgamaldmfs
      241 vllggvvaml paflheilhh gpeglgilra mpalgsvcvg lwlarhplhr nagrvllfav
      301 agfglcvigf glsqhfwlsa lillfygafd gvsvvirsti lqlatpeemr grvssingif
      361 isssnelgaf yagtmakvlg lvpavvlggf avlsvagita wknptlrkln lrdlq
//
LOCUS       WP_176020219             721 aa            linear   BCT 11-JAN-2025
DEFINITION  M3 family metallopeptidase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020219
VERSION     WP_176020219.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..721
                     /product="M3 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=78961
     Region          38..719
                     /region_name="Dcp"
                     /note="Zn-dependent oligopeptidase, M3 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0339"
                     /db_xref="CDD:440108"
ORIGIN      
        1 mttrlalava mtlglalpay sasaatpaaa naqqanpffa dsplplhfpq fdkikdsdfa
       61 pafdagmaqq lkeveaiant kakptfdnti ialeksgdtl drattvffsl vgadtndtrk
      121 klqadysakf aahsdaialn gklfariqal ydsrttlgld aegvrlveky ydnyvragak
      181 lseadkatlk kmnaelanlg tkfsqnvqse vnasaitvnd vkeldglske qiaaaaeaak
      241 argldgkyvi tllnttgqpp ltnlanralr qkiyeasttr gsrggefdnt alvarimqlr
      301 adkaklmgfa nfaaynltnq taktpeavna mlgklapaav anakreaadl qamidqeqka
      361 agkptfklep wdwafysekv rqakynfdes qlkpyfemkn vlengvfyaa gqefglsfkq
      421 rtdlpvyhdd vtvydvfdad gsqlaififd pyaraskrgg awmnsyvsqs kltgfkpvva
      481 nhlnipkppa gqptlltwde vsttfhefgh alhgmfsnvk ypyfsgtavp rdfvefpsqv
      541 nemwadnpai lknyakhyqn gsampqalld kvlaaakfnq gfatteylga amldqrwhqi
      601 gpdqvpaakd vmaferaale kdgiyyapvp pryktpyfsh imggysagyy ayiwsevlda
      661 ntqkwfrdng glsrkngdhf ratllskggs vdamqlfrdf aghepqiepl lekrgltgag
      721 n
//
LOCUS       WP_176020232             257 aa            linear   BCT 11-JAN-2025
DEFINITION  TatD family hydrolase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020232
VERSION     WP_176020232.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..257
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28345
     Region          4..254
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mkllvdshch ldasefdgdr eavidrarta gvqwqvvpav taaswpklrl vcqqatglyp
       61 ayglhpmfld qhrpehllql rawiererpc aigecgldff vegldaeaqq ayfigqlkla
      121 refdlpvivh arravdavia airrigalrg vvhsfsgspe qaaqlhrlgf llglggplty
      181 draqrlqrlv remplqqlll etdapdqpda girgqrnepa rlaviarhia slrgvdvvdv
      241 aqattdnarr lfslpap
//
LOCUS       WP_176020102             396 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 18 protein [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176020102
VERSION     WP_176020102.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Funkhouser,J.D. and Aronson,N.N. Jr.
  TITLE     Chitinase family GH18: evolutionary insights from the genomic
            history of a diverse protein family
  JOURNAL   BMC Evol Biol 7, 96 (2007)
   PUBMED   17594485
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Fukamizo,T.
  TITLE     Chitinolytic enzymes: catalysis, substrate binding, and their
            application
  JOURNAL   Curr Protein Pept Sci 1 (1), 105-124 (2000)
   PUBMED   12369923
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465181
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..396
                     /product="glycoside hydrolase family 18 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004568 - chitinase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008061 - chitin binding [Evidence IEA]"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=43032
     Region          32..385
                     /region_name="ChiA"
                     /note="Chitinase, GH18 family [Carbohydrate transport and
                     metabolism]; COG3325"
                     /db_xref="CDD:442554"
ORIGIN      
        1 mfrqtmavla vlvaaalpia apaapaqppi fgayypggsa erypvssipa erlthlfyaf
       61 stiedgrcai gaeasanfva laelkrrhph lrtlisiggw gaggfsdaal teasrrrlvd
      121 scmalfferh agsfdgvdid wefpvsggpk elahrpqdra nltklaqafr valdargrka
      181 gqpmlltaal aagrlqtdgp ydpaasydlp alakvfdfin lmsydmgtgf ssvstfnapl
      241 hevpadplap elrrwnnvag avqyyrergv pasklvlgvp fygrgfkvtg esadglyqay
      301 sapadagdwr vikaryldqp gwdkywqpqa qspwlynpae kifisyedpr siglraqfar
      361 eqglagvfmw eltgddeqas llnamlapwq karvgd
//
LOCUS       WP_176020239             186 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020239
VERSION     WP_176020239.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..186
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19908
     Region          4..166
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 msvptiavfv gslrkescnr klahalekla gdkarfqyvq igdlplydqd fdasypaqgt
       61 rlkdqvraad avlfvtpeyn rsvpgvlkna idigsrpygd safagkpaav igasigqigt
      121 avaqqhlrns lafldmhvlg qpeafihfkd glidadgtih negtqaflqg yvdrflalia
      181 vhakgd
//
LOCUS       WP_176020248             300 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020248
VERSION     WP_176020248.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..300
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32936
     Region          17..142
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mspirvqqvr haeahvaihd vrqrvfvqeq gidavlerda ldpvcahvla ldaqgqpvgt
       61 grlapdgrig rmavlaayrg hgvgeallea lvqaghqlgl aelhlhaqlp ardfyarqgf
      121 lpegpefeea gighqqmrrr lqavsaidsr aeavaittai ihrarrrlwl hsrqldpgll
      181 dappvqaalr rfvtarhdkq lrmivhdaaa iasagaplla lfqrlpsviq frevadpidr
      241 alasacllnd agdfyfrlig hrldgesaia lparsqpfeq qlqrvwdrsr ecselralgi
//
LOCUS       WP_176020260             692 aa            linear   BCT 11-JAN-2025
DEFINITION  acyltransferase family protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020260
VERSION     WP_176020260.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Bera,A., Biswas,R., Herbert,S. and Gotz,F.
  TITLE     The presence of peptidoglycan O-acetyltransferase in various
            staphylococcal species correlates with lysozyme resistance and
            pathogenicity
  JOURNAL   Infect Immun 74 (8), 4598-4604 (2006)
   PUBMED   16861647
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Slauch,J.M., Lee,A.A., Mahan,M.J. and Mekalanos,J.J.
  TITLE     Molecular characterization of the oafA locus responsible for
            acetylation of Salmonella typhimurium O-antigen: oafA is a member
            of a family of integral membrane trans-acylases
  JOURNAL   J Bacteriol 178 (20), 5904-5909 (1996)
   PUBMED   8830685
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15196437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..692
                     /product="acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=75697
     Region          4..367
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
     Region          438..680
                     /region_name="SGNH"
                     /note="SGNH domain (fused to AT3 domains); pfam19040"
                     /db_xref="CDD:436916"
ORIGIN      
        1 mqerspgyfp hidglraiav lavilyhlka swlpggftgv dvffvisgfv vsasvdrlpa
       61 iggwaglarf yarrmrriap alvacllvta mfsallipes wlsetsdktg rmaffglsnw
      121 vlastgndyf sprtefnpyt htwslgveeq fyllfpmlfl awakgrrgaw lsvglfaaat
      181 vaslgyavfr agqggheida fylttarfwq lgagvllfql lslsgrftpp pspprgiswr
      241 spllllsvva lgyglwsarp ghspwidglw pvlgtlgllg llqrspggwi gralaatpmv
      301 tvgrlsysly lwhwpvfvlf rwtvgletig tgaaallcva llswlswrwv eqplrhgarw
      361 risnarwvva glgvlvvgag lqtalvktqq ytslsvvsra pldwypyakg lkkeipdcrv
      421 rvsnvpvlgg qarlyergec pgraastrql fvagdshala yhemlqrlav ldgapirlys
      481 sggcalvglr awqgpnpace aytrnvledi qaraqpgdvv llaglrlprl seqyalfdva
      541 qvradhlset asagrkaeia hwieqltplt drgvrivlea pkpvlpappy rcsdvfnrhn
      601 picangmtva rseieqlrep vlaalqqvaa glpgasvwdp mpllcpgerc lptrdgkplf
      661 fdgdhlsgys nrlllpdfqr qlqrlqapav ap
//
LOCUS       WP_176020302             263 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020302
VERSION     WP_176020302.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Upton,C. and Buckley,J.T.
  TITLE     A new family of lipolytic enzymes?
  JOURNAL   Trends Biochem Sci 20 (5), 178-179 (1995)
   PUBMED   7610479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10139723
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..263
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=27556
     Region          77..253
                     /region_name="SGNH_hydrolase_like_4"
                     /note="Members of the SGNH-hydrolase superfamily, a
                     diverse family of lipases and esterases. The tertiary fold
                     of the enzyme is substantially different from that of the
                     alpha/beta hydrolase family and unique among all known
                     hydrolases; its active site closely...; cd04501"
                     /db_xref="CDD:239945"
     Site            order(84,110,139,233,236)
                     /site_type="active"
                     /db_xref="CDD:239945"
     Site            order(84,233,236)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239945"
     Site            order(84,110,139)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:239945"
ORIGIN      
        1 mmgigkylgf llgllvasgg vradqgaavs rllvtpvdql srdevsylqr tvadfaqlqk
       61 yraantalpa prgghprvvf fgdsitegwg adgsstffpg kgyinrgisg qttaqmlvrf
      121 sqdvlalrpn vvvilagtnd iagntgpatq amiednlqam ldlakahgia vvlasvlpvs
      181 eypwmpgiap apkvralnaa lkreadargl vyldyyaama nraggldaql atdgvhptar
      241 gyalmaplae aaikraqanv pkr
//
LOCUS       WP_176020307             191 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176020307
VERSION     WP_176020307.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..191
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20165
     Region          2..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msprssdapq rvidaaaqml arvglnatsi revtklaeap lgstyhhfpg gkqellarat
       61 tmagdkvetl liellkegav qglqqflalw rerllrsgfr agcpvlaaav eepveaapsq
      121 praaaaevfa rwqghlteaf vaegrahada aglaslvias vegavamsra rqdiapfdqv
      181 aeqllraash r
//
LOCUS       WP_176020384             371 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020384
VERSION     WP_176020384.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..371
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38991
     Region          1..348
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(21,23,54,96,235,302,322,324..326)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(21,23,54,96,98,105,183,186,188,235,242,302,322,
                     324..325)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(23,98,183,186,188,325)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mlftphrlga ltlpnrivmp pmtrsraaag nvataqmaey yaqragagli vsegtqispq
       61 gqgyawtpgi hsqaqvqgwr rvtdavhaag griyaqlwhv grvshvalqp dgaapvsasa
      121 llaegvkvfv dptgagpesg vgemlqhsmp ralaeeeipg ivadyaqatr nalaagfdgv
      181 elhgangyli nqfidsqanq rtdgyggslq nrlrflrevv qavvavaggd rvgvrlaplt
      241 tlqgavddtp qatylaaahl lgelgvgylh iaeadwedap lmpvafkqal rmiypgtliy
      301 agkysaerag qaltegwadl igfgrpfian pdlperlrtg aalnapdrat yfgggeggyt
      361 dypaleeaal a
//
LOCUS       WP_176020404             138 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020404
VERSION     WP_176020404.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..138
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14773
     Region          54..137
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mndpetiqfr eavptvedyc qlravaglsa ktreaatral pntifgvcay qgselvamgr
       61 iigdggchlq vcdiavlprl qgqglgkavm qrlsdwmqgn lppsayvsll adgeahrlya
      121 qfgfaptapa sigmyrrf
//
LOCUS       WP_176020436             636 aa            linear   BCT 11-JAN-2025
DEFINITION  CocE/NonD family hydrolase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020436
VERSION     WP_176020436.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 636)
  AUTHORS   Turner,J.M., Larsen,N.A., Basran,A., Barbas,C.F. 3rd, Bruce,N.C.,
            Wilson,I.A. and Lerner,R.A.
  TITLE     Biochemical characterization and structural analysis of a highly
            proficient cocaine esterase
  JOURNAL   Biochemistry 41 (41), 12297-12307 (2002)
   PUBMED   12369817
REFERENCE   4  (residues 1 to 636)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   5  (residues 1 to 636)
  AUTHORS   Bresler,M.M., Rosser,S.J., Basran,A. and Bruce,N.C.
  TITLE     Gene cloning and nucleotide sequencing and properties of a cocaine
            esterase from Rhodococcus sp. strain MB1
  JOURNAL   Appl Environ Microbiol 66 (3), 904-908 (2000)
   PUBMED   10698749
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..636
                     /product="CocE/NonD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=70899
     Region          42..635
                     /region_name="COG2936"
                     /note="Predicted acyl esterase [General function
                     prediction only]"
                     /db_xref="CDD:442179"
ORIGIN      
        1 mrvravavav alslsstvla adtppmtpdi sgkpfvapdv grdydkrvvm vpmrdgtkly
       61 tvivvpkgah napilltrtp ydaagranrs dsprmrdllp qgdevfvdgg yirvfqdirg
      121 kygsegdyvm trplrgplng tkvdhstdaw dtidwlvkhv pesngkvgml gssyegftvv
      181 maltdphpal kvaapqspmv dgwmgddwln ygafrqvnfn yfamqtekrg kgaplpslgy
      241 ddystflrig sagdyarftg vdqltwwkkl vqhptydafw qgqaldavma ktplkvptmw
      301 lqglwdqedm wganhayqam egrdtgnthn ylvmgpwrhs qvnydgsqlg alkfdgdtal
      361 qfrrdvlkpf fdqylvdgap kadtppvlvy ntgenhwdrl qdwprsceka caasskplyl
      421 raggklafqa paagegdyee yvsdpakpvp fvprpvrfgd rdmwttwlvk dqrfvdgrpd
      481 vltfiteplt aplriggtpv vnlqastsgt dsdwvvklid vypdqeastp emggyelpvs
      541 laifrgryre sfsdpkalaa nqvlpyrfdl pnanhtfqkg hrvmvqvqss lfplydrnpq
      601 syvpniylak padyqkatqr vwhsaaqasf ielpvy
//
LOCUS       WP_176020456             309 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176020456
VERSION     WP_176020456.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34042
     Region          11..70
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          99..294
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(109,113,152,166,168,229,246,273)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(110..111,115..116,118..119,122,126,128..134,194,
                     223..227,234..235,238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mndlasggdr ldllrtflri vdsgslsaaa lqlgttqptv srrlqalerq lglrllqrst
       61 hgllltedgq rcqrhaqrvv dewealqael hgqtqmlsgr lrvmvphafg qaqllptmld
      121 flaqhpqlsl ewiledrrpd fiaegidcav rvgavdeprm valplaevpr ivvaapslad
      181 arsittpeqa qalpwislvt yyrerlllhd aqgrahtlsi tprllsdnlf vvqqaaragl
      241 gaavvsawlv akdltegrlv qllpdwqapp lpvhlvfpaa rqqplrlraf idamkaalpq
      301 lhgmrpapr
//
LOCUS       WP_176020463             141 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020463
VERSION     WP_176020463.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..141
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14381
     Region          8..135
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mrdghgldla llilrvatgg fllphalgkl fgwfngpgla gfagelrgfg lpaaaplpll
       61 lallqvasgt avmlgwqtri aalvaaafia ftallalpkg wfwmrggaey pllwtlalla
      121 ialagpgawa vdglvlsgdi a
//
LOCUS       WP_176020472             313 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176020472
VERSION     WP_176020472.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..313
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=34011
     Region          130..311
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mstglllgvl sivsvllala vwlwgtasnr eqrqasvqha eqqlargtgp asapadaarq
       61 aplpapgrrt lpwdgllqra glaqgwklpl lmllpgigls vfavlrlgtf wmfpltllly
      121 llgcwlwlmr rtgklqaqll hqlpdfldnl vrltalgnsl qaafqvasmq tnaplrglld
      181 ttvryarggm dldralnlaa qpyrmdvlkv lavvmgvsir iggradqilq rmgdfmrdle
      241 qaqqelaatt setrmsawvl gllppasavl maisspeffq pvlhdplghk illialgmel
      301 tgafllyrla ksl
//
LOCUS       WP_176020497             108 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020497
VERSION     WP_176020497.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..108
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11920
     Region          10..105
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(31,34)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mqiidaatpe qfqqllaehp ralvdfhkdq cpgcrmldms lqrvasgtag qgttllrvql
       61 evvgeaffre lglrqtptls lfrdgdecmr mpgfqspqqi eaaiaefl
//
LOCUS       WP_176020511             550 aa            linear   BCT 11-JAN-2025
DEFINITION  (2,3-dihydroxybenzoyl)adenylate synthase [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176020511
VERSION     WP_176020511.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436966
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..550
                     /product="(2,3-dihydroxybenzoyl)adenylate synthase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0008668 -
                     2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
                     [Evidence IEA]"
                     /GO_process="GO:0019290 - siderophore biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=59168
     Region          10..540
                     /region_name="EntE"
                     /note="2,3-dihydroxybenzoate-AMP synthase component of
                     non-ribosomal peptide synthetase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG1021"
                     /db_xref="CDD:440644"
ORIGIN      
        1 mipsavdsrl plqqqwpeal varyraaghw rgetfpgflr eraerhaddi avvagdvrls
       61 yaqlwheagr igagllalgl qpgervlvql gntasfistv cglfraglvp vyalpahrit
      121 elahfarkae asayistdvh egfdhrglar alqdevpavr hvlidgeaae fvaleslqgd
      181 rgqlpadpdp qsvaflqisg gstglsklip rthddyiysf rasneicgid rdsvylvalp
      241 aahnfpmssp gffgalyaga rvvlspgpgp daafpliare qvtccglvpp lallwaqaaa
      301 tskhdlsslq vlqvggaklv peaarrvidg lgctlqqvfg maeglvnytr lddpqeliva
      361 cqgrpisadd evrvvddhdn pvaegevghl ltrgpytirg yhndaaasar sftddgfyrt
      421 gdrvqqlpgg ylvvqgragd hinragekis aeeiedhlla hgsvfdaavv sipddylger
      481 scafviqqge vikapalkaw mrgrglaafk vpdqivfvds fdttavgkis rrelraqlra
      541 rhlqqtggtr
//
LOCUS       WP_176020561             540 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020561
VERSION     WP_176020561.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 540)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..540
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=59101
     Region          31..540
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mnpvpcravr lplrlhplml alaalplplf aqeaapapsv nineyivrgn tvldprdier
       61 avepflgpgk tladvekard avhalyqqag yqsvyvelpe qqvsggvvll kvqqtpigql
      121 rvvgtkhesp erirdrvpal aegkvpdfdq aqkeltalne ggrrqvmplv regqvpgtmd
      181 vdlqveeksp wrasaalnnd hsadteklrl saslahdnlw rrghsasigv fiapedmdqa
      241 kvfsasytvp fegtpwslea sgyksdsrvl naggqggagt gtgtnvigng hsiglklnyr
      301 lpgsgawwrq lslgvdfkdt eedtqmgkds lktplkyapi tlafvgvrqg esdqlsintq
      361 lvagtrrlfg ygsdaiafdq krywadpsfv afkadvanth tfgsdwqwya rgslqvtdap
      421 lvsaeqfaag gmytvrgyls aeaigdyggl anlewrtpaw slwsgtdlrl ysfadaaylr
      481 lrqplpeqrd kynlasvglg aqlrlgehlq lrldyawpya dgpvtrkddp rlhfnistsy
//
LOCUS       WP_176020584             783 aa            linear   BCT 11-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020584
VERSION     WP_176020584.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..783
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=86369
     Region          9..782
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mpmptldrrl liavaatamf asglaaaapa ktaadkayas vdpfigtgge ghtypgatvp
       61 fgmvqlspdt riqprekayg waagyryddt sivgfshthf sgtghsdlgd illmpftgnp
      121 glergdpekp rsgyasrfrh ddekaepgyy avtlddykvr aelttsarvg vhryafpkgs
      181 eakvlldmrt smydypgkil wsrvrvrgdg titgfretrg waagrqlyfa mrfsrplagh
      241 elhnteqdiv ykgfappgek dpkqraqieg rqlvgtfdfg kldaplvvkv aispvseaga
      301 ianldaevad fdfdrvraqa kqewtqalsv ldidapehar rsaytalyht llgptlfmda
      361 dgqyrgadna vhqakgytny stfslwdtyr alhplltlvq pekrnsdfvn smlahhehsp
      421 ygmlpvwsfh gledwcmigy havpviaday vkgirgfdad kalkamveta nygpydgiaq
      481 yrelgyvpid eegeaasktl eyafddwtia rmaqamgkad vaatfdkrag nwrnafdkdt
      541 gfmrarkrdg sfrtpfdpsa sgygtdyteg nawqyswyvp qdvaglaaah ggsdallarl
      601 devfnakvdp aifehmedit gligwyahgn epshhvayly shagqpwrtq arlkqimdtq
      661 yadrpdglag nddvgqmsaw yvftalgfyp vapgsgeyil grpflpktal rlpngktfti
      721 vaeglddkht yvgsvtlngk plqrtflrhd eilaggelhf smqaepnrdw pgqgaqapys
      781 msr
//
LOCUS       WP_176020592             209 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF3299 domain-containing protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020592
VERSION     WP_176020592.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..209
                     /product="DUF3299 domain-containing protein"
                     /calculated_mol_wt=21271
     Region          49..192
                     /region_name="COG3495"
                     /note="Uncharacterized conserved protein, DUF3299 family
                     [Function unknown]"
                     /db_xref="CDD:442718"
ORIGIN      
        1 mnrsakvlag vlavvllasc gqpavdapqp qassaaaspa vasavidrwd almpaedsfq
       61 rpppqiglsr gngmdgvggl iddtgsgalp gqaidhsspv paqqfgssav vdgvdgrald
      121 ldgyvvplam ndagqvdell fvpfygacih vpppppnqii hvtlatpitm galwdpyrls
      181 grlqvkhfea diasasydaa aatlsaisr
//
LOCUS       WP_176020605             177 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020605
VERSION     WP_176020605.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..177
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19585
     Region          20..172
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mstppptppp alplvsslvr hyedlvdylr rrfaspglar evvhdvcvrl lerpapadvr
       61 qptallrrma hdaavdrcra edlrrqsvep raglpevacd gagparqaaa aqelaqlvdv
      121 irampcrrrq vfilhkihdi pqaavarrmg iglkaverhl rlamldcrrs ldvralt
//
LOCUS       WP_176020615             892 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176020615
VERSION     WP_176020615.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 892)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 892)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 892)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 892)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..892
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..892
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=94841
     Region          14..868
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mnapnrapgn gacrplrarl pilvaailfa rattssasta ddevffdaaf lpagasarld
       61 lerftqadyv apgayrgdir lngqwqartd ivyreldgss rlcldaerlq gygiapsrll
      121 adpaqvplrp wpqgefcdpl gdlipgatav fdagaqtldl qvpqlylrne argyvdpsqw
      181 dagipalavg ynanayhynn gsgarysgfv glnasgrvag wqlvhqgalt lggsqpqryr
      241 ssaaylqhdv vpwkakltvg dtatpgdlfe svrlrgallg sddrmlpqsq rgfapvvrgv
      301 aesnarvivr qrgavlheas vapgpfeltd lyptgyagdl evevreadgr srrfnvpysa
      361 vpqllrpgqs rwsaglgqvd englsdapgl lqlqyqrgln nalsayggvs agedyraava
      421 gaafntawga laadvslart avqglpvmsg ssfrlaynrn vvrtgtsfav aayryatrdy
      481 vslrdwaslr darardqdvd svarqrnrmd lsmnqqlger ggqlfvigtr rdfwnapgrq
      541 ldlsigysnq wkslsyslnf qrtrdsidfg rgylqdrvpg adlpvaraqd arvdnrlmlm
      601 vslplgrsar aplgnlmhtr srngepatql stngissldd rfsygatlsr iagsnsvdln
      661 tgyrgargqw aasisngssy tqlglgasgg avlhgdgltl spplgdtval vhaagaagar
      721 iengggarld krgyavvpfl tpyqlntisi dpkgtgfsve lqetarsvap ragamvrldf
      781 strsshglmv dartedgrpl pfgaeatdaa gsnvgvvgqg srlllsglqd sgpvqvqwgt
      841 gadqqcvlqv qipaarstdg ytvidgrclr ptptanshpa appplaalen ap
//
LOCUS       WP_176020638             319 aa            linear   BCT 11-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Stenotrophomonas
            sp. NA06056].
ACCESSION   WP_176020638
VERSION     WP_176020638.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..319
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33913
     Region          7..297
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 msastgsrlv iyaalagnla iaiakfiaag lsgssamlse gvhslvdtln evlllyglhr
       61 aekapdtlhp fgygrelyfw sfivallvfa agagvsayeg iqhirqpepa tnhaisysvl
      121 gisilfegas wwvalrefrr skgslgyfea frrskdpstf tvlledsaal lglgfalvgl
      181 laaqllempv ldgvaslcia svlaltafll aretkgllig epahpavaqr imavavtdpd
      241 lrsangvttl qmgpeqvvam lsaefeddrs tpqieacitr iesavkqefp elvalfikpq
      301 tpevfaarra aldrpatad
//
LOCUS       WP_176020697             297 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176020697
VERSION     WP_176020697.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32934
     Region          7..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,228,245,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     222..226,233..234,237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mgvenydqla lfalvarers ftraaaqlgm sqpalsrsmr qleerlgvrl larttrsvsp
       61 teageqllrv iaprfeeidt elaqlsayrd kpagririta gehaaltvmq pvlgkllpth
      121 adlnievivd ygltdivaeg fdagirmgeq vakdmiavrv gpdlrmavvg spayfrhhpk
      181 pksphdltrh ncitirlpth ggifawefek kgqelkvrve gqlvfnnial rlgaaleglg
      241 laympedlvr phvqagtlvh vlqdwcpsfp gyhlyypsrr qsspaftvlr dalryrg
//
LOCUS       WP_176020745             396 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020745
VERSION     WP_176020745.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..396
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=43487
     Region          <50..313
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mysrifirla aplaltlllp faigfewpva lrwailttmt lswlgfawwt araqahrspe
       61 harvmreqdq lltelrsfvg neidgsrgev erardlirqa vsslggsfda mnrksrqqsq
      121 alsrivdrag deggagldva rfaqhashrm eqlvealeqv sgqssttvqh idqmaqhldg
      181 ifalledvks iadqtnllal naaieaarag eagrgfavva devrnlsers ttfneqirkl
      241 ahsskdaiak vretvshmas rdmdrsrear qeaaamldnv aqinaslgdg mrevsdcars
      301 idgsvaeavr alqfediatq alggvhthld rltainreav alqellhrng gvfdeeiasa
      361 lqrtgsrlre lrsewerpph kpvaqqsmga gtvelf
//
LOCUS       WP_176020783             260 aa            linear   BCT 11-JAN-2025
DEFINITION  ParA family protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020783
VERSION     WP_176020783.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..260
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27628
     Region          1..249
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mriwavanqk ggvgkttttl algrglaalg hrvllidldp hasltrafgv piepapagvl
       61 elfgappadl stlshasttg gldyvcaqas latlerrsan qpglglalqn alarhqgqhd
      121 yilldcaptl gllminalaa adrliiptqa eplalhgldg mvrtgemver srrrplpisi
      181 lptlfdrrtr tgneslramq drhasrvwed aipidtrisn aagltlpsig edypgrglaa
      241 yrralnwilg edaraleqaa
//
LOCUS       WP_176020784             365 aa            linear   BCT 11-JAN-2025
DEFINITION  chemotaxis protein CheW [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020784
VERSION     WP_176020784.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..365
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=38442
     Region          <87..>214
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          223..364
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 mnttgmlddy ldellgdiav apvasdaapr pasaaadaer eptwddlpae viyetdtlaa
       61 apasddatle aafdaaatpa adaereptwd dlpaevvyet dtvavaspva ppgpeptwdd
      121 lpdeviyetd aadslahtds pglqaafeaa adgevvpala ppavtkvaar pepapmpsma
      181 rvavappprv avdtpssnrp gtwqelqaqa hqpassphpq nrragertsr wlrlrcgtqa
      241 yalellkvqe vvlpvpllpl rgtapemlgi mnlrgqvvpv mdlglhlgaa saeddaqtri
      301 vvleengetl glrvsavedv anltdsqiep pdtaricqis nelfrgvari sqrpmillda
      361 tqllg
//
LOCUS       WP_176020766             501 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54 dependent transcriptional regulator [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176020766
VERSION     WP_176020766.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Arora,S.K., Ritchings,B.W., Almira,E.C., Lory,S. and Ramphal,R.
  TITLE     A transcriptional activator, FleQ, regulates mucin adhesion and
            flagellar gene expression in Pseudomonas aeruginosa in a cascade
            manner
  JOURNAL   J Bacteriol 179 (17), 5574-5581 (1997)
   PUBMED   9287015
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20556987
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..501
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=54567
     Region          5..119
                     /region_name="FleQ"
                     /note="Flagellar regulatory protein FleQ; pfam06490"
                     /db_xref="CDD:428975"
     Region          <140..493
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 msesrilvld ndavraertv allefmdfnp rwvsdaadfd larqrqndwm avivgnldds
       61 aastalyawl ggsslpppvl ladgdatafa hrhglheani wpleaplrha qmeallrras
      121 lkrldaehqa gavqeqgptg ngpavtelrt mieqvaafdt tvlvlgesgt gkevvsrsih
      181 qrsprrdgpf vaincgaipa elleselfgh ekgaftgalt arkgrfemae ggtllldeig
      241 dmslpmqvkl lrvlqersfe rvggnqtirc nvrviaathr dlesriadgk fredlfyrln
      301 vfpidvpalr erredlpalv etiatqlart grgevrftpe alqalagyew pgnvreltnl
      361 verlavlhpg asvrvqdlpa ryrgdaalat vavaaappvv aseerldlrs fsfhtpgsgn
      421 qpslehgiav nraaapaalp ddgldlrnhm anielgline alertqgvva haaqllglrr
      481 ttlveklrky giereqaela s
//
LOCUS       WP_176020806             260 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176020806
VERSION     WP_176020806.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..260
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29600
     Region          33..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(34,59)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(41..42,53,56,60..61)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          105..259
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mmrseaerke lggflkacra rvepatlglp agrrrtpglk reevalaigv svswytwieq
       61 grevraspev lerlaqvlrm sdderayafa lsgygvples pdetvtdglr qlveamqpip
      121 ayvrntrfdi lawnpaiael fvdygqlaph erntlrlmfl yppyrtliln weemtrglla
      181 sfraamaqap dkapflalae digthseqfr ewwpehdvrr fdegakklnh ptrglldlqy
      241 valvpesrhd lslvtylprr
//
LOCUS       WP_176020827             130 aa            linear   BCT 11-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176020827
VERSION     WP_176020827.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629346
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..130
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=14368
     Region          17..111
                     /region_name="DUF4440"
                     /note="Domain of unknown function (DUF4440); pfam14534"
                     /db_xref="CDD:434023"
ORIGIN      
        1 menrspegly eaqlrvleqq lrdalldgdh gaatallspm lfmmdgqggr mldlpwmqdw
       61 rqghlqihal qvhavetllc grlallsgdv qlhvhwlgre hvrrlrllrv wtscsgagga
      121 qllsmtvlag
//
LOCUS       WP_176020835             204 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176020835
VERSION     WP_176020835.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 204)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132634
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..204
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23080
     Region          70..202
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd03674"
                     /db_xref="CDD:467542"
ORIGIN      
        1 mngdngryfs ghpafmsett eslavlddrl rsllhdyark epahdalaae fgtliddved
       61 afrrerlagh ftascwlvsa dgqrlllthh rklqrwlqlg ghadgdrdla rvalkeaeee
      121 sgltglvldd paifdldkhw iperkdvpgh whydvrfvir alggedfvls eeslelawrp
      181 vaevaadpes desmqrmarr wlar
//
LOCUS       WP_176020850             833 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176020850
VERSION     WP_176020850.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 833)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 833)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 833)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..833
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86247
     Region          13..82
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          84..144
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(90..92,95)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          169..820
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     human copper-transporting ATPases, ATP7A and ATP7B;
                     cd02094"
                     /db_xref="CDD:319783"
     Site            order(468,470,775)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Site            order(512..514,577,593..595,624,664..666,686,689,692,711,
                     714)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319783"
     Site            order(776,804,808)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
ORIGIN      
        1 mstasvtavp gttstlslpi egmtcascvg rveaalakve gvasvsvnla teradirssg
       61 pidrdaliqa vesvgyevpa attelavegm tcascvgrve rallavpgvs qasvnlater
      121 atvrgvagid alvaaidnvg yaahaidggt qvdeeaaekk daervalkrd lilasvlaap
      181 vfvlemgshl ipgmhhwvms tiglqaswyl qfvltalvla ipgrrfyqkg fpallrlapd
      241 mnslvavgta aafgysvvat fiprllpagt vnvyyeaaav ivalillgrf levrakgrts
      301 eaikrlvnlq akvahvsreg rivdipinev llgdlldvrp gervpvdgev tdgrsfvdes
      361 mitgepipve ksagssvvgg tvnqkgaltl ratavggqtm laqiirlveq aqgsklpiqa
      421 vvdkvtlwfv pavmlaalat flvwlifgps paltfalvna vavliiacpc amglatptsi
      481 mvgtgrgaem gvlfrkgeal qllkdakvva vdktgtlteg rplltdleia dgfdraqvla
      541 rvaavesrse hpiaraivea ateqgialpa mddfesvtgm gvratvdgar vevgadrfmr
      601 slgvdigsfa vladrlgneg ksplyaaing rlaaiiavsd pikpstpaai aalhqlglkv
      661 amitgdnaat aqaiarqlgi ddvvaevlpe gkveavrrlk aaygqiafvg dgindapala
      721 eadvglaigt gtdvavesad vvlmsgnlqg vpnaialska tignirqnlf wafayntali
      781 pvaagalypv wgvllspvfa agamalssvf vlgnalrlrr fqapmadash vah
//
LOCUS       WP_176021023            1056 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit [unclassified
            Stenotrophomonas].
ACCESSION   WP_176021023
VERSION     WP_176021023.1
KEYWORDS    RefSeq.
SOURCE      unclassified Stenotrophomonas
  ORGANISM  unclassified Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="unclassified Stenotrophomonas"
                     /db_xref="taxon:196198"
     Protein         1..1056
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113421
     Region          1..1040
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mdfsrffidr pifaavlsiv ifaaglisip mlpigeypev vppsvvvrtv ypganpkvia
       61 etvatpleea ingvegmiyl ksvagsdgvl qmtitfrpgt dpdeaavkvq nrvaqaqarl
      121 pedvrrqgvt tqkqsptflm vvhltspngk ydtlylrnya rlhvkdalar iqgvgdaqif
      181 gggdyamraw ldpdkvaarg ltasdvvram reqnvqvsag qlgaepmpns qfltlinaqg
      241 rlrseqefgd ivlksgtdge vvrlsdvarv elgagdytlr sqldgknavg igifqapgan
      301 aleirdavma smdemqktmp advkyeavyd ttifvrdsik avvstlleai alvvlvvilf
      361 lqtwrasiip liavpvsivg tfgalyllgf sintlslfgl vlaigivvdd aivvvenver
      421 nieegltpla aahqamrevs gpiiaialvl cavfvpmafl sgvtgqfykq favtiaistv
      481 isainsltls palaarllkp hgapkdaptr iidrlfgwvf rpfnrffkss sekyergvsk
      541 ilgrrgavfv vyavllvgtg fifklvppgf iptqdklyli agvklpegss iartdemlrk
      601 vakiaqetdg vahtisfpgl nalqftntpn tgvafiplkp fserhgrtaa qinaeinqki
      661 aglqegfafa mmpppilglg ngngyqmfiq drgnlgygal qnavqsmqga vaqtpgmafp
      721 itsyqanvpq ldaevdrvka kaqgvqltel fdtlqtylgs ayvndfnqfg rtwqviaqad
      781 gqfrdsvedi gklrtrndrg emvpigsmvt vketygpdpv lrfngypaad lageadprvl
      841 ssaeamnnlt aiaakvlpvg matewtdlsy qqatqgkaaf ivfpvaimla flvlaalyes
      901 wslplavili vpmtllsalf gvwmtggdnn vfvqvglvvl mglacknail ivefarelem
      961 ggkgiveaal eacrlrlrpi vmtsiafiag tvplvlshga gaevrsvtgi tvfagmlgvt
     1021 lfglfltpvf yvalrkfvtr ngggqlvqhg eptihh
//
LOCUS       WP_176020979            1030 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176020979
VERSION     WP_176020979.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..1030
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112882
     Region          1..1007
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msiaefsirr pvttimcfvs lvvvgliasf rlplealpdi sapflfvqip ytgstpeeve
       61 rtiirpvees latmtgikrm rssatseaas ifiefsdwdr diaiaasdar eridairsdl
      121 pddvqrynvf kwsssdqpvl kvrlasttdl ttaydmldre fkrrieripg varveitgap
      181 pneveiaidp nrlnahglsi nelsdrlrtl nfsisagqid dngqrvrvqp vgeitdlqem
      241 rdlvinakgl rlgdiadvrl kparmsygrr ldgnpavgld iykersanlv dvsrgalaev
      301 eairaqdsmr dvqikvidnq gkavtsslle laeaggvgli lsvtvlfffl rhwpstlmvt
      361 laipicftit lgfmyfagvt lniltmmgll lavgmlvdna vvvvesiyqe rerlpdqprl
      421 asiigtrnva ialsagtlch civfvpnlfg etnnisifma qiaitisvsl laswlvavsl
      481 ipmlsarmat pklvhsqtgm iarlqrryaq lldwslrhrg wsllgillvv lvslvpmklt
      541 kidmfggdgg kdifigymwk gaytyrqmse evarveawve enrerlhvqq vyswyseqeg
      601 sstvvtldek yakdikalqe elrkglpksa rtdyfvgnqg gdggggggnq gvqvqlvgds
      661 samlqeigqe vlpllaqrte lrdvridnge kggelkvhvd reraaafgfn aeqvasfvgl
      721 alrgapmref rrgdnevpvw vrfagaeqss pedlagfsvr tgdgrsvpll slvsvdvgss
      781 atqigrtnrq ttltikanla ekitapdgrk ameavlkpmn fpagygftfd ggdygddnea
      841 mqqmvfnlli alvmiyvvma avfesllfpa aimsgvlfsi fgvfwlfwit gtsfgimsfi
      901 gilvlmgvvv nngivmiehi nnlrrggmgr tqalvegsre rlrpimmtmg tailamvpis
      961 ltdtqmfgng peyspmarai agglafstvv sllflptiya vlddlrnavv rliqrargrd
     1021 vtaavgqell
//
LOCUS       WP_176021029             241 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021029
VERSION     WP_176021029.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 241)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..241
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25533
     Region          2..239
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mtpsrtilit gassgigagi arslarpgar lvlgarrvdr lqaladelrq qgadvrvhal
       61 dvtqraqvea fadaarqhfg sidvivnnag vmplsrmasl kveewdrmid vnirgvlygi
      121 aavlpgmiaq rsgqiinias vgaltvspta avycatkyav raiseglrqe hrelrvtcih
      181 pgvveselan sitdpaaael mvgyraialq pdaigravrf aieqpadvdv neivvrpvat
      241 m
//
LOCUS       WP_176021065             222 aa            linear   BCT 11-JAN-2025
DEFINITION  YoaK family protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021065
VERSION     WP_176021065.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..222
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=23642
     Region          4..214
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mgirlptwvw igavalscva gmvnvvgflg fehqavshmt gstsqlgmal aqgdwravgh
       61 lwglliafsl gamvsglliq dsalqlgrry gvalalesll llmaiplfkq qqiwgalaaa
      121 macglqnama ttfsgavvrt thlsgmftdl giglghllrg lplqvrrltl sgliisgfla
      181 ggvigawlfv rwqydallap alltgltgiv yvvyqqwarw rr
//
LOCUS       WP_176021069             233 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021069
VERSION     WP_176021069.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..233
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25367
     Region          10..231
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mlqirksatr glaehgwlss rhtfsfasyy dpryvsfgpl rvinedkvig gqgfgthshs
       61 nmeivsyvlg galehkdsmg tgsvlrygdv qrmsagsgvs hsefnhsatd pvhflqiwlf
      121 pqtenitpsy eethftpesk rgqlrliasp dgadgslhih qdarifatil dgeqklhhal
      181 atgrgayvqv argqlqvngi tleagdalqv sdeaqltlen gndaevlvfd lpl
//
LOCUS       WP_176021072             379 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021072
VERSION     WP_176021072.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..379
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38702
     Region          12..374
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(20..21,24..25,28,60,110..111,113..115,118,137,
                     140..141,144,209,212..213,216..218,221,249,253,302..303,
                     307,311,327,330..331,334..335,338)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 mtpsspraqq hatraaffip gfataawapm vpyakakagl sdaslgglll clglgsllam
       61 plagaltarl gsrrlmiatt alillalpll tlaptplalg atlfvfgagv gamdctmnmq
      121 avaverdagr pmmsgfhafy siggfvgagc mtgllvlgtp lwlssliava amllvallsa
      181 phwrpqrilh dgpmlavphg vvlfisvlaf ivflaegsml dwsavflaev rqvprdqaga
      241 gfavftlamt amrlfgdgiv erlgrtrtiv mggiiaaagf tlatlvpsfa malvgyvlvg
      301 lgcanivpal fsmagqqram pesiaitavt tlgyagilag paaigalaha tslgfaflcv
      361 aamllgvaas arslarrlp
//
LOCUS       WP_176021087             164 aa            linear   BCT 11-JAN-2025
DEFINITION  CinA family protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021087
VERSION     WP_176021087.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Galeazzi,L., Bocci,P., Amici,A., Brunetti,L., Ruggieri,S.,
            Romine,M., Reed,S., Osterman,A.L., Rodionov,D.A., Sorci,L. and
            Raffaelli,N.
  TITLE     Identification of nicotinamide mononucleotide deamidase of the
            bacterial pyridine nucleotide cycle reveals a novel broadly
            conserved amidohydrolase family
  JOURNAL   J Biol Chem 286 (46), 40365-40375 (2011)
   PUBMED   21953451
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Martin,B., Garcia,P., Castanie,M.P. and Claverys,J.P.
  TITLE     The recA gene of Streptococcus pneumoniae is part of a
            competence-induced operon and controls lysogenic induction
  JOURNAL   Mol Microbiol 15 (2), 367-379 (1995)
   PUBMED   7538190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..164
                     /product="CinA family protein"
                     /calculated_mol_wt=17004
     Region          9..160
                     /region_name="PncC"
                     /note="Nicotinamide mononucleotide (NMN) deamidase PncC
                     [Coenzyme transport and metabolism]; COG1546"
                     /db_xref="CDD:441155"
ORIGIN      
        1 msiptdaeln aqaaalgqrl qqaslqlvta escsggwiak cmtdiagssa ffdcgmvvys
       61 yeakqrllgv raqtleqfga vsretvlemv sgalvnsgag iavavtgiag pgggspdkpv
      121 gcvwigwkrr ggyaraelfq fdgereairr qtvaaalhgi daql
//
LOCUS       WP_176021121             146 aa            linear   BCT 11-JAN-2025
DEFINITION  group III truncated hemoglobin [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021121
VERSION     WP_176021121.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Keppner,A., Maric,D., Correia,M., Koay,T.W., Orlando,I.M.C.,
            Vinogradov,S.N. and Hoogewijs,D.
  TITLE     Lessons from the post-genomic era: Globin diversity beyond oxygen
            binding and transport
  JOURNAL   Redox Biol 37, 101687 (2020)
   PUBMED   32863222
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Bustamante,J.P., Radusky,L., Boechi,L., Estrin,D.A., Ten Have,A.
            and Marti,M.A.
  TITLE     Evolutionary and Functional Relationships in the Truncated
            Hemoglobin Family
  JOURNAL   PLoS Comput Biol 12 (1), e1004701 (2016)
   PUBMED   26788940
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Wajcman,H., Kiger,L. and Marden,M.C.
  TITLE     Structure and function evolution in the superfamily of globins
  JOURNAL   C R Biol 332 (2-3), 273-282 (2009)
   PUBMED   19281958
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Vinogradov,S.N., Hoogewijs,D., Bailly,X., Arredondo-Peter,R.,
            Guertin,M., Gough,J., Dewilde,S., Moens,L. and Vanfleteren,J.R.
  TITLE     Three globin lineages belonging to two structural classes in
            genomes from the three kingdoms of life
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11385-11389 (2005)
   PUBMED   16061809
REFERENCE   5  (residues 1 to 146)
  AUTHORS   Wittenberg,J.B., Bolognesi,M., Wittenberg,B.A. and Guertin,M.
  TITLE     Truncated hemoglobins: a new family of hemoglobins widely
            distributed in bacteria, unicellular eukaryotes, and plants
  JOURNAL   J Biol Chem 277 (2), 871-874 (2002)
   PUBMED   11696555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..146
                     /product="group III truncated hemoglobin"
                     /GO_function="GO:0005344 - oxygen carrier activity
                     [Evidence IEA]"
                     /GO_function="GO:0019825 - oxygen binding [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16969
     Region          14..127
                     /region_name="TrHb3_P"
                     /note="Truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 3 (P); cd08916"
                     /db_xref="CDD:381257"
     Site            order(30,43,46..47,53,56..57,60..61,71,73..75,78..79,82,
                     84,88..89,92,116,119..120,123)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381257"
ORIGIN      
        1 mnatpttvpp iaspelcsee evtrlvhdfy arvrdeerlg pvferhvhdw pehlaqlvdf
       61 wsamlrgtrr fkgspmskhm aidlekdlfd rwlvlfhitt aecnnppmqa laddvaaria
      121 etfwrryqml rwpqvmlpvl gvrtkd
//
LOCUS       WP_176021125             277 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176021125
VERSION     WP_176021125.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13797492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..277
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29930
     Region          3..156
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          <118..277
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 madrlaille rfavtasvfh agalcginsl egegeagqlh lvrsgplqvs hgaqtvqvev
       61 pslllyprpl phrfhtdpqh gadmacanlh feggrlnpis aalpdficlp ladlyggdaa
      121 lellfeeafe qrcgrtvmvn rlfevvmiqv lrqlmeggem rgglfaglgh prlrlalvam
      181 heapaqawtl edladvagms rsvfaasfre amgttpghyl qgwrvglaqq alrqgrplkr
      241 iadevgygse aalsrafkah tgqsprqwre qarvaaa
//
LOCUS       WP_176021209             300 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfurtransferase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021209
VERSION     WP_176021209.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..300
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31158
     Region          38..297
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mkpidppwtt lvdvatlaaa lgagvrvvda ratastavrv vdarasladp qagsglyaqg
       61 hipgavhadl nrdlsdltrv ghgrhplpds dafaarlgqw gigtdtqvvv ydgsdgsmaa
      121 arlwwllrli ghtkvavldg giaawhaagq platgssdva alpaypgrfd tsqiasadei
      181 esrlkhapgw lvdaragerf rgevepldpv aghvpgavnr pfalnvldgr lrdaeelrae
      241 lqsvignqdp qrvvlmcgsg vtachlllam esaglsgari yadswsgwvs dssrpvatga
//
LOCUS       WP_176021253             278 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021253
VERSION     WP_176021253.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..278
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28971
     Region          3..276
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mtktrvlaal imapvaiaai lllptqwlaa aaaavlligl wewlkladve dtlartvllv
       61 lnlllmvllv wadagtlvlf qiatlvgvaw wlaalvwlrf fnfgaqpgsp arilkllagt
      121 laivpawaal vlihaggdpp ghqghlwlla alalvwaads gayfagrrfg khklaprisp
      181 nktweglvgg livgvavavg lgwlagidaa hlpgllvtsv vavfasvlgd lfeslikrha
      241 gakdsghlip ghggvldrvd gvlaaipvfa lgkeifgf
//
LOCUS       WP_176021270             300 aa            linear   BCT 11-JAN-2025
DEFINITION  peptidylprolyl isomerase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021270
VERSION     WP_176021270.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..300
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=32529
     Region          45..249
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mphrrclalt alalacllps lasaatpyrs pqqildasaa sdwrtpdaan llymdlpagr
       61 viielapqfa prhvaniqtf ahehfwdgts iyrsqdnfvv qfgdadadda akakpfgsaa
      121 rklpaefera saglkvsvlp drdgwaaqtg fvdgfpvgqd pqagkawlah cygmlgagrs
      181 needssigae lyvvtgqspr qldrnitlvg rvlkgmells aiprgpapmg fytdpklrtp
      241 ivsirrasdv pvaertpiqv lrtdsktfad tvearrnrvd dfykrpaghi dlcnipvpvr
//
LOCUS       WP_176021297             732 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021297
VERSION     WP_176021297.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 732)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..732
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79405
     Region          42..711
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mpshhprfkp hslalalaal lpsvafaasd ddshrdrhlt elssvqvtas plqgdaesla
       61 rpvevlager ldeqkagtlg dtvaklpgvq stffgpgvgr piirgqegpr vavlsngmgn
      121 mdastvsadh atsiepflad qievlkgpat llfgsgaigg avnvvdgria relpdrplsg
      181 raelrgnsvn dersgmfrld gvsgnvvlhv dglvrngddf ripgyavidg ledhhddhdh
      241 ageegeeprr grldnssirt raggvgatwl geggyfgvsa styrtnygip ngahvhadgd
      301 dhdhghdhdh geeeegeehd vridmvqnrf etkagiynpv sflkninarv aytdyehvel
      361 eagtpstrft nrgiegrlea vqqqiggwdg afglqvgnsd fgakgeeafv pdtgtknigv
      421 fvlqekqfgp fklelggrhd qvkldptgdy qrrkfdatnl saagiwklnd avdlrigvds
      481 seraptneel yaagahiatr sleigdanlk tergqrielg ihthserldf saaiyqtkfk
      541 dfiyladtgv teslpvrawt qqdavfkgae aealvhlfeg gagdwdlrvf gdyvqakldg
      601 ngsrtldiav phgdhnhnys velantgylp riaparvgad lrwakdgwra svgavrysrq
      661 kdvaqneeps ngytlvdahl ayrwdrsdsn syelfldgsn ltnrevrpht sllkdysplp
      721 grgvafgira ff
//
LOCUS       WP_176021311             201 aa            linear   BCT 11-JAN-2025
DEFINITION  HD-GYP domain-containing protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021311
VERSION     WP_176021311.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..201
                     /product="HD-GYP domain-containing protein"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22117
     Region          <16..198
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mplprppdll haqaclidal smslqmrday trhhcdrvgl laqhlalhcd ldeeacaqvg
       61 laarfhdigk igipddvlls prrhsdeera imrehpvrge hiflatgrsd aapvarlira
      121 hheafdgsgy pdglqgenip lgarivtivd aydamtsarp yraamehetv lqildeqagg
      181 lvdpyvlqrf hgmlkhepal l
//
LOCUS       WP_176021346             490 aa            linear   BCT 11-JAN-2025
DEFINITION  MATE family efflux transporter [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021346
VERSION     WP_176021346.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..490
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52336
     Region          13..449
                     /region_name="MATE_yoeA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Bacillus
                     subtilis yoeA; cd13138"
                     /db_xref="CDD:240543"
ORIGIN      
        1 makapldlts gpigrnlllf alpilagnia qslngsvnav wvgrflgeaa ltatananni
       61 mffligsvfg fgmastilig qaigardiaq arrvvgtsat ffiglsviia iagwflahsl
      121 laamgtpaas lplaeaylri iflamptlya faflsaalrg agdsrtpfrf llvsvvldia
      181 lnpvlifgmg lfpelgiags awatlvsqtl slaglllymr hkrhtlwlgr admhlfkldm
      241 tilralvvkg vpmglqmvli slsvimlmtm vnqygtdtga aygaslqlwn yvqmpamaig
      301 aacssmaaqn vgaqrwdrvr gtarqgilfn flltgalilp lvlldqysla lflpqgsesl
      361 qiarhlnhiv igsflffgvs fvisgvvrst gavlppllil aaslwgvrvp faeflqpywg
      421 adaiwwsfpa gslvsmllsl ayyrwggwrk arminkpvha eelatpseip acppspvadp
      481 daaleatrph
//
LOCUS       WP_176021394             401 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021394
VERSION     WP_176021394.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13213516
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..401
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=43912
     Region          <17..129
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Region          146..388
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mlarlnhnam lrysglftwg tvglwlaiyl idpvsltles ldgeagfrii pwasaylafg
       61 fvywvltrsl gesrpgffdh aalilltaca igvsyfsgta lgsillmvva gllpwllgpr
      121 igvvwlvasn lavlpvyiqp lgfppviavl qavgymgfss fvfvialvar rqaeareeqr
      181 rlnaelratr allaesarvn ertrisrelh dllghqltal tlnlevaghl aegqalehvk
      241 rshalaklll gnvrevvsql retgaidlaa alrpltehvp sldiqleiee plnvedpqra
      301 hvllrctqei itntvrhaga rhlwlrvyre vpdqvvvear ddgvgaetvn vgnglrgmre
      361 rlqqcggqlq vetrpgegfr lratvpatvl taltqvpegv r
//
LOCUS       WP_176021484             143 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: OsmC family protein [unclassified Stenotrophomonas].
ACCESSION   WP_176021484
VERSION     WP_176021484.1
KEYWORDS    RefSeq.
SOURCE      unclassified Stenotrophomonas
  ORGANISM  unclassified Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="unclassified Stenotrophomonas"
                     /db_xref="taxon:196198"
     Protein         1..143
                     /product="OsmC family protein"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /GO_process="GO:0006972 - hyperosmotic response [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=14838
     Region          5..139
                     /region_name="osmo_induc_OsmC"
                     /note="peroxiredoxin, OsmC subfamily; TIGR03562"
                     /db_xref="CDD:274650"
ORIGIN      
        1 mgisrhatah wegdlksgkg qlstpqsgll dktrygfnsr fgdekgtnpe eliaaahagc
       61 ftmalsaklg eagftptsld teakvdlsme ggpqlsqirl kvkavvpgid aaqfraiadd
      121 akqncpvska lsavpislea elg
//
LOCUS       WP_176021547             134 aa            linear   BCT 11-JAN-2025
DEFINITION  GFA family protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021547
VERSION     WP_176021547.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..134
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14485
     Region          15..>116
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mgittvagva vqaqhrasch cgtvelllel pegivdprrc dcsmcrrrga iaasvardgl
       61 qivrgqahlr lyqfnthvae hyfcgvcgiy thhrrrsspd qygynvacle gidpfalgti
      121 pvndgvnhpa drtg
//
LOCUS       WP_176021552             697 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021552
VERSION     WP_176021552.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 697)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..697
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76137
     Region          14..697
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mpalpsrrpl lytlflptll asaiaqaqdg taartldkvt vvaerastat ktdtaltetp
       61 qaisvvtqql ftdrgahnlq evlrysagvt adawgldtrn dassvrgldp vqyqdglrrs
      121 ygfsplarpe vyglervevl rgpssvlyga gatggiinam skrptfgatr geiglqlgsf
      181 drrqlqgdig galnddgtva grfvglvres nmqtdvlkdd rvylapslsw rgerstltll
      241 asyqhdktgs sqqflplaat lyaapgrrld pttfigdagf dridsrvysl talfdhrfnd
      301 avslrsavry idgrttlqql yvdsysnpen pfidadrrvv nrtaygtqpd iqvlsadnav
      361 qfdfstgvfq hlllagvdys qykeqlqrld atgtpidvya pvsiaptvrg werqpdqtss
      421 qlgvyvqdqi rwadrvslvl garrdharsk tegqpsqtdn attyraglig elgggvspyl
      481 sysesflpvs gqdlfgsafk pmrgrqaegg ikwqparnml ltlaayrite tnrqtndpdn
      541 vlnvvqtgqi rskgvelegq fqfandltvt aaiarneaev srsnfalevg erlndtpqdl
      601 asawvskafq lddaarmklg lgvrhvgntv slgnggrvit psytladalv evqvtnwtwa
      661 lnitnltdkr yyapcrtfgd cfagyprvvt gtisyrf
//
LOCUS       WP_176021623             247 aa            linear   BCT 11-JAN-2025
DEFINITION  cysteine hydrolase family protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021623
VERSION     WP_176021623.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..247
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25174
     Region          48..230
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mnftafglas ligmaavapv vaaepahpti rhmagaptia sldaaktavl vidfqneyfd
       61 asaapgfagg rmvipdgvaa lrqarrvvdf adahgirvih vqhvlpagap lfaqgsvnaa
      121 fhrdmqprkg eavvqkdnvs vfagasaavl dkalqdagid tlivtglqth acvagaarda
      181 aaaprgyrvi vasdavasrd ldlangqtig hralheasla qiddvfgdvm ttdallalpv
      241 hkaadga
//
LOCUS       WP_176021646             240 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021646
VERSION     WP_176021646.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..240
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=26219
     Region          1..226
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mrhglarvls kagvcsrsea arwiaegrvr vagrivrdpe fpianpappi evdgqpmgap
       61 qrlylmlnkp rgvvttvqde rgrdtvyrcf dgaglpwiap vgrldkaseg lllfsndpqw
      121 aarltdpdtg pqktyhvqvd rlpdddtlaa lragvedege fllalavrvl rsgdktawle
      181 vvldegrnrh irrllaafdl qvlrlvrvai geltlgdlgk gqwralevsd qqrlgaaapg
//
LOCUS       WP_176021657             163 aa            linear   BCT 11-JAN-2025
DEFINITION  peptidylprolyl isomerase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021657
VERSION     WP_176021657.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..163
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=17502
     Region          4..142
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 msliatfdtt qgpikvelfa dkapltvanf vnlvkrgfyd glifhrvipd fmiqggcpqg
       61 rgtggpgykf edekngvkhq vgslsmanag pntngsqffi thiktdwldg khtvfgqvle
      121 gqaivdsvkq gdvihsitle gdtdallaaq aervgewnkl fpa
//
LOCUS       WP_176021661             708 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021661
VERSION     WP_176021661.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..708
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76551
     Region          36..679
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mkpsllttai tfalilasqp vlaadtdsst aavkdldvvt vsaqldqarn alspdigssq
       61 yqitaediqk qplgasapls qvllqapgvv qdsyggvhvr gdhanlqyri ngvllpesis
      121 gfgqtldart iksirlmdga lpaqfgerta avvdittrsg aelgnggsag ittgsygkvn
      181 pnaswwgnqg rwswfltgny dqnevglenp tsarkplhdd thqgkafadl tylvndstrl
      241 svfagfannr fqipvnpgqt pqfgyldttt ydssqldetq rettrfgmlv lqgtlgqtay
      301 qlsagqrysd vaynpdivgd lvfsgvasqv qrsnrantlq adfstplgdn htlryglygn
      361 yehaaannss wvfpvdadgr qtsttpqlip drnafhasta alyvqdewri gddwtvnygl
      421 rgdrfkafgh tegqlsprlg vvwnasgstt vhagysryft ppaselvags dlalfdgtsn
      481 qqpaggsntp lsersdyydi gvsqqvgdhl tlgldaydrr vhrlqdegqf gaayiystfn
      541 yrrghihgle fsadysngpi sayfnaaynk amgtqvitsq ynldpdalay vqqnwihldh
      601 dqkltssggi syafsghnrv ganyvygsgl rsdnegvpng gelpsylqln lsaahdfnad
      661 sghplhvqla vlntldrsyq lrdgggigvf apqwgprrga ylslqqdf
//
LOCUS       WP_176021720             186 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: nucleoside deaminase [Stenotrophomonas].
ACCESSION   WP_176021720
VERSION     WP_176021720.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas
  ORGANISM  Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Stenotrophomonas"
                     /db_xref="taxon:40323"
     Protein         1..186
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=19977
     Region          27..178
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mlyaqvhltl pawihdqidl drrypgdeak valaielsrl nvdhasggpf gavvfgpddk
       61 viaagvnrvm phstslahae nmaymlaqqr lqtprlnavl spvtlatssq pccqcygatv
      121 wagidrllig ansadveelt pfdegplpad wvgelnkrgi evvqglnrda arsvlrayge
      181 sdgary
//
LOCUS       WP_176021744             837 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021744
VERSION     WP_176021744.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 837)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 837)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 837)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 837)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 837)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 837)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..837
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87989
     Region          1..837
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mnllrhawra lrrealagdl ltvfaalvlg vavmtavgtl vnrvnlalts saaemlggdl
       61 gvagrddppa afadeaqrrg lahtrlasfg svlfqgdasq masikaveag yplrgalrvr
      121 atpggaliad agmpakgqay adprllqalg lkagddlefg agtlriagii esepdaggdl
      181 ltlsptllvn radvegtgll gpgsrinyrl mftgpatdia afrqwllpqv kgmrllsvnd
      241 tqrgvrqafd lagrflglsa llavllagva talaanrfal rridqvailr clgarqrdvl
      301 fglalqllml avpacaigig lgmaaqeglv qvlgslvpqr lplpeampal tgagigllll
      361 fgfglppllr lrgvppmrvl nrsfaalppa sllayvaala aslvlavqvt gdlklalwvl
      421 gglaglavaa gvvgflllql lrglqhrlhg nwrlglaalt rrrmlavmql vglslslcal
      481 lllavigpgl lqqwrerlpa dtpnyflini qpeqrdsvla alhglgadda siepmatgrl
      541 iaingkpplr vdrtpaegnq aqgegqrddd denrplnfsw rstfppantl vngtfwtpds
      601 tapeasveig wakrygvhpg dritiavgeq erefavtsvr kadwntfrpn ffvllnpnav
      661 gdtphnllsa fhlpagqaag lgalvraqpn lslldvdavi sqvrdvmerv aqavqlvmvf
      721 sllagvlvll aalqatager rydsavlrtl gatrrqlrga vlvefgalga laallavgaa
      781 avigvavsqk vfelpllppw pglllggllg iglsllagww gtrrilhtpp alalrea
//
LOCUS       WP_176021755             168 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA thioesterase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021755
VERSION     WP_176021755.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..168
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18411
     Region          4..149
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mstelkshql smtvlmspem anfsgkvhgg ailrlldqva yacasryagr yvvtlsvdqv
       61 vfrqpiavge lvtflasvny tgtssmeigv kvvaedilkr svrhanscff tmvavdeegr
      121 ptpvpplqpa ssdekrrqaa alirrqlrqe meqrhlella snppspee
//
LOCUS       WP_176021779             250 aa            linear   BCT 11-JAN-2025
DEFINITION  NRDE family protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021779
VERSION     WP_176021779.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Bard,F., Casano,L., Mallabiabarrena,A., Wallace,E., Saito,K.,
            Kitayama,H., Guizzunti,G., Hu,Y., Wendler,F., Dasgupta,R.,
            Perrimon,N. and Malhotra,V.
  TITLE     Functional genomics reveals genes involved in protein secretion and
            Golgi organization
  JOURNAL   Nature 439 (7076), 604-607 (2006)
   PUBMED   16452979
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..250
                     /product="NRDE family protein"
                     /GO_process="GO:0007030 - Golgi organization [Evidence
                     IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=26705
     Region          1..250
                     /region_name="Tango2"
                     /note="Uncharacterized stress-responsive protein, TANGO2
                     (Transport and Golgi organisation 2) family, contains NRDE
                     motif [General function prediction only]; COG3332"
                     /db_xref="CDD:442561"
ORIGIN      
        1 mcllalgwlh hprwrlvmag nrdefharpt aalapwqdet sviggrdlrs gggwagvgag
       61 grmavvtnvr dpqasqtgps rgalvadylr grdpagthmq rlatvasaya pfnllladgn
      121 sleylgnhpa erqtlgpgvh gmsngaidap wpktrrlmda lsvwladgcn aldplwqala
      181 dehrpadsdl pdtgiglere rwlspafirg ddygtrastv llidanghga iherrfgpqg
      241 aalgqsqvdf
//
LOCUS       WP_176021846             275 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021846
VERSION     WP_176021846.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..275
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29851
     Region          19..259
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 msthsapeei pmqdddghdl airvrglvnh fgsqtvhegl dldvrrgeil gvvggsgtgk
       61 svlmrsilgl rvpnagqiev lgrdaradda esrlhiernt gvlfqdgalf ssltvgenvq
      121 vplkehhrel perwhyelal lkvklaglpa dainklpsql sggmrkragl aralaldppl
      181 lfldeptagl dpigaaafdr liktlqealg ltvflithdl dtlyaicdrv aviadrkvva
      241 naplpeierl dhpwiqeyfh gpraraarge qiesa
//
LOCUS       WP_176021907             309 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176021907
VERSION     WP_176021907.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..309
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33828
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..287
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,222,239,266)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     216..220,227..228,231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrltamtvf vevaergslt aaaevldmsr amvsrylaev egwlgarllh rttrrvsltg
       61 ageaalarfr qmlaigeelq gelasddpep hgtlritasv sfgqshlara vaafvqrhpa
      121 arielllvdr mvnlveervd lavriarqid psliarrlai crsvlcatpa ylqvrgtpta
      181 pehlvthncl thhyvgkslw qlhragrsls vavggnisan easllleavr anagiamlpt
      241 yqvapllrsg eliellpeys ldelgihavy asrrqqpaim rrfldflaec faspafqdld
      301 wrpsgkent
//
LOCUS       WP_176021908             212 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021908
VERSION     WP_176021908.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..212
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=22231
     Region          2..212
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 mkialvgatg nigrqiarha langhqltvi vrsaqdlpae lagahpvias lddqdalvaa
       61 itghdvlasa ygprpgddig rvgevaaqla daarkanvpr lvvvggagsl evapgvqlvd
      121 tpnfpeaykp yalahreafn rlqavddldw tffspaaeig pgeergqyrv qlkafladas
      181 ghsrisyady gaafvaelea rkypkqiita ay
//
LOCUS       WP_176021992             265 aa            linear   BCT 11-JAN-2025
DEFINITION  siderophore-interacting protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021992
VERSION     WP_176021992.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..265
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=29905
     Region          1..257
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mtehhnsrlr ldvrfreltv lrtetvtphm rrivlggddl agfdspgadd hiklffpnds
       61 gemvlpvlta egrsypdgkq pspardytpr wwdhetgela idfvlhdqgi agpwaeraqt
      121 gdtlliggpr gsfvvadsyd ayvligdeta lpaiarwldv lpegaevqay ievadederq
      181 dlpqyenvri hwlerngfpa asstlledml tdfeapdgda fywiatesrr armmrkfieg
      241 hlgvqrdwir stgywkahpd eqdgd
//
LOCUS       WP_176021981             141 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021981
VERSION     WP_176021981.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..141
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=15114
     Region          <72..134
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mlrlntalal nlvltllgat samamaadpq vstevfverg dnptfelqea pavvystapa
       61 tppdtflqip mvvllvaqld elghvsnvmv mrssglrefd raaftavdqw rfepvvvegv
      121 aqharvrvrl tfvptaeapp g
//
LOCUS       WP_176021995             236 aa            linear   BCT 11-JAN-2025
DEFINITION  YceI family protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176021995
VERSION     WP_176021995.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..236
                     /product="YceI family protein"
                     /calculated_mol_wt=23905
     Region          65..230
                     /region_name="YceI"
                     /note="Polyisoprenoid-binding periplasmic protein YceI
                     [General function prediction only]; COG2353"
                     /db_xref="CDD:441920"
ORIGIN      
        1 msatrklllp laltlaiaac skpadtaapa adaaapatte qaattpaada aaaapaaaai
       61 aiasgtykld pthtdvlaqw shfgfsnpsa hfgnaegtlv ydatdvtkst vevklplsgl
      121 nsftakfdeh lksadffdaa kfpaasfkst kvesagtnkl tvtgdltikd itkpvtldvt
      181 vngggehpma kvpaagfdat ttikrsdfgv gayapnvsde vkiritteat gekpaa
//
LOCUS       WP_176022061             123 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176022061
VERSION     WP_176022061.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..123
                     /product="VOC family protein"
                     /calculated_mol_wt=13242
     Region          1..117
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 mnpilhvevp vadldraiaf yrqwlqvdva apinvhdcrm aylpfndadv gasmalvhga
       61 dylpseqgar iylgvddldd slrralqaga vlcfgpavag dwrvaeirds egnrialqal
      121 vna
//
LOCUS       WP_176022063             366 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176022063
VERSION     WP_176022063.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..366
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=39357
     Region          129..365
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mpsflrhlls plslaglvti lvvgltlgvh tpgaglrwav lglflllfav hsqlpsregv
       61 rliagvmqav lavamvalep rtgtapillv vlvaqlaehw pprvvllial aanvalyavl
      121 kqaafpqplm ivllyggfqv faaltahyar stalardala rvnadllatr alladsarda
      181 erlrlarelh dvaghkltam rlnlralaad palagrdgll laeqlsgell tdirqvvqsm
      241 rddrgldldt alhalaapfp rprlqvqiae glrvtdpqla etvlrlvqea ltnaarhada
      301 gtvwltmtke nsrlridird dgqraerise gngivgmrer lavmqgelql artehggmhl
      361 iarlpa
//
LOCUS       WP_176022082             444 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatase PAP2/dual specificity phosphatase family protein
            [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176022082
VERSION     WP_176022082.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Pulido,R. and Lang,R.
  TITLE     Dual Specificity Phosphatases: From Molecular Mechanisms to
            Biological Function
  JOURNAL   Int J Mol Sci 20 (18), 4372 (2019)
   PUBMED   31489884
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Patterson,K.I., Brummer,T., O'Brien,P.M. and Daly,R.J.
  TITLE     Dual-specificity phosphatases: critical regulators with diverse
            cellular targets
  JOURNAL   Biochem J 418 (3), 475-489 (2009)
   PUBMED   19228121
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12932297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..444
                     /product="phosphatase PAP2/dual specificity phosphatase
                     family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=49012
     Region          34..205
                     /region_name="PAP2_Aur1_like"
                     /note="PAP2_like proteins, Aur1_like subfamily. Yeast
                     Aur1p or Ipc1p is necessary for the addition of inositol
                     phosphate to ceramide, an essential step in yeast
                     sphingolipid synthesis, and is the target of several
                     antifungal compounds such as aureobasidin; cd03386"
                     /db_xref="CDD:239481"
     Site            order(109,117,143..145,179,185,189)
                     /site_type="active"
                     /db_xref="CDD:239481"
     Region          306..434
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
ORIGIN      
        1 matlvatasp searpwrral lwlallgpff fasygfanwm agrhaelpvm afawearipf
       61 vpwtivpyws idlfyaisff lcrrrleldr halrllsaqv iavacfllwp lrfsferpdi
      121 ggvfgwlfdv llgfdkpfnq apslhivlli vlwvkfaqyl hgawrlvlhv walligisvl
      181 ttfqhhfidi ptgllagwlc vwlwpeqgtp plrawqatrd pkrwrlaaly algaglllvp
      241 vvmlrgtalw llwpvvslll vslayagldt aafqkrsdgr ltmaarwlla pylaaawins
      301 rlwtrrapqp vpvidavwlg rlpgaalpvp lvgvvdacae lscrapgaay asvpmldlva
      361 ptaaqlraaa daierlreqg pvlvccalgy srsaasvatw llrtgrarda aeavtivraa
      421 rpaivlhdvh lqviaaaaar etva
//
LOCUS       WP_176022126             253 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176022126
VERSION     WP_176022126.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..253
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26263
     Region          6..226
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 melssefwwf iliglgaqlv dgalgmafgl vsssvllsmg lppaqvsasv htaevfttga
       61 sgvshlvagn vdkrlffrla lpgalggalg ayvltqvpgd lirpliylyl lvlaiiilar
      121 aagrwmpkge irrvpvlgff aglldasggg gwgpvatstl larggqartt igtvnaaefv
      181 vtltisatfl lsmglqhlqi vaglliggmm aapvaallvk rvkerwvlva vgvlvlgisl
      241 fqvghalfgy lyr
//
LOCUS       WP_176022150             499 aa            linear   BCT 11-JAN-2025
DEFINITION  peptide MFS transporter [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176022150
VERSION     WP_176022150.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..499
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53971
     Region          19..499
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 msvnatantp epalpdfntt mghprplwml fmtefwerfa fygirwalvl yivaqfyngn
       61 aagegdasri ygaylalvya aaifggyvad rvlgyqrsil tgavimavgl fmislpqehi
      121 fklglatiiv gnglfkpnis tmvgklyglk derrdsgfti fymginigam iapvlteyla
      181 rkvfgtsemp sykvvfiasg vgmlislvwf yigraglkgi gappagaegf griimvlvgs
      241 lfaipvayfl latgatalaw ilgvmfaala vlllvegire gkvqrdrvia mliifafnvm
      301 fwmffeqags sftflaeniv nrqmgewtfp tawfqsvnsv aiitlapiia wiwvalgran
      361 psiprkfglg llfngaafal lmyalsqmvv dgkipfwtlf mvyviqsvge lclspiglsm
      421 vtklapvrlv gfgmggwfls tgignnlsgi fagvvsgegg mtvesalkgy tfgfwaligs
      481 gvilflvapl inklmhgvk
//
LOCUS       WP_176022152             464 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrolipoamide acetyltransferase family protein [Stenotrophomonas
            sp. NA06056].
ACCESSION   WP_176022152
VERSION     WP_176022152.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..464
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=47465
     Region          4..460
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 msqtknfnlp dlgeglpdat ivewfvkegd vikldeplvs metakavvev pspfsgtvlk
       61 lsgaagdiip tgavlasfal dpnlpqradg qdtghshgha apaapaaptp pplptaaapv
      121 aaeeakpaaa erddagtvvg amqssnavha eqalavggvk avpavratar klgvdlsrvr
      181 atgtdgavtm advkqaaadg sakigatpap vaaaayaapa paqvsapvqs eartplsaag
      241 kpmrtqppgv vakgqpeplk gvrrnmarvm adahskvvpt tlnddadiha wlpgndvtar
      301 lvrsivvaaq kvpamnawfd gealtrtlha qvdigiavdt ddglfvpalr nadmldargi
      361 regvnrlreq vearsiaase lsgytislsn fgmfagryat pvvvppcvai vgagrarhqm
      421 tpvmggveah kviplsvtfd hraatggeaa rflrammddl alas
//
LOCUS       WP_176022156             512 aa            linear   BCT 11-JAN-2025
DEFINITION  GGDEF domain-containing protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176022156
VERSION     WP_176022156.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 512)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 512)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 512)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..512
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55926
     Region          <159..376
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          282..510
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mtdqpdprpa pgtaigspar vravaddgrg drvvlqggsg valqqlfaga dapepllaaf
       61 angmatlpge lgdmgdrlqs aqasadwpry gramrqlidk yirtidqhsp dgqpdslrls
      121 eqlrlllgga mvallqhdpd lrdqaqalag rlrqwqpgaa lepieqgare lghqigvrae
      181 swqeqqalll elfalllenv sellddrswl qgqiaavrql lagpleaesv ertraelrev
      241 iykqgllrqg iddskaamrg lmgefiermd gmaastgeyh drigsyalql rearsiadln
      301 hllqevmqdt gkvqlqaaqa rdhlasarqe veraeqrinq leqdlraagd laridpltqa
      361 lnrrgldell qrelaraarn ssplglavid lddfhqtnde hghaggdall qhlvavcrll
      421 lratdgiarl ggdefvlvlp etpgadsmat vqrlqrslah rvltvqdrrv pvhfsaglsq
      481 wqpgddadtl lrraddalyv akregknrvh ag
//
LOCUS       WP_176022180             302 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176022180
VERSION     WP_176022180.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..302
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33297
     Region          24..176
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <178..297
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mdnalqelrr laanaenrrt etgiprvamv qgeipehala avyepminli lqgsksmtvg
       61 ektlhydpat yfimsvdlpa vgavhptptg epylavsltl dadiistllc dttdeasgrg
      121 vpssqteafn vaavtpelmd awvrmlrlme qrsdipalap vyereilyrv lqgphgcmlr
      181 qlatpdsala rissaiqrir hdfskplrva slarqvamse safhrhfkaa talsplqyqk
      241 qlrllrarqm lathgkgvtt tamevgyesp tqfsreyara fglppsqdma rmlasrrmql
      301 pe
//
LOCUS       WP_176022222             433 aa            linear   BCT 11-JAN-2025
DEFINITION  aminotransferase class V-fold PLP-dependent enzyme
            [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176022222
VERSION     WP_176022222.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 433)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424849
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..433
                     /product="aminotransferase class V-fold PLP-dependent
                     enzyme"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0031071 - cysteine desulfurase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006534 - cysteine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=47242
     Region          70..423
                     /region_name="CsdA"
                     /note="Selenocysteine lyase/Cysteine desulfurase [Amino
                     acid transport and metabolism]; COG0520"
                     /db_xref="CDD:440286"
ORIGIN      
        1 mdsrrrsllr agallpaaaa lsslpaagat ryagpmqipa ttvapdvlar degywatvas
       61 hfditdevnh lengywgamg retlasyqrh taevnrgnaw ygrrafpaqy mavhrqvadm
      121 lgvgadeial trgateamla liggynrlaa gdqvlyadid ydsminamrw lqqrrgvqve
      181 rialpvvpdr eqilqaydea farlprlkll lltqvshrhg lvlpvadiae rarargidvi
      241 vdaahgfgqi dyavpdlkad fvginlhkwi gapvgvgamy vrrgrvadld pymgetddgr
      301 vgsrvhtgtv nfaaylalpe aialhqriga askqarlryl rerwtvparq mahidvlssp
      361 dpalasalas frlrghasve enqalqkrll eehriftthr dgldsgacvr vtpsvftrpa
      421 qmdalvqala ala
//
LOCUS       WP_176022236             176 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [unclassified
            Stenotrophomonas].
ACCESSION   WP_176022236
VERSION     WP_176022236.1
KEYWORDS    RefSeq.
SOURCE      unclassified Stenotrophomonas
  ORGANISM  unclassified Stenotrophomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="unclassified Stenotrophomonas"
                     /db_xref="taxon:196198"
     Protein         1..176
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19659
     Region          3..162
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mtalrglfld hyeafrkrlr rrlgsddlal dalqetwlrv ermgnivpqr spvaylfrms
       61 inaasdqrqa harmltgtel dalmdetadh ldpatvtfgq vemaqlelal relperqrai
      121 lvaarieqlp ietialqhgv sarmigkelk kalqhcagrl drplvqrfgp gagkps
//
LOCUS       WP_176022250             231 aa            linear   BCT 11-JAN-2025
DEFINITION  ComF family protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176022250
VERSION     WP_176022250.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..231
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=25523
     Region          9..231
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mhlplpsalg ellqaafrll lplrclvcse pghdtldlcp acladlpwag raclrcalpl
       61 pdaalpicgt crdeppaqta thasllylpp vdqllvrykf hqdlsagrll aqlmlrnppp
      121 wtcaplvpvp lhrkrlrqrg ydqaaelcrl lqlptwrgly rrrhtapqse rsaeqrrdnl
      181 fdafdvrgav parltivddv mttgstvlei aetlrlvgag evrawvcarv p
//
LOCUS       WP_176022255             187 aa            linear   BCT 11-JAN-2025
DEFINITION  fasciclin domain-containing protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176022255
VERSION     WP_176022255.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Clout,N.J., Tisi,D. and Hohenester,E.
  TITLE     Novel fold revealed by the structure of a FAS1 domain pair from the
            insect cell adhesion molecule fasciclin I
  JOURNAL   Structure 11 (2), 197-203 (2003)
   PUBMED   12575939
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..187
                     /product="fasciclin domain-containing protein"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=19285
     Region          13..186
                     /region_name="FAS1"
                     /note="Uncaracterized surface protein containing fasciclin
                     (FAS1) repeats [General function prediction only];
                     COG2335"
                     /db_xref="CDD:441906"
ORIGIN      
        1 mhallqrval taslavlcgt aslsfaadtv mvggaamyps ktivenalns kdhttlvaav
       61 kaaglvdtln gkgpftvfap tneafaklpa gtvdtlvkpe hkadltkilt yhvvagthts
      121 qqlmadarkh ggmvslktve gepltvklhd galwvvdakg gkaaisiadv rqsngvihvv
      181 dtvlmpk
//
LOCUS       WP_176022293             335 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176022293
VERSION     WP_176022293.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..335
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35745
     Region          260..>318
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mshvamiaaa rrwmpvalal alaacsgkee tpaaaargaa apvaaapaap avaakvqsmg
       61 teqlresasq alrenrmyap agdnaieyyl alrdktpdda svksaltdll pytliaaeqh
      121 lgredfaeaq rlvaliekvd asapalprlk eglskgvqva akrtedetek vkkdaedrtr
      181 qlaeqqrlte qrakeaeaak qiaaqqdvar rdserqeaer qatarrdaeq kqqqaaaqqa
      241 saarqaataa apslrpvstp aprypaealr sgtsgevlme itvgtdgsvt narvlratps
      301 rvfdrealna vkrwrfepvn apvttrrtlv fapgg
//
LOCUS       WP_176022312             301 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176022312
VERSION     WP_176022312.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..301
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31298
     Region          4..293
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mnpdvlivgg syagiaagli lararrpvti idaglprnrf ashshgvlgm dgisgaellk
       61 narqqlldyp tvrwltaeav qatagadgve vhtadgqvlt arklllatgi adqlpelpgm
      121 aerwgstvlh cpychgyevg ggsigllggh pmsagkaplf adwgnvtffs qglpisdeel
      181 aamqqrgvqi ettpvvgvhg eqptwlevel adgrriaqra lfvpagqama tplvqqlgca
      241 lvesplgvli evdmmkqtsv pnvhaagdat tvgnitlama egvragigvh halvaedslp
      301 r
//
LOCUS       WP_176022208             771 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176022208
VERSION     WP_176022208.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 771)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 771)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..771
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..771
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=83143
     Region          36..747
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mntpptllal aigtalvapl haaestdaah dtpttlnalq viatprgaav aptqvvgpnr
       61 yvinatdlda mvsgnnglsm lknvpgasyt atdglgldis atslfvrgfr mnemgitfeg
      121 vplndngfls ltgtsvvnvg vpdgigsitv spggapvsvl sssvnggsle yrlrdlqdtp
      181 slrikqgvgs nntlvttvsg qsgqlgesgp kllvdlqrvs adkyqgagtq kflrgdlkaq
      241 qdvawgdftv flsdskaavw gynnisfdmi rklgwkadsf ypdyawayyv aspgnadksc
      301 gaytcgelse lipydtgqvt rdrvasinhr fqitpalsgn vqlynansht qatltdptvp
      361 spngapfseq vqtphlnrlg gmfnlqfeag ahtittgfwq ekskaaakte wyqqpllgeg
      421 kplkatgpfd vygpafqtdn asswvtrsrq fylhdnyavt dtlvlgmgfk avdfsttggg
      481 igdaperpvy gtlrakssfl phvslywspt drtdafidla ntmngyrvaq rgnigytasa
      541 wtitdqqefd rvagtlrpek nwnltvgash rfdrltvtad vfyndirnrl lsaaigtqfa
      601 qintvrlmpk mhvigadlgi tadltehlqf yqgialarsy ydsdfvvgdt vypikgnaqp
      661 gypqlslvsd lsahfggwrf gatstsylrq pftyendirv ptfwqvnayt aytlgphspv
      721 pglelrldvs nlfnrnnigt atiagssfsg dyqtlqrsap rqvmfstsms f
//
LOCUS       WP_176022523             812 aa            linear   BCT 11-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176022523
VERSION     WP_176022523.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..812
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=89127
     Region          7..806
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 msalshrpla riacllalav tpwlqaapaa lerevntfig skddgntfpg asapfglvqv
       61 spigshysgw rydddkirgf ghsfisgagc weqggqvsvl pvtgsigpgg dfdtanpkqf
      121 dhkayasayt hdgeigqagy ykvrltsygg idaeatartr aaaerytfsq rqgdghvlvn
      181 vgqanerhsv igsvvdvvgd rvvegklvtk sfcgghqytt wfriefdrpf kahgtwgegg
      241 glpgarhsme geqkpngawl sfdlakgqsv tavsaishvd aegartnlra egmqggallg
      301 fermralsqq swreqlgrvr vqggtaddrt vfysavyhal lqpmtgndad gryrgyddgi
      361 hradgwtyye yfslwdtyra qnqwlaltrp dvardigrtl laideqggwl prwgyanfet
      421 nimtgdpvtp flvdlwrfga lkgresqawd alrrnafgtp plnsrmagrs gnptyldkgy
      481 vvydrafpsk gmdvdphhgg satleyalad calsqmadgl ghaqdaatlr ergrnwrkvw
      541 dpqvrdaetg fsgfprprte dgqwytpadg hysprshhgf hegtawqyqw laqqdvpglv
      601 eamdgreqag rrldaffamd alqadplnaa rkewvvgpys yynqfrynpn nepdlhspwl
      661 ytligqpwkt aavvraaqql ftnapngltg nddlgtmsaw ylfsaiglyp avpgsgefll
      721 htprfakvev elgngrtlri eapgadgrrl qyvqgvqvdg kahapvwlgw nqlqqgpklr
      781 faldgtaptq gwgtavkdlp vswcaapgsq lh
//
LOCUS       WP_176022487             329 aa            linear   BCT 11-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176022487
VERSION     WP_176022487.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..329
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=34121
     Site            order(46..47,49,87,90..91,94..95,97..98,159,162..163,
                     166..167,170)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          72..191
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
     Region          85..153
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          158..185
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mvtlwlpmva avaaallaaa vlwplrqqgr rgfvlgvval gvagaclyll vgnpraaqvq
       61 aapsvatlrd gvealqqalq rdpqradgwv llgrsqaelg naaaaaeafs raaalapdep
      121 gvlveaaqar aqadpgkqfd dtalawlqra rtlspdaera swllgialrq rgrnaeaadl
      181 wstllprlep gaaqalqaqi aiareaagqp sdtsatapal lqvrvqlpas lktgnwpast
      241 qvfvlaravg gppmpvaark lplagfpatv glgdgdspmp taplsahrev evlarisrsg
      301 sanrseddlq tvpvkvtlph dgvvelrfp
//
LOCUS       WP_176022442             185 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176022442
VERSION     WP_176022442.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..185
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=19311
     Region          107..184
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mmllipavap kaatekernv mvtivdappp pppppppppp qdtppppvkn lsppkpspvp
       61 pppqapvvdv peprandivt ppsppsppap ptsieasvdi sskamnppry ppaafragiq
      121 geviliidvd aqgnvtnvtv ekssrnrdld raameaarkw rfnaaeaggk kaagrvrvpv
      181 nfaln
//
LOCUS       WP_176022436             256 aa            linear   BCT 11-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176022436
VERSION     WP_176022436.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..256
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=27391
     Region          24..195
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mntnaplpag dvpadrndrt rilrafnasl atvlvlvavf alqdhfdwrp wavapleakg
       61 llgligapll hasvehiaan saaililgtl agsvypkatl ralpllwvgs gigawmlgnp
      121 gsfhlgasgv thglmfllas lgllrrdraa iatgligmlf yggmlmtvlp hadgvswqsh
      181 mggafagiia allfrnadpl pprpryswed eeedveplad deleppspqr vpvlwqpreg
      241 qdyvvipfrr pddprg
//
LOCUS       WP_176022386             551 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176022386
VERSION     WP_176022386.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..551
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59030
     Region          17..535
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(30..31,34..35,38,76,134..135,137..139,142,162,
                     165..166,169,254,257..258,261..263,266,294,298,465..466,
                     470,474,490,493..494,497..498,501)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msttpapaka qltqghkkvi fasslgtvfe wydfflygsl aaiiakqffs gvnettgmif
       61 allafaagff vrpfgaaffg slgdrigrky tflvtilimg istflvgvlp nyasigfaap
      121 viliilrlaq glamggeygg aatyvaehap ddkrglytsf iqctatlglf mslliilacr
      181 yflgneafea wgwripflvs illlgvsvwi rlqlsesplf qqmksegkgs ktpfrdslkg
      241 gnlklmllvl lgaaagqavv wyggqfyalf flssmlkvda ttsylliaaa lalgvpffif
      301 fgwlsdrigr kkiilagcll aavtyipifk glthfanpai eearssspal vvadpntcsf
      361 qfdpvglrkf tsscdvataa ltkagvpydv qpaaagslam vnvgsasvts yeaagltkee
      421 gkakadafga elkgalttag ypakadgsri nyagtifmlw llvlyvtmvy gpiaaylvel
      481 fptrirytsm slpyhigngw fggflpaisf alvagtgnly yglwypiiia lmsvvigglf
      541 lretkdvdit k
//
LOCUS       WP_176022565             294 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Stenotrophomonas sp.
            NA06056].
ACCESSION   WP_176022565
VERSION     WP_176022565.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..294
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31685
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdlnavrmlv qvaearsftv aagqlglsqs glsraigrle aslgvkllqr ntrnvaltpd
       61 gqqfveqvgp llcgmedaer lladrpctps gvlkisapsm fgrkvlvpll gpllqrhpql
      121 qveavlsdrl vdlveegfda alrtgtiadq rmvarplkpl rwvtvaspay laaqgepadv
      181 aalqdhacla vrnlrsgrqv dwqflqdgql reitpptrmv fdsgdplvea aiagigivqv
      241 mdfavadala dgrlqrvlqp yegrsralsl iyppsrqhsp klqvlaeall agdw
//
LOCUS       WP_176022575             265 aa            linear   BCT 11-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein
            [Stenotrophomonas sp. NA06056].
ACCESSION   WP_176022575
VERSION     WP_176022575.1
KEYWORDS    RefSeq.
SOURCE      Stenotrophomonas sp. NA06056
  ORGANISM  Stenotrophomonas sp. NA06056
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Lysobacterales; Lysobacteraceae; Stenotrophomonas.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Stenotrophomonas sp. NA06056"
                     /db_xref="taxon:2742129"
     Protein         1..265
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=27969
     Region          12..265
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mpsmtasrsp vssitidats lqilqqqhae lrrppasltk lmtaytaydl laqaggswsd
       61 tiaidardvh evaddetrmg lvpgerialg klleglmvvs gndaalalar hlagsqaafa
      121 qhmnshaqal dlhdthfisv sgittpghls tardmamlaa hllvrypdll aitaqrsfah
      181 rtlhkanqna llgeegvdgl ktgytqaagf claatarrsc agharplrli nvvlgadsra
      241 srddqvraql dagfaiaava eaqrv
//
LOCUS       WP_176022701             230 aa            linear   BCT 11-JAN-2025
DEFINITION  outer membrane protein [Brucella pseudintermedia].
ACCESSION   WP_176022701
VERSION     WP_176022701.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Lambert,M.A. and Smith,S.G.
  TITLE     The PagN protein mediates invasion via interaction with
            proteoglycan
  JOURNAL   FEMS Microbiol Lett 297 (2), 209-216 (2009)
   PUBMED   19552707
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Pulkkinen,W.S. and Miller,S.I.
  TITLE     A Salmonella typhimurium virulence protein is similar to a Yersinia
            enterocolitica invasion protein and a bacteriophage lambda outer
            membrane protein
  JOURNAL   J Bacteriol 173 (1), 86-93 (1991)
   PUBMED   1846140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007631
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..230
                     /product="outer membrane protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24683
     Region          73..230
                     /region_name="LomR"
                     /note="Opacity protein LomR and related surface antigens
                     [Cell wall/membrane/envelope biogenesis]; COG3637"
                     /db_xref="CDD:442854"
ORIGIN      
        1 mnlkvilgas liaiaanssa faadaimsqe pvpfaapmfs wggayiggei gwgwgrdkld
       61 gdggsyaefk pngflggiya gynfdlgnsv ilgidanfdy ndlkesqdyw sddtlpvrts
      121 lesklewsga vraragyaid rfmpyiaggv afgqvknsit igdgssysds qtltgwtaga
      181 gidyaatdni tlrleyrytd fgnkdfdfgd vstrgsyktn dirlgiaykf
//
LOCUS       WP_176022713             157 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Brucella pseudintermedia].
ACCESSION   WP_176022713
VERSION     WP_176022713.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..157
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17707
     Region          18..153
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 maekllvsrw deidnltpra lyamlklrvd vfvveqkcpy peidgkdfea fhlrildgee
       61 laaslrvlpp eqdgkpvkig rvvvapdyrg yklgqrlmse aiefaqarfp vtaielggqs
      121 hlqkfygsfg feaisdeyle dgiphvdmrl epretia
//
LOCUS       WP_176022871             470 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Brucella pseudintermedia].
ACCESSION   WP_176022871
VERSION     WP_176022871.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..470
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50520
     Region          1..470
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mldtalierf saivgeknal tapedlaayl ieqrdlyhgr tplvlrpgst eevaaimkla
       61 tetktpvvpq ggntglvggq qpdesgtaii lslgrmnrir nldavgnlvt leagvilknl
      121 qdavekagrl fplslgaegs cqiggnlgsn aggtavlayg nmrelclgle vvlptgeiln
      181 dlryvkkdnt gydlkdlfvg segtlgvita avlkifpqpk gkgvayaglr npedvlrlfq
      241 latehagpsl tgfelmprvg veftvrhvdg vrdplesphd wyvlidisss rseedarttl
      301 etilteafen diiqdaaige svaqaqsfwk mreemswaqk peggsikhdi svpvasipaf
      361 iqeanaatle mipgarvvcf ghigdgnlhy nvsqpvgadk eaflarwhel nhrihtivas
      421 yggsisaehg igqlkreela ffkqdvaldl mrriksafdp agimnpgkvl
//
LOCUS       WP_176022960             290 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome c1 [Brucella pseudintermedia].
ACCESSION   WP_176022960
VERSION     WP_176022960.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10490041
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..290
                     /product="cytochrome c1"
                     /EC_number="7.1.1.8"
                     /GO_function="GO:0008121 - ubiquinol-cytochrome-c
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31505
     Region          50..288
                     /region_name="Cytochrom_C1"
                     /note="Cytochrome C1 family; pfam02167"
                     /db_xref="CDD:426633"
ORIGIN      
        1 mkkilknfaa fgvaplvalg ialggasaae ggnaaepehf pihhpkqekw sfsgpfgtyd
       61 kgqlqrglkv ykevcaachs mnlvafrtle glgyspeqvk alaaeyeved gpnadgemft
      121 rkalptdhfp spypnaaaaa aanngaappd fsliakarav ergfpqfifd vftqyneagp
      181 dyihslltgf deqppagmqi aegthynpyf iagkslamak plsdeqvtyd dgspetvdqy
      241 ardvsaflmw aaephleerk rtgfrvmifl ilfaglvyva krsiwsdvkh
//
LOCUS       WP_176022990             251 aa            linear   BCT 11-JAN-2025
DEFINITION  SIMPL domain-containing protein [Brucella pseudintermedia].
ACCESSION   WP_176022990
VERSION     WP_176022990.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Vig,E., Green,M., Liu,Y., Yu,K.Y., Kwon,H.J., Tian,J., Goebl,M.G.
            and Harrington,M.A.
  TITLE     SIMPL is a tumor necrosis factor-specific regulator of nuclear
            factor-kappaB activity
  JOURNAL   J Biol Chem 276 (11), 7859-7866 (2001)
   PUBMED   11096118
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006821
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..251
                     /product="SIMPL domain-containing protein"
                     /calculated_mol_wt=26412
     Region          15..250
                     /region_name="YggE"
                     /note="Uncharacterized conserved protein YggE, contains
                     kinase-interacting SIMPL domain [Function unknown];
                     COG2968"
                     /db_xref="CDD:442208"
ORIGIN      
        1 mnnrattlla tsfsaimlag altlpalaqe nqmtkqpari avtgegtmta spdmailnls
       61 vlreaktare amtanneama kvleamkkag iedrdlqtgg iniqpryvyp ddknglkeps
      121 itgytvsnsl tvrvrdlakv gnvldesvtl gvnqggdlsf vndnpsatin earkravada
      181 iakaktlada agvgigrvie ineqsrppmp mpiaraqfkt masaapedav pvaagensyn
      241 vsvnvvfeik e
//
LOCUS       WP_176023026             240 aa            linear   BCT 11-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Brucella pseudintermedia].
ACCESSION   WP_176023026
VERSION     WP_176023026.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 240)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 240)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 240)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..240
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26012
     Region          18..240
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mnqtfrpgra saradiidgv rrglplvvag apfgllfgal avdnglslae avfmsaviya
       61 gasqmvgldl fgqsiapwmi vmsifavnfr hvlysastgr rirhfklwqk alaffvlvdi
      121 qyaeveqrae agkpvtfvwy malgltfylt wvlealiggl fgnlitdpya fgidfllpiy
      181 flgmvmsfrh rqnwlpvviv saisavaayk lvgspwhvtl galggvvlaa viakpregea
//
LOCUS       WP_176023059             370 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella pseudintermedia].
ACCESSION   WP_176023059
VERSION     WP_176023059.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13388447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..370
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40253
     Region          12..>279
                     /region_name="NatB"
                     /note="ABC-type Na+ efflux pump, permease component NatB
                     [Energy production and conversion, Inorganic ion transport
                     and metabolism]; COG1668"
                     /db_xref="CDD:441274"
     Region          174..370
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 mrisnivqlg vkelrglard pmllilivya ftlaiytask ampealnnaa iaivdedqsp
       61 issrittafy ppyfvpprli ssyemdarmd egldtfalni ppnfqrdlla grsptiqlnv
      121 datrmsqaft gggyvqsivs sevseflnry rgsaqtpvel nlrarfnqdl nkgwfgainn
      181 vissvtmlsi iltgaalire rehgtiehll vmpvtpveim vskiwsmglv vliasafali
      241 vvvqgllavp iygsvtlflv gaalqlfatt slgiflataa gsmpqfgmll mlvllplqvl
      301 sggttpresm peiiqtimla apnthfvila qsilfrgagl svvwpqflal ivigsvlfyf
      361 alqrfraflr
//
LOCUS       WP_176023045             625 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-binding protein [Brucella pseudintermedia].
ACCESSION   WP_176023045
VERSION     WP_176023045.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 625)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 625)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418077
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..625
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=68520
     Region          116..535
                     /region_name="HerA"
                     /note="Archaeal DNA helicase HerA or a related bacterial
                     ATPase, contains HAS-barrel and ATPase domains
                     [Replication, recombination and repair]; COG0433"
                     /db_xref="CDD:440202"
ORIGIN      
        1 mseigsnsep reqgayvqrn rtegyviqcd gegaivsals gpssaasddy wavgqlisir
       61 agdnrvvgli rnvlvpgdvw irggdntlhv hveflgevrv qpngqttfng gisqfphpga
      121 iahriratdl aaiyaqtgqs svsigtltqd atvpahisvd dlisrhfaiv gttgvgkssa
      181 vmlllrriva qkpnlrvlil dphnefasaf pdlavavdqt nielpfwmlr ldefadvifr
      241 grapdpmeld mlrdlvqlar ekmqgaetss aktlrrqlad rqsvsadtpv ayrlpdlial
      301 idqrmgllds kaerpylrsl karlesisad prfrfmfavt ggpetmrqai grifripqng
      361 rpictfqlag lpsevvnava svlcrlafdi alssegslqt lviceeahry ipadrdagfw
      421 ptrqaiaria kegrkygsyl gvisqrpgel dptilsqcns ifamrlgner dqeiikgair
      481 ggaqsmagfl ssianreaia fgeafstpmr ltfetvpshq lpgrsksesa lsgwrsdgkv
      541 sldqiveklr afesssqtep adrfpdedsl wgnpvstthr dhasiddefh rpsplkpqtp
      601 lsldtkqsie kmgelvrsfr kdrer
//
LOCUS       WP_176023063             257 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella pseudintermedia].
ACCESSION   WP_176023063
VERSION     WP_176023063.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..257
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27086
     Region          3..246
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtllsvknls valggkaals dasfdihgge figligpnga gkttllrail glvasggeil
       61 ldgddlhrvt astkaqklay lpqerdvawp vsvemlvslg rsalkpivas mnaqdealvd
      121 aamqrmdvaq frdrsamels ggerarvlia rvlaqdtpvi ladepvagld pshqlglmes
      181 faalakegkt vvaslhelsl aaqhctrlil lhngrvvadg vptkvltpql lhdvygirak
      241 imtvddefiv hpisrvg
//
LOCUS       WP_176023074             220 aa            linear   BCT 11-JAN-2025
DEFINITION  DedA family protein [Brucella pseudintermedia].
ACCESSION   WP_176023074
VERSION     WP_176023074.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..220
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=24045
     Region          17..174
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mesiigdlgq fisdhrawag pivgiiafge slaiigmfip atpimiaigg lvgagiiepi
       61 pviigaiiga vigdiisyfl gwwlgrniih kwplnkhrsg vararllfrr ygfsavflgr
      121 ffgpirctvp mvagmmsmdq trfqtanvls alvwapvmfl pgwlagrgag lfarmdgdhm
      181 fwfavgitiv tiivtvigvr ffkarprrer krrvqvtpae
//
LOCUS       WP_176023133             408 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Brucella
            pseudintermedia].
ACCESSION   WP_176023133
VERSION     WP_176023133.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..408
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45328
     Region          72..388
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 msefliaypw aetlaalggl flsafianfl ikaillklld rvvqktsfgq deelkrhgvi
       61 srlanivpal iissgilavp glpegaitvi rnvaiafiil tlalainsvf glidtlyhrr
      121 pearyrpmkg yiqvaklavy ivatvliiat lldkspvill sgvgamaavl ilvfqdtlls
      181 lvasmqiass nmvrvgdwie mknldangdv teialytvkv qnfdktitti pirklitepm
      241 knyrgmqesg grrikralyi dqntirflsn eeqtklasvd wladylpkka keiaewnqkl
      301 gdrannpvnr rqftnigtfr ayvdnylrnh sgvhkgmtll vrqmdptpeg lpleiycfan
      361 ttvwasfeqi qsdifdhlya vlpefglraf qkpsgndfrk ltvsalsg
//
LOCUS       WP_176023073             170 aa            linear   BCT 11-JAN-2025
DEFINITION  EF-hand domain-containing protein [Brucella pseudintermedia].
ACCESSION   WP_176023073
VERSION     WP_176023073.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Persechini,A., Moncrief,N.D. and Kretsinger,R.H.
  TITLE     The EF-hand family of calcium-modulated proteins
  JOURNAL   Trends Neurosci 12 (11), 462-467 (1989)
   PUBMED   2479149
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11473824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..170
                     /product="EF-hand domain-containing protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18586
     Region          50..139
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
ORIGIN      
        1 mksktafiav iatsllavpa laqennsant dktatetpvt psrdmkfrqg pvdlekfsrl
       61 ddlkaadsdg dgvlsraeie alaqkrivsr aadrmerrld ingdgkvtla eienqrkkef
      121 aaldrnedgk idrsemraak mhhargshkg phhtghhkgp mkgqaekpqe
//
LOCUS       WP_176023138             463 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Brucella pseudintermedia].
ACCESSION   WP_176023138
VERSION     WP_176023138.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..463
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49654
     Region          17..452
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mvppreielt keitggfaal gvtgillkgv eaagmtepkp iqlqaiphql egrdilgiaq
       61 tgsgktaafs lpilqkiigl gdkrrpknar alilaptrel avqieqtirn vskhahista
      121 lvlggvskls qikriapgid vliatpgrlt dlmreglvdl sqtrwlvlde adrmldmgfi
      181 ndvkriakat htdrqtalfs atmpkeiaal agsllrdpvr vevapqgtta aeitqvvhpv
      241 htkekrrlls allgdkamrs vivftrtkhg adavvrhler dgyevaaihg nksqnarqra
      301 lngfrdgslr iliatdiaar gidvpgishv vnydlpdepe tyvhrigrtg rngasgasit
      361 lydpaaeesk lravervtrs klpikdapve lapapapraa apgerpqkth rkgatppkpr
      421 raapkagdhr gaahatadaa pkakrpfrrk rrnangnggq raa
//
LOCUS       WP_176023135             281 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Brucella pseudintermedia].
ACCESSION   WP_176023135
VERSION     WP_176023135.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..281
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30944
     Region          157..275
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 msyktvvays rsepelkrvl savgllkqkl pdihviglys ipspivyadp ngfidpgmfe
       61 lhdkqhkels erlkhvfeee mrrqganyey ritrsetgta adgvltaclg aelliagqpd
      121 pddpatndet adtivfnssc pvllvpyapv lpmvsldriv vafngkreaa ratfdalplm
      181 khadkteivw vdppeieged ralashdiae sisrhgievt ptaiasngry aqdalrehii
      241 aqrsdllvmg ayshsrlrel vfggvtrsml nelpiltlfs r
//
LOCUS       WP_176023140             247 aa            linear   BCT 11-JAN-2025
DEFINITION  alanyl-tRNA editing protein [Brucella pseudintermedia].
ACCESSION   WP_176023140
VERSION     WP_176023140.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V.
  TITLE     Evolution of aminoacyl-tRNA synthetases--analysis of unique domain
            architectures and phylogenetic trees reveals a complex history of
            horizontal gene transfer events
  JOURNAL   Genome Res 9 (8), 689-710 (1999)
   PUBMED   10447505
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Cusack,S., Hartlein,M. and Leberman,R.
  TITLE     Sequence, structural and evolutionary relationships between class 2
            aminoacyl-tRNA synthetases
  JOURNAL   Nucleic Acids Res 19 (13), 3489-3498 (1991)
   PUBMED   1852601
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Schimmel,P.
  TITLE     Classes of aminoacyl-tRNA synthetases and the establishment of the
            genetic code
  JOURNAL   Trends Biochem Sci 16 (1), 1-3 (1991)
   PUBMED   2053131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..247
                     /product="alanyl-tRNA editing protein"
                     /GO_function="GO:0002161 - aminoacyl-tRNA editing activity
                     [Evidence IEA]"
                     /GO_function="GO:0002196 - Ser-tRNA(Ala) hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004813 - alanine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006419 - alanyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=26966
     Region          5..242
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
ORIGIN      
        1 mayetealfr edsylstaeg tvlaitesgg iildqtnfya tsggqpgdig fferadgtri
       61 eiaatvtgen kneiihvpae gqaspaigek lvlhvdwprr yklmrmhtac hllsvvcpfp
      121 itgaavgede srvdfdlpdp tytkefvtek lmervnanda vsirwisdee flanpdivks
      181 knvrppiglg rirlvligen gavdsqpcgg thvsgtqevg eihigkiekk gkenrrfrir
      241 fgalpes
//
LOCUS       WP_176023180             203 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Brucella
            pseudintermedia].
ACCESSION   WP_176023180
VERSION     WP_176023180.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..203
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22273
     Region          6..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maekgrprsf dretalraam fvfwekgfdg asladlttam ginapslyaa fkskeelyle
       61 alalyageig veiwssldet pnvrtaferf lfatidaycq etvprgcmit ldalhrthss
      121 dkvctvlrsr rqsnietlkk rlergvrdgd ippsvnceav atfyatvqng msilardggt
      181 rqdlaatamg amaaweklvf sea
//
LOCUS       WP_176023188             206 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Brucella
            pseudintermedia].
ACCESSION   WP_176023188
VERSION     WP_176023188.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..206
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23007
     Region          1..202
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mlkiwgrins tnvkkalwia reldlayeqi dvggqfgglk dpaylarnpn gliplledgd
       61 tvlwesntit rylaavygkg tlwiedpakr aqaekwmdwa stslasnfsd vikhlvrlpe
      121 aerdpavler glqglaqsmr iandglkgaa wfsgdhfgig dipigcyaya wfefpiarps
      181 lprledwyer lkqrpayqaa vmtplt
//
LOCUS       WP_176023225             305 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Brucella pseudintermedia].
ACCESSION   WP_176023225
VERSION     WP_176023225.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..305
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32836
     Region          4..293
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(28..29,32,87,100,102,132,166,253,256,292)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(224,229,244,253..255,258,280,284)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mggfasigec mielsgnegd qwrmgfagdt lntawymral teksypveyv tafgqdsfsq
       61 kqrvfltsng igiahspiid glhpglyait lngaersfty wrsdaaarrl asdrealeks
      121 lhgrdiiyfs gisvaiilpe hrdtffevlr qcraagsria fdpnfrhqlw pdrkmaqdii
      181 seamriadia lptfpdeqal fgdkdasaca drlaalgvke ivvkdgtepa llvaggervl
      241 vpsvaaqavd ttgagdsfng aylaarlngl spvdaarkah lvaarvveir galapmetar
      301 aafad
//
LOCUS       WP_176023257             205 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Brucella
            pseudintermedia].
ACCESSION   WP_176023257
VERSION     WP_176023257.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22170
     Region          3..169
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 markqnpstr snlldaalgv irtkgyaats vddicakasl skgaffhhfs skedlavaaa
       61 nywsettgal fadaayhape dplervlayv elrkqlvqge lpdftclvgt mtqevyetna
      121 pireacwasi sghantlvpd ieaamerypi agdftaesla lhtqaviqga fiiakasgdp
      181 qravesidhl kryisllfkq pantr
//
LOCUS       WP_176023271             340 aa            linear   BCT 11-JAN-2025
DEFINITION  AI-2E family transporter [Brucella pseudintermedia].
ACCESSION   WP_176023271
VERSION     WP_176023271.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..340
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37583
     Region          1..323
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mlkagnaali liagcvlial lyygsavfap vvfaffiiml vwpiqrslsl itsryvalai
       61 tfllvvflll gfgwliawtm gqvgrrilid avryqmlydq lrtwleghgi aasvlwsenf
      121 svswtlrtlq sigsrlnntf sfwivalvyv llglaeteef garirqlknq aaanaflras
      181 rsastkiryy mllralmsia tgsfvwlltr lmglpfaetw gfaafilnfi pflgplvatl
      241 fitafafthf aswqlvlavf iglnivqsvi gsvieprltg ktislspfat lfsvfawgal
      301 wgifgafigv pitivaltfc ahysatgwla eifgfprepl
//
LOCUS       WP_176023326             281 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella pseudintermedia].
ACCESSION   WP_176023326
VERSION     WP_176023326.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..281
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=30916
     Region          13..272
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 msaepslika eetrktaial kdvqisfkla dggrfdavae snlevtenef vaivgptgcg
       61 kstllnavag llvpasgtve isgqrlqgln rkagylfqqd almpwktvld nvaigleiag
      121 tpkaqareqa rewlgrvgla sfgdryphml sggqrkrvgl aqvlirnpky llmdepfgpl
      181 daqtrvimgd llldlwsqdk kavmfvthdl eeaialadrv vimsagprar imaeykiplv
      241 rpreiseirl ddkfheihre iwsalkeevl kgyqqtsgek k
//
LOCUS       WP_176023340             332 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella pseudintermedia].
ACCESSION   WP_176023340
VERSION     WP_176023340.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..332
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34990
     Region          25..329
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mnneqrryip drlgtpfsri faswemlllg vaiaifians faspyflnaw nlsdatfnft
       61 ekaliafamt lliisgeidl svaaiialas tamgaaaqag igtpglvmig igtglvcgai
      121 ngglvaglkl psivvtigtm slfrgisyiv lgdqafggyp esfayfgqgy vfwvisfefa
      181 lfvlfavlfg vllhwtsfgr rvyaignnef asrfsgipve ktkfvlflmt gvmsgiaavc
      241 ltsrlgstrp siaqgwelei vtmavlggvs ilggsgtivg vviaafvmgl vtfglgllnv
      301 pgivmsifig lllivtislp ilirqlkarr aa
//
LOCUS       WP_176023342             453 aa            linear   BCT 11-JAN-2025
DEFINITION  FGGY-family carbohydrate kinase [Brucella pseudintermedia].
ACCESSION   WP_176023342
VERSION     WP_176023342.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..453
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=48608
     Region          3..400
                     /region_name="ASKHA_NBD_FGGY_NaCK-like"
                     /note="nucleotide-binding domain (NBD) of Novosphingobium
                     aromaticivorans carbohydrate kinase and similar proteins;
                     cd07772"
                     /db_xref="CDD:466792"
ORIGIN      
        1 mkriaildig ktnakvvvld aasgeeiaas ripntvlrdg pyphydieal wrfflkslaa
       61 fakepgfdai sitthgasaa lvaedgklam pvldyeldyp peiraayaai kpdfedtfsp
      121 slslglnlga qlhflktmfp dhfarahrif typqywawrl tgiaatevts lgchtdlwlp
      181 kesafsalvd rldirekfpp lrsafdalgn vlpeiakeig lsrpvpvhcg ihdsnaslla
      241 hlmdrdgpfs vvstgtwvvs favggnfdgl dpqrdtlanv daygravpsa rymggrefdi
      301 mteglsvppa adlpgivarv lerqimalps avpgcgpyph sklrwinadt asdaqryvaa
      361 ciyaalmtet clhllgadgp vivegpfagn atyldalanf tgrdveavtg stgtalgagl
      421 lagatvpekh grifkpgdga yaayrkqwlr nta
//
LOCUS       WP_176023352             250 aa            linear   BCT 11-JAN-2025
DEFINITION  SURF1 family protein [Brucella pseudintermedia].
ACCESSION   WP_176023352
VERSION     WP_176023352.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Reeves,J.E. and Fried,M.
  TITLE     The surf-4 gene encodes a novel 30 kDa integral membrane protein
  JOURNAL   Mol Membr Biol 12 (2), 201-208 (1995)
   PUBMED   7540914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..250
                     /product="SURF1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0033617 - mitochondrial cytochrome c
                     oxidase assembly [Evidence IEA]"
                     /calculated_mol_wt=27749
     Region          13..230
                     /region_name="Shy1"
                     /note="Cytochrome oxidase assembly protein ShyY1
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3346"
                     /db_xref="CDD:442575"
ORIGIN      
        1 mmpspkneqa vqkttsrffl glisvlgavf flifmglgiw qverlqwkld liarvdarvh
       61 aepvaapgrd dwanvnqkdd eyrhvtltgt ylndkevlvh altergagyw vltpmrssdg
      121 altfinrgfv psdrrdpssr retqiagett vtgllrmpep ggfflrpndp arndwnsrdv
      181 aafaqkldlg qvapyfidad aksgtgtlpi ggltvvkfrn shlsyaitwf alaamvagaa
      241 iffwrhehks
//
LOCUS       WP_176023356             333 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella pseudintermedia].
ACCESSION   WP_176023356
VERSION     WP_176023356.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..333
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36321
     Region          1..332
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mgslllksvh krygaqevlk dinlevrdge fiifvgpsgc gkstllrsia gledvssgqv
       61 lingedvtvt ppskrgiamv fqsyalyphl tvkdnmglgl kqagtpkaei etrvskasam
      121 lsldpylgrr paemsggqrq rvaigralvr epelflfdep lsnldaalrv qtrleiaklh
      181 relkatmiyv thdqveamtl adrivvlnag rieqvgspme lynkpdnlfv agfigspqmn
      241 fvdgarigda gaktvgirpe hisvsresgk wkgkvihaeh lgadtilyve teaaglitvr
      301 lfgehhyned dvifitpddg kvhrfdangk air
//
LOCUS       WP_176023422             251 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Brucella
            pseudintermedia].
ACCESSION   WP_176023422
VERSION     WP_176023422.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..251
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26390
     Region          12..240
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; pfam01925"
                     /db_xref="CDD:460386"
ORIGIN      
        1 mtysfslilt iaitflgagf vkgvtgmglp tvamgilgal isplaaasll iipsfvtnlw
       61 qlmagpsfrg lmlrlwsmml aivvgtiagt avlvggniai ttsllgfslv iyaaytlfar
      121 qlqvpekler plspvtgflt gmiagatgif vipavpylss lglkkddlvq alglsftvst
      181 aalgiglssr qaysgdllli svlaivpala gmfigqffrs rirpesfrrw fliglmllgl
      241 emalrplfsl s
//
LOCUS       WP_176023435             218 aa            linear   BCT 11-JAN-2025
DEFINITION  PIG-L deacetylase family protein [Brucella pseudintermedia].
ACCESSION   WP_176023435
VERSION     WP_176023435.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..218
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24936
     Region          15..210
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 midlpsltnp grplrllclg ahsddieigc ggtllslies gmplhvewcv lsgneerrae
       61 aeasardflr gaerfnirla sfedsyfpaq srdikqwlie qrgrgqpdmv fthrhgdahq
      121 dhrtlneltw nlfrdqvile yeipkwdgdl gqpnaysalp aaimerkvel lmkhfgtqrs
      181 kdwfdaetfr glarlrgmec rapetyaeaf harklrlf
//
LOCUS       WP_176023456             415 aa            linear   BCT 11-JAN-2025
DEFINITION  polysaccharide biosynthesis/export family protein [Brucella
            pseudintermedia].
ACCESSION   WP_176023456
VERSION     WP_176023456.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..415
                     /product="polysaccharide biosynthesis/export family
                     protein"
                     /GO_function="GO:0015159 - polysaccharide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0015774 - polysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44765
     Region          18..>142
                     /region_name="Wza"
                     /note="Periplasmic protein Wza involved in polysaccharide
                     export, contains SLBB domain of the beta-grasp fold [Cell
                     wall/membrane/envelope biogenesis]; COG1596"
                     /db_xref="CDD:441204"
     Region          <155..>372
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
ORIGIN      
        1 mahrimknri aahlratmla glilaggsfa algegqayrv gandvlqvtv ygqpsltgly
       61 pvdvdgnigy pivgnipvng ltinevgeki agslsqhipg ltvtatinqy apvfvvgdvk
      121 vpgkyqfrpg mvalelmalg ggagkaetpa ltagmqlitv qqeyadlqmq itamtirrar
      181 feaelngtef tyslpeqsaa nketvaltqq mldgektvfn vrrnnlaaer kaleaqaasy
      241 gdeietlqqs iklhdteigl lqenvdssks lvdrglaaks nlrdmerdls atrraalela
      301 sflararqnq lamqqrianl deirrseaat alqdidlnia rmerrsnaql qtmaeiakss
      361 gniasstlrq klvfsisriv dgsfqdivan erteikpgdi lrveldmsrv ggsps
//
LOCUS       WP_176023469             292 aa            linear   BCT 11-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Brucella
            pseudintermedia].
ACCESSION   WP_176023469
VERSION     WP_176023469.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..292
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31286
     Region          8..283
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mmgpfrciad lrgqlmespv wddrrqtlfa cdieagriye idldrgplre wsfasavasl
       61 gltesgglvv alsrevilfd petgnretlw safeepatsr lndgkvgpdg afwvgsmdgr
      121 pereaisrly rvtgngdasv kaegfrisng lawtadgktm fhtdsrgpwi drydfdpetg
      181 gvsgrkrird ldeqagrpdg gacdaegayw sagvsagvln rfdrdgnlle klpvpvpapt
      241 mpcfcgpdlt llaitshrqv peaalvaapl sggvflagts vagaavhrmr gv
//
LOCUS       WP_176023525             303 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Brucella
            pseudintermedia].
ACCESSION   WP_176023525
VERSION     WP_176023525.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..303
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=32103
     Region          10..294
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mdlagyrrvl rgisgvhata ydargeidag ltggivgria qagvhnivtg gntgefyslt
       61 edevirlqai aiaavdgkaa vtaaagrsvr eairvasaag kagadgvmih hpldpfaaph
      121 aqvdyfiaia eaidlpivay irsdliplde mvrlathpkv agvkfasqnt mlffeccrat
      181 kgteatwicg laeswalpfy alggrgftsg lvnvapkrsl avwnaleagd fararavves
      241 iadfetmrtk yrnganvtvv kealqiqgfe vgkvrlpglp qletndretl rkivsgwetd
      301 giv
//
LOCUS       WP_176023531             523 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Brucella pseudintermedia].
ACCESSION   WP_176023531
VERSION     WP_176023531.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..523
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=57156
     Region          27..521
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 maapydlkdd kvvviigsga gggtlgnela qkgidvvile agkrhefedf indewdsfaq
       61 lawlgkrtts gswrvshdfp nlpawivkav ggttthwaga slrfqdyefq tlthygkieg
      121 anlldwpitl aelepyyaka edkmgvtrtn gieglpgnnn fkvlkagadk lgykechtgr
      181 mainsaprdd rmgcqqtgfc fqgckwgakw stlyteipkg eetgklevrp ectalkiehn
      241 aagkvtgvly adkdgkqhfq karvvcvagn siesprllln sasskfpdgl anssgqvgrn
      301 ymrhttgsvy asfekpvhmy rgttmagiir deaahnpkrg fvggyemeti slglpfmaaf
      361 lnpggwgrgf tsalddyvnm aglwivgedm pqeknritls kdvkdehglp vpdvyyddhp
      421 ndiamrnhay aqgkalyeav gairtfptpp ypsthnlgtn rmsakpqdgv vnkhgqthdi
      481 knlfvsdgsq fttggaenpt ltivalairq adyiaeqmkk rai
//
LOCUS       WP_176023581             344 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Brucella pseudintermedia].
ACCESSION   WP_176023581
VERSION     WP_176023581.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10524380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..344
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=38160
     Region          173..340
                     /region_name="MTS"
                     /note="Methyltransferase small domain; pfam05175"
                     /db_xref="CDD:428349"
     Site            order(207..213,232..233,256..258,276)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
ORIGIN      
        1 mitpaqqtlf lpfdqgildm peegqsflac glsadrrled ewkqaliflq pwrpdwlale
       61 kegfkaiprl apkldeerrf aggllllgkh rgrneawfae llervepggw iavsgdkklg
      121 vdsfrkwvgn iaeisdrmsk nhavvfwlrr padltgdfia alkplaanid dvfrtepgmf
      181 shgvidkgsa llvphmekiv fgnvadlgag wgylaaqclk fadrikaidl yeadfealea
      241 argnlerlaa svpisfnwfd vtsekltgiy dtvvmnppfh egrvtdvslg qafiaaaasr
      301 lktggrllmv anrqlpyett lkglfknvtl leeangfkif dakk
//
LOCUS       WP_176023558             365 aa            linear   BCT 11-JAN-2025
DEFINITION  microcin C ABC transporter permease YejB [Brucella
            pseudintermedia].
ACCESSION   WP_176023558
VERSION     WP_176023558.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 365)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..365
                     /product="microcin C ABC transporter permease YejB"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042884 - microcin transport [Evidence
                     IEA]"
                     /calculated_mol_wt=40547
     Region          1..365
                     /region_name="YejB"
                     /note="ABC-type microcin C transport system, permease
                     component YejB [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4174"
                     /db_xref="CDD:443333"
ORIGIN      
        1 mgayilrrll lmiptifgim aisfavvqfa pggpvervia qlsgqggdal drlsgggsdf
       61 gqsavdsgsv nskyrgaqgl dpqfiadlek qfgfdkpple rfgqmlwnyl rfdfgrsyfr
      121 disvidlike kmpvsislgl wltflsymis iplgirkaik dgsrfdtwts aviivgyaip
      181 sflfailliv lfaggsffdw fplrgltspe faqmsfwgki gdylwhmvlp vtalvlsafa
      241 tttlltknsf leeirkqyvt tarakglten qvlyrhvfrn amliviagfp gafisafftg
      301 sllietifsl dglgllgyqs vinrdypvvf anlyifslig llvgllsdlt ytwidpridf
      361 errdv
//
LOCUS       WP_176023607             291 aa            linear   BCT 11-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Brucella
            pseudintermedia].
ACCESSION   WP_176023607
VERSION     WP_176023607.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..291
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31703
     Region          8..284
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mtvvkttlfa dhvaelgegp gydplsgnvw wfdilgqkli eknwdsgeth vhalgmkasa
       61 lavidrdrql ivsehglfir erangrltlh hpleadneit rsndarvhps gsfwigtmgk
      121 kaepdagsiw wyregqvkkl fsgititnsi cfspdgkiay fadtdrniiw rvdtdpetgl
      181 pvsdksvfhh rteeggvdgs vvdaegtlwn acwggrslna yspqgrlirs valpvgqpsc
      241 pafvgpdata mivtsahegl ndearrsdph agkvllldlt vagrhdppvr l
//
LOCUS       WP_176023614             206 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Brucella
            pseudintermedia].
ACCESSION   WP_176023614
VERSION     WP_176023614.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22638
     Region          6..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvprgrprsf drdaaldkvm kvfwakgyec aqindfttai gitppsfyaa fgnkeqafre
       61 avdyyrrtig avpfdalena ptiheglrqw lektadsafa cpaggcmisv ssiqckpena
      121 pvkeflqair hanherfskr lrsavatgel padtdiaqmt efyhmiqqsi sfeardgnsr
      181 aavqkiidma mlampacatg kpdpvs
//
LOCUS       WP_176023666             370 aa            linear   BCT 11-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Brucella
            pseudintermedia].
ACCESSION   WP_176023666
VERSION     WP_176023666.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..370
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=39219
     Region          29..263
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mmskslkiwf avvglsaaal asaeanpsia vdvatgkvya qqeafqrwyp asltkmmtay
       61 vafralqsgq mtlespvrmt vnaakeppsk mgykpgsvmt ldtalkimlv ksandvavav
      121 aeavggtesa fvqrmnaeaq rigmvgshfa npnglhdpnn yttardlavl avqlrrefpq
      181 yahyfateai dpgagkkvqa nynillgryd gadgmktgfv casgfnlass atrngrtvla
      241 ivlgadrqea ravqaaqlms dafrasaggg vtlatlrpta ganlnqatdm rkaicsqeam
      301 adrwdgrdve gklkinspyi hamdrdpvpv rvglvsepgp itrasqldis qipvpmprpq
      361 raagvttavn
//
LOCUS       WP_176023790             471 aa            linear   BCT 11-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Brucella
            pseudintermedia].
ACCESSION   WP_176023790
VERSION     WP_176023790.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009012
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..471
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=51804
     Region          40..456
                     /region_name="ArgD"
                     /note="Acetylornithine/succinyldiaminopimelate/putrescine
                     aminotransferase [Amino acid transport and metabolism];
                     COG4992"
                     /db_xref="CDD:444016"
ORIGIN      
        1 mtrtnatpkp klltvgeaka ldlprmtelf tahlnpgqlh fmkllgfhrv kieradgmyy
       61 ydqngrpild ffggfgslaf ghnhprilea rrqfqeemrh eiaiafmsqy atalaydiaa
      121 cspgdldmvf lgssgseame aaikvaeraa gaskpkivya ensfhgktkg vlsitdggly
      181 rgefklvdnt vrvpfgdiea ienafradpe igvivletvq ggggiiqada efwqklrglc
      241 dqygviwvad evqcglgrtg kfyafehygv ipdvtalaks lgggktamaa miarrdiymk
      301 aygtpktami hamatfggig eacvtsieal nvlydehlid naaevgdyll erlrevqsry
      361 palvkdvrgk gmmvglefhd fsqtmpavlr pvlamldekl kgslpgfigs hllrdhgvlv
      421 afteynrnvi rlepplicer qhvdafikal devlsrgivr ivrdfvkaqi k
//
LOCUS       WP_176023795             132 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Brucella pseudintermedia].
ACCESSION   WP_176023795
VERSION     WP_176023795.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..132
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14288
     Region          13..128
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mprfiadild srvslllari vltfvfwssg laklfdfgan vaemesfgly pgwlfnsatl
       61 llqiggslmi ifsrgtwlac galavftilt ipvahpfwtk egeeafrdmt valehislig
      121 glaiaailar kv
//
LOCUS       WP_176023875             242 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Brucella pseudintermedia].
ACCESSION   WP_176023875
VERSION     WP_176023875.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..242
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25903
     Region          6..239
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 maqdlngkvg avtgaasgig fecakhmvea gmtvflvdrd ekalvekcae lgdkakplvi
       61 dllnpasvat mmpqileqag qldvfhanag ayiggplweg dpdawdrmln lninaafrti
      121 havlphmmer ktgdiimtss vagvvpviwe piytaskhav qafvhtvrrq vaphgirvgg
      181 vlpgpvvtal isdwpkakld ealangslme akevaesvmf mltrprniti rdlvilpqsl
      241 dl
//
LOCUS       WP_176023931             266 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: creatininase family protein [Brucella].
ACCESSION   WP_176023931
VERSION     WP_176023931.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Yoshimoto,T., Tanaka,N., Kanada,N., Inoue,T., Nakajima,Y.,
            Haratake,M., Nakamura,K.T., Xu,Y. and Ito,K.
  TITLE     Crystal structures of creatininase reveal the substrate binding
            site and provide an insight into the catalytic mechanism
  JOURNAL   J Mol Biol 337 (2), 399-416 (2004)
   PUBMED   15003455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..266
                     /product="creatininase family protein"
                     /EC_number="3.5.2.10"
                     /calculated_mol_wt=29186
     Region          4..256
                     /region_name="ArfB"
                     /note="Creatinine amidohydrolase/Fe(II)-dependent FAPy
                     formamide hydrolase (riboflavin and F420 biosynthesis)
                     [Coenzyme transport and metabolism]; COG1402"
                     /db_xref="CDD:441012"
ORIGIN      
        1 mkrywsdyts eafsrlerek lvavlpvgai eqhgphlpla vdaaivdgmv ketiarlpet
       61 srvlflptqa igksnehsly pgtltfsaet iirmwceiga cvaasgvrkm allnshggqi
      121 svmdivarel rirhnmmvvs inwfglgmpe gvysehdlkh gihagdmets vmlemhpdlv
      181 dmskaqdfrt ltetfasdfk hlslsggakp awqiqdinpy gaagdatlat aekgratidf
      241 aaerlvevla eieraplswl dnktaw
//
LOCUS       WP_176023982             265 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Brucella pseudintermedia].
ACCESSION   WP_176023982
VERSION     WP_176023982.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 265)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..265
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28370
     Region          8..265
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mhsvsflrrt isaalfsvli aspafaekir fgvtsgphae iaealapvak akgleieive
       61 fsdgalidpa tndgdldang fqhtpyfnqq nrdrglnlva vggrtvllpm agyshkyksl
      121 gelpegaqis ipndpsnagr alklleaggv lkltpgvtfn ateldivdnp kkvkiipmet
      181 aqlprsledv dfsvitshfa lsaglvpsrd ailiedqlsd yfcllavaek nkdapwvqtl
      241 vesykspdvk afiekkfggn iiagw
//
LOCUS       WP_176023983             377 aa            linear   BCT 11-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Brucella
            pseudintermedia].
ACCESSION   WP_176023983
VERSION     WP_176023983.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 377)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..377
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40354
     Region          24..362
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mnvlvrsenv ssaaldetrl trpiieirsl tktydekagp vidnlslqiq kgtihgiigr
       61 sgagkstlvr clnglvhpsd gkvfvsgrei talgqdelrl vrrevsmifq hfsllssrta
      121 fgnvalplel agadrqtiks rvndllglvg lkerahayps elsggqkqrv giaralalep
      181 svllsdeats aldpetteqi lsllkdinrr lgltivlith emdvvrqiad yvtvldqgri
      241 vesgptfdif afpespiars flasivahdl ppevsdrllp tpvvgsdpvl riifsgeaah
      301 apvvatlvqr fginpnilhg ridyiggkpl gimtlvaegg padlaavrsy lsslnlhgev
      361 ighvvrsafa gahrala
//
LOCUS       WP_176023987             531 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Brucella
            pseudintermedia].
ACCESSION   WP_176023987
VERSION     WP_176023987.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 531)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433522
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..531
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59152
     Region          45..524
                     /region_name="DdpA"
                     /note="ABC-type transport system, periplasmic component
                     [Amino acid transport and metabolism]; COG0747"
                     /db_xref="CDD:440510"
ORIGIN      
        1 mrkfallaal savllagtaa yaadeprsgg vinfvapygd sfstldiqas patqdefyak
       61 aihrtlydwd adlnkpvlgl atdvtvsddr lvytyklrqd affhngkplt addiiwsytr
      121 imdpkkafpp aryiaeikga eeytqgkake isglkkiddh tleitlkqpi dpgfqfmrnn
      181 taiypagegd seefqrhpig lgpykfaeyv pgsrltvekw dkyyekgkpy adkinimimg
      241 daaardvafr nkeidvavlg paqytaylad pelaknmvev aevytravgf npdfkpfqdk
      301 rvrqainyai dsdliikrlv kdkayravgw lpnsspafdk dakpypydpe kakallaeag
      361 ypdgfefelt atqneswglt ivqaiipmla kvgikvkakp veasvladvv pagnfqaymw
      421 slesgpdalt amqcfysttp qsacnyqkfs ntefdkivda aklaktdeek nellkkannl
      481 lqeeapvwff nynkavmahq pwlhglqpns aelavqsyek lwvddtvpsg r
//
LOCUS       WP_176023990             326 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella pseudintermedia].
ACCESSION   WP_176023990
VERSION     WP_176023990.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..326
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35733
     Region          6..326
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mseqplleve nlridivsgs skhnvvedvs ftidagetfg lvgesgcgks italsmigll
       61 rkplsitgga irfkghdlrs mssremrkrr gnriamifqe pmtalnplsp vgrqiaemfv
      121 lhrgatwhea erkavealas vqvpapeqrv knyphqmsgg mrqrvmiaia lacnpdllia
      181 depttaldvt vqaeilrlmq elctargtsv lmishdlgvi akmcrrvgvm yaghlveerv
      241 taglfhhpah pyahgllasl pqlgsrqkeg rlrlqeiegv vpsisafpkg crfeprctra
      301 tdvcrvqkpg wtplddagvv rcfhhe
//
LOCUS       WP_176023999             253 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Brucella
            pseudintermedia].
ACCESSION   WP_176023999
VERSION     WP_176023999.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..253
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27222
     Region          6..248
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 miehtplfla iaviaaflvg lskgglpsvg tlavplmalv ispitaaall lpiyvisdtf
       61 glylyrqhfs arnlailtpa avlgvgigwm fsahlsptfi gmlvglvgil fcfnawfgar
      121 yrrkarkadv pggvfwgllt gltsfvshsg appfqmyvlp qhlpklvfag tstilfaivn
      181 avklvpywql qqfsnldtsl glwlipaaiv gtfvgakltr impdgpffll vqltlfglsl
      241 kliadwivpy ffg
//
LOCUS       WP_176024020             276 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella pseudintermedia].
ACCESSION   WP_176024020
VERSION     WP_176024020.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 276)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..276
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30529
     Region          2..267
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mlvdiknlqi sfetrtsrfd avrgvslqlg reklgivges gsgksltara lmkllppiae
       61 vradklsfdg idilsaterg mrqirgkrag filqdpkysl npvktigvqv aeawrthkgg
      121 gkrqameaav dlldqvmirn prevaklyph evsggmgqrv miammlapdp elliadepts
      181 aldatvqaei lrliddlvsk rgmglllish dlplvshfcd rvmvmymgrv meelkaselv
      241 raehpytkgl lncipslmhp rdrlpvlnre eswlns
//
LOCUS       WP_176024041             262 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella pseudintermedia].
ACCESSION   WP_176024041
VERSION     WP_176024041.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..262
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27571
     Region          1..255
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mgrfakiifg vaavtfliap lfailplaft ssvfltypvp gwsarwfeel atadvwrrai
       61 vnsliigsgt milatvlgtm aalglrnril flsgpvktlf llpmvvpavv lgvgmqllfv
      121 rlgiansylg vivahtvisi pfvlvsvtga lsgidkrvel aaeslgaspl tvfrkitlpl
      181 ampgiasgav lafatsldev vltlfvagpn qrtlarqmfs tirenispai aaaaflfiag
      241 tvllglaaml frrkrmgegv st
//
LOCUS       WP_176024046             270 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella pseudintermedia].
ACCESSION   WP_176024046
VERSION     WP_176024046.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 270)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..270
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29099
     Region          7..261
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 msntfdwrwi prgillglla faifgplanl llwavaerwy fphtlplqyg fsfwanvfsp
       61 rgnalsslgt svliaaltvi vslglaipag yalarlklpf rglilltlli pqafpnlpvy
      121 vniaqmfysf glngtitgvv lvhvthglvy avwiataafs aidreieeaa rsmgasalrt
      181 fvditlpiaa pgllasaifv flesldeftg tyfvgapdis tlplllytas sggnyqiasi
      241 salillvpsi afmfvverfl radvlskvgr
//
LOCUS       WP_176024167             264 aa            linear   BCT 11-JAN-2025
DEFINITION  YdcF family protein [Brucella pseudintermedia].
ACCESSION   WP_176024167
VERSION     WP_176024167.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..264
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29253
     Region          22..257
                     /region_name="ElyC"
                     /note="Lipid carrier protein ElyC involved in cell wall
                     biogenesis, DUF218 family [Cell wall/membrane/envelope
                     biogenesis]; COG1434"
                     /db_xref="CDD:441043"
ORIGIN      
        1 mfyslskifw lffqpvtiif slvliaflai wrgmrsfsmg llalslatlf laayttlgav
       61 llapledrfa kpdtmpqhvd givvlggymn geinagrkgf elnsaadrif eamrlaklyp
      121 dakiiisgge gaffeesake adstrqmlad lgfsgeryif enssrntven aafskelaqp
      181 kpgevwllvt sayhmprsig cfrkagfdvv awpvdfktra serlalyles pnealsrfsv
      241 amrewvglaa ywlagktdml lpql
//
LOCUS       WP_176024166             270 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Brucella pseudintermedia].
ACCESSION   WP_176024166
VERSION     WP_176024166.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..270
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28255
     Region          4..242
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 msnlqtriit aivlgaaalw ltwigglgft lfsiaiglam fhewasltap kqtlfsrmfg
       61 wgwlvltsil lvmdksallt igvliagtli lfltqwragr gwpaaglfya gfsavslsll
      121 rgdepfgfta ivflfavvws tdiaayfngr alggpklapr fspnktwsga iggaaaavag
      181 gilvaslvaa pggwlvplla lllsivsqig dlaeswvkrq fgakdsgrll pghggvldrv
      241 dglvaaaall ylfgaifaep dvpsaiffsf
//
LOCUS       WP_176024198             413 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Brucella/Ochrobactrum
            group].
ACCESSION   WP_176024198
VERSION     WP_176024198.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..413
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=44594
     Region          69..362
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mvkkptptrt tasrtirqsd akvrdgdihv nvevgaltgs svrrqamfwv gavavfvlfl
       61 vvfssvllpf vagmalayfl dpvadrlerl glsrlaatvv illiflmali lglmivvpil
      121 atqladfisk ipeyitqlqs llanedsqwl kkyigidssv iqqnlssllq qgagflstll
      181 qslwnsgksl idiaglfvvt pvvafymlld wdrmvssids wvprrqlhtv rriaaemnaa
      241 vagfirgqgt lclilgtyya igltltglnf glligffagl isfipyigsf vglalaigva
      301 lvqfwpdwim icavagvffl gqfvegnilq pklvgssvgl hpvwlmfalf afgslfgftg
      361 mlvavpaaaa vgvlvrfaln sylqspmydp ayhqpdpdag plieagenag rek
//
LOCUS       WP_176024308             267 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella pseudintermedia].
ACCESSION   WP_176024308
VERSION     WP_176024308.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..267
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29646
     Region          10..258
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mkrkginaqk igawiaflig aiyflvplig tfefslrmrr geysfdayrv vfsdpnfqat
       61 fgysillgll tivfgvllvv ptaywvrlrl pqlrpvmefi tllplvipai vivfgylriy
      121 nssswlpfta stratdvllm fgymtlslpy myravdtamr tidvntltea aqslgagwgr
      181 imfkvifpnv isgvmsgafi tfaivigeft lasllnrpaf gpylqlvgan rayepsalai
      241 isfgitwlsi imlqlvsrln kfkttag
//
LOCUS       WP_176024355             170 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Brucella pseudintermedia].
ACCESSION   WP_176024355
VERSION     WP_176024355.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..170
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18705
     Region          37..140
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 mawkfmfasa vlavartmpg ifiankgpav vsdnamdmel kpapinpdwv legnpqarss
       61 eqsaskdgaa ytaiwdctag tfrwyfgwde tvyildgevh vtdadggtrt lrtgdvayfr
      121 ggtwatwkid nylrkvafmr rtlpapasfi yrasdaakrr lgrrksgaln
//
LOCUS       WP_176024462             461 aa            linear   BCT 11-JAN-2025
DEFINITION  ADP-ribosylglycohydrolase family protein [Brucella
            pseudintermedia].
ACCESSION   WP_176024462
VERSION     WP_176024462.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..461
                     /product="ADP-ribosylglycohydrolase family protein"
                     /calculated_mol_wt=50498
     Region          146..440
                     /region_name="DraG"
                     /note="ADP-ribosylglycohydrolase [Posttranslational
                     modification, protein turnover, chaperones]; COG1397"
                     /db_xref="CDD:441007"
ORIGIN      
        1 mkaweltrdl lrdtkpvirt aeeqtwdasa vmkaqddlma mfwksnvpgs aapeclmaga
       61 lqslenkgfv lapyeellrd glaalgkgdf etlyridmrl rvlmraaqpd pdhpsqktvr
      121 ygswdafdaa vqwpddvlya iqsddfrdrt aaawmaqlvg aaagtalegy taenimavfg
      181 pirdyvrepn tyndditfei afleafgdkg savtsadiae rwtsliplgw saeaialsnm
      241 rrgltppesg tcdnpfdewi gaqmrgticg mvvpgrarea arlawmdaei shagngilge
      301 vfnavmaara fvvsdtrell vstaalfpve teygavlafa ldacrsagnw qdawakcdae
      361 yaeynwihvy pnaaaqvial wfgegdfdrt leivcgighd vdcnaaqils miaiqrgsgi
      421 iaerwskpll adhivtymrr pakisfdalv dqtveaarna v
//
LOCUS       WP_176024576             285 aa            linear   BCT 11-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Brucella
            pseudintermedia].
ACCESSION   WP_176024576
VERSION     WP_176024576.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..285
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31098
     Region          32..266
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 mlkkkepnri sksiltairn rtgyrplnan iaggdvvias ynvhkcigid kqfnpqrtae
       61 viseidadvi alqeadrrfg ersglldlgl lerrhglipv pitatmpkgh gwhgnvllfr
      121 egvvrnvqql klpgveprga lvadlqfpag plrviaahlg llkrsreqqa esiltvlqea
      181 dtlptlligd lnewrigkrs slaalmptfn hvatavpsfp srfpvfaldr vlgaphnlvt
      241 svevhntpla rlasdhlpik ahldlksats lleelspeif nsrtg
//
LOCUS       WP_176024584             145 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Brucella pseudintermedia].
ACCESSION   WP_176024584
VERSION     WP_176024584.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..145
                     /product="OsmC family protein"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /GO_process="GO:0006972 - hyperosmotic response [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=14969
     Region          3..141
                     /region_name="osmo_induc_OsmC"
                     /note="peroxiredoxin, OsmC subfamily; TIGR03562"
                     /db_xref="CDD:274650"
ORIGIN      
        1 mdrkatavwq gtlkegkgtl dtqsgalkdl pydfkarfqd esrrsgtnpe ellgaahagc
       61 famqlsallt ehgtppekle ataavtvgpa agggfeisrs altlnatipg isaedfeala
      121 nkakqscpls kalgaievtl daklv
//
LOCUS       WP_176024591             152 aa            linear   BCT 11-JAN-2025
DEFINITION  cyclic nucleotide-binding domain-containing protein [Brucella
            pseudintermedia].
ACCESSION   WP_176024591
VERSION     WP_176024591.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Wang,Z., Jiang,Y., Lu,L., Huang,R., Hou,Q. and Shi,F.
  TITLE     Molecular mechanisms of cyclic nucleotide-gated ion channel gating
  JOURNAL   J Genet Genomics 34 (6), 477-485 (2007)
   PUBMED   17601606
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Kaupp,U.B. and Seifert,R.
  TITLE     Cyclic nucleotide-gated ion channels
  JOURNAL   Physiol Rev 82 (3), 769-824 (2002)
   PUBMED   12087135
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Canaves,J.M. and Taylor,S.S.
  TITLE     Classification and phylogenetic analysis of the cAMP-dependent
            protein kinase regulatory subunit family
  JOURNAL   J Mol Evol 54 (1), 17-29 (2002)
   PUBMED   11734894
REFERENCE   4  (residues 1 to 152)
  AUTHORS   Aiba,H., Fujimoto,S. and Ozaki,N.
  TITLE     Molecular cloning and nucleotide sequencing of the gene for E. coli
            cAMP receptor protein
  JOURNAL   Nucleic Acids Res 10 (4), 1345-1361 (1982)
   PUBMED   6280140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10034975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..152
                     /product="cyclic nucleotide-binding domain-containing
                     protein"
                     /GO_function="GO:0030551 - cyclic nucleotide binding
                     [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=16411
     Region          15..128
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(83..84,93..95)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(115..117,121..123)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
ORIGIN      
        1 maldddiril gtvglfesft aeqlrllafg aerlvlragr elfregqsad cayivvsgsi
       61 tlfheqnegr vairpvgpga migemaliaq tsrltgavae aetevirisr aifrrileey
      121 peaaaalhsh isrnllelig eiekvaprln gg
//
LOCUS       WP_176024620             351 aa            linear   BCT 11-JAN-2025
DEFINITION  dipeptidase [Brucella pseudintermedia].
ACCESSION   WP_176024620
VERSION     WP_176024620.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..351
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37766
     Region          4..350
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 mqrvfdghnd vllrlwenar kgedpikefi ggtdvghida prsrkgglag gicaiyvpsg
       61 ehielgkpda nghyetplsp plerspsldi aldmaaialk leaaggwklc rngrdldetl
      121 nsdtfaavlh megceaided laalevfyaa glrslgpvws rnnifahgvp faypmspdtg
      181 pgltetgkrl vkacnakgil idlahitekg fwdvaklsdq plvashsnah altpvarnlt
      241 drqldaires kglaglnyat tmlradaked adtplsdvvr hvdymvermg idcvalgsdy
      301 dgatipaeig daagtqnlvi alqkagynde elaklcrgnw irvlkqawhe a
//
LOCUS       WP_176024652             332 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Brucella pseudintermedia].
ACCESSION   WP_176024652
VERSION     WP_176024652.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..332
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37179
     Region          9..324
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 miqassvkrs ivfflvpnfs miafataiep lrianrmlgy dayqwrltsv dgkpvtasng
       61 vecavnasle derrflqreq rpsmvfvcsg vyveefrnks vfawlreeyn rgvavgglct
      121 gahilaaagl lsgkrcaihw enlpgfseaf pkaevyadlf evdsnlytca ggtasldmml
      181 kligddfdan lvnkiceqal tdrvrspqdr qrlplrarlg iqnskvltii emmeanlsep
      241 qalinvahti glsrrqverl frqemgrspa ryyleirldr arhlllqssm pvvevavacg
      301 fvsashfskc yrelygrspq qeraerkmli aa
//
LOCUS       WP_176024738             188 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Brucella pseudintermedia].
ACCESSION   WP_176024738
VERSION     WP_176024738.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..188
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=20464
     Region          <50..180
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mtktlvllfh pdlgrskana alarraaalp dvevvgmqet ypegvdmvrd gereaarllg
       61 adrivlqfpv qwystppllk awqdavltrm fyiayeaegr rlegtplmia atagntaeay
      121 rrgganmfai sdiftplrvt anrcgliwte pfvlfradkl sageietagk nyaaaltnwi
      181 ansgskkg
//
LOCUS       WP_176024757             346 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella pseudintermedia].
ACCESSION   WP_176024757
VERSION     WP_176024757.1
KEYWORDS    RefSeq.
SOURCE      Brucella pseudintermedia (Ochrobactrum pseudintermedium)
  ORGANISM  Brucella pseudintermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Brucella pseudintermedia"
                     /db_xref="taxon:370111"
     Protein         1..346
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36812
     Region          28..346
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msasqyqqdl gqkdlaraqp fklgdfirrr pesitffllv aictivsvin paflqastli
       61 digrasvvmg lfalgvfiil aaggidvsft aiaattvysl tllvqsympe lpiifiilma
      121 iaggiflgvl ngllvhhlnv pslivtigtq ylfrgfllaf vgtvwimslp ptmgafgrlp
      181 lfqsesatga titmpfyflv lpaaailtww ilnrtlmgra ifamggnsqi aarlgynlrt
      241 ihiflfgyag glaglagiih vcanrqsspf dfvgteisvi aavvlggari tggtgtvvgt
      301 llgvllitvi nsvlvlvgip stwqrlvvgc fillaaaffv trqrkk
//
LOCUS       WP_176025175             818 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Escherichia coli].
ACCESSION   WP_176025175
VERSION     WP_176025175.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 818)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 818)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 818)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 818)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..818
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..818
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=90339
     Region          5..818
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mdtvniyrls fvsclvmamp camavefnln vldksmrdri disllkekgv iapgeyfvsv
       61 avnnnkisng qkinwqkkgd ktipcindsl vdkfglkpdi rqslpqidrc idfssrpeml
      121 fnfdqanqql nisipqawla whsenwapps twkegvagvl mdynlfassy rpqdgssstn
      181 lnaygtagin agawrlrsdy qlnktdsedn hdqsggisrt ylfrplpqlg skltlgetdf
      241 ssnifdgfsy tgaalasddr mlpwelrgya pqisgiaqtn atvtisqsgr viyqkkvpps
      301 pfiiddlnqs vqgtldvkvt eedgrvnnfq vsaastpflt rqgqvrykla agqprpsmsh
      361 qtenetffsn evswgmlsnt slyggllisd ddyhsaamgi gqnmlwlgal sfdvtwassh
      421 fdtqqdergl syrfnyskqv datnstisla ayrfsdrhfh syanyldhky ndsdaqdekq
      481 tislsvgqpi tplnlnlyan llhqtwwnad asttanitag fnvdigdwrd isistsfntp
      541 hyedkdrdnq iylsislpfg nggrvgydmq nsshstihrm swndtldern swgmsaglqs
      601 drpdngaqvs gnyqhlssag ewdisgtyaa sdyssvsssw sgsftatqyg aafhrrsstn
      661 eprlmvstdg vadipvqgnl dytnhfgiav vplissyqps tvavnmndlp dgvtvaenvi
      721 ketwiegaig ykslasrsgk dvnviirnas gqfpplgadi rqddsgisvg mvgeeghawl
      781 sgvaenqlft vvwgeqscii hlperledtt krlilpch
//
LOCUS       WP_176025241             673 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Azospirillum argentinense].
ACCESSION   WP_176025241
VERSION     WP_176025241.1
KEYWORDS    RefSeq.
SOURCE      Azospirillum argentinense
  ORGANISM  Azospirillum argentinense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Azospirillum.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Azospirillum argentinense"
                     /db_xref="taxon:2970906"
     Protein         1..673
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=69645
     Region          167..666
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 magdaaftal rgveaasayr nvnqvagglv vvagefaler gatngalngs tpipserrsr
       61 lqqrrdaada alraaldalp tfpemashaq rlgevetslg rfrdyrrgvd ealardagqr
      121 spdvvsgfgg titahierig alrllleava pppkpatlql vqlrsyaadm aehagrergl
      181 fsalvassrp vapgqaeala ksrgrleqaw dgiralrtrp ditpdlarai dgveaayfqa
      241 faetrqavlk ggadgryplt sdewmvratv gidsilalag tvgaaidaav agtaeearsd
      301 llvslavftl slllgvggsl lvirrvvrpl tamtgamrql adgdlavaip gagrrdeiga
      361 maqavqvlqe havarerlea eqrreqeare rravalarlt hgfeakvsgl vgtlssaate
      421 meatagsmst aaqqtnqqsf avaaaseqts tnvqtvaaat eqltasirei gnraaqsqai
      481 ttravadarr tdetvrlmag caqrigevvg liqaissqtn llalnatiea aragdagkgf
      541 avvahevktl asqtaqatdd iaaqivqvqt vtrdavaaiq giaavigevn eiataiaaav
      601 eeqgaatqei trnvqqaaag tqevasniag vqqaandtgt aathvlsaaq elsqqaerlt
      661 gevgdflagv rga
//
LOCUS       WP_176025403             256 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Azospirillum argentinense].
ACCESSION   WP_176025403
VERSION     WP_176025403.1
KEYWORDS    RefSeq.
SOURCE      Azospirillum argentinense
  ORGANISM  Azospirillum argentinense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Azospirillum.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Azospirillum argentinense"
                     /db_xref="taxon:2970906"
     Protein         1..256
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27593
     Region          1..245
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mpfvsieqag ygvpsggtil dridwtigeg efhalvgrsg cgkttllklv agllapstgt
       61 vrvqgqpvqg pgaqvgfvfq aptllewrtv ldnlllpvsl trrpqpadrr kaeelldlvg
      121 lsglegrfps qlsggqqsrv alaralvtep plllldepfa aldaitreel qddllklcar
      181 hrttvlfvth diaeavylad rvavmeggql rhalpvplar prgrdvrysp rfnalclelr
      241 hamdgsksdv aleras
//
LOCUS       WP_176025402             399 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Azospirillum argentinense].
ACCESSION   WP_176025402
VERSION     WP_176025402.1
KEYWORDS    RefSeq.
SOURCE      Azospirillum argentinense
  ORGANISM  Azospirillum argentinense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Azospirillum.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 399)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 399)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 399)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Azospirillum argentinense"
                     /db_xref="taxon:2970906"
     Protein         1..399
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=42208
     Region          18..393
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 msgghilivd ddtanirala svledrhevr fatsgrrale lasadppelv lldvmmpgld
       61 gyavcrllkt dpatadvpvi fitslsspee eafgletgav dyvtkpfspa ivrarvathl
      121 slrranrslk denehlealv rertrklaqa qrekmaalrq mvagvahein tpigvalgsa
      181 shlgdrvaam terlaanqlr raelerflas agelaallsg tiarageivr cfkgvaadhg
      241 glrqtialrp fleqvteslr pqweplghrm avdcpadlrm vsnpailsai leqlvrnale
      301 hafpagrhgl vtvgavasgp dtvllsvadd gagiaegtag rilepffttr rgtgsvglgl
      361 nivdnlasdr lggsftiasr sgggtlatlh lpartppdl
//
LOCUS       WP_176025436             436 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Azospirillum argentinense].
ACCESSION   WP_176025436
VERSION     WP_176025436.1
KEYWORDS    RefSeq.
SOURCE      Azospirillum argentinense
  ORGANISM  Azospirillum argentinense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Azospirillum.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 436)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Azospirillum argentinense"
                     /db_xref="taxon:2970906"
     Protein         1..436
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45147
     Region          84..432
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mdrpsvtdar sfsatgdavs eprpaglrta lrdkasalfg rgtdprqgap ceaapvtlpa
       61 ngrhldasgp qggaaaiame alalngvthr ygrvvavddv svtigageiv clcgpsgcgk
      121 ssllriaagl eavqtgsvri ggtvvaderg avpperrgvg lvfqdyalfp hlsvldnvrf
      181 gltalsgeaq rkraletlgq vgmagyadsf phhlsggqqq rvalaralap npavllldep
      241 fsgldarlre qvrdetlhvl kqngaatmlv thdpeeamfl adrialmrag kvvqvgnpvd
      301 lytrpvnafa aeffgevnrl agvvqggavd tpvgpiptei adgtavdvli rpealklsaq
      361 paatvpagdl pvlarvmaar llgrtslvhl dvpdgkggsv hlhsrmpgqf lpaeqshvsv
      421 cmdlcqafvf pagapt
//
LOCUS       WP_176025446             463 aa            linear   BCT 11-JAN-2025
DEFINITION  CpaF family protein [Azospirillum argentinense].
ACCESSION   WP_176025446
VERSION     WP_176025446.1
KEYWORDS    RefSeq.
SOURCE      Azospirillum argentinense
  ORGANISM  Azospirillum argentinense
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Rhodospirillales; Azospirillaceae; Azospirillum.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Azospirillum argentinense"
                     /db_xref="taxon:2970906"
     Protein         1..463
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50290
     Region          67..451
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mstlfgrkaa ppslavaspp peepkpapvp apaavsvppl aavrpvnrsl ndirsqvlar
       61 idpatiadmp aetlrplver liddiattsr sqlngreqaa latelvhdmi glgpleplla
      121 ddaitdimvn gpsrtfaeqr gklvempvrf rdaghllnia qriasavgrr vdesspmvda
      181 rladgsrvni vvpplaldga cisirkfarr tigfrelvef rsmsepmara leivgrcrln
      241 viisggtgsg kttllnamsr pieatervit iedaaelqlq qphvvrletr ppnlegqgqv
      301 tqrdlvrnal rmrpdriiig evrgaeafdm lqamntghdg smstihannp rdalsrvenm
      361 vlmagmnlps rairqqiaga vnvivqvqrm rdgvrrithv telvgmegdv iltqdlftfe
      421 frgenrdgil egryaatglr prfadrlayf gqeaawntat tgp
//
LOCUS       WP_176025494             178 aa            linear   BCT 11-JAN-2025
DEFINITION  TlpA disulfide reductase family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_176025494
VERSION     WP_176025494.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..178
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=19047
     Region          42..158
                     /region_name="TlpA_like_family"
                     /note="TlpA-like family; composed of TlpA, ResA, DsbE and
                     similar proteins. TlpA, ResA and DsbE are bacterial
                     protein disulfide reductases with important roles in
                     cytochrome maturation. They are membrane-anchored proteins
                     with a soluble TRX domain containing a...; cd02966"
                     /db_xref="CDD:239264"
     Site            order(73,76)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239264"
ORIGIN      
        1 mnttpsaqrr tgraryiaaa vvvaaiavag ffafngkstv pdatftllsg qkvstggdlk
       61 gkvylvnfwa tscatcmqem pqmvdtynrf kgqglefvav amnydpptyv anyaqtrqlp
      121 fkvalddgsv akqfgnvqlt pttfvvdkdg kilkryvgap qfaeldallk kaldgnaa
//
LOCUS       WP_176025606             406 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia vietnamiensis].
ACCESSION   WP_176025606
VERSION     WP_176025606.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..406
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43248
     Region          7..392
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(17..18,21..22,25,57,112..113,115..117,120,141,
                     144..145,148,228,231..232,235..237,240,263,267,319..320,
                     324,328,344,347..348,351..352,355)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mlknrdfqkf llgylfssfg nymtpvaltf amvgqpngll nlatvlaart apsallsifg
       61 gwsadsisrk htiiisdlir flsvgavgii llkgvqavpv isammfvsgl rqalgrpalg
      121 gmtrvliedd ndlplangql saidsfsgiv gplaaallsn rismggvvim daatfilnal
      181 lialithnps rrelgdtkgy rrtlkdiaag crefasrkwl vamtvqisll qalvsvpfal
      241 igpqlmssrl hgielwsavv svegagallg swfaaavrvk nilfvaevlv lgtclpmltl
      301 glgfpvpili vasllfgfct avygvlldva lqryvpervl srviavcvsi svilnpiafl
      361 vtnplvdtfg shrllifggw ftlistafvl wavrpsktvd iylapl
//
LOCUS       WP_176025608             157 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia
            vietnamiensis].
ACCESSION   WP_176025608
VERSION     WP_176025608.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..157
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17324
     Region          6..144
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mpepvldrvd rhllavllen grasnldlak avglspaqtl rrhrrleeig airryetrlc
       61 pdtlgfgvta fvhvtmergh irdlskfqkl vsdlaqiqec fsvtgdidyv lkvvardlkg
      121 lstflletlm ripgvsgvhs svcldeikct sampvet
//
LOCUS       WP_176025620             924 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Burkholderia
            vietnamiensis].
ACCESSION   WP_176025620
VERSION     WP_176025620.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 924)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 924)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 924)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 924)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 924)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11534155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..924
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=94019
     Region          12..79
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          101..163
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(107..109,112)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          180..922
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mteslastat htieldidgm tcascagrve kalakvpgva rasvnlater asvaatmdvg
       61 atqladavrq agygatpvag eptasaqpaa apqapapasi eldidgmtca scagrvekal
      121 akvpgvtras vnlaterasa daapdvsasr lvdavrqagy gatpvaatpt adragpasfe
      181 ldiggmtcas cagrvekala avpgvarasv nlaterasvq aagtldaaal iaavtsagyq
      241 aslaaeaqaa aagpaaadpa qttdarkrrd airernlvig aavlstpliv pmlvaplgid
      301 amlpgwlqlv lasivqfgfg arfyraawha vkartgnmdl lvalgtsaaf glslwmllre
      361 pahpghlyfe asavivtlvr fgkwlearak rqttdairal nalrpdrari vehgverdvp
      421 laqvrvgttv airpgervpv dgrivsgrsh vdeslitges lpvpkddgdp vtagsingeg
      481 alvvattaig aettlariir lvesaqaeka piqrlvdrvs evfvpsilgi avltltgwli
      541 agagaetail navavlviac pcalglatpa aimagtgvaa rrgvlikdaq alelaqratv
      601 iafdktgtlt egkpsvtafd avdisreqal avaaavqrhs dhplaravva aydadvaarg
      661 gaavaadaaa atdaravagr gvearvdgrl valgssrwrd elgiavppel garaaelera
      721 gntiswlmra daprallali afgdtvkpga rdaiaalsah gvasvlvtgd nrgsaaavaa
      781 algidevhaq vlpddkarvv aelkrthggv vamvgdgind apalaaadvg iamatgtdva
      841 mhtagitlmr gdptlvadai diskrtyrki qqnlfwafvy nligvplaal gwlnpviaga
      901 amafssvsvv tnalllrrwk gkar
//
LOCUS       WP_176025625             192 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_176025625
VERSION     WP_176025625.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..192
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=21204
     Region          18..>150
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          63..89
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(66..67,70..72,74..75,79,82,90,92,96..97,100..102,
                     104..105,109,112,121,123,126..127,130..132,134..135,139,
                     142)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          90..121
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          123..150
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mrtvseieee meeyqeegnl gkvmdlvdel gnmqdrlyka iaegdlneal yfdslgfdls
       61 eatclrvaak ygqckligyl irngadvhan gdealcfaae hghleavqrl velgadvhaq
      121 eekpvklath tekigivqyl veagasidav leitgsgsfy pelhqwaqsy krkqklegel
      181 sqkdestpkt ki
//
LOCUS       WP_176025676             297 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia vietnamiensis].
ACCESSION   WP_176025676
VERSION     WP_176025676.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006586
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..297
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=31643
     Region          82..289
                     /region_name="TesA"
                     /note="Lysophospholipase L1 or related esterase. Includes
                     spore coat protein LipC/YcsK [Cell cycle control, cell
                     division, chromosome partitioning, Lipid transport and
                     metabolism]; COG2755"
                     /db_xref="CDD:442045"
ORIGIN      
        1 mkkplkaanv vppvggllkv rlsplsrrkt msgiipklin hnaralmarg iiaslfgmfv
       61 macsgcgggg dgsppsaeaa iqrpakavli eaygdsttvg ytvtngvsei nsqnqiavlq
      121 qlltarfgaa vtvsnqgvgs teasqllngt dgvhlpwaqq maqskadivt ieyglndayd
      181 yivpadgieq espqrfgeil selvriaqsa gkqviliept pschpvrldr lqyyvmqvda
      241 vaqqmkvplv shywpiasmp nwqsllsdct hpttqlyain aqatfdviap lianhin
//
LOCUS       WP_176025761             235 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Burkholderia vietnamiensis].
ACCESSION   WP_176025761
VERSION     WP_176025761.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12785252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..235
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26156
     Region          <3..>179
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
     Region          102..>179
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Site            134..140
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:350677"
ORIGIN      
        1 mtqadekgva qldvpwlkep islsdakeii stfesvfsdl esgkqfdpdk arkrpgegat
       61 rkqlvlrani qaleyeemrr ealqsvpasp klpqsirpef allphqqagl awmqhlfslq
      121 tdyqvrgail addmglgktf qllalmawll ekdptmnpml vvapvsllen waeeankffq
      181 pgafgyrkps sriaaalrvn ttmtawcsqa agrtlsdics favrrccerq ptwss
//
LOCUS       WP_176025766             329 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-binding protein [Burkholderia vietnamiensis].
ACCESSION   WP_176025766
VERSION     WP_176025766.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 329)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 329)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 329)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10598562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..329
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35937
     Region          46..172
                     /region_name="AAA_22"
                     /note="AAA domain; pfam13401"
                     /db_xref="CDD:379165"
ORIGIN      
        1 mtpaqkllva ietcelphph fmehfqplkq rienalagra srierimgps rvgksmlina
       61 lvrefgetki dgrrrvpvlv vpvptpattl elpksvvaal gmpvqrsits gamgtrmleq
      121 lklvgtrvvi feeashlvee gsrfpvraaa dwfkaladsh nltlflfgvp rlkilfdnne
      181 qlrlrasapr lllpydsrva ddmrafhscv aafanlfaeh gfpialspaa ltyqcyllsg
      241 gligivsrfm qeladrmaae gphpltfadc healkgvtat gspnfpafes pdtvenavap
      301 aalhqaflhv mrdndlavpi innqpetvq
//
LOCUS       WP_176025935             274 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Robbsia andropogonis].
ACCESSION   WP_176025935
VERSION     WP_176025935.1
KEYWORDS    RefSeq.
SOURCE      Robbsia andropogonis
  ORGANISM  Robbsia andropogonis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Robbsia.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 274)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 274)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Robbsia andropogonis"
                     /db_xref="taxon:28092"
     Protein         1..274
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31241
     Region          23..274
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mqlnnnssid iidladhdgs ndistalksv riwatlgwhd ikqryrrsii gpfwftlstl
       61 imvvvlgaly stllrqnird ylpylavglv vwqyigtman egcmafigsa slikqiripl
      121 tihvcriawr nfaillhslp vvvvlmmvfg nwprpefllv pvalallflh gvwigvtlgi
      181 lcarfrdvpp ivtnliqvvf fftpvmwspe ilknrawiae ynplyhliet vrapltgrpi
      241 sweswawsig llivgfgvaq ylmrrsrnrv pywl
//
LOCUS       WP_176025932             355 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Robbsia andropogonis].
ACCESSION   WP_176025932
VERSION     WP_176025932.1
KEYWORDS    RefSeq.
SOURCE      Robbsia andropogonis
  ORGANISM  Robbsia andropogonis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Robbsia.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Robbsia andropogonis"
                     /db_xref="taxon:28092"
     Protein         1..355
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37900
     Region          122..325
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mswqngllsw flrrrvralr hspldpvrvr qgaekmiwpa rpatgwvire medltvkasd
       61 aastpsrvss stpadglpas apkatappai atapvlstpg rvpgewitta sprllkttrr
      121 vvlylhgggy ffcsprthra itctlarrgl arvcapdyrl apeypapaal ddalrvwhal
      181 rdsgepadqi vvagdsaggg lalallqalr dagepmpaaa vlfspwtdla ltgatlesha
      241 gtdvlmdaqg lhdatalvlg aggldardpr isplygdfhg lpplliqasd vemllddarr
      301 vaerareagv nvtleitcgv phawqmfapv lpearralvr aaqfirghth pnrqa
//
LOCUS       WP_176025981             246 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Robbsia andropogonis].
ACCESSION   WP_176025981
VERSION     WP_176025981.1
KEYWORDS    RefSeq.
SOURCE      Robbsia andropogonis
  ORGANISM  Robbsia andropogonis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Robbsia.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Robbsia andropogonis"
                     /db_xref="taxon:28092"
     Protein         1..246
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=25881
     Region          7..230
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          85..112
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          115..142
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(116,120..121,124..126,128..129,133,136,142,144,146,
                     150..151,154..156,158..159,163,166,175,177,179,183..184,
                     187..189,191..192,196,199,208)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          144..175
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          177..208
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mtmmsrmraa vlgrsarygs mrqavagvaa msilagcgvn aqmasaaspd avikavkfdd
       61 asavqralqs gfnpnttdaq gmpllvlaar eksdkvteal ladsrtdvek tdsagenamm
      121 laaivkdasi vrmliakgak vdkpgwtplh yaastgddti vtmlldahan vdarspndtt
      181 plmmaarggy astiqllikr ganplvknql gmtaldfgkr ysepdsvkll tsieqqyraq
      241 hpqaaq
//
LOCUS       WP_176026020             479 aa            linear   BCT 11-JAN-2025
DEFINITION  HDOD domain-containing protein [Robbsia andropogonis].
ACCESSION   WP_176026020
VERSION     WP_176026020.1
KEYWORDS    RefSeq.
SOURCE      Robbsia andropogonis
  ORGANISM  Robbsia andropogonis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Robbsia.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Robbsia andropogonis"
                     /db_xref="taxon:28092"
     Protein         1..479
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=52825
     Region          22..216
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 mieienkadl ltrlftamae rgelpslqss sdriiaslkd eeayladltn lvlsdislsq
       61 kvirqansam rhsfgdeiis israirvlgv ntveqfsael pdiadfqans phldtgrdal
      121 kramvasefa rnmthrhasq aseeavlstl myllaptvla lylekdwqqv ldytrlypdv
      181 tirdacrevl gvsltdiaaa larhfnvpet ladcmagalp dagvrndsht qwlimistva
      241 aevatmiekk taprdieqfv kpylnalgmd aptlnnaleh aqsaavrvdr ggrgrsddae
      301 afempanpme rfgealthvr slaptlntag viplvvenig qclnlrngfl lllntkenvy
      361 aakvtygegv rdhlvdlrfn agfednifhq algsrnptff qdiradsfvh rvpewyktaf
      421 ptarsivfvp vhlndrcial fcgtwgaiaa srpllhgesq svkaladeis rslersirr
//
LOCUS       WP_176026023             455 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Robbsia andropogonis].
ACCESSION   WP_176026023
VERSION     WP_176026023.1
KEYWORDS    RefSeq.
SOURCE      Robbsia andropogonis
  ORGANISM  Robbsia andropogonis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Robbsia.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Robbsia andropogonis"
                     /db_xref="taxon:28092"
     Protein         1..455
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48420
     Region          27..423
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(28..29,32..33,36,75,133..134,136..138,141,161,
                     164..165,168,252,255..256,259..261,264,292,296,349..350,
                     353,357,373,376..377,380..381,384)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mnthvhapeh qamrtravta aavgtalewf dftlygalaa tvlptsffpa mdptsallas
       61 latfgvglaa rplgaiicgh lgdklgrrnv mlatvsvmgl ssmlmgllpt yasigvwapf
      121 llvllrilqg falggestga qlmaiehasa drrgkysgll glcsplsqim angvllalss
      181 lmsaeafdgy gwripfvlsf vlvivgvyir lrvsetpafe alrktgvvqv ghplrdalrl
      241 hwrtvlrwml ffcgpaaify livvfslsyv tktlavpkqt gflllmgani caivgalagg
      301 mlsdrigrrk alalgscmtl lmlflyfqil dtrhfflmll amgfflgftq fqsgiqpvaf
      361 aeafptnvry sgsalaytga nliaggpmpv lavwlfavcn gspwgvvavc vvlnvislva
      421 iltapetlgi dmnradskva vmgssahdai qshsh
//
LOCUS       WP_176026085             193 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Robbsia andropogonis].
ACCESSION   WP_176026085
VERSION     WP_176026085.1
KEYWORDS    RefSeq.
SOURCE      Robbsia andropogonis
  ORGANISM  Robbsia andropogonis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Robbsia.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Robbsia andropogonis"
                     /db_xref="taxon:28092"
     Protein         1..193
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21994
     Region          21..186
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 meppftahtm tdrnnditat vvrerarlan firrrisnpd daedilqdvl hefvqayrlp
       61 apieqasawl fraarnriid rfrkkkeepl pgssneedda gseyrldlvl pardggpeaa
      121 yarvlllkal qdaldelppn qrevfiahel egrsfkdmvm etgvtlntll grkryavlhl
      181 rtrlqaiyde lgm
//
LOCUS       WP_176026098             360 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Robbsia andropogonis].
ACCESSION   WP_176026098
VERSION     WP_176026098.1
KEYWORDS    RefSeq.
SOURCE      Robbsia andropogonis
  ORGANISM  Robbsia andropogonis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Robbsia.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Robbsia andropogonis"
                     /db_xref="taxon:28092"
     Protein         1..360
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39903
     Region          53..178
                     /region_name="CatE"
                     /note="Catechol-2,3-dioxygenase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2514"
                     /db_xref="CDD:442004"
     Region          225..347
                     /region_name="CatE"
                     /note="Catechol-2,3-dioxygenase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2514"
                     /db_xref="CDD:442004"
ORIGIN      
        1 minrpeehgl pqrprvvdcg hahgerpllf qdrkmmnsdi gkdcavehgf faprrlahan
       61 vfvsdyqras rfyrdvfgfe evysqpdnka sfisngntyh dfalvdinsr yakpgqkpdl
      121 nhfafevese aalvagykaa iasgvsykst edhdvahsly qkdpdgneve iyadmvadwr
      181 serkgvfskk kpiwipgetn ipldkhyypv dpeirsipds lvhgrrvthi alvtrdyaam
      241 lafytgivgl rviagggade yallagthsm gdivlyrpgl asnlpthhig vevtsladld
      301 aaatriadfg aqvigrfshp ardvvfvtdp dglpiqlyvn kawrpeviat ispserpylv
//
LOCUS       WP_176026103             362 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Robbsia andropogonis].
ACCESSION   WP_176026103
VERSION     WP_176026103.1
KEYWORDS    RefSeq.
SOURCE      Robbsia andropogonis
  ORGANISM  Robbsia andropogonis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Robbsia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Robbsia andropogonis"
                     /db_xref="taxon:28092"
     Protein         1..362
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=37932
     Region          <214..>348
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mawptiavcl wigqitnhmv pmlvvaggaf tvglgalqrf trisimpmll aclgmmlstw
       61 igsrigaslt amllasaiwa alggwaairg pgltwicqqs aialfvagsf agsnsgnasv
      121 anssfpidfg lmlqailpqf gelvhgsgtf gvstdyaaqr almvgiggav qigflgaafl
      181 fwpraippil psqslrsdtr galatalraa lactaaslav hmlklqhsyw apmtalvvlk
      241 pslkeefhsv lqrcigtvtg atlvtlaiff lrpspgwlii atslcalsay alnrvsylff
      301 saaltayivc mlglvdpgqi apeialyqer igatligcgm alvidyllka iglnanrrpg
      361 md
//
LOCUS       WP_176026154             862 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Robbsia andropogonis].
ACCESSION   WP_176026154
VERSION     WP_176026154.1
KEYWORDS    RefSeq.
SOURCE      Robbsia andropogonis
  ORGANISM  Robbsia andropogonis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Robbsia.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 862)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Robbsia andropogonis"
                     /db_xref="taxon:28092"
     Protein         1..862
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=93990
     Region          15..830
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mdayeqiqss nprgvqnnrp lkldtpagkd vlmplravgh srigrgysft vdmvstsrkl
       61 elkqliaqpv tlwmrqndkt ykphhgyvht vrrlgmdggl vhtqlefasw lhflrfrkda
      121 riwqdktvid iltdvfnahp qargrfkfkl fgelrdplpq rsfcmqyedd wnfvhrlles
      181 eglwfyfeqs pdgqshtmii tdynyycdel qpgqidfsra qmdaevegfs hwsgtrtlqs
      241 trytgvtgdy kspgsskars kdtlpnqgdl pqqnevyeyt gkytwpdykr gdhlatlrme
      301 emesrakrfh gagsirrmda gryfelrnhp dhqndvqqer eflaidvrwf iannlstgnt
      361 rplpgslete vadaradylg dqlgaektgs aklsasasgg sagffltlve aqrmsvpyrs
      421 pfehrkpqmr iqtatvtgpa gsevytdsln rikgkfewdr lnsgdenasc wlrvamsdtg
      481 gsyggvhvpr vgeeilvdwv dgdcdrpivt grvyngsktp nwhsngllsg yrskeyggsg
      541 ysqmvlddst sqprmqlyss sansqlhlgy lvaqngntrg aylgsgfdlk sdaygairag
      601 qglyvsthpa naaqpmnvta aseqlasaes vaelasqast snqaeslqdg ldalkkltda
      661 tqynvagnsg gvggntgggg tgnangfstp imliaspaga glstqdsahi tanqqvnivs
      721 gkstnvaagk sliasvmeki slfaqnagik lfaskgkvei qaqsdemkla alndvtitss
      781 sgkvvisadk eiwigaggsy ikitselien gtsgqilekg aswskqgass mrlptpitsv
      841 tkgcswktat asansassvp le
//
LOCUS       WP_176026199             766 aa            linear   BCT 11-JAN-2025
DEFINITION  type IV secretory system conjugative DNA transfer family protein
            [Robbsia andropogonis].
ACCESSION   WP_176026199
VERSION     WP_176026199.1
KEYWORDS    RefSeq.
SOURCE      Robbsia andropogonis
  ORGANISM  Robbsia andropogonis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Robbsia.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Kumar,R.B. and Das,A.
  TITLE     Polar location and functional domains of the Agrobacterium
            tumefaciens DNA transfer protein VirD4
  JOURNAL   Mol Microbiol 43 (6), 1523-1532 (2002)
   PUBMED   11952902
REFERENCE   2  (residues 1 to 766)
  AUTHORS   Christie,P.J. and Vogel,J.P.
  TITLE     Bacterial type IV secretion: conjugation systems adapted to deliver
            effector molecules to host cells
  JOURNAL   Trends Microbiol 8 (8), 354-360 (2000)
   PUBMED   10920394
REFERENCE   3  (residues 1 to 766)
  AUTHORS   Ghai,J. and Das,A.
  TITLE     The virD operon of Agrobacterium tumefaciens Ti plasmid encodes a
            DNA-relaxing enzyme
  JOURNAL   Proc Natl Acad Sci U S A 86 (9), 3109-3113 (1989)
   PUBMED   2541431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466229
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Robbsia andropogonis"
                     /db_xref="taxon:28092"
     Protein         1..766
                     /product="type IV secretory system conjugative DNA
                     transfer family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=83542
     Region          213..615
                     /region_name="VirD4"
                     /note="Type IV secretory pathway, VirD4 component,
                     TraG/TraD family ATPase [Intracellular trafficking,
                     secretion, and vesicular transport]; COG3505"
                     /db_xref="CDD:442728"
ORIGIN      
        1 mkkrilldil laalagavlf lgarplhler lvtdpleraa ligsvcgtcv vwgicasavl
       61 lkratmldrv vagglvalla italvvagqf agaalfakle klpdsviglw tlrdywqafg
      121 deksvkrslf iasvvsaaip llpivavaaa lvakpkrelh gdarfarahe irryglmdea
      181 ngrtrgkvgv rdpsiivgry kgkyltfrgm qfvmvaaptr sykgvaivip nlltfsdsvv
      241 vldvkgenfd ltsryrqacg qkvfrwapfd eggythrwnp lfkiarspaf vrvgrlqria
      301 arlyhtsdar nkffyeqasd lflglalylm emtddctfgq vlrlatkpdk tvrehlselm
      361 qhetkegepl sgdclgalsr vlaspdetml nivstfnsgl rlfsnaivdq atsacdfdld
      421 rvrrepisiy vvlpvrdlsv asllanlfft qciednldvl pgedptiryq cllvldefpa
      481 igridvidkg nafiagywir lltilqsktq tepnelygva gtrtlftnha vlvayapgnq
      541 qdakelsetl gtftqkatst srsrgrntst gtntsdqgra lmldqelkrm epyqeivlgf
      601 qrpilcekat yfedalfidr mravsptlaa vaddlpcedd ikaawqagel ratgipinnp
      661 rqyhaalsak aageirlarq agakaltaae llaldqrqpg pvatnvaltg faddlvelgl
      721 vmrddvrall agirldigaa hgvgldslse panvpadydm teaang
//
LOCUS       WP_176026249             380 aa            linear   BCT 11-JAN-2025
DEFINITION  ParA family protein [Robbsia andropogonis].
ACCESSION   WP_176026249
VERSION     WP_176026249.1
KEYWORDS    RefSeq.
SOURCE      Robbsia andropogonis
  ORGANISM  Robbsia andropogonis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Robbsia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Robbsia andropogonis"
                     /db_xref="taxon:28092"
     Protein         1..380
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41727
     Region          90..376
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mqtgfflwkm petailgtrv itkpfkvqav aqllattndt vrrmvddsgi ivarqesgpk
       61 trlfsvenif elaryraakr sknpkkrqvv atvyapkggv gkttlasnlg tlfalkglrt
      121 liidldfqan ltlslgydse ltreeasetg vslskiveyh fgnllpsyps pngratlqda
      181 ikkpfgdcgp hlvpadltld rldtmltyea legrgpdlmi pklirdgsaq kdaafdtsgy
      241 dvilfdaapa knritrgall asdfvispvs mekfstkals ylssvltemq eqfdrspell
      301 ivgnffdphr irvmgqlmti tqkyadswle qsirrsedfp kalngetdlp lvlqkpssqa
      361 aaelqacada llkrmgmidg
//
LOCUS       WP_176026263             298 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Robbsia andropogonis].
ACCESSION   WP_176026263
VERSION     WP_176026263.1
KEYWORDS    RefSeq.
SOURCE      Robbsia andropogonis
  ORGANISM  Robbsia andropogonis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Robbsia.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Robbsia andropogonis"
                     /db_xref="taxon:28092"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32850
     Region          13..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(105,109,148,163,165,223,240,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(106..107,111..112,114..115,118,122,124..130,192,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 manmralegm lefvavverg tftsaarhld vsvshvsrqv sklearlgaq lfvrntrqmh
       61 iteagkrlfe kshpllqdll saqetilenr eaiegtikis lagkyaedrl vpaltrfcae
      121 htgvhldldl sarnvdlmae gfhlavrmgp mgttssltat rllsvplhvl akpallrslp
      181 eiqtpkdlpp esclplvnrp wnfakdnrne gikplgrfss nsgaaiiraa ldglgianvp
      241 ayysdrvian gslvriledw rsieesifyi vyptgrhmpv rvrrligylq dtlksaan
//
LOCUS       WP_176026367             253 aa            linear   BCT 11-JAN-2025
DEFINITION  TlyA family RNA methyltransferase [Brucella intermedia].
ACCESSION   WP_176026367
VERSION     WP_176026367.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..253
                     /product="TlyA family RNA methyltransferase"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27065
     Region          11..253
                     /region_name="YqxC"
                     /note="Predicted rRNA methylase YqxC, contains S4 and FtsJ
                     domains [Translation, ribosomal structure and biogenesis];
                     COG1189"
                     /db_xref="CDD:440802"
ORIGIN      
        1 msgeasdknl rldqllvelg lfatrsrard aiqrgtvkvd gkpvtkpgqt vlrnanvavd
       61 dpasayvsra alkliaaldh fgldvkgrta ldigastggf tqvllergan hvlaidvghd
      121 qlhetlradp rvtnkeglna ralefsdldg reidcvvsdv sfislklalp aalafaqkga
      181 icallvkpqf eagreaigkg gilrdpkdge riaeelrlwl etqawwralg lcpspieggd
      241 gnreyllagk kdq
//
LOCUS       WP_176026344             136 aa            linear   BCT 11-JAN-2025
DEFINITION  GFA family protein [Brucella intermedia].
ACCESSION   WP_176026344
VERSION     WP_176026344.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..136
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15008
     Region          1..121
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mdkvtggclc gkvrfeavgq pyrvgichcl dcrkhhgalf hasaifpqta vtvegetgdy
       61 agrhfcprcg ssvfghsgde ieinlgslda pdqfkptyel wiirreswlp pfpdmhgyer
      121 drdgssrfee giygda
//
LOCUS       WP_176026383             248 aa            linear   BCT 11-JAN-2025
DEFINITION  SURF1 family protein [Brucella intermedia].
ACCESSION   WP_176026383
VERSION     WP_176026383.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Reeves,J.E. and Fried,M.
  TITLE     The surf-4 gene encodes a novel 30 kDa integral membrane protein
  JOURNAL   Mol Membr Biol 12 (2), 201-208 (1995)
   PUBMED   7540914
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..248
                     /product="SURF1 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0033617 - mitochondrial cytochrome c
                     oxidase assembly [Evidence IEA]"
                     /calculated_mol_wt=27681
     Region          1..247
                     /region_name="Shy1"
                     /note="Cytochrome oxidase assembly protein ShyY1
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG3346"
                     /db_xref="CDD:442575"
ORIGIN      
        1 mtklqqsrrf pwgiviasai alvillvlgt wqverlqwke aliasteqri hepplplsem
       61 ekvykqegsv eyrpvtvsgt fmhqgerhfl athegaagyn vytplmledg rfvlvnrgfv
      121 pyekkdpstr iegqidgpvn vtglardpls akpgfflpdn dpsknifywk dwtamaesad
      181 lpnldeivpf fidadskpnp gglpvggvti idfpnnhlqy aatwyglala ligvvgtwlw
      241 ryrkasrg
//
LOCUS       WP_176026420             624 aa            linear   BCT 11-JAN-2025
DEFINITION  terminase large subunit [Brucella intermedia].
ACCESSION   WP_176026420
VERSION     WP_176026420.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Fung,H.K.H., Grimes,S., Huet,A., Duda,R.L., Chechik,M., Gault,J.,
            Robinson,C.V., Hendrix,R.W., Jardine,P.J., Conway,J.F.,
            Baumann,C.G. and Antson,A.A.
  TITLE     Structural basis of DNA packaging by a ring-type ATPase from an
            archetypal viral system
  JOURNAL   Nucleic Acids Res 50 (15), 8719-8732 (2022)
   PUBMED   35947691
REFERENCE   2  (residues 1 to 624)
  AUTHORS   Xu,R.G., Jenkins,H.T., Chechik,M., Blagova,E.V., Lopatina,A.,
            Klimuk,E., Minakhin,L., Severinov,K., Greive,S.J. and Antson,A.A.
  TITLE     Viral genome packaging terminase cleaves DNA using the canonical
            RuvC-like two-metal catalysis mechanism
  JOURNAL   Nucleic Acids Res 45 (6), 3580-3590 (2017)
   PUBMED   28100693
REFERENCE   3  (residues 1 to 624)
  AUTHORS   Black,L.W.
  TITLE     DNA packaging in dsDNA bacteriophages
  JOURNAL   Annu Rev Microbiol 43, 267-292 (1989)
   PUBMED   2679356
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..624
                     /product="terminase large subunit"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0140657 - ATP-dependent activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69427
     Region          3..617
                     /region_name="YmfN"
                     /note="Phage terminase-like protein, large subunit,
                     contains N-terminal HTH domain [Mobilome: prophages,
                     transposons]; COG4626"
                     /db_xref="CDD:443665"
ORIGIN      
        1 mtktpaldrv nayaravldg vevagphvrn acqrhfddla qahergyfwd dakanramrf
       61 feerlklndg qfdgkpfklh asqafklgsi fgwvdsdgnr rfrrvyieeg kgngkspfag
      121 glglyglmsd geagaqiyaa gakkeqaqil fqdavkmara apklskritf sggigrefni
      181 aflekkaffr piskdagktg sgprphyalc devhehpdrs vmemlergfk frqqpllfmi
      241 tnsgsdrnsv cweehehavr vaagtrtpdd dfsyvgevid dttfayvcal dkgddpledq
      301 scwkkanpll gviltekyla gvvdqakqip gklngilrlh fcvwtsadka wmprdtveav
      361 mddfdpieeh rgkqlflsvd lsaardmtal acavktgtkt meredgstie lptfdawiea
      421 wtpaetlkar aladkapydv wveqgflnas pgkrirfdfv aqrvaqlsqe fdiegiaydr
      481 yaydkfreel daigvevehi phpqggkrrs kasdkkieaa keaglpepqg lwmpgsvtel
      541 enaiidgrvr lrrnpvlmta lmgatfdrdp ldnrwfvktk asvridtava lamvtgfaad
      601 tpievkssls pwddpeftlt kvas
//
LOCUS       WP_176026450             201 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Brucella intermedia].
ACCESSION   WP_176026450
VERSION     WP_176026450.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..201
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21762
     Region          13..200
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mttqtyehrl kagakgaplf ivfhgtggde nqffglaeql lpdativspr gdvseygaar
       61 ffrrtgegvy dmedlaratd kmagfiaala aeykpsevig lgysnganim anlliekgrv
      121 fdkaallhpl vpfrpkdnpa legakilita grmdpicppd ltealaqyfe rqkadvelvw
      181 hagghelrqt elaavqslla y
//
LOCUS       WP_176026526             337 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Brucella intermedia].
ACCESSION   WP_176026526
VERSION     WP_176026526.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..337
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37488
     Region          6..194
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(9,11,101)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(48,100..101)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            99..101
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 misvsiivpv ysgeaylrql cqrvafvrar lidngapfev selifvedga rdasgaiidd
       61 lgteydwvkp fhlsrnygqh aatvagimks sgdwvvtmde dlqhppeeie gllakavklg
      121 gdvvyanpee avhqsfmrdw tsktfkslmv rlsgnrnitv fnsfrlirgs iareasqacg
      181 hstyfdmtls wftqrvsnvt mllkderyie tgksgyslks lfsharrllf stqvkalrig
      241 saigglavcl aflfsfiviv vklidpsiip vtgwpslmit imffggvsif ltglvieyis
      301 ilvmethgkp lynfvdrssd klladyfrgr ltpenee
//
LOCUS       WP_176026477             243 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Brucella intermedia].
ACCESSION   WP_176026477
VERSION     WP_176026477.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 243)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19108954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..243
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26511
     Region          19..191
                     /region_name="NUDIX_AcylCoAdiphos_Nudt19"
                     /note="Nucleoside diphosphate-linked moiety X)) motif 19;
                     cd18870"
                     /db_xref="CDD:467582"
ORIGIN      
        1 mvqlpsspik agkalrprda aslllvdrsg stprilmgrr haslafmpgk fvfpggrtdp
       61 mdgaigatae lhnndvakll agmgaraslr raralglcai retfeetglr igqaasapvi
      121 lpahrdwsaf fdngmipals slryfaravt ppdnvrrfdt rffiafrdhi peldgqplvp
      181 sgeledldwv sidqidrldv ahitqailke aralltnads elpatlpvvq yckrhgrfvr
      241 evi
//
LOCUS       WP_176026642             199 aa            linear   BCT 11-JAN-2025
DEFINITION  nucleoside deaminase [Brucella intermedia].
ACCESSION   WP_176026642
VERSION     WP_176026642.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..199
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22652
     Region          21..>128
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mqtnelklle klidvieqdi ipltergvae gnkvfgaall rksdlslvla etnnetenpl
       61 whgevhtlkr fyempengrp dtkdmvflst hepcsmclsa itwsgfdnfy ylfshedsrd
      121 afsiprdlki lkevftlepg gynrdnafwh shsipkmvas lpdadrlrlr kkldaifaky
      181 delsdtyqss kdgnaipln
//
LOCUS       WP_176026684             326 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Brucella].
ACCESSION   WP_176026684
VERSION     WP_176026684.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..326
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=34824
     Region          43..324
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 madtalkant asrdskapav nslsavilgi alvgllaapf mvypiflmkm lcfalfasaf
       61 nlllgytgil sfghaaffgg aayitahtvk vwgvtpelgl vlgvlaaaal glvigylair
      121 rqgiystmit lalaqmffff clqaafthge dglqgvprgy lfgiidlnqp mtmyyfvlav
      181 fvlgvfviwr iinspfgmil ksvrenenra islgysvnry klaafvmsaa laglagglka
      241 lvfqfatltd vgwqmsgevi lmtllggigt ligpivgaaf vvalqnylat sdfpvtivtg
      301 vifmacvllf rkgivgefyg wlerrk
//
LOCUS       WP_176026706            1055 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Brucella intermedia].
ACCESSION   WP_176026706
VERSION     WP_176026706.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 1055)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1055)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1055
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..1055
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=111949
     Region          1..1034
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 miselfirrt rlaivisiii siagaiaifs lpiqqypqit pptvnvsasy pgasaeviad
       61 vvggpletai ngvdgmmyms stssnagqys lsvtfevgtd pelaqinvqn raqlaisrlp
      121 aavaqqgvsv rsrspdfvlg iafyspddsl naleitnfat ttivdalarv pgvgeanvvg
      181 aseysmrvwl npqrmdalgi tvdevsaaiq rqniqatlgq agappmrvgt elqytlvaeg
      241 rlrdteefgn ivvrtgadga kvflrdiarl elgarnyasr asfaghesam lqinqspgan
      301 aiqtatavea elerlssrfp aglqyhvvyd atrfveaslq lttrtlfeaf vivlavtfif
      361 lqdwratlis alaipvsmlg avavlfavgy slnmisllal vlaiglvvdd ailvvenvkh
      421 vledepdipv idatrkamhq itgpiisttl vllavvtpta flegiggqly rqfavtissa
      481 lvlssfvalt lspalaafll rhgqrgyrrg plawfsssme ktregygkiv gvlvkhwvip
      541 vagvvacfal ayfvfvnlpa tflpdedqga lfvdiqlpsa asldrtnliv envrktlset
      601 egvqdvitva gfsilqstst pnsamavaal tpwadretka lqlnsivngl rakfsqvpga
      661 nvavfappai agmgavggld frlqalqgqp peeiaqvvaa llgsinqrpe iagaattfna
      721 nvpqiyvdvd rsraealgls vsdiyaaiga nfgsryvndf tlngrvfqvn lqadsdfrah
      781 sedilklhvr nrsgamvplr svvslttvla pfvitrynla asaqvnavta pgsssgqama
      841 ameqvasevl pegygyewsg lsfqerrssg qetlifalaf lfaylflvaq yeswalpavv
      901 ilslgaallg avagltffgl qnslyvqiam vlliglaakn ailivefake qreagltage
      961 aaragaeqrf ravmmtavsf ilgilplils sgagagarqa vgvtifggmv aatslglllt
     1021 pglyfviqrl aeylperlgg rpdekkdsvs etvqe
//
LOCUS       WP_176026739             151 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NUDIX hydrolase [Brucella].
ACCESSION   WP_176026739
VERSION     WP_176026739.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 151)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..151
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=16382
     Region          13..136
                     /region_name="NUDIX_ADPRase"
                     /note="ADP-ribose pyrophosphatase; cd04673"
                     /db_xref="CDD:467557"
ORIGIN      
        1 mktvpvfpip akvhgvslic rregrfllve rgkepwkgwl afpggsieag etpeqaaire
       61 lkeetaldak alshvitvdl alegkayars yylsvfralh vsgreiagdd aasihwltie
      121 emalakvtds tldvarsvae tedkcpdinp v
//
LOCUS       WP_176026811             217 aa            linear   BCT 11-JAN-2025
DEFINITION  YitT family protein [Brucella intermedia].
ACCESSION   WP_176026811
VERSION     WP_176026811.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441691
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..217
                     /product="YitT family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=23359
     Region          28..>204
                     /region_name="YitT"
                     /note="Uncharacterized membrane-anchored protein YitT,
                     contains DUF161 and DUF2179 domains [Function unknown];
                     COG1284"
                     /db_xref="CDD:440895"
ORIGIN      
        1 madiadnaap lidasksaap drhrlyedam amligtsfia lgitlysqat lmtgstagia
       61 lliqyatgae fgllyflinl pfyyfavrrm gwaftirtfv avammsgfar lmplsvdfss
      121 vhplfaalmg gtligmgvla lfrhrsgvgg vnilalylqd tygiragwfq lgldgvimla
      181 slffipwenm mlslvgaiam nliiainhkp grylgis
//
LOCUS       WP_176026807             568 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase [Brucella
            intermedia].
ACCESSION   WP_176026807
VERSION     WP_176026807.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..568
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=61322
     Region          36..373
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          456..565
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mseapeyanq elperesmef dvvivgagpa glaaairlkq anpelsvvvl ekggevgahi
       61 lsgavvdpvg idqllpgwre eeghpfktpv tadhflvlgp agsvrlpnfa mpplmnnhgn
      121 yivslgnvcr wlgtkaeelg veiypgfaat evlyndegav igvatgdmgv erdgthgpny
      181 trgmallgky tlvgegargs lakqliskfk ldegrepaky giglkelwqv dpsrhkpglv
      241 qhsfgwpldm ktgggsflyh lednmvavgf vlhlnyknpy lspfeefqrf kthpairdvf
      301 eggkrlsyga raiteggfqs vpklsfpgga ligcsaglvn vprikgshna vlsgilaadk
      361 iaeaiaagra ndepveiens wrssligkdl krvrnvkplw skfgtivgva lggldmwtnq
      421 lfgfsifgtl khgktdarsl epaakhtkid ypkpdgvltf drlssvflsn tnhdenepvh
      481 lqvadmklqq tsehdvfagp strycpagvy ewvdadgnaa adpqakdvrf vinaqncvhc
      541 ktcdikdpnq ninwvppqgg egpvyvnm
//
LOCUS       WP_176026814             124 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF423 domain-containing protein [Brucella intermedia].
ACCESSION   WP_176026814
VERSION     WP_176026814.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006411
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..124
                     /product="DUF423 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=12685
     Region          <47..124
                     /region_name="YgdD"
                     /note="Uncharacterized membrane protein YgdD,
                     TMEM256/DUF423 family [Function unknown]; COG2363"
                     /db_xref="CDD:441930"
ORIGIN      
        1 mqkrsdswpq nvlfstlagl cgafaiaaya gaahggenhl gniaplllgh apaflalsli
       61 vpgsraaylg gallalglal fcgdlfmrdm tgdrlfpmaa ptggslmilg wlvvavagwf
      121 srtk
//
LOCUS       WP_176026909             410 aa            linear   BCT 11-JAN-2025
DEFINITION  M48 family metallopeptidase [Aquimarina sp. TRL1].
ACCESSION   WP_176026909
VERSION     WP_176026909.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Bode,W., Grams,F., Reinemer,P., Gomis-Ruth,F.X., Baumann,U.,
            McKay,D.B. and Stocker,W.
  TITLE     The metzincin-superfamily of zinc-peptidases
  JOURNAL   Adv Exp Med Biol 389, 1-11 (1996)
   PUBMED   8860988
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Stocker,W. and Bode,W.
  TITLE     Structural features of a superfamily of zinc-endopeptidases: the
            metzincins
  JOURNAL   Curr Opin Struct Biol 5 (3), 383-390 (1995)
   PUBMED   7583637
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..410
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46834
     Region          8..410
                     /region_name="M48A_Zmpste24p_like"
                     /note="Peptidase M48 subfamily A, a type 1 CaaX
                     endopeptidase; cd07343"
                     /db_xref="CDD:320702"
     Site            order(276..277,280,354,358,398)
                     /site_type="active"
                     /db_xref="CDD:320702"
     Site            order(276,280,354,398)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320702"
ORIGIN      
        1 mtpnllfyll imilvvvflf dtildilnas hynnkipdel kdiypeeeyq ksiayktmnf
       61 rfkivqssit liatllfffl dgfswldtia rsistnptii sliffgiimv asdilsipas
      121 yyrtfvieek fgfnrtstkt ffidkikevl miifigggil flviwfyqlt geqfwiyswl
      181 lislftlcmn mfytkiivpl fnkqtplaag elkdiieays ekvgfrlkni fvidgskrst
      241 kanayfsglg sekritlydt liknlsneei vavlahevgh ykkkhiiynl vlsiivtgit
      301 lwilslfinn pilsealgve qpsfhiglva fgvlyspise itglvmnyis rafeyqaddf
      361 aketynahal isslkklskn nlsnltphpa tvfvhyshpt llqrirnlnk
//
LOCUS       WP_176026911             155 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Fur family transcriptional regulator [Aquimarina].
ACCESSION   WP_176026911
VERSION     WP_176026911.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..155
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18326
     Region          15..149
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mgnksntqnd qnivknvfts fleekghrkt peryailqei yesddhfdie slyikmknkn
       61 yrvsratlyn tiellmeckl vrkhqfgqsq aqyeksyfdr qhdhliltds gevlefcdpr
      121 iqsikktiee ifevditnhs lyfygtkkks tnqdn
//
LOCUS       WP_176026746             269 aa            linear   BCT 11-JAN-2025
DEFINITION  class II glutamine amidotransferase [Brucella intermedia].
ACCESSION   WP_176026746
VERSION     WP_176026746.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Zalkin,H. and Smith,J.L.
  TITLE     Enzymes utilizing glutamine as an amide donor
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 72, 87-144 (1998)
   PUBMED   9559052
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Zalkin,H.
  TITLE     The amidotransferases
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 66, 203-309 (1993)
   PUBMED   8430515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000620
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..269
                     /product="class II glutamine amidotransferase"
                     /EC_number="2.4.2.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006541 - glutamine metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29507
     Region          2..253
                     /region_name="YafJ"
                     /note="Predicted glutamine amidotransferase YafJ [General
                     function prediction only]; COG0121"
                     /db_xref="CDD:439891"
ORIGIN      
        1 mcrwaaylgp etylediiss pchslvaqsh daheaktrtn gdgfgvawyg hrdepglyrd
       61 ilpawsdqnl rslarqirsr lflahvrast ggltsrsnch pfvsgrwsfm hngqighfdr
      121 lrrrleshls daiygqkhga tdselifllm lefgldndpv lamkrmvatv vekavrggvp
      181 pflrltaafs dgsqlyairy atdafaptly tatlggssgi cvvsepldge aanwmavpan
      241 sfvtvsrqgr iaieafeepi srpqdavtv
//
LOCUS       WP_176026959             134 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: rhodanese-like domain-containing protein
            [Aquimarina].
ACCESSION   WP_176026959
VERSION     WP_176026959.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..134
                     /product="rhodanese-like domain-containing protein"
                     /calculated_mol_wt=15146
     Region          27..130
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
ORIGIN      
        1 mnlrffptil lclllvncnt tpqkdtavik visveemtsl leaekvqlid vrtpreyasg
       61 hiegainidv ndkdfekkiq qidkskpvav yckrgrrsnk catymekagy tkvydlkggl
      121 tkwtyegkpv lmke
//
LOCUS       WP_176026965             464 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: anthranilate synthase component I family protein
            [Aquimarina].
ACCESSION   WP_176026965
VERSION     WP_176026965.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Kerbarh,O., Bulloch,E.M., Payne,R.J., Sahr,T., Rebeille,F. and
            Abell,C.
  TITLE     Mechanistic and inhibition studies of chorismate-utilizing enzymes
  JOURNAL   Biochem Soc Trans 33 (Pt 4), 763-766 (2005)
   PUBMED   16042594
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Dosselaere,F. and Vanderleyden,J.
  TITLE     A metabolic node in action: chorismate-utilizing enzymes in
            microorganisms
  JOURNAL   Crit Rev Microbiol 27 (2), 75-131 (2001)
   PUBMED   11450855
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414943
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..464
                     /product="anthranilate synthase component I family
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52791
     Region          5..460
                     /region_name="TrpE"
                     /note="Anthranilate/para-aminobenzoate synthases component
                     I [Amino acid transport and metabolism, Coenzyme transport
                     and metabolism]; COG0147"
                     /db_xref="CDD:439917"
ORIGIN      
        1 myklitdykq iladtitpvs vylkirdrfp nslllessdy rgtensfsyi cfnpiasiki
       61 enetiyqsfp dkttkelpit ettnvpqlie qfgnnfevse sdfkfinngl fgyisydavr
      121 yfenisitkk egsleipdmi ynvyqniiai nhfnneayif shcyhtdsni aeiesllqvk
      181 nfasynfttq getvsnlnde eykkhvalak khcqrgdvfq lvlskrftqe fkgdefnvyr
      241 alrsvnpspy lfyfdygdfk ifgsspeaql vvkddiaeih piagtfkrtg ndeqdaelak
      301 klaadekena ehvmlvdlar ndlsrngnnv tvetyrevqf yshvihlvsk vtgkkhadtt
      361 tmqvvadtfp agtlsgapkh ramqliekye tvnrdfygga igfmdfsgnf nhaimirtfl
      421 sknhklhwqa gaglvnesne eselqevynk lgaltkalkl aesi
//
LOCUS       WP_176026962             173 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TlpA disulfide reductase family protein [Aquimarina].
ACCESSION   WP_176026962
VERSION     WP_176026962.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..173
                     /product="TlpA disulfide reductase family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=19869
     Region          55..156
                     /region_name="TlpA_like_family"
                     /note="TlpA-like family; composed of TlpA, ResA, DsbE and
                     similar proteins. TlpA, ResA and DsbE are bacterial
                     protein disulfide reductases with important roles in
                     cytochrome maturation. They are membrane-anchored proteins
                     with a soluble TRX domain containing a...; cd02966"
                     /db_xref="CDD:239264"
     Site            order(67,70)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239264"
ORIGIN      
        1 mkrsvlliai illfsgckge qqltmtpkev lvkggveipi ydfksfesll hiddgkvrli
       61 nfwatwckpc iaelpyfeli nseykekgve vllvsldlpt dvesklipfl kkqqikskvv
      121 llddpdantw ipkvseewsg sipatiiykg ktryfyersf tynelktelr kmm
//
LOCUS       WP_176026992              63 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Aquimarina].
ACCESSION   WP_176026992
VERSION     WP_176026992.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 63)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 63)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..63
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..63
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7066
     Region          1..63
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 mnkgtvkffn etkgfgfiid edskkehfvh isgvldeire gdevefelre grkglnavnv
       61 kvi
//
LOCUS       WP_176027024             258 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: zinc ribbon domain-containing protein [Aquimarina].
ACCESSION   WP_176027024
VERSION     WP_176027024.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Rigden,D.J.
  TITLE     Ab initio modeling led annotation suggests nucleic acid binding
            function for many DUFs
  JOURNAL   OMICS 15 (7-8), 431-438 (2011)
   PUBMED   21348639
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446337
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..258
                     /product="zinc ribbon domain-containing protein"
                     /calculated_mol_wt=29717
     Region          7..243
                     /region_name="DR0291"
                     /note="Predicted nucleic acid-binding protein DR0291,
                     contains C4-type Zn-ribbon domain [General function
                     prediction only]; COG1579"
                     /db_xref="CDD:441187"
ORIGIN      
        1 makkeitveq klralydlql idsrvdeirn vrgelpleve dledevagln krldklntdl
       61 dtideniknk knlieeakal ikkygeqqkn vrnnreynal skeiefqele iqlsekhike
      121 fkaqivqkne iikqtkekvt dreahlahkk geldailaet ekeeqaliak ssdyqrdiee
      181 rlitayhrir knvknglavv piergasggs fftippqvqm eiatrkkiit dehsgrilvd
      241 pelareekek mqaifakl
//
LOCUS       WP_176027096             786 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Aquimarina sp. TRL1].
ACCESSION   WP_176027096
VERSION     WP_176027096.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 786)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20710189
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..786
                     /product="TonB-dependent receptor"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87034
     Region          26..110
                     /region_name="CarbopepD_reg_2"
                     /note="CarboxypepD_reg-like domain; pfam13715"
                     /db_xref="CDD:433425"
     Region          97..711
                     /region_name="FepA"
                     /note="Outer membrane receptor for ferrienterochelin and
                     colicins [Inorganic ion transport and metabolism];
                     COG4771"
                     /db_xref="CDD:443803"
ORIGIN      
        1 mknivfclli lvsaatikaq ennfiisgkv qskelpvpfa tvyiengtvg tntdingnyk
       61 leipagnvvl vvqsqgyrtq kkeinntqse nitidfslve dalgleevvv satrnrverk
      121 tapvvvssik prlltatqsl sladglnyap gvrietncqn cgftqvrlng ldggytqill
      181 nsrpvftsll gvygleqipt niidrvevvr sggsalygsn aiagtinvit kdpilntwei
      241 gsnlsvidgd aldknmtfnv ttvaddltsg vtlygayrnr deydanndgf teitelrntt
      301 vgtkafmkpn ersrvsinln aireyrrggd rldlapqftd iteeldhdtf iggidyeins
      361 kdntnkfqly tsasytnrds yygglggart hqdsitanna fgttkdlawi ngaqytkyfk
      421 nedvlttgie ynitntedvi sgykrmidqs vnsfgayaqy ewkpsekfta llgtrldniq
      481 vdgdytiggi ardvdvsqta lsprltisyl lteklrlrgg yargfrapqa fnedlhissv
      541 ggepqfvils dkldaeysna ftsslnyskt idllqidfll egfytiiedp ftlistgavl
      601 engsileevr ngenatvfgt nfefglspdp qwrfqlggtv qrteynepql lfesdgtpge
      661 sdivieefvr vpnlygylna twlpnkkfnv dvtgtysgem ivplvvsdtg flqlnevhpf
      721 fdlniklesh idfnenfmit ftggvknlfn syqddfdtgp trdsdyiygp nlprtffvgi
      781 klgknh
//
LOCUS       WP_176027130             227 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Aquimarina].
ACCESSION   WP_176027130
VERSION     WP_176027130.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..227
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25724
     Region          143..223
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mdinytpldn pvwyslqqth helgvfykdi afyhpdfcpf ggvfkpsemi talseyskht
       61 tdfyvvgtsp scpphltvck elicnqmvld spipiihtht ttalgtehhq dlfdlvntvq
      121 pgyfkkytcr mgqyygiyid nilvavtger mkmnqftevs avvthpdhtg ngyakqlvak
      181 tanaifaqnk ipylhvastn igairlyekl gfrtrrqisf wqlslth
//
LOCUS       WP_176027102             205 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Aquimarina].
ACCESSION   WP_176027102
VERSION     WP_176027102.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..205
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=23174
     Region          10..200
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mvlkdildtn pklyktlkik geekkyapge sigtqeanqn stafilkgvf kvtlkgenpl
       61 llyhidaksq giisfmnfyn dtirtsvtai knsrllwvpn tdilrlgnsy pllkntmlss
      121 yhynnqellq amdtiisssi ekrfidyllk kssiygtnkl yipwneiasd lqvskttvfk
      181 vvkrlkttkq itlsggqivl nrfsv
//
LOCUS       WP_176027151             243 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: thioesterase II family protein [Aquimarina].
ACCESSION   WP_176027151
VERSION     WP_176027151.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..243
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=27737
     Region          1..237
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mkiialpfag gnkysfrkle khvppsiqwi tlelpgrgsr fkesrledis lmiedllrqi
       61 kphieespym iyghsmgtll gyeltkalmq lsyklpeclf ftgrgapnkv tftkkstlpk
      121 dvfwkeveem gglpkelley edlldlnypi lkgdfkaied yvftpmtslf pmplyvcmge
      181 eeigegpgkt sidcikawne ktdapqkiqw mhgdhffilk npkeivdriv nafheatgvi
      241 anf
//
LOCUS       WP_176027154             423 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Aquimarina sp. TRL1].
ACCESSION   WP_176027154
VERSION     WP_176027154.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..423
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46599
     Region          13..405
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(14..15,18..19,22,55,110..111,113..115,118,138,
                     141..142,145,220,223..224,227..229,232,254,258,311..312,
                     316,320,336,339..340,343..344,347)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mkkyitylsl lmfslmgtdl tdfalsiwil dqpdgsisly sfvwfceaap avflapvigs
       61 lidrwnkkkm iiygqlvagi gsmilmtlhy lgqlhpwhim ivagvgsias tfvfqafyvs
      121 tkalvpkdql vraqglsstl natiqmglpi vapilyklig msniflfdgi tfftsviafs
      181 ilsfvvveis sekfsmkndy kvvkefvkqq kgflylysff flinflvgli tvlftplild
      241 fsneyvlglv lacvgvgsli gggamaskkt fnnpiqiiiw anvfvglili sffiqvnpwi
      301 lgiggmmila lisvsaivne affqtvvptk ilgrltgfsg ffigtaapls fllsgfvvdq
      361 lnhffkanti dfmnhfpgts ittsivvvfv iagslltils liyrrnpnlk kldalykial
      421 ekk
//
LOCUS       WP_176027170             309 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GlxA family transcriptional regulator [Aquimarina].
ACCESSION   WP_176027170
VERSION     WP_176027170.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..309
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35056
     Region          8..309
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 messkkttly fyvtdqvhll dlggvlhvfq eaidlgfpyq lefisssqki kssaglwlsg
       61 iklftevslt qndfifipgf sshdtefsfp ttafndwlia khnlgctics icsgafilan
      121 sgilnhlqct thwslidrlk keyptlhvkk dvlfteenri ytsagivtgi dlalyliekr
      181 hgkevaikia kelvvykrrk gtesqesvyl qhrnhideki hmvqdwiihn lektatindl
      241 aalvnisprn ltrifkkqtg ttiaayrtki rvekakslli hsdhkiayia tlcgfkttkq
      301 lqhilknhl
//
LOCUS       WP_176027178             245 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Aquimarina sp. TRL1].
ACCESSION   WP_176027178
VERSION     WP_176027178.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 245)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440744
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..245
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27812
     Region          16..233
                     /region_name="COG1223"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440836"
ORIGIN      
        1 mtlsdlyfee egtidlndit fdaegkekid qfikeyshae alkqynlpin nklfffghtg
       61 cgktmtakal akalgkkiiv vnlgaivssr lgetaknitt lfkkvtrqgs ilfldefdsl
      121 gkirdyddtd ssemkrivnt liqlidylpd naiiiaatnq shvidtallr rfeikihfql
      181 phhqlldsyy nhildkypak frnikreydi sfaeakvlai navkkqviee eekkkaalin
      241 initn
//
LOCUS       WP_176027262             425 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: replication-associated recombination protein A
            [Aquimarina].
ACCESSION   WP_176027262
VERSION     WP_176027262.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..425
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=47370
     Region          1..424
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 mnkplaerir pktleaylsq ehligdngsl tqqikrgmip slilwgppgv gkttlaniis
       61 sesgrpfytl sainsgvkdv reviekakqs gglftaknpi lfideihrfs ksqqdsllga
      121 vekgwitlvg attenpsfev ipallsrcqv yilnafgkee leallhramk edefmaskni
      181 tlsetdallr lsggdarkll nifelivssq esdsiqitnd lvlklvqqnt vrydktgeqh
      241 ydiisafiks irgsdpnaav ywlarmiegg edvkfiarrl iilasedign anptaliman
      301 ntfqavttig fpeariilsq caiylatsak snasymainh aqqlvkqtgd lsvplhirna
      361 ptklmkelgy genyqyahnh kdnfvsqefl peeisntkly epgdnqrena frsflknrwk
      421 dkyny
//
LOCUS       WP_176027376             108 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: roadblock/LC7 domain-containing protein [Aquimarina].
ACCESSION   WP_176027376
VERSION     WP_176027376.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     Dynein light chains of the Roadblock/LC7 group belong to an ancient
            protein superfamily implicated in NTPase regulation
  JOURNAL   Curr Biol 10 (21), R774-R776 (2000)
   PUBMED   11084347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..108
                     /product="roadblock/LC7 domain-containing protein"
                     /calculated_mol_wt=11623
     Region          8..100
                     /region_name="COG2018"
                     /note="Predicted regulator of Ras-like GTPase activity,
                     Roadblock/LC7/MglB family [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:441621"
ORIGIN      
        1 msektplqld kvledtgada allldlegnv isashvdyeq niaamvqmiy amgsdlsqdl
       61 kngeleqllv kasagffvvn khgedaiivi fskevskigr clkmintl
//
LOCUS       WP_176027414             323 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Aquimarina sp. TRL1].
ACCESSION   WP_176027414
VERSION     WP_176027414.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..323
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36682
     Region          5..300
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mggknfalmg aagyiapkhl kairetnnnl iaaldkfdsv gildsyfpnt dffveferfd
       61 rhieklqrrk gihtdyvsic tpnylhdshi rmalrrgsda icekplvlnp wnikplidie
      121 kesgnrvhti lqlrlhpsil alkeqvdngp kdkiydidlt yltsrgswyn sswkgdvsks
      181 ggvatnigvh ffdmlcwifg gvtdnrvhlh tkdsaagyle lerarvrwfl sidyanipne
      241 ikekgqrtyr sievdgnaie fstgftelht esykgilrge gyglvdarps ieiihdvrea
      301 eivslkgdyh pflkkpilek qya
//
LOCUS       WP_176027442             325 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: M23 family metallopeptidase [Aquimarina].
ACCESSION   WP_176027442
VERSION     WP_176027442.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..325
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36802
     Region          <147..300
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mskvkyyyds etlsyrkiey kkghkiglai lgvlgaflag fillviylni pqlqtpkeka
       61 ykreldnmkl qfellnkrlk rdeailqeva erddniyrly fgakpipkel rnagfggvnr
      121 yrdlegfdns eiiiratkqi dkitkqivvq sksldeiakl aeqkedllst ipaiqpians
      181 dlkrmasgyg wrsdpftkak kfhygmdfsa ntgtpvyasg ngvvtradsn ssgygkhiri
      241 dhgfnyvsly ahlskynvek gqkvkrgdii gfvgstgrsv aphlhyeifk gkerinprnf
      301 yygsltseef nemlkassli netld
//
LOCUS       WP_176027468            1037 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Aquimarina sp. TRL1].
ACCESSION   WP_176027468
VERSION     WP_176027468.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..1037
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113825
     Region          1..1024
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnltkfsisq nrvvlsilgv vlimgmafyq slsrdsmppy tvrvativss fpgasperve
       61 elvtdkiekv vqelpelknv kstsrtglsv vkvelkmdvt peklqsvwdr lrrkldalkg
      121 lpsnvepmld ddgigevfgi avgitsdgys yremkeyadd lrddlikled aakveingdq
      181 eervfvmfdn tklkayglta gklkgiinnt nilssggein vederiilep tgnfnnlsdi
      241 ksmlipigqg dqvvaledit tirkgyinpp kqkvsingke aislhvslke ganviklgee
      301 idqvlkkweg klpvglevqr iasidsyidl kindfvgnli qsivivlavm llflgirtgl
      361 iiaslipmvt ittimimgll gtglnqitla alimalgmmv dnaivvaesv mvkmeqgvsv
      421 ktaaidscse lftpllistl ttsaaflaff laesvmgdim gplfvvisia llsswiials
      481 ivtllcvffl kikkkekdqk psfldklins lktkykalim falswkksvl igivvlflls
      541 ifgftklafv ffpdsdrnmi tmdinlpegt kisttqktvd aieayirkel evteqrsegi
      601 anwaafigkg psaydlgysa deansnyahi vintssftvn aemvkqlday cfntfpnadi
      661 kvgflgsggg gvpieikvsg dnpdrlavis eaiktrlsgi ngtknikddw gpkgkkfvie
      721 idqnkaqsag itnqdiatsl qtvldgfkag efregdkfip ivmmsdqgke qtlasletln
      781 vyaqnsgksv pllqvanvip kwqyskikrl dltrtmiiss elteegnask imsemkpwle
      841 eqkkewgdey tytlggdaen taenmgavak ylplagfiiv mlliiqfnsf rkmtmivsti
      901 plgvigmvig llvfrvpfgf maflgiisla givinnaivl vdrieieeke lqripqdaii
      961 gaclqrfrpi llatfttvlg liplylggge lwepmavtim igllfgtvit lvfipafysv
     1021 lykvdysdyt fneslle
//
LOCUS       WP_176027535             186 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Aquimarina sp. TRL1].
ACCESSION   WP_176027535
VERSION     WP_176027535.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..186
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22130
     Region          1..155
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mekdqviitg iingnekilt rfydeniryi qgyvlrnhgk pedvedvfqd almvlyqkln
       61 sgifeltgsi rtyfygickn iwrnqlrrkp iftdgkhmle eitydsllad ienqereqfy
      121 kkyfqqlstd nkqllylffe gksmkeiaqi tgyseiytrk kkflakkkll emmeqdplyn
      181 elravs
//
LOCUS       WP_176027518             147 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: molybdenum cofactor biosynthesis protein MoaE
            [Aquimarina].
ACCESSION   WP_176027518
VERSION     WP_176027518.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..147
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=16595
     Region          10..143
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 mnkknlknif vegaistkfi gesiakhqtk ttigahdifl gqvradiidg kkvtaieyta
       61 yeemanlkah eireetfdkf dltcmhvyhs kgivksgeic lfvfvsspkr keafraieyl
      121 vneikanipv fgkeifddas hqwkvnt
//
LOCUS       WP_176027569             684 aa            linear   BCT 11-JAN-2025
DEFINITION  leucine-rich repeat domain-containing protein [Aquimarina sp.
            TRL1].
ACCESSION   WP_176027569
VERSION     WP_176027569.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   3  (residues 1 to 684)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..684
                     /product="leucine-rich repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=78751
     Region          396..>650
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          425..447
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          490..531
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          532..550
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          551..572
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          573..594
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          595..616
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          617..638
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
ORIGIN      
        1 mknqirdiee rlgvtlekyd yknehqvnty stwtkstnir elvlkdicie nihvllpfsk
       61 hlhtlkltnc tvhniselfn feslvnitld nvtitnveev aqgnssnmpy egflqvvdlk
      121 nmkvdhlsvl lpmaknltyi yltnciirnf yeinlfpkly hltldkvtih knerdhyhti
      181 ipdrkfwfly lknmeienis dfssisetii didiinckig sirelhqfpa lkcltidalt
      241 tvddvkpgtp nlpfklkecv ipateeeatv etfdleklga iasciqtltf kndnisnidy
      301 lknltslkai kfdrvtarlk dflpiaaqii sldfsestik nssqiqhfkn levlkidadt
      361 nkqsfgdfkm llplkdqvkk fdlwefsdnh mrnlelieqf talesvfilr askkvakrif
      421 tlsglkklsi hirakkknvf dvkalkniee lyieseepir lkggkhlehl kvlsldsycn
      481 skkihqiknl qylkitpsvn vnelpaiptl tklkieahed yeilgleqfp nltelsiegt
      541 nkirlgylpk lkvldvsstf pqeidflnel pnleklslen ncltevkgld tltnlkmlni
      601 sentiqnidg lanlknleql nlyeneisei rvlntlpslk qvnvagntie kpevydqlnk
      661 peiavfyglp kvpfwiwkdq dfel
//
LOCUS       WP_176027584             376 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Aquimarina sp. TRL1].
ACCESSION   WP_176027584
VERSION     WP_176027584.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..376
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=42757
     Region          46..376
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 mgikisntkk kdrressfdl ssiltqeitl fgnafntkkk eqwyaelsvl lksgidlrng
       61 lellsdtqkk ekdqklmkfm lsqlvtgtpf seilkhnknf tdyeyyairi geqtgelaqi
      121 tlelsdfykr knelrreiva altypvivmc tamiviafml ryvvpmfvdi fkqnnvdlpg
      181 vtkgiinfsd fisihgillf gaivvcigvl ffvskkqwyr kilgsvqlki pilgnyfqki
      241 ymaqftqais lltsakvpmv esidlvknmi nfyplqqgly ktkqlilagd alsasfaksp
      301 ifdkkmiamv rvaeetnqte fifqklneqy nqqvkyqsqv isnvlnpilt lfvgvivgvi
      361 liamylpmfr lssvig
//
LOCUS       WP_176027613             142 aa            linear   BCT 11-JAN-2025
DEFINITION  SMI1/KNR4 family protein [Aquimarina sp. TRL1].
ACCESSION   WP_176027613
VERSION     WP_176027613.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10558574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..142
                     /product="SMI1/KNR4 family protein"
                     /GO_process="GO:0042546 - cell wall biogenesis [Evidence
                     IEA]"
                     /calculated_mol_wt=16741
     Region          7..126
                     /region_name="SMI1_KNR4"
                     /note="SMI1 / KNR4 family (SUKH-1); pfam09346"
                     /db_xref="CDD:430545"
ORIGIN      
        1 mpfsieekyi ieteselnvk fpiefktwmm ksnggeliih efefelypff dksdkkrisr
       61 tcnhighetk narewngfpd ngiaigsdgf gnqlilshng nrnltdelhf wnhetrqvek
      121 iaesinklyi ekslfwnrkf nk
//
LOCUS       WP_176027708            3471 aa            linear   BCT 11-JAN-2025
DEFINITION  RHS repeat domain-containing protein [Aquimarina sp. TRL1].
ACCESSION   WP_176027708
VERSION     WP_176027708.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 3471)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..3471
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..3471
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
                     /calculated_mol_wt=383172
     Region          2265..3213
                     /region_name="RhsA"
                     /note="Uncharacterized conserved protein RhaS, contains 28
                     RHS repeats [General function prediction only]; COG3209"
                     /db_xref="CDD:442442"
ORIGIN      
        1 mgkrihhlfv cciflffids gysqdkviyd psviagains gtglefrpdl smfssgvtvs
       61 sgtdlrlsva sdqppygwfs yevrlrvtpr lstgvfdptq syvvtllvss nsvagsgqhs
      121 idvrehrigd sygahivvee gryqnlstss vdvngyipen itlsaslwvs hygvlsdmip
      181 tigatfdgvs nelsfawdni sgadhyqlew swvdsygdrf ntslgadqia fstldfkgns
      241 triqtkatgy sipliyskgy liyrvravgh ytsniskyqy grwssgvlpk tsvsdwpdyy
      301 titsdheegk nwqfqasyae egkkkevvsy fdgtlrnrqt vtklntddhv vvgeviydaq
      361 grsaievlpv pttwsqlgyv rdfnqssllp gapydyedfd ldhqnildqp ttdkgmdpss
      421 gaskyyglan dlttpfrsri adagghpfsq ieympdntgr irrksgvgit hqlgrgkeme
      481 yyygtpeqke lnrlfgynvg hhghykknlv idpngqasvs yldpqgrtia talsgdaagt
      541 gltglseeqd tslhqemtvd llgklsrgak dtaldntikt stggfgplyd aleyggtkvs
      601 afdrgyrfny tlsnapffed ncspttvvqy pfvydleiai edldgvslla tpvvekvdms
      661 rvtsgtfilp eatasvprgs ytiskslsvd realasyada yvarlqdand acyispeevs
      721 nlpvlsfegc fmtcseceaa llsdygsksq yvttqveayd ysslshlsat eleeektrla
      781 avfaiqwdal iracnapcqe gvldggapsd vvsssslscs ishsilrndm kplgqygayr
      841 gavyndqttg gsgiienssv lsifstsnel istrtssgeh nswrnprhea hdpapsgsgl
      901 ytsghyyted gqisyikvkq littrivagq pteeitydpm liegavvres adreyvytep
      961 qnlalvtdfl rddiwqdswt ssllvyhpey cyitynravc gmtstvsggk mnsdgydayl
     1021 gsvksyaaak aagllgsles lsasdpyfrg tipavensts rnaresvire sllsnyngsg
     1081 msamafsygt lvcnsisscd lglgssptaa silgkvdgfs dvskqdqfwn tykanygvak
     1141 qvvqslfsni yarnngcyng cigeqapptt lltvlsgyst svnnqvggli qggaagicad
     1201 lhselykeke krfkpsdnly ssgdnggdiy ndlanftnye yyiatgvcpk ardlemylny
     1261 yfkeygsgip asstyrggyl tpalftdlgg shptdaavei rtnltaankt ldirfyqnnq
     1321 avgtipisvs lpasfsntwq nygagtwqit svkqiyssyd asserfryqv laevtiggtt
     1381 tqeivlsgqt qariaacsit eadgvgeyig dgsgtdisgc nnttrfetal rdvmyeleqr
     1441 gtlnngsvsl nsmssysgsy latffgagaa lwkadgrgty eltvggvtrl tmelgqvldp
     1501 avievitgan vnylyndkgq itqqqlnity readhfpkia tarlyescdv vtgvcrlinl
     1561 lccgdindlv ggdnqviciq nqqaeetfea glltllnegi lnenrldtpy tisspltsdf
     1621 lnntkyreri srytkdipgi nvstdfnscf flrrsnhfee lmlifsadpt adasaiahht
     1681 nstqcgdsnw aifriqqrrs dganvlnigr itkldiqkeg vlafthtdrs tnqeiattgs
     1741 ianllpmrtn tvcqvsgfrp dcqffedppv dcigeaiaea nqfandikhl vnavfrnvdl
     1801 agiginqgrl inlqgypeyt nfiqkvltvk salpcttcyd kffdysikeh vkfsitrtss
     1861 nvyalsinls dihqvsipln vpsgeipkqi dsithssngr ftvvstdlng kqytslhnfr
     1921 gvkindpndh kspilfqffc ntdynatsla qnpdnldnen idgicgdavl ennlehalki
     1981 alnegitsmk enrpvsstif delffgnvnl qkrienhfgl tdptsvydyq fdsaetepiy
     2041 hrfatghiqt rgtmhliltr sggyitsikl sleedffdis eiidieivrs nieltqgvnn
     2101 sisggtfcti nykdslgglk qaknviitfs asdlprtyen qflcdllswp vslvptrivs
     2161 elnenetlst styardlnns kksnppsaks ttiadetipc gptvcippvv eplsctttys
     2221 aytgvmsrig dteaedivsa edfcqyslqy lvadyeyylt klgivstldl yyltisefga
     2281 tefnygypgm rrtykgrsav idlyqahvss sgdsakswta fttdylntsg nedicvprpf
     2341 ftdftevtvt ipddtdcqqf vksvraaytr dvydsyiagk raefiaeyls qaidnavetf
     2401 dmtyydkeyq ytlyyydqsg nllqtvppeg vdrftdtelq asdasgesln srinqhrtnd
     2461 iarenssllp ahelltkyry nslnqlvwqk tpdggitrfa ydelgriias qnanqlaanq
     2521 fsyttydalg riveagaltp tvgisirekt gtlvytatgn vvstrvedqy pqnisrdrve
     2581 vtrtryndls igaaeifetv sdqsiyrstt rnrvagiyyy dqyssttler qydhaifyhy
     2641 dihgnvkelv qhdkqmaltl ddptsgmkrt qyeydlisgn vhrvtyqkgk adqfihqyry
     2701 dadnrivgvs tsdngriwee daryayfshg plartvlgsr qvqgldyayt lqgwlkgvng
     2761 esldptadmg gdgssasdva kdalgyslsy yegdyqsigt ttgssfvysn spglestknl
     2821 yngnikqmvt slidnnesml ssqinhyeyd qlnrikkmqg sqltgmtatp syhssysydk
     2881 ngnlqqlhra tvnsqgsvvd mdalqytykt vtdpetgqqv rsnqlshvdd tiagstfndl
     2941 sdqnpgnysy daigqliedk qegihniewr vdgkvkkirk sngtevsfyy dglgnrigkr
     3001 vlpenkttly srdaqgnvlg vyqantsgav atdmrlkehh iygssrlgie eknialssdq
     3061 avaeatvgnt vgdkryelsn hlgnvmsvis drktatvtgn lttftpdvls fsdyypggml
     3121 lpnrhgnssd yrygfqgqem dneikgegns inykfrmhdp rlnrffavdp ltheypnisp
     3181 yafsenrlin tidreglest fyllglrein gieylvpika fevensitii ggkkihldks
     3241 nnsfiygtdg rwhrmsqeqa nqslyalgdt neevleaing meyadneaka aivhnnievg
     3301 aeyilmvaai ygnlqisraf ksnsitkntk stktpattgi aveqvpkvka qinsrhilns
     3361 dkigaknakt kastvapdei lkrdlddfns gnfkklkdgn idingniygv knegatlfpi
     3421 sgegfmkltq gqikaiklik nvpadklqka atgagistet lnfakefvkk y
//
LOCUS       WP_176027753             422 aa            linear   BCT 11-JAN-2025
DEFINITION  hemolysin family protein [Aquimarina sp. TRL1].
ACCESSION   WP_176027753
VERSION     WP_176027753.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441338
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..422
                     /product="hemolysin family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=48173
     Region          1..422
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
ORIGIN      
        1 mevdilvivf slilsaffsg meiayvssnk ihieiekkqg dflskiltrl tkkpsrfiat
       61 mlvgnnialv iyglfmgkll vrvlsgyype vspsllllfq tiittgiill taeflpkvff
      121 qiysntllkv fsfpayvfyv vftpislfvi wvsdvvlktf fktkgddvrl afsktelgdy
      181 iteqmetvee hdeidseiqi fqnalefsdv rsrevmvprt eiiaievrqs veeisklfie
      241 tglskiivyn stiddvigyv hsfelfkkpk slksvlmpvv fvpetmyvkd vlnlltkkhk
      301 svavvideyg gtsgiitied iveelfgeie dehdtvekve eqleerkyrf sarlevdyln
      361 etykldlpes eyyetlggmi vnhteeipee gdvvrigdfq vdiietsntk ieivelqltp
      421 ee
//
LOCUS       WP_176027766             186 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Aquimarina].
ACCESSION   WP_176027766
VERSION     WP_176027766.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..186
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21863
     Region          6..180
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mdfslnddik lltalkkgcq kafkfiystf yeilcvyiln ftsnreeaed ivqdtllklw
       61 qkresivint slksylfqav ynrfvdnyrr ekkryeildt irlsalnsly teeeqqhesq
      121 kikilqqiie qlppkckeif llskmrglky qqiadelgis iktvenqigi ayqkirvalk
      181 nsnlsf
//
LOCUS       WP_176027746             409 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TolC family protein [Aquimarina].
ACCESSION   WP_176027746
VERSION     WP_176027746.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..409
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47028
     Region          25..407
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrkknmrtti llgmllfqfv csgqtlqeyl keaaannpel qamkyqiqge eekikevgsl
       61 petsvgagyf msepetrtga qkaklsvqqk ipwfgtnask rktqqtksem tkskyevlkr
      121 kiflqieqky yqvyglkatl kvleqrekil dtykelglva vennkastvd ilriniakng
      181 ilnskevikg ailsaesafn qllhrdgfdp lhivdnlfip eeeptmmldd ityhpelity
      241 dyyqevlenq litnkreamp digvgvdyiv veerpdmnfs dngkdivmpm vtfsfplfsk
      301 kyssrskqid lekeavaqkr eatqnvleki mdtaindrit arinyttyqk nideallaee
      361 iirktyetgt idfeevleiq elilefekkk ieaiqayysh sailnylrq
//
LOCUS       WP_176027768             556 aa            linear   BCT 11-JAN-2025
DEFINITION  glycerol-3-phosphate dehydrogenase/oxidase [Aquimarina sp. TRL1].
ACCESSION   WP_176027768
VERSION     WP_176027768.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Austin,D. and Larson,T.J.
  TITLE     Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol
            3-phosphate dehydrogenase of Escherichia coli K-12
  JOURNAL   J Bacteriol 173 (1), 101-107 (1991)
   PUBMED   1987111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..556
                     /product="glycerol-3-phosphate dehydrogenase/oxidase"
                     /EC_number="1.1.-.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0004368 - glycerol-3-phosphate
                     dehydrogenase (quinone) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=62722
     Region          20..>56
                     /region_name="Pyr_redox_2"
                     /note="Pyridine nucleotide-disulphide oxidoreductase;
                     cl39093"
                     /db_xref="CDD:476868"
     Region          40..549
                     /region_name="GlpA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0578"
                     /db_xref="CDD:440343"
ORIGIN      
        1 mknkrqfsvh erasqlkrvt srlfdvviig ggvtgagial daisrglsvc liekndfasg
       61 tsnkstklih gglrylkqle iglvresgre raivhklaph lvvpekmllp lyeggtygkl
      121 mtaiglkvyd fladvsgndr rkmlsvseti eqepllkkeg lqgggyyaey rtddarltie
      181 llkkahvlga evlnycevvs fgyteegnmd tahcldhitn eklmisarff vsatgpwsdv
      241 ikqldtskke ktlqlskgvh iviprdklll rqaiyfdvdd grmifaiprg kvtyigttdt
      301 vytaslkriv itrkdvkyli davnrmfpla eltirdviss wagirplvye agktpselsr
      361 kdeifisktg lvsiaggklt gyrkmaerim ntlfsiddsi gnratkgalt deipltnypl
      421 qsreevvlyr rqlkerlasl gvedeyicwy lvstygkqad kilekithfn neevieklir
      481 aelwygvhhe mvvtlsdffv rrtgylyfei ekiktfrtvv asdlqnylgf diaemahqhq
      541 vldqlltdat tfyete
//
LOCUS       WP_176027809             237 aa            linear   BCT 11-JAN-2025
DEFINITION  tRNA1(Val) (adenine(37)-N6)-methyltransferase [Aquimarina sp.
            TRL1].
ACCESSION   WP_176027809
VERSION     WP_176027809.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..237
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26901
     Region          3..233
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 mskpfvfkrf evhqercamk igtdgvllga wasvsdtvhs ildvgtgtgv ialmmaqrsp
       61 aeivdaleid sdayeqavdn fegspwgdrl fcyhasfqef vteiedsydl iisnppffae
      121 dykttdvkrd larfeealpf ehlihgavhl lneqgklali vpfkeekrii elaaqvslfp
      181 qritrvrgtp dtvlkrslle lgfldkmcee eelviessrh qyteaymklt kdfylkm
//
LOCUS       WP_176027835             123 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: BlaI/MecI/CopY family transcriptional regulator
            [Aquimarina].
ACCESSION   WP_176027835
VERSION     WP_176027835.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..123
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=14298
     Region          1..122
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mklskteeql mkylwkleka fmkdlleeyp epkpatttva tllkrmadkg fvaytlygks
       61 reyyplvekt tyfsthvnsl iknffnnsas qfasfftset nlstaeleel rkivdqeiek
      121 kkk
//
LOCUS       WP_176027839             222 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SCO family protein [Aquimarina].
ACCESSION   WP_176027839
VERSION     WP_176027839.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..222
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25465
     Region          66..221
                     /region_name="Sco1"
                     /note="Cytochrome oxidase Cu insertion factor,
                     SCO1/SenC/PrrC family [Posttranslational modification,
                     protein turnover, chaperones]; COG1999"
                     /db_xref="CDD:441602"
ORIGIN      
        1 mlrffsrykf fgivllvlsa iiisiiysil kptpvlpiye pemvntelvd stvqhirkyh
       61 kiapfsltnq ngktitekey dnkiyvadff fttcqsicpv mtghmkkiqd elmndasvll
      121 lshtvtpdid tvaqlkryak rkgvndtkwn lvtgdkkqiy nlarksylaa ksngdggpyd
      181 mihtenfilv dtkkrirgfy dgtdeeeidr llddieilkk eq
//
LOCUS       WP_176027874             358 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FecR family protein [Aquimarina].
ACCESSION   WP_176027874
VERSION     WP_176027874.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..358
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=41009
     Region          <134..350
                     /region_name="FecR"
                     /note="Periplasmic ferric-dicitrate binding protein FecR,
                     regulates iron transport [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG3712"
                     /db_xref="CDD:442926"
ORIGIN      
        1 mnkkhtyiis keekkelqhr intsirkvqq kekrnrkrff yfssaasvii ligatfiyny
       61 kkssdtlyqy veitninnas ltdgtikviq nnkevislhe enpsityskt gksiqvnnkk
      121 vavsettdth tetfntivvp ygkrsfltls dgskvwlnsg skltyastfk kdkrevhltg
      181 eaifdvahdk erpfhvlthd ydvevlgtvf nvssypedsf tktslksgsv kinygtadff
      241 gkrsslkiip gnqisydrvs rkitrgkedi lacmswrdgv fifhkknlsd iikkvsryyn
      301 idiesdhpei ekltfsgsld lkdsieevld vlkettkfty ikqdqkiiin yknsppmk
//
LOCUS       WP_176027909             796 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: inorganic phosphate transporter [Aquimarina].
ACCESSION   WP_176027909
VERSION     WP_176027909.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..796
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=87463
     Region          4..>211
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 msdiyilmiv alailavadl vvgvsndavn flnsaigska isfrtimiva sigiaagaif
       61 ssglmevark gifvpgefyf deimiifmav mitdillldf fntlgmptst tvsivfellg
      121 aavcvaliki gadsslttsd lghfintkka tqiisgills vavafsvgai vqyvtrllls
      181 fqfekkakwv galfggialt ailyfifikg ikgtsyaksi vdviysggas glldwandff
      241 stsfesvkel akakkdfvki seeagtvslt lrglleiyvl pivgigfvil salsyllisv
      301 fkidiykiii ivgtfalala fagndlvnfi gvpvaawqsy eawsasgvpa hefsmailgk
      361 kvdtptlllf gaglvmvltl wfskkaryva eteinlsreg esrerftpnf lsrgvvrgam
      421 lmsqyasail pasvqakiek qfekpviaia kdkkyempaf dkvraavnlm vagvlisiat
      481 smklplstty vtfmvamgts lsdrawgses avyrvagvfn viggwfftaf iafvasatla
      541 flihlggtvm iaillliavv llvrntlnyr krakaekeed rlkksesssv qgvieesadn
      601 iksfvnrank iygntlesli kydlialkkt kkgiskldae veelrdnify fiknldessv
      661 sasnfyitil gyiqditqsl eyitksghkh vnnnhkklrf nqikdlkeid vqvndlfgki
      721 krifdtrdfd hidtiinekq elydrlnqki dkqvartrte enspknttly fgllletkdl
      781 itatmnllet yrghke
//
LOCUS       WP_176027945             187 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DNA-3-methyladenine glycosylase I [Aquimarina].
ACCESSION   WP_176027945
VERSION     WP_176027945.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..187
                     /product="DNA-3-methyladenine glycosylase I"
                     /EC_number="3.2.2.20"
                     /GO_function="GO:0008725 - DNA-3-methyladenine glycosylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006284 - base-excision repair [Evidence
                     IEA]"
                     /calculated_mol_wt=21659
     Region          1..187
                     /region_name="Tag"
                     /note="3-methyladenine DNA glycosylase Tag [Replication,
                     recombination and repair]; COG2818"
                     /db_xref="CDD:442066"
ORIGIN      
        1 meihrcawcv gdslyeqyhd eewgvplhde qelfeflile tfqaglswit vlkkrenfrn
       61 afdnfdyqki alytddkkqa llqnagiirn klkvnatvsn aqafikiqee fgsfdtyiws
      121 fvnhtpiins wahhkdcpat tdtsdiiskd lkkrgfkfvg stviyafmqa igmvndhvvd
      181 cfrhkev
//
LOCUS       WP_176027949             290 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Aquimarina sp. TRL1].
ACCESSION   WP_176027949
VERSION     WP_176027949.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..290
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31754
     Region          11..192
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mitidpsqvt tgklhgmmlg aigprpiafa stidgdgnpn lspfsffnvf sanppilifs
       61 parrvrdnti khtlenaqet kevvinivny divqqmslss teypkgvnef eksgltmvss
      121 akvapfrvge spvqfeckvn eimpmgnegg agnliicevv lmhvkeevld eagkidqhki
      181 dqvarmggnw ysranmgmfe vpkplttmgi gidalpetik hstvftgndl gklgnvekip
      241 lpeeaiafvd nsteiktkld qdnveeihkf akqylekddi htawnilaak
//
LOCUS       WP_176027960             250 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: hydroxymethylpyrimidine/phosphomethylpyrimidine
            kinase [Aquimarina].
ACCESSION   WP_176027960
VERSION     WP_176027960.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..250
                     /product="hydroxymethylpyrimidine/phosphomethylpyrimidine
                     kinase"
                     /EC_number="2.7.1.49"
                     /EC_number="2.7.4.7"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008902 - hydroxymethylpyrimidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008972 - phosphomethylpyrimidine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009228 - thiamine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009229 - thiamine diphosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=28108
     Region          6..240
                     /region_name="HMPP_kinase"
                     /note="4-amino-5-hydroxymethyl-2-methyl-pyrimidine
                     phosphate kinase (HMPP-kinase) catalyzes two consecutive
                     phosphorylation steps in the thiamine phosphate
                     biosynthesis pathway, leading to the synthesis of vitamin
                     B1. The first step is the phosphorylation of...; cd01169"
                     /db_xref="CDD:238574"
     Site            order(6,13,15..16,18,22,25..26,29,32..37,39,42..46,51..52,
                     54,56..57,60,63,67..68)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238574"
     Site            order(12,24,45,81,208)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238574"
     Site            order(107,144,170,205,207)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238574"
ORIGIN      
        1 mrnrpyviti agfdpsggag lvadsktfdh lkcyglavct antiqddkcf kcchwiekqv
       61 ikrqlqtlle rfdievvkig iiedwellhe iidvltvynd rikivvdpvl rsstnfdfkk
      121 qeeqievfna vlkkitlitp nydeiealfp ekdieetiay isgrtglllk gghrleaigk
      181 delylpsgev ftynpkgknh sekhgsgcvl ssaiaaylar gfslhkavyr gkrytekvlq
      241 snksllgyhg
//
LOCUS       WP_176027964             728 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Aquimarina sp. TRL1].
ACCESSION   WP_176027964
VERSION     WP_176027964.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 728)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..728
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81678
     Region          34..700
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msnkvygiic mlfsvvgiaq ekvqdsikke pekldevlvk avrveadapi tysnvskeel
       61 sgrnlgqdip illnylpgvv ttsdagagvg ytgirvrgsd atrvnvtlng ipfndsesqg
      121 tfwvnlpdfa ssvenlqlqr gvgtstngsg afgaslnllt davsekgyge itnsfgsfgt
      181 rkhtlkystg lldnkvefsg rlsaiasdgy idraasdlks yflqgayitd gtlikaiafg
      241 gheityqswn gvdektlidn rtfnsagqye dengnirfyd nevdnykqdh yqlhwnqkfd
      301 nywssnigln ytygrgyfeq ykededfedy dftpinigge iinttdlirr rwlkndfyvi
      361 nanvnykken ldikaggffs hydgdhfgev iwaqyaggse irdhyysgng rkneftvfgk
      421 ttykvnekws afldlqgrfv tykttgltsd rvalqvdety dffnpkigtt ytidkqnhly
      481 asyaiahrep rrddfengin taeklqdvev gwrlfsdklv lntnayfmwy kdqlvltgai
      541 ddvgepirat sgesyrlgie vdaqvvilkd kllvrpnial sdnknkdfik tegdalvslg
      601 dthisfspqi iagnvieyhp venmtigfls kyvgeqymgn idskkskldd ffvndlnivy
      661 eitgfsvfks vvlsgvvnni fdhkyesngy fytyqddfst pgtitteegv gyypqaginf
      721 llgatlkf
//
LOCUS       WP_176027983             153 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: single-stranded DNA-binding protein [Aquimarina].
ACCESSION   WP_176027983
VERSION     WP_176027983.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Bianco,P.R.
  TITLE     The tale of SSB
  JOURNAL   Prog Biophys Mol Biol 127, 111-118 (2017)
   PUBMED   27838363
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..153
                     /product="single-stranded DNA-binding protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=16980
     Region          5..119
                     /region_name="Ssb"
                     /note="Single-stranded DNA-binding protein [Replication,
                     recombination and repair]; COG0629"
                     /db_xref="CDD:440394"
ORIGIN      
        1 msgtlnkvml ightgdevkm hyfeggncig rfplatndsy vnkstgervv stewhnivvr
       61 nkaaeiceky lkkgdkiyie grlktrkwqd eqgkdryste iqctdftflt pknesgqpgg
      121 smpgmqpqqp aatenpstss ventnaeddd lpf
//
LOCUS       WP_176028010             363 aa            linear   BCT 11-JAN-2025
DEFINITION  adenylate/guanylate cyclase domain-containing protein [Aquimarina
            sp. TRL1].
ACCESSION   WP_176028010
VERSION     WP_176028010.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Sinha,S.C. and Sprang,S.R.
  TITLE     Structures, mechanism, regulation and evolution of class III
            nucleotidyl cyclases
  JOURNAL   Rev Physiol Biochem Pharmacol 157, 105-140 (2006)
   PUBMED   17236651
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163659
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..363
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016849 - phosphorus-oxygen lyase
                     activity [Evidence IEA]"
                     /GO_function="GO:0032555 - purine ribonucleotide binding
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=40883
     Region          5..>138
                     /region_name="NtrB"
                     /note="Signal transduction histidine kinase NtrB, nitrogen
                     specific [Signal transduction mechanisms]; COG3852"
                     /db_xref="CDD:443061"
     Region          <137..358
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 mftvpplfql ilnkqktgyl vvdknlmite sggdqntfaf fkeetlqfpe slldfipely
       61 gyeeylsqlf egkcpeisld ninkttpane lhyvnltilp fhrdntqqet nfilvlisdv
      121 tpkstiqqtl kqqrnelill rqdlkatner lrfivqhyip fevgknllen ktvpklggie
      181 revtvlfadl rnftstcekl hpqktvhmld iyldiatkai slhggvivny mgdaimavfn
      241 apneqknhae ravkaglrik ekamntdats egvpslyfgi gintgiatig nigaewhyqy
      301 taigdmvnva sricgqaken evligeqtlq yikndvtaik lppiklkgks dnmhlyqist
      361 ftk
//
LOCUS       WP_176028021             269 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glycogen/starch synthase [Aquimarina].
ACCESSION   WP_176028021
VERSION     WP_176028021.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10550881
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..269
                     /product="glycogen/starch synthase"
                     /EC_number="2.4.1.21"
                     /GO_function="GO:0004373 - alpha-1,4-glucan
                     glucosyltransferase (UDP-glucose donor) activity [Evidence
                     IEA]"
                     /GO_process="GO:0005978 - glycogen biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30977
     Region          6..236
                     /region_name="Glyco_transf_5"
                     /note="Starch synthase catalytic domain; pfam08323"
                     /db_xref="CDD:400563"
ORIGIN      
        1 mkdkrilyvs sevipylpet eissmsfeap rmvnskggqt rifmprygni nerrhqlhev
       61 irlsgmnlvi ndldmpliik vasipkermq vyfidneeyf krkatltded gnlfpdnder
      121 aiffakgvie tvkklnwspd iihvhgwlas llplylrhyy aneplftesk ivtsvyghgy
      181 egaldknmqe kvkfdgipee kisvlenpty dnlmkvavdn sdavvvgsee iseelvkhle
      241 tidqpvldyk rpeefataye sfyqtevfv
//
LOCUS       WP_176027871             932 aa            linear   BCT 11-JAN-2025
DEFINITION  CHAT domain-containing protein [Aquimarina sp. TRL1].
ACCESSION   WP_176027871
VERSION     WP_176027871.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 932)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 932)
  AUTHORS   Zeytuni,N. and Zarivach,R.
  TITLE     Structural and functional discussion of the tetra-trico-peptide
            repeat, a protein interaction module
  JOURNAL   Structure 20 (3), 397-405 (2012)
   PUBMED   22404999
REFERENCE   3  (residues 1 to 932)
  AUTHORS   Allan,R.K. and Ratajczak,T.
  TITLE     Versatile TPR domains accommodate different modes of target protein
            recognition and function
  JOURNAL   Cell Stress Chaperones 16 (4), 353-367 (2011)
   PUBMED   21153002
REFERENCE   4  (residues 1 to 932)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     Classification of the caspase-hemoglobinase fold: detection of new
            families and implications for the origin of the eukaryotic separins
  JOURNAL   Proteins 46 (4), 355-367 (2002)
   PUBMED   11835511
REFERENCE   5  (residues 1 to 932)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12138749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..932
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..932
                     /product="CHAT domain-containing protein"
                     /GO_function="GO:0004197 - cysteine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=107925
     Region          66..135
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
     Region          68..96
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(69,72..73,76..77,79,103,114..115,118..119,121..122,
                     148,151..152,155..156,159)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          101..142
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          147..173
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          163..881
                     /region_name="COG4995"
                     /note="Uncharacterized conserved protein, contains CHAT
                     domain [Function unknown]"
                     /db_xref="CDD:444019"
     Region          236..262
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(238..239,242..243,245,275,278..279,282..283,
                     285..286,309,312..313,316..317,320)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          267..303
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          308..336
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mrslfaffli cffynvsytq entplqqeil nsyerittst tksypekake lhalsfpkkt
       61 addslftaql yhqigifnfr nsdyenavrn trravkirss fkdslpskln nslnnlayil
      121 lkndkhalaf rhyqqlinne qkdrftikay vqivsilvdw gdyhqalhyl eeaallvann
      181 pqlqpqlyki ylsfsfvyse mesetyskka ilflqkaeka ikelnrtpsi gvqltiynry
      241 ghcydelsdy kkaiewyqka lsldhdqmtt nhlttlynni gyayfkikes dtaytyyqka
      301 lekdtlnsmi hdnlgdfyls rrryvdalqs yqkaisyean lfslpnykkl pssevllrap
      361 qkvklvndlk dkayawlsyy qvskkkqqll yaletiktad mlidtirsqs tekqskyfwr
      421 skgvdlymla tsvcyllqkp aeafyfmeks kslsllenlt keearkrtnl prkiiekeqt
      481 lkhnilaaeq sfytdttktk seklqhirqq rkklevfidf lkkqypayya lqkkqsiisl
      541 qayrtqiqng tgnsiqymls edsgyglfit knqthffkip eaislnknlr diqpfftkpi
      601 fstkervafk klsfaiyqal fpveiratia qekkivvipd hrlhlfpfes litylgkesn
      661 qlpfliydvd ihyqysfsll hklaqkdsmv nptaiafapv rfsnkklttl srseqklnei
      721 grlfpttlft kekasknnfi keaapysivh lsthanavsn kepwiafhda slslselyfi
      781 qsnaelvild acktalgemk qgegilslsr gffhagansv isslwstnek ssneiilsfy
      841 qflkkgedks salrkaklqy lqthqasels pyfwapliln grkknvfhtp sysyflvigg
      901 sillllllig gyvlfkkkns kqeyagnnsn si
//
LOCUS       WP_176028025             382 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: alpha/beta hydrolase [Aquimarina].
ACCESSION   WP_176028025
VERSION     WP_176028025.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..382
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44789
     Region          19..249
                     /region_name="YbbA"
                     /note="Predicted hydrolase of the alpha/beta superfamily
                     [General function prediction only]; COG2819"
                     /db_xref="CDD:442067"
ORIGIN      
        1 mkksiillla fiitassygq viyekfksik ldqtrelkiq lprnykkned kiypliivld
       61 gdylfepvvg nvdyfsywed mpesivvgin qdktrqedsr ydladflpvn kgaefyefig
      121 qellpyldqt yrtaqlkiiv ghdhtanfin yflfkenpif hgyinlspdl apnmkdriia
      181 alsnrtsdtw fymatgtqdv ekirnnvvgl dekikeidnd nvkyffdnfe esthytlvgk
      241 aipralevif emyrpiskkk ykevilhlet sayeyltdly ktteelygik rkirindfia
      301 istaieknkn weeleplgkl arkehpdtml gnyylgmyye qigepkkamr ayengflqse
      361 vafltkdfml ekvnkikedf gw
//
LOCUS       WP_176028028             343 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Aquimarina sp. TRL1].
ACCESSION   WP_176028028
VERSION     WP_176028028.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..343
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=38881
     Region          13..334
                     /region_name="AKR_Tas-like"
                     /note="Escherichia coli Tas protein and similar proteins;
                     cd19094"
                     /db_xref="CDD:381320"
     Site            order(19..21,26,48,53,87,130,178..179,203,231..237,240,
                     242,250..252,286,303..307,311,315)
                     /site_type="active"
                     /db_xref="CDD:381320"
     Site            order(48,53,87,130)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381320"
ORIGIN      
        1 mrytklpntd ikvskiclgs mtwgeqntek egheqldyam sqgvnfidta elysipsrke
       61 tqgstekiig swlqknknrd qliiaskivg paeftahire gkfvksefed aihkslerlq
      121 tdyidlyqlh wperntnffg klgyshyeke lwednfaavl qslegfiqsg kirhiglsne
      181 tpygvmryie earkgapkmi tvqnpyslln rkdeigltev lhrenvghlp ysplgfgqlt
      241 gkyldatpen arvtlfpqys ryhnensfka trayneiakk ygisltqmsl afvtdrpfvt
      301 sniigatsva qlkenidsin ltlskeilke inavhadnpn pap
//
LOCUS       WP_176028062             272 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Cof-type HAD-IIB family hydrolase [Aquimarina].
ACCESSION   WP_176028062
VERSION     WP_176028062.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11576316
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..272
                     /product="Cof-type HAD-IIB family hydrolase"
                     /EC_number="3.-.-.-"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30719
     Region          7..261
                     /region_name="HAD_YbiV-Like"
                     /note="Escherichia coli YbiV sugar
                     phosphatase/phosphotransferase and related proteins;
                     belongs to the haloacid dehalogenase-like superfamily;
                     cd07518"
                     /db_xref="CDD:319820"
     Site            order(12..16,46..48,69,150,152,185,193,215..217,219..220)
                     /site_type="active"
                     /db_xref="CDD:319820"
ORIGIN      
        1 mdlsqiklia tdmdgtllns kgevsrhfyq lfdslkqlgi tfvaasgrqy ysiihklspi
       61 kddiivvaen galtvqreee lqstpidqdt ylellditkk lpgsqvilcg rkkgyiedyg
      121 deftsmlqey ygkyeivedl atitddeflk iaichqegae ahlypalkhl edrlkvkvsg
      181 diwldlshpl ahkghaieql qkklnilpee tlvfgdynnd lemlksaqys famknalpsv
      241 kstakymtks ndeqgveyil ekvieakqkv ll
//
LOCUS       WP_176028104             256 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Aquimarina sp. TRL1].
ACCESSION   WP_176028104
VERSION     WP_176028104.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..256
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=27939
     Region          10..253
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mttnrkdgsl ytkiegkiah iefghpssns fpsvlldrle rainelsvne evsvivlkse
       61 gekafcagas fdellaikni eegtvffsgf akvlnamrkc skliigrvqg kvvgggvglv
      121 aacdyslate aasiklsela igigpfviep avsrkigtta fgelaldptq wknaywakeq
      181 glyarvfeni seldkelelf tekmanynpa sikeikkilw kgteewddll veraaisgel
      241 vlsaftknal qkfkkn
//
LOCUS       WP_176028210             424 aa            linear   BCT 11-JAN-2025
DEFINITION  nucleotide sugar dehydrogenase [Aquimarina sp. TRL1].
ACCESSION   WP_176028210
VERSION     WP_176028210.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..424
                     /product="nucleotide sugar dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=47137
     Region          10..416
                     /region_name="WecC"
                     /note="UDP-N-acetyl-D-mannosaminuronate dehydrogenase
                     [Cell wall/membrane/envelope biogenesis]; COG0677"
                     /db_xref="CDD:440441"
ORIGIN      
        1 mtshnikenk iaviglgyvg lplaiefgkh nfnvigydin psrieglrkg vdftnevsen
       61 dlkrvksihy tfneeelsfa difiitvptp idkfkkpdlg pligaselvg rylsngnivi
      121 yestvfpgct eevcvpileq nsgltfnidf fcgysperin pgdkirrvhn ivkvtsgsne
      181 eiaelidkly ttivvagthk assikvaeaa kiientqrdl nisfvnelal ifdkmnidtl
      241 evleaagtkw nflpfrpglv gghcigvdpf ylthkaeslg yhpevilsgr kindemgvhi
      301 ankvvklmvk eghrvknaka lvlgitfken cpdirnskvi dvinelkefg msvdvfdpya
      361 splevkdeyg irlmekiedk ydtivltvgh nefknidisa ygnsnaviyd vksflpksiv
      421 tdrl
//
LOCUS       WP_176028212             464 aa            linear   BCT 11-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Aquimarina sp. TRL1].
ACCESSION   WP_176028212
VERSION     WP_176028212.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..464
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53471
     Region          6..395
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mgtkskglvk asfiysigni gtlvlnfflv pmytfflsqe elgffdvias svtlisplff
       61 ghiesavirw ligkkereni ghivsnssli filgisffsl cyfiltffik hdlflfiyly
      121 lianffyiii kqvirsvyss fhyvitevif tvivfvfavf lakeyklkgi llayfysfls
      181 llvylifikf hkylsiyeik kstmkellsy siplvpntfs lwtntmanky iillylslss
      241 ngiyaiafki ayvvqilnri fylslqdkmf eiygkkefeg yfsetfrkys ailfsivill
      301 iasqkiflpi viddkflsam nfipilslgv lfmslasvig iiyqcekkni rgsktsmisg
      361 avilvlgfvf ipkyglygas svflignlvl lfyryidvnk fitlkirier fiiyivltfl
      421 islfsltnki ellllnllla ivlallinks ivlkyyflfi nrkc
//
LOCUS       WP_176028099             324 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Aquimarina sp. TRL1].
ACCESSION   WP_176028099
VERSION     WP_176028099.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 324)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..324
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36382
     Region          1..316
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mlkvqnisfa yqtapviknv sftinkgqhi alvgasgcgk stllkiiygl lqvtegrlyw
       61 ddneilgpny hlvpgeeymk ylsqgfelta yrtvsenigq ylsnfepelk kgrvkellei
      121 veleefaatk venlsggqkq rvalaralak kpelllldep fgnidnfrrs slrrnlfnyl
      181 krnkitsita thdktdilsf tdetiviqkg eviahkntie lyrhpknlyi aslfgeinni
      241 visdlitsad hssalvyphe itivskssis vlvrksyfkg nhfliesvln gtsilfiehh
      301 tflppgekiy itipedllls raat
//
LOCUS       WP_176028227             231 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Aquimarina sp. TRL1].
ACCESSION   WP_176028227
VERSION     WP_176028227.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 231)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..231
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25792
     Region          2..229
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mitiqnltkk yvdsvvlsie eltiekgssf glvgnngagk ttlfstlldl ikptsgfitn
       61 nevrvdesee wksftaafid esfligylta eeyfyfigel rgrnkadvdt llatyedffh
      121 geilgkkkyl rdlskgnqkk vgivatlign peviildepf anldpttqir lkkiikelad
      181 npevtvlvss hdlmhvtevc erivvldkgt vvrdiktsee tlqeleahfn k
//
LOCUS       WP_176028238             194 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Aquimarina].
ACCESSION   WP_176028238
VERSION     WP_176028238.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..194
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=22791
     Region          12..188
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mehivkgifg hlvtlsdsew kevsshfklk kypnksyllr egqianetff iikgccrafh
       61 nfdgkeknic fsrencwetd vdsffnnkps atyiqaiedm tvlsltldnk lrlfkyhqrf
      121 eryfrilaeq mitylldvli krdtlcaekr flalkkrqaw vfqripqyhi asflgisats
      181 fsliqkdlll knsv
//
LOCUS       WP_176028473             594 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: tetratricopeptide repeat protein [Aquimarina].
ACCESSION   WP_176028473
VERSION     WP_176028473.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18640031
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..594
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=69426
     Region          19..241
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(19..20,23..24,26,50,53..54,57..58,60..61,84,87..88,
                     91..92,95)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          19..43
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          48..78
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          83..111
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          118..145
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          480..588
                     /region_name="CpoB"
                     /note="Cell division protein CpoB, coordinates
                     peptidoglycan biosynthesis and outer membrane constriction
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG1729"
                     /db_xref="CDD:441335"
ORIGIN      
        1 mrflyfillc slpvfgqsiq laknytdqge yekaisvykk lykqnpyrln yilgltsayq
       61 qlekfneaek vlkeainksp knlqflvelg hhfdlqglke katfeynkai dsydqnntnq
      121 ayslaqafek yslldqaali yekgmtynpg anfnlrlaki ygeqgkvekm fqsylslikt
      181 qpsykniilr nfsdyitedp lhepniifrk lliknlqknp dilynemlsw ffvqqkqfnk
      241 afvqekaiyk rkneslqrii dlariaishk dleaatmiln yileaedahn dmkltahkii
      301 lkartdkask keykkineqy lhvfdtygrs retiglqtdy ahflafnqdm kqeaitflkd
      361 ilkkerlsrf qssrikmkia dilvldqkfn qaliyytqvq nalknnflaq darfkvakts
      421 yykgdfkwaq tqldvlksst sqliandame lsliisdnsl edstytalki yakadllafq
      481 nknreaietl ekilvshkge kiedeafykq aklyekekey ekakvnylki iefystdila
      541 ddayyalaal ytqhlgqpek akelyekiif nhadsiyyvd arkkyralrg ddin
//
LOCUS       WP_176028488             252 aa            linear   BCT 11-JAN-2025
DEFINITION  thioesterase II family protein [Aquimarina sp. TRL1].
ACCESSION   WP_176028488
VERSION     WP_176028488.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..252
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=28417
     Region          17..250
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mkniakwfpy gipdtktasv nvfcfhyagg sataykdwal sdtsvsfipi elpgrgtrim
       61 dpliedfsil ipelvtiilp fitptipfyf fghsmggaia felayqlehh hqlspdkiii
      121 agrhaphmpd pstlhswlnd eklieelkvl ngtpkeilen kemiqfllpm irgdlrlhes
      181 ftyknqkita sivahaankd kdatkeimvh wkevttgefd iqefagdhff vqqlgknyia
      241 llqtllqanv ie
//
LOCUS       WP_176028491            1096 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Aquimarina sp. TRL1].
ACCESSION   WP_176028491
VERSION     WP_176028491.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1096)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 1096)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 1096)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 1096)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1096)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 1096)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 1096)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1096
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..1096
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=125079
     Region          2..189
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
     Region          309..488
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 miakilkfet ktrwkkpisw fffllmifqs iwftqgayty yaneatlmng aalfyknfag
       61 ggmimiiiva ivtggvlfkd iqhksagily tmpineksff lgrflaalst nlilgtglfv
      121 gmllvpysgi gsadkfgptp wgqmlegffl ltvpnlfllt vacfaalvff rkmaagylgi
      181 fvvailfmvt etirpntpyt tflqlldpfg ygytteildt lpatakntty lpltymyfih
      241 kaiwtggail lliisykkfs fkyfikalsp kakknivpdt ettsfssdig vpevqlffsa
      301 kefikklsrl avlefknvir pvnfkvimim valmfflqnl vwnptyylga qlpttasmtl
      361 trittgaaim illmiwsvel ffkdktsniw qitdalpvpv wvsqfskyla mcgvafilsv
      421 tiilcgilaq vakggwehid lwlyaedllg ykwgwltyvl nisfaffiag ltgnrfathv
      481 ltvgyylfnl isvefdiiee irytytltpg vedfseisgy giwnlasnwf fllwatlaii
      541 fvllgihfwr rgkafdfkrk itfrtnqlni ygkgavllmv iafislqsfi vsevnekgnf
      601 qpeevlnsqa asyekkykri lsepqpkith aeldialype erkaiskaal tltndcnhsi
      661 dtvylsmapf ttikkllwnh spikiskkde elrmyaipls idtaasgvls vysqkeysgf
      721 tqkgenpqpe llfngsffsi reiiptigyd vhrelkknre riehqlprve nrmpsienai
      781 amqqdvfapd akwltgkiql stsktqfava pgklvktwnd qqrshymyei teptpfawyi
      841 ssseqeqlqf rthdvdvsil hhkkhhynli hyqeaidntl dfintqlgny pysenrmvei
      901 pfyqekqysy antiatseke gwiadiqeip eqsyltflta sqlirqwvyr nihianvqga
      961 dmlqtalpea lalqivlekh gaegvhsile kkynayiker gndpnteipl lytdgapyla
     1021 qnkgtlvlyk mmkkmgadtf tlvvknsirq frdtpvpfta lyrrflvnls kedqieikkd
     1081 ietvqeipal lydkai
//
LOCUS       WP_176028498             179 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Aquimarina].
ACCESSION   WP_176028498
VERSION     WP_176028498.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..179
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=20189
     Region          11..173
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mslesenskk lseffgkeye slrryvgaki sntanrdaed iiqdvalklf sgadryapin
       61 nvagfvyrsi knkiidvmrt tkktqaidtd qdilklagal yqsadnypsd qmvsvlkkci
      121 qqlkpayrdi iiavdfegys ykeisfetgi sigtlmsrrh raigilykki eqevnkiqs
//
LOCUS       WP_176028502             527 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: S41 family peptidase [Aquimarina].
ACCESSION   WP_176028502
VERSION     WP_176028502.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..527
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=59530
     Region          43..355
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mgyskkytpl ligvamgvgv flgskldfra sssrlfsynp kkeklnrlid yidyeyvdei
       61 ntdsivevtv nrilenldph svyipseele gitenmqgdf igigvsyysy kdtisvinti
      121 kggpseksgi kagdrilmag qdtlygerlv rdkladklkg elnsqvqlkv yrrgtgifdv
      181 vvkrgrvpiq svdafymvde nvgyikinrf aettykefke alkelqknnm kelildlrdn
      241 gggfiapalk iadeflvdet lmmftknkkg aidnsyatde gdfetggiyi llnensasas
      301 eilagalqdn drgvivgrrs ygkglvqrem algdgsavrl tisryytptg rsiqkpykng
      361 neayfkeyme rykngelqha dsiqvadslr frtpggkivy ggggiipdvf vskdttrvge
      421 tleymlrsgy iaryvfeeld kkrayynsls kenftkefvv dnsfvdhfls ytekkgveln
      481 lvgyrdqlkk ylraiiaeql fdknvfeeil nqddkminkv lelskke
//
LOCUS       WP_176028509             149 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: nucleoside deaminase [Aquimarina].
ACCESSION   WP_176028509
VERSION     WP_176028509.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..149
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16493
     Region          6..145
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mldpfddahf mrkalmeaea ayekgeipig avvvvadrii arahnltell ndvtahaemq
       61 aitaaanylg gkylkectly vtiepcqmca galywsqigr ivygardhqr gciemgtklh
      121 pkttmeggvm eeecsailkr ffiekrnln
//
LOCUS       WP_176028513              65 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cold-shock protein [Aquimarina].
ACCESSION   WP_176028513
VERSION     WP_176028513.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..65
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6917
     Region          2..63
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 megtvkffne skgygfitnd etgkdifvha sglngealne gdkvaydeek gkkgtiaarv
       61 rvlhg
//
LOCUS       WP_176028525             588 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Aquimarina sp. TRL1].
ACCESSION   WP_176028525
VERSION     WP_176028525.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 588)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..588
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=64961
     Region          21..585
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 matltttkia iagrlitsyk elrihqtlga hhqvilscra dvleqfsdel igvskdflge
       61 vitisvvsqq nfseykellf kgvitkvqai krphvsgnli eivamsssil aedgahttsy
      121 ldlgvaeild vtyrgydtgk letsfrprts dtihysvqkg esnfaytarl aattnnwfyy
      181 dgvklvfglp seeetnlvyg qglshfaisl eplpnsfnch tydyltgeyy qkntkdvstp
      241 psgyhslttn kahqlyaktg nqylhpytds qlqhrferqv enhahaiaar qviasgvsdn
      301 pgvqlgtiin vsgygrfrii svthgniegg eyknnfeaia sdidvyplmn mfhtpvstie
      361 mgevidnvdp eglsrvkvrf pfqeeggttt pwipvvtpya gadkgfhfip eigetvvchf
      421 ennhaerpyv tgsiyhgqaq pvsyqsdann ikaiktrsgh sielndtqgg emititdkns
      481 niiridtatn nieiaalenm tltakniair aeeninmvag kdfansvaen ynvmtknstf
      541 iveetaitds kkqenvsdei vlssnkenlt lasgktvdvq skekvklf
//
LOCUS       WP_176028528             901 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: OmpA family protein [Aquimarina].
ACCESSION   WP_176028528
VERSION     WP_176028528.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 901)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 901)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458387
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..901
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..901
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=100947
     Region          148..410
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
ORIGIN      
        1 mstgiekvvv vnssgtvryv knlvvkanev tevkahyypd tpetlkgfak wivkpkeeap
       61 ftkddhegli gdvrtlrilp kycgprqfiv eafmeaptnr pasqliingv atqkiiksqw
      121 skknggksig dtpikygddi wlhletegln gatldidvyn dqwgtdgkvl tisnakcvhg
      181 evnlrvknty swrsgtgafr tngekfyika rlkgkketik dqngkedhgk flvidnkivt
      241 rkvekaestr paiigetevn veryelcrfe kivitddkke vpvfdekklq ltdkkkaefq
      301 vsetihfdfd ksairadake vldgiaslll dnpfvpselg ahcdirgdhd yndqlsnkra
      361 aaavkylink gvsrktitsq gygkrkllik gediseaehq lnrrvtikfk ifsndaqsiv
      421 fdtiapdksi kkeisvtvdg yitdqclrkg tqrhkasevk vleltpqgkk gpytydgtsd
      481 ikhkvysnis vsvlkvdalr yiwphktttn nfeyyinscr yysnkekptv ivkaypdikw
      541 dfhfflklsn plavkwqgld apgvarmrkv ngkiaaqnkw kqteaaigvv lkaswnkkdd
      601 tnykddfevt skyedkfkwi ynvfsslrel skgitkttkg katkalgska pfsvemvppn
      661 fclgaewqla rgevnqksik eigteykiyl ksdpligvkl iidllggait aasyattgnp
      721 vagdivlair ewaekgyete kvqvnfriwf dliisgtihg gvdfqsntas dknsasanle
      781 tklgveltag veltakvviv kvgsahvkgh asagvklgit sghhikydty kglyykpslk
      841 idpciaqvvv yievglsykv vsadwkpini nekrkfwdef diiknledis krkaeiqlik
      901 p
//
LOCUS       WP_176028549            1163 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Aquimarina sp. TRL1].
ACCESSION   WP_176028549
VERSION     WP_176028549.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 1163)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1163)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1163
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..1163
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=129388
     Region          14..1150
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mqnnqkkvdk efglsswaid nkttiyvmmg iflvlglsay fgmprenfpe inetkiyisv
       61 pypgntsedi erlivdpled klknvsnvve ilstsqedya iitvefdedi svpeakqkvk
      121 devdsekane dwptfngakv epnvfdlsis eetpimnini tgdypveklk eyaeyledei
      181 edlpeikkvd irgaqekeve vavdiykmma aqvsfddvin tirngnltms agnmissgqr
      241 rtirilgeiv npddldnfvv ksnngavylr diaqvsfkee ekttyarefg esvvmldvkk
      301 rsgknmveav ekitkrlsta kedvfpndln itvandqsak tinqvndlvn niifgiilvv
      361 gvlmfflgfr nalfvgfaip msmfmsfmil salgytmntm ilfalimglg mlvdngivvv
      421 envyrlmeee gmsrieaakk gigeiafpii istattvaaf vplgmwpgvm gqfmiyfpit
      481 lsvvlgsslf vaifinsmlv sqfmeigekv lstkqlirls iilvgtgtli lfiggdvral
      541 gtlmiftaim fwvykyflkk manvfqrktl vwvenlyqrf ltfalkgwra yafvvgtfal
      601 lfivfamfga sigsqrtkve ffpdnkpnqi mvyieypqgt diektnritk eieqrvyavl
      661 nnkeyiegad ynflvesavs qvgegagnpq tdggsnaemp hkgkitatmr eykyrngkds
      721 ealrqkvqda lkgiypgvai svekdpvgpp vgypinieie gpdynelvnv aeemrnfint
      781 knipgieelk idvnkgkpam qvvvnrekag elqvaagqvg nqlrrsifge kagvykkdge
      841 dydiyvrfnk enryntsalf nqsvtfrdpn sgriievpvs avasqrntss fsaikhkdak
      901 rvvtvysglq pgytdagaiv sqiqnemanf ttlpkgvkid ytgqieeqnk qmsflmgaff
      961 aglglimlll vfqfssiskp tiimiaifls figvfggili tgasfvimmt mmgiislagi
     1021 vvnngvvlld ytqllidrkk velnlkedev lpneevlkli vkggkarlrp vlltaittvl
     1081 gliplaigfn idffslfnef npkiylggdn vifwgplawa viygliiatf ltliivpslf
     1141 fivnrikvrf gkkkvaavpa vts
//
LOCUS       WP_176028561             608 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: peptide MFS transporter [Aquimarina].
ACCESSION   WP_176028561
VERSION     WP_176028561.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 608)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 608)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..608
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=67104
     Region          7..418
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 madtvkaahq kelfghpvgl fvlfftemwe rfsyygmrgl lvlyiatsat andpglgwtt
       61 kdalwlygwy tmlvyvmsip ggiiadkwlg qkktvmlggl llclghgvla iptstaffgg
      121 lalvilgvgc lkpnistmvg glykegdirr dkgftlfyig inlgaflagi ivgivaakyg
      181 whwgfglagi gmvlgqivym wgqkylvgvg dfigakesvn keaakkpltk iekdrvivll
      241 isflivivfw gafeqagglm nlytdvkvnr vtgfggpewl qeipaavfqs lnagyiiifg
      301 tviagfwvww rkkgkesssl fkmaigtiim glgfvfmmfa skeaaaenfg kaamfwifma
      361 ylfhtigelc aspvalsfit klapvkyasi mmgiyfactg fgnklagaig essqlepyeg
      421 kmiankevvy sfvnkaeytk evdgkeitek dyainrdknf eiraalypqg dkvefadyek
      481 gtslnslfvl gnseghntss qllaylkenn vtkenpyhak llfekdeeka kieankgdgk
      541 dysvsfkiee eqnaleynif tiitvftvaf glllivflkk lkvlthgaed nerdlrneea
      601 egfeladn
//
LOCUS       WP_176028562             738 aa            linear   BCT 11-JAN-2025
DEFINITION  peptide MFS transporter [Aquimarina sp. TRL1].
ACCESSION   WP_176028562
VERSION     WP_176028562.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 738)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 738)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..738
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81761
     Region          17..738
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mnsnitdtnd ffkdkvlghp aglfvlffte mwerfsfygm rallvlffta slfdegwgwp
       61 rehasalfgs yvglvylstm lggyfadkii gfrwavvvga llmtlghgam avetpffiym
      121 glgllvfgng ffkpnmtsii semyknhqek kdgaytifym gvnagaffgi llcgylgeki
      181 gwsygfglag ifmlfgliqf wlaqnifgdi glkpkkeeqt kvstseednd krvpfskgql
      241 vliticsalg ilwilndpaa kisegafnif dfqmlglegn nfviltalvl flglliyrlt
      301 kysqltkekl iavtffaflt iffwaifeqs pntltvfakd ytdrvlegts ayifkvintl
      361 iaivplgiit wvlwllfkqt fakykwsnii latsfvivwg vtiwmisnef kassynvtys
      421 nvngkteevk iisseayken dvikikdiqs lsiydqkeas ngnnkiengy lidgkgnqvg
      481 eclaakvvgf skepkpgafg ttvnnvdvvi tnslgesvsk kvkisseekg elnvgdeilv
      541 kiahsikydl nqtsqttati ssvnsaveip aswfsilnsl fiiafaplfs kwweskynps
      601 anmkygigmf llaigmacva fgangiepga ktasvsiiwl ilvylfhtmg elcispvgls
      661 yvsklvparm iafmfgvwyl avaigmkgag kfgenidkia dtegisyffw mltivsvvvg
      721 aisilfepii kklmhgvr
//
LOCUS       WP_176028566             166 aa            linear   BCT 11-JAN-2025
DEFINITION  C40 family peptidase [Aquimarina sp. TRL1].
ACCESSION   WP_176028566
VERSION     WP_176028566.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..166
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=18294
     Region          <49..165
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mkkiifllia tslffsscgs skrsksfasa kktsvhkksn kkiksiisya ktfngtkyky
       61 ggttrrgmdc sgliytsfkk envplprtsr smaskgkpvs lkrispgdll ffrtnknkkv
      121 inhvglvvas gkniqfihas vskgvtissl nerywnscfv garril
//
LOCUS       WP_176028609             378 aa            linear   BCT 11-JAN-2025
DEFINITION  FecR family protein [Aquimarina sp. TRL1].
ACCESSION   WP_176028609
VERSION     WP_176028609.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Van Hove,B., Staudenmaier,H. and Braun,V.
  TITLE     Novel two-component transmembrane transcription control: regulation
            of iron dicitrate transport in Escherichia coli K-12
  JOURNAL   J Bacteriol 172 (12), 6749-6758 (1990)
   PUBMED   2254251
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467275
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..378
                     /product="FecR family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=42964
     Region          155..377
                     /region_name="FecR"
                     /note="Periplasmic ferric-dicitrate binding protein FecR,
                     regulates iron transport [Inorganic ion transport and
                     metabolism, Signal transduction mechanisms]; COG3712"
                     /db_xref="CDD:442926"
ORIGIN      
        1 mddkhflfll ekylakkatp eeeqilmdyy esfqekalwn eqiesedeik kriyskiknq
       61 iqqdensiri nnllkyaavf igligslyff kntiinlvts sntdsliskr dhitltldng
      121 kietlsedgi hkivdtdgnv igekkgneik yfknkkatnt aynklsipfg krlnlvlsdg
      181 tkvklnsgst isyptqfsdk etrhvsiqge ayfdvvkdps rpfivdanqv hikvlgtqfn
      241 vshygtspdi qtvlvegaie lyntpktais strvkltpgq kgswnktakk iivdsvdvqp
      301 yiawiqgklv fkkmsfihia etlerhfdiq ikndypllnh qiysasfnge tieeilktfs
      361 edtpfsftrk gniisitk
//
LOCUS       WP_176028615             161 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Aquimarina sp. TRL1].
ACCESSION   WP_176028615
VERSION     WP_176028615.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..161
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17565
     Region          4..134
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mikddldwki levlqqnsrt pyavigreig lsasavaeri qrledsgvie gyattinlkk
       61 aglplsayis iqvqktnhat fvsyikefpe viqcsrvtgk dclimkcalk dsshlanvid
      121 rlavygdptt lvvlsevirn gmickeiiel aaaletgdmp d
//
LOCUS       WP_176028656             135 aa            linear   BCT 11-JAN-2025
DEFINITION  VanZ family protein [Aquimarina sp. TRL1].
ACCESSION   WP_176028656
VERSION     WP_176028656.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009512
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..135
                     /product="VanZ family protein"
                     /GO_component="GO:0005576 - extracellular region [Evidence
                     IEA]"
                     /GO_process="GO:0046677 - response to antibiotic [Evidence
                     IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=15217
     Region          14..125
                     /region_name="VanZ"
                     /note="VanZ-like family protein (function unknown)
                     [Function unknown]; COG5652"
                     /db_xref="CDD:444373"
ORIGIN      
        1 miikhllahk yiialvflyt saitwlslak filpepirve gsdklghfla yflfgciwfs
       61 lfffseklsk tftysvtias vigiaygalm eilqgvltdy rspdwydiaa nttgiilaal
      121 flnlikkklt klrte
//
LOCUS       WP_176028672             482 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TolC family protein [Aquimarina].
ACCESSION   WP_176028672
VERSION     WP_176028672.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..482
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54032
     Region          26..474
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mkikisilly vllgvwttea qqkkwtlqec veyalennit ikqsalsvet adidkndafa
       61 nflptvnasa snfwntgltt dfltgtlktq tsrnsnysvs vgvnifnglk nirqfqrakm
      121 nqllsqynlg kskddivlsv ansylqilln reslkviekq heitlenlkr tkdqveagvl
      181 pqgdlleiea tsadeitriv qaenavkiar valaqillik dyesfdiaek dylvptseil
      241 ekpveqvigk arearyevqi aeqnqllaek dlqlarsdyy ptlngsfsyg tresgakvpv
      301 qvldpdnplr tmpvgvvpst gevvttqkpn lltqeqnplp ffdqlsnndg isyglslnvp
      361 ifngfsvrnn vkrrkvavke aafrleqakl dldsnvyqay ldargtaeay easevavkaq
      421 erayeyakdr ydvgltnafd fsqskfrled aqskavrakf dyifklkvle lyfgvkvadi
      481 kl
//
LOCUS       WP_176028731             606 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Aquimarina sp. TRL1].
ACCESSION   WP_176028731
VERSION     WP_176028731.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..606
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=66586
     Region          13..601
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 matlsttqia isgrvipsfr slsiqqhlgd hhhlelvcrt dvlehasdei igdskdflge
       61 titvqvqadt qyedyrelqf kglitavnat kahqsgasgd iviieamstt vlaedgihtt
      121 syidlalsel lertyqgydv gklataftpr qsdtihysvq knesnfaysa rlaastnnwf
      181 yydgvqlvfg tpsseetqlv ygrdlesfsv rmhpkpnkfa yatqdyltne lyqkrsseva
      241 taaagyhsla tnkgnvlysk etniyhhgvt dqnlqqrfeq qvefhtqaie skqviahgvs
      301 dnpgvhlgav iqvegygsfr vievrhtnie ggnyknhfqa itteidvypl atmlqhpvst
      361 ieigkvtdna dpegmsrvkv qfpfqeitge ttpwirvltp hagadkgfhf ipeigetvvc
      421 qfennhserp yvagslyhgv akaenwqseq nnvkairtrs ghtielndte geekiniydn
      481 egsiitfdtq akslyvqsae nmeftaknir lvaeenidvq argnintase gdtsilsega
      541 tnlqatgdtt insdanvtve assnaefkgq qavvegqsva elkgqqttvq gqmtalqgas
      601 gkvdit
//
LOCUS       WP_176028747             373 aa            linear   BCT 11-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Aquimarina sp. TRL1].
ACCESSION   WP_176028747
VERSION     WP_176028747.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..373
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=41653
     Region          <213..333
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 meqqeyitrl enenkelkkr lgkinkqkqk snkikkglig llsvplfgvp lkksisnaih
       61 eykerksvsv dtvsdvtsnv iwrvtriglf ailmavipsl vllyqtklly nqnamiksqn
      121 slieadrrss lvtvmgdvls dvnqelknka sgersisrtl earivslsma mkpyqfkend
      181 qliekpispe kgqllfallr sqigkqssrd ifltgdfnyt slknanlgrg allqfarlnh
      241 sdfsgseive gnlkrvelke anltgtflse sdlsqanlyk admkkaelig vnftnanlfg
      301 vdltganlse atlwgtklkk anltavkldn aivhredwia yvsdsldldg gsdirknyrl
      361 kkqgkkqfli vak
//
LOCUS       WP_176028758             322 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Aquimarina sp. TRL1].
ACCESSION   WP_176028758
VERSION     WP_176028758.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..322
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=33399
     Region          2..318
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 msvlvytese ggnfkkaafe vasyakevas mlgttvtavs inasnneelg rygvdkvlnv
       61 ssgnleqfsa kayaevikqa aekenatvvv vgssidskfv apalavnlna gyasnvvalp
      121 estapfkvkr tafsnkafgv veissdvkli glssnafgii enevsaaven fepavgdenf
      181 svhvtavdka tdkvsiadae vvvsggrglk gpenwgmieg ladvlgaata cskpvsdmgw
      241 rphgehvgqt gkpvasnlyi avgisgaiqh laginsskvk vvinndpeap ffkaadygiv
      301 gdafevvpkl ieklkefkan na
//
LOCUS       WP_176028762             143 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: energy transducer TonB [Aquimarina].
ACCESSION   WP_176028762
VERSION     WP_176028762.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..143
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=16266
     Region          64..139
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mnklllffal vcmtmasyaq dniilsrena nekgitpiwp rcdrsrqtpi kcfdnklrdh
       61 iirnfqypdi alkdglsgtv tvefiinkkg kvevlevtga hrylqreair iiralpkmep
      121 akwgqkpiai aftvpitfvk pki
//
LOCUS       WP_176028783             141 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Aquimarina sp. TRL1].
ACCESSION   WP_176028783
VERSION     WP_176028783.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..141
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=15592
     Region          11..135
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mkiqlkridq dyhfeltner ghvthidnkt engghdlaps pmeyvlmgva gcsaidvisi
       61 lkkqrqqita ysaevdgrre kiggaspfke ikvtvylege idpdkakraa qlsfdkycsv
      121 sktleptavv vyqvvlnnea i
//
LOCUS       WP_176028813             187 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Aquimarina sp. TRL1].
ACCESSION   WP_176028813
VERSION     WP_176028813.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..187
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21785
     Region          8..176
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mrivqfykne tlliskaakg hkeaqyklyk syaakmlsvc ryyikdihha eevmlsgflk
       61 afmnlnkfks egsfegwirr iminesisyl rkektqlfte eiiggkeisw nnieteleve
      121 eiqslidslp sgyrmvfily avegykhqei akmldisest sksqlfkark mlqrkminqn
      181 imnngtv
//
LOCUS       WP_176028833             238 aa            linear   BCT 11-JAN-2025
DEFINITION  cell division protein FtsQ/DivIB [Aquimarina sp. TRL1].
ACCESSION   WP_176028833
VERSION     WP_176028833.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..238
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=27676
     Region          2..238
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mkkllgyikf gvlfllivll yafttarnhe rkieeikvef ieeqspyvne tmvnklliqn
       61 qnratsvgke ilalnkvekq ldqhemiqns dvylsvdgkl kvsirqrtpi arvdavtpfy
      121 vdtkgeimpl snnysahvpl vynvserevs eifpllkeir edeflkkhvv svyrnrqgny
      181 elgfrvyafk vnfgkaenlk skvsnfkafy kkaikdknlk eyrtislqfr nqvvctkk
//
LOCUS       WP_176028917             237 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CPBP family intramembrane glutamic endopeptidase
            [Aquimarina].
ACCESSION   WP_176028917
VERSION     WP_176028917.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..237
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=27189
     Region          139..225
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mnrivknrsv ipksrllvil lgfpiissii sllllrrdll tfkqvdffsv fwgiiivwyl
       61 vqiviikril nssclsfndi gyrfnkketl yfilgylifa filfgvieyl lasiditstk
      121 lnslsdfsnl tpktslqrfi fiiaglvagi seefvyrgfa inglenhnin kwsailiaai
      181 pfvfqhglks ldqfwwffit giimgliyvv skrklyinii ihwlvilsam lailqvl
//
LOCUS       WP_176028968             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Aquimarina sp. TRL1].
ACCESSION   WP_176028968
VERSION     WP_176028968.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34662
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mnytlhqlqi flkivekgsi tkaseelhlt qpavsiqlrn fqdqfpiplt evigrkiyit
       61 dfgkeiaeaa qkiiqevdqi shktlayqgq lsgvlkisvv stgkyiipyf lsdfmkkhse
      121 vnlvlevtnk emvvssleen svdfslvsvl pkhlkisktn lmenqlylvg sttdtfekkm
      181 ydtsilselp liyrepgsgt rhtmeeyleq nnivarkqme ltsneavkqa viaglgysim
      241 pligirndle anrlqiipvk gfplksiwnl islknkkfsp vaaaflsyve erkdeiirqk
      301 fqlinl
//
LOCUS       WP_176028979             153 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Aquimarina].
ACCESSION   WP_176028979
VERSION     WP_176028979.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..153
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17844
     Region          4..142
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 melldntdkt ilrilqrdsk ktakeianll nltvspiyer ikrlekrgyi ekyvaivnkn
       61 lidlpitafc qvslqshhes fidkfenqil nlkevqecyh magqvdfllk inmrsleeyh
      121 efvrtklski enigilnttf slkvikqtse lyl
//
LOCUS       WP_176029065             197 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: thioredoxin family protein [Aquimarina].
ACCESSION   WP_176029065
VERSION     WP_176029065.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..197
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22092
     Region          85..171
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(107,110)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mkklllplfs iliascgsta tttstdtvtp ppnsetsvit ekhpetkqet kpailigkqp
       61 rkaleatpya twfspnyday nvdsevvqki kpllgditik vfmgtwcgds kretptfyki
      121 ldaadydykn lelitvdrsk ktpsahekgl diqrvptfif ykdgkeigry veyaretlek
      181 dmlailsgks ykhayed
//
LOCUS       WP_176029059             193 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Aquimarina].
ACCESSION   WP_176029059
VERSION     WP_176029059.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..193
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22545
     Region          <126..192
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
ORIGIN      
        1 mrkasiedke lvtdilvsaf aplkgdnsin livkqdhkrv qrmrilmayl fekafyfgev
       61 fissnnkacl llhfphkekt tlrtillnir laffcigier vfevlkrqri akqfypkerh
      121 irpvilavke dakgngtaar lmlhvkdqyk dnqlpviidt sseynvklyk rfgfklikke
      181 kglkfpiyfl rln
//
LOCUS       WP_176029075             311 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Aquimarina sp. TRL1].
ACCESSION   WP_176029075
VERSION     WP_176029075.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..311
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35255
     Region          8..189
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(11,13,97)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(44,96..97)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            95..97
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mrintlsivi pcfneqdnik flfeelkkvl ndfdfvvemi fvddgskdgt fgeiekiadv
       61 dnrvtgisfs rnfghqiall agmekakgda vvtmdgdlqh ppevipemiq qynqgydivn
      121 tkridgvsts lfkrktskwf yalinklsdv rvepnsadfr lmsretvdaf lkikeqdrft
      181 rgliswigfk qtfvaytsqp rysgktsytl kkmlvlavng itsmsskplr islylgllff
      241 vtgivysifi lynffkgvnv egwtsiliti lilggvqlfi msiigeyvsr ifnetkarpl
      301 ylvkketgqk s
//
LOCUS       WP_176029087             180 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: carboxymuconolactone decarboxylase family protein
            [Aquimarina].
ACCESSION   WP_176029087
VERSION     WP_176029087.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..180
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19677
     Region          43..176
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mstfnvptre evsennqaif dnlnkalgfv pnlyatyahs ntalenylnf anaktslsak
       61 ekevvnlavs qvnnciycls ahtaigkmng fddqqilelr egkasfdnkl dalaklaknv
      121 tenrgradqn vvenffnagy skgnlidtiv lvgdktisny ihsttqvpvd fplaqpletv
//
LOCUS       WP_176029143             388 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA dehydrogenase family protein [Aquimarina].
ACCESSION   WP_176029143
VERSION     WP_176029143.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..388
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43609
     Region          6..368
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mskmyfteeh elfrkslqdf lkkevvphie kweetgtidr fiwkkfgdmg yfgiaypeef
       61 ggldldlfyt villeelqki nsggfaaaiw ahaylamthi nkegdqrike eylspsitgd
      121 kigclcvtep fggsdvagmr ttavkdgdhy vingsktfit ngvysdylvv aaktspelgn
      181 kgisifvidr dtpgvssvkl dklgwrasdt geiafdgvri pkenlmgeen kgfsyimqhf
      241 slerlimgin aharseyave ytiqymsere afgktldkfq alrhsiaema seiemskefn
      301 ysvarrldkg eyvvkeatms kllstkiade vaykclqmlg gygymedypl arlmrdsrlg
      361 pigggtseil keiiakiiid kkeykpat
//
LOCUS       WP_176029168             318 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Aquimarina sp. TRL1].
ACCESSION   WP_176029168
VERSION     WP_176029168.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..318
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35914
     Region          83..318
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 miktvlfyik ivsvaslfis plcthaqene kefnsayvki ddfiegtlva pyadkevplv
       61 ifimdagsin rdgndrmskn ntfknlsyel akkgiatfry dkrlfkmthl gikenevsfd
      121 dyisdaksvv tffsqndkyt kiiilghgqg slvgmiaaqe ntdafisvgg ngqsidqiii
      181 eqigkqapgl sknviqafde lkktgratsy dpalesifkl dlqpfikswm kytpteeisk
      241 ltipiliiqg drdihvepse syklrdavpn akyvifekmn hilkeingnr lenqksfdee
      301 wreimptvid tisdfvnq
//
LOCUS       WP_176029170             286 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AraC family transcriptional regulator [Aquimarina].
ACCESSION   WP_176029170
VERSION     WP_176029170.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..286
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34194
     Region          18..>68
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          55..281
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnrytlhetf vvqqyssdew egephkhnyf eiifiesgsg hhiingtkin ykknniflla
       61 pedthhfevd rhsrftyfkf tellfsckin lpdrkywlkr ieqllhqpni ipgdvishee
      121 drrviwdihn lvikefkeek iyyqeiisna istilsiivr nisekynsnq rdinvgdnki
      181 dqilshirqn vydndltkin yladlfnmsq ssistyfkrk tgesihqyvt kykmklvehr
      241 lqhtdftiae iayqlgytde shltktfkkh fsmspkqyrk eiiele
//
LOCUS       WP_176029171             131 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Aquimarina hainanensis].
ACCESSION   WP_176029171
VERSION     WP_176029171.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina hainanensis
  ORGANISM  Aquimarina hainanensis
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Aquimarina hainanensis"
                     /db_xref="taxon:1578017"
     Protein         1..131
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15074
     Region          3..108
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mytiirvlfg vllvfhgiyn vikytaflel meksfrvsnv fglgfveafv slipfiqfgf
       61 glflilgfft rnvlifavll haffmiflle tgvenialiq lmfliisvgl lfknhynlns
      121 mdytrdmfmt l
//
LOCUS       WP_176029176             228 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Aquimarina].
ACCESSION   WP_176029176
VERSION     WP_176029176.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 228)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..228
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24858
     Region          1..226
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msnviqirgi irdfklgqet vhvlkgidld ikhgeyiaim gpsgsgkstl mnilgcldtp
       61 tdgtyelngn dvskmtdnel adirnkeigf vfqtfnllpr ttaldnvalp mvyagaskke
      121 raeragevlt dvgladrmdh kpnqlsggqr qrvavgralv nkpsiilade ptgnldskts
      181 veimqlfddi haagntvilv theediaeha hrvirlrdgi iesdihqk
//
LOCUS       WP_176029258             292 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: mechanosensitive ion channel family protein
            [Aquimarina].
ACCESSION   WP_176029258
VERSION     WP_176029258.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..292
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31247
     Region          25..291
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mqtsekvvdt avtatteagg tildslggff nsiqegigqy glkivggiia liiglwiikm
       61 vmkavkkafn ksnidqtlkp flvtlvnfil klllfisiag ivgiptatfa allaaiglai
      121 ggafngslgh maagvmilif rpfkvgdlie tegklgfvke isifvtilet fqnkteiipn
      181 gaitagtitn lstkgnlrvd mpfgiqygtd ikkakqivld vlqadknvlk dpaprvavnn
      241 lgangvella lpystcedyw dvywdtrqki vealgeqsye aplpqrivtm ks
//
LOCUS       WP_176029211             192 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Aquimarina].
ACCESSION   WP_176029211
VERSION     WP_176029211.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..192
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=22312
     Region          14..188
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 msltsilqti skeytplsdk tiahwaslik qrtypkgyil vkegqysdml yyivkgaika
       61 yylkdgknvt dwfafegdfm caitsyflqv psphyietle evhllsitre emnllcdnyh
      121 dferlgrisc tktmlqlqqr ivslqfetaq qryenllerf pvitqraslr diasflgitq
      181 etlsrirant ri
//
LOCUS       WP_176029365             119 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: BlaI/MecI/CopY family transcriptional regulator
            [Aquimarina].
ACCESSION   WP_176029365
VERSION     WP_176029365.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..119
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
                     /calculated_mol_wt=13801
     Region          1..101
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mkqltkaeed imqilwelee gnvaaiieef pdpkpayntv stivriletk gfvtykkkgr
       61 ghiyypavkk seysnqrihk lmdgyfqgsf ksmvsffvkk nevsmeevee mikeinkke
//
LOCUS       WP_176029413             166 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cupin domain-containing protein [Aquimarina].
ACCESSION   WP_176029413
VERSION     WP_176029413.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..166
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18975
     Region          1..152
                     /region_name="CFF1"
                     /note="Predicted sugar epimerase, cupin superfamily
                     [General function prediction only]; COG3542"
                     /db_xref="CDD:442763"
ORIGIN      
        1 mntaqsiikh ldlqphpegg yfretyrske eipkaalpdt ysssrnytta iyflltsdtf
       61 safhrikqde iwhfydgapi qlhmispegh ysmvrigkdf sngelpqftv pggywfaanl
      121 qkeatfslvg ctvspgfdfq dfelpkrdyl qslfpehtqi itlltr
//
LOCUS       WP_176029434             195 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Aquimarina sp. TRL1].
ACCESSION   WP_176029434
VERSION     WP_176029434.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..195
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22569
     Region          5..182
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mthytdqeii drtlegdtai faalveryqy mvytvvyriv rnkeeaeeia qdsfvkayqs
       61 lgtykgkskf sswlytiayr ksldrvrnqs vtfttsvidk vsekalkqve naldymeske
      121 qneivleaim klpekesviv tlyyleensv keiaaivgis pqnvkiklyr arkklysllk
      181 dyvspeikdr ygral
//
LOCUS       WP_176029444             245 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: metal ABC transporter ATP-binding protein
            [Aquimarina].
ACCESSION   WP_176029444
VERSION     WP_176029444.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..245
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27147
     Region          1..236
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mketiavrid dltvaynykp vlwdidlvip egvlmaivgp ngagkstlik sildiidpia
       61 gsvqiygkpy rknrnlvayv pqkgsvdwdf pttaldvvmm gtygslgwik rpgkkekkaa
      121 lealekvgml sfrsrqisql sggqqqrifl aralvqnaai yfmdepfqgv dattekaiin
      181 ilkelrksgk tvivvhhdlq tvpeyfdwvt flnvkkiatg pvkdifnddn ltktyginyk
      241 vsilg
//
LOCUS       WP_176029495             254 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ParA family protein [Aquimarina].
ACCESSION   WP_176029495
VERSION     WP_176029495.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..254
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27675
     Region          3..252
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mgkiiaianq kggvgkttts vnlaaslgvl ekkvllidad pqanatsglg ldveaiekgt
       61 yqilehtvdp ldaiietssp nvdiipahid lvaieielvd kdqreymlks ildpikskyd
      121 yilidcapsl glltlnaltc adsviipiqc eyfaleglgk llntiksvqk ihnvnldieg
      181 llltmydsrl rlsnqvvdev qkhfnemvfk tiiqrnirls eapsygesii nydasskgat
      241 nylslaheii kkns
//
LOCUS       WP_176029507             432 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Aquimarina sp. TRL1].
ACCESSION   WP_176029507
VERSION     WP_176029507.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..432
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48005
     Region          1..426
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 menldaarlq maftlifhiv facigmvmpf fmvvshykwl ktrdavylkl tkswqkgvai
       61 ffvtgavsgt alsfelgllw pefmkhagpi igmpfslega affveavalg fylygwnklp
      121 ekfhwftgvi iglsgvssgi lvvaangwmn apsgfdyidg eflnidpvqa llnpawftqa
      181 lhmvlaafta tgfavagvha yqiykkkkva vhkkafniai tfgaiaailq pisgdisakd
      241 iakrqpvkla ameahyttek gvplyiggiv npetqevsyk ielpkmlsfl afgdvnaevk
      301 glndfpeder pnvpvvhysf qimvgiggll mmigifyfis rkkkkwqqrt vywllfaiis
      361 plgfialeag wivtevgrqp wiihkimktk davtpmpgiv fsfysylvvy llltvavtwl
      421 mtrqikvlns sk
//
LOCUS       WP_176029522             207 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: trimeric intracellular cation channel family protein
            [Aquimarina].
ACCESSION   WP_176029522
VERSION     WP_176029522.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..207
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22357
     Region          2..200
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mtlfdaldll gvtacaisga lsamnrkfdl fgifiiafvt aigggtvrdv ligqtpvswm
       61 qstltiylig cvttlsiifr nklyylkksl flfdsiglgv ftiigveagi rtgldpifci
      121 slgaitgcfg gvirdilcne ipvifrkeiy amvsilggic flvlnafhvk aniiyiatvl
      181 liisirllvv tykvslplft vknnkes
//
LOCUS       WP_176029539             220 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DUF805 domain-containing protein [Aquimarina].
ACCESSION   WP_176029539
VERSION     WP_176029539.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..220
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=24951
     Region          2..120
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 mnwyitalnk yaefngrarr keywffalfn llfaivaiil dnvlgiaire igygplygiy
       61 alatiipgla vavrrlhdig ksgwmiliaf ipfigaiwll ilfttdsdpg eneygpnpkq
      121 fediapieeq ssngdlilil vvswmlfsrt fytflpkiid nfyslgwfkp lstlmglvws
      181 ciplalgfiv kdktkqllvf ilggvyille lyslitqflf
//
LOCUS       WP_176029541             285 aa            linear   BCT 11-JAN-2025
DEFINITION  leucine-rich repeat domain-containing protein [Aquimarina sp.
            TRL1].
ACCESSION   WP_176029541
VERSION     WP_176029541.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..285
                     /product="leucine-rich repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=32375
     Region          <23..>248
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          34..56
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          57..79
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          80..102
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          103..125
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          126..165
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          166..188
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          189..211
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          212..234
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          258..280
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
ORIGIN      
        1 mgliiesikg fltniirkek yyslkkalrn pervrvlklt ngdlktiptt igqlrnleil
       61 elshnqlrsl peemgdlhkl relwldynql eylpssmvkl hnlevlwvdh npltgipegv
      121 eelpniqeis pgnhfvrgak kgkrsfgtsk sgekllkeai rnpknverlc lsnynleeip
      181 ssiealtnlk vlllsnnqlt slpkeigalq klevlilnnn qltsipkeiv qlpllkkisv
      241 rgnwlmsipk eitqlpsiee iwvdkeqyai ipkaierlps lkkvs
//
LOCUS       WP_176029543             146 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Aquimarina sp. TRL1].
ACCESSION   WP_176029543
VERSION     WP_176029543.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..146
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=16066
     Region          <28..>143
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          63..91
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(64..65,68..70,72..73,77,80,91,96..97,100..102,
                     104..105,109,112,121,123,125,129..130,133..135,137..138)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          93..121
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mnykitlfts llclfsqfsi aqdiskelll airngdtetl nthvtadeld tcfslknsqy
       61 nylaisiktn sltaikyfie kganiegict tktplmyavk sgniaivkyl iskganidaq
      121 tprgataidy adkykqteik aylsnl
//
LOCUS       WP_176029594             224 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Aquimarina sp. TRL1].
ACCESSION   WP_176029594
VERSION     WP_176029594.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423066
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..224
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25265
     Region          45..>152
                     /region_name="SmtA"
                     /note="SAM-dependent methyltransferase [Secondary
                     metabolites biosynthesis, transport and catabolism,
                     General function prediction only]; COG0500"
                     /db_xref="CDD:440266"
ORIGIN      
        1 mnknlstkki kkpwptkdam qqiyemnlwg gkrtefysgi gshapiiitp yieaitsflk
       61 gfdtpitlcd lgcgdfnvgk mlvpftkqyi avdivpdlie rnkrefaden vtfycmdial
      121 delpagdcai lrqvlqhlsn teiqqilekl yaykyviite hlpeeniepn kdiisgqgir
      181 lkkqsgvnvl appftmkvke kkelvsvasp thkgvivthc yqlf
//
LOCUS       WP_176029560             238 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: RDD family protein [Aquimarina].
ACCESSION   WP_176029560
VERSION     WP_176029560.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..238
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=26838
     Region          5..149
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 mdnfqietaq nvsiqqniag igerilayli dlmilivyvf imafvvgvls davtnqwvls
       61 llfglpffly fllwetfwdg ktpgkaamki kvakldgsrp kfsdylirwl lrlvdisiss
      121 ggvaicvill rgkgqrlgdm aanttvidek krvsfkdtil vevaddylpv ypqvtvfdda
      181 qirkikavyt aakrdgkhnv ilqlsekvss lmevspeekp lqfidrvlsd ynyytqql
//
LOCUS       WP_176029625             196 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Aquimarina].
ACCESSION   WP_176029625
VERSION     WP_176029625.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..196
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=23115
     Region          16..196
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mqeefdqyiv sflqsfpdln seelafmrsy ltvetyakka flfkcgevqk eigfvckgll
       61 rryyinekgn kittgfvnen kyatdypafi rqqpskyyie clepsiiikl pyekiqegyr
      121 kfkrsemygr liaeyvltvq tdrvesflfk naeeryldfi aqnqdiinri slshlashlg
      181 ierqslsrir skiskr
//
LOCUS       WP_176029646             368 aa            linear   BCT 11-JAN-2025
DEFINITION  SMI1/KNR4 family protein [Aquimarina sp. TRL1].
ACCESSION   WP_176029646
VERSION     WP_176029646.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..368
                     /product="SMI1/KNR4 family protein"
                     /GO_process="GO:0042546 - cell wall biogenesis [Evidence
                     IEA]"
                     /calculated_mol_wt=43232
     Region          17..148
                     /region_name="SUKH_6"
                     /note="SMI1-KNR4 cell-wall; pfam14568"
                     /db_xref="CDD:434043"
ORIGIN      
        1 mkeikifkee stislreikd aeelwnkkfp sdfksfllky nggipypnhp tihsendael
       61 wsierflsig diiiqkkhpm tytlhdieae dfvphnlnnd eilvfafgdr giyfmslqqh
      121 qygqiyfany sggdgivkin tnsfteffns ltiaswyeee ydpdfdfkel hysdnkifqy
      181 yfyytpndpd lglqrfkevf aiygdiqppe dgypnipqky vddrlkldfl lkqgcstdgl
      241 llyakkasti hylveelrld inkmykgryp lqnyltttyq aeiksnyeli sellemgiem
      301 dwsisgtkid qsvdatmtek lrllndeyln yeiqdkewwa kngkpsghip fkkskyiadk
      361 lntykskt
//
LOCUS       WP_176029734             335 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Aquimarina sp. TRL1].
ACCESSION   WP_176029734
VERSION     WP_176029734.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..335
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37651
     Region          58..300
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mnsilkikpl gfpwetsdpf lfcayhedry pegnqelgpa vslegriigq dfekkdgwrm
       61 yhgskvpgfp ahphrgfetv tivqkglvdh sdslgaagrf gngdaqwmta gkgilhaemf
      121 pllnqdtvnp fllfqiwlnl pkahkmvtph fkmlwnetip eqvvtdengk qvflkmyags
      181 mqetapappp hswaadadne vaiwtihmea nssytfpiat egvnrslyfy egdtlhsegy
      241 eipvdhriit npvnsltitn gntkakllll qgkpidepva khgpfvmntm eeirqamady
      301 qqtqyggwpw atyehvhdre kgrfaqfadg tveik
//
LOCUS       WP_176029778             264 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Aquimarina].
ACCESSION   WP_176029778
VERSION     WP_176029778.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..264
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29884
     Region          9..259
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 msqenqhivi qtenlsigyr qhkklmvvaa dinlklyege liglvgangi gkstllktia
       61 kvhpllhgsi flsdkeirky tpqelatqls vvlterissk nltvkelval grhpytnwvg
      121 klteediniv kkaidithin eltekrcfel sdgqlqkvli araiaqdtpi illdeptthl
      181 diyhkayilk llkrlafetk ktilfsthei dfaiqlcdkm ivmntdgfef grpkeliqcr
      241 sfsslfpqdl iifdsetgty kvrn
//
LOCUS       WP_176029858             106 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: YegP family protein [Aquimarina].
ACCESSION   WP_176029858
VERSION     WP_176029858.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10538412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..106
                     /product="YegP family protein"
                     /calculated_mol_wt=11570
     Region          11..54
                     /region_name="DUF1508"
                     /note="Domain of unknown function (DUF1508); pfam07411"
                     /db_xref="CDD:429450"
     Region          52..106
                     /region_name="YegP"
                     /note="Uncharacterized conserved protein YegP, UPF0339
                     family [Function unknown]; COG3422"
                     /db_xref="CDD:442648"
ORIGIN      
        1 mfelknkegs qyhftlkakn gqvilssevy nskaaaqngi asvqknasqd nryerktakd
       61 grfffnlkas ngqvigssqm ytsesgmeng insvkqnavd aqinei
//
LOCUS       WP_176029859             367 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: OmpA family protein [Aquimarina].
ACCESSION   WP_176029859
VERSION     WP_176029859.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458387
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..367
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40410
     Region          <148..367
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
ORIGIN      
        1 mkkiallvsf lilgtglkaq dlpqnpepgk cyvrcttpdv yenqdvqvmv tpeykklksy
       61 patyevvtek vlvkeaskvl tvipakykte tvtyvkkqga stlkvipakl gngsetveik
      121 payaqwelga papdcassnp ddcrywcykg ypaefttipt ktlasnanvq kspiseqtat
      181 ytkrvvsepa rvvekeipaq ystvkktvlv kdayseeivv patyktvkke vvskkggltt
      241 wrevecslve ysalpinwnl gsatltaqak niidtrlmpv lannpgtkme iashtdsrgs
      301 kasnkdlsdr rakavvdyli tkgintsrlv angygenrlk nrcadgvsct erqhavnrrt
      361 efrlinn
//
LOCUS       WP_176029890             206 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Aquimarina].
ACCESSION   WP_176029890
VERSION     WP_176029890.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..206
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24059
     Region          33..178
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 miqrtqlpnk snestvysif ienfghvslk hfdikrdasi lhtwvnepya ffwgmqgssl
       61 eevkkeyiel lkpdhydift gyhndqpaff lerytpskdi isnyydakns dcgvhiivap
      121 pvqnkipgft lhlfqtimdf vftnttidri lvepdirnkk mftlcerigf vtdktvelph
      181 ktaqlafldk nryqqqkthk lsihkq
//
LOCUS       WP_176029891             220 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Aquimarina sp. TRL1].
ACCESSION   WP_176029891
VERSION     WP_176029891.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..220
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24670
     Region          20..220
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mqttkalslh hiiktptvqk ektpvlfmfh gygsdendlf sfaselpdel ciisvrapyp
       61 mqpsgnawya iyfdadngkf sddeqaiesr dkiatfidea ieayhldasn vsilgfsqgt
      121 ilsyavalsy pekiknvial sgylneailh enyskndfsk lniycshgsv dpvipidwar
      181 kapaffdtlg vkttlqefpv ghgvhpqnfy qfkewlqnhi
//
LOCUS       WP_176029903             220 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Aquimarina].
ACCESSION   WP_176029903
VERSION     WP_176029903.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 220)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..220
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24331
     Region          1..218
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mikatdihky ygdlhvlkgv nlhikeseiv sivgasgagk ttllqilgtl dtpnrttssf
       61 leisgsditr lskkqlskfr netlgfifqf hqllpeftal enicipafik ntpkavaekr
      121 akellhflql shrsnhkpsa lsggeqqrva varalinnpr vvfadepsgn ldseaaenlh
      181 klffklrdef gqtfvivthn qelanmadrk lvmvdgkist
//
LOCUS       WP_176029953             159 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Aquimarina].
ACCESSION   WP_176029953
VERSION     WP_176029953.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..159
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18142
     Region          5..141
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 makfkldeid hqildmlien trtpftdiak kllisagtvh vrvkkmeeag iiegssltld
       61 yrklgysfia yvgiylqnts qtkfvlerin nipfvtvahi ttgkfnifck irakdtthak
      121 diifllddie gvyrtetmis leesindkkr lmhsifkdl
//
LOCUS       WP_176030000             219 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Aquimarina sp.
            TRL1].
ACCESSION   WP_176030000
VERSION     WP_176030000.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10583942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..219
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24288
     Region          22..165
                     /region_name="Pyridox_ox_2"
                     /note="Pyridoxamine 5'-phosphate oxidase; pfam12900"
                     /db_xref="CDD:432864"
ORIGIN      
        1 mcnhsvsaln kvvrgskrat yekdtvyqil ddtfmcnigy vwennaivip taygrdkdii
       61 yihgslknrm mrgiletgkv clsithldgl vlarsafhhs anyrsvnvfg svrevqdade
      121 kmkalecimn hmvaghwesv rkpnkkefda tlviavtidt asakiraegv ideksdmnsd
      181 ywagvvpikq vagrpesdek laegivipds vltyvannr
//
LOCUS       WP_176030007             409 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: HD domain-containing protein [Aquimarina].
ACCESSION   WP_176030007
VERSION     WP_176030007.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437595
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..409
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47611
     Region          8..406
                     /region_name="YdhJ"
                     /note="HD superfamily phosphohydrolase [General function
                     prediction only]; COG1078"
                     /db_xref="CDD:440696"
ORIGIN      
        1 mkkrnklkif ndpiygfiti pselifdlle hkyfqrlrri sqmglsylvy pgahhtrfhh
       61 algcmnlmqk svnalrfkgv liseeeeeal yiaillhdig hgpfshameh siveeinhes
      121 islmfmeain keftgkltla iqifkgeyhr nflhqlisgq ldmdrldylk rdsfytgvae
      181 gninserlit mltvvndelv veekgvysve qfllarrlmy wqvylhktgl vaenilirvl
      241 krakeltesg melqaspala fflknkitke nfledeldtf sklddydiis amkewsvcdd
      301 fvlsnlsrmi ierdllkiki kkkpfeknkl akhikkitkd yeiseeeary fvfsgsisnq
      361 ayhqnkqnin ilyknrkiad ivgatdqfnl kalskpvtkh ficypkqkd
//
LOCUS       WP_176030041             217 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Aquimarina].
ACCESSION   WP_176030041
VERSION     WP_176030041.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..217
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=25222
     Region          17..206
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 melfnvlitk gsyksstyse neiinnkera snklylikeg avkislltek geeiipvlln
       61 ksqifgvnal fgdryssfts esinnnttiy mfdintiyem vtedsnlqnd llhilkeeyn
      121 eienrirvli irsayqrlvq vlielkdkfg yqcpytnnvi inspfnqddl anymrisrvt
      181 anniinklke ksllqyrkkq iiltkrfltn hkpcfra
//
LOCUS       WP_176030052             160 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Aquimarina].
ACCESSION   WP_176030052
VERSION     WP_176030052.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..160
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18584
     Region          7..138
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mnhfdyvdqq illqiredar kpfsqiaeel kisnslvhqr irklkqqgvi qkaefvvdek
       61 qigfktksyv girlrearya eevvkglqei pqvlecnyvs gyyaifilvf aydnqhlrki
      121 lyeqihkidg vagtdsficf dtnfkrpipl dyltknaane
//
LOCUS       WP_176030082             496 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: DEAD/DEAH box helicase [Aquimarina].
ACCESSION   WP_176030082
VERSION     WP_176030082.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..496
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58029
     Region          4..494
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 mnrkkelydy qqrdidkifk rlnefpenyn llyqlptggg ktvifsemvr rytertekkv
       61 vilthrielc gqtskmlnef gvnnkiinsn vkelndqdey acfvamvetl nnrlneeqle
      121 lknvglviid eahynsfrkl fkffencfil gvtatplssn mklpmkdnyq elivgdtiqe
      181 lidkgflavp vtytydvglg slkigmngdy tvkssedlyt nmmmqdkllk ayeerskgkk
      241 tlifnngitt svhvydtflr agypirhldn tntrqeredi lkwfkhtdna iltsvsiltt
      301 gfdepsvecv vlnratkslt lyfqmigrgs riltdkseft iidlgnntar fglwnanvdw
      361 qlifrspdfy yenligdeei ernfkyvfpe eirkkfgnsv diefdiesey aktkrfglrs
      421 ksvldksieq hakmcaense dvfdarilsk lldkdieyrv rrysycisks tknyrdwlqe
      481 dyerklrsri nqlftd
//
LOCUS       WP_176030136             233 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Aquimarina].
ACCESSION   WP_176030136
VERSION     WP_176030136.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 233)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..233
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25692
     Region          1..223
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 miaienieki yrteevetta lnqlsltvkk gefvsimgts gcgkstllnv iglldtvdsg
       61 symfdgeeva hcsekeragi rkenvgfvfq nfnlidelsv yenvelpliy nkvpakerkk
      121 rvgeilervg ishrskhfpl qlsggqqqrv avaralvtkp kliladeptg nldsksgnev
      181 melltelhae gatiimvths sydakfssri vlmkdgiivs eeenvnkvdv liq
//
LOCUS       WP_176030177             165 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Aquimarina sp. TRL1].
ACCESSION   WP_176030177
VERSION     WP_176030177.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..165
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=18905
     Region          1..163
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mrksknksfe niyqqhhpmv lqmclgfakg drdtandlsq evfirvwnnl tsfrgassyk
       61 twiyritvnt clqyvekekk aqtlpipeia drtsgmeavt npkismlyna igqlkkvdrl
      121 iimmvlenqd yasisevigi spanvrvkih rikkrlettl kkqvt
//
LOCUS       WP_176030156             757 aa            linear   BCT 11-JAN-2025
DEFINITION  GH92 family glycosyl hydrolase [Aquimarina sp. TRL1].
ACCESSION   WP_176030156
VERSION     WP_176030156.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..757
                     /product="GH92 family glycosyl hydrolase"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=85154
     Region          1..757
                     /region_name="COG3537"
                     /note="Putative alpha-1,2-mannosidase [Carbohydrate
                     transport and metabolism]"
                     /db_xref="CDD:442758"
ORIGIN      
        1 mknytkwtll giaaimlsct tdkvtapvqs tnhlsyvdpf igtgghghty pgatipfgml
       61 qvspdngisk wdwcsgyhys dslaigfshl hlsgtgigdl adirlmpvtk kvaidqqans
      121 rdsipyssry sheqeaaspg yykvfledpq vmaefttdkr tayhrytyke gdkqsviidl
      181 gfginwdqtt astirvvdky tvsgyrhstg waknqkvffv akfsksisdy alvtdrtyav
      241 ktsvvtgkkt taqlffntld kkelevkvsi ssvseanala nmakdpipfd fehkkseaaa
      301 qwntqlskia vstsvdslkt ifytalyhaq lapvlfgdsn gevrmendsi rktegfemys
      361 tfslwdtfra ehplltiiap ervpdmiqam llyykergtl pvwtlygnet ntmtgyhsip
      421 viteayikgi egfdvetayq amkmtmtqtd rgldhyqqys yipytlldes vtitleyayn
      481 dwcvaqlaka lgkkedyayf mkrsqafthl fdpetgfmrg ksedgnswhe pfdpkysahr
      541 vhadytegna wqhswfvlhd veklialhgg eekftqkleq lftesseitg dnvsvdisgl
      601 igqyahgnep shhiaylynf ankpwktqyw vreilktqyd ttpeglsgne dcgqmsawyv
      661 fsamgiypfn pasgiyqigs pvfekvtitv daetsftila dkasdknlyi qsatlngipl
      721 nrtyitheel lkggtlhfim gdtpnkswgi ttkqtpp
//
LOCUS       WP_176030192             243 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Aquimarina sp. TRL1].
ACCESSION   WP_176030192
VERSION     WP_176030192.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..243
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26329
     Region          1..240
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mksndkpliv itgassgiga ataqlfsekk hpllliarri eklenlqlpn tlckqvdvts
       61 ydqlqeaite aetlfgpada iinnagvmll gdiatqdple wkkmfdvnil gvlhgmqavl
      121 pgmkerqqgt iinissiagr ktfpnhaayc gtkfgvhait enareeaalh nvrmvtiapg
      181 avetellsht tsqeikdgyd swkkemggvl spidiassiw yaynqpqgvn ireivlaatk
      241 qqp
//
LOCUS       WP_176030063             296 aa            linear   BCT 11-JAN-2025
DEFINITION  M28 family metallopeptidase [Aquimarina sp. TRL1].
ACCESSION   WP_176030063
VERSION     WP_176030063.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Turner,A.J.
  TITLE     Exploring the structure and function of zinc metallopeptidases: old
            enzymes and new discoveries
  JOURNAL   Biochem Soc Trans 31 (Pt 3), 723-727 (2003)
   PUBMED   12773192
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..296
                     /product="M28 family metallopeptidase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0008235 - metalloexopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=33296
     Region          101..295
                     /region_name="Iap"
                     /note="Zn-dependent amino- or carboxypeptidase, M28 family
                     [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]; COG2234"
                     /db_xref="CDD:441835"
ORIGIN      
        1 mkmcdykkvl llllillfqf sfsqeggtky eadiinfqke vvakltghkp ikgkkkltsr
       61 assserktta dflfnslkdi glspkrhsyd aqdskgkqys gvnvyaeiea tngsdeyvil
      121 tahydtakgs pgavhnatgv almyyvankl mglsernrnf mivffdqqea nmagckifss
      181 klkkdetkvh smhrvdyigw dndedraiel ltsniglesl yrseatrpvf krlvatpesr
      241 vfsnlgfeti titaelkngd nspyahqtad kyttvnflyl vyvsevvfkv mrslsy
//
LOCUS       WP_176030197             136 aa            linear   BCT 11-JAN-2025
DEFINITION  Fur family transcriptional regulator [Aquimarina sp. TRL1].
ACCESSION   WP_176030197
VERSION     WP_176030197.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..136
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15204
     Region          6..135
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 msaivlkkig irpttnrili ynylstekka vslsdlescf asmdratlyr tikifeeaql
       61 vhqiddgsgi pkyarcnqna vapshddthl hfhclkckkt scltncqipk iqvpnhyqvs
      121 evtmmikgtc decsra
//
LOCUS       WP_176030201             367 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Aquimarina sp. TRL1].
ACCESSION   WP_176030201
VERSION     WP_176030201.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..367
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40814
     Region          6..105
                     /region_name="PspE"
                     /note="Rhodanese-related sulfurtransferase [Inorganic ion
                     transport and metabolism]; COG0607"
                     /db_xref="CDD:440372"
     Region          117..289
                     /region_name="POD-like_MBL-fold"
                     /note="ETHE1 (PDO type I), persulfide dioxygenase A (PDOA,
                     PDO type II) and related proteins; MBL-fold
                     metallo-hydrolase domain; cd07724"
                     /db_xref="CDD:293810"
     Site            order(169,173,225,243,246,250..252)
                     /site_type="active"
                     /db_xref="CDD:293810"
ORIGIN      
        1 mtdtlisvee lrtklenker iqvidirple ereewkipgs vhvdvyhqlk sgkedvfstm
       61 dflkdetvvt vcaagktsli ameqlrkkgv kaysleggmr swtrawntai tedkhlkiiq
      121 vrrtgkgcls yiigsdgeal vidpsldiev yisiaknnnw kithvldthi hadhfsrakr
      181 laatvkaqll mppntalqyp yekiqdqqli sfgltniqai atpghtsdsf syllqekylf
      241 sgdtlftkgv grpdlkantd qakikagily dslqkilsls keiivfpghi sepvsfdgkt
      301 ianslgniid tvplltlekq lfvqallani pltppnyeki valnykgdik ereligleag
      361 anrcais
//
LOCUS       WP_176030220             177 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: NADPH-dependent FMN reductase [Aquimarina].
ACCESSION   WP_176030220
VERSION     WP_176030220.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..177
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18979
     Region          2..161
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mkniiaiggs nsknsinktl atyaanlits atttvvdlnd felplysidt eteqgipeea
       61 vrlnrtiesa daivislaeh ngsyavgfkn afdwlsrihk evwknkpmll lstspggrgg
      121 atvlqaaktt fphlggniia dlaipsfhtn fvdgkiinee imsilntkin eleaaii
//
LOCUS       WP_176030285             230 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD family hydrolase [Aquimarina sp. TRL1].
ACCESSION   WP_176030285
VERSION     WP_176030285.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12008676
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..230
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26124
     Region          6..180
                     /region_name="Hydrolase"
                     /note="haloacid dehalogenase-like hydrolase; pfam00702"
                     /db_xref="CDD:459910"
     Region          101..218
                     /region_name="Haloacid Dehalogenase-like Hydrolases"
                     /note="The haloacid dehalogenase (HAD) superfamily
                     includes carbon and phosphorus hydrolases such as
                     2-haloalkonoate dehalogenase, epoxide hydrolase,
                     phosphoserine phosphatase, phosphomannomutase,
                     phosphoglycolate phosphatase, P-type ATPase, among others.
                     These...; cl21460"
                     /db_xref="CDD:473868"
ORIGIN      
        1 mglehikvia fdaddtlwvn epffrkaeqd fcdifashlp kdqvnemlfs tqmknlplyg
       61 ygikpftlsl ietamditgg qldgdivall lqkgkemlet pvvllegiee tlavlatkyr
      121 lvmatkgdll dqerkliksg lqhffhhiei vsdktekqyt qlvrhldiqp heflmvgnsl
      181 ksdivpvlam gghafhipye ttwvhemiee eithpsfktf aqareilayl
//
LOCUS       WP_176030321             296 aa            linear   BCT 11-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Aquimarina sp.
            TRL1].
ACCESSION   WP_176030321
VERSION     WP_176030321.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..296
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=33860
     Region          134..238
                     /region_name="YdiL"
                     /note="Membrane protease YdiL, CAAX protease family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1266"
                     /db_xref="CDD:440877"
ORIGIN      
        1 myiekgkegs lgmwkyiplp laflglmaan ywfvttfdvd vaamfeqqit ekgknrffae
       61 nlltfviflg glffwvkfvh rqgirsltts rkkidwkril fmfilmglfv vasvtisyfi
      121 dpsqfiwnfd aekfailfll svllipfqts feeylfrgym mqgiglaarn rwvplvvtsv
      181 lfglmhlanp evdkigliil vyyigtgffl giitlmdegl elalgfhlan nlvtallita
      241 nwtafqtdsl fidmsepdks fevllpvfvv fpifigilak kyqwtgwkek lmgkvs
//
LOCUS       WP_176030349             184 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Aquimarina].
ACCESSION   WP_176030349
VERSION     WP_176030349.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..184
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21445
     Region          9..182
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mkltqlnteq lvnkcrnkdq haqmeiyrry ykamyntayr ilkngmdaed imqeaflnaf
       61 tkleklendk lfgpwlkriv inlslshikk skpndeldwd rvehtlhddd qgvseedtst
      121 tsitskivqt lhtlkqnyst ilslhliegy dydeicdimd itpancrtmi srakeslrkk
      181 ieia
//
LOCUS       WP_176030355             262 aa            linear   BCT 11-JAN-2025
DEFINITION  polysaccharide biosynthesis/export family protein [Aquimarina sp.
            TRL1].
ACCESSION   WP_176030355
VERSION     WP_176030355.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..262
                     /product="polysaccharide biosynthesis/export family
                     protein"
                     /GO_function="GO:0015159 - polysaccharide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0015774 - polysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=28622
     Region          <93..231
                     /region_name="Wza"
                     /note="Periplasmic protein Wza involved in polysaccharide
                     export, contains SLBB domain of the beta-grasp fold [Cell
                     wall/membrane/envelope biogenesis]; COG1596"
                     /db_xref="CDD:441204"
ORIGIN      
        1 mphlrlfali sivvsvfsck tptdvvyfqn sdnleeivsk nsftpvfkvd diisvlvsat
       61 dmeaarpfnm tqgtstgasg qppagggqaa nptylideng lidfpvlgel kvagltriqv
      121 kelikeklri yikepivnvr lmnfkitvig evnrpgsyti pneritiiea lglagdltil
      181 gkrenisvir ekdgvnvyhk vnltskelfn spvyylaqnd vlyvepnkar vrsskanrdt
      241 ntfgiimsiv gvalsglail lr
//
LOCUS       WP_176030362              80 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl carrier protein [Aquimarina].
ACCESSION   WP_176030362
VERSION     WP_176030362.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 80)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..80
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=9029
     Region          1..80
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mtveniltgi kesfviileh ddfelttetv addvegwesi thmmligeve kkfnvkfklm
       61 dlmkmenvgd lvaaikkeln
//
LOCUS       WP_176030395             323 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Aquimarina sp. TRL1].
ACCESSION   WP_176030395
VERSION     WP_176030395.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..323
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36401
     Region          3..251
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mdktihwgil gcgsiarkfa qdlqtvpnaq ltavasrste naqnfanqyn artyytsyea
       61 lckddnidii yiatphvfhh eqtllclhhk kavlcekpfa mnkeqvqemi tlaqknklfl
      121 mealwtyflp hyqellsiin nkelgairsl tadfgyystf dpdsrvynka lgggslldig
      181 iyplfaalsm igypddiqas anmtstgvde nchiklqyks gvsaslysti tkktkteail
      241 vfeegtihih sqfhkptsft iekngkketr kfpvttfgyn feavhaqeml lagktespim
      301 sfdkslqliq lldqvrqqin liy
//
LOCUS       WP_176030378             427 aa            linear   BCT 11-JAN-2025
DEFINITION  nucleotide sugar dehydrogenase [Aquimarina sp. TRL1].
ACCESSION   WP_176030378
VERSION     WP_176030378.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..427
                     /product="nucleotide sugar dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=46873
     Region          5..419
                     /region_name="WecC"
                     /note="UDP-N-acetyl-D-mannosaminuronate dehydrogenase
                     [Cell wall/membrane/envelope biogenesis]; COG0677"
                     /db_xref="CDD:440441"
ORIGIN      
        1 mqnikiavig lgyvglplar lfatkfsvvg fdinanrike lqsgvdstle vdntvlqsvl
       61 kqeasdaqgl fcsddlndia tcnyyivtvp tpvdknnrpd ltplyksset vgkvlskddi
      121 viyestvypg vteeecvpvl ekisgltfnk dfyvgysper inpgdkehtv ekilkvtags
      181 tpeigekvda lyasvitagt hlaptikvae aakviensqr diniafvnel akifnlmgid
      241 tndvlkaagt kwnflpfkpg lvgghcigvd pyylaqraqe fgyhpeiila grrlndsmgq
      301 yvaseviklm vqkdikikna kvlvlgitfk encpdvrntr avdvinnlks fgtditiydp
      361 wanpeevahe yeletvtelp eetfdavvla vahkeflsld lqkllnkngv lydvkgildt
      421 slvngrl
//
LOCUS       WP_176030398             154 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SRPBCC family protein [Aquimarina].
ACCESSION   WP_176030398
VERSION     WP_176030398.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790656
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..154
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=17954
     Region          3..152
                     /region_name="SRPBCC"
                     /note="Ligand-binding SRPBCC domain [General function
                     prediction only]; COG4276"
                     /db_xref="CDD:443417"
ORIGIN      
        1 mklyrlsqkq rlplsveaaw nflsdpknls vitpdymgft ivsgadrkmy pgqiiqyivt
       61 pvlgikntwv teithvvdqh yfvdeqrfgp yalwhhkhfi keipggveme diidyklpfg
      121 ilgrcihpfi vkpkleeifk yrrkklidlf gtfd
//
LOCUS       WP_176030401             292 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Aquimarina sp. TRL1].
ACCESSION   WP_176030401
VERSION     WP_176030401.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..292
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33223
     Region          7..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..292
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(111..112,114..115,118,122,124..130,224..229,
                     235..236,238..239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mgyqlelrhf tyflavaeel hfrkaaerlf isqpglsrqi kqmeeiigaa lfirnkrnvt
       61 ltaagvylkk eiefifnhid ftirqtslid kgsegevrig flgsamqtvi pdllvkanha
      121 ypdiqfslee ttnhdqvegi lkdhldigfv rldrvpegia kktvhmdtfs lvlpqdheld
      181 vasfqsidqv agenfilfss dysplyydki msicedkgfh pkvthksvha qtifrlvenk
      241 lgvaiiptsl qhgfdmnikf ieipairqqa ilsviwkkdn rnpalkmiqp fl
//
LOCUS       WP_176030482              87 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl carrier protein [Aquimarina].
ACCESSION   WP_176030482
VERSION     WP_176030482.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 87)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 87)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..87
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=9639
     Region          2..83
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mktailetik dglvdsianl tkeqiqlesh lkndlgidsl ssmffltyle dniegfevna
       61 dtiearhfnt lqsiydyvqs elgvlas
//
LOCUS       WP_176030499             316 aa            linear   BCT 11-JAN-2025
DEFINITION  MlaD family protein [Aquimarina sp. TRL1].
ACCESSION   WP_176030499
VERSION     WP_176030499.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Dutta,A., Chandravanshi,M. and Kanaujia,S.P.
  TITLE     Conserved features of the MlaD domain aid the trafficking of
            hydrophobic molecules
  JOURNAL   Proteins 89 (11), 1473-1488 (2021)
   PUBMED   34196044
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Isom,G.L., Davies,N.J., Chong,Z.S., Bryant,J.A., Jamshad,M.,
            Sharif,M., Cunningham,A.F., Knowles,T.J., Chng,S.S., Cole,J.A. and
            Henderson,I.R.
  TITLE     MCE domain proteins: conserved inner membrane lipid-binding
            proteins required for outer membrane homeostasis
  JOURNAL   Sci Rep 7 (1), 8608 (2017)
   PUBMED   28819315
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444651
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..316
                     /product="MlaD family protein"
                     /GO_process="GO:0015914 - phospholipid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=34354
     Region          2..296
                     /region_name="MlaD"
                     /note="Periplasmic subunit MlaD of the ABC-type
                     intermembrane phospholipid transporter Mla [Cell
                     wall/membrane/envelope biogenesis]; COG1463"
                     /db_xref="CDD:441072"
ORIGIN      
        1 mkftrevktg ilavcaiall ifgysflkgk nlfennrtly aiydnvegli psspvtingl
       61 vvgkvvaidf fdasgklivk fsvnndfkfs knslakisgs gliggkslai iptyqqglea
      121 knkdtlngkv eggiidlmts kltplqqkie lavmnadsll vsinkvlsed tqnnintifs
      181 dlsttvrnfk qasgslnaml sgneqklnnt ftnldqmstn lnkfsgslsq vdaaklsrel
      241 eavlanfnki ssdinagkgt vgkllkdkkl ytnleqaskq letlledlrl npkryvhisv
      301 fgkkntpyvk ptdsiq
//
LOCUS       WP_176030515             362 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [Aquimarina].
ACCESSION   WP_176030515
VERSION     WP_176030515.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..362
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=40548
     Region          25..360
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mnsktiaygi lravsiligi llllwflyki qsilvyiafa avislmgrpl vlflkrklkf
       61 nntlavvftl fitialflsi fllfvpiite qgqligeini nkigddldrl neevsnyfni
      121 nklnllevlk qtdlmkyldl kiipnlinsf lsgfgavlig lfsilfisff llkdsqllen
      181 sllvfakked etkfmraftk ikdllsryfv glllqvlilf tlytilflif gvhnpiaval
      241 iaaifnlipy igplfggilv lilattsnlg mdfstvilpk ltyiligyli iqlidnfanq
      301 plifgnsvks hpleifiail ifgslfgisg livavpfyta ikviskefls eykivkqltk
      361 gl
//
LOCUS       WP_176030534             207 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: flavin reductase family protein [Aquimarina].
ACCESSION   WP_176030534
VERSION     WP_176030534.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..207
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22921
     Region          32..167
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mkkkisraei damehlykin linscsgfks anligsvaan gdtnvavfss vvhlgsnppl
       61 lgmifrpltv prntydnike gsyytinhih kplieaahht sakypkeise fdktnltpey
      121 ksgcmlpfva gapvqmlmky veeytiksnd tillvgeike lfvneelltd egfidlskaq
      181 vatingldgy aipekskrlp yqrvkvn
//
LOCUS       WP_176030546             210 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Aquimarina sp. TRL1].
ACCESSION   WP_176030546
VERSION     WP_176030546.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..210
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=24652
     Region          13..208
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 melelrreyg nifeeelire iiqvsvykev pagvtmmeig qyvkamplil qgaikilrnd
       61 kegdelllyf lekgdtcamt lncclgetks eiraitekkt qllmipiekm eewtsrfksw
      121 rtfvfqsyhn rlmemleaid niafykmder llkylkessk vhdstivhht hqeiaydlht
      181 srvvvsrilk klenqgkifl nrnsiqllfn
//
LOCUS       WP_176030582             313 aa            linear   BCT 11-JAN-2025
DEFINITION  sirohydrochlorin chelatase [Aquimarina sp. TRL1].
ACCESSION   WP_176030582
VERSION     WP_176030582.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..313
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=35219
     Region          1..247
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mkegillcgh gsrreaavts fkrlvtilkd ryqdsyevdy gflefnhpty eaavermyln
       61 girkiyalpv ilfagshakn dipyelntiq syyedlhiam akhigvnsfl ldlaakrike
      121 teatipgfnr kesclvvvgr gttdpdansd vckltsmlwe glgygfatta ysgtaypsvk
      181 eslllteklg fkrtivipff fftgvlleri ysqvtamddk vadqefiytd pfgtdelllk
      241 afderleeak tgtanmncql ckyrkqvigf esdygkeqig hhlnvkgilf eedekpgekk
      301 ntlghkikkv lgi
//
LOCUS       WP_176030632             153 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Lrp/AsnC family transcriptional regulator
            [Aquimarina].
ACCESSION   WP_176030632
VERSION     WP_176030632.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..153
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17229
     Region          4..142
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mealdtfdie ilkiiqknnt tiqkeigekv hlsaaavqrr ikkmtaagvi qsniavidpl
       61 kvglavtlfv ivtleherle lvdeakekfk ncpevqqcyy vtgkgdfvlt ivvptmgdye
      121 rltrelffan nnvkrfetyv tlervktgld itl
//
LOCUS       WP_176030600             172 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Aquimarina sp. TRL1].
ACCESSION   WP_176030600
VERSION     WP_176030600.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18514852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..172
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19877
     Region          1..169
                     /region_name="MnaT"
                     /note="L-amino acid N-acyltransferase MnaT [Amino acid
                     transport and metabolism]; COG1247"
                     /db_xref="CDD:440860"
     Region          86..167
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
ORIGIN      
        1 mrirpvekke aeqlrvigia tfedtygsln tpenmkiyle knfskkqllk eldnpdskfy
       61 fleeqekvlg ylkinvgssq teycldeale veriyilsiy qgrgygskll dkaveiakta
      121 gvkniwlgvw eknlkainfy qkngfvvfht hifklgdeeq tdllmkkvil de
//
LOCUS       WP_176030657             125 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acyl-CoA thioesterase [Aquimarina].
ACCESSION   WP_176030657
VERSION     WP_176030657.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..125
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=13978
     Region          4..124
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 meeriekset rifkavfpnt tnhyetlfgg talqlmdevs ficatrfsrk kvvtistdki
       61 dfkkpipags ivelvakvvv vgrtscsvqv difkedmysd erekavtglf kfvaidqdkk
      121 ptpii
//
LOCUS       WP_176030659             149 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Aquimarina sp. TRL1].
ACCESSION   WP_176030659
VERSION     WP_176030659.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 149)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..149
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=17559
     Region          1..130
                     /region_name="SoxW"
                     /note="Thioredoxin-related protein SoxW [Posttranslational
                     modification, protein turnover, chaperones]; COG2143"
                     /db_xref="CDD:441746"
ORIGIN      
        1 mkklcfllli tsttlltaqh relkwvtnfd takklskrth kpilmyftgs dwcapckmlk
       61 edffhspefk ktakdfvlle vdyprredii teeqrqlnsq likkynkekt fpkiivfnsr
      121 ekiigtisay sqlrdpsgyf sfihdmlkk
//
LOCUS       WP_176030679             332 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: PKD domain-containing protein [Aquimarina].
ACCESSION   WP_176030679
VERSION     WP_176030679.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461763
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..332
                     /product="PKD domain-containing protein"
                     /calculated_mol_wt=37616
     Region          45..>274
                     /region_name="COG3291"
                     /note="Uncharacterized conserved protein, PKD repeat
                     domain [Function unknown]"
                     /db_xref="CDD:442520"
ORIGIN      
        1 mkttsntnyh idrsiilffi gviiisasvf gyrlanhtpc divdfsfdss slrvgeiirf
       61 kdktkgivne rewdfgdstk idtriapfht yehpgqytvr lringncegi tqtltikeka
      121 fvldstklar fkvpvsievg kelrikdetk nartwewrfg etadvnstdk npkyvyktpg
      181 lktitlivng dvrygtkkki nvlpkpslvd nkpvrrvprn spkstipyap tigvapisdk
      241 pketkapfig lnklkeklll vadekqtakn fneylcgnln lsivvnrkkt tfiefcqrik
      301 gkgikikele ivraenncik nlvirysktg lf
//
LOCUS       WP_176030682             207 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: C40 family peptidase [Aquimarina].
ACCESSION   WP_176030682
VERSION     WP_176030682.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..207
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=23132
     Region          <77..196
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mklllktlll isifigiasc ggakkalaea rekarrdsia laqknailpi qnkygtilnv
       61 apkkidnipl fkfiddwmdt pyrmggetkq gidcsffsqy lyhdifdvli ertaqkqyda
      121 pdtnkflgqe ylvegdliff nkqgsehypi thvgvylkng kfvhstarrg asgkngvqis
      181 dltkahwqkm fvsagrkprt aktsdsq
//
LOCUS       WP_176030689             825 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Aquimarina sp.
            TRL1].
ACCESSION   WP_176030689
VERSION     WP_176030689.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..825
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=92249
     Region          11..821
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mqlldylkdk kadaafhiaq slakeyyndt ynaahilkal lhkdvglrdf fkqidgdiyy
       61 ieewaevrie alprvtsipd elygdksvds vlleadtikl klgedtitpl gllisictpg
      121 vgfsyeqlkt lplksedlli aagqsgksvq gtktvtthqt kdgknidvsv leqfcvdktl
      181 eaqnngledv fgrdaeikmi teilgrrskp nvlitgesgv gktvlldgfa nevvngtvpe
      241 ilkhaqiyel dfinmvsgas yksevedrfk kiltaikqfd kpillideln nltdknngnq
      301 glvnilksel akgevtfiat vtndafrkhi evdeglsrrf envdleepge kealkmisnt
      361 iekyrahhdl evsdhtieea irlakrfskd rslpdsaidl idrtmsatry mlgttvaqia
      421 lvkesleaie asegdelkkv eeskwlfddl knkfsyllfs elieedtllk gesfaenksh
      481 iltvlnkfev saaaekrein kndvsatian ktgipvgklq adekerllqm eellkkrvig
      541 qdhavkiitd silesrsgls kpglpigsff ftgptgtgkt elakslaefl fqteeaiirf
      601 dmsefkeehs aallygappg yvgyeeggml vnkirqkpys ivlfdeieka hpsvfdiflq
      661 ildegklndr lgktgdfsna vilftsnigs dhvvksfede vipkssdlle imsrhfrpef
      721 lgrlteiipf apitkenvvk ifniqlkdlh kalgkqeitl eltekaqeyl alkgftpkyg
      781 arplrgiirt elraplsrml itgkigkgak vhldveqekl twkyd
//
LOCUS       WP_176030697             852 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ATP-dependent Clp protease ATP-binding subunit
            [Aquimarina].
ACCESSION   WP_176030697
VERSION     WP_176030697.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 852)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 852)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 852)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..852
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..852
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=95744
     Region          1..836
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mddnfsprvk dviayskeea lrlghdfigt ehlmlgllrd gsgkaisild aldidltnlr
       61 rkveilspan pnvtitfnek knlhltrqae ralkttflea klfqsssint ahlllcilrn
      121 endpttklln klkvdydnvk dqfkymitne eeyieerpka esfsedddnm agegskenpf
      181 nspgsgtktn kksktpvldn fgrdltamae egkldpvvgr skeiervsqi lsrrkknnpl
      241 ligepgvgks aiaeglalri vkrkvsrilf dkrvvtldla slvagtkyrg qfeermkavm
      301 neleknddii lfideihtiv gaggatgsld asnmfkpala rgeiqcigat tldeyrqyie
      361 kdgalerrfq kviveptnie etieilnnik ekyeehhnvn ytpeaieacv kltnrymtdr
      421 flpdkaidal deagsrvhit nidvpkkild lekkleevke lknsvvkkqk yeeaaklrdd
      481 eknlekelgi aqeqwekesk lhketvdeen vadvvsmmtg ipvnriaqte snklaelpnl
      541 ikgkvigqde avnkvvkaiq rnraglkdpn kpigsfiflg qtgvgktqla kvlakelfds
      601 edtlirvdms eymekfavsr ligappgyvg yeeggqltek vrrkpysvvl ldeiekahpd
      661 vfnmmlqvld dgyltdslgr kidfrntiii mtsnigarkl kdfgqgvgfg tsakksqsde
      721 hakgiiesal kkafapefln rvddvivfna leredihkii dielkklysr iknlgynlsl
      781 sekakdyisd kgfdqqygar plkraiqkyi edalaeeiit sklqegdaif mdleddsnel
      841 sisikkaees en
//
LOCUS       WP_176030738             216 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: rhomboid family intramembrane serine protease
            [Aquimarina].
ACCESSION   WP_176030738
VERSION     WP_176030738.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..216
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=23936
     Region          3..188
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mqninvvmll iiganvlvsi kgfndysffe kykfniggir rgeqlrmlts gflhvdmthl
       61 ffnmfslyff apvvisylgd ikfliiylgs llvgnilsll fhkdeyhysa vgasgavsgi
      121 iysailfkpg mslfimfipi pipayifgig yllysiygmk sktdnighda hfggavggyi
      181 ltllmaprll ttnllmvfll aipilillll kklgkl
//
LOCUS       WP_176030662             479 aa            linear   BCT 11-JAN-2025
DEFINITION  LptF/LptG family permease [Aquimarina sp. TRL1].
ACCESSION   WP_176030662
VERSION     WP_176030662.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Owens,T.W., Taylor,R.J., Pahil,K.S., Bertani,B.R., Ruiz,N.,
            Kruse,A.C. and Kahne,D.
  TITLE     Structural basis of unidirectional export of lipopolysaccharide to
            the cell surface
  JOURNAL   Nature 567 (7749), 550-553 (2019)
   PUBMED   30894747
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 479)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..479
                     /product="LptF/LptG family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54229
     Region          1..450
                     /region_name="LptF"
                     /note="Lipopolysaccharide export LptBFGC system, permease
                     protein LptF [Cell wall/membrane/envelope biogenesis, Cell
                     motility]; COG0795"
                     /db_xref="CDD:440558"
ORIGIN      
        1 mkiidryilt sflktffplf iiimfilllq tiwlfisela gkdldfsvim kfltfatprl
       61 ipmvlpltil ltsimvfgnf senyefaamk ssgislqram rmltgfmilv glgafwfsnt
      121 iipesekrfi nlrknivkvk pamvitpnqf ndlgdinirv sdkhgdndqf ltdviihkks
      181 vrpgnytvik avegelqgsk dsdlitlvlk dgnyyediqe nkpnskkklp fvkthfkqyv
      241 lnidlselgn vdmdaqqysk ghnmlnvael keeidtisst ynlkrkslht evdviigaeg
      301 lnknikidtl qasndtlnle kyftarqkve isnnaissvd vvlrkitssk ksltfkkral
      361 nkyemslhdk yalgiacvll ffvgaplgai irkgglglpi vvgvvlflvy hfigifakng
      421 aeedgippfl gswlatfvvf plsifltyra trdrgffnfd fitvpirnff vkrfskkkk
//
LOCUS       WP_176030837             456 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Aquimarina].
ACCESSION   WP_176030837
VERSION     WP_176030837.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..456
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50661
     Region          41..437
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mstrrsfikk stlagagiai apavtfgktg knkkgklkvg vigvglrgtn nldnlllrdd
       61 vlitavcdid pkridialer iaktgqekpk vfgnddydyr nllsleevea vvistpwlwh
      121 tkmakdsmla gkytglevsa antleecwdl vntheetgsf lmilenvsyr rdvlavlnmv
      181 rqqvfgelvh yrcgyqhdlr avkfndgkqp ygggvefgek gtsearwrtq hsllrnadvy
      241 pthglgpvai madinrgnrf vsltshaska vglnnyivnh pnggkehpna sikwkqgdii
      301 tstietarge tiivthdcnl prpyslgfrv qgvhgvsefd yhtkrihieg etgghgwedm
      361 eqwlvqydhp lwkkygthat asghggidff vihafveaak ekvappmdvy daaawsavtp
      421 lseasianng epqdfpdftr gnwikrkpyd wikdty
//
LOCUS       WP_176030846             187 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Crp/Fnr family transcriptional regulator
            [Aquimarina].
ACCESSION   WP_176030846
VERSION     WP_176030846.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..187
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=21625
     Region          13..187
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mdklakyika rididdnvls tivssfesrt iakgkfaikk nqlvtdyyfi lsgglrmyiv
       61 hndieltryf afegemiadi skikargrsn tyieaiente lltikhekme llyetypiwq
      121 kfgrllwees fasvlngvhn fqtlsakery ldimkrsdiv krvplkdlss flgitpssls
      181 rirkeik
//
LOCUS       WP_176030848             213 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: spermidine synthase [Aquimarina].
ACCESSION   WP_176030848
VERSION     WP_176030848.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..213
                     /product="spermidine synthase"
                     /EC_number="2.5.1.16"
                     /GO_function="GO:0004766 - spermidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=24211
     Region          <88..191
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mkkllsyvwp ltrtidstin gpleltwing kkvldsknan ysygtlqkll tyglskieip
       61 ptatilllgl gggsiinplr krfqhkgkit aieidpvvie iakeeffide sknlqivcqd
      121 ashfvykcvh hydiiivdlf idnkvpeeyy svifwrnllr llnkngkvvf nagihvknyk
      181 qidqliqtls dtitfeqyhd vegantllig syi
//
LOCUS       WP_176030903             144 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF2147 domain-containing protein [Aquimarina sp. TRL1].
ACCESSION   WP_176030903
VERSION     WP_176030903.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Barison,N., Cendron,L., Loconte,V., Proctor,E.A., Dokholyan,N.V.
            and Zanotti,G.
  TITLE     Protein HP1028 from the human pathogen Helicobacter pylori belongs
            to the lipocalin family
  JOURNAL   Acta Crystallogr D Biol Crystallogr 69 (Pt 8), 1387-1394 (2013)
   PUBMED   23897462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..144
                     /product="DUF2147 domain-containing protein"
                     /calculated_mol_wt=16319
     Region          1..140
                     /region_name="COG4731"
                     /note="Uncharacterized conserved protein, DUF2147 family
                     [Function unknown]"
                     /db_xref="CDD:443765"
ORIGIN      
        1 mkyiilfiip flfmcpatvd eeayigkwei kggsvieiyk ekqvfygkiy kraaqplsnl
       61 ngldnknpvk elrgrpivgm iildkltyne gelsggtiyn adsgktytvk vwinsddlnv
      121 cyiraykgwv fktftakrvp pslh
//
LOCUS       WP_176030935             198 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Aquimarina].
ACCESSION   WP_176030935
VERSION     WP_176030935.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22596
     Region          2..167
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 maskadqtka fiikkvapif nkngyaatsl sditkatglt kgaiygnfkn keelaieafn
       61 mvvkgvlrri teyqnrsdsp fekltlltkf yrnyydyiye yggcpiinmg vdannqntel
      121 fahvqytier iqknlvkiie qgkkegeikp aidswlyakq iytmiqgavf mtytmndeny
      181 lssimdkvdq milneikk
//
LOCUS       WP_176030945             201 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Aquimarina sp. TRL1].
ACCESSION   WP_176030945
VERSION     WP_176030945.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..201
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22321
     Region          <94..173
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mklnfllfic llqicckkeq gslatmsksp spytqqypql dhlfkkhpty iassfdfpvg
       61 kpdakgyyna qhfgenahlg edwngikggn sdlgdpiyai angyvsfaqd igggwghvir
      121 iihqyqgsyy esvyahchti avkkgdllhk gtpigtigna hgkyyahlhl eirnhifmdi
      181 gqgysndtkg yihptnfins n
//
LOCUS       WP_176030938             169 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphoglycerate mutase family protein [Aquimarina sp. TRL1].
ACCESSION   WP_176030938
VERSION     WP_176030938.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Fothergill-Gilmore,L.A. and Watson,H.C.
  TITLE     The phosphoglycerate mutases
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 62, 227-313 (1989)
   PUBMED   2543188
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..169
                     /product="phosphoglycerate mutase family protein"
                     /calculated_mol_wt=18939
     Region          31..159
                     /region_name="HP_PGM_like"
                     /note="Histidine phosphatase domain found in
                     phosphoglycerate mutases and related proteins, mostly
                     phosphatases; contains a His residue which is
                     phosphorylated during the reaction; cd07067"
                     /db_xref="CDD:132718"
     Site            order(34..35,80,123..124)
                     /site_type="active"
                     /note="catalytic core [active]"
                     /db_xref="CDD:132718"
ORIGIN      
        1 mkhiciflfs ifiigcsspt tstasettty flirhaekdl sdprnpnpml tekgnirakk
       61 waailapssi dyvystqflr tkltatpiaq knkvpittya pnkllskdfk qktkgkttvi
      121 ighsntipsf intllqkkky ddlehedygk lfiikitgdq itetvldin
//
LOCUS       WP_176031082             385 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxal phosphate-dependent aminotransferase [Aquimarina sp.
            TRL1].
ACCESSION   WP_176031082
VERSION     WP_176031082.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Mozzarelli,A. and Bettati,S.
  TITLE     Exploring the pyridoxal 5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 6 (5), 275-287 (2006)
   PUBMED   17109392
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..385
                     /product="pyridoxal phosphate-dependent aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=43037
     Region          2..382
                     /region_name="AspB"
                     /note="Aspartate/methionine/tyrosine aminotransferase
                     [Amino acid transport and metabolism]; COG0436"
                     /db_xref="CDD:440205"
ORIGIN      
        1 mmqtakrlet veeyyfstkl revralaaag kpilnmaigs pdlappkevi esiqeslyqe
       61 gahkyqsyqg lpelrkamad fyqnkyavsl dpnheilplm gskegimhis maylnegdev
      121 lvpnpgypty tsvtklvgak plfydlneag gwepdldfle kkynlskvki mwvnyphmpt
      181 gaagskelfe klirfakkha illvndnpys fvlnesplsi lsvdgakeva lelnslsktf
      241 nmagwrigkv mgakekieai lkvksnmdsg mfqgiqrgai talhlseewy hsmnaiyser
      301 rkliwslass lgctydinat gmfvwaklpk gvdavdfidr ilyensifit pgdvfgsngk
      361 gyirfslcin eesikeamkr lqvav
//
LOCUS       WP_176031135             164 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Aquimarina].
ACCESSION   WP_176031135
VERSION     WP_176031135.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..164
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19381
     Region          2..164
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mhsafshlvt lykqrlywhi rnmvknhddt ddvlqnvfik vyhnikkfkg dsklyswlyr
       61 iatnesltfl nkkakklnis neelhlqlaq nlesdvyydg deiqlklqka iatlpqkqqq
      121 vfnmkyfqel kykeiseile tsegalkasy hiaskkietf lrnh
//
LOCUS       WP_176031179             164 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: RNA polymerase sigma factor [Aquimarina].
ACCESSION   WP_176031179
VERSION     WP_176031179.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina
  ORGANISM  Aquimarina
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Aquimarina"
                     /db_xref="taxon:290174"
     Protein         1..164
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=19376
     Region          6..162
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mdkdlehsfv thldqnqniv hkvcrlytnd reshndlfqe itiqlwkayp kfrgdakfst
       61 wmyrvalnta itlyrkskks iktadfdamd fkikaeeydd eveeqlklmy kavkelndie
      121 kalvflyled ksyreiadtm gitevnarvk mnrvktklkk ilnp
//
LOCUS       WP_176031200             259 aa            linear   BCT 11-JAN-2025
DEFINITION  ParA family protein [Aquimarina sp. TRL1].
ACCESSION   WP_176031200
VERSION     WP_176031200.1
KEYWORDS    RefSeq.
SOURCE      Aquimarina sp. TRL1
  ORGANISM  Aquimarina sp. TRL1
            Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia;
            Flavobacteriales; Flavobacteriaceae; Aquimarina.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Aquimarina sp. TRL1"
                     /db_xref="taxon:2736252"
     Protein         1..259
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29281
     Region          1..256
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mivitqlnqk ggvgkttnti higaelakrg ynvllidadq qcdltestgv vdskydiidf
       61 lnrkhgfrlk krshnffvlp gnhnffpdkf kredlqkait gtctdenggt fllkdhfdfi
      121 fvdvppeaik pnitsapemg liasdyfitt lfadpssikn ldwflekafn ikkkynnklk
      181 iagvyfgnvl ptrksveryk skveelskgl lyktyirmda kiidaseegk tifqyspncr
      241 aakdyvqltd eilksvsne
//
LOCUS       WP_176031687             410 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176031687
VERSION     WP_176031687.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..410
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44580
     Region          14..359
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mlsaslnnsv hssatfglcf aihfllalda liivpfsaqm alsthtnpan sgllvavyav
       61 taslvclwvr ggenagnesr klislllaaa fftlctalln sfysllvvra ltglcagaal
      121 vlnlnlvvll sdhhnkkrnt aillstfpca laigipvllf itehvgwqss ifllgcclai
      181 tallfllifm qkhkrnipas vnhdcqikqn nihlfnkkls fallfsfvvv mstfiistqf
      241 pvmlitnfsi sntslsycyl lsgvcsfivi qlyarskfsn rttsylvyfl sgvmlltvlv
      301 gfntsrstfs aalfilfiia sscrsmilvt elivalqaqe rsafislqna iqhfaiaasg
      361 ifasllvkte dnqtlnfntl vavatllisv tivmwkhvnr lghnftsesq
//
LOCUS       WP_176031756            1038 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Pseudoalteromonas sp.
            McH1-7].
ACCESSION   WP_176031756
VERSION     WP_176031756.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 1038)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1038)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1038
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..1038
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=112713
     Region          1..1029
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mlkasvkhai lvavtvlics ilgivaafki pvqmipdlev rtisvvtnwp gatpqdveke
       61 ilieqerylr slanlkrmss yastgeaeie lefpfgvdvn ealinvsnal sqvpnypenv
      121 dqpvlysssf ssnafmffnl kpqsgnplni didmlrdyae dfirpemerv sgvsqvnvrg
      181 galyqvqilv dqqklasrgi slvdvrnair srnqdasagd idsgkrryll rmvgrfqsaq
      241 aleelvvsqr qnttiklkdi aevkldhyev rdvaynnger almlsvrres gsnvmaikee
      301 mmqvvarinr dmlshnglql tllsddvryv kgsvenvwtn lilgallatl vmfwflkspr
      361 stligvmgvp ictiaaflgl llfdrtinvi slagvafaig mtvdntivvl enieqarrrg
      421 ldklqaaisg vqevwpavla stlttvlvfa pilfiqqeag qlysdvaiai saaiiasmlv
      481 alfvvpaana nfacknitsg mlstltlpkv vpamlssssa rvgcivlgsv lllggawlfm
      541 pkaeylpege epkafsmmia ppgynlshmq kigdeilpyl nkhlekddsd fvagktqlpp
      601 lkyysmsvgv gsiwllsepy ngeyidemmd aitskfrsyp gmrafssrgs iissndggsr
      661 avaldisgtd qtalyraada vyrlagevfd npqidsapss ltldqpliei qprwqrlaev
      721 gmsadelgyt vaalsdgayv delilgddkv dvflfseagn qqslsqlaqs pvvtkaglip
      781 lssladlqek adsdslrrvd grrtvtvyii pprnvaleqa qelvrtellp qlqrqgdllp
      841 gvnvsiggaa dqldktkeal gsnfivalal cylllvaifk hwgyplfima tvplgmaggl
      901 lgliainglg svtgafhqpf dmitmlgfli llgtvvnnpi livdqsrrnl entsmsvyea
      961 visalqtrlk pivmstmttl cglaplvfip gegselyrgv gmivlcgiam ativtltilp
     1021 allvtflkrp lessvskl
//
LOCUS       WP_176031773            1057 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Pseudoalteromonas sp.
            McH1-7].
ACCESSION   WP_176031773
VERSION     WP_176031773.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..1057
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115143
     Region          1..1032
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mfskyfinrp ifafvisivi vlaglaamrs lpvaqypeia ppqvevravy pgasadvleq
       61 tvatpienai tgvegmmymt ststnsgvtt iavtfeigtd vdqaavdvnn rvkqvearlp
      121 eetrrqgvvv qktssnflqv hafyspdgtr dslwtsnyvt mnildrvkri pgttnvqifg
      181 akdyamriwl rpdimsqlev tadevasair eqnsqyaags igatptsqda qslvysvtak
      241 grlstaeefe niivranpdg stlrlkdvar valgskdynf qgtinakeav llgvflqpga
      301 naldvakave aeieqikpqf ptglahvnsy dttrfvevsi revlktlgea milvflvvyl
      361 flqnwratli ptlavpvsll gtfaglymlg ysintltlfg mvlsigivvd daivvlenve
      421 rimheqglqa keaavkamqe vsgpvvaivl vlcsvfvpia flggltgelf rqfaitisis
      481 vslsgvvalt mtpalcvlll khehkqdakf flwfndwfhr vtgryvgavs fmvrrgfvgl
      541 tlmaamigat vflwqktpss lvpdedqgyy miavflpdgs slertakvan eviaaaksnp
      601 anenvvaftg mdfigggfkn saatmfvtqt hwderdvsak elvgelfmkt ahinealvla
      661 fnpppifglg ttggfevflq nkggsdpakl kqgmqmimae aqkspiltgi qtlwrpdapq
      721 lkvhmdreqa ramgvninsa fnalaanlgn yyvndfnkfg rawqvimsae aefrmtpedv
      781 griyvknnrg emvpisaftd ieysrgpetm nrynnlsavk lmgeaapgys sgqaiaefer
      841 ianavlppdm tyewtgsafq ekqnsgttgi algmavimvf lilaalyerw slpvsvmlal
      901 pfgtfgalvs iwiagltndv yfqiglvtll glasknaili veyalmkyqe gwspataale
      961 aarlrfrpii mtslafilgv vplvmssgag agarhsvgtg vmggmlsatf lavfflplff
     1021 ywlmarrlse krskqalsde iakhhkeehv etdeglv
//
LOCUS       WP_176031780             453 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Pseudoalteromonas].
ACCESSION   WP_176031780
VERSION     WP_176031780.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 453)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 453)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..453
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=51119
     Region          3..453
                     /region_name="SalY"
                     /note="ABC-type antimicrobial peptide transport system,
                     permease component [Defense mechanisms]; COG0577"
                     /db_xref="CDD:440342"
ORIGIN      
        1 mkelvilawq glkqkpklsa lmvinlavgi tlmltmsaiv kqsssevigy kgdslytagl
       61 nyfdvdedvn dfrqfprwty qdaqalqqan lpyeyvsfny ttefivglad nsvrpisvea
      121 sgtdsgmfnv ldvpfiygta wnaqseksge aiaviskhan dhlfggvdsv gqfiqvqgeq
      181 irvagvvdlt rykrrfqdls fsnnynhdvf iplnyayaqn fprtgqvtcr tddlyttisp
      241 rsgsidmlks aecgyltvwf qyhndvelvq laelktwlnn yikqqqalgr fqhknltdfy
      301 smgelyiliq rfmaweaiyl tfsyllfgic lvntvgilla kfqanrklis lyralganqs
      361 vimiihflei lmltlaaivl gfilafagle lmfhlrmyqt dymaiaeqvr qiyqfdsela
      421 lvttlgifla vglsglypvy rssrvspase lrg
//
LOCUS       WP_176031812             496 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176031812
VERSION     WP_176031812.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..496
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=54388
     Region          4..480
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(61,63,67,70,74,107,110..111,120..127,132,135,138,
                     231,235,238,241,243,416,418..419,421..422,425,428..429,
                     431,433..436,445,449,451,465,472..477,479..480)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(147..150,158,173,176,206,223..226,229,247..249,281,
                     381,383,409)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(150,247,278,281)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mhqvplying efsqsqsdkw ldvvnpanqe vlakvpcatn eevqaaihsa qeafktwrnv
       61 pvterarimm ryaallkehq eeiatiiche lgktfedakg dvwrgievve qacnapsmmm
      121 getvenvarn idtysytqpl gvcagitpfn fpamiplwmf pmaivcgntf vlkpseqdpl
      181 tpmrlvelfe eagapkgvlq vvhgskdqvd qileapeira vsfvgscgvg qyiyskgtqn
      241 lkrvqacvga knhmvimpda kkeqvinnlv gssvgaggqr cmgisvavfv gqsqqwvdel
      301 kdamakvrpg vwddpeaayg pqttpqakar ilslidsgqq qgatclldgs eftvegyeng
      361 nwvgptlfsn vttdmdiyke eifgpvlccv fvdsldeait linnnpygng tslftasgga
      421 arkfqreiev gqvginipip vplpffsftg wknsfygdqh tygkqgvrfy tetktitsrw
      481 fddeavsgpn msinlr
//
LOCUS       WP_176031821             442 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: dicarboxylate/amino acid:cation symporter
            [unclassified Pseudoalteromonas].
ACCESSION   WP_176031821
VERSION     WP_176031821.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..442
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=47052
     Region          13..422
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mkttysisyf lqkkmlwlqi vvalilgitv gillspkgvg lvsaelslqi aqwvalpgnl
       61 flaliqmvvi plvlssiilg iagnkdtafl kqvglrifpy fvmttfiavi iglvvasyie
      121 pgkyvdsqll dnlnsqhttt vtatvelksi permvaiips nitqstldkd mfaivmyaif
      181 igiaittltq kqkslllelt ttaqtlslqi vnwamllapf avfgllcdit irigidallg
      241 vsayvatvll gllllmfvyl flassagkis pwrflsaikg aqllafstss saavmplsmr
      301 taeqplsvkk pivqfiiplg atinmdgtal yqviaalflt qvfgitlsds qilllilttv
      361 gasigspstp gvgivilasv ltsfgipaag ialilgvdri ldmcrtvlnv tgdltacvvm
      421 erlikldttp knaiddgeks ta
//
LOCUS       WP_176031844             791 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Pseudoalteromonas sp.
            McH1-7].
ACCESSION   WP_176031844
VERSION     WP_176031844.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 791)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 791)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 791)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114434
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..791
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86646
     Region          4..88
                     /region_name="ATPase-cat_bd"
                     /note="Putative metal-binding domain of cation transport
                     ATPase; pfam12156"
                     /db_xref="CDD:463475"
     Region          91..790
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 manscfhcle pipkgfvgsv tfegntqpvc cigcqavaet iisqgmsdyy tyrtesagkv
       61 eelipeqlkm llsydndeiq edfvetsgdt kevllsvegi scaacawlie kqllalggii
      121 rvdvntsthr amivwqdkkv klsdiikslm eigykaypfq adeeaaqkqa vakayirrlg
      181 vaglmtmqvm mfafamyfgm fsgmeedfeq yfrwislila spvilysamp fltnavkglk
      241 akqlnmdlpv slaifgayga styatfmevg evyfesicmf tfllllgkyl efrarlkase
      301 ftanlqkllp ltarkiddqn neqhiaakkl klndrilvka getipadglv isgnttvdes
      361 mmtgehqpvk kyqghqvyag tvnhdgvitl einkigqntl lnqiirlqhn altkrpklve
      421 vtdkvaqwfv acllvfasit aigwypispd kafwvtisvl vatcpcalsl aiptaltcav
      481 asltkkgili keahvletat kltrvafdkt gtltdgrfsi khveilqtqy tesqilelaa
      541 alerfsehpi arafahitpa dnliqdvevi agsgikgrwr shelalgksh wfnnhasfaq
      601 atlfvdgkai adfyfndkvk nnaesvvekl qqtgltchml tgdssnagke lsaqlaldsy
      661 qigctpelkq qavdtwseqg evvamvgdgi ndspvfnsah lsvamdtgad iskntadvvl
      721 lnsdlnaila lqqvakqtrr ivkqnltisl myngsilpla alglippwia vigmsassii
      781 vignslrllk l
//
LOCUS       WP_176031850             277 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Pseudoalteromonas].
ACCESSION   WP_176031850
VERSION     WP_176031850.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 277)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..277
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30192
     Region          6..223
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mtspllefdq vnkqfagkav lnninliiep gmvmgllgrn gagkttllri alglisqntg
       61 vvrcldsdnr qlspackqri gyvpqqpcgy qgfkvndala lhksfypnwd stleqtwlsr
      121 leldgnalvs nlsggqqqsl alimamsyrp qllildepvs sldpiarraf msdlfelale
      181 agsgvlfssh itsdverias hiaiikdgev lvsgeldslk eqikivpnsa sdplpgatil
      241 hqsqrstvyq asscnlrskk pehnitnleq lfvelhq
//
LOCUS       WP_176031916             125 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Pseudoalteromonas sp.
            McH1-7].
ACCESSION   WP_176031916
VERSION     WP_176031916.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..125
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=13133
     Region          <2..>101
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(6..7,10..11,13..14,18,21,32..33,36..38,40..41,45,48,
                     56,58,60,64..65,68..70,72..73,77,80,89)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          30..56
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          58..89
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mnnaliqaad cdlesakkll eagatpngmp limsiqcgae divslfikag vdlntsysdt
       61 tpliravtag ypnivkllvv ngaepslkds ggktamqrla ecsmprlnqq nkkliaeyln
      121 gakli
//
LOCUS       WP_176031855             444 aa            linear   BCT 11-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Pseudoalteromonas sp.
            McH1-7].
ACCESSION   WP_176031855
VERSION     WP_176031855.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..444
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=46783
     Region          6..430
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 msenqkmglt arimigmvlg valgfilqti lgdskevlip lglfdlpvkg ffvdglfhig
       61 gqifiaslkm lvvplvfisl vcgtcslsdp kklgrlggks iglylittai aitvaitlal
      121 ffapggdvev pstasfdakq aptlvqviin mfptnpidam angnmlqiiv fallfgiama
      181 lsgdagsrla avfedlntiv lklvtllmnv apygvfclma klfttidmgl ivelgkyfmv
      241 vvlallihaf inysilfkll tglspvvflk kmkdacmfaf stssssatmp vtletatkkl
      301 gahnsvasft iplgatinmd gtaimqgvat vfiaqvfgvd ltindylmvi ltatlasvgt
      361 agvpgvglim lamvlnqvgl pvegialiig vdrlldmtrt avnvtgdcmv tcvvaksene
      421 fdiavfndpd aakeleetts rvkt
//
LOCUS       WP_176031926             495 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_176031926
VERSION     WP_176031926.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..495
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=52941
     Region          1..495
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mtrsilfrli lttllsmgtv lllfgvydyv nqsmvlkqkl dtdvalaqer mglalpnavw
       61 nfqeqqvkkf ieaeaksdki skvvvsdmeg atfaqtegte tagvlkskli fddggsenev
      121 gwltvyvdsn siddalrgla fssiikvlll aailvavlsf ifqrlvvspl nevaekmati
      181 asgegdltqq ivvkrddeig rlassfnefe hkiaelinhv kksvddsfvv seninsvsse
      241 gvdfltsqqa etdqiatait qmassaleie nnakltlesa etanteankv reafqqsiha
      301 ieelveqlde aatvissles svqgivsvld viqsiaeqtn llalnaaiea arageqgrgf
      361 avvadevrsl asrtqsstae ihdtinqlqh gsqsavavme kskgkgtesm saanlasesl
      421 vsitgsvesi thmsshissa vseqstvaea lsknineavt agqggmskiq qvqiysddmk
      481 alasklqalv kvfkt
//
LOCUS       WP_176032023             211 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176032023
VERSION     WP_176032023.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..211
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22604
     Region          2..210
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mlnpeylfsf liastviava pgpsnaflma qtftngraag mqsalgfalg gvihtifavv
       61 glsallkase aayttvqylg aaylaylgii tikdtlgqaq pacedkphvs tkkpknvmlq
      121 ammtevlnpk valffiafip qfvdsnlats ttmqlamfgl lypilafpid cmyiyggdki
      181 agyfrqhpaa piwidrisgl ifialavnll r
//
LOCUS       WP_176032016             671 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein
            [Pseudoalteromonas].
ACCESSION   WP_176032016
VERSION     WP_176032016.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..671
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=72304
     Region          152..671
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mnltvsqriw ggfititlll lliggnslir ianidnstqq vnslslpals ksselkveft
       61 lmskmaqgsf yarsetelat lrqmfserqk ifdktyselq qvvasnnkla ssssdvgksy
      121 dafvkamnsl vteksselsl rdklkeqlsd ldmaaedatm vtvdiidldg ledsdkrafq
      181 aanslennfs svvtsandlv tvedintlei vrneqkylve elgrnidlir gpvtaldsgl
      241 fadlegyyta lkdtvtgsns iaenqkrlil alaetqkela daekttqaal sqlddllsea
      301 sqvafnlqqg vrsdvgkanl wtwigmmvat imavgvayit vsritkplse vnrvlnivas
      361 gdmtqrlddt akdefgelsk scntlisslr elitgiisrs tqlaaaseet stittessqa
      421 iknqqaqveq aatattemss tshgvsnsah qalqeiknad keaervkgis henkhtieql
      481 akevdeasrv inklhqdsas igsildvirg iaeqtnllal naaieaarag eqgrgfavva
      541 devrslaskt qestqeiqam ieslqagaee avsamskgkq qaescvnqsd lanealnsit
      601 aavsqahdvs eeianaaneq qqvaqeiser lesivtiaeq taegasqtsi sssevaklae
      661 elrlsvdqfk v
//
LOCUS       WP_176032024             265 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_176032024
VERSION     WP_176032024.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 265)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..265
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28794
     Region          7..259
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mavtpqfqvd klsvqlggka ilkalsftin pgefigllgp ngagkstllr tlyqyispss
       61 gqllfngnpl ngygrkayar nvavvlqdip vefnlplfdm vlmgltpnks llatitaaek
      121 qtifraieqv glshkceqcy sslsggekqr amiaramvqa pqvlimdept shldikyqiq
      181 imelakqlgv tiiasfhdln lasalcdrll ilsngelvad gaplevinea llsqvfgvca
      241 evytvrhppn nseiphirfh ygyql
//
LOCUS       WP_176032032             262 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Pseudoalteromonas sp.
            McH1-7].
ACCESSION   WP_176032032
VERSION     WP_176032032.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10563595
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..262
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=30120
     Region          10..177
                     /region_name="BMT5-like"
                     /note="rRNA (uridine-N3-)-methyltransferase BTM5-like;
                     pfam10354"
                     /db_xref="CDD:463056"
     Site            order(207,209..210,214,219,226,230..234,236..237)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275371"
     Region          221..244
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
ORIGIN      
        1 mildknwril tvgdgdlsfs yslakylkpi hltasiydse salkhkyqdn afdklanigi
       61 diitefdvtk tscwhrlskq sfdavifqfp lipafasyes fqqqtlsvnt lnrqllrkfl
      121 lnatkyaldp agvnlgiits kdvkpyiewn ieqslitntd lcylgqstfd iskfpeylir
      181 nvdrdkhvkd tsgvsyywsi nhshpitskl qmphylapnh cticragpfv sevdalshqe
      241 skkhksmqkh edqwqlylqq hk
//
LOCUS       WP_176032040             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176032040
VERSION     WP_176032040.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46258
     Region          17..396
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(27..28,31..32,35,67,122..123,125..127,130,150,
                     153..154,157,236,239..240,243..245,248,272,276,329..330,
                     334,338,354,357..358,361..362,365)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mgeqksttkk qglgrdfwiy rlgqslslvg davgmlalgw wilektgsaa vmgtmlaipm
       61 aigvvltplf gpigdrysrk hvialsdiir aivfvalaac vmfdhfdkal lvalftvntt
      121 agalfssssr sivaqlvdka llkeainkte ginamagivg gllggalvsv fgvmvafwvn
      181 tatflvamsc sllirantka sessgvmgvk twwnavlegf rvvfqvrill glslivmfin
      241 ftvaplevlv pylvkeveql pawyvglles glavgsilgv vlfgfiaqkv sldrimlfaf
      301 lllgvcigsm afnihiyqvl vsltliglat vwanvvlssq vmasvpdilr srigatlgfm
      361 gkgiepvsms avgisvdkvg fsttllvlga valvvapcly llphfktfmr leaeqagdfl
      421 ktsypaldka vkaggi
//
LOCUS       WP_176032069             227 aa            linear   BCT 11-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Pseudoalteromonas sp.
            McH1-7].
ACCESSION   WP_176032069
VERSION     WP_176032069.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 227)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 227)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 227)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..227
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24920
     Region          7..227
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mkvavykgfw dmlplnlavl pwgilcgsla vqngftplea qlmsllvfag saqlvaieli
       61 akdtalitll ittfiisarh llyglairnk mvdkplkwrs siaffltdel fafshhhray
      121 qgklrllyal vaggsfyvaw nlwtligiia gqflpdltnl gldfaiaaif ialvipsitt
      181 vpilcacics aisilifklv hfefglitsa llgmtvgyll qsykerr
//
LOCUS       WP_176032076             300 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sulfite exporter TauE/SafE family protein
            [unclassified Pseudoalteromonas].
ACCESSION   WP_176032076
VERSION     WP_176032076.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..300
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=32311
     Region          65..283
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mlqriarptm wplfftlgvy atliwiqgfy qalgqivses sialtmaigs fvaggtalgg
       61 gavafpvmtk llnidpatak vfslaiqsfg mtaatitifc rripvyknvi imalpmagig
      121 vtlslffiap faprllvksi fsflllcfal tlvlrwwrka hhqpssefiq pkmvrfmiva
      181 figgvasglv gsgadialfa llviaynadv kkatatsvvv mtftslvgss inawhlntit
      241 aeinsyllaa ipivvvgapl gayvcskvkv ghlvsfllil ialevsftcy elyptlrnwy
//
LOCUS       WP_176032081             161 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GAF domain-containing protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_176032081
VERSION     WP_176032081.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Ho,Y.S., Burden,L.M. and Hurley,J.H.
  TITLE     Structure of the GAF domain, a ubiquitous signaling motif and a new
            class of cyclic GMP receptor
  JOURNAL   EMBO J 19 (20), 5288-5299 (2000)
   PUBMED   11032796
  REMARK    Erratum:[EMBO J 2001 Mar 15;20(6):1483]
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005630
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..161
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18090
     Region          <10..>160
                     /region_name="GAF"
                     /note="GAF domain [Signal transduction mechanisms];
                     COG2203"
                     /db_xref="CDD:441805"
ORIGIN      
        1 mktpqkpdne qervaalkdl vildtepees ldrvtrftah ifdvpialis lvdtdrqwfk
       61 srfgldaret erdisfcgha iledtifvvh naledprfcd nllvqgdphi rfyagaplkl
      121 ssgftigtic iidvepreft qvdcgilhql aqdivtaiqn k
//
LOCUS       WP_176032184             199 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Pseudoalteromonas sp.
            McH1-7].
ACCESSION   WP_176032184
VERSION     WP_176032184.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..199
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=22910
     Region          14..196
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mdallklkqa iasyyalsqe twsaieaitt iksfakddwl yqegeypttf aflyqglvrl
       61 vntntagqey nkrffvagef pgvmhalhra epanqgiqal eptevvlinf kqfrallmdn
      121 pelmrfqihy leknwllekd krelymvqld aterylaflk eqpelaerva qyhlashlgi
      181 tptqlsrirk slknsgsft
//
LOCUS       WP_176032355             444 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ankyrin repeat domain-containing protein
            [unclassified Pseudoalteromonas].
ACCESSION   WP_176032355
VERSION     WP_176032355.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..444
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=49998
     Region          <235..346
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          248..278
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          280..311
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 meqvliwpaq ypmllkglie qngayildai eawpncqqik deqgvsttil pplfylawlr
       61 plepfeacyf qhiddyddkq rqyvnsvtrh ieengveqde liktliqrlg qysniqmqlq
      121 nqslsfiell cekqfektli wlievgiqfa peevvslwcn seeaihatll dnlqtcvcdr
      181 detaklatdg lldgrqtfel lcamcdqdev akqleqallf qltqqqvkqs ailtlvnqga
      241 kgvakdskgr saimlaieng fvsavepmlt yhnvneldec grnfmhyaaa snsaamiemi
      301 fdhgddptla diygdtpyrv amkqqaltsk qtfeqrgiie lsndakyqki ktvhmlyafa
      361 aillplqlfl fftdevdekt iatlvttaas igifaiarrk rsnplypnns tpwsllgvna
      421 lawvsigiqv lfsvlvliav lslr
//
LOCUS       WP_176032345             544 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein
            [Pseudoalteromonas].
ACCESSION   WP_176032345
VERSION     WP_176032345.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..544
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=60053
     Region          15..544
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mkqmnkllgl mkvpsklrls lilsvviial vklssalalr dslteerrth aknlientis
       61 qlnmvatett lsetqrkeki kklinaaryg dsgyfflfdl hgnmvthpik ptlngasmvr
      121 hdkrfireaf sqfvvianqn qqgfaqykwp kpgtqklesk lsfianlnhy nwaigtgiyl
      181 edveaqfhdq lismtaetlg yailliflss lisknitkpl dkltrtmgii ssqkdltill
      241 ksegrdeltq maiafnhmna hfrdvlhdin gnthslasqa eelsciteqi qagiaqqnte
      301 tesvqnrmls lnqvaqsvnh eskraldkvm attelttkgl ahvdenvsvi ahasqsvdsa
      361 qqavldlqrs steigvvldv ikkvaeqtnl lalnaaieaa rageqgrgfa vvadevrtla
      421 qrtqqstddi qaiinslhhg vattveemqn crtasekslk vsleckqale qinhsiatvn
      481 dinldiakws ekqsedinem ttnisgiati anqtalgaeh tkassqqlse msqrlsqmvs
      541 efkv
//
LOCUS       WP_176032360             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [unclassified Pseudoalteromonas].
ACCESSION   WP_176032360
VERSION     WP_176032360.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47116
     Region          10..391
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(20..21,24..25,28,61,116..117,119..121,124,144,
                     147..148,151,242,245..246,249..251,254,278,282,336..337,
                     341,345,361,364..365,368..369,372)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mpslsknsef hlhwvgvmlt qigayftlia lpwltlsvan nnpttlavim acfgiphslf
       61 illggsiadk yspllvikis rfgfalstll falslylyep slvllisfal faggfsalgf
      121 panqsfipri vlpehilkan vltmgssfvi qacapvlvgf sllgiksyle vnglfrtnie
      181 hlivafflda ilvtlaacct lkirhqdkeq smtsssvfrs mlksfqysft hpnlkiilly
      241 lmlisilihg plfimlpylv kvtlnmdesa lsyllasqgi gtfigatlva ickpnmqnlg
      301 kyilvldllt aivfiqlgfq ssllllcisl vaigcaagft vvagttwyql nvpieklsga
      361 ialvlfaihg liplssmllg tlldrfevsq ittllgvttt liciiglasv kirnmgkvss
      421 aianqatklk evphna
//
LOCUS       WP_176032372             208 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176032372
VERSION     WP_176032372.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..208
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22027
     Region          1..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 melhsltlfa iaclainlip gpdviyivsn tmkgkisagm qaalglgtgy fvhtiaaclg
       61 lsaiilssaf afsvvkwlga aylvylgvqs irsmwrgdsl lqpkkpetqt gnvfiqgilv
      121 svlnpkvalf flsflpqfvd laapstslqi lilgilfsfl atvcnlayav agswlfnrpn
      181 atrysraleg vsgmlllgla gkvivsek
//
LOCUS       WP_176032378            1053 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit [unclassified
            Pseudoalteromonas].
ACCESSION   WP_176032378
VERSION     WP_176032378.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..1053
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=116164
     Region          8..1028
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mqstekglia wfarnpvaan llmifiivgg lltafsirkq mfpqydsnwi svqaiypgaa
       61 pqeveegiti kieesmegle gikrlitysn rgysqtwiev deqydtkevl devkmqvdav
      121 stfpsgmerp ivrhdkatqe vmwlslngdl tphdlkelgn riheemlslp gvnlvrfdgg
      181 ldyeisieis pdkmreygls fravadavkn fsanmsagqi rsengyismr venqayrgde
      241 frklplltlp dgaqvylgdv aiindgfeeg lqyskyngkn slvfevsask dqditkvasv
      301 iknyleakkg alpqgvelep fidltyylng rlnmmlenma lggvlvmlml alflrvrlaf
      361 wvmmglpvsf lgaflmmpig fldvtinlas lfafilvlgi vvddaivvge sahaeiekhg
      421 hsldnvvrgv krvaipatfg vlttvaaflp qtlatgptaa fskaiggvii lcllfslves
      481 klvlpahlaa mkdkpsnpkn pfhrlrekmd rglqsliens yrpfinrcih yrytvivgfl
      541 avlivsagmf agglvkfvan pkiphdfpri sidmnlssse tatlnsiqki eqmvlsvdke
      601 ieaeygkkmi rdymvnmngr tsanimvilv epdarpidtf alsakwrdam ptlpgvksln
      661 iqdsimnggr ddgdisfrle grekaalqev aaklkdklat iegvgdinds mqsatdevql
      721 elkplayslg ltladvasqv nfsyygleaq rilrdgeeik vmirypkehr dtisdiqdvr
      781 iltpqgaevp lvevadvklv dgvnrirren akrtinvwas vdtevaqpfe iakqirdeyl
      841 psllknypsv qsavagrvqe emdsvaeqir dfalslmiif allaiplrsy sqpliimsvi
      901 pfgvvgavfg hmvlgmtmss lsffgiiava gvvvndslvm vdfvnkarda gtslkdaave
      961 agckrfrail ltslttfigl vpiimetslq akivipmavs lafgvlfatv itlvlipcqy
     1021 valedvkrlg rkwlkkdghe qskvatelks ntn
//
LOCUS       WP_176032408             364 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176032408
VERSION     WP_176032408.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..364
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40320
     Region          143..362
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 maittdhtlv ekrrsfwdag plifsifyff plafswtqeg svnlvaqlli ylgfvwlywq
       61 siaktgiali tllslmtllc ivgslattgt sslfgfvaff cgfslqgkyk vygflgllis
      121 ilftshfiip ahtiyflmpa icvslglfif gwvthrervh rqlqrqseqe ikrlgavaer
      181 eriardlhdl lghslssial kaelaskfaa aqsyeqaqse alqvaelare alsevrqavt
      241 gyhqlaldaq lhimasrlkd kgiavslnls aveidkekea slcffakevc tniirhsdad
      301 kvsvqlqqtq qsisveikdn gsvksikegn glmgirarlk ecggqlvyht eqgayfkavi
      361 evss
//
LOCUS       WP_176032428             247 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: HesA/MoeB/ThiF family protein [unclassified
            Pseudoalteromonas].
ACCESSION   WP_176032428
VERSION     WP_176032428.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   VanDemark,A.P. and Hill,C.P.
  TITLE     Two-stepping with E1
  JOURNAL   Nat Struct Biol 10 (4), 244-246 (2003)
   PUBMED   12660720
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Rizzi,M. and Schindelin,H.
  TITLE     Structural biology of enzymes involved in NAD and molybdenum
            cofactor biosynthesis
  JOURNAL   Curr Opin Struct Biol 12 (6), 709-720 (2002)
   PUBMED   12504674
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):140]
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Lake,M.W., Wuebbens,M.M., Rajagopalan,K.V. and Schindelin,H.
  TITLE     Mechanism of ubiquitin activation revealed by the structure of a
            bacterial MoeB-MoaD complex
  JOURNAL   Nature 414 (6861), 325-329 (2001)
   PUBMED   11713534
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..247
                     /product="HesA/MoeB/ThiF family protein"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26773
     Region          5..247
                     /region_name="ThiF"
                     /note="Molybdopterin or thiamine biosynthesis
                     adenylyltransferase [Coenzyme transport and metabolism];
                     COG0476"
                     /db_xref="CDD:440244"
ORIGIN      
        1 mtelsdkerl rysrhlllke vgeqgqlalk qahvavvgcg glgspalfyl aasgigkltf
       61 idhdevelsn lqrqilykvn hlgqqkakaa akvlaslnnd itltpinarl tqeniaells
      121 eadvildcsd nfttryllnk ycyqtnkvli agaaiatqgq lmcfdfraks pcyacifptd
      181 sqaptencgn fgvlspilgi igaqqallav nvllghhqgs yfsyidaltl vqhqlllvke
      241 dscsecs
//
LOCUS       WP_176032436             692 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent receptor [Pseudoalteromonas].
ACCESSION   WP_176032436
VERSION     WP_176032436.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..692
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76545
     Region          26..665
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mklklstitl allplfshhv ladddletiv vtgdfqneti qtlsasasvv deltitkrga
       61 qyldeilgat anvnftagas rgrfmqirgv glrsqfvdpi ypsvgllidg inysglggsa
      121 llfdtesvvv yrgpqgtkfg sdalagivev ntqmattaps lklklgagny gsyeagiaag
      181 aglsdntaar vslyqresdg yvdnlylnkp tqtqdeqaar lklnsqvsdn laleftfhhi
      241 dtdngydgft ldnsrnsvad epgqdnlesd afafrgkytr sdlfdvefkv sgldadalys
      301 fdedwvcndp skpelcgagl hpegysstdv yarnyekgdi eflikdkqsd wvvgmyakrn
      361 dvdltrhytw latpftsays ieskaifgqy vhhlsdktrl igglraeqyd adyldsngft
      421 iatddlmwgg kvaleyqavp rtmiytslsr gykvggvnge alakakdegl niptehhyfd
      481 peyvwnaefg vkgqsedkrh lvrvtafymq rddiqlkqwq vsnqqfagyi dnasegsnyg
      541 lelegtfsyn erlgftysag yleteiedfv aasgisldgr dqaqapnyqy sfavnyelmn
      601 nlvvalgveg kdnyylsdsh neqagnhnli naslsyygdn wsltawgrnl adedivvrgf
      661 rfgnnpldgw qphtyvqyge prvyglsfty el
//
LOCUS       WP_176032445            1038 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Pseudoalteromonas sp.
            McH1-7].
ACCESSION   WP_176032445
VERSION     WP_176032445.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 1038)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1038
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..1038
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=113311
     Region          1..1038
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 mlaqiiiqsl knkflvmlvf lglglmgfra ldkipldaip dltdvqviik tsypgqasei
       61 veqqvtypls twllsvakvk avrgwsffgd syvyvifedg tdpywartrv qeylsraeti
      121 lpdaakpsmg pdasgvgwif qyvlkdttns rdlsemrelq dwflkfelqs vpgvsevatv
      181 ggmektyqvv ldplklmqyg ltiaqvrsai hnanseqggs vmeiaeaeym irgrgylstl
      241 ddfdnialgi vndegmpltl khvatiktgp qlrrgiadln glgevvggiv imrdgenalt
      301 tinhvkakia qlssalpdgv efevvydrsk litasvdnlq skiliemavv avvcfafllh
      361 irstlvvvls ipfslligfl amqwsglnan imslggiaia vgalvdsaiv mvenvnrhll
      421 nhqkrtgiqp snrekykiie taatevgpvl fislliitig ffpvfalegq egklftplal
      481 tktfvmaata llsvtlvpvl msllikgqip detrnplnai lirgytpfin falaspklvm
      541 figgvvavsm vyplmkmdse fmpdlyegdl lympstlpgv siaeagsilq ktdqliktvp
      601 evesvfgkvg radtatdpap ltmlettiql kpveqwragm tlekiiaele skvklpgvtn
      661 twvqpiktri dmlstgvktq lgikisgesl teltalgeqi egllnqlest gsvyaertqs
      721 gryidiepnr veaakyglmi sdiqdvvkfa lgganisevv dgrtrfpinl ryprvyrdni
      781 daletvpflt ptgawvtlgq vasievkdgp aviksenglm sawvfisvtp dvaisdyvde
      841 asallasnid lperytytft gqyehierle kklleviplt vlvifvllyi afrssaqall
      901 vlctlpiais galwfvyfcg ypisgavvvg mialggvaae fgvvitlyln qaraeqsnlv
      961 eavregallr irpkamtvft ivaglipimf smgsgdqimq kiaapmiggm lvspimsmlv
     1021 ipagylvlyr ykqrklee
//
LOCUS       WP_176032474             192 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: glutathione S-transferase family protein
            [Pseudoalteromonas].
ACCESSION   WP_176032474
VERSION     WP_176032474.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..192
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22517
     Region          1..192
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mkligsntsp yarrirmwaa tkqielsyhh idifspeghn elvqynpark ipfllddtql
       61 vcdsnliiry lrekyqlpvp swdqenwlil inacsdslie lllskrsgfd ieqdklffnl
      121 qrerightlh alneactsdt flhcdylqis lyclldwvlf relidlsdyd nlvafhdrlq
      181 hqpiaqktdp rn
//
LOCUS       WP_176032521             427 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: lipopolysaccharide biosynthesis protein
            [Pseudoalteromonas].
ACCESSION   WP_176032521
VERSION     WP_176032521.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..427
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47187
     Region          2..408
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mlnklirqag vllsgnlfas vlnflsvais lkalgvesfg qvtllqayil vislcfnpqa
       61 wqgliryfsl etdqagllts tlkydlicav lgtvlailia plytesfkls eytellqwca
      121 lyvlinqtsv aigilryqer ykalalqnvi savlffvcvl vgfwlalgvd yyvasylltl
      181 glgvvfiqwl clpytlslfk arkdnnvmls narkkefnkf nftvhmtala dipvkqldni
      241 lvgavvsvsa agayrvikqi atistkvtap lnqvlypevn tllaskeysk vkgamlkiit
      301 lllvpslvvv vlasvstgyw ipvmfseell aykwhiitfl lihaiataft pvhpiflalg
      361 yvkrlfmitl fsnlvlcagi lllgpqiglw giviaifiqy vltiicklpl iltrlaremd
      421 esttlht
//
LOCUS       WP_176032535             399 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Pseudoalteromonas sp.
            McH1-7].
ACCESSION   WP_176032535
VERSION     WP_176032535.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Py,B., Loiseau,L. and Barras,F.
  TITLE     An inner membrane platform in the type II secretion machinery of
            Gram-negative bacteria
  JOURNAL   EMBO Rep 2 (3), 244-248 (2001)
   PUBMED   11266368
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Salmond,G.P. and Reeves,P.J.
  TITLE     Membrane traffic wardens and protein secretion in gram-negative
            bacteria
  JOURNAL   Trends Biochem Sci 18 (1), 7-12 (1993)
   PUBMED   8438237
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444639
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..399
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=43822
     Region          1..397
                     /region_name="PulF"
                     /note="Type II secretory pathway, component PulF [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG1459"
                     /db_xref="CDD:441068"
ORIGIN      
        1 mefeykaids ngsrhqgtie andqaqaqqr lnaeglspie ikaiaksssf sglftqkvtl
       61 dqlefftsel slllesgvrv dkgidiirqs nsdpalgrll nqiassikkg eslsqafgkh
      121 ealfgplyis llkigetsgn lpevlqrlaa dlkfqkdlks qvstaltyps viffvclmav
      181 yfvltfivpk msgiftdlsq apwytqmiig vsqffidnql fiiggvitsl vlggyalqqp
      241 earnwlyvqa skipgigaii ttserirfaq smsmmleagl qldttlalta etlkhpdfkr
      301 dakqalkqlk sgkqlgvvls ktrifpdffl siikvgeetg qlpkvfneva nrsrtdleqv
      361 iskfttmlep imllfmggfv ggivitmlls mvsindvpl
//
LOCUS       WP_176032524             419 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: flippase [Pseudoalteromonas].
ACCESSION   WP_176032524
VERSION     WP_176032524.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..419
                     /product="flippase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46710
     Region          5..406
                     /region_name="MATE_Wzx_like"
                     /note="Wzx, a subfamily of the multidrug and toxic
                     compound extrusion (MATE)-like proteins; cd13128"
                     /db_xref="CDD:240533"
ORIGIN      
        1 mrrklfinsa lliierfvvl ffsfasallm aryagtelfg rfstivafgs lflvftqmgl
       61 nnisskyftl yphnsafyln asllvrfifa vliipiayvl gwltltptda ylvallvalq
      121 vgnaatvief ffiakqsita tlvprvvikv ackiallvai ilelpialwi iltgleyill
      181 alayllllkr qppakqerln taprlqrgar lllqrgkwll lsslaavlyl kidqimlasf
      241 vdtqavahya aaaklsefwy vlpvlvanvf mpklvslyra qpklywqlqr rsylyssiaa
      301 iivialtlwl aepvvlllfg eayrssilil qihifgclfi fsrafmsrwl ilsnnhklsl
      361 hshlvgaivn ivlnavlipq yggvgaaiss vvaygmasig fmvfyrstrt ylatlvkvs
//
LOCUS       WP_176032555             300 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ketopantoate reductase family protein
            [Pseudoalteromonas].
ACCESSION   WP_176032555
VERSION     WP_176032555.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..300
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33059
     Region          4..295
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 masihivgdg aiglllaqhl sqshhvtlit rtkravtyhy qqqsdtqvia cqhtlsteip
       61 aksidtliip vkayqvvdai telypklsah gslilshngm vdcskelakl gsnqsayfls
      121 tsiagykikd tvyhtgqgat wfgplnlsaq chyqklfsql fgtfknaqtt sdimpilwrk
      181 lainiainpl saleqikngq lrqpkyaari lnlmnevqfi aakagvnval nelltlaytv
      241 mmqtaenrss mnqdiannrr seidamcgyi cklaakqhit vpynqqllde vkkcelntsv
//
LOCUS       WP_176032624             318 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176032624
VERSION     WP_176032624.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..318
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=35441
     Region          32..303
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mriwslllfa fpllgianep ilplepttgl nadkvslgra lffdkrlsrg dqvscaschq
       61 lpshgadvkp lsrgvnnalg elktptvyna alnirqawdg raqslydqvd spilnpkehd
      121 mtwpevvakl nqdkvlvaqf akvysrgitp htvkdaiatf eeslitlnap fdlwlkdssv
      181 klpesviagy elfkrygcis chqgrnvggn mfarmgtfgd yfgdrntpik kadfgrfnvt
      241 gneqdrfvfk vpslrlaskq ayffhdgsht slesaieama ryqlgrkipd tdmqklvafi
      301 nslaghhhem dlerqnee
//
LOCUS       WP_176032572             543 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: methyl-accepting chemotaxis protein
            [Pseudoalteromonas].
ACCESSION   WP_176032572
VERSION     WP_176032572.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..543
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=58793
     Region          12..543
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mfsnftlrak iitfaaaifv sllavafvgl qalrhasesd niarinqlmk stvnivkqfe
       61 hfaqqnllte qqakkmaiqv lrenkyhdse yvyvvndkmd fvatphdpql hstsfndfrd
      121 asgksiggmv krlvgnevdq iityhwtslr dgeivdltsv vqktprfgwy vgtgisykev
      181 nerywdtaiw lvalslvvai ilttalarfg lslshklgae indvltivkh vsrgnlttpi
      241 ntasckdysi laamaymqdg lkgvveglkq ascalqtqts dsesrsiqle qlthslsset
      301 qmvasaitel tasaqavveh aqqaagsvqe aerqgnaadk ltaqaaqeia lleqqidsag
      361 nniqvldeev snianvltvi qsiaeqtnll alnaaieaar ageqgrgfav vadevrqlaq
      421 rtqtsteeir nmitklqsat qdakasvnls iatsektvsm ssdaskalvq vadslksilh
      481 mshqiaqaaq eqlsagedta qrvvtisdta sqtasvseka hkatdtikal ssnleievak
      541 fri
//
LOCUS       WP_176032672             290 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_176032672
VERSION     WP_176032672.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..290
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31525
     Region          1..274
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mdiiskikeg lghfspaeek varlilaelt faasatigel aekaqvshas itrlarslgc
       61 hnvrdlkfkl tqsaaigerf tsaepiekek isqvytsiqe iltlnaglid eatveqasei
      121 icatrhclif gvgggsslma qecqnrlfrl dvlsnahcdp mmmrmvaatv nkgdvvicls
      181 lsgvspdvrd aaliakeyga qiiaicpngd laniadhhlp iktqesdyif kpsaaryamm
      241 aaidilssev airnqkrsre klrrlktqld qhrdkssnsp padkrfplgd
//
LOCUS       WP_176032676             326 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176032676
VERSION     WP_176032676.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..326
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36173
     Region          7..306
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(28..29,32,91,105,107,139,173,266,269,305)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(232,237,254,266..268,271,293,297)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mksmikrivf fgecmvehna dgvtafggdt fntawylaql lrqvkhdeit vsyatalgtd
       61 gasadltaml saahinqdyi ivtpesrlge ywisldnnge rrftfardks pvkayfnrdq
      121 rliqalqdkq vdaiylsgvs lailcdsqrr clfqalamfk eaggmiffdn nyrqalwpss
      181 eakqsylalm plvdiafltd edeyavygtq gvndiislhq qrsmqpqilv irqgakpcll
      241 vssndtpviy iaaqhikpaf ildtcgagda faggfmaqwl lgtelrsaar fahrvaakvi
      301 qhhgalipeh llpsletqec hyenal
//
LOCUS       WP_176032677             299 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: SMP-30/gluconolactonase/LRE family protein
            [unclassified Pseudoalteromonas].
ACCESSION   WP_176032677
VERSION     WP_176032677.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..299
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32416
     Region          29..297
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mkkillsfll lqssgcvian tnadtedwiv dgvftqgieg pavdsagvly avnyqqqgsi
       61 gkvtakgqve tlltfkngsi gngirfdkeg nmyiadyinh nilkvtssal kqggdlsefv
      121 slfahhdgmn qpndlaimdn gilfasdpnw qassgnlwri nttgevtlle agmgttngie
      181 vspdnktlyv nesvqrkvwr ydideqgnis nkkllitfnd fgldgmradn qgnlyiaryg
      241 agviavaspe gellkeiklt gkhptnvafg gnngkrlfit mqkrgaiema evefagrer
//
LOCUS       WP_176032681             265 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: M48 family metallopeptidase [Pseudoalteromonas].
ACCESSION   WP_176032681
VERSION     WP_176032681.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Lew,R.A.
  TITLE     The zinc metallopeptidase family: new faces, new functions
  JOURNAL   Protein Pept Lett 11 (5), 407-414 (2004)
   PUBMED   15544561
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..265
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=28463
     Region          62..247
                     /region_name="M48C_Oma1_like"
                     /note="Peptidase M48C, integral membrane endopeptidase;
                     cd07331"
                     /db_xref="CDD:320690"
     Site            order(124..125,128,187,191,230)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320690"
     Site            order(124,128,187,230)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320690"
ORIGIN      
        1 mkklvlaiav aatlvgckts ptgrtqlaly seqqmdqmgv asfeqmkqeq kvylsantnr
       61 yvkcianali aqlpthyanq qwevvvfedd sanafalpgg kigvhtgiln vaenqdqlaa
      121 vmghevghvi aehanervsq ssilqlglqa gaavlemnnv eyrnailqgl glgaqygval
      181 pfsrshesea dvigldlmak agfnpegsva lwqnmakmse qrppefmsth papenrikql
      241 eanmvtakat ankarasgft psckr
//
LOCUS       WP_176032690             120 aa            linear   BCT 11-JAN-2025
DEFINITION  GFA family protein [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176032690
VERSION     WP_176032690.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..120
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12985
     Region          7..113
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 maerfvggcl cgqirfiaig vphnphtcsc kmcqrhsgal tlawvefard evswdgeggm
       61 pkiwrssqys srafcpncgs tlgaiddapv ialalgvfdt nsrqslqpis hsysvntwhn
//
LOCUS       WP_176032761             677 aa            linear   BCT 11-JAN-2025
DEFINITION  S9 family peptidase [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176032761
VERSION     WP_176032761.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18486225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..677
                     /product="S9 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=75053
     Region          45..85
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          52..265
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          92..126
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          249..409
                     /region_name="TolB"
                     /note="Periplasmic component TolB of the Tol biopolymer
                     transport system [Intracellular trafficking, secretion,
                     and vesicular transport]; COG0823"
                     /db_xref="CDD:440585"
     Region          429..677
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
ORIGIN      
        1 mpfglkqtli ctllasaalp tvaqtevglq akdifeleya sdpqispdgt kvvyvrnsnd
       61 vmkdakrqnl wlvdtksgaq splfsdehny sqpswspdgt klafvsnlsg stqihvhyva
      121 qnrtalltql qsgisgltws pdgkwlafsq kvaekpavia kmpekpkgak wsdpaividk
      181 ayyqadgkgl ikpgyrhifv lpseggtprq ltsgsyhhgg klawradska ivfsakriad
      241 weykrlegdl fevdfkrnit qltsapgrey apsfskngkq laylstsnel npyrnsklni
      301 mnwqdktsnm iakdfdrsiq aprwisrdrl vfsyddhgkr klasintkgk isditdtvsg
      361 ttlgrpylsg efsanfsgni aftqgsserp advavttrkg kvtrltnlne dllahttlgk
      421 vheityrssf dgeqiqgwyi tppnfdpqkq ypllleihgg phlaygphfs aelqryaaqg
      481 yvvfydnhrg sssygerfam llkykysske dfadhnsgvd amiakgfidk dnlfiaggsa
      541 ggiatayaig ltnrfnaavv vkpvinwlsk vlsadsglgq iptqfpgmpw ehvdhywqrs
      601 plslvgnvtt ptmlmtgeed lrtpmaeteq fyqalklrkv dsvmvkipga phgiagrpsr
      661 miskiehtla wfekykk
//
LOCUS       WP_176032813             286 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176032813
VERSION     WP_176032813.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..286
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31548
     Region          81..267
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mkfsyfndkd gsvltrasrg itglmctlap pvtarlgqvl lmsphgkrdy qfknkkpsge
       61 mniltslgrv hvnifglgsk tvilshgwad nsscfdtlip elvaagycvv aidhaghgqs
      121 cgkrahllaf iealdtlieq leaqrheiva lvghsmgava lmnlpdyhlh nrviiniatp
      181 vqffelmfer vtragisekm ltqvldaita kygthwhhir dkfhdsvsqf qptfihdtqd
      241 kfapfehvha liataperli qtsglghrri lgdtgiiksi tqrita
//
LOCUS       WP_176032818             224 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GntR family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_176032818
VERSION     WP_176032818.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..224
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25232
     Region          6..222
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 msfldeqavt ssdkaffrmr keivegeiaa gsklsemels tkyevsravv reainrlesc
       61 hlverkanvg arvvtltpeg lmelyqirea legmaarlaa qymtegevqd legllssqfd
      121 evknqhsyyq eagdldfhyr iilgsknasl ismlvnglyh lvrmyrvqlg magprvttaf
      181 dehkhivrai snrdpelaei lmrrhiqysk nniaaklasn qshi
//
LOCUS       WP_176032729             262 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE
            [Pseudoalteromonas].
ACCESSION   WP_176032729
VERSION     WP_176032729.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Mathevon,C., Pierrel,F., Oddou,J.L., Garcia-Serres,R., Blondin,G.,
            Latour,J.M., Menage,S., Gambarelli,S., Fontecave,M. and Atta,M.
  TITLE     tRNA-modifying MiaE protein from Salmonella typhimurium is a
            nonheme diiron monooxygenase
  JOURNAL   Proc Natl Acad Sci U S A 104 (33), 13295-13300 (2007)
   PUBMED   17679698
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Persson,B.C. and Bjork,G.R.
  TITLE     Isolation of the gene (miaE) encoding the hydroxylase involved in
            the synthesis of 2-methylthio-cis-ribozeatin in tRNA of Salmonella
            typhimurium and characterization of mutants
  JOURNAL   J Bacteriol 175 (24), 7776-7785 (1993)
   PUBMED   8253666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF047790.1
            Evidence Source    :: NCBIFAM
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     gene            1..262
                     /gene="miaE"
     Protein         1..262
                     /product="tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase
                     MiaE"
                     /EC_number="1.14.99.69"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0045301 -
                     tRNA-(2-methylthio-N-6-(cis-hydroxy)isopentenyl
                     adenosine)-hydroxylase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006400 - tRNA modification [Evidence
                     IEA]"
                     /calculated_mol_wt=29771
     Region          6..256
                     /region_name="MiaE"
                     /note="tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE
                     (synthesis of 2-methylthio-cis-ribozeatin) [Translation,
                     ribosomal structure and biogenesis]; COG4445"
                     /db_xref="CDD:443544"
ORIGIN      
        1 mlekytdllt pinqflgcet phtwiqkasq sehlslllid hmhcelkaaq saaflirkya
       61 iddasaktll swlqpyedfi yrgigegdfs gskneligel tarpeyaynq dilskmvrli
      121 keelhhfeqv ldiirarnip ieyvqasrya sgmikyirtf epaalvdkli igayiearsc
      181 erfaklapcl deeigkfyis llrsearhyq dyidlahqva natdpkrcdv agriqlfrqv
      241 enelissadp dfkfhsgapa aq
//
LOCUS       WP_176032846             282 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176032846
VERSION     WP_176032846.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..282
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32805
     Region          77..234
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 midvslilla lspafllcva weyikhheyy dwrdsmlnal lallhqgsda lallvlmplf
       61 ywlhqfalft ielnlftllf gfilqdflyy wfhrashcih wlwsahvvhh ssnkmnftta
      121 frqsllypiv gmwlfwlpmi llgftptlvf aivainlafq ffvhtqtvnr lgmverifnt
      181 pshhrvhhas npdyidknfa gvliiwdklf gtfveeridi ticygirgaa pkqtpvdvnf
      241 aqwrhmfhrf sqantlkgkw lalfgypthl pdkpkstasv kp
//
LOCUS       WP_176032845             303 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Pseudoalteromonas sp.
            McH1-7].
ACCESSION   WP_176032845
VERSION     WP_176032845.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..303
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34109
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..286
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mntqdlivvm ktaqlgnisa aaaqldmqva tasaaikrve khlgfqlfvr strslrlskq
       61 getylpiceq alalldsgkk qvldndneid gelrltapsd fgrnillpwl delldeypkl
      121 alklilndhn ldfyrdgvdi alrygapeds sfygfkicdv plllcastey lekqgtpksh
      181 edlsehqglf flirgskfdt wkltkneqty kvvlkgrrts ndadvvkrwc aqgagislrs
      241 aidvadqleq gvvqsilndy rveckplwli cpskqminps vrvlrdklrv ycqalvekae
      301 ryk
//
LOCUS       WP_176032930             720 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TonB-dependent siderophore receptor [unclassified
            Pseudoalteromonas].
ACCESSION   WP_176032930
VERSION     WP_176032930.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 720)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 720)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..720
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..720
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80711
     Region          24..720
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mrskahqsaa lslmlsliyf spttlantqn stknieridv vgqpikrnsg ptgldltike
       61 tpqsvtvlsh dfiddfeldd ledvlvqatg isrykfgagd nteftsrgyl inalvkdglp
      121 tsiagpqesr ldtivydrve vlrgaaglma gagqpsatln vitkqpdrdg fvevgaevgs
      181 wnkvrshlda tgaltddkal agrlilayed kdsfvdkens nkivaytqlh hyfsddteas
      241 ftvhyqdsel klspwglpif ysdgssveid kktnlsspds fngnthqsyh fklshqlnld
      301 walnfgaqys kteaditmty fsgnpdkqtg lglqggdrrw vetvdgtnfi lglvgrfdlf
      361 drshqvnvty lnadfestdd ryeeldankr tvfyplqsiy nrhpashlna tdkqfigywd
      421 kttkeqslai ssklvltddl havagikffd yertnerdfa wsgfssdkgd esgeslylgf
      481 vydineqvst yvsytdayep qldkvdvnlk qldpitarni evgvktnlld drlrlnvayf
      541 dslkedfgvv ipeyadqrpa ryrpvdgaea dgfeielnad itdnwqvnlg ysdfdvvden
      601 gedinlyapr qtlnvstkyt yeawsfglna twdtdrkvdi lnvpgvdlgl paggrrgavr
      661 aeqdsqtlin ahvkydyskq lsfklnvsnl tdesfydtyg fvpkkysepr aynfsvkyrf
//
LOCUS       WP_176032945             349 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: OmpA family protein [Pseudoalteromonas].
ACCESSION   WP_176032945
VERSION     WP_176032945.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..349
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37776
     Region          60..342
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          237..339
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(241..242,275..276,279,283..284,287,329,333)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mkiktlsllv amaasataha ntteptegvy lgvfgdyyda dwqnhrdmag ldvedstgwg
       61 aeigyrfdkf wsgrieyadm dfdlggisng sldaerygid glyhfdggpf yglvglkkmn
      121 ldaisdntfa nlgagvrhhf tehlflnaea avyqgleagf tdvggkigin ysfgsagkse
      181 avapapapvv aqapqdsdkd gvvdsedkca ntpmtdavda sgctlyetke dkvsllvrfp
      241 hddatfsqqy vddinavakf lkehknadvl ieghasavgd adynqqlser raknvaeklv
      301 dmgidsmrit tvgygeerlk npantlkaha enrrveahvs skekvkvkr
//
LOCUS       WP_176032961             734 aa            linear   BCT 11-JAN-2025
DEFINITION  CapA family protein [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176032961
VERSION     WP_176032961.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 734)
  AUTHORS   Candela,T. and Fouet,A.
  TITLE     Poly-gamma-glutamate in bacteria
  JOURNAL   Mol Microbiol 60 (5), 1091-1098 (2006)
   PUBMED   16689787
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006724
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..734
                     /product="CapA family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0045227 - capsule polysaccharide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=79565
     Region          128..449
                     /region_name="CapA"
                     /note="Poly-gamma-glutamate biosynthesis protein CapA/YwtB
                     (capsule formation), metallophosphatase superfamily [Cell
                     wall/membrane/envelope biogenesis]; COG2843"
                     /db_xref="CDD:442091"
ORIGIN      
        1 mkkiialmll ltlsacsved pnetgpsdtd knedqsqqdr dneatnlsvq iqtrdgnavs
       61 gatltinslq ftsaangtid latlpfgayv atiqhpdylp lvftfanqhs dpqtielqlk
      121 pssdslktll fagdtmfgrr yfnpslitmg nslpstsdgl iqpqsagada qalvkympal
      181 fnsvdfasvn lespilqnpt tvhpskefaf fslpaslval ndlgidyval gnnhvydyqa
      241 qglsdtiryv eqaglshsga gndtesalap ysltlgetti dfisatsitg dqhtityvas
      301 vqkggaadlt dttairesvn qasndgrfvv aqlhggdeys yaptayianr fdvvsnsgan
      361 lmiahhphva qgfglyngvp ailglgnfvf eqnrletflg litiveleta gepkidaika
      421 ypvyledytp klvsgdlana llkriaefss pdvgislhsg faevnfdtps ivettqqhvi
      481 svaagehiid lrqyaqssey vsrialnqsq aqltlgrdll ffgdfedwdn dteagevsrw
      541 liesddtypc lvgkyrgvqg lclqrtqfde tatrvpfkht irtmpitpap staqayhelt
      601 lygyakgnna grfnadiril tsedsllfse stpellpagt ydwqvfqqdi tlpddsvtlg
      661 denlpargvq fglsmtppts gesalflddv amiswqrsls ltnnqwqsgg ihgfefikit
      721 tpsptelvlt fsqq
//
LOCUS       WP_176032996             772 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176032996
VERSION     WP_176032996.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 772)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 772)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..772
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..772
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86190
     Region          39..747
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msshnyimgt svlfaslnct glsaseedlf slsldqllev kvearkvtes lqrtpisvsv
       61 lsqqqiqqrn itdllsasyf ipnvdvtttg ensgcthcan itirgvgqvd pipttdpsvg
      121 vyvdgvylar sagtmsrfld veqieilrgp qgtlfgknti ggavnirtsp vvdetifkts
      181 ltlgefdrrd ltmvvnqpls dhiairvama kydkdgfvrr vngsqegged dfslsaklhy
      241 qvsddlsfrw qysrqtqsrg sapsilaakn ddailiqlyn ifaelgggve pieplqvfdd
      301 kylsaseqsn snsfrhtgis lqadyrltda mslksitayr sldafysrdf dnnpvnigvt
      361 qdwqwqnqrs qefnltaqfd dydwllgvyy fdenisyrad fnffdglfqa leaiptpidg
      421 splsaptdig gagnplnaaf dfhnrflnei entsyaifgh mnyhfsptws givgarytre
      481 dkrqevtgla leadvlllsr tnqseagavt pswkvfspml glqyqpneha mfyltgsrgf
      541 ksggfnglps saaairpfep ehltayesgl rsqwldnrlr inisafylqh kdmqlrgges
      601 tqegveifid nvgktktrgv ewefeglldd dvgasisgaf trsefvdvgn atqvtldstp
      661 irtpkwslts siwknwylgg nkrlhtrldw syrskmytdv fnspfaqtdh lrllsarvql
      721 dfsehlsisv hannltdeyh figandfrev fgiaeywlap prevgvtmtl nf
//
LOCUS       WP_176033048            2894 aa            linear   BCT 11-JAN-2025
DEFINITION  non-ribosomal peptide synthetase [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176033048
VERSION     WP_176033048.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 2894)
  AUTHORS   Islam,M.S., Leissing,T.M., Chowdhury,R., Hopkinson,R.J. and
            Schofield,C.J.
  TITLE     2-Oxoglutarate-Dependent Oxygenases
  JOURNAL   Annu Rev Biochem 87, 585-620 (2018)
   PUBMED   29494239
REFERENCE   2  (residues 1 to 2894)
  AUTHORS   Reimer,J.M., Haque,A.S., Tarry,M.J. and Schmeing,T.M.
  TITLE     Piecing together nonribosomal peptide synthesis
  JOURNAL   Curr Opin Struct Biol 49, 104-113 (2018)
   PUBMED   29444491
REFERENCE   3  (residues 1 to 2894)
  AUTHORS   Bloudoff,K. and Schmeing,T.M.
  TITLE     Structural and functional aspects of the nonribosomal peptide
            synthetase condensation domain superfamily: discovery, dissection
            and diversity
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1865 (11 Pt B), 1587-1604
            (2017)
   PUBMED   28526268
REFERENCE   4  (residues 1 to 2894)
  AUTHORS   Pang,B., Wang,M. and Liu,W.
  TITLE     Cyclization of polyketides and non-ribosomal peptides on and off
            their assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 162-173 (2016)
   PUBMED   26604034
REFERENCE   5  (residues 1 to 2894)
  AUTHORS   Marahiel,M.A.
  TITLE     A structural model for multimodular NRPS assembly lines
  JOURNAL   Nat Prod Rep 33 (2), 136-140 (2016)
   PUBMED   26429504
REFERENCE   6  (residues 1 to 2894)
  AUTHORS   Strieker,M., Tanovic,A. and Marahiel,M.A.
  TITLE     Nonribosomal peptide synthetases: structures and dynamics
  JOURNAL   Curr Opin Struct Biol 20 (2), 234-240 (2010)
   PUBMED   20153164
REFERENCE   7  (residues 1 to 2894)
  AUTHORS   Schofield,C.J. and Zhang,Z.
  TITLE     Structural and mechanistic studies on 2-oxoglutarate-dependent
            oxygenases and related enzymes
  JOURNAL   Curr Opin Struct Biol 9 (6), 722-731 (1999)
   PUBMED   10607676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13484185
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..2894
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..2894
                     /product="non-ribosomal peptide synthetase"
                     /EC_number="1.14.11.-"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_function="GO:0031177 - phosphopantetheine binding
                     [Evidence IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /GO_process="GO:0019184 - nonribosomal peptide
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0044550 - secondary metabolite
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=324386
     Region          6..>2397
                     /region_name="PRK12467"
                     /note="peptide synthase; Provisional"
                     /db_xref="CDD:237108"
     Region          2294..>2550
                     /region_name="alpha_am_amid"
                     /note="L-aminoadipate-semialdehyde dehydrogenase;
                     TIGR03443"
                     /db_xref="CDD:274582"
     Region          2598..2884
                     /region_name="TauD"
                     /note="Taurine catabolism dioxygenase TauD, TfdA family;
                     pfam02668"
                     /db_xref="CDD:367137"
ORIGIN      
        1 msdgfltspq qrdlfqileh drsgaqivve lkgsvdiaal keslstvver heifqtdytv
       61 ipgmkyplqv laganlewse helsesslte iakvqneefq ksgnsstvyi slvkeaenkh
      121 hiilcchala mdyqavmtml kewsycydai hgsgcpelee plqyidyaaw ldelqmsdda
      181 fegnkfwsny ckdfsprfsf aleepttera ytqhsqvvnl psvyteqlna ycsqhdlraq
      241 dvlcsmwlli vsrmsgqsnq avsfrvegrd deqlqsvmgi vqkdipicvd itefksflpl
      301 vkqlsrqlts iqswqdfykw pecwreease sldigfafyn sastltcsns elswapkhiq
      361 lapslhklal haevnidnni elcwrfdsna yteqviqqin nafitqmryl lsaqvdglhn
      421 ipifeleeaa ldntkvktst gntvnkaihq lvaeqikqcp dkvalehdsd tlsyqelgnw
      481 anaiaqkldd ngvekgevva vfaprsflli aamlgisran avylpldtey peerikymie
      541 dsnvskvicl addqqqleky nlqlitvnkp cesiaynknh eycqdddaym iytsgstgnp
      601 kgtliphhsv iahtlsmiey yqmsvadrsl lfapanfdps ieqiyvalas gatlcirgpv
      661 vwspaelaek iaqyqlsvvn iptaywnhvv ddwqnlpsle kvsslrlmiv ggdrmvadka
      721 nswnelfent vrlinaygpt eatvtalahe vgrdqsnais igqplqgrea yildekmnpl
      781 ppgfvgelyl ggmslakgyi nrdeetrakf vtceigsqrk rlyrtgdrgy ydidglfyft
      841 grndaqlkvq gyrvelgeie sqvhaiagvt eavvighpsn gdadsvelma fftaeaatid
      901 veqlkntlks kmpdymipna lfqvesfpmt psgkvdrkal vseidkyqke esrpylaptt
      961 etetvlakvw esvfsqdkvs inssffglyg nslkamrmia nirdalevkl tikeiydses
     1021 lasmaalide kkgkatskqt qlpeikplsg tediplsygq ermyfldkig estkyhmtgf
     1081 vkisgqidtk alekaiayti arhdslrtkf selgerlcqi vephiqlplq qldmsteadi
     1141 tdlssyratl eswvekpfnl gelplirall vrfaedkwvl glcmhhivad glslniildd
     1201 itssyrdfvq qkdvevvhpa iqytdyakwq rdfinektla nevkfwnkel sgyqnlemlt
     1261 dhprpkvlsg kgervlfnld kgqfdslksl cdsrqltvfs mlisavhlll qrysnqtdfc
     1321 lgipvanreq sqiqdtvglf lntvafnlkg isqdssvgrf lettqekmle vqsnqalpfe
     1381 kvvelvepdr dlsrnplfqv lvnyldlnnn idfagcdael ieplqisakf dltfdfantd
     1441 agglelqiey sqdlynrsti dkigeqllyl leslqaqwls pikdisylse adknailshs
     1501 rgkksdlaat svkdlfaqqv qvsghktaik cegmefsyet ldarsnqvan mllqssqfvq
     1561 gdfvgilmer senilitmlg iikaggafvp ldptypaerl gyivensdmr lvicsdtlsv
     1621 qasqygdevt vcrisetehl sraaaskkle qeqlayaiyt sgstgkpkgv qishgsfvnf
     1681 lmsmqvepgf nrddsilait pysfdialle lflpivsggt cvigsnaqla nieslantis
     1741 dvkpsvlqmt pstwsallnf gidlpnsira lcggesmptq lkrqlldvts dawnmygpte
     1801 ttiwssctki srdesvalgq pilntdlyil denlslspqg aqgeiyigga glstgyiard
     1861 dlnsqsfids pwgrlfktgd mgrwvgerdn lsvqylgrkd tqvkvrgfri elseiesile
     1921 qqadvsaava misgkgdmtt leafvqvidg gsvdtqsllt ilkqqlphym vpnyiqlleq
     1981 lpktpsgkvd rkalanqftv anevqtyelp kskteqelsv mwcdvlgvsh vsktdgffkl
     2041 kghslklasl ykrikahfdv tfslrdlfea dsleqmasli drhtsggnkq eaiirntsat
     2101 egplsfaqqg lwladqidnh htrynnvaai altgslntak leqaincvve khavlrtaim
     2161 mdvekgiphq klaaigtval pieplhhlpe feqpdainkv vteeeayqfn lsaaplwrar
     2221 llqlspekfi lvlnfhhiit dgwttrlfis elcrfyeqgh neqsttdtcd svsyidyavw
     2281 qrdtrkdelq qlrfwqqyla dmpntmlals dksvpqagdv itgsqqyelg adltsqlrrf
     2341 sdqthfspfm llqtafnlal aaltgekdiv igtdvanreh yqlentmgff vnqvalrnav
     2401 dhdskvsefl dqvksntldv lsnqevpfek vvnhlrgtqa nrkspifqik lfldqapdte
     2461 ialenvhcev ldigepkarl dltlglleys dtikgklvyn anvisekrvd ellaifeaal
     2521 rqiaagadtv kvgelinslq qnlatqrqnq enallekqst lkitgrrrga dnngsaivlt
     2581 ppsnisepms isasqpgvnl rnwinsnkai vdsyysryga ilfrnfnvgs venfssianl
     2641 lisdlvedng ehnpvdghat vqtpvqysse hhllwhnent fnstwpsrim fgcqvaaleg
     2701 getplvdtna vyqalpvevv ekfkqhgvmy vrnysrtddv glgwesvfct tdkaiverkc
     2761 keqnirfewl ekdklrtyav rpafvtdqen kcywvaqiqh whfsclddnt rqsiatvyse
     2821 seyprncyfg ngdkiedgfv sdllalykkl essfawqdgd allvdnvmma hgrnpykgdr
     2881 kllvsmgnli tfes
//
LOCUS       WP_176033133             271 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: carbon-nitrogen hydrolase family protein
            [Pseudoalteromonas].
ACCESSION   WP_176033133
VERSION     WP_176033133.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10166075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..271
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30127
     Region          3..265
                     /region_name="nit"
                     /note="Nit1, Nit 2, and related proteins, and the
                     Nit1-like domain of NitFhit (class 10 nitrilases);
                     cd07572"
                     /db_xref="CDD:143596"
     Site            order(41,94,111,115,128,153..154,156..157,178)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143596"
     Site            order(41,111,153)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143596"
     Site            order(112..113,134..136,154,157..161,163..164,186..187,
                     190..191,193..195,197..198,228,258..259,262..263,265)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143596"
ORIGIN      
        1 makvialpmc saqtaevnla ylrrqlallv ieeetlvclp eswlafcena qqawegahhs
       61 eqyltelsal crqygiwlaa gtiatlgvde kylaasylfn scgeivaryn kihlfdanis
      121 dktkqyrese rtlpgqeivv adspfgkigf svcydlrfas lyqamrvlga elflvpsaft
      181 catgaahwqp llqaraienq cyvvaaaqsg nhengretyg hslivspwge iladtktsle
      241 pisqkidral ldsirrnmpv mdhnrfksef l
//
LOCUS       WP_176033160             639 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176033160
VERSION     WP_176033160.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..639
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=69861
     Region          114..608
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mrvstftrll aillttasil lgasllwask vlteldvqga aynqvkntvi ielegtiedy
       61 lsagdsqyls kadaqinalq qdvnnlpeal saqirqklqq lqqdisekyr algklsgnel
      121 alldnalrqm sgsasslvky aikaqesdlk aayfelasdy fsevsnlsly tyqlvmsyep
      181 qteqslmasl rrltdiaqqi eqlenlgvms evdedelflg aeaedlalei kaelvswpkr
      241 ygrdlnntlq qskerqagml alrgdiksis enilqaeaql iadqaavkan vfmlfggaig
      301 llvilagtvy lvqfkqvltp lrqlrdgfaq liesnelsni ksknqdteig eiasyfnqli
      361 drqraeader samlgvintf meemntnlak istqaggtfe qveknqaqld svrqlgaean
      421 hinaqvadna nntfeamtqs vayaesmlsa ssttqkrveq gleslnellt gvsdvskvid
      481 missiaeqtn llalnaaies aragehgrgf avvadevrkl aqqtqasltd ihqqlnalsd
      541 nsnkvstqis aladeaqqqt nhaqelkrns egvahsaqsa nqvaahamel anqqsdlldt
      601 fgkamdnmkg qvnsshqqvq qiqqslkekm qeirstlgl
//
LOCUS       WP_176033164             670 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-binding protein [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176033164
VERSION     WP_176033164.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 670)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 670)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 670)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 670)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 670)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 670)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418077
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..670
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=75944
     Region          156..664
                     /region_name="HerA"
                     /note="Archaeal DNA helicase HerA or a related bacterial
                     ATPase, contains HAS-barrel and ATPase domains
                     [Replication, recombination and repair]; COG0433"
                     /db_xref="CDD:440202"
ORIGIN      
        1 mdvsaslitd lliegkrkes figrpfylsy disrllvcda wkadvkgipa gafllafydg
       61 edgveeavll ralsqtklpt dndvitsmie yykdnldisg ragsekkgkl deftryefsf
      121 sglecrvlgv fyrgengkie fgadlenfys annysvykat gdvlefivnq rdddgiagqk
      181 sdfkigsvry sssrrhqaqe etvkvwvnpk dflgkrsamf gmtrtgksnt vkkvieatee
      241 isqkalipll sappetlefd qsgspsfpvg qiifdingey ananrqdsgt aiydlykekv
      301 vrysvlekgn dfkvmkvnff kdiesgfsli ssylqeqsig gdyvnnftav sfeppestnp
      361 hgsdwtrynr liaaykccly ragfkptgen vrfkgaseln saiieggtid pskgisleea
      421 ctwfekvweq ydesefikgy vnkkgyewan ddlksmmvfl stykspgkkt qvsgykklrv
      481 kqllalhtts mdesfeseip kflqdgkivi vdlsqgepvv qrlfsekicr stfniamdrf
      541 iknlpnnfiq fyfeeahnlf pkkddkdlsq iynriakega klhlgmiyat qevssissni
      601 lkntqnwfia hlnnidetke lekyydfkdf tqslvrfsat ndkgfvrmkt ytnpfivpvq
      661 idrflankgm
//
LOCUS       WP_176032895             615 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: M1 family metallopeptidase [Pseudoalteromonas].
ACCESSION   WP_176032895
VERSION     WP_176032895.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   Evnouchidou,I., Koumantou,D., Nugue,M. and Saveanu,L.
  TITLE     M1-aminopeptidase family - beyond antigen-trimming activities
  JOURNAL   Curr Opin Immunol 83, 102337 (2023)
   PUBMED   37216842
REFERENCE   2  (residues 1 to 615)
  AUTHORS   Agrawal,R., Goyal,V.D., Kumar,A., Gaur,N.K., Jamdar,S.N., Kumar,A.
            and Makde,R.D.
  TITLE     Two-domain aminopeptidase of M1 family: Structural features for
            substrate binding and gating in absence of C-terminal domain
  JOURNAL   J Struct Biol 208 (1), 51-60 (2019)
   PUBMED   31351924
REFERENCE   3  (residues 1 to 615)
  AUTHORS   Peer,W.A.
  TITLE     The role of multifunctional M1 metallopeptidases in cell cycle
            progression
  JOURNAL   Ann Bot 107 (7), 1171-1181 (2011)
   PUBMED   21258033
REFERENCE   4  (residues 1 to 615)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   5  (residues 1 to 615)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176143
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..615
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0004177 - aminopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=69619
     Region          27..463
                     /region_name="M1_LTA4H"
                     /note="Peptidase M1 family including Leukotriene A4
                     hydrolase catalytic domain; cd09599"
                     /db_xref="CDD:341062"
     Site            order(155,157..158,283..287,308,311..312,315,330,334,341,
                     392,397)
                     /site_type="active"
                     /db_xref="CDD:341062"
     Region          504..611
                     /region_name="Leuk-A4-hydro_C"
                     /note="Leukotriene A4 hydrolase, C-terminal; pfam09127"
                     /db_xref="CDD:462686"
ORIGIN      
        1 mtklsaltls lamaglvhta nvnaavdeht yanlndvitt hlhldldvdf ddkqlegfve
       61 htldwqnsqa ttlvldtrdl eidkvmyqgk sgnwhiakfd lakrddvkga kltihfkeqa
      121 kkariyynsl pvasglqwlt pqqtaskshp fmysqsqaih arswipvqdt pamrvtysar
      181 vqtpkdvrav msadntgafi kdgdywfdmp qaippyliai gagnleykem shqtaifaep
      241 qildasvaef ndtqamidkt namygeyawg rydllmlpps fpfggmenpr lsfitptvva
      301 gdkslvnlia helahswsgn lvtnatwedl wlnegftsyv enrimeevfg rdravmeqal
      361 daaslraqlk tiaapdtrmn lelngrdpdd afssvpytkg qlfliyleek fgrdrfdkfv
      421 ktyfntfsfk slttdefvay ldknllqqyp givslekake wiyepglpsd apnptsdafe
      481 kvdaltqawl kdektladlp tdawtvhewl hfinnlprdl aiermealdk afqltqstna
      541 erafawymla vgngyqaiyp dlekhlvsig rrklivnlyk slinngkrdw ayrvyqqarp
      601 gyhplaqgti dalfk
//
LOCUS       WP_176033253             326 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sterol desaturase family protein [Pseudoalteromonas].
ACCESSION   WP_176033253
VERSION     WP_176033253.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..326
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36975
     Region          125..291
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mleqlwqsii dlpgylfdan krvylpylfs ailmaipvyf aaeqarsgkg flrfmfpkrv
       61 wwcqsakldy cllvtnrlik aatftpivlt mvpvalalss aleamfgpal hldapewvvv
      121 llftlflfiv ddltrfllhl mlhkipflwe fhkvhhsasv ltpftiyrsh piesylyacr
      181 maltqgivvg sgyyvfgssl smydilgana fvfifnicga nlrhshiwls wgdkiegwfi
      241 spaqhqvhhs dnpahfdtnl gsalaiwdrm ygslikaska ekitigvgqy daghdtltai
      301 ylkpfklawk tllpknkknh pplkpr
//
LOCUS       WP_176033409            1051 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit [unclassified
            Pseudoalteromonas].
ACCESSION   WP_176033409
VERSION     WP_176033409.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..1051
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=116432
     Region          12..1024
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msdiekapqr giiayfannp vaanllmvfi limgfisymt iqrqmfpnfe inyvtvsavy
       61 pgaspqeiee gilvkieeal kdvteikkgv yraargsgsa qleiykdedl tevedkirsr
      121 vnsiatfpas mepaqvqlve frqdvvnval agnlplnalk piakeiedel leiptislvd
      181 rstpnyeigi evdpdalrry nltisdvsna irrystnisa gqirtdsgii avrvenqmyr
      241 gnefrnipvk vgdngakiyl qdiaeikdgl tegeyyfrln genavflsvk atkdqnmipi
      301 aqavhkyiee knqtlpsglr lepivdmtyy lnarlemmks nmlqgallva imltlflrfk
      361 lalwvmiglp vcflgaflfm palgisinii slfafimvlg ivvddaivig esayseierk
      421 ghsvknvvig akrvatpatf gvlttiavfa pmlfssgpes affksisgvi ilclifslie
      481 skwilpahia htkikpmran srraafnkkf fafvngpykr fiercvewrw tvllsfvaml
      541 vfslslvtsn lvrfipfpkv pedypkieit mndnvsdeqt iaamqaielm vrnvdkeivq
      601 efgqgiikdv yawnqsrtkg svlatlveed lrpftafela rrwreampei tavksiivyd
      661 svgeqsggeg efgyrllgsd idtlnaagrq liamlqqqpg lfdisssidp askevqialk
      721 pvayelglql sdvaiqvgns fyggeaqrvi rdgeeikvmv rypeldrral aslkrtiitt
      781 aqgkevmlgd vvefiekpgi nyirredgfr tvyvygside eliepdavvk niednilpdl
      841 lkqfpgvktk lggsveerqa qtseqilffa agmlmvyill avplksyaqp livmsvipfs
      901 lvgalwghli fgldmstmsm fglvaaagvv indslvmtdy inqaraegvr ikeavveagc
      961 arfraitlts ittfagvmpi ifetslqarf vipmavslgf avlfatlitl vlvpalylil
     1021 advqaagarl kgkirrkplt ddepldeaei q
//
LOCUS       WP_176033462             793 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176033462
VERSION     WP_176033462.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 793)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..793
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88918
     Region          41..755
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mkplgkipfa ksticlsmla asssfyatae tqsddganeq iekitvtsrr keetiieipm
       61 qvstissmdi adrnlvsaed fyrtlagaas prgqlilrgl sggntafpdt tsvfvddvpf
      121 tfenlndver vevlrgpqgt lygsnaiggt vriitkkpvl defeffastq igsekdvdgl
      181 hrnismgvni plvddtlalr vsgntehery qmvnmntgvq gnadrgfirg qllwqvdpet
      241 svtlgyahtt fsdtgtttgd rstpgyywdy sltaneeady gydvdffkvs cpetaerpqc
      301 nagsapiank gvpqkyqiwd lmdpwsdatn dlftiniqdd nifdiaslty agshrtyeed
      361 siqtswsrld asdmfrtwii dhrkyervth qlrfqnidin splswtigay ydeveygfdp
      421 nyqnqyhekg dkvsalalnw wgadatqigi dtfgnpqnnw nltnirdyte elaffadvay
      481 efdlgdsgsl evnggvrrfe lkdgshytqe giwatsednl sgeesgnryk fsvsyrptee
      541 msvyglyseg yrpggnngpl aasceadpla knrkdrytsd aienyelgfk asvldrkvdf
      601 saavyridwt diktsvymdt cgfsytangg eaksegfefe starltddlt msfntsytss
      661 eitqdnesis asagdkmtmv pewnaylald qniqlfgkda yirgeysfyd eykthfnvrd
      721 edktpaysvf nvsgriqlsd slklsvfvnn lfdketatym rarsrnanns aaqeyinyln
      781 grtislrvdy tff
//
LOCUS       WP_176033473             552 aa            linear   BCT 11-JAN-2025
DEFINITION  GspE/PulE family protein [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176033473
VERSION     WP_176033473.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..552
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=61219
     Region          1..541
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mtqemktlae lllsagaikq deidfalqeq vitgeklsev lerngfvsqr alaqqlatll
       61 klpyidlahy ipepealkkf nfnlckgsqf iplkcdertl tiatsnenid glralvykyc
      121 qlhldihlae kgviqkllhn hyfylnnpve kilqdeidhl iadkesvrtl dtlltnilrf
      181 avkkratdih irpmeksisv afrvdgvmrs afalpkelsr ltstikmras mdiaeqrlpq
      241 dgsfevvvng lsydirvstl gcpygenlva rilprevelr slsqlgflpe hlgliesmfn
      301 kpsgiilltg ptgsgktttl haglssldml kknivtvedp ieyrlplarq tqvnekagyg
      361 fadairhflr hdpdvilvge irdnetahta vtaaetghlv lstlhtndvm gviprlrsld
      421 vsnhmiadsl vgvvsqrlvr kncrhcseev qstaeemqyl gldkpvvlak gvgceacght
      481 gflgrvpvye imsvdkslch lielnkpvse lyahakagny vsmhsvatsl vlngtttvde
      541 lqnlvakeve yn
//
LOCUS       WP_176033556             703 aa            linear   BCT 11-JAN-2025
DEFINITION  multicopper oxidase family protein [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176033556
VERSION     WP_176033556.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 703)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 703)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..703
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=78809
     Region          86..695
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mknlilpilg vvmtasctsv ehsheshtad hpnhseqhkv fepnyfdlrd ynpvnitpef
       61 isaahtqgin scdyqyiape ldkfvapavi qskggslnft lavqyherei agcntwlrny
      121 aykqdgqkef kpapvgptlk vapgdvlrft lenrlpscel apdylcsgkg haghhsnaml
      181 sdeeanhint phnfnvtnfh thglwvspse rsdnvlleiq pgqgfeyevr ipeshpqgtf
      241 wyhahvhgst alqvssgmag aiiieggnpk kdigtqaqik dktdqlfvlq qvaydcngti
      301 eyyeaderpe yvkdckaddk alnifgpgdw qktkrrtlin gqvvpkiemr pneiqrwrfi
      361 hagvretikl svidkpewqn nmnpvplgfl nqisvdglnt gridrwqldg qkteiealqp
      421 gyradylyqa pskagvywlv dldsapqksl qgvpedtael lqivvkgepv askdavlpts
      481 aelisyrahd aptqgeiaam dksenkesmm fylgsrvsvn aaiatakqek kdfncqniwn
      541 edinngvlld nhhlsdkekg kdtifsvdgk pygqietrel tlgtwqrwdl ctrglapmhp
      601 fhihvnpfya prvgpdgkeq wvwrdtlaie kgadkpktde ngvnlsgsap htvvyskyry
      661 peslpgfngn vkqqytgefv lhchildhed qgmmqkvkli esk
//
LOCUS       WP_176033568             153 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176033568
VERSION     WP_176033568.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009501
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..153
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17227
     Region          1..153
                     /region_name="COG5628"
                     /note="Predicted acetyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:444356"
ORIGIN      
        1 mnivkvdtnn aqvyanlyqg ygaefspiid dkpnenglfe iypqltgsvt gyllyldgip
       61 aaltaideks pkayeicdfy vlpyfrknkv gkrfisslfe qlggsweikq vagaehatsf
      121 wrdvvgdyts gnyiediyed hkwgtvtrqc fsh
//
LOCUS       WP_176033596             283 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176033596
VERSION     WP_176033596.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 283)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20139405
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..283
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31420
     Region          <45..132
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
     Region          155..276
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 mgagtfkikn mslaeletav qwaqqegwnp gvndaycyfh adpngflmgy lgdepiatis
       61 vvkydggfgf lgfyivkpey rgrgygikmw haamqylksc nigldgvvaq qenyeksgfk
      121 layrniryeg igggdkphlt nlvslkdtsf dvlkayeekf fpaprteflq awihqpnsya
      181 cgiyeegklf acgvirpcht gykiaplyae spelaeqmfl alksqvpqss piyldvpevn
      241 aaaialaqkf rlsavfetar mytgqfpelp lekvfgvtsf eig
//
LOCUS       WP_176033625             306 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator
            [Pseudoalteromonas].
ACCESSION   WP_176033625
VERSION     WP_176033625.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34036
     Region          10..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(103,107,146,160,162,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(104..105,109..110,112..113,116,120,122..128,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mkdvfsaipi fvavveagsf slaaerlgmt ksavskriss lednlgtrlf hrstrklvlt
       61 esgeefsdya rnsvyiaqqg itaatlnqgk pkgtlkinap mtfsrlhlap hlkefldlyp
      121 dikvilsmdd qvvdmiagay dvgirigelk dssliarkla kcnsvvcasp eylqqagipn
      181 tphdlkdhnc iyyslfqagv ewtffkadkk lkveptgnfi vnnsdaicem llqglgicqm
      241 ptfivqryln tgqlvpvlan ydlpdhsifa vyperrhipe kvkvfidfle eklhsvywev
      301 dsgkss
//
LOCUS       WP_176033651             386 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: Gfo/Idh/MocA family protein [Pseudoalteromonas].
ACCESSION   WP_176033651
VERSION     WP_176033651.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..386
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41858
     Region          5..276
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mdnckirmam vgggegafig avhriaarld gqielvagaf ssdpqksitm gkqlglaptr
       61 cyddyhmllq seaalpeser ihfvaivtpn hlhfpiaaka ieygfhvlsd kpatlnlsea
      121 lqlqtllqqt nclyglthty tgypmvkear hriatgelgn irkvvveysq gwlaseddeq
      181 skqaswrlda sqsgisccmg digvhaanlt eyvsgltits lcadlntvvc grqldddgtv
      241 llrfdngakg vllasqialg eennltlkiy gdkasiewsq mepnslwlrm kdapaqllrt
      301 gagtlchaat natrvpaghp egyleafani ylnfamliqa rqqqpdvqpe dfdvpsiqaa
      361 vrgmafiena vaasaketkw hpfnig
//
LOCUS       WP_176033816             798 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176033816
VERSION     WP_176033816.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 798)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 798)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13784517
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..798
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=86728
     Region          21..234
                     /region_name="MacB_PCD"
                     /note="MacB-like periplasmic core domain; pfam12704"
                     /db_xref="CDD:463676"
     Region          <165..798
                     /region_name="ADOP"
                     /note="Acidobacterial duplicated orphan permease;
                     TIGR03434"
                     /db_xref="CDD:274576"
ORIGIN      
        1 mianylvtal rafkqqkqhf vlnvlglsvg laaailvalf aknelsydsq qpnadrvyri
       61 sqdfselgla vvpifnysna klaleysqve dvfgltmvel treamvdvrv geqgyklnal
      121 ygatpniesf idistlsgdl knalstpnsi alsesealri fgsvgiignt lqhqsgqytv
      181 ravfadlpdn thfafknlvh vkhdptklgm nssyvyvrla pntdvaalek tlseryyyee
      241 magkisinlh plfalhltak spfemkagga kqvvmicvgl svlliliasf nfinmtvaqs
      301 akrakevgvr kalgasktql viqflsesvl valfstilac vlvelllpsf nglvdralfi
      361 dyispfggai fvvamsvgil aglypaffms sfsakrvlsg dlqrgntaif vrkslltlqa
      421 slsigliias atllqqlahl qslplgyqtk qrlviselpv edvftkqpss lvnritaieg
      481 velatildtr ltvsinntlq ptwpngeasq sltpvigsgf nivkglgltl lagrdfspey
      541 ssdwayreng vtkvstiise qvakqagyhn vadiigktik dtgrsvdmlv vgvvedvkvg
      601 ntkdassnim flcgfsylss vseliltinp hrlpeittqv taaladvadl yepkinlled
      661 nykavlkade rvsqvvlift tlavfltclg tfglasfatv rrqkevavrk vlgasrvsiv
      721 nilakeflml vavsvaiayp vtywlvgdwl anfndritqd fwvygiaafa vagitwltva
      781 tlafkaasmr pslilrye
//
LOCUS       WP_176033739             376 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: GNAT family N-acetyltransferase [Pseudoalteromonas].
ACCESSION   WP_176033739
VERSION     WP_176033739.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..376
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43714
     Region          3..375
                     /region_name="COG3146"
                     /note="Predicted N-acyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:442380"
ORIGIN      
        1 mteyqhrfih sltevteaqw ervspphvft syewllalel sgctsketgw iphhlmierq
       61 geliailpgy ikshsygeyv fdwafaeaye rhgvdyypkw lcgvpftptq gpriltkaps
      121 adlleyinat ltslaplgis gvhinfcqqs dlltqshltm rrnvqfhwhn kgyagfedfl
      181 arltsrkrkm vtkerqavta qginiswidg keistaqlda fflsyqltyl krsrhqgyls
      241 rdffqqviil mpdkfrlcca ylnhdiiats lylvdgdtly grywgaieds ydflhfelcy
      301 yqgieyaian qlavfdagaq gehklvrgfe pvwrqsyhrl fqpdfqqale dftkreadal
      361 ehyfiecqak lpfkhq
//
LOCUS       WP_176033817             235 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein
            [Pseudoalteromonas].
ACCESSION   WP_176033817
VERSION     WP_176033817.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas
  ORGANISM  Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 235)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Pseudoalteromonas"
                     /db_xref="taxon:53246"
     Protein         1..235
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25847
     Region          1..218
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mikltnlnrv frtqdietta lnninlvvne gefvaimgps gcgkstllsi lgmldsptsg
       61 qfefagtdia gysekqlsql rkasigfvfq sfnlideltv fenvelplqy qniskkerkq
      121 rveqilkrva idhradhlpq qlsggqqqrv avaralvinp kliladeptg nldskngeev
      181 mamlrelnre gttvimvths ekeggyadrl vrlldgqvml dkanaqgqpp kseva
//
LOCUS       WP_176033844             714 aa            linear   BCT 11-JAN-2025
DEFINITION  M3 family metallopeptidase [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176033844
VERSION     WP_176033844.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417402
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..714
                     /product="M3 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=80039
     Region          38..714
                     /region_name="Dcp"
                     /note="Zn-dependent oligopeptidase, M3 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0339"
                     /db_xref="CDD:440108"
ORIGIN      
        1 mkktviaaai ystlfvsgcs nystemtsav saetayinpl lnvstltyqt pmfdkikdeh
       61 fmpaftlgma ehleeveria snpatptfen tlvameksga llkrtssvff nligtdssvk
      121 rrqlqkelap mlaehrdnin lnaalfgrik slydnrnsle ldseskrlld vyytnfvrag
      181 aklsaedkek irkineehss lttqfsqnll aetsaisviv ddkaaldglt erqilatkra
      241 aeaaghkdky ligitnttrq pilasltnra lrqqiwqasa yraqsgdndn tqiiirlaql
      301 raekaallgy kswadyglek qmagnpkavy dmlgsmvpav vsnvekeaad iktliqsegh
      361 sfdikpwdwa yyaekvrqsr ydldetevkk yfefnnvlen gvfytmnkly gvsfkarpdl
      421 pvyhpdvkay elfdnngesl aiffadyfar egkrggawmn sfvgqselln qkpvvinvmn
      481 iakapdgept fvsynevttm fhemghglhg mfsdvkypsl agtavsrdfv efpstfeedw
      541 aahpevisny akhyqtgepi pntlldkvir srtfnmgydt leymasalld mewhtispeh
      601 aptdinefeq aalekhgval dyvppryksa ffahsmgggy sagyyaymws eilaadayay
      661 vqklgglkle ngekyrkhil svgnsrpvmd sykafrgkep ttaallkrrg ldpk
//
LOCUS       WP_176033877             464 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine
            ligase [unclassified Pseudoalteromonas].
ACCESSION   WP_176033877
VERSION     WP_176033877.1
KEYWORDS    RefSeq.
SOURCE      unclassified Pseudoalteromonas
  ORGANISM  unclassified Pseudoalteromonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="unclassified Pseudoalteromonas"
                     /db_xref="taxon:194690"
     Protein         1..464
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=49481
     Region          2..454
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 mikmdfswla avlktsynge nlavanintd trtiesgevf lalkgpnfdg hrflevakar
       61 gaiaaivscp dedidlvqfv vddtrialgq igkavidtva pktiaitgsv gkttvkemca
      121 ailaqkgkvl atkgnfnndi gvpltllrlt eedqyavvel ganhlgeiay ttalvspdva
      181 tvcnvapahi egfgsidgvg kakgeifsgl kvngvavina dsdyaamwqe nltvtnvkry
      241 slheqldiwm devaldelar ptfklcrdnq svrvslplsg qhnvsnalia aalttelgas
      301 leevatglaq maevkgrvnm iqvsdtlrvv ddtynanvks vnaaidllas msgykvlalg
      361 dmaelgegar eyhkevgeya kqqgidelfs lgvlsssasn vfekpnrhfs treslmkalk
      421 vvlaeqsgrc tvivkgsrsa rmellveelv nagqsdsetg evtc
//
LOCUS       WP_176033931             893 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Pseudoalteromonas sp. McH1-7].
ACCESSION   WP_176033931
VERSION     WP_176033931.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 893)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..893
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=99000
     Region          51..646
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mthkcnqifn cacgsklwqs llpkdfnpsc elndqtedna tesfimhain ggtiltmreg
       61 mnenveaigi kdgkicaags fedvkkefsd svpkveeieg aatlipafie phvhiipsav
      121 inagldlspf ygqqlrenvf pkdkynfdwv kkvltekadn mtagegwilg hnmdpslfss
      181 gnkvinadkl dgisnsvpiy itntsghlay innaaikvid ehnisveaen gskkqkkvst
      241 gkngvleels emvpvlkvli etydyengki klqakerikq efdklfesav shgstymlda
      301 aldekqieil kayakssksk vriggaylid sldqlntsig slglpnsgde dfnlsflkli
      361 adgssqgltg yqytpydcne nyevfahaeq sdfneenedk ikklaeqnit glfnygypie
      421 fnglmriann ygwptmthan gdhaidrtls afkqagitkn tidqrrdrie hcsllspstm
      481 aemehlgisp sftighvgyw gwnfkntiig qqradqldlc asainnhgmr itlhsdysvt
      541 pmgplrymeq aitrlmesap nqnlevlnpn erltpfqalk amtydaawqc hadkwvgsle
      601 vgkcadftil aesplryqnr knmaypaqgm rdipvlktfk ggkqvfvqpq esylsniswd
      661 nqnkaltfky tgpkvsppkg veakiwyqlq dengdaltdk ytepmnnvyf nrkveictes
      721 lskfdsatkf ylvagvflqs kkadviaasa lidkccgtse vndktsinkl qlmpssgsis
      781 fevpsdiqkp kngtcwlfit dvntnygwdn gqvapnlegd gstqgtstdt giyycknltd
      841 eliespidld sldlelgkty kvgiclgsny riaayavtqc vdkpqrinpi gtl
//
LOCUS       WP_176033900             188 aa            linear   BCT 11-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Pseudoalteromonas
            sp. McH1-7].
ACCESSION   WP_176033900
VERSION     WP_176033900.1
KEYWORDS    RefSeq.
SOURCE      Pseudoalteromonas sp. McH1-7
  ORGANISM  Pseudoalteromonas sp. McH1-7
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Pseudoalteromonas sp. McH1-7"
                     /db_xref="taxon:2745574"
     Protein         1..188
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=20332
     Region          19..187
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 mskyalifpp nfklvlyama vmcvvqvlgg lfgfpvyrfg ivphdihhls svftapfvhg
       61 swghlmsnll glsisgylaa rlpkfkrstf fivvatgllv wlfagnanhi gasgivmgyf
      121 glllgaalfn rdilgivsfv tllvltyyan isflatlfdf saqtsssshi fgflsgllaa
      181 yitkpkrv
//
LOCUS       WP_176034126             133 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease, partial [Burkholderia multivorans].
ACCESSION   WP_176034126
VERSION     WP_176034126.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 133)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 133)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 133)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 133)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         <1..133
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          <3..127
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 rvgvyismth illpfmilpl ysvmksippt yqraavslgs hpfaafwrvy vpqtypgvga
       61 gallvfilai gyyitpallg gpndqmvsyy vayftnvtin wgmacalggl llaatlvlya
      121 vygrftrtnv slg
//
LOCUS       WP_176034229             288 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia
            multivorans].
ACCESSION   WP_176034229
VERSION     WP_176034229.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..288
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=32099
     Region          5..277
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mfdqivfagg gnrcwwqagf wdvaqpalgl rprviagisa gaatacmlyt rdaawvmryy
       61 eealrenrkn vywrnlfgre pvfphyriyr qalldiygep faqlasapei rigvshvprw
      121 lgarsavaag lvayniekyl rktlhptlgr tlgfrpefvr aqdcahvdel adlilqssct
      181 ppftpvlrrg grpvldggmv dnvpvgalda spgdvlvlvt rryprpqmft vahgdqrrly
      241 vqpstkvpis swdytspaqm qhaydlgrrd gehflarvga mtdgrvaa
//
LOCUS       WP_176034168             842 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Burkholderia multivorans].
ACCESSION   WP_176034168
VERSION     WP_176034168.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 842)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 842)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 842)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 842)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 842)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10833107
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..842
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..842
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87833
     Region          135..191
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(140..142,145)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          235..829
                     /region_name="Haloacid Dehalogenase-like Hydrolases"
                     /note="The haloacid dehalogenase (HAD) superfamily
                     includes carbon and phosphorus hydrolases such as
                     2-haloalkonoate dehalogenase, epoxide hydrolase,
                     phosphoserine phosphatase, phosphomannomutase,
                     phosphoglycolate phosphatase, P-type ATPase, among others.
                     These...; cl21460"
                     /db_xref="CDD:473868"
     Site            order(525..529,679..680,707,726..727,730..731)
                     /site_type="active"
                     /db_xref="CDD:319763"
ORIGIN      
        1 msdaqrlrdp rddtdgsgtc ctgparsapa qrtadaarca hgdaasrgas shassrdhda
       61 apavgtdahr khehhaahgh ghdeaghehn hahahdhshe hrhdhedscc appaptlapl
      121 paaeataagn vrsafrimqm dcpteetlir kklggmdevs alefnlmqrm ltvehvpgaq
      181 paierairtl gmtpeaasag tpasaapaea pakpwwplal agaaaiasea aswaglpawl
      241 sallaivavl scglttyrkg wialrngnln inalmsiavt gamaigqwpe aamvmvlfti
      301 aelieaksld rarnaiqglm rlapdtatvq dadgtwrtid aarvvlgaiv rvkpgerigl
      361 dgevvsgrst vnqapitges lpvekatgda vyagtinesg sfdyrvtala snstlariih
      421 aveeaqgaka ptqrfvdrfa riytpivfav allvaiappl vvggawrdwi yralvllvia
      481 cpcalvistp vtivsglaaa arrgilvkgg vyleegrkla wlaldktgti thgkpvqtdv
      541 dahaadidls rarhlaasla arsdhpvsqa iaaaardana pafadvqdfe allgrgvrgt
      601 idgvrywlgn hrlveelerc spaleaklda lerqgksvvm liddarvlai favadtikdt
      661 sraaiadlha lgirtamltg dnphtaqaia aqagiddarg nqlpedklaa vdelarggag
      721 avgmvgdgin dapalaradi gfamgamgtd taietadval mdddlrkipa fvrlsrathr
      781 vlvqnigfal gvklvflglt vaglgtmwma vfadagasli vvgnglrlls narafggapa
      841 ar
//
LOCUS       WP_176034240             907 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia
            multivorans].
ACCESSION   WP_176034240
VERSION     WP_176034240.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 907)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 907)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 907)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 907)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..907
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..907
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=94971
     Region          47..855
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mrksiksrar lqfalkpsha cvlaalggva athagaapaa earptpevrf sdtlllkgrg
       61 qridvsrfgr gnpvapgeyt vdialngkwi grsalrfvgv pgsdsaalcv daalatrlaf
      121 ddaaltdvgr aelakiragd cgdfalladg asyrfdqadf rleltvpqaa lqrqprgyvs
      181 pelwdagips atlkynfnty rsssfghasn maylglnggi nvagwhlrht gsyawstgsa
      241 grydavstyv qrdlpalrsq vtlgevftdg sifdsvglrg vtiatddrml pdsqrgyapl
      301 vrgvansnah vkisqngntl yetnvppgaf eindlyptgy ggdllvtvte angsthsftv
      361 pyasvsqslr egntrfsvsl gqfreqlvda hpnfaqatiq hgfsnlftgy agaiaargyv
      421 aglvgsafnt rwgafavdft qakaqipgaa sttgqsarit ysklvpatdt siaiaayrys
      481 srgfwtarna iyarslvasg rraddvarer sqlqltvsqn lgarwgsaya igsmqnywnq
      541 pgsttsvqlg ysntlklagh nlsynlsfsr qrsgfaqdfd nqlyasltip lgksiqaptl
      601 saslsrdtrg gssqllglyg sagengefsy svtgsrspgs lygggtaqyr apftslsaga
      661 sggsgqsqfs agvsgalvah sggitfandl getaalvear dakgarvtng sgiridgrgy
      721 aivpslspyi lntisidpkg ipldvelqst srqvaprana lvavrfatat graalitarl
      781 pdgnslpfgt hvfdstganv gviaqsshlf vrgipesgvl takwgngpqd acsfsyrlpt
      841 aprkdagyar vdaicgggal adapsyaipl ssrpaiddag dsavptqhad tqvsasrnps
      901 atkeisq
//
LOCUS       WP_176034330             147 aa            linear   BCT 11-JAN-2025
DEFINITION  HIT family protein [Burkholderia multivorans].
ACCESSION   WP_176034330
VERSION     WP_176034330.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..147
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16752
     Region          1..126
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mecvfcredg gevlwqddrl rvalatgehd ypgfcrviwg ahvaefsdlg dderahlmrv
       61 vyaveravrr vmqpnkvnla slgnmvphvh whviprfsnd ahfpqpvwap rqrsvseall
      121 rtraaqasll hnavreeiqr tndprqp
//
LOCUS       WP_176034244             257 aa            linear   BCT 11-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Burkholderia
            multivorans].
ACCESSION   WP_176034244
VERSION     WP_176034244.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..257
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28459
     Region          12..253
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mssplqsesi reqvaelrer gfvvarglvg eqqcatlkri aqqqleeaaa piefeadlry
       61 pgapeskhap gghtvrrlld aygrdpafae raiapeigaw mreyfgeqpv lsrahhncmm
      121 tkhpaygslt gwhrdfrywa feradmvsvw lalgpetnen galwlvpgsh taefgpdafd
      181 dakffrsdlp anramidaat cpslntgdvv ffhcntlhsa gqnrsddvkf slvytyhgis
      241 nrpipgarsa skpevqf
//
LOCUS       WP_176034407             126 aa            linear   BCT 11-JAN-2025
DEFINITION  sirohydrochlorin chelatase [Burkholderia multivorans].
ACCESSION   WP_176034407
VERSION     WP_176034407.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..126
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=13192
     Region          1..>126
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 mtshgivlfg hgardprwae pferlatrlr aaggaaqvsl aflelmtpsl daavaaqaaa
       61 gctrvtvvpv ffgqgghvrr dlpqlidacr aahpgveirc atavgeddgv ldaiarycid
      121 qlerda
//
LOCUS       WP_176034392             459 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia multivorans].
ACCESSION   WP_176034392
VERSION     WP_176034392.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..459
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48987
     Region          7..457
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mtrqqqsfdt ivereqglrh altsgqmami aiggaigtgl flgsgfaigl agpsvlvsya
       61 vgalialllm galaemtvah ptagsfgaya ehyvgplagf lvryaywfav vfaigteisa
      121 iavfmkywfp avpgwywvig fsalliavnl asvtlygsve yafsllkiaa ivvfivlgay
      181 lvwsappasg igfanytahg gfmpkgpwgt wvavivaifs ymsieavaia ageardpqha
      241 vtrafrstvf rlvlfylltl slmlaivpwt qagtdespfv kvmaathvpy aagvinfvll
      301 iaalsamnsq lyvttrmmfs lsrarlapav fgrlgangvp raalwistsg vavaavlvav
      361 spdtaftvmm aiamfgalft wlmifvthlr fraryrgpal afrmwghpvg sllgaalvas
      421 illttafthe frmtmavgvv fvvllvgaya lhyrhehar
//
LOCUS       WP_176034474             421 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia multivorans].
ACCESSION   WP_176034474
VERSION     WP_176034474.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..421
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=43969
     Region          205..412
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(212,252,290,393,396)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(212,393,396)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(212,252,290)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 msfrsslaat vlgasvllsp favraapagw vaawatalqp ipelaspppl yrapdvagrt
       61 vrqivyptas graarirvsn aygraplvie aaslgrageg aaladgaaap vrfggkasvt
      121 lapgqeldsd pvaldvvagr pyaisfymgp kqrmtvwhrv snqlnyvssa gdhvndagaa
      181 afrtrftqya wvtelaveag gahasvaaig dsitdglrss lnrnrrwpda farrladaga
      241 tsigvvnlgi sgnrllsdsp cygaalasrf erdalsragv kaaivligin dinfaamppr
      301 agldcddpht rvtaaalidg yrrlidaahr rgvkvfgatl tpadlppare airlevnrwi
      361 rsggafdgvv dfdaalrdpa rpsvlqyryd sgdgihpsda gyaamaeavp lerlkaiaag
      421 e
//
LOCUS       WP_176034545             540 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia multivorans].
ACCESSION   WP_176034545
VERSION     WP_176034545.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 540)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..540
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58989
     Region          10..537
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msgttvstqd epllslehln vrfgdtvavd dvtfaigrge rvalvgesgs gksvtalsil
       61 rllrdadvgg tirfagqdlg akseremral rgadiamifq epmtalnply tigaqiaeti
      121 vlhdgvsaae arkraialla rtgiaepdrr vdsyahqlsg gqrqramiam alacrprlll
      181 adepttaldv tiraqivdll lelqreeaek rgmaillith dlnlvrrfae rvavmergrl
      241 vesgpverif aepqhpytqr llnsrpqrav apvmpiapvl ldarhvsvqf arkrpglagw
      301 fgttpvtavs dvsvsvrqge tlgivgesgs gkstlamall glqktvhgdi qfqgralsty
      361 rgreqtalra nmqvvfqdpf sslsprhtie rivgeglelh rpdltpdarr aksvavlrev
      421 gldrtvlhry phefsggqrq riaiaralvl eprvlildep tsaldvsiqq qvlkllanlq
      481 qkynlgyvfi shdlevigam ahrvavmqgg mivesgdveq ifarpshpyt qkllkavwka
//
LOCUS       WP_176034556             273 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Burkholderia multivorans].
ACCESSION   WP_176034556
VERSION     WP_176034556.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..273
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28440
     Region          2..272
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mlktrvitai amlavllpvt lyaplaafga liavvlvfaa wewarllklp gagpvvyaiv
       61 aalalaatap lgidaaasrp lfaaagvfwl lvgpfvlrrk pelagrvwrp fllaaglvif
      121 aacwhalvaa raqgvpfvls lllvvwladi gayfagkafg krklavtisp gkswegavgg
      181 wlavmvvsgi amaahrfept lfsayamhyg mggawaaltl lvvysvigdl fesllkrqag
      241 vkdssgllpg hggvldrvda llpvlplaml llg
//
LOCUS       WP_176034607             281 aa            linear   BCT 11-JAN-2025
DEFINITION  NRDE family protein [Burkholderia multivorans].
ACCESSION   WP_176034607
VERSION     WP_176034607.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Bard,F., Casano,L., Mallabiabarrena,A., Wallace,E., Saito,K.,
            Kitayama,H., Guizzunti,G., Hu,Y., Wendler,F., Dasgupta,R.,
            Perrimon,N. and Malhotra,V.
  TITLE     Functional genomics reveals genes involved in protein secretion and
            Golgi organization
  JOURNAL   Nature 439 (7076), 604-607 (2006)
   PUBMED   16452979
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..281
                     /product="NRDE family protein"
                     /GO_process="GO:0007030 - Golgi organization [Evidence
                     IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=30695
     Region          1..253
                     /region_name="Tango2"
                     /note="Uncharacterized stress-responsive protein, TANGO2
                     (Transport and Golgi organisation 2) family, contains NRDE
                     motif [General function prediction only]; COG3332"
                     /db_xref="CDD:442561"
ORIGIN      
        1 mcliafdwqp daaagpvftl aanrdeffrr tsaplswwed vpgvlagrdl eaggtwlgvs
       61 rdgrfaaltn yrapfdirag aptrgklvsd ylggpavapl dylaqlaeha avyngfnllv
      121 gdwkrrelaw fcnrapeges raapplavaa gvhalsnarl dtpwpkvvrk raelgtlltd
      181 nptpsldeli almrdtrvad ddalphtgip lereralsaa fietpeygtr gttalrvtmk
      241 egvrltveik ersdddgshr tvrpgefera fafdidvttp r
//
LOCUS       WP_176034563             144 aa            linear   BCT 11-JAN-2025
DEFINITION  NfeD family protein [Burkholderia multivorans].
ACCESSION   WP_176034563
VERSION     WP_176034563.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Green,J.B., Lower,R.P. and Young,J.P.
  TITLE     The NfeD protein family and its conserved gene neighbours
            throughout prokaryotes: functional implications for stomatin-like
            proteins
  JOURNAL   J Mol Evol 69 (6), 657-667 (2009)
   PUBMED   20012272
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Kuwahara,Y., Ohno,A., Morii,T., Yokoyama,H., Matsui,I., Tochio,H.,
            Shirakawa,M. and Hiroaki,H.
  TITLE     The solution structure of the C-terminal domain of NfeD reveals a
            novel membrane-anchored OB-fold
  JOURNAL   Protein Sci 17 (11), 1915-1924 (2008)
   PUBMED   18687870
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..144
                     /product="NfeD family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=15121
     Region          18..142
                     /region_name="YbbJ"
                     /note="Membrane protein implicated in regulation of
                     membrane protease activity [Posttranslational
                     modification, protein turnover, chaperones]; COG1585"
                     /db_xref="CDD:441193"
ORIGIN      
        1 mmsaqlfwwv gvgvlvvael ltgtfyllmi algfvaggll qlagfaphvq igaaaaialv
       61 ammalrrsgl grkqkrdtst npdvnldiga tvtvgawhdg rarvqyrgae wdvelaager
      121 ddarvyqvsa vrgnclvvva kpag
//
LOCUS       WP_176034614             369 aa            linear   BCT 11-JAN-2025
DEFINITION  C40 family peptidase [Burkholderia multivorans].
ACCESSION   WP_176034614
VERSION     WP_176034614.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..369
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37676
     Region          <6..175
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mlriwvpvav vsllaacssv ppqtasrssg mtiktprafp ppanfpkfvd hsvgqeeisi
       61 qamslvgvpy rwggntpasg fdcsglvryv mdraadvnlp rttadmssrg vsiepdqiap
      121 gdliffnttg rphshvgiyv gklrfvnaps tggtvrldyl tnpywakrfd girrvappra
      181 tptpfdapty earrdesrtp ataavsaptp aapapvvmat asqppayaat qaprvsaapp
      241 aavaaaaapv stvstvstaa aapvdpyepp parlsaarqq aasaggdaia atsntmpagt
      301 pevgtpiptt altaaeaaaf daeppaaaap srnseaavqv lrastqsapv gartgtaddp
      361 iarfangsy
//
LOCUS       WP_176034616             153 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia multivorans].
ACCESSION   WP_176034616
VERSION     WP_176034616.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..153
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16738
     Region          14..126
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(15..17,31,48..50)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(62,65,69..70,79,97,101,107,111,114..115)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 msmteskpsa agpltigeva almrvsthtl ryyeqagllr aisrnaaghr lyapadldwl
       61 afvmrlkstg mpiaqmqqfa alraqgeptl garrrllvah rdavrahlae lqasldaige
      121 kiahyealer eserqasssh slkeqdehhg tsr
//
LOCUS       WP_176034652             390 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia multivorans].
ACCESSION   WP_176034652
VERSION     WP_176034652.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..390
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42119
     Region          29..390
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mksqssppat gapsfvspsg spsgadarae nfvqiidvvk kfgdteavrs vnlsvrqgel
       61 fallgssgcg kstllrmlag letvtsgkil idgedlaqmp pyrrpvnmmf qsyalfphms
      121 vesnvafglk qegtpkaelk ervaaaldlv qmgkyakrkp hqlsggqqqr valarslvkr
      181 pklllldepm saldkqirqr tqielvnilh kvgvtcimvt hdqeeamtma nrlavmsegq
      241 ivqigspnev yeypnsrfsa efigstnlfd gvtvedepdh vyiesselps rlyvshgitg
      301 plgmpvtvsv rperialtrk ppegafnwar gaitnvaymg gyslyhvkld ggktvianvs
      361 slaiseldtp algdeiyvrw satagvvlts
//
LOCUS       WP_176034629             748 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Burkholderia multivorans].
ACCESSION   WP_176034629
VERSION     WP_176034629.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 748)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..748
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..748
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=80970
     Region          43..743
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mnspleatpd arrdaspgrv rasegtfels rkrvdeldai freggllara ldgyrprasq
       61 iemaravasa measarrmpe peifearkrp arrlgetggg aadagvsdaa neadadagdn
      121 tliveagtgt gktyaylvpa mlwggkvivs tgtkhlqdql flrdiptvrn alavpvtvam
      181 lkgranylch yylqrtadng rlpsrqdtay lqeivrfaki tksgdkaela svpetapvws
      241 mvtstrdncl gqecphykec fvmqarreaq qadivvvnhh lffadimlrd tgmaellpna
      301 ntvifdeahq lpetatlffg etlsttqile lardtvaegl shardavewv klggaleraa
      361 rdvrlafadd qivrmslaql gddhplfaal daleaaldal asalasqaer aeslgaclrr
      421 arelqdllag wvapgaaeaa aqadaaaagd aaaaagdpne kvrwvevfah tvqlhetpls
      481 vapifakqra gvprawifts atlsvrgdft hyaaqmglss rrsmtlaspf dyqtqgllyv
      541 prnlpqpssp aftdavfdaa lpaieaaggg vfmlcttlra vdriasklrd viesrgwntp
      601 llvqgdasrt elldrfrayg nailvgsqsf wegvdvrgda lslvvidklp fappddpvla
      661 arldalakkg lspfavhqlp qavitlkqga grliraetdr gvlmicdtrl vdkpygrriw
      721 qslppfkrtr eiavvqdffd eqraarra
//
LOCUS       WP_176034708             338 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia multivorans].
ACCESSION   WP_176034708
VERSION     WP_176034708.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146979
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..338
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36920
     Region          180..317
                     /region_name="Acetyltransf_8"
                     /note="Acetyltransferase (GNAT) domain; pfam13523"
                     /db_xref="CDD:433280"
ORIGIN      
        1 mlaevrpdgy tvpdtcrltf anelcaardg aeirvshgdg igaqllraql tddgalrlva
       61 ynhraapaeq rravlaalaa afavdvarps vrldaaawpa valdalrasg vlgdggqcmr
      121 egwaqqadlw lvearppcat lptltdgrrh prrppaprae vyardmpalg vrftlrgwqp
      181 addpariarw fdaprvrdgw pgaqpgtaad fephvtplvg cfdgepfayf eavwlkedal
      241 aphvaardyd ralrmlvges rwrgahciaa wlpsvvhylf lddprteaig cavpaghari
      301 adllarhgfa rrrrlaladg qplwmctrrd tffsgrhv
//
LOCUS       WP_176034693             388 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia multivorans].
ACCESSION   WP_176034693
VERSION     WP_176034693.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..388
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42205
     Region          1..386
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mqfdltddqr aieraidkic arfgddywle rdraggfphd fhaalaeagw lgiamdpayg
       61 gaglgmteaa lmmraisasg aglsgasavh mnifglnpvq vfgsdaqkar flppliagrd
      121 kacfavtepd agldtthltt qarrdgdhyv lsgrkiwist aqvankmlii arttpleqva
      181 kptdglslfy tdldrsrvev reidkmgrka vdsnmlfidn lrvprddlig aegegfryll
      241 hglnperili aaeaiglgqa alrratqyan ervvfgrpvg qnqaiqhpla lawmqleaaw
      301 lmvmkaatry dagqpcgaea naakylgaea afhacqtava thggmgyake yhverylrec
      361 miprlapvsp qlilcyiaek vlglpksy
//
LOCUS       WP_176034714             343 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia multivorans].
ACCESSION   WP_176034714
VERSION     WP_176034714.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..343
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=37213
     Region          206..340
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 msgarrsraa grlrawfgws vcmllialaq pawavrcvan gggtvltesi gnvasyptda
       61 pdgyviwvsp prtttgycyk dlggsmktfg ewiyfyanpe qqnpaawgle igirylgqdy
      121 fgrssqpgdg vqtstyvqpc rlsdadvrag rcekfplsit yqvvvrkrgs wtqppsdvya
      181 vfqfdgkggl nyinpsfryk lsglqklkpt pcmvdvkvtp epgvvkfgqi qatangfspa
      241 vprktfsval tkqcsvpvrv dgyfetaqtv rngllvpaad snfgigiedr ngtaipfnqq
      301 fvlaqmpgsv nyqsvtldav lksfgapkig pftgtatirl fiy
//
LOCUS       WP_176034791             739 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia multivorans].
ACCESSION   WP_176034791
VERSION     WP_176034791.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..739
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=78358
     Region          70..>208
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          210..707
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msrglieagh agaamsrrsf lrfgmslgaa aggglllgfs lpaagddtrr sviggdadep
       61 aragvfapna fvqidrsgrv tlvmpkvemg qgvytalpml iaeelevpls svtldhappn
      121 eklfldpllg gqltggstsv ryaweplrra gatarvllvs aaakqwnvdp aachaengev
      181 rhppsgrras ygeladaaak lpvptdvtlk kpeqfkligt pakrldspek vdgvaqfgld
      241 vrlpgmlyav ivnspvfggt vasvddtaak kipgvrqivr vddavavvgd htwaakrgas
      301 alvvkwnega nanvstkdlf adlaqaaang kgavarkdgd vdhafsnakt rvdavyeqpl
      361 lahatmepvn ctvhvrsdac evwvgtqvpt rardtaqrit glpaehivvh nhllgggfgr
      421 rletdmigqa vkiakqvgap vkvvwtreed iqhdmyrpcy hdrisaalda ngkpiawrhr
      481 ivgssilarf appafkdgvd pdavevaidl pydvpnqlid yvrqeprhvp tafwrgvgpt
      541 rstfvvesfi delaaqaktd pvqyrralld ktprarnvld iatkaagwga alpqgqgrgv
      601 svmhafgsff aivadvavdd gevrvtrvvc avdcgmtvnp ntieaqvqgg iifgitgaly
      661 gevtiengrv tqrnftdyrv lrinetppid vhivksgeap ggigepgtaa taaavanaif
      721 aatgkrlrkl pignqlkta
//
LOCUS       WP_176034763              96 aa            linear   BCT 11-JAN-2025
DEFINITION  putative quinol monooxygenase [Burkholderia multivorans].
ACCESSION   WP_176034763
VERSION     WP_176034763.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..96
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10715
     Region          4..86
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 maeiavvali vakpgaedkl ravlerivep trnevgalqy dlhrdlkepa rfvfierwes
       61 eealaahars ahilayreaa adwiersevr vlskla
//
LOCUS       WP_176034871             424 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia multivorans].
ACCESSION   WP_176034871
VERSION     WP_176034871.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..424
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41730
     Region          5..>327
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mrshadspaa hhggsltifq gaalyigavl gtgvialpal aadvagpasl lawaalvvls
       61 aplaatfaal garypdaggv styarrafgp kaaavvgwcf yfavpagapa aamfggayva
      121 avtgggqttv iataaaliai vsaanafgvt vsgrmqlvls allvtlllaa vlasaphart
      181 anlhpfaphg wlavgqaaal lvwsfagwea ithlaaefrr pahdmprsag iavvvvglly
      241 lsvaaasvmv lgpsagasga plaeliaggi gghaqvlata aallltlgtm nayfagaakl
      301 gaalgrdgal pawlaqgsqv ggvprrslaa iavlaaaala attlagvgpt plvlvtsgcf
      361 vmvyglgaaa alkllprgsi ayrcawisli avaglfvttg wyvvcpllla ggallylrmm
      421 vrrg
//
LOCUS       WP_176034875             673 aa            linear   BCT 11-JAN-2025
DEFINITION  BCCT family transporter [Burkholderia multivorans].
ACCESSION   WP_176034875
VERSION     WP_176034875.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..673
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73238
     Region          3..514
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mpdsrssprt tfkpqvvlps laligallvv callpdeaga lfsagqqwvv arfdwfyvla
       61 vtaflvflvl iaasdfgnir lgpddagpef sfvswtamlf aagmgiglmy fgvgepmqhf
      121 lkpptvepas pgaareamlm tffhwgfhaw aiyglmglvl ayfgfrynlp ltlrsglypv
      181 lrervngwig havdafalvg tvagiattlg ygvmqisagl htvagwdtgg nafrvglval
      241 vvilaglsaa sgldkgvrrl selnlllafl llafvaiagp ttfllralsd nigqylsslv
      301 dlsfrtyaya pprdegwfgg wtilywawwv swspfvgmfi arisrgrtir qfvigvllvp
      361 tafnlvwmtv fgnsaiwlda hdaagalaqt atnvdallfr ffdflplsql lsivaillia
      421 vffvtsadsg afvidqiatr gaarspvwqr lfwaallgvt aavllvaggl galqamtlma
      481 alpvaiimla lcyglwrgla adrahysqdv apatsfwtgq hwrhrlthil rqtteadarq
      541 fvadtvmpal rkvadelrag gvdahvqrds ddavrltvpt aeqrdfvygv rltaktapaf
      601 lmreaaepqs arpqvygiit ffedgrlgyd ieylrgdevi advlrqyery vslaadkrth
      661 llsrapghat ese
//
LOCUS       WP_176034797              99 aa            linear   BCT 11-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Burkholderia
            multivorans].
ACCESSION   WP_176034797
VERSION     WP_176034797.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..99
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=11454
     Region          6..99
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mpvkartvrl tplaeadlea iwsytyerws ldqaeryige lsaafkrlar resvgwpsra
       61 ggnysrylvg shvvfyrett etldvirvlh qrmdvdrhl
//
LOCUS       WP_176034916             434 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia multivorans].
ACCESSION   WP_176034916
VERSION     WP_176034916.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46336
     Region          9..417
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(22..23,26..27,30,69,127..128,130..132,135,155,
                     158..159,162,245,248..249,252..254,257,285,289,344..345,
                     349,353,369,372..373,376..377,380)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 maidsrvvrr vaaasvigat vewydfflyg vvagivfdkq yfpaddafvs tmlayatfav
       61 gfitrplggl lfghlgdrvg rksaliltml imgvstagva flptyaqigm wapallltlr
      121 vlqgiglgge wggavlmaye yapphrrgly aslpqiglai glclaagvva alsrvlpdaa
      181 flswgwriaf aaslllvavg fyirtrvadt pefvalkrqr rdtklpvvel lgsyrraill
      241 gmgaryidgv ffnvfavfsi gymtrnlsis rgdallgvms aavvmcafip vfgslsdrlg
      301 rarvyrwgat lcglsvlpaf wllhahstnl ltvwlalvip fgifyamayg peaalfaelf
      361 danvrytgis fvyqvsgifa sgitpivata llranggepw lvgvyvmlsa llsivsarai
      421 eksggvagva vrat
//
LOCUS       WP_176034966             421 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia multivorans].
ACCESSION   WP_176034966
VERSION     WP_176034966.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 421)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 421)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 421)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..421
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45325
     Region          <198..391
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mntmtiassp qsgaalkrel kaaearkrtm allliaplai flllvfvvpi gtlltravqn
       61 peiaaalpnt vaalshwdrk tppadaayaa laadmtkvad sdamgalarr lnteipgyrs
      121 lvaktaramp lkgdadaalt paqtrarlie ldarwgevay wqaiakngsa yspfyllaal
      181 dhkqdgfgsi vhadpdqsiy laifgrtfvi giavtlfall lgyplaywis tlserranla
      241 milvlipfwt svlvrvaawi vllqneglin kaligsglla hplallfnrv gvyismthil
      301 lpfmilplys vmksipptyq raavslgshp faafwrvyvp qtypgvgaga llvfilaigy
      361 yitpallggp ndqmvsyyva yftnvtinwg macalgglll aatlllyavy grftrtnvsl
      421 g
//
LOCUS       WP_176034980             412 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia multivorans].
ACCESSION   WP_176034980
VERSION     WP_176034980.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..412
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42768
     Region          22..399
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(32..33,36..37,40,72,127..128,130..132,135,156,
                     159..160,163,235,238..239,242..244,247,271,275,328..329,
                     333,337,353,356..357,360..361,364)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mnvatqagwv srlfpalsea slrrylsgqv asvlgswtqn vtlnlliyhl sgsaailall
       61 nfllygpqli vapvagarig stnarrvtlc vlttslllts slfalsligl lgvklilaha
      121 laigvssave tparqvlllt slrdathtsn avamntmvyn vgrmvgptia gfvyptlgpr
      181 asfaiyalal cfmaacvrsi rtasvnrpsr aesglrdavg yvlsdafsar ylpilacigl
      241 fagsyqtlvp lladqgfhda arftgvffac agagslsaav llssafgpga srrfiayapw
      301 tavgaltvla attdavgsip afyalgfslt faatstnati qrqcpehvrg glvgmygmay
      361 ngtmpfgyll vgsasealgv rhtfaamaav lacgvmavia wqrftdsrsg aq
//
LOCUS       WP_176035051             788 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia multivorans].
ACCESSION   WP_176035051
VERSION     WP_176035051.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 788)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 788)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..788
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..788
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85693
     Region          70..770
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mlltlaarpt rgrlalacaa afalpgayaa ssdsaptdpv rdpanrsara vvpaasavsa
       61 aaaepagdtl savsvtarrq pldpdtpavv esmtreridt htnvttedal kyapnlmvrk
      121 ryigdrnsvf agrdfnelqs arglvyadgl llsnllgssy aypprwslia pddiarvdvl
      181 ygpfsalypg naigstvllt trrpdkleas lstqfftqry rdgygfadsf ggnhqtaria
      241 nrigrfwfsl sldrlendgq pmqyaspnas ynaklgravp vtgaatdigp ngkartivga
      301 qslerteqin etvrmgyaft drvdatltlg hwenhyrqhg dtflrdaagq pvyggnvaig
      361 gqnltiapga fapqrgdqen wlyafglngr lasgwrlsgi vsaydvsrdv lraastaqgg
      421 agtlfqgdgt gwrtldlkae apevhghaft fgyhydnyfl rnvtyntadw lngpvtslas
      481 vyrgdtrtqa lyaqdawrfa pgwlatlglr yerwdaygga lgnasgtfgy adrsanalsp
      541 kvalqwdatd vwrfrlsfat gtrfptvgel fqgtisnnai vnnnptlrpe kaidwdftae
      601 rdvgvgvvra svfqsdlrds iysqtsvaga stvtnisnvd rvrvrgvela fsgenvglkg
      661 laidanvsas naqiladaan payvgsrfpr iprmranlla syrfdehwla svgvrysgrq
      721 fntldnsdvn pdvyggtsaf tvvdvkaryr fdrhwtasvg idnltdrryy vfhpypgrtf
      781 ygelkwsl
//
LOCUS       WP_176035058             436 aa            linear   BCT 11-JAN-2025
DEFINITION  replication-associated recombination protein A [Burkholderia
            multivorans].
ACCESSION   WP_176035058
VERSION     WP_176035058.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..436
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=47972
     Region          1..434
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 msdlfqvepr rplaealrpk tladvigqth llgegkplrl afesgkphsm ilwgppgvgk
       61 ttlarltala fdcefialsa vlggvkdire amdqaketln rtgrhtilfv deihrfnkgq
      121 qdallpfves glvtfigatt enpsfevnsa llsraqvyvl ksltddemrq llkraqhial
      181 dglefddkav dtligyadgd arrflnlleq aqtaassagv ttidgdfvgs amtlnarrfd
      241 kggdnfydqi salhksvrgs spdgalywfc rmvdggadpk ylarrivrma wedigladpr
      301 amqiandaae tyerlgspeg elalaqaviy lacaaksnag ynafnqamaf vkqdksrevp
      361 vhlrnaptkl mkelgyghay ryahdepnay aagetylpdg mrephwykpv prgleskiad
      421 klawlreldr eagkkd
//
LOCUS       WP_176034849             130 aa            linear   BCT 11-JAN-2025
DEFINITION  TraR/DksA family transcriptional regulator [Burkholderia
            multivorans].
ACCESSION   WP_176034849
VERSION     WP_176034849.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 130)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 130)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 130)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..130
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14332
     Region          3..121
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 malderqrha llqrlneseq alraelrase dqrasesyae lagaspdegd eanadlfvdv
       61 dhaligmkla elrairraqq rmvdgsygdc idcagpvgya rlrarptaer cthcqalyer
      121 ryataprasl
//
LOCUS       WP_176035072             543 aa            linear   BCT 11-JAN-2025
DEFINITION  LVIVD repeat-containing protein [Burkholderia multivorans].
ACCESSION   WP_176035072
VERSION     WP_176035072.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Adindla,S., Inampudi,K.K. and Guruprasad,L.
  TITLE     Cell surface proteins in archaeal and bacterial genomes comprising
            'LVIVD', 'RIVW' and 'LGxL' tandem sequence repeats are predicted to
            fold as beta-propeller
  JOURNAL   Int J Biol Macromol 41 (4), 454-468 (2007)
   PUBMED   17681373
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..543
                     /product="LVIVD repeat-containing protein"
                     /calculated_mol_wt=56785
     Region          127..527
                     /region_name="COG5276"
                     /note="Uncharacterized secreted protein, contains LVIVD
                     repeats, choice-of-anchor domain [Function unknown]"
                     /db_xref="CDD:444087"
     Region          164..199
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
     Region          206..253
                     /region_name="LVIVD repeat"
                     /note="LVIVD repeat [structural motif]"
                     /db_xref="CDD:293789"
ORIGIN      
        1 mrfmtrvaia tsistlvlag cggdddtvsa tpavsvadyv vprvpscspg dtpetalqgq
       61 vpaalrqsgf ggfncnlkrv sqlqgegasw saatytdkqg qtcfyhatig ptpifnnpda
      121 pprvnpgvpv inisdpvhpv rvtsltstam idpweslrvn vargilaadn glgsaggpel
      181 dlydiatdct rpqllasvpv gtgadggvvp gtaplghega fspdgltyyi gsptaksyya
      241 vdltiptrpk lisaismael gfgsgphgls vsqdgtrayf valgnagaaa gmgpppldnl
      301 nsngdngffv vdtsevqnrr pnaqmhriat vpvrdgsvaq htipflvsgk pyllevdegg
      361 agglqdpsat avkaacnagm tpfplghiyd maneatprli selrlethvp qncskvipdl
      421 qglstftygs hycsvdnren atalacsyfn sgvrvfdird pskpkeiayy nppsakspga
      481 gsghlmlgqy rpggpdwcta rldfdfdrhl lttacsdngl lvlsfengsw pfpestkake
      541 ign
//
LOCUS       WP_176035127             212 aa            linear   BCT 11-JAN-2025
DEFINITION  2-hydroxychromene-2-carboxylate isomerase [Burkholderia
            multivorans].
ACCESSION   WP_176035127
VERSION     WP_176035127.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Thompson,L.C., Ladner,J.E., Codreanu,S.G., Harp,J., Gilliland,G.L.
            and Armstrong,R.N.
  TITLE     2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class
            glutathione transferase from Pseudomonas putida
  JOURNAL   Biochemistry 46 (23), 6710-6722 (2007)
   PUBMED   17508726
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122490
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..212
                     /product="2-hydroxychromene-2-carboxylate isomerase"
                     /EC_number="5.99.1.4"
                     /GO_function="GO:0018845 - 2-hydroxychromene-2-carboxylate
                     isomerase activity [Evidence IEA]"
                     /GO_function="GO:0043295 - glutathione binding [Evidence
                     IEA]"
                     /GO_process="GO:1901170 - naphthalene catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24030
     Region          12..191
                     /region_name="DsbA_HCCA_Iso"
                     /note="DsbA family, 2-hydroxychromene-2-carboxylate (HCCA)
                     isomerase subfamily; HCCA isomerase is a glutathione (GSH)
                     dependent enzyme involved in the naphthalene catabolic
                     pathway. It converts HCCA, a hemiketal formed
                     spontaneously after ring cleavage of 1; cd03022"
                     /db_xref="CDD:239320"
     Site            18
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239320"
ORIGIN      
        1 mttgldtaqp awffdfvspf syllleqhdk wpampfepva vslnelqrhw gqrpsadvpa
       61 kriftyrhal fraeqlgirf kmppvhpfds dkalrlaiat radiatvlem frfiwregnd
      121 pstpagfaal cervgvsdgd aliefeetsa qlrrntddai algvfgvptf wmnrqlfwge
      181 dalpmvlyca rtpnwlesqe vkristlpkg ra
//
LOCUS       WP_176035128             315 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia multivorans].
ACCESSION   WP_176035128
VERSION     WP_176035128.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..315
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34951
     Region          24..70
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          102..303
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(117..118,120..121,124,128,130..136,229..234,
                     240..241,243..244)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 medddrtasl diwlvrvlrt lllersvtqt alrlnqtqpa istalrklre tlndpilvrg
       61 ksgmvpteyg asllgaatra lrevdfistp hgdfdpssar rtfriaapdy lndffmptli
      121 erfrdaapha hleidslnpa ldhagalesg aldlvignwp kpdpqfarqd lfsdtivclm
      181 rdahplarep ltreayasaa hvaptpytgd krnaieigla raglarrvvt tlpyfgivpq
      241 vllqtdlift ttrrfathya qllplvvvpp pvpfpriksy llthpqpdrp tdiawlcalm
      301 qsvsdeltaa rarrr
//
LOCUS       WP_176035147             835 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            multivorans].
ACCESSION   WP_176035147
VERSION     WP_176035147.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..835
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=90812
     Region          16..789
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mageillnvl rggyaqfdri vkldtplgnd wlvplyvkin arlgrnfevt vdassvvgdk
       61 iklnalmlqp vtlwirqtdg aylpihgyvq qvrrlgsdga lsyfqlrfas wlsflklssd
      121 rrdwqeaggw qiladvfdkh pqsngqyrse lrgairsysh rvqwetdwnf vhrsmeevgv
      181 farfdfakdg kshqvvvmdd lyfgpslpkp emkfsragad eefdgltqls eqqdvqsatl
      241 tlgtadykrp dldkrvsmpa aeleelpghg eeylytgsqt wpsadagyeq arirteewas
      301 rarryfavgs pryalpgywf kvtghpilds lpeeerelsi iasdwliqnn lpgiealtrf
      361 prslrgeiel araagtgvat ahrdggvgfi qveieaqrrr tpfrspfehr kpemhlqtai
      421 vvtdsdeeih tddgnrvrvr ttdsrkdrda astpwiraam pdagakrggy fplrkgdqvl
      481 lgfvngdcdr pvivsrlhgg atmpvwhthg llsglrsrey ggdgfnqlvm ddatgqnrvh
      541 lysssysshl hlgylieqsd ntrgafigng fdlksnayga vraeqglyvs tqpataqpln
      601 vtaateplag aeavfetvsk asetnraesl qdgqtalksf tdatrhtvag sasggrtagg
      661 gtgnangfsk pvmllsspeg iaastqqsvh vtanrhanvv agqnvnlaag ksllasvldr
      721 islfaqnlgi kifaakgpvd iqaqsgpasl vglqdvkies adgrliltaa kevwigaggs
      781 yiriksglie nattgqilek caswdkpgga sgtirdplqa apvstdggrg alfsg
//
LOCUS       WP_176035212             411 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia multivorans].
ACCESSION   WP_176035212
VERSION     WP_176035212.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..411
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43641
     Region          9..411
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtdantdapr tivvigggqa agwvlktlra egyagrlvmi adephlpyer pplskavlag
       61 dadietvrvv rpdefdalnv eawqperaas idrarrvvkt asgreieydr lviatggtsr
      121 rlpdaivhts nlhylrtlde aaalgeklra srrvlviggg wiglevaata rklgvdavvv
      181 egaprlcgrs vppivsdflc dlhrangvdv rlgaalasld aqpddaskvr atladgttid
      241 adfavagigl alnaslasda glavddgivv defgatsdpa ifacgdvanh hngwlkrrvr
      301 leswanaqnq aiaaakavlg vraayaeipw fwsdqydvnl qilgdlpada qlvvrgdlaa
      361 rratlfflgd ghvrgvvain narelklark wmnqgravdr ealadttkal a
//
LOCUS       WP_176035219             430 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia multivorans].
ACCESSION   WP_176035219
VERSION     WP_176035219.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..430
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=47028
     Region          4..412
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mttptriviv gggiaglqla trlgerlgks graqvtvvdr spthvwkpml htiaagtrdv
       61 qqqqvifvah acehgytyqp gelqgldrtr rrvrlgeirs qdgavvlear eleydvlila
      121 lgsqandfgv pgvrehcyfi dsqrqaeafn ealrmrvfrs vardealrva ivgagatgve
      181 laaelsrlle vaqaygdatv rerlqltlle sgprilaafp pkisasaqqq lerigfrvlt
      241 strvtsaapn gfhygddsfa eadlmvwaag vkapefmqal ggldtnranq ivvgptlqat
      301 tderifaigd casllpdgqe rplpptaqva tqqaehlarh lpawldgkpm pafafhdfga
      361 lvslsdydaf gtlgqfgffr ggfirgrfaq lshlmlyrrh qqalhgfrka tmlwiaerin
      421 gcvqprirls
//
LOCUS       WP_176035253            1269 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Burkholderia multivorans].
ACCESSION   WP_176035253
VERSION     WP_176035253.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1269)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 1269)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 1269)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 1269)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 1269)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11534155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1269
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..1269
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=129846
     Region          11..>169
                     /region_name="copA"
                     /note="copper-exporting P-type ATPase CopA; PRK10671"
                     /db_xref="CDD:182635"
     Region          102..>254
                     /region_name="copA"
                     /note="copper-exporting P-type ATPase CopA; PRK10671"
                     /db_xref="CDD:182635"
     Region          185..>339
                     /region_name="copA"
                     /note="copper-exporting P-type ATPase CopA; PRK10671"
                     /db_xref="CDD:182635"
     Region          358..424
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          444..506
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(450..452,455)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          527..1267
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mteslasasl htielgvdgm hcggctgrvq ralagvpgvv datvdlerqa atitaretve
       61 parlvdavga agyratvrea vagsdamaaq agheaspgaa atvlldidgm tcascvsrve
      121 kalakvpgvt hasvnlater atveasadvs aaqlveaveq agygatpies apaiatsapv
      181 dhkaahsvel didgmtcasc vsrvekalak vpgvahasvn lateratvea svdvsaarlv
      241 eaveqagyga tpiesapava tsepvdhkas hsveldidgm tcascvsrve kalekvpgvt
      301 hasvnlater atveasadvs aarlagaveq agyratpves apsavtaapi dhkashsvel
      361 didgmtcasc vsrvekalak vpgvthawvn lateratvea sadvsaarlv eaveqagyga
      421 tpiesaraav tsepvhhkaa rsvefdidgm tcascvsrve kalakvpgva ratvnlater
      481 atveasadvs aarlagaveq agyratpves apstvtsapv drdathsidl diggmtcasc
      541 vsrvekalek vpgvthasvn laterasvra agpldvdali tavttagyra tpaptpapsa
      601 danaaassip tapdrdarkr qealrernlv iaaavlsapl vapmlaaplg idamlpgwlq
      661 lvlasivqfg fgarfyraaw havkaragnm dllvalgtsa ayglslwmll rdpahpghly
      721 feasavivtl vrfgkwlear akrqttdair alnalrpdra rivdngverd vplaqvrvgt
      781 ivsvrpgerl pvdgrvvsgr shvdeslitg eslpvpkddg davtagsing egalvvetta
      841 igaettlari irlvesaqae kapiqrlvdr vsavfvpail giavltlvgw llagagaeta
      901 ilnavavlvi acpcalglat paaimagtgv aarhgvlikd aqalelaqra tviafdktgt
      961 ltegkpsvta fdavdvprdd alalaaavqr hsdhplarav vaaydaqrna qaapvatdar
     1021 avagrgvear vdgrllalgs trwrdelgiv vppaldaraa eleragntis wlmhadapra
     1081 aialiafgdt vkpgardaia alavrhvasv lvtgdnrgsa aavaaalgid evhaqvlpdd
     1141 karvvaslkr ehggvvamvg dgindapala aadvgiamat gtdvamhtag itlmrgdpal
     1201 vadaidiskr tyrkiqqnlf wafvynligv plaalgwlnp viagaamafs svsvvtnall
     1261 lrrwkgrar
//
LOCUS       WP_176035267             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia multivorans].
ACCESSION   WP_176035267
VERSION     WP_176035267.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33777
     Region          11..70
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          101..301
                     /region_name="PBP2_DntR_NahR_LinR_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators that are involved in
                     the catabolism of dinitrotoluene, naphthalene and
                     gamma-hexachlorohexane; contains the type 2 periplasmic
                     binding fold; cd08459"
                     /db_xref="CDD:176148"
     Site            order(107,109..110,114,172,209,276)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176148"
     Site            order(108,111..112,115..116,119..120,122..123,126..127,
                     129..133,135,198,226..230,233..234,237..238,241,255)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 mnkshpvvtd lnllrvflai selrsltaag erlgltqpav shalrrlrnl fddplfvrtp
       61 tgmaptdaar qlhgpltraf diidlavqqv ahfdpatanr vfrismsdms efyflpplla
      121 klaevapgvr veiasaavea vgaamrsgei dlalgyvpdp gpgcvseplf tdehvcmvra
      181 ghplrkrtpt qadlaslryi yassnatghr mvetwldelq vertivlrlp hfivapeivq
      241 htdlaiifpr svaerfnrgr afrilplpfv lppieielht haqfssdpgi awlralivdm
      301 frrpva
//
LOCUS       WP_176035270             344 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia multivorans].
ACCESSION   WP_176035270
VERSION     WP_176035270.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..344
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=37789
     Region          34..93
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          124..324
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(139..140,142..143,146,150,152..158,250..255,
                     261..262,264..265)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mtpsvpgrpp plrtdapptd adacdglrvq dldlnllktf ravyaerhvg raalqlgvtq
       61 psvshalgrl rlmfrdalfv rtgtgveptp raqrlavsvd qalailqhvl degcrfapdt
      121 tqrvfrlhms dfaasaflpt llaeferrap gavietlhvd ecqlnvales gridfalghf
      181 adasshfqrt allhercvll mprrtarrva lpddfvldgd apdtlrfvav tshpqsmqll
      241 drhglmplvr valpdfmvvp vllqhgdyal ilpetialtf aaqqpctlha iagagewavn
      301 aywhrrfdad pghrwlrall lelfsigtla pfdawlapqp paca
//
LOCUS       WP_176035288             222 aa            linear   BCT 11-JAN-2025
DEFINITION  O-methyltransferase [Burkholderia multivorans].
ACCESSION   WP_176035288
VERSION     WP_176035288.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..222
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=23297
     Region          43..220
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mdqdqwnrvd ayfsatlvps ddvldaalaa seaaglpain vapnqgkllq llatirgarr
       61 ilevgtlggy stiwlaralp pggrlvtlel npahaavatq siaragfadv vsvvvgsakd
      121 slarliadge apfdfifida dkdnnrayld aalklsrpgt vivvdnvvrr grvadpdnrd
      181 pdvvgvregf arivaepklt ttavqtvgqk gwdgfsisiv ge
//
LOCUS       WP_176035276             292 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia multivorans].
ACCESSION   WP_176035276
VERSION     WP_176035276.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..292
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30774
     Region          24..270
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mqephspgts raapadgdaa dtggapgtgm lqrafailra lagmqqdgvr vthlakavgl
       61 tqgtahrilq sliaegmveq dersklyrls vdffalaala gnpssmrtlc ppallrlcas
      121 lgetifllvk sgfdavcldl cegpfpirsf tgdiggrval gvgqgslail aflpeaeree
      181 virfnvprir gygvldevyl rteidrvrql gyagrnsgvl dgmagvavpi ldrtgypvga
      241 lsvgtlasrl gddrmpmlve llrrqaeaig prtnpfdaal rrpmhglsgk ag
//
LOCUS       WP_176035294             331 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia multivorans].
ACCESSION   WP_176035294
VERSION     WP_176035294.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..331
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35536
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..291
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(103,107,146,160,162,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(104..105,109..110,112..113,116,120,122..128,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdnpiramri farivemnsf traalslgis ratatrtvqe leaalgmpll vrttralrtt
       61 pegdayyrrc lritadvdel easirraarh psgplrvdlp gpvasaivlp algtfharhp
      121 dlvlmlgvsv raadmvgdav dcsvrlgelp dssfvarplg alervtcasp ayldrcgvpr
      181 tlddldshra vgstsgsgqr aaecdfmvdg avrkirldvi vgvddehayl acgvhglgli
      241 qppravaqpl idagllrevl pqwrpaavpv savyvkrphv spgvrafvdw iaerfeaaar
      301 eraagvigwe arwraperid mpvegvsaai a
//
LOCUS       WP_176035306             221 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia
            multivorans].
ACCESSION   WP_176035306
VERSION     WP_176035306.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..221
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24412
     Region          12..174
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtpppadsgr rarkriqmla hladtaarlf dahgydavtm eqiadqadva krtlynhfat
       61 keavlahwle relardlahl qrdvarrrtf asriacvlda saawceqhpa hllaylrhrf
      121 lsigatapeg gdpggrdiap vwhqliadaq ragelnrslp aeqlatwfhh lylgamlrwl
      181 tvpglslkqe fraiarlfve gaqtaptapr asrasraapa r
//
LOCUS       WP_176035319             296 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia multivorans].
ACCESSION   WP_176035319
VERSION     WP_176035319.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..296
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30206
     Region          8..293
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mqrsgaamkt vgviglgnmg rgiasslkrg gfdvlgfdas aesvrqlade gvrpcasiae
       61 iasavdvlil slptsaivea vvlgdggvas hakrglivid tttadpnstr kvaaaldahg
      121 vafidgpvsg gpkgaatatm tmvlggaeeh iaavqpvlsa isakqvhvgp agaghvtkll
      181 nnlltgvhll vtseavraae aagvdkarli ealsggsgrn satltnyptw ilnerfdsgf
      241 tmklmrkdmr lalellqrah vsapiaseag rlwaasaesi gdaedfnriv efvdar
//
LOCUS       WP_176035347             481 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia multivorans].
ACCESSION   WP_176035347
VERSION     WP_176035347.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..481
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48433
     Region          19..428
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(26..27,30..31,34,66,116..117,119..121,124,146,
                     149..150,153,282,285..286,289..291,294,322,326,378..379,
                     383,387,403,406..407,410..411,414)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mdtatpafpr alarivatvs vgfvvtqldv tivnialahm aaalhlsvag lqwvvdaytl
       61 afavlmlsag algdrfgarr lyvaglalfa iaslacgaav apamliaara vqgvgaaaml
      121 pnslallnda crhdpalrar avgawtaags vsiaagpvlg galiaafgwr siflvnlplc
      181 aaglaaafaw ipadraaass apqartldvr gqlvaiamlt altgaviewr plglahpvva
      241 ggfvlavlaa aafvaiesra atpmlplalf rrrtfnaavl fgicvnltyy gtvfvialyl
      301 qrvrgesalq aglaflpltg gfllanlasg ravarygpra pmlagalvaa lgygslhfvd
      361 gstplpallv pfllipsgmg favpamttav lasveparag iasavlntar qaggaigvaa
      421 fgavagsgga vpvvdglrid tgvsvallia aallatrvrp dahrdahrda hggrrplqtt
      481 d
//
LOCUS       WP_176035380             316 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia multivorans].
ACCESSION   WP_176035380
VERSION     WP_176035380.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..316
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32485
     Region          28..314
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          211..314
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(216..217,250..251,254,258..259,262,304,308)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mqrtnhalra rrcavvaalv aagfvasgaa yaqnaggatv tpvgngtvaa salpantgtg
       61 sasaaasgtl vrgtagtlap ppanatpgqv vvggkvpdea tkaavlqklr dtygaanvld
      121 qievgdvatp pnwsanvqkl lgaqlkqisk gqlkingtqi emkgevhnea qrqqiasdma
      181 ntlnptytir nglrvsaseq glldqtlanr tiefetgsat ltpqgkqild qmaaalaklq
      241 nrtvdiight dnsgnrtsni alsqaradav kgylitrgia pqqmtttgvg pdqpiapndt
      301 aegrarnrri efrvgq
//
LOCUS       WP_176035445             346 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia multivorans].
ACCESSION   WP_176035445
VERSION     WP_176035445.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..346
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38321
     Region          15..323
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mvpmsrpaga trttqvaiva lppvsmsgvg pivdalhlan eidgrllyrw qvcswdgrpv
       61 plagsaqwha daafndaiac dwliviserf qqfadyrlfl aslarvgqrt plvsgihhgv
      121 wwlamagqls gyrvsvnwet yqqfaeqfer sivtqqifei drdratcagg qatvdfmlam
      181 igrehgpels eriadalgag tlrsgeerqr ipfvtapger hprlndalll meaniedplt
      241 tdeiaglvgv srrqlerlfr qylgampsky ylnlrllkar tqlqrtsksv vqvslacgfs
      301 saahfsnayr erfgvtpred rrawlekqtg ggsepragal vergkd
//
LOCUS       WP_176035400             198 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia multivorans].
ACCESSION   WP_176035400
VERSION     WP_176035400.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..198
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20826
     Region          1..188
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mttilqinsa artqgaqstl lsneltaklq qsnpgakvvv rdlladglph ldesvlgaff
       61 tpaenrsaeq naivaksdal iaelqaadii vigapmynfg issqlktyfd wiaragvtfr
      121 ytengpegli kgkkvyvvsa rggkyagtph dsqtpylrsf lgfvgmtdvs fiyaeglnmg
      181 peaqsaalag areaiaaa
//
LOCUS       WP_176035446             229 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia multivorans].
ACCESSION   WP_176035446
VERSION     WP_176035446.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 229)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..229
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24830
     Region          1..229
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 mflygfgpvl wagtvqtiel svlslatava lgligavakl shnrvlraia tgyttlirsv
       61 pdlvlmlllf ysiqiwlnqf tdlvgwtqld idpfvagvlt lgfiygayft etfrgaflav
      121 prgqleagaa ygmsgarvfv rilfpqmmrf alpgignnwq vlvkatalvs iigladvvka
      181 aqdagkstfn mfffilvaal iylaittvsn lvliqlekry smgvrhael
//
LOCUS       WP_176035512             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia multivorans].
ACCESSION   WP_176035512
VERSION     WP_176035512.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33037
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..295
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(103,107,146,160,164,230,247,274)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(104..105,109..110,112..113,116,120,122..128,191,
                     221..224,228,235..236,239)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mqvdlgdlna fvavarakgf reaarttgts asglseavrr letqlgvrll hrttrsvapt
       61 eagqrllarl mpalseveaa ldvvnsfrer pagtlklnvp lsaarlvlps ivprflaayp
      121 eirlelvvee nfvdilevgc dagiryderl eqdmiaipig prsqrfataa apeyldrrgr
      181 pkhpselldh aclrgrfasg smplweferd gevvrvdpsg plvvqiggav dlvveaarsg
      241 lgivhlyeew lrphldsgal epvlegwwrp fygpylyypg rrlvpaplra fidfikaege
//
LOCUS       WP_176035524             258 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia
            multivorans].
ACCESSION   WP_176035524
VERSION     WP_176035524.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..258
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=28324
     Region          21..223
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mthqtnnvie lpyaldvnhf lsaldganrs alvphlqlch vdtgeilcda gsalpavyfp
       61 vttavsvqyt magkptlava eigcegvvcd dvvggdsamp rrvvvyrggf ayridarrfn
      121 daceasplir rqifmrvqvv laqmsqtlfc srhhpmqhql grwlliahdr srsveipith
      181 gmlaqmlgvr retitdiaqt lqklglirqh rgsivltdpt alahatcgch lairdeaqri
      241 lafgretras tqcrvhtl
//
LOCUS       WP_176035522             153 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia multivorans].
ACCESSION   WP_176035522
VERSION     WP_176035522.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..153
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=15951
     Region          1..152
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mitltlngse qhfdgnpdmp llwylrdvlg htgtkfgcgm alcgactvhl dgvairscit
       61 pvaaaagkhv ttiegvsada thplqqawqe lnvaqcgycq agqimqaasl lktnphptda
      121 diddamsgni crcgtytrir aairlavsrg gaa
//
LOCUS       WP_176035536             297 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia multivorans].
ACCESSION   WP_176035536
VERSION     WP_176035536.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..297
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32063
     Region          12..270
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mpapiktllt presdignlv vrrvlparaa rlvgpfiffd emgpavlpag hgidvlphph
       61 iglatvtylf dgtlmhhdsl gfrqkivpgd vnwmtagrgi vhserspded rprdqpvhgi
      121 qtwvalpveh edtapafvhh aadtlpvfer dgarvcviag tafgltspve vfsptlyaya
      181 qftaggrlal daehdergvy lvdgdlridd tplavstmav lepgatvtla sthgarvmll
      241 ggahlpgerf vewnfvsssr ekidaardaw aaqtfgkvpg eedewtrqpa rkpqssa
//
LOCUS       WP_176035621             441 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia multivorans].
ACCESSION   WP_176035621
VERSION     WP_176035621.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48396
     Region          30..433
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(43..44,47..48,51,83,133..134,136..138,141,161,
                     164..165,168,265,268..269,272..274,277,305,309,360..361,
                     365,369,385,388..389,392..393,396)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtaldaaarr spaaaaspae ldltykkvfw rivpflmlcy vvayldrvnv gfaklqmsqd
       61 lafsetvfgl gagifflgyf lfelpsnmlm hrigariwia rimitwglls amfafvktpt
      121 qfyvlrfllg laeagfypgv ilyltywfps hrrakiiavf msaipvsgif gnplsgwime
      181 afhggsgfhg wqwmfmieav pavlvgiati lyldnnirsa kwlnerekql ledeiaaqpq
      241 eqqkhghslk avfadprmww msliyfafvt gqygltfwmp tlvkstgitd tlqvgllsai
      301 pfvvaivvmn lfghsadkrr errwhlivpa lmgavgfava asyshntavs ivflsiaagg
      361 vltcaplfws lptaflsgsa aaagiaiins vgnlagfasp yvigylkdlt hstssgmyvl
      421 aamlvigafa vwltpaklvn r
//
LOCUS       WP_176035638             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia multivorans].
ACCESSION   WP_176035638
VERSION     WP_176035638.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46508
     Region          18..401
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(31..32,35..36,39,71,121..122,124..126,129,149,
                     152..153,156,253,256..257,260..262,265,293,297,347..348,
                     352,356,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtaaapplha atmrrlnlrl ipflmllylv ayidrsnisv aalqmnadlg lsaemyglga
       61 glfyvtyilf evpsnlflar vgarrwiari mitwgviaag msavhtpgql yamrlllgaa
      121 eagftpgiiy ylsawypasd raramsffyi gatlasvigl plsgallnln gvlgvegwrw
      181 lfllegvpal llgivvlrrl pdtpadarwl paderawlea mlrdtapreh lshgaalrra
      241 fgdrnvwala afwllqafgt igltlflpll vkslsgqssf avgslsalpf lfacvamyan
      301 grhsdlgger alhlgvpmll agallvgaiy vhvlpvayal lvlavgfnwa atpvfwavtt
      361 eyvsgltaaa sialinavan iaglalppvm grikdvthsy dlalllvava llvggvlglr
      421 iasrrravpm aarrag
//
LOCUS       WP_176035653             603 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia multivorans].
ACCESSION   WP_176035653
VERSION     WP_176035653.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 603)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12379621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..603
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62717
     Region          1..284
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
     Region          329..603
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 maswldytln glivgniyal lavglalifg vshlinfahg svymvgafig wlcltrfglp
       61 lpvalaavvl gcgalgiaie riglrplrha ariapllati gisfildqla qlafgadpra
      121 vptplpdwhl rlggatlgsl dlliagigia aaallygflr ftrlgwavra taqdrdaalq
      181 mgvdvdrvnq tvfaiacalg gvsgllvgmy ynsidpamgf qatlkgvval ligglgnvpg
      241 aiagslllgl vesygvalfg tsyrdlfafg llivflvwrp nglfsanral ppepmtgtfl
      301 aaakalrvpr paivalvala avlpwlgasp yvlqtltnaw lygllalslt lvagtvgqis
      361 lghaallvig ayasallssd lgwspavtip cagaitavlg tllvypafrl rghyvsiatl
      421 gigevvslvi lnwdgltrgp lgitgiaplp wastaqaayw ftltvlvafa lvqvrllrsh
      481 lgrtlravre ddvaarahgi apnrykaiaf avggvaagvs ggiaahlysy inhqtfdsqv
      541 silaltmvil gglgnvlggi agalaliglp elfrwaadyr mliyglvlll lvrfrpqgll
      601 gtv
//
LOCUS       WP_176035641             649 aa            linear   BCT 11-JAN-2025
DEFINITION  arylsulfatase [Burkholderia multivorans].
ACCESSION   WP_176035641
VERSION     WP_176035641.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888040
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..649
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=69333
     Region          47..615
                     /region_name="PAS_like"
                     /note="Bacterial Arylsulfatase of Pseudomonas aeruginosa
                     and related proteins; cd16025"
                     /db_xref="CDD:293749"
     Site            order(57..58,95,156,158,263,406..407,466)
                     /site_type="active"
                     /db_xref="CDD:293749"
     Site            order(57..58,95,156,158,263,407,466)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293749"
ORIGIN      
        1 msmsasrsvp frlrvvcaia agalslascg gvdgnpppqa datpsakrpn ilyimaddlg
       61 ysdihafgge istpnldalv asgrilsnhh tgtvcaitra mlisgtdhhl vgegtmgvpt
      121 derrglpgye gylndralsf aqllkdagyh tyiagkwhig sgivgsatgs gqtpdqwgfe
      181 rsyvllggaa tnhfahepag ssnytedgry vqpgqpgqpg gtggnpavfy stnfytqkli
      241 qyidsnhsdg kpffayaayt sphwplqvpd pwlhkyagvy dagydairna riarqkalgl
      301 ipadfkpfdg lpettvaspa tandgtanak yvsavhsaad gyrdygagkv dklwsslspa
      361 erkaqaryme iyagmvenld yniglliqhl kdigeydntf imfqsdngae gwpidsgadp
      421 tatdtanaqe ptysalgtdn gkqnaqrlqy glrwaevsat pfrltkgysa eggvstptiv
      481 hlpgqtqqlp tlrafthvtd ntatflavag vtppsqpapp lintltgvdq nkgkvvygnr
      541 yvypvtgqsl lpvltgaang evhtapfgde aygraylrsa dgrwkalwte pplgpldghw
      601 qlcdlttdrg ettdvsaqnp svvstlidqw kaymsnvggv eplrprgyy
//
LOCUS       WP_176035695             380 aa            linear   BCT 11-JAN-2025
DEFINITION  elongation factor Tu, partial [Paraburkholderia fungorum].
ACCESSION   WP_176035695
VERSION     WP_176035695.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia fungorum
  ORGANISM  Paraburkholderia fungorum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia fungorum"
                     /db_xref="taxon:134537"
     gene            1..>380
                     /gene="tuf"
     Protein         1..>380
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
     Region          1..380
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makgkfertk phvnvgtigh vdhgkttlta aittvltkkf ggeakaydqi daapeekarg
       61 itintahvey etanrhyahv dcpghadyvk nmitgaaqmd gailvcsaad gpmpqtrehi
      121 llarqvgvpy iivflnkcdm vddaellelv emevrellsk ydfpgddtpi ikgsaklale
      181 gdtgelgeva imnladaldt yiptperavd gsflmpvedv fsisgrgtvv tgrvergvvk
      241 vgeeieivgi kptvkttctg vemfrklldq gqagdnvgil lrgtkredve rgqvlakpgs
      301 inphthftae vyvlskdegg rhtpffnnyr pqfyfrttdv tgsielpkdk emvmpgdnvs
      361 itvklinpia meeglrfair
//
LOCUS       WP_176035683             530 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxylesterase/lipase family protein [Paraburkholderia fungorum].
ACCESSION   WP_176035683
VERSION     WP_176035683.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia fungorum
  ORGANISM  Paraburkholderia fungorum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Fojan,P., Jonson,P.H., Petersen,M.T. and Petersen,S.B.
  TITLE     What distinguishes an esterase from a lipase: a novel structural
            approach
  JOURNAL   Biochimie 82 (11), 1033-1041 (2000)
   PUBMED   11099800
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Anthonsen,H.W., Baptista,A., Drablos,F., Martel,P., Petersen,S.B.,
            Sebastiao,M. and Vaz,L.
  TITLE     Lipases and esterases: a review of their sequences, structure and
            evolution
  JOURNAL   Biotechnol Annu Rev 1, 315-371 (1995)
   PUBMED   9704093
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Cygler,M., Schrag,J.D., Sussman,J.L., Harel,M., Silman,I.,
            Gentry,M.K. and Doctor,B.P.
  TITLE     Relationship between sequence conservation and three-dimensional
            structure in a large family of esterases, lipases, and related
            proteins
  JOURNAL   Protein Sci 2 (3), 366-382 (1993)
   PUBMED   8453375
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Myers,M., Richmond,R.C. and Oakeshott,J.G.
  TITLE     On the origins of esterases
  JOURNAL   Mol Biol Evol 5 (2), 113-119 (1988)
   PUBMED   3163407
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006294
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Paraburkholderia fungorum"
                     /db_xref="taxon:134537"
     Protein         1..530
                     /product="carboxylesterase/lipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0016298 - lipase activity [Evidence IEA]"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=54641
     Region          27..521
                     /region_name="PnbA"
                     /note="Carboxylesterase type B [Lipid transport and
                     metabolism]; COG2272"
                     /db_xref="CDD:441873"
ORIGIN      
        1 mnayhrrame wliavtipli mlgcggsvhs papadpsvva teqgqvkgiv angvraflgl
       61 ryaapptgal rwkppapaaa yasspydash vgsvcvqgta aaptgsedcl fvnvyvpgtt
      121 agttalpvlf wihgggfilg sgaatdgsal alkanaivvt inyrlnalgf lahpalaaed
      181 pngatgdygi mdqtaalawv qkniaafggd ptnvtifgds agghsvyvql aspgsaglfa
      241 kavaqsggfs rqqeslqqae tdgvgyaktw gctdpssavc lrnlpasall qgnpvawyat
      301 idgkvlpgst saafasgqyn rvpvmsgfte degtyfvaaa fdaqgkpvta sgyeaaiqgf
      361 lgvsgaataa lypanqfssp gqalakatgd ylftcgemqd adnlakyspa vymyrfsdpa
      421 pysvhslisv lpptamnyga fhssdldyww qlipsptanq atlsgamtaa lagfahtgnp
      481 nsgstvaswp lytpatrrtl dfgypvsnty daytahqcsy wygqapshgl
//
LOCUS       WP_176035777             422 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paraburkholderia terricola].
ACCESSION   WP_176035777
VERSION     WP_176035777.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia terricola
  ORGANISM  Paraburkholderia terricola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 422)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Paraburkholderia terricola"
                     /db_xref="taxon:169427"
     Protein         1..422
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45946
     Region          <200..416
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mtiaadstpe stgrlkrelk aaesrkrama llliaplaif lllifvvpig alltraaqnp
       61 evvsalphtl salsgwdrks pppdtayaal avdltavads dgmgalarrl nveipgyrsl
      121 vaksarampf vddnsqplkl tpgqihakfv elderwndia ywqaiaknas vyspfyllas
      181 ldhkqdafgh iiptdpdqqi ylavfsrtfv igaavtffal llgyplaywi stlsdrranl
      241 vmilvlipfw tsilvrvaaw ivilqseglv nkaligsgll hdplsllfnr tgvyismthi
      301 llpfmilply svmksippty qraaislgsh pfaafwrvyv pqtypgigag allvfilaig
      361 yyitpallgg pndqmvsyyv ayftnvtinw gmacalggll laatlvlyvi ygrftrssls
      421 lg
//
LOCUS       WP_176035800             557 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Paraburkholderia terricola].
ACCESSION   WP_176035800
VERSION     WP_176035800.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia terricola
  ORGANISM  Paraburkholderia terricola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Paraburkholderia terricola"
                     /db_xref="taxon:169427"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60628
     Region          25..383
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          453..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mtpaslieqy gpresmeydv vivgggpagl saairlkqla aakgvelgvc vlekgseiga
       61 hilsgavmdp raitelipdw keqgapltvd vtedrflflt etgsksvpaw alpdnfrnhg
      121 nyvislanvt rwlgtmaeaa gveifpgfpa aeilyhddgs vkgvatgnlg igkdgqpten
      181 fqlgmelhak ytlfcegarg hlgrqldekf rlrdgvdpqv ygigikelwe iepskhrpgl
      241 vmhtagwpln tdtyggsfly hmdnnqvvvg fvvglgytnp ylspfeefqr ykthpairgf
      301 leggkrvsyg araitagglm slpklvfpgg alvgddagfl nasrikgsha aiktgmlaae
      361 aafdavqagr rndeltaype sfrtswlhte lhrarnfkqw mskglylgtl mvgieqklfg
      421 gnvpwtlhhq hadhemlkpa sqctpitypk pdgrltfdrl ssvfisntnh eenqpahltl
      481 kdptvpvnvn lqtyagpear ycpaavyefv ktddggerlv inaqncvhck tcdikdptqn
      541 ivwvtpeggg gpnypnm
//
LOCUS       WP_176035810             413 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Paraburkholderia terricola].
ACCESSION   WP_176035810
VERSION     WP_176035810.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia terricola
  ORGANISM  Paraburkholderia terricola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Paraburkholderia terricola"
                     /db_xref="taxon:169427"
     Protein         1..413
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44901
     Region          19..372
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mlaharvpdt spvtrwgdev krilcvrldn lgdvlmttpa lhalregapg rhltllgsks
       61 gvalapfldd vddvieydap wvanphtnar tladdqqmqe rlrrggfdaa viftvysqsp
      121 lpaamlcyla giprrlahcr enpyslltdw lrepepqqrt rheverqldl vrqvgahsad
      181 trmrfsvhan dratlqaqla argvdgdaay ivlhpgataa srrypperfg kvaarlaret
      241 rapvlitggs terplveavi eaagprvrkq lhdlsgalkl gelaaliera svlisnnsgp
      301 vhlasalatp vvdlyaltnp qhtpwqtpnr vlfrdvecrw cyrsvcpqqh hacllgvapg
      361 evvraaldlr aqaqahrqpv dgaaetasqa ahepddapra dspppftgip vap
//
LOCUS       WP_176035859             839 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Paraburkholderia
            terricola].
ACCESSION   WP_176035859
VERSION     WP_176035859.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia terricola
  ORGANISM  Paraburkholderia terricola
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 839)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 839)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..839
                     /organism="Paraburkholderia terricola"
                     /db_xref="taxon:169427"
     Protein         1..839
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=91725
     Region          14..820
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mgaqdiigai tggliqsdrl lkldtalgnn vlvpqrvvgh srigrhfeft vdvvstsdtv
       61 elktliaqpv tlwvqqtdrs ylprhgyvht arrlgsdtgl tsyqigfasw mhflrfrkda
      121 riwqnkpade iltdvfnmhp qaqgafrfal srplpprsfc mqyeddwnfv hrlmeseglf
      181 gyfeqagdgk shtlvvtdnl dtfqplsprt vrfyragtns etdalvqwsg trtlqsttlt
      241 trtfdykapa ssanpkgtni ptlptqgnlp qqaevyeytg aytygsqdrg dalskirmee
      301 wesrakrfyg sggvrgtdag rwfelddhpd hatdsgqnrq favieaawfi ennlpvssra
      361 adfphslkgd latvrashas eeslkvrhad gsegfflvei eaqrkivpyr spfdhhkpkm
      421 hlqsaivvgp aneevytdql nrikvrfhwd rlndgdekas cwvrvamsdt gggyggvhvp
      481 rigeevlisw vdgdcdrplv tgrvyngatq phwhsnglls gyrskeyqgs gynqmvmdds
      541 tgqnrvhlys tstnahlhlg ylidqsgnsr gpylgsgfdl ksdaygavra sqglyvttyp
      601 atsqpldarq ttsqlvnaes vlesmsdast ahqaeslreg ydslkaftda trnnvsgsss
      661 ggntagggtg sanafgeplm lfgspsgial stqqsvhias daqtnlvsgq sthiatgksl
      721 iasvaqklsf fvqnagmklf aakgkveiqa hndnieltaq ksvklvsatg qiqaiakgei
      781 lltsggayir lkdgnieiha pgnidvkgaq hsfngptrid ekfpswndsa prravdfsg
//
LOCUS       WP_176035904             168 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator transcription factor, partial [Pantoea
            brenneri].
ACCESSION   WP_176035904
VERSION     WP_176035904.1
KEYWORDS    RefSeq.
SOURCE      Pantoea brenneri
  ORGANISM  Pantoea brenneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Erwiniaceae; Pantoea.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Pantoea brenneri"
                     /db_xref="taxon:472694"
     Protein         <1..168
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          <30..161
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 kacvlpenpa syrvvrkksy lfnkavaqvl idrgftipti fltgfgtipv tvramktgay
       61 efltkpvdpd rilqavseam riaeqnmats qekremtlrh qtltpresev mllaisglln
      121 kqiaaemgvs eitakvhkrr vmekmnarsl sdlvraaerl niantrrr
//
LOCUS       WP_176036013             271 aa            linear   BCT 11-JAN-2025
DEFINITION  molybdopterin molybdotransferase MoeA, partial [Pseudomonas
            aeruginosa].
ACCESSION   WP_176036013
VERSION     WP_176036013.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         <1..271
                     /product="molybdopterin molybdotransferase MoeA"
                     /EC_number="2.10.1.1"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0061599 - molybdopterin
                     molybdotransferase activity [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
     Region          <15..269
                     /region_name="MoeA"
                     /note="Molybdopterin Mo-transferase (molybdopterin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG0303"
                     /db_xref="CDD:440072"
ORIGIN      
        1 gqhvrrrgee lrrgapvlra gqrlrpqelg llaslgvatv svrrrlrigl lssgdelrep
       61 gqtllagqiy nvnrycigal lrglgfevhd eevladelva srdalslaas ewdalvtsgg
      121 vsvgeedhlk raiaelgevn lwrlaiqpgk pfafgsvagk pwlglpgnpa aalvtallva
      181 rpfllrqqgl fdvvprplal paafdwpqpr arrqylrarl dergrveihp qqgsamllaa
      241 swadglavie rgatlgvgda idflpfsalm a
//
LOCUS       WP_176036089             242 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella tritici].
ACCESSION   WP_176036089
VERSION     WP_176036089.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..242
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26558
     Region          7..238
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mnthiktppa vvlrnisrgf rgktvlehis leipqgqfvs llgesgsgkt tllralagld
       61 ddaeteghfv vpvsmsvlfq dsrllpwmkv ldnvtlglrr pdpaeaaram leavglgdka
      121 dvwpatlsgg qkqraslars llrepellla depfgaldal trmrmhallf rlietrrptv
      181 ilvthdvdea lllsdrilvl kdgriaedha vdlphprrtr ldkftalrqr llqslgvegn
      241 al
//
LOCUS       WP_176036132             274 aa            linear   BCT 11-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Brucella
            tritici].
ACCESSION   WP_176036132
VERSION     WP_176036132.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..274
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=30115
     Region          1..255
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mhererhrii lsavqekpvi tiqdlvelte aseatlrrdi aslhmqgrik rvrggaeaih
       61 ppqfgnlagr pfkvsesena drkraiarea valceegdsi iinggstafq mvhylaprrl
      121 qvltnsfaia ehllrqskst vivpggaiyr dqslilspfd ndvirnfygr rmfmgcqgis
      181 plgvmesdal iiqseqklmg qadelvlmvd stkftrrssl ilcpldrvst litddgisde
      241 arrmvenagi rlivaqvsan agkgdprees aeva
//
LOCUS       WP_176036144             831 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA translocase FtsK [Brucella tritici].
ACCESSION   WP_176036144
VERSION     WP_176036144.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 831)
  AUTHORS   Jean,N.L., Rutherford,T.J. and Lowe,J.
  TITLE     FtsK in motion reveals its mechanism for double-stranded DNA
            translocation
  JOURNAL   Proc Natl Acad Sci U S A 117 (25), 14202-14208 (2020)
   PUBMED   32513722
REFERENCE   2  (residues 1 to 831)
  AUTHORS   Crozat,E., Rousseau,P., Fournes,F. and Cornet,F.
  TITLE     The FtsK family of DNA translocases finds the ends of circles
  JOURNAL   J Mol Microbiol Biotechnol 24 (5-6), 396-408 (2014)
   PUBMED   25732341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..831
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..831
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=89697
     Region          <140..>265
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          213..826
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 mrnlrenfpq stgnraenaq dpklprgqtg shnpasddaw kvhfslganv rftrtpevel
       61 lrrrgeelps inersqtnaa eatpaisvge vaeaqpmava elqktvsqgm vrspvapvpp
      121 ampavtvaaa vapvqtvlka apvvaktvnp aqpsafayls dfafwegcdi dtalvpaepl
      181 vsavpaeprk plptvesila qfrirewnkq pelvavapvq pvaetpvvpa asapreivap
      241 epvaaveiet papqpvvatp eiapevagea tedevvltva eaeehvveev vapepaiekp
      301 apvkaapsia lyqpqplpra eapvmhgeye fpprdllqmp peqdgnvitq emlersagll
      361 esvledfgvr geiihvrpgp vvtlyefepa pgvkssrvig laddiarsms alsarvavvp
      421 grnvigielp nanretvylr emidsrtfea snyrlplclg kgiggepiia elakmphllv
      481 agttgsgksv aintmilsll yrfkpeecrl imvdpkmlel siydgiphll tpvvtdpkka
      541 vvalkwavre meeryrkmar lgvrniegfn araasakgkg etvmctvqsg fdketgeaty
      601 iqeeldltpm pyivviidem adlmmvagkd iegavqrlaq maraagihli matqrpsvdv
      661 itgtikanfp trisfqvtsk idsrtilgem gaeqllgqgd mlhmagggri vrvhgpfvsd
      721 eevekvvnhl keqgrpdyla tvtedeeded atpeaavfda tsmgsedgdd vyeqaikvvm
      781 rdkkcstsyi qrrlgigynr aaslvermek dglvgpanhv gkreiltgsr d
//
LOCUS       WP_176036101             329 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella tritici].
ACCESSION   WP_176036101
VERSION     WP_176036101.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..329
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35444
     Region          4..323
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 msslleirnl rtefgaldrp llavddlslt ldkgeilglv gesgsgksmt lrsligiirp
       61 kgrvfgqviw kgrdlvamse aelrgvrgre iamifqepma slnplvsirv qigenlaaha
      121 tldrnarkkr avelldivgi psaaerlddf phefsggmrq rvmiaialas dpellladep
      181 ttaldvtiqd qilrliqtla remgmsvvlv thdmsvvaqt cdrvavmygg rlcetgptrs
      241 virdphhpyt qgllrsiprn iaprtplysi pgtppalsdl pvgcaftarc flgeaacaak
      301 rpalelidvt haacchklaa avakiplea
//
LOCUS       WP_176036148             438 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrolipoamide acetyltransferase family protein [Brucella
            tritici].
ACCESSION   WP_176036148
VERSION     WP_176036148.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..438
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46970
     Region          4..437
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mahftiklpd vgegvaeael vewhvkvgdv vreddllaav mtdkatveip ssrggkviai
       61 ngevgekiav gselvrleie gsateekpve kagenpapat vetvkpqpap tpetpvllqt
      121 pvppkpaapk resagrpftg agpirgegek platpsvrlr ardagvdlrr vrgtgpagri
      181 thedldlffq qetgaapals gyaadssvne ikviglrrki aermaeakrh iphitiveev
      241 dvsqieelra klnheqkegr prltllpfii raivkavkeq pglnahfdde adiirqfggv
      301 higiatqtpn glivpvvrha esmsvfaaas elsrvtdaar ngtakreelt gstititslg
      361 plgaiattpi inrpevaivg inkmavrpmw dgvqfvprkm mnlscsfdhr vidgwdaavf
      421 vqklksllet pamifveg
//
LOCUS       WP_176036187             240 aa            linear   BCT 11-JAN-2025
DEFINITION  copper homeostasis protein CutC [Brucella tritici].
ACCESSION   WP_176036187
VERSION     WP_176036187.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Latorre,M., Olivares,F., Reyes-Jara,A., Lopez,G. and Gonzalez,M.
  TITLE     CutC is induced late during copper exposure and can modify
            intracellular copper content in Enterococcus faecalis
  JOURNAL   Biochem Biophys Res Commun 406 (4), 633-637 (2011)
   PUBMED   21362400
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Li,Y., Du,J., Zhang,P. and Ding,J.
  TITLE     Crystal structure of human copper homeostasis protein CutC reveals
            a potential copper-binding site
  JOURNAL   J Struct Biol 169 (3), 399-405 (2010)
   PUBMED   19878721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..240
                     /product="copper homeostasis protein CutC"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24929
     Region          2..240
                     /region_name="CutC"
                     /note="Copper homeostasis protein CutC [Inorganic ion
                     transport and metabolism]; COG3142"
                     /db_xref="CDD:442376"
ORIGIN      
        1 msallevcvd sadglrsaie ggadrielcs alelggltps lglielaska pipvyamirp
       61 rggnfcfsae deaimladir narnaglagv vvgaslsdgs ldavmlerli aeakglgvtl
      121 hrafdlvpdm eialqqaial gferiltsgl sqtaedgldk lrrlaeiage gisimpgsgv
      181 naenvgrime atgaaevhas crvpveekdp raiafgfaae qsfrtcvqrv ralktaiara
//
LOCUS       WP_176036195             217 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Brucella tritici].
ACCESSION   WP_176036195
VERSION     WP_176036195.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..217
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24867
     Region          3..203
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mtlklylhpf ssycqkaita fyekdivfea rmldgtepva seftslwpfg kfpvltgngk
       61 lvfeatgiie yleaayphtr rlipsdplvs advrmwdrff dnyinypqqr lvyialgreh
      121 ddggdrwraa fdtayafldl hmegrewvsg ddfsladcaa apsllyadwt yaipekfanv
      181 wayrkrllar psyaraldea rpfrhlfplg apeegrd
//
LOCUS       WP_176036296             298 aa            linear   BCT 11-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Brucella tritici].
ACCESSION   WP_176036296
VERSION     WP_176036296.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..298
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32146
     Region          8..289
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mmgpfrciad lrgqlmespv wddrrqtlfa cdiygrriye ididaaidtg rgvlrewtfa
       61 sqvaslglte sgrlvvalsr qlvvfdpetg seeplwsayd epitsrlndg kvgpdgafwi
      121 gsmdgrpere aisrlyrvtg dgnasvkaeg feisnglawt adggtmfhtd srgpwidryd
      181 fdletgdisg rkrirdldel sgrpdggacd aegaywsagv sagvlnrfdr egnllekvpv
      241 pvpaptmpcf cgadltllai tshrqlpeaa leaaprsggv flaqasvaga pvtrmrga
//
LOCUS       WP_176036346             186 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Brucella tritici].
ACCESSION   WP_176036346
VERSION     WP_176036346.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10658186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..186
                     /product="flavin reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=19362
     Region          33..177
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; smart00903"
                     /db_xref="CDD:214900"
ORIGIN      
        1 mvstvtylrd sasryidepe dievspgelk aamrqlaggv svvtagyddg rtgatvtsat
       61 alsvepptii vninrgssvw saisrhnhfc vnvlssgqqs iadrfagkgg ikgtaryaga
      121 ewyslesgal altgalasvd cavedvierh thaivigrvl kivtgsgepl lyhngsyrll
      181 dvvsga
//
LOCUS       WP_176036298             280 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella tritici].
ACCESSION   WP_176036298
VERSION     WP_176036298.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 280)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..280
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30635
     Region          9..266
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mirdtsilsk lwitlvwlvt gffvlnvlav itavvvssfg trwlgtwlpd afttrwyaaa
       61 waefqldqvl lvtfqvvfav vilsgilgvt aayamarrdf pgkkfvllif llpllvppit
      121 fgiplatvly kfgvggtfwg vvlanlvptv pfvilvmipf ieqidpkvea aarvfgagtf
      181 klfihvllpm lmpgvlaaml lvlvrtvamf eltfltagpt sqtlvvalyy svfaagvrsv
      241 qsidamaviy mvtslvwlll alrfvnptqi varnrqpsah
//
LOCUS       WP_176036353             283 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella tritici].
ACCESSION   WP_176036353
VERSION     WP_176036353.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..283
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=31080
     Region          19..272
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mlmeaprtia rekagnsvpa ialnnvtrrf vtpdgkmmta lrdftmnvaq gefacvvgpt
       61 gcgksttlnl vtglakpsag evrlmgkpie gispdigfvf qadalfpwln vidnvsagpr
      121 yrgmgkdeay dkarswiarv glarfekhyp hqlsggmrkr valaqtfine pkillmdepf
      181 saldvqtrtl mqgelldlwq qsgasvifvt hdleeaiala dkvyvltagp atvksvydid
      241 iprprvmedi rydsqfvdia kviwddlree vqigqkrala ngn
//
LOCUS       WP_176036373             768 aa            linear   BCT 11-JAN-2025
DEFINITION  transglycosylase domain-containing protein [Brucella tritici].
ACCESSION   WP_176036373
VERSION     WP_176036373.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 768)
  AUTHORS   Spratt,B.G., Zhou,J., Taylor,M. and Merrick,M.J.
  TITLE     Monofunctional biosynthetic peptidoglycan transglycosylases
  JOURNAL   Mol Microbiol 19 (3), 639-640 (1996)
   PUBMED   8830253
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..768
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..768
                     /product="transglycosylase domain-containing protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0008360 - regulation of cell shape
                     [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=83362
     Region          51..684
                     /region_name="MrcB"
                     /note="Penicillin-binding protein 1B/1F, peptidoglycan
                     transglycosylase/transpeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG0744"
                     /db_xref="CDD:440507"
ORIGIN      
        1 masrddrnrr iepsfggeek kddevfrvde edrmartqqr rrrqsdepep rssrrgknkp
       61 rgffgflrrs iywclvlglw ggiafagvlv yfaakmpptt dwtipdrppn vrivdvngnl
      121 ianrgttgge avglhemspf ipkaviaied rrfyshfgid piglaravvt nvvsgravqg
      181 gstltqqlak nlflspdrtl erkvqevmla lwlehkytkd qilemylnrv ylgsgafgvd
      241 aasrryfnks akdvnlmeaa tlagllkaps rlspardpea aaaraklvlg amrqegmidd
      301 sqmaiaesep mtrapsywqg senyvadkvv aelpeligea keditvqtti dlnlqragee
      361 aikdqisqng kkmnasqgal vsidstgavr amvggvdyat sqfdrvtdar rqpassfkpf
      421 vyltaleqgr tpdsvrndap vrigkwtpsn dngkymgqvt latalshsln svaaqlvmev
      481 gpqtvidtah rlgvqsklea naslalgtse vtlleladay vpfanggyra pvyfitkvtd
      541 sdgkvlyqke dgvgprvide rnvgmmnaml rrtvedgtak raafgwpaag ktgtsqnfrd
      601 awfvgytanl ttgvwfgndd gkgmkrvfgs tlpvaawksf mkeahkgvpi aelpghydiq
      661 nvvpggsdgi dpnapydpgm mpqdpygnqp magngddgyw ppapdstarn giqqssetgr
      721 plaeqpgaat ypanandsyr pvppgdvggg qqsgksttll diimgnsq
//
LOCUS       WP_176036392             849 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella tritici].
ACCESSION   WP_176036392
VERSION     WP_176036392.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 849)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 849)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 849)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 849)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 849)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 849)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 849)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..849
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..849
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89393
     Region          4..848
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 msaaksfsla lrfalremrg glsgfyifla cialgvaaig gvnsvarsvs tgiasegqsi
       61 lggdvsfaln qreatveera fiekqgrmae satmrsmarm pdgsdqslve vkavdaaypl
      121 ygqlkvapeq sladmtgdkd giygaavaqd flnrmglslg akvllgsqmf elrgliesep
      181 dllssgfnfa prflvsldgl rasgliqpgs lvdhiykval pdgapdaaia evrrqaaadf
      241 pdagwnirsr snaapalsan ierfsqfltl vgltalivgg vgvanavray ldgkrgviat
      301 fkslgaparf avlvylvqim vigligivlg lilaaiipya aamalanylp vaggggffpg
      361 alalaavfgl ittlafaiip lgrardipat alfreqgfeq rglppllylg lavlliaala
      421 glalyvaydr riaaifivsa iaafgvlrlv adgirwlarr vrrvrstalr lavgnihrpg
      481 altpsvvlsl glgltlmvai alidgnlrrq vtenipaqap dfffvdiqnr diadftklvs
      541 givpdgklts gpmlrgriva fngtnvrdmt ippeaawvlr gdrgitfsnt vpenstlteg
      601 ewwpadysge plvsfaereg kelglklgdt vtvnvlgrni nakiasfrqv qwetlamnfv
      661 mvfspntfag apatwlatlt ipdsqknlap dvlrqvtktw pavttvsvtd alnvandlis
      721 qlatairaaa sialaasvlv lggalaagnr arvhdavvlk tlgatrgtli sayvleymll
      781 glatalfalv agsvagwyvv veimklkasf lpdvalmtva ialvltvgfg lagtwrvlgq
      841 kpaqvlrti
//
LOCUS       WP_176036434             419 aa            linear   BCT 11-JAN-2025
DEFINITION  lytic murein transglycosylase [Brucella tritici].
ACCESSION   WP_176036434
VERSION     WP_176036434.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR02283.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..419
                     /product="lytic murein transglycosylase"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009253 - peptidoglycan catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45703
     Region          14..345
                     /region_name="MltB"
                     /note="Membrane-bound lytic murein transglycosylase B
                     [Cell wall/membrane/envelope biogenesis]; COG2951"
                     /db_xref="CDD:442193"
     Region          363..418
                     /region_name="PG_binding_1"
                     /note="Putative peptidoglycan binding domain; pfam01471"
                     /db_xref="CDD:460223"
ORIGIN      
        1 maagnwkhsl kiglallasl aispavaaps kaqvesqyrn wlekdlwpea kaagvsravf
       61 dqafagvsin wklpdlvipg ekpstpkeqk qaefgapgky fnaktiasvt sggkarygqy
      121 asllkrieqk ygvpgpilla vwgresgfgt vkipynayev lgtkafmatr kdmfrkelia
      181 aleiaskgyi deaamksswa galgqpqfmp tsylkhavdf dgdgkrdiwn svpdtlasia
      241 nylklhgwqk grdwgfevnv pqnvscsleg pdqgktiaew aklgitrvng kpfpaneika
      301 tsfllmpagc ygpafvvspn fyvlkdynms dlyalfighv gdriaygagd fsrawgdvgs
      361 myrsdigamq krmqalgydv gkpdglpgfk trrsiglwqa rngapetcfp qpellrqir
//
LOCUS       WP_176036451             239 aa            linear   BCT 11-JAN-2025
DEFINITION  CpaD family pilus assembly protein [Brucella tritici].
ACCESSION   WP_176036451
VERSION     WP_176036451.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009319
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..239
                     /product="CpaD family pilus assembly protein"
                     /calculated_mol_wt=25744
     Region          30..234
                     /region_name="CpaD"
                     /note="Type IV pilus biogenesis protein CpaD/CtpE
                     [Extracellular structures]; COG5461"
                     /db_xref="CDD:444212"
ORIGIN      
        1 mtysvrgfcr isarpalval slallagcan rqhvtvgalp ddyrtnhpit iaereqvtdi
       61 pvaqasqkls pmqrgiiqga itnyrrsgsg mlyvlvpsga snqaaayrls tevsatlrrs
      121 gikanniaie nypvdnpeaa apirisyyam tagttpcgrw pddlastpen khyanfgcas
      181 qnnlaaqvan padllgprvm spidsdrtte rlngdqgyvk mspaqtdnwq etrsqqaey
//
LOCUS       WP_176036492             202 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Brucella tritici].
ACCESSION   WP_176036492
VERSION     WP_176036492.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22502
     Region          6..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvprgrprsf drdaaldkvm kvfwakgyec aqindfttai gitppsfyaa fgnkeqafre
       61 avdyyrrtig aapfdalena ttiqegmrqw lelsadsafv cpaggcmisv ssiqckpenv
      121 pvkeflqair hanhdrlsrr lqraietgdl psdsditqmt efyhmiqqsi sfeardgnsr
      181 anvqkiidma mrampakvks pa
//
LOCUS       WP_176036528             265 aa            linear   BCT 11-JAN-2025
DEFINITION  ParA family protein [Brucella tritici].
ACCESSION   WP_176036528
VERSION     WP_176036528.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..265
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28588
     Region          5..260
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mnkmariiti anqkggvgkt ttainlatal aaigetvliv dldpqgnast glgidrrnrp
       61 lssydvltqe ssvpdaampt dvpnlhivps tldllgieme iaqsadrtrr lrdalrfdsg
      121 vserfsyvlv dcppslnllt lnamaaadsv lvplqceffa leglsqllqt vdqvrstinp
      181 elsiqgivlt mfdsrnnlaa qvvddvrafm gekvyrtvip rnvrvseaps hgkpailydl
      241 kcagsqaylq laseviqrer qlqaa
//
LOCUS       WP_176036456             259 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Brucella tritici].
ACCESSION   WP_176036456
VERSION     WP_176036456.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 259)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..259
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27864
     Region          1..259
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mrkllvaati lalftagsaf aktirigvtp gphaqimekv kevaekngle idiqefsdyv
       61 ipnmaladga leansfqhkp yldnqvadrg fdivsvaetv nfpmglyskk lkniseladg
      121 atiaipndpt nggrallvla engiikidpt kglkvsaldi venpknlkfv eldaaqlprs
      181 medvdaavin tnyameagln patdplvreg ekapyvnilv vrtadkdadw vktlissyhs
      241 devkefiatt fkgsvapaw
//
LOCUS       WP_176036554             829 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Brucella tritici].
ACCESSION   WP_176036554
VERSION     WP_176036554.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 829)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 829)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 829)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   4  (residues 1 to 829)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   5  (residues 1 to 829)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   6  (residues 1 to 829)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457627
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..829
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..829
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85705
     Region          7..72
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          126..185
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          229..825
                     /region_name="Haloacid Dehalogenase-like Hydrolases"
                     /note="The haloacid dehalogenase (HAD) superfamily
                     includes carbon and phosphorus hydrolases such as
                     2-haloalkonoate dehalogenase, epoxide hydrolase,
                     phosphoserine phosphatase, phosphomannomutase,
                     phosphoglycolate phosphatase, P-type ATPase, among others.
                     These...; cl21460"
                     /db_xref="CDD:473868"
     Site            order(526..530,677..678,704,722..723,726..727)
                     /site_type="active"
                     /db_xref="CDD:319763"
ORIGIN      
        1 msetlnqirf ridgmdcasc aakidtavrr vrgiedvsvs vtagtmtvsh dgtgdldkva
       61 skvrslgygv eplieekava krehshdhsh hdhdhdhaac gghhdhhdhd heahdkaiav
      121 tansfrfqvd gmdcascaak idtavrrlsg vtdvsvsvtn gamtvnhdgt aksdeiagkv
      181 talgyrtala etaaagagst pkataptkpl pwwrskkgqm mlacggglva ayivghlypp
      241 lalwavtaam liglvpiarr aymaaingtp fsiemlmtia avgavfidat eeaaavvflf
      301 lvgellegva agkarasiqs ltmlvpktaf lekngataev aadslavgdv isvrpgdrmp
      361 adgeiltges avdeapvtge stpvgkaegd tvfagtingd gvlrvrvtaa aqdntiarvv
      421 rlveeaqeak apterfinrf styytpgvvv vaalvailpp llagggwnew vykglailli
      481 gcpcalvist paaiaaalss garrgllmkg gavletigki taacfdktgt ltegkpqvtd
      541 vlagdlpede vlrlaaslda gsshplalai vgaaeqrnlk lsvitqgkah ggkgvsgtvg
      601 emdlflgsrr aandiaaipd alaslivacn degktvsvlv angkiagaia mrdepradai
      661 aglqelkaan irtvmltgdn rrtaeaighd lgievraell pedkqrivge lrkdglivak
      721 igdgindapa laaadvgiam gggtdvalet adaavlhgrv gdvaemvdls krtmrnihqn
      781 iaialglkav flvttvlgit glwpailadt gatvlvtina lrllrqpar
//
LOCUS       WP_176036573             433 aa            linear   BCT 11-JAN-2025
DEFINITION  ammonium transporter [Brucella tritici].
ACCESSION   WP_176036573
VERSION     WP_176036573.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..433
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44325
     Region          32..431
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mlitgrnkqt allatlpalv amagtamaqd aaptptldtg dtawmltsta lvlmmtipgl
       61 alfyggmvrk knvlstvmqs faitclmsil wmvagyslaf tdggslnsyv gglskaffsg
      121 vtmesltgti peyvfitfqm tfavitpali agsfaermkf ssmlvfltlw lfivyipvah
      181 wvwgggfmas dgvldfaggt vvhinagvag lvaaliigkr dgyghtnmap hnlvlsviga
      241 allwvgwfgf nagsaagana lagvamlntq vatagaalaw mvvewaiagk psvlgiisga
      301 vaglvavtpa agfvnpmgal iigivagvvc yvaavkikha lgyddsldaf gvhgvggfvg
      361 avltglfada ainpasegat igkqffgaai tivytaiata iilyvvkaim glrpskqaei
      421 egldialhge svq
//
LOCUS       WP_176036574             858 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA translocase FtsK [Brucella tritici].
ACCESSION   WP_176036574
VERSION     WP_176036574.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12144184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..858
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..858
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015616 - DNA translocase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=92855
     Region          28..194
                     /region_name="FtsK_4TM"
                     /note="4TM region of DNA translocase FtsK/SpoIIIE;
                     pfam13491"
                     /db_xref="CDD:463896"
     Region          275..857
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 mrqgyspsyp lrderitedr lklanlfrrq fyilfglgll altgmavgal atwnvadpsf
       61 shatdnpvtn algypgavfs diamqffgla svpallplav wsllmmtrgg igriakrsfa
      121 wlgaallfaa iascfavpes wpmpiglggv fgdmilkfpg lflgsfpqga iasgialila
      181 vpafwlclfa sgivgrgagi vnsaqpsarr sveeddfsad dedddasagg gfqlmgalth
      241 laltstanfk rltglgrrrp raedfddmrv vrrnaeirna prrepgfgap aaaedeppfd
      301 mddmddgapl vgqewhdapp prsrkarveq aapspkpgpr aqreaqpsfl kdngvfemps
      361 lhflaepklv qrdpalskda leqnarlleg vledfgvrge iinvkpgpvv tlyelepapg
      421 ikssrvigla ddiarsmsai aarvavipgr naigielpnp kremvylrem lasrdfeqsk
      481 aklalalgkt ingepviadi akmphvlvag ttgsgksvai ntmilsllyr mtpqecrlim
      541 idpkmlelsv ydgiphlltp vvtdpkkavv alkwtvreme dryrkmskvg vrnidgfnqr
      601 vglaqkkgep iartvqtgfd rntgeaiyet eeldlepmpy ivviidemad lmmvagkdie
      661 gavqrlaqma raagihvima tqrpsvdvit gtikanfptr isfqvtskid srtilgeqga
      721 eqllgqgdml fmagggriqr vhgpfvgdde verivqhlkl qgvpeyldai tedeeddegg
      781 sgpagtgnle dsddpydqav avvlrdkkas tsyiqrrlgi gynraasiie rmedegivgp
      841 anhagkreil vptgdddf
//
LOCUS       WP_176036580             142 aa            linear   BCT 11-JAN-2025
DEFINITION  EVE domain-containing protein [Brucella tritici].
ACCESSION   WP_176036580
VERSION     WP_176036580.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Bertonati,C., Punta,M., Fischer,M., Yachdav,G., Forouhar,F.,
            Zhou,W., Kuzin,A.P., Seetharaman,J., Abashidze,M., Ramelot,T.A.,
            Kennedy,M.A., Cort,J.R., Belachew,A., Hunt,J.F., Tong,L.,
            Montelione,G.T. and Rost,B.
  TITLE     Structural genomics reveals EVE as a new ASCH/PUA-related domain
  JOURNAL   Proteins 75 (3), 760-773 (2009)
   PUBMED   19191354
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006808
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..142
                     /product="EVE domain-containing protein"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=16295
     Region          2..137
                     /region_name="EVE"
                     /note="Predicted RNA-binding protein, contains EVE domain
                     [General function prediction only]; COG2947"
                     /db_xref="CDD:442190"
ORIGIN      
        1 maywlfksep fkwswemqka rgekgeqwdg vrnylarnnm ramklgdkgf fyhsneglev
       61 vgivevcals hpdsttddpr wdcvdiravr dmpkpvtlkd vkanpklekm alvtsmrlsv
      121 qpvmedewie vcrmggldvk di
//
LOCUS       WP_176036582             329 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-dependent glycerol-3-phosphate dehydrogenase [Brucella
            tritici].
ACCESSION   WP_176036582
VERSION     WP_176036582.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..329
                     /product="NAD(P)H-dependent glycerol-3-phosphate
                     dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0047952 - glycerol-3-phosphate
                     dehydrogenase [NAD(P)+] activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0046167 - glycerol-3-phosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=33539
     Region          7..326
                     /region_name="GpsA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0240"
                     /db_xref="CDD:440010"
ORIGIN      
        1 msgktskiai lgggawgtal aamacssghd tclyardeam veainrthrn phylgeielp
       61 aainastdav avveradavl avipaqamra glsqlsnlip qtapvvlcak gierstgrlm
      121 sevvaevlpn hriaalsgps fatdvarglp tavtiaceda vtadqlaall sgpafrcyst
      181 tdlkgveigg alknvlaiaa gaavgrgfga saqaalvtrg faelrrigqa mgarpetimg
      241 lsglgdlmlt csssqsrnys yglalgrged ltnrplaegv atapiaaelc rqhaisapii
      301 datgalldgt itideavtal lnrplkted
//
LOCUS       WP_176036639             156 aa            linear   BCT 11-JAN-2025
DEFINITION  nucleoside deaminase [Brucella tritici].
ACCESSION   WP_176036639
VERSION     WP_176036639.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..156
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16558
     Region          1..138
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 msrdstfldq aiklafdnve qggrpfgavv vkggkviatg vnrmqadcdp tahaellalr
       61 aagktlqspr ldgcevyasg qpcpmcfaam rmagvekirf aysneqaepf glstakiaae
      121 lakplnaqtg isfehsppek dpelyevwsi knkaga
//
LOCUS       WP_176036674             220 aa            linear   BCT 11-JAN-2025
DEFINITION  Fic family protein [Brucella tritici].
ACCESSION   WP_176036674
VERSION     WP_176036674.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..220
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=24101
     Region          13..>178
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 msggaesqrh svaleaeiit dpqkkaetea rnglrqfdia mqavaqaier kqfklrvsli
       61 lslqrealie lsgyagnfrp sgveihgsnh qpvaahlvae lvedlceyvn anwetatpih
      121 laayvmwrln wihpfsdgng rtsrtlsyli lcikldailp gfpaipdqiv enrtpyfkal
      181 daadaayaeg ridvsemekl lsgmlaaqli saferaggrs
//
LOCUS       WP_176036710             532 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Brucella tritici].
ACCESSION   WP_176036710
VERSION     WP_176036710.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..532
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58020
     Region          1..532
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mtdtydyivv gagtagcala nrlsadqnrs vllleaggkd nyawihipvg ylycignprt
       61 dwcftteaep glngrslgyp rgkvlggcss ingmiymrgq ardydlwrqa gcegwgwndv
      121 lplfkksedy fagasdvhga ggewrvenar lhwdildafr daavsagipa tddfnggdne
      181 gvsyfkvnqk rgirwntaka flrpvldrnn ltvetgahvr rieieelrat gvtfdqngtt
      241 rtvkakrevi laagavgspq ilelsgigrg dvlqqagipv klerkqlgen lqdhlqlrca
      301 ykvtgiptln ekanklvgka migleyllrq sgpmsmapsq lgvftrsdps fetanlqyhv
      361 qplslekfge nvhpfpafta svcnlrpdsr gsihikspdh rtqpairpny laaesdrrva
      421 adairitrhi vaqaplqkfs peefkpgpay etqeqlekaa gdigttifhp vgtcrmgqda
      481 eaivdprlrf ngiaglrvad asvmptitsg ntnsptlmia ekaaqmiiad nr
//
LOCUS       WP_176036753             371 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella tritici].
ACCESSION   WP_176036753
VERSION     WP_176036753.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 371)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..371
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40275
     Region          1..351
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 marlkiasvs kafnefqals evsldvkdge fvailgpsgc gkttllrmia gfedvdggei
       61 higdsrvshv dcsvppekrq vgivfqnyal wphmtvaenv gyslrvakva kaerearvkq
      121 alalvdldgf gdrrpanlsg gqrqrvalar clvaapslvl fdeplanldv hlrasmedef
      181 aafhkrtgtt iiyithdqae amaladriav ldhgklqqfd tprklyeepa semvasfiah
      241 gmvlpaevvs faqaghceal vlgsraqvrc sgiemprana qlcvraedla ltetggipvr
      301 vkrsvyrggg srieaspltk paihlhfevr dpvrleegde vriairsgwi iptdempvrk
      361 vstgfpignk i
//
LOCUS       WP_176036762             139 aa            linear   BCT 11-JAN-2025
DEFINITION  group III truncated hemoglobin [Brucella tritici].
ACCESSION   WP_176036762
VERSION     WP_176036762.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Keppner,A., Maric,D., Correia,M., Koay,T.W., Orlando,I.M.C.,
            Vinogradov,S.N. and Hoogewijs,D.
  TITLE     Lessons from the post-genomic era: Globin diversity beyond oxygen
            binding and transport
  JOURNAL   Redox Biol 37, 101687 (2020)
   PUBMED   32863222
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Bustamante,J.P., Radusky,L., Boechi,L., Estrin,D.A., Ten Have,A.
            and Marti,M.A.
  TITLE     Evolutionary and Functional Relationships in the Truncated
            Hemoglobin Family
  JOURNAL   PLoS Comput Biol 12 (1), e1004701 (2016)
   PUBMED   26788940
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Wajcman,H., Kiger,L. and Marden,M.C.
  TITLE     Structure and function evolution in the superfamily of globins
  JOURNAL   C R Biol 332 (2-3), 273-282 (2009)
   PUBMED   19281958
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Vinogradov,S.N., Hoogewijs,D., Bailly,X., Arredondo-Peter,R.,
            Guertin,M., Gough,J., Dewilde,S., Moens,L. and Vanfleteren,J.R.
  TITLE     Three globin lineages belonging to two structural classes in
            genomes from the three kingdoms of life
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11385-11389 (2005)
   PUBMED   16061809
REFERENCE   5  (residues 1 to 139)
  AUTHORS   Wittenberg,J.B., Bolognesi,M., Wittenberg,B.A. and Guertin,M.
  TITLE     Truncated hemoglobins: a new family of hemoglobins widely
            distributed in bacteria, unicellular eukaryotes, and plants
  JOURNAL   J Biol Chem 277 (2), 871-874 (2002)
   PUBMED   11696555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..139
                     /product="group III truncated hemoglobin"
                     /GO_function="GO:0005344 - oxygen carrier activity
                     [Evidence IEA]"
                     /GO_function="GO:0019825 - oxygen binding [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15668
     Region          9..122
                     /region_name="TrHb3_P"
                     /note="Truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 3 (P); cd08916"
                     /db_xref="CDD:381257"
     Site            order(25,38,41..42,48,51..52,55..56,66,68..70,73..74,77,
                     79,83..84,87,111,114..115,118)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381257"
ORIGIN      
        1 mtlfinqphp sidpasiekl vatfygrare devigpifaa avhdwdhhia qiaafwssvi
       61 lktgnyegrp maphlklalk nehfdrwldl fektareifp peaaiifidr arriadsfem
      121 aiatntgqis aprhsrrpl
//
LOCUS       WP_176036765             318 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Brucella tritici].
ACCESSION   WP_176036765
VERSION     WP_176036765.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..318
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35620
     Region          4..237
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mapriavlgc gywggnhirt lkslgalqai sdsraeqaer fatefnvpsv pveelftrpd
       61 idgivlalpa qfhsqyaiqa vkngkdvlve kpialdipaa eaeveaaren grvfmvghvl
      121 rfhpafekll dmvksgelgd iryvhshrvg fgkfhnefda lwdlaphdls milaitgeep
      181 savrgegvat ldhltdiahl hldfpngirg hlfasrlnay rerrltvtgt kgmavfddge
      241 pwdrklalys hevwrendqw sfksvepvyi pveegmpltr elqhfmhcie trekprtdgk
      301 eaisvlrilt egtvrhpr
//
LOCUS       WP_176036786             328 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Brucella tritici].
ACCESSION   WP_176036786
VERSION     WP_176036786.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Xun,L., Belchik,S.M., Xun,R., Huang,Y., Zhou,H., Sanchez,E.,
            Kang,C. and Board,P.G.
  TITLE     S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of
            glutathione transferases
  JOURNAL   Biochem J 428 (3), 419-427 (2010)
   PUBMED   20388120
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418207
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..328
                     /product="glutathione S-transferase family protein"
                     /EC_number="1.8.5.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37274
     Region          1..327
                     /region_name="ECM4"
                     /note="Glutathionyl-hydroquinone reductase [Energy
                     production and conversion]; COG0435"
                     /db_xref="CDD:440204"
ORIGIN      
        1 mgllvdgkwh dvwydtestk grfersksqf rnwvtadgsa gpsgeggfka epgryhlyvs
       61 yacpwahrtl ifralkgled visvsvvdyl maeegwtftg ttgstgdaly gskrlyeiyt
      121 radpnysgrv tvpvlwdker qtivsnesse iirmlntafn dfgnasldfy pealrgeida
      181 lndfiypnin ngvyragfat tqeayeeafg qlfaaldsle drlsrqrylt gdrlteadwr
      241 lfttllrfdp vyvghfkcnl rriadypnlw nytrelyqtp gvaatvnmeh ikghyyrshk
      301 tinptgvvpl gpeidfsaph drdrfpka
//
LOCUS       WP_176036800             294 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cytochrome c1 [Brucella/Ochrobactrum group].
ACCESSION   WP_176036800
VERSION     WP_176036800.1
KEYWORDS    RefSeq.
SOURCE      Brucella/Ochrobactrum group
  ORGANISM  Brucella/Ochrobactrum group
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10490041
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Brucella/Ochrobactrum group"
                     /db_xref="taxon:2826938"
     Protein         1..294
                     /product="cytochrome c1"
                     /EC_number="7.1.1.8"
                     /GO_function="GO:0008121 - ubiquinol-cytochrome-c
                     reductase activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31912
     Region          54..292
                     /region_name="Cytochrom_C1"
                     /note="Cytochrome C1 family; pfam02167"
                     /db_xref="CDD:426633"
ORIGIN      
        1 mknilknfaa fgiaplvalg iafassmgga saeeggnaae pehfpihhpk qekwsfsgpf
       61 gtydkgqlqr glkvykevcs achsmnlvaf rtleglgysp eqvkalaaey evqdgpnadg
      121 emftrkalpt dhfpspypna aaaaaannga appdfsliak aravergfpq fifdiftqya
      181 eggpdyihsl ltgfdeqppa gmqiaegthy npyfisakal amakplsddq vtyddgspqt
      241 vdqyardvsa flmwaaephl edrkrtgfrv iiflilfagl vyvakrsiws dvkh
//
LOCUS       WP_176036816             129 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA thioesterase [Brucella tritici].
ACCESSION   WP_176036816
VERSION     WP_176036816.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..129
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14066
     Region          7..129
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mstdnepngt ltirvsampk dansaydifg gwvmaqmdma agirsaerak grtvtaavre
       61 msfarpvkig dtlcvytdit rvgrtsitlr veawakryls dkrdlvthae fimvsldadg
      121 kptpvpqee
//
LOCUS       WP_176036861             214 aa            linear   BCT 11-JAN-2025
DEFINITION  lytic transglycosylase domain-containing protein [Brucella
            tritici].
ACCESSION   WP_176036861
VERSION     WP_176036861.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Robertus,J.D., Monzingo,A.F., Marcotte,E.M. and Hart,P.J.
  TITLE     Structural analysis shows five glycohydrolase families diverged
            from a common ancestor
  JOURNAL   J Exp Zool 282 (1-2), 127-132 (1998)
   PUBMED   9723170
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Holtje,J.V.
  TITLE     Lytic transglycosylases
  JOURNAL   EXS 75, 425-429 (1996)
   PUBMED   8765311
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Thunnissen,A.M., Isaacs,N.W. and Dijkstra,B.W.
  TITLE     The catalytic domain of a bacterial lytic transglycosylase defines
            a novel class of lysozymes
  JOURNAL   Proteins 22 (3), 245-258 (1995)
   PUBMED   7479697
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..214
                     /product="lytic transglycosylase domain-containing
                     protein"
                     /GO_function="GO:0008933 - lytic transglycosylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=22284
     Region          10..195
                     /region_name="MltE"
                     /note="Soluble lytic murein transglycosylase or regulatory
                     protein s (may contain LysM/invasin domain) [Cell
                     wall/membrane/envelope biogenesis]; COG0741"
                     /db_xref="CDD:440504"
ORIGIN      
        1 mktkfvvvca lvgamssfgl npalsapste ptnlaallka rqqnksaeae kptttpkkas
       61 vvtrraapat kgstgkraqs kdttarsakg gstysniinr yastygvpsa lahavvrhes
      121 nfqpnvrgka geiglmqikl starglgytg sakglyepst niqfgmkyla maqklgggst
      181 cgtilkynag hgatrmnpts akycssvkay mral
//
LOCUS       WP_176036886             469 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Brucella tritici].
ACCESSION   WP_176036886
VERSION     WP_176036886.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..469
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50384
     Region          23..467
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mslenvvala rnengiaaav gilkqrfger aqtgqaireq hghtttyvpt qapdivifae
       61 taqevqdvvr icaehrvpvi afgagssleg qvnapaggvs ldltrmnrvi avhaedldcv
      121 vepgitrrel neylrdtglf fpidpganat lggmastras gtnavrygtm renvlalkav
      181 mpdgrliets krvkktaagy dltrllvgae gtlgiitelt lklqgipqai sggicpfpdv
      241 dsacrtviet iqmgipvari elvntlqmqa lilhsklpye aqpylfvefh gtengvaeqa
      301 elfgeiaagn gggefrwthd aeerdrlwra rhdaylasfl lrpgckgvst dvcvpisrla
      361 dcigetekdl aetgliapiv ghvgdgnfhl lllldtgdas emeraeafmd rlakraiame
      421 gtctgehgig qgkmkylame lgeatdymra iknaldpdni mnpgkilis
//
LOCUS       WP_176036911             144 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Brucella
            tritici].
ACCESSION   WP_176036911
VERSION     WP_176036911.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Leiros,H.K., Tedesco,C. and McSweeney,S.M.
  TITLE     High-resolution structure of the antibiotic resistance protein NimA
            from Deinococcus radiodurans
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 64 (Pt 6), 442-447
            (2008)
   PUBMED   18540048
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..144
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16643
     Region          3..140
                     /region_name="NimA"
                     /note="Nitroimidazole reductase NimA or a related
                     FMN-containing flavoprotein, pyridoxamine 5'-phosphate
                     oxidase superfamily [Defense mechanisms]; COG3467"
                     /db_xref="CDD:442690"
ORIGIN      
        1 mmiremseyd irdmiqhthl gqlayvldnr pfiiplsfrf sggslysftt dgqktealrk
       61 ndavcilfdh iesrtnwrtv vlngryreie redeknsiva lmaseptwwe payiktiakd
      121 gkerkldpvf frididsatg hqtg
//
LOCUS       WP_176036927             159 aa            linear   BCT 11-JAN-2025
DEFINITION  tRNA (cytidine(34)-2'-O)-methyltransferase [Brucella tritici].
ACCESSION   WP_176036927
VERSION     WP_176036927.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000715
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..159
                     /product="tRNA (cytidine(34)-2'-O)-methyltransferase"
                     /EC_number="2.1.1.207"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008173 - RNA methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0141098 - tRNA
                     (cytidine(34)-2'-O)-methyltransferase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=17741
     Region          3..148
                     /region_name="TrmL"
                     /note="tRNA(Leu) C34 or U34 (ribose-2'-O)-methylase TrmL,
                     contains SPOUT domain [Translation, ribosomal structure
                     and biogenesis]; COG0219"
                     /db_xref="CDD:439989"
ORIGIN      
        1 melrvalyqp dipgntgtil rmaaclgfav dliepagfdi sdrslkragm dyleqaaltr
       61 hpdwrhfedw rlqagrrivl lstkaaipyt dyqfqendil lfgressgvp dnvhdcadtr
      121 llipmmpgar slnlavsvam tagealrqrr eivdslrqe
//
LOCUS       WP_176036918             348 aa            linear   BCT 11-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Brucella tritici].
ACCESSION   WP_176036918
VERSION     WP_176036918.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10181064
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..348
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=37894
     Region          100..329
                     /region_name="CE4_Mlr8448_like_5s"
                     /note="Putative catalytic NodB homology domain of
                     Mesorhizobium loti Mlr8448 protein and its bacterial
                     homologs; cd10968"
                     /db_xref="CDD:213025"
     Site            order(107..108,239,243,279..281)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213025"
ORIGIN      
        1 mslrsikgsl kypliragle aiafsgasal fpsaggrgvv ftmhhvkped atdqsdpnai
       61 lsitphtlem aieaaleagl lpvqlhdlpr llseqadtrk yvaftlddgy rnnaefaapv
      121 farysipyti fittgfverk rsmwwrtiaa lvteansfqf dfgggilevr sespnqksaa
      181 farlvqfmqc fdedeavari daaaqtvgid aislvdesvm npselrslal dplvhlgaht
      241 vthvnlrrvd dkrlvkeiad stesvqryag yrprsfaypy gwkaavgere igavsaagfd
      301 vgvttqpgvl qqtgampaaa iprislngyf qkkryikalv sglpfkll
//
LOCUS       WP_176036965             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella tritici].
ACCESSION   WP_176036965
VERSION     WP_176036965.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..359
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38294
     Region          9..359
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mlhssnikad iavraeglnl afgpatilkn idlslpkgqt lallgpsgcg kttllrlvag
       61 llaptkgsit ingvtvadak tgsfippekr hlgmvfqdya lwphmtvfgn vsfplemrgl
      121 graerekrva saldrvglsg fgeraisdms ggqqqrvaia raivaepglv lfdeplsnld
      181 relrenmvte igqlvanlgl taiyvthdqs eafsladqva vmragvieql aapealveep
      241 ttpevadflr lgcvvpveqr dnayriarte ihiahgshag qathvllpsr svrsvpasda
      301 ailatvlrsq frgdghlttv rigsqqdghe ltyldsirls pgvpvgisvd asqlrwfsk
//
LOCUS       WP_176036995             333 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella tritici].
ACCESSION   WP_176036995
VERSION     WP_176036995.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..333
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36775
     Region          1..333
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 maelqlrdvr ksfgnfevik gvdmdirpge fmvfvgpsgc gkstllrlia gleeissgsl
       61 sidgkvvnsf apskrgiamv fqsyalyphm tvyenmafgm qlagkskdec ksriqkaaem
      121 lqltpylerl prqlsggqrq rvaigraivr dpkvflfdep lsnldaalrv atrleiaklh
      181 qsmedttmiy vthdqveamt ladricvlrd grveqigtpl elyekpnslf vagfigspkm
      241 nfltgrysep fgahtvglrp ehlvivsdna hwtgqvihte ilgsdtyvyi dlgleeplvv
      301 resgvaarrs getlsvspmg envhrfdekg rav
//
LOCUS       WP_176037036             205 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Brucella tritici].
ACCESSION   WP_176037036
VERSION     WP_176037036.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..205
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21734
     Region          1..191
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mdlvsllafa gilvvaagtp gpnvgalvar visrghkgvf pfmfglwlgd aiwlslavwg
       61 laalantfht aflilkyvgv aylvylswkm wiapvdevad gdavprqgea gklflsalai
      121 tlgnpkimvf ylailptvvd ithvslvgwg elllvmfavl aavdtawvvl aaqarrflrs
      181 prmmrianrt sagmmagaav aiatr
//
LOCUS       WP_176037065             355 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella tritici].
ACCESSION   WP_176037065
VERSION     WP_176037065.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..355
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36851
     Region          12..345
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtantttaat dstfnsgsal ltlmklrtfi alfvvfiffs faapnflsaa nlilmskhva
       61 lnaflamgmt fviitggidl svgsivglcg mvagglliyg idlgigytiy fniieislit
      121 lavgvavgfi ngllitklnv apfiatlgtl yvarglalls sdgqtfpnlv gredlgttgf
      181 aflgsgsilg lpvsiwiliv valaaayiar ytplgrqifa vggneraarm sgirvdrvkm
      241 fvymfsgfca aiagliisse lmsshpatgn sfelnaiaaa vlggtsmsgg rgtiggtiig
      301 afvigilsdg lvmmgvssfw qmvikglvii iavvvdqaqr rlqqrvtlmq makag
//
LOCUS       WP_176037131             227 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Brucella tritici].
ACCESSION   WP_176037131
VERSION     WP_176037131.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..227
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25770
     Region          18..227
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mdeiqkneqa engsqafrrt alhdmlvnhl rdmiiegqle pgtrlhegql geqlgvsrtp
       61 lreaikylas eglvelvpsr gavvkrfsaa dvkdmltvlr tleelagkla celasdkeia
      121 dvrslhdemi erykhadrlq yyklnqqihl aivrlaknpt ladihqmlqt rlkrirfvgh
      181 egtekwaaav sehqemieal eardatrlse vlgrhltkaw ervrdsl
//
LOCUS       WP_176037140             160 aa            linear   BCT 11-JAN-2025
DEFINITION  CAP domain-containing protein [Brucella tritici].
ACCESSION   WP_176037140
VERSION     WP_176037140.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Gibbs,G.M., Roelants,K. and O'Bryan,M.K.
  TITLE     The CAP superfamily: cysteine-rich secretory proteins, antigen 5,
            and pathogenesis-related 1 proteins--roles in reproduction, cancer,
            and immune defense
  JOURNAL   Endocr Rev 29 (7), 865-897 (2008)
   PUBMED   18824526
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..160
                     /product="CAP domain-containing protein"
                     /calculated_mol_wt=17275
     Region          45..159
                     /region_name="YkwD"
                     /note="Spore germination protein YkwD and related proteins
                     with CAP (CSP/antigen 5/PR1) domain [Cell cycle control,
                     cell division, chromosome partitioning, General function
                     prediction only]; COG2340"
                     /db_xref="CDD:441910"
ORIGIN      
        1 mqqkqgftln rrgflvlvgg alavsavpln malaagdndp tpifnairka nglplmatds
       61 kleqaalyqa rrmasygkig hsvgwgngfv arlrqagirg paaenvasgq rdtqavfdaw
      121 mkspghrknm ldptfehygl awatpenkpt yiywammlgl
//
LOCUS       WP_176037189             400 aa            linear   BCT 11-JAN-2025
DEFINITION  GGDEF domain-containing protein [Brucella tritici].
ACCESSION   WP_176037189
VERSION     WP_176037189.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 400)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 400)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 400)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..400
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44091
     Region          131..379
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mpkldfltly ivillnsltv ciiwtaiafs yrkfrpariw llsttlllvg gfvlslqgne
       61 gafwpavtgn tiiiygfcla yvgaryfhgq kggwrlalgi slasfavmaa fhsswqgrni
      121 ayavgqsvpm vmtvvylarq kniglggqia imafllgivg haietslnia awagefdqsl
      181 yfsiesyalv cviysgmiwn fgfivmamnr lhgdmakvae tdeltglpnr rhfmkrltra
      241 elafsedgta ysvmlididn fkqwndtygh algdqalvhf sdvavdvlnr rgvlarlggd
      301 efsilltkmd eqeateiard vvraindapl vfngqklvit vsigiaseer dnetsdldvf
      361 aradlalykv kqagrngyat rtktvnasrs pllerqlvtd
//
LOCUS       WP_176037229             398 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella tritici].
ACCESSION   WP_176037229
VERSION     WP_176037229.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..398
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43533
     Region          1..376
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 msqvdiqnit ksfgslkvld dinisirdge fltlvgpsgc gkstlvriia glesqsagti
       61 svdgasvnhl rpherklsmv fqsyalyphm tafdniavpl tveklsller iplikhlspr
      121 rkrltqeiaq qveavagqlk ieallgrkpa qlsggqrqrv algramvrqp raflmdepls
      181 nldaklrvhm rteltelhkr mgatfiyvth dqieamtmsd rvammdggkv qqlgtptely
      241 ehptnlevar figsptintm pasigpagrv eiqgrplgia vnlpqgesvt igirpealdl
      301 lslkqtatgq piidarlrrt enlgaeflhh ldltgteats fimrttsphe dihegdavrl
      361 tfdptlchif gpdgrraekt hvllsgddsg rakhgstr
//
LOCUS       WP_176037281             285 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella tritici].
ACCESSION   WP_176037281
VERSION     WP_176037281.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 285)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 285)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..285
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32327
     Region          30..285
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mtsrvlkens gvkentvtsg plarvhaais disdsliayr ialifgwqdv aqryrrsrlg
       61 afwltinmav yigalgmifg tlfrsdmpey lphicsgiia wglissslse scttfsgasg
      121 iilqvrlplf thilrslwkn iiifchnvli fpvlllilgq nfnlhtllil pglliliinl
      181 swimlvlatv ccrfrdmtqi vtnvlqisfy ltpiiwdvki lpdtssklif elnpfyhllq
      241 liraplfgea paiytwllti siaimgwffa lvffgkyrwr ipywl
//
LOCUS       WP_176037245             371 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella tritici].
ACCESSION   WP_176037245
VERSION     WP_176037245.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 371)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..371
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40768
     Region          1..356
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 migqklmlag vqkrfgetwa vhettldira gefvsiigps gsgkttlltm vagfeqptng
       61 riivgdvdit tlppnrrnvg mvfqkyalfp hltvrqniaf plkmrrlgsk tdirsrvdem
      121 lelirlndfa drypnqlsgg qqqrvavara lvfsppvilm deplgaldkk lreamqfeik
      181 riqenlgatv iyvthdqeea ltmsdrivvm hdgcvqqvgt pselynepng tfvadfigsi
      241 nfipatyrgn kngkcildis ervaveldal lhpklahksi gseirlavrp ehvgifsdpk
      301 kgqlsgtvea svfigsstvv lvrldafpdi dlrvqlpatt sspvlrknsr vgvnldtlsl
      361 ltfdletrla a
//
LOCUS       WP_176037282             246 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella tritici].
ACCESSION   WP_176037282
VERSION     WP_176037282.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..246
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27364
     Region          1..244
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 msliklenvs vefpiynasn rslknrvlni atggsverrr dglvivrgle nvsltlrdhd
       61 riglighngs gkttllrvls giyvptqgra tiqgqcvsli nislgidpea tgrenirlrs
      121 ammgihpkdl aynvekieef sglgefldvp frtyssgmqm rlafatstai rpeilimdew
      181 lstgdedfke ranqrmkelv ettnilvlas hsralleknc nriiwlehgk vkmdaspqkv
      241 lpiyfg
//
LOCUS       WP_176037385             163 aa            linear   BCT 11-JAN-2025
DEFINITION  CinA family protein [Brucella tritici].
ACCESSION   WP_176037385
VERSION     WP_176037385.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Galeazzi,L., Bocci,P., Amici,A., Brunetti,L., Ruggieri,S.,
            Romine,M., Reed,S., Osterman,A.L., Rodionov,D.A., Sorci,L. and
            Raffaelli,N.
  TITLE     Identification of nicotinamide mononucleotide deamidase of the
            bacterial pyridine nucleotide cycle reveals a novel broadly
            conserved amidohydrolase family
  JOURNAL   J Biol Chem 286 (46), 40365-40375 (2011)
   PUBMED   21953451
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Martin,B., Garcia,P., Castanie,M.P. and Claverys,J.P.
  TITLE     The recA gene of Streptococcus pneumoniae is part of a
            competence-induced operon and controls lysogenic induction
  JOURNAL   Mol Microbiol 15 (2), 367-379 (1995)
   PUBMED   7538190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003960
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..163
                     /product="CinA family protein"
                     /calculated_mol_wt=16695
     Region          7..160
                     /region_name="PncC"
                     /note="Nicotinamide mononucleotide (NMN) deamidase PncC
                     [Coenzyme transport and metabolism]; COG1546"
                     /db_xref="CDD:441155"
ORIGIN      
        1 msaliaeeka vavldacrka gimiataesc tggliagalt diagssdvvd rgfvtysnea
       61 kaemigvpme linrvgavsk evalsmaega lshsradvtv avtgiagpgg gsdekpvglv
      121 hiasarkgyp tlhrefrfgp ktraeirhat vlaaldlvle nlr
//
LOCUS       WP_176037415             140 aa            linear   BCT 11-JAN-2025
DEFINITION  HIT family protein [Brucella tritici].
ACCESSION   WP_176037415
VERSION     WP_176037415.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..140
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15112
     Region          7..138
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 msatyddnni fakilrgeip strvyetddv vafmdvmpqg tghtlvvpka psrnlldakp
       61 etlanvvqvv qkiaqavkta fnadgvtvmq fnepasgqtv yhlhfhvipr fegvalrpht
      121 gqmedaavls anaekiraal
//
LOCUS       WP_176037477             331 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Brucella tritici].
ACCESSION   WP_176037477
VERSION     WP_176037477.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..331
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36062
     Region          52..303
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(69,154,156,158..159,186,235,256,259,272,274,303)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 msisrrnfiv tasaagagla lspleltraa aetgsskvkp psqvenpgfh rfqfgdfeit
       61 tlsdgrragq apektyavdq dpkvvaalle enllpadrfv nsftpvlint gkelvlfdtg
      121 mgagareagl gkltsaleas gyktddvslv vlshfhpdhi gglmedgkpa fanaryaagq
      181 kefgfwtdpa rldspaktva emvaknvkpl aekmtflddd revvsgihsv aayghtpghl
      241 afrvetggks lmlvsdtanh fvitlqrpew hvsfdidkea avqtrkrmfd miatdrlpfi
      301 gyhmpfpala ylkregegyr yvaetyqlre k
//
LOCUS       WP_176037499             580 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Brucella tritici].
ACCESSION   WP_176037499
VERSION     WP_176037499.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13474615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..580
                     /product="M23 family metallopeptidase"
                     /calculated_mol_wt=62838
     Region          <311..559
                     /region_name="PRK11649"
                     /note="putative peptidase; Provisional"
                     /db_xref="CDD:236946"
     Region          <408..526
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mvfwsapane rkvaataepd faafrsalkg eplsshslkp frqvrfslht hlrfclalit
       61 amaiagggfl fttgrlvghg haaqpvmvnp atlaqhhaat kearltpavn gdptsrisrr
      121 idiaegvedg darlytyqhv vldlkgssra alddtlrggi svpkslpkrp eeelergvpv
      181 nvslakpava sgakvheiiv apqsrerlga llqaagiave dskrleeala rtelvpgdnl
      241 ellvdksrqh sdgeqhiala rfehgdidka iygraddgvf ratgnerlfa rlsrdamlta
      301 yhpqnavsns gsissrleqa gapktivgev eklasqngis lnggkkpdli dllfrksaet
      361 epelvfveft tdgksrrlyr hegnngadyf nedgssmtky lmqkplpngr lndgfgwrih
      421 pvlhvrkhhn gvdydapigs pivaagdgvv elisyqkgyg kyvrirhqgg ysttyahlss
      481 akkglkvgdr vkqgeeiayv gstgystgph lyyelkvgdq yvdpltarln agekltgssl
      541 nsfreeidhv gqivnemklp vmpaapeatk sasgkssrhh
//
LOCUS       WP_176037561             782 aa            linear   BCT 11-JAN-2025
DEFINITION  LPS-assembly protein LptD [Brucella tritici].
ACCESSION   WP_176037561
VERSION     WP_176037561.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..782
                     /product="LPS-assembly protein LptD"
                     /GO_process="GO:0015920 - lipopolysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87559
     Region          32..778
                     /region_name="LptD"
                     /note="LPS assembly outer membrane protein LptD (organic
                     solvent tolerance protein OstA) [Cell
                     wall/membrane/envelope biogenesis]; COG1452"
                     /db_xref="CDD:441061"
ORIGIN      
        1 mvlphsfsrl trgtalacvl alpfisvaal pspasaqdtl aanyksdpna rmllqadelv
       61 ydrdvntvta qgkvrieydg nhlvadkvty nqqtrrmtat gnveiverdg nkiysdhmdv
      121 tdsfrdgfvn glrvettdnt rfaaesaers ngeittfnng vytacepcak npdkpvlwqi
      181 karkiiwnst tktvrfehgr feflgmplaw fpafemadpt vkrksgflfp gfsykddlgf
      241 giknsyfwal apnydltlst taytkqgflt eaewrhrlen gtynlriagi hqnkpeefdl
      301 ntvdreednr gmvaskgdfe lnsrwrfgwd vmaqtdrnfs rtydiegyna qtqvskiylt
      361 ginnrnyfdl nfyrfnvqes ypvtdvykdy emhskqpwvf psldysytmp epvyggelnf
      421 ntnlqvlyrq nanytplgtr fprvpgfdgt narltteaew krtfitpagl vitpllalrg
      481 daigantnfn ladagytdal vrsealrama taglelrwpi lfsttssthi iepiaqlyvr
      541 nneryagelp nedaqsfvfd atnlfsrdkf sgydrveggt ranlglrysg nfnnsdwaly
      601 alggqsfqlg gvnsygtsdf vnvgadsglq darsdyvami gtsnstglal aargrfdkes
      661 fsvqrgelea qqswqkltvs aqyayiapqp aygyndlrqe vtgsatarin tnwrvfgsgt
      721 ydlvsetlvr assglaydde cftysmaytq trnpgedkts ygigfnislr tlgdigsgtq
      781 tf
//
LOCUS       WP_176037641             294 aa            linear   BCT 11-JAN-2025
DEFINITION  YdaU family protein [Brucella tritici].
ACCESSION   WP_176037641
VERSION     WP_176037641.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007954
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..294
                     /product="YdaU family protein"
                     /calculated_mol_wt=32709
     Region          3..121
                     /region_name="YdaU"
                     /note="Uncharacterized conserved protein YdaU, DUF1376
                     family [Function unknown]; COG3756"
                     /db_xref="CDD:442970"
ORIGIN      
        1 mtkmpwvrff psdwlggtrg msavetgiyi tliatmyerg epivedharl arlcgasnsa
       61 frkaldtlid egkitrieag lwndrvekeq vylseksevg sraanarwsk khnknntasd
      121 adalqtqcqg nanqkpdtry istdvdiket rtrdftsefe shfwpiypnk vgkpvartaf
      181 ikarakadle timaglrayv sktddrawcn pstwlnqerw adapaqvprg happggqqpa
      241 mmadltgall rqmtdrqnde pdsenrstie tsysggnhgt sapafrltap egrr
//
LOCUS       WP_176037668             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella tritici].
ACCESSION   WP_176037668
VERSION     WP_176037668.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..359
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39371
     Region          1..354
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masidiqsvr ksygehavlh gvdleikdge fivlvgpsgc gkstllrmia gleditagqv
       61 qisgkrvnel apkdrdiamv fqsyalyphm svadnmsysm rlrktpkeki asaikstatk
      121 lglepflerr pkalsggqrq rvamgraivr qpkaflfdep lsnldarlre qmraeikklh
      181 gelkatsiyv thdqieamtl adrivamhgg vvqqvgpple lydrpanlfv agfigspamn
      241 fldvtyqeqd skahlsltdg tqialaspms lddgdratlg irpehvtleq sgnlpthvdl
      301 veptgfgiil hlslhglpfk vftldrdall aegtvhvsfp tqhlhlfdkd gnrvearrt
//
LOCUS       WP_176037701             314 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Brucella tritici].
ACCESSION   WP_176037701
VERSION     WP_176037701.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..314
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36244
     Region          85..243
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mdsnpvffdv trvaiplyvl gilielvair ywqrkgefet kdaftsllmg agnvaaglll
       61 gfvsvtallw vwqfrffdlg lywwvfviaf ifddlryycy hriahrvrwv waehvnhhss
      121 qhynlttalr qswtgqmtgm fvlqvpmvll gfhpaviafv ygfnliyqfw ihteavgklp
      181 kpiefifntp shhrvhhatn pryldanyag tlivwdrmfg tfveelpedm prygivknvg
      241 tfnpvrvafh ewvgmfkdvf ssgltlrqrl mymiappgws hdgsrktsed lkadyvrlnp
      301 lqagkaglpe gfet
//
LOCUS       WP_176037707             375 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella tritici].
ACCESSION   WP_176037707
VERSION     WP_176037707.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 375)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..375
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40696
     Region          1..358
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 matlslknat ksfgnidvik gvdldiadre fvvfvgpsgs gkstllrmia gleeitggdl
       61 tidgerindt ppderglamv fqtyalyphm nvrdnmgfal klagvakaer drkveevakt
      121 lqldqlldrk pkqlsggqrq rvaigramvr epkiflfdep lsnldaalrv qmrielarlh
      181 drlnatmiyv thdqveamtl ahkivvlrdg kveqvgsple lyhhpvnrfv agfigsptmn
      241 fievkasavd adgvtvqlan grfvkalvks egvsagaplv lgirpehlhp aadgilegei
      301 mvverlgget ylyvqnesat glivaeaggg saaraheaak lgfdptdahl ftpdgkaler
      361 ferhplllte kktql
//
LOCUS       WP_176037735             371 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella tritici].
ACCESSION   WP_176037735
VERSION     WP_176037735.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 371)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..371
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40049
     Region          1..370
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 msflkisdly ksygnvsvlk dinieidegg flvlvgpsgc gkstllntia glepitsgdi
       61 aingktvsgl hpsqrdiamv fqsyalypnm tvagniafgm eirkvpkaer dkaiqevadi
      121 lqighlldrk psqlsggqrq rvamgralvr npqvflfdep lsnldaklrv dmrteikrlh
      181 srmkttivyv thdqieamtl atkiavlkdg ilqqfgtpae iynnpanmfv adfmgspamn
      241 lvtarvekng sgyaihlgrg edeplklplk aapqglgaye gkdivfgirp ealtdldgad
      301 rnadavvegd clidvvepag sdtfavtrlg gkhvvarlra daritagqsa qlafnldksv
      361 ffdpssqerv l
//
LOCUS       WP_176037756             326 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella tritici].
ACCESSION   WP_176037756
VERSION     WP_176037756.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..326
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35531
     Region          6..326
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mseqalleve nlridivsgs skhnvvedvs ftigagetfg lvgesgcgks italsmigll
       61 rkplsitgga irfkgqdlrs issremrklr gnriamifqe pmtalnplsp vgrqiaemfv
      121 lhqgatwhea erkavealas vqvpapeqrv knyphqmsgg mrqrvmiaia lacnpdllia
      181 depttaldvt vqaeilrlmq elctargtsv lmishdlgvi akmcrrvgvm yaghlveeri
      241 taglfhhpah pyahgllasl phlgsrqkeg qlrlqeiegv vpsisafpkg crfeprctra
      301 tdvcraqkpg wtpledagvv rcfhhe
//
LOCUS       WP_176037771             174 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter small permease [Brucella tritici].
ACCESSION   WP_176037771
VERSION     WP_176037771.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..174
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=19214
     Region          1..159
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mtkaidffyk ilgallvfll agmaimvfvn vilryaansg ltvseelsry ffvwvaflga
       61 vltfrenshl gieslvarfg rqgritcmai sylivllcsg iffwgtwkqf dinasmvapv
      121 tglsmiwvyg vglftggamf iiaaerflra vtgrltdeei atfagehsld hlme
//
LOCUS       WP_176037766             253 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Brucella tritici].
ACCESSION   WP_176037766
VERSION     WP_176037766.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..253
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27205
     Region          6..248
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 miehtplfla iaviaaflvg lskgglpsvg tlavplmalv ispvtaaall lpiyvisdmf
       61 glylyrhhfs arnlailtpa ailgvgigwm fsahlsptfi gmlvglvgil fcfnawfgar
      121 yrkkarkadv pggvfwgvlt gltsfvshsg appfqmyvlp qhlpklvfag tstilfaivn
      181 avklvpywql qqfsnldtsl glwlvpaavi gtfvgakltr impdgpffll vqltlfglsi
      241 kliadwivpy ffg
//
LOCUS       WP_176037714             353 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella tritici].
ACCESSION   WP_176037714
VERSION     WP_176037714.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..353
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37910
     Region          5..351
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtairpgsvt fenvtkkfgn ftalpdlslt vepgtlvtll gpsgcgkttt lrllaglehp
       61 tagriliggk dvtnlpaner dvsmvfqsya lfphmnsldn vayglessgl kkaearerae
      121 eglklvglag mghrlpaels ggqqqrvava ralvlepqvl lldeplsnld arlrrrvrte
      181 irelqqrlgf tavyvthdqd ealavsdtii vmkegniaqk gsprdlyetp asafiadfmg
      241 eanvvpcevm taeggeavir vgslthrvta rnarpgpaql airpnavtlq pkadggfpgr
      301 iahsaylgdh ieyeietehg klfivdpave ealppqtdvs iefktrglai inq
//
LOCUS       WP_176037804             391 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella tritici].
ACCESSION   WP_176037804
VERSION     WP_176037804.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 391)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..391
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42164
     Region          <166..391
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mtvlsgktar amfliapllv fialfflwpl gvmmkqavsd tavlrvlpqt adavslwdgq
       61 srpspemkqa lvtdlkastd qqavgdmvrr lnsaqsgfrt lmsktlsaie kgdpvpdlem
      121 idkrwsrpef wqaianalsp ttdrnllaav dmerdasgei vsmapgtsan raimlrtfwi
      181 aalvtlscav igypyavlla sskgwvrnvl faavllplwt sllvrtaawf illqdkglin
      241 dtliwlgitd tpfplifnra gvviamthvl lpfmvlpiys vlasipsnlm paaaslgapp
      301 wraflrvllp lsmrgilsgm llvfmsaigy yitpaliggp sdqmissiia yyatgsanwg
      361 magalglvll vaclvlyavy grltadeqgr a
//
LOCUS       WP_176037812             357 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella tritici].
ACCESSION   WP_176037812
VERSION     WP_176037812.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..357
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38769
     Region          3..357
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mpaflevadt rvrygnnevl kgvnlsvkkg efvallgssg cgkttllrti agfnmpsgga
       61 irvdgrdvtr lppdkrgmal vfqsyalwph mtvtqnmgyg lrirgasket ikqkveevar
      121 llglnsller kpaalsggqr qrvalgrala iqpdilllde plsnldarir lsvrheisal
      181 qrrlgitavh vthdreeamv madrivilne geiaqagape evynhpasdf vaafmgaenl
      241 ievpiqikad rieiaagann kastisagrr nlsdgmasar frseaahlca pgtdrntptp
      301 elaldgtveq tsypgglwrh mirvgdrhim vdaqeshqpg snveiripeh alflfdk
//
LOCUS       WP_176037813             286 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter permease [Brucella tritici].
ACCESSION   WP_176037813
VERSION     WP_176037813.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 286)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..286
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30607
     Region          10..268
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mtlllepfsy symlnamwvs alvggvcafl saylmlkgws ligdalshsi vpgvagayml
       61 glpfsigaff sgglaaaaml flnqrtklke daiiglifss ffglglfmis lkptavsiqt
      121 ivlgnilait pedtlqlaii gfvslsllll kwkdlmvvff denharsigl kpnllkimff
      181 tllsastvaa mqtvgaflvi cmvvtpgata ylltdrfsrl lwiavaigai tsftgayvsy
      241 fldgatggii vvlqtlvfls vfllapkhgl laarrkavia lrefqq
//
LOCUS       WP_176037823             345 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Brucella tritici].
ACCESSION   WP_176037823
VERSION     WP_176037823.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442477
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..345
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /calculated_mol_wt=38223
     Region          11..337
                     /region_name="AKR_Tas-like"
                     /note="Escherichia coli Tas protein and similar proteins;
                     cd19094"
                     /db_xref="CDD:381320"
     Site            order(17..19,24,46,51,85,128,179..180,205,233..239,242,
                     244,253..255,289,306..310,314,318)
                     /site_type="active"
                     /db_xref="CDD:381320"
     Site            order(46,51,85,128)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381320"
ORIGIN      
        1 mkplgrtglt vteiclgtmt wgiqntesda heqldialds ginfidtaeg yaipmspesy
       61 gktetyignw lkksgkrdki vlaskiaggg rqkwirdgar psrdsvreav enslkrlqtd
      121 yidlyqvhwp mrahyhfgqs wsfdpsktdg taetqqmhdv llglgdmvrd gkirhiglsn
      181 etawgtmqwl rlaeqhslpr iasiqneysl lqrqfdfdma elalcedvgl laystlaagv
      241 ltgkylggkl pagsraaise ggiwrnnvhs epairayidv akkhgldiaq maiaftltrp
      301 fmtstiigat tvdqlktdia ahqvklsddv lsdiekvyrq yprpl
//
LOCUS       WP_176037826             398 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Brucella tritici].
ACCESSION   WP_176037826
VERSION     WP_176037826.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..398
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41588
     Region          2..349
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mtdmtaarrn iviltiaqal gassppivis lgglvgqkls sdpalvtlpv slfnlglalg
       61 tlpaaffmrq fgrrnaymlg alvgasagvi aaagifassf vifclgtlta gfyaayvqsy
      121 rfaatdaatg dmkaraiswv mvgglvaaiv gpqlviwtrd tipgamfags flsqavlgll
      181 alpvlfmlra pkirkdpnai hdtgrplgei lrsprfilsv aagvcsyalm tfvmtaapia
      241 mvghghsvdh aalgiqwhvl amfapsfftg klitrfgkek italglvlia fsaiialggf
      301 dvghfwgali flgigwnfgf igatamvtdc htpaergkaq gandfimfgt vacasffags
      361 llhssgweti nwlvfpival vlvplilrlk pkgaaaei
//
LOCUS       WP_176037869             443 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Brucella tritici].
ACCESSION   WP_176037869
VERSION     WP_176037869.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..443
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47041
     Region          19..437
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mkyapqdksg selaiscnri ekldlalady avrdwnarei flnqrfetar telgcwqsls
       61 esneelppla gltmtvkacf dtegwvtscg skalqdtapa itsaalvhrl rlggatllaq
      121 tnmtefayga lgvnthfgtp rtpldpagea iaggsssgaa vavargysdf avcsdtsgsa
      181 ripaafcgvv gfkpsrgrye tdgmhwlsts fdvpgiitss vahcrliddv atgtatrkps
      241 tskpirlavp rlpsetafde iigklfgacr saleasgivi rdielpslte sakiavdggm
      301 igaeayalhr drlavdfasy dplvgtriqk grenpaylyv navsalaacr eqfdaniegf
      361 dgfilptvpm lppvlaalad edtylalnrr afsltefanr ldlpsislpi gkhpvglmlt
      421 grrgedeall aiaellepla akl
//
LOCUS       WP_176037943             234 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Brucella tritici].
ACCESSION   WP_176037943
VERSION     WP_176037943.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..234
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25949
     Region          21..217
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mnlaatnttd qnggnarwlp vynglreavv shrllpgtkl pedelatiys vsrafvrsal
       61 qalahdrlvr lepnrgafva epsreearev fearlliepq vaalaakvik leqvkqlrqh
      121 lhdehaalha grdseaimls alfhthlaei sghsilagfv gdllprssli islywerret
      181 tcqsdahhal vdaieehrad daaalmkthi ldllaglnle rvekeqkrls dilr
//
LOCUS       WP_176037912             349 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Brucella tritici].
ACCESSION   WP_176037912
VERSION     WP_176037912.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..349
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=37390
     Region          12..256
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mnrdkqvktd frwgiwgtgt iaaafaadiq attgmrvsav csrasetaet frrrigadka
       61 fgdsgeflsd anidavyiat psamhvlqam qaiaagkpcl iekplsldaa garqieaaak
      121 aknvfameam wsrflpaira tkqhidngri gtvtrieadl syiraydpqs rffspdlggg
      181 aafdlgvypv slalyflglp dhvdgrwqra ksgvdmrtef qlgwqgatas lscgfdrdgd
      241 nrmliegtrg tilihapflk aqrltlfsal aarsslgpng gnglfgkvmn rlplpgrtie
      301 tyafsgnglq fqaeavrdav hsgqisnatm pldqsaavad ivrkvlara
//
LOCUS       WP_176037950             271 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Brucella tritici].
ACCESSION   WP_176037950
VERSION     WP_176037950.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..271
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28629
     Region          11..268
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mtktvsdees sqklvpavmr aaqildqiak saqesgkgsv dglklsdlar rtglpkssvh
       61 glcqtlvhlk llklnsdgsf tmgsqsvrwa nvfmagsdiv dafheavaea dglgahtltl
      121 shlegpdviy lscrnstapl gitfrigmrv pavftatgka mlaamspqel arhlpaewpd
      181 litpasapsl kvleaemaea kakgysldng qlregmfcig aaicdrpfhp aagialsmma
      241 aearadiied mgtrvralan dvadrmgwls t
//
LOCUS       WP_176037982             263 aa            linear   BCT 11-JAN-2025
DEFINITION  inositol monophosphatase family protein [Brucella tritici].
ACCESSION   WP_176037982
VERSION     WP_176037982.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Atack,J.R., Broughton,H.B. and Pollack,S.J.
  TITLE     Structure and mechanism of inositol monophosphatase
  JOURNAL   FEBS Lett 361 (1), 1-7 (1995)
   PUBMED   7890024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10108155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..263
                     /product="inositol monophosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0008934 - inositol monophosphate
                     1-phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006020 - inositol metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28513
     Region          6..248
                     /region_name="IMPase"
                     /note="inositol monophosphatase and related domains. A
                     family of Mg++ dependent phosphatases, inhibited by
                     lithium, many of which may act on inositol monophosphate
                     substrate. They dephosphorylate inositol phosphate to
                     generate inositol, which may be recycled...; cd01639"
                     /db_xref="CDD:238817"
     Site            order(36,40,46,69..70,86..91,213..214)
                     /site_type="active"
                     /db_xref="CDD:238817"
     Site            order(39,41,92..93,95..100,152..154,156,158..159,167..168,
                     171,174..175,178,182..188,196,200..203)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238817"
ORIGIN      
        1 marsallnvm vqaamkagrs lardfgevqn lqvslkgpgd yvsqadrrae qivytelsra
       61 rpdygflmee sgeveskdgq hrwlidpldg ttnflhgipv favsialerq gqivagviyn
      121 pamdelytae rgggaflndr rlrvasrnkl vdsvigtgip hlgrghhghy lvelrnvmae
      181 tagirrmgav aldlayvagg rldgfwedgm hpwdlgagml mireaggfvs dknggqdifg
      241 tktivagnei iqkallktin kpi
//
LOCUS       WP_176037989             331 aa            linear   BCT 11-JAN-2025
DEFINITION  SRPBCC family protein [Brucella tritici].
ACCESSION   WP_176037989
VERSION     WP_176037989.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167397
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..331
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=36794
     Region          159..>282
                     /region_name="COG4891"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443919"
ORIGIN      
        1 mkspetvspd sserltvavp vafvygllly vmiwsrhyvd ampviaglml lpmavaslas
       61 slsdpraekg lwrhvrmgwa iigglvvism vlfheagicv amaapffmaf salgsavtlw
      121 iirqfrsrrs ttlvialplv vlpaelqmsy tphdgavttv ieiaappevv wqqtveirnv
      181 rpdelswtfs hgilgvpqpt darlngtgig avrdlqwthg vnfqeivtqw eenrllawdf
      241 rfgpgsippe veahikvdss ylklaqgdyr lepvanghtr ltltthyria tpidfycdlw
      301 gklflndfhg vvlkvirdrs ekiarrgdri t
//
LOCUS       WP_176038009             234 aa            linear   BCT 11-JAN-2025
DEFINITION  MOSC domain-containing protein [Brucella tritici].
ACCESSION   WP_176038009
VERSION     WP_176038009.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12233312
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..234
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26376
     Region          20..176
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
     Region          173..216
                     /region_name="3-alpha"
                     /note="3-alpha domain; pfam03475"
                     /db_xref="CDD:460938"
ORIGIN      
        1 mtetlihsvl agkvaplgar gvpsgidkqp vsgkarvtfe gldcdaqgdr kvhggpekvl
       61 hhyphdhyav wreeigenpr lnlrgafgen istsgldehn vavgdrfrlg salvevsqgr
      121 qpcwklnerf atadmavrvq ktgrtgwyyr ileeghvetg dtmilvdrls pdwtlhrvwh
      181 llyvdtlnyd elsvmaelsh ladswkryav rrlenrkved wslrlegkta esqk
//
LOCUS       WP_176038017             397 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Brucella tritici].
ACCESSION   WP_176038017
VERSION     WP_176038017.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..397
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41318
     Region          22..368
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,149,
                     152..153,156,225,228..229,232..234,237,265,269,318..319,
                     323,327,343,346..347,350..351,354)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 meqvsgreda aparapiitk eriavallfl mngyifggwa pkipefaerl gldsagmglm
       61 ilvfglgsla mmpvagalsa hrgsgmvvri falafipall vialvpnvit avivmfyfgg
      121 tmaamdvsmn anavavekkm rraimsscha fwslggliga atggfliaqf gstvhalvtt
      181 ivaailiaia wpsiipdteh hhpsgekqkl tlprsplpwl vgvmalfsmv pegaildwga
      241 yhmrqdlgas vtvagfgfaa fsgsmaimrf agdlvrdrfg avktlractv iaiigmlivg
      301 fgnssttaii gfaicgigis nmvpiafsma gnmpgvnpsv glsiattlgy sgmlvapsli
      361 gfvakhsgfg vvflalpvll lvvlafssla ryadhkh
//
LOCUS       WP_176038028             364 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Brucella tritici].
ACCESSION   WP_176038028
VERSION     WP_176038028.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 364)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 364)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 364)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 364)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 364)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..364
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39584
     Region          2..364
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 mrlvsftakg yrslrsvrfd lgqvtvfvge ngagksnlyr alqlvkaaae gnlstevvre
       61 ggmqsamwsg nrrkhetari ileavfeder lasrlsyrve aglpppvsga fpfepqikee
      121 qlnldtgrrp vdlmgrrgpa afardgegrr mehparllts esglavlgqs ghypeigdls
      181 aqirgwrfyh gfrsdrdapv rqpsiaataa mldedggnla svfatlahir qdtvdldrlv
      241 adalegaklv ipypdetatf glnfpafppr tfrpgelsdg qirllalaga llsyrlppli
      301 alnepeaslh pdmipslarm iaqasersqi wvvthsaala saitehcgar pirvskqdge
      361 tvle
//
LOCUS       WP_176038052            1596 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD-glutamate dehydrogenase [Brucella tritici].
ACCESSION   WP_176038052
VERSION     WP_176038052.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 1596)
  AUTHORS   Minambres,B., Olivera,E.R., Jensen,R.A. and Luengo,J.M.
  TITLE     A new class of glutamate dehydrogenases (GDH). Biochemical and
            genetic characterization of the first member, the AMP-requiring
            NAD-specific GDH of Streptomyces clavuligerus
  JOURNAL   J Biol Chem 275 (50), 39529-39542 (2000)
   PUBMED   10924516
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1596
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..1596
                     /product="NAD-glutamate dehydrogenase"
                     /EC_number="1.4.1.2"
                     /GO_function="GO:0004352 - glutamate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /calculated_mol_wt=175425
     Region          1..1595
                     /region_name="Gdh2"
                     /note="NAD-specific glutamate dehydrogenase [Amino acid
                     transport and metabolism]; COG2902"
                     /db_xref="CDD:442147"
ORIGIN      
        1 mtakqdrssk vkgskaskee kkggkskalt afsqllfewa ppedlaayda aaldssarhg
       61 yaalesyrkg ksiisvdngi erhgrpvsvi tivndnmpfl ldsimgelnd hasqifmvvh
      121 pvldiarekd elvilgeasq lapakgverv slvqihlpal nkqakadlta aikrvlgqvr
      181 aavsdwkpml arldgaiady krvsemtsdp ampeaiafle wlrddrfifl glreltfkgk
      241 gdkrelvpvk etlgilndne vrvlrkdddd tvtprevtef ldsneplivt kanslslvhr
      301 rsyldyvgvk ifgekgeaig elrlvglfts vaytssvagi pfirskadav ikhlgfnred
      361 hsgkalinvl eeyprdelfq idvesltana elilalgerp rvravprldr fgrfatvlvy
      421 iprdrydsvv rekighylvd vyggdsfefh pvflqngltr vqfvirrher stphvdreal
      481 eaevrsivrt wddavressd sadaktvala asfppsyrei ftapealvda griaglsaea
      541 plfvdfyryr tdgpdavslk lyhhgapvvl sqrvpllenm gfrvvseqti dlphagkdga
      601 avyvhdmqlv naygapvdls ddgemledvf rnvwdgladn dgynalvqta rltarqimil
      661 rsygrylqqa giaysqgfia aalnrypeia sdlyslfdlr fnpsakrrda aekklvdaie
      721 tallgvpsid ddqilrrfrn lieatlrtna yqpdaggkpr vtfafklnpr lveglpnprp
      781 yreifvygpe vegvhlrfga vargglrwsd raqdyrtevl glvkaqqvkn avivpvgakg
      841 gfypkrlpvg gdrnavfeag rdaykvfist llsvtdnied nhvvppaevv rhdnddpyfv
      901 vaadkgtatf sdtanaisqa hdfwlddafa sggsagydhk gmgitargaw eavkrhfref
      961 dmdiqtepft vagvgdmsgd vfgngmllse qirlvaafdh rdifidpnpv padgfaerkr
     1021 lfelprsswq dydrsklsag ggiysrsqkt itlspeaaav iglgktsgtp qeimtailks
     1081 kvdllwfggi gtyirssaet daqvgdrand airitgsevg arvigeganl gvtqrgriey
     1141 alaggrgntd aidnsagvnc sdvevnikia laaamrsgnl krparnkllv smtddvselv
     1201 lrnnylqpla lslserqgla elpyqarfma elenrklldr kveylpsdal laerqkagqp
     1261 ltrpelavll ayaklslsdd lvasqlpdep yfqsllfgyf pkrmtktyae eisghrlrre
     1321 ivatllandv inrggitfis rladttgksp adivrayvav rdgfdidtiy daidaldskv
     1381 pgdvqnqfyh lvgemlqatt awvlrndttr anltelvdti traraelepr fdglmpeylk
     1441 stlqadkaaf vekgapekla qrlanlqlag impdialiah ladadrvvta ktyfgvseaf
     1501 rigrieeaar sipvtdyydg lalsrasdti tqaargitia alkrfakekd paaawfaadg
     1561 arieqvksrm valteggdlt vsrlavaagl msdlaq
//
LOCUS       WP_176038100             350 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella tritici].
ACCESSION   WP_176038100
VERSION     WP_176038100.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 350)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..350
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36975
     Region          10..329
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mnqkdcvmpl veisnlkvaf ddvpvlhgid lsiergeavg lvgesgcgks vtwlaalgll
       61 pkkasisgsv llegrellta srgtlenirg griamifqdp ssslnpvirv grqieeavrl
      121 hrnlkgpaar aealrlmelv gipdagrrid nyphefsggq nqrlmiamal agnpdiliad
      181 epttaldati qaqildllaa lraetgmavv fishdlgavs qicervsvmy agriveqagt
      241 ealftaprhp ythglfdsip sleggrswli piegtvpepg klpqgcafsp rclsasdlca
      301 rslprlgvpq gdagegrmva cfhpypaash llpsigghis tpastraiaq
//
LOCUS       WP_176038105             177 aa            linear   BCT 11-JAN-2025
DEFINITION  EF-hand domain-containing protein [Brucella tritici].
ACCESSION   WP_176038105
VERSION     WP_176038105.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Persechini,A., Moncrief,N.D. and Kretsinger,R.H.
  TITLE     The EF-hand family of calcium-modulated proteins
  JOURNAL   Trends Neurosci 12 (11), 462-467 (1989)
   PUBMED   2479149
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11473824
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..177
                     /product="EF-hand domain-containing protein"
                     /GO_function="GO:0005509 - calcium ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19486
     Region          46..139
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
ORIGIN      
        1 mksktafiav iatsllsfpa laqenssant dkpaaetavt prkdmkdkrg pidlekfsrm
       61 ddlkaadtdg dgilsraeie alalkrivsr aadrmerrld ingdgkvtla evenqrkkef
      121 aaldrnedgk idrsemraak mhhqtrgshh kgphhmgkhk ggehkgpmkd qaekpqe
//
LOCUS       WP_176038111             187 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Brucella tritici].
ACCESSION   WP_176038111
VERSION     WP_176038111.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10536250
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..187
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=20084
     Region          4..170
                     /region_name="Ser_hydrolase"
                     /note="Serine hydrolase; pfam06821"
                     /db_xref="CDD:399658"
ORIGIN      
        1 mpatliipgf kgseaghwqr qwlhddpsal lveqddwhyp vlsdwmhale sklaenpgav
       61 lvahslgcal vahlasrpsa ahvagallva padaetmark ddrfqsftpl prqelgfpsi
      121 vvasrndeym sfakaealsh vwgsgfvdlg haghinvasg fsrwpegiil asslhrepin
      181 ntlsqaa
//
LOCUS       WP_176038170             390 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella tritici].
ACCESSION   WP_176038170
VERSION     WP_176038170.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 390)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 390)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..390
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42614
     Region          <162..388
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 miaasrkpgg sglaalvcla vplviyifly lvpigsvisi sldnrelsss lvnfssadsq
       61 drnaqaaalv admramdgsr qaavarelnq elsgfrtlfl ktaraadtie pelagltgfd
      121 prwneekywr viaqnseris frhferatgl kvneegrlet ggddiylqim wrtltiaiqv
      181 tlvtllisyp layaalhapr kmaafilvav lmsfwtsilv rttawvillq tsgvlntfll
      241 wtglikeplq lifnrfgviv amthvllpfa iipmmnvmrt ipksqvdasr slgagpvesf
      301 lrvyfpqslr gvgvaagtvf ilalgfyitp altggpkdqm lsfyiadfvk ralnwgmasa
      361 lsvlllsivv mlvslfgalr wlanrrggia
//
LOCUS       WP_176038221            1061 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Brucella tritici].
ACCESSION   WP_176038221
VERSION     WP_176038221.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..1061
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113548
     Region          1..1040
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnfsrffvdr pvfagvlsvl ifvagligmt glpiseypev vppqivvraq ypganpavis
       61 etvatpleeq ingvegmlym qsqatadgvm tltvtfalgt dpdqaqqlvq nrisqaeprl
      121 peevrtlgvt taksspdltl vvhlispdgr ydvnylrnya vlnvkdriar vpgvgqvqif
      181 gggdysmrvw idpqkaaerg lsasdianai rqqnvqaaag vigaspsvsg ldlqlsvnaq
      241 grlqspeefa nivvksgseg eitrlgdvar vemgaadysl rslldnkqav gmgvfqapgs
      301 naleisenvh aamadlkktm pegvdfdivy dttafvkasi esvvhtllea ivlvvivvil
      361 flqtwrasii plvavpvsiv gtfavmyvfg fsinalslfg lvlaigivvd daivvvenve
      421 rnieqglspv eatyramqev sgpiiaialv lvavfvplaf itgltgqfyr qfaltiaist
      481 visafnsltl spalaalllr ghdapkdrlt rimdkafgwf frgfnrffga sseaygrgvg
      541 silsrkslvm glyvvllgvt fvlfravpgg fvpaqdkqyl igfaqlpdaa tldrsedvir
      601 rmsdialkhp gvanaiafpg lsingftnss nsgivfvtlk pfeerktpel sanaitadln
      661 qqfgaiqdaf iamfppppvq glgttggfkl qledrnglgf kalddatkaf lakayqtpel
      721 aglyssyqin vpqlyadldr tkarqlgvav tdvfetlqiy lgslyvndfn afgrtysvri
      781 qadanyrsha edigklkvrs qsgemiplsa llkveqtvga erairyngfl sadingnpap
      841 gfssgqaqaa ieriaeetlp pgiayewtdl tyqqilagss gflvfplall lvylvlaaqy
      901 eslalplsii mivpmgimaa ltgvwltggd nnvftqigli vlvglsakna ilivefarel
      961 elsgrsvvqa aveasrlrlr pilmtsmafi mgvvplvtst gagaemrsam giavfagmig
     1021 vtafgifmtp vfyvlirkls gerplkhaga kieaphlapg e
//
LOCUS       WP_176038270             353 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella tritici].
ACCESSION   WP_176038270
VERSION     WP_176038270.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 353)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..353
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38664
     Region          1..347
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mstvecrsil krygaqevir dfnleisdhe fvvflgpsgc gkstilrmia gleeitggdl
       61 liggqrmndr dpgdrgiamv fqnyalyphm tvqeniifgl eragipkqti adrlkpvvaa
      121 lglevylgrk pselsggqqq rvaiaramik tpevflfdep lsnldaklrg slrveianlh
      181 relkttsiyv thdqleamtl adrivlmkdg rieqmgtpee iyqapatlfa agfigtpnmn
      241 ffelnadeek iadetislpr psglkpgpvt vgirpgafrl neaggqirgq iernefhgen
      301 rlvtiragkh vfsiavptsm rlqeghnigl dvvpnslhlf dahtglrnsi sgg
//
LOCUS       WP_176038276             319 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella tritici].
ACCESSION   WP_176038276
VERSION     WP_176038276.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..319
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32610
     Region          15..318
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mqqgtagnly isvqrsrnrg ltglyvvvgi fvllyawlfp gilsvggfsk ftqnwfplal
       61 vtmaqallml nggitlaigp lvslgaviaa ttmgsafgvf ggvvavilsg fvigaltgsi
      121 vafmrlpaii vtlagsfiit giallilprp ggfipdwlsd flaghspsaf iilvlvvlgw
      181 klflatpmgl giyaagenpt gayrsgipve kvkvisfals gvlatcaglf vaaqtgsgdp
      241 vigtpftlns iaaavlggvg flggkgtmrg aicgslllsv minvmfflgf ppvaqyiaqg
      301 liivgavalp efagkwrks
//
LOCUS       WP_176038308             336 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD:protein FMN transferase [Brucella tritici].
ACCESSION   WP_176038308
VERSION     WP_176038308.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..336
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=36897
     Region          47..330
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 mrieggqrvs rrlvlaggaa gvvfwatpkh avsldlpepi iwrgqamgap akiilyhpdr
       61 siaerllrev vqeaerleni fslyredsel aelnrngala spspdlvevl richecwqas
      121 dglfdptvqp lwnclkkhfs qehpspdgps rqlwdealak vgfshvlfdd nriafskrsm
      181 sltlngiaqg yvtdrvtall qregvehalv dmgeyralgs rpdgtawrig iadleagart
      241 eehvdirdqa latssftgfq fdesgrfnhl lnpktgfsaa lygrvtvtaa saamadalat
      301 afnlmdskqi edtlqklrgv sahvvtrngt nlrfpa
//
LOCUS       WP_176038345             293 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Brucella tritici].
ACCESSION   WP_176038345
VERSION     WP_176038345.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..293
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30812
     Region          1..282
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mskvadiitr lhvvaqdgsk sarrlaalvl adpdyaskaa iseiatragv septvtrfcr
       61 algcdgvrdf kfflaqalai ggqyltaeip ardvresria tavtdaaiaa iqrasdgldm
      121 svlmkvaerl aaggpvlclg sggissmlat emqnrlfrlg lpvsaqvdgq lqrmyaavtt
      181 hettviafsv sgfarsvvea vlvarqygaq tvaitpagsd lakaadvlip yqanedgniy
      241 kptssrfall aildmiatat aeargpkvle slrrikhsln tltiddprlp lgd
//
LOCUS       WP_176038360             313 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella tritici].
ACCESSION   WP_176038360
VERSION     WP_176038360.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..313
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32897
     Region          2..309
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mrlssssvrl ltpvfslvll laavfymqpr amsytglnll fnlavpiala tiaqmlimav
       61 ndldlsmgtf vsfvvcvaat ylnttpvigv lilvaaiaay aalgalihlr nlpsivvtlg
      121 msfvwggfav lllpspggqa pdwarwimta kppfmpmaiv asiliavvth fivmrstfgv
      181 lmrgaggnsr sieragwsvt miragtyala affavlagia lvglttsada nialrytlls
      241 iagvilggge fvggrvspig avigaltltl agsflsfmri spdwqigaqg gilivvlalr
      301 lflnrlekre kkq
//
LOCUS       WP_176038349             123 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Brucella tritici].
ACCESSION   WP_176038349
VERSION     WP_176038349.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..123
                     /product="RidA family protein"
                     /calculated_mol_wt=13128
     Region          1..121
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 msrkqvfgas hvplspavra gdtvyisgqv pvgpngqive ggieaqtrqa lenvkaalal
       61 agatmedvvk ttiwledard fgrmnavygs yfpkeppart tvesrlmidi kieveaiaya
      121 pkk
//
LOCUS       WP_176038361             315 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella tritici].
ACCESSION   WP_176038361
VERSION     WP_176038361.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..315
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32782
     Region          11..315
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msrlavltnr pwiwsfiata ivwiitilft ggagahglsh aaftfasfsv ivglgqmfvi
       61 tlgpgnidls vpanmtlaat lalklmdtqd gmvlaglgva ilvgvaigic nyalikllri
      121 ppiiatlsms fliqstaiws nrglrvkppe slaqfttsst lgipnvaiia lilsvigwvl
      181 lkrsiygrwi saigqnpfaa rmagvpvdgt rfvtyllcav laslcgflla cfsggaalnm
      241 gaeyllmsia vviiggtava ggdsnipgiw gaalfmfliv smlntygfga gvrlvltglt
      301 iiaviilasg rraer
//
LOCUS       WP_176038430             235 aa            linear   BCT 11-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Brucella
            tritici].
ACCESSION   WP_176038430
VERSION     WP_176038430.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..235
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25291
     Region          7..233
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 msrisrkeer iaelaalvde vgvlrlrdaa arlgvsemti rrdiggdggm lnclggyiip
       61 tqdgvngdyv fdfekdshan akaqacaaaa aliepydtvf idcgttmphl ahripqnqhi
      121 tvvcyalnia eilsqrsdvr livlgglyhp eaasfsgdeg idvlkrvnin kaflsaggvd
      181 dqhgvtcshf hevpikqmam qravekhlvi dkskygkvra arfagtadft sivsg
//
LOCUS       WP_176038502             450 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Brucella tritici].
ACCESSION   WP_176038502
VERSION     WP_176038502.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..450
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48094
     Region          <290..442
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mtgnqaktst kkvfgerkep pvliiargek ishftfrpwm aalggaafla lsvgylgata
       61 ylvlrddlms agiarharnq qlyedrisal rtevdritsr qmldqqvmen kvaelmqrqq
      121 tlsardgkla pllerasqlq pmpempteka pdleqhsqli pdealagref pgvdpiitgp
      181 vpgkspagkp drradagsig lrlsgglsge stletsdkil atitqnlhri eseqngkvrv
      241 ladaayekad sildtlnaag lrietpanaa vamggplipv sspgmvvndf dmqlrnldsa
      301 ldrldqvrkr vsalplanpa pgkpvtslfg vrrdpflgta afhsgidfra aygqtvksta
      361 agkvvkagrf ggygnmveid hgngfstrfa hlssvlvrdg qqvaagtivg eagssgrstg
      421 shlhyevren grainpvnfl kagkqiepll
//
LOCUS       WP_176038520             323 aa            linear   BCT 11-JAN-2025
DEFINITION  dipeptidase [Brucella tritici].
ACCESSION   WP_176038520
VERSION     WP_176038520.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..323
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=34859
     Region          34..319
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 miidglqcgh fdretfqslq kagvggvvvt cgfwegaies ldslgrwrdl vrantdvaei
       61 altsqdvari gssgkvaiil gfqnanlfgg rirfvelfae lgvrvvqlty nnqnelagsc
      121 yetedsglar fgkeviremn aagilvdcsh vgdrstldai easakpiavt hanarslfdh
      181 krnksdavlk algqtggvig casyrnitgd dycqsieawc gmvartvdia gidsvaigtd
      241 rshnftppdy swmrqgrwtr gvdygaasaa rpgkapppaw fhevedmavi pgglrsvgfs
      301 eeevakithg nwlrlyeatf rka
//
LOCUS       WP_176038523             263 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella tritici].
ACCESSION   WP_176038523
VERSION     WP_176038523.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..263
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29004
     Region          2..261
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mnrvlrfagl ivlvfiaapl vivvpmsfsn arslqfpppg ywlgyyqayf tdwtwlrpti
       61 nsiviatatm iltmvlvvpa tfalvrhrfr gkgiadlmml mplavphivm avgyysyfgt
      121 fgivhtrlgv vlahcclsvp iaflvlsanl kgfdrtlera aqslgasptr tfihvtlpil
      181 rpgliisalf afiqsfdetv vaifisgrda etlprkmfds irqeadpvia vistllfiav
      241 ilgvtapavi arlrnrqmri rvl
//
LOCUS       WP_176038539             259 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Brucella tritici].
ACCESSION   WP_176038539
VERSION     WP_176038539.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..259
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26517
     Region          7..256
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mvlsnsilaa vgsgsvvgfm lgllggggsi latplllyvv gvsqphvaig tgalavsvna
       61 fanitshalk ghiwwrcgvv fsalgtigal igsslgkald gdrliflfgi lmivvglfml
      121 kpkkrldver rpidlrmclv taavalasgs asgffgiggg flivpglmla tgmpminaig
      181 tsllsvgafg latalnyats glvdwwlage figggviggv fgmilatrls gyrntlnrif
      241 aaiifivaay ilyrnwtgi
//
LOCUS       WP_176038567             200 aa            linear   BCT 11-JAN-2025
DEFINITION  cysteine hydrolase family protein [Brucella tritici].
ACCESSION   WP_176038567
VERSION     WP_176038567.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..200
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21510
     Region          4..184
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mrtvlialhy qnevlhadgk irvgvaeksd greelkekaa rllaavrghg ipvvlvriaf
       61 rpdhadvvqn gkifrdvvan kamidgswga dfhdgfgpvd geyvvkhsrn nafygsqlee
      121 vlrvlkaerl viagistnfv veatvrcasd mgyeiivasd acssaslaqh qaslenmkll
      181 adimtvdeva qmiaagglqs
//
LOCUS       WP_176038546             187 aa            linear   BCT 11-JAN-2025
DEFINITION  type II toxin-antitoxin system VapC family toxin [Brucella
            tritici].
ACCESSION   WP_176038546
VERSION     WP_176038546.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003923
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..187
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /calculated_mol_wt=20891
     Region          43..178
                     /region_name="VapC"
                     /note="Ribonuclease/mRNA interferase VapC, contains PIN
                     domain [Defense mechanisms]; COG1487"
                     /db_xref="CDD:441096"
ORIGIN      
        1 mpsfdiagak rwlrsfpsgn isrrpdsklp ffdgnnlasq gllldtcvyi dqmqgklpde
       61 ieeflskrhs yhssvavqel ahsmgaldpn dprtahvqkv isdtiesmte hrtsvpdidv
      121 lgraailngv icrlqhysdd qkrkclqdct lflqglkggf viltrnvkdf dmclqlvpag
      181 rvlfyrv
//
LOCUS       WP_176038572             293 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Brucella tritici].
ACCESSION   WP_176038572
VERSION     WP_176038572.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..293
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=31538
     Region          3..293
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mshfygvipy lvsplkadgn idekvlgdlc ndligkgvtg ltplgssgey aylsdekkrr
       61 ivevvveasn grvsvvpgva svstegaieq arlykkigad givgvlesyf plseqevrny
      121 fldiansvdl pivvytnpnf qrtdlsidti stiadhpniv glkdastntg rllsiinrce
      181 gkldvfaass hiavsvllmg gkgwfagpac vlpeqsiely nackrgeweh aakiqkrlwg
      241 fnevfaryrl asclkaalqi qgyevgdpir pqtpldanav kivkdalqaa sal
//
LOCUS       WP_176038618             114 aa            linear   BCT 11-JAN-2025
DEFINITION  TraR/DksA family transcriptional regulator [Brucella tritici].
ACCESSION   WP_176038618
VERSION     WP_176038618.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Hall,T.M.
  TITLE     Multiple modes of RNA recognition by zinc finger proteins
  JOURNAL   Curr Opin Struct Biol 15 (3), 367-373 (2005)
   PUBMED   15963892
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Brown,R.S.
  TITLE     Zinc finger proteins: getting a grip on RNA
  JOURNAL   Curr Opin Struct Biol 15 (1), 94-98 (2005)
   PUBMED   15718139
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Vassylyeva,M.N., Perederina,A.A., Svetlov,V., Yokoyama,S.,
            Artsimovitch,I. and Vassylyev,D.G.
  TITLE     Cloning, expression, purification, crystallization and initial
            crystallographic analysis of transcription factor DksA from
            Escherichia coli
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 9), 1611-1613 (2004)
   PUBMED   15333933
REFERENCE   5  (residues 1 to 114)
  AUTHORS   Paul,B.J., Barker,M.M., Ross,W., Schneider,D.A., Webb,C.,
            Foster,J.W. and Gourse,R.L.
  TITLE     DksA: a critical component of the transcription initiation
            machinery that potentiates the regulation of rRNA promoters by
            ppGpp and the initiating NTP
  JOURNAL   Cell 118 (3), 311-322 (2004)
   PUBMED   15294157
REFERENCE   6  (residues 1 to 114)
  AUTHORS   Matthews,J.M. and Sunde,M.
  TITLE     Zinc fingers--folds for many occasions
  JOURNAL   IUBMB Life 54 (6), 351-355 (2002)
   PUBMED   12665246
REFERENCE   7  (residues 1 to 114)
  AUTHORS   Klug,A.
  TITLE     Zinc finger peptides for the regulation of gene expression
  JOURNAL   J Mol Biol 293 (2), 215-218 (1999)
   PUBMED   10529348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..114
                     /product="TraR/DksA family transcriptional regulator"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13045
     Region          <43..114
                     /region_name="DksA"
                     /note="RNA polymerase-binding transcription factor DksA
                     [Transcription]; COG1734"
                     /db_xref="CDD:441340"
ORIGIN      
        1 mtsnlyeqkr rsekfkpvle krrrellrrl aaiendfeqp rnqddddrai ernndevlee
       61 lgqagqkela aieaaihrle agtfgictrc gkeinerrle avpyapccqa caek
//
LOCUS       WP_176038661             578 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease subunit [Brucella tritici].
ACCESSION   WP_176038661
VERSION     WP_176038661.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 578)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 578)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 578)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 578)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   6  (residues 1 to 578)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..578
                     /product="ABC transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62780
     Region          31..284
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
     Region          327..559
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mtntsaktwk pdaiwlaapa llllavffll pmfrllglsf tddaegsfsl vnyerlgdsl
       61 lywrilgitl eisaltaifs vlfgypiamw lasledrkrg nmlmlvllpf wtsylvktfa
      121 wmillgkngv fnsillgsgv adrpvnlmyn elgvligmvh amiplavlsm lpvmtgidnr
      181 ltlaastmga srsdrfwlvy fplsmpgvva aglltfitsl gffivpaflg grqqtmlaqa
      241 iitqvqeivn wpfaavlatm lvvaalvvig iynklfglss lssgngvqsk kamspdnplr
      301 klgygilalv arifrpldrl fppkeggspf rtiyvvllig flmlpglivi plsftsgrnl
      361 afpppgfslr wfeeyfnsai wmsatmrsfg vafataffat vlgglaalal srsssrlngl
      421 ifglilapmi vpriviavgl fylmaqiglv atdtglvigh tllalpyafi tigsvlknyd
      481 wrlnqaaetm gagkltvlrl itipllrggl lsaalfafvt sldeltiaif vsgglkttlp
      541 kqmwddmflq lnptlaavsv ivllivtvil llarkler
//
LOCUS       WP_176038722             506 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Brucella tritici].
ACCESSION   WP_176038722
VERSION     WP_176038722.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..506
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55991
     Region          6..487
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mslvsiqnls ltlheplfan ldlvigeger lgivaangrg ktsllrllvg egeptlgtit
       61 rsrglkigyv sqyvpeslfs rsfyevvldg lddeardyes wradivlddl nvseelrqrp
      121 igqlsggwqr lallarawvs epdvllldep tnhldlekvr llenwlnalp rsvavvvssh
      181 drafldavtk rtlflraeks pifalpysqa rvaldeidaa darqfekdmk tvqqlrrqaa
      241 klnniginsg sdllvvktkq lkaradkiee sakaahvers agkitlnsrg shakalvvld
      301 qaeiatpdgr llfktgqlwi npgdrivllg angmgktrll tlvreailap dqaqagikat
      361 pslvlgysdq alselrpdwt pfetitrsfd igdqrtrsll agagmtlemq akplerlsgg
      421 qkarlamlvl rltnpnfyil deptnhldie gqealevell rneaaslivs hdrsfvrnvg
      481 nrfwmierkr pvevespeff fdgigs
//
LOCUS       WP_176038724             188 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Brucella tritici].
ACCESSION   WP_176038724
VERSION     WP_176038724.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 188)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..188
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21635
     Region          103..173
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mkekalklsr lssltplilr keirafclri ikeqyaieyn ekwhadldsl llsndlnwfs
       61 tpnrgrfyta scgetgkiia agglydlsyk pttqsrlqtr yeytapvcqi vrvyldssyr
      121 rrgigrqivk aleadayelg yhqcylhada eatntlrfwr algykdfgrf sylagsrvdt
      181 cvdfdkqi
//
LOCUS       WP_176038729             139 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA thioesterase [Brucella tritici].
ACCESSION   WP_176038729
VERSION     WP_176038729.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..139
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14751
     Region          17..127
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 msvptetssn sdynflemvf pdranhygtl yagnaleilt raafatasiy takpvvmaev
       61 lkikfhspva vgtvleitan ilnasrrsvt vgvsitnqns enaapvitgq frmvavdsag
      121 hptdvqknln mtcgkeics
//
LOCUS       WP_176038756             372 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Brucellaceae].
ACCESSION   WP_176038756
VERSION     WP_176038756.1
KEYWORDS    RefSeq.
SOURCE      Brucellaceae
  ORGANISM  Brucellaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 372)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Brucellaceae"
                     /db_xref="taxon:118882"
     Protein         1..372
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40957
     Region          1..324
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtklevknls rtfgstrave dvslnvdege lvcllgpsgs gkstvlrmig gferpstgsi
       61 lidgadvtnv pperratgmv fqshalwthm nvfanvafgl klrrlgreei rtrteralnm
      121 vgltgygnrr psqlsggqqq rvalarslvl epkillldep fasldqhlre rlreevreiq
      181 hragitmifv thgqdealal adrvaimrdg rieqvdrpdv vyrqpqtefv agfigqmnll
      241 agdvhagslr aggialpvsl sdgpatlair pedlclqran gewdatvlrv tdfgthlave
      301 lrtetgaqfk amtspseewv pgmrtkmlpr kftvyrdgrv calpmptlds dksarasylt
      361 ysktlqlsdn qh
//
LOCUS       WP_176038761             164 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Brucella tritici].
ACCESSION   WP_176038761
VERSION     WP_176038761.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..164
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=18607
     Region          62..164
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mnlhnlipwh rnargtfsti parrdplqsl hdqvdrlfde afrlgttgql wfgsefdtwp
       61 kiditdeeaa vrivadlpgm eqkdidlsin dgvltlkgek taetenkdsk laerfygrfe
      121 rqipigydld edkvdahfen gvlkitlpks egsrsrpksi lirs
//
LOCUS       WP_176038821             175 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-binding protein, partial [Brucella tritici].
ACCESSION   WP_176038821
VERSION     WP_176038821.1
KEYWORDS    RefSeq.
SOURCE      Brucella tritici (Ochrobactrum tritici)
  ORGANISM  Brucella tritici
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 175)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 175)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 175)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10598562
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Brucella tritici"
                     /db_xref="taxon:94626"
     Protein         1..>175
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
     Region          47..>149
                     /region_name="AAA_22"
                     /note="AAA domain; pfam13401"
                     /db_xref="CDD:379165"
ORIGIN      
        1 mntdelkelk rhiygtyles prdrklrnml qgmvdnvddh lnggggsrqt alfvigesgs
       61 gkshslkhhc ghiaefqqre nefgetitpf lsieasssst mkgfaitlls amglpanskq
      121 tetqlfsavk tqlkargily lhvdeaqhli rhdsqkvite vqdglkslmq ipdwp
//
LOCUS       WP_176038876             920 aa            linear   BCT 11-JAN-2025
DEFINITION  phage tail tape measure protein [Burkholderia multivorans].
ACCESSION   WP_176038876
VERSION     WP_176038876.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474873
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..920
                     /product="phage tail tape measure protein"
                     /GO_process="GO:0098003 - viral tail assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=99169
     Region          <12..87
                     /region_name="CCDC22"
                     /note="Coiled-coil domain-containing protein 22;
                     pfam05667"
                     /db_xref="CDD:461708"
     Region          72..816
                     /region_name="COG5283"
                     /note="Phage-related tail protein [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:444094"
ORIGIN      
        1 msdrslrlev vlkaldqasr pireitgrnr alvkdlrdtr trlkelgdtq krigefrelr
       61 rgmqeteaka raaqervrql aqqmkaaesp traltrehqq avraakalag qldqerqrld
      121 gvrsslaasg vstrnlvehq ralrssiaet navlteharr ldamnnqqqr iaaartkmgv
      181 mrgaaaemai ggyaaratgq hiladlrepl aeakkiqner grilglglge ratqdaeryv
      241 ramktpgvai adnmtlmrda msifadehha qmvmptlakm kfaneamfga dqgheneekf
      301 mnmlkvielr ggtkseaafi keanmvqqvl tatggrvggd ewrnfiqtgk vaakqmrqda
      361 fyyqmepliq emgghaagtg vqaaysnlmq gkttvraakr lvelglvdkk sveyntignv
      421 krikpgalig gdlfnaspfe wmekvllpkl kakgitsdak ileefstimt ngnganlfat
      481 mymqreqihk nerlnrgayg idklhalgqq qtegkelial ekvrnlrtvi geqvlpvynr
      541 alelttsvle rllgfakeyp tftravaiga aglgvllavl gtltitlaav lgplaivrfs
      601 msmlgiqgsv lvralgaiar tllfvgrval tspigiviag ialaallivr ywepikaffs
      661 gfwqgladgl kplaplvsra fgilgaafap lkplfvwlmg aakgvrdwlt rllppvdask
      721 esldaatgag rafgawladi irgladastr faefgsnlms glvdgitngl gavktaiqra
      781 gdsvvswfke rlgihspsrv faalggftma gleqglrngq dgplatvrel gkrivaagag
      841 igltgaaiag saplsvdnrp pliaataara pasapapiti nvyaspgmda nalaqkvlqv
      901 mrqeqaaqaa rersrlrdrd
//
LOCUS       WP_176038896             145 aa            linear   BCT 11-JAN-2025
DEFINITION  ester cyclase [Burkholderia multivorans].
ACCESSION   WP_176038896
VERSION     WP_176038896.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Sultana,A., Kallio,P., Jansson,A., Wang,J.S., Niemi,J., Mantsala,P.
            and Schneider,G.
  TITLE     Structure of the polyketide cyclase SnoaL reveals a novel mechanism
            for enzymatic aldol condensation
  JOURNAL   EMBO J 23 (9), 1911-1921 (2004)
   PUBMED   15071504
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..145
                     /product="ester cyclase"
                     /EC_number="5.5.1.-"
                     /GO_process="GO:0030638 - polyketide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16246
     Region          9..131
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
ORIGIN      
        1 mnpvdsvaiv enfwrevwqq pqnpeaidrl vhedfvissg ghdivgreaf kawvrefqsk
       61 vhnfefhvve sfqnatgtrv asrwrvtgrn nglmgtepng apfemtgtav wdvgpdgllr
      121 hnwvernaye vhgaiispga qphvf
//
LOCUS       WP_176038942             603 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia multivorans].
ACCESSION   WP_176038942
VERSION     WP_176038942.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 603)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12379621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..603
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62791
     Region          1..284
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
     Region          329..603
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 maswldytln glivgniyal lavglalifg vshlinfahg svymvgafig wlcltrfglp
       61 lpvalaavvl gcgalgvaie riglrplrha ariapllati gisfildqla qlafgadpra
      121 vptplpdwhl rlggatlgsl dlliagigia aaallygflr ftrlgwavra taqdrdaalq
      181 mgvdvdrvnq tvfaiacalg gvsgllvgmy ynsidpamgf qatlkgvval ligglgnvpg
      241 aiagslllgl vesygvalfg tsyrdlfafg llivflvwrp nglfsanral ppepmtgtfl
      301 aaakalrvpr paivalvala vvlpwlgasp yvlqtltnaw lygllalslt lvagtvgqis
      361 lghaallvig ayasallssd lgwspavtip cagaitavlg tllvypafrl rghyvsiatl
      421 gigevvslvi lnwdgltrgp lgitgiaplp wastaqaayw ftltvliafa lvqvrllrsh
      481 lgrtlravre ddvaarahgi apnrykaiaf avggvaagvs ggiaahlysy inhqtfdsqv
      541 silaltmvil gglgnvlggi vgalaliglp emfrwaadyr mliyglvlll lvrfrpqgll
      601 gtv
//
LOCUS       WP_176038963             165 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia
            multivorans].
ACCESSION   WP_176038963
VERSION     WP_176038963.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..165
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18118
     Region          4..143
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mpgitlddld lrilailqdd asvsnlqlae ralsspptcm rrvrrlteag virrqvamld
       61 pvaigtavta iieisldwqt aedydafeay vcaepavtqc yrvspgpdfv vvadladvae
      121 ydefarrlft gasnvrnvrt ffsthrakfe tnarvghgmr krgge
//
LOCUS       WP_176039034             147 aa            linear   BCT 11-JAN-2025
DEFINITION  PaaI family thioesterase [Burkholderia multivorans].
ACCESSION   WP_176039034
VERSION     WP_176039034.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..147
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15654
     Region          1..135
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mtdivdharg alraqpfsml lgtelmhige nevslclavr delrqqhgfv hggvisylad
       61 naltfagala lgprvvtgey kinylrpavn gtlvaraklv yagrhqatcq chvfvidgdh
      121 erlvaiaqgt inrvgdgknp gapqeta
//
LOCUS       WP_176039116             702 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            multivorans].
ACCESSION   WP_176039116
VERSION     WP_176039116.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..702
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=77482
     Region          11..702
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mqlsdipsff qlqsnrlfti etplkgrsel vlvnftcsen lsdlfhidtq lasqdrsiel
       61 kkmigqpvti tlqltdaias seeryfhgyv vafshldtdg glttysavik pwlwmlsrrq
      121 dirifqektt qdilsalfrd ygsmasfefr lskatqnrsy ctqyketdle faqrlmqedg
      181 lfyyfehtkd ghkliitdns iaakpidgms pileyskgea rddlavvknf sarrqlessr
      241 vglktydyka pgarrfsggn tgvdqgdvpa yeiydylgeh gfpgsdrged larfraqala
      301 ahskiftgtt tsrrmmpary fqldehydhe gkpedrqfli tgvmhagsnn yqvgegaaty
      361 acsftcirkk ipyrppftia kptiigpqta vvvgpkgeei ytdslgrvkv qfpwdrlger
      421 nqssscwvrv gqpwagsgfg mvniprigde vvvifldgdp drpliisrvy naqnmppwal
      481 pasatqsgil srstkggnvn tanairfedk kgeeevwlha ekdqrieveh deshwvgndr
      541 tknvdhdetv hvghdrtetv gnnetitigv drtervgnne tltvggnrne tiegmenlli
      601 altstetvgl akaltvggay tvtvagaint aaglasaeev glskttmvgk tytvtagdri
      661 elrtgkasiv lessghitis gtsidilgsd avtvdgktvd ln
//
LOCUS       WP_176039128             715 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia multivorans].
ACCESSION   WP_176039128
VERSION     WP_176039128.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..715
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=76402
     Region          36..692
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 magapqplss nrpasrfara lggmmrefwr mdgarlihva ktvlaavlal gvsmrielas
       61 prtalvtvvi lmmhqhsgmv margfyrgvg mlvgnlaalv ligafpqerv lflsalvlwi
      121 gcctwgaayf rnyqsygfvl agyatciaai psidrpydii anvvtglsev sigivsaglv
      181 salllprhvr avllktgedh yadfvgfvrv almqrvpdde rnrrylrlia araqlenlrs
      241 aavfedpdlr arndimtrla gefldasarf halhqyrdri aragdartar fldalgesaa
      301 rvlppddpar pfelraveqv adalgcelat lpddatlert lpdpvvarda itglfllrqa
      361 lgslhacltd fialrrhpda paapqpdsvr pariattanr mvsaaaglra alavsavslf
      421 wivsgwtgaa gavvsatias alysimpapa aatrqvalgc taawlasltf dfalmprldg
      481 faplaaalal fvalgsylns fpktaafglg fsiyfcfltn imnpgvyapt atldagfssi
      541 lgivaaslay slvapyagdw attrylrglr rlvsddacfg altglmprfd agvrdfmlqi
      601 aarpatgrlg qhelfawtfa sleigrsivd lriasaaaps pppawpaher alcasisrlf
      661 aqpstdalra aeqaavdala algrdaaprl rhcvnfllvs lrcnliplpm qpdar
//
LOCUS       WP_176039174             148 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease, partial [Burkholderia multivorans].
ACCESSION   WP_176039174
VERSION     WP_176039174.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 148)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         <1..>148
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          <1..148
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 pvvvvgvgmy lffaplglan tytgliaaha algvpfvvtt vaatlqgfnq nlvraslslg
       61 anpvttffrv tlpviapgvm sgalfafats fdevvvtlfl agadqttlpr qmftgireni
      121 sptiaalati livfstslll alewlrgr
//
LOCUS       WP_176039203             824 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia
            stabilis].
ACCESSION   WP_176039203
VERSION     WP_176039203.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 824)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 824)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 824)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 824)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..824
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=87634
     Region          516..780
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mrhfllgwll aavvsaahaa apapaaasaa sgtapaltpq qarqaldvle nprqraqvet
       61 tlraiaavgv lsapapvvaa sdaaaasgas aaaapaalts nglasmlvrq garwtaqigg
      121 alneslrsll dvgsvgswwh drlvradera dlahaiwiii avlvpalvve wfskrllrra
      181 laavaarrad tshrtvpdsv tpdddtappp dapepldasn asdaapassp grgharrhtt
      241 llhrmpralv slalravpll vfvgvasltm svigdagapv eaaleslidi yvicrlvtiv
      301 srlffqpyar qlrllhisda wadfaqrsia rivivtgact aaveiaanfg lseaghvall
      361 kavalvghvm isalilqcrq pvaariraag adqptfaaig naladawapv svfivmalwf
      421 vwaldvhngy rvlitlggrs iavmiamrmv sivvfgalar lfqdreedrt lvhahayryy
      481 plvrrivsgt iglvtvvlll qtwgvpvfra fetgtighrl asalmtiaia aivalvvwet
      541 aniaierrlq rwtregnlvr aarlrtllpm lrsllfvmia lvvvltglsq lgvnvgplla
      601 gasifgvalg fgsqklvqdf itgifllmen amqvgdwvtl agvsgtveyl sirtvrlrag
      661 dgslytipfs svttvnntnr glgnaavkvs iaygedidra iatlkeigaa lrddpkyhdg
      721 ilsdfsywgi dqvdgaalal agqmqctdst rwsvqrefnr riaetfrerg irianpqrsv
      781 vayadgsrpd gnheddhgsn arngnaaeta prppspgepd rkpr
//
LOCUS       WP_176039212             368 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia stabilis].
ACCESSION   WP_176039212
VERSION     WP_176039212.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..368
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40354
     Region          4..368
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mksddvivsf rgvrktydge tlvvksldld ihrgefltll gpsgsgkttc lmmlagfefp
       61 tggeirldge llnnvpphkr nigmvfqnya lfphltveqn vaypltvrkl paaeraerva
      121 halkmvqmer fakrypaqls ggqqqriala ralvfepklv lmdeplgald kqlrehmqye
      181 lkalheklgv tfvyvthdqg ealtmsdrva vfdkgivqql dtvdrlyesp cnefvanfig
      241 dsnrlrgtia rvdgefcefr lddgtqlvgr rigdaaegap avacirperm slaahgvngh
      301 ahgaaanrlt gearsliyfg dhvrmrcalp gqdecfvkvp lgtgaidafs pgapvslafa
      361 pehlrvfa
//
LOCUS       WP_176039276             522 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia stabilis].
ACCESSION   WP_176039276
VERSION     WP_176039276.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..522
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52280
     Region          37..448
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,157,
                     160..161,164,288,291..292,295..297,300,328,332,384..385,
                     389,393,409,412..413,416..417,420)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msqsspasra gaaaaphagg rlpaaatlav asatcslivl dtnvvavslp siarsfhasf
       61 adiewvvsay mtafaacllp aggladrfgr krmlgaglal fflaslgcgv aptagwliaa
      121 ravkgggaal lltaalavia nrfpegrera rawaiwgmcm giataiaplv ggaitqwigw
      181 rwvfllnlpv cvllaagarv aidesrdpha krvdaagsll fggalacaia aligapshgw
      241 lsaptlgrla laaalfaafi gaerwqarpm idlalfrqpr fvgavlamfg yaacaqvmmt
      301 flplylqnaf gmsaidaglg mlpfafamia gpslgaalaa rvssggvlag glaligagnl
      361 ataaltasgd yrlvalgmfv tgcgagimng dtqkaimacv ppnrtgmasg istttrfsai
      421 vtavgvlgav laastharld rllsatpglr afadapfmss llagdlaral drvppsaaga
      481 lahaapvafa sgfadaltvs gglalvaagv ayklltqpmr aa
//
LOCUS       WP_176039321             159 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia stabilis].
ACCESSION   WP_176039321
VERSION     WP_176039321.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..159
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17263
     Region          14..134
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mtsgdplfti asidaaqthp lramvllngd lnacelagdh apttlhvgvr drtgivaias
       61 lceeardddr arpawrlrgm avhpavrgmg fgrvlvqicv rhaeergaal vwctaresay
      121 rfyeklgfat dgapvtmpgr tdtafhvmrr yldrhsppa
//
LOCUS       WP_176039360             673 aa            linear   BCT 11-JAN-2025
DEFINITION  BCCT family transporter [Burkholderia stabilis].
ACCESSION   WP_176039360
VERSION     WP_176039360.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..673
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73269
     Region          3..514
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mpesrpspht tfkpqvvlpa lavigallvv callpseaga lfaagqqwvi arfdwfyvla
       61 vtaflvflvl iaasdfgnir lgpddaepef sfvswtamlf aagmgiglmy fgvgepmqhf
      121 lkpptvdpgt paaareamlm tffhwgfhaw aiyglmglvl ayfgfrynlp ltlrsglypv
      181 lreringwig htvdafalvg tvagiattlg ygvmqlsagl htvagwdtgs nvfriglvav
      241 vvilagvsaa tgldkgvrrl selnlllafl llafvvvagp tlflfralgd nigqylsslv
      301 alsfrtyaya ppreegwfgg wtilywawwv swspfvgmfi arisrgrtir qfvigvllvp
      361 tafnlvwmtv fgnsaiwldt hgaagalaqt atnvdallfr ffdflplsql lsivaivlia
      421 vffvtsadsg afvidqiatr gnahspvwqr lfwaallgvt aavllvaggl galqamtlia
      481 alpvaiimla lcyglwrgla adrahysqdv apattfwtgq hwrhrlthil rqtteaearq
      541 fvaetiepal rkvadelras gvdahvqrds ddavrltvpt aehrdfvygv rvtvksaaaf
      601 lvreaaepes arahvygivt ffedgrlgyd veylrgdevi advlrqyery vslaadtrth
      661 llsrapghat eae
//
LOCUS       WP_176039340             226 aa            linear   BCT 11-JAN-2025
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Burkholderia
            stabilis].
ACCESSION   WP_176039340
VERSION     WP_176039340.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Sciara,G., Clarke,O.B., Tomasek,D., Kloss,B., Tabuso,S.,
            Byfield,R., Cohn,R., Banerjee,S., Rajashankar,K.R., Slavkovic,V.,
            Graziano,J.H., Shapiro,L. and Mancia,F.
  TITLE     Structural basis for catalysis in a CDP-alcohol phosphotransferase
  JOURNAL   Nat Commun 5, 4068 (2014)
   PUBMED   24923293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Koga,Y.
  TITLE     From promiscuity to the lipid divide: on the evolution of distinct
            membranes in Archaea and Bacteria
  JOURNAL   J Mol Evol 78 (3-4), 234-242 (2014)
   PUBMED   24573438
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Koga,Y.
  TITLE     Early evolution of membrane lipids: how did the lipid divide occur?
  JOURNAL   J Mol Evol 72 (3), 274-282 (2011)
   PUBMED   21259003
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..226
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23938
     Region          37..212
                     /region_name="PgsA"
                     /note="Phosphatidylglycerophosphate synthase [Lipid
                     transport and metabolism]; COG0558"
                     /db_xref="CDD:440324"
ORIGIN      
        1 mdqrktatrs epplprtwda rlarslvrpl vdtpvtpnhl ttlrlligla gawclahggf
       61 gwsnagafli vlsnfvdhtd gelarisgks skighfydla adalvtialf vsmglgivaq
      121 ggqmaaspvl lgavagaava lifflrmrie siagkagtkq afaggfeted vlyllpivtl
      181 vngvepflla asigaplfaa wvvidwwrvv rrgnlpqnpt eiqask
//
LOCUS       WP_176039415             288 aa            linear   BCT 11-JAN-2025
DEFINITION  MOSC domain-containing protein [Burkholderia stabilis].
ACCESSION   WP_176039415
VERSION     WP_176039415.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..288
                     /product="MOSC domain-containing protein"
                     /EC_number="1.7.-.-"
                     /GO_function="GO:0016661 - oxidoreductase activity, acting
                     on other nitrogenous compounds as donors [Evidence IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=31107
     Region          1..281
                     /region_name="YcbX"
                     /note="N-hydroxylaminopurine reductase subunit YcbX,
                     contains MOSC domain [Nucleotide transport and metabolism,
                     Defense mechanisms]; COG3217"
                     /db_xref="CDD:442450"
ORIGIN      
        1 mpaiaelfvy pikscagial sraqlletgl aydrhwlitd pdgqmitqrt hprlalirta
       61 ldsdalvlna pgmrkirtpl dgdatpatpa maatvwrdtv daidtgaeta awlteflgtp
      121 aklarfgada rrgcnrkwtg eidthtqfad gypllvigqs slddlnarla akgapaipmn
      181 rfrpnivvsd ldayeedfve hldtdgatpv rlrlvklctr cpmptidqat gapdpawphe
      241 ptdtmqayra npnyedaltf ginaivvega gawleigqsl eaeigfgd
//
LOCUS       WP_176039258             513 aa            linear   BCT 11-JAN-2025
DEFINITION  FGGY family carbohydrate kinase [Burkholderia stabilis].
ACCESSION   WP_176039258
VERSION     WP_176039258.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Yeh,J.I., Kettering,R., Saxl,R., Bourand,A., Darbon,E., Joly,N.,
            Briozzo,P. and Deutscher,J.
  TITLE     Structural characterizations of glycerol kinase: unraveling
            phosphorylation-induced long-range activation
  JOURNAL   Biochemistry 48 (2), 346-356 (2009)
   PUBMED   19102629
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426119
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..513
                     /product="FGGY family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=54209
     Region          8..497
                     /region_name="GlpK"
                     /note="Glycerol kinase [Energy production and conversion];
                     COG0554"
                     /db_xref="CDD:440320"
ORIGIN      
        1 mtdsrnaila idegtsgtra aivdasghvs cleylplsve spqpgvveqd anaildktla
       61 vcratlaqah aqhvrivala latqratavl wdtrtgralv pamvwqdtrh aaeldrlaad
      121 wdhvlvpqvg rpagvrspyl wavhqmrasq avadahragc lafgtidtwl lwhlsdarec
      181 vttpthatsa sayllgehry fdpwldalgf prellpalre dadafgrtrr dvlgidvpil
      241 acagdqfaga vglgcvergq amcvhgtgsf vdlltgtarp dagshaqpgh ahdgtlamta
      301 rrhggvshys letfvattgs alrwvceklr wfddpaqisa lagtvqsarg vtfvpaltgl
      361 rvprmepnar allsgisiat tqaevayavl egiahsvasc meanqavara dvselivggg
      421 lagsdtllqi qadvsgvpvr rmregdrasl rgaaflagas gllwdsldaa catlvtdavf
      481 epsidadrrq grraawhari aselahaadf aha
//
LOCUS       WP_176039428             319 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia stabilis].
ACCESSION   WP_176039428
VERSION     WP_176039428.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..319
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34226
     Region          10..227
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mnappapyti dvdrlnkhfg dkhvvkdvsl rvargeifgf lgpngsgktt sirmmcgllt
       61 pdsgsgtclg ydivrdsaqi krrvgymtqr fsywedlsir enldfvarvy gmadrkaava
      121 raldglglas radqltgals ggwkqrlala acmlhepell lldeptagvd paarrdfwee
      181 lhrlaaqgis vlvsthymde aerchklayi aygellaqgt saeivasqrl straitgehl
      241 telsarlram pgvdqtvvfg salhvsgrdr alldatlara vapdggdasw qvapidtgle
      301 dvfiylmgra sgppggass
//
LOCUS       WP_176039440             218 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia stabilis].
ACCESSION   WP_176039440
VERSION     WP_176039440.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..218
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23205
     Region          1..215
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msfrlylsfl aasavliyap gpvnlltmnq alragwrral pcvwggtlav llqlaltalc
       61 lnslvhineh altvlrwaga aylvwlgakq wlnrapaaap aasaqagagt aiaepdadsg
      121 ralfwrgvat sglnpktllf fpsffpqfis pnadwslnlq flllattfal lfaggvasma
      181 lfshrlsral qrparmramn rvtggllvgm gaimvgwn
//
LOCUS       WP_176039441             548 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176039441
VERSION     WP_176039441.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..548
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=55927
     Region          15..270
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
     Region          297..545
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mqnhevsadd appkaqrgiq svevagrlld alarrrkplg lselaaaadl staqahtylv
       61 sltrlalvkr daitgnyepg plslrlglms ierqpayraa lphaarlaet vglsvalsvp
      121 galgptivri ehggyplhvn lhvgsvmsld ttatgrvfra fgdpaqldam aasqagagdt
      181 lagaegaqpt pdadaqqaal dairvrgier gvdrpspgvs amcvpvfdal grlqlaitvi
      241 gstgsidvgw dgpiaaalrd aarqataslg aepadappap atgaayvppa laddakaqrg
      301 inaldstgel llalvsagra lplrdlaaaa gmpaaksfph lvslqkigll srddagcfgg
      361 gplgqalgli amqrvsptrd aeaeivalag atdmsvaaat lgplgptvir leesarpqhv
      421 slqvgtvmsl vntaigrifa agmpddvlad lladepvrla gtaapaddaf rarlaairad
      481 eldfafdapv pgigtvaapv fdhtgsirlv iaiigssrgf prgpdsalaq tllaatrrls
      541 wrfgwigr
//
LOCUS       WP_176039442             446 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia stabilis].
ACCESSION   WP_176039442
VERSION     WP_176039442.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..446
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48164
     Region          31..417
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(44..45,48..49,52,84,134..135,137..139,142,162,
                     165..166,169,267,270..271,274..276,279,307,311,362..363,
                     367,371,387,390..391,394..395,398)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 msaplqadga havaagagst dddalyrrig rrivpflfic yivsildrsn igfaqlqmrq
       61 dlgltdamys lgavlffvgy vlfevpsnal lrrfgarrtf arimflwgav svamitvdsa
      121 khfyvlrfll glfeagffpg vvfyltywyp arrrasvlsi fyagvavagm vggllsgwlm
      181 rgmsgvlglh gwqwmfaieg apaillgvia wfwlcdrpeh arwltdadrr rlaadlaadh
      241 agagtpaphs lrqvlaeprt ylfafiyfsl ttallmllfw mplmirefgi hdvvqislls
      301 vvpnaigavg liaiarrsdr krerrrhfaa cafggavala lltlhlpsiv vmmallsvaa
      361 mlifaahpvf wavpsayfsg agaaggiali ssigvssgmi tpwlvglirt rtgsmdpaml
      421 miaallaaca vamlagvrat pregsa
//
LOCUS       WP_176039462             236 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176039462
VERSION     WP_176039462.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..236
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25581
     Region          8..227
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 maprivppal kaieqetmad kvyqqlreal msgrfapgqa lslrsvaeav gsstmpvraa
       61 ltrlraeral vdgpnralvv ppmtldmlde lrdvrialeg ciaeracarm tdpqiaavrk
      121 tcetmqahve vgrsraylqs nfafhsaiya hgasentlai venlwmrvgp flnmvaldip
      181 hmrrsmdahr aivdalerrd gagvragial diggaahdla etlraeqtpr tvnakp
//
LOCUS       WP_176039457             266 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176039457
VERSION     WP_176039457.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..266
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29187
     Region          78..258
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          202..256
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mdrlfseiam hqalgraidh lgqprfwrfl vlllnemapf dnalataigr dgvplvldey
       61 dtggtdkvsp vplylnglyl ldpflqaahd gladgcyrle evapdlfrqs eyflsyfrda
      121 vgddeiqilv rpnadmllsl slgaaarfdv eplgkltaam pwvlatirqh wrlvgdaara
      181 tpdadlgarv eqalarfgag vltdremsia rmvlrgnssk aiaerlaisp etvkvhrrhl
      241 yaklgissqp elfsrfiqal gedaag
//
LOCUS       WP_176039471             289 aa            linear   BCT 11-JAN-2025
DEFINITION  PilZ domain-containing protein [Burkholderia stabilis].
ACCESSION   WP_176039471
VERSION     WP_176039471.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..289
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30112
     Region          171..276
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mrlptdyval trddlsagvp lgfdlydadg aallpagatl rdaaqhaflf dhfrpvrlrd
       61 dadphghgaa apvtrmglsa gaaigirrrv gttrvlqrcr ligvaasgal fvepqpaavl
      121 efargddvea vaigraavsr fgatvesvqa sgaapfmils ppgfvdrlrt raeprvpvri
      181 aacctggagd aqgigmvrdi slsglsiavd rtiaatgepl rvqlpyaagd rievlaldgt
      241 vraahadpht paltlhhaaf getgaedlir lkallfdrlm asadtdhlr
//
LOCUS       WP_176039484             766 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Burkholderia stabilis].
ACCESSION   WP_176039484
VERSION     WP_176039484.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..766
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=83857
     Region          178..765
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 msyvvavram ceftarrgdl dlrftpapta legiaghgav tskrgaryet eialagtwgt
       61 lavrgradgy dpvtnrleei ktyrgsldam panhrtlhwa qakvyahlmc darglteidv
      121 alvyfdivse retvltqtld aatlaaffae qcacfvgwae retahraard aalralafph
      181 gqfrsgqrel avavyraard erclmaqapt gigktlgtvf pllkacgege ldhvffltak
      241 tpgralalea aatlgagtpa lplrvlelva rdkacehpds achgescpla kgfydrlpaa
      301 rdaaigagll drdtvrstal ahdvcpyyla qelarwsdmv igdynyyydg samlhtlaqq
      361 nqwrvgvlvd eahnlldrar kmysasldpf afeaareaap valrkafdrl arawgtvnra
      421 qaeryaaypd ipgpivsavq nlvaaigehl tdaprangda llrfhfeaiq fgvladafds
      481 asifdatlhg epmprqpald gvatagrrrr vqstlcvrnv ipagflaqry eaaratvlfs
      541 gtlspfhfyr dtlglpgdtg wldvdgpfra eqltvrvash vstrwrdrdr slepiadlia
      601 aqyatrpgny lgflssfdyl grvvalmqar hpdvpvwaqa pgmaeserda flarfaaggr
      661 gvgfavlgga fsegvdlvge rligafiatl glpqvndvne qmrramdarf gngydymyly
      721 pglqkvvqaa grvirtehde gvvhliddry rrrevrdllp rwwrig
//
LOCUS       WP_176039492             151 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia stabilis].
ACCESSION   WP_176039492
VERSION     WP_176039492.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..151
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=15510
     Region          1..150
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mvtlninget rtvdapddmp llwvlrdlvg ltgtkfgcgi aqcgactvhl dgvaarscvl
       61 pvaavadrki ttieavgatp aghkvqqawr eldvvqcgyc qsgqvmaata liasnpnpsd
      121 adidaamagn icrcgtynri raavkqaakg a
//
LOCUS       WP_176039561             155 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Burkholderia stabilis].
ACCESSION   WP_176039561
VERSION     WP_176039561.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..155
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=16058
     Region          30..140
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 mseahvsvdv aqqarfcfev afagttlspv ltdeppplgd grgpnpvrll aaavasclaa
       61 sllfalkkqr vdpqpvtahi dvdmvqneag rvrvgamavr lsigktwadl aaatraldrf
      121 daycvvaesl ragipiavdv cdangatlec aatde
//
LOCUS       WP_176039543             275 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia stabilis].
ACCESSION   WP_176039543
VERSION     WP_176039543.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..275
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28447
     Region          4..261
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 msgltidglt vrygrrdvlv slsagplprg citallgpng sgkstllrtl agltraasga
       61 laldgepfvp gllgarshgv vylpqalpag vrlqvlesvv varratrhgl maagragggq
      121 gddiaalavl arlgiealal rtldelsggq rqlvglaqal ardpqvllld eplsaldlnh
      181 qhqvmaalhd itrerqlvtv vvlhdisaal rgcdramllh rgrivrfgmp edvvtpasla
      241 dvfgvaarie rcsrgqlqvl idglaatgpv aaasr
//
LOCUS       WP_176039550             963 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia stabilis].
ACCESSION   WP_176039550
VERSION     WP_176039550.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 963)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..963
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..963
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=104691
     Region          42..962
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mknhglsrrg flkasvlagv avyvaplgsr afaalfeekl ltpvkwdsvt gipqfridgi
       61 akvtgskvfa rdvraadmph wpqqqshali lrvtqadrty egfdlsllgd elkpdrvvta
      121 ddlardgvaf ptfygddmll pagktpaylg havailiyhd farfrfakna lkfrddviry
      181 gavtgplerd pwgtfryvrv ggktaydddv ysslkdapif psmmrkhlpv wpdgkehgkl
      241 deqgmflagq iaseldhpsa dwlvfdreyn tqsvdtaale pdnancwyda atqsmhlvvp
      301 tqsplevaes aaamvakcrf pvkklfvhpc ytvgygskdh fnvpfyglvc alyadgrpvr
      361 fandryeqfq tslkrhafkm hyriavdrnt gllqsfkgdf eangggrmnf spsvamvgat
      421 aaqsiyyfpk sdlasvaias raidagsarg ygtlqsmaat emavdeiaaq lnidpidfrl
      481 rnalrsgmkn tqgaipagal rvdevlerak qhplwthrva rkaefeaanp gkrygvgfac
      541 vqkdfgtgae asfakvefde hgkvslrhta aeigtgmsts qavavakwlg rpatdvqvav
      601 tewpdlpvet sgdpylmsqa dqdrlsanpr wspnyaspss atnsayyfth streaaravf
      661 ryglwpaams iwtrglgggq aapytiried arwvdgklta dglepltfeq lakqahalgl
      721 ptgavvhvfn rwqwtdaefe vggtverlpv dglslrvgap ktgdkagddn gpvpgtaapa
      781 gatamrgtlp ptangyrvld rkrvfippts rnnaavtyyt avgtlvelav heatgkveli
      841 thhsimecgn qispqlvsgq lqgglamgig halheylply edgpgngtwn fnryqlpras
      901 dvavwsqtgd ilpplsetdp pkgvaevvmi pvvgaivngi ahaighrftd lpvtpqkiqe
      961 vla
//
LOCUS       WP_176039584             331 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia stabilis].
ACCESSION   WP_176039584
VERSION     WP_176039584.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..331
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35017
     Region          130..304
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mkdkpdgvav psrvvpfpas isdeardalr rlvgddgvpl nalhvmpppd dhdawmrvka
       61 aadahyaaai eqlggylrss vetiraghad ihvatpadai sgecavidlh ggalvlggga
      121 acragaqmqa drlgircygv dyrlppehpy paalddciaa yshvleryap dnivisgrsa
      181 ggnlaaamvl rardeglplp aalvllspea dltesgdsfe tnrlvdvvlp gslmpnnlly
      241 angadlahpy lsplfgdfaa gfpptfiqsg trdlflsnav rlhralrraq vptelhvfeg
      301 mphggfmgap edrelgreia gfvrahlral n
//
LOCUS       WP_176039586             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia stabilis].
ACCESSION   WP_176039586
VERSION     WP_176039586.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21467
     Region          2..205
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mlfiksvvmg lsiavpvgpi gmlciqrsls rgfqagfatg igaacadaiy gllgalgiag
       61 ivtafpmltv glkigggafl vwlawtiarq apaasamqre lprttvlrdf lttfgltlsn
      121 pmtilsfvgi faalgplsga regamwpsvs lmvagvfigs atwwlclssa saalrtkmsf
      181 afmhglsrvs avviaafgai qlaagvrgvi
//
LOCUS       WP_176039690             304 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176039690
VERSION     WP_176039690.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33371
     Region          10..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..295
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(105,109,148,162,165,229,246,274)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(106..107,111..112,114..115,118,122,124..130,192,
                     223..227,234..235,238)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 msrrdpmagl hvfmtvatag nftraaaalg ltpaavslai gqlegelnvk lfnrstrgvs
       61 lteagqrywr qtepayrqvm qardelkdar sepsgllrvt alplarllvi apvlavfrer
      121 ypkvrleiry enelvdiakd gfdagirlad rlqpgmigvr iapalscalv aspgylarhg
      181 apasiaaleq hacirfrfse sgrlhkwllh dgrrdvdldp egvfvtndad avidaalagv
      241 giafafmrer ierdlrdgtl vevlpgvcrt lppmwlyyvn rkhvpaklra fidvlrerag
      301 adva
//
LOCUS       WP_176039708             235 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia stabilis].
ACCESSION   WP_176039708
VERSION     WP_176039708.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..235
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24624
     Region          51..149
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mslpasaakf dparaheyak qsrialagyd achelaacml asaigasdar ilvagaggtg
       61 qeicvsaale pgwrftavdp sapmlalars nveaagvgar ttfvedgvdt lpdapafdga
      121 tligvlhhvp gddakaallr aiarrlkpga plviagnhrr yadhprllda wqqrwrmkga
      181 tpdavraqla kilqgadppa seeavfdlln dagfdaplrf faslfwgawi avrra
//
LOCUS       WP_176039711             128 aa            linear   BCT 11-JAN-2025
DEFINITION  GtrA family protein [Burkholderia stabilis].
ACCESSION   WP_176039711
VERSION     WP_176039711.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Mayer,M.J., D'Amato,A., Colquhoun,I.J., Le Gall,G. and Narbad,A.
  TITLE     Identification of Genes Required for Glucan Exopolysaccharide
            Production in Lactobacillus johnsonii Suggests a Novel Biosynthesis
            Mechanism
  JOURNAL   Appl Environ Microbiol 86 (8), e02808-19 (2020)
   PUBMED   32060027
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Kolly,G.S., Mukherjee,R., Kilacskova,E., Abriata,L.A., Raccaud,M.,
            Blasko,J., Sala,C., Dal Peraro,M., Mikusova,K. and Cole,S.T.
  TITLE     GtrA Protein Rv3789 Is Required for Arabinosylation of
            Arabinogalactan in Mycobacterium tuberculosis
  JOURNAL   J Bacteriol 197 (23), 3686-3697 (2015)
   PUBMED   26369580
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..128
                     /product="GtrA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=13715
     Region          11..128
                     /region_name="GtrA"
                     /note="Putative flippase GtrA (transmembrane translocase
                     of bactoprenol-linked glucose) [Lipid transport and
                     metabolism]; COG2246"
                     /db_xref="CDD:441847"
ORIGIN      
        1 mirtlyaaer arlirfgvsg lcstglhali aaamfalfda tpvianataf acstafsyla
       61 ntlwsfssrt twgnfarfla vamaglvvtm llahgtetlg larawsvvav vlcvppvtfv
      121 lhrlwtyr
//
LOCUS       WP_176039750             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176039750
VERSION     WP_176039750.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32204
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdrfesmsvf veivstgslt taaerlglsp smvgkhlnal earlgvkllh rttrrhhlte
       61 agalylercr dildrvetad daasalggdp agqlriaapi sfgvtqlapa vaaflaqypr
      121 vdielvltda avdpvgdgid lafrigplad sslvarplqs yyrmvvcaap gylarrgipa
      181 appdllnhdc lghtrwgprh pwrfdgpdgp ievpvayrlr vdsgpalrea alagggvilq
      241 plglvkadld agrlhqllae yeshgrdfyl lyardtgapa klrafiefal nhfavaepgr
//
LOCUS       WP_176039765             286 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia stabilis].
ACCESSION   WP_176039765
VERSION     WP_176039765.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..286
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=31002
     Region          29..269
                     /region_name="YktD"
                     /note="O-Methyltransferase involved in polyketide
                     biosynthesis [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3315"
                     /db_xref="CDD:442544"
ORIGIN      
        1 mtdtredapd staarvalwr alhveldapp hvladevglq llapapgwqq rgdmdpqftr
       61 pfrasivara rfiedlvvgq aargvsqyvi lgagldsfvq rrpdmasrvt vfevdppapq
      121 awkrrrlvel gfgvpdwlrf vpvdfeakqs wrdalvgtgf dagkpavvvs tgvsmyltre
      181 anaaalreva slapgstlam tfllplehad pdvrpglema akgarasgtp fisffmpaqi
      241 qalameagft ktehvsaael trryfadrtd glrppnnaee llvati
//
LOCUS       WP_176039780             285 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176039780
VERSION     WP_176039780.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..285
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31483
     Region          17..272
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mneplkqqdt enpkseasyv vpglerglri laefsprepv lgapelskrl giprttvfrl
       61 lqtleslgfl eradkdrnyk lgiavlrlgf eylssleltd lglpvieslr datgftthiv
      121 irdgrdvvfv akaqsqspvf ssirvnvgtr lpahatthgh vlmgdlslke lhalypertl
      181 nrmtsatpet vdalyevire dtlrgygisn ssfergisvv tapvrnetqr ivacitvtvp
      241 rpeidaalva dglidkvqra aaelsrrlny rsddehtflk alglr
//
LOCUS       WP_176039785             296 aa            linear   BCT 11-JAN-2025
DEFINITION  peptidylprolyl isomerase [Burkholderia stabilis].
ACCESSION   WP_176039785
VERSION     WP_176039785.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..296
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=30999
     Region          135..283
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mmtkmkmlam vagslvlaap fvahaqddvi anaaqasvtq adiagllkav spegrerlaa
       61 dpatldqivr stlaqkavla eakskgwdkq aqvqaaveqa qrdivvrsyl tsvnappady
      121 psdaelqsay danraaftap ralhvaqiyi avpqnadaat ldkarkqatd lanrarsgdf
      181 aalakansqd kasaanggdl gfvpdtlmvp avrqaadalk pgqvsapirt pagfhvvkli
      241 dvraaaprpl advkeqlrtm lraqrtqqna qaylaklaan apinedalkk alasar
//
LOCUS       WP_176039803             381 aa            linear   BCT 11-JAN-2025
DEFINITION  metallophosphoesterase [Burkholderia stabilis].
ACCESSION   WP_176039803
VERSION     WP_176039803.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..381
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=40835
     Region          113..381
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mrsffvrfia igvlfhlyvg iriipdafas pvartvaalv lasfvvlipv gmfsrrfdeg
       61 waatlvgwvg slvmgffssl laltllrefv llgvivwrqf vhagawsgas adtavgvlaa
      121 avlvtaigfv garrtaavkr vsipvaglpa gldgltivql sdihvgptik rpyierivra
      181 vnaldadvvv vtgdvvdgsv krlrehtapl grmksrygsf lvtgnheyya gahawidefr
      241 rigltvllne hvlierggar avlagvtdft aggfdpahrs dperalagap hdvgtkilla
      301 hqprsaeaan ragftvqlsg hthggqflpw ppfvrlqqpv igglsrfgdl wlytsrgtgy
      361 wgppnrfgvp seitlirltr g
//
LOCUS       WP_176039811             203 aa            linear   BCT 11-JAN-2025
DEFINITION  cysteine hydrolase family protein [Burkholderia stabilis].
ACCESSION   WP_176039811
VERSION     WP_176039811.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..203
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21089
     Region          24..192
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mqhptirtla gataptsiaa artallvidf qneyfsgrlp ipegpralgn aqrviafadr
       61 agipvfhvqh vdtadspifa dgsdgfrfha dlqpaphhav vkktsvsvfp ttdldarlka
      121 agidtlivtg lmthacvaga ardavplgya vivvddacat rdldvadggt vphrdlhrat
      181 laalsdtfgd vlttaqvlal dva
//
LOCUS       WP_176039814             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176039814
VERSION     WP_176039814.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32811
     Region          11..69
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          100..295
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(115..116,118..119,122,126,128..134,226..231,
                     237..238,240..241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrnrineeit frklevllaf meagslakaa ealgvstvsv hralhtleeg mhcalfrheg
       61 rnliptdaal vlaevagevl ktmtdgirst reaagygagq lkigslyslt irtvpevvia
      121 lkerrpelqa elvlgsnadl ldklrqgaid atlmalpdpd aeiesialfe demffatpvd
      181 spyaqrdaid lgacrdvpfv slgegfathh gfteafravg vtpnvvmrvg difslinlvs
      241 ggvgcsllpg rvrdlfahki alvplagpti rqtiglsflh rrerdpnlla latvcrltvk
      301 gpnar
//
LOCUS       WP_176039848             160 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system protein [Burkholderia stabilis].
ACCESSION   WP_176039848
VERSION     WP_176039848.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Korotkov,K.V. and Sandkvist,M.
  TITLE     Architecture, Function, and Substrates of the Type II Secretion
            System
  JOURNAL   EcoSal Plus 8 (2) (2019)
   PUBMED   30767847
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Wandersman,C.
  TITLE     Secretion across the bacterial outer membrane
  JOURNAL   Trends Genet 8 (9), 317-322 (1992)
   PUBMED   1365398
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..160
                     /product="type II secretion system protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0015627 - type II protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0015628 - protein secretion by the type II
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=17482
     Region          1..90
                     /region_name="PulG"
                     /note="Type II secretory pathway, pseudopilin PulG [Cell
                     motility, Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG2165"
                     /db_xref="CDD:441768"
ORIGIN      
        1 msarrrargf tlielmvalt llallatval pltdlvkrra deaelrralv virsaldtyk
       61 aaaddgrier sadasgyppd lrtlvegvdd ktspggarly flrkipadpm cecdgkaadd
      121 mwetrsyasd pasfssgddv fdirstnrke glngvpynqw
//
LOCUS       WP_176039899             736 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia stabilis].
ACCESSION   WP_176039899
VERSION     WP_176039899.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..736
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=77386
     Region          57..>192
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          200..728
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mtieldnpgs vqpsrrtflk aagaaaavsl tigfewaglg rralaatapa adfapnaflr
       61 itpdgavtvi akhvelgqga ytgiativae eldadwssvr vesapadakr yanlafgtmq
      121 gtggssaman swqqlreagg karamlvsaa aarwkvpage lttangvvth aksgktaayg
      181 tlvadasklp vpdkvalkqp adfklighri prvdasaksn gtahftldtt fpgmriallq
      241 rpprfgatvk sfdataakav pgvvavvqvp rgvavvatgf waakqgrdal kvewdetnae
      301 krssdeimre yrqladkpgt sarkdgdada aiagaarkla atyefpylah apmepldavv
      361 kltpdsceiw agdqfqtvdq gnaahvaglk peqvqihtly aggsfgrran awsdyvveav
      421 siakalgadg kpvklqwtre ddiqgglyrp myfhkldagl tadgrlvawr hrivgqsila
      481 gtpfeafmvk ngvdatsveg aanlpyavpn vsvelatakt gvpvlwwrvv gsshtayave
      541 afideaahaa gkdpyafrrd llekeprmra vlelaaqkag wdpakplpkg rgrgiavaea
      601 fksyvaqvae vsvdadgkvk vervvcavdc giainpdiva aqmeggigfg lgavmhsait
      661 lkdghveqrn fdsyqvlrma empkvevhiv psaeaptgvg epgvapvgpa vanaifaatg
      721 krhyvlpfds adsaka
//
LOCUS       WP_176039954             311 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia stabilis].
ACCESSION   WP_176039954
VERSION     WP_176039954.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..311
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33423
     Region          80..286
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mpidtdiaal lerlareepp sslaglrhat dmtlrtwhgp lesidrtetl tiptrdgqqi
       61 svraywpsgt gdralpqpai lyahgggwcl gtlelydnpc ralanatqcv vlsvdyrlap
      121 ehkfpvpled fcdalawvcr qaaslgldpa riavggdsag anlaaaaclv ardlggppia
      181 hqlllyppld asmdtdsyrt ygqscyltke vmqycfamyl pdpaegrssy vsplraashe
      241 glppvtllac efdplrdeaq ayaarlrhag vpvdltvlpg mihacihmgg vapaarhlfe
      301 vagaairrlf q
//
LOCUS       WP_176039971             512 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia stabilis].
ACCESSION   WP_176039971
VERSION     WP_176039971.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..512
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52289
     Region          16..438
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,142,
                     145..146,149,273,276..277,280..282,285,313,317,371..372,
                     376,380,396,399..400,403..404,407)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtlsdsrrna valaavclts lmfgleissv pvilptlehv lhgdfngmqw imnaytiact
       61 tvlmaagtla drfgrkrvyv igtvlfgats llcglapnvp vlvagrllqg asggamlicq
      121 iavlshqfre grergrafgi wgivfgiglg fgpivggaiv alaswpwvfl vhaplaaval
      181 vliggavqes rdphagtldv agivtlslav lglafyitqs aelgltsaag lgvlgatvla
      241 ligffvaera sarpmfdfsv friraftgai fgsmgmnfsf wpfmiylpiw fqvalgydsv
      301 taglallayt lptlvappvg erlalrygpg vvipgglfti aagfalmrlg saaehaswlt
      361 mlpgcviagi glgltntpvt ntttgavpsa ragmasgidm sarmislaln iaamgfvlva
      421 givaslkagv agaigdaalr rlaqeiasgr tdglqriapa laqadpsgaa lhaalvhgfg
      481 wvmvygaagv avlatasava faparrgaav ce
//
LOCUS       WP_176039973             379 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Burkholderia
            stabilis].
ACCESSION   WP_176039973
VERSION     WP_176039973.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..379
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41775
     Region          26..362
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 mstpvtthda faehapevlf rvvnrvalit lnrpaalnal syamigelaa lfercrtddq
       61 ivavvlrgag ekgfcaggdv ralyrmvaqr etwlpffvde yrldhaihtf pkpvvalmdg
      121 vtmgggmgla qgaalrvate rskiampetr iglvpdvgat hflsrmpvel elyvgltgam
      181 lsgadalsak ladlcvpsaw ldtfetries vkwdgdvlpa lrkvfeppcn vvphaaldsq
      241 mpwivrhfdk rstverivat ltqdlareel trehrqwlqa tldalsghsp tmlcvtreal
      301 lrgrqmtlae sfrmelgiva raieegdfce gvrahlvdkd rkprwapasl velraervrh
      361 fltspwklfa hpladlgaa
//
LOCUS       WP_176039989             228 aa            linear   BCT 11-JAN-2025
DEFINITION  energy transducer TonB [Burkholderia stabilis].
ACCESSION   WP_176039989
VERSION     WP_176039989.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10507740
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..228
                     /product="energy transducer TonB"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0031992 - energy transducer activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24196
     Region          157..227
                     /region_name="TonB_C"
                     /note="Gram-negative bacterial TonB protein C-terminal;
                     pfam03544"
                     /db_xref="CDD:427361"
ORIGIN      
        1 mlarplpehr pagrprqfrq tshrpvrrlg giaavlalha vliyallngl anrvveiiqh
       61 pvsvriiepv kppppppapp kpivkaappk sappppvfvp ppevpvqapp qatlthtatp
      121 vvsapavpap papttlkaps hevgvvcpns dqvraslryp realennitg nvlvefvvda
      181 dgrvsdehva rsadpildra alaavrrfsc lsqgqsvrvq vpfsfnln
//
LOCUS       WP_176040008             433 aa            linear   BCT 11-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Burkholderia stabilis].
ACCESSION   WP_176040008
VERSION     WP_176040008.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..433
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=46307
     Region          5..431
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 mslnddatfw rnarqhlvry ggtfepmiie rahgsfvyda dgraildfts gqmsavlghs
       61 hpeivsvise yagkldhlfs gmlsrpvvdl atrladitpd gldralllst gaesneaair
      121 maklvtgkye ivgfaqswhg mtgaaasaty sagrkgvgpa avgsfaipap ftyrprfern
      181 gaydtlaeld yafdlidrqs sgnlaafiae pilssggiie lpegymaalk rkceergmll
      241 ildeaqtgvg rtgtmfacqr dgvtpdiltl sktlgaglpl aaivtsaaie erahelgylf
      301 ytthvsdplp aavglrvldv vqrdglvara nvmgdrlrrg lldlmekfdc igdvrgrgll
      361 lgveivkdrr tkepadglga kitrecmnlg lsmnivqlpg mggvfriapp ltvseaeidl
      421 glslleqaia ral
//
LOCUS       WP_176040009             325 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176040009
VERSION     WP_176040009.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 325)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 325)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..325
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35238
     Region          23..198
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          232..314
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 magsvfatie npiffcerpa mtdpltevvt llqpgarhsk tvqgaspwsv nrtvagepfy
       61 caildggcri aidghapiel lpgdfmlipa aygvamssfe plppgvetgp pvvldtgefr
      121 vgepgnpvdt rmmvgncsfg spdaallvsl lpqfvhvrge prlttlvqlv rdesraqrpa
      181 reivlarlle vlliealrft tetnaspglv rgladirlaa airrmherpa hpwtivelak
      241 eaalsrstff erfsravgva pmeylltwrm alakdllrrn egriaeiagr igyssastfs
      301 vaftrhvgrp paqyardera avsea
//
LOCUS       WP_176040038             520 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Burkholderia
            stabilis].
ACCESSION   WP_176040038
VERSION     WP_176040038.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..520
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54311
     Region          24..520
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mpspirsses ldvdallaal pgriadvpar waaqspahpa liedarrlsy gdlaqavdaa
       61 aaslaslgvq ggdrvmivae ncvaqiallf aaaridawal vsnarlsage ldaiaaharp
      121 kliafttdas pdarahaary datpagalpv digawsyrvd asapgepvaa dgaaqcaali
      181 yttgttgapk gvmlshrnll fiaatsstlr rvspddvvyt vlpvshvygl asvclgslya
      241 gatlrlaprf apeavrvala degvtifqgv pamhaklleh lhthghawra prlrfaysgg
      301 spldanlkar vertygvplh ngygmtessp titqtpldap radssvgvpi pgvdvrivap
      361 dgtdvpqgev geirvrgpnv mlgyyrnaea traavspdgw lstgdlarqe adgavtiagr
      421 skeliirsgf nvypveveqv lnahpdvvqa avigravegn eevlafvelv pgavadetal
      481 nawcaerlap ykrpahirvl dalpaastgk vlkhklrela
//
LOCUS       WP_176040045             314 aa            linear   BCT 11-JAN-2025
DEFINITION  ketopantoate reductase family protein [Burkholderia stabilis].
ACCESSION   WP_176040045
VERSION     WP_176040045.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..314
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32646
     Region          1..312
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkiailgaga mgslfgglla esgeavtlid vndahldair rdglridddr gerriralqa
       61 vrpeaaqada vaspdasfdl livftkslht rsaldgvral lgphtfaltl qnglgnvetl
      121 nafvpleril vgvttwpada agpahvrshg agtirmmtad gaarpfaaav adalsragla
      181 ctldadvwaa iwekvafnaa lntlcaatgc tvdqlgnhhd gprlalaiaa etaavarakg
      241 iavdgeriar nvghairehr ghrpsmlqdv lagrrteida isgkvvaaar etgvavphte
      301 tllalvrlid arid
//
LOCUS       WP_176040068             895 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            stabilis].
ACCESSION   WP_176040068
VERSION     WP_176040068.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 895)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 895)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..895
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..895
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=97621
     Region          15..827
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnsqelrsal lagpvqherl vkldtplgpd vllpqrvkgr srlgrhfefi vdtvsvsdnl
       61 elkkliaqpv tlwilqadqt yaphhgyvha arrlgsdsgv thyqivfasf lhflrfrrdq
      121 riwqdrsadd iiadvlnqhp qakgrftfkl yqplpprsfc mqyeddwnfv hrlmesegly
      181 gfweqdkdgk shrlvivdri dalpalsprt vrfhhagtgd eadtltqfsg trtlrsvert
      241 trtfdykqpp tasnpkatht ptianqgdlp qqlevyeytg aytypeqsrg dhlskiwmee
      301 qeshakrfhg vggvrrmdag rtfaladhpe hdkddagqre fvvietawii vnnlpvageq
      361 talphslqae vgrivqagga dasqvrhadg segffrisve aqrttvpfrs plehakppmh
      421 lqsaivvapq geevhtdeln rvkvrfhwdr lndgdekasc wlravasdsg ngygavhphr
      481 sgeevlvdfv ggdcdrpiiv gklyngatsp qwhtngilsg yrskeyagag ynqlvlddat
      541 aqnrvhlyss qtnahlhlgy lidhtgnnrg sylgsgfdlr sdaygavran rglyvttypk
      601 ppasqpldvq etqqqlvrae glmeamsdvs aqhqgesldp ghtalkqftd atqnsvsgsa
      661 sggrtagggt gsanafkqpv mlfgspagig mstqqsaqla adqhinlvsg qsthvaagks
      721 liasvldris lfaqnagikl fagkgkvevq ahadnielta qkalklmavt esiegaaake
      781 illtsggayi riadgnievh apgkidikga qhafsgpthl sqamptlpns ggnydqafia
      841 hwagtdipva ntryqmfsng kllsegvtna agetgltqsh vphdvvvkfl gksng
//
LOCUS       WP_176040076             323 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176040076
VERSION     WP_176040076.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..323
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35092
     Region          6..321
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpasprsilv lafpraqlld vsgplqvfas vnelarergq pepyaprvva adagpietss
       61 glvvmadslr saarrpdtvi vaggkgvhaa sqdarlvrwv rqqaararrv asvctgafll
      121 aeaglldgrr avthwarcde faarypnvrv etdpifireg alwtsagvta gidlalalve
      181 edlgratald varelvvflk rpggqaqfsa mlsmqhtddr fgelhawmae hltadlsvpa
      241 laervrmser sfvrhyragt grtparaveq irveaaqrll getawpvkri aarcgfgsee
      301 tlrrsfvrvl gvspqgyrer fvp
//
LOCUS       WP_176040085             284 aa            linear   BCT 11-JAN-2025
DEFINITION  ferritin-like domain-containing protein [Burkholderia stabilis].
ACCESSION   WP_176040085
VERSION     WP_176040085.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10090058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..284
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32766
     Region          44..173
                     /region_name="Ferritin_like"
                     /note="Ferritin-like superfamily of diiron-containing
                     four-helix-bundle proteins; cd00657"
                     /db_xref="CDD:153097"
     Site            order(52,84,87,139,169,172)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 mvrpdqlntn asktppvmpw riedidlnri drqraaaned lllllcassf iesgsdlyts
       61 nlseffnddp evsawlnnaw eheelqhgra lkayiahvwp efdwdtafan ffaeysktcs
      121 veafektral emvarcvvet gtatlyrain ecsdepvlke itdnirsdev rhykhffkff
      181 kkynqlegng rlavlgalmr rvleikneds eialrhvfai rypdrvgdsq ynreraarin
      241 slvrrnlsad mcvkmllkpl dlpakiqpgv hypltkitrh vflr
//
LOCUS       WP_176040099             786 aa            linear   BCT 11-JAN-2025
DEFINITION  LPS-assembly protein LptD [Burkholderia stabilis].
ACCESSION   WP_176040099
VERSION     WP_176040099.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..786
                     /product="LPS-assembly protein LptD"
                     /GO_process="GO:0015920 - lipopolysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86973
     Region          76..757
                     /region_name="LptD"
                     /note="LPS assembly outer membrane protein LptD (organic
                     solvent tolerance protein OstA) [Cell
                     wall/membrane/envelope biogenesis]; COG1452"
                     /db_xref="CDD:441061"
ORIGIN      
        1 mppkplfpnv fpgdgvprkr rlalallavp glvpavsyaq lsgaaaqpqp ldspwdlrla
       61 pqledhplkd gakpaafvia dhtsgtaeqd laakgsaelr rgdaivkada ihydqdtdma
      121 daygqvrvfn ggtsfvgpea hlkieanqgf mtapkyhfnm tggsgsaerv dmldnersvf
      181 vngtytacqc stnpawyikg srfdfdtgad egtarngvlf fqgvpifasp wmtfplsger
      241 rsgllpptfs vnssngfels lpyyfniapn rdltltprii srrgvmteat frylspsysg
      301 tftanylpdd rlahrnryai ywqhqqnfgg gfggyvyynk vsdntypedl gstnqfingt
      361 qtlyqqeagv tynngpwsvl aryqhwqtlp psiapysrep qlnvkytkyn vggfdfgaea
      421 dysrfritta dategdrivf npyiaygvyg pgyfvvpkvq yhfasydlny lssttpnspk
      481 rftesiptvs fdtglifdrs vrlfgqdfiq tleprlyyvy tpyrdqsnap lfdtaesdfg
      541 laeiyqpntf vgndriadan ritagltsrf idprtgdera rfviaqqyyf adqrvtlnsg
      601 qsavlarhsd livgaalklg sgfmsetafq ynqnnnqlvk ssvgfgyspg errvinvgyr
      661 ytrsnttldn qpinqflisa qwpltrrlya igrfnydlag drvvdgllgl qydadcwalg
      721 vgvqraangv nssgqqnsst rfmmqltlkg lstvdnglvs afragvpgyt plppppppms
      781 rfsnye
//
LOCUS       WP_176040112             265 aa            linear   BCT 11-JAN-2025
DEFINITION  (Fe-S)-binding protein [Burkholderia stabilis].
ACCESSION   WP_176040112
VERSION     WP_176040112.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..265
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28306
     Region          <8..255
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mnerqypaap ahaylfatcl vdlfvpeagl davrllereg ltvhyprgqs ccgqpayssg
       61 npdearrvaa aqldlfaepw pvivpsgsca gmirhhwpal faddpvhgpk araiaertye
      121 laeflvhvld vrldtavasa ghdervvlht scaarremgt rvhgvalvda lpgvtriehe
      181 reseccgfgg tfslkhpdis gamvrdkvas acatgcdrlv sadcgcllni ghaaakagep
      241 lpvehlasfl wrrtagaasl rgder
//
LOCUS       WP_176040125             254 aa            linear   BCT 11-JAN-2025
DEFINITION  ParA family protein [Burkholderia stabilis].
ACCESSION   WP_176040125
VERSION     WP_176040125.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..254
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28074
     Region          1..253
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mrrvvfnqkg gvgkstivcn laaisasegl rtlvidldaq anstryllgd aapdaqpgva
       61 gffetaltfn frpvevasfi hptpfegldv mpahpdldtl hgklesryki yklrdalnel
      121 dtydavyidt ppalnfytrs aliavercli pfdcddfsrr alytllenvk eiqqdhnaal
      181 evegivinqf qpraslpqrl vdelvdeglp vlasrlsasv kireshqqst pvihlepghk
      241 laqefralhr elag
//
LOCUS       WP_176040141             205 aa            linear   BCT 11-JAN-2025
DEFINITION  SCO family protein [Burkholderia stabilis].
ACCESSION   WP_176040141
VERSION     WP_176040141.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..205
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22421
     Region          51..205
                     /region_name="Sco1"
                     /note="Cytochrome oxidase Cu insertion factor,
                     SCO1/SenC/PrrC family [Posttranslational modification,
                     protein turnover, chaperones]; COG1999"
                     /db_xref="CDD:441602"
ORIGIN      
        1 mlhsrfgrra rqgwmlacaf taalllagcd napkfqnldi tgntqfgsdf slpdttgkvr
       61 tladfkgkav vmffgythcp dvcpttmael sealkqlgpd aakrvqvlfv tvdperdtpa
      121 llgqyvpafd psfiglrpad eaalkkvtkd frvyyakvpg ktpgsytmdh taasyvfdrd
      181 gklrlfvrdg qgpgpwvhdl kllvd
//
LOCUS       WP_176040218             278 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176040218
VERSION     WP_176040218.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10677008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..278
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30675
     Region          111..275
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          217..274
                     /region_name="HTH_LUXR"
                     /note="helix_turn_helix, Lux Regulon; smart00421"
                     /db_xref="CDD:197715"
ORIGIN      
        1 mrilqpdpaa rghyligvrp dtlgstlrav gtpgfvgavt efvndsidad avhlerwrad
       61 tgstsghvve wlgsgslrfa adtlrvmdly yqdychadpl vaplrgqagt llvqrhvdgi
      121 aqgefrrrif depgiaqecl lvhgnahvqy alglartvgr aafttdelfh frqmvdllfp
      181 mfelhartca arrvtsgsga anaasragfd arlerqdvql srreheicrl mlcgrsvpea
      241 aqqldvklst aesyvkrafa klgvrtrrel fdwvlvdc
//
LOCUS       WP_176040229             430 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia stabilis].
ACCESSION   WP_176040229
VERSION     WP_176040229.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..430
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46348
     Region          38..419
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 msfdfctprm rracrrapvl waallaagav haqqspftld aalqsatdhs asmqaaqasv
       61 rasseaavka gqlpdpmlka gidnlpvngg qrftvgqdfm tmrrigieqe wvsgdkrrlr
      121 saladeqvgr eragylvqla dvrrqtataw ldaiyakqal alqqalldhm hheldatqas
      181 yrgakasagd vvqaramlaq tqdqvlkaqq syrtalialg rwtaapvadv tgtppapesf
      241 vsslppdelr lsqpalvaas ndiavaeagt avanserspn wtweiayqqr ggaysnmvsv
      301 gvtiplpinr knrqnrdvae kaelatkarl myedtlrqvq adirtqsetl asgrarianl
      361 sasllpaadq rvqlanaayr agtgsladtf aarraqleaq lqvldlrrdv sqtwaqleyq
      421 vvpatlaaaq
//
LOCUS       WP_176040232             336 aa            linear   BCT 11-JAN-2025
DEFINITION  sodium:calcium antiporter [Burkholderia stabilis].
ACCESSION   WP_176040232
VERSION     WP_176040232.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schnetkamp,P.P.
  TITLE     The SLC24 gene family of Na/Ca(2)-K exchangers: from sight and
            smell to memory consolidation and skin pigmentation
  JOURNAL   Mol Aspects Med 34 (2-3), 455-464 (2013)
   PUBMED   23506883
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Besserer,G.M., Nicoll,D.A., Abramson,J. and Philipson,K.D.
  TITLE     Characterization and purification of a Na+/Ca2+ exchanger from an
            archaebacterium
  JOURNAL   J Biol Chem 287 (11), 8652-8659 (2012)
   PUBMED   22287543
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..336
                     /product="sodium:calcium antiporter"
                     /GO_function="GO:0008273 - calcium, potassium:sodium
                     antiporter activity [Evidence IEA]"
                     /GO_process="GO:0006874 - intracellular calcium ion
                     homeostasis [Evidence IEA]"
                     /calculated_mol_wt=35586
     Region          19..332
                     /region_name="ECM27"
                     /note="Ca2+/Na+ antiporter [Inorganic ion transport and
                     metabolism]; COG0530"
                     /db_xref="CDD:440296"
ORIGIN      
        1 mtfmflelaf mlvvilvaae vftnalehlg erlkisegvt gslfaavgta lpetmvplla
       61 laggtanqqv neeigvgail gaplmlatlt tflmtlavir srglrgtiap ertgfvrdmn
      121 yflaafslat vamfvphhnw avrallaaml vgiyvmyvvm tfrasnqlvd aghgteapha
      181 mllsrvglpt nlatialqll iglallvgga kgfihgvegv shvlgvsall lsliivpiat
      241 elpekvnsvl wirrkkdtla fgnitgamvf qgtllpaigi mltpweprpe vltgviitla
      301 aaawlrinar trglaiwall angagyagyl fltlvr
//
LOCUS       WP_176040237             431 aa            linear   BCT 11-JAN-2025
DEFINITION  multicopper oxidase family protein [Burkholderia stabilis].
ACCESSION   WP_176040237
VERSION     WP_176040237.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..431
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=47253
     Region          64..327
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mvsrrqflsg sgaallgaam vskagaaslp eaptmaktgt qpplvppngr pympvatlng
       61 wtlpwrmkng wkefhltaep vvremapgmn anlwgyngqs pgptieaveg dkvrifvtnr
      121 lpehttihwh glrlpngmdg vggltqphip pgktfvyefq leahgtfmyh phademvqma
      181 mgmmgmfivh pkdrgtmpvd rdfvfllaay didpgsytpr vnemtdfnmw tfnsrvfpgi
      241 dplpvragdr vrirfgnltm tnhpihlhgy sfevagtdgg wippaarwpe vtadvavgqm
      301 raieftadrp gdwafhchks hhtmnamghq vpnligvpqk dlaqrigklv pdymamgstg
      361 gamggmempl pdntlpmmtg tgpfgplemg gmftvlkvrq glgrndyrdp gwfrhpkgtv
      421 ayeytgelpd g
//
LOCUS       WP_176040273              63 aa            linear   BCT 11-JAN-2025
DEFINITION  CsbD family protein [Burkholderia stabilis].
ACCESSION   WP_176040273
VERSION     WP_176040273.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007103
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..63
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..63
                     /product="CsbD family protein"
                     /calculated_mol_wt=6682
     Region          1..56
                     /region_name="yjbJ"
                     /note="Uncharacterized conserved protein YjbJ, UPF0337
                     family [Function unknown]; COG3237"
                     /db_xref="CDD:442469"
ORIGIN      
        1 mdrnriegkl kqvkgsvkea lgkvtgdrkt eaegvaeqqa gkiqeqagea adavrkhtgt
       61 drh
//
LOCUS       WP_176040285             187 aa            linear   BCT 11-JAN-2025
DEFINITION  flavodoxin family protein [Burkholderia stabilis].
ACCESSION   WP_176040285
VERSION     WP_176040285.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..187
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=19786
     Region          3..184
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mvnvavvfhs gyghtsviae avargaekie gavvklipvd aidqhwsyla ndadamifgs
       61 ptyvgsvsaq fktfmdastk qwgnwrdkla agftvsasqs gdklatlqql alfaaqhhmm
      121 wislglmpgn nsstgsvddi nrlgsflgsm aqanadqggd tilesdrlta ellgervaka
      181 alrwida
//
LOCUS       WP_176040297             586 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia stabilis].
ACCESSION   WP_176040297
VERSION     WP_176040297.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..586
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=63903
     Region          7..586
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mkktrrlavl pitilitlaa qaqqapspsd qaaaaranae qnqqvqqrrd alqrdatvqa
       61 pgvrsdvprp eaypvlptet pcfridrfal dvpdslpaas kaqgasalpm drfafardwl
      121 thyagqcigk qgvdlivkgl sqailargyi ttrvlvpeqd lstgtlklal ipgvirhvrf
      181 vdeklrgtwk tafptrdgdv lnlrdieqgl eqmkrvssqd vtmqiapgnv pgesdvvldv
      241 krgkpwtvva sidnsgtrat gklqgnvslg idnplglndi fnvgfnqdle fgdkrfgshg
      301 wnafysvpwg ywtgtlsayt styfqplaav nqtfvasgnm ktvdfrlnrv lmrsqddvfg
      361 aqvrltrrfg dsyiegttip sshqnatfle fglndrhyfg ssqfdgslay rqglgwlgst
      421 dsmfaaeggq tyrfkmvvld anlstpfvig tqpfkyvttf hgqytgntvs yldsitigsr
      481 ytvrgfdget llagsrgfyw rnelqvpiaq tglaayagld ygrvwgpepv alvgtqlaga
      541 vigvkgsvat rfgayaydlf agtpvykpsg fetarvtlgf qltaqf
//
LOCUS       WP_176040311             238 aa            linear   BCT 11-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Burkholderia
            stabilis].
ACCESSION   WP_176040311
VERSION     WP_176040311.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..238
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=25175
     Region          14..208
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mngipttfiv qgalwllvvf svvtwtlivv kaiqslrasa rnrrytrafw aansfheaaa
       61 ldganspvge laatgfdalr radessahdl ehswsrhdll erhlrqqihn arrreeagla
      121 vlasigstap fvglfgtvfg iihaltaith sasasidvva gpigealvat gigiavavpa
      181 vlaynffvrr vkaasadlda fatdfvtlaq kagfrvpatv tapapahrsg etrqeafa
//
LOCUS       WP_176040312             358 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia stabilis].
ACCESSION   WP_176040312
VERSION     WP_176040312.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 358)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..358
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39062
     Region          12..335
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 msntasynvr siwytrcpvp tplgiaahlg wldsefagdg itvralqesq haalhhahvd
       61 hsldnafrqg gsipalwara agadtrvval twvdeaqaiv alpetgltrp kdlrgrrigl
      121 prrdgeridi fraaalrgfv salsldglgp gdvewvdvpa snlrapvstp ltrdaafshp
      181 asltsrrlya aeaaalvrgd vdaiyvkgsl gletahliga qpvvdigfhp dpqirinngs
      241 prpltvnast lerhpdivsr flarvtdveg warehedevl gylgretgsg hdwlrlayga
      301 dvhrrlrtdl deasiaaldd fkrflvdwqf lptdfdvraw idrraldgia tlsrdaar
//
LOCUS       WP_176040331             197 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176040331
VERSION     WP_176040331.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..197
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22032
     Region          8..166
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkkgtdtqas apdtrerilq tasalfyreg travgvdliv aqagvaktsl yrhfatkddl
       61 ieafllreda dfwahwdvva qqykrtpree ldaqlqwige riarpgyrgc pqiniaaeya
      121 ddnhparkva vahkqelrrr ltelagamrv depetfalrl atvidgalss gralhehgpv
      181 hflqeiaqll lpkkgrk
//
LOCUS       WP_176040340             613 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp70 family protein [Burkholderia stabilis].
ACCESSION   WP_176040340
VERSION     WP_176040340.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Fernandez-Fernandez,M.R. and Valpuesta,J.M.
  TITLE     Hsp70 chaperone: a master player in protein homeostasis
  JOURNAL   F1000Res 7 (2018)
   PUBMED   30338057
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 613)
  AUTHORS   Mayer,M.P. and Bukau,B.
  TITLE     Hsp70 chaperones: cellular functions and molecular mechanism
  JOURNAL   Cell Mol Life Sci 62 (6), 670-684 (2005)
   PUBMED   15770419
REFERENCE   3  (residues 1 to 613)
  AUTHORS   Bukau,B. and Horwich,A.L.
  TITLE     The Hsp70 and Hsp60 chaperone machines
  JOURNAL   Cell 92 (3), 351-366 (1998)
   PUBMED   9476895
REFERENCE   4  (residues 1 to 613)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   5  (residues 1 to 613)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
REFERENCE   6  (residues 1 to 613)
  AUTHORS   Rensing,S.A. and Maier,U.G.
  TITLE     Phylogenetic analysis of the stress-70 protein family
  JOURNAL   J Mol Evol 39 (1), 80-86 (1994)
   PUBMED   7545947
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418513
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..613
                     /product="Hsp70 family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0051082 - unfolded protein binding
                     [Evidence IEA]"
                     /GO_function="GO:0140662 - ATP-dependent protein folding
                     chaperone [Evidence IEA]"
                     /calculated_mol_wt=65544
     Region          7..608
                     /region_name="DnaK"
                     /note="Molecular chaperone DnaK (HSP70) [Posttranslational
                     modification, protein turnover, chaperones]; COG0443"
                     /db_xref="CDD:440212"
ORIGIN      
        1 msdprysigi dlgtthcals yvdsaasdge kiaqqvlpia qltapgales rdllpsflyl
       61 pheseltqgd ltlpwtasra favgemartr gagtpirlvs sakswlghag vdrraailps
      121 dappevsrvs plessirylt hlreawdhah pdapfadqdv tvtipasfdp aareltaeaa
      181 raagysrmtl leepqaalys wiqksqggwr kqvqvgdlil cvdvgggttd lsliavverd
      241 gnlelhrvav gehillggdn mdlalahiva rklaqqgtqa dpwqlralty acraaketll
      301 sdpstdavpl vvpsrgskli ggsirteltr teltqtileg ffpqvdaaar pvsrarvglt
      361 qlglpyaqda gitrhlaafl grqvaaldtl egvqhtlpqg atflhptavl fnggvfksal
      421 ltqrvldtln swlaaegapp arllegadld lavargaayy gyvkrgrgvr irggtarayy
      481 vaiesampav pgleppvqal cvapfgmeeg sdaalppqef glvvgepvqf rffgssvrrq
      541 dqvgtlldyw speelqelee iqatlpaegr tvgevvpvkl harvteagtl eleaipsgtn
      601 erwkvefdvr gaa
//
LOCUS       WP_176040359             210 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator transcription factor [Burkholderia stabilis].
ACCESSION   WP_176040359
VERSION     WP_176040359.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..210
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22890
     Region          7..199
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mtspapivyi vdddsgmrts lawllesvgi vsegfanaad flarfdvnlp aclvldvrmp
       61 eksgfdvqae lnargatlpv ifvsghgdip msvralqnga idfvekpyns qqmlervqra
      121 lrlaqqrhav dqrhrelrqr ldaltareke vlrgvvdgka skqiasdlsi svktvdvhra
      181 sikeklgats iaalvrdvmv vwgddgessr
//
LOCUS       WP_176040380             286 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176040380
VERSION     WP_176040380.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..286
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31507
     Region          9..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          105..270
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 madasdnllg aylrdrrekl dpaalglpvt rrrtpglrre evaqrahvsa awytwleqgr
       61 ggapsadvld rlaralllnd aerehlflig rghppevryh atdsvtprlq hvldsleasp
      121 aivrsatwdv vawndaaaat ltdyatlppa rrnilrlifv dprvrdaqsn wnqvarfavg
      181 afradvargg atqtvqafvd emratsaefd alwrdhdirs heegtkelrh pavgrialey
      241 safavsgrpd ltlviftpet aadrarirrl vaarekaaae yapaas
//
LOCUS       WP_176040442             727 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia stabilis].
ACCESSION   WP_176040442
VERSION     WP_176040442.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..727
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78225
     Region          46..727
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mpsrrtprra rtlrpwrtsl palitlcvas nahastgdrt dteppatast satpagrelp
       61 tisvnasaav dptvgyqprt ssiaggsdrp lkeipqsvav vsssvmqdqq arslddvlgn
      121 isgvtqtntl ggtrdaftkr gfgsnndgsv lvdgvrtpvl hsylatidrv evlkgpasll
      181 ygmqdpggvi nlvtrkpedt fggslsasrt shggssaqfd ltgplgkpgq vaggtlafrl
      241 tgeydtsryw rsfgrqrdal iapalswhda ntsidvsyqy vdyttpfdrg tvlvngqldd
      301 alryrryeea wsqssgiqet lrariehrfs dawrmratyg wgrdrydqti tratafnsrt
      361 galtrssdan lgrndsdqia tlgllgnvtl agmnhalyig geyerqrsfr gdtirgkttt
      421 gfnlydpvyg llapggvpnp kqsdsrsvvh aysmvvqdsv kltdrltavg glrweswqqe
      481 sgmgrpfvfa drshgnvwlp qfglayaltp altayanvsr sfkpnvasnv aaplapeygr
      541 vveaglkfsl kpgitgtlaa yqidkrnvav tvgdltstig tarsrgield vagqitrhls
      601 vigsyaytna tdrdsntslv nvahhtgslf avydtaianl pgrwrfggga rlvgarpgdt
      661 ansftlpgyv tvdafaayet tigkfptrfq lnvknlldkt yypssnnnli vavgeprlvt
      721 ltttvsf
//
LOCUS       WP_176040472             355 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia stabilis].
ACCESSION   WP_176040472
VERSION     WP_176040472.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..355
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38249
     Region          3..332
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,226,287,308,310..312)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,174,177,179,226,233,287,308,
                     310..311)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,174,177,179,311)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            179
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mdalftparv grytlqnrlv mapmtrsraa fdgtpgelaa eyyaqraglg livtegtqps
       61 ddgqgylttp giytdahvag wkivsdrvha rggrlfiqlm hvgrmshpdn tphhrqgvap
      121 saiapdvpmf tmkgmqeipa pralttaevr dtvndfrfaa rraieagadg veihgangyl
      181 vqqffapnan trddayggsi enrarfaiev aeaivdeiga drtairlspg svlwgidega
      241 qgpdlyrhla tqldrlglay lhvmhqgdep lladlrerws gtlivnrpgr trdaigtdva
      301 tgiadleayg qmvlanpdfv trlrtgapmn daqhatffgg dargyvdypa lsgaa
//
LOCUS       WP_176040515             551 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia stabilis].
ACCESSION   WP_176040515
VERSION     WP_176040515.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Gournas,C., Athanasopoulos,A. and Sophianopoulou,V.
  TITLE     On the Evolution of Specificity in Members of the Yeast Amino Acid
            Transporter Family as Parts of Specific Metabolic Pathways
  JOURNAL   Int J Mol Sci 19 (5), 1398 (2018)
   PUBMED   29738448
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Vangelatos,I., Vlachakis,D., Sophianopoulou,V. and Diallinas,G.
  TITLE     Modelling and mutational evidence identify the substrate binding
            site and functional elements in APC amino acid transporters
  JOURNAL   Mol Membr Biol 26 (5), 356-370 (2009)
   PUBMED   19670073
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12146941
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..551
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=59602
     Region          31..470
                     /region_name="AA_permease_2"
                     /note="Amino acid permease; pfam13520"
                     /db_xref="CDD:404414"
ORIGIN      
        1 msqaglranr tsdveatish dstghtlhrg ltwkdafwvt sgvpagvlft iggvcatigq
       61 pawaiwiaai tmgliqsaty aeisglfphk sggasvygai gwvrysklia pvsvwcnwla
      121 wspmlalgcg laasyaltsl fpadaavlhw qlkvadlgfi kpglslrina tfiiatilll
      181 itfklqhsga skaartqril giasltplli vgivpfvtgd vpmsnllpll plghdahgnv
      241 taatfgswng qgvtmalgam fmagwasygf etavcytref rdprrdtaka ifwsgalclv
      301 vmtlvpmafq galgtqamld psigdgtgva aamakivggg awvanavvvm lmlsillivm
      361 tsmmgssrtl yqasvdgwlp kylshvnehg sptramwtdl gfnlvllmms dymtvlsisn
      421 vcymlfvfln lqsgwihrmd rgnwdrpfrc ptwllvggai cgyanlvyvg aganlqgegt
      481 lrngliamll ivpvflyrhy wqdrgrfpaq mqrdmelevp krvmwlnlmp yaaligaglt
      541 iwlsyyfawv k
//
LOCUS       WP_176040516             205 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176040516
VERSION     WP_176040516.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..205
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22430
     Region          15..179
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msptstppgs rdrgrprefd tdvaveaaar vfweqgyhat sidtlceatg vfrgslyrtf
       61 gdkhgllvaa fdqyaegava rlkerlaadl pprdtlreal myytrigtrl serrgcfitn
      121 aaiellpgde alrphiestl lriatqlsla vargqqsgdf drnldpeevg rfllclvqgm
      181 rvlgkssase selvsivdia mralt
//
LOCUS       WP_176040538             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176040538
VERSION     WP_176040538.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33861
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,160,162,223,240,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mnqlqamrvf trvvelssfn laarqlgmsa aavtrsvgml eahlnmrlln rttrslslte
       61 tgreyldgcr tiiekldeie snlvqatrdp rgtlriaasa tsvaaglgtl lstyraehpr
      121 irfdvttfdt hvdmveggyd vcfcddrrlv natfvsrmlt svrdvvvasp eylarhgtpn
      181 dpvelnehsl ltvsngtars wefsdvdgsy rvytgnalas sgsmmvriaa lnhmgitqlp
      241 hplvaddlar gmllpllery evnggprsvs mlypsrnyls tkvrsfidyv vehyrapdrt
      301 aarlata
//
LOCUS       WP_176040560             164 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Burkholderia stabilis].
ACCESSION   WP_176040560
VERSION     WP_176040560.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..164
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=17217
     Region          1..148
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 midivvndtr hslenvpedm pllwvlrdrl kltgtkfgcg kglcgactvh legqavracl
       61 ipavaangrh vttieglspd grhplqlawv aedvpqcgyc qpgqlmqaaa llkggqpvdd
      121 aaivsamsgn icrcgtyari hraikrsasg dpalkaaiep akea
//
LOCUS       WP_176040591             306 aa            linear   BCT 11-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Burkholderia
            stabilis].
ACCESSION   WP_176040591
VERSION     WP_176040591.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..306
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33122
     Region          87..304
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 miwfgiatye lngrvaagla mdgalydaqa vlkraggdda pldvdslvad wplrgahtva
       61 rleaaareia agrldatpla gyrlhvpyap rrifaaasny heharemgte lapreesspy
      121 mfmkaetsvv ptlaevvmpp qaervdweve lavvigrsgr hiavadafdy vagytilndv
      181 sardlnrrtd ypfkhdwfrg ksfdtfgplg pwlvpracia epqnlrmrla vngetmqdgn
      241 tgemifsiae qihylssilt lqpgdliatg tptgvgmgrg iylqpgdvmv asidgigsie
      301 nplvrg
//
LOCUS       WP_176040622             463 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia stabilis].
ACCESSION   WP_176040622
VERSION     WP_176040622.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..463
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49730
     Region          36..451
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mdndrpgrsa svaamndigt rmhrddadgr rkphllglst lvifglayml pmtvfttygl
       61 vtsetnghlt aayavtlvam lftarsyghm arlmpsagsa ytfasrnfgt sagfmvgwal
      121 lmdylfipmi sylaigiymk qlfplvpasv wivasivlit glnivgirlv nrvnlilias
      181 qlvfiaifvi asarvaageg lslavalpas gdasaifags ailclsflgf davttlseet
      241 reprrtvpra illctlasgl lfmliayvgq vvfpdwhafk dldsaslelm rrigggalsa
      301 lfvavyvagc fasamagqas vtrvlfamgr drvlpervfg hlharlrtpv ratlavgavs
      361 lsalfitldl astmisfgal vafaivnlcv mrsylcraen rhvvgwitfg vmpaigfamn
      421 vwlwsglsrq tfyvgigwlv lglcqlvwlt rgftrpaptl smn
//
LOCUS       WP_176040639             220 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia stabilis].
ACCESSION   WP_176040639
VERSION     WP_176040639.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Kane,E.I. and Spratt,D.E.
  TITLE     Structural Insights into Ankyrin Repeat-Containing Proteins and
            Their Influence in Ubiquitylation
  JOURNAL   Int J Mol Sci 22 (2), 609 (2021)
   PUBMED   33435370
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Mosavi,L.K., Cammett,T.J., Desrosiers,D.C. and Peng,Z.Y.
  TITLE     The ankyrin repeat as molecular architecture for protein
            recognition
  JOURNAL   Protein Sci 13 (6), 1435-1448 (2004)
   PUBMED   15152081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12158766
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..220
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=23693
     Site            order(22,26..27,30..32,34..35,39,42,52,54,59,63..64,
                     67..69,72..73,77,80,89,91,93,97..98,101..103,105..106,110)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          22..52
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <24..111
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          54..89
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 msitwdgitg vgvlgdaeva rrhaladaak ggnwttmldl vakdsalvna trpggtslyt
       61 plhqaaygga prevaaellr lgawrmlrda qrsravdiav arghrhlvdl ltpqpkrfvp
      121 dgalreiqrh fhamivgria hlrvdalrlp elepllefdt qadhmwfavp gmyggfgyal
      181 rtdgdaavlv ssswsrvvgg sgqrheitan gctlveegfv
//
LOCUS       WP_176040652             232 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia stabilis].
ACCESSION   WP_176040652
VERSION     WP_176040652.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..232
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25362
     Region          26..189
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 myfemqaldg rqrsnlvhsa vlprpiawvs srsaegalnv apfsffnvms gdppilcfcv
       61 gsrdgvlkdt aqniaargef vvnlvssaqa rrmvvtsidf dtavdesvea glamassrlv
      121 dvprirdspa smecrvrqlv didarrtlvi gdivgmhlid eavtdaermf idplpmqlig
      181 rlhspgwyce vtrafqmatp slaqwrdmer dglarqylda plpaapmpqg ai
//
LOCUS       WP_176040669             210 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia stabilis].
ACCESSION   WP_176040669
VERSION     WP_176040669.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..210
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23252
     Region          1..210
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mtrvlyiegs pnkaysasie vcsafldayr qehpdhviqk ldiwdlampe fdeaalaaky
       61 aglngaaltp eqaaawqwie rlaapfhead kflfgvplwn fsipyklkhl idaisqkdvl
      121 ftfddsgfsg klagkkaavv yarglgyqsp gsftpagefd lqrpymetwl rfvgvqdvag
      181 ivvertlfgp dgkvdrsrai deartiartf
//
LOCUS       WP_176040705             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176040705
VERSION     WP_176040705.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33663
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,222,239,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     216..220,227..228,231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mldlndlalf vqvvragsfs eaarrlrmpa ntlsrridql egqlgtrllh rstrklapst
       61 egqalferya paldrifeie rqhadgqaps gtvrvtamag lfevfrlewl aefyarypqi
      121 sidfllddtp sdligeridl alrmgietgg sfrvrriaag ttilaaspay lkrrgaprtp
      181 relaghdclt vssrqgrsmw rlqgprgsqe isidsrfsvn dmrvvaqaci aglgiallpq
      241 llaepaieqg klvrvlpayr rsgtglglql vytsrpplpp avavfaefll eklseavcgq
      301 pngeadr
//
LOCUS       WP_176040706             192 aa            linear   BCT 11-JAN-2025
DEFINITION  YceI family protein [Burkholderia stabilis].
ACCESSION   WP_176040706
VERSION     WP_176040706.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..192
                     /product="YceI family protein"
                     /calculated_mol_wt=20502
     Region          18..192
                     /region_name="YceI"
                     /note="Polyisoprenoid-binding periplasmic protein YceI
                     [General function prediction only]; COG2353"
                     /db_xref="CDD:441920"
ORIGIN      
        1 mnkyltiaag alaaslsfsa faaastyqld pghtypsfea dhlaglsvwr gkfdksggtv
       61 tldraaktgt vdvttditsi htgsvkldeh lqnadffdaa kfpqaiykgt itfdgdrpat
      121 vvgnltmhgv trpltlkids fkcmphpmfk revcgvdaag efdrgdfgvd lgkaygfsmk
      181 trllitaeal kq
//
LOCUS       WP_176040872             787 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Burkholderia stabilis].
ACCESSION   WP_176040872
VERSION     WP_176040872.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 787)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 787)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..787
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..787
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85947
     Region          69..769
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 msytfvarps rgrlalacaa vfawpaahaa stdnarvdap rdgverpaga aapasavaav
       61 pfpptgdtlt avsvtaqrqp vdpdtpavve sitrerieth tnvttedalk yapnlmvrkr
      121 yigdrnsvfa grdfnelqsa rglvyadgvl lsnllgssya ypprwslipp ddiarvdvly
      181 gpfsalypgn sigstvlltt rrpekleasl stqfftqryh dgygfadsfg gnhqtarian
      241 rvgrfwfsls ldrlenngqp mqyaspnsay npklgravpv tgaatdigpn gkprtivgaq
      301 tierteqlne tvrmgyaftd hvdatltlgh wenhyrqhge tflrdaagnp vyggnvsigg
      361 qnmtvapnaf apqrgdqenw lyalglngrl dsgwrlsgvv saydvsrdvl raastvqgga
      421 gtlfqgdgtg wrtldlkaea pevkghtftf gyhydnyflr nvtyntadwl agpttslasv
      481 yqgdtrtqal faqdawrfap gwlatlglry erwdayggal gnaagtlgya drnanalspk
      541 valqwdatev wrfrlsfatg trfptvgelf qgtisnnaiv nnnpnlrpek aidwdftaer
      601 dvgvgvvras vfqsdlrdsi ysqttvsgas tvtnvsnvdr vrvrgvelaf sgenvglkgl
      661 aidanvsasn aqiladaanp ayvgsrfpri prmranllas yrfdehwlas vgvrysgrqf
      721 ntldnsdvnp dvyggtssft vvdlkaryrf drhwtaslgi dnltdrryyv fhpypgrtfy
      781 gelkwsl
//
LOCUS       WP_176040899             137 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176040899
VERSION     WP_176040899.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..137
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15333
     Region          19..100
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(20..22,36,53..55)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mtttvekvvl ppipakryft igevselcgv kphvlryweq eftqlrpvkr rgnrryyqhh
       61 evllirrire llyeqgftin garnrldspg garaaaapde hevqavdara agkpgatvdv
      121 valrqalldv ldglkhd
//
LOCUS       WP_176040910             330 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Burkholderia stabilis].
ACCESSION   WP_176040910
VERSION     WP_176040910.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..330
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=35691
     Region          125..328
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 myslmagvla vamlciagal mlwrhgevkr gqadvqrfid sriepaaraa gaiqreprpa
       61 agtasapgaa rapaapasrw ahwrelgaey lgnvasragi edargkalla llglvavglv
      121 agsrggwlgc iaalvcgasl lvfwlvsriq rrrltivrql psfldgivrl vtlgnsvpaa
      181 fqaallttea plrgcldhvs rmlrtgveid ramghiatvy htkefelvgs vlrlsvrygg
      241 radvmldrms tfmrdleqae relaamsset rlsawvlvml piaigsfvia tnplylqsmw
      301 ndytgrqllf iafmlqvagg iwlyhmaklr
//
LOCUS       WP_176040992             275 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia stabilis].
ACCESSION   WP_176040992
VERSION     WP_176040992.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..275
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29060
     Region          66..271
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mtilyrgmdr aaldaaylnt kavpdfpall ascqsrsaal ydaiagrrel rygarpaqry
       61 dwlpcgqpga plfvfihggy wqhcakedfa yaasgplarg ydvvlaeytl aptasmteiv
      121 aeigalldhl aadrdglgia grpihlsghs agghltamyr ahpavaaals isplvdlepi
      181 slcclndklq ltaqeieacs plryigpgap tvvavgdael pelirqahdy aaacdaager
      241 iahvqlpgmk hfavlddlan pdgkmlaalr aiapr
//
LOCUS       WP_176040995             487 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia stabilis].
ACCESSION   WP_176040995
VERSION     WP_176040995.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..487
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51991
     Region          58..467
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(68..69,72..73,76,110,160..161,163..165,168,188,
                     191..192,195,307,310..311,314..316,319,346,350,399..400,
                     404,408,424,427..428,431..432,435)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mnsqsldlgg naggpasarp paasagvgad aaplparrvt lgdfmddlpv galhrfvvwv
       61 igiglffdmy eiflvstigs alqneyglsr qsadfkllla safigmfvga lclgsladri
      121 grrkaflltl mwysafslvg afsvnadmlv acrfltgigv gaiypvadsf lseilpkekr
      181 grlaawaytt syvavplvgf lalwlnplhv agvagwriil aigslgavyv lciqhrlpes
      241 prwllaqgrt teahaalrrf adsagvrmpd qfaesaepqr plglgerial lrrepygary
      301 lmlavfhlfq gfgyygfgtl agtvvksrgf dvtdstlfia lsfvgypigs llsipllnwi
      361 errtlviasi lsiavfglcf aysgntvliv cfgllttcas nvfsnayhvy qaeifparvr
      421 staigstyal srivsgalpf vllpvlvgyg agamfgvisv algivaitlr vlgplttrrs
      481 qdeinpv
//
LOCUS       WP_176041007             321 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176041007
VERSION     WP_176041007.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..321
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35396
     Region          13..>176
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          98..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(108,112,151,165,167,232,249,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(109..110,114..115,117..118,121,125,127..133,194,
                     225..226,228..230,237..238,241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mqrkfddlll gsielfclaa elgsftlaat aasvtpaavs rsvarleerl gvrlfvrttr
       61 qirltdsgrr yfeqcrdals qlvdaereat gqqatpagvl rismptpygh yrvlpllpaf
      121 rerypdvhve thlsnrnidf aeegfdlair grapadsnlv arkledaelv ivatpgylkr
      181 agtptaidel haheciqfel pssgrpvpwl fddgsdeidv attghygtsg dvlagvtlar
      241 sgaglfqtyr fiveqdlrag tlveilpglg grsrpfmlly pharflssrv rvfvdflveh
      301 lerapvkqak partrrtgak r
//
LOCUS       WP_176041020             185 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia stabilis].
ACCESSION   WP_176041020
VERSION     WP_176041020.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..185
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19613
     Region          77..179
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(81..82,117..118,121,125..126,129,174)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mktmlaarva vclwfaggfv avpahaddaa dmrpsagdiv rqlapqgasr slrgivierp
       61 pvrtqddapr psvnlaiqfe fssarftpds kalldnlgha lsddalqhdh frivghtdas
      121 gnahanlvls krraqavady lvsqfgidgt rlavegvgsa rpkdpahpra alnrrvevvn
      181 ldgge
//
LOCUS       WP_176041026             461 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia stabilis].
ACCESSION   WP_176041026
VERSION     WP_176041026.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..461
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48264
     Region          16..449
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,141,
                     144..145,148,275,278..279,282..284,287,315,319,371..372,
                     376,380,396,399..400,403..404,407)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mhrsprrarw lalagvaias flgcidftiv ntaipdirsa fdvgidqvqw vvtafvials
       61 sctipvgqla drhgrrrvml asmavfggas lgaglasglv alvlwrvvqg iacaglytas
      121 aalvatmfpe sergkalgll fsvnglglal gpvaggllvd algwrwiflv nvplivtsfl
      181 lcagrltqda aapmqrrtrf dwpgvalllt ilpcglvavv rggewgwtsp atlglllval
      241 lsaaaltrvk rhaaapllql alfrqrpfvl avcataglaf fycaaflfmp lylgelrgqd
      301 saapgwlllp ttavmamvsp pagrgydrfg avaimalgfv allvsalmqa tfgattawww
      361 vlagfacmgl gwgcvlgpsl taalaavpea lagtalgmat mvhnvggsmg laaatvlyrf
      421 satpdggfit gyrsvmlmlv ivcivvlwil avehrrdlra r
//
LOCUS       WP_176041051             216 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia stabilis].
ACCESSION   WP_176041051
VERSION     WP_176041051.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..216
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22414
     Region          7..205
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mslhypllfa ylaaivllia tpgpvvmlvv gtvarrglrq gvltavgana aslvmiaaam
       61 lmvfgvvlvs ermltglhvi gcvfiavlai rtllgewrag rapggngege gepasrarrl
      121 pgvvrgflvg ianpkdllff vaffpqfvgi tpdsrvslai laglwiavdf tiltgymaai
      181 nhplihrkqr witassasvl lvialaglgg aiagla
//
LOCUS       WP_176041078             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176041078
VERSION     WP_176041078.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33217
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..295
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,190,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mqnldallif arvaemtsft raaeslgiqk grvsmvirel erdvgvallh rttrrvqlte
       61 dgrafysrar dllaevqelq smfsgngtpl rgrlrvdmpt elarsvvipa lpqlmaaype
      121 lelelssndr rvdlvqegfd cvirlgpivd etliarplgk lrmtnaasps ylarhgiprt
      181 lddlrtqghr mvhysltlga rhagweypdg egyaslplps aiqvnsvqty haaglaglgl
      241 iqagyptlah hvesgalvev lpdlrpeplt aslvvahrrn lsprvrafmd wiegvlepyf
      301 d
//
LOCUS       WP_176041079             196 aa            linear   BCT 11-JAN-2025
DEFINITION  flavodoxin family protein [Burkholderia stabilis].
ACCESSION   WP_176041079
VERSION     WP_176041079.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..196
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=20714
     Region          11..189
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mtlhtspint vvvyhsghgh ttrmasaiae gadavlvaid adgniaadaw dtlagadail
       61 lgsptymggp swqfkkfada sskawfeggw rnkifggftn sasingdkln tleyffllag
      121 qhggiwvsmd ikpanvkasl rddlnrmgsy iapmaqtpad aspeemspgd letarrygar
      181 vamiagqfrs gksrss
//
LOCUS       WP_176041103             568 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia stabilis].
ACCESSION   WP_176041103
VERSION     WP_176041103.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..568
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=59924
     Region          1..550
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mefdflivgg gtagavmasr lsanpdcrvl lveagadvap gaepadirda fpastlnagy
       61 fwsgltatar dggrpapypq arvmgggssi ngmfalrgmp sdyrrwadag agrfswdsvl
      121 pyfrkveddr drpgkaggvh aiermpkaqw pafvrameqa aqrcgfpsip dineepgdgf
      181 fpmplaidsd trvtstgcyl trevraranl eilsetqvmr lrmtgntvqg vevlrdgaiv
      241 hlsarnvvvs aggifspall lrsgigpaat lsslgirvva drpgvgrnlq nhpymffalt
      301 lprgkriaad lrrfavaglr sssdapgcpa sdlfsfvigr vsgasfgpdf alvgsalyap
      361 ksrgsvtles adplvnpvvn frfmsdpadp qrmiksarlt erllrepgva aqyheafllp
      421 galavtqfnr tgltgkmlam aaeaaanapg vvrraifgra frsggpvayr gggreisddd
      481 ilssispmgh pvgtcamgsa ddamavvded frvhgirnlf vvdasvmpli psantnlptl
      541 mlaelaadri gardscirav agidasgr
//
LOCUS       WP_176041104             580 aa            linear   BCT 11-JAN-2025
DEFINITION  thiamine pyrophosphate-binding protein [Burkholderia stabilis].
ACCESSION   WP_176041104
VERSION     WP_176041104.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..580
                     /product="thiamine pyrophosphate-binding protein"
                     /GO_component="GO:0005948 - acetolactate synthase complex
                     [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0030976 - thiamine pyrophosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0009097 - isoleucine biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009099 - L-valine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=61086
     Region          29..578
                     /region_name="IlvB"
                     /note="Acetolactate synthase large subunit or other
                     thiamine pyrophosphate-requiring enzyme [Amino acid
                     transport and metabolism, Coenzyme transport and
                     metabolism]; COG0028"
                     /db_xref="CDD:439799"
ORIGIN      
        1 mnadqrrspv tigeaeagts fvalddirpr rgaevlvevl rsegvryvfg npgttelsfi
       61 daltdapdls yvlglqeaav vamadgyaqa sgrpgftnlh tvgglghamg allnakaart
      121 plvvtagqqd trhaytdpll ygdslgvarp avkwarevsh pdeigvlvrr afndsaaaps
      181 gpvflslpmd vmerattepv prrsaidrts ipsalpdlak alasirpgrl amvvgdevfa
      241 agasaaavav aetlgapvfg pswpahlpfp tshalwcgnl pmtvadmhet lrdfdavfvl
      301 gghfsitily stgpaipsac rlyqlasdpq dlgrihatal gcvgalrasl qallpmlrea
      361 sqhrraeida lhaeaqrgra rqrasleeqv asklnaamtt plvaahevar algpttplvd
      421 espatmplir ralhsagtrq yygtrgailg wgmgaavgls lglgrepvva iigdgsalya
      481 pqalwtaahe glpvtfvvvn nqeynilkky mksqqhfvsa hadrfvgmdl kdppidflal
      541 arswgvaarr varagdiaaa vecgiasgrp nlieipvsvt
//
LOCUS       WP_176041194             220 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176041194
VERSION     WP_176041194.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..220
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23875
     Region          27..182
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msnsgmekal etekrgrsyg gvapevraae rrealiraat rvfgtvgfrk atvrsicqea
       61 klndryfyaa fdstedllrc tylhhaqqlh eavaqavaar ggdlresvda glaaffaflr
      121 dpcaarvlll evmgvsadtd mtyqrmlidf gklimaigap geattpvert eqrliglalv
      181 gamtnvgaaw llteyrdpea qmiascrkvl lgtlraiget
//
LOCUS       WP_176041217             356 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia stabilis].
ACCESSION   WP_176041217
VERSION     WP_176041217.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..356
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38540
     Region          26..265
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mtaplpirlp pflrnalrpl ldpyrryrha klihaarvsl ailvsialst glrvphgews
       61 titvlivvgg lqhhgnirkk aaeralgtsi galaglglil lysvvhapla iyllmalacg
      121 fcayhaigka gyiallsait mvivaghgdn eivdglwrav nvltgiaial afsfalplya
      181 tyswryklad alracaavha rlagdrhvsd dahlkemaal sallvqlrsl mpsvskecet
      241 smtqleaiqr slrlcigyle ilssavptrd dvaareymrv dmkavnrrir dtlvgasral
      301 kfgtpgrlap rrrpadpphd apppqlsgyv sitaklagev dqlreklldt arswni
//
LOCUS       WP_176041195             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176041195
VERSION     WP_176041195.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32997
     Region          9..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..294
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,229,246,273)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,193,
                     223..227,234..235,238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 madlrdvnln rlaifvavvd agsltaaaer lglaktvvst hmqrlesevg anllvrttrr
       61 lsvtdagrtf ydacraivra tenaldavss dagplrgtlr vsvpidygal vvapavvalr
      121 dthpgldvel vandrvvdlv adnldvairi grladsnyra vqlgtyekwl vaspafvarh
      181 glprdpdala alpfvmlstl prphtleldh arggntsvrc aapvvsntat acraivlagg
      241 gfglltdfst addvaagrlv rllpawgsap agihavypst rlpspkvraf idamkarige
      301 arpvpaaknr rsr
//
LOCUS       WP_176041244             504 aa            linear   BCT 11-JAN-2025
DEFINITION  MDR family MFS transporter [Burkholderia stabilis].
ACCESSION   WP_176041244
VERSION     WP_176041244.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..504
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53167
     Region          38..422
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(39..40,43,74,124..125,127..129,132,152,155..156,159,
                     284,287..288,291..293,296,324,328,381..382,386,390,406,
                     409..410,413..414,417)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mttdtlltpp aaeaarrdap tglivaalll vmllsaldqt ivstalptiv gelggldqls
       61 wvvtayllss tvvlplygkl gdlygrkivl qvaivlflag salcgvaqdm tqlivlralq
      121 glgggglmvv tmaaigdlvp pdrraryqgm fggvyglati igpllggflv ehlswrwift
      181 inlplgflal avigiafrph tahvkhridy mgatflatal tcvilftseg gsllpwtspq
      241 lwmtlvlglv aiggfiyeer laaepimple lfrhrtfvlv sligfvvgia lfgsvtfipl
      301 ylqvvkgstp sqagmqllpm mggmlvtsiv sgrlisrlgs yrmfpiagtl tggiamalls
      361 tltldtplht myaymallgi glgmvmpvlt lavqntvefr hmgvatsgat lfrsiggslg
      421 vaafgalfsh glqsrmmhal pagtelppal gpatvhqlpd avrdaylhaf agslhvvyla
      481 aatviaiafv lawfvedapl rkhs
//
LOCUS       WP_176041249             123 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia stabilis].
ACCESSION   WP_176041249
VERSION     WP_176041249.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10523110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..123
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=12734
     Region          54..119
                     /region_name="BON"
                     /note="BON domain; pfam04972"
                     /db_xref="CDD:428229"
ORIGIN      
        1 mksrflivva givaltsvtc yaqsatpdtq aakpaatssr sakkaerlen rtfakkvrqa
       61 ivkapgigna qvtvfakakt gevtlagmit desqdkaave aarqvpgvts vtsklelrme
      121 ggq
//
LOCUS       WP_176041251             105 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF485 domain-containing protein [Burkholderia stabilis].
ACCESSION   WP_176041251
VERSION     WP_176041251.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..105
                     /product="DUF485 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=11542
     Region          1..105
                     /region_name="YjcH"
                     /note="Uncharacterized membrane protein, DUF485 family
                     [Function unknown]; COG3162"
                     /db_xref="CDD:442396"
ORIGIN      
        1 mtlnasavsr irehakfrel vderarlgrv lmvivlgayf glialvalrp dllstpawtg
       61 svttvgvifa vvvivagwgf twlyvrvand rferltdell gevqq
//
LOCUS       WP_176041323             421 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia stabilis].
ACCESSION   WP_176041323
VERSION     WP_176041323.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..421
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=43802
     Region          205..409
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(212,252,290,393,396)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(212,393,396)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(212,252,290)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 msfrssiaaa vlgavvfvsp laasaapagw vaawatalqp ipdlaapppl yrapdvagrt
       61 vrqivyptvs graarirlsn aygrvplvve aaslaragdg aalaggaavp vrfggkasat
      121 lapgqelesd pvaidvtagr pyavslqmgp nqrmtvwhrv snqfnyvsap gdhvsdpdaa
      181 vfrtrftqya wvtelaveag sarasvaaig dsitdglrss lnrnrrwpda larrltasga
      241 dsvgvvnlgi sgnrllsdsa cygtslasrf erdalsragv kaaivligin dinfaamppr
      301 agldcdhpht qvsaaslidg yrrlieaahr qgvkvfgatl tpaglpagre airlevnrwi
      361 rsgggfdgvv dfdavlrdpa rpsvlqrryd sgdgihpsda gytamadavq ieqlqavvgg
      421 k
//
LOCUS       WP_176041325             197 aa            linear   BCT 11-JAN-2025
DEFINITION  YbhB/YbcL family Raf kinase inhibitor-like protein [Burkholderia
            stabilis].
ACCESSION   WP_176041325
VERSION     WP_176041325.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..197
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=20518
     Region          40..196
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mrvdrritpp apsgrpspfi iallcaaafa alpayaegpf tvssddltpg grvgaanvfd
       61 rgdckggnrs pqltwrnppp gtrgyavtif dpdapghgww hwavagipat vtslpadasa
      121 sgflrrigas earndfgidg yggpcpppgk phsyvitiya lkgtdlrvaq grpapmfdhe
      181 igtlaigtar lvvtygq
//
LOCUS       WP_176041328             443 aa            linear   BCT 11-JAN-2025
DEFINITION  carotenoid oxygenase family protein [Burkholderia stabilis].
ACCESSION   WP_176041328
VERSION     WP_176041328.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Poliakov,E., Uppal,S., Rogozin,I.B., Gentleman,S. and Redmond,T.M.
  TITLE     Evolutionary aspects and enzymology of metazoan carotenoid cleavage
            oxygenases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1865 (11), 158665 (2020)
   PUBMED   32061750
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Sui,X., Kiser,P.D., Lintig,Jv. and Palczewski,K.
  TITLE     Structural basis of carotenoid cleavage: from bacteria to mammals
  JOURNAL   Arch Biochem Biophys 539 (2), 203-213 (2013)
   PUBMED   23827316
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Kloer,D.P. and Schulz,G.E.
  TITLE     Structural and biological aspects of carotenoid cleavage
  JOURNAL   Cell Mol Life Sci 63 (19-20), 2291-2303 (2006)
   PUBMED   16909205
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Wyss,A.
  TITLE     Carotene oxygenases: a new family of double bond cleavage enzymes
  JOURNAL   J Nutr 134 (1), 246S-250S (2004)
   PUBMED   14704328
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..443
                     /product="carotenoid oxygenase family protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006720 - isoprenoid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48870
     Region          10..439
                     /region_name="COG3670"
                     /note="Carotenoid cleavage dioxygenase or a related enzyme
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]"
                     /db_xref="CDD:442887"
ORIGIN      
        1 mtvfdlnsga iapvadevdl vdlrvtgsip reldgallrn gpnppggrfe ghdmlswwpe
       61 aamlhaiafe ggratgyrnr wartqrwaav hapeqaphlp dtnpnvnvlq hagellamae
      121 ggaplaitag ldslgvsrrh agfdggmtah pkvdpvtgel mtfradwrap wlrygvvdah
      181 gvqrvdiavd lpapsmmhdl aitetrslll dlnvgydfsm lkhghrmplr whddrparig
      241 viprhggdvr wfgvepcfvq hvvnaydcda scivldvvry pwflrldart grfdenpvge
      301 lwryvidtan glidegplad ggielprine srtgrryryl yaveqpnnae mrgvmrfdha
      361 rgtttryavp agdqnsepvf vprpggtded dgwllvmvyr avtdtsdvvi ldaraidagp
      421 vatvhlprrv pagfhgawvp rer
//
LOCUS       WP_176041240             339 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176041240
VERSION     WP_176041240.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12168323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..339
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37045
     Region          27..201
                     /region_name="AraC_binding_2"
                     /note="AraC-binding-like domain; pfam14525"
                     /db_xref="CDD:434015"
     Region          255..335
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mpltpnaevl salyrnclfr sglrmdahel vsaelsehal rwqrgvpdta lfkgqlnhls
       61 iyalqygaev evaprpfdgf slvhtslagg aeiecdghvm gvsegrtavl aprtrvrlrw
      121 rsgtrqlivk vpdslmraag grrpddaapg lapgfllpts lasqwdliaq sllnmlavad
      181 dggiraewrd hferslalfl rvhcppspaa thagpvpqar gapakagsrg girqmdalhe
      241 fiharlcapi sledlarvag vslrtlnvlc rryhgatpme llrnirldaa rvqlltdpmv
      301 sitdtaltfg fghlgrfsay yfarfnelpr dtqkkrqps
//
LOCUS       WP_176041329             243 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia stabilis].
ACCESSION   WP_176041329
VERSION     WP_176041329.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..243
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26171
     Region          4..210
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mspillygip agcsfgsiva lewagrpyrl sriampsvat sdaylalnpv aetpafitan
       61 gdvlteslai lghigaqtld sglafrqgsa dfdrlnrmla wlnttffnaf galwyvyehs
      121 tegaekaalq aygrgkvlka hrqlealler gegpwllgtr rtladayfag iarwadyhav
      181 ferdafpria alrarladda gvqfahaiee nlplpaslaf eghvslddvl asardlavpa
      241 ral
//
LOCUS       WP_176041330             331 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176041330
VERSION     WP_176041330.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..331
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35376
     Region          25..83
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          113..307
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(123,127,168,182,184,242,259,286)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(124..125,129..130,132..133,136,140,142..148,211,
                     236..240,247..248,251)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 manddavvar ieihrfflwt ltvnlndlyl fvqavdagsm saaarrldlp kstvskrvae
       61 lertlgarlv hrtsrsfrlt pvgaeffeha raavieaesa rdavlrqaae pagivritss
      121 vpvaqhilap clpalaiahp klllqihasd rlvdiaqegf diavrshfap lpdsalvqrp
      181 latspivvva spgylaraga phepadlarh dglhpgqqpw rlqrggdtvd vtprirlqad
      241 estlllqaam aglglaclpd wiasdplasg alvrvlpgwr agavtttllm phrrgqlpgv
      301 raaveflvrh varhhgggvd eaddalaras d
//
LOCUS       WP_176041367             476 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia stabilis].
ACCESSION   WP_176041367
VERSION     WP_176041367.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..476
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49570
     Region          21..476
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mqtrdtaaps geqgdaplag daletalvae lgealvtrsa dvdpryftay nepagvrpra
       61 lvrprgvddv srtlalcarl gqpvvpqggl tglargaval ggevvlsmer fagiealdaa
      121 agtmtvragt plqtvqeaae aagftfgvdl gargscqigg mlatnaggtr airygmmreq
      181 vlgleavlad gtvvssmnrm lknnagydlk qlfigsegtl gvvtravlrl hpllaapata
      241 lcrvrdydav lglwnrvrtl pevvsfeamw pafydyvarh tpgvvapfag dggfavliec
      301 atsapggdah ealetglaag idaglvedav latserqard lwtlreglai dalphlvnfd
      361 vslptgelga faerceaalr arwpdvvclf fghvgdgnvh igvslagmtd adadaldhcv
      421 yavvrdmggs vsaehgigal krpylahtrs daeiglmrrl kaaldprgil npgkvl
//
LOCUS       WP_176041378             561 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia stabilis].
ACCESSION   WP_176041378
VERSION     WP_176041378.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..561
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=61157
     Region          10..539
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mttqrtlege fdyvivgagt agcvlanrlt edpdisvlll eaggkddyhw ihipvgylyc
       61 ignprtdwly ktqpeaalng ralsyprgrv lggcssingm iymrgqredy dswaqetgda
      121 gwswdsvlpi fkrsedhhag esdvhgaggy wrvekqrlrw eilesfaqaa qqtgipatdd
      181 fnrgdnsgvg yfevnqkrgv rwntskaflr pamarpnltv itgaqaqrvi fdgrravgve
      241 yhgggtdyva raraevllts gavnspqlle lsgigcgrrl qalgidvvqd lpgvgenlqd
      301 hlqlrmafrv egvrtlntms ahwwgklmig aeyallqrgp msmapsqlga faksdpddpa
      361 ltrpdleyhv qplslerfge plhsfnafta svchlrptsr gsvhiasadp glapaiapny
      421 lstdhdrrva analrltrri asapalaryr peeilpgaqy rteaelieaa gavgttifhp
      481 vgtcrmgrad deravvdsrl rvrgiaglri vdasvmpfit sgntnsptlm iaerasdmir
      541 adrraareat pvrteaaata v
//
LOCUS       WP_176041379             404 aa            linear   BCT 11-JAN-2025
DEFINITION  cation:proton antiporter [Burkholderia stabilis].
ACCESSION   WP_176041379
VERSION     WP_176041379.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001451
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..404
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43669
     Region          13..390
                     /region_name="KefB"
                     /note="Kef-type K+ transport system, membrane component
                     KefB [Inorganic ion transport and metabolism]; COG0475"
                     /db_xref="CDD:440243"
ORIGIN      
        1 mksafsflpn wplvpdavfw aglalfaagl cgelcyrawr lpritgyavi gliagsfgfg
       61 vidsstdets rllmnvalgl llfelgsrld lrwirrnpwl iasslaeatl tfvlvlfvml
      121 algvsgmval vlsaiaiats psmviqlkte lraegqvsqr litltalnsv yaivltklvt
      181 swlhqeaygn vfatilqply liagsfivay lvarscnflf rhmtstmrde hsfvalfglv
      241 mlaiavaqal klstlltlll agiivknlea rpqlwpehfg tagwlltvvl fvltltsftw
      301 gdialgglla ivlivtrlva klagvaafak psgigmkqgi algialtpms alsyllvddt
      361 yqlypnfdph lraivmcsiv vlqlvspfiv yrclsavger sdsn
//
LOCUS       WP_176041441             557 aa            linear   BCT 11-JAN-2025
DEFINITION  alkaline phosphatase family protein [Burkholderia stabilis].
ACCESSION   WP_176041441
VERSION     WP_176041441.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Goding,J.W., Grobben,B. and Slegers,H.
  TITLE     Physiological and pathophysiological functions of the
            ecto-nucleotide pyrophosphatase/phosphodiesterase family
  JOURNAL   Biochim Biophys Acta 1638 (1), 1-19 (2003)
   PUBMED   12757929
REFERENCE   3  (residues 1 to 557)
  AUTHORS   Gijsbers,R., Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Structural and catalytic similarities between nucleotide
            pyrophosphatases/phosphodiesterases and alkaline phosphatases
  JOURNAL   J Biol Chem 276 (2), 1361-1368 (2001)
   PUBMED   11027689
REFERENCE   4  (residues 1 to 557)
  AUTHORS   Bollen,M., Gijsbers,R., Ceulemans,H., Stalmans,W. and Stefan,C.
  TITLE     Nucleotide pyrophosphatases/phosphodiesterases on the move
  JOURNAL   Crit Rev Biochem Mol Biol 35 (6), 393-432 (2000)
   PUBMED   11202013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..557
                     /product="alkaline phosphatase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=58360
     Region          47..535
                     /region_name="AtaC"
                     /note="c-di-AMP phosphodiesterase AtaC or nucleotide
                     pyrophosphatase, AlkP superfamily [Signal transduction
                     mechanisms]; COG1524"
                     /db_xref="CDD:441133"
ORIGIN      
        1 misffgkqrk mavmvagala lasagahaaq dgngqgedgg harrvvkhvl lisvdglheq
       61 dlarcigant cpniavlaks gvtyanaytp glsdsfpgla alvtggspkt aglfydvsyd
      121 rnlyapgdtt csgkqgwnvv fdettgidaf nggklvhldg ggafnpqaip harvngqcvp
      181 vyphnyvktn tvfeavkagv pnahtawadk hawgydwlng psgtgvddlm rteinsidpa
      241 tntdytdiys htarfdnlhv qalinqiegr dstgtksapv ptlfgadfqt lsvaqkspva
      301 kgggyldadf tpngqvanai tyvdnsighi vaalkqanly tstavivtsk hgqsptdhtk
      361 lvkngdtltk lleannyldp ngnfgqnntt tgnlndgsgl vgtgfvqtdd vgliwlrdrs
      421 qrtavvqtlk anlgcnapgi cadgsqayvl ygaaladrfg dpangrtpdi ivqpnpgviy
      481 tsstkkdeeh ggnapddshl gllvsypgih rartvtdlvg tkqvaptile llgadprllh
      541 avvaentrvl pglgigr
//
LOCUS       WP_176041413             371 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia stabilis].
ACCESSION   WP_176041413
VERSION     WP_176041413.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..371
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39427
     Region          5..349
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,236,303,323,325..327)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,103,110,183,186,188,236,243,303,323,
                     325..326)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(27,103,183,186,188,326)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mtqdplfqpl rfgaltlpnr ivmppmtrsr asqpgdeane lmaayyaqra saglivsegt
       61 yiaplgkgya wtpgihtpaq vsgwrkvtda vhaahgrifa qlwhvgrlsh tsllggrqpv
      121 ssspiqakgv nvfvagedgs tpgfvqasep raltideige ivgqyraaar haieagfdgv
      181 elhgangylv nqfidsnant rtdayggsle nrlrflreva qaliegtgda srvgirlapl
      241 ttlngcvdad pettylaaak llgelgvgyl hiaeadwdda plmpvafkqq lraaypgvli
      301 yagaytaera reaiaagwad lvafgrpfva npdlperlrt gamltphdrn tlfggdargl
      361 tdyptlaqaa a
//
LOCUS       WP_176041446             936 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Burkholderia stabilis].
ACCESSION   WP_176041446
VERSION     WP_176041446.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 936)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 936)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 936)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 936)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 936)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11534155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..936
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..936
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=95556
     Region          11..79
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          112..174
                     /region_name="HMA"
                     /note="Heavy-metal-associated domain (HMA) is a conserved
                     domain of approximately 30 amino acid residues found in a
                     number of proteins that transport or detoxify heavy
                     metals, for example, the CPx-type heavy metal ATPases and
                     copper chaperones. HMA domain...; cd00371"
                     /db_xref="CDD:238219"
     Site            order(118..120,123)
                     /site_type="metal-binding"
                     /note="metal-binding site [ion binding]"
                     /db_xref="CDD:238219"
     Region          192..934
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mteplasaal qtielsvdgm hcggctgrvq ralaavpgvv datvdldtha atvtaqetve
       61 pgrlvdavae agyraavret aveavaatha ahashaeapp ataaalpaat ieldidgmtc
      121 ascvsrveka lakvpgvtra svnlaterat vdatinvsas qladavkqag ygatpvadar
      181 paesaaptsa dleldiggmt cascagrvek alaavpgvar asvnlatera svhgagalda
      241 atliaavtta gyraslaaap aagaetqlss paqdpdarkr reavrernlv igaavlsapl
      301 vapmlaapfg vdlmlpgwlq fvlasivqfg fgarfyraaw havkaragnm dllvalgtsa
      361 ayglslwmll rdpahpghly feasavivtl vrfgkwlesr akrqtteair alnalrpdra
      421 rvvehgverd vplsqvrvgt avsirpgerv pvdgrivsgr shideslitg eslpvpkdgg
      481 dpvtagsing egalvvetta igaettlari irlvesaqae kapiqrlvdr vsevfvpail
      541 giavltlvgw liagagmeta ilnavavlvi acpcalglat paaimagtgv aarhgvlikd
      601 aqalelaqra tviafdktgt ltegkpsvta feavdvprae alalaaavqr qsdhplarav
      661 vaaydkdvaa hgdtvpsaaa gaatdarava grgvearvgg qllalgstrw rdelgivvpp
      721 aldaraaele ragntiswlm radapralla liafgdtvkp gardaiaals trgvasvlvt
      781 gdnrgsaaav aaslgigevh aqvlpddkar vvaelkrahg givamvgdgi ndapalaaad
      841 vgiamatgtd vamhtagitl mrgdpalvad aidiskrtyr kiqqnlfwaf vynlvgvpla
      901 algwlnpvia gaamalssvs vvtnalllrr wkgrar
//
LOCUS       WP_176041456             312 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia stabilis].
ACCESSION   WP_176041456
VERSION     WP_176041456.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..312
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33342
     Region          66..311
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mdtlhlvdpe irpmletwpt vtlgidnlaq srervlplpp pdlagstler rtvpgpagap
       61 dvpvlvylpe agarplpaiv hmhgggyvrg aakdleavhr shvtqlgcal isidyrlape
      121 tvfpgaiedc yaalawvfrh adtlgidasr igvagesagg glaaalalla rdrgeyrlaf
      181 qhlvypmldd rtctrtphph agefvwhaan nrfgwtsllg hapgidgvsp yaaaaratrl
      241 dglppaflsv gsldlflden ldyaqrllra gvptelhvlp ggvhgfdivp garvsetarr
      301 lshdalrrfl hg
//
LOCUS       WP_176041484             234 aa            linear   BCT 11-JAN-2025
DEFINITION  MOSC domain-containing protein [Burkholderia stabilis].
ACCESSION   WP_176041484
VERSION     WP_176041484.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12233312
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..234
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25684
     Region          8..183
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
     Region          180..223
                     /region_name="3-alpha"
                     /note="3-alpha domain; pfam03475"
                     /db_xref="CDD:460938"
ORIGIN      
        1 mssearpvia vgigavriga srplagtpha saidkravds clwlgtlgfa gdeqadsrhh
       61 ggpdkavhhy ahdhyawwta qigardvlaq pgafgenlst qgvtehdvcl gdvftvggav
      121 lqvsqsrqpc wklnarfdhp rmaalvqqsg rtgwyyrvlh egwvapgdvl alherrhpqw
      181 plsavldvly rrtldmaald alcdvpalpp gwrkmldkrr aerqvedwtk rleg
//
LOCUS       WP_176041548             268 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia stabilis].
ACCESSION   WP_176041548
VERSION     WP_176041548.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..268
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=27913
     Region          9..247
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 mrarpivavt adrilrgahp nhtagekylt alvdgagala fvlpalgarq padtivaavd
       61 gllltgsysn vephhyggaa sapdtlhdpa rdatalplir aaidagvpvl aicrgmqeln
      121 vayggtlhqr lhattgfgdh rerpadpler qygpahvvql apggllqria rgaheatvns
      181 lhdqgierlg agltveasap dglveavsvr garafalgvq whpewrfaeq plsrdifaaf
      241 gaacrarmah rihaaggdlp stavsdvd
//
LOCUS       WP_176041597             337 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Burkholderia stabilis].
ACCESSION   WP_176041597
VERSION     WP_176041597.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..337
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=37667
     Region          31..304
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mslpappdtp arpeekdlfd rgasdwvvsp eaafdawlam qdyrrssadv yraqwgaflt
       61 wlrthqknla tvdtatianf vgelpirktq rmrylrlier vldhirrtey astnparfia
      121 qdgeatwrka rdneptgflt pveratllay lfspigvsgs aywkerrdra lvaaflgagi
      181 ktgearalti scintsgtsl qipsthpdfa rethlasfai alleawlter krqeipgelv
      241 fpashagrpm hkatmlraid aivesaglts srtaraspqt lrntyaaelf ehdvppervg
      301 kwlgfmrpis snrlhrawkn wrdgladgda tdsdeth
//
LOCUS       WP_176041608             521 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia stabilis].
ACCESSION   WP_176041608
VERSION     WP_176041608.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..521
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=55429
     Region          1..521
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 metydhivvg ggsagctvah rlvkagrrvl lledgpkdds lfiripatfi rvlgtqrtvt
       61 fesepqpgaa grktyvpqgr tlgggssvna mlyvrgtrdd yddwaalgct gwgwddvlpv
      121 fkraeshlrl sepfhgtdgp lkvgdtrfrh plslafvkaa qeagiayndd fngaaqhgvg
      181 fyhttifdgq rgstaatyla daighpnlrv ltgcrvtrvr fdgrratgve wrtesgatgs
      241 aaaradvvla agalstpkll mlsgigpgah lrahgidvlh dsrdvganyq dhlevsiygr
      301 shapvsllge drglkalrhg lqwmlcrtgl ltsnvvesga fvdttgsgrp diqfhvlptl
      361 vgdvdreplp ghglsinpcl lrprsrgsvq lrgsdpaapi lfdsgalsdp advaglvrgv
      421 alarqiirap slarivreae tltdaalady vrrraktvyh pagtcrmgnd ahavvtprla
      481 vqgvdglric dasvmprivs gntnaptimi aercaafmla d
//
LOCUS       WP_176041610             833 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            stabilis].
ACCESSION   WP_176041610
VERSION     WP_176041610.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..833
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=89582
     Region          14..788
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 madlaafirt pfflqdkrll alsfphddap svtdsygrhr parlvverlv aheglgidft
       61 fdvtllsges gvtladmlgk llavsmvrpd gglrhftgyc tefslvrndd siaeyravlr
      121 pwshflrtrv nnrlflgqsl qqqigtllad yqglapswew rvrgddpart mnvqggglge
      181 sdwnyivrhl eaagclywwe hdekglkliv gddstvqcpa vdgrspeirf qthdgpmaad
      241 aisqwsavrs laagsysata fdfkaphaas aqiptlhpsg vapqverhey vghygfvket
      301 rsgdalarmr meeieaaasr fdaagnhhgi lpgrwfqlsd hfstasgspe dhrylileah
      361 heaannylqa dgkpeyrnrf vaglrhtpwr pgrglnsepv rvlapqtatv agakgagsvd
      421 vdeygrvciv yhwdraaqts arirvaagwa ggekgmiahp rvgsevlvmc ldgnpdrpvv
      481 sgttynaerm ppwalpdqqv ltglrsrelg dagnaaggrs nhvllddtpq qlqlklrsdt
      541 daseltlghn vridntqgrt dqrargfelr tdahgavraa kgllvtsear pdarahatdi
      601 getvarleka hdlheslsss ahdvkaqesg dqdavhqair tqndglkgsg gnpqqgefpe
      661 faqpflafas pagilatttg sthvasdqhv altsgahtsi gagqsmlvsa qeavrvaafe
      721 kgirlvaaaa didiqalkds invlakldvk vdanritita keevlinggt sytrwsgggi
      781 vhgtkgewta haashtfigp dslpvparaf pgtacapcmv naasmaspfa aka
//
LOCUS       WP_176041619             240 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia stabilis].
ACCESSION   WP_176041619
VERSION     WP_176041619.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..240
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25228
     Region          2..236
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mdkvilitga ssgigegiar algapgvklm lgarrtdrld aiardlratg aavetcaldv
       61 tdrrsaqafa daaleawgri dvlvnnagim plsplvaghh dewdrmidvn ikgvlwniaa
      121 vlphmdargt gqiiniasig alsvvptaav ycatkfavra lsdglrqehp alqitcinpg
      181 vveseladti thaptqafmh eyraialqps digravrhvi elpasvsvne ltirptgqvs
//
LOCUS       WP_176041650             375 aa            linear   BCT 11-JAN-2025
DEFINITION  J domain-containing protein [Burkholderia stabilis].
ACCESSION   WP_176041650
VERSION     WP_176041650.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10154716
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..375
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=42351
     Region          <152..>239
                     /region_name="Borrelia_P83"
                     /note="Borrelia P83/100 protein; pfam05262"
                     /db_xref="CDD:114011"
     Region          202..250
                     /region_name="DnaJ"
                     /note="DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock
                     protein 40) proteins are highly conserved and play crucial
                     roles in protein translation, folding, unfolding,
                     translocation, and degradation. They act primarily by
                     stimulating the ATPase activity of Hsp70s; cd06257"
                     /db_xref="CDD:99751"
     Site            order(226..228,237,243..244,247..248)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
ORIGIN      
        1 mtarrgaavv iapshetasl skaqktfntl vkeiekrrer lgawdavmpa fqkkfvdgll
       61 pleqastalr iellhrldda flqkglskae qrtlseliag marnlldvsd daqlkgiydr
      121 hratgyddka aaapepakpa pepaprveaa ddldslspde laarmqaeqd eqfrrdmaah
      181 eareaqrakr kkapkqsaaq akreaeqaes srsirevyrk lasalhpdre tdpreqerkt
      241 vlmqrvnlay akgnllqlle lqleieqidr raidglgeer ltryngiled qlreldqeiv
      301 hvetgfrrty giapsvkvap dtvvrmltrd iagmqrsnhd lsvvlrefdd pekvrdwlkd
      361 vkrqhassrf dddpf
//
LOCUS       WP_176041652             163 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia stabilis].
ACCESSION   WP_176041652
VERSION     WP_176041652.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 163)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..163
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=18266
     Region          11..142
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04688"
                     /db_xref="CDD:467570"
ORIGIN      
        1 misfdagshr fnlraaaviv qreyvllhrv dgddfwslpg grvepgepaa htvvremree
       61 igasvraekm lciaenfyth agrqhhevgv yftaeleags plsdvttahr gaeadkgltf
      121 awflrdrlse idvqpaflre llnadrhtla hvvqqdehye iay
//
LOCUS       WP_176041663             452 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia stabilis].
ACCESSION   WP_176041663
VERSION     WP_176041663.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..452
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=48369
     Region          16..434
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mdnitpnlat draprmpriv ivgggagglq latrlgdtvg rrgqaevvlv drypthfwkp
       61 llheaasghr dpashtieya aqakrhgfrf vqgalqrvdr aartatiaav qdadgteilp
      121 qrelgyddlv lavgsvtnff nvpgaarhal plenldqaed frrkflaact kanhlaeqhp
      181 arraapicin vigagatgve laaalrhaiq qlttyrfkal vsardvhirl ieggprilpa
      241 lderlsgkmh aqlralnvdv ltdtrvaevg adavttatge rlasditiwa agvagpailr
      301 eigdialnrs nqvivtdtlq tpddphvyaf gdcaacpsag asgflppraq vahqqavylv
      361 nafarrvagk pvagftfrda gtvvslgqag avyqadvgar srslivdgla aiglykflyr
      421 khlfsvvglk ralfqslshw lqsrnqpsik lh
//
LOCUS       WP_176041690             295 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176041690
VERSION     WP_176041690.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..295
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31467
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mlldnlelfl rivekgglaa agrevglspa tvserltale rhygaalltr ttraisltde
       61 grtlvagarr llaeadeles rvrlgvqtls gpvrlsapad lgrervvpvv daflgehpgv
      121 tvdlhlgdgy vdlvgqgldf airrgtlads slrsrslgra rrvvcaspay laahgtprhp
      181 ddlaahdciv mrfgldlyae wpfnidgelk rvmvrgrrva ndgalvrawc iaghgvalks
      241 lvdveqdlas galvevlray spgdvdlqiv ypgsaaqprr vralidrlaq alaga
//
LOCUS       WP_176041702             210 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia stabilis].
ACCESSION   WP_176041702
VERSION     WP_176041702.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22078
     Region          2..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 midlstlalf sgaclaltat pgpdmllias rsvsqgrrag fatlagiqag tychalaaal
       61 glsqlflalp vaydvvrfag aayllylawk tfrsnptals pvasqrryss aaifrqgltt
      121 nllnpkmalf vlalfpqfvr pehgsiavqi lvlatvlnli gllvngaviv sasrlsqrig
      181 arrrpsklpq yllgtvfvgl aarlavagrn
//
LOCUS       WP_176041764             339 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-quinone oxidoreductase [Burkholderia stabilis].
ACCESSION   WP_176041764
VERSION     WP_176041764.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10143004
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..339
                     /product="NAD(P)H-quinone oxidoreductase"
                     /EC_number="1.6.5.5"
                     /GO_function="GO:0003960 - NADPH:quinone reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0070402 - NADPH binding [Evidence IEA]"
                     /calculated_mol_wt=35598
     Region          1..333
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            order(40..41,127,131,134,157,160..162,181..182,186,201,
                     225..226,247..248,250,272..274,322,327)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
ORIGIN      
        1 mkaieitefg apdvlklaer prpepkrgev likvaasgvn rpdvfqrkga yapppgasdl
       61 pglevageiv ggdlsdaaln pfglklgdrv callagggya eyavvplpqc lpvpdgltdi
      121 eaaslpetff tvwsnvfdra qlgageggeq etllvqggss gigvtaiqia halgfrvfat
      181 agtadkcrac ealgaerain yktedfvevv kslthdrgvd vildmvagsy vprelsalad
      241 ggrlvliall ggakaevnlg eilrrrltvt gstlrprpve fkariaaqlk vrvwpliadg
      301 rikpviyrvl paaeaaqaha lmessehtgk ivldwgtna
//
LOCUS       WP_176041789             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176041789
VERSION     WP_176041789.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33402
     Region          8..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(104,108,151,165,167,226,243,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(105..106,110..111,113..114,117,121,123..129,194,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mddflsphla lfvdvvdqqs fsaaarrlgv aassvtrrid rleaqlgirl lhrtthalrp
       61 teagqllyer amrmlaelrg lqedlhsqhd epsgllrvdc papfgrlhlm aalaafmqrh
      121 palqvdlmlt dsmvdlqgar lgadvdlavr igpledsrfv atvlapqrrv lcasaaylar
      181 rgepespdal aghdclawhg apppgawrfd grrhvpaqpr frsnhseall eaaidglgla
      241 hlptwlagda lrdgrlravl pqyatapepa tihvlrqqar gsarasrlva flatwfaqpa
      301 wdaawa
//
LOCUS       WP_176041815             375 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Burkholderia stabilis].
ACCESSION   WP_176041815
VERSION     WP_176041815.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 375)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466462
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..375
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39640
     Region          50..366
                     /region_name="RepA"
                     /note="RecA-family ATPase [Replication, recombination and
                     repair]; COG3598"
                     /db_xref="CDD:442817"
ORIGIN      
        1 mnlvtstaqt qadatilpla kpaptskpep asdgvivvng asmhpqpmnw lwdgyfacgk
       61 mtllagepgt gkttiamsig atvtqggiwp dgtvaeagni viwsgeddpr dtltprlmaa
      121 gadmnrvyfv tgtriegkvk cfdpardmpa lketcekign vrlliidpiv savsgdshkn
      181 tetrralqpl vdlaasvgaa llgithfnkg kagsnpaqwv ngsvaftava rvvliaakvk
      241 rdsdedirif araksnigpd dggfeyqieq cepaagvpss ciawgdevsg sahellgnqe
      301 knegrgssav dsareflael lsagdipaka ieadaeqagi alrtlrrasd alrvekykgk
      361 dskwywslpe lanre
//
LOCUS       WP_176041833             797 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia stabilis].
ACCESSION   WP_176041833
VERSION     WP_176041833.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..797
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=87218
     Region          25..742
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mpmqsttpts pppapepkkr pwwqkvllgf aamcvalvva gglvlgyalv vawpnmpsld
       61 altdyrpkvp lriytsdhvl igefgeerrd vvhfkdvpds lkkailaied arfydhggvd
      121 ltgivragfv altnghasqg astitmqvar nfflssekty trkiyemlla yrieraltkd
      181 qilevymnqi ylgqraygfa saarvyfgkd lkditlaeaa mlaglpkaps aynpvvnpkr
      241 akvrqeyilq rmlelnfitr eqydeavaqp lvvkgpgrdf svhaeyvaem vrqmmyaqyr
      301 eetytrgfnv vttidsadqq vaytalrkgi mdyerrhgyr gpegfielpa gaddreqaid
      361 dallehpdng eliaavvtaa sprqitvafi dgsnatidgd nlrfasgals anaqpnrrir
      421 pgaivrvvkn dagkwsitql pqvegaflsi vpqdgairsl vggfdynknk fnhvtqawrq
      481 pgssfkpfiy sasldkglgp atvindgply fsaaetggqp wepknygggf egpmsmrtal
      541 qrsrnlvsir ilnhigtkya qqyitrfgfd aerhpaylpm algagqvtpl qmagaysvfa
      601 nggyrvnpyl iaevtdpnga ivaraqplva eqnapraida rnayvmnsll qsvaqrgtga
      661 rtnvlkrtdl agktgttnds hdawfagyqh tlaaiawigy dnprslgdre tggglslpvw
      721 idymgaalkg vpefkptvpd gveslggely fadftpghgf vstvgvpqvp aaqnvdeavp
      781 hvdeqekqdi mnlfrgh
//
LOCUS       WP_176041878             302 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia stabilis].
ACCESSION   WP_176041878
VERSION     WP_176041878.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..302
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=32171
     Region          6..274
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 maldrsarpe rtafvfaggg slgaievgml rellnhgerp dfvvgasaga inaayfagqp
       61 dgdgvaklea lwcnirrrdi mpfsmlgllr tvlqnrahlv eatalrmlle rhlryqyver
      121 aslplhvvat dmlsgneivl ssglvvdavl asaaipgvfp pvriddrlmv dggvanntpi
      181 siavargatr ivvlpagfac alrkppasai aqamhaltlv iarqlvrdla fyqsraaicv
      241 vpplcpldvs pydytrckel ielaaertra wlgegglgqt fipgalheht hsaerptcda
      301 ga
//
LOCUS       WP_176041892             218 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia stabilis].
ACCESSION   WP_176041892
VERSION     WP_176041892.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 218)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..218
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24505
     Region          1..217
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 mirlsqvrkt yqtksgprtv ldgvdvdias gekigilggn gagkstliri isgaerptsg
       61 rvhrgmsvsw plafggafqt sltgidnlrf icriydvsve dklpfvheft elgrylnepi
      121 ktysagmrak lafaismavd fdcflidevt avgderfrqk chvelfekrn sramifvshd
      181 pgfirancqr atvlhrgkly efpemdeayh fyremqrv
//
LOCUS       WP_176041895             203 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia stabilis].
ACCESSION   WP_176041895
VERSION     WP_176041895.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..203
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22636
     Region          1..203
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mkligslgsp yvrkarivla ekkidyklel envwapetdi hasnplgkvp clvmedgaav
       61 fdsrviceyv dtlspvgkli ppsgrervev rcwealgdgv ldaavairle htlrdeaqrs
      121 aswiarqqrk iddalvamsq glggktwcvg nhytladial gcalgyldfr mpelnwrdrh
      181 pnldkhfvkl mqrqsfvdtl pqn
//
LOCUS       WP_176042022             288 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia stabilis].
ACCESSION   WP_176042022
VERSION     WP_176042022.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..288
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=32044
     Region          5..277
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mfdqivfagg gnrcwwqagf wdvaqpalgl rprvitgisa gaatacmlyt rdaawvmryy
       61 eealrhnrkn aywgnlfgre pvfphyriyr qalldiygep faklaaapei rigvshvprw
      121 lgarsavaag lvayniekyv rktlhptlgr slgfrpefvr aqactqvdel adlilqssct
      181 ppftpvlrrg grpvldggmv dnvpvdaldp spgdvlvlvt rlyprpqmft vahgdqrrly
      241 vqpsskvpis swdytspsqm rhaydlgrrd gehfltrvda mtggrvaa
//
LOCUS       WP_176041968             519 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia stabilis].
ACCESSION   WP_176041968
VERSION     WP_176041968.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..519
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53875
     Region          16..465
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(23..24,27..28,31,63,113..114,116..118,121,142,
                     145..146,149,273,276..277,280..282,285,313,317,371..372,
                     376,380,396,399..400,403..404,407)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msvdvslknk ialaaiclsa vmlgleitsv psilptlehv lpadfkqlqw imnaytiamc
       61 sslvamgala drfgrkrvft igivvfgias licglassap lliaarflqg vsaaamlscq
      121 vavlshqfqs gpergvafaw wgvvfglglg fgpivgglia sfanwewvfl ihvliavlav
      181 slaragvves sdphalkidi ggmatlslsv fclvylitqg qkpevgnpvg mgalaiavvs
      241 filfvvvenr varpmfdfka frvrnfsgal lgacgmnfsf wpfviyfpiy lqavlgyssv
      301 aagltvlayt lptvvvppva erlllkrgpn fvipvglfti aagfllihlv ataghaswit
      361 llpgclvagi glgltntpvt ntatgslppe ragmasgmef sarmislain iaimgfvlvk
      421 gvsagvadal palaqsrhlv davsagnfva adaggipvav graaltrgfg wvtlygtiap
      481 lllgfaaaiv fgrkkpapva tndersgadd kqpaltsid
//
LOCUS       WP_176042085             383 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia stabilis].
ACCESSION   WP_176042085
VERSION     WP_176042085.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..383
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41753
     Region          6..382
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mirdqetlng lldsiarfvr erlvpneehv adtdeipddi vadmkamglf gltiperfgg
       61 lelmmeeevl avfelcqasp vfrsllgttv gigsqgilfd gtpeqqekyl prlatgelia
      121 sfaltepeag sdaaslrtta irdgddyvvn gtkrfitnap hagiftlmar tnpedkgsgg
      181 isafivdakt pgisfgkrdk kmgqkgahtc dvifdnvrvp aanliggkeg qgfktamkvl
      241 dkgrihiaav cvavaermls malsyamerk qfgkpiadfq lvqamladsk aeiyaarcmv
      301 vdaarrrddk lpvsteasca klfasemcgr vadravqifg gagymseyai erfyrdvrlf
      361 riyegttqiq qiviarnmvr daq
//
LOCUS       WP_176042099             429 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia stabilis].
ACCESSION   WP_176042099
VERSION     WP_176042099.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..429
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46237
     Region          14..417
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(27..28,31..32,35,67,117..118,120..122,125,145,
                     148..149,152,252,255..256,259..261,264,291,295,345..346,
                     350,354,370,373..374,377..378,381)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mhsleqvtma kvfrrlvpff mlcyfisfld rvnvgfaslq mndaigltpa qyglgsglff
       61 llyflfevps nlllvrvgtr iwiarilitw glisgatafv agpwsfyavr lllglaeagf
      121 fpgvaycitl wfpsayrarv mgyllvaapl ssvigspisg mllglrgldg lgglqgwqwm
      181 flieaapavv lgfvtlrylk gsprdahwlq aderewlaar mtsednrrrg ehgvpvarvf
      241 sdrrvwmlaa mafgffltiy gigfflpqiv ksfgltnvqt gfvtaipyvi gsaslvfwar
      301 radrtgerrw niaipaliaa aalvgaglid apvlklgcfc vlafgvfgal pafwaintdl
      361 lsgaaaaasi awigavgnlg gfagpyllgv tkdrtggyta alllmavvav iaagialsvg
      421 rqrrtyhpa
//
LOCUS       WP_176042120             410 aa            linear   BCT 11-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Burkholderia stabilis].
ACCESSION   WP_176042120
VERSION     WP_176042120.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..410
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43543
     Region          5..363
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 minprdsivs lagvvagqia lfacifvigr rfgpeslghf nyllalatfa gtllalryel
       61 acvddapges fnafvnvsal slvatagfgi viavasrtdl qlvavyalas fvqlaagsyl
      121 nslrrygwia lsrvvingaf laglvlslac pacghvdvfa lyawvtaavs ivmaaailfs
      181 gyragysfrl srgffvrnrr falyilpstl casvltyals iaiphwfdaq sagyfaaayr
      241 lgffpvslia qsvggvfrrd aigamagpda gttvprvyrt yaralavlaa vymagglllf
      301 aplvdlffga swrgsvgfyh slmplfalql iyvplsqifl atraqridfl fqltsgacla
      361 galgiarlmn lsaqtsvqif sltgavlmaa gialtyrvld tnlsrfrala
//
LOCUS       WP_176042133             320 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia stabilis].
ACCESSION   WP_176042133
VERSION     WP_176042133.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..320
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34552
     Region          10..223
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(51..52,54,68..70,76,78..79,120,222)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(51,53..54)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(76,79,82,89)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(112,116..119,121)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(117..118,141..143,195..196)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          237..320
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 midgltvrva akhdeaadic sfelvradgl plppfsagsh idvivpggpt rqyslcnapd
       61 enhryriavl rdpksrggsa gmhdrvnagd tltisaprnh falapgaths lllaggigvt
      121 pilcmaerla ridasfdmhy ctrsrprtaf ldriarapya grvqvhfdde adsqrfdiaa
      181 rlavpepgth lyvcgpkgfm davlttaras gwpeaqlhye ffaaderqkd qdgrfeveia
      241 ssgrvivvek nesvvqalak agieietsce qgvcgtcatr vlagepehfd lcltpderaa
      301 ndqflpccsr sksarlvldl
//
LOCUS       WP_176042149             304 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia stabilis].
ACCESSION   WP_176042149
VERSION     WP_176042149.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..304
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=33830
     Region          26..278
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mqnphslpdy llqsdavrer farlkardvi ldvrhlgkrf rspqgevval ddisfrthrr
       61 efvcvigpsg cgkstliril aglesqtsgd vlldgkpvqg pgadrgmvfq gytlfpwltv
      121 kknvmfglkr ngsgngeaer ealqwldlvg ltrfanvyph qlsggmkqrv aiaralanrp
      181 rillmdepfg aldaqtrakm qahlldiwrn idvtilfith dldeaillad rilvlkanpg
      241 evqelievpv prprgysqln tpefiatkar lealihpept geapdedavr phmirmtdvt
      301 dnve
//
LOCUS       WP_176042165             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176042165
VERSION     WP_176042165.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33696
     Region          17..74
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          103..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(113,117,156,170,172,231,248,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(114..115,119..120,122..123,126,130,132..138,199,
                     225..229,236..237,240)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mssdpvpcpn kpldlldval fvraallanv taagrefgvs aavasariaq lerqlgarll
       61 hrttrrislt qdgeifmtra dallsaadaa rasvghgrse pygrlkvsms ssfgrqhvap
      121 vipaflrryp svsldlrlsd eivdlvddgy dvairlgalk dstlvarkla anrrvlccsp
      181 aylaergtpr hpadlaqhec vilgdqrdws fttpqgpltv rvggrlvasn geairealvd
      241 gfgiaikstw dvgpllasga lvtvlddypf addvaiwavy psrahvplkt lvfiaflaeh
      301 fgdppywdhv dgr
//
LOCUS       WP_176042169             308 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Burkholderia stabilis].
ACCESSION   WP_176042169
VERSION     WP_176042169.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..308
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32215
     Region          7..272
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(34..35,38,90,103,105,134,167,253,256)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mtaafpeila lgeamiefnq sqpgrpeflq gfggdtsnfc iaaarqgasa gfvsaigddp
       61 fgrlladmwh vehvdttyvr idraaptgvy fvthgasghq fdylragsaa sryaagdlpl
      121 dalaaakavh lsgislaist tacdaafaai dharrngakv sfdtnlrlkl wplpraravm
      181 realrqtdic lpswddvtal tgandrdaiv damlehgpqv valklgkega yvatpnerrv
      241 vpgftveavd atgagdcfgg afiarivagd dpfaaaryan aaaalsttgy gavapiphrd
      301 averlmqg
//
LOCUS       WP_176042196             558 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 39 protein [Burkholderia stabilis].
ACCESSION   WP_176042196
VERSION     WP_176042196.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14304616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..558
                     /product="glycosyltransferase family 39 protein"
                     /calculated_mol_wt=62580
     Region          24..375
                     /region_name="ArnT"
                     /note="PMT family glycosyltransferase ArnT/Agl22, involved
                     in glycosylation of proteins and lipid IVA [Cell
                     wall/membrane/envelope biogenesis]; COG1807"
                     /db_xref="CDD:441412"
     Region          450..555
                     /region_name="Arnt_C"
                     /note="Aminoarabinose transferase C-terminal domain;
                     pfam18583"
                     /db_xref="CDD:465810"
ORIGIN      
        1 mndtpsrlpl nritlvlllv alaivwfapl glrhlipsde gryaemarem fvtgdwitpr
       61 yngykyfekp plqtwlnalt fawfgigewq arlytalasf agvllvgytg arlfnplsgf
      121 laavvlasap ywnlmghfna ldmglafwma lslcslllaq rpglrpaavr gwmwacwaam
      181 afavlskglv glilpgavlv lytliardwa lwkrlylvsg lviffaivtp wfvlvqqrnp
      241 effnfffvvq qfrryltpeq nrpgplyyfv pvllvgflpw lsvvwqsirh alrmprqpng
      301 fspmlvlliw safiflffsa shsklisyvl pvapalalii gaylplmsad rfrrhllgyl
      361 vffvvaafgi iflayqgdar tpnalyrafq mwlyaglavs aaltlaaawl nrragvaaal
      421 aafgaawlaf gtiggtghde fgryssgall apavraelak lppdtpfysi emldhtfpfy
      481 mghttimvqr qdelafgisv epnkwvptvd ewitrwkqet halaimppgq ydalvkqgvp
      541 mrviahdnrr vivekpqs
//
LOCUS       WP_176042221             402 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia stabilis].
ACCESSION   WP_176042221
VERSION     WP_176042221.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..402
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40518
     Region          15..334
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mktlspdavl ppdgrasgfa rstlvalvvf aaitpllllv apavagqlat qlglsasqig
       61 tyffvelgaf slatapsylw lgrvdarrva acaialfgag nlltalwmpg faallalrav
      121 talgggslmv lcmtsaatse nsdrvyglwv vgqliagaig lfvlphvfaa fglralyval
      181 aalallaapl srgfpsslga rtasaptayg nathvprhfv alaigavltf ylaigsvwtf
      241 asraaaeagl dpqsagnvla iasvmgiaga alascaggrl arrvmlaagy allatslval
      301 aamrhaggyg aaifafkfaw tfvlpfilat vaqidtsgrl vatlnfviga glaagpllag
      361 lmldaggtmh alfagatava ivsyaalrhi drrahpsvss qp
//
LOCUS       WP_176042199             375 aa            linear   BCT 11-JAN-2025
DEFINITION  C40 family peptidase [Burkholderia stabilis].
ACCESSION   WP_176042199
VERSION     WP_176042199.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..375
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=38468
     Region          <6..175
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 msriwvpvav vsllaacssv ppqsasrepg mkittprafp apanfpkfvd hsvgqeeisi
       61 qamslvgvpy rwggntptsg fdcsglvryv igraadvnlp rttadmsgrg vsiepdqvap
      121 gdliffnttg rphshvgiyv gklrfvnaps tggtvrldyl tnpywakrfd girrvappra
      181 tptpfdapty earrdapaap aapvataras aapaprpavv aarpvtapap vvaaapaptp
      241 rvaaadpfep pppriaaaqq qaesagaisp pfatssagnd rpaqpseppv tsagttipti
      301 aiqpsdslaa agdkfepppa araaaqqaws nepaaapapp tapvqvmras tqsapiraat
      361 gtaddpiarf angsy
//
LOCUS       WP_176042237             492 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA recombination protein RmuC [Burkholderia stabilis].
ACCESSION   WP_176042237
VERSION     WP_176042237.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..492
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=53895
     Region          <37..>238
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          154..492
                     /region_name="RmuC"
                     /note="DNA anti-recombination protein (rearrangement
                     mutator) RmuC [Replication, recombination and repair];
                     COG1322"
                     /db_xref="CDD:440933"
ORIGIN      
        1 mtmtlllaav vvlavalava ivaivrgggr hddaavlgdq iedaahaqar averlerelr
       61 geivenargs rtelagsftq lqqtlaaqlt svatvqnnqi egfaqqlgkl vagnaqqfda
      121 mresvqrqaq qareeqtgal rlfgdtlnrq ltqlteandr rigevratle qrlkeietnn
      181 aakleemrrt vdeklhatle qrlgesfklv sdrleqvhrg lgemqtlaag vgdlkkvltn
      241 vktrgtwgev qlealleqml tpdqyaknva tvpksterve fairlpgrda gtrdappvwl
      301 pidakfpred yerlidaqer adaaaveeaa ralearvrle artiaekyvs pphttdfall
      361 flpteglyae ilrrpgltdl lqrdyrvtva gpttltalln slqmgfrtla ieqrssevwq
      421 vlgavktefg kfgdvlartk aqletvtrsi esaeqrtrvm srklkqveal pgdtaagllg
      481 aegndgadad da
//
LOCUS       WP_176042285             294 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia stabilis].
ACCESSION   WP_176042285
VERSION     WP_176042285.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..294
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31394
     Region          12..263
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 msasiktllt presdignlv vrrvlparaa rlvgpfiffd emgpavlpag rgidvlphph
       61 iglatvtylf dgslmhhdsl gfrqkivpgd vnwmtagrgi vhserspded rpreqpvhgi
      121 qtwvalpveh edtapafvhh aadtlpsftr dgasvrviag safgltspvd vfsptlyaya
      181 efaaggtlal daehdergvy lvdgdltldg tplaaatmav lepgatvala sangarvmll
      241 ggahlpgerf iewnfvsser akidaaraaw aaqtfgkvpg eenewtrqpe rkaq
//
LOCUS       WP_176042261             506 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Burkholderia stabilis].
ACCESSION   WP_176042261
VERSION     WP_176042261.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..506
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53679
     Region          13..490
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(70,72,76,79,83,116,119..120,129..136,141,144,147,
                     240,244,247,250,252,426,428..429,431..432,435,438..439,
                     441,443..446,455,459,461,475,482..487,489..490)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(156..159,167,182,185,215,232..235,238,256..258,290,
                     391,393,419)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(159,256,287,290)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnpvpaytsd advghyvdga pvagrsgrfq dvlnpalgra vrrvaladgs evqqavasan
       61 aafpawaatp pirrarvlhr flqlmnehrd tlaaiitaeh gkvfsdaqge vargidiief
      121 acgvpqllkg dftdqvstgi dnwtmrqplg vvagitpfnf pcmvpcwmfp vaiatgntfv
      181 lkpserdpsa alfiadlltq aglpagvfnv vqgdkgavda lldhpdvqav sfvgstpiaa
      241 yvqqravqsg krvqalggak nhlvvmpdan ieqavdalig aaygsagerc maisvavlvg
      301 dvadkivpav aerarklvig dgmspevemg pivtgealkr iegyieqgvs egaqlvvdgr
      361 glrvpgreag fftggtlfdh vtpemriyke eifgpvlgcv rvkdfgeavd linahefgng
      421 vscftsdggi arefarriqv gmvginvpip vpmawhgfgg wkkslfgdmh aygeegvrfy
      481 trqksvmqrw sssigkgaef amptak
//
LOCUS       WP_176042294             275 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176042294
VERSION     WP_176042294.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Santos,C.L., Tavares,F., Thioulouse,J. and Normand,P.
  TITLE     A phylogenomic analysis of bacterial helix-turn-helix transcription
            factors
  JOURNAL   FEMS Microbiol Rev 33 (2), 411-429 (2009)
   PUBMED   19076237
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..275
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30339
     Region          90..275
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
     Region          <217..275
                     /region_name="CitB"
                     /note="DNA-binding response regulator, NarL/FixJ family,
                     contains REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG2197"
                     /db_xref="CDD:441799"
ORIGIN      
        1 mhlappapts hggpvigvrp qtlgnairaa gtagfadava rfvneslvtd aihlerwrpd
       61 pgaasgylie wlgswgdryq elcalmdayy rdfwqtdplv epvrgttgtv llqrhvgglp
      121 dgdfrrrffd eqrvtqecml vhgnaniqya lsvtrstdqa afsrgelfhl rqmadllfpl
      181 lemharscaa rriapaagpa pshhgfdari arqgvrlsrr eqeickllls grsvpdaatl
      241 ldirhstaet yvkrafaklg vrtrselfdw alidg
//
LOCUS       WP_176042339             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia stabilis].
ACCESSION   WP_176042339
VERSION     WP_176042339.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46066
     Region          13..417
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(25..26,29..30,33,72,130..131,133..135,138,158,
                     161..162,165,247,250..251,254..256,259,287,291,343..344,
                     348,352,368,371..372,375..376,379)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mtqslpsarq pgraataafi gtmiewydfy iyataaalvf gelyfpshdp fvstmasfat
       61 favgffarpl gglifghlgd rigrkkalmt tlmmmgvatv cvgllpdysk vgmlapallv
      121 alrvvqgiav ggewggavlm agehapqgrr tffasfaqlg spaglilsli afravtsmdk
      181 adflawgwrl pflassvllv vgimirlgvn espefarvke anrtvklpva evfrsasglv
      241 llcigantig iagvyftntf miayttqyvg vsrslildsl favaiiqffa qpvaawiaer
      301 iggarflkla allamlspyp mfmlvqggts asliagiala vvcmagfysv iagfvsdvfp
      361 ahvrysaisl ayqicgaiag gltplvgtwl ahrfagqwwp lavfytclag isllsivald
      421 arraaqpaaa ealgsh
//
LOCUS       WP_176042346             437 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrolipoamide acetyltransferase family protein [Burkholderia
            stabilis].
ACCESSION   WP_176042346
VERSION     WP_176042346.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..437
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46954
     Region          2..437
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mgihvikmpd igegiaevel vawhvevgqt ikedqpladv mtdkaaveip spvtgkviel
       61 ggrigemmav gselirleve gdgnlkagap vretkvetap vaatpskpaa dvpaekpaap
      121 rdakrapaap hraepaaqpr aalapgerpl aspavrqraw dmgielryvr gsgeagrilh
      181 edldayarts gsaarpsqah gyderndetd vpviglrrai arkmqeakrr iphfsyveei
      241 dvteleslrt elnrrygdtr gkltplplli ramvialrdf pqinarfdde agvvtrygav
      301 hmgvatqtdg gltvpvlrha eakdvwsisa eiarladavr tnraqrdels gstitisslg
      361 alggivstpv inhpevgivg vnriverpmi rdgavvarkm mnlsssfdhr vvdgadaaef
      421 iqavravler pallfve
//
LOCUS       WP_176042348             308 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176042348
VERSION     WP_176042348.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33438
     Region          15..71
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..298
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(110,114,153,167,170,233,250,277)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(111..112,116..117,119..120,123,127,129..135,197,
                     227..231,238..239,242)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mktahqlksg dlfslnvflv aathlsfraa sieldvtpsa ishsiksleq rlgvrlfnrt
       61 trsvsltdag erlvdklrpa issvaeamls vdglrdapsg tvrinasega irlvlkpvla
      121 rflrdypqvh ldivtdgklg divaggfdag irlaeavpqd miavrvsdpv rfaavaspay
      181 faargrpdvp qdlhrhdcir frfdsgaiyr weferrgvve tvnvsgpltl tdqplmvdaa
      241 idgigiafvp dhlvrealdg grlervltdw cpvmpglcly ypghrhvsgg lralidmlrm
      301 pssgadrt
//
LOCUS       WP_176042352             301 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia stabilis].
ACCESSION   WP_176042352
VERSION     WP_176042352.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 301)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..301
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31704
     Region          35..264
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mqslsgssap spapapahvn gvarraphap ratgarmiaa lqwgvtlllc aflivpvvms
       61 vlagltvnyf rglssgltlr wleqvwqqyh gsvalslyva fatlaivlvv gvpagyalar
      121 sksriaraie ealvlpvalp glasalallv vyggftafrm slwfivvghv vftlpfmvra
      181 vaavaagadl rtleegaasl gasfvtrfvt ivlpnlrpgi vagalavltl sigefnltwm
      241 lhtpdtktlp vgladtyasl rlevgsayti lfllmtlpll vamqwlgvdp sgtralkrrp
      301 r
//
LOCUS       WP_176042408             155 aa            linear   BCT 11-JAN-2025
DEFINITION  nucleoside deaminase [Burkholderia stabilis].
ACCESSION   WP_176042408
VERSION     WP_176042408.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Xiang,J., Xu,W., Wu,J., Luo,Y., Yang,B. and Chen,J.
  TITLE     Nucleoside deaminases: the key players in base editing toolkit
  JOURNAL   Biophys Rep 9 (6), 325-337 (2023)
   PUBMED   38524700
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..155
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17604
     Region          2..136
                     /region_name="TadA"
                     /note="tRNA(Arg) A34 adenosine deaminase TadA
                     [Translation, ribosomal structure and biogenesis];
                     COG0590"
                     /db_xref="CDD:440355"
ORIGIN      
        1 mdfvkrtidl amknveeggr pfatvivrdg eivaespnlv aqtsdptaha eilavrdacr
       61 klgtehltdc eiyilaspcp mclgslyycs pkcviyittr edyapfyrdd rkyfeldtfy
      121 aeyakpvger rlpmvqqkha daigvyrrwk elnak
//
LOCUS       WP_176042396             366 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia stabilis].
ACCESSION   WP_176042396
VERSION     WP_176042396.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..366
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39580
     Region          28..361
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mptqpstpaa slalqdkthd ahashdsraq rylqllllvi aagaiypmly lrqvyqptml
       61 qffriddvql gylysslgti flvsylpsgw ladrlsprwl icfsliatga lglvyatgps
      121 fntlvlifgs wglttgltfw aavikrvnmi agpdeqgrff glldlktlaa ipelwlvaai
      181 vfcgyqvfwa tysfsaylhe gnfglsataa gfittlklwm rpvggigggf lgdrvskvsv
      241 lfwalvlaal slvgliaapp hspqamlvvl vlfigiltya irglywslld dckvpthcag
      301 laiglisvlg yspdvfvpli ngyvtqtypg ahgyqlyfgy iaaialcgag aaaflkyrln
      361 rikesa
//
LOCUS       WP_176042438             321 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176042438
VERSION     WP_176042438.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..321
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34438
     Region          5..320
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpkvvgifav pgvqlldvsa pldvfaqana ecgkpfyalr viagesgpir sssgarllpd
       61 wivpdiperi dtllvagapd aarialrtdv lawlrsaavq srrygsictg afilaatgll
      121 kgrhltthwa aadalaeayp slavdadaly vrdgklrtga gvtagldlal alveedlgre
      181 iarrvaaqlv mffkrpggql qfsrkgearp agrsvlqevq rwiaanpefe hsvaemakha
      241 gmsprhfarl fraevgmtpa awveatrisa arhllenghd tpkqvaakcg fanadtlrrs
      301 ftrhvgitpa eyrkrqavla k
//
LOCUS       WP_176042478             286 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Burkholderia stabilis].
ACCESSION   WP_176042478
VERSION     WP_176042478.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 286)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..286
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30741
     Region          34..286
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mlhavfsarf ssgqparfar parllaaall aavfgvalsn garadtaplk vgistspqie
       61 alkvaakeak aqgldvkiie ftdwntpnaa lankdidvny fqhipflena nkqggynfvs
      121 iapgtimkig lyskkvknfa dlkdgarvai andpvnggrg llllqragli tlkpgvdyra
      181 tthdivanpk hlkiipleas qlarslddvd lvqgypsfik lagtidpnsa llfdgtenks
      241 faiqwvvrpd svndprirkf iaiyqhspav rkaldnafgs lyaiaw
//
LOCUS       WP_176042483             198 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia stabilis].
ACCESSION   WP_176042483
VERSION     WP_176042483.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21518
     Region          6..158
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrysvehkhe trarildaas rlfrqegygg sgigpltkaa gvtngafygh fkskgeafrs
       61 vvldgldqlr qgvarfkaeh garwrrpfvs fylgprrtce lgescalpsl spevmradde
      121 trdayeqalr qivdevasgl gdtpdddrai aflallsggv tlaravrdpa laeriadavg
      181 ryavviaert dvqpeqqa
//
LOCUS       WP_176042486             196 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia stabilis].
ACCESSION   WP_176042486
VERSION     WP_176042486.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..196
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=19990
     Region          4..196
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mndflfglmi alsvgpvalm ianygmragt atgvraavgv aaadgcyavv aftigamlag
       61 tlashlsmfr fvgalvllam garmlwqalk drrrtldgda plpgnrpfts mfvvtlanpl
      121 tillfygyat aaagaqrhwl agaacvfags lagqlvfafg gsligrivks pgwlaashvv
      181 aalvvlgygv aglvra
//
LOCUS       WP_176042520             163 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia stabilis].
ACCESSION   WP_176042520
VERSION     WP_176042520.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 163)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..163
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17761
     Region          27..158
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mnasapaasp saadldwrwk sfdaltarei ysilearsav fvveqncvyr diddadqdaw
       61 hlaafdptgr lagylrvllp daqntdvrig rvlttaafrg aglgngllsr alehiraqwp
      121 dtpvslhaqa hlqrfygafg ftpssdvhde dgiphvwmss ara
//
LOCUS       WP_176042526             499 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Burkholderia stabilis].
ACCESSION   WP_176042526
VERSION     WP_176042526.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..499
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53492
     Region          5..471
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mnlhslnsls avdarrliag rqispvelld aciaqmervn phvnalaatr fdlarseara
       61 aeqavmrget lgllhglplg vkdleetagm lttygsphfr nnvpshdnal varlraagai
      121 ltvktntpem gagantrnav wgatgnpfaa elnaggssgg aavalatdml pvctgsdtgg
      181 slripaalcg vvgfrpspgl vpsdtrllgw spltvagpmg rtvadtrlql atmvglhrge
      241 plgiecdsrs ildaqgidps tlrvgytedf gacdvsndtr qtfrakiaal shhvgvcepv
      301 nfelgevdrc fdviraqnfi aglkdiyerd pdllgqntra nyemglamsi sdvvwahaeq
      361 trifrrfqpi fddydviasp tcsvspfpwq qaslteidgr plenyyrwlg vtyvvslvtn
      421 pslslpagtd hadmpfglqf igpqrsdrrv ldiaqaleev fardeslkrp apdiarlmas
      481 haalksivtd ppddsvayr
//
LOCUS       WP_176042557             271 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia stabilis].
ACCESSION   WP_176042557
VERSION     WP_176042557.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..271
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29091
     Region          19..265
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtdaarhatd gdmiyatvdl tlkagertll dgfthafrpg eiwcvagpng agkttllatl
       61 aglqppaggr veidgrplga wlpaplaqrr almpqqlhda fsatvfdtvl lnrfpylggw
      121 gwerdgdraa ardalatlgl talasrdvls lsggerqrva laatlcqdap lmlldeplah
      181 ldlhhqidcl talaawldag prtvlfschd lnlarrfath allldgrgqa wagpvydvlt
      241 perasdafgy plvlirengr dallpawper q
//
LOCUS       WP_176042569             454 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia
            stabilis].
ACCESSION   WP_176042569
VERSION     WP_176042569.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..454
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=48488
     Region          159..437
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 menlqnrlls hrlasvirdf hqpvmiwqaa ilvgalcfaw vaarfvhgri darrraagra
       61 pgagaqslkr alfplfgglf vgaaqlafdp fmstsllsla lvplfgigli yvlfffarrv
      121 fardghthaw lsivekivst vvwaamvltv lgiqrdviaw ldsvqfrvan ahltlmslis
      181 galwvcvtlm vamwlgsvle erlarastld anlkvvlsrv grallvfaav liglslvgid
      241 vtvlgvfgga vgvglgfglq kiasnyvsgf iilldrslrl gdaisvgglq givtqirtry
      301 tvvrgldgne tlipneklit dvvqnqssyl trgyakvavq vaytsdveha lalladaakg
      361 vprvltepap tpylvsfgad gidlelgfwi edsakgtsgv rsavnrniwr lfsehgisip
      421 fpqrevrvvg lpdgfpatna tagdgaadgr apaa
//
LOCUS       WP_176042592             294 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia stabilis].
ACCESSION   WP_176042592
VERSION     WP_176042592.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..294
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30572
     Region          3..286
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mqtavgfigl gvmgtpmaln laragtpliv wsrsngsdda lrdagarvae rpddvfaacr
       61 tvilmlanda aidavlgrgt pdfaarvgah tivnmgtnsp eysraladei aaasgryvea
      121 pvsgsrkpae tgqlvvmlag apddvdavrp lvkplcrdsf vcgdvpsalt mklavnlfli
      181 tmatglteat hfaqqhgidl arfadvlnag pmasdvsrvk lgklvaadfs vqaaitdvlk
      241 narlvaesar sigiasplld ichalysete qaghgsddmi avihaieqrt aner
//
LOCUS       WP_176042594             330 aa            linear   BCT 11-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Burkholderia stabilis].
ACCESSION   WP_176042594
VERSION     WP_176042594.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..330
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=34943
     Region          <9..324
                     /region_name="FAD_binding_2"
                     /note="FAD binding domain; cl46878"
                     /db_xref="CDD:481218"
     Site            order(34..35,38,41..42,66..67,70,73..74,97..98,101,
                     104..105,108,128..129,132,135..136,159..160,163,166)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          48..74
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          79..109
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          113..136
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          140..166
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          180..232
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          299..325
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mtvsspavpl pgaldpdhda lvarlaapda svrriallel adledpdlvp sfvaalrddp
       61 sadvrgeaar vlgaweqpdv vdalcralld pdddvrataa qslselkdaa sgtvlcgwae
      121 rpesfvrgav lrglrelrdp dafapalral dadtsavrae avavlgwlrd rralsplari
      181 vtadvdadvr rvavgalgfa apddttvita llaalrdaew qvreesagtl gklrvalard
      241 plvaaldddy wqvrlrtvra lgqlrdtaaa pavaallaht isnlrkeaal algelrdagt
      301 lpalhdaled rdpevrkavr iairqigetq
//
LOCUS       WP_176042599             403 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia stabilis].
ACCESSION   WP_176042599
VERSION     WP_176042599.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..403
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41505
     Region          8..390
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(18..19,22..23,26,61,108..109,111..113,116,139,
                     142..143,146,221,224..225,228..230,233,263,267,316..317,
                     321,325,341,344..345,348..349,352)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mpdsryrwvi vaagglmgci aigamfslpv flrsiardtg wsmtgisgam tlgfiamafa
       61 smawgslsdr igtravvvtg avllsaslal asrapsllaf qltfglavgg ataavfapmm
      121 acvtgwfdth rslavslvsa gmgmapmtms plaawlvsah gwrtsmllia alaaavmipa
      181 sllvrrapal dgthaaappa gapgamsvwd alrspqfmvl lltnffccat hsgpifhtvs
      241 yavtcgipli vavsiysveg lagmggrivf gilgdrigak rmlvtgllaq algalgyyfv
      301 rtldgfyava tlfgfiyagv mplysvlare nfplrmmgtv iggcamagsl gmaagpvagg
      361 livdtfgsyg wlyigsfaig vgafliammf rpfaktrpdt vaa
//
LOCUS       WP_176042621            1049 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia stabilis].
ACCESSION   WP_176042621
VERSION     WP_176042621.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..1049
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114779
     Region          11..1027
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msvsheegrf nlsawalrhq alvvyliala tlagilaytr laqsedppft frvmvirtfw
       61 pgasarqvqe qvtdrigrkl qetpaidflr sysrpgesli fftmkdsapv kdvpetwyqi
      121 rkkvgdigyt lppgvqgpff ndefgdvytn iwtlegdgft paqlhdyadq lrtvllrvpg
      181 vgkvdyfgdp dqrifievnn aqltrlgisp qqlgqainaq ndissagvlt taddrvfvrp
      241 sgqfdnvdai adtliringr tfrlgdlatv krgyddpvvt qmrangkavl gigvtmqpgg
      301 dvirlgkald aeskdlqaql paglkltevs smphavahsv ddfleavaea vaivlvvslv
      361 slglrtgmvv visipvvlav talfmymfdi glhkvslgtl vlalgllvdd aiiavemmav
      421 kleqgytrar aaafaytsta fpmltgtlvt vsgflpiala ksstgeytrs ifevsaiali
      481 aswfaavvli pllgyhmlpe rkraaheahl pddhehdiyd trfyrrlrgw idwcierrfv
      541 vllitgalfv vslmgfslvp qqffpssdrp ellvdlrlte gasfaatlre terlekvidk
      601 rpeidhsvnf vgsgaprfyl pldqqlqlpn faqfvitaks vedreklatw lettlrdqfp
      661 avrwrlsrle ngppvgypvq frvsgdsiat vrsiaekvaa tmrgdartvn vqydwdepae
      721 rsvrfeidqk karelnvtsq dvssflamtl sgttvtqyre rdkliavdlr apkvdrvdpa
      781 klaglalptp ngpvplgslg rfkptleygv vwerdrqpti tvqsdvraga qgidvthavd
      841 aklnalraql pvgyqinigg sveesakaqk sinaqmplma iavftllmiq lqsfsrvlmv
      901 vltaplglig vvatlllfgq pfgfvamlgv iamfgiimrn svilvdqieq diavghgrvd
      961 aiigatvrrf rpitltaaaa vlalipllrs nffgpmatal mggitsatvl tlfylpalya
     1021 twfrvkrder dpqdgpphgg stpaapsga
//
LOCUS       WP_176042628             386 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia stabilis].
ACCESSION   WP_176042628
VERSION     WP_176042628.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..386
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41854
     Region          25..386
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mnsqssapva gapssvstsg advraenfvq ivdvvkkfgd teavrsvnln vrqgelfall
       61 gssgcgkstl lrmlagletv tsgkilidge dlaqmppykr pvnmmfqsya lfphmsvesn
      121 vafglkqegt pkselkerva salelvqmsk yakrkphqls ggqqqrvala rslvkrpkll
      181 lldepmsald kqirqrtqie lvnilnkvgv tcimvthdqe eamtmanrla vmsegqivqi
      241 gspnevyeyp nsrfsaefig stnlfdgvtv edepdhvyie spelpsrlyv shgisgplgm
      301 pvtvsvrper ialtrkppeg afnwargris nvaymggysl yhvkldagkt vianvsslai
      361 teldtpalgd eiyvrwsata gvvlts
//
LOCUS       WP_176042638             336 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Burkholderia stabilis].
ACCESSION   WP_176042638
VERSION     WP_176042638.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..336
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=36797
     Region          9..292
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 mdllaitfdq irdayalgpg gpprqvserv whlptddggv avklyapehq graakeaavl
       61 ahfethgdar frvqtlkrtt vgeplsagsg ahamvtrwea gqfrtydtfs paewdalgas
      121 laalhlsleq lhlpsldtlr arltaidadg vrrslldald rarsvdgaan lrcyvdlalr
      181 midryypgsi eafpaddpqh pihndynqfn ylfadanada gtlpplildw eatigaprey
      241 elvrclnhlp leapqraeaf vhaywrvrsv npaqiawavd aaclqhalkl wvvqgwldep
      301 srfaahlgga vtmasamvda rgqlidffsr caeags
//
LOCUS       WP_176042702             425 aa            linear   BCT 11-JAN-2025
DEFINITION  GspE/PulE family protein [Burkholderia stabilis].
ACCESSION   WP_176042702
VERSION     WP_176042702.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..425
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=44972
     Region          <36..423
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mhfpppaapl htqppsahsd asaaaapral daaqlddapa vrlltdtlha arvrdasdih
       61 vepfeagwri rlridgvlhe harpplhlrd alvtrikvla rmdiaerrlp qdgrlriaid
      121 ggvrgdyrvs slptlfgekl vlrrletmpp dltlarlgfd aqqaaameaa iraphglvlv
      181 tgptgsgktl slycalqmld rdthnvctve dpaeiqldgi sqvgvaekag ltfatalral
      241 lrqdpdiimv geirdaetad vaikaaqtgh lvlstlhtnd apaavarlld igvapynlaa
      301 alhlvtaqrl vrrlcvacrv rsdaparvll eagcdpaala agwrpfvarg cpachgigyr
      361 griglhqtmp vspglaeriv arasvgelaq caaaegvrnl rdaafarvqd gttsiaeava
      421 atpta
//
LOCUS       WP_176042789             425 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter large permease [Burkholderia stabilis].
ACCESSION   WP_176042789
VERSION     WP_176042789.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..425
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44735
     Region          1..424
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mtiavflfsl lgamavgmpi afslivcgla lmvqsgtvdv qivtgnming ldnfifiaip
       61 ffmlagelmn agglskrivg mvmamighvr gglgyvtiaa aivlaslsgs aiadtaalsa
      121 illpmmrkag ydpqrsagli assgiiapml ppsmglvmlg aiggisitkl fiagifpgii
      181 mglslvavww wmsrkaesgv iprqpmsvvl kslregiwal llpviivggm kfgiftptes
      241 avvavayalf aglvvyrelt fadiyrclva sakttaivmf vvaaafissw mittadlpgq
      301 laqilrpfmd sptilmlliv lllvivgmal dftpmilili pvllpvikqa gidpvyfgiv
      361 fimcnaigmi twpvgtvlnv vsgvgklsfd avsravlpfl iaetivalil vlfpqlvlap
      421 lnwih
//
LOCUS       WP_176042874             682 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia stabilis].
ACCESSION   WP_176042874
VERSION     WP_176042874.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 682)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 682)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18540890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..682
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=73589
     Region          27..277
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
     Region          <213..682
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
ORIGIN      
        1 mnavtttetq aldtaanvlq aadpskhmil vplsrlvlrp tgrnvrktpr msipelaasi
       61 qrvgllqnli vipaadglhy evvaggrrla alkllakkhr iakdwqvpcl qvadgtarta
      121 sltenvqrea mhpadqfeaf aalvaegrpi ediaadfsvt plvvqrrlkl anvsprlmad
      181 yradavnldq lmalagtddh aaqesafyda pqwqrqpsal rerltereid ayrhplvrfv
      241 gldayeqagg gvrrdlfaeg dagvylndaa llerlaqdkl agiaaevkae gwawvdaapa
      301 atyadlqafq raprerrepn kreaqrierl qakmqevaea idaatdadde dkadalqeeg
      361 erlgeqlqal edglqgygan vkaaagaivt idrngeavih rgllreaeak alrtlerlrq
      421 gfsdpdaand degeedeqpk aaaisdrlaq rlsahrtaal qievarhpqv alaaqvhgmv
      481 qtvlqsrnyg hdlplgvrlt vqdrlegmap dwpqspaava lrelqeawgg klpedsaalf
      541 aallameqge lvkllavcva gavdvvtpra taqqpgaela qavgldmaaw wqptaegyfk
      601 hvpkaavlqa vgefapesvn rlaklkkadi aseaerlakg tgwmpaifkt adapeegpqg
      661 aerdgaeeva tvmhepaeel aa
//
LOCUS       WP_176042911             290 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia stabilis].
ACCESSION   WP_176042911
VERSION     WP_176042911.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         1..290
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31442
     Region          15..280
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mttarsldrt ypalrttegg gfvvhrpfpt rllmdfdpfl lldemgpvdy apgeakgapd
       61 hphrgfetvt yaldgrfchr dssghagtlg pgdvqwmtag agvvhsempd pafaqaggrs
      121 hgfqlwvnlp rrdkliapry qeipadrips atspdgrarv rviageafgv raaietrtpi
      181 lyqhftlepg atvtqpvpag yrvfaypidg tglygpdrqa vdarhmvvyg ddgdtvtfaa
      241 gdtpldllli ggvplnepiv rygpfvmnte eeirqavvdy qtgrmgriea
//
LOCUS       WP_176043028             399 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase [Burkholderia
            cepacia complex].
ACCESSION   WP_176043028
VERSION     WP_176043028.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..399
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44480
     Region          50..394
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mtrpvalvsp deparpiesl ripadlsgaa gvnrargair hisadddlaa vtawlarytd
       61 apgtltayrk eaerlllwta iqhgkplssl thedllvyqr fladpqpawr wvttarkkpg
      121 raspdwrpfa gplsptsvrh amtilnamfa wlveagylag nplslarrrg varkpavtry
      181 lthewwevvk ttietlpagt ererlhaarc rwlftvlyla glrateiast pmgavfcrrd
      241 aagverwwie vlgkgnktrl vpatdeliae laryrrvhgl ppspyqgerr plllplighe
      301 kplsrgsihq ivkevfalaa arlrargpew qaqaeqlaga sahwvrhtag shmtdrqvdl
      361 rfvrdnlgha slattsvylh aeddarheat qtrhrlgwn
//
LOCUS       WP_176043132             330 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia vietnamiensis].
ACCESSION   WP_176043132
VERSION     WP_176043132.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..330
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=34237
     Region          153..330
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mnmyrlfagc liavsfaapg dasaecwfin gkselianlp lkdeyyvapg tpvgtvlddv
       61 sispdtvaya rcrlpespir nvyggvpvgn tgafttgvpg iglifyetdp pdsfghrfvh
      121 ywgdgigpwr pgdwgwwgwv sstprlgsrl gvmlvvtgpv gvgsvaggsv yarmtisglp
      181 vgtlrtggfr ittpacsvpn vsvvmgevsa srfrgvgtta gdtpfdlrln acpagrtaiy
      241 yrldpttsvv pgtgesvaal tgsrpatgig lqlldalgkp lvygstmqva gyagsagdys
      301 vplraryyqt dasvtagnan aavtvtisyd
//
LOCUS       WP_176043072             278 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase, partial [Burkholderia stabilis].
ACCESSION   WP_176043072
VERSION     WP_176043072.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia stabilis
  ORGANISM  Burkholderia stabilis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 278)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Burkholderia stabilis"
                     /db_xref="taxon:95485"
     Protein         <1..>278
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
     Region          <1..278
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 qenmsasphv lpgsrdgfrm gdaklvdtmi vdglwdvynq yhmgitaenv akeygitree
       61 qdafaalsqn kaeaaqkagr fddeivpvsi pqrkgeplqf atdefvrhgv taeslaglkp
      121 afskdgsvta anasglndga aavlvmsaqk aaalgltpla kikayanagv dpsvmgmgpv
      181 pasrrclera gwtpgdldlm eineafaaqa lavhkqmgwd tskvnvngga iaighpigas
      241 gcrilvtllh emakrdakrg laslcigggm gvalaver
//
LOCUS       WP_176043133             877 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_176043133
VERSION     WP_176043133.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 877)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 877)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 877)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 877)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..877
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..877
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=92672
     Region          53..860
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mekkysgpha eiaprlkpic alvfsivasw qtdalavade harpqqiaqm efaqvefegg
       61 flnngagsid vsrysrgnvv ragtyspdvy vsgrwagrfe vpfksvadsp daqpcfdkal
      121 lerigvelta lsqeirtlle qqggcvrigq aipeatvgfd fndlrldlgi pqvslsrtar
      181 gyvspdrwsa gvpvamlgyn anvyhaqasg ahgstqgyvg vdsgfnvqrw hfrhsgsfnw
      241 ddrgrrryqn vatyvqrdla swssqfvagd tytsgdlfds tsfrgvriss ddrmlpdsqr
      301 gyapvvrgva ntnakvtisq ngvklyettv apggfviddl yptgyggdln vvvteadgst
      361 htfsvpyaav pmslrpgqnr ysftagavrn lsnttplltq atwqhgftnm ltgyggataa
      421 qgylaamvga vlntgwgaig vdvahattrv qndrtysgqs frvsyaktva atgtnvaiaa
      481 yhystngyfg lndamtardr svsggplrqv yrqrnraslv asqqlgdkgg slsvtastst
      541 ywnragsdvd ftvgysnafr svaynvsatr qrdawgqast lvylglsipl gstrpatlst
      601 sfnhdtrgst qiatslsgsa gvdsnvsygv nvnrssgpgg aqtsgganvs yrgaraelsa
      661 svgasadyqq ysigargavv ahrggvtlsq plsetfaive akhaegarvt nasgvrvdan
      721 gyaivpyltp fsmndvsldp kglstdvelk etsqrvapla gavpllvfkt dygrsavirl
      781 rqadgspvpf gavvtdqagk digvvgqagk llarglaeqg elnvgwesda grsgcrlsya
      841 lpanprgagq ralrsldlpc vaagaeqyap teaqpaa
//
LOCUS       WP_176043151             280 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia vietnamiensis].
ACCESSION   WP_176043151
VERSION     WP_176043151.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..280
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=31473
     Region          147..>233
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mqrrypggqg grsrssdwqe rderayrgvg rgitdepspw peeayesayh rfrsedvgpe
       61 dwgsewsera arspaeersa gwrdapagar epgrgygerr rdpqrtgger ggepqwrtgg
      121 yrgergydar dpcddrpgea pdlsrfggga mrartgpkgy trsderired vcerlarale
      181 idvsdvsvev rdgcvvlegt vptrwmkhgi edlsddcmgv rdvenrvrvr rdgehdtgtv
      241 lrpsqrtvtp trpnpntrep epesgaarrd engadreprh
//
LOCUS       WP_176043156             235 aa            linear   BCT 11-JAN-2025
DEFINITION  PIG-L deacetylase family protein [Burkholderia vietnamiensis].
ACCESSION   WP_176043156
VERSION     WP_176043156.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005328
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..235
                     /product="PIG-L deacetylase family protein"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0019213 - deacetylase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25767
     Region          6..>163
                     /region_name="LmbE"
                     /note="N-acetylglucosaminyl deacetylase, LmbE family
                     [Carbohydrate transport and metabolism]; COG2120"
                     /db_xref="CDD:441723"
ORIGIN      
        1 mtaptrwlvi sphlddavfs cgqaiaqapg svvvtvfagi pardtaappw drragfrsad
       61 eavrarrded rralalldar pvwldffddq ygapaatdei aarltdtlda hpgygvlapa
      121 glfhrdhlqv qqaalsvlhd lhaagdtsra wrfyedapyr ridglmskrv sewrergwfa
      181 rpvaapagdr sdsaaakaaa vdayqsqial fephmradlr epetywqlec dstsg
//
LOCUS       WP_176043149             153 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Burkholderia vietnamiensis].
ACCESSION   WP_176043149
VERSION     WP_176043149.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..153
                     /product="RidA family protein"
                     /calculated_mol_wt=16986
     Region          28..137
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 msqpthtrir mfntkdtypn qtldndlcqa vragntvyvr gqvgtdfdgn lvglgdpraq
       61 aeqamrnvkq lledagsdlt hivktttyli dpryrepvyr evgkwlkgvy pistglvvsa
      121 lgqpqwlmei dviavipdnw qpaqasasvr eeq
//
LOCUS       WP_176043161             443 aa            linear   BCT 11-JAN-2025
DEFINITION  NRAMP family divalent metal transporter [Burkholderia
            vietnamiensis].
ACCESSION   WP_176043161
VERSION     WP_176043161.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..443
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46930
     Region          27..429
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 msdlrdddap haaptstsas apapaakpwy rrlgpgllag asdadpsnva vyaqagsqfg
       61 fnmlwmivvt lpmmvvvqla aafagrtnrk glvagirehf sdrlaktliv mvvivnvvnv
      121 gadlaamgda talvaggrsy wyaalygias lalqvlmsye ryarwlkwmt lgllayvlel
      181 gfvhvdwrnl lhtlllphia fthdyattav avlgttlspy lfvwqaalev eetqaerrng
      241 dgdtasapat rrdterritf dtwtgmivtn avsfcimvig aavffthgrh digstaqaae
      301 alrpiageaa fvvfafgivg cgllaipafa gsaaygcaea wqfreglnep vhrapafygv
      361 lalcvlvgia icfgpvnpik alywsavfng iaavpmlvlv mllaqrrgaa gqpgsgvasr
      421 vlgwlavalm aasvvvmvvd mla
//
LOCUS       WP_176043198             431 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia vietnamiensis].
ACCESSION   WP_176043198
VERSION     WP_176043198.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..431
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46309
     Region          109..420
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mpltigtpsc rrvslrahsf iaalilasvt araqeapvtl daalqsatdr saamgaaqas
       61 vrassevavk agqlpdpmlk agvdnlpvsg qqkytigqdf mtmrrigieq ewvsgdkrrl
      121 rsalandvvd reragylaql antrqqtaaa wlnavyakka vslqqelvgh mtheleatka
      181 syrgakataa dvtqaqamla qtqdqllkar qtfqtaligl srwtatpvsd vtgeppapqs
      241 yvsslppeel rdvqpalita srdiavadad tavansdrsp nwtwevsyqq rggaysnmvs
      301 vgvsiplpin rknrqnrdaa ekaelgtkar lmyedaqrqv eanvrtqaat lasgrdridn
      361 lrnsllaaad qrallataay kagtgsladt faarraqlda qlqvldlqrd vsqtwaqley
      421 qvvpasmsvs q
//
LOCUS       WP_176043240             430 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia vietnamiensis].
ACCESSION   WP_176043240
VERSION     WP_176043240.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..430
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=46996
     Region          16..345
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mnemksnsvd vaiigagpsg avaaallrna grsvlvlerq hfprfsiges llpqsmryle
       61 eagmlqavve agfqfkngay fvhrdrmssf dfrdkfsdgw gtayqveraa fddllircae
      121 kqgaqvrfgh avrafhagdt prldvvdeag heysvqasfv ldasgfgrvl prllgleapt
      181 glptraaifs hvedrlpags tdrdkiciav hperrdvwfw mipltngrss vgcvadaafl
      241 dvpeakqeal lrellqtept larlvgskpf vmpvrricgy asnveslhgh gyallgnage
      301 fldpifssgv tialrsahla vatlerqlrg etvdwardyd valrkgidtf rafverwysg
      361 alqdivfhed kasdvkrmvc silagyawde tnpfvrepar gldilaqlcc ptgasgnaaq
      421 aatpdgarrr
//
LOCUS       WP_176043221             317 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia vietnamiensis].
ACCESSION   WP_176043221
VERSION     WP_176043221.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..317
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35008
     Region          2..307
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mrriglvlvp qfqvmsllal svfdianlra grslyevsvi sedggpveas fgmcastrpa
       61 haaelhtvfv gaslskpplt dgmrqllldl sgkvermasi clgafllada glldgrratt
      121 hwayvdqfrk rfpavsvekd cifvrdgriw ssagmstaid malamleedl gadaalevak
      181 dlvierwrrs gaqpqtsvll ehparsnrih dvityirqhl gteltvekla dvarmskrqf
      241 trrfkdetgl tpakavdrir letardflts sswtidtiar etgyadperm rrsfvrafgq
      301 ppqalrrpat aepvdpd
//
LOCUS       WP_176043327             696 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein, partial [Burkholderia
            vietnamiensis].
ACCESSION   WP_176043327
VERSION     WP_176043327.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 696)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..>696
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
     Region          25..696
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mdirssalgd lklrelyeai sngvlqqgrv lmldtplgkn alvplrargs arigrdysyt
       61 idvastrddt allslmhqpv tlqiqqvtap faipvyrpvh gfvhrvaylg gngglstyqi
      121 efssalvfle kthneegwle kdareiisdv ldrypqlrgq yrfsllsdpa krswcrqses
      181 dlhfvnrlae aegwyfywih envaegdapk ttlvivdhvs tlpdakavef irandsnesd
      241 gfahwagvqt mqstryisra fdykrpasdf qaesalaats yvaeerrqkv ersvpdvpmt
      301 vyestaygys ssdtgearar rlvevwdara sryfgvggvr wldagsrfvl nghprheggd
      361 akkreflvie arwfiennvp igqqtaefpq slratlaeqq aihserfktp ghaadgsagf
      421 fvieveaqpt aveyrspldh pkpimsieha lvvtpdgaea wtndrnqirv hfawdrknpp
      481 daftssplls slqsdtgngy gavhvprare wvivgywngd cdkpfvlgri nggatpspwh
      541 snallsgfks egfgktgayn sfvhddstnq ggtrlvsytg ksyaaltqgy likhegntrg
      601 kylgagfilh adefgavras kglsisahsk syddeqmgvd earsqlqqag mlveslssas
      661 ttaqaeslqt gqdalkalsk diqhpvsgdt sggvta
//
LOCUS       WP_176043364             195 aa            linear   BCT 11-JAN-2025
DEFINITION  DedA family protein [Vibrio parahaemolyticus].
ACCESSION   WP_176043364
VERSION     WP_176043364.1
KEYWORDS    RefSeq.
SOURCE      Vibrio parahaemolyticus
  ORGANISM  Vibrio parahaemolyticus
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Vibrio.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Vibrio parahaemolyticus"
                     /db_xref="taxon:670"
     Protein         1..195
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=21638
     Region          6..193
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 msmkplleqy gylalivsif fegigipmpg qslmiaasil aseqvmnlsm vmviswlscf
       61 lgntcgyllg yyfegwldkk gyisgpkmqk lqntiqkygp aclvvsrfie gmkqfmplac
      121 giakmprref llgnalaati wvlvfsllth fafehlsals hlyshykyai wasaavvfal
      181 mllgllkrkk akssl
//
LOCUS       WP_176043455             584 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia vietnamiensis].
ACCESSION   WP_176043455
VERSION     WP_176043455.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..584
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=63748
     Region          7..584
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mkiakrltal pitalvslav haqqaptpad qaaaakanae qdrqaqqqwe aqqravtvra
       61 psvrsevpkv eaypalptet pcfridrftl dvpaslpdaa kaqgasalpm drfafarewl
      121 nhyegqcvgk qgidvlikgl sqailargyv ttrvlipeqd lstgtlklsl ipgmirhvrf
      181 adeklrgtwk tafptrdgev lnlrdleqgl eqmkrvssqd vsmqivpgal pgesdvvldv
      241 krskpwtvva sidnsgtrat gklqgnlsvg idnplglndm lnvgvsqdle fgdkrlgshg
      301 wngfytipwg ywaatlsast ntyyqqiagv nqtfiasgns ktvdfklarv larsqndvfg
      361 gyfrlsrrfg qsfiedteis qqrrndtiie lgvtdrhyld gaqfdgsaay rqgvggfgaq
      421 ddmlaagpty rfkmavldan lsvpfviskq pfryvgtfhg qytgntlyyl ddmtigsryt
      481 vrgfdgetml assrgfywrn elqmpigqtg qaiyagldyg rvwgpqpial vgtqlagavi
      541 gvkgsigtrf gayaydlfag tpiykpsglp tarvtfgfql tsqf
//
LOCUS       WP_176043469             603 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia vietnamiensis].
ACCESSION   WP_176043469
VERSION     WP_176043469.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 603)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12379621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..603
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=62705
     Region          1..289
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
     Region          329..603
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 maswldytln glivgnihal lavglalifg vshlinfahg svymvgafvg wlcltrfglp
       61 lpvalaavva gcaalgiaie riglrplrha ariapllati gisfildqlv rlvfgadpra
      121 vptplpdwhv riagatlgal dlliagigia aaallygflr ftrlgwavra taqdrdaalq
      181 mgvdvdrvnq avfaiacalg gvsgllvgmy ynsidpamgf qatlkgvval ligglgnvpg
      241 aiagslllgl vesygvalfg tsyrdlfafg llivflvwrp nglfsakral ppepmtgtfl
      301 aaarhvrvsr pavaalivla aalpwlgasp yvlqtltnaw lygllalslt lvagtvgqis
      361 lghaallvig ayasallssd lgwspavtip cagaitavlg tllvypafrl rghyvsiatl
      421 gigevvslvi lnwdgltrgp lgitgiaplp wastaraayw falavlvvla llqvrllrsh
      481 lgrtlravre ddvaarahgi apnrykaiaf avggvaagvs ggiaahlysy inhqtfdsqv
      541 silaltmvil gglgnvlggi vgavaliglp elfrwaadyr mliygvvlvl lvrfrpqgll
      601 gtv
//
LOCUS       WP_176043564             316 aa            linear   BCT 11-JAN-2025
DEFINITION  ketopantoate reductase family protein [Burkholderia vietnamiensis].
ACCESSION   WP_176043564
VERSION     WP_176043564.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..316
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32778
     Region          1..307
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkiailgaga lgcaigaalt eggnevwlln rsaahveamr rdglrvddrn gsrhvkvrat
       61 traaeagvvd lvivlvksfd tdaamrgave ligpetlvls lqnglghedv ladivgrerv
      121 lagktyvggv mrnpghiesg vagkathige ldgritprtn aiadtfnasg ldttvsaniv
      181 gtmwdkllvn vatgaltgtt gltygqlyde pllkatalaa vaeamavaha agvtlstddp
      241 erawtlageg lspgfktsml qslekgsite idfingavvr wgqrhgvptp vnatlvacik
      301 giergmadrk kqetta
//
LOCUS       WP_176043570             417 aa            linear   BCT 11-JAN-2025
DEFINITION  flippase [Burkholderia vietnamiensis].
ACCESSION   WP_176043570
VERSION     WP_176043570.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..417
                     /product="flippase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44456
     Region          4..402
                     /region_name="MATE_Wzx_like"
                     /note="Wzx, a subfamily of the multidrug and toxic
                     compound extrusion (MATE)-like proteins; cd13128"
                     /db_xref="CDD:240533"
ORIGIN      
        1 mtavrknfal lfalqistyv vplvtlpllt rvlgpqqygr lsfvlavtty finlanysfd
       61 ltatprvala dgklersrif watvsaqwai tvagfavlla ltllvphfaa ertalligfg
      121 mavgaaltpg wyfqgiqkls vysvtvvvyr acsvvaffaw vrtpddllha vainaavpvl
      181 cgvtllaylf lrrevdsvrv gvadiaaalk ggsqvflast sisfyastnt vllsivsgsv
      241 aagyfaagdk liraavgllq plraatyphv tylmhhardd afaflrkliv lqgalvlams
      301 atiyvcapfv vrmlygdafa ptvgvlrcla lvpfmacmtd lfgvqtmlpm gmkrtfsiil
      361 issgalnvtl lpplamlfae rgaaiavlia esavavalay vlcrervgll nlsarsg
//
LOCUS       WP_176043585             215 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia vietnamiensis].
ACCESSION   WP_176043585
VERSION     WP_176043585.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..215
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22837
     Region          1..212
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msfrlylsfv aasavliyap gpvnlltmnq alrtgwrral pcvwggtlav llqlaltalc
       61 lnslvhldth alavlrwaga aylvwlgckq wlsrapadaa aaaapatgsa ardaesgral
      121 fwrgvatsgl npktllffps ffpqflvpna dwslngqfll lattfallfv ggmasmalls
      181 hrlsralqrp armhamnrat ggllvgmgai magwn
//
LOCUS       WP_176043618             237 aa            linear   BCT 11-JAN-2025
DEFINITION  KilA-N domain-containing protein [Burkholderia vietnamiensis].
ACCESSION   WP_176043618
VERSION     WP_176043618.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Iyer,L.M., Koonin,E.V. and Aravind,L.
  TITLE     Extensive domain shuffling in transcription regulators of DNA
            viruses and implications for the origin of fungal APSES
            transcription factors
  JOURNAL   Genome Biol 3 (3), RESEARCH0012 (2002)
   PUBMED   11897024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10516234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..237
                     /product="KilA-N domain-containing protein"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=25801
     Region          35..133
                     /region_name="KilA-N"
                     /note="KilA-N domain; pfam04383"
                     /db_xref="CDD:367917"
ORIGIN      
        1 mkkenarpsk aessaveqrk ftpaisstsr ieraivseyd gmavsftgdg wfnatapaar
       61 ygkepaqwlr lpatvshiaa lqrkygnfty srtrrgaggg twlhpklaip ftrwldddfa
      121 vwcdeqidhi lcgglsvwqk vggeqsdtad replltaaaa ivarhrlpfg tvyealntfa
      181 gvtharemtc dqvvesaefg arllagnatt tdfeqidrnr allgitsaql ellggar
//
LOCUS       WP_176043658             308 aa            linear   BCT 11-JAN-2025
DEFINITION  YoaK family protein [Burkholderia vietnamiensis].
ACCESSION   WP_176043658
VERSION     WP_176043658.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..308
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=30735
     Region          7..222
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mnldgasrnl tvaalltlsg gyldaytyvg hghvfantmt gnvallginl sagewaaalr
       61 hvpplggfvv avlvahllgl aaqrgwmrht afasliveia flglaasglv gassawlipg
      121 itfvatlqtl sfthlealsy tsvmttgnlr raaqklfvgl iprydagalh dsallatisf
      181 cflggavcgg lvtrlapdva lwgavlplvg afaeivrrar qragdpagga ggdggngsdg
      241 gngsdsgngs ngrngsnatn atnatnatng tngtngtngt ngtngtngtn gtngtnaaap
      301 eyvasrra
//
LOCUS       WP_176043643             460 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA cytosine methyltransferase [Burkholderia vietnamiensis].
ACCESSION   WP_176043643
VERSION     WP_176043643.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000826
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..460
                     /product="DNA cytosine methyltransferase"
                     /EC_number="2.1.1.37"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003886 - DNA
                     (cytosine-5-)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006304 - DNA modification [Evidence IEA]"
                     /calculated_mol_wt=50825
     Region          11..398
                     /region_name="Dcm"
                     /note="DNA-cytosine methylase [Replication, recombination
                     and repair]; COG0270"
                     /db_xref="CDD:440040"
ORIGIN      
        1 mtkrkgaaap kkynvislfs gamgldlgld stgrfellac vekvpafcet iranraqgrl
       61 radlkvfegd isdldpaevl aacglkpgel dvlvggppcq afstagrrma tqdprgtllw
      121 qylrfvehmq pkfflmenvr gllsaalkhr piaerpergg pplepderpg svvrlfaedm
      181 qniaslsgsg yhmdcfevna vnygapqlre ralfignryn vvvdfpnpth gpahsipaqg
      241 sliepdaaik pwrtlrdaig giddpgevil dfsprkksfl slipqgsnwr slpvelqqes
      301 mgsawyakgg rsgwwrrlsy dlpcptlvtm pnhastslch ptevralslk eyaliqefpk
      361 dwvfkgttsq qyaqvgnavp vrlgtvagnv iakeldalaq rnwladatkp edyrvvyvqs
      421 hvrtrqwfkd gkayvwedge tnesvtyeap qtlrkissma
//
LOCUS       WP_176043674             214 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia vietnamiensis].
ACCESSION   WP_176043674
VERSION     WP_176043674.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789896
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..214
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23173
     Region          9..214
                     /region_name="COG2945"
                     /note="Alpha/beta superfamily hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:442188"
ORIGIN      
        1 mnvhtqksli agpvgqieia vdlpdavrer raaprgialv ahphplfggt mdnkvaqtla
       61 rtlvqlnyvv yrsnfrgvga tegvhdngig eaddllavla hvraqpglae lplvlagfsf
      121 gtfvlshvgk rlrdageaie rmvfvgtaas rwqvadvpen tlvihgetdd tvpigsvydw
      181 arpqelpvvv ipgaehffhr klhvlkriiv dawr
//
LOCUS       WP_176043713             307 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia vietnamiensis].
ACCESSION   WP_176043713
VERSION     WP_176043713.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..307
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33249
     Region          7..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..292
                     /region_name="PBP2_LTTR_like_4"
                     /note="TThe C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08440"
                     /db_xref="CDD:176131"
     Site            order(111..112,114..115,118,122,124..130,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176131"
ORIGIN      
        1 mginfdltdl qafravvelg sfrkaaesis isqpalsrri dkledalgvr lferttrsvt
       61 lttvgrvfap saeqllddld vallgirdvs ssrlghvtia cvpsvayyfl pnviasyhrr
      121 fprirvklld asanevlsav isgeadfgvs fmgsqepeve frlllqerfv aacrrdhpla
      181 gkkrvtwnel yaydyvsvdk tsgnrllldq altavapraa svcetrhvtt mlglieaglg
      241 vaavpsmamp grdhpvltsv plvepvvkrr vgivkrrgrt ltpaaeafhr avldarrsaa
      301 agseaaa
//
LOCUS       WP_176043774             180 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_176043774
VERSION     WP_176043774.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..180
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=18855
     Region          <43..180
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(50,52,56..57,60..62,64..65,69,72,81,83,85,89..90,
                     93..95,97..98,102,105,114,116,118,122..123,126..128,
                     130..131,135,138)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          50..81
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          83..114
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          116..146
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mslhssfvar rggnlravrd ddpprarmpa alatwlawhd fpdlhscgid gvtplmlaal
       61 qgedgvldal lahgarldal ddagngalwy aciggapapi lrlieagadv dhandddvtc
      121 lmqaaasgri evmqlllscg asetlcapdg rsardmatdr alqllreshr lahatqddaa
//
LOCUS       WP_176043881             212 aa            linear   BCT 11-JAN-2025
DEFINITION  2-hydroxychromene-2-carboxylate isomerase [Burkholderia
            vietnamiensis].
ACCESSION   WP_176043881
VERSION     WP_176043881.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Thompson,L.C., Ladner,J.E., Codreanu,S.G., Harp,J., Gilliland,G.L.
            and Armstrong,R.N.
  TITLE     2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class
            glutathione transferase from Pseudomonas putida
  JOURNAL   Biochemistry 46 (23), 6710-6722 (2007)
   PUBMED   17508726
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122490
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..212
                     /product="2-hydroxychromene-2-carboxylate isomerase"
                     /EC_number="5.99.1.4"
                     /GO_function="GO:0018845 - 2-hydroxychromene-2-carboxylate
                     isomerase activity [Evidence IEA]"
                     /GO_function="GO:0043295 - glutathione binding [Evidence
                     IEA]"
                     /GO_process="GO:1901170 - naphthalene catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23466
     Region          8..188
                     /region_name="DsbA_HCCA_Iso"
                     /note="DsbA family, 2-hydroxychromene-2-carboxylate (HCCA)
                     isomerase subfamily; HCCA isomerase is a glutathione (GSH)
                     dependent enzyme involved in the naphthalene catabolic
                     pathway. It converts HCCA, a hemiketal formed
                     spontaneously after ring cleavage of 1; cd03022"
                     /db_xref="CDD:239320"
     Site            15
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:239320"
ORIGIN      
        1 mnatrtatwy fdfvspfayl qqerfdtlpp divfepkpiv lgallahwgq kapaeiaakr
       61 vftyrhaqyr adklgiafrm ppahpfnpir plrlaiamgg spdairrifr hiwrdgndvs
      121 tpdgfaalce avgfpdgvta vdaqpvkdal rantdraiah gvfgvptfel dgdlfwgeda
      181 tdmfvdcats rawldspevr ristlpeglr rg
//
LOCUS       WP_176043928             353 aa            linear   BCT 11-JAN-2025
DEFINITION  C40 family peptidase [Burkholderia vietnamiensis].
ACCESSION   WP_176043928
VERSION     WP_176043928.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..353
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=36141
     Region          <6..175
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mlriwvpvav vsllaacssv ppqsasrsag mkittprafp apanfpnfvd hsvgqeeisi
       61 qamslvgvpy rwggntptsg fdcsglvryv lgraadvnlp rttadmssrg asidpdqiap
      121 gdliffnttg rphshvgiyv gklrfvnaps tggtvrldyl tnpywakrfd girrvapprg
      181 tptpfdapiy darrdapaaa tapvvaaaav rrpayasspa rataqaavpa vstttavtta
      241 aaaaaspapy eppprmsvpv ssaggdtmam tpvlppagps eevgtqiptt altaaqaaaf
      301 daeppsampa pssagsaepv qvqvlrastq aapvsprtst addpiarfan gsy
//
LOCUS       WP_176043957            1085 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia
            vietnamiensis].
ACCESSION   WP_176043957
VERSION     WP_176043957.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..1085
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114353
     Region          1..1058
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mwivrlalrr pytfvvlall ifiagplall rmptdifpni dipvvsivws yngfsaedma
       61 kritsnyera ltsdvddieh iesqslngvs vvkvffhpga dinraiaeaa snaasilril
      121 ppgtlppnii tynastvpil qlglssdtla eqqlydlgns firtqlatvq gaavplpygg
      181 kirqivvdld tralqakgla pidvvnaina qnlilpggta kigtheydvq lngstqtvaa
      241 lndlpvktig gsvvyvrdva hvrdgyapqt nivradgkra alltvektgs astltiidqv
      301 kamlpkiaag lpkalhiaal ddqsvfvksa iqgvvreali aacltalmil lflgswratl
      361 iiavsiplav ltsllalgal gqtinimtlg glalavgilv ddatvaieni thhlergepl
      421 edailtgage iavptfvstl sicivfvpmf lltgvarylf vpmaeavifa mvasyffsrt
      481 lvptlamvlm rakgqgrppr gvfariaglq aaferrfdai rlgyrallaa aiahrrrfaa
      541 afvlacvast glfafagqdf fpaidtgeir lhlraptgtr ieqtarltde veakvrsvip
      601 arelagmldn igvpvsginl tydssdpigt edadvmitlk pghaptaayv arlrnllaqs
      661 fpgvtfaflp adivsqilnf glpapvdiqi vgnkldqnra vanallaklr gvrglvdari
      721 qqpgdepaid vnvdrtkaie aglqqrdvaq nllialsgss qttpnfwldp rngvsypvlv
      781 qtpqytidsl qalanvplpt sgapspqrpa ggpaagapaq nllgtlgsfs rttqqavvsh
      841 ynvqpvldif asvqgrdlga vtadvtklvd daraqlppgs sivlrgqvqa mhesfagllg
      901 glalaialvy llmvvnfqsw ldplvivggl paslagiawm lfvtrttlsv paltgtilci
      961 giatansilv vnaarellag gaspwqaald agfsrfrpvv mtalamligm lpmalglgdg
     1021 geqnaplgra vigglafgtl stllfvpvvf gfvhawlerr rdaarargas gmpsapaapd
     1081 tpalr
//
LOCUS       WP_176043996             395 aa            linear   BCT 11-JAN-2025
DEFINITION  YncE family protein [Burkholderia vietnamiensis].
ACCESSION   WP_176043996
VERSION     WP_176043996.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..395
                     /product="YncE family protein"
                     /calculated_mol_wt=41366
     Region          50..268
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          <179..>376
                     /region_name="COG4946"
                     /note="Uncharacterized N-terminal domain of tricorn
                     protease, contains WD40 repeats [Function unknown]"
                     /db_xref="CDD:443973"
ORIGIN      
        1 mhskrfhlrr arllaaltla ttavaahaad wivsgndgky qrvegrdtyl asppadtltl
       61 ldasvfppki alqvdvengi qgppqavait pdaklalvga ptrydpaakq laydtfvqvv
      121 tldaspptia rielgthpqg iaidragrlv lvanvdgsvs ilridgtqvt ldgslkigkk
      181 rlagisfthd gkhalvslrd eqgvavlnvd ggkvtdsgtr lstgvapyti dvssddrwav
      241 vsnvglaglp gytgtlagda dsvalidvsh tpfrtvqylt vpslpegvai spngkwiavq
      301 amdgsnltpd npgrhkrgkv vlfeiragra vqtseapgge aaqgiaftad srhvivqfnv
      361 erqlalyave ggklrdtgtr ialsggpssl rtlpr
//
LOCUS       WP_176044018             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia vietnamiensis].
ACCESSION   WP_176044018
VERSION     WP_176044018.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45747
     Region          21..426
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(34..35,38..39,42,81,139..140,142..144,147,167,
                     170..171,174,257,260..261,264..266,269,297,301,353..354,
                     358,362,378,381..382,385..386,389)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msafppavar atgsagavsh rrivfasfig taiefydfyv yataaalvig pvffphssat
       61 aqalsafvtf giafiarpig sflfghfgdr igrkstlvas llvmgistta igfvpgydti
      121 gtlapvllcv lrfgqgiglg gewggaalla tehappgkrg wfgmfpqlgp svgflmsngl
      181 ffalalslsd eqfrswgwri pflvsavlva vglyvrlkia etpafqaale rdervrvpia
      241 tlisqhwqpt llgalamvvc ytlfyistvf slsygvsalh iprqsflgll cfavvfmgla
      301 tplsawaadr fgrkpvlaag aiaallsgfa mepllgsgsm plvalfltle lflmgvtfap
      361 mgallpelfp tnvrytgagv aynlggilga siapyiaqll aargglswvg gyvsvaaals
      421 ligvllmret rdaslv
//
LOCUS       WP_176044080             321 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia vietnamiensis].
ACCESSION   WP_176044080
VERSION     WP_176044080.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..321
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34582
     Region          11..224
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(52..53,55,69..71,77,79..80,121,223)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(52,54..55)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(77,80,83,90)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(113,117..120,122)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(118..119,142..144,196..197)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          237..321
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 msaptltvrv arkwqeardi cgfefvaddg splprfdaga hidvhlpggl vrqyslcndp
       61 rhgdryriav lrdadgrggs raihdevrqg dtlrigmprn qfplardash hlllaggigv
      121 tpmlsmaeql saagesfdlh ycarslerma fveqintaaf rdrtrlhvdd gdaaqrfdlp
      181 aaldaapagt hlyvcgprgf mdavldaara rgwpdarlhy effggavvas gaerafqvrl
      241 assgkvvdvp adctvvaala ahgidvltsc eqgvcgtcvm rvlegepdhr dsylteaeqa
      301 agdqfmpccs rarsdllvld l
//
LOCUS       WP_176044104             151 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia vietnamiensis].
ACCESSION   WP_176044104
VERSION     WP_176044104.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10159541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..151
                     /product="VOC family protein"
                     /calculated_mol_wt=16406
     Region          3..135
                     /region_name="PhnB_like"
                     /note="Escherichia coli PhnB and similar proteins;
                     cd06588"
                     /db_xref="CDD:319899"
     Site            order(3..8,24,62..63,66,83..88,90,94,123,133)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:319899"
ORIGIN      
        1 mqvqpyltfy graeealqfy elalgaktmf kmhfkdappn pdfpmspema dkvmhasfti
       61 gdsmimcsdg dcsqpgggah agyslslnpa tvedgqklfd aladggevtm pfgktfwalg
      121 fgmakdrfgv hwmvnvedls qrddlakhaq a
//
LOCUS       WP_176044153             289 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_176044153
VERSION     WP_176044153.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..289
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=31101
     Region          50..276
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(130,133..135,137..138,142,145,155,157,161..162,
                     166..168,170..171,175,178,187,189,191,195..196,199..201,
                     203..204,208,211)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          155..187
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          189..214
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mrykktitag aiaalvgvts plwwpiqaqg tnitgfkrya pehffsgqql tlaqaihdgd
       61 lgrvqqltpk tdlnapgakn ttllsyavqe iapvkndasn pryqiisvlv ksgadpkapv
      121 gssggsvvdv alradtpnll rvllnsgldp nwlyngdtpm ifavaenrll pqlkllvehk
      181 anvnardslg ktalfeatmi qqwdvvdyll ahgadpktas qlgvsygwvl qnelknhtta
      241 dssartrieg irrkivaaga pwppldpkeq raamrargek vvtpagqtd
//
LOCUS       WP_176044203             473 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia vietnamiensis].
ACCESSION   WP_176044203
VERSION     WP_176044203.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..473
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50479
     Region          4..473
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mipseafvsa crdaigavhv ltdphdtepf ltdwrrrykg sacavlkpad taevaalvrl
       61 anthgvalvp qggntglagg atpdasgsqa vlsvarlnrv rafdphnnti tveagvilad
      121 vqarareggr lfalslaaeg sctiggnlst naggtavlry gnarelclgl evvtpqgeiw
      181 eglrglrkdn tgydlrdlfi gaegtlgiit aavmklhplp aaqvtalaal esphaaldfl
      241 alaqraagpl ltgfelmsdf cmqlvgkhyp qlrypferth aqtvllelsd neseahartl
      301 fetlmeqafd aglvvdavva enlaqsrafw dlrehiplaq adeglnikhd iavpissiar
      361 fidetdaaiq qaapgarmvt fghlgdgnlh ynvqtpaggd pkaflaqfqt pinrivydnv
      421 hrhrgtisae hgigqlkidd aqrykspvet almrtlktal dprglmnpgk vlr
//
LOCUS       WP_176044397             311 aa            linear   BCT 11-JAN-2025
DEFINITION  SPFH domain-containing protein [Burkholderia vietnamiensis].
ACCESSION   WP_176044397
VERSION     WP_176044397.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..311
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33433
     Region          2..282
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 mdslivwvvl lviaivivsk tvkivpqqha wvlerfgryh atlspglniv lpfvdriayr
       61 hvlkeipldv psqvcitrdn tqlqvdgvly fqvtdpmkas ygssnfvlai tqlaqttlrs
      121 vvgkleldkt feerdfinhn ivsaldqaaa nwgvkvlrye ikdltppkei lhamqaqita
      181 erekraliaa segrkqeqin lasgareaai qksegerqaa inqaqgeaaa ilavadanaq
      241 aiqkianaiq sqggmdavnl kvaeqyvgaf snlaeqgntl ivpanlsdlg taiasaltiv
      301 knatpaaggr g
//
LOCUS       WP_176044406             361 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein, partial [Burkholderia vietnamiensis].
ACCESSION   WP_176044406
VERSION     WP_176044406.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         <1..361
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
     Region          1..328
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 weldlfgrvq slkdqalaqy lstsyarqat eislvsqvad qyltllsted llkvtentlk
       61 taqasydltk lqfdngtgse ldlrqaqtvv eqalanqqaq araraqavna lvlligeplp
      121 ddlpagmsld aqnlltdvpa glpsdlltrr pdvmqaeqtl laananigaa raaffprisl
      181 taafgtaspt lgglfkagta awsfapqltm pifeggqnia nlnlanvqkr ieianyekai
      241 qsafrevsdg laargtydlq iaalerneha qqrrfdlsdl rykngvdsyl svltaqtdly
      301 saqqslisar larwtnlvdl yralgggwiq hagetprapd vtegydkaaa papasaaatn
      361 g
//
LOCUS       WP_176044470             422 aa            linear   BCT 11-JAN-2025
DEFINITION  lipopolysaccharide biosynthesis protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_176044470
VERSION     WP_176044470.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454936
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..422
                     /product="lipopolysaccharide biosynthesis protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45435
     Region          12..401
                     /region_name="RfbX"
                     /note="Membrane protein involved in the export of
                     O-antigen and teichoic acid [Cell wall/membrane/envelope
                     biogenesis]; COG2244"
                     /db_xref="CDD:441845"
ORIGIN      
        1 mlkrfgnpdv akavanlvwl glerltqigv aiaisgllar yfgpdvfgkw qyantlllvl
       61 apltwvcgae ilvptivqra gaqpgtqpga vlgsafvlri gvsaaalaat wiaigagafd
      121 plvgamlagl avtmvfrepf vgvinawlqs mtyskpqlvt smvtalvkal lvwllvraaa
      181 sparfawlwa leaaaigfal llyyrhrngg algwtfdkpl frhfatagtv fwlglicmyl
      241 flkldrlmle rhvsfadlgr yaaaqqlnen witlalmlaq tiapafvyrv qdvarlrrni
      301 vrliamtaal mtagalvlda aaplvvgkvf grgyeasvdi frwavwlsvp agieaignli
      361 vlkyqakfvl lakwvlalai aalvnvlaip rlglygalvg laagyvaaaa vnfyyirikl
      421 rp
//
LOCUS       WP_176044504             349 aa            linear   BCT 11-JAN-2025
DEFINITION  LLM class flavin-dependent oxidoreductase [Burkholderia
            vietnamiensis].
ACCESSION   WP_176044504
VERSION     WP_176044504.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..349
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38369
     Region          40..338
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 mkkvsnvrid hiafltpgny pdedasagfe rtlelfrvge algydsawvr qrhleravss
       61 aatflaaasq rttriglgaa viqmgyenpf rlaedlatvd vlshgrlnvg lsagapnhga
      121 llgerlfdtd pdlvdfshar varlrrnlag dwlgdddtfv esaagrvrpr vgpyalgltg
      181 rlwygggsrr siewaarngf nllignlttg egtdsyvdaq lrqlelyrah wseatapria
      241 lgrvivptdg anarereryr afadgrhart lapqgerrtl fapdlvgtsd eilerlladp
      301 vvgqvrelrl elpydlpfen yrqiledfit ciapalgwqp vgrrepaaa
//
LOCUS       WP_176044510            1059 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_176044510
VERSION     WP_176044510.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..1059
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=112288
     Region          14..828
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnmqntvaal rggllqqdrl lkldtplgan vltvqravgr arigrayeft ldvlstdsdv
       61 elkkliaqpv tlwiqqadrs yrpvngyvht arrlgadggl ttyqltfadf thflkfrrdq
      121 riwndttvdq iisdvlnqhp qarghfrfal sqplpsrsyt rqhdtdwhfv hrlmesegly
      181 ttwqqaddgk shtlvitdnl qafaplspqt vrfyrggaas dadaftqwsg trtlqsvtrt
      241 trtfdyknps qpsnpkgttl ptmagqgefp dqlevyeytg aytyldqtrg dhltkirmee
      301 wesqakrfhg aggvraidag rrftlsdhpe hdrdpadqre fatigvdwwi ennlpvasss
      361 adfpyslrea ltqaqegyga dpafrvphdd gsvgfylvev eaqrvsvpyr spfehekpkm
      421 hletaivvgp qgeevytdel nrirvqfvwd rlnpgnenas cwvrvvqsdt gggyggvhvp
      481 rigeevlidy vggdcdrpla vgrvynganq pqwhsdgils gyrskeylgs gynqlvmdda
      541 tgqnrvqlms ssansllhlg yiidqngntr gsylgsgfdl rsdaygavra srglyvtthp
      601 kaansqpldv teaqqqlvsg esliealsgv seqhqaeslk daqeamraft datqdrasgn
      661 asggrtaggg tgsanafkep vmlfgspsgi amstqeslhm vandhvnvas gqsvhvaagk
      721 sligsigqkl slfvqnagmk lfagkgkvei qaqsdnvevt aqkavkvvsa tdrieiaadq
      781 gilltsggay irvkdgnvei hapgkidvkg ashtfagpas lgyplpsarp dqpgqlelfh
      841 kymngeavkg glftvkdvng tvlkkgaldn sgytvvsglp pgavrvefgk dprasdqpan
      901 yfkqakwpae pvapspeaaq aaasgqlasq lqgmapaast aamgfasgsg agaalgglag
      961 aalpaaaaav ggagvasavq tasslsgaak qvaamvqtar qgglaalaap aanaasgalq
     1021 salpgvagva gkaatttata saaggmklpt sgfggplks
//
LOCUS       WP_176044539             504 aa            linear   BCT 11-JAN-2025
DEFINITION  MDR family MFS transporter [Burkholderia vietnamiensis].
ACCESSION   WP_176044539
VERSION     WP_176044539.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..504
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52543
     Region          38..422
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(39..40,43,74,124..125,127..129,132,152,155..156,159,
                     284,287..288,291..293,296,324,328,381..382,386,390,406,
                     409..410,413..414,417)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 metntlvavp ptaaagrdap sgpivaalll vmllsaldqt ivstalptiv gelggldrls
       61 wvvtayllss tvvlplygkl gdlygrkvvl qaaialflag salcgiaqdm pqlivlralq
      121 glgggglmvv tmaaigdlvp pdrraryqgm fggvyglati vgpllggflv ehlswrwift
      181 inlplgalal avigvafrpq aapvkhridy mgaaflatal tcvilftseg gsllpwsspq
      241 lwltlvlgav aiggfvyeer laaepimple lfrqrtfvlm sligfvvgia lfgsvtfipl
      301 ylqvvkgstp sqaglqllpm mggmltmsva sgrliarfgt yrpfpiagtl lggvamalls
      361 tlsldtslht iyaymallgi glgmvmpvlt lavqnavefq hmgvatsgat lfrsiggslg
      421 vaafgalfsh glqsrleqal panvtlpaal gptavqqlpa avrdaylhaf agslhgvyla
      481 atgviaiafv lawfverapl rtrr
//
LOCUS       WP_176044550             840 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_176044550
VERSION     WP_176044550.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 840)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 840)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..840
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..840
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=91324
     Region          1..771
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 malfevprtl svagaalply ggqpiltpvk ltgsetigel feytlelktp dalafsqsia
       61 anvnldklig teltvsiqle gkghfipglv gnagmaniga gtreitgvvs haailredgr
      121 sivyaitlrp wlwhatkncd crifqdmsvv eitdavlaay pfpvdkqltt prpnkawpkr
      181 diqrqhfesd wiflqrlwee wgifyffehs egkhrlvlcd smgalkpqad ayatvryeap
      241 tgrrideehi halsishalt tgavtsvdyd ytwpradlki gredprdtal arqehytwgd
      301 yaqpqagaag lsgdhndprt eaeyltlvqm qayrcqglra sgkgnlrgmv pgqtfvlshy
      361 pqdaanreya viasrltiee vgeasgsgqr yhcevdftlq ptnepfrllr tiakphitgv
      421 eyavvtcpen qeiwtdsygr vklqflwdrl gkndehsscw vrqagawhgd qfggiflprh
      481 gqevtvsfin gdpdlpiivg saanafnmpp yelpknqala ayrsreiggr ranslvlddt
      541 ngkiqahlss degssqlnlg yitriagnsg rqdergrgae lrtdgdgvfr aatgmlltte
      601 grpnaqgqak amsetirrle daqtlhaals raaqegqaqe adghqsdlak tieaqngqir
      661 gvandanpfp efsephllia gkagvevttp atvhvaaqqv avtseghvgi aggrslfasv
      721 rdtislfaqr aairisaamg diilhavtss irlesaksiq lltkviqitg verlelhggk
      781 trmvlddsga qiftpgkfva fasthslpgp hdspislapk giciecmlka arggsalvlr
//
LOCUS       WP_176044553             911 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            vietnamiensis].
ACCESSION   WP_176044553
VERSION     WP_176044553.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..911
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=98232
     Region          1..788
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mlsltqartl sisgaalpty stgglpafap vrlqgsevvg rledcrylvt lrtddafafs
       61 psvtanldld kivgtevtvs iqlegigqfi pglagnaglg nigagtreit glvtaarvag
      121 edrhsilyel elrpwlyrat ltqdcrifqd msvveitdav lakypypvdk rlagafrgiy
      181 pkrdvqrqaf etdwaflqrl weewgiwwwf ehesghqrlv lcdtmgghhp hgaayetvry
      241 lspdgkride ehihalsvts rltsgsvtvv dydytrpran ltvteenprk tasadgavyd
      301 wgdysqplag aqgvegqpnd teqesrhlar vqlearrcag lrangrgnlr gltvgrtfal
      361 tgypqqaanr eyvvlsttld ieevgdrtga satyrceaqf ellpanepfr lersvrkpvl
      421 sgpekaivvg pagqevwtdk ygrvkvqfgw drqgkldeha giwlrvvspw qgadmgatfl
      481 prighevavm hyygdpdlpv itgspvnefr qptldlpanq avavlrgref qgtasghvai
      541 ddtqgqiqtq iasdagssvl algnirrivk ktgradargk gfdlrtdywg vvralmglfi
      601 stdgqpngag qtkeakaavg rltrarelqe slsglaqhhe aqqrdadqse vakaikarnd
      661 airgdtpage ndfpelkepd lvlasaagvs vaaersvhma snediavtsg rhvgfavghs
      721 lfasvsnafs lfvhkagmkl iaaagkvrie aqtdgidvka kqsvgvmstt dsielhaake
      781 ivlhagstqi risdqgytvh tagehtihag shqtdgpqgq gggfppfpks gpgqlevlrh
      841 yvtdapvdkn tiavtdslga vhkgtldasg rtivsglapg avtvqyghdp hdswamssyl
      901 rqpswnpaga a
//
LOCUS       WP_176044587             485 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia vietnamiensis].
ACCESSION   WP_176044587
VERSION     WP_176044587.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..485
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53097
     Region          74..449
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mierrisirl iagavalvvl agcttfsrdg gfntvsttas erlgkealfv rteqdrdava
       61 qrtrellgkp lamddavqva llnnaglqas yaelgisead lvqagrlpnp gfsfsrthws
      121 dnfgitrtfs anvlailtlp latriesrrf eqtkletada mlkvaadarr ayvsavaaeq
      181 sakyaeqvkd sasagaelah rmqqagnasr ldyareqafy adaatqvaka rqqafaarek
      241 ltrvmgvwgt atqyslperl pdlpkerpel kdlevfamqn rldiqaarlr tqgvatslgl
      301 skatrfvnal evgylnnfet dkghergyei sveipifdwg sakvaraeal ymqsasklaq
      361 tavdarsevr esyvayvtny diarhyrdev vplrktisde mllryngmla safdlladsr
      421 eqfnavngyi dalkdywlae tdlqlalggr lpppdrpvda farsnqqsat aaatlaapht
      481 qsegn
//
LOCUS       WP_176044818             111 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator, partial [Paraburkholderia
            phenoliruptrix].
ACCESSION   WP_176044818
VERSION     WP_176044818.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia phenoliruptrix
  ORGANISM  Paraburkholderia phenoliruptrix
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 111)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Paraburkholderia phenoliruptrix"
                     /db_xref="taxon:252970"
     Protein         <1..111
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
     Region          <1..109
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 pgeavpavvp vsrlrlfres ilvagsnpkt miflsafmpq fidhqrllpl qfaqmyltia
       61 llvlvvhtiy ssgvrhlhgr lragravaam rrmtglvfvg fgvelltakq p
//
LOCUS       WP_176044907             452 aa            linear   BCT 11-JAN-2025
DEFINITION  TrkH family potassium uptake protein [Lactiplantibacillus
            plantarum].
ACCESSION   WP_176044907
VERSION     WP_176044907.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus plantarum
  ORGANISM  Lactiplantibacillus plantarum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactiplantibacillus.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Corratge-Faillie,C., Jabnoune,M., Zimmermann,S., Very,A.A.,
            Fizames,C. and Sentenac,H.
  TITLE     Potassium and sodium transport in non-animal cells: the Trk/Ktr/HKT
            transporter family
  JOURNAL   Cell Mol Life Sci 67 (15), 2511-2532 (2010)
   PUBMED   20333436
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Durell,S.R., Hao,Y., Nakamura,T., Bakker,E.P. and Guy,H.R.
  TITLE     Evolutionary relationship between K(+) channels and symporters
  JOURNAL   Biophys J 77 (2), 775-788 (1999)
   PUBMED   10423425
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415019
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Lactiplantibacillus plantarum"
                     /db_xref="taxon:1590"
     Protein         1..452
                     /product="TrkH family potassium uptake protein"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015079 - potassium ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49703
     Region          19..447
                     /region_name="TrkG"
                     /note="Trk-type K+ transport system, membrane component
                     [Inorganic ion transport and metabolism]; COG0168"
                     /db_xref="CDD:439938"
ORIGIN      
        1 mimrqlahfk ffdtlskkmv agfiililig tvllslpwat panvhtslid vlftsasatc
       61 itgltvvnta ahwttfgqlv ilvlsevgal gymtfavllf nimrrqigls tqlmvkasln
      121 lerlsdtksv mkyvvglsll fqlgglglla idfvprfgwr hglyvslyha vmsfcnagfd
      181 vfgdslqgfr ndpyvltvtm iliiagglgf lvwrdvllyh trkrltlnsk ltllttfslf
      241 vigfvlllit erdlellptg mpwvnrtint lflsvtprta glitmptqgl qagsllvimi
      301 lmfvggtpgs taggiktttf gvlmfqsiaq lrgrrdvefs hrrfsqenin ralmliflas
      361 ivltvatlil tqtekipkgf gleyvlfevl safgtvglsl gltpnltlig kivimmlmfi
      421 grvgiftsly alsrrqarvn lirypaenil ig
//
LOCUS       WP_176044925             145 aa            linear   BCT 11-JAN-2025
DEFINITION  GAF domain-containing protein [Lactiplantibacillus plantarum].
ACCESSION   WP_176044925
VERSION     WP_176044925.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus plantarum
  ORGANISM  Lactiplantibacillus plantarum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactiplantibacillus.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Heikaus,C.C., Pandit,J. and Klevit,R.E.
  TITLE     Cyclic nucleotide binding GAF domains from phosphodiesterases:
            structural and mechanistic insights
  JOURNAL   Structure 17 (12), 1551-1557 (2009)
   PUBMED   20004158
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Ho,Y.S., Burden,L.M. and Hurley,J.H.
  TITLE     Structure of the GAF domain, a ubiquitous signaling motif and a new
            class of cyclic GMP receptor
  JOURNAL   EMBO J 19 (20), 5288-5299 (2000)
   PUBMED   11032796
  REMARK    Erratum:[EMBO J 2001 Mar 15;20(6):1483]
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Aravind,L. and Ponting,C.P.
  TITLE     The GAF domain: an evolutionary link between diverse
            phototransducing proteins
  JOURNAL   Trends Biochem Sci 22 (12), 458-459 (1997)
   PUBMED   9433123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10588018
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Lactiplantibacillus plantarum"
                     /db_xref="taxon:1590"
     Protein         1..145
                     /product="GAF domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=15995
     Region          <52..>120
                     /region_name="PtsP"
                     /note="Signal transduction protein containing GAF and PtsI
                     domains [Signal transduction mechanisms]; COG3605"
                     /db_xref="CDD:442824"
ORIGIN      
        1 mtlaenanqr nyqhlvdqly qtsdfdfvgv alqanqaphq itwqyvagnr geqfrkiilr
       61 sgigiaglvv rtgkpfwnna lqnatytdvl ytpiaqaecl tsaaaipivt tefrlvtgvl
      121 lasyrstqtv sdqtisrlsh ylatf
//
LOCUS       WP_176044953             458 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Lactiplantibacillus plantarum].
ACCESSION   WP_176044953
VERSION     WP_176044953.1
KEYWORDS    RefSeq.
SOURCE      Lactiplantibacillus plantarum
  ORGANISM  Lactiplantibacillus plantarum
            Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales;
            Lactobacillaceae; Lactiplantibacillus.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Lactiplantibacillus plantarum"
                     /db_xref="taxon:1590"
     Protein         1..458
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50921
     Region          1..442
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 mfqlrdyqqe svdavynsti hghhsivvqs pprtgktvim adiarratak gnqvlfivhr
       61 reileqaeat fkqddvnmsl ckmgmvqtit rhideltkpa iimideahha lsksyqriiq
      121 afpdalkllf tatpwrmdgk gldviaddiv lgkpisqlid qgflapvdyy apseidvtql
      181 ktkrngefde ksidqavkpk iygnavkhyl klapgkqaia yaynvasaer ladafnqagi
      241 taravsgktd rttreqivas yragkiqvvt naelftegld lpnvdcviml rptqslslyl
      301 qfamrsmnpr vgkraiiidh vnnverfglp tvdrqwilgg rdkhskssng spiksvsvcp
      361 ecfatfyrkg eicpfcgael geekvietde siklkkiean krlalakeia ennaakavad
      421 ktpgelttya eikayaklhn fkpgwafyqa klkglirk
//
LOCUS       WP_176045080             463 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1644].
ACCESSION   WP_176045080
VERSION     WP_176045080.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..463
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46915
     Region          31..430
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,157,
                     160..161,164,288,291..292,295..297,300,328,332,385..386,
                     390,394,410,413..414,417..418,421)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msdcnpvpvs vpltaasrpt areqrftlal vaigmfmavl dstivnvalp amrtslgatv
       61 aelawivday tlsfaalila ggalsdrfga khvylaglal fvaasaacgv assvailvaa
      121 rfvqgmgaal flpaslavvr stfdvpaera raiavwagia svavavgpvl ggilvddfgw
      181 rsaflinvpt gavafagaav lvaastarha hpfdwagqgv gaaalgalcf avielptrgp
      241 gaaevrcall aaacaaavlv vverrarhpm vplawfrnrv fvamnlmgsl vyvgyfgllf
      301 vlslylhgrf gmsarqtgmt llpfalslsl gnllsgklhd rvrpvtlman glgmaalaip
      361 aiavaltlra pwpvvwaama afgtgtalsv apmiatvleq vpadaagvas gflnaarqag
      421 slfgvaiaga atillpdltd alwavaalgc vayasaafaa rta
//
LOCUS       WP_176045090             184 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176045090
VERSION     WP_176045090.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..184
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19833
     Region          42..177
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 mtnrlppfdp asatdeqkav ladilsgprg nlngpflgwi aspelaqhaq klgafcryrt
       61 glplrlsela ilvtaarwrs qaewhihhpi aldagvpaat adairlgvap afesdddali
      121 hafaselydt rrvsdatfar aqarfghetv vnlvallgyy alvamtlntf gmradgqtel
      181 pfpe
//
LOCUS       WP_176045100             160 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia sp. BCC1644].
ACCESSION   WP_176045100
VERSION     WP_176045100.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..160
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17373
     Region          <39..135
                     /region_name="ElaA"
                     /note="Predicted N-acyltransferase, GNAT family [General
                     function prediction only]; COG2153"
                     /db_xref="CDD:441756"
ORIGIN      
        1 mtphdtlftv apidavqthp lratillngd lnacelagdh apttlhvgvr dgrsslvaia
       61 slceeprddd parpawrlrg mavhpavrgm gfgrvlvqvc vrhaeargaa lvwctareaa
      121 yrfyeklgfv adgapmtmpg rtdtafyvmr ryidrhsppa
//
LOCUS       WP_176045126             226 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: CDP-alcohol phosphatidyltransferase family protein
            [Burkholderia].
ACCESSION   WP_176045126
VERSION     WP_176045126.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Sciara,G., Clarke,O.B., Tomasek,D., Kloss,B., Tabuso,S.,
            Byfield,R., Cohn,R., Banerjee,S., Rajashankar,K.R., Slavkovic,V.,
            Graziano,J.H., Shapiro,L. and Mancia,F.
  TITLE     Structural basis for catalysis in a CDP-alcohol phosphotransferase
  JOURNAL   Nat Commun 5, 4068 (2014)
   PUBMED   24923293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Koga,Y.
  TITLE     From promiscuity to the lipid divide: on the evolution of distinct
            membranes in Archaea and Bacteria
  JOURNAL   J Mol Evol 78 (3-4), 234-242 (2014)
   PUBMED   24573438
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Koga,Y.
  TITLE     Early evolution of membrane lipids: how did the lipid divide occur?
  JOURNAL   J Mol Evol 72 (3), 274-282 (2011)
   PUBMED   21259003
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..226
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=23911
     Region          37..212
                     /region_name="PgsA"
                     /note="Phosphatidylglycerophosphate synthase [Lipid
                     transport and metabolism]; COG0558"
                     /db_xref="CDD:440324"
ORIGIN      
        1 mdqrktatra epplprtwda rlarslvrpl vdtpvtpnhl ttlrlligla gawclahggf
       61 gwsnagafli vlsnfvdhtd gelarisgks skighfydla adalvtvalf vsmglgivaq
      121 ggqmaaspvl lgavagaava lifflrmrie siagkagtkq afaggfeted vlyllpivtl
      181 vdgvepflla asigaplfaa wvvidwwriv rrgntpqnpt eiqask
//
LOCUS       WP_176045141             541 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [Burkholderia].
ACCESSION   WP_176045141
VERSION     WP_176045141.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..541
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57578
     Region          20..463
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mpgqgnaqps vplsrsahpd aghgkfkkql sltdltfigl gaifgsgwlf aashvstiag
       61 pagifswllg gfavlllgiv ycelgaalpr aggvvrypvf shgpllgylm gfitliafss
      121 liaievvaar qyaaawfpgl taegssdptt lgwlvqaall cfffylnyss vktfakanni
      181 isifkfivpl avigvlftff kpanltvhgf apfgmpgiem avsaggiifa ylgltpivsv
      241 asevrnpqrt ipialilsil lstliyvllq lafigsipta mlaagwhdvs kafslpyrdi
      301 alalgvgwla vmvvadamis psgcgniymn atprvvygwa ktgtffkvft rvdeasgipr
      361 aglwltfgla ifwtlpfpsw ealinivsaa lvlsyavapv svaalrrtap dlprpfrava
      421 fgitgpasfv iaalivywsg wstvswllgl qivmfviyla crrwvptahl slaeqvrssa
      481 wliafyaami vlsylggfgg tgqlahpydt vvvaavalai yywgantgvr adklqlddde
      541 d
//
LOCUS       WP_176045160             673 aa            linear   BCT 11-JAN-2025
DEFINITION  BCCT family transporter [Burkholderia sp. BCC1644].
ACCESSION   WP_176045160
VERSION     WP_176045160.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Ziegler,C., Bremer,E. and Kramer,R.
  TITLE     The BCCT family of carriers: from physiology to crystal structure
  JOURNAL   Mol Microbiol 78 (1), 13-34 (2010)
   PUBMED   20923416
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003438
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..673
                     /product="BCCT family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0071705 - nitrogen compound transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73380
     Region          3..514
                     /region_name="BetT"
                     /note="Choline-glycine betaine transporter [Cell
                     wall/membrane/envelope biogenesis]; COG1292"
                     /db_xref="CDD:440903"
ORIGIN      
        1 mpdsrpsprt tfkpqvvlpa lavigallvv calrpseaga lfsagqqwvi arfdwfyvla
       61 vtgflvflvl iaasdfgnir lgpddaepef sfvswtamlf aagmgiglmy fgvgepmqhf
      121 lkpptvdpgt paaareamlm tffhwgfhaw aiyglmglvl ayfgfrynlp ltlrsglypv
      181 lreringwig htvdafalvg tvagiattlg ygvmqlsagl htvggwdtgs nvfriglvav
      241 vvilagvsaa tgldkgvrrl selnlllafl llafvvvagp tlflfralgd nigqylshlv
      301 elsfrtyaya ppreegwfgg wtilywawwv swspfvgmfi arisrgrtir qfvigvllvp
      361 tafnlvwmtv fgnsaiwldt hgaagalaqt atnvdallfr ffdflpfsql lsivaivlia
      421 vffvtsadsg afvidqiatr gnahspvwqr lfwaallgvt aavllvaggl galqamtlia
      481 alpvaiimla lcyglwrgla adrahysqdv apatsfwtgq hwrhrlthil rqtteaearq
      541 fvaetvepal rkvsgelras gvdalvqrds ddavrltvpt aehrdfvygv rvtaksaaaf
      601 lvreaaepda arehvygivt ffedgrlgyd veylrgdevi advlrqyery vslaadkrth
      661 llsrapghat eae
//
LOCUS       WP_176045196             285 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176045196
VERSION     WP_176045196.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..285
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30173
     Region          4..>170
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
     Region          91..278
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(106..107,109..110,113,117,119..125,208..213,
                     219..220,222..223)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mktldieavq afvltadlks ftraaeamdt tqsavslkik rledglgrrl lertprqvrl
       61 sadgmaflep arelvaahhg avgafgtgqr rlvigvshhv vgadlpmllr rmseaepalv
      121 leirvaasrd vldafdrgql daavalqhds rrldgetils esfgwmaapd feyhppqplr
      181 latqaepcsv rrmavgalde agvawtevfv gggvatigaa vsaglavaal ghrvapagtv
      241 dvgtryglpp lptrdvvlhs nltdararqa lrtlgaalrs svgmr
//
LOCUS       WP_176045257             444 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176045257
VERSION     WP_176045257.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..444
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=47224
     Region          32..421
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msaslaassp spqpalrllp addadranda rvaalldrla pelaadaarn dvdgrfphen
       61 farlhragli aqvvprehgg ggatlarasr ivaavaradp atalvltmty lqhralgrad
      121 nrwpaqvrra vfdsavahga linalrvepa lgspsrgglp atiarrdgdg wklsghklys
      181 tgipalrwla vwartdepep rvgvflvprd rdadgdrirv ieswnhlglr asgshevvfd
      241 dvrlpadhav dvrapeawav saathadada qadqqawmva llgslydava rasrdwlvgf
      301 attrapsglg aplatlprvq eavgeiegwl hanrvllddh ivrtdagtap pvttsglvkr
      361 tvteqairtv eqalklsgnh glsranpler hyrdvlcsrv htpqddaiav aagravldaa
      421 sasrmkagte easrseverg rpda
//
LOCUS       WP_176045271             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176045271
VERSION     WP_176045271.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33213
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..288
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mlsedelall dairatgsls raaarlgkap stvshaarql etrfdallfd rrgyrlqltq
       61 agqlltdeaa rlaldvarlt qrvrqvasgw edrlsivsde vlefdtllpv vrafdaldsg
      121 vslrfthevl ggtwealrdg radlvvgatn eppaipgfkw felgamewvf avsprhplaa
      181 vdgaltrdai gahravvvad ssrraagray gllggqavla vpsmrakila qrdalgvgwv
      241 prrrvtslla rgelvekqta gprepnllyv awhgdrdgra lqwwleqlre prlaqrlldg
      301 idvtg
//
LOCUS       WP_176045282             195 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC1644].
ACCESSION   WP_176045282
VERSION     WP_176045282.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..195
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20280
     Region          1..193
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msmlismaaf alassitpgp vnivalsaga rhglgaslry aagatlgfva lflliglglh
       61 aalarwpvlt tatqwsgiaf llymalrlal ddgrlsadpd vagpsaaaga amqwlnpkaw
      121 lacvaamgay aadgdrtqvw lfaalylvic fasiacwaya gaslrhrlan arrmrvfnrl
      181 malllagsal flldv
//
LOCUS       WP_176045287             251 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176045287
VERSION     WP_176045287.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..251
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=27456
     Region          38..246
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mhdhsvapsd aaarpadqpp epgplpalst lfgqcawfrt lapehqalvl aqsrveqcea
       61 gdviahrlap seywigvhqg llklaifnvs grgctfsgvp sggwfgegsv ikrelrkyev
      121 vaiqrstvlf vpvdtfhall dtslpftrfv ihqlnnrmge fiasiqnsrl ldvdarvaqa
      181 laqlfnpdly pdtgpslsis qeelgmlvgv srqrinqalq qleklgalrl aynqievvdl
      241 halarfgmeq l
//
LOCUS       WP_176045309             310 aa            linear   BCT 11-JAN-2025
DEFINITION  AEC family transporter [Burkholderia sp. BCC1644].
ACCESSION   WP_176045309
VERSION     WP_176045309.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..310
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31309
     Region          18..305
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 migpillala pvallvafgh glrrtgfiad afwpqaerlc yyvllpalfa dglanarlqs
       61 lpvlplaaal vgstalaaal lllvrpfvrv dgagftsvfq gavrfnnyvg talaaglfga
      121 kgialaavcv aaivptvnlm cvlvfarygd mrlgagalar qilsnplvva cvlgiamqag
      181 gvafpaavep avralgaasm plgllcvgaa lkfdaarawl rpvcvasafk flamplltla
      241 agravglgda altvallfqa lptssasyim arqlggdapl magitafqti aaalampvvl
      301 talasapafr
//
LOCUS       WP_176045299             382 aa            linear   BCT 11-JAN-2025
DEFINITION  epoxide hydrolase family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176045299
VERSION     WP_176045299.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..382
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42240
     Region          5..108
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          73..>199
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mhaapfdiai pdhalddlrr rlrdtrapml tpagawqqgv dgawlrelta ywaerfdwra
       61 aeralnrlpq fvadaggqrv hfihrrgvgp rpyplvithg wpgsvfefea lidrlcdpga
      121 fggdpddafd vvvpslpgfl fspapeapgm aafqvadrwa almsglgyrr fgaqggdlga
      181 gvsialgarh advvdaihln ylpgsyeppt daaapltede rafatqrgew aaleggyahv
      241 hmtkpqtlav alndspagla awiaekfraw sdcdgdvarr fshdtlltgi slywftgcig
      301 ssmqmywenr lqpmrfaagq rvavpvafar fpkeiscppr swlervfdva qwtdmprggh
      361 faaleepell andirrffrr fr
//
LOCUS       WP_176045303             418 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1644].
ACCESSION   WP_176045303
VERSION     WP_176045303.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..418
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44498
     Region          17..395
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(27..28,31..32,35,69,124..125,127..129,132,152,
                     155..156,159,234,237..238,241..243,246,270,274,325..326,
                     330,334,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 msvpaagvfr slrsfnyrvw aigslvsnig twvqrtaqdw lvltqlthhd asavgtvmal
       61 qfgpqllllp wtgyaadrfd qrkllmttqa lmgvlalalg altvagvarl ehvyvfaflf
      121 gcaaafdapv rqtfvaelvg drelanaval nstsfnaarm igpaaagfmi asvgtgwafv
      181 anglsffavl vsllllrede lranlragrs rgglldgfry vwrredlkai lvmlfligtf
      241 glnfqlfist maasvfhvda rgfgflssmm avgtvsgall aarreqprfr hlwfgaalfg
      301 lgctfaalap sywlfaaalv ltgiaaitfm nstnslmqls tepamrgrvm alrlavalgg
      361 tpigapvagw vanhlgprwa lgvgaasgfa aalvathfvk rsraqaqadg aldrydgv
//
LOCUS       WP_176045319             727 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176045319
VERSION     WP_176045319.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..727
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79143
     Region          39..722
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mkpqpaieqp sieparwrtw ldplgdaard waasdgliwl hlaktvlaal lamgiamrle
       61 msqprtamtt vfvlmqplsg mvfaksfyrv lgtaaglvaa lalgglfaqq pelymagitl
      121 wiggcialav rnrhfrwygf vlagytaali glpavmtpqt lfqsaltraa evalgiacsg
      181 avsalilpls sakalmrslg irhatfatft agalagdvar gdferrfadf vddivgfean
      241 rafasfedph irarsrrlar lnsefmnact rlhalhqlvk rlranhsdav ldalaphvda
      301 lalrfaalrd erqhgvtpat gallelrrfh salpkaaras rrtieahaag glldfdtaie
      361 llyrfigeyl gyadtyasld qddhafersv thyavktnsf fvgfaflrti vavgamsafw
      421 iasewpsgpl aviataiaca lsstsprapk fvaqmsvgaa fatavgygfl cyvypnidgf
      481 pllcatlapv lglgaflamr pglsgygigf avffcllagp dnaiaytpev linnglaivi
      541 amlacslvfa vvfpthmpwl tgriahdlrr qvtlacegap dglaqrfqss thdlmaqlrt
      601 llvrrtrqhr damrwmlstl evghavidlr deleafsask ppqtlrwtas idavlkelpr
      661 ffddptpghh artlksvnla iraaqhtlqa wyavpdarrs mqrivgclhf mrsalldkda
      721 pfnrhrh
//
LOCUS       WP_176045320             315 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [unclassified
            Burkholderia].
ACCESSION   WP_176045320
VERSION     WP_176045320.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..315
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34428
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdtlqnmrvf srvvetgsft aaaqslnstt gamsravsel earlrtrlmn rstrrlalts
       61 agesylrrcr qiladvdrae eeascaherp agvlrmhsfa svghhyvlpa ltryhaqfpd
      121 vsielslsqr mpdlfdgtsd mavvtasslp dselvshllg stfsilcasp dyvkrhgvpa
      181 rpqdlaahac ltlctpafpt hewvlegpeg veqihvagpv qtntaeslal airdgigigm
      241 lplysaidal rdgtlvrvlp ahilqkmnvy alypsrrfvd akvrtwveml raqvpgmiar
      301 dvemlnaidr epqaa
//
LOCUS       WP_176045334             473 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia sp. BCC1644].
ACCESSION   WP_176045334
VERSION     WP_176045334.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..473
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=50987
     Region          83..470
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mtarpafpsp dasgssapra psrllrraaf vlgaavlgyg afaiafpaqv paaigtvvad
       61 wtganphpvv lqrpaaqpls avaqlgralf hdpslsasgk qscaschspd haygppnald
      121 vqpgglamtq qgyrpppslm ylyrqpnfsi gpdagendaa psvaqqaasa agvvkaqkva
      181 gtsaapqlvp qggmfwdgra dtlqqqafgp llnpvemans siedvahkla qsshrvqfek
      241 lfgarvfdsp qlavseamfa iaryqvedps fhpynskydr wlegrarltq aelrglrlfn
      301 dpdkancagc hlskpgkdgl ppmftdyqye algaprnkal aqnrnpafyd lgvcgpfrdd
      361 lkdqtqycam fltptlrnsa trhvffhngv fhtldqvmaf ynersispqk fysrgadgkv
      421 deyddippky ranvdvtdap fdrkpgdtpa mtaqdikdie aflgtlndep aqh
//
LOCUS       WP_176045358             460 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia sp. BCC1644].
ACCESSION   WP_176045358
VERSION     WP_176045358.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..460
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49563
     Region          3..451
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mkqpedqlhr gleerhinlm algatigvgl flgsatairt agpailltyl lggiaiflim
       61 ralgemaitn pvagafsrya rdylgplagy ltgwtywfvw ivtcmaeita vgvymhmwfp
      121 gvpnwiwala almamgsvnf iavklygefe fwfalikivt ivlmiigggl miafgigngg
      181 vatgisnlws hggfmpngin gviaalpivm faylgvemlg ltagearnpe ksltkavnsv
      241 fwrvlifyig alfvimslyp wdqigtqgsp fvmtfsrlgi paaagiinfv vltaalsscn
      301 sglfstarml ynlaqqgqap amlgrvnrsg vpvygvivsv allligvlln ylapqhvftw
      361 ltsvstfgai wtwcviliaq mrfrrtlsad kiarlpirvp fyplgsfval gflalvvvlm
      421 aftpdtrval vigpvwivll giayalfyan rpaasaptks
//
LOCUS       WP_176045347             858 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia sp. BCC1644].
ACCESSION   WP_176045347
VERSION     WP_176045347.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 858)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 858)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..858
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..858
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=92914
     Region          60..712
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mhpfqssstr vnrrnvssvr afcarwvara qpvaaaavar vkplaatawr hvrhptrrgv
       61 lltaaavpal flvyvvvlip ftpgigdirk arvdqpaqvl sadgkllaef kpsnrewvpl
      121 kqisphmvda liatedhrfy ehhgldwkrt asaalhtfsg srqggstitq qlarnlypde
      181 igraptltrk vkeaitalki eavyskdqil etylntvpfl ynaygvemaa rtyfdksade
      241 ldvldsatlv gmlkgnsyyn pvlnperalq rrntvlgqmv kygklspaqf aqlqrrplri
      301 dferqkeppg paphfaqqlr kwliawadrn dyniysdgli vrttidsrlq qmatqaltlq
      361 gnqlqgiann awsgrdgcgt dnevfrtfmr espeykaaqd agkddaaamk llagdrgfmr
      421 alckaktdvq agflaidprd gqirawvgsr dftsepfdhv aqarrqpgst fkpfvygvaf
      481 angmkpddtf idqpveiplk ggeiwrpndd vpptgkpmtl rdaialsrnr itaqvmekvg
      541 paavarlard mgvrespler vpslalgtsp vtlkemvasy atiangglyv epqmvtrien
      601 rqgevlaeya papperalda etdktllgvm rdvvtrgtgg sirtrfgirg dvagktgttq
      661 dnadgwfilm qpglvagawv gfddgrvtlr sdywgqgahs alpivgdffq raqrarivda
      721 kakfdtepsp gwfaslrerv tdlfdtwfpp epkkapapgr aqrierppea degaasdasa
      781 asapeaasgg vveewvpase vaasaaalsa gasqpqpaqp pasasmtsgs sagigaaspa
      841 apvqppapsa pdatgasq
//
LOCUS       WP_176045382             396 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176045382
VERSION     WP_176045382.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..396
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=43695
     Region          223..389
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 metrwapqes qatsdeadig vadfselmar iyqgpletpp wagalelvrr wlqanyvtli
       61 lraaasdrra plsvhasefg pvvpgegqaa yndyyysldp fvglpadrvv tvddvfgdtg
      121 wlsselykqf lkpqdvryil gadlrtpsgv ecrfrvcrnh askqfsardk aicalllphl
      181 kraielhsrl dsaeversiy anaidrmqvg tialdengti idmnsvadei lkqnngltia
      241 rgtieatdaq enrtlkrlir havmghhgta tatveampit rsfdkprlgl lvrtvllsdw
      301 sednkrrpav tlflrdpdrk pqgaqeiirk lfdltpaets lallltnglt leeaaeesgi
      361 skntarthlr aifsktgvtr qatlvrillg svvplg
//
LOCUS       WP_176045416             206 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176045416
VERSION     WP_176045416.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22178
     Region          3..169
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnassgaevr qhilniakpi mlhkgfsavg lneilaaagi pkgsfyhyfg skesfgeall
       61 esyfegylah ldnllkhqag tgaerlmtyw gnwlhtqcad dpegkclavk lgaevsdlse
      121 amravlrrgt sqiierlagg ieagladgsl ravddpphta ailyelwlga tllekihrnr
      181 qpleramaet lrmlnltpaa qggaqs
//
LOCUS       WP_176045418              99 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: putative quinol monooxygenase [unclassified
            Burkholderia].
ACCESSION   WP_176045418
VERSION     WP_176045418.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..99
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=11050
     Region          3..92
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 malhviaslf lkpehaqtae aelrsmvakt rtepgnrryd lfreqdgspn lhlyeiyddq
       61 aafdahlasp yfgefrtksa dwftappvik vlsgidvae
//
LOCUS       WP_176045465             481 aa            linear   BCT 11-JAN-2025
DEFINITION  sialidase family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176045465
VERSION     WP_176045465.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 481)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 481)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 481)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..481
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51136
     Region          144..428
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Region          177..238
                     /region_name="Sialidase propeller 2"
                     /note="Sialidase propeller 2 [structural motif]"
                     /db_xref="CDD:271234"
     Region          243..302
                     /region_name="Sialidase propeller 3"
                     /note="Sialidase propeller 3 [structural motif]"
                     /db_xref="CDD:271234"
     Region          311..364
                     /region_name="Sialidase propeller 4"
                     /note="Sialidase propeller 4 [structural motif]"
                     /db_xref="CDD:271234"
     Region          375..428
                     /region_name="Sialidase propeller 5"
                     /note="Sialidase propeller 5 [structural motif]"
                     /db_xref="CDD:271234"
ORIGIN      
        1 mrrtivspsl virlsaamam aaaatahaep vvvsgpspfa actiggpgtn yvnaevepwl
       61 avnpanptnm igvwqqdrws nggahglvag ytfdggatwa rtpqpfsaca pgglkyeras
      121 dpwvsfgpdg taysvsisfn qsnngnavaa svstdggqtw srpavliand epttqffndk
      181 esvtaspvka gtayavwdrl elpngnpyan lhtqafrgpt lfskttdggk twsaakvivn
      241 vpsrqqtign qivvdpksgt lydffdliqp pfskaagkva fikstddgat wtkpqviarl
      301 qtvgvtdpnt gepvrtgdii pepaidpasg qlyvvwqdsr fnggkydeia vstskdggat
      361 wstpqqlntp tgrpafnpsv rvdntgavmv tyydfrdlqa gntttlptgf wrkisldggt
      421 tfaterrvgg pfdmklapna egffigdyqg ldvrpsssfh pffiqtnagn ltnrtdvffa
      481 p
//
LOCUS       WP_176045509             314 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Burkholderia sp. BCC1644].
ACCESSION   WP_176045509
VERSION     WP_176045509.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..314
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31614
     Region          2..314
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtilviaehd nasikaatln avaaaqalga agggdvhvlv aghdaqaaad aaakiagvsk
       61 vlladaphla dglaenveat vmniakdysh ilapataygk niapriaakl dvaqiseitg
      121 vvsadtferp iyagnaiatv qsgdaikvvt vratgfdpva aeggnatvek ievaadagqs
      181 rfvsrevtkl drpeltsani ivsggrglgs genytkvlep ladklqaalg asraavdagy
      241 vpndyqvgqt gkivapqlyi avgisgaiqh lagmkdskvi vainkdpeap ifsvadygvv
      301 gdlfalvpka vaal
//
LOCUS       WP_176045520             358 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia sp. BCC1644].
ACCESSION   WP_176045520
VERSION     WP_176045520.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..358
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=38164
     Region          29..358
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mksfarrasr tsvkliaaaa cvaattpaha qssvslygqv dewvgatkfp gsdrawnvsg
       61 ggmstsywgl hgaedlgggy kaiftlesff raqngqfgrf qgdtffarna yvgidspygt
      121 vtagrltthl flstilfnpf ydsytfspmv yhvflglgtf ptypsdqgav gdsgwnnavs
      181 yaspsfggln fgamyafgnq agdngskkws aqfnyangpf aatatyqyvn fnngprdlsa
      241 lvagmksqgi alvgatydlk lvklfgqymy tkndqvagsw hvntaqggvs vplgagnama
      301 syaysrdagg ldqtrqtwav gydyplskrt dvyaaymndr isglsngntf gagirakf
//
LOCUS       WP_176045556             397 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Burkholderia sp. BCC1644].
ACCESSION   WP_176045556
VERSION     WP_176045556.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..397
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44270
     Region          48..393
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mpppvpsdta lrplpidslt vpaaldgrag tnrsgsahpq iaaandldav rawlarfvdt
       61 pttfqnyrke aerlllwavi acgkplsslt hedlvvyrqf llapapadlw canggrkhpr
      121 ddprwrpfyg plsaasqrqa lvilnvmfsw lvqagylagn plalsrqrqr rpaprvtrhl
      181 gqplwqsvkd aiaamprdda rasfhadrar wlftllylgg lriteaadtt mgqffcrrda
      241 nghdrwwldv tgkggrqrlv pataemmael sryrrahglp alpsdgeptp lvlpvgqtrk
      301 pltraalhri vkqvfrhaad qlrangeagd qqarvleqas ahwlrhsags hmadgrvdlr
      361 lvrdnlghvs ltttsqylha dddwrhqete ekhrigw
//
LOCUS       WP_176045573             294 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176045573
VERSION     WP_176045573.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..294
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29885
     Region          21..261
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mihfnltegv lvsslqaltv ldlagiaial llggmakgit gigvpliamp ilsqflpirh
       61 avlllsmpii lgnipqaleg gqvlatarki aapiagtvig nivgvaills lnpghaqaas
      121 gallivaaal mlaapklnlp eawqkpvgfa lgfgaalmes iasvpgplla tylissgatg
      181 rvftkqiaii lvvsivtlit tfsgaahasa adlaisaaas lpaiagmwlv rplrdkmspk
      241 ifrmvvllfv lvaasqmiwk sgvlrhgsph vaqgdsahav rnqqaapspv ahaf
//
LOCUS       WP_176045604             207 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC1644].
ACCESSION   WP_176045604
VERSION     WP_176045604.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..207
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22008
     Region          15..194
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msfalssgid qfkplavaay ilalsitpgp nnvmlaasga nfgflrtlph lfgitigatt
       61 lvvlsatglg vvfieypaar lalfvigaly laylafkian agrpaakdae tkpfsfvqaa
      121 mfqfvnpktw lmaanlivlf svdgegfiss vigicilmvv infpavsvwa vlgvgmqtml
      181 qterarviyn rtmallllac vpllfwk
//
LOCUS       WP_176045608              85 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl carrier protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176045608
VERSION     WP_176045608.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Moretto,L., Heylen,R., Holroyd,N., Vance,S. and Broadhurst,R.W.
  TITLE     Modular type I polyketide synthase acyl carrier protein domains
            share a common N-terminally extended fold
  JOURNAL   Sci Rep 9 (1), 2325 (2019)
   PUBMED   30787330
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 85)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   4  (residues 1 to 85)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10455525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..85
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=9301
     Region          11..67
                     /region_name="PP-binding"
                     /note="Phosphopantetheine attachment site; pfam00550"
                     /db_xref="CDD:425746"
ORIGIN      
        1 mseslqfkep irkrlaglfk dreigddddf fdlgasslsi velqvkieed fgvtvptakl
       61 mreptlagwt elyraaavaa avvek
//
LOCUS       WP_176045771             434 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1644].
ACCESSION   WP_176045771
VERSION     WP_176045771.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46372
     Region          9..417
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(22..23,26..27,30,69,127..128,130..132,135,155,
                     158..159,162,245,248..249,252..254,257,285,289,344..345,
                     349,353,369,372..373,376..377,380)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 maidsrvvrr vaaasvigat vewydfflyg vvagivfdkq yfpagdafvs tmlayatfav
       61 gfvtrplggl lfghlgdrvg rksaliltml imgvstagva flptyaqigm wapvllltlr
      121 vlqgiglgge wggavlmaye yapphrrgly aslpqiglai glclaagvva alsralpdaa
      181 flawgwrvaf aaslllvavg fyirtrvadt pefvalkrqr rdtklpvvel lanyrqaill
      241 gmgaryidgv ffnvfavfsi gymtrnlsis rgdallgvms aavvmcvfip vfgglsdrlg
      301 rarvyrwgat lcglsvlpaf wllqtqstnl lavwlalvip fgifyamayg peaalfaelf
      361 danvrytgis fvyqvsgifa sgltpivata llrvnggapw lvgayvmlsa llsivsarai
      421 ekrdamagva vram
//
LOCUS       WP_176045773             316 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia multivorans].
ACCESSION   WP_176045773
VERSION     WP_176045773.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..316
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=35193
     Region          25..75
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          110..309
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(125..126,128..129,132,136,138..144,238..243,
                     249..250,252..253)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mqffhsdlna mhhdlrrldl nlllvfdaly rhrsvaaaah elamspsals halarlrdai
       61 gdalfvrlgn emqptvradd iatwagdald amskglarar rfdpahsdrt fvfaatdyta
      121 favlpafvaq iqeaaprlri rvvhsdrkia vdelaagrid falgyheeav adapgiedfd
      181 wfsddyvvia saahptirrr ltldqylaar hvvvtpwnes rgvidyvldr lglardvavq
      241 lptvlaapfm iaqsallmtv pnraaqtlrh aapirlfpap feiprytlkv yshakhartd
      301 ahrwirarll earpha
//
LOCUS       WP_176045774             551 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia sp. BCC1644].
ACCESSION   WP_176045774
VERSION     WP_176045774.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..551
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=60153
     Region          1..537
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mtrsfdyvvv gagsagcvla nrlsdggrht vclleagpad nsmwihvpig ygktmfhpvy
       61 nwgfhtdpdp nmhnrrlywp rgrtlggcss ingliyvrgq qqdydhwaal gnrgwswrec
      121 lpyfrrlehn tlgdgptrgt ggplwasair qrhelvdafv aasnrlgvrt vddfntgdqe
      181 gvgyyqlttr nglrcstava ylkpargrpn lhvetdaqal kvlfegaqas gvryvqhgkv
      241 hevralrevi laagalqspq llqvsgvgpa alldrhgipv vadrkgvgen lqdhlqvrli
      301 yevtkpittn delhswvgra kmglqwalfr ggplaiginq ggmfcralpd esatpdiqfh
      361 fstlsadsag gsvhpfpgct ysicqlrpes rgtvrirtdd ardapsiqpn yldterdrrt
      421 tvagvrfarr vaaaepmapl mkrevrpgad aqtddellef creygqtifh psgtakmgva
      481 sdplavvder lrvygtrglr vvdcsimptl vsgntnvpiv mvaekasdmi ledareadrg
      541 rsvapaaeav a
//
LOCUS       WP_176045822             508 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Burkholderia sp. BCC1644].
ACCESSION   WP_176045822
VERSION     WP_176045822.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..508
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53945
     Region          16..491
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(72,74,78,81,85,118,121..122,131..138,143,146,149,
                     242,246,249,252,254,427,429..430,432..433,436,439..440,
                     442,444..447,456,460,462,476,483..488,490..491)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(158..161,169,184,187,217,234..237,240,258..260,292,
                     392,394,420)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(161,258,289,292)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnaavpqttl alptakllid gafvesqsae wgdivnpatq etigrvpyat ldevdaaias
       61 aqrafqtwkt tpigarlrim lkfqdlvrrn leriahtlta eqgktlpdaq gdifrglevv
      121 ehacsigtlq qgefaenvag gvdtytlrqp igvcagitpf nfpgmiplwm fpmaivcgnt
      181 fvlkpseqdp lstmqlvela ieagvpqgvl nvvhggktvv drlcthpdik aisfvgstrv
      241 gthvynlgsq hgkrvqsmmg aknhavvlpd ahreqsinal vgagfgaagq rcmatsvvvl
      301 vgkardwlpe lvekakalki naghepgtdv gpvvskaaha ritalidegv kagakleldg
      361 rdvkvpgyer gnfvgptifs gvttdmsiyt eeifgpvvvv leadtldeai alvnrnpmgn
      421 gvglftqsga aarkfqseid igqvginipi pvpvpyfsft gsrgsklgdl gpygkqvvqf
      481 ytqtktvtar wfdddatagg vnttialr
//
LOCUS       WP_176045845             523 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1644].
ACCESSION   WP_176045845
VERSION     WP_176045845.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..523
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52489
     Region          37..515
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(38..39,42..43,46,78,128..129,131..133,136,157,
                     160..161,164,288,291..292,295..297,300,328,332,384..385,
                     389,393,409,412..413,416..417,420)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msqsspasrp aaaaasraga rlpaaatlav asatcslivl dtnvvavslp siarsfhasf
       61 adiewvvsay mtafaacllp aggladrfgr krmlfaglal fflaslgcgv apsagwlita
      121 ravkgggaal lltaalavia nrfpegrdra rawaiwgmcm gvataiaplv ggaitqwigw
      181 rwvfllnlpv cvllaagarv aidesrdpha krvdaagsll fgaalacaia aligapahgw
      241 lsvatlgrla lavallaafi gaerwqarpm idlalfrrpr fvgavlamfg yaacaqvmmt
      301 flplylqnaf gmsavdaglg mlpfafamva gpslgaalaa rvssggvlag glvligagnl
      361 vtaaltasgd yrlvaigmfv tgcgagimng dtqkaimacv ppdrtgmasg istttrfsai
      421 vtavgvlgav laastharld allsaapglr afadapfmss llagdlaqal grvppsaagv
      481 laraapvafa sgfadaltvs gvlalgaavv ayklltqpmr dgv
//
LOCUS       WP_176045839             435 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1644].
ACCESSION   WP_176045839
VERSION     WP_176045839.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46715
     Region          25..427
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(39..40,43..44,47,79,129..130,132..134,137,157,
                     160..161,164,259,262..263,266..268,271,299,303,354..355,
                     359,363,379,382..383,386..387,390)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mstahpsaav spddalhgtl yrkvtlrlit lfclcyfaay ldriniglak lqmldalkfs
       61 dtvyglgagl ffggyilfev psnlvlqrvg aklwiarimi twgllsgatm fvhtpmqfyv
      121 vrfllgaaea gflpgvllyl tqwypdarra rivalfmvgl plssmigspi sgwimrafdg
      181 ahglggwqwl fllealpsvl lgfavlrwlp nsiesaqwln adekralran ldadpsgnks
      241 halgkaftdp kvwalglidl cvllglyavs fwlptilrdt gvkdayhigw lmvipnaaav
      301 latlycgass drarerrwhi vvpfmvsava lavaassshg tlgtillfsl inagaaaamp
      361 vvwalpstfl kgsaaaggia facsianlgg fgstyfigwl rdtfhsqsag lygfaacmvv
      421 gcalalaypa rlvnr
//
LOCUS       WP_176045885             315 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176045885
VERSION     WP_176045885.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..315
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34653
     Region          1..>169
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..290
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdalrsmrvf vraielgnfs avareegtgq ptiskivaaf eqelgvrlle rsttslaptd
       61 egrrfydrck rvldeyesav aevrgqtlrp agklvvnapl glgelrlnal vleflaawpe
      121 idvelhltdr vidlveegvd vairlghvlp pdavarhias sprllvatpg yvaqapalrr
      181 pedlakhayv gyartdiigs elqfargdet vtvpvhgryr vnssialrec flagqavgsa
      241 pawlvqdlid ggqlvrllpk wdmvpphalh lvyasrrhlp lrtrtflqfm tqripelpgf
      301 ratatpsait trptr
//
LOCUS       WP_176045888             141 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia sp. BCC1644].
ACCESSION   WP_176045888
VERSION     WP_176045888.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 141)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..141
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15557
     Region          20..136
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04667"
                     /db_xref="CDD:467552"
ORIGIN      
        1 mpqilapdta petsavpvke ratvvcyrde qvllvaraas rwalpggtik rgempleaah
       61 relceetgmt gqdltysmqf tglakvhhvf faevgpdqtp qanneiekck wfpidsvdgl
      121 rasiptkriv elvynheirk a
//
LOCUS       WP_176045930             106 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176045930
VERSION     WP_176045930.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002085
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..106
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11823
     Region          8..102
                     /region_name="ManC"
                     /note="Mannose-6-phosphate isomerase, cupin superfamily
                     [Carbohydrate transport and metabolism]; COG0662"
                     /db_xref="CDD:440426"
ORIGIN      
        1 mklglnesla rlddegtlft tlfrhgtldv elyrprvedm qtphtrdeiy viatgtsrfv
       61 vdgrecdvaa gdtlfvpafa vhrfvgfsdd fstwvffygp eggera
//
LOCUS       WP_176045965             818 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176045965
VERSION     WP_176045965.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 818)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 818)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 818)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 818)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..818
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..818
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86859
     Region          515..776
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mrhfllgwll aavvsaahaa apvpaaasaa tgtkpaltpq qaqqaldvle npreraqvet
       61 tlraiaavga lsapavaase aaaassasav saptaltsng lasmlvrqgs rwsteiggal
      121 keslrslldv gsvgswwhdr lvraderadl ahaiwimlav lapalfvewf akrllrrala
      181 avaarragts rptvpdsvip dddappdtsa ppdatdaaea apassqgqgh arrhttllhr
      241 mpralvslal rvvpllvfvg vasltmslig dagtpiesal ealidiyvic rlvtivsrlf
      301 fqpdarqlrl lhisdawadf aqrsiarivi vvgactaave iaasfglsea ghvallkava
      361 lvghvmisvl ilqcrqpvaa riraagadrp sfavignala dawapvsvfv vmalwfvwal
      421 dvhngyrvli tlggrsiavm igmrmvsivv fgalarlfqg rdedrtlvhl hayryypllr
      481 qivsgaigiv tlalllqtwg vpvfrafetg tighrlasal vtiaiaaiva lvvweaania
      541 ierrlqrwtr egnlvraarl rtllpmlrsl lfvmialvvv ltglsqlgvn vgpllagasi
      601 fgvalgfgsq klvqdfitgi fllmenamqv gdwvtlagvs gtveylsirt vrlragdgsl
      661 ytipfssvtt vnntnrglgn aavkvsiayg edidraiatl keigaalrdd pkyrdgilsd
      721 fsywgidqvd gaalalagqm qctdstrwsv qrefnrriae tfrergiria npqrsvvaya
      781 dgsrpvgnge ngshdgngva aetaprppsn deparkpn
//
LOCUS       WP_176045971             203 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176045971
VERSION     WP_176045971.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..203
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=21621
     Region          <33..202
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(77,79,83..84,87..89,91..92,96,99,108,110,112,
                     116..117,120..122,124..125,129,132,141,143,145,149..150,
                     153..155,157..158,162,165,174)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          77..108
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          110..141
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          143..174
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          176..201
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mrserftrai raaamtvala aiagcahlpd qpaygqadpa alrrydsdwf daarvgrvdi
       61 lralhdagyp vdttdgrgyt avilasydgq paaldyllsa gadacigdrh gntalmgalf
      121 rnepdiarrl idthcpidqt ngagetalgf atlfnrfeli pllvahganp nhvdrrgqsl
      181 lqlalthdna yaadalrqag arq
//
LOCUS       WP_176045992             291 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176045992
VERSION     WP_176045992.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..291
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31770
     Region          52..285
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mlkpevdslv phvpfsrrkf mqaalggafa aavlpvsaqt vttdsegldv dtieirsgda
       61 svpayraqpk dktnlpvviv iheifgvhah iadvcrrfak lgylaiapdl yarqgnaaky
      121 ptikelsehi vskvpdrqvt edldatvawa gknggdlarl gvvgfcwggr qswlyaehnp
      181 hvraavawyg fvegktdemt pfnpvdhasl lkvpvlglyg ekdanitqas ladmrkaiqt
      241 sdsklarese ivvypdagha ffadyrpsyv kadaeeswkr aiawlhkygv m
//
LOCUS       WP_176046007             232 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176046007
VERSION     WP_176046007.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17575897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..232
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=24433
     Region          1..149
                     /region_name="PgpB"
                     /note="Membrane-associated phospholipid phosphatase [Lipid
                     transport and metabolism]; COG0671"
                     /db_xref="CDD:440435"
     Region          <78..148
                     /region_name="PAP2_like"
                     /note="PAP2_like proteins, a super-family of histidine
                     phosphatases and vanadium haloperoxidases, includes type 2
                     phosphatidic acid phosphatase or lipid phosphate
                     phosphatase (LPP), Glucose-6-phosphatase,
                     Phosphatidylglycerophosphatase B and bacterial acid...;
                     cd01610"
                     /db_xref="CDD:238813"
ORIGIN      
        1 mfdlsshlwi mitafggagl tlplaitiav wlalgyswqr aaawlgvlaa aigvvaltki
       61 aflgwgigir awdftgfsgh amlstsvypv aiflalirtr tpvriagial glaagvavgv
      121 srvaldahsp sesitgcivg aiaalafiag swravphrws vpavvaslai vtvalhgitv
      181 pshrwvtkva lqlsgherpf vrarwkanpn yrpasqpssl qrtesstrtl rt
//
LOCUS       WP_176046045             138 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176046045
VERSION     WP_176046045.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..138
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14879
     Region          1..125
                     /region_name="COG3607"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]"
                     /db_xref="CDD:442825"
ORIGIN      
        1 mhkmvfinlp vadlprskaf yqalgyevvp eytndmaaci kisdtifaml lvrpffqtft
       61 gkaiidpatq vqvlsclsce nraevdaiva kalaaggsap qppreypnmy ghgfddpdgh
      121 awelmampld asgqgqvs
//
LOCUS       WP_176046109             416 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176046109
VERSION     WP_176046109.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..416
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=45703
     Region          8..202
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mnrqqswtrt aapgeiiyse gfagepvifl itdgkvelst rcddkrviva tlgrgeffge
       61 sallaaepra htakalsfcq ltvvpagmld deiervsall rhivrtmirr vkrkddqlat
      121 ythadfmpgv lsyahllalm anadaretsd swarrpmqah aaetsvplae virkcraiag
      181 hsrphvlaml rrmeklnlvs ieaaqadaag gatdyaassd arqvvtfdaa rvidraqqva
      241 dhdldlsins elelieladl esligvdktl llnklsngei adevfafrks kvlsyveqkg
      301 vayfsrrngr rggdvraled lvwvdqrtlf dvisafdtyd laklianldd ravadklfsv
      361 mtearrnevs wvmrreikld pieveeieqr vldavraaka paagvapvas tsssda
//
LOCUS       WP_176046086             261 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Burkholderia sp. BCC1644].
ACCESSION   WP_176046086
VERSION     WP_176046086.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..261
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=29118
     Region          2..220
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mnvlivyahp eprslngalr dfavehleaa ghsvqvtdly amnwkaafda ndvtdrapda
       61 rfdpsldskh afatgtqsed iareqdklkw adavilqfpl wwfsmpaimk gwvervyayg
      121 faygvgehsd thwgdrygeg sfagkramvi vttggweshy sprgingpid dilfpiqhgv
      181 lyypgfdvlp pfviyrtgkm ndarfeetra algrrlddlw teqpipfrrq nagdyaipal
      241 tlkdgiapgq vgfaahlahe h
//
LOCUS       WP_176046112             144 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176046112
VERSION     WP_176046112.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401225
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..144
                     /product="cupin domain-containing protein"
                     /calculated_mol_wt=15628
     Region          23..126
                     /region_name="cupin_bxe_c0505"
                     /note="uncharacterized protein bxe_c0505, cupin domain;
                     cd06980"
                     /db_xref="CDD:380385"
     Site            order(28..34,43,45,47,49,67,69,71,73,91,93,95,112,114,116)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380385"
ORIGIN      
        1 mstptttsfs hvrpqdtayr geglrdffly rdlgiaaatn gkvvaqlvra nhapvagtgw
       61 hrheaefhiv imlkgwarfm ygeqetlvaa gdcvhqapgi vhylfdyspd meyleivgpa
      121 dfksidvdgp cavppptpwg eaga
//
LOCUS       WP_176046127             206 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176046127
VERSION     WP_176046127.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22940
     Region          12..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpiptddpgr rarkriqmla hlaatgarlf dahgydavtm eqiaaeadva krtlynhfpt
       61 keavlahwle gelardlahl qrdvarrrtf asrigcvlda saawceqhpa yllaylrhrl
      121 vsigavepei dgengsdiaq vwwqlivagq ragelngtlq aeqlatwfhh lylaamlrwl
      181 tvpglslkre fqsiaklfie gaeakn
//
LOCUS       WP_176046159             241 aa            linear   BCT 11-JAN-2025
DEFINITION  ZIP family metal transporter [Burkholderia sp. BCC1644].
ACCESSION   WP_176046159
VERSION     WP_176046159.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Dempski,R.E.
  TITLE     The cation selectivity of the ZIP transporters
  JOURNAL   Curr Top Membr 69, 221-245 (2012)
   PUBMED   23046653
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Guerinot,M.L.
  TITLE     The ZIP family of metal transporters
  JOURNAL   Biochim Biophys Acta 1465 (1-2), 190-198 (2000)
   PUBMED   10748254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..241
                     /product="ZIP family metal transporter"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24453
     Region          27..235
                     /region_name="ZupT"
                     /note="Zinc transporter ZupT [Inorganic ion transport and
                     metabolism]; COG0428"
                     /db_xref="CDD:440197"
ORIGIN      
        1 mtptaklall tlppvlaacf galaaawrap gpktssviqh ftggivfaaa alellpqdra
       61 halfpvvvgf vlgialmlai ralsgtietr fedarlpvsl iivtaidlvi dglvlgiafs
      121 asdesgiilt valtlevlfl alsvsaalaa agigrmlsiv vpvglaalls iaaiagnaaf
      181 aglptniyaa llglgtvall ylvteellve ahevpetpfa taaffigfiv ffliegsvka
      241 g
//
LOCUS       WP_176046187             190 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Burkholderia sp. BCC1644].
ACCESSION   WP_176046187
VERSION     WP_176046187.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..190
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19786
     Region          15..161
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mttdprtdae rridivalcg slraqsynaa lldaaalvap rgmhvtrfdr lgefplfnpd
       61 aeypspaavr dlidrlnaad gvliaspeya hgvtgvmkna ldwvvgceav vykpvavlna
      121 sprathadaa lretlsvmsa rivepasitl pvlgsqldaa giaahppfaa aladalhalg
      181 aviaesrstr
//
LOCUS       WP_176046177             317 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176046177
VERSION     WP_176046177.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..317
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33433
     Region          9..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..294
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(107,111,150,164,166,229,246,273)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(108..109,113..114,116..117,120,124,126..132,193,
                     223..227,234..235,238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 madlrdvnln rlaifvavvd agsltaaaer lglaktvvst hmqrleseig anllvrttrr
       61 lsvtdagrtf ydacrdivra tetaldavss dagplrgtlr vsvpidygal vvapavvalr
      121 dlhpgldvel vandrvvdlv adnldvairi grladsnyra vqlgtyekwl vaspafiarh
      181 glprdtdala alpfvmlstl prphtleldh vrggsaavrc vapvvsntat acraivlagg
      241 gfglltdfst addvaagrlv rllpgwhtap agihavypst rlpspkvraf idamktrige
      301 tpppaparpv rstradg
//
LOCUS       WP_176045984             148 aa            linear   BCT 11-JAN-2025
DEFINITION  GatB/YqeY domain-containing protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176045984
VERSION     WP_176045984.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Deniziak,M., Sauter,C., Becker,H.D., Paulus,C.A., Giege,R. and
            Kern,D.
  TITLE     Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins
            from an ancient and the modern pathways of aminoacyl-tRNA formation
  JOURNAL   Nucleic Acids Res 35 (5), 1421-1431 (2007)
   PUBMED   17284460
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..148
                     /product="GatB/YqeY domain-containing protein"
                     /calculated_mol_wt=15643
     Region          1..146
                     /region_name="YqeY"
                     /note="Uncharacterized conserved protein YqeY, may have
                     tRNA amino acid amidase activity [General function
                     prediction only]; COG1610"
                     /db_xref="CDD:441218"
ORIGIN      
        1 mslkeqised mkaamrakes erlatirllm aaikqrevdd rvtlddadit avidkmikqr
       61 kdsisqfqaa grddlvakeq aelvvlggym paqlsdaeva aevqaavaqt gaagpqdmgk
      121 vmgvlkgkla gradmtavsa qvkaaltk
//
LOCUS       WP_176046199             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176046199
VERSION     WP_176046199.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32664
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdrlqamqiy vqivergnft qaadalqlhr pavtkavqql eqelgvrlln rstrrvsvta
       61 egeafharcv qllgsiddaf asfpkqravp kgrlridial alaktvvipa lpefqqrypq
      121 ielvlgasdq padligegid cvvrvgtlkd ssmvartvga vpmvtcaspa yltrhglprt
      181 ldelrthrav nfftggnrri lewtfrphge tvavklassl ltdnsealls cglaglgivh
      241 alrpalqpsi daglliellp gvpavpkpvs vlypnrahls dkvrvlidwl telfarrypa
//
LOCUS       WP_176046213             315 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176046213
VERSION     WP_176046213.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..315
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34165
     Region          2..315
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhrigffvcr gydaldlggp lsafnqvata aghtpydlhv isqaggpiqg ntglsietrp
       61 vgrrtfdtvv fvggdiepmq tpenvaaakr ltartsrvas vctgafllae tgsldglraa
      121 thwryaalmq srfprikvdg dsiyvvdgrv wtsagiasgi dlalgiietd mgaeiaravs
      181 rllvvpyrrp ggqsqfsams qmepesdrir ialnfarehl aealpverla daarlslrqf
      241 grafrretge tpakaverlr veaarlrlqg gsepieqial avgftdperm rrafiklhgh
      301 ppqairresr snaar
//
LOCUS       WP_176046221             360 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176046221
VERSION     WP_176046221.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..360
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39397
     Region          1..358
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msfltltdlt ktfgeltava dvnlsveqge fvsllgpsgc gktttlqmia gfvdvtrgri
       61 aldgqditdl kpnrrglgiv fqsyalfphm svaenvgfgl dmrgvdkaer aeriraalal
      121 vrldalahrf prelsggqrq rvaiaravvi eppvllldep msnldaklre dmqfelraiq
      181 rkigtttimv thdqsealsi sdrvvvmeag ritqtdtpyr ayerpenrfv sqfigkanll
      241 pgtivahdgd airidlghdl aetgrtaylp prerdvrvgd avsvcirpek lrlcapdagr
      301 faatvtsrff lgsqwlyrvd salgevlvcc qnegaeplae gapvgidwhs davrvmrrea
//
LOCUS       WP_176046223             264 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC1644].
ACCESSION   WP_176046223
VERSION     WP_176046223.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 264)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..264
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28392
     Region          1..253
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mrkngpfala fhtlvilfvl aplvivvlva ftpdetltlp thglslrwfr aildypdfvs
       61 affnsvklaf asatlslaia lpaglaigra tfpgraflng lllsplvipg lvlgiallrf
      121 faligatgsf awlvlahmiv itpfvmrlvl asvagldrsi eqaacslgad pwttfrritl
      181 pmivpgitgg wllafinsfd eltmsifvts pqtvtlpvrm ymyatesidp mmasvsalvi
      241 fitagamlll drvyglnril igqh
//
LOCUS       WP_176046239             322 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176046239
VERSION     WP_176046239.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 322)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 322)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12168323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..322
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34521
     Region          22..198
                     /region_name="AraC_binding_2"
                     /note="AraC-binding-like domain; pfam14525"
                     /db_xref="CDD:434015"
     Region          248..320
                     /region_name="HTH_18"
                     /note="Helix-turn-helix domain; pfam12833"
                     /db_xref="CDD:432818"
ORIGIN      
        1 mdialsrhap nrlgtlqapd everavahrl gphrmaaygr dpfhaelyev plhhgallel
       61 cygretridf gddadhflfr ltlagtcelq agsivaragp geltvsspal asrlstspdc
      121 rnlvlrlerg alerklqdml qatltrplqf elasggagaa lvlptfeylc rlgvqpgiga
      181 aspvfgadlt awlmslllth lphsysdala rgtpplpahv rracdhvdah lgeslalaal
      241 aavagvaprt lqhafraflh ttpaayvrer rlaavhaalq rgdtcsvtdv liahgihgfg
      301 hfakayarry ghapsvtarq pr
//
LOCUS       WP_176046251             517 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Burkholderia sp. BCC1644].
ACCESSION   WP_176046251
VERSION     WP_176046251.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 517)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 517)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 517)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..517
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=56429
     Region          <55..>204
                     /region_name="PRK13560"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:106506"
     Region          155..513
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mrparagaml gfrprdaarl hpdpimsfpd eddfhrllda lttcvllhda qtkaivwanr
       61 aacialgfsv eellplkapd mtrpepkyqr eiavsawdra lvdgpqvyew cyrsrtgvdm
      121 lseatatyvp lrgrdvvmvq frdisaeeav rqqlrryear lrefmqdlde giavvtphgg
      181 vqfisesgrr vlglaadepl gevldycses drdrlvaqlr dapsaypsap qryrivrrdg
      241 sscwlrilcr qveiegdldg llvqfrdvsd evaiedarra earllehagr ynamgemasv
      301 iahelsqpla avrnfiegav qrlngrgavd daiwglrsad rqaehaalii ksvrefivkr
      361 epvvavadlr diladvayfi elrakeagvt vaivqagtpl pircervlig qvilnlafna
      421 ieafascert prtltlgtae laglaelrai dngpgiadga hdrlfdgfss skaggngigl
      481 slcksivtrh ggriaaspad gggldcrvtl plagtha
//
LOCUS       WP_176046261             151 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176046261
VERSION     WP_176046261.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..151
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16278
     Region          6..137
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mpdealdrld lailealqen artplsevgr riglsqpats ervkrleerg iiagygarid
       61 paalglgmta iirlkttheh ikpalrafae mphvievhrm tgddcfllkv lvptpgqlet
      121 lidaiarfgs vttslvlrse pvktigkall g
//
LOCUS       WP_176046285             206 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176046285
VERSION     WP_176046285.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23459
     Region          9..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mqiarqaqqe rseqtrseil gialeqfstr gfdavslrdi adaagvnham iryyfgnken
       61 lwrasvtqlf drfmegvalp dpasdtfsid avkqyirnyv rycaahpeha rlmmqeanrd
      121 serlqwmaet fvrprhdrsv plvryvsett dglaridpvv llymitaiaq vpylltaemr
      181 yahgidalde kaidahcdav vafifr
//
LOCUS       WP_176046301             304 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia sp. BCC1644].
ACCESSION   WP_176046301
VERSION     WP_176046301.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..304
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31776
     Region          5..298
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mdthhevivv ggsfaglsaa mqlararrrv lvidagrprn rfaehahgff gqdgkppaqi
       61 vaeasaqlaa yptvrriege vrtagrdadg rfhvtladgs rasadrlila tgirdelpal
      121 pglaerwgis vlhcpychgy evsgqrlgvl athplsvhqa ilipdwgptt wftqgvvdan
      181 eeeaallaar gvrierspvv gilgaaprid alrladgqvv pidalfigar tgmasdlaqq
      241 lgcafddgpl ghairvdtwk qtsvagvyaa gdasslmtna tfasasgvaa gvgahrslif
      301 glha
//
LOCUS       WP_176046318             349 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176046318
VERSION     WP_176046318.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 349)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..349
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37434
     Region          29..225
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          257..340
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtynphllie rpnldmsepl lppipdvhdl vselllgmrl sgvqyrriqv arpfglnfgh
       61 vtgraqfhfv vrgpvllrda sgdtmrleag daillphgrv halvsdadap crelngfeva
      121 kicdtvasva sagaspasca ttepgagdal ifsacmeldl ggmqplvgtm pefmhvgtll
      181 arypeirpml damereacta ragfagilar ladvvaafiv rgwvecgcgd atgwvqalre
      241 pklgraival hrdpgrnwsv aelateagvs rsvfaerfla atgmtpvryl tdlrmrlaaq
      301 wiardhesie avayrlgygs laafsrafkr vvgkppgavr adgevraea
//
LOCUS       WP_176046325             382 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176046325
VERSION     WP_176046325.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..382
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=41169
     Region          19..363
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mnddykvelp eaaviargrr lrvgviglgi gskhiegwre hpdvdvvaia dpdakrlakv
       61 gdafgidary asadamlaae rldvvsvctp nkfhreltla afdagchvlc ekpmalnade
      121 gremliaaqr agkrlminfs yrfsaqsral kaqvesglfg dfyfgrtvwh rrrgmpgfgg
      181 wfgtkalagg gplidlgvhr ldlalwlmgy pkpvwvmgst ydpiarelaa ragktfdved
      241 laaamirfdn gatlaleasw atniqeaelm etrllgtrag llqknlnegy tfdahvfieq
      301 ngaqfdmrln ppaegahsam ydyaeailcd vphpapgeeg livmeildai yasaaagepi
      361 rihapgpaav daapvvdldv ag
//
LOCUS       WP_176046340             418 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC1644].
ACCESSION   WP_176046340
VERSION     WP_176046340.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 418)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 418)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..418
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45069
     Region          <195..412
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mtiapsspst aalkrelkaa earkrtmall lvaplaifll lifvvpigtl ltravqnpei
       61 atalpntvaa lsgwdrkapp adaayvalaa dmtkvadsea mgalarrlnt eipgyrslva
      121 ktaramplkg dndaaltpaq trekiidlds rwgdaaywqa iakngsqvsp fyllaaldhk
      181 qdgfghivqa dpdqsiylai fgrtfvigia vtlfalllgy playwistls erranlvmil
      241 vlipfwtsvl vrvaawivll qseglinkal igsglishpl tllfnrvgvy ismthillpf
      301 milplysvmk sipptyqraa vslgshpfsa fwrvyvpqty pgvgagallv filaigyyit
      361 pallggpndq mvsyyvayft nvtinwgmac algglllaat lvlyavygrf trtnvslg
//
LOCUS       WP_176046380             207 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176046380
VERSION     WP_176046380.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22734
     Region          1..149
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mlrlaarsfa tqgyaattmr aiadqagiea asiyyhfssk eelvdvvmeh gadsivqhik
       61 ehfdalppda tadarfkaal vgqmsalikf gdyalahgrl ltqlpdkvre rqvkrrerhq
      121 qlwtavfddl rtegflredv dialcrvfvl gcinsvqtwf dpkkgsldkv adqlatmffe
      181 gvkpaagakp aakarrgsrk aelaass
//
LOCUS       WP_176046384             262 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176046384
VERSION     WP_176046384.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..262
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28093
     Region          13..252
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mnrtdkqqgv tltverglev lhafraarap lsnaelvrrt glpkatvsrl tttlisigyl
       61 rrvgggrqfe lsagalsigh ayleanpvtr lvtpvmqkla dklnlsvala vphrldmvyi
      121 awrasariat lrlgvgsllp mattsvgray lyglpdalra pliaelldaa gddadtvren
      181 ldaafedlkq sgvcmsvgey qrnaygvalp ivvgrnrtlm alncgavele pdmtairqrv
      241 tpelkaaaet lsfilsdvdc ep
//
LOCUS       WP_176046401             371 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176046401
VERSION     WP_176046401.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..371
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38623
     Region          26..345
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mgtpdtgrlt vpaldaslvd wldsnatqld tsadskaevv prlaaaglfr igvpaslgga
       61 ggtttdaias iaavaehsla aafvlwgqrs fieyllqspn talrerllpa lldgtcagas
      121 glsnamkylc gieslqieaa rrteaaedcr ltgrmawvtn lraeqfvvaa avsfrdgrps
      181 aivaiphdap gltrsadldl ialrgsntaa lqledvptds awlihadaqa flpavrpafl
      241 glqcglsigl arralaearh aaettrgilg pevdtcaael saacallssg iadgslrmhp
      301 nrlfelritl atlvasavnl eleasggrgy lrdaglgfdr rwreaafipi vtpsvvqlka
      361 qlaaqtrsia a
//
LOCUS       WP_176046423             730 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia sp. BCC1644].
ACCESSION   WP_176046423
VERSION     WP_176046423.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 730)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..730
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78064
     Region          47..730
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mvtgtkaarh araiaaggal cvaaagsapa qasdaggapq agaaaavlpa idvngaadga
       61 svglvgrrtt agtktdtava eipqtinivt aqqiemtgaa dlnqalryvp gfstfgadsr
      121 tdwyaalrgf tptlyvdgia apntavianw rvdpytidsi ailrgptsvl ygagepgaiv
      181 dahtkladge rvreagvqig ndarkqvmld vgdkldpdgk iayrfvgvar dgnaqtgpng
      241 drrvalapsf rwrpnadtsl tvsatflqds gdissnflpa sgtvlpnpng rlsqdiymgd
      301 psfndyrkkq wslgyalehr vnaiwtlhqd vrwshlsldd atvfgngfap rsttdmmrfa
      361 glfqlnysrl didnhaqarf gtgplehtll fglqfdrqtt tnsvwlalap slnlyhpvyr
      421 pvtaaifsgp tslghvdqyt alnafgvyaq dqirwqrwtl tlggredvvn arfddrtagt
      481 qarqdvsafs grvgltyqgd aglspyvsys tsfdpvigvr mfggglpkpt rgaqteaglr
      541 wqppgrnlml saavyridqt nvvtptpvnl dptgttsvqt gkvrsrgiel savgkvtrel
      601 sivasyayqd vknvqandas lnnwpvsvpl prqmasmwad wtwrtgalsg lgigggvryq
      661 sasagapdns ltvpsatlyd lalhydmphw rfalnvanlf drryvsgcqs yavcvfgner
      721 tvlasakynw
//
LOCUS       WP_176046453             477 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1644].
ACCESSION   WP_176046453
VERSION     WP_176046453.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..477
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47857
     Region          34..434
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(40..41,44..45,48,80,130..131,133..135,138,160,
                     163..164,167,291,294..295,298..300,303,331,334,387..388,
                     392,396,412,415..416,419..420,423)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msdrapalds alaaaapapr tslraifptv aaaslgfaiv qldvtvvnva ipslghsfgs
       61 svhglqwivd aytlsfaall ltsgtladrf gsrrlfaygl alfllaslgc alapslvali
      121 aarvaqgvga amilptslal ithacandsa arvkavawws atggaisaag ptlggllids
      181 lgwraiffin lpicaiglwl tlrhvqdsaa artrlfdpag qivavlalgl ltggiiraga
      241 qgvgdpyaag aliasavlga lfvaierrva apmlqlaffr iarvpgvlai gavtnaafyg
      301 lifslslyfq nargftates glalapltii mlaniasarl avrygfratv iiglavslag
      361 yawlwhtlaa htpyvllapg laamaigggi aipaltstml gsveagrsgt asailntarq
      421 vgaaigvaal galvagqgaa ivagaahafa vaavlvavci vvavrwpgda pdtgvrp
//
LOCUS       WP_176046522             283 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176046522
VERSION     WP_176046522.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..283
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30116
     Region          36..245
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mlnalepvsq atvagrhvvf rthghahgpv vrmaspsdvg emikpfvfld lidtqapigq
       61 pafgwhphsg iatltlaidg hgtyaestgh egtmapgdie wmsagrgvwh tgsvvppvka
      121 fqlwvalppg relapafsqh lsiddiptdg parvllgrhg davspidapa ginylvvqlk
      181 agerwtcrpp qghrvgwtav mdgslrtpda vrqgelvvfd asdaaiefea vadtrfvvgt
      241 aiphphelhl gyysvhtsaa alaegereiv righelratg vmr
//
LOCUS       WP_176046541             450 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TRAP transporter large permease [Burkholderia].
ACCESSION   WP_176046541
VERSION     WP_176046541.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..450
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47454
     Region          1..446
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 melailsvsf liflvlgvpv sfalgiacvl tymveglpia tamqamisgm nafsflavpf
       61 fifsgelmlh ggiadrilrf aqatvghfrg glgmanvvac tlfggvsgsp tadtsamggv
      121 viplmkregy saayavnvtt haslagalmp tstnmiiyaf aaqgitgmlh gqpvsgvsig
      181 dllfsgllpv lwvmgfvlaa aywqavrhgy prredgssal pkfpgwyavl rsfvgavpgl
      241 mviaiilvcv akgiatatea aaiavvyslv ltavvyrtlt aeklrralsh aarttgvvll
      301 liavsnmlrf qmsyleipda iegllkqsta apwlmllyin iiqvflgtfv dmaahilitt
      361 plflpiamac gvgpvqfgim lllncslglv hppigsvqfv gcaignvsig ettkmawpyy
      421 laifsainiv tylpffstwl pslisghavf
//
LOCUS       WP_176046552             125 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176046552
VERSION     WP_176046552.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..125
                     /product="RidA family protein"
                     /calculated_mol_wt=13436
     Region          1..125
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 maieyiaern pltrnlprsl atkagdlvfv sgqvarnedg slvtggidaq trrtlqnvah
       61 vlalagctld dvvkttvwle dagdfaefnr vyaeffpgnk psrstlqatn mvgtkieiea
      121 iacrp
//
LOCUS       WP_176046553             267 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176046553
VERSION     WP_176046553.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..267
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29731
     Region          11..221
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mstdsvhpav litmphshys ekarwaldrl elayqeqpha pllhrlatip nggssvplll
       61 hrgarftdst dilvhidllh ggdclyprdv dlrpeveale tqfdevlgph arrwayaqll
      121 perslllhvm srgvprfeav llpiilpgve rliraalrit pasatrsier vrgvfteidg
      181 rladgrrflv gerftaadlt faalaapvlf ppgyraaypa ldhvpaamrd evlrlrdtaa
      241 gqfalrlyae erdrthtapq ewncsae
//
LOCUS       WP_176046560             205 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC1644].
ACCESSION   WP_176046560
VERSION     WP_176046560.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..205
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21830
     Region          1..202
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mtelivvvti tllavispgp dfamvtrnsl llsrragvlt aqgiglgvtv hvsytllgvg
       61 llirqslwlf ntvkligaiy liylgvkmlm akahdgqpdt paaplsdlaa lrtgfltnal
      121 npkttvfivs lfmqavrldt plivqigygs fiavahagwf slvavcfsat vvrdrllslr
      181 hwidrtfgcl lvgfgvalai arggr
//
LOCUS       WP_176046576             136 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176046576
VERSION     WP_176046576.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163498
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..136
                     /product="VOC family protein"
                     /calculated_mol_wt=14966
     Region          10..119
                     /region_name="VOC_like"
                     /note="uncharacterized subfamily of vicinal oxygen chelate
                     (VOC) family; cd07246"
                     /db_xref="CDD:319910"
     Site            order(10..15,17,32,48..49,51..53,64..66,68..73,79,100,105,
                     113..116)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:319910"
ORIGIN      
        1 matfqpagwh tvtprivvpd penlvefirt vfdargefra glpaeirigd svvmisggdg
       61 lrdpmpafly vyvedtdaih rraiaahais leapadmpyg drramvrdpw gniwqiathq
      121 rdlsadeirs rlagge
//
LOCUS       WP_176046588             339 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Burkholderia sp. BCC1644].
ACCESSION   WP_176046588
VERSION     WP_176046588.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..339
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36873
     Region          11..323
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(16..18,48,53,79,142..143,183..184,207,236..242,278,
                     295..298,303,306..307)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(48,53,79,142)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 mslkdtllag nrlgfgaapl gnmfrdipde earatveaaw argiryfdta psygaglaes
       61 rlgdalagrc rddyfistkv grivldemed aktrdygeks gifahgranr lvsdytadat
      121 lrsiegslkr lrtdrldivw vhdiaqdiyg dewlaqfeva rkgafrvlgk lreegvigaw
      181 glgvnrvepi elvldlaepq pdgmllagry tlldheralq rvmpaaaarh vgivvggpys
      241 sgvlvggahy eyqkappeiv ekverikaia arhdvpvkaa alqfvlahpa tvsvipgasr
      301 aeriaedaaa lafdipadfw remreqqlva pdaplplar
//
LOCUS       WP_176046581             229 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176046581
VERSION     WP_176046581.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..229
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23900
     Region          43..172
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkkrlepaph dvsapvepag tagarapega sapagavagv rrkkapdqvr aqllaaasei
       61 athhgvaalt ldavaeragv tkgalqyhfa nkqglldalf gqatarfgaq mdarmaadps
      121 gdgaaarayl havldsanpa astdvlrvlv asmiteqdtr erwsvpmrew trpdpvpleq
      181 aatlmicrla adglwisell dsvevsvelr aeivrqldam skgvfpkgg
//
LOCUS       WP_176046591             339 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Burkholderia sp. BCC1644].
ACCESSION   WP_176046591
VERSION     WP_176046591.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Penning,T.M.
  TITLE     The aldo-keto reductases (AKRs): Overview
  JOURNAL   Chem Biol Interact 234, 236-246 (2015)
   PUBMED   25304492
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Mindnich,R.D. and Penning,T.M.
  TITLE     Aldo-keto reductase (AKR) superfamily: genomics and annotation
  JOURNAL   Hum Genomics 3 (4), 362-370 (2009)
   PUBMED   19706366
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Jin,Y. and Penning,T.M.
  TITLE     Aldo-keto reductases and bioactivation/detoxication
  JOURNAL   Annu Rev Pharmacol Toxicol 47, 263-292 (2007)
   PUBMED   16970545
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Sanli,G., Dudley,J.I. and Blaber,M.
  TITLE     Structural biology of the aldo-keto reductase family of enzymes:
            catalysis and cofactor binding
  JOURNAL   Cell Biochem Biophys 38 (1), 79-101 (2003)
   PUBMED   12663943
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14442752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..339
                     /product="aldo/keto reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36980
     Region          13..323
                     /region_name="AKR_AKR15A"
                     /note="AKR15A family of aldo-keto reductase; cd19152"
                     /db_xref="CDD:381378"
     Site            order(16..18,48,53,79,142..143,183..184,207,236..242,278,
                     295..298,303,306..307)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381378"
     Site            order(48,53,79,142)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381378"
ORIGIN      
        1 mslkdklpgn kilgfgtapl gnmfrnipda eaaatveaaw qhgiryfdsa pfygaglaei
       61 rlgdalanhp rdeyvlstkv grvildeved vsardlgekg glfehgrpnr ivndytadat
      121 lrsiedslkr lrtdrldivw vhdiaqdfyg dewlaqfeva rkgafrvlsk lreegvikaw
      181 glgvnrvepv elvldlaepq pdgmllagry tlldheralq rvmpaaaaqn vgivvggpys
      241 sgvlaggthf eyqkaspeil akverikaia trydvpikaa alqfsmshpa tvavipgasr
      301 periaedqaa lnvvipadfw rdmreqglia anaplptdr
//
LOCUS       WP_176046618             238 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC1644].
ACCESSION   WP_176046618
VERSION     WP_176046618.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 238)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 238)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 238)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..238
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24730
     Region          29..235
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mtrrtvqlvg slvaiiavgw alargigadt fhqraddlay yagqhmllvv ysmtlaiavg
       61 vpagvllsrp rfqhqaerfm qvfnigntip slavlaialg ifgigdvpai valflasllp
      121 itrnayegmk nvpaalreaa kgigmtgwqs lvrvelpdal piivggvrta lainvgtapl
      181 ayligadslg slifpgiyld nqpllllgas ltailalvld givaagsrhw larhggaa
//
LOCUS       WP_176046624             255 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF169 domain-containing protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176046624
VERSION     WP_176046624.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..255
                     /product="DUF169 domain-containing protein"
                     /calculated_mol_wt=27756
     Region          4..228
                     /region_name="COG2043"
                     /note="Uncharacterized conserved protein, DUF169 family
                     [Function unknown]"
                     /db_xref="CDD:441646"
ORIGIN      
        1 mkdtlaglsa nlerllklrs ipfgmklfer redmeavpri rrpkaihsld qivgqtarlg
       61 ftvgitaddl vgaqcrsvvg lghakdaewa sgqqmagvwy atqedsrahq aamhcvadgk
      121 ydalvvspla agriepdial fyatpgammy finglqwsgy krfdwsvvge sacadswgra
      181 lstgqpslsi pcyaerrygg vlddemlmal apdalelait gmealsrngl rypfaqygiq
      241 qdvragmevs ypktt
//
LOCUS       WP_176046649             137 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176046649
VERSION     WP_176046649.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..137
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14675
     Region          6..137
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mryvsleskk delllaarvl mmilfvlfgw qklngfsgtv aymastgnpa pelaatiava
       61 velaggalia igfytrplal vvaaytlata lighrywalq gmeqymatin fyknvsiigg
      121 llllaltgpg rysvdrk
//
LOCUS       WP_176046671             143 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176046671
VERSION     WP_176046671.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..143
                     /product="RidA family protein"
                     /calculated_mol_wt=15597
     Region          10..141
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mnqdqsiqgr vvpgkatprg rfphitragd flfvsgtssr rpdntiagas advlgtvqld
       61 ireqtrtvie nirdilrseg adlsslveis sflvnmndfg gynavygeyf detgptrttv
      121 avhqlphphl liemkaiaya pkr
//
LOCUS       WP_176046682             306 aa            linear   BCT 11-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176046682
VERSION     WP_176046682.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..306
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33290
     Region          87..304
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 miwfgiatye lngrvaagla megalydaqa vlqraggeda pldvdtlvad wplrgaqtva
       61 rleaaareia agrldvqpla gyrlhvpyap rrifaaasny yeharemgte lapreesspy
      121 mfmkaetsvv ptladvvmpp qaervdweve lavvigrpgr hiavedafdy vagytilndv
      181 sardlnrrtd ypfkhdwfrg ksfdtfgplg pwlvpracia epqnlrmrla vngetmqdgn
      241 tgemifsiae qihylssilt lqpgdliatg tptgvgmgrg iylqpgdvmv asidgigsie
      301 nplvrg
//
LOCUS       WP_176046687             340 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia sp. BCC1644].
ACCESSION   WP_176046687
VERSION     WP_176046687.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..340
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=34845
     Region          9..340
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkvrslciaa lscaaaglla grsshaqssa tlygligldv asskrsggpp aaiamqspgl
       61 tapywglrvv edlgggyral avlesffqpv nggigrtsad pywgrnayag iegpfgtvtl
      121 grqtnllyla eqavnpfras ilfsplvmqt fvasyggtia gdtvwnnaiq ytsptvgglt
      181 tsavyapggl agasgaanag lslryasgpl tavaaaqrtr iaagaaaptq saylagfaya
      241 fsrvtlygai qgtrtsatdt gshtfeagms vpvtsrlaal aewaytrrta lrtavsrntg
      301 aagldytlsr rtdvyalamy drlggsgiat twalgirhlf
//
LOCUS       WP_176046690             108 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia sp. BCC1644].
ACCESSION   WP_176046690
VERSION     WP_176046690.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..108
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11278
     Region          29..103
                     /region_name="CytC552"
                     /note="Cytochrome c551/c552 [Energy production and
                     conversion]; COG4654"
                     /db_xref="CDD:443692"
ORIGIN      
        1 mmfkpfaapl lcalalataa tpghaatsas eqtcrachtl dttkigppfr aiaahyrdds
       61 dalaklqksm legstgkwgs atmppnaisa ddaarfakwi mslnrdgk
//
LOCUS       WP_176046701             126 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176046701
VERSION     WP_176046701.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..126
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13868
     Region          12..115
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 mtnitnlvdl mrapakltqs rvpsgllldg npmqtlshhy ispcgqfscg iwectpgrwt
       61 ieydeseyce mlsgvasvrd adgrervlra gdrfvippgf rgtwevvetc rkiyashapq
      121 aarpgv
//
LOCUS       WP_176046720             215 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC1644].
ACCESSION   WP_176046720
VERSION     WP_176046720.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..215
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22361
     Region          6..208
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mqpsgslygf laiggmlavt pgpnmvyvms rsiaqgrtag lislagvmig ylfymfgaaf
       61 gittlfmsvp yagtvlgavg avyllylawq avrpggrspf evqalpdeqp mrllamgatt
      121 svlnpklaml fvsllpqfid yrqgsvfgqs lflgslliaa fasanglvai csssiakflh
      181 grptlllaqr wamgvilggl gvqmvveask lagva
//
LOCUS       WP_176046721             482 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia sp. BCC1644].
ACCESSION   WP_176046721
VERSION     WP_176046721.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..482
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50492
     Region          25..478
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mshpatsaqa rpvqdtapqa gglrrnylsl peliaqsigl vgvsggigvl ipavfatagn
       61 gtwlaylfai vallfsswsi svfardsasp galyayvsag igpiwgaicg wslliayava
      121 aagilqgtin tflvlgretg llggatpvgt vlgltvataf aawyiafrdi rlstrftlfv
      181 elatllliav vviatiafgg hpvdraqltl egvkptqlql gmvlaffsft gfesatvlga
      241 eardpfraip ravlisvvgp allfvigayg mvsafhgqtp pldrvdgpla vlahrlgagw
      301 vgvlidagva lsffaaffss inaaarivyt fgrqgvlhas tgraharnat phvavaviaa
      361 salvtalvft argtalldsy gylssiatyg wllayvlvai gaplylrrqr rlrarhvais
      421 ivavvllaip lagsvypapd gvyawlpyvf vallaiglgw flvlrirfpe rlreleaell
      481 tk
//
LOCUS       WP_176046751             338 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176046751
VERSION     WP_176046751.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..338
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37706
     Region          59..210
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <223..319
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhlapvrytp gqrdddvaia asnqadqqst nrsrvcdlrq alatrvarwt egadhvttai
       61 pnlsfhrrea ptqpmecmve psfglvvqgt krviqsgday iydanrflit sldlpgstqv
      121 ieasheepfl giglkldfhv laelmmqvap dhddapvgrg lvvgdmtepl fdalnrllal
      181 lddpnaipvl apyvereiyy rlltsdqgar lrqiasagsq gnrvsrairw lrahydeslr
      241 vddlaaqvqm ssstfhhhfr qltgmsplqy qkwirlnear rlmlserlda asasfrvgya
      301 sptqfnreys rlfgnsprrd idslrsgtdv vlsiaasy
//
LOCUS       WP_176046806             419 aa            linear   BCT 11-JAN-2025
DEFINITION  M48 family metallopeptidase [Burkholderia sp. BCC1644].
ACCESSION   WP_176046806
VERSION     WP_176046806.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Bode,W., Grams,F., Reinemer,P., Gomis-Ruth,F.X., Baumann,U.,
            McKay,D.B. and Stocker,W.
  TITLE     The metzincin-superfamily of zinc-peptidases
  JOURNAL   Adv Exp Med Biol 389, 1-11 (1996)
   PUBMED   8860988
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Stocker,W. and Bode,W.
  TITLE     Structural features of a superfamily of zinc-endopeptidases: the
            metzincins
  JOURNAL   Curr Opin Struct Biol 5 (3), 383-390 (1995)
   PUBMED   7583637
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..419
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46691
     Region          8..415
                     /region_name="M48A_Zmpste24p_like"
                     /note="Peptidase M48 subfamily A, a type 1 CaaX
                     endopeptidase; cd07343"
                     /db_xref="CDD:320702"
     Site            order(279..280,283,361,365,405)
                     /site_type="active"
                     /db_xref="CDD:320702"
     Site            order(279,283,361,405)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320702"
ORIGIN      
        1 mspfsftllf aiavlamvvt klwlasrqir fvaahrngvp aqfsatiplt ahqraadytv
       61 ertrltmlei vvsaavlvgl tllggvgald tlltgwlgrg ygqqvalvaa vlvitsvidv
      121 pfeyyrqfgi eqrfgfnrmt krlfftdmlk nsllgaalgl pllfvvlwlm nqagslwwlw
      181 twivwvafqm lvlliyptfi apifnkfepl kddvlrsrie slmkrcgfaa kglfvmdgsr
      241 rsahgnayft gfgaskrivf fdtllarlsg qeieavlahe lghfkrrhvm krmlvsfvls
      301 llllallgwl aqrtwfytgl gvipsldtsn agaalvlffl aipvflffat pfssltsrkh
      361 efeadafaas qtdaqdlvsa lvklyednas tltpdpvyta fyyshppasq ridrllqha
//
LOCUS       WP_176046861             211 aa            linear   BCT 11-JAN-2025
DEFINITION  SCO family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176046861
VERSION     WP_176046861.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..211
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22738
     Region          53..206
                     /region_name="Sco1"
                     /note="Cytochrome oxidase Cu insertion factor,
                     SCO1/SenC/PrrC family [Posttranslational modification,
                     protein turnover, chaperones]; COG1999"
                     /db_xref="CDD:441602"
ORIGIN      
        1 msparpaphr risrfirtaa alaaavalaa cthdeprwnl tnvtghlpdl sftltggdgr
       61 pvdadafhgr ialvyfgyth cpdvcpetma rlmevlgklg pqandvrilf vsvdpardtp
      121 qlmqsyvaaf daahargltg tdgqieslak ryrvayqmek rdpsggyevt hssavyifda
      181 tgrarllatd rdspdaiaad vrriidtast t
//
LOCUS       WP_176046879             347 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176046879
VERSION     WP_176046879.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..347
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38324
     Region          15..323
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mvpvsrpaga trttqvaiva lppvsmsgvg pivdalnlan eidgrllyrw qvcswdgrpv
       61 plaggaqwha daafndaiac dwlivvterf qqfadyrlfl aslarvgqrt pvvtgihhgv
      121 wwlamagqls gyrvsvnwet yqqfaeqfer sivtqqifei drdratcagg qatvdfmlam
      181 igrehgadla eriadalgvg tlrsgeerqr ipfvtapger hprlndalql meanvedplt
      241 tdeiaelvgv srrqlerlfr qylgampsky ylnlrllkar tqlqrtsksv vqvslacgfs
      301 saahfsnayr erfgvtpred rrawlekqtg ggseprggal verggkd
//
LOCUS       WP_176046894             320 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176046894
VERSION     WP_176046894.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..320
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34810
     Region          4..192
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          224..306
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mttdllsdvl tdlradavvt grftlsapwa irkpavagap frtcagspff lsvagaapvh
       61 vepgdfvllp hgdehvmass ldeppvpfdt lmadkgirpr fdtplefvag gggatselyt
      121 givvyrdivr splftvlppl ihvrandaav apwlastlqs fieesmacqp gwavaatrla
      181 dvlfvqllra hlqssanhtg wlrgltdpqi gramalmhrd prrnwqlasl aadagmsrsr
      241 fcarfaelvg etpivhltay rmylasgela hgklrlieia ervgytseka farafhrwsg
      301 maprryarna qdlydlarhg
//
LOCUS       WP_176046909             455 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia sp. BCC1644].
ACCESSION   WP_176046909
VERSION     WP_176046909.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..455
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48436
     Region          2..449
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mknlqrhlsa rhirflalgs aigtglfygs asaiqlagpa vilayilgga avymvmralg
       61 emavrepvag sfghyatenl gpfagfvtgw tytlemviva iaditafgiy mgfwfpdvpq
      121 wiwvlgvvai icglnlchvk vfgelefwls iikvgaivam igggvaillt gmhfghsadv
      181 ptfanlwnhg gflpngmggl iaslsvvifa yggievigms ageakdperv iprainavpa
      241 rillfyvltm vvlmsispwt gvggdgspfv qifsalgvks aatilnlvvi saaisainsd
      301 ifgagrmmfg marqgqaprv lmttsrhgvp wvtvlvmaga llvgvvlnyl mpkdvflvva
      361 aiatfatvwv wlmillsqva mrrrlssaev aalkfkvplw pvapaltiaf mgfvivmlgw
      421 fedtrvalyv gaawlallaa vfyarirpkf apasr
//
LOCUS       WP_176046906             257 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Burkholderia].
ACCESSION   WP_176046906
VERSION     WP_176046906.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..257
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27963
     Region          1..>240
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mnllelddlc vaydtphgrr tvvdglslal prgdigcllg asgcgkttvl raiagfepvr
       61 mgrimldgap vaapsldvpp errrigmmfq dyalfphlsa adnvafglrr mpkterrmrv
      121 aemldlvgla dsggayphel sggqqqrval aralapspel llldepfsnl dvdtrerlaf
      181 elrdilkrtg htailvthnq aeafaiadri gvmkdgqlaq wdtpyalhhh pasafvadfv
      241 rrdaladera ralargr
//
LOCUS       WP_176046943             382 aa            linear   BCT 11-JAN-2025
DEFINITION  glycerate kinase [Burkholderia sp. BCC1644].
ACCESSION   WP_176046943
VERSION     WP_176046943.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..382
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38358
     Region          2..362
                     /region_name="GlxK"
                     /note="Glycerate kinase [Carbohydrate transport and
                     metabolism]; COG1929"
                     /db_xref="CDD:441532"
ORIGIN      
        1 mkiviapdsf keslsaidva rqieagfrei fadaaylclp iadggegtvd aliaavggdr
       61 rsatvedplg rpvaaaygll sdgtaviema aasglhlvap mernplvtss rgtgeliraa
      121 lddgarrfiv giggsatndg gagmlqalga kltdadgrei grgggalaal ahidtatlda
      181 rlascrfeia cdvdnplvgp ngasavfgpq kgatpatvac lddnlrhfad viardlnrpv
      241 aalpgggaag gmgaamlacl natlrpgvqi vteavglhea irdaqlvvtg egcldgqtvh
      301 gkapigvari aaehgvpvia iggavsgtag aiyqhgvdam fasvrracsl geafeeaasn
      361 vrfaarniaa airlghriaq rs
//
LOCUS       WP_176046972             136 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176046972
VERSION     WP_176046972.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..136
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=14918
     Region          32..134
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mntnptlaer qtntvhpaaa eaarrpaitp svdivennrg vtlradlpgv presldvkvh
       61 dntltieadt hidtpsdlrv rhaevratry artfvlspdl dtsridanlr dgvltltipr
      121 reetrprrid vtagna
//
LOCUS       WP_176047038             234 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176047038
VERSION     WP_176047038.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..234
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24912
     Region          37..232
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mlthrrwtsl dnanhgwlra kyhfavtadg tpehgplgpl ivwnddeiav gsgfpmhghr
       61 dveiityvrq gvlghrdtlg segtidagdv qvmsagtgir haefnrgdmp lklyqiwllp
      121 ranggapgwg tkqfpkgers grfvvlasgh adddddgalp iradarvlga tlkageqvrq
      181 algatrrayl vaasgrievn gervgpldgv aitneaaldi vavedselvm vdag
//
LOCUS       WP_176047053             255 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176047053
VERSION     WP_176047053.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..255
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27785
     Region          1..251
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mldiervsws pggaidvlds vtltvaegef vglvgpngsg ktsllrcifr yarpdagrva
       61 ldaqdvwrmr pravaqrvav lqqetpddfg ltvdelvgmg rtphkrpfda esaddrrive
      121 salhdvglve rraqrfasls ggekqralla ralaqqpell lldeptnhld lrhqlellar
      181 vrrlgiatla tihdlnlaaa ycdrlhvlah grvvasgapg dvlteallrd vfgvtvlvdr
      241 hplsgrprit plhpe
//
LOCUS       WP_176047100             461 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Burkholderia sp. BCC1644].
ACCESSION   WP_176047100
VERSION     WP_176047100.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..461
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=49537
     Region          92..452
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mkprqptaga farswlhltg afalaatlvt lagcdgqpga gtpaapaasa asasgaanlv
       61 asatvaasga vvatnqpqtr aqvyegvrrm talgkqlffd ptlsgsgkla caschspdha
      121 fgppnalavq lggddmkhpg fravpslkyl qgvpqftehf hdsddegdes vdagptgglt
      181 wdgrvdtgae qaripltspf emnsspakva qavkaapyad efravfgvkv ldddaatfka
      241 vlraletfeq tpelfspyts kydaylagra qltpaelrgl qlfndekkgn caschisqra
      301 ldgtppqfsd fgliaiavpr nralpvnrdp rfydlgacgp ertdlkgrde fcglfrtpsl
      361 rnvtlrktff hngvyhtled vmrfyverdi hpekfypvvh gkvqiyddlp krywpninre
      421 apfdrkrgeq palnaaeikd viaflgtltd gyqqtaapag h
//
LOCUS       WP_176047039             138 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176047039
VERSION     WP_176047039.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..138
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14491
     Region          6..129
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mdrykylpll griligapfl msglsklaah attvgyiasv glpapslafi vavlveaggg
       61 lllmsgyrar pvalamalfs lvtavffhhn fadqnqmihf lknvmmaggl lqiayfgaga
      121 fsldarnart alriapav
//
LOCUS       WP_176047106             304 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176047106
VERSION     WP_176047106.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33003
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          90..273
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(105..106,108..109,112,116,118..124,216..221,
                     227..228,230..231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdlaalaifr avvrengvtr aaaklnrvqs nvttrikqle eelgaalfvr dgrrlvltpa
       61 ghtllpyaer llaladeard avredtprgr lrlgtmesta asrlptilah yhhawpdvsl
      121 elqtgttgwl idrvrdfeid aalfarppep gtlpdtfetv pifredlvll tprghppvrt
      181 prdvilptli afergctyrk yverwyaahg vkparvlelg syhaivacva agagvavapr
      241 svldlqpetg niaahtipel egidtllawr qgyasaalaa lrdaltqatq qpasdtkpav
      301 tvta
//
LOCUS       WP_176047128             294 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176047128
VERSION     WP_176047128.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..294
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32053
     Region          10..278
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 msssekppat veqflqhltq eydglsnrlk viarhvethr dqlglegiqs laeacgvqps
       61 avvrfakhfg fsgfsemqrl freglaqqia pgraynlrlr dvieagsssl qpeqiadefi
      121 kgsiagmqql rqtldsqala qavdlladtq aiwiagsrra fpiavyldya lqhtdkrigl
      181 fsalgsmhlg qirsvregdv mivisfmpya eetvqvaqqa vqrgarviai tdsrmsplar
      241 eaevtlmvqd setfgfralt atmglaqslf valayrlels ylptadgahg tkag
//
LOCUS       WP_176047144             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176047144
VERSION     WP_176047144.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34504
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdtlqnmrvf vrvvdagsft aaaqqmnstt ayasravsdl eahlrtrlln rttrrialte
       61 agerylqrce qilayvdqae aeagdaharp sgklkvhcft slgqhylvpa iaryrerypd
      121 vhveltlaqr mpdlldegyd vaivvgrdlp dsglvsqrlg esysvvcasp gyveahgvpq
      181 rpadlaqhvc lgmvapgfhf dewalagpng devvpitapp frvnvaeala vavregmgvg
      241 glplysaigw lrsghivrvm peyrshvmni yalypsrqyl dakirtwvdf lrdelpvtlq
      301 adeaaleqyt rat
//
LOCUS       WP_176047169             749 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Burkholderia sp. BCC1644].
ACCESSION   WP_176047169
VERSION     WP_176047169.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..749
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=81504
     Region          43..744
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mnspleatpd arrdtssagr vrapegtfel srkrvdeldt ifgeggllar aldgyrprts
       61 qiemaravas ameasarrmp epeifetrkr parrlgdgdk saepgadgat aaesdndaad
      121 ntliveagtg tgktyaylvp amlwggkviv stgtkhlqdq lfqrdiptvr nalavpvsva
      181 mlkgrsnylc hyylqrtadn grlpsrqdta ylqeivrfak itksgdkael asvpetapvw
      241 smvtstrdnc lgqecphyke cfvmqarrea qqadvvvvnh hlffadimlr dtgmaellpn
      301 antvifdeah qlpetatlff getlsttqil elardtvaeg lghardavew vklggdlera
      361 ardlrlafan dqivrmslaq lgddhpmfga ldaldvalda lasalasqae raeslgaclr
      421 rarelqdlla gwvapgaaea aakadaaaag dkaasdgdpn ekvrwvevfa htvqlhetpl
      481 svapifakqr agvprawvft satlsvrgdf thyaaqmgls srrsmtlasp fdyqsqglly
      541 vprnlpqpss paftdavfda alpaieasgg gvfmlcttlr avdriasklr dviesrgwnt
      601 pllvqgdasr telldrfray gnailvgsqs fwegvdvrgd alslvvidkl pfappddpvl
      661 aarldaltkk glspfavhql pqavitlkqg agrliraetd rgvlmicdtr lvdkpygrri
      721 wqslppfkrt reiavvqdff dehrsekrm
//
LOCUS       WP_176047236             390 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176047236
VERSION     WP_176047236.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..390
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42414
     Region          83..339
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 misieelqri adaplhswlg tlavsvvvil vvtivhrlga rivkriaqpy plmsailryi
       61 dkpslvvlal laleflwvqa ddgmsfvrgm rtaaavgsiv sltwllvrla agvgdaiiqa
      121 hpidtadnlq arrihtqakv lvrtvmvliv iigtgaalmt fpnvrqvgas llasagvagl
      181 vagiaarpvl gnliaglqia ltqpirlddv vviqgewgri eeitgsfvsv rlwdqrrlvv
      241 plqwiienpf tnwtrsssei igtvylsvdy ltplaplree larlvhaape wdgrvqvlqv
      301 tdatertmql ralvsaadsp scwdlrcrvr egliaylqdr ypqclprnrm elyphesapd
      361 apnperphar apaastaant aadpqaaegr
//
LOCUS       WP_176047292             297 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Burkholderia sp. BCC1644].
ACCESSION   WP_176047292
VERSION     WP_176047292.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..297
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=29949
     Region          1..287
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mevgfcgpgl mgapmirhll aaghrvsvwn rsrdkaealv kdgaqvvgtp relaervdtv
       61 fvcvldgrav gdvvfgehgl lsgaaaarrl lrivdhssip paatrdyaar aaalgvgwvd
      121 apvsggvpga qagtlavmag graadldavr plidtyasri thmgdagagq taklcnqaiv
      181 tatvtaiaea vglaqasgid aarlaealag gwadsvllqt fvprmtsggh ppigalatfq
      241 kdvdaiadaa rdtgavmpvs atvqqvlrlg aaqglagadf aafidivrpg ngrqqas
//
LOCUS       WP_176047308             405 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1644].
ACCESSION   WP_176047308
VERSION     WP_176047308.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..405
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41774
     Region          8..392
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(18..19,22..23,26,61,108..109,111..113,116,139,
                     142..143,146,223,226..227,230..232,235,265,269,318..319,
                     323,327,343,346..347,350..351,354)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mtdsryrwvi vaagglmgcv aigamfslpv flraiardtg wsmtgistam tlgfiamafa
       61 smawgslsdr igtrpvviag avllsaslal asrapsllvf qltfglavgs ataaifapmm
      121 acvtgwfdth rslavslvsa gmgmapmtma plaawlvsvr dwrtsmllia alaavvmipv
      181 sllvrrapal dhapapaaps aagapvamsv aaalrspqfm illltnffcc athsgpifht
      241 vsyavtcgip livavsiysv eglagmggri afgilgdrlg akrmlvagll aqalgalgyy
      301 fvrsldgfya vatlfgfiya gvmplysvla renfplrmmg tviggcamag slgmaagpva
      361 gglivdtfgs ygwlylgsfa igigafliam mfrpfpkphp etvaa
//
LOCUS       WP_176047309             256 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176047309
VERSION     WP_176047309.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..256
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28558
     Region          10..245
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mtpsnvvpls aaplyvqikd tlrarildgt yaphsrmpse helcaifdvs ritvrqalgd
       61 lqkegllfkl hgkgtfvskp kafqnvtslq gfaeamssmg yeivnqlrsf rtvkadrhla
      121 tklnvpegap lveihrvrll nrepvsleqt wvpealgkrl agadlatrdi flvlendcgi
      181 plghadvsid ailaddeivd alrveesspv lrierlthdt sgapidyeyl yfrgdafqyr
      241 lridrqkark sarkqq
//
LOCUS       WP_176047314             162 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia sp. BCC1644].
ACCESSION   WP_176047314
VERSION     WP_176047314.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 162)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 162)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..162
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17048
     Region          22..147
                     /region_name="NUDIX_ADPRase"
                     /note="ADP-ribose pyrophosphatase; cd04673"
                     /db_xref="CDD:467557"
ORIGIN      
        1 msgsshpasv aaapvravpa vigivlherd vllvrranpp dagcwgfpgg kiepgepiad
       61 avvreiaeet tvevaaldaf taldafdyda sgavrqhfim vavlcrwlrg tpvagddald
      121 arwfgideld rddlpmsagv rdvarraier aaslgdarra pv
//
LOCUS       WP_176047335             273 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Burkholderia sp. BCC1644].
ACCESSION   WP_176047335
VERSION     WP_176047335.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..273
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=28147
     Region          2..272
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mlktrvitai vmlavllpvt lfapltafga ligavlvfaa wewarllklg gagpvvyavv
       61 aalalaattp lgidaagsrp lfmaagvfwl lvgpfalrrk pdlaggvwrp fllaaglivf
      121 aacwhalvaa raqgvpfvls lllvvwladi gayfagkafg krklaitisp gkswegaigg
      181 wlavmvvagg amaahafept lfsafaaryg mpgawaaltl lvaysvigdl fesllkrqag
      241 vkdssgllpg hggvldrvda llpvlplaml llg
//
LOCUS       WP_176047367             154 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Burkholderia sp. BCC1644].
ACCESSION   WP_176047367
VERSION     WP_176047367.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..154
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17485
     Region          48..138
                     /region_name="PhnO"
                     /note="N-acetyltransferase, GNAT superfamily (includes
                     histone acetyltransferase HPA2) [Transcription, General
                     function prediction only]; COG0454"
                     /db_xref="CDD:440222"
ORIGIN      
        1 mldptdlrll yqlrpaepgd fpfaealthg nmggyykrhg lvwrsdlfya swresenfil
       61 eadgerigvl rvteegdslh irdvqiaagh rgqgagtyml dmshrwarar glhelqlrvf
      121 vdnpaarlyq rmgyrvagpr laqlgsirhm vrpv
//
LOCUS       WP_176047373             347 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: microcin C ABC transporter permease YejB
            [Burkholderia].
ACCESSION   WP_176047373
VERSION     WP_176047373.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..347
                     /product="microcin C ABC transporter permease YejB"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042884 - microcin transport [Evidence
                     IEA]"
                     /calculated_mol_wt=38513
     Region          1..347
                     /region_name="YejB"
                     /note="ABC-type microcin C transport system, permease
                     component YejB [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4174"
                     /db_xref="CDD:443333"
ORIGIN      
        1 mwsyilkrll lmiptligvl tltfaviqfv pggpveqavq elrkgateqg avpfgmraht
       61 gvdaqqlaql kalygfdkpp lerywlmlkr farfdlgdsy frhqsvwslv vqklpvsisi
      121 glwtffltyl isvplgiaka vrngspfdia tslvvlvgya ipgfvlgvll lvlfgggsfw
      181 qlfplrglts dnfaqlslvg kvldylwhia lpitasvvgs favvtmltkn afldqirrqy
      241 vltarakgls ersvlwkhvf rnamlplivg fpaafigaff tgsllietlf sldglgllsy
      301 esvvrrdypv vlgtlylftl iglatklisd lcyvwvdpri qfdnler
//
LOCUS       WP_176047396             267 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: inositol monophosphatase family protein
            [Burkholderia].
ACCESSION   WP_176047396
VERSION     WP_176047396.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Atack,J.R., Broughton,H.B. and Pollack,S.J.
  TITLE     Structure and mechanism of inositol monophosphatase
  JOURNAL   FEBS Lett 361 (1), 1-7 (1995)
   PUBMED   7890024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10108155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..267
                     /product="inositol monophosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0008934 - inositol monophosphate
                     1-phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006020 - inositol metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29401
     Region          4..245
                     /region_name="IMPase"
                     /note="inositol monophosphatase and related domains. A
                     family of Mg++ dependent phosphatases, inhibited by
                     lithium, many of which may act on inositol monophosphate
                     substrate. They dephosphorylate inositol phosphate to
                     generate inositol, which may be recycled...; cd01639"
                     /db_xref="CDD:238817"
     Site            order(33,38,44,67,83..88,210..211)
                     /site_type="active"
                     /db_xref="CDD:238817"
     Site            order(37,39,89..90,92..97,149..151,153,155..156,164..165,
                     168,171..172,175,179..185,193,197..200)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238817"
ORIGIN      
        1 mhpmlniavk aarragqiin rasldldlie irkkqqndfv tevdkaaeda iietlktayp
       61 dhailaeesg esenesefkw iidpldgttn fihgfpyycv sialehkgvv tqaviydpnk
      121 ndlftatrgr gaylndrrir vgrrdrlada lvgtgfpfre kdgldayarl ftemtqactg
      181 lrrpgaaald lanvaagrld affeqginvw dmaagsllit eagglvgnyt gdadflhrhe
      241 ivaanpkiya qmipilnrys rvhpaae
//
LOCUS       WP_176047450             174 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: gamma carbonic anhydrase family protein
            [Burkholderia].
ACCESSION   WP_176047450
VERSION     WP_176047450.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Smith,K.S., Jakubzick,C., Whittam,T.S. and Ferry,J.G.
  TITLE     Carbonic anhydrase is an ancient enzyme widespread in prokaryotes
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 15184-15189 (1999)
   PUBMED   10611359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429531
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..174
                     /product="gamma carbonic anhydrase family protein"
                     /EC_number="4.2.1.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18067
     Region          1..170
                     /region_name="PaaY"
                     /note="Carbonic anhydrase or acetyltransferase, isoleucine
                     patch superfamily [General function prediction only];
                     COG0663"
                     /db_xref="CDD:440427"
ORIGIN      
        1 mtiyklgeta ptihesvfva dtaaiigkvv leenasvwfg atirgdneti avgagsnvqe
       61 gavlhtdpgf pltiaenvti ghqamlhgct igegsligiq avvlngavig rnclvgagav
      121 vtegktfpdn slilgapakv vrelsaedia rlranaktyv errahfkeql vrig
//
LOCUS       WP_176047466             269 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176047466
VERSION     WP_176047466.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..269
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29492
     Region          8..256
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 msqpipdskt siqviermmr lldalaahsd pvslkelaqr telhpstahr ilndmvtcrl
       61 vdrsdpgtyr lgmrllelgn lvkarlsvrd aalmpmrelh rltgqtvnls vrqgdeivyi
      121 eraysersgm qvvraiggra plhltsvgkl flaadetsrv rayatrtgls ghtqnsitdi
      181 aklereltiv rqqscardne elelgvrcia agiyddsgkl vaglslsapa drlqdawlgq
      241 lsrtaltise slgyrpapsk didglqrqa
//
LOCUS       WP_176047486             472 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1644].
ACCESSION   WP_176047486
VERSION     WP_176047486.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..472
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49688
     Region          18..421
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(30..31,34..35,38,78,136..137,139..141,144,164,
                     167..168,171,253,256..257,260..261,264,292,296,348..349,
                     353,357,373,376..377,380..381,384)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msrpqspsaa qpqlrpgraa faafvgttie wydfyiygta aalvfgkvff astmdpgvat
       61 llafvtfwag faarplggiv fghlgdrvgr ktalvitlvm mglattgigl lpgyaqigvw
      121 apaglvvlrv lqgiavggew ggavliasen apkhrsilya afaqqgsptg nllataaffa
      181 lsalptpsfl mwgwripfll savlviigmv irlkleesad mqrvlarkrt vklplrdvvr
      241 dhwvvvllaa gtlpvinvty frstfalswa tkelgyaqgt flgilsislv vqfllqpvga
      301 wfvskvdmrr amcwilipei vlmpvmfhal atrsywvava gmcistipsa mfygavggvl
      361 arvfpaniry tglslayqls alvvgggtpv laqailnatg sivgvavasg lyalvslvcm
      421 lallnrtgyr adelstaers daaewgtegg saesaadgna qpgeggalkp ag
//
LOCUS       WP_176047489             473 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia sp. BCC1644].
ACCESSION   WP_176047489
VERSION     WP_176047489.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..473
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50730
     Region          8..462
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mqtegqfqhi aareqglrrt lsarqmamia iggaigtglf lgsgfaigfa gpsvlvsyai
       61 gafislllmg claemtvahp tsgsfgayae hyvspwagfl vryaywaciv lavgtevtai
      121 alymkywlpg vpgwlwivgf sallvfvnar svdvfgavey gfsvvkiaai vgfivlgayv
      181 vfgnpglvgd gaaragfhhy tehggffpkg awgtwvaviv sifsylsiem iavaageaed
      241 peravtrafr stivrlvlfy lvtlalmlai vpwtaagrde spfvkvmeai hlpgaaglin
      301 fvvliaalsa mnsqlyittr mmfslsragh apkalgevna rgvpfgalml stlgialatv
      361 lsvlypdasf timmavsmfg alftwmmifv thycfrrrra alglpapafr mrgfplltll
      421 gaglmlavmv ttyftaefhm tlifgipflv alsvvyavwy rraqpvlqpg aks
//
LOCUS       WP_176047572             196 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC1644].
ACCESSION   WP_176047572
VERSION     WP_176047572.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..196
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20140
     Region          4..190
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mndflfglmi alsvgpvalm ianygmragt atgvraaigv aaadgcyavv aftigamlas
       61 tlashlslfr ivgalvllam garmlwqalr drrrtldgdl pppgtrpfis mffvtlanpl
      121 tillfygyat aaagvhrhwl tgaacvfags lagqlvfafg ggaigrfvks pgwlaashvv
      181 aalvvlgygv aglvrv
//
LOCUS       WP_176047532             123 aa            linear   BCT 11-JAN-2025
DEFINITION  type II toxin-antitoxin system VapC family toxin [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176047532
VERSION     WP_176047532.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Arcus,V.L., McKenzie,J.L., Robson,J. and Cook,G.M.
  TITLE     The PIN-domain ribonucleases and the prokaryotic VapBC
            toxin-antitoxin array
  JOURNAL   Protein Eng Des Sel 24 (1-2), 33-40 (2011)
   PUBMED   21036780
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003923
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..123
                     /product="type II toxin-antitoxin system VapC family
                     toxin"
                     /calculated_mol_wt=13318
     Region          2..117
                     /region_name="VapC"
                     /note="Ribonuclease/mRNA interferase VapC, contains PIN
                     domain [Defense mechanisms]; COG1487"
                     /db_xref="CDD:441096"
ORIGIN      
        1 milvdtsvwi dhlragdatl tslleaervl ihpfvvgels lgslrdrqtv ldalrdlpas
       61 tsatddevqr mieiaplhgl gigyvdahll asvrltsgsk lwtrdrrlla aaerlqlaah
      121 pah
//
LOCUS       WP_176047611             371 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Burkholderia sp. BCC1644].
ACCESSION   WP_176047611
VERSION     WP_176047611.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..371
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39356
     Region          5..349
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,236,303,323,325..327)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(25,27,59,101,103,110,183,186,188,236,243,303,323,
                     325..326)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(27,103,183,186,188,326)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mtqdplfqpl qfgaltlpnr ivmppmtrsr asqpgdeane lmaayyaqra saglivsegt
       61 yiaplgkgya wtpgihtpsq vagwrkvtda vhaahgrifa qlwhvgrlsh tsllggaqpv
      121 ssspiqakgv nvfvagedgs tpgfvqasep ralsvdeire ivdqyraaar haieagfdgv
      181 elhgangylv nqfidsnant rtdqyggsle nrlrflrevt qalidgtgda srvgirlapl
      241 ttlngcvddd pettylaaat llgelgvgyl hiaeadwdda plmpvafkqq lraaypgvli
      301 yagaytaera reaiaagwad lvafgrpfva npdlperlrt gatlaphdrn tlfgggaqgl
      361 tdypalaqaa a
//
LOCUS       WP_176047604             192 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176047604
VERSION     WP_176047604.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20300
     Region          26..159
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 marprspdkh eailaaaara laedgatatt ariarlagva egtvftyfet kdallnalyl
       61 slkagmream msgfpehapv eqavrhawng yvswgvanpd grralqqlgv sgriddahra
      121 agaegfggin allreqvaat galnrdeayg fcaalfmsia etamesiard paradayres
      181 gfralwavlh av
//
LOCUS       WP_176047630             706 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Burkholderia sp. BCC1644].
ACCESSION   WP_176047630
VERSION     WP_176047630.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..706
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=76230
     Region          37..639
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mtdhtanspp qpappprrrr vwrtlagall gltlacagig awtinriwtq lpsvehlavy
       61 rpalplrifs rdgdllaeyg verrefvple ripplmrhal laaedakfye hgavdiggla
      121 ratfanvvtg qpgqggstit mqvarnfylt rdkllsrkla eilmaakler eyskdkllel
      181 ymneiylger aygfaaaanv yfgkpldals ageaavlagl pkapsafnpv vnparatarr
      241 nyvlgrmhal gqlddatyra avdapialat tpppgiiaap yvaerarrim verfhddayt
      301 lgldvtttis mrdqraaeaa lertlnrqpr akrdarngle galvsldaat gdmlalvgga
      361 dfnrnvfdha lqayrqpgss fkpfvysaal ekgyfpgvlv ddtqrtltra etgaqpwrpr
      421 nfgnhyegfi pvrrglmrsk nlvavslmqa tdaryvqqha vhfgfdaqrn paslplalga
      481 gavtplelas aygvfanggt rmeprlilsv kqrhggamye atapsgervv sarnafvmds
      541 mlrdvvragt argalalrrd daagktgtsn gskdvwfagy ssgivavawl gydtprpmgr
      601 atgatlalpv wldymktavd grtpvattpp qdvalvdgdf vyaeytrgtc tanvpayirs
      661 rfacggmaaa daldasgdsg khdepmpaav daaerervld lfrtdd
//
LOCUS       WP_176047633             308 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176047633
VERSION     WP_176047633.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33785
     Region          9..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mhrtgmtele vvlavarras frgaalelgm sttavssava glearlkvrl fnrstrsvsl
       61 tdagqryvdr iapalaeirs ageeaatgpd tpsgtlrina pqgaahlllg plfhpyaqry
      121 pdvridivse srlidivaeg fdagirlaea vpqdmiaval srdirmlvva tpeylkrhgt
      181 prhprdlleh qsigmrmahg giyhwelerh gqklqmdlpv rfvlnemaai kqatlfglgi
      241 gfisewfiee elesgalvpv lepwcpsfgg lrlyysghrf vparlralid lahelrltaa
      301 plrdghkg
//
LOCUS       WP_176047645             439 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia sp. BCC1644].
ACCESSION   WP_176047645
VERSION     WP_176047645.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 439)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 439)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10396284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..439
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=46121
     Region          19..283
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Site            order(25,27..28,30,49..51,84..86,122..124,134,138,
                     157..160)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187579"
     Site            order(100,124,134,138)
                     /site_type="active"
                     /db_xref="CDD:187579"
     Region          330..429
                     /region_name="DoxX_3"
                     /note="DoxX-like family; pfam13781"
                     /db_xref="CDD:463982"
ORIGIN      
        1 mnavlpstcq hdrtgarsmt vlvcgangfi gralcaqlea gghrvlrgvr hadgprdiai
       61 dfardvdpqa wlarlngvdv vinavgllad rrgatldavh raapcalfta ccragvrrvi
      121 qisalgverg dtryfaskha adcflqtlpi dfrivrpalv ygtdgtsarf frmlaslpvq
      181 vlpaggrqrl rpvhvddlae vvarlvvqpg daqpagsqvi dvvgrdevey remlagyraa
      241 lgfapaarvs lpgplagaaa vlsgvlpgam ftrdtwtmlr ggntgdpaat aavlgrpprg
      301 idsfigaqaa alrrdalamw rrpllrgala ivwiwtaias afihplhasl allapahltg
      361 lpalialyaa saldfafgia tvaapsrrlw aaqaalivay aaviavtmpg llaepfgpvl
      421 knvpilaill ilfseeeqa
//
LOCUS       WP_176047699             350 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia sp. BCC1644].
ACCESSION   WP_176047699
VERSION     WP_176047699.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..350
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=37025
     Region          4..350
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mqrkalliga cvlcatsaha ssvtlygivd syvefdrigs lstlrqsggg sstsrfgltg
       61 vedlgggtst kfvlesgfsp adgsfqggtl fyrqayvslq ntrygnlrlg rqytpafyiv
      121 ydgdpfglne rlsplallat stdtitsntt ppiprfnqaa sylspdwngl rvmatygfpt
      181 pntlstqagr nygaglqyri gglylgagfq gdtsagnltp vvapsttrhy vlaanyafar
      241 vklyaaflyg vvtaphlpaf stasvgasin vgaldrvlvs vvrrdvkgsa ndatalgvgy
      301 dhplskrtsl yarylymkng gdarntivvg mqpqpggteq vlalgivhrf
//
LOCUS       WP_176047706             202 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176047706
VERSION     WP_176047706.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..202
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21686
     Region          1..199
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 msivfywhpq ssaspiacal aelqvpherv kvdirageqr rpeflalnpn gkvptltvdg
       61 apmfealaih lwlgenwgvk qglwpvagtp erlaalswca wayvtygavl srlfltthgd
      121 eqirdagqaa rataeldsll glldahlarq pwmlggeysl adlvvgsvvg ysamvgapva
      181 ahpkvqawlg kvksrpamqg dv
//
LOCUS       WP_176047754             282 aa            linear   BCT 11-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176047754
VERSION     WP_176047754.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..282
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31433
     Region          11..263
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mtsihdrvaq avtpeliaaf reegavcikg ifspdevaal ragidanlaq pserakvasr
       61 pddpgwffed fcnwqhnday rdfivrspap svaaalmgte nvrlhhdhll vkepgtrqrt
      121 pwhqdqpyyn iegddnvsmw ipvdpvples tlefvagshr gpwlmprtfm dkeakwfpeg
      181 sladlpdiea draafpirhw alepgdmvcf rmltlhasgg tqnrrrafsi rfvgddirha
      241 prrwktspef pglaeqladg aaldhplfpv vwsrgagqvg ai
//
LOCUS       WP_176047726             506 aa            linear   BCT 11-JAN-2025
DEFINITION  peptide MFS transporter [Burkholderia sp. BCC1644].
ACCESSION   WP_176047726
VERSION     WP_176047726.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..506
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55360
     Region          7..485
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mmhspvsqtr sfttvfliem werfgyygma allvlfmvdr lgftdshanl twgaftalvy
       61 aapsiggwig dkvlgarrtm iigatvlcag ylmlavpndq ltymyaslgv ivvgnglfka
      121 naanlvrriy egddaridsa ftiyymavni gstvsmlatp wikdhwgwha afavccggml
      181 lailnfmlmh rtlahvgsqp ddepirwkrl gavalggval alvtlyvlqh kqlavasvwt
      241 aafailaifa ymiakserse ragliaalvl igqvilffif yvqmstsltl falrnvdprf
      301 ilfdttlftw saaqfqalnp iwimllspll vwvynavaks grdlpvaaky algfgavaag
      361 ylvftisgry avdgrvsswf mvwgyglysl gellvsglgl amiaryvpar msgfmmgayf
      421 vatgvsqylg svvanfaqmp shelpatdsl plylslfekl gwlaaigmvl allllplmnr
      481 lsrqhqrcaq erreealqtq gvaaaq
//
LOCUS       WP_176047770             432 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_176047770
VERSION     WP_176047770.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..432
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45956
     Region          18..415
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,150,
                     153..154,157,249,252..253,256..258,261,289,293,351..352,
                     355,359,375,378..379,382..383,386)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 msstsgvaal tvgksavrwk ifvvmlslia inyvdrasls vampyisqef nigpamegli
       61 lssffwtyav mqipggmlad rfkpriviat atvfwgffqa iaalctnaps llltrlglga
      121 aeapiypagg klnaiwmtqt ergrgatlld ggaplgaalg avliagliav lgswrlafav
      181 agvgtvlagl lawhyirnsp rehagvndle aeyieashas dlaaepagas grsrdffkyr
      241 svwcmffgwm cfnsvfygll twmpnylhkv hgfdikqmgg stfiiffsgf vgellggwia
      301 dkwkaaggrp nvvmrtlfgi aaviatvsif svayvkdpvv cvallsstlf flrwcglywc
      361 ipsslgtrnk igflgglmnl ggniggvtvp ivvgaivqft gsyflalmvf aaagvgllvc
      421 ssaidyenkl pv
//
LOCUS       WP_176047795             309 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrodipicolinate synthase family protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176047795
VERSION     WP_176047795.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Lawrence,M.C., Barbosa,J.A., Smith,B.J., Hall,N.E., Pilling,P.A.,
            Ooi,H.C. and Marcuccio,S.M.
  TITLE     Structure and mechanism of a sub-family of enzymes related to
            N-acetylneuraminate lyase
  JOURNAL   J Mol Biol 266 (2), 381-399 (1997)
   PUBMED   9047371
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..309
                     /product="dihydrodipicolinate synthase family protein"
                     /EC_number="4.-.-.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_process="GO:0071704 - obsolete organic substance
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=33600
     Region          8..301
                     /region_name="DapA"
                     /note="4-hydroxy-tetrahydrodipicolinate
                     synthase/N-acetylneuraminate lyase [Amino acid transport
                     and metabolism, Cell wall/membrane/envelope biogenesis];
                     COG0329"
                     /db_xref="CDD:440098"
ORIGIN      
        1 mtssstpryr gifpvvpttf tdtgeldlas qkravdfmid agsdglcila nfseqfaitd
       61 derdvltrti lehvagrvpv ivttshystq vcaarslraq qlgaamvmam ppyhgatfrv
      121 peaqvfafya rvsdaiaipi miqdapasgt alsapflarm areieqvayf kietpgaank
      181 lrelirlggd aiegpwdgee aitlladlha gatgamtggg fpdgirpile afregrhdda
      241 yaryqawlpl inhenrqsgi ltakalmreg gviacerprh pmpelhpdtr aellaiarrl
      301 dplvlrwah
//
LOCUS       WP_176047838             353 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176047838
VERSION     WP_176047838.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..353
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=39476
     Region          82..314
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mkpsqfakgf qarpdittse krtaldrlna idgivksetp tpaptksakk diapppapel
       61 tidpsidesp qyrawrlenr yapgqviels lkaikhspfn prhfylkssi aelavnlakq
      121 gqqqaihvip dydnpgtyfv sdggrrvral keankesvka ividvpigiq syklgydlnv
      181 qrdtqtvfdn avvwrrfldd khfqsqkels ehlgldestv avalsigklp epimqemvvr
      241 pdrfgsnmay qvgryhnarg teatlrlink ivsddlstrq vsdivkgrva aqetpkvagr
      301 qryaqrleik lggksvgdlk sygedrielr lrglpkdkrd aileqlerml lse
//
LOCUS       WP_176047912             268 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176047912
VERSION     WP_176047912.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..268
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26844
     Region          1..264
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mlislvlggf vgavlgltga gggilavpal vvgmswpmqq atpvalvava gsaalgaleg
       61 frrglvryra allmavagvp lttlgvrlah llpqrlllal fsltmlvvag rllrqalrha
      121 pvdaeasplc vgrvnpdtgr lvwswpvgva lastgamtgl mtgllgvggg fvivpmlrkf
      181 tnvsmhgvva tslmvialvg tggvlatlvs gtrapldvtl wftvatalgm aagrgasrhl
      241 aarhvqagfa avlvcvalgl lakaafga
//
LOCUS       WP_176047920            1049 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia sp. BCC1644].
ACCESSION   WP_176047920
VERSION     WP_176047920.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1049)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1049)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1049
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..1049
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114684
     Region          11..1027
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mstpheegrf nlsawalrhq alvvyliala tlagilaytr laqsedppft frvmvirtfw
       61 pgasarqvqe qvtdrigrkl qetpaidflr sysrpgesli fftmkdsapv kdvpetwyqi
      121 rkkvgdigyt lppgvqgpff ndefgdvytn iwtlegdgft paqlhdyadq lrtvllrvpg
      181 vgkvdyfgdp dqrifievnn aqltrlgisp qqlgqainaq ndissagvlt taddrvfvrp
      241 sgqfdnvdai adtviringr tfrlgdlatv krgyddpavt qmrasgravl gigvtmqpgg
      301 dvirlgkald aeskdlqaql paglklvevs smphavahsv ddfleavaea vaivlvvslv
      361 slglrtgmvv visipvvlav talfmymfdi glhkvslgtl vlalgllvdd aiiavemmav
      421 kleqgytrar aaafaytsta fpmltgtlvt vsgflpiala ksstgeytrs ifevsaiali
      481 aswfaavvli pllgyhmlpe rkrhaheahl pddhehdiyd trfyrrlrgw idwcieqrfv
      541 vllitgalfv vslmgfslvp qqffpssdrp ellvdlrlpe gasfaatlre terlekvidk
      601 rpeidhsvnf vgsgaprfyl pldqqlqlpn faqfvitaks vedreklatw lettlrdqfp
      661 avrwrlsrle ngppvgypvq frvsgdsiat vrsiaekvaa tmrgdartvn vqfdwdepae
      721 rsvrfeidqk karelnvtsq dvssflamtl sgttvtqyre rdkliavdlr apkadrvdpa
      781 klaglalptp ngpvplgslg rfkptleygv vwerdrqpti tvqsdvraga qgidvthavd
      841 aklnalraql pvgyqinigg sveesakaqk sinaqmplma iavftllmiq lqsfsrvlmv
      901 vltaplglig vvatlllfgq pfgfvamlgv iamfgiimrn svilvdqieq diaaghgrid
      961 aiigatvrrf rpitltaaaa vlalipllrs nffgpmatal mggitsatvl tlfylpalya
     1021 twfrvkrder dpqdgpppgg stpaapsga
//
LOCUS       WP_176047927             330 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Burkholderia sp. BCC1644].
ACCESSION   WP_176047927
VERSION     WP_176047927.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..330
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34739
     Region          6..301
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(37..38,41,93,108,110,139,172,261,264,300)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(230,235,252,261..263,266,288,292)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mkaaldvvty geamamfvat epghlahagq ftkriagadl nvaiglsrlg frvgwmsrvg
       61 rdsfggyvld tlaregidas cvtvdprypt gfqlksrndd gsdptveyfr kgsaashlsc
      121 ddyvadyvlg arhlhltgva paisatscel afllaremra agktisfdpn lrptlwpsad
      181 vmaktlnala tladwvlpgl aegrqltghd tpadiagfyl aqgargvvik lgaegayfrt
      241 adgcegtvvg ervervvdtv gagdgfavgv vsallegrsv eqavargnri galaiqvigd
      301 seglptreal drlenvsnra drleetvtaq
//
LOCUS       WP_176047977             214 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176047977
VERSION     WP_176047977.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..214
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24183
     Region          1..200
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mltvwgrrts fnvqkvlwlv gelglpyrhi aaggehgslq tpafaalnpt cripvidwdg
       61 dvvweshtil rylaarvpnn pfwcrdtfar sraerwmdws qtalepdvmt glfwalvrtp
      121 perrddaivl dkaarsathy rlldrllstq pflggatpgl adipagatlf ryfsldverp
      181 plphveawya rlcrrpayre qvmvsfdalr gqpg
//
LOCUS       WP_176047989             187 aa            linear   BCT 11-JAN-2025
DEFINITION  shikimate kinase [Burkholderia sp. BCC1644].
ACCESSION   WP_176047989
VERSION     WP_176047989.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Herrmann,K.M.
  TITLE     The shikimate pathway as an entry to aromatic secondary metabolism
  JOURNAL   Plant Physiol 107 (1), 7-12 (1995)
   PUBMED   7870841
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Bentley,R.
  TITLE     The shikimate pathway--a metabolic tree with many branches
  JOURNAL   Crit Rev Biochem Mol Biol 25 (5), 307-384 (1990)
   PUBMED   2279393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..187
                     /product="shikimate kinase"
                     /EC_number="2.7.1.71"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004765 - shikimate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=20001
     Region          18..179
                     /region_name="AroK"
                     /note="Shikimate kinase [Amino acid transport and
                     metabolism]; COG0703"
                     /db_xref="CDD:440467"
ORIGIN      
        1 msaavataga ralparaflv gmmgagkstl gralaaslgw tfadsddeie rrtgrsvaal
       61 fdivgeggfr llethivdel tqranvivat gggailnprt rarlgergcv iylhadpdal
      121 wrrtrddtrr pllqvaeprq tlaalyrmrd plyrecahal vdttahgvar atadvltvll
      181 armnapd
//
LOCUS       WP_176048038             388 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176048038
VERSION     WP_176048038.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..388
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42204
     Region          1..386
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mqfdltddqr aiesaiekic erfgddywle rdraggfpad fhaalaeagw lgiamdpahg
       61 gaglgmteaa lmmrtisasg aglsgasavh mnifglnpvq vfgneaqkar flppliagrd
      121 kacfavtepd agldtthltt qarrdgdhyv lsgrkiwist aqvankmlii arttpldqva
      181 kptdglslfy tdldrshvev reiekmgrka vdsnmlfidn lrvprddlig negdgfryll
      241 hglnperili aaeaiglgqa alrratqyac ervvfgrpig qnqsiqhpla qawmqleaaw
      301 lmvmksatry dagqscgaea naakylgaea afqacqtava tlggmgyake yhverylrec
      361 miprlapvsp qlilcyiaek vlglpksy
//
LOCUS       WP_176048042             140 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia sp. BCC1644].
ACCESSION   WP_176048042
VERSION     WP_176048042.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 140)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..140
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=15344
     Region          13..127
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04667"
                     /db_xref="CDD:467552"
ORIGIN      
        1 mstgpdtlav tkerativcr qrssvllvar tasrwslpgg tirrgetple aaqrelaeet
       61 rlvglaldya vqfggltklh hvfvaevpah ltprasneia rckwftvdrl dtlrasvptr
      121 kiiellrldc fsaivngplr
//
LOCUS       WP_176048056             755 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia sp. BCC1644].
ACCESSION   WP_176048056
VERSION     WP_176048056.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 755)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 755)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..755
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..755
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=81668
     Region          63..755
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mkkveqrkme watgtrlrai aaaasvafgt aaaghafaqt apavnagaaa sassaqngaa
       61 aststgaqng tlpaitvnaa sagdgtvglv akrsrsgtkt dtplneipqt invvtaqqie
      121 mtgatdvnaa lryvpgfssy gsdnrsdwya alrgftptay vnglqvpnti nlaswrvdpy
      181 midsisvlrg ptsvlygagd pgaiidvqtk ladgervrea gvqignyark qfmidvgdkl
      241 dpdgkyayrf vgvardgnal tgpnndqrva lapsfrwrpd adtsltlaat ylqdwgdiss
      301 nflpavgtvl pnpngqinkd vyegdgsfny yrkkqwsvgy qfernltpaw tfrqntrlmh
      361 lsldngsvfg ngfvdgsttd vsrwagvfqm nysrfdidnn legrfatgpl qhtlllgfqy
      421 nrqtatdsew laaapplniy npvytpvtls vfsnpdttyr tntyttmntf glyaqdqikw
      481 nrwtltlggr edwvnmrmdd raagtstkad vtaftgrvgl tyqgdyglsp yisyatsfnp
      541 ligvnlvggg lpqptrgkqi eaglrwqppg knlmlnaaiy qinqtnvlts alpsqddtgt
      601 ksvqtgevrs rgielsatgk vtsnlsvias yvyqdvknvk andvslnnwp vdiprprqma
      661 slwtdwtwht gplagfglgg giryqsasag aadnsltvss vtlfdaglhy dtrnwrfavn
      721 gtnlfnrhyi sgcqsynvcv fgtdrtviat akynw
//
LOCUS       WP_176048213             173 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176048213
VERSION     WP_176048213.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..173
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=17882
     Region          1..172
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mkqyqkhlvf aalmaafgst salaadgtin fhgkivattc qidnsniqvp lgaigvdqla
       61 aagresrrvp fqialsacdd qlsgvraqfe gmahgddptl laigsggtdd akgvgiqlmh
      121 ddgepigins etdtlqltpg snvlnfaany vstsdqteag eangtasftl hyr
//
LOCUS       WP_176048259             504 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Burkholderia sp. BCC1644].
ACCESSION   WP_176048259
VERSION     WP_176048259.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..504
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53295
     Region          11..487
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(68,70,74,77,81,114,117..118,127..134,139,142,145,
                     238,242,245,248,250,423,425..426,428..429,432,435..436,
                     438,440..443,452,456,458,472,479..484,486..487)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(154..157,165,180,183,213,230..233,236,254..256,288,
                     388,390,416)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(157,254,285,288)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnanskdvpt vkllidgafv esatnewrdi vnpatqqvla rvpfatvaev daavqaahta
       61 yatwkntpia armrimlkfq dlvrtnqqri aktltaeqgk tipdaegdif rglevvehac
      121 sigslqlgef aenvaggvdt ytlrqplgvc agitpfnfpa miplwmfpma ivcgntfvlk
      181 pseqdpmstm elvelaieag vpkgvlnvvh ggkevvdaic thplvkaisf vgstavgthv
      241 ynlgsahgkr vqsmmgaknh avvlpdanre qtinalvgag fgaagqrcma tsvavlvgea
      301 rdwlpdlvak akllkvnsga eagtdvgpvv sktakerils lieagvgega kleldgrdvk
      361 vagyesgnfi gptifsgvkt dmsiytheif gpvlvvlead tldeaialvn anpfgngvgl
      421 ftqsgaaark fqseidigqv ginipipvpv pffsftgsrg sklgdlgpyg kqvvqfytqt
      481 ktvtarwfdd dttagpvntt irlh
//
LOCUS       WP_176048274             634 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Burkholderia sp. BCC1644].
ACCESSION   WP_176048274
VERSION     WP_176048274.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 634)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 634)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..634
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=67500
     Region          10..634
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mpqpfvqpvt agrtdllaqa harstavglr aherpdfapl srialrelld tnhalfshar
       61 pvmedlhaqi adtqslvllt dadgvilhsi gdadfiekan rvalctgvsw aegargtnai
      121 gtalasgqav vvhgsehflr anhiltcsca pivdpfgrtl gtldvsgdpr gssphtlalv
      181 rmsaqlienh lfanqcgeal rlrfhahedc vdslfaglva fgpdggliaa nrsaqfqlga
      241 sfdalqhqas dalfgmrfgq laqqaarapg atfrltlstg vrvlarcefp daqktavavt
      301 ppapavrvra pdpdtitfat ldtgdarmaa vlervakirg rdlpllilgq tgtgkewlar
      361 alhqasprad gpfvavncaa lpdslieael fgyedgaftg arkrgspgki aqadggtlfl
      421 deigdmplaq qvrlmrvlqe ravmplggar alpvdvrvvc athrdlrami adgtfredlf
      481 yringlavtl palaartdlp alvdrilarl arsepmprri aadvldaftr hrwpgnlrqm
      541 tnvlrtagml aedeaeiala hlpddfwldc ddapaataaa tpsasataha gttlqshqaa
      601 vidavlarhg gnvsaaarel glarntvyry lrrh
//
LOCUS       WP_176048283             327 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176048283
VERSION     WP_176048283.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..327
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36221
     Region          2..327
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhraailayd dcyafslggf adilqvansh lkkqhgetgt ryewhfvsqs ggpirtsngl
       61 evntqpirpr qrfdlvfips ahyaghkafd rllasqsgac dwlitqwnag acvaanctgt
      121 fllaqtglld graatttwwl adqfrarfpr vnlqvepvit evdrlicaga sasyllqtih
      181 iverlsgptv aslcaktmli dvsqtrqtpy lplladkahg dslvhraqhw lqknmakevr
      241 msalaneldv sertlirrfq aalnqtplry lqslrieaar glfeaadlti eevavkvgys
      301 dvssfcrlfk ervglspgay rgrfrts
//
LOCUS       WP_176048323             457 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: nucleobase:cation symporter-2 family protein
            [unclassified Burkholderia].
ACCESSION   WP_176048323
VERSION     WP_176048323.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..457
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47199
     Region          21..430
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mnsashpvdr vlprrqmltl glqhmlvayi gaiavpliva salkmspadt tvlistalfc
       61 sgistilqtv giwklgvrlp ilqgvafssv gpviaigltp gvgfagvcga vigagiittf
      121 aapligrlrr lfppvvtgci vtviglqlfp vayqwagggd aaklqfgels flavalvvav
      181 vilavnrfan aflrnlsvli glvagsllai algmgnftnv aaapwftvpy pfhfgtpvfa
      241 ivpvltmvvv mivqmvesmg lfvaigdive kqvseedvvr glrangvasa iagtfaafpf
      301 iafmenvglv iltgvrsrwi vavsgalmci valvpkigai vastpsaalg gagiamfgvv
      361 vaagvqtlak vdfennrynv livgftiata lipvmapkvf ahmpdwtqpf lhsgvvlacl
      421 vsvllnalln gvpaaepves hvhadaahrs gmarecd
//
LOCUS       WP_176048330            1013 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176048330
VERSION     WP_176048330.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 1013)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 1013)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1013
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..1013
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=107434
     Region          132..881
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 maesagsspl ggaltsgamq masaaspvag kiaptasavm qalaaggnpa qiaasmaapa
       61 agmlnplagq lasgalsgmr aaaapamsaa aapvaddhpl vgqplsdlas apqffmpgqt
      121 aakpgaqepa lpfsettrll rlqssltgnr alsiaairgg ealsempgyt ldliaqnpsi
      181 dlkdvlnqav tvnitlqdgs erqihgylvr fgferndggi ahyrgelvpw lwylgkrvns
      241 riyqqvtvld vlrkvfadyg alvdyqthvk qelkpedyvv qfqesdlnfv srllerhglf
      301 yyfeyrqdgh tlviaddsas cpdqahdpvv tynaasgvqq adrltalsas retqpgvval
      361 htfdykhpks rpyvelptla dqgnapklev ydgssafayk dtsageaeak rrlevfewqa
      421 kvfrgesgcr gltvgrkfri dghfwfdpak qddneflvvg leidaknnfd dastqpgsfr
      481 nsltlirski pyrpvrrhdk pvmpgpqsai vvgpkgqeih tdgmgrikvq fpwdrygknd
      541 qesscwirvs qpwagrgwgt vaiprinqev ivdflngdpd rpiivgrmfn aeqtppyglp
      601 dgahqmgfhs nstpggggfc evvihdkkge elvnihsqkd mattvqnnhv tvvngpnqtn
      661 vvtqgqhasi vrkaisvqsq dehiqhtakt avilhaqeqh malkakgpvq iesdtehvhv
      721 kgsqsivlec gkakitlsan geivldgtrv vvlgsqsvdl npdgttgpaa pplvpvtdpa
      781 apaqdlaapa aggggggggg gggaaaaapa hakqhakgap kkkavatglg agvdqlaaks
      841 ptlerdiakl qkdgwniqyg panqgsstnk sghpptivid gndrgnpqav vqglahetgh
      901 alyqgtpdys skanyvnsel adegaatmnn ikvqreivah ggpdiqiagd panapaynaa
      961 ynqfvrngda taaraaighv ygtgehasvp vngqyvnyqt yygswydrny psh
//
LOCUS       WP_176048336             345 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter permease [Burkholderia].
ACCESSION   WP_176048336
VERSION     WP_176048336.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..345
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35818
     Region          20..345
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msndthpvpp lasgdtpaaa sslksrffnp aarqkllafa slvllivffs faspnflevd
       61 nlvtilqata vngvlavact yviitsgidl svgtlmtfca vmagvvltkw gmplplgila
      121 allfgalsgc vsgfviakmk vppfiatlgm mmllkglslv isgtrpiyfn dtpgftaiaq
      181 dslignlipa lpipnavlil flvaigasiv lnrtifgryt falgsneeal rlsgvnvdaw
      241 kiavytfsga vcgiagllia srlnsaqpal gqgyeldaia avviggtsls ggagsivgti
      301 igafimsvlt nglrimsvaq ewqtvvtgvi iilavyvdil rrrrr
//
LOCUS       WP_176048374             389 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: electron transfer flavoprotein subunit alpha/FixB
            family protein [Burkholderia].
ACCESSION   WP_176048374
VERSION     WP_176048374.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..389
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=39974
     Region          61..369
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mntikridpr rpfiitaagl kritlgeegs adanaaygaa hghgaaaakp rralqdpkhv
       61 mlvvahgerg alddhsrqai aaaavladaq tevallafge lkddvaelgv dklleltgfd
      121 rrtfdpesel qalqacvaal apkhvfvpdn atgdgdlgrr yaaaagasva thvveidakh
      181 vgayaqagra fatralpdvi llaqnavdak lpfvgagerl aadfirpahd atqpyrdlgl
      241 deidaaqval eeadfivsag ngvsdigafe qlagafgaai gasrvavdng hftrdkqvga
      301 tgktveasvy iafgisgavq hlqgikdcrh viavnldgsa piakranltv vgdaqatiaa
      361 lieqvqaara argespaavg trepegvaa
//
LOCUS       WP_176048377             341 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176048377
VERSION     WP_176048377.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..341
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37393
     Region          11..318
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mspdrtasls hfafmplpnf tmiaftnaie vlrmanylsg qplyrwsvis pdggpvtasn
       61 gltvdtgpae cagqpdivfv cggvdvqrat tpahlsalrr farsgiplgs lctgtyalak
      121 sgllagyaca ihwenmsalk eefpdtrflk elfvidrdri tctggvapld mmlnliaarv
      181 gtarvtqiae qfivehvrdt saqqrmplva rlgsankslf evislmenni eeplsreela
      241 rlanmsqrql qrlfrehlgm tpthyyltlr lrrarelllq tdmsimhitm acgfqsachf
      301 sksyrdafgv aptrerrkqv aplaqgaasa apafpthvlh a
//
LOCUS       WP_176048400             314 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176048400
VERSION     WP_176048400.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..314
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34318
     Region          5..225
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mqpilsvsdl sktyasgfqa lkhvtldirp geifallgpn gagkttligs icgivtpteg
       61 rvtvgghdir dqyraaremi glvpqelttd afetvwatvs fsrglfgksp dpayiektlk
      121 alslwdkrdn klmtlsggmk rrvmiakals heprilflde ptagvdvelr rdmwklvdsl
      181 resgvtillt thyieeaeem adrigiilgg elvlveekre lmrklgkkql tvqlehplad
      241 vppalvpfgl eraddgaalv ytydshrdda siaklinalg sagigfrdlh ttqssledif
      301 vslidnrrng vqga
//
LOCUS       WP_176048456             332 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176048456
VERSION     WP_176048456.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..332
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36458
     Region          21..328
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mtsavavapa acvspvssla hfgfltlpnf smiafssave vlrmanyvgr adhykwsiys
       61 ldgapahasn giavrptqal dytnlpdvii vcggirirdv vdegardtla alaerglplg
      121 gictgayalm ssglldgyrc tvhwenlsal hsefpqvgfa delfvvdrdr ltctggtapl
      181 dlmlnlvgmr fgqqlaaqvs eqfilerirs stdtqpipvd arvgfsrael ievvrlmean
      241 ieeplsleel arlvrlsqrh lqrmfkvyln vspthyyltm rlkrardllr ttdasiarvt
      301 tvcgfhspch fskayraqfg hapsyerrlp gr
//
LOCUS       WP_176048480             321 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia sp. BCC1644].
ACCESSION   WP_176048480
VERSION     WP_176048480.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..321
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34700
     Region          11..224
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(52..53,55,69..71,77,79..80,121,223)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(52,54..55)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(77,80,83,90)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(113,117..120,122)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(118..119,142..144,196..197)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          237..321
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 msaatltvrv arkwqeardi cgfefvsddg splprfdaga hidvhlpggf vrqyslcnhp
       61 ergnryqiav lrdadgrggs raihdevrqg dtvrigvprn qfplapdaph hlllaggigv
      121 tpilsmaerl fssgmpfdlh ycarstdrma fverintagf rdrtrfhvdd gapeqrfdla
      181 avlaaapegt hlyvcgprgf mdavlnaart rswaearlhy effggavass gadrafqvri
      241 assgkvidvp aectviaala angvdvltsc eqgvcgtcvt rvlegepdhr dsylteaeqa
      301 agdqfmpccs rsrsdllvld l
//
LOCUS       WP_176048495             232 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia sp. BCC1644].
ACCESSION   WP_176048495
VERSION     WP_176048495.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 232)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 232)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..232
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23385
     Region          48..126
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          144..230
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mndtvetpre psrrrfapll laaaalfagh ahaedatsgk tiatqgtatg vaacigchgs
       61 qgegnaaagf prlagtnaay lsaqlaafad gsrqnpvmqp lskllspher davsayfasl
      121 papagvftpd dasidptntg awlatrgrws qglpacaqch gpgglgvgta fpplagqpaa
      181 yvagqlngwk hgtrppgpmg lmpmiagkls dadidavaay yarggtaqgd kr
//
LOCUS       WP_176048547             850 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176048547
VERSION     WP_176048547.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 850)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 850)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..850
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..850
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=92902
     Region          14..804
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnsqelvrai ggglfqqarl lkldtplgqn vllpqtvhgv srlgrdftlt vdavstrdni
       61 elkkliaqpv tlwveqqgdt ylpwhgyvqt arrlgfnggi tayqirfmsw lgflryrrdq
      121 riwqdrtade iltdvfnqhp qaagmfrfal saplrnrsfc mqfehdwhfi hrlledeglf
      181 gyfeqaedgs hhtlvitdsl hslpaaappr vpflraasgd etqalvqwsg trtlqsshyt
      241 trtfdykspg talnpkgtdv ptrpdqgdlp nqaevytytg pytygaqgdg nrqstirmee
      301 wesrakrfhg fggmrgidtg rvfeltdhva hppserdgnr favvetvwwi knnipaapsh
      361 fphglaaqfd amkaqlgdaa gamtvrhtdg segfylveie aqrqtvpfrs pfehpkpemh
      421 lqtatvagpk geevhtdeln rikvrfhwdr lnegderasc wlrvassdtg ggygsvhvpr
      481 igeevvvdwm sgdcdrpivt arlyngatqp qwhtdgllsg frskeyagsg ynqlvmddat
      541 gqnrsqlyss tansllhvgy lieqsgntrg ayvgsgfdlr tdaygavran qglyvtthpk
      601 svssqpldvr etqqqlvgae slleslsdvs ethqaetlkp grdalktftd atqqsvpgaa
      661 sggrtsgggt gnanaftqpa mlfgspagig masqqslqiv adrhvnivsg qnthlaagks
      721 lvasvissvs lfaqnagmkl fagkgkieir ahdddvelta qktvkivaat aqidlaskqp
      781 illtsggayi rigngnieih apgkvdfkgg dhsfsgpast dypmprlpeg vcsecrrsaa
      841 kmksaltprt
//
LOCUS       WP_176048575             463 aa            linear   BCT 11-JAN-2025
DEFINITION  alkaline phosphatase [Burkholderia sp. BCC1644].
ACCESSION   WP_176048575
VERSION     WP_176048575.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Vimalraj,S.
  TITLE     Alkaline phosphatase: Structure, expression and its function in
            bone mineralization
  JOURNAL   Gene 754, 144855 (2020)
   PUBMED   32522695
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Sharma,U., Pal,D. and Prasad,R.
  TITLE     Alkaline phosphatase: an overview
  JOURNAL   Indian J Clin Biochem 29 (3), 269-278 (2014)
   PUBMED   24966474
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..463
                     /product="alkaline phosphatase"
                     /EC_number="3.1.3.1"
                     /GO_function="GO:0004035 - alkaline phosphatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0106219 - zinc ion sensor activity
                     [Evidence IEA]"
                     /calculated_mol_wt=48047
     Region          28..463
                     /region_name="PhoA"
                     /note="Alkaline phosphatase [Inorganic ion transport and
                     metabolism, General function prediction only]; COG1785"
                     /db_xref="CDD:441391"
ORIGIN      
        1 mstikciaaa lavagfacga aqaagqaknv ifflgdgmgp ttvtasriyk vgesgqltme
       61 tlartarikt fsndaqttds apsmaaymtg vkmnnevlsm ssdtravapg sdangnktvn
      121 ncapgngqpv atllelakar gkavgsittt elthatpaat yshichrdaq ydiaaqaapg
      181 gagynaalgd gvdvlmgggr nhwtpfdaat nkrgradgrn llnemkakgy tvvatkdqla
      241 qagngklvgl fsstshleye ldrvagkgeg psqpslaemt skaidvlskn sngyflmveg
      301 gridhalhgt nakraledta afdeairval skvdlsntli vvtadhdhtm tingyskrgn
      361 pildisrnyr dgqpskdadg ntyttlvfgn ganrpnvrts vdsatatnea ylqevgvrmg
      421 sagsethggg dvmlfadgad akafkgtidn tkvfglvrsa fgf
//
LOCUS       WP_176048610             236 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176048610
VERSION     WP_176048610.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..236
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25476
     Region          15..169
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mnaphcvtep nilyfgtpvv lvstlnengt anlapissaf wlgwrgvigi aassqttrnl
       61 lrtgecvlnl psaaqahavd riarttgtyp vpdgkrakgy vfepdkfgta glteaasqtv
      121 appralecpv hmeavvaath gigeetpdlr ghirvfevri qrvhvhpdll mddhpdridp
      181 dkwsplimsf qkfyglapqq vhasrlaeip erayrspdie rsrevgapag apkpig
//
LOCUS       WP_176048614             847 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176048614
VERSION     WP_176048614.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 847)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 847)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 847)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..847
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=89049
     Region          25..843
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mvltaiagwt thaigapvva advdaspaaa tqvasvefds gflpgqhggg nvdlsrfekg
       61 navlpgsygv dvyvnenlvt tmqvafrasa rsidaqpcfg eaqledlgvd vqrlapdvls
      121 rlrdgracle vadaipdatt sfefgeqrlr vsipqtalrr sprgyvgper wdegvtagml
      181 nynanvysrr gsggptitqg yvgltggvnv gawrfrhegs yswstgggah yqdiatyaqr
      241 dltalksqft igesytsgel fdstqfrgvq lasddrmlpd svrgfapvvr gvantnarvt
      301 irqngmtiye ttvapgafvi ddlyptgygg dlivqvtead gsihqfsvpy aavpmslrpg
      361 vhrysfvagt vrdmesnrnp lfmqgtwqqg ltnlvtaygg atvaqgylsg migtalntry
      421 gafgfdvtqa stsvpgmkrf sgtsarlsya ksitqtetdi alaayrysts gyfglndamr
      481 vrervanggn vdsvarqrsr tslsvnqalg gragrlalnv aatnywnrgg tdysysatys
      541 ntfrnmtygv svlrqqnsmg rsdtqyyvsa tipfgrtspv tattsfshst sgenqalatf
      601 sgsagrddnv sysvtanhts gygntsndgs gsvvyrgsag elsatvgaga gyqqgsvgir
      661 ggmvahrggl tlsqplsetf aivkaddaag arvmnsagar vdgrgyavvp fltpyslnai
      721 eldpeglstd vemksttqqv apragavplv efatasgksa vidarrddgs alpfgaavvn
      781 aqgneigvvg qgsrifargl ddsgtltvrw sdtgdascsi nyslpvaksk aashgvrqly
      841 svcvagr
//
LOCUS       WP_176048616             210 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Burkholderia].
ACCESSION   WP_176048616
VERSION     WP_176048616.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..210
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22042
     Region          2..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 midlstlalf sgaclaltat pgpdmllias rsvsqgrrag fatlagiqag tychalaaal
       61 glsqlfvavp iaydavrfag aayllylawk tfrsnatals pvasqrrhst atifrqgltt
      121 nllnpkmalf vlalfpqfvr pehgsiavqi lvlatvlnli glvvngavil sasrlsqrig
      181 arrrpsklpq yllgtvfvgl aarlaiagrn
//
LOCUS       WP_176048625             413 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1644].
ACCESSION   WP_176048625
VERSION     WP_176048625.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13023536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..413
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44236
     Region          44..408
                     /region_name="MFS_MdtG_SLC18_like"
                     /note="bacterial MdtG-like and eukaryotic solute carrier
                     18 (SLC18) family of the Major Facilitator Superfamily of
                     transporters; cd17325"
                     /db_xref="CDD:340883"
     Site            order(45,76,126..127,129..131,134,154,157..158,161,243,
                     246..247,250..252,255,282,286,335..336,340,344,360,
                     363..364,367..368,371)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340883"
ORIGIN      
        1 menaavargg ravalglren gwqfallvlv nafvggmvgi ertvvpligs eqfhlestal
       61 itsfivsfgl vkafanlvsg qladtwgrkr vlitgwlfgl pvpfmiiaap nwewviaanv
      121 llglsqgfaw smtvimkvdl vgpksrglav glnecagyfa vgatafatgy lasryglrpt
      181 piylgvfyai aglllsilvv rdtrdhvrle sgrlagasvl sfrevfmlts frdrnlfaas
      241 qagminnlnd gmswgifplf fttlglgier igilkavypi vwgscqivtg plsdrwgrkg
      301 livagmwvqa aglaltaltg qfrwwlvasm llglgtamvy psliaavsda sepgwrarsl
      361 svyrfwrdlg yaigalsagl madrfgfaaa ilvvaavtfa sggvvaimmr erh
//
LOCUS       WP_176048654             454 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Burkholderia sp. BCC1644].
ACCESSION   WP_176048654
VERSION     WP_176048654.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..454
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=47987
     Region          220..408
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mrfdqrfrla reqgqparrg ascfpmrrvl lrgviatacv agvhgaaaqa ghdaaplapv
       61 ttdlvdvpff sstrttwggl rastaapldi ayplhasnms tntgrddpva rfgacvayrv
      121 lceaardave rgyasrfdyg lasalpamvt qpafergavd lasaepftla epdrgtragt
      181 iagslhtsla raelpagvaa qivrmlagri dpklrgetgd tfrvafepdg satrpgrvrv
      241 taldirfrgq hvtgvwfapq agspgayydl dgmplagarf ampvaakris spfgtrvhpv
      301 sgarhvhsgv dlaapagrav hasergvvtf igteprgygk yvvirhdggy asyyahlsaf
      361 eptlrtgmrv vrgqrvgavg stgtatgphl hfevrrharl vdpialvqta kaaklkgeqr
      421 vvfnrvarda rtqlasatwa qpvaisktsa shag
//
LOCUS       WP_176048670             317 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Burkholderia].
ACCESSION   WP_176048670
VERSION     WP_176048670.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..317
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34525
     Region          11..70
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          100..296
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(114..115,117..118,121,125,127..133,225..230,
                     236..237,239..240)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mysligktat frqlkaldmi arlgsvsraa eelnltqpav slqvrlleea vgaallqrvg
       61 rgvqltaage ivsryareil hlwseagdev aaltgdlggt lrigaittae ylippllvkf
      121 tatrphvkty fkvgnrddii rmlatheidl avmgsapkel rthavefakh pmvfvaapgh
      181 plmqrkrval kdlesahllv rergagtrst veslfknagh rfhvgselss neaikqmaea
      241 glgiaflslh acalelrtgl lgqlpfpgnp ierewyvvtl adrrisqvtg lfrdflikqg
      301 apvidgatva pherrrk
//
LOCUS       WP_176048709             424 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1644].
ACCESSION   WP_176048709
VERSION     WP_176048709.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..424
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46162
     Region          9..403
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(21..22,25..26,29,61,111..112,114..116,119,139,
                     142..143,146,228,231..232,235..237,240,268,272,330..331,
                     335,339,354,357..358,361..362,365)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mklfratgiv lvmlcvmyfi tyldrvnvst aaagfgkefg lnkteiglvf safaypylvf
       61 qiiggwvsdr fgarrtllac gllwavatll tgmagglasl laarlllglg egatfpaats
      121 amsrwvprek rgfaqgitha fsrvgnavap aavvavmavy gwresfyicg visivwvavw
      181 alvytehpkd hpritqaeld alpppkqkpa tvpwgplfrr mmpvtivyfc ygwtlwlfls
      241 wipqyflhsy dldlkksavf asavffagvi gdtlggivtd riyartgslk rarswmvsic
      301 mlftllsllp llfmhdlyvs maclaagfff aemtigpmwa vpmdiapeys gtasgmmnsg
      361 salaailspv isgfvidrfg swelpfigsm vlmgvgvlla frmqpdsrfa dapaeqpath
      421 rspa
//
LOCUS       WP_176048711            1013 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding and (Fe-S)-binding domain-containing protein
            [Burkholderia sp. BCC1644].
ACCESSION   WP_176048711
VERSION     WP_176048711.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1013
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..1013
                     /product="FAD-binding and (Fe-S)-binding domain-containing
                     protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=110416
     Region          24..539
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
     Region          492..1012
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mksavspslv rpvhlvpsqg aalsplferl rtemrgdvha drasrgryat dasiyqimpl
       61 gvvvprdqdd lrvaldiard rkipvlarga gtsqcgqtvg ealvvdnskw lnrivefdaq
      121 ahtvtvepgi vldhlnawlk phglwfpvdv stgaqctigg magnnscgsr sieygnmvhn
      181 vlaidailad gsecrfgsla qpvtdrrtle llhgveriai rerdeiverv pkvlrrvagy
      241 nldlfdcqnp raytddghan lahllvgseg tlaysrqitl klaplpahkt lgvvnfptfy
      301 qamdtaqhiv klkpvavelv drtmidlsme npafrpvieq alvgqpqail lvefagesrd
      361 aqlaqldrla elmadlglpd svvkmtdaga qkalwdvrka glnimmsmkg dgkpvsfied
      421 cavplehlae ytrrltdvfh khetegtwya hasvgtlhvr pildmrrdga trmreiaeea
      481 aalvreykga ysgehgdglc rgewvawqyg prlnaafaei kalfdpdnrf npdkivnppk
      541 mdtrehfrfa pgyaalplqp aldwsawnva rnpltgeeta pgsgtdithg lasavemcnn
      601 nghcrkfdag tmcpsyrvtr deqhvtrgra ntlrlavtgq lgadglagdd vkaaldlcvs
      661 ckgckrdcpt gvdmarfkie arhawnrkhg atlrerlvay lpryapwaar mrgaiafang
      721 vpvvasamkr wiglapqral pafarpfltd agmgagtsvs sqdtgsvtre vllfvdtfsn
      781 yqepdnaraa qavleaagyt vhfnvreger plccgrtfla aglvdeakae akrtldtlrp
      841 ylergvaivg lepscllsmr deflaygygd eaarlashaf lfeeflvreq eagrlslplh
      901 aidakealvh ghchqkafga ftpvqtvlrw ipglkvspve ssccgmagsf gyeaehyaas
      961 qamaelsllp avraraedai vvadgtscrh qiqdgaqtqa vhvarvlaqa lqn
//
LOCUS       WP_176048735             219 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia sp. BCC1644].
ACCESSION   WP_176048735
VERSION     WP_176048735.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 219)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 219)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..219
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23229
     Region          <55..121
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          <157..218
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mkkrmlllaa lvaagallal ygptllgfyr lqrhidtaaq addadggpwp rvtdtcmgch
       61 gvkgtslnqa ypslagqpaq yvavqlrafa sgqranptmg plamtmsete vahladyyak
      121 qvpvdnryfk adarlrakge qrvkgaacaa chgarltgqa qfprlagqgy dyllaqldaf
      181 angtrseatg tmqrvtkams addrmaiaty lasvspgkq
//
LOCUS       WP_176048752             311 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176048752
VERSION     WP_176048752.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 311)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 311)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401161
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..311
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35291
     Region          14..95
                     /region_name="cupin_MtlR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to MtlR, N-terminal cupin domain; cd06976"
                     /db_xref="CDD:380381"
     Region          31..284
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnpdleivpt hrdesfrawv hdyphsvakw hfhpeyeihl iqashgkvfv gdhigdfgpg
       61 nlivtgpnlp hnwvseladg ervlsrdvvl qfsrdaiekm vgafselqpv idliddaarg
      121 vqfpdrvgae vaplmlelan ahgcrrveil mslfdrlssc rerrvlagpg yrsnaqhyms
      181 stinqvlsyl qqnlpgmlre tdvaafagms vstftrffrr htgssfvryl nrlrineace
      241 llmfsdltvt dicyrvgfnn lsnfnrqfla mkqvppsrfr alhrlnephg rddappprra
      301 pprtpdrtlh t
//
LOCUS       WP_176048782             521 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia sp. BCC1644].
ACCESSION   WP_176048782
VERSION     WP_176048782.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..521
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=55763
     Region          1..521
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 metydhivvg ggsagctvah rlvkagrrvl lledgpkdds lfvripatfi rvlgtrrtvt
       61 fesepqpgaa grktyvpqgr tlgggssvna mlyvrgtrdd yddwaalgct gwgwddvlpv
      121 fkraeshlrl sepfhgtdgp lkvgdtrfrh plslafvkaa qeagiayndd fngatqhgvg
      181 fyhttifdgq rgstaatyla eaiahpnlrv ltgcrvtrir fdgrratgve wriesgatgs
      241 aaaradivla agalstpkll mlsgigpgah lhahgidvlh dsrdvganyq dhlevsiygr
      301 shapvsllge drglkalrhg lqwmlcrtgl ltsnvvesga fvdttgsgrp diqfhvlpil
      361 vgdvdreplp ghglsinpcl lrprsrgsvq lrgndpaapi lfdsgalsdp advdglvrgv
      421 alarrvirap slarivreae tltdaalady vrhraktvyh pagtcrmgnd ahavvtprle
      481 vqgmdglric dasvmprivs gntnaptimi aercaefmla e
//
LOCUS       WP_176048784             177 aa            linear   BCT 11-JAN-2025
DEFINITION  2,4'-dihydroxyacetophenone dioxygenase family protein [Burkholderia
            sp. BCC1644].
ACCESSION   WP_176048784
VERSION     WP_176048784.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14449000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..177
                     /product="2,4'-dihydroxyacetophenone dioxygenase family
                     protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20137
     Region          37..160
                     /region_name="cupin_DAD"
                     /note="2,4'-Dihydroxyacetophenone dioxygenase (DAD), cupin
                     domain; cd20302"
                     /db_xref="CDD:380436"
     Site            order(53..54,57,63,65,82,84,86,88,101,104..108,110..112,
                     129,135,137,145,148,151)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:380436"
     Site            order(77,79,94,115,130)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380436"
ORIGIN      
        1 mvdkavsefw qnipaianpf kpdalpeayi pnaatddery yvpftetvss rplwispsqn
       61 kwcdilmake aglvnrhyhp hevfaytlsg kwgylehewt atrgdfvyet pgeghtlvaf
      121 dhpepmraff ivkgpliwld edgnpdgyfd vhsyiamcka hyekvglgaq aieklfr
//
LOCUS       WP_176048785             434 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1644].
ACCESSION   WP_176048785
VERSION     WP_176048785.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..434
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45629
     Region          7..406
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mtspsssrsa wtyenrllli lfmtfgfvff drlalsflfp fmsaelhltn tqlgmvssal
       61 altwalsgaa tgawsdargt rkplliaavl gfsvcsalsg lvggfaslia fralmgiaeg
      121 pvlplsqslm vesstpsrrg lnmgllqgsa agllgamigp pvvigiatty gwreafyvsc
      181 ipgfliafci wrwvrevppg gvryaqadgt gvpaasgtai nrwallkern illcvliscc
      241 fltwfvviis fapvflvenr hlspsdmgvv mtclgaawvf wgfavpaisd rigrkptmiv
      301 faliaavcpm vmihvgsvwa lgtlvfvtyt glgcftlfma tipaetvppr aiasalglim
      361 gageliggfv aptvagfaad kyglqfamwt sttgailacv lsfglvetap avlrkralag
      421 aasgrldaqn lggr
//
LOCUS       WP_176048790             532 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia sp. BCC1644].
ACCESSION   WP_176048790
VERSION     WP_176048790.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..532
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=57678
     Region          2..532
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 msdrtfdyiv igagsagcti athlverrkg tvllleaggh dkdlfihmpg glakaiprht
       61 wpyaadpsdd vkgrsiavpq grvlggsssv ngmlyvrghr ndydrwenef gckgwgadem
      121 lryfakaenn esltapyhgn kghlqvteir yrhplsqafv ragqqmgldy lvdyngerqe
      181 gvgfyqatif ngergstaat ylkairnrpe fslevdalve rveieggrat gvtyrqgsrr
      241 vtakaraeii vtagaigspk ilqlsgigpr svlegagvpv rhvlpvgenf hdhmhmsvna
      301 tirtpvslyg qdkgwralkh giewkffrsg iltspvlegf afvdtcgqgq pdvqfhflpt
      361 idsfddpigv tqgrthgiti ktghlqphsr grvmirssnp adlpridgry ladrrdvdgq
      421 iraaklalki lrqpalaehv deifspdcpp ddeagiedwv rgaaktvyhp vgtcrmgtda
      481 assvvdpqlr vhgiaglrva dsstmpsips gntnaptial aekasdliag aa
//
LOCUS       WP_176048824             280 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: helix-turn-helix transcriptional regulator
            [Paraburkholderia].
ACCESSION   WP_176048824
VERSION     WP_176048824.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..280
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30678
     Region          82..263
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 maaflerltp hleraaqlqa qryvfstdal vghafvnrsr qpviltsteg ellrhnepaq
       61 hllqstslvr iagrrivlpe pfysrfledc aeterrvrsg eprayedaah yrvmripgea
      121 apparrqghg hgamtsqggt daansglpav epgadssdml yvfynlivpg evsatfglrt
      181 iamlifyhpr sappvdedll aaafdltpae sriahlladg ltpkdiatrv gvqpdtvrkq
      241 mqsiyqktgt nrqpdlvrll lhlpgasavg yvqaardwkl
//
LOCUS       WP_176048929             126 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF805 domain-containing protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176048929
VERSION     WP_176048929.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..126
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=13420
     Region          5..122
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 mgfseavrtv lnkyatfegr arraeywyft lvsvilsivv qiigaggrdg glitllllgi
       61 iclvslalii pgiavsvrrl hdtgrsgwfl lialipivgg illlvwmcsr gtdgpnrfga
      121 dpipav
//
LOCUS       WP_176048955             487 aa            linear   BCT 11-JAN-2025
DEFINITION  catalase [Paraburkholderia kururiensis].
ACCESSION   WP_176048955
VERSION     WP_176048955.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia kururiensis
  ORGANISM  Paraburkholderia kururiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Paraburkholderia kururiensis"
                     /db_xref="taxon:984307"
     Protein         1..487
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=54960
     Region          2..474
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 mtsntlthlt saagapvadn qnsmtagprg pvmlqdvwll eklahfdrev iperrvhakg
       61 sgafgtlkvt hditqytkar vfaqpgketp lfmrfstvag ergaadaerd vrgfsikfyt
      121 eegnwdvvgn ntpvffirdp lkfpdfihtq krdpytnlrn nvaawdfwsr hpeslhqvti
      181 lmsdrgipkn yrqmhgfgsh tysfinasne rfwvkfhfks lngienytne eaaqviaadr
      241 esaqrdlveh idqgnfprwa friqvmpead aakvpynpfd itkvwphkdy plidvgviel
      301 nrnaqnyfad veqaaftpan vvpgigfspd rllqgrlfsy gdtqryrlgv nhhqipvnap
      361 kcpfhhafhr dgamrtdgnl ggtvnyepnr fgdftqdrna aepplaggtv dhydhredgd
      421 yysqpgalfr lfdaaqrerl faniaatidg vpkeiverqv ehfrradaay aegviaamaa
      481 raeerkv
//
LOCUS       WP_176048987             216 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia sp. BCC1644].
ACCESSION   WP_176048987
VERSION     WP_176048987.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..216
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24167
     Region          61..147
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mhdsrhssll advaayygar laehgqtarg vdwngedgqr lrfaqltkiv apdahgfsvn
       61 digcgygalv dfldehtagr rhvyagndvs pemvdaarqr yrdranvsfh vgdaplatad
      121 ygiasgifnv hrghddetwl dyihatldvl hatsrlgfsf ncltsysdpp fmrperlyya
      181 dpcalfdrck rrysrhvall hdyglyeftl lvrkdg
//
LOCUS       WP_176049049             235 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176049049
VERSION     WP_176049049.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Upton,C. and Buckley,J.T.
  TITLE     A new family of lipolytic enzymes?
  JOURNAL   Trends Biochem Sci 20 (5), 178-179 (1995)
   PUBMED   7610479
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..235
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=24729
     Region          43..214
                     /region_name="FeeA_FeeB_like"
                     /note="SGNH_hydrolase subfamily, FeeA, FeeB and similar
                     esterases/lipases. FeeA and FeeB are part of a
                     biosynthetic gene cluster and may participate in the
                     biosynthesis of long-chain N-acyltyrosines by providing
                     saturated and unsaturated fatty acids, which it...;
                     cd01836"
                     /db_xref="CDD:238874"
     Site            order(53,90,118,209,212)
                     /site_type="active"
                     /db_xref="CDD:238874"
     Site            order(53,209,212)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238874"
     Site            order(53,74,118)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238874"
ORIGIN      
        1 mgypfataal vpllfaqgry vrrvtprlpe aagprdgvag dgpplrvlvv gdsaaagvgv
       61 ttqrdalsgq lahalaathr vswkllartg lttrelvdwl aaepaepfdv avtslgvndv
      121 tggvaparwl aqqaelvrll agrfrvghai lsavppmerf palpqplawy lglrakrlna
      181 alagwagaqp hctflrvdlp lerhlmavdg fhpgesacav waaqvaaavr qrvta
//
LOCUS       WP_176049070             387 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: porin [Paraburkholderia].
ACCESSION   WP_176049070
VERSION     WP_176049070.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..387
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=41890
     Region          15..387
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mhfnavneet ivrkkhlala vpatvafaag sayaqssvql yglmdlsvpt yqshadangn
       61 hvigmgigge pwfsgsrfgm rgaedigggt qvifrleaey rvadgqmedp gqlfdrdawv
      121 glqndtfgki tagfqntiar dasaiygday gssklsleeg gwtnsnnfkq mifyaagptg
      181 trysnglawk klfnngifas agyafgnqts fglnsvyqga lgyngdafav stfyshvnkq
      241 gfanqsfsvg gnytfgilra nagyfrywgd qgslgqrqdn awtvsfklsp kgpldyelgy
      301 qqmrvhnaay nsdgdipnan lgtfdpasgl hngfketlyg svfyhfskrt evylagdymr
      361 lhggytvgst fgsnnqvevt ggirtrf
//
LOCUS       WP_176048968             124 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Paraburkholderia kururiensis].
ACCESSION   WP_176048968
VERSION     WP_176048968.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia kururiensis
  ORGANISM  Paraburkholderia kururiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 124)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 124)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Paraburkholderia kururiensis"
                     /db_xref="taxon:984307"
     Protein         1..124
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13324
     Region          39..124
                     /region_name="CytC552"
                     /note="Cytochrome c551/c552 [Energy production and
                     conversion]; COG4654"
                     /db_xref="CDD:443692"
ORIGIN      
        1 mkatyknmga caallagfag laglagsgaa haqqtkrmae ptelvdqqhc mfchtsdspf
       61 lapsfhqiae ryrkvpdatv mleqklrlgg rahwgdtpmp lpperggpls pedahtliqw
      121 vmtq
//
LOCUS       WP_176049209             160 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein, partial [Paraburkholderia
            kururiensis].
ACCESSION   WP_176049209
VERSION     WP_176049209.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia kururiensis
  ORGANISM  Paraburkholderia kururiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 160)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Paraburkholderia kururiensis"
                     /db_xref="taxon:984307"
     Protein         1..>160
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          1..>160
                     /region_name="TagH"
                     /note="ABC-type polysaccharide/polyol phosphate transport
                     system, ATPase component [Carbohydrate transport and
                     metabolism]; COG1134"
                     /db_xref="CDD:440749"
ORIGIN      
        1 miqldrvtkv yparggkkvv lddvnfvler gqkigilgpn gagkstlirl lagveqptkg
       61 airrhmslsw plafggafqs sltgldnlrf vcrvygcnes kmrafvdefs glgrylrepi
      121 kvyssgmrar lafalsiave fdcflidevi avgdqqfqer
//
LOCUS       WP_176049312             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderia].
ACCESSION   WP_176049312
VERSION     WP_176049312.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..436
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45726
     Region          21..426
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(34..35,38..39,42,81,139..140,142..144,147,167,
                     170..171,174,257,260..261,264..266,269,297,301,353..354,
                     358,362,378,381..382,385..386,389)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 msaspptvah atgsagavsh rrivfasfig taiefydfyv yataaalvig pvffphgsat
       61 aqalsafvtf giafiarpig sflfghfgdr igrkstlvas llvmgvstta igfvpgydai
      121 galapvllcv lrfgqgiglg gewggaalla tehapqgkrg wfgmfpqlgp svgflmsngl
      181 ffalalslsd eqfrswgwri pflvsavlva lglyvrlkit etpafqaald rnervrvpva
      241 tlvtqhwqpt llgalamvvc ytlfyistvf slsygvsalh iprqsflgll cfavvfmgla
      301 tplsawasdr fgrkpvlivg aiaallsgfa mepllgsgsm plvalfltie lflmgvtfap
      361 mgallpelfp tnvrytgagv aynlggilga siapyiaqll aargglswvg gyvsvaaais
      421 ligvllmret rdaslv
//
LOCUS       WP_176049322             436 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: replication-associated recombination protein A
            [unclassified Burkholderia].
ACCESSION   WP_176049322
VERSION     WP_176049322.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..436
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=47982
     Region          1..434
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 msdlfqvepr rplaealrpk tlaevigqth llgegkplrl afesgkphsm ilwgppgvgk
       61 ttlarltala fdcefialsa vlggvkdire smeqakdtln rtgrhtilfv deihrfnkgq
      121 qdallpfves glvtfigatt enpsfevnsa llsraqvyvl kslnddemrq lltraqeial
      181 dglafddkai dtlvgyadgd arrflnlleq aqtaatsagv atidadfvsn amtlnarrfd
      241 kggdnfydqi salhksvrgs spdgalywfc rmidggadpk ylarrivrma wedigladpr
      301 alqmandaae tyerlgspeg elalgqaviy lacaaksnag ynafnqamaf vkqdksrevp
      361 vhlrnaptkl mkelgyghay ryahdepnay aagetylpdg mreprwyqpv prgleskiad
      421 klawlrdldr eagkkd
//
LOCUS       WP_176049348             116 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF190 domain-containing protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176049348
VERSION     WP_176049348.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..116
                     /product="DUF190 domain-containing protein"
                     /calculated_mol_wt=13200
     Region          4..103
                     /region_name="COG1993"
                     /note="PII-like signaling protein [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:441596"
ORIGIN      
        1 mdrvflrfyv heqhrlhwkp lwewlleeas rmgvaggsaf ramagfgqhr vlhedrffel
       61 qgslaievef ivtedeaqrl lerlshekvr vcyammpahf gvidtlgapp aqgpaa
//
LOCUS       WP_176049326             216 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: trimeric intracellular cation channel family protein
            [Burkholderia].
ACCESSION   WP_176049326
VERSION     WP_176049326.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..216
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23670
     Region          19..216
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mrrrpsggrv phprltlaia ileaiatlaf aisgfieark nrldsvgtfv valatafggg
       61 tlrdillerr pfywvvhddy viaifvlalf apfvlrmlsr lsaerlllia daiglgifsi
      121 sgtaialdae mprfiavmmg vitgvvggiv rdvlcndipl ilrdsrpyat cafvgcwfyl
      181 llvwlqfdsv ysvllatgfi lvarlatfkf dvrlph
//
LOCUS       WP_176049368             235 aa            linear   BCT 11-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Burkholderia sp. BCC1644].
ACCESSION   WP_176049368
VERSION     WP_176049368.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..235
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=26056
     Region          81..232
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 medidkraia kevkrfqyei wqragvthnt vphllqlfrp dhaahvhgye yevaegslgi
       61 hgigkdryqv aglvdpanni ikiagnltye vqrftaahel ghmvlhpgms lhrdrpltge
      121 wsppdkrere anhfaacfla peklvrqafe arfctstlhl ddttafylvg ccqmqdllrs
      181 stgslefara vatakafgpg nyfkplself gmsptamair ldelglveng raiaa
//
LOCUS       WP_176049364             114 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: cupin domain-containing protein [Burkholderia].
ACCESSION   WP_176049364
VERSION     WP_176049364.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..114
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12852
     Region          13..113
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 msdfitvlre tcptpvldat kwkriggdph tvnlnaylsk dgskimgtwi ctpgkfevny
       61 ekweychfld gyciitpege ksvhlkagdv fviepgmkgt wevvetvrky fvfa
//
LOCUS       WP_176049554             288 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176049554
VERSION     WP_176049554.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..288
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30828
     Region          29..283
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mpanplpddd ladsdtddaa sgengekvrs giqsievgfr lldvltsepr ammlrdlaqr
       61 agmspakahr ylvsfsrlgv vsqdpvsgry elggfalqmg larlarvdgv klarialtef
      121 rdrldqtvgi avwgnqgpti vhwmesshpa kaslklgdvm pllgsatgll faaylprskt
      181 aamlerelad trrsphhggp rtldevdavl advrkheaar vegmllptih afcmpvfdav
      241 gelalaival gqegsfdiaw ggeidtalra caqklsyelg yspdarda
//
LOCUS       WP_176049558             408 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176049558
VERSION     WP_176049558.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..408
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=43789
     Region          1..291
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mrlalvlmgg garaayqvgv lkalaeiare adpqrhtlpf avvcgssaga inatslasha
       61 ddfshgvrrl lefweplrad yvyrsdwlgi aaagarwlaa mtfgwaarrs prglldntpl
      121 ahllqrelsf hrieqmlear llhalsital syssgrhltf yqaaqpiqaw rraqrtarlv
      181 dlsashllas saipfvfpav plvldgqiey fgdgsirqia plspaihfga drivvvgaad
      241 prpeipaang tglvrgyptl aqigqqvlas vfldsigsdi eriehinrmi ehlphqvevd
      301 sgwrhvdvla iapserieli aakhlkqmpa tmrgllgaig gsqpagasfa syllfeeaft
      361 relielgyvd graqrdalas wiaqadggsa paagrppgdg laageirv
//
LOCUS       WP_176049611             205 aa            linear   BCT 11-JAN-2025
DEFINITION  SCO family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176049611
VERSION     WP_176049611.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..205
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22419
     Region          51..205
                     /region_name="Sco1"
                     /note="Cytochrome oxidase Cu insertion factor,
                     SCO1/SenC/PrrC family [Posttranslational modification,
                     protein turnover, chaperones]; COG1999"
                     /db_xref="CDD:441602"
ORIGIN      
        1 mlhsrfgrra rqgwmlacaf taalllagcd napkfqnldi tgntqfgsdf slpdtagkvr
       61 tlgdfkgrav vmffgythcp dvcpttmael sealkqlgpd aakrvqvlfv tvdperdtpa
      121 llgqyvpafd psfiglrpad eaalkkvtkd frvyyakvpg ktpgsytmdh taasyvfdrd
      181 gklrlfvrdg qgpapwvhdl kllvd
//
LOCUS       WP_176049665             249 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Burkholderia sp. BCC1644].
ACCESSION   WP_176049665
VERSION     WP_176049665.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26262
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkilvpvkrv vdanvkvgvk sdqsgvdian vkmsmnpfde iaveeavrlk eagvateviv
       61 vsvgvtqaqe tlrtalaiga drailvestd sveplavaki lkalvdkeqp qlvilgkqai
      121 dddsnqtgqm laalaglpqa tfaskvtvad gkatvarevd ggaetlslsl pavittdlrl
      181 nepryvtlpn imkakkkple tvkpedlgvd vaprlktlkv veppkraagv kvpdvktlve
      241 klkteakvl
//
LOCUS       WP_176049654             361 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: AI-2E family transporter [unclassified Burkholderia].
ACCESSION   WP_176049654
VERSION     WP_176049654.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..361
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=39704
     Region          86..352
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mekqpdssrd aqnrephlrs vrltsdfslp klsaleigsy lfailamwlv ielkllggll
       61 agllvyqlih tiapvierht tsmrarwvav vllsiaivga ltsltigiie hfertvpnlq
      121 slldqlmqiv eqtrartpaw ianllpvdve qmktkaavlm hshmdqlqqs gksvargfgh
      181 ilfgmiigam iaigvehgkv rrplstalvt rvsrfadafr rivfaqikis ainavftgiy
      241 llvalpifhq rlplsktlvl vtfivgllpv ignlisntli vavslsvsmg taiaslaflv
      301 iihkleyfln akiiggqies rawelllaml imeaafglpg viaapifyay lkrelyllrl
      361 i
//
LOCUS       WP_176049651             204 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysE family translocator [Burkholderia].
ACCESSION   WP_176049651
VERSION     WP_176049651.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..204
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21441
     Region          1..203
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mpnfmlflat siaitfapgp dnlqvlargi sqgraagfva algftagilf httlaalgva
       61 avlrsspvaf qilklagaay lvwigikalr sqglanahar ppqplgtifr qsvignlmnp
      121 kvtlffvvfl pqfvdphgaq gvtlqmfelg alfmlqtavv fslfgvgagm igawlkrrpk
      181 agvwldriag atfiaigirv alkd
//
LOCUS       WP_176049615             298 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC1644].
ACCESSION   WP_176049615
VERSION     WP_176049615.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790524
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..298
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31017
     Region          1..294
                     /region_name="COG4120"
                     /note="ABC-type uncharacterized transport system, permease
                     component [General function prediction only]"
                     /db_xref="CDD:443296"
ORIGIN      
        1 mslfsflgal eiglifslva lgvlisfril nfpdltvdgs fplggavaat lisagydpft
       61 stlfaivaga aagfitgwln vclkimdlla silmmialys vnlrimgrpn vpliteptlf
      121 tvlqpdwmpd yvlrpallai vvvvaklgld wffssqlgla mratganprm araqgiatgr
      181 atlagmalsn alvalagalf aqtqggadis mgigtivigl aaviigetll parrlvlttl
      241 avvlgaivyr ffialalnse figlkaqdln lvtaalvtia lvlpatrkkl farkngga
//
LOCUS       WP_176049667             498 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176049667
VERSION     WP_176049667.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 498)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..498
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=53584
     Region          5..498
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mtarihelld rwlseaparp fihlpdrsls yadvgalada lerelrddgv rsgdrvlvva
       61 encaehaall iacsrvgaws cgvnarmapg evdafagkad arvlyftsgv spaagahaar
      121 hdarpscvng larsavhtaa rvepeplasd vaaviftsgt tgapkgvmmt hrgvlhfarv
      181 saesralgpd drvyayapmt hifglgtvll aslhagaale mrpqfepael fdalahrrvs
      241 qvqgppmlfs rllrycaeqg ivrpeapclr ylyagagpld lalkqqveal faqtlhhgyg
      301 lseyagslha trlgetrgdt sagyafpgae lrivdpatgq alpagargei wlrgtglmpg
      361 yfrdpqatad vmreggwyas gdlgelhddg alfivgrlke miirsgfnvy pgeveqalnr
      421 fpgilnsavv gqkqadgnea vvafveldaa raldetalrr ylreqlapyk hparfipidk
      481 lpfnsngklm rrqlqerl
//
LOCUS       WP_176049682             320 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Burkholderia sp. BCC1644].
ACCESSION   WP_176049682
VERSION     WP_176049682.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..320
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=34420
     Region          10..223
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(51..52,54,68..70,76,78..79,120,222)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(51,53..54)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(76,79,82,89)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(112,116..119,121)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(117..118,141..143,195..196)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          237..320
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 midgltvrva akhdeaadic gfelvhadgl plppfsagsh idvvvpggpt rqyslcnasd
       61 ehhryriavl rdpksrggsa gmhdrvnagd tltisaprnh falahdaths lllaggigvt
      121 pilcmaerla ridasfdmhy ctrsrtrtaf ldhiahapya srvqlhfdde genqrfdiaa
      181 rlaapapgth lyvcgpkgfm davlttarat gwpeaqlhye ffaadarqtg rdgrfeveia
      241 ssgrvivvek nesvvralak agiaietsce qgvcgtcatr vlagepehfd lcltpderaa
      301 ndqflpccsr sksarlvldl
//
LOCUS       WP_176049687             160 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-binding protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176049687
VERSION     WP_176049687.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..160
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=17588
     Region          18..157
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mnigqaatgs sprevrarfr arldalrdia swvraeserd aapawvdqle laiveaasna
       61 mrhggatspa rvgqrdfgiv lvlrfrpdrv vvdlfdagra apnglferyh ltpvfdpghi
      121 ehlpesgmgl gilyacvdvv ayrrrlginr lrlvkhrarg
//
LOCUS       WP_176049688             112 aa            linear   BCT 11-JAN-2025
DEFINITION  STAS domain-containing protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176049688
VERSION     WP_176049688.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..112
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12218
     Region          4..101
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(20,22..24,30,53,55..57,59..61,64..65,86,90..91,93)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            56
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
ORIGIN      
        1 mltetttldd itlmqirvar fdsfvaprir ddlvglvqqg ahrivvdlqh vsfvdssglg
       61 amvsgykald rrgdivlcga sdavrtllrl trmdrvfhvv advdaacayl rt
//
LOCUS       WP_176049743             374 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC1644].
ACCESSION   WP_176049743
VERSION     WP_176049743.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 374)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13386660
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..374
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40445
     Region          13..>122
                     /region_name="YhgE"
                     /note="Uncharacterized membrane protein YhgE, phage
                     infection protein (PIP) family [Function unknown];
                     COG1511"
                     /db_xref="CDD:441120"
     Region          174..371
                     /region_name="YadH"
                     /note="ABC-type multidrug transport system, permease
                     component [Defense mechanisms]; COG0842"
                     /db_xref="CDD:440604"
ORIGIN      
        1 msrllvifrl gvkelwslar dpillalivy tfsasiyvaa tarpetlhkv piaivdedas
       61 plsariaaaf fppqfapppi vdaaaadrgl dngdytfsid ippdfqrdvl agrhatiqln
      121 vdatrmtqaf tgggyvqqiv sgeidafvqr yrgapsppvd lamrmrfnpn ldevwfgalm
      181 elinnvtmls miltgaalir erehgtiehl lvmpvtaaei mlakvwsmgl vvtvaavasl
      241 tlvvggalhv pipgsiplfv agmalhlfat tsmgiflatl vrsmpqfgml lvlvllplql
      301 lsggltpres mplavqdiml aaptthfvel sqrilyrgag ldavwlqfav lfaigcvlfl
      361 lslmrfrkti aqmt
//
LOCUS       WP_176049770             144 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176049770
VERSION     WP_176049770.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..144
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=15733
     Region          42..144
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mthltrydpf siepvsdlfq glfrplrgma mtdepdlasm kidvtesdda ykvnaelpgv
       61 akedidvqvt grtvtinakv ersneqkdge rvirrerysg aigrsfslsg eiddanatat
      121 yqdgvlsltl pkkapvgqkk ltis
//
LOCUS       WP_176049779             333 aa            linear   BCT 11-JAN-2025
DEFINITION  bestrophin family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176049779
VERSION     WP_176049779.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..333
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38330
     Region          1..321
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 mhlgksyrls efliwtrwki yellifgsvp vvlyqffsvt wlsipltiva llgtatsfiv
       61 gfknvqtynr amdaleiwtd ilsksrrwgq ltrdfvtdde iarklvyrhl awltalryel
      121 rrpriwestn krynaeyrrf yrvpewehdi rellpkylss setaqalssa siatfvlslq
      181 gtslrtlhma gqlnssfyme lqktigdfid lqarserfkn fpyprqyatv sslfvrffcl
      241 slpfgllnef nrlndsvsgf mhgnmvwlvv pcsvavswmy tsleqvgest enpfeggand
      301 vpistlcgti erdlkamlge pardpssrtv ial
//
LOCUS       WP_176049797             455 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin monoamine oxidase family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176049797
VERSION     WP_176049797.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..455
                     /product="flavin monoamine oxidase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49376
     Region          10..455
                     /region_name="YobN"
                     /note="Monoamine oxidase [Amino acid transport and
                     metabolism]; COG1231"
                     /db_xref="CDD:440844"
ORIGIN      
        1 matidqsanh esdvliigag lsgmkaalel rdagkrvlil eardrvggrs mpgevggqtv
       61 dfggqwvgas qkllreqata lgvpmyrqyt ngnslvnidg kvhaytstpk lpflstlelg
      121 ltlhrwkrdm qtlpvgapwl aenalqwdam sievwidkhv dttaardfar lvtsaitcte
      181 tlhvsylffl eclrqgggle tmmgvdggaq qdkflggawq ipkrmadrln gcivldapvs
      241 tieqdengvr aicpqrtyea ryaivtappa lasrirftpp lpakragllq rmqmgavikm
      301 hvayptpfwr rrglngsvas vgrhlgfvfd qspadesvgv lvgliegnha lelsglgkaa
      361 rrehviadlv hyfgddaaap ldyadhdwtt dewalggyas hmppgvltsy gdsirepfgr
      421 ihwagtetat ecigyfegal esgiraadev ikalr
//
LOCUS       WP_176049692             232 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar transferase [Burkholderia sp. BCC1644].
ACCESSION   WP_176049692
VERSION     WP_176049692.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..232
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26242
     Region          <56..231
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mpldtrlavv sprraahslr larlawrwha cryasvkrll diavasasll llsplfgvva
       61 lcirledrgp vlfwqrrvgr hgrefafpkf rsmivdaerr rteiahlnqh gaagvtfkra
      121 ddpritrvgr firrmsidel pqlwcvlkgd mtlvgprppl pqevarytlp drgrllvtpg
      181 ltciwqvsgr aniafpqqvt mdleyirers laldlkllck tvpavlrghg ay
//
LOCUS       WP_176049806             343 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176049806
VERSION     WP_176049806.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..343
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36656
     Region          24..326
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 msfsflparr alaatltaal alagavvpqt ahaegriria eqfgvvylml nvardqqlie
       61 kegrkagldi kvdwvrlsgg aavndallsg avdvagagvg plltvwdrtr grqnvkgvas
      121 lgnfpyylvs snpsvktiad lsakdriavp avgvsvqsrv lqyaaakqwg dkqfdkldal
      181 tqaiphpdat aailanssvi tghfgnppfq eqelagnpna hivlnsydvl ggpssatvly
      241 atekfrndnp ktyrafvtal adaarqiaad peraadtyir vnaskidral llkilrnpqv
      301 qfktapqntl plaqfmhrtg airnepkswr dyffddpata ggs
//
LOCUS       WP_176049829             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176049829
VERSION     WP_176049829.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32117
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrlsamety vsvveagsfs aaakrmnlgq paisksiaql eerlgvrlll rstrgltttd
       61 agqrfyehak vaireadrae hvvrdasasl sgklrvsaav sftclhvlpk ldtflsrhpd
      121 leidlalddr nidlleegtd valrmgtlid ssmiarriar sprlvvgtpa yferagipqs
      181 padlaghqai vyaqrgggea wsfsrngaev avavsgrlrv saaegmrtav iggmglavas
      241 rwmfspelat gavqavltdw tlppvdlwav fpagrlvtar arafvefveq alaegepapa
      301 p
//
LOCUS       WP_176049830             333 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176049830
VERSION     WP_176049830.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746445
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..333
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35576
     Region          6..313
                     /region_name="chlor_reg_RclR"
                     /note="reactive chlorine-specific transcriptional
                     regulator RclR; NF040475"
                     /db_xref="CDD:439702"
     Region          6..119
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
ORIGIN      
        1 mtlesdwlsr fmalvtvtgk leircafgap waiayerspa ceipyhvvlr grailenpdd
       61 gavrelgsgd ivlfphgsph vlhdgsglpp vpafkrpggh vligenagtg erldmlcgrf
      121 vvapphdrli rrhlppdlvv raavdsrmpd alavtarlta lvelmraesl eqqlgglail
      181 nalsaalfal alraisetgq aptgllalag hprlapaiva mlddparpwt lpelaglcsm
      241 sratfmrhfq sklghsaadl ltdirmslaa nalrqpsasa eavssdvgyq svaafrrvft
      301 rwagmtpgdw rrqsmgerrd aatpidgdat dae
//
LOCUS       WP_176049854             311 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176049854
VERSION     WP_176049854.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..311
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33734
     Region          3..311
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mphrvavlvy pdfqlldaag piaafeiagr yrqghytlrt iaaqaglvrs ssgvswaaea
       61 lppastidtl lvaggdnmdd rmsdprllrf vqrcarrgtr vtsvcsgsll laaagvldnr
      121 ratthwscse qfacrfpqvh lepdrifved gpfwtsagis agidlalalv gndlgeqvar
      181 lvarqlvvyy rrpggqsqfs almemncasg rfkplldhvr rnlaarhrvg dlaeracmsp
      241 rhfarafqae tgltpakave klrveaaraa lesgavslqr valecgfgdt enlrrsfqrl
      301 lgvppsalra r
//
LOCUS       WP_176049898             140 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176049898
VERSION     WP_176049898.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..140
                     /product="RidA family protein"
                     /calculated_mol_wt=15337
     Region          1..129
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 maealnppev wapfgafsma viqgdgrivy lkgqvaldrd gqvvgqgdmr aqvrqtldni
       61 ravlaamggq mqdvislvhy atdidafmqa gdirkqyfve pypvtttvqv erlyhpdlli
      121 eitaiaeipq arfhrpaspt
//
LOCUS       WP_176049903             302 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sterol desaturase family protein [Burkholderia].
ACCESSION   WP_176049903
VERSION     WP_176049903.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..302
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34586
     Region          87..243
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mltttgklay fvtlfivavs lveaavltwr rsrqpepfdw nevwlsladl agrkllalvp
       61 lslatplfdf awahrlftip lhsvalallv fvgqefcyyw yhrashrvrf fwsthavhhs
      121 pnqltlssaf rlgwtgkiag aamfftplvw lgvrpeavla ilsfnlmyqf wlhntwmpkl
      181 gwleyvfntp sahrvhhasn ldyldanygg vlivfdrlfg tyvaeradep cryglvtptr
      241 srnpfvvele hwaslardva tardvwtair fvmlppgwrp gnqgetteel rrrrlvavrt
      301 da
//
LOCUS       WP_176049924             337 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC1644].
ACCESSION   WP_176049924
VERSION     WP_176049924.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..337
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34314
     Region          23..337
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mnlpdssstp sttlataagn gdapppramw aqlrrstlfy plvglivvci ammiaspsfl
       61 saanlenvlr qvsinaiiav gmtcviltgg idlsvgsvma lsgtlaaglm vagvnavaal
      121 aigiavglgf gflngvfvaf agmppiivtl atmgiargla liytggypid glpdwvaffg
      181 sgkvlgiqap vlimlvvyai awllldrmpf gryvyaiggn eqatrltgvr varvklivyt
      241 lagltsalaa ivltgrlmsg qpnagvgfel daiaavvmgg tsisggrgai lgtlvgalll
      301 gvlnnglnmi gvnpyvqnvi kggiillaiy isrersr
//
LOCUS       WP_176049944             307 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176049944
VERSION     WP_176049944.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..307
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33537
     Region          34..186
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <199..293
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mdmtdivasr esgrrelasl igrfapadgs hstavpglml hrhtrpvdlg cgvsraalvi
       61 aaqgakrviv agqayeydth nclitsidlp ilsrvtrasa dapylclslt ldpqrivela
      121 aemrlpepda gpegegiala eltpplldaa lrllrlldtp adipvvapli ekellyrlmt
      181 tgegtrlrhm aiagsqthri araiewirdh faepmrvesl aqavnmsvss lhhhfkhvtt
      241 lsplqyqkql rlhearrlll rqggdvgsva avvgyesasq fsreysrlfg appmrdvvhl
      301 rkkellg
//
LOCUS       WP_176049970             209 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176049970
VERSION     WP_176049970.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..209
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22405
     Region          18..172
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 msesssripl sprkaprqrr svatvdaive aaarilerdg fdgyttnava alagvsigsl
       61 yqyfpnrdal taalveresa rllddvdraa alsscdevlr mlvrgavahq mrrpvlarli
      121 dfeearlplg araarvadri hatllhalgl rdaprvaapd vvahdllaiv kgvvdaagar
      181 getdaaplea rawravrgyl resreskla
//
LOCUS       WP_176050022             286 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MurR/RpiR family transcriptional regulator
            [Burkholderia].
ACCESSION   WP_176050022
VERSION     WP_176050022.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..286
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30560
     Region          4..283
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 maanfdelas riraqfsels pqfqagaafl ldhpdevats smrkvaqraq vqpaslvrla
       61 qqfgfpgwne lrdlcvarvr trpepltqra rslvrpdaka slahdllaaq qhnlsataaq
      121 nehaladaar lirkashvhv agfrscypva fgfvygyrlf rptvsllngv agslemelrt
      181 iakqsvtvvv sfapysaeat rvaqaakaqg skivaitdsa vspialhada qlifthdsps
      241 ffpslvaaha maealvaqll alegsdaiaa lerteaelha kgayvv
//
LOCUS       WP_176050074             246 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176050074
VERSION     WP_176050074.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..246
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=25355
     Region          10..239
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; pfam01925"
                     /db_xref="CDD:460386"
ORIGIN      
        1 mqthtltiiv lvfllagavk gmiglglpti amglltlamp psaaaslllv psfitnvwql
       61 wlgpsfgpll rrlwpllagl tigtlagglp alaagstwth aalgvvlily glwglaaarl
      121 papgrhekwl savvgyltgv vtaatgvfvv pavpylqalr lskddliqal glsftastia
      181 lglqlhvsga lqtvdlgvsa lalvpalagm aggqyarrvm sekafrrcff vglialgaym
      241 aaaewl
//
LOCUS       WP_176050087             504 aa            linear   BCT 11-JAN-2025
DEFINITION  MDR family MFS transporter [Burkholderia sp. BCC1644].
ACCESSION   WP_176050087
VERSION     WP_176050087.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..504
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53138
     Region          38..422
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(39..40,43,74,124..125,127..129,132,152,155..156,159,
                     284,287..288,291..293,296,324,328,381..382,386,390,406,
                     409..410,413..414,417)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mttdtlltpp aaeaarrdap tglivaalll vmllsaldqt ivstalptiv gelggldqls
       61 wvvtayllss tvvlplygkl gdlygrkivl qaaivlflag salcgiaqdm tqlivlralq
      121 glgggglmvv tmaaigdlvp pdrraryqgm fggvyglati igpllggflv ehlswrwift
      181 inlplgflal avigvafrph tahvkhridy mgaaflatal tcvilftseg gsllpwtspq
      241 lwmtlvlglv aiggfiyeer laaepimple lfrhrtfvlv sligfvvgia lfgsvtfipl
      301 ylqvvkgstp sqagmqllpm mggmlvtsiv sgrlisrlgs yrmfpilgtl tggiamalls
      361 tltldtplht myaymallgi glgmvmpvlt lavqntvefr hmgvatsgat lfrsiggslg
      421 vaafgalfsh glqsrvmeal pagtelppal gpaavhqlpd avrdtylhaf agslhvvyla
      481 aatviaiafv lawfvedapl rkhn
//
LOCUS       WP_176050123             414 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia sp. BCC1644].
ACCESSION   WP_176050123
VERSION     WP_176050123.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..414
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43986
     Region          14..414
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 msdentqaqp apgtvvvigg gqaagwvlkt lraegyagrl vmiadephlp yerpplskav
       61 lagdvdietv rvvrpdefda lnveawqper aasidrarrv vktesgreie ydrlviatgg
      121 tsrrlpdaiv ktpnlhylrt ldeaaalgek lrasqrvlvi gggwigleva atarklgvda
      181 vvvegaprlc grsvpqivsd flldlhrsng vdvrtgaala sldaqpddts kvratladgt
      241 tidadfavag iglalnasla sdaglavddg ivvdefgats dpaifacgdv anhhngwlkr
      301 rvrleswana qnqaiaaaka vlgvrapyae ipwfwsdqyd vnlqilgdlp adaqlvvrge
      361 laarratlff vgdghvrgvi avnnarelkl arkwmnqgra vdtealadtt kala
//
LOCUS       WP_176050206             430 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia sp. BCC1644].
ACCESSION   WP_176050206
VERSION     WP_176050206.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..430
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=47170
     Region          4..412
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mttptriviv gggiaglqla trlgerlgrs graqvtivdr spthiwkpml htiaagtrdv
       61 qqqqviflah ardhgytyqp gelkgldrar rrvqlgeirs qdgevviear eleydvlila
      121 lgsqandfgv pgvrehcyfi dsqqqaetfn ealrmrvfrs iardepfrva ivgagatgve
      181 laaelsrlle vaqaygdetv rerlqltlle sgprilnafp prisasaqrr leqigfhvlt
      241 strvtsadan gfhygdgsfa eadlmvwaag vkapdfmqal ggldtnranq vvvgptlqat
      301 gdehvfaigd casllpdghe rplpptaqva tqqaehlakh lpawldgtpi ppfafhdfga
      361 lvsisdydaf gtlgqfgffr ggfiqgrfaq fshlmlyrrh qqalhgfska tllwiaerin
      421 gwvqprirls
//
LOCUS       WP_176050189             203 aa            linear   BCT 11-JAN-2025
DEFINITION  cysteine hydrolase family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176050189
VERSION     WP_176050189.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..203
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21105
     Region          24..192
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mqhptirtla gataptsida arsallvidf qneyfsgrlp ipegpralgn aqrviafadr
       61 agipvfhvqh vdtadspifa dgsdgfrfha dlqpaphhav vkktsvsvfp ttdldarlkg
      121 agvdtlivtg lmthacvaga ardavplgya vivvddacat rdldvadggt vphrdlhrat
      181 laalsdtfgd vltteqvlal gia
//
LOCUS       WP_176050210             292 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176050210
VERSION     WP_176050210.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..292
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32058
     Region          1..276
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mgtsiralll sqmdsftpse qkvaqalldr ypslglgpia qfakqaevsd ptvfrfvvri
       61 gfpnyssfqq alhdeidtam nsplarmdaf hsetglrdsh saifqrlses lattieglda
      121 aafdaavall adpdvrvfcg ggrytaplas lfsftlayar phvqavepnv nlasvaladm
      181 grgdvlvifd frryqkdsir faqaahrlgt rillitdewr spigefaeiv lriqgrpfam
      241 lqtnvpalal aealvigvtn rlpelarqrm ekierlntag ieqdtnrrnl pe
//
LOCUS       WP_176050219             215 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176050219
VERSION     WP_176050219.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..215
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23076
     Region          7..203
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mtsthsltfy tadtpnghki aiyleeagia hdlvhvnlsa geqrspafla inpngkipai
       61 vdhdtgltvf esgailgyla aktgclhpet laertavqqw lhfqiggigp mlgqlwwflh
      121 asktvnaeai dryrkeatrl ygvvngrlse saylassrys iadiaafpwl rtaaeldldv
      181 agfphvarwl adiaarpavq rgliacrapa aaaah
//
LOCUS       WP_176050256             323 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176050256
VERSION     WP_176050256.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..323
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35003
     Region          6..321
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpaaprsilv lafpraqlld vsgplqvfas vnelalergq papyaprvva veagpvetss
       61 glvvmaeslr saardpdtli vaggkgvqaa skdarlvrwv qqqagrarrv asvctgafll
      121 aeaglldgrr avthwarcde faarypnvrv esdpifireg alwtsagvta gidlalalve
      181 edlgratald varelvvflk rpggqaqfsa mlsmqrtddr fgelhawmae hltadlsvpa
      241 laervrmser sfvrhyragt grtparaveq irveaaqrll getawpvkri aarcgfgsee
      301 tlrrsfvrvl gvspqgyrer fvr
//
LOCUS       WP_176050231             304 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: sterol desaturase family protein [unclassified
            Burkholderia].
ACCESSION   WP_176050231
VERSION     WP_176050231.1
KEYWORDS    RefSeq.
SOURCE      unclassified Burkholderia
  ORGANISM  unclassified Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="unclassified Burkholderia"
                     /db_xref="taxon:2613784"
     Protein         1..304
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35093
     Region          85..242
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mrfdvellll alapvfllci aweawhlart raqdhvyawr dtlcnaalal mhqgadkiaw
       61 lfvipvyayc yqhyrlftwh dswlsfavlf vaqdflyyvf hrashrvrwl waahvvhhss
      121 ermnfstafr qslmypvagm wvfwlplafa gfppqqvvgi vlinlafqff vhtqaigklg
      181 wleyvlntps ihrahharna ryidrnyagv lviwdrlfgs yvdetpddpp qygiverlgs
      241 nnplvatfhe wvsmvsdalr vdgwrnklra ifgppewasa yhaqiaeaan qdprtvplaa
      301 ardq
//
LOCUS       WP_176050278             238 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MIP/aquaporin family protein [Burkholderia].
ACCESSION   WP_176050278
VERSION     WP_176050278.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Tajkhorshid,E., Nollert,P., Jensen,M.O., Miercke,L.J.,
            O'Connell,J., Stroud,R.M. and Schulten,K.
  TITLE     Control of the selectivity of the aquaporin water channel family by
            global orientational tuning
  JOURNAL   Science 296 (5567), 525-530 (2002)
   PUBMED   11964478
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Duchesne,L., Deschamps,S., Pellerin,I., Lagree,V., Froger,A.,
            Thomas,D., Bron,P., Delamarche,C. and Hubert,J.F.
  TITLE     Oligomerization of water and solute channels of the major intrinsic
            protein (MIP) family
  JOURNAL   Kidney Int 60 (2), 422-426 (2001)
   PUBMED   11473620
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Park,J.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the MIP family of transmembrane
            channel proteins
  JOURNAL   J Membr Biol 153 (3), 171-180 (1996)
   PUBMED   8849412
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001739
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..238
                     /product="MIP/aquaporin family protein"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24582
     Region          1..218
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
ORIGIN      
        1 mspyiaefig tailvllgng avanvllakt kgkgadlivi vmgwamavfv avyvtasfsg
       61 ahlnpivtis lalagkfaws kvggyilaqm lggmagallv wlayrqhfak eadadlklav
      121 fctapairsv thnvlteaic tfvlilgvly laspqvglga ldalpvgllv lgigislggp
      181 tgyamspard lsprimhall pipgkrdsdw ryawvpvvgp llggaaaagl ylhlhsti
//
LOCUS       WP_176050309             131 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA thioesterase [Burkholderia sp. BCC1644].
ACCESSION   WP_176050309
VERSION     WP_176050309.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..131
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14112
     Region          7..131
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mtdstlelpq mqpalrvvpq phdanvhgdv fggwimsqvd iagsipasqr angrvatvav
       61 nsfvfkqpvf vgdllsfyat itrtgntsit vdvevyaqrm rlmgeivkvt eatltyvatg
      121 adrkprqlpp l
//
LOCUS       WP_176050329             531 aa            linear   BCT 11-JAN-2025
DEFINITION  MDR family MFS transporter [Burkholderia sp. BCC1644].
ACCESSION   WP_176050329
VERSION     WP_176050329.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024942
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..531
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56667
     Region          33..425
                     /region_name="MFS_Azr1_MDR_like"
                     /note="Saccharomyces cerevisiae Azole resistance protein 1
                     (Azr1p), and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17502"
                     /db_xref="CDD:341045"
     Site            order(34..35,38..39,42,73,123..124,126..128,131,152,
                     155..156,159,285,288..289,292..294,297,325,329,382..383,
                     387,391,407,410..411,414..415,418)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341045"
ORIGIN      
        1 mavhtaahhs sgqvlpfres llamigisfv tmlvaldqtv vgtalptiva elrgfdlyaw
       61 vatsyllssv itvpifgrlg dyygrkpfvi vsivvftaas vlcgmandml ylvlarglqg
      121 igggmlvgta facipdlfpd svvrlrwqvl mssafgiana vgpslggvlt qsfgwrsvfy
      181 vnlpvgllsl ffvwrylphl rhvahdrkmr ldwpgallia lslgalqlfv ewlpkygvas
      241 waslllvvav aagvglwhwe krcaqpilpf dmfgnralsa lfvlailagf smfsllfyap
      301 llfqggfgms pkeaglvitp lvvfitigsi mngrvvtrir npnamlhvgf vlfaiacagi
      361 vvsthttptw mlmalmvagg iglgfvlpnl tvfaqqaagr ehlgiatall qslrmvggml
      421 gtaltgtlvn qmysggvrna ltadhamqwh aqladpqili draaqgglva eltraghnga
      481 llleaaresl vgaihlgvam aavvavvsvw qcrrvppial rrkiephvaa d
//
LOCUS       WP_176050330             320 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia sp. BCC1644].
ACCESSION   WP_176050330
VERSION     WP_176050330.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..320
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34768
     Region          81..282
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mswqskfacw llrwqfrpet trevldpara rrftdlrmvv prrapsgyrl rqcygagdap
       61 lrgewlertd asagrgpgrt llyfhgggyy fcstrthrpl vfgltkragv rsfsldyrla
      121 penrfpaald dalaayrqll algtppesiv lggdsagggl alatlvalrd rgeplpagai
      181 lfspwtdlaa tgatlrtndg adpmfagaal pkaaklylgd apathpyasp lyadftglpp
      241 lyiqvgstev llddsrrvae kakaagvave ievwpdmphv wqlytpmvpe ardaldraaa
      301 flrrvavera vqrvgeasia
//
LOCUS       WP_176050396             243 aa            linear   BCT 11-JAN-2025
DEFINITION  alanyl-tRNA editing protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176050396
VERSION     WP_176050396.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V.
  TITLE     Evolution of aminoacyl-tRNA synthetases--analysis of unique domain
            architectures and phylogenetic trees reveals a complex history of
            horizontal gene transfer events
  JOURNAL   Genome Res 9 (8), 689-710 (1999)
   PUBMED   10447505
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Cusack,S., Hartlein,M. and Leberman,R.
  TITLE     Sequence, structural and evolutionary relationships between class 2
            aminoacyl-tRNA synthetases
  JOURNAL   Nucleic Acids Res 19 (13), 3489-3498 (1991)
   PUBMED   1852601
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Schimmel,P.
  TITLE     Classes of aminoacyl-tRNA synthetases and the establishment of the
            genetic code
  JOURNAL   Trends Biochem Sci 16 (1), 1-3 (1991)
   PUBMED   2053131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..243
                     /product="alanyl-tRNA editing protein"
                     /GO_function="GO:0002161 - aminoacyl-tRNA editing activity
                     [Evidence IEA]"
                     /GO_function="GO:0002196 - Ser-tRNA(Ala) hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004813 - alanine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006419 - alanyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=26350
     Region          3..243
                     /region_name="AlaX"
                     /note="Ser-tRNA(Ala) deacylase AlaX (editing enzyme)
                     [Translation, ribosomal structure and biogenesis];
                     COG2872"
                     /db_xref="CDD:442119"
ORIGIN      
        1 mttqalfred ayltqcdaiv qavgddgirl drtvfyplgg gqagdsgtlt lpdgsaitia
       61 dtrkakfdga tpddavhvpa pgqeasvaal apgtrvvari dwlrryrhmr lhtaahlmcs
      121 vlpygvdgcs vtadyvrldf atsdsidrdd verrlaglva gahpvttewi tddemaerpe
      181 lvrtmsvkpp mglgrvrllr ienvdlqpcg gthvrntsei gelrvaklek ksartrrlvl
      241 efa
//
LOCUS       WP_176050382             213 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: carbonic anhydrase [Burkholderia].
ACCESSION   WP_176050382
VERSION     WP_176050382.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Lindskog,S.
  TITLE     Structure and mechanism of carbonic anhydrase
  JOURNAL   Pharmacol Ther 74 (1), 1-20 (1997)
   PUBMED   9336012
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10096752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..213
                     /product="carbonic anhydrase"
                     /EC_number="4.2.1.1"
                     /GO_function="GO:0004089 - carbonate dehydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23041
     Region          11..190
                     /region_name="beta_CA_cladeA"
                     /note="Carbonic anhydrases (CA) are zinc-containing
                     enzymes that catalyze the reversible hydration of carbon
                     dioxide in a two-step mechanism in which the nucleophilic
                     attack of a zinc-bound hydroxide ion on carbon dioxide is
                     followed by the regeneration of an...; cd00883"
                     /db_xref="CDD:238448"
     Site            order(33,35,42,44..46,58,61,83,88,98,101,180)
                     /site_type="active"
                     /note="active site clefts [active]"
                     /db_xref="CDD:238448"
     Site            order(42,44,98,101)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238448"
     Site            order(43..46,48,50..51,53,58..60,62,64,78..79,82..83,121,
                     180,182..183,185,187)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238448"
ORIGIN      
        1 mnrpksmlva niawaretre htpgffdala rgqnprvlwi gcadsrvpae tithcapgel
       61 fvhrnianlf hpdddnsasv leyavrvlkv dhvivcghyg cggvrasllp ppadlphvar
      121 riaplcalar rhrdtldgld dtaaadrlae lnvleqvrll raspivrgre rpplvhgwif
      181 sladgrllel dsgyatppvd vepalattaa alg
//
LOCUS       WP_176050436             119 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: c-type cytochrome [Burkholderia].
ACCESSION   WP_176050436
VERSION     WP_176050436.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 119)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 119)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..119
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12774
     Region          19..111
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mnnafktaav alvaglaigt ahaaditkgk elveshncaa chgaqmnkpi naeyprlagq
       61 hadylvwamr qyqmgltnpl lgrnnaimqa qvqslsvsdm kdiasyiesl ketdlvfkk
//
LOCUS       WP_176050496             221 aa            linear   BCT 11-JAN-2025
DEFINITION  histidine phosphatase family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176050496
VERSION     WP_176050496.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..221
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24274
     Region          6..204
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 mattqilfir hgetawnrik riqghidipl adsglaqakr laarlerear dgaridavys
       61 sdlmraqqta qpfadalgls lqlreglrer sygafqghds teietlfpda yaawqtrdpg
      121 fapeggesqr elyhrvlhal epivaahpgg riacvahggv ldcvyrfang ielsaprnyp
      181 llntsinvvd yvdgraqvvq wadvshleaa sddddgyrkv l
//
LOCUS       WP_176050517             186 aa            linear   BCT 11-JAN-2025
DEFINITION  YceI family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176050517
VERSION     WP_176050517.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..186
                     /product="YceI family protein"
                     /calculated_mol_wt=19380
     Region          7..186
                     /region_name="YceI"
                     /note="Polyisoprenoid-binding periplasmic protein YceI
                     [General function prediction only]; COG2353"
                     /db_xref="CDD:441920"
ORIGIN      
        1 mkvsvsrsml aalaavsfva sgaahadvdl akskvsavsk qmnvptegaf kkfsaqvkfd
       61 pakaaqgtaq mtidiasfdl gdkmyndqva gkdwfdakay pqatfvssai apaggnkynv
      121 tgkltikgks etvtvpvtva qsgatqtfdg vlpikrsafn vgtgewkdts ivadevqikf
      181 hlvatk
//
LOCUS       WP_176050518             193 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: YceI family protein [Burkholderia].
ACCESSION   WP_176050518
VERSION     WP_176050518.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..193
                     /product="YceI family protein"
                     /calculated_mol_wt=20829
     Region          18..192
                     /region_name="YceI"
                     /note="Polyisoprenoid-binding periplasmic protein YceI
                     [General function prediction only]; COG2353"
                     /db_xref="CDD:441920"
ORIGIN      
        1 mkkqliiaag alaaslsfsa faesvtyqfd pshtypsfea dhmgglsvwr gkfdkssgtv
       61 tldraaktgt vdvttdiasi htgsakldeh lqtaeffdva kfpqanykga ikfdgdkpvs
      121 vvgnltlhgv tkpvtlkidg fkcmphpmlk revcgvdavg efdrsdfgld ygkqygfkmk
      181 tkllitaeal kqq
//
LOCUS       WP_176050533             469 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia sp. BCC1644].
ACCESSION   WP_176050533
VERSION     WP_176050533.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..469
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50225
     Region          14..467
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mnhpappait rrplppamld alraafgerv sttdavrahh grdespfdpq lpdavvfahs
       61 addvrevvsl cslysvplip ygagsslegh llavrggvsl dlsemnrvls inaedltvtv
      121 epgitrkaln ealrdtglff pidpgadasi ggmtatrasg tnavrygtmr envlgltavl
      181 adgrvvktgs rarkssagyd ltrlfvgseg tlgviteitl rlhplpeavs aaictfptmg
      241 davravieti qigvpiarve fvdalavrsi nrhsnltlte aptlffefhg teagvkeqae
      301 lvqalagqnn gqgfewatrp edrtrlwaar hnayfamlql kpgcravttd vcvpisqlaa
      361 cveetevdlr asslpcpivg hvgdgnfhva ilidpdkpee iaeaehindr iveralrlgg
      421 tctgehgvgl hkmrflpkeh gdnaidtmra iklaldprnl mnpgkiftc
//
LOCUS       WP_176050604             232 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176050604
VERSION     WP_176050604.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..232
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24888
     Region          10..232
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mfqirraedr chthqgwles shsfssagra anayppvgal hvlsedriap trgfgmqqrr
       61 dveivtyvld gtlahrdslg cgaivraggv qrmsagtglv hsetnpsrdr plhllqiwlq
      121 paergerpgy eerhfaddek rgrlrlvaap dggdgalsmr adarifagli dgdeaatfdl
      181 ragrstyvhv vrgdvevngr alaagdgari ggvdavafar graaevllfd va
//
LOCUS       WP_176050647             270 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176050647
VERSION     WP_176050647.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 270)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..270
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28985
     Region          15..264
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtdaarhags dlryaavdvt lkagartlld gftqafrpge iwcvagpnga gkttllatla
       61 glqppaggqv eidgrplaaw rpellaqrra lmpqqlhdaf satvfdtvll nrfpylggwg
      121 werdgdraaa hdalatfdlt alasrdvlsl sggerqrval aatlcqdapl mlldeplahl
      181 dlhhqidcls altawldagp rtvlfschdl nlarrfatha llldgcgraw agpvydvltp
      241 erasdafgyp lvlirengrd allpawparq
//
LOCUS       WP_176050686             460 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176050686
VERSION     WP_176050686.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..460
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=48945
     Region          161..428
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 menlqsrlls hrlasvirdf hqpvmiwqaa ilvgalcfaw vtarfvhgri darrraagra
       61 pgagaqslkr alfplfgsvf vgaaqlafdp fmstsllsla lvplfgigli yvlfffarrv
      121 fardghthaw lsivekivst avwaamvltv lgiqrdvlgw ldsvqfrvan ahltllsvis
      181 galwvcvtlm vamwlgsvle drltrastld anlkvvlsrv grallvfaai liglslvgid
      241 vtvlgvfgga vgvglgfglq kiasnyvsgf iilldrslrl gdaisvgglq gvvtqirtry
      301 tvvrgldgne tlipnerlit dvvqnqssyl trgyakvavq vaytsdveha lalladaakg
      361 vprvlaepap tpylvsfgad gidlelgfwi edsakgtsgv rstvnrniwr lfsehgisip
      421 fpqrevrvvg lpdgfsaaga tagldpaaan gavdgrapaa
//
LOCUS       WP_176050693             459 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid permease [Burkholderia sp. BCC1644].
ACCESSION   WP_176050693
VERSION     WP_176050693.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..459
                     /product="amino acid permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49075
     Region          7..457
                     /region_name="AnsP"
                     /note="L-asparagine transporter or related permease [Amino
                     acid transport and metabolism]; COG1113"
                     /db_xref="CDD:440730"
ORIGIN      
        1 mtqqqrsfdd ivareqglrh altsgqmami aiggaigtgl flgsgfaigl agpsvlvsya
       61 igalialllm galaemtvah ptagsfgaya ehyvgplagf lvryaywfav vfaigteisa
      121 iavfmkywfp avpgwywvig fsalliavnl asvtlygtve yafsllkiaa ivvfivlgay
      181 lvwsapaasg igfanytahg gfmpkgpwgt wvavivaifs ymsieavaia ageardpqha
      241 vtrafrstvf rlvlfylltl slmlaivpwt aagtdespfv kvmaathvpy aagvinfvll
      301 iaalsamnsq lyvttrmmfs lsrarlapav fgrlgtngvp raalwistsg vavaavlval
      361 apdtaftvmm aiamfgalft wlmifvthlr frsqyrgpal afrmwghpfg sllgaalvaa
      421 ilfttaftre frmtmvvgvv fvvlltlaya lhyrhehar
//
LOCUS       WP_176050695             538 aa            linear   BCT 11-JAN-2025
DEFINITION  multicopper oxidase family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176050695
VERSION     WP_176050695.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..538
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=58096
     Region          91..538
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mirrtflsra igvaaaslfa rtawaqhagh agmagmdsmd dmpgmsgmsg msgmsghaqh
       61 gkpataalaa adalpagapl aalrtlanes rdpgtfratl vaqpvarpml rgarpttfwq
      121 fgagaqgpvv gplidvregd tveikfvnkl pqpstihwhg lpvppdqdgn psdpvapgas
      181 rvyrftlpkg sagtywyhph phmmtaeqvf rglagpfvvr aaddplagwp ernlfvsdlk
      241 lardgtiapn dmmdwmngre gqfvlvngar rpridvagde rwrvwnacsa rylrvafddg
      301 rafehagtdg glfdaprrvt slliapgera ellvragdra srvvlqaaey drrkmamshd
      361 dghgslppdp alaladvafa paaaralpat lravpplgep vahktvafge emdmdammkg
      421 aaqgrpagmr fmingetyaa hratltsrrg dverweirnt tdmdhpfhlh gtqfqviera
      481 sggsrttepf rawrdtvnvr sgetvsilvt qdmpgermfh chilehedlg mmgtlkvv
//
LOCUS       WP_176050746             319 aa            linear   BCT 11-JAN-2025
DEFINITION  complex I NDUFA9 subunit family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176050746
VERSION     WP_176050746.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Parey,K., Wirth,C., Vonck,J. and Zickermann,V.
  TITLE     Respiratory complex I - structure, mechanism and evolution
  JOURNAL   Curr Opin Struct Biol 63, 1-9 (2020)
   PUBMED   32058886
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Babot,M., Birch,A., Labarbuta,P. and Galkin,A.
  TITLE     Characterisation of the active/de-active transition of
            mitochondrial complex I
  JOURNAL   Biochim Biophys Acta 1837 (7), 1083-1092 (2014)
   PUBMED   24569053
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..319
                     /product="complex I NDUFA9 subunit family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0010257 - NADH dehydrogenase complex
                     assembly [Evidence IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=33960
     Region          5..278
                     /region_name="NDUFA9_like_SDR_a"
                     /note="NADH dehydrogenase (ubiquinone) 1 alpha subcomplex,
                     subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs;
                     cd05271"
                     /db_xref="CDD:187579"
     Site            order(10,12..15,34..36,74..76,93,116..118,129,133,
                     156..159)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187579"
     Site            order(129,133)
                     /site_type="active"
                     /db_xref="CDD:187579"
ORIGIN      
        1 mdrqtvallg gtgfigsrlv nalidagkqv rigtrrrdha rhlqmlpvei velealdtrt
       61 larfvagaha ainlvgvlhg grgtpygpgf erahvalpaa lasactevgv rrllhmsalg
      121 adsrgasmyq rskgdgeaal haiaatdsla ltifrpsvvf gpgdaflntf anlqrtvpvl
      181 plampdarfq pvfvgdvvra fvntldlaaa hgktyelggp tvytleqlvr ycgtlvgrqa
      241 rivrlpdala rlqasvfecl pgepvltrdn latmsvpnvl sgplapelgi spaslesiap
      301 aylgeatkrs rfdwfrsrr
//
LOCUS       WP_176050759             369 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia sp. BCC1644].
ACCESSION   WP_176050759
VERSION     WP_176050759.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..369
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39082
     Region          1..365
                     /region_name="LhgO"
                     /note="L-2-hydroxyglutarate oxidase LhgO [Carbohydrate
                     transport and metabolism]; COG0579"
                     /db_xref="CDD:440344"
ORIGIN      
        1 meqmdcvvig agvvglaiar elaargreti vleaadaigt gtssrnsevi haglyyprgs
       61 lkamscvhgr dmlyefceth hvphrragkl lvatsaaqvk qlkaiaarav engvldllpl
      121 traeaqtlep alecvealfs pstgivdshq lmlallgdae rngamcalks pvesidvlrg
      181 grfvvrtggd apteieaacv insaglgaqa larrtrgldp rwvpplylar gnyfslsgra
      241 pfshliypmp draglgvhlt ldlggqarfg pdvewcdslr yevdparata fyasirafwp
      301 glpddalqpa yagirpklag pgeppadfiv qgaaqhgvrg lvnlfgiesp gltaslalaq
      361 rvgemtayr
//
LOCUS       WP_176050801             354 aa            linear   BCT 11-JAN-2025
DEFINITION  M48 family metallopeptidase [Burkholderia sp. BCC1644].
ACCESSION   WP_176050801
VERSION     WP_176050801.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Lew,R.A.
  TITLE     The zinc metallopeptidase family: new faces, new functions
  JOURNAL   Protein Pept Lett 11 (5), 407-414 (2004)
   PUBMED   15544561
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574487
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..354
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37462
     Region          136..319
                     /region_name="M48C_Oma1_like"
                     /note="Peptidase M48C, integral membrane endopeptidase;
                     cd07331"
                     /db_xref="CDD:320690"
     Site            order(202..203,206,259,263,303)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320690"
     Site            order(202,206,259,303)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320690"
ORIGIN      
        1 mrssrlrrva rvaaslgiga aalaatfaha sdtaataags apaatpatap apsastapva
       61 psaaeaaqpt gaavpakaya qtpqqqvryg naiafrtlip splleqltan eytqivqaaa
      121 dsnrllpanq prvkrlraiv aklapysvkw ndrvkswtwd vnairsrdir ltclpggkvl
      181 vyggmldrvr lnddelgvll ahgiahalre harsnfsats qtslraaalp plfgvgdplp
      241 qalnlgerlq slhyeptdet eadviggdia aragfdpraa itlwdklava trankatgfi
      301 ythpystarr qdllnrlpdl iplyakaigk rvdslpdyag isaqrrkvvr raag
//
LOCUS       WP_176050831             288 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176050831
VERSION     WP_176050831.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..288
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=32187
     Region          5..277
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mfdqivfagg gnrcwwqagf wdvarpaldl rprvitgisa gaatacmlyt rdaqwvmryy
       61 eealrhnrkn aywgnlfgre pvfphyriyr qalldiygep fakladapei rigvshvprw
      121 lgarsavaag lvayniekyv rktlhptlgr tlgfrpefvr aqactqvdel adlilqssct
      181 ppftpvlrrg grpvldggmv dnvpvdaldp spgdvlvlvt rlyprpqmft vahgdqrrly
      241 vqpsskvpis swdytspsqm rhaydlgrrd gehfltrvga mtggrvaa
//
LOCUS       WP_176050996             261 aa            linear   BCT 11-JAN-2025
DEFINITION  peptidylprolyl isomerase [Burkholderia sp. BCC1644].
ACCESSION   WP_176050996
VERSION     WP_176050996.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..261
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=27809
     Region          100..247
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mndvlsdapv alringvaid daaiaaeaah hgdapdplda arralavrel lrqravslal
       61 ldegapldda avdallerel thlpepgrad ceryytqhpa rfrrndivya shvlfamtdr
      121 vplaplrqra eaaladvvas pdtfeavara ssncpsaevg gslgqllrgd tvpefeaalf
      181 dtdglgvlpk lvntrfgfhi vrierrvpgd avpfdeaaaq iaaylservr erairqyvai
      241 laggarvegv afdgangplv q
//
LOCUS       WP_176050913             312 aa            linear   BCT 11-JAN-2025
DEFINITION  carbohydrate kinase family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176050913
VERSION     WP_176050913.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..312
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33774
     Region          4..290
                     /region_name="ribokinase_group_A"
                     /note="Ribokinase-like subgroup A. Found in bacteria and
                     archaea, this subgroup is part of the ribokinase/pfkB
                     superfamily. Its oligomerization state is unknown at this
                     time; cd01942"
                     /db_xref="CDD:238917"
     Site            order(52,250,253)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238917"
     Site            order(192,220,248,251..252,255,277,280)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238917"
ORIGIN      
        1 matlicgsia ydsimtfegr frehilpdqv hlinlsflvp tmrrefggca gniayalhll
       61 ggdarmmgtm galdaqpyld rldqlglrrd hvrvlpdtyt aqamittdld nnqiaafhpg
      121 ammqshlnha gdapdiklai vgpdgfdgmv qhveelakag vpfvfdpgqg lplfdgatlr
      181 rsielatyva vndyeaklvs dktgwsedei asrvdalvit rgehgatirh kqgteqipvv
      241 paeriadptg cgdafrggll ygiehgldwa ttgrlaslmg slkiahqgpq tyvltraeid
      301 arfetafgys lk
//
LOCUS       WP_176051014             306 aa            linear   BCT 11-JAN-2025
DEFINITION  bestrophin family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176051014
VERSION     WP_176051014.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Qu,Z. and Hartzell,H.C.
  TITLE     Bestrophin Cl- channels are highly permeable to HCO3-
  JOURNAL   Am J Physiol Cell Physiol 294 (6), C1371-C1377 (2008)
   PUBMED   18400985
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Tsunenari,T., Sun,H., Williams,J., Cahill,H., Smallwood,P.,
            Yau,K.W. and Nathans,J.
  TITLE     Structure-function analysis of the bestrophin family of anion
            channels
  JOURNAL   J Biol Chem 278 (42), 41114-41125 (2003)
   PUBMED   12907679
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..306
                     /product="bestrophin family protein"
                     /GO_function="GO:0005254 - chloride channel activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33984
     Region          1..299
                     /region_name="YneE"
                     /note="Predicted membrane chloride channel, bestrophin
                     family [Inorganic ion transport and metabolism]; COG3781"
                     /db_xref="CDD:442995"
ORIGIN      
        1 mivrprqnwl rmlfvwngsv lqsiipqlvf maivstlavf tngrifgeki plntapftlf
       61 glalaiflaf rnnasferfk earhlwgnll iaartvtsql nrylpdgvst vernrladll
      121 iaftyalkhq lrhtdptadl qrilgtertv elggkcfkpv aildelrggi vralgrapgs
      181 datcwmfetq ldelgksvgg cerilstpip fsysvllhrt vyaycvllpf glvdstefft
      241 plicvfisyt lialeaiane vaepfglapn alaldamtrt iersvlelgd rpmpeefvpa
      301 styqit
//
LOCUS       WP_176051022             145 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176051022
VERSION     WP_176051022.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..145
                     /product="RidA family protein"
                     /calculated_mol_wt=16128
     Region          28..137
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 msqpthtrir mfntkdtypn qtldndlcqa vragntvyvr gqvgtdfdgn liglgdpraq
       61 aeqamknvkq lleeagsdit hivktttyli dpryrepvyq evgkwlkgvy pistglvvsa
      121 lgqpqwlmei dviavvpdnw qpnra
//
LOCUS       WP_176051027             946 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent Clp protease ATP-binding subunit [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176051027
VERSION     WP_176051027.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 946)
  AUTHORS   Guo,F., Maurizi,M.R., Esser,L. and Xia,D.
  TITLE     Crystal structure of ClpA, an Hsp100 chaperone and regulator of
            ClpAP protease
  JOURNAL   J Biol Chem 277 (48), 46743-46752 (2002)
   PUBMED   12205096
REFERENCE   2  (residues 1 to 946)
  AUTHORS   Hoskins,J.R., Sharma,S., Sathyanarayana,B.K. and Wickner,S.
  TITLE     Clp ATPases and their role in protein unfolding and degradation
  JOURNAL   Adv Protein Chem 59, 413-429 (2001)
   PUBMED   11868279
REFERENCE   3  (residues 1 to 946)
  AUTHORS   Gottesman,S., Squires,C., Pichersky,E., Carrington,M., Hobbs,M.,
            Mattick,J.S., Dalrymple,B., Kuramitsu,H., Shiroza,T., Foster,T. et
            al.
  TITLE     Conservation of the regulatory subunit for the Clp ATP-dependent
            protease in prokaryotes and eukaryotes
  JOURNAL   Proc Natl Acad Sci U S A 87 (9), 3513-3517 (1990)
   PUBMED   2185473
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..946
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..946
                     /product="ATP-dependent Clp protease ATP-binding subunit"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=103623
     Region          83..877
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
ORIGIN      
        1 mpalcdicha rpavaratvm qdgerktisi cdyhfrqlmr hqsmlnpfds llggggsssl
       61 fgelgdespl saeipresvd ptdafseqtl ellqraaeka helrrselds ehllyaladt
      121 dvcaallkel klspqdikay idehahtgta dpdapldkls isprvkkavq yafqasrdlg
      181 hsyigpehll iglasvpdsi agtllkkygv tpealrqkvv kvvgkgaedg rvdaptgtpn
      241 ldkfgrdlta iarqgkldpv lgraqeiest ievlarrkkn npvligepgv gktaivegla
      301 qrivngdvpe vlrdkrlvev ninsmvagak yrgefeerak qlidevtakq delilfidel
      361 htivgagqgg geggldianv lkpalargel sligattlne yqkyiekdaa lerrfqpvfv
      421 pepsveqtiv ilrglrdsle ahhqvtfsdd afvaaaefad ryitsrflpd kaidlidqaa
      481 arvrigatsr pvdiqegeaq iaqlkreqdy atsrkrfdqa kqfeeqinek qkavdemmea
      541 wqrktgsetl evtvesvaev vsrltgipvs eltqeerqkl lqmeeqlrer vvgqsdavva
      601 vsdavrlsra glgqthrpia tflflgptgv gktelakala etvfgdeqai iridmseyme
      661 rhavarliga ppgyvgydeg gqltervrrr pysvilldei ekahpdvynv llqvfddgrl
      721 tdgkgrvvdf sntiiiatsn lgaaiimdnl tqpeaarktd kavreelmqv lkghfrpefl
      781 nridevivfh alsknnirsi vqiqldrvvr taaaqditlv mggslvdhlt evgyqpefga
      841 relkrqirqt ietrlakeil adrlksgdrc evdfdtdsde vkfnklaape akepkdakkd
      901 adgkarpngk aakasgdtka ddapadappp aaksgkkssg akkdah
//
LOCUS       WP_176051149             198 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Burkholderia sp. BCC1644].
ACCESSION   WP_176051149
VERSION     WP_176051149.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..198
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20729
     Region          1..188
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mttilqinsa arsqgaqstl laneltaklq qsnpgakvvv rdlladalph ldesvlgaff
       61 tpadnrtaeq naiaaksdal iaelqaadvi vigapmynfg issqlktyfd wiaragvtfr
      121 ytengpegli kgkkvhvvta rggkyagtpn dsqtpylrtf lgfvgmtdvs fifaeglnlg
      181 pdaqsaalas areaiaaa
//
LOCUS       WP_176051172             532 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Burkholderia sp. BCC1644].
ACCESSION   WP_176051172
VERSION     WP_176051172.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..532
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57793
     Region          1..449
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mkssiqrnig pfalmltglg siigsgwlfg awkaakiagp aaicawiiga vvilaialty
       61 aelgamfpes ggmvryarys hgslvgfisa wanwiaivsv ipieaeasiq ymstwpypwa
      121 halfvngelt tpglllsavl vviyfllnyw gvkafarant aitifkflip gatilglmlt
      181 sfhsenlgta snasfapygw savltavats givfafngfq spvnlagear npsrsvpfav
      241 itsilialvi yvllqmayig svnpadvakg wahfnfsspf aelaialnln wlaillyvda
      301 fispsgtgtt ymatttrmiy amernntmpk mfgnvhpiyg vprqamwfnl lvsfiflfff
      361 rgwsslaavi svatvisylt gpislmalrr aatdierpls iplmkliapf afvcaslily
      421 wakwpltgei illmivalpv yfffqaksgw sgwgadlkaa wwlvaylptm avlsligske
      481 fgghgvlpyg wdmlvvaaia lvfyfwgvnt gyrtkylder eshdeilegi ga
//
LOCUS       WP_176051183             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176051183
VERSION     WP_176051183.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33347
     Region          8..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(104,108,151,165,167,226,243,272)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(105..106,110..111,113..114,117,121,123..129,194,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mddfltphla lfvdvvdqqs fsaaarrlgv aassvtrrid rleaqlgirl lhrtthalrp
       61 teagqllygr atrmlaelrg lqedlhsqrd epsgllrvdc papfgrrhlm aalaafmqch
      121 palqvdlvlt dsmvdlqgar lgsdvdlavr igpledtrlv atvlapqrrv lcastaylar
      181 rgepespdal aghdclawhg apppgawrfg errhvpaqpr frsnhseall eaaleglgla
      241 hlptwlagda lrdgrlravl pqyaatpepa tihvlrqqar gsartsklva flatwfaqpa
      301 wdaawa
//
LOCUS       WP_176051219             137 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176051219
VERSION     WP_176051219.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..137
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15540
     Region          19..106
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(20..22,36,53..55)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mtttvekvvl ppipakryft igevselcgv kphvlryweq eftqlrpvkr rgnrryyqhh
       61 evllirrire llyeqgftin garnrldspg serraaepve pesqaadvrv sgkpggtvdv
      121 ialrqalldv idglkhd
//
LOCUS       WP_176051224              96 aa            linear   BCT 11-JAN-2025
DEFINITION  putative quinol monooxygenase [Burkholderia sp. BCC1644].
ACCESSION   WP_176051224
VERSION     WP_176051224.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..96
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10419
     Region          4..86
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 maeiavvali vakpgaeekl rtalegivgp trneagalqy dlhrdlkepa rfvfverwgs
       61 eealaahars ahilayreaa adwiesseir vlsklv
//
LOCUS       WP_176051301             204 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC1644].
ACCESSION   WP_176051301
VERSION     WP_176051301.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..204
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20914
     Region          12..204
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mptlldtllp lagvqllsva spgpnfvivt stavvsrrag vmtglglaaa sgtwaaiaia
       61 glsllvthva wvhtalrlag aayliwlglk mivtarkplp vsapaaasdw naakkgyvvs
      121 mtnpksvafy gsifalmvpa hapawldlav valsvaisaa wycamallas hpsvrrllvr
      181 rkavldttag lllmgvggrm lagr
//
LOCUS       WP_176051323             411 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1644].
ACCESSION   WP_176051323
VERSION     WP_176051323.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..411
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44006
     Region          14..393
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(25..26,29..30,33,65,115..116,118..120,123,143,
                     146..147,150,225,228..229,232..234,237,265,269,321..322,
                     326,330,346,349..350,353..354,357)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 midpnkgrra glavfallyl gfcisyidrs aialslvaig kefqvgtavq gavmstfyig
       61 yaamqipggw iadrwgskkv ivasvafwsl ftlmtglaws lasliairfi fglgeggypg
      121 aavkgvtesc aredrpkmsa flmssnyvgs fiapliiapl ilylgwrhaf vvaggaglvf
      181 allyliavkd thrkrdsagr saridgaatr allkmpimwk illtwfcmgi vnkgldawmp
      241 ayllterhld lkavgmltpl pfvaasvsta lggwilsrwf dgrekwlmaa ccaisgffly
      301 emytaetvtg viayqsivyf fksfvlagvf alpvkflpqk ligtgagmvn fggqvagfva
      361 pavigllvsi tgnydtvfgf livatafavl islsirlspe ggarlvtaee a
//
LOCUS       WP_176051317             425 aa            linear   BCT 11-JAN-2025
DEFINITION  epoxide hydrolase family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176051317
VERSION     WP_176051317.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..425
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46706
     Region          39..143
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          110..>251
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 msstpfspmr rhllatsvaa gvsamlptal haatgasgir pftahipdea vadlrrriaa
       61 trwpgretva desqgvrlar mqallrywgt dydwrkgear lngfpmfite idgldihfih
      121 vrsrhenamp mimthgwpgs ifellkaigp ltdptahgas addafhvvvp slpgfgfsgr
      181 ptktgwgsdh iarawgelma rlgytrfvsq ggdcgsvish rmamqrvqgl agihvnmpat
      241 vppdiatlla tdspapasls pkekaayekl atfyrdncgy sammvtrpqt vgyaladsps
      301 gqaawmydki sqwtysggvp ersiprdeil ddislywltn tatsaaqiyw edhsnnfnav
      361 dialpaaitv fpgeiyqapr swaersyrnl iyfnevdkgg hfaaweepel farevragfr
      421 plrra
//
LOCUS       WP_176051336             304 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia sp. BCC1644].
ACCESSION   WP_176051336
VERSION     WP_176051336.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..304
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33781
     Region          1..300
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mtrhdiefps esttlrgwfy epeqrstdgk aspaivmahg fsavkeqyld ryaevfaang
       61 favllydhkn fgasdgfprq eidpvqqkrg yrdaisylqt radvdgdrig iwgtsysggh
      121 vlevaaidrr vkcvvsqvpt isgyqsglrr trsdlvpaml arfdddrrqr faggppamlp
      181 avsadssvac amagvdayrf ftesaaqfap nwrnevtlrs aelsrenepg qyvdrisptp
      241 llmivadqdv ltptdlclka wenalqpkrl lqikgghftp yiehfdatsr aavewftqhl
      301 ggvr
//
LOCUS       WP_176051345             116 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176051345
VERSION     WP_176051345.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..116
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=11706
     Region          42..>108
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mkktphlstl lavstavllg aapltnaiaq dasadngmkt essqpvtdtw ittkvksqla
       61 atdgmksvdi svktvdgvvt ltgvlptkia vkkaiavsra vkgvkhvdas glkaka
//
LOCUS       WP_176051449             430 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176051449
VERSION     WP_176051449.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..430
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46363
     Region          38..419
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 msfhfgtpla rrarrrapml waallvagav haqqppltld aalqsatdhs asmqaaqasv
       61 rasseaavka gqlpdpmlka gidnlpvngg qrftvgqdfm tmrrigieqe wvsgdkrhlr
      121 talaneqvgr eragylaqla svrqqtataw lnavyakqal alqqalldhm nhefdatkas
      181 yrgakasasd vvqaramlaq tqdqllkaqq vyqtalials rwtavpasdv tgtppapesf
      241 vsslppdelr lsqpalitaa ddiavaeadt avanselnpn wtwevayqqr ggaysnmvsv
      301 gvtiplpinr knrqnrdvae kaalatkarl myedtlrqvq adirtqsetl asgrerianl
      361 gaallpaadq rvqlanaayr agtgsladtf aarraqldaq lqvldlrrdv sqiwaqleyq
      421 vvpstmataq
//
LOCUS       WP_176051486             313 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176051486
VERSION     WP_176051486.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 313)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 313)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13797492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..313
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33191
     Region          2..191
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          <173..311
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mdalsqllsl gcsrvelemr clldgtftia ydapppseva fhlmlsgqcr lrvaggrtqq
       61 lgegdllllp gggayeilda igargavtvp vrelaatnvt vlpvqsnigd vdsanvdmlc
      121 grlvfgrgag dlmlralprv mhiglcessg leplqmlmgl lrsemsreqp garaivdalg
      181 qalltyalra ygqdtqmlsg wlavavdarl gpsiramlqa pahpwtvasl gnvaamsrat
      241 yarhfrekag msvgafvaqi rmmhacallr dsgsgqaaig eavgyrseaa fgkafrdvlg
      301 mtpgrwrrth rcv
//
LOCUS       WP_176051504             263 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD family hydrolase [Burkholderia sp. BCC1644].
ACCESSION   WP_176051504
VERSION     WP_176051504.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..263
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=28326
     Region          14..222
                     /region_name="Cof"
                     /note="Hydroxymethylpyrimidine pyrophosphatase and other
                     HAD family phosphatases [Coenzyme transport and
                     metabolism, General function prediction only]; COG0561"
                     /db_xref="CDD:440327"
ORIGIN      
        1 mqplslapad tfssvrfvlt dmdetlthrg rlaaqtyaal erlqahgirv ipvtaapagw
       61 cdqmarmwpv dgviaenggl firrspdghg aerrywhadd aldgardarr riaqhvakav
      121 paarhaddqd frltslayar tgsgqddrir dalvaagada tinnlwiigw vggydklsms
      181 lrvlsdaygv dadeapacva ysgdstndap mfgyfthtag vstvvdylqq lpvlprwitq
      241 gpggsgfvef adailrarad dqg
//
LOCUS       WP_176051522             293 aa            linear   BCT 11-JAN-2025
DEFINITION  endo alpha-1,4 polygalactosaminidase [Burkholderia sp. BCC1644].
ACCESSION   WP_176051522
VERSION     WP_176051522.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 293)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008090
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..293
                     /product="endo alpha-1,4 polygalactosaminidase"
                     /EC_number="3.2.1.109"
                     /GO_function="GO:0016798 - hydrolase activity, acting on
                     glycosyl bonds [Evidence IEA]"
                     /calculated_mol_wt=31902
     Region          1..276
                     /region_name="COG3868"
                     /note="Predicted glycosyl hydrolase, GH114 family
                     [Carbohydrate transport and metabolism]"
                     /db_xref="CDD:443077"
ORIGIN      
        1 msarsfasva lmlllaacgg dadssapgts vasaatrasp pvawkplvpg tswqwqidgn
       61 tinetvldrv nnprkmfdvd mertdaatiq rlkangiyvv cymetggred grgdagqfpd
      121 svlgypvegy edherwldir qtkilmpiml arldqakkkg cdgvepdldd gyrqetgfpl
      181 trddqlrynt aliaaahdrg msmglkngsg iavamakiad walneecnnf hecdgyasfi
      241 alnkavfnve ytrpdgmtla dfcpadnran fdgilkwssd tlaalpraac rfe
//
LOCUS       WP_176051568             290 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176051568
VERSION     WP_176051568.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..290
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31470
     Region          15..280
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mttarsldrt ypalrttegg gfvvhrpfpt rllmdfdpfl lldemgpvdy apgeavgapd
       61 hphrgfetvt yaldgrfrhr dssghagtlg pgdvqwmtag agvvhsempd pafaqaggrs
      121 hgfqlwvnlp rrdkmiapry qeipadript atspdgrarv rviageafgv qaaietrtpi
      181 lyqhftlepg atvtqpvpag yrvfaypidg tglygpdrqa vdarhmivyg ddgdtvtfaa
      241 gdspldllli ggvplnepiv rygpfvmnte eeirqavvdy qtgrmgriea
//
LOCUS       WP_176051563             399 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: amino acid aminotransferase [Burkholderia].
ACCESSION   WP_176051563
VERSION     WP_176051563.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Christen,P. and Mehta,P.K.
  TITLE     From cofactor to enzymes. The molecular evolution of
            pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Chem Rec 1 (6), 436-447 (2001)
   PUBMED   11933250
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Alexander,F.W., Sandmeier,E., Mehta,P.K. and Christen,P.
  TITLE     Evolutionary relationships among pyridoxal-5'-phosphate-dependent
            enzymes. Regio-specific alpha, beta and gamma families
  JOURNAL   Eur J Biochem 219 (3), 953-960 (1994)
   PUBMED   8112347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10013160
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..399
                     /product="amino acid aminotransferase"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42591
     Region          3..388
                     /region_name="PRK09257"
                     /note="aromatic amino acid transaminase"
                     /db_xref="CDD:181731"
     Site            order(107,142,209,254..256,292,295)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
ORIGIN      
        1 mslfsavqla prdpilglne afnadarptk vnlgvgvytn eegkipllra vreaekvrve
       61 aglprgylpi dgiaaydaav qklllgndsp liaagrvvta qalggtgalk igadflrtvn
      121 pnvkvaisdp swenhralfe aagfevvayp yydaatngvn fegmlsalns yeagtvvvlh
      181 acchnptgvd lteaqwqqvv dvvkarnlvp fldmayqgfg enieadaaav rlfaaadlna
      241 fvsssfsksf slygervgal siitsskeea trvlsqlkrv irtnysnppt hggavvaavl
      301 aspelhaswv qelgemrdri ramrnglver lkasgvdrdf sfinaqrgmf sysgltsaqv
      361 drlrdefgiy avgtgricva alnmrnldav anavaavlk
//
LOCUS       WP_176051583             209 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia sp. BCC1644].
ACCESSION   WP_176051583
VERSION     WP_176051583.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..209
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21840
     Region          1..206
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mslsallafa lilsvgvatp gptvllamsn gsryglrham vgmlgavtad vvlvalvglg
       61 lgvlldaset afvtlkllga awlayvgvrm lmssgsaave qadvpatpdr rtaflksffv
      121 amsnpkyylf msallpqfvd rshaiapqya ilaativaid vigmtgyall gvhsvrvwka
      181 agekwlnrvs gslllmlagy valyrkaah
//
LOCUS       WP_176051682             306 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ABC transporter ATP-binding protein [Burkholderia].
ACCESSION   WP_176051682
VERSION     WP_176051682.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia
  ORGANISM  Burkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia"
                     /db_xref="taxon:32008"
     Protein         1..306
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=33812
     Region          9..266
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mpsndgrass rqafvevdel skqyredipp vfedvtfrmd qgeficvigh sgcgkstiln
       61 vlagleeass gvavmagrei agpsldrgvv fqghallpwl takqnvefav rsrhpdwsra
      121 aitehtlrfl dmvglshavd kkpselsggm kqrvgiaraf sveprmlmmd epfgaldalt
      181 rgviqdellr icaatnqtvf mithdvdeai lladriflms ngprarlaei vvnplprsrt
      241 retlvnepqf yvirnylidf lvrrsaliqq eieggkshhk strvvrldan ptavvnleqs
      301 raarla
//
LOCUS       WP_176051692             318 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176051692
VERSION     WP_176051692.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..318
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34134
     Region          8..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..296
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(105,109,148,162,164,230,247,275)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(106..107,111..112,114..115,118,122,124..130,191,
                     224..228,235..236,239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdlsqrtrai lsfvhaadgg sfaaagrmlg itsaavsknv agleqalgvr lmnrttrtlk
       61 ltdegavflr qarvaleald aavdsivaqr lgpqgrvris tsaafgrdhl qpvlpgllar
      121 ypglsvevdf ddrivdvvrd gydivirggd irdsalvsrp ifrmhaalva spaylvrhgi
      181 prapdelgah rliarrfldg giatwgfrmr dgsvvefdpg esalltfsap eagvqaavdg
      241 lgiarvgvhl awahlragtl kvllrrhflp gtyemaiqyp hralkasrvq atvdylldaf
      301 aanerlhvpl kaldayga
//
LOCUS       WP_176051729             315 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176051729
VERSION     WP_176051729.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..315
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34907
     Region          11..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(112..113,115..116,119,123,125..131,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrkfkipnmg alvafeaaar hesfthaake lfltesavsr qiatleaslg vrlfarvkqr
       61 vvltragkly gtqvrralet ldrdtlsiia hgsgggylel avlptfashw lipriksfyd
      121 rtpdvrvnmg srtdlfsfed thfeaaihyg kptwpgtssd ylfgeevvpi cspalldgpv
      181 ervedllayp llhsttrpga waqwfethgv edirtmqgvr yelhtmlisa aaaglgialv
      241 pkffveeqlq qlglvvpcda atvgdsayyl vyptefshsk plelfrgwll eqasayaape
      301 raeedadmed dedve
//
LOCUS       WP_176051756             424 aa            linear   BCT 11-JAN-2025
DEFINITION  NupC/NupG family nucleoside CNT transporter [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176051756
VERSION     WP_176051756.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Hirschi,M., Johnson,Z.L. and Lee,S.Y.
  TITLE     Visualizing multistep elevator-like transitions of a nucleoside
            transporter
  JOURNAL   Nature 545 (7652), 66-70 (2017)
   PUBMED   28424521
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Johnson,Z.L., Lee,J.H., Lee,K., Lee,M., Kwon,D.Y., Hong,J. and
            Lee,S.Y.
  TITLE     Structural basis of nucleoside and nucleoside drug selectivity by
            concentrative nucleoside transporters
  JOURNAL   Elife 3, e03604 (2014)
   PUBMED   25082345
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Munch-Petersen,A., Mygind,B., Nicolaisen,A. and Pihl,N.J.
  TITLE     Nucleoside transport in cells and membrane vesicles from
            Escherichia coli K12
  JOURNAL   J Biol Chem 254 (10), 3730-3737 (1979)
   PUBMED   374403
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449426
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..424
                     /product="NupC/NupG family nucleoside CNT transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005337 - nucleoside transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_process="GO:1901642 - nucleoside transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=43919
     Region          1..422
                     /region_name="NupC"
                     /note="Nucleoside permease NupC [Nucleotide transport and
                     metabolism]; COG1972"
                     /db_xref="CDD:441575"
ORIGIN      
        1 mdilrsllgm lflllvayll snnrravsgr tmiaalltqf aigalvlfvp sgrtalagaa
       61 sgvnrvldmg nhgiafvfgg lvdakmfqlf gdggfvfglr vlpmiifvta lisvlyyigv
      121 mkwivailga glakvlgvsr ieacsavati flgqsempal vkpfvrnmts aeiftvmasg
      181 masvagsvlv gyaglgvkme yllaasfmav pggllfgkll fptvepsrvv vdgldfddkr
      241 aanvieaaas gasvgmriai nvgamliafv glialmnliv ggaaafagfp qvtlvgiigh
      301 lfaplawiig vpwhdatlag nfigeklifn efvaygdlsp ylkggehvaa aglqvldpkt
      361 laivsfalcg fanfssiail aggfsavape rrsevarhgl raltaatlsn lmsaaiaglf
      421 fslh
//
LOCUS       WP_176051775             385 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176051775
VERSION     WP_176051775.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..385
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=43095
     Region          1..385
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfsltqeqe mlvsslrqfv ekelqphefa vdraddvppe ladsirrkal elgfyafnmp
       61 esaggpgldy vtqalverel grtswalhvf varpskilma ckgdqieryl kptvrgervd
      121 cfaltepgag sdamgirtra vrdgddyvin gskhfishad tadfvilfav tgeeevrgqk
      181 rkrvtcflid kdtpgmtvrr gphctslrgy hqseiflsdc rvsaaqilge ehrgfeland
      241 wltagrvmva annigraqra femaaewaat rqqfgkrigd fqgtsfklad mqteiraael
      301 vtlytaqkld lgtmtdgdaa lakllatetl grvtdhavqi yggmglmdel pierfwrdar
      361 ieriwegtse iqrhilskei lrrys
//
LOCUS       WP_176051776             262 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176051776
VERSION     WP_176051776.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..262
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=27943
     Region          6..256
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 msnedirier hdgvvtlrln rpakrnslar phldflrdtl dalandpatr clvltgtgsa
       61 fcagadvdew aeaerngeld tygwserahr fvealaafpr ptvaalngst vgagadigfa
      121 cdfriastaa tlrcgytgmg yspdmggswf lprlarpdvv rryiflnerw naqdalaagf
      181 vsevvdadaf aqhvaafaar laqgpsvafg hakallaqsl thtlaeqlrg elaacvacgh
      241 sedgqealra svegrapnfv gr
//
LOCUS       WP_176051779             291 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia sp. BCC1644].
ACCESSION   WP_176051779
VERSION     WP_176051779.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 291)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..291
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31614
     Region          37..260
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mntlstpvag avplgrakad rywllvvpll avlivlyvyp lvrvlwlgfa vpepglhnya
       61 rlldnrgvhr vlwttlrvca vttvfsvalg yaiayamahv gprqrmalmf gllvpfwasv
      121 lvrafswlfl lgeqglvntl lmriglidap lplmrneigv vigmihfmip yavlplyanm
      181 kgidpqlvra sqglgagalv tfrkvyfpqt rpgivgaail vfifslgfyv tpvilgggrt
      241 vmiaeyistq ilqlmnwgsg aalaslllas ilaalallar fvdlrelfga r
//
LOCUS       WP_176051782             156 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein,
            partial [Burkholderia sp. BCC1644].
ACCESSION   WP_176051782
VERSION     WP_176051782.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..>156
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
     Region          1..>155
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkvlvavkrv vdynvkvrvk sdstgvdian vkmsmnpfde iaveeavrlr eagvatevia
       61 vsvgvtqaqe tlrtalaiga drailvestd sveplavaki lkalvdkeqp qlvilgkqai
      121 dddsnqtgqm laalaglpqa tfaskvtvad gkatva
//
LOCUS       WP_176051784             237 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia sp. BCC1644].
ACCESSION   WP_176051784
VERSION     WP_176051784.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..237
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25828
     Region          6..229
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 msqtsgsmia frrpdgqelq gylatpakte gapavvviqe wwglndqirg vadrlarcgy
       61 falvpdlyrg kstveeeeah hlmtgldfgd aasqdipgav tylktlasrv avtgycmgga
      121 ltllslqyad adagvtwygl ppldyidpak lkvplmghwg tqdaffaidq vdalekkltd
      181 akvgfefhry lahhafanet avgpgriagt qfdpvwsqia wdrtltffgr tlwakqg
//
LOCUS       WP_176051803             321 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Burkholderia sp. BCC1644].
ACCESSION   WP_176051803
VERSION     WP_176051803.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..321
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34419
     Region          5..315
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mpkvvgifav pgvqlldvsa pldvfaqana ecgkpfytlr iiasesgpir sssgaqllpd
       61 wivpdvperi dtllvagaps aghitlrtdv lawlrsaavq skrygsictg afilaatgll
      121 kgrhltthwa aadalaeafp slavdadaly vrdgklrtga gvtagldlal alveedlgre
      181 iarrvaaqlv mffkrpggql qfsrkgearp tgrsvlqevq rwiaanpele hsvadlakha
      241 gmsprhfarl fraevgmtpa vwveatrisa arqllenghd tpkqvaakcg fanvdtlrrs
      301 ftrhvgitpa eyrkrqavpv e
//
LOCUS       WP_176051810             441 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia sp. BCC1644].
ACCESSION   WP_176051810
VERSION     WP_176051810.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..441
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46917
     Region          9..414
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(22..23,26..27,30,69,127..128,130..132,135,155,
                     158..159,162,243,246..247,250..252,255,283,287,339..340,
                     344,348,364,367..368,371..372,375)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mgtsvkqpkr aalasfvgtt iewydfysya taaaivfgpl ffpgenrfis llasfgsfav
       61 gffarplggv mfgylgdrfg rkrsllatlm lmavstvaig llpthaqagv iapillvlmr
      121 vlqgiavgge wggavllage hapegkrtff asfaqlgsas glilsmlafg aistlskddm
      181 mswgwrvpfl assvllivgf virasvsesp efeevkksgn iaqkplreal kywpllllai
      241 ganvygiagv yfsnifmisy atqflsldrs mvlhcmtiva vlqfvvqlaa aflaqrfgtt
      301 rvllitgawa aivpflmlpl vhmgtplsit vgvglatlae sgyysvvagf vsgifvarir
      361 ytaisiayqv cgalaggltp lvatiiaqnt apqwwplaiq ytsaavvssl cvwlisrrvs
      421 iddagaprkq edalprgart v
//
LOCUS       WP_176051836             228 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176051836
VERSION     WP_176051836.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         1..>228
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
     Region          25..>228
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mttqdllaqy gpresmeydv vivgggpagl saairlkqla aekgteigvc vlekgseiga
       61 hilsgavmdp rainelfpdw kergapldve vtedrflfls eksavttpnw alpanfqnhg
      121 nyvislgnvt rwlgqqaeal gveifpgfpa aeilynddgs vkgvatgnmg vgkdgepten
      181 fqlgmelhak ytlfaegcrg hlgrqliskf kldanaepqa ygigikel
//
LOCUS       WP_176051844             191 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein, partial [Burkholderia sp.
            BCC1644].
ACCESSION   WP_176051844
VERSION     WP_176051844.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia sp. BCC1644
  ORGANISM  Burkholderia sp. BCC1644
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Burkholderia sp. BCC1644"
                     /db_xref="taxon:2676293"
     Protein         <1..>191
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
     Region          2..191
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 anlslregei vgllgrsgsg kstllriiag lieptggevt ylgkplsgpa egvamvfqtf
       61 alfpwltvlq nveaglealg vgarerrera laaidligld gfenayprel sggmrqrvgf
      121 aralvvdpti llmdepfsal dvltaetlrt dlldlwtqgr mpiksvlivt hnieeavfmc
      181 drilvlssnp g
//
LOCUS       WP_176052113             790 aa            linear   BCT 11-JAN-2025
DEFINITION  tetratricopeptide repeat protein [Paraburkholderia caribensis].
ACCESSION   WP_176052113
VERSION     WP_176052113.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 790)
  AUTHORS   Perez-Riba,A. and Itzhaki,L.S.
  TITLE     The tetratricopeptide-repeat motif is a versatile platform that
            enables diverse modes of molecular recognition
  JOURNAL   Curr Opin Struct Biol 54, 43-49 (2019)
   PUBMED   30708253
REFERENCE   2  (residues 1 to 790)
  AUTHORS   Blatch,G.L. and Lassle,M.
  TITLE     The tetratricopeptide repeat: a structural motif mediating
            protein-protein interactions
  JOURNAL   Bioessays 21 (11), 932-939 (1999)
   PUBMED   10517866
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18415115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..790
                     /product="tetratricopeptide repeat protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=86034
     Region          2..203
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          7..32
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          71..99
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(72,75..76,79..80,82,106,109..110,113..114,116..117,
                     140,143..144,147..148,151)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          104..134
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          105..785
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          139..167
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          173..201
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          244..269
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          275..303
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(276,279..280,283..284,286,310,313..314,317..318,
                     320..321,344,347..348,351..352,355)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          308..338
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          343..371
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
ORIGIN      
        1 mhdipsllna alahhqagrl adaqtlydti lqrdpaqsda lhfsgllacq tdradagial
       61 mrasiaanpn avyynnlgnv llgrrqfgea iegyrhavtl rpdyaeahnn lgnalraagd
      121 anasmlscar aielrpgyae aynnlgnalk dlgdldnavl aygkavsfkp dyadafsnla
      181 raqagrgkad esiaafrrai eldpgrvdsh dslatllhas gdadaaiaal qraaqlapad
      241 aarhrklaqw lrgrkrwdea aqsltraver apndasgyle lgdtyehgdk ldaailcyrt
      301 atelsprdgh ahhrlavall kqrradealk saqkavelep hsavprvnlg dvlsvlgdae
      361 gaiasyrrgi aldgemelah nrllfdlath aptppsvtla darefgarma ararrcehpa
      421 pqndgrklri gfvsgdlqlh pvgifiesvm ehfadgsfdl iaystraked ditarlkqrf
      481 sawrslvnvp deqavqmird dridilvdls ghtvynrlpv fawkpapvqv swlgyfgttg
      541 lneidyvlgd phvlpvdeas hyvektwrlp dsylcftppk ddvavgplpm tlnghvtfgy
      601 fgklvkitpn vivewsrilh avpdaklmmk ahelgaehar rstleqfaaq gidasrlile
      661 ggsprheyla synrvdimls pfpypggttt aealwmgtpv valkgdrfvt hicesvlnaa
      721 glaewigrde deylalactw aaqaerlaal raglraqtla splcdarrfa knlkaafegm
      781 waqylapqaa
//
LOCUS       WP_176052161             216 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Paraburkholderia caribensis].
ACCESSION   WP_176052161
VERSION     WP_176052161.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..216
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22923
     Region          10..216
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mfgithfeff vvavfllnvt pgpdtayivg rsvaqgrgag lmsalgisag ccvhslacaf
       61 gltallaast taftvikfvg aiylvylgvr lilvkpeasq atgstrmrga pgapnslrql
      121 fmqgfwtnvl npkvvlffvs ffpqfvsads nhkilsfltl gvvfvvmsma wnsfvawvag
      181 svtrrfsgkp gvkkwldrtv gsafvglgir latatr
//
LOCUS       WP_176052181             213 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Paraburkholderia caribensis].
ACCESSION   WP_176052181
VERSION     WP_176052181.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..213
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23044
     Region          4..213
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mhhylpillq ialvyliali spgpnffmit qlslagrrgl gaasalgvgt gstvwaslam
       61 lgfatvlqri dwlyngiria gaiylvwfgi klvwastkrg etivvnvetp pandrgahfr
      121 awrtgmltcl tnpkscafwt sifatlfpah pppwfygval amigmmsvgw ygsvalmfat
      181 ertqrgyrrl rrpidgvcga llvglgakva aes
//
LOCUS       WP_176052169             400 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent rRNA methyltransferase [Paraburkholderia
            caribensis].
ACCESSION   WP_176052169
VERSION     WP_176052169.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..400
                     /product="class I SAM-dependent rRNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=43644
     Region          3..399
                     /region_name="RlmK"
                     /note="23S rRNA G2069 N7-methylase RlmK or C1962
                     C5-methylase RlmI [Translation, ribosomal structure and
                     biogenesis]; COG1092"
                     /db_xref="CDD:440709"
ORIGIN      
        1 mntvtlkpsk eksllrrhpw vyanaidrvd gkpaagatvl vrahdgrfla raaysphsqi
       61 rarvwsfden epvdhaffkr rvqralahrq smvhntgatr lifgeadglp glivdyyiqd
      121 detkrgqivc qfmaagveaw kdaivqalag atgcpnvyer sdvsirekeg leqtvgvlag
      181 dappetlias engvryhvdv rnghktgfyv dqrdnralvq elsngrdvln cfcytggfsl
      241 aalkggakrv vsidssgeal alaqanvtan gfdaeratwl dadafktlrr lyddgerfdl
      301 ivldppkfap srehvdraar aykdinltgl kllrpggllf tyscsgaida elfqkivaga
      361 aadarvdari lkrlgagvdh plltafpege ylkglllqia
//
LOCUS       WP_176052232             427 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Paraburkholderia
            caribensis].
ACCESSION   WP_176052232
VERSION     WP_176052232.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..427
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45378
     Region          64..303
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mvfskvltvc aisaafvasa vttahadpla dveggplgra qvqrlalded gylpavklse
       61 qivripvaad gdvtlettiy kpegpgpfpm vvfnhgkihg dprmqtrsdp vslarefvrr
      121 gyvvvapnrq gfadsggtyv qdgcdvtrng msqaadvatt vdymskqsyv dakhivvagt
      181 shgglatiay gtnaasgvrg linfsgglrq dactdwqgnl thafgtygek trvpslwlyg
      241 dndsiwpstl vskmyaaytd naqgkgatak mvdfgsyknd ahrlvgdrdg vqvwwpsvea
      301 flarvgmptg vqyrvaeptq pkathfasid avdsvpfvde agragyrnfl hqypsrafav
      361 sdsgawswae ggddpmsvav ancqkqsadp chlyavndav vwkdgatrta dadspskdgs
      421 kpalasr
//
LOCUS       WP_176052274             316 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Paraburkholderia caribensis].
ACCESSION   WP_176052274
VERSION     WP_176052274.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..316
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34833
     Region          76..277
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mswqsalacw flrrqfhpqt rhptisaera rrltakrayt prvpsgwtld erygerdwpl
       61 rgewltrvdg rhtatilylh gggyyfcspq thraasfgla srsgarvfsl dyrlapehpf
      121 paalddalaa yrrlledgtk pdsiviagds aggglalatl valrdagepl pagailfspw
      181 tdlaatgasl qtndgidpmf hgpsiaraar lylddtpath pyasplyael kglpplfmqv
      241 gstevlldds rrvadkaraa gvdidfeiwr kmphvwqlwa pfipearral dlaarfvarv
      301 tseprdihpa sersia
//
LOCUS       WP_176052317             157 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Paraburkholderia caribensis].
ACCESSION   WP_176052317
VERSION     WP_176052317.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 157)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140358
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..157
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17637
     Region          3..117
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd04667"
                     /db_xref="CDD:467552"
ORIGIN      
        1 mkqratvvcr mgtrillvgk ansrwslpgg ktnagesfea aavrelmeet rlqatgmqyl
       61 fefagartch hvfaayvder qtpvpsneit rctwakvtdi sdldtsvstr givdvlalnr
      121 nydprvrsry qradafvqnl realqdarmr gwtpalw
//
LOCUS       WP_176052352             501 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54 dependent transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176052352
VERSION     WP_176052352.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..501
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=53906
     Region          2..124
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <146..444
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mnststtgas drtvlcmapt pdealaaflg aagwqvvhar ttaaaeklld rgdikvglvt
       61 lpddvtqqql saleacmrhg eanwiaqiap ghatddltsr fildycfdfv tapcmndrli
      121 falghahgls nlrrasfrpq pslgahgmvg hcepmqklyr ridkcaqtda pvfiagesgt
      181 gkeltaravh dgsaraqqaf vaincaaipp tllqaelfgh ergaftgalq rkigriehah
      241 ggtlfldeig dmphecqavl lrflqegtie rlggntsvkv dvrvisathv nleaavkdgr
      301 fradlyhrlc vlrldepplr ergsdirlla dyalsmykqd gthkirgfss gavvsmsnyd
      361 wpgnvrelin cvrravvmte grfitetdlg lpevsgarak tlaeirtqae ieaieealrr
      421 hghnlsgaaa dlgvsratly rlmnanrmnp danamrsmrr sgegrtdgat dgssdpggad
      481 dgddsdagsh rpravaampv g
//
LOCUS       WP_176052359             374 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Paraburkholderia caribensis].
ACCESSION   WP_176052359
VERSION     WP_176052359.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..374
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38412
     Region          181..>372
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 mdpstdpadr epsadtahsg lparhpiaaf ggwlarvdpg thrrikglrl vtayglasal
       61 gtlqdvthgl prgtsvglla anfalwasvs earttrpess rdlallcaaa algaamyvcv
      121 aqpllvfgha gpelvlvtga flvgylkrfg vtggglgsqi yigqllayga nlvpadlpai
      181 aiagliamla sivprllsgp aerpavvaal spgpkpvpgr pspefvmglq aasgalvvva
      241 lnawlnlaes vwaitactyv vagsatgtvq rvrrriigtl vgvplglicl piaehaplli
      301 wlaaalamvv ysmalperyd iacgafaftl ivtlavngmh sipfltaraw etliggalgl
      361 laatvifplr vreg
//
LOCUS       WP_176052355             755 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Paraburkholderia caribensis].
ACCESSION   WP_176052355
VERSION     WP_176052355.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 755)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..755
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..755
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=84086
     Region          175..753
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mtyvvavrtl ceftarrgdl dlrftpapsa legiaghqav tarrasgyea eitltgthgg
       61 ltvrgradgy dralnrleei kthrgdlerm panhralhwa qalvyghllc earaldaltv
      121 alvyfdiasq ketvlteqht aaslraffed qcerfvawaa retahrdarn talnalrfpy
      181 gefrsgqrel svavfraard ghclmaqapt gigktlgtif pllkacgadh ldrvffltak
      241 tpgralalea ieslhrgeaa lplrtlelva rdkacehpdk scdgdscpla rgfydrlpaa
      301 rdtalqartl draavreaal ahgicpyyla qemarwcdvv igdynyyfds samlyaltql
      361 ngwrvavlad eahnlpdrar rmysatldqh afrgarhaap aalkkpfdrl nrewnalnre
      421 rraayevlpd vppklqsalq nliasigdql aetpqsvden alrfyfdalh fmslveqfgd
      481 hsivdvtldt phgaarakpa tqicvrnvip apflkpryaa arativfsgt lspqhfyrdm
      541 lglpadtgwl dvegpfraeq lnvhvahhvs trwrdrersl epivdliaqq yaarpgnylg
      601 flssfdylqr vagsmrerhp qvpiwtqepr mderardafl arfatggagv gfavlggafs
      661 egidlvgerl igafiatlgl pqmndvneqm rrtfdaqfgn gydyaylypg mqkvvqaagr
      721 virtehdagv vhliddryrr advkrllprw wkiat
//
LOCUS       WP_176052386             210 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176052386
VERSION     WP_176052386.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..210
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22536
     Region          23..184
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtdhttprra saakaegtcp rgrprefdta avlteaskvf wrngfhgtsv ddlcnatgvl
       61 rgslygvfgd khgimmaald hyaegaiagl verlnanvpp dvalrnallh htrtassltg
      121 cfitnstlel qpddealhak iraiqrrvvt llaaavirgq atgvfngdld ekaaadfllc
      181 mtqglrvlnk ckrkedelka vvdiamralt
//
LOCUS       WP_176052450            1067 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Paraburkholderia
            caribensis].
ACCESSION   WP_176052450
VERSION     WP_176052450.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..1067
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=115497
     Region          1..1047
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 miarlirwsi hnrflvllat vlitawgvys leetpldalp dlsdtqviik asypgkapqv
       61 iedqvtyplt ttllgvpgak tirayssfgd afvyvlfddk tdqywarsrv leylnqvqsr
      121 lppgatvslg pdatgvgwvy eyalvdrtgr hdlgelraln dwflkfelks vpdvsevasi
      181 ggmvrqyqvv ldpdklrayg itqgmvadal gkanqgsggs vvelaeseyv vrssgylhsl
      241 ddfrnvvlrt ndagtpvllg dvariqigpe prrgiaelng qgevaggvvv mrsgknaltt
      301 ieavkarlae lkrslpqgve vvttydrsql ieravdnlkd klieefivva ivcavflfhl
      361 rsalvavlsl plgvlaafiv mryqgvnani mslggiaiai gamidaaivm ienahkhlea
      421 yehahpgkpi ttvqrwelia tsaaevgpal ffslliitls fipvfslegq egrlfsplaf
      481 tktytiaaaa glsvtlvpvl mgylirgrip heasnpinrv lvrlyrplle atlrrpwfai
      541 glavvalvlt aiplsrlgge flpqldegdl lymptalpsi stekaaellq qtdrliktvp
      601 evatvfgksg raetatdpap glemfettiv fkprsqwrpg mtpeklrdel drtvkvpgls
      661 nlwvppirnr ldmlstgiks pvgvkisgad ltqidriatq veavvkdvpg vssalaervn
      721 ggryinvdin rqaaarygls vadvqsvvss avggenvgev itgrerfpin iryprevrds
      781 lerlrqlpvv tdrgaqiqlg dvanlqiadg ppsirsenar lsgyvyvdir nvdlqsavka
      841 mqravaekvq lppgysiaws gqfeyleraa aklrtvipvt lvvifvllfl tfssaadall
      901 lmstvpfalv ggfwliwvlg havsvatsvg fialagvaae fgvvmllylk galnrrlelg
      961 epmteatlld airegavlrv rpkamtasvv laglipiivg hgagsevmqr iaapmvggmv
     1021 tapilsmfvi paawlllqrr rvrhqarfph avpsgtqvps vqtgetq
//
LOCUS       WP_176052468             242 aa            linear   BCT 11-JAN-2025
DEFINITION  cysteine hydrolase family protein [Paraburkholderia caribensis].
ACCESSION   WP_176052468
VERSION     WP_176052468.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..242
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26357
     Region          36..220
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 msdanqaaqe nanpyadpan palpqtgfkl dparaalvvi dpqndflsps gaswpvfgps
       61 itenntvanl gqlfktakqv gltvaisphy yypcdhewhf ggplekvmhn icmfdrkgpn
      121 tledfegsga dfldeykpyi ldgktiiasp hkvygpetnd lalqlrkkgv sqiilagmaa
      181 nlcieshlre lieqgfevav vrdatagprl pdgdgylaam infrylahal wtteqtvrel
      241 ts
//
LOCUS       WP_176052514             206 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176052514
VERSION     WP_176052514.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..206
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23648
     Region          9..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkrkrltreq skdqtrlrll daaqaifmkk gfvaasvedi aeaagytrga fysnfrskpe
       61 lflellrrdh esmqadlqni feenatredm easvlryysr mpsenkcfll wveakllaar
      121 dvrfrvrfna fmhekleqlt ayitefsvrv gtplplpaet lalglmglcd gmqffftvdp
      181 qrfsagraee vlgsffarvv fgrtme
//
LOCUS       WP_176052515            1040 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Paraburkholderia
            caribensis].
ACCESSION   WP_176052515
VERSION     WP_176052515.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..1040
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114549
     Region          12..1024
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msavhdeegr fnlsawalrh qalvmflitl atafgilayt klaqsedppf tfrvmvirtf
       61 wpgatarqvq eqltdrigrk lqetpaidfl rsysrpgesl ifftmkdsap vkdvpetwyq
      121 vrkkvgdiaq tlpqgiqgpf fndefgdvyt niytlegdgf ssaqlrdyad elrtvllrvp
      181 gvgkvdyfgd pdqhiyveit ntqltrlgis pnqlaqains qnsvspsgtl ttyddrvfvr
      241 ptgqfkdlna ladtliring rsfrlgdiat ikrgyddppv tqmrfqgkpv lgigvtmqpg
      301 gdvirlgksl dekmkdlqah lpaglklvev ssmphavars vddfleavae avaivlvvsl
      361 vslglrtgmv vvisipvvla vtalcmylfd iglhkvslgt lvlalgllvd daiiavemma
      421 vkleqgwsrt raaafaytst afpmltgtlv tvsgflpial aksstgeytr sifevsaial
      481 iaswlaavvl ipmlgyhllp erkrqphepe dhehdiyetr fyrrltgwit wcierrfvvl
      541 aitvilfvvs lagfalvpqq ffpssdrpel lvdvrlpega sfeatlrqaq riekalagrp
      601 eidhsvnfvg sgaprfylpl dqqlqqpnfa qfvitaksve ereklarwle pklrndfpai
      661 rtrlsrleng ppvgypvqfr vsgddiatvr giaekvaatm ranpgtanvq fdwdepaers
      721 vrfevdqkka relgvtsadv ssflamtlsg ytvtqyrerd klisvdlrap knervdpsql
      781 ltlamptpng avplgalgrm rddleygviw erdrqptitv qsdvrgnaqg idvthavdkq
      841 laqirstlpv gyrieiggsv eesakgqtsi naqmpimiia vlvllmiqlq sfarvlmvvl
      901 taplgligvv atlllfgkpf gfvamlgvia mfgiimrnsv ilvdqieqdi aqghkrfdai
      961 vgatvrrfrp itltaaaavl alipllrsnf fgpmatalmg gitsatvltl fylpalyaaw
     1021 frvrgeerdp rpapsdhsgn
//
LOCUS       WP_176052413             204 aa            linear   BCT 11-JAN-2025
DEFINITION  LemA family protein [Paraburkholderia caribensis].
ACCESSION   WP_176052413
VERSION     WP_176052413.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..204
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=22052
     Region          1..196
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 mtksllfipl lfafcvlagc gtdrphvrnd eaqaafsevl dlyndrlsla deatalarpy
       61 lptgssvlad iasarssvaa lhatpefvea palfarfdva qrqltdamsq lvvacesvhr
      121 lsvtprfrql qarlatsagr iaaardryds aarrynaslh dfpfslaqai hadagkptfs
      181 vrdgspvhrr prtdfgalrg slrv
//
LOCUS       WP_176052559             753 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Paraburkholderia caribensis].
ACCESSION   WP_176052559
VERSION     WP_176052559.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..753
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=81662
     Region          54..751
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mnsslqsssa asagatdaaa tladeraakp asgggalaas lshkrssela difaadglla
       61 rqiegyrpra sqiemarava aameasgram pepamfeaqk rparrlqqsa saaqseseda
      121 atadsnsegg entliveagt gtgktyaylv pamlwggkvv vstgtkhlqd qlfqrdiptv
      181 rdalavpvsv amlkgranyl chyylqrtad ngrlpsrqet sylqdiirfa kitrtgdkae
      241 lasvpetaav wsmvtstrdn clgqecphyk dcfvmqarre aqqadivvvn hhlffadiml
      301 rdtgmaellp tantvifdea hqlpetatlf fgetlsttqf lelardsvae glghardavd
      361 wvklgaaler sardvrlafk edsvrlsigq lpddhplfpa leavetelda lasalagqse
      421 raeslaalvr rarelqevls gwttpptete rdaasdaaka aeksdpnekv rwievfshtv
      481 qlhetplsva pifakqragv prawvftsat lsvrgdfahy aaqmglnsrr smtlpspfdy
      541 gtqgllyvpr nlpqpsspaf tdavfdaalp aieasgggvf mlcttlravd rianklrdvi
      601 esrgwnmpll vqgdasrtel ldrfrsygna ilvgsqsfwe gvdvrgdals lvvidklpfa
      661 ppddpvlsar ldaltkkgls pfavhqlpqa vitlkqgagr lirsetdrgv lmicdtrlvd
      721 kpygrriwqs lppfkrtrei dvvreffeek aqa
//
LOCUS       WP_176052702             352 aa            linear   BCT 11-JAN-2025
DEFINITION  permease [Paraburkholderia caribensis].
ACCESSION   WP_176052702
VERSION     WP_176052702.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..352
                     /product="permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=36567
     Region          78..346
                     /region_name="YraQ"
                     /note="Uncharacterized membrane protein YraQ, UPF0718
                     family [Function unknown]; COG0701"
                     /db_xref="CDD:440465"
ORIGIN      
        1 mnatrptsss aaptwpifvl laiaglfyvk wfpyynraft aasthsigas ilmgkaaspp
       61 apswnaalay alaygkaiwq amvlglllgs avqallpahw varllgktgf gsvaagglla
      121 vpgmmctcca apvvaglrar qaspggaiaf wlgnsvlnpa tlvfmgfvlg whwaglrlvl
      181 giamvfglgy lanrlvtpte tqvadarlve ligeqrdgnp farwlsifar mavrlvpeyi
      241 vlvlllgaar awlfpqvgpe igndivwiva lavagmlfvi ptagevpivq amlslgmgvg
      301 pagallmtlp pisvpslaml arsfrprvlt vvavgvvafg vlagllaval gf
//
LOCUS       WP_176052659             215 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Paraburkholderia caribensis].
ACCESSION   WP_176052659
VERSION     WP_176052659.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006783
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..215
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=22075
     Region          6..215
                     /region_name="YwnB"
                     /note="Putative NADH-flavin reductase [General function
                     prediction only]; COG2910"
                     /db_xref="CDD:442154"
ORIGIN      
        1 msktlkialf gatgmigsri aaeaarrghq vtafsrnpgr apadvanlka aqadvtdaas
       61 vaagarghdv vasayappqd nlaqidkatr alvegtraag ikrlvvvgga gslevapgkq
      121 lvdtegfpda ykaialahrd vlpilraasd ldwtffapaa liapgerkgt frtganaliv
      181 daqgnssisa edyavafvde leqgrfvhql ataay
//
LOCUS       WP_176052710             383 aa            linear   BCT 11-JAN-2025
DEFINITION  C40 family peptidase [Paraburkholderia caribensis].
ACCESSION   WP_176052710
VERSION     WP_176052710.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..383
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=38908
     Region          <18..176
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mlrlalslll vallaacsga pqktvrssgg pyassggayr tappgfprfv dhsigreeis
       61 iqamslvgvp yrwggntpds gfdcsglvhy vvqraasvnl prttadmssr gdsiepdeia
      121 pgdliffntt grphshvgiy vgklrfvnap stggtvrldy ltnpywakrf dgirrvapal
      181 nkptttpfda psyeaaapvs ptpavaaaea apkpaapdma ggaygssrga sgayaaqtra
      241 qpapvasqgi vapaataaas vdqfeppppg msaaqlqara agamsptpva spvaataada
      301 tysrvygsaa rpasapdaid aaadayeppp paavaarqar qaqvsgdsre lggvqimras
      361 tasrpvpapt qtnddpiagf any
//
LOCUS       WP_176052727             180 aa            linear   BCT 11-JAN-2025
DEFINITION  nucleoside deaminase [Paraburkholderia caribensis].
ACCESSION   WP_176052727
VERSION     WP_176052727.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Ko,T.P., Lin,J.J., Hu,C.Y., Hsu,Y.H., Wang,A.H. and Liaw,S.H.
  TITLE     Crystal structure of yeast cytosine deaminase. Insights into enzyme
            mechanism and evolution
  JOURNAL   J Biol Chem 278 (21), 19111-19117 (2003)
   PUBMED   12637534
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Carter,C.W. Jr.
  TITLE     The nucleoside deaminases for cytidine and adenosine: structure,
            transition state stabilization, mechanism, and evolution
  JOURNAL   Biochimie 77 (1-2), 92-98 (1995)
   PUBMED   7599282
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10101196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..180
                     /product="nucleoside deaminase"
                     /EC_number="3.5.4.-"
                     /GO_function="GO:0001882 - nucleoside binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0019239 - deaminase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009116 - nucleoside metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=19816
     Region          30..126
                     /region_name="nucleoside_deaminase"
                     /note="Nucleoside deaminases include adenosine, guanine
                     and cytosine deaminases. These enzymes are Zn dependent
                     and catalyze the deamination of nucleosides. The zinc ion
                     in the active site plays a central role in the proposed
                     catalytic mechanism, activating a...; cd01285"
                     /db_xref="CDD:238612"
     Site            order(48,66,72..74,102,105)
                     /site_type="active"
                     /note="nucleoside/Zn binding site [active]"
                     /db_xref="CDD:238612"
     Site            order(70,75,79,103..104,107..108,111..112)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238612"
     Site            order(72..74,101..102,105)
                     /site_type="active"
                     /note="catalytic motif [active]"
                     /db_xref="CDD:238612"
ORIGIN      
        1 mslshpskqn asdfpeqgla ptreqivrhl rhasvvaera tlmghhpfga ilvgpdqetv
       61 lieqgnvdtv nhaesvlari aalnftpqyl wsctlyttve pccmcagtay wanigrvvfg
      121 mteerllqat gnhaenptms vssqyvfdhc qkrvdligpv teveeeimqv qhafwalrsg
//
LOCUS       WP_176052748             594 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Paraburkholderia caribensis].
ACCESSION   WP_176052748
VERSION     WP_176052748.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..594
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=64667
     Region          60..594
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mkigkrlaal pltalvtlas naqqtptpae aaaaaranae qnqqlqqqrd aqqreqtvna
       61 pavrstvpka gvypdlphes pcfridtfal dvpatlpdia rkhgasnlpl dpfwfarewl
      121 dhyrgecigk sgldiltkgl qqtilsrgyv ttrvllleqd lstgtlkval vpgvvrhlrf
      181 adpemrgtwk safpardgdl lnlrdleqgl eqmkrvasqd vdmkieptdt pgesdivlnv
      241 khskpwtfvv sadnsgtdat gkwqgnvslg idnplglndv fmvganqdls fgnktlgshg
      301 fngsysvpwg ywtatlsgnt ntyyqnvagv nqtfvssgns qtatfrlarv lsrsqsdvlg
      361 ayvqlskrfg esfiegttip iqdrnntfie lgatdrhyfg gaqfdgtlay rqgihglgat
      421 gdpnpnlynp gdqatqhpty lykmatldan lsipfaiasq nfryvttfhg qftndllfyi
      481 ddltigsryt vrgfdgetml aaekgfywrn elqwpvfqtg qtlyagvdyg rvfgpntgil
      541 agtqlagavi girggipaky agfsydlfag tpiykpagfp tsrvtvgaqa tmqf
//
LOCUS       WP_176052768             319 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Paraburkholderia caribensis].
ACCESSION   WP_176052768
VERSION     WP_176052768.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888684
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..319
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34995
     Region          24..230
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd16282"
                     /db_xref="CDD:293840"
     Site            order(79,81,83..84,166..167,185,222)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293840"
     Site            order(79,81,83,166,185,222)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:293840"
     Site            order(79,81,166,185)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:293840"
ORIGIN      
        1 makafasqad leekkitwtq lsenayayta egdpnsgvvi gddgvlivdt tatpamaqdl
       61 iakirsvtdk pikyvvlshy havrvlgasa yfaegaqqii asrgtyemiv ergeadmkse
      121 ierfprlfag vetvpgltwp tlvfekeitl flgklevria hlgaghtkgd tvvwlpsqkv
      181 lfsgdlveyd aacycgdaql eqwpatleal ralnadmlvp grgpalttpe evnkgldytk
      241 dfvttllqsg reavadkldl kaamahtrka mdpkfghvfi yehclpfdvs raydeasgit
      301 hpriwtaqrd kdmwdalqa
//
LOCUS       WP_176052783             223 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Paraburkholderia caribensis].
ACCESSION   WP_176052783
VERSION     WP_176052783.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..223
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24581
     Region          1..207
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mkifhvdssa krersnsral srqfienlra egvdvevdyl dvtvdtpphv tevfaiatyk
       61 qehertadmr atlaasdalc krlleadafv fampmynwsm psafkafids atrpgityka
      121 dadgnivgql nrqkvlfitt rgadlrpgnp fssmdaltpa lkaafafiga ndprfvdaqp
      181 lqfsdqears dalkrahael agvaadwaaw erarvgrelq etv
//
LOCUS       WP_176052799             314 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176052799
VERSION     WP_176052799.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..314
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35322
     Region          3..61
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..281
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,103,142,156,158,217,234,261)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(105..106,108..109,112,116,118..124,185,211..215,
                     222..223,226)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdlndvrifv svvqtgslmn aasrmgvpla tisrrirale kelnvqller sargtrltda
       61 garlyqhasl gveilkdgee avvsdqamlk grlrlslppa fdiwwdllhd fqrrypdirl
      121 hvytterrvd lieegidval rvgaiaheam varrmlsyrh vlvaspqlie rfgmphepaa
      181 lsrlpcalwn rapndantwq lgkttvephi vlttndyaql rhralngefv teippflaad
      241 sirqgrlvpl lpayplpdqq vnllypshrh psaivrtyle fcqsriawfv dqcaidwkss
      301 sqdasapdsl aqsk
//
LOCUS       WP_176052827             219 aa            linear   BCT 11-JAN-2025
DEFINITION  FMN-dependent NADH-azoreductase [Paraburkholderia caribensis].
ACCESSION   WP_176052827
VERSION     WP_176052827.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..219
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23954
     Region          5..203
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mnslnvllld csprrdnsts rhftrhllpa maellgrdir itrrelgaqp lppiteayae
       61 slvlpgevak erfgaalavs delireldqa dmlwistpvh nftvpavlkn widhvvridv
      121 tfkagasgkv gllrdrptfv avtaggamfr epayqpdffr pylsavlgvi glkditfmqa
      181 aglvstdepl alveakaaqw lrdnpqrhet ceaspssia
//
LOCUS       WP_176052903             140 aa            linear   BCT 11-JAN-2025
DEFINITION  ester cyclase [Paraburkholderia caribensis].
ACCESSION   WP_176052903
VERSION     WP_176052903.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Sultana,A., Kallio,P., Jansson,A., Wang,J.S., Niemi,J., Mantsala,P.
            and Schneider,G.
  TITLE     Structure of the polyketide cyclase SnoaL reveals a novel mechanism
            for enzymatic aldol condensation
  JOURNAL   EMBO J 23 (9), 1911-1921 (2004)
   PUBMED   15071504
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..140
                     /product="ester cyclase"
                     /EC_number="5.5.1.-"
                     /GO_process="GO:0030638 - polyketide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=15688
     Region          21..137
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
ORIGIN      
        1 mtltpvqmdg kieehigfer rddvegvlat ltpdvehdvv gwpagpvrgr devrpfyeal
       61 fadlsesrve clrrlhgdgf vvdeslwrgk apgrpfgleg rgrplefrml hvlefaesgq
      121 iarenvwvdl aaiirqlpqs
//
LOCUS       WP_176052898             308 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176052898
VERSION     WP_176052898.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34268
     Region          4..61
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,222,239,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     216..220,227..228,231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdvnaltllv eiidagnlse aarrlkmtra nvsyhlnqfe ksiglqlvrr ttrrveptei
       61 glklyehgra irnsllaake sistlgeslq grvrlsvpsg ygqlvmsawl iafrreypgi
      121 vldvmfenrv edllrdevdi avrvmseppq nlvardmgtv rwvacassay aaqhgmpvql
      181 delrtapiit savvgrqlrv aaylrderhe vllepglise nflflrdail aglgvglvpd
      241 yvvhddigrg dvvtaldpwr lsifgtnmym lympnlhhtr atsqfiefml dearkagrga
      301 tparhapl
//
LOCUS       WP_176052930             397 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Paraburkholderia caribensis].
ACCESSION   WP_176052930
VERSION     WP_176052930.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 397)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 397)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 397)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 397)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 397)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..397
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44060
     Region          1..390
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 mlntlainny rsirelvipl trlnlitgpn gsgksniyra lrllastaqd giiaplareg
       61 glnsvvwagp edrsgrmrrg eipmphrakg tpasrlklgf ageefgyavs mglvtsagne
      121 drdttssfal dpefkresiw agpvlrpasl lvdrdgsvvr rrldqgwdvl thqlpryesl
      181 fsevgrdkls pevfsvreai rgwrfydhfr vdadslarqq qigtrtlvld hdgrdlaaaw
      241 qtireigdre aldeavndaf pgawveiesq pggffylrfh qegllrplga aelsdgtlry
      301 lllcaalltp rppelmvlne peaslhpdlt malgrlirra arnsqlwvvs hstrlaaale
      361 ededcnpiil ekvfsettip gqhlldrpaw swadgkn
//
LOCUS       WP_176052931             289 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Paraburkholderia caribensis].
ACCESSION   WP_176052931
VERSION     WP_176052931.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..289
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=29418
     Region          1..286
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mktvgviglg nmgrgmalsl krggfnvlgf daapgvadkl qedgvqaras isditrdadv
       61 lilslptsdi veqvvlgegg vaasakpgli vvdtttaepg strkvaaala erkvgfvdgp
      121 vsggpkgaat atmtmvlggs dadvaavepi lavmsakrvh vgpvgaghvt kiinnmltgv
      181 hllaaseavr aaeangvdpq klvealnggs gknsatltny ptwifngkfd sgftmklmrk
      241 dvrlamalld sadatapiak eagrlwaasa dsigdaedfn rivqfidkq
//
LOCUS       WP_176052944             665 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Paraburkholderia caribensis].
ACCESSION   WP_176052944
VERSION     WP_176052944.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 665)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 665)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..665
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=72205
     Region          13..649
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mrddakttgs ltsresgwlt psiqkahers etfglnaamr pdydvlthge lrmkleqnlv
       61 lcahatpvme tlreqiantq smivltdaqg lilhsigddd flqraekval kaganwaeer
      121 qgtnaigtai aertatvvhg dqhylaanrf ltcssvpild pygdlvgvld vtgdhrsyhq
      181 htmalakmsv qmienhlfan tfrntlqiaf hgrpeflgtl megimaftcd grflsanrsa
      241 qfqvglplaa mrahtlsslf glttpelidr lrashghhit ldlnngtvvc anvefrrptl
      301 gsetawpada aasarpaaar apltktaspa napsrldsld tgdpqvravv akvrkvlgkd
      361 ipilitgetg tgkellaqai hndsprragp fvavncasip enlieselfg yedgaftgar
      421 rkgavgkllq anggtlflde igdmpyplqv rllrvlqerv vdplgssksi pvdiaiicat
      481 hrnlremivq nrfredlyyr lnglvvrlpp lrertdlaiv iermlqsvps deiadaplsv
      541 addvktlfeq cawpgnfrql gnllrtaaam veddgqirre hlpddffddl rsssalaara
      601 adyplplhda rmqdvqacai aaavarhngn vsaaaralgi srntvyrkmp slcaadppng
      661 gasen
//
LOCUS       WP_176052946             335 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176052946
VERSION     WP_176052946.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 335)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 335)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..335
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36288
     Region          2..204
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          236..319
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdavsdvlrv vrlggavylh aeltapwcmi gradqslcta ylpksdrvvs yhlitegtcw
       61 arlpdcsepp icvgagellv vpqgeahimg saldltpvpa gpliesqlaa mpgevlnlsy
      121 ggggartsll cgflacddal tnpvlgslpr lfkvdvrnda hsawieaslr yaateaaqrr
      181 agsaivlsrl sellfvwavr rciddlpadr knwlagvkdr fvgralsilh aqpaynwtvd
      241 elarkvglsr safaarfsel lgqppmqyla rwrlivaaqe lsysskaiaa iaeevgyese
      301 safhrafrre fgqppatwrk rhshvngtda lapsq
//
LOCUS       WP_176052953             249 aa            linear   BCT 11-JAN-2025
DEFINITION  creatininase family protein [Paraburkholderia caribensis].
ACCESSION   WP_176052953
VERSION     WP_176052953.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Yoshimoto,T., Tanaka,N., Kanada,N., Inoue,T., Nakajima,Y.,
            Haratake,M., Nakamura,K.T., Xu,Y. and Ito,K.
  TITLE     Crystal structures of creatininase reveal the substrate binding
            site and provide an insight into the catalytic mechanism
  JOURNAL   J Mol Biol 337 (2), 399-416 (2004)
   PUBMED   15003455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..249
                     /product="creatininase family protein"
                     /EC_number="3.5.2.10"
                     /calculated_mol_wt=26806
     Region          2..246
                     /region_name="ArfB"
                     /note="Creatinine amidohydrolase/Fe(II)-dependent FAPy
                     formamide hydrolase (riboflavin and F420 biosynthesis)
                     [Coenzyme transport and metabolism]; COG1402"
                     /db_xref="CDD:441012"
ORIGIN      
        1 mllhlstwte ieqylkrsra ivvpigsneq hgptgllgtd wlcpeiiare aeksadilva
       61 ptfnigmaqh hlgfpgtisl rpstfiaaig dwirslaahg fekilflngh ggniasieaa
      121 fsevyveasf akrragfamk lanwwdlegv gelarkqfpe ghgvhatpse iaitqwafpd
      181 aiksadyspk iapsgpirea ldfrarypdg rmgsdpaqas pekggelvrl aasglvreln
      241 afaseplpg
//
LOCUS       WP_176052995             233 aa            linear   BCT 11-JAN-2025
DEFINITION  carbonic anhydrase [Paraburkholderia caribensis].
ACCESSION   WP_176052995
VERSION     WP_176052995.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Lindskog,S.
  TITLE     Structure and mechanism of carbonic anhydrase
  JOURNAL   Pharmacol Ther 74 (1), 1-20 (1997)
   PUBMED   9336012
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10096752
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..233
                     /product="carbonic anhydrase"
                     /EC_number="4.2.1.1"
                     /GO_function="GO:0004089 - carbonate dehydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25799
     Region          11..191
                     /region_name="beta_CA_cladeA"
                     /note="Carbonic anhydrases (CA) are zinc-containing
                     enzymes that catalyze the reversible hydration of carbon
                     dioxide in a two-step mechanism in which the nucleophilic
                     attack of a zinc-bound hydroxide ion on carbon dioxide is
                     followed by the regeneration of an...; cd00883"
                     /db_xref="CDD:238448"
     Site            order(33,35,42,44..46,58,61,83,88,98,101,181)
                     /site_type="active"
                     /note="active site clefts [active]"
                     /db_xref="CDD:238448"
     Site            order(42,44,98,101)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238448"
     Site            order(43..46,48,50..51,53,58..60,62,64,78..79,82..83,121,
                     181,183..184,186,188)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238448"
ORIGIN      
        1 mnhpkrllls nlawsqevsa repefftela rgqqprflwi gcsdsrvpae rvtnaqpgel
       61 fvhrnianly tsddgntssv ieyavhalkv ehviicghhh cggvraalsp psdalpivnr
      121 riaglrelae rhrdelhaia dfdervdrfa elnvieqvrl lrespivrra prppqvhgwi
      181 fglraglitq ltdmdeardi aeahaearae araeghaqah aeaspsvavr daa
//
LOCUS       WP_176053020             235 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paraburkholderia caribensis].
ACCESSION   WP_176053020
VERSION     WP_176053020.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 235)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..235
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25486
     Region          9..234
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msepinatpp lvdirhlvks yrrgvqtvpv lsditlaige gdfialmgps gsgkstllnl
       61 iagidrpdgg elrvggldit rlnesalaqw raahvgfifq fynlmpvlta fenielplml
      121 trltrkerre rvalvldmvn lgnrahhyps elsggqqqrv aiaralitdp tlivadeptg
      181 dldrasaeev ltllqrlnre lgktiimvth dahaagaara lvhlekgeli dgtar
//
LOCUS       WP_176052994             341 aa            linear   BCT 11-JAN-2025
DEFINITION  S1C family serine protease [Paraburkholderia caribensis].
ACCESSION   WP_176052994
VERSION     WP_176052994.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..341
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=35388
     Region          68..329
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mgsrprfvdd lsgalpsaaa agssdddall daysrtvvda lervraavvf itaerrvpga
       61 perharagtg sgfiftpdgy lltnshvvhg athirvqlad gtkfdadlvg ddphsdlavl
      121 rigspeplph valgesgklr vgqiaiavgn plgleqtvta gvvsalgrsl rsnsgrmiyd
      181 viqtdaalnp gnsggplins agqvigvnta iipgaqsisf ataidtakwv imqifahgrv
      241 rrayigvagt tfalprrvqr yfalesesgv rvmeivkgsp aalgglrtdd tivavdgqvv
      301 egvdalqrvl dgsrigrsvs vsvlrgaqrv evvvvpveqs v
//
LOCUS       WP_176053044             421 aa            linear   BCT 11-JAN-2025
DEFINITION  leucine-rich repeat domain-containing protein [Paraburkholderia
            caribensis].
ACCESSION   WP_176053044
VERSION     WP_176053044.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..421
                     /product="leucine-rich repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=46280
     Region          98..>410
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          109..150
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          173..194
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          195..239
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          217..231
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          240..261
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          262..283
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          284..305
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          306..327
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          328..349
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          350..371
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          372..393
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
ORIGIN      
        1 msdtppsstn pntedlpspt wrratpwaig aavvllliil lvafgtsrrs pderalgelg
       61 fikatcsnsd gsaappdsac lalrakptlt asevaaaiph lkdsdrkiel nlsntqienl
      121 dplkeldtld sldltgtpvw nldalkdmhs lkrlvlhrtd veniaalkgl tglqsltlwd
      181 trvsnldalk nltdlrqldl rdtqvrdldp ledlphletl klggarnvrd idalgqltal
      241 ksldlnetqi dsiaalkklh dmqalylant plrdidvikg mpslktlvld gskvddidam
      301 rglrqldtlv lartqitsie alkeltalqr lnladtrien idalkdlknl qmlnlfrtrv
      361 rnidalkslt nlqelylant pvedidvlkg ltglrelvly gtkarnvdel kaalpktriv
      421 w
//
LOCUS       WP_176053048             383 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Paraburkholderia].
ACCESSION   WP_176053048
VERSION     WP_176053048.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..383
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38773
     Region          9..373
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(19..20,23..24,27,59,109..110,112..114,117,136,
                     139..140,143,208,211..212,215..217,220,248,252,301..302,
                     306,310,326,329..330,333..334,337)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 mtfdqpaarl atrlaflvag fgvacwaplv pfakqrlgvd dgvlgllllc lglgsviamv
       61 itgalsaryg skpiivaagf glavilpflt ivstpltlgi vllafgaslg sldvamniha
      121 vdvermegrp lmsgfhalfs iggfagsmlm tfllsmhiap lestllcavp mlgaiavars
      181 rliqtahake gplfaaprgi vlvlagltai tflvegalld wsallitgag lvaaaqggvg
      241 ymifsvamta grlggdavta rvgdramvfw ggwvamggfv vlltapstai amagflligl
      301 gasnvvpvlf rqagaqramp salavvaitt tgyagnlvgp agvgfvangv glpgafwmla
      361 allclvpcca rlvtakrsqv evs
//
LOCUS       WP_176053058             339 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176053058
VERSION     WP_176053058.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..339
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37281
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdkllamkvf tkvvemnsfa raadaldipr asattiiknl eanlhtrlmq rttrrlnltp
       61 egagyyercv rvladideie dslanvvkgp rgklrvdmpg slgrlivmpr leefreryph
      121 velmlgfgdr hvdliqegvd calrvgnldd stlvarrlga lstitaaspa ylarygeprs
      181 leeleqhvav hyfssrtgrt lglnfdvnge srdmkmnggl avndadayvm cgvngagiiq
      241 apsfmlashi eagelkeila pwkvrsmpls avyphnrhla pkvrvfvewv aeicaqspla
      301 farnrppvdg ardvrvvasq sprladtvds demdmavst
//
LOCUS       WP_176053068             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176053068
VERSION     WP_176053068.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34296
     Region          7..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,219,
                     221..224,231..232,235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdkvynmsif akvvemgsft avanhldttv gnisravsvl eqnldtrllq rstrrllitd
       61 agrrfyersi ailadieqae aeardaqlep rgklrvhtvp gigrrlvara alayrraypd
      121 vsvdlllsqr mpnlleeqld vavviartlp dsayvsqkig vshcilaasp aylaqhpape
      181 rpedladhtc vllgtvdysp dewclesagg rvvhrptgph fgvndmdams ttlkdgagig
      241 liaafsaidd lrngslvrvl pryhtyernv yavyssrrfv dakikrfidv lkadvggeln
      301 ayaaelgigi eqv
//
LOCUS       WP_176053109             694 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Paraburkholderia caribensis].
ACCESSION   WP_176053109
VERSION     WP_176053109.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..694
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75971
     Region          8..688
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mvtdgatvlh vgktviaall algiamllel psprtamttv fvlmqpmsgm vlsksfyrgm
       61 gtalglvaai giaalfpqtp elyltaiaiw tgyctaaavr qrhfkwyayv lagytailia
      121 iptvtapntv ymsaltrvae vtigilcsag vsallfpiss sdallqalrs rysdltklas
      181 eallgtmswd qfekrfgslv dgmvgleatr tfaifegplm rsrsrriarl nnefshacsr
      241 lhalyqllrr lrdsnstial ellhpfveql seilgesrdf tltfddtpnq iasrfrsfrs
      301 tiasraqaqr smlratdpda cmdydtatel llrfvaefir yartyeslka dshaleksnv
      361 eytvntspyv vaftflrtva avgvaawfwe atawpsggfa vigsaiacal tslspnaakq
      421 awqialgaig atavgylytc yvypnidgyp llcafltpal afgaylvvrp ggaaygvgfs
      481 vffcllagpd nvvvydpdtl innglaivas igvsavifav vfpsqmpwlv grierelraq
      541 vpyafnselr gldqrfhsit hdimaqlrpv lvndskrhrv alqwllatle vgnavidmrr
      601 qmhrlqrpge pspgwfgeid vvrdalsnlf lepngqallr aydavddail avqtetahte
      661 dvlkaeharr ilaslhlfrt vllddaipvr drir
//
LOCUS       WP_176053118             349 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Paraburkholderia caribensis].
ACCESSION   WP_176053118
VERSION     WP_176053118.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 349)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..349
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=37693
     Region          2..349
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mldsaginve iydsisaagl tdiaasnlae egesgedqas tkqqlksliq ipvsigsvqv
       61 grlglegkal slnavdhevl glmgshvvli lhiehlnrll drqaemrspt ldsligirdg
      121 glheaklsil gklcatvvhe tkqrfgsiaa ngaagirwln rdtpdieeai tsfrsvvrda
      181 dqsgeiirsv salyrgseps krpfdinesi mgalaliqsd isiyqiefea tledapivvs
      241 gdevlinqvl vnimvnaves lksvddnvrk lsvrswrenm rrarieivds gigvteqdkr
      301 aprkakkpgs ssfglgldfc rdvlqahnat ielhqreprg civgislpi
//
LOCUS       WP_176053124             156 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176053124
VERSION     WP_176053124.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..156
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17229
     Region          4..144
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mgyrkidstd arildylqrd sgltnvelag rvglspspcl trvkalerdg visryvavld
       61 paalglhvdv firvrlkeqa retmaafeda mklrdevidc ylmsgeadyl lrvmvpdvrs
      121 lerftvehla rlsgvasiqs slslkevksr apipvp
//
LOCUS       WP_176053131             244 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator transcription factor [Paraburkholderia
            caribensis].
ACCESSION   WP_176053131
VERSION     WP_176053131.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..244
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=26731
     Region          13..207
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 msatqtyppd akvlivdddr amrdglsnlf rsvalqvhtf stpteliafe cspsptclvl
       61 dvrlpgqsgl alhqtivgsa pempvvfisg yadtptavsa lkagaidfld kpfqeldlls
      121 avgrglqlsh erlehtaims iltrsfeklt hrereimall stglrnkhig mrlglsevtv
      181 kmhranvmrk leieslvdlv riadalgmhh wdqvhdshsp svscrpnegl rlltaskrrs
      241 aapr
//
LOCUS       WP_176053137              96 aa            linear   BCT 11-JAN-2025
DEFINITION  putative quinol monooxygenase [Paraburkholderia caribensis].
ACCESSION   WP_176053137
VERSION     WP_176053137.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..96
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10428
     Region          5..80
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mtvkiliati tttpehvdtv ktalvaavaa vrkeagcery dlhhdadnqn rfvmverwsn
       61 qtaltdhang aafqklaatl tdratleiin lveisq
//
LOCUS       WP_176053165             157 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176053165
VERSION     WP_176053165.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..157
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17641
     Region          1..141
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mkldrvdvri lqalqqdahi kaadlaeslg lslspfyrrv rlleergiis shvtlldqek
       61 agfpvsayvs vavdkksapl lktfeqeign feevmecylm tgafdymlrv vapdiagler
      121 fvmeklakid gvkdintsia lrrvqykttl pvriree
//
LOCUS       WP_176053249             310 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176053249
VERSION     WP_176053249.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..310
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34621
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..284
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,162,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mirlddlalf irtaalgsfs naareadllp gqvsaaiqrl ereldirlfa rstrslrlta
       61 egegylpyah evlavlqagh erihdeqral qgtlkiaaps dlgrnvllpw itefreahpk
      121 lslklflsdh ltdvyrdpvd iairygvaen asyvalplae nnrrvlvasp syinrfgrpk
      181 kldellmhqc lpyalggray dkwnfpadgv rrqvavkgvl qcddadiarr waidgrgiay
      241 kswidvcrdv qagmlevlip dqpgeavpls lvcphrkqfs pavrqlygel rgritalasa
      301 lndyvifkef
//
LOCUS       WP_176053236             347 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Paraburkholderia caribensis].
ACCESSION   WP_176053236
VERSION     WP_176053236.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Thorn,A., Egerer-Sieber,C., Jager,C.M., Herl,V., Muller-Uri,F.,
            Kreis,W. and Muller,Y.A.
  TITLE     The crystal structure of progesterone 5beta-reductase from
            Digitalis lanata defines a novel class of short chain
            dehydrogenases/reductases
  JOURNAL   J Biol Chem 283 (25), 17260-17269 (2008)
   PUBMED   18032383
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..347
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=39184
     Region          13..298
                     /region_name="5beta-POR_like_SDR_a"
                     /note="progesterone 5-beta-reductase-like proteins
                     (5beta-POR), atypical (a) SDRs; cd08948"
                     /db_xref="CDD:187652"
     Site            order(13,32..34,47..49,71..73,110..111,140,163..164,166,
                     173..175,294)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187652"
     Site            order(114,140)
                     /site_type="active"
                     /db_xref="CDD:187652"
ORIGIN      
        1 mktvvvagav gvigrgvlvh yetkgvdlva vsrrapdfpt rarhlavdll drescealla
       61 qvpeathlvf aayqekptpa elvevnlrml knmvevmekh apnlqhvtlm qggkaygvhi
      121 gpfpspakes dprhmppnfy ydqedflrer svgkswswta frpegvagia vgnpmnllmv
      181 iavygtlaka lgvpmsfpgs raaydalyqi tdtrilasav dwagetdacr geiynitngd
      241 yfrwsrvwpr laeffevsvg epfpmllqqm mpdkaelwnr lvkkhnlrdy pydqivswkf
      301 gdmifktnfd nisstikark hgfhdcidse emyiemltdl reqryip
//
LOCUS       WP_176053280             241 aa            linear   BCT 11-JAN-2025
DEFINITION  GGDEF domain-containing protein [Paraburkholderia caribensis].
ACCESSION   WP_176053280
VERSION     WP_176053280.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 241)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 241)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 241)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..241
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26202
     Region          <72..239
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mprissvdap asdapdlfqn enealekara ihataaadad dyrqslgeli ghferlmret
       61 rrligrsdra eremqalaqq lahrathdal tgvfnrsavi eraskalrrd savmiildid
      121 efkrvnddfg hpagdavimg ivaclrrivg ergfigrvgg eeftvllpgh evddalrlae
      181 nmreaigkhv faspvdrhit asfgvsanpa gtsfdtaygl adaalyrakr ggrnrvefas
      241 p
//
LOCUS       WP_176053387             743 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Paraburkholderia caribensis].
ACCESSION   WP_176053387
VERSION     WP_176053387.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 743)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..743
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..743
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=79956
     Region          6..736
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mneqsigqsv rridgrlkvt gaapytadrn lpgmvhaygv fstvasgril ridtteasrv
       61 pgvidifhha hfprlyrvpk spissatilt atitdesrlp fedgtvyyag qfvalvvadt
      121 fehareaayr vrveyatnra vagldqgval seprdggrgh srgapepafn eaehridlty
      181 rtpvethnpm emhasvaywq gdslhlyeas qgvtvhrnti arvfgltpeq vtveapfigs
      241 gfgsklfmwp hsvaasaaar avgrpvklvv praqmftttg hrpetlqrlr lsadasgrlt
      301 slrhesintt sftdaftenc ggvsrslysc pnvlvshktv qvnqgsstsm rapgaapglf
      361 alesaidela eqvgmdpmaf rllnistrde aanlpwssnh lreaieqgsq rfgwanrdlr
      421 pgavrdghev igygmaacnw dayrtpaear vqlrddgsay ltcaiqdigt gtytiaaqvv
      481 adltglpver ievklgdssf paapvsggsw atasvipaia eatrnaiaql rtfatannav
      541 fasekpesir fesgrlvsgt rsidfaavlk aqrlanaegy ahtpgaptgq ysfrsfgahf
      601 vevrwdpgis rlrvarvvsa idvgrvinpl tarnqvegai vmgigmalfe ateydprtgk
      661 pgnnnyaeyp vpvhadqpdi dvilldypdl alnefgargi geigitglaa avanavhnat
      721 gkrirdlpit ldklidvdhp vfa
//
LOCUS       WP_176053472             381 aa            linear   BCT 11-JAN-2025
DEFINITION  YncE family protein [Paraburkholderia caribensis].
ACCESSION   WP_176053472
VERSION     WP_176053472.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..381
                     /product="YncE family protein"
                     /calculated_mol_wt=38369
     Region          5..190
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          <235..381
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mkkpllvvll vatavlaacg ggdnsastpa sstpapapsk llttiavpns ttpafsfdig
       61 yteagryyla drnnksvdvv dtksntliaq itggftgaga stdasgpdgi vgvtgtstly
      121 vgdvdsvkiv dtaamktvkt ipistsgsrv degcydpddh limfaspget ppyvtfistt
      181 tqavvskltf tgssgleact ydaasksfli nndgttanpt geldvitass vtsgtpavsk
      241 afslgkceps gialgpnsdv ligcdpsagn plitlildrn tgaqlasipf ggtdqvaydp
      301 gsnryflpar hwvtsgtaaa sgftpqmgvi dgatrkllyt vavgtgahsv aidsglgqvy
      361 vpfqpgaaaf pnggisvfat k
//
LOCUS       WP_176053477             310 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Paraburkholderia caribensis].
ACCESSION   WP_176053477
VERSION     WP_176053477.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..310
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31542
     Region          2..307
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtilviaehd nvsiktatln tvaaaskigg dvhvlvagsn aqgaadgaak iagvskvlla
       61 dapqlaegla eniegtvlni ardylhilap ataygkniap riaahldvaq isditavnst
      121 dtferpiyag naiatvqsgd pvkvitvrtt gfdpvaaegg sasieeieaa adagisafvn
      181 reltkldrpe ltsasvivsg grglgngeny tkvlepladk lgaalgasra avdagfvpnd
      241 yqvgqtgkiv apqlymavgi sgaiqhlagm kdskvivain kdpeapifsi adyglaqdlf
      301 eavpelttli
//
LOCUS       WP_176053429             272 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Paraburkholderia
            caribensis].
ACCESSION   WP_176053429
VERSION     WP_176053429.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..272
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27072
     Region          9..267
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mehviassaa lglvvglila ltgaggaila vplllfvlhl niaeaapial lavgvsaalg
       61 almglqariv ryraaalmav tgtafspvgl wlahrlpngp ltlvfagvla yvalrmfrqa
      121 ttgtphevrs gaalqpcqln ngtgrfvwts actralafag igagflsgll gvgggfvivp
      181 alrkatnapv ptimatslav itlvsasgvi staisghmnw pvgapfaaga lggmlagrlv
      241 asrmsanrlq qgfalvagli avgmvakvam sv
//
LOCUS       WP_176053480             557 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Paraburkholderia caribensis].
ACCESSION   WP_176053480
VERSION     WP_176053480.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..557
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=59808
     Region          1..527
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mydyvivggg pagcalaarl sedasnrvll leagpadtnp yihmpvgffk mtggpltwgy
       61 rtaaaaetqr rqipfaqgrv lgggssinam vytrgqpsdy dawerdgctg wgfrdgvlpy
      121 lrrmednerl cneyhgvggp lgvsdlitvn eltkafvrag qeaglpynsd fngaqqegvg
      181 vyqvtqrngr rcsaavgylr dararsnltv ktnclvsriv iekgravgve faeqhsrtnv
      241 vvaraerevi vtagaigspk llmlsgigrp adleragvkp lhslkgvgen lqdhfdidiv
      301 yelnghysld kyakkhmmll agleykifnk gpvtsniaeg gafwysdssv ptpdlqfhfl
      361 pgagveagvp pvpsgsgctl nsyflrprsr gsvtlhsadp adapvidpay irdpydlkva
      421 vegirqsrei mtqnalrkfi ksehfpggav rtqaqyeeya qqygrtgyhp vgtckmgvdd
      481 msvvdpqlrv hgieglrvad ssvmprivss ntnaptlmia ekasdlirgr aaaqapaagq
      541 lanhsgraap vaaatla
//
LOCUS       WP_176053481             381 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Paraburkholderia
            caribensis].
ACCESSION   WP_176053481
VERSION     WP_176053481.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..381
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41430
     Region          3..379
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mklsetheqi rdmtrrfsqe virplaeeld reerfpaeiy rqmgelglfg itvpekfgga
       61 gldvtayalv meelsrgyas vadqcgllel vgtllsihgt deqrakfmep llraalrpay
      121 citesdagtd vsgirttatr tadgwelsga klwihnapva dlafvlartd paagkrgmsi
      181 fivdchlagv skgpkehkmg qrasqvgelh fdrvklphda llgqegrgfh immsvldkgr
      241 vgiaalavgi aqagleaale yaqtrkqfgs hiaefqgvqw mladmakdir aarllvhdaa
      301 erletgdras iacsmakcfa gdtavkhsan avqifggsgy irgyeverly rdakitqiye
      361 gtnqiqrtii ardliangas v
//
LOCUS       WP_176053486             461 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Paraburkholderia].
ACCESSION   WP_176053486
VERSION     WP_176053486.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..461
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49321
     Region          21..426
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(33..34,37..38,41,80,138..139,141..143,146,166,
                     169..170,173,255,258..259,262..264,267,295,299,352..353,
                     357,361,377,380..381,384..385,388)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mntspvssgn apvisrsavn rvlvasvvgt aiewydffly atasalvfak lffpsfdpvv
       61 gtiaafgsfa vgylarpfga vffghfgdri grkatlvatl timgvstfvi gllptyasig
      121 vwapillvam rfmqglgvgg ewggavlmvv etaparkrgf fgafpqlgvp lglmlstavf
      181 kavssmpsda ffswgwrlpf llsvaliaig lfirlrvmes pvfeqikasr qvvkapliel
      241 lrrhpkdlvl tigtrfavdi tfnvinvfvl vygttrlgls rglllnaiiv gcafalitlp
      301 lfgklsdvig rrtvfmlgav fvaiygfaff plletrnptl ifvayacgia lsqasvygvq
      361 stwfaelfgt rvrytgaslp yqiagiitsg ptpliatylf atygqtlpis iyiaatgvls
      421 lvcafflaet frrdlsaepe deaaaalgar asahsphplt r
//
LOCUS       WP_176053500             240 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Paraburkholderia caribensis].
ACCESSION   WP_176053500
VERSION     WP_176053500.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..240
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=26999
     Region          4..213
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mrsvhivhah peprsfctam ahdarrvlta rgdnvsfsdl yalefdpvvr asdftrradp
       61 dylvyaleqr halehdtvap dirrevdalm asdilmlvfp lywfsvpalv kgwidrcfls
      121 galyggkriy grggmvgkra vigvtlggre hmfgaqgihg elargmlrhl lqgtlgyvgy
      181 evlepffawh vpycssaera qtlarwsdfv erldaqpcmt mprledyddi fcphpqtasr
//
LOCUS       WP_176053520             681 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Paraburkholderia].
ACCESSION   WP_176053520
VERSION     WP_176053520.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..681
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=73855
     Region          9..675
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mnlpslrdwi fslktflagm lalyiafwfd lprpywalas vyivsnpfvg atrskalyrv
       61 igtvlgalas valvppfaet pyllsavial wtgvfvyisi straarsyvf llasyslsvi
      121 alpalsnplt ifdvavarte eitlgivcas ivgsvffpsr laptliertd swfrdatlyt
      181 keslagravg alvsgsrqkm atsvrgfefl lsqlaydhvs pailarseel qgrmqlilpi
      241 tsaladivaa trqsgpgvpv glnellrdtc rwmdaslged pehgapllrm riaqldpard
      301 elttwqaall tsalsrlrqv vdlwadcrtl rdmivhekan wrprfrhwrv gtrhafldrg
      361 lalfsassaa lvifvsssiw iasgwqdgaa avslgaigvc ffaaldepvp mmitflkcat
      421 tgvvisafyl fvvlpsgqdf gmlviffsfv fvplgllmpr pkwglistlv alttatflgi
      481 dsaydanils flnanlagla gvvfasvmtg virpfgtdaa tarltrsswr dvvlsasals
      541 idqqrdlnar mldrlvqlip rvapseddkh psteslrdmr valntldlrr lsgkfsgelp
      601 lmlnrvlddv rsyyercles ggrqgvpstl aadvdaaigr iladfaadpg apgyklrkga
      661 lhalvglrls lfpaatldva a
//
LOCUS       WP_176053541             145 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Paraburkholderia caribensis].
ACCESSION   WP_176053541
VERSION     WP_176053541.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..145
                     /product="RidA family protein"
                     /calculated_mol_wt=15974
     Region          28..137
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 msqpthtrir mfntkdtypn qtldndlcqa vragntvyvr gqvgtdfngq lvglgdpraq
       61 aeqamknvkq lleeagsdms hivktttflt dvryrepvyq evgkwlkgvf pistglvvta
      121 lgqpqwlmei dviavipdgw tppqg
//
LOCUS       WP_176053569             332 aa            linear   BCT 11-JAN-2025
DEFINITION  transketolase family protein [Paraburkholderia caribensis].
ACCESSION   WP_176053569
VERSION     WP_176053569.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467696
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..332
                     /product="transketolase family protein"
                     /EC_number="2.2.1.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35444
     Region          26..331
                     /region_name="TktA2"
                     /note="Transketolase, C-terminal subunit [Carbohydrate
                     transport and metabolism]; COG3958"
                     /db_xref="CDD:443158"
ORIGIN      
        1 mstlmkkprl ktsamiasia gegqltrsap fghalaelar sksnvigmta dlgkytdlhi
       61 fgkefpdryy qmgmaeqllm gaaagfaheg aqpfvttyav fatrraydfi hqtiaednld
      121 vkivaalpgl ttgygpshqa aedlalmram pnmtvidpcd aldieqmvpa iaahpgpvya
      181 rllrgnvpav ldeydytfel gkakllrdgn dvllissgim tmrslevaka leadnigvgv
      241 lhvptikpld tatilreakr tgrmvivaen htvigglgea vartllgagv tppfrqialp
      301 deflaagalp tlhdrygist dtmaasiktw lg
//
LOCUS       WP_176053575             369 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Paraburkholderia caribensis].
ACCESSION   WP_176053575
VERSION     WP_176053575.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..369
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39140
     Region          3..345
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,57,99,227,299,319,321..323)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,57,99,101,108,175,178,180,227,234,299,319,
                     321..322)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,101,175,178,180,322)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            180
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 msklfskvav gsydiahrvv lapltrmrae sgarpgplma eyyaqrtsrg alligeatia
       61 apngngylga pglyddsqia gwkavtdavh akggkiflql yhagrqsnaq lqpnggrpvg
      121 psevphggva yteagwvpnt pnrpleteei agivesfrta agrgvkagfd gvelhgangy
      181 lfdqflqdgs nkrtdeyggs ianrarllld atravisvwg adkvavrlgp sgswgdmsds
      241 npealftyva deldklgiay lhliepriag nvedeardqq pvaakslrth fhgpiiaagg
      301 fdgesaeail qsgdadlvaf grhfianpdl perlrkglpl npydratffg gtdvgytdyp
      361 fhdeaavaa
//
LOCUS       WP_176053598             367 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176053598
VERSION     WP_176053598.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..367
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=40738
     Region          1..316
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mkiaivvldg vqaldiagal dvfyeanrcl retcqyqvsl vgervghiac snsmqlcvpf
       61 dytafqapvd vlvvtgrpyl snarpkrdfl nwlrdcafqs krigsicsga fllahagvln
      121 grevtvgwsd asalsrecpl arirpdkvlv rdgnlvssag atagwhlcls qvaddwghel
      181 avrvatrlgm dmdhegrpyi dpaarkntfi ekvqryvtdh iadelsieel anavsvsrrs
      241 fsrlfakhaq ktpsafveel rvdaarkilg etdhplktia fkcgfhnath mrmvflrris
      301 atpmqcrqqm rgvqgvhgmp rhrdraeqsv dleataycap gyapllhdgt ghdwaafrmr
      361 rlppsqw
//
LOCUS       WP_176053601             215 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Paraburkholderia
            caribensis].
ACCESSION   WP_176053601
VERSION     WP_176053601.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..215
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23355
     Region          5..212
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mnteltlyes kaspnarrvr iflaekgiei pakavdlgak eqfsaayaai nprlqvpalv
       61 lqdgttigev paiwryieda ypvkpallgt tpqqkaliam werraeldgf aavmegvrna
      121 vaglkgrals gphayeqipe iversqqrva nffadfndrl kqvpfvagde fsaadittlv
      181 tidfaaggmk mnvpaefdtl qawygkvstr psska
//
LOCUS       WP_176053611             280 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Paraburkholderia
            caribensis].
ACCESSION   WP_176053611
VERSION     WP_176053611.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 280)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..280
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30370
     Region          6..253
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 msaqpilklr avgksygatr vlkgidldvm rgeivtligp sgsgkttalr cmnflepyde
       61 gevwikgqll gyrsagrtsr drdseasvae vrrpvsmvfq qfnlwphmsv ldnvaaplvl
      121 akkmrradar akahaalarv glqhkadvyp arlsggqqqr vgiaralaie pevmlldept
      181 saldpelvee vlnvirslaq dgmtmvmvth emsfaakisd kvvfmeagqi vesgppsqlf
      241 gnsrtprlqq flkpwfdrsl sfsapaprtd saaqtsgaps
//
LOCUS       WP_176053612             421 aa            linear   BCT 11-JAN-2025
DEFINITION  M20 family metallo-hydrolase [Paraburkholderia caribensis].
ACCESSION   WP_176053612
VERSION     WP_176053612.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Turner,A.J.
  TITLE     Exploring the structure and function of zinc metallopeptidases: old
            enzymes and new discoveries
  JOURNAL   Biochem Soc Trans 31 (Pt 3), 723-727 (2003)
   PUBMED   12773192
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Nagase,H.
  TITLE     Metalloproteases
  JOURNAL   Curr Protoc Protein Sci Chapter 21, 21 (2001)
   PUBMED   18429165
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10133867
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..421
                     /product="M20 family metallo-hydrolase"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=44222
     Region          25..415
                     /region_name="M20_bAS"
                     /note="M20 Peptidase beta-alanine synthase, an
                     amidohydrolase; cd03884"
                     /db_xref="CDD:349880"
     Site            order(96,107..108,141..142,149,206,209,229,231,305,
                     367..368,393)
                     /site_type="active"
                     /db_xref="CDD:349880"
     Site            order(209..212,215..216,231,242..246,248,251,255..256,
                     258..260,262..264,266..267,269..270,278..285,289..290,
                     292..295,303,305,366)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:349880"
ORIGIN      
        1 mmragthhla ddalraaasv ddtrllasie alaafgarsd ggvnrpalsa tdlearrhlv
       61 gyahalgctv ttdacanlfi hrpgsdaapp vmtgshidtq psggkldgcy gvlaglecma
      121 alndagirtr rplevaiwtn eegtrfapga mgssafveps rmpaylnaad adgvtlgaal
      181 eryrhalpgl psrgdappah afvelhieqg pqlenagvpl givtgiqgvr wyefhcqgva
      241 ahagttpmpm rrdamtlava lrasleaiat slggehtrit fgrwsvtpns intipsdvtf
      301 svdfrhpdah vldsfdaqvs acaqrhgaci aplfthapvr fdatvlarld aachaleapa
      361 lrltsgafhd amylsqhcpt amlfvpsrdg ishnpaeatd arhlvlgara lahtlttlcn
      421 d
//
LOCUS       WP_176053637             414 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Paraburkholderia caribensis].
ACCESSION   WP_176053637
VERSION     WP_176053637.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..414
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=44201
     Region          5..356
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 metdtkrivv igagfaglws algaarklde lrvpadqvev vvinstpyhs irvrnyeqpl
       61 datlvpladv ldpagvrrlq gmvrsidlpd rrvgfesgds stqwirydrl ilaagselar
      121 paipglreft fdvdtfdgaa klhahllalp erpeapgryt vvvvgagltg velaaelpar
      181 lrgiaggnas aevrviladr sakigqamgg aqpvieealr aqgvelrpgv slesvtrggi
      241 qltnsepida atvvwcggmr aspltaqfpv tpdafgrvpv daflrvdsvp gvfaagdcar
      301 ilidgerpsv mscqhsrpmg rhaghnavcd llglamlplc idwyttildl gpwgavyteg
      361 werrlasqga aakqtkrtin ceriyppstk credilqaaa pvvqappytv rdad
//
LOCUS       WP_176053744             328 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176053744
VERSION     WP_176053744.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..328
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34920
     Region          9..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          99..319
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(113..114,116..117,120,124,126..132,251..256,
                     262..263,265..266)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mslpavpdlr qlryfvtvae ekhfgraaar lsmtqpplsq airaledtlg velfartkrs
       61 veltsvgsdl lpevrrllag aeglrplaqs largeagvls lafvstadyg llppllrefg
      121 arhprvrlel leatsdvqid elvagrvdag lvigplppry asqlswlpla replviamst
      181 emaariefda eldaagdgas gagaaewrde plslaqagda plvvfprrla pgfydmimdc
      241 ygaagltphi gqeaiqmqti vslvsagmgv alvpqslrnl rrtgvvyrpl reavpavvtg
      301 lvwrtaevsp vlagfidivr ahadvlag
//
LOCUS       WP_176053782             184 aa            linear   BCT 11-JAN-2025
DEFINITION  SRPBCC family protein [Paraburkholderia caribensis].
ACCESSION   WP_176053782
VERSION     WP_176053782.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Radauer,C., Lackner,P. and Breiteneder,H.
  TITLE     The Bet v 1 fold: an ancient, versatile scaffold for binding of
            large, hydrophobic ligands
  JOURNAL   BMC Evol Biol 8, 286 (2008)
   PUBMED   18922149
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10566222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..184
                     /product="SRPBCC family protein"
                     /GO_function="GO:0005488 - binding [Evidence IEA]"
                     /calculated_mol_wt=20322
     Region          41..182
                     /region_name="Polyketide_cyc2"
                     /note="Polyketide cyclase / dehydrase and lipid transport;
                     pfam10604"
                     /db_xref="CDD:431388"
ORIGIN      
        1 mkallravvm vacvaavigv lfiplprafd lstrivtvmp idrdsstvfd yvttpahwpa
       61 whpsslsvtg atdhslgige rtteefrvag rrgevvwtvv drkrpekwti dgtiqgrpag
      121 tvsyaltaea nrkdgkdvtq fertftyrsp tlwfallnaa llrakiqaes deavdrlkei
      181 lekp
//
LOCUS       WP_176053906             663 aa            linear   BCT 11-JAN-2025
DEFINITION  beta-galactosidase [Paraburkholderia caribensis].
ACCESSION   WP_176053906
VERSION     WP_176053906.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 663)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 663)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 663)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448998
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..663
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=74744
     Region          1..619
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
ORIGIN      
        1 mrlgvcyype hwpesmwkdd arrmkslgie qvriaefaws riepspgeyd wgwldravdv
       61 lgdaglqvvm ctptatppkw lidrhpdilp vgadgrpraf gsrrhydfss psyfdasrki
      121 ceavaqrygk hpavaywqtd nefgchntvv syspaavarf rawlkeryqn vdalnrawgt
      181 vfwsmeyrsf deidapvatv teahpshrld yrrfasdeva rynrmqveii rahspgrpva
      241 hnfmqlftef dhykvardld vatwdsyplg aleeqwyape ikakflrtgh pdfasfnhdv
      301 yrgmsklpfw vmeqqpgpvn wahwnpaplp gmvrlwswea fahgagcvsy frwrqapfaq
      361 eqmhaglntp dnrldiggse aeqvaheiar vsaadadana nvrskialiy dyeakwlfei
      421 hpqgadfhyp rfafeyysal rslgfdvdvi aadapldgya mivvpplpvv pgdfavrlaa
      481 sgaqivlgpr tgsktpdlqi panlppgala sllpirvwrv esmrpnvtep vhingagdgl
      541 regqarhwrd lidaadersf gvrarfadgh payvqhgsvh yfaslfddrl teslfariat
      601 eagltptplg dsvrisrrgk ltyvfnytng rhviegvdas rfvigaheve pqgvaayrte
      661 dte
//
LOCUS       WP_176053916             152 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Paraburkholderia caribensis].
ACCESSION   WP_176053916
VERSION     WP_176053916.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 152)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10120901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..152
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=16915
     Region          <30..123
                     /region_name="COG4119"
                     /note="Predicted NTP pyrophosphohydrolase, NUDIX family
                     [Nucleotide transport and metabolism, General function
                     prediction only]"
                     /db_xref="CDD:443295"
ORIGIN      
        1 msartiscgv vlldpdgrvl lahatetthw dipkgqgeeg eaphvtalre meeetgiavd
       61 asrltdlglf vyrrdkdlhl faararadel dltrctctsm fprrsdgtmi pemdafrwaa
      121 pdevehyasr sltrlfqttl slaelhrmld ta
//
LOCUS       WP_176053917             471 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Paraburkholderia caribensis].
ACCESSION   WP_176053917
VERSION     WP_176053917.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..471
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=51051
     Region          94..454
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mwrdvaglrt rqawragwlg algvsvamml tacdagsaqa dgahaaaavq avqrvqaspg
       61 garmqrvsad aaaampaggq traqvyesvk kmtavgkqlf fdpslsgsgk lacaschspq
      121 hgfgppnals vqlggqdmrq qgmraapdik ylqkvpsfte hyhdsddegd esvdagptgg
      181 lmwdgrvnsa rdqarmplts sfemgstpqk vaaavkaapy anqfrdafge hvfdsddatf
      241 kavlqalevf eetpelfypy tskydaflag kaqltkaelh glqlfndetk gncaschisq
      301 raldgsapaf sdfglialgv prnralavnh dphfydlgac gpertdlkgr deycgifrtp
      361 slrnvalrkt ffhngiyhsl eevvrfyaer dtnpekfypv vkgkvqkfdd lprkywanln
      421 tdppfdrkpg dkpaldesei kdvvaflktl tdgyqpeapr ppagahivss r
//
LOCUS       WP_176053772             670 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Paraburkholderia caribensis].
ACCESSION   WP_176053772
VERSION     WP_176053772.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 670)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..670
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71850
     Region          1..466
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          602..667
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(624,633..635,642)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            634
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mfnkilianr geiacrvaat ckrlgvtsva vysdadanak hvaacdeavh iggstaaesy
       61 lrveriieaa iatgaqavhp gygflsened fahacekagi afigppveai aamgskaaak
      121 almhsaavpl vpgyhgddqn adllhrqade igypvllkas aggggkgmrv vtrteefdaa
      181 lasckreaas sfgndrvlie kyltrprhve vqvfadrhgg avylfdrdcs vqrrhqkvle
      241 eapapglqph vrramgeaav aaaravnyvg agtvefimte ggefyfmemn trlqvehpvt
      301 emvtgldlve wqlrvaagep lplaqdqlri eghaieariy aehpargflp stgtlkhlrm
      361 pqgvefslgv ggerapvrid sgvregdtit pfydpmiakl ivhgasreea lkrmsqalrg
      421 cevvgphtnv eflqrivasv pfstgdldtg lierhhdalf apvekpflea lalacgallt
      481 reggvahgas pwdalshwrl nggytqtlsw rdveketafa vvfsrdgetr tlthdgrtep
      541 fswwtgagqh eygatigaah vtgrvfidgd tfhvfcrgea lafewqnlla haadaehgeg
      601 rltapmpgkv iavlveqgav vekgqplivm eamkmehtig apaagkvaev lyavgdqvtd
      661 gaqllvldve
//
LOCUS       WP_176053940             494 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA recombination protein RmuC [Paraburkholderia caribensis].
ACCESSION   WP_176053940
VERSION     WP_176053940.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Kosinski,J., Feder,M. and Bujnicki,J.M.
  TITLE     The PD-(D/E)XK superfamily revisited: identification of new members
            among proteins involved in DNA metabolism and functional
            predictions for domains of (hitherto) unknown function
  JOURNAL   BMC Bioinformatics 6, 172 (2005)
   PUBMED   16011798
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Bujnicki,J.M. and Rychlewski,L.
  TITLE     Grouping together highly diverged PD-(D/E)XK nucleases and
            identification of novel superfamily members using structure-guided
            alignment of sequence profiles
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 69-72 (2001)
   PUBMED   11200231
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Slupska,M.M., Chiang,J.H., Luther,W.M., Stewart,J.L., Amii,L.,
            Conrad,A. and Miller,J.H.
  TITLE     Genes involved in the determination of the rate of inversions at
            short inverted repeats
  JOURNAL   Genes Cells 5 (6), 425-437 (2000)
   PUBMED   10886369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..494
                     /product="DNA recombination protein RmuC"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=54815
     Region          157..481
                     /region_name="RmuC"
                     /note="DNA anti-recombination protein (rearrangement
                     mutator) RmuC [Replication, recombination and repair];
                     COG1322"
                     /db_xref="CDD:440933"
ORIGIN      
        1 mtmvliaava vlavalvial fmlmrgsgga hqqmqfdelg erldaaalaq treyerlere
       61 lrgeiaetar vsrtelsggf sqfqqtlasq ftsmttvqaa kidgfaqqlv kltdtnaqql
      121 davrhslqqq aqqareeqgv tlkrfgetlq qqlaqvtean drrfaevrat ieqrlkdiea
      181 nnstkleemr rtvdeklhat leqrlgesfk lvsdrleqvh rglgemqtla agvgdlkkvl
      241 tnvktrgtwg evqleslleq iltsdqyakn iatipksndr vefaiklpgr qptpdaaatp
      301 vwlpidakfp redyerliea qersdpvave dasralegri raeaktiaek yvspphttdf
      361 allflategl yaeilrrpgl tdllqrdyrv tiagpttlta llnslqmgfr tlaiekrsse
      421 vwqvlgavkt efgkfgdvla ktksqletvt rsieaaevrt rqmnrklrdv ealpeeraag
      481 llgdslsgvd aees
//
LOCUS       WP_176053950             298 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Paraburkholderia caribensis].
ACCESSION   WP_176053950
VERSION     WP_176053950.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 298)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15202679
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..298
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32214
     Region          21..141
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          169..282
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 mclqneeagv pdpnrndvid yrpftsddia aghalssavr wrhrpddwrf aarigrgfva
       61 edasgvigta lawrfgreaa tlgmiivtpe rqrsgvgrkl iellmnelgp rtllihaspa
      121 glslcetlgf qrtgtinqhq gaafqpplvs lppgerlrpl gvndaprlve lasrasgldr
      181 sdllpalldi asgialdrdg eligfalfrr fgdghvigpv vapdspdfsr akalishwla
      241 lhagmfvrid tpaefglssw leglglphvd svekmmrngp lpvdaqfkqf altsqavw
//
LOCUS       WP_176053969             584 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Paraburkholderia caribensis].
ACCESSION   WP_176053969
VERSION     WP_176053969.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..584
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=63302
     Region          60..584
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mktrkrlaal pltalisltg qaqqaptpad taaaaranae qnqqvqqqrd aqqraqavns
       61 pavrstapka dgypvlptds pcfridtfal dvpdtlpdai rkqgasalpl drfafarewl
      121 nhyagqcigk rgfdiltkgv qqlilsrgyv ttrvllpeqd vskgtlaval vpgvvrhlrf
      181 anpdtrgtwk safpardgdm lnlrdleqgl eqmkrvasqd vnmkveptss pgesdvvidv
      241 krtkpwsvva svdnsgtrat gklqgnlslg ldnplglndv lalsanqdle lgdkhlgshg
      301 fngsysvpwg ywtatlsgnt ntyyeqiagv nqtfvssgns qtaafrlarv lsrsqndvfg
      361 mqlqlskrfg esfiddtsip tqkrdntfie agltdrhyfg aaqfdgtlay rqgvgglgat
      421 sdpypdgpty rfhmavvdan lsvpfavakq nlryvstvhg qftndtlfyi ddltigsryt
      481 vrgfdgetml aaekgfywrn elqwaigqtg qalyagidyg hvygqntafl agtqlagavi
      541 girgslptri agfaydlfag tpiykpdgfp tarvtvgfqm taqf
//
LOCUS       WP_176054002             134 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator [Paraburkholderia caribensis].
ACCESSION   WP_176054002
VERSION     WP_176054002.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..134
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=14902
     Region          1..119
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mptvllvddd vetldawqym ceahgyatcv aedgraaldm lrerdvdivv adwrmpvmsg
       61 svlchhvrne rnlaeivfil vsgepsppaf vyydgflrkp ldptdllsam drllleraad
      121 grrkrnvsta pkng
//
LOCUS       WP_176054026             442 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia caribensis].
ACCESSION   WP_176054026
VERSION     WP_176054026.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..442
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48000
     Region          22..421
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(35..36,39..40,43,75,125..126,128..130,133,153,
                     156..157,160,253,256..257,260..262,265,293,297,347..348,
                     353,357,373,376..377,380..381,384)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtarqtlres daaralynrl nwrllpflla cymfayldrv nvgfakfqmq sdlgfsdaay
       61 gvgagiffls yvlfelpsnl llpkigarkt fsrilvlwgi tsacmlfvrn vpmfygmrfl
      121 lgifeagfap gmiyylscwy gptrmaraia ivflagplgg ivggplsawl isalsgvhgl
      181 agwqwmflve glpcivlgvl tlfvlsnrpa darwlsadek qllesetgva hahnhsfkav
      241 ardprvylla fayfsiifpi yaisfwlptl ikeqgvsdtl rlgwyvaipy vaagigmyva
      301 grssdrsger rlhcalpali gallliasif tqghlfatla lltaatammw maytvfwamp
      361 aeyikgpaaa ggialintig lsggfwgpaa igwartatgn sqlalivmav mpviagllil
      421 anrstrkpvh eaaeltlspe sn
//
LOCUS       WP_176054049             152 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydroneopterin aldolase [Paraburkholderia caribensis].
ACCESSION   WP_176054049
VERSION     WP_176054049.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Illarionova,V., Eisenreich,W., Fischer,M., Haussmann,C.,
            Romisch,W., Richter,G. and Bacher,A.
  TITLE     Biosynthesis of tetrahydrofolate. Stereochemistry of
            dihydroneopterin aldolase
  JOURNAL   J Biol Chem 277 (32), 28841-28847 (2002)
   PUBMED   12039964
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..152
                     /product="dihydroneopterin aldolase"
                     /EC_number="4.1.2.25"
                     /GO_function="GO:0004150 - dihydroneopterin aldolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0046656 - folic acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16589
     Region          37..152
                     /region_name="FolB"
                     /note="Dihydroneopterin aldolase [Coenzyme transport and
                     metabolism]; COG1539"
                     /db_xref="CDD:441148"
ORIGIN      
        1 mdrfnpgssp ihftvvlpss arpahepaep pqrgaaldiv yiegfvaqtv igidaaelhe
       61 rqpvqldlai gvpslracet driddtinya avraelhtll athkvqllea laeqiarlli
      121 drfgaqwvrv klckpakfdd vaavgviier qr
//
LOCUS       WP_176054068             249 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Paraburkholderia caribensis].
ACCESSION   WP_176054068
VERSION     WP_176054068.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26369
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkvlvpvkrv vdynvkvrvk sdntgvdvtn vkmsmnpfde iaveeavrlk eagvvsevva
       61 vscgvaqsqe tlrtalaiga dravlvesne elqplavakl lkaladkerp slmilgkqai
      121 dddanqtgqm laalaglpqa tfaskvvvad gkatvsrevd ggaqtlsltl pavittdlrl
      181 nepryvtlpn imkakkkple tvtpedlgvd vtprlktlkv seppkrpagv kvadvsalvg
      241 klkteakvf
//
LOCUS       WP_176054071             464 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia caribensis].
ACCESSION   WP_176054071
VERSION     WP_176054071.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..464
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49043
     Region          22..428
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,150,
                     153..154,157,263,266..267,270..272,275,302,306,356..357,
                     361,365,381,384..385,388..389,392)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 msvnaagrld rlpicsfhwk ilgliaggaf ldafdiylan gsvaamvkeg ftdlqhgamf
       61 vsatfvgmmi gayaaghigd rlgrrysyql nlgifglasi aacfapniew livlrfimgv
      121 glgaelvvaa gtlaefvppa trgkwvslla iiinsglfaa laagywiipn lgwrymfaia
      181 gigalvvwfl rhrmpesprw lestgridea eatlaaiere vearvgilpp vqrvvnlnvg
      241 avplralfap gmrgrtcvaa ltaiavnigl ygfiawlptf fvseglsivk slgfvmlmsi
      301 gspvgglvgy liadrigrak givlaallsi llgwiyvtlr epaqiivvgf clvttiytit
      361 tlglfgyipe lfptevrlrg tgvagtcgra asiatpylal llyqrvgvgg viamvsvifa
      421 vlcvaicilr vetsrhaled vapgtsdats aaghrdgaha aeha
//
LOCUS       WP_176054069             310 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Paraburkholderia caribensis].
ACCESSION   WP_176054069
VERSION     WP_176054069.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..310
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31547
     Region          2..310
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtilvivehd naalkaatln tvgaaqkigg dihllvaghn aqgaadaaak vagvskvlla
       61 dapqlaegla enieatvlem aknyshilap ataygkniap riaakldvaq iseitavvga
      121 dtferpiyag naiatiqsqd pikvitvrat gfdpvapegg sasigkidaa adagisqfvs
      181 revtklsrpe ltsaniivsg grglgsgeny tqvlepladr lqaalgasra avdagyvpnd
      241 yqvgqtgkiv apqlyiavgi sgaiqhlagm kdskvivain kdeeapifsv adyglvgdlf
      301 svvpeltval
//
LOCUS       WP_176054174             117 aa            linear   BCT 11-JAN-2025
DEFINITION  BON domain-containing protein [Paraburkholderia caribensis].
ACCESSION   WP_176054174
VERSION     WP_176054174.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Yeats,C. and Bateman,A.
  TITLE     The BON domain: a putative membrane-binding domain
  JOURNAL   Trends Biochem Sci 28 (7), 352-355 (2003)
   PUBMED   12878000
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458109
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..117
                     /product="BON domain-containing protein"
                     /GO_function="GO:0008289 - lipid binding [Evidence IEA]"
                     /calculated_mol_wt=11390
     Region          50..>117
                     /region_name="OsmY"
                     /note="Osmotically-inducible protein OsmY, contains BON
                     domain [Cell wall/membrane/envelope biogenesis]; COG2823"
                     /db_xref="CDD:442071"
ORIGIN      
        1 mnafktlkla gaalivvasv nawaqgseaa sattptqgas kssirkanra lskkvaqals
       61 kggvdttgin vlvkggavtl aggvtdpsqi dkatsiakgv sgvtsvknal tireggq
//
LOCUS       WP_176054177             207 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Paraburkholderia
            caribensis].
ACCESSION   WP_176054177
VERSION     WP_176054177.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..207
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22421
     Region          5..203
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mktsyelyga ptgnciraai aleeaglpya vrpvdlasge hrsaaylaln pagkvpvlie
       61 rqqnvppvvi aqsnaiilya aerplgrllp ddslarsvvy erffffvtdv iavshaaffl
      121 rgagvpagqt llvermlaal esaeryvsdd aymagktfsi adiaaftitq svksqlpwar
      181 lpnlrrwyeq vearpalarg lkafdpg
//
LOCUS       WP_176054259             541 aa            linear   BCT 11-JAN-2025
DEFINITION  multicopper oxidase family protein [Paraburkholderia caribensis].
ACCESSION   WP_176054259
VERSION     WP_176054259.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Kosman,D.J.
  TITLE     Multicopper oxidases: a workshop on copper coordination chemistry,
            electron transfer, and metallophysiology
  JOURNAL   J Biol Inorg Chem 15 (1), 15-28 (2010)
   PUBMED   19816718
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Bento,I., Martins,L.O., Gato Lopes,G., Armenia Carrondo,M. and
            Lindley,P.F.
  TITLE     Dioxygen reduction by multi-copper oxidases; a structural
            perspective
  JOURNAL   Dalton Trans (21), 3507-3513 (2005)
   PUBMED   16234932
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Nakamura,K., Kawabata,T., Yura,K. and Go,N.
  TITLE     Novel types of two-domain multi-copper oxidases: possible missing
            links in the evolution
  JOURNAL   FEBS Lett 553 (3), 239-244 (2003)
   PUBMED   14572631
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Ouzounis,C. and Sander,C.
  TITLE     A structure-derived sequence pattern for the detection of type I
            copper binding domains in distantly related proteins
  JOURNAL   FEBS Lett 279 (1), 73-78 (1991)
   PUBMED   1995346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..541
                     /product="multicopper oxidase family protein"
                     /EC_number="1.-.-.-"
                     /calculated_mol_wt=58663
     Region          85..541
                     /region_name="SufI"
                     /note="Multicopper oxidase with three cupredoxin domains
                     (includes cell division protein FtsP and spore coat
                     protein CotA) [Cell cycle control, cell division,
                     chromosome partitioning, Inorganic ion transport and
                     metabolism, Cell wall/membrane/envelope biogenesis;
                     COG2132"
                     /db_xref="CDD:441735"
ORIGIN      
        1 mirrdflart lsvavaslfa rnvfaqhsmh gmsgmsdmdd mpgmssthaa nshaahatpk
       61 lapetalpag aplaalrkla nessepgvfr atlvaqpvrr qlmpghstsl wlygdaaqgp
      121 ivgplieare gdtveirfvn rlpqpstihw hglpvppdqd gnptnpvapg ashvyrftlp
      181 pgsagtywyh phphmmsaeq vfrglagpiv vraaddplaa fperhlffsd lklasdasia
      241 pndmmdwmng regqfvlvng arrprievaq derwrlwngc narylrlslg gegehtftqv
      301 gtdgglldqp rdgltellla pgeraeiivr agaassaail taaaydrrkm tmtegkslpa
      361 dparpladvr fvpssptaar avpptlrpis pllsadaaad kvpqksvvft eamdmaamhr
      421 pgaamsampp gmqfmingai fdpsrialts rrgevevwsi enrtdmdhpf hlhgtqfqvi
      481 grerggtstr epflawrdtv nvqpgetvri atvqhdager mfhchilehe dlgmmatlkv
      541 v
//
LOCUS       WP_176054279             206 aa            linear   BCT 11-JAN-2025
DEFINITION  trimeric intracellular cation channel family protein
            [Paraburkholderia caribensis].
ACCESSION   WP_176054279
VERSION     WP_176054279.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..206
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22795
     Region          9..206
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mhprltlals imealaifay aisgfieart rrldavgtfl vamatafggg tvrdilldrr
       61 pfywvehqwy ailifvlsff apfvlkaytr vfnervllva davglglfsi sgtslaldaq
      121 mpwfvasmmg vatgvfggii rdvicnevpl ilrdsrpyat calvgcwvyl lldyinfdtv
      181 ysvliatgfi lvarlvtfkl dvrlph
//
LOCUS       WP_176054309             446 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Paraburkholderia].
ACCESSION   WP_176054309
VERSION     WP_176054309.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..446
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47582
     Region          27..429
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(41..42,45..46,49,81,131..132,134..136,139,159,
                     162..163,166,262,265..266,269..271,274,302,306,357..358,
                     362,366,382,385..386,389..390,393)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mstpgavaag grddkltata diirkvtwrl mplimicylf affdrinisf akfqlqsdlg
       61 fsdtayglga slfvigyvlf evpsnmllyk vgarrwiari miswglataa mvfvqnewqf
      121 yglrfvigam eagfapgvly yltlwfpasy rgrvtsllfl asafsglvga plsglvlgqm
      181 dgvfgirgwh wlfmlgglpc ivlgilvlkv lkdriedagw lspaeksyls sqiaqqtqpt
      241 thghsllgai rtpgfltlgl iyfliqiasy glnfwaphli rvagtqspti iglltavpyi
      301 cgaicmvivg rlsdasgerr kfvsgllvma avgffaagff dkqtvmlvva lavlgagvia
      361 sipafwalpp klvtgagaag gialintlgq lggivspvmv grvrdvtgst tpalyvigal
      421 slicaliily glpqslrqkd htgraa
//
LOCUS       WP_176054284             234 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Paraburkholderia caribensis].
ACCESSION   WP_176054284
VERSION     WP_176054284.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..234
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=25220
     Region          1..224
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mnlesvlfsq gfgsrrqcra liadgrvsvg gatladpdad vdtnalafev dgaawpyrer
       61 ayillnkpag yecsrdpqhh lsvfnllpaq fatrgvqcvg rldqdttgll llsddgqfvh
      121 aytspkrkvp kvylattrhp lddaqltalr egvllhgeak piaavaahar gehaleltvl
      181 egkyhqvkrm vaaagnrvea lhreriggla lpaslaegaw qwldeadlga lrng
//
LOCUS       WP_176054308             241 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176054308
VERSION     WP_176054308.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..241
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27043
     Region          14..234
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mqnsdidegl tppplmpkve rqrlhdtvve hirrfivegv lepgkklner elcetlgisr
       61 tplrealkvl aaeglidiep nrgasvskms eaelretfel msgleafsge laaermtaae
      121 lteikalhya mlacraqndl agyysrnqai hdkineaarn salrqtyiav nrrlqalrfr
      181 snfqipkwds aihdhddmlk aleardgkrl sailrqhlld krdavlqvqs redaaaaklk
      241 a
//
LOCUS       WP_176054323             567 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Paraburkholderia caribensis].
ACCESSION   WP_176054323
VERSION     WP_176054323.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..567
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=60460
     Region          270..550
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          445..547
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(448..449,482..483,486,490..491,494,537,541)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 msisaypwrs vfvwiallal twlalfspft agwngscaal vllavsaciv vatrrmwarr
       61 astqhvlrsi daalaslpad ikrntplvlt vgepgsvlsr vfdkdavivt daaiwvrhdd
      121 psklmhlada lkrwrggqgp davawlmtsd dpasavtlqa tlkrwrvain eagravgyrl
      181 pvcialyate trdrsldcpw fgvsasvqld phstaeqlsv llgafaerav pedrrpralt
      241 aiqldalarw afeavllplv etqrgmqalt lnafgvtava gpvvpdslyg qfvasttald
      301 lpaaagitqr yplpiplirg iapqpvrral pvslahafvw favwfcaaaa asawqnralv
      361 sgvlahmary eaippaqdaa rvdalaavkr drddleqyas agvpprlglg lyrgapllpv
      421 vnrliagyqp papapstiel dsmslfdsgs pklksgsnra ligalemika hpdkriliag
      481 htdsvgsrgg nlalsearas avrdwladas glsvtrfaiq gygdtrpkas ndgeagraan
      541 rrveitlvpd cradrgdgft hgqpacs
//
LOCUS       WP_176054324             778 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Paraburkholderia
            caribensis].
ACCESSION   WP_176054324
VERSION     WP_176054324.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 778)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..778
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=85301
     Region          34..729
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 madiqkyttl spadsrlvtg rqayfldvlg agnespmsvi sfeaverige pyritltlth
       61 pdqlarsdyl gkdakfsivp adaqprrfsg witrfsklkt trdftsyeiv veahlsrlas
      121 vrasriyqhq ttpeiieavl rkhgfqghqf rfrlrrqypq hafrmqyqvs dlayvqmlmq
      181 kegiwcriae dehgdvvhfs ddidhyvyqp rldvpyreta gleagveavy glsthsysva
      241 qgytvadynp dkawerfkan anvasedatt ygkpyiygtn hldadgaqwe aqlrheaaia
      301 wqiiyegesn vlalqparil hvdapladap dgqvivevrh rgardtaysn syraipsgrr
      361 frlrldedaw prvigslsar vtspgkykya yltqqgyyvv rfdldfdewn pggesvplrl
      421 akpfagalqt gfhfpaldgt eavvefrdgd pdkpyiaafh hhsqavdhvt sddrwlsrnv
      481 irtqsnnklr medwegqegi klstehsgks qlnlgylvda kkqkrgegfe lrtsgygair
      541 agkglfisad drpnasgqql dmqqaqamla saltqmkalg emvktaqavl adlegqntln
      601 naalknlqsp svlvsapaai alvtpetiqh sagdnvtlta gknidagame nftvaagqiv
      661 svfanaggmk lvaaqgknei qaqsgsiemt asqnikmlas egsveisakg slslkcggae
      721 iklangniel ncpgdvklnc itlqkggpvn anaetksfdi lsclsalqrv tsaggafv
//
LOCUS       WP_176054337             101 aa            linear   BCT 11-JAN-2025
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Paraburkholderia
            caribensis].
ACCESSION   WP_176054337
VERSION     WP_176054337.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 101)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..101
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10851
     Region          7..91
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 mtlkvfqckq cgstvfpary fcfecggaew leraaergtv defttvrrrv gaqdgadvll
       61 asvttdvgpi viarldravr vgddvglaid ehnrvlalpi a
//
LOCUS       WP_176054340             208 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176054340
VERSION     WP_176054340.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..208
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22562
     Region          6..173
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvqrgrprtf drdaaiisam hlfwehgyes tslsqlkaai gggisapsfy aafeskealy
       61 kealarymel ygkvtrslhd tslppregvf lallrsarmq tesghpkgcm valgvveass
      121 igseavtqll revrsrtrag frtcvargik sgelrsstdp aslsialdsf fqglsvlard
      181 rikyavieka vtdamgiwda avdqsmpk
//
LOCUS       WP_176054356            1081 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit
            [Paraburkholderia].
ACCESSION   WP_176054356
VERSION     WP_176054356.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..1081
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115166
     Region          3..1059
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mlkivrlalv rpytfivlal liliagplaa lrtptdifpd iripvisvvw sytglqpddm
       61 sgrivtyyer tlgttvndve hiesqsfrgy givkiffqpn vdirtataqv tsvsqtvlkq
      121 mppgttppqi lnynastvpv lqialtsnkl deqkladyat nyirpqllsv pgvaiptpyg
      181 gktrevqidl dpqalqarql saqdvanala qqnqivpagt ekigpfeyni klnnspiala
      241 elndlpiksv ggstiyirdv ahvrdgfppq tnivrvngqr avlmsilkng nastldiiag
      301 vkaklpivea tlpsslkivt ladqstfvkg avsgvaregv iaaaltslmi llflgswrst
      361 liiaasipla vlsaiaalaa lgetlnvmtl gglalavgil vddatvtien inwhleqgkd
      421 vrsaildgaa qivtpafvsl lcicivfvpm lllngiaryl fvpmaeavif amvasfilsr
      481 tfvpmmaayl lrphasdgha sgelcavmaa hgamdhvips rnplvrlqrg fehrferlrr
      541 iyrvllglal tsrlrfvtgf mvavigslav lspwlgrnff pdidsgaivv hmrgpsgtri
      601 edtaaladrv edvireivps dqlasitdnl glpnsginlt ynnsgttgpq dgdilvslrp
      661 dhaptsgyvk tlrtklprtf pgvtfaflpa divsqilnfg apapidvqva gpnqaanhry
      721 aiellrkirl iggvadpriq qasnypeftv rvdrsradql gitesnvtds lvaslsgtsq
      781 vapsfwlnsh ngvsypivaq tpqyrmtsls alsnltvsga dgrsqllgai asitrgagdl
      841 vishynimpl ydvfatmqgr dlgavaasiq hvlhatakdl pkgstvtlrg qvqtmngaft
      901 glllglggav lliyllivvn fhswsdalvi vsalpaalag ivwmlfttqt plsvpaltga
      961 ilcmgvatan silvvsfare rlavggdplv aaleagftrf rpvlmtalam iigmtpmalg
     1021 mgdggeqnap lgravigglm catcatllfv pvifslvhrn drpqpaqcsl tsndrgeshv
     1081 h
//
LOCUS       WP_176054385             251 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paraburkholderia caribensis].
ACCESSION   WP_176054385
VERSION     WP_176054385.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..251
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26870
     Region          1..246
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 msphsvpllq vrglarrfgp rtvfeqvsfe largeivslv gpsgcgkstl lraiagldrh
       61 segtvlleqh sqrgpsdrig mifqeprllp wlsvadnvaf aagprqghdp rvdtllaevg
      121 lsgvrdalpk qlsggmaqrv alarglfgep dlllldepfs avdaitrsrl qrvllalahs
      181 hgttillvth dldealllsd rvlllsppgn dgpshiarei hvaaprprnl rdpamdalrd
      241 tlldgiastp i
//
LOCUS       WP_176054427             184 aa            linear   BCT 11-JAN-2025
DEFINITION  thioesterase family protein [Paraburkholderia caribensis].
ACCESSION   WP_176054427
VERSION     WP_176054427.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10594194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..184
                     /product="thioesterase family protein"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21046
     Region          32..164
                     /region_name="4HBT_2"
                     /note="Thioesterase-like superfamily; pfam13279"
                     /db_xref="CDD:463826"
ORIGIN      
        1 mnlllrlflt fllsprrghl hvldtcvtpf rvwpndldvl rhmtngryft ildlarvdlm
       61 irsrvwpqik rqgwypvvtl etmrfhrsle lwdrydvatr vigwderhvf leqafirdgv
      121 qvalgvvrtr flkrsggtvp tgellglagv tqtspalpew vvqwsaaegg mtppaaprem
      181 sarn
//
LOCUS       WP_176054433             251 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176054433
VERSION     WP_176054433.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..251
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27105
     Region          63..208
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mvmatksaaa agpdraeqas rmqdgdnaga lgtagapaar rpgrpsgsgr gpeqrarlld
       61 aalalfarqg ivdttlgqva reagftpamm hyyfktrdql ldvliderfl plraklsgsf
      121 qanpddpiag itllaqrlve vagdypwfps lwireviseg gllkqrmher fgnanqksgi
      181 efiekwqkeg klnrelepsl vflsviglti lplatssmwr ndparrklta ddiarhaval
      241 lthgatppaa t
//
LOCUS       WP_176054494             331 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176054494
VERSION     WP_176054494.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..331
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36618
     Region          1..320
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mkvavvifdg vqaldvagpl dvfaeantfl pehqryqisf vgleagmvta sngmqfavpf
       61 gyadfdtqcd llliaggpql pdlrppvpfl dwlrrqanga trygsvcnga fllahaglld
      121 rrevtthwad agrladdfpq tcvqpdrifi rdgrlftsag vtagidlcls lvaedwghel
      181 avrvakrlvv yiqreggqsq yspyvgvrkd ddpiigkvqr yvmdhitdvl sieqlasavs
      241 vsrrtfsrlf akyakvtpsa fveqvrvdta rklleetdap lktvafkcgf hsathmrttf
      301 arrlnvtpkq yrqrfrgevg ehtleldala e
//
LOCUS       WP_176054530             451 aa            linear   BCT 11-JAN-2025
DEFINITION  2-hydroxycarboxylate transporter family protein [Paraburkholderia
            caribensis].
ACCESSION   WP_176054530
VERSION     WP_176054530.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..451
                     /product="2-hydroxycarboxylate transporter family protein"
                     /calculated_mol_wt=47272
     Region          27..450
                     /region_name="CitS"
                     /note="Na+/citrate or Na+/malate symporter [Energy
                     production and conversion]; COG3493"
                     /db_xref="CDD:442716"
ORIGIN      
        1 mksstqaals atssgrtqap havvewwwrv fdlrigslpl pvyvlmlgvl gamaakgkla
       61 adlptgialv avggftcael akripwirhi gatsifaafi psmlvyyklm pepvvkavtt
      121 ftktsnflyl fiaaiivgsv lsmdrqmlik gfvrifvpva agslaaalvg tavgtalgld
      181 arhalfmvvv pimaggvgeg alplsagyaq imgveqgplf aqvlsavmlg niaaiccagl
      241 lsylgtrrpe wtgngrltra gdsdddiaqr pasfefdvgs vaaagstaia fyllgvlshq
      301 lfgwpapvvm lvlvvaaqlf qlvsprvrgg arfmygffst avtyplmfai svamtpwgei
      361 vtafhwvniv tavstvltlt vtgffvgrlv gmypveaaiv nathsglggt gdvailtaan
      421 rmelmpfaqi atriggaltv maalgvfayw k
//
LOCUS       WP_176054561             311 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Paraburkholderia caribensis].
ACCESSION   WP_176054561
VERSION     WP_176054561.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..311
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33197
     Region          80..283
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mlepemiafv ertkglyprd rsvstfaeqr avyeqyaaaf tpplpdgvtt hdapftspdg
       61 htfgvrlyap aerarsmgtv lyfhgggfvv gsldshglit ariaadtglc vvtvdyrlap
      121 ehaapaahdd clavtraald srlpfgplpr slqlagdsag gtlaasvamr lrdegkagvh
      181 gvalvypmlg iepqwpards eadapmltla dvrrygalyw sspardhawt vpleasrydg
      241 lpptlaigve hdplrddarv faeriraagg qasapvgigl vhgswralat spgvqwmhre
      301 vcrflvehaa g
//
LOCUS       WP_176054576             745 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Paraburkholderia caribensis].
ACCESSION   WP_176054576
VERSION     WP_176054576.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..745
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..745
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=79503
     Region          64..>211
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          217..738
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msqglldaqn gkprdddaar vtrrtflkfs asvaataggg lmlgfsmpaq sqgdvrksvi
       61 ggdgvetpqs gvlapnafvq idtagkvtli ipkvemgqgv ytsipmliae elevpldsvt
      121 idhappdesr ftdpllggql tggstsirya wepmrragat trvllinaaa qqwqvdpasc
      181 haengqviha dtkrsiaygq lvdaaaklpv pqnvplknpk dfkligtqak rldspekvdg
      241 samfgldvrl pdmvyaaivn cpvfggtlas vddtaakkip gvrqivkidn gvavigdhtw
      301 aakrgasalk itwnegagaa vsmktivddm ekasqnngav arkdgdvnna fsqaktrvda
      361 vyqqpflaha tmepvnctvh vkpdscdiwv gtqvptrard agakvtglsp dkivvhnfll
      421 gggfgrrlef dmvtqavkva kqlnvpvkvt wtreediqhd myrpyyydki sagldangkp
      481 iawqhrivgs silsrfappa vkngvdpdav evaadlpydl pnqlidyvrq ephaiptafw
      541 rgvgptrgtf vvesfidela aqtktdpvky rrdllgkspr alnvlnvatq aagwgstvpk
      601 gqgrgvsvmh afgsffamva dvavdqgevr vnrvvcavdc gmvvnpntve aqiqggiifa
      661 itaalyseit idrgrvqqsn ftdyrilrin etptidvhiv ksseapggig epgtaaaqpa
      721 ianaiyaatg krlrqlpvgn qlmna
//
LOCUS       WP_176054593             300 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Paraburkholderia caribensis].
ACCESSION   WP_176054593
VERSION     WP_176054593.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..300
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33331
     Region          <149..295
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mqhandsaln vavttspalg dslllmtvar nlqlsgktvt vfsqhmqalr dwfpgidiqp
       61 alredevdar lrpfhtiiql hanrpvprle qrhpdvlvle hlcrapstep maarlaqfcr
      121 eslrlqhaep gnglavpagl vhrkhplrva ihptastpdk rwlaprfvrl alalkakgfe
      181 phfivtdeer adwehvqqhg iglprlgtld nvaawlvesg wfigndsgig hlasclrvpt
      241 lslfmrrgia rtwrpgwgag kvlvggawlp tgrlkergwk yalsvnqvlr afqqlqheav
//
LOCUS       WP_176054618             759 aa            linear   BCT 11-JAN-2025
DEFINITION  LPS-assembly protein LptD [Paraburkholderia caribensis].
ACCESSION   WP_176054618
VERSION     WP_176054618.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..759
                     /product="LPS-assembly protein LptD"
                     /GO_process="GO:0015920 - lipopolysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=83427
     Region          41..730
                     /region_name="LptD"
                     /note="LPS assembly outer membrane protein LptD (organic
                     solvent tolerance protein OstA) [Cell
                     wall/membrane/envelope biogenesis]; COG1452"
                     /db_xref="CDD:441061"
ORIGIN      
        1 mvlcllaplq vnaqlagdaa daerlsdaws lriapqltet pnppdakpat ialgesvtgt
       61 vdsdlslkga aelrrygfvv qgdalhydpd ydvanaygsv rivskgdvfd gpfsqlrvna
      121 sagfiaqpry hfylnggwgs gkradlldne rskiedgtys tcacetnpaw yirasqftmd
      181 rgadegvarn gvlffqnipl laspwlsfpl dgarrsglls ptwsmsskng vditvpyyfn
      241 iapnydltia prymskrgam lsadyrylts assgslsiay lpnditther rysidldhvw
      301 nigsgfgayv nynrvsdanv stdlgsgsaf pttsttlyqq eagltynsgp wsvlareqhw
      361 qsfssdttyn repqlnvryn rydaggfdyg feadatrftl ssddatqgtr fvfnpfvsyp
      421 ivrpgwfftp kikwhfasyn ltsiasdapa gqprnvnvni ptlsldsgmt feravriwgs
      481 syiqtleprl fyvytpyrnq tyaplfdtte adfglgelfs dnafagndrv sdesrltaal
      541 tsrlidaatg derarfviaq rydfrqprvt lydtedtanv artsliagss ikvgaginve
      601 nalqysqann yltqgsigla wspatahvln iayrytrant tldfqpvnqf ivsgqwplak
      661 nlasvarvny dmsthrliag llglqydaqc wslalaleky tnatgstsps tgtrvlmqlq
      721 lkglsrtdrg lldqfkadvp gyssapaeaa pvsrfseyq
//
LOCUS       WP_176054624             398 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar ABC transporter permease [Paraburkholderia caribensis].
ACCESSION   WP_176054624
VERSION     WP_176054624.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..398
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=41858
     Region          43..393
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mtpdltssds hakhgaslas ghrvkqlfar ykllalllav aviwvffsfl tegafvtprn
       61 lsnllrqmsi tgmlacgmvf viisgeidls vgsllgllgg vaailnvthh wplaatlpvv
      121 mllgvaiglf ngwwstylrv psfivglggm layrgvllgv tggstiapvs ddfvfigqgy
      181 lpriagdtla vvlfvllaal tvrqrqkrqh ynlsvvplwq dgvkivatgl illafvatln
      241 ryggipvpvl lllallgift yiatqtvfgr riyavgsnle atrlsgvntn rvklaifalm
      301 glmcafggli ntarlaagsp sagsmgelda iaacfiggts mrggsgtvyg aligalvmas
      361 ldngmsmldv dsywqmivkg gilvlavwid vvsgsdrr
//
LOCUS       WP_176054642             320 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Paraburkholderia caribensis].
ACCESSION   WP_176054642
VERSION     WP_176054642.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..320
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35604
     Region          14..194
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(17,19,103)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(50,102..103)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            101..103
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 mtvanktevp eisvvipsyn ckgcleelca rldrvlaglv stfeivivdd rspdnswplv
       61 ewlserhssv rgirlsrnfg qhiaitagik gargnyvvlm dcdlqdpper ipdlyakvke
      121 gydlvlarrv erahsgfrvi aakayfglls kltgesvdgs ygtfsilsrr vadgylqfte
      181 rdrhflfiir wmgfncgtie yshaerhagk ssynlrrlir hafdgmffqt svfltwivka
      241 gifctaasfv sgiyfiyryl vasalpgwts lavavlfstg lilasvgavg myvsrifeaa
      301 kgrplylvdr ecgcsegefe
//
LOCUS       WP_176054688             293 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Paraburkholderia caribensis].
ACCESSION   WP_176054688
VERSION     WP_176054688.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..293
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31494
     Region          13..270
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mpssikavlk phvrdignla vrrvlpamaa rlvgpfiffd hmgpatlpag tgldvrphph
       61 iglatvtylf egaimhrdsl gseqkivpgd vnwmtagrgi vhsertpepd rtngstvhgi
      121 qtwvalplad edvepsfehh pgatlpeier ngvtlriiag tsfgktspar tfsgtlyaaa
      181 hfspgsvlal epehdergvy lvdgdlsldg epleaasmav ltpgetvtla saqgatvmll
      241 ggekldgerf iewnfvassr ekieraklaw tnqemgkvpg etewiplper kpr
//
LOCUS       WP_176054706             224 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Paraburkholderia
            caribensis].
ACCESSION   WP_176054706
VERSION     WP_176054706.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..224
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24032
     Region          1..220
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 msesisltsp idgfkfdvlh qlptsarrgg viivqevfgi dayvtadvar wsslgfevla
       61 psmfdrqerg fvashdaegl qtglkyaren gednpisdiq acidtlrakg pvyivgycyg
      121 gtvawraasr atglsavssy ygsgvaasas lepycpvich fgakdpyipa lesktainav
      181 hpdvpvyvye nsghgfnneg sdsdpldvrl arqrtlalfe rypg
//
LOCUS       WP_176054709             218 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator transcription factor [Paraburkholderia
            caribensis].
ACCESSION   WP_176054709
VERSION     WP_176054709.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..218
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23722
     Region          13..207
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mrkvaaedhr eqlvhiiddd etvrdgiaml lssvdiavkv yssgeeflhs dvpecpscvv
       61 ldvrlrgmsg lalqqsiktr lglpvifvsa hgdvemtara mkagaidfls kpfrgqdmld
      121 avtaaievdc trrrqesaia alvscyeqlt trerevmalv aggahnkkia lqlelsevti
      181 klhrgnamkk mrsmsfahfv lqahalglas ldpllvtt
//
LOCUS       WP_176054731             250 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176054731
VERSION     WP_176054731.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..250
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27001
     Region          33..160
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpdaphprag rrqtvkapta grepmpgrsp rlarrrhetr vrllhaafel vaekgmdgvt
       61 ineitdaadv gfgsfynhfd skegifaalv dwlfeefadt ldqvasglad paeviaicvr
      121 htllracrep vcgqllireg lspralstgl gqrllrdaer gmaekrfvia delmcvisvi
      181 gtvlagiaae ldlsmssrra vssrktltsr aekfaegtaa ivlqafglar leaekiarrp
      241 lpavpqdapa
//
LOCUS       WP_176054733            1057 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Paraburkholderia
            caribensis].
ACCESSION   WP_176054733
VERSION     WP_176054733.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..1057
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114970
     Region          29..1042
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnardhenar dgapldyfdk aaaggtgfnl sawalrhqql vifliglatl fgvigytqla
       61 qsedppftfr tmviktywpg atarevqeqi tdrlgrqlqa apyvdniksy srpgesmiff
      121 amkdsapvrd vpetwyqvrk kvgdiraalp kgavgpffnd efgdvytniy alegdgytpa
      181 qlhdyadklr tvllrvpgva kvdyfgdpdq hifveisnaq ltrlsvtpqq laqaidaqna
      241 vapvgtitta ddrvfvrpsg afkdeqalad mlvtvnrrtf rlgdiatikr gyddppvtqm
      301 rvggqgglgi gvtmqkggdv idlgkaldar taelqaslpa glklaavasm phavkhsvdd
      361 fveavgeava ivlvvslvsl glrtgmvvvv tipivlavta lcmhlfgigl dkvslgtlvl
      421 algllvddai iavemmavkl eqgwsrmraa afaytstafp mltgtlvtvs gflpialaks
      481 stgeytrsif evsaislvvs wfaavvlvpl lgfhllpehk vqsdgghghe hdvydtgfyk
      541 rlsgwvaaci drrwvvlgvt avlfviamga ftrvpqqffp nserpellvd lrlpegasfe
      601 atlreskrle kvlegkpgid hfvdfvgtga prfylpldqq lqqpnfaqfv itakdvetre
      661 elmhwldakl ekdfsgvrtr varlengppv gfpikfrvsg ddiatvrsia etvadktrad
      721 srtrnvqfdw depaersisf eidqnrarql gvtsedvssf lamtlsgytv tqyrerdkli
      781 nvdlrapnse rvdpakltsl aiptpngpvp lgslghvrdt leygviwerd rqptitvqad
      841 vrgdaqgidv trgidqalat vraklpvgyr idvggavees vkgqtsinae mplmiiavlt
      901 llmiqlknfa rtfivvltap lgligvvaal llfgkpfgfv allgviamfg iimrnsvilv
      961 dqidqdiaag qarfdaiiga tvrrfrpiml taaaavlali pllrsgffgp matalmggit
     1021 iatmltiffl palyatcfrv rrdecgtqqv vvehtev
//
LOCUS       WP_176054737             254 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176054737
VERSION     WP_176054737.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..254
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27445
     Region          36..>159
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtkttnrptt krpsraapvv papaapviee reprgarrkr etrarlldaa lrlmaekgme
       61 gvaineitea advgfgsfyn hfeskeaiya tlvdnvfeef admldrlagg itdpaevvav
      121 svrhtvlrar hdpvwgrfli regfsaramt rglgqrlmrd igngiaakrf vvadpfigfl
      181 avggtvlsai aaelnfvapg ataadvlkel gfsgehfper taamllqtlg lkraeaekia
      241 arplpvveet veen
//
LOCUS       WP_176054793             317 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paraburkholderia caribensis].
ACCESSION   WP_176054793
VERSION     WP_176054793.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..317
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32721
     Region          16..317
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mrtlirrhva pnaapfivav liaalfvtga nvndrfstls nllnihqqat glalvalgqt
       61 lavltggidl svgslisvta tltsgisdat qggwgmaisa aialsvivgl angllvlwlr
      121 vhpliitlgm gailqggily yangpagsvp dgfdalaygr yanvpvtatv vlllyagvsy
      181 fmrntrlgry vylvgdddna atlsgiprkr vilfvytfss lcagltgiyl aaqfgsgqpy
      241 lganytlasi tpvvvggtil sggrggvvgt llgvyllsml nnlinfagvp sqyqlivqgi
      301 aiiaavcvnv qqkrrla
//
LOCUS       WP_176054822             264 aa            linear   BCT 11-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Paraburkholderia
            caribensis].
ACCESSION   WP_176054822
VERSION     WP_176054822.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..264
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29940
     Region          11..235
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mvahytseqq eefirtferd glvilpgllp keklvkwrea fdvllkerva gnktavrgeq
       61 rhyitlpftg vfadetifcn pdilavverv agedpvmcql atdtplkgst yqdvhrdtpa
      121 lfenfletps fqlavnfplc dvtlengpfe ttigthrmda aeamqrhrdg efplhaipmk
      181 lgdvmirdvr alhrgtpnnt dvprpmvvig ysrnwyfrpe vnvqippdvl atlspkakrl
      241 lrympvlhae aqdddaesyt rfay
//
LOCUS       WP_176054825             146 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Paraburkholderia
            caribensis].
ACCESSION   WP_176054825
VERSION     WP_176054825.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..146
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=15852
     Region          43..146
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 msdvyfgtdl fseldrlqrq msslfggtps slrssrsgtf ppinvgttde sveivafapg
       61 ldpakfdvtv dkgllsiage raaeqsqlpe garqyarerf tgtfrrviel pqqadpnkvq
      121 aryvdgclli tvgkreaskp raitvq
//
LOCUS       WP_176054837             311 aa            linear   BCT 11-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Paraburkholderia
            caribensis].
ACCESSION   WP_176054837
VERSION     WP_176054837.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..311
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34555
     Region          37..309
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mntwqpslrt pdpairildk rfehyrlaha rverlwtgcr waegpvwfgd agvlywtdlp
       61 nnrilkwdea teavstwrap sskangmtrd rqgrlivceh gtrrvtrtey dgrvtvladt
      121 fegkplnspn dvvvtrdgsv wftdppfglv sdymgqigtp elpafvyrid aqsgqiecva
      181 dniegpngla fspdertlyv vasrvrprti mafdvmdnrk lgrgrvlida kdgtpdgfrv
      241 dvdgnlwcgw gtgsdeldgv rvfapdgtai ghialperca nlcfggrdnn rlfmasttsv
      301 yalfvntrga v
//
LOCUS       WP_176054857             340 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176054857
VERSION     WP_176054857.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..340
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37707
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..292
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(101,105,144,158,160,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdklqamqvf trvvdsnsfs raadalqmtr ssvttiiqnl eahlkvrlln rttrrisltp
       61 egaayyerca riiadvedsd ttfsspatpr gklkvdmpgs igrllivpal adfqqrypdi
      121 dlmlgvgdkp vdliqdgvdc airmghlpds tlvarrvgas efvtlasaey verygvpqtl
      181 eeldahvavn yfssrngrvi emdfvvdgep veirmrsrla andgeaylqc giqglgliqv
      241 pyffalphie agrlvevlsd wrpapfpiwa vypqnrhlsa qvrvfvewaa erfeschllr
      301 kdmalafapa parrashiei aaqsetgdar hvllretams
//
LOCUS       WP_176054858            1082 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Paraburkholderia
            caribensis].
ACCESSION   WP_176054858
VERSION     WP_176054858.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..1082
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=116759
     Region          1..1042
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mniskffidr pifaavlsvv illagiialt klptaeypev vppsvvvraq ypganpkvia
       61 etvaapleeq ingvenmlym qsqansdgnm tttvtfklgt dpdkaqqlvq nrvsqamprl
      121 pedvqrlgvt tikssptltm gvnlvspndr ydltylrnya linikdrfaq vpgvgevalw
      181 gsgdysmriw ldptkvarqn ltatdvikav reqnvqvaag ivggapmttn ipmqlsvnaq
      241 grlkteeefr riilktspdg avthlgdvar velgaseyal ragidgkkav qiiifqqpna
      301 nslqisddir kltaemqqdm pdgvraeivy dptqfvresi davvhtlfea ivlvvivviv
      361 flqtwrasli pllavpvsiv gtfslmlafg ftinalslfg mvlaigivvd daivvvenve
      421 rniaagltpl easyeamrev sgpiiaialt lvavfvplaf msgltgqfyk qfamtiaist
      481 visafnsltl spalsalllk dhhapkdwlt rvmdrilgpf fsafnkvfhr gsetygkgvg
      541 givqrkaamm vvyaillggt lllgkvvpgg fvpaqdkdyf vsilqlppga sldrtqkvvd
      601 dmgaiarrqp gvkhttefpg lsvtglmnss ssglvfsvtn pskergkgek aadivgglna
      661 kyagikdaai atfppppvqg lgtiggfklq iedrgalgye alnkatqafl aeaakapelg
      721 psfssyqinv pqlnveldre raeqlgvsvt dvfdtmqiyl gslyvndfnk fgrvyqvrvq
      781 adaqyratad silqlktrnn rgemvplssl vkvtptygpe mvvryngyla adinggpapg
      841 yssgqamaav eriaektlpr gikyewtdlt yqqiltgnaa fwvfpisvll vflvlaamye
      901 sltlplaill ivpmsilsal fgvwltrgdn niftqiglmv lvglsaknai livefarele
      961 mqgrtivqaa ieacrlrlrp ilmtsiafim gviplvvstg agsemrramg iavffgmlgv
     1021 tffglvltpv fyvilrklag gkqladkhgh hphihgpddh edvqsvssgk ngpkvaepal
     1081 se
//
LOCUS       WP_176054864              96 aa            linear   BCT 11-JAN-2025
DEFINITION  HU family DNA-binding protein [Paraburkholderia caribensis].
ACCESSION   WP_176054864
VERSION     WP_176054864.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Khanaka,H., Laine,B., Sautiere,P. and Guillaume,J.
  TITLE     Characterization and primary structures of DNA-binding HU-type
            proteins from Rhizobiaceae
  JOURNAL   Eur J Biochem 147 (2), 343-349 (1985)
   PUBMED   4038648
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002493
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..96
                     /product="HU family DNA-binding protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030527 - structural constituent of
                     chromatin [Evidence IEA]"
                     /GO_process="GO:0030261 - chromosome condensation
                     [Evidence IEA]"
                     /calculated_mol_wt=9521
     Region          1..96
                     /region_name="HimA"
                     /note="Bacterial nucleoid DNA-binding protein IHF-alpha
                     [Replication, recombination and repair]; COG0776"
                     /db_xref="CDD:440539"
ORIGIN      
        1 mnkqelidav aastgeskas tgegegeald aileavtsav trgeavqlia fgsfstgacs
       61 ertgrnpstg etitipaakt vkftagnsfk davnaa
//
LOCUS       WP_176054893             781 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Paraburkholderia
            caribensis].
ACCESSION   WP_176054893
VERSION     WP_176054893.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 781)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 781)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..781
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..781
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=85885
     Region          28..731
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 maggfegdsl rlngltgrqs yfldvtgntg asasglsvvs faaterlgep yqvtvrlthp
       61 lrlaradylg kdatfsivpe dldgrrfagw itsftelrtt pdstsyevvl eahfsklarv
      121 hasriyqhvt apeiieqvlk rhgfrghqfs frlrrqhpqh afrmqyqmdd lawvqllmkq
      181 egiysyitag ehgdvlnvcd didhyvyqps ldvpyreqag lesgieavss lvtrtqtvar
      241 sfqvadynpd sawerfrdda niaaedktty gqpyvwgthh pdaqaakwea qlrhetaias
      301 qvvyegesnv lalmparilh idealpdapn gqvvvevvhr gardeaysnr ykaipsdrrf
      361 rlalderawp tiagtlsarv tspdeykyay ltaagyyvvr fdldfdtwnp ggesvplrla
      421 kpfagalqtg fhfplldgte vaiafhdgnp nrpyiahamh nsqavdhits dnrwlsrnvi
      481 rtqsnnklrm edwegqegik lstehsgktq lnlgflvdsk rqkrgegaev rtsghaavrg
      541 gkgllftahd kpgatgelld mepglallrr aldqssalae tvktaqaiaa dcerqkalld
      601 etidqlkrag ifvtapegia lvtggdlqys aarnliatag gnadmsvvrr itmaageavs
      661 vfaqrmgikl fagkgkveiq aqndamslds erdmtiksan grvvieakee lvlkcggsyl
      721 rmtttgiedg trgdrtwkaa sfsrrgpahl peelpvlpkp aatqcalras qsgmpfakle
      781 a
//
LOCUS       WP_176054985             317 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176054985
VERSION     WP_176054985.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..317
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33454
     Region          16..292
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 marqrpnppt aaepaiaari taampiltpv hrrmgefvla nqfraatmri delatavgas
       61 iatanrfara lgfdgypafr ealvrgfeat lapverlrsa qesqtngdel fsasleqaat
      121 nlgttrstid gaaaeaavda iiaarrvfil gcgasaflas lmehnllpyh dnvqslalig
      181 gpthaarrlf nagrgdlvia iafpryvddt ielarraasl gadvlaltdg ptsplaalat
      241 rslfiraerr laatseatvl aviealcdav afrakrsaqa aanmtefvlp wltdtsalqp
      301 hskpatrpts sqakknk
//
LOCUS       WP_176055004             172 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Paraburkholderia caribensis].
ACCESSION   WP_176055004
VERSION     WP_176055004.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14388526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..172
                     /product="cupin domain-containing protein"
                     /calculated_mol_wt=18975
     Region          67..137
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cd02208"
                     /db_xref="CDD:380338"
ORIGIN      
        1 mqpiegdilp fseyleltak piaepvvwrw qaiesetrlr ahnpqgtlal sggnvdehgt
       61 vapdislviq vlkpsemter hrhsfwhlyi arsgsgelaf gedgvterie sgdtvfvpaw
      121 cyhtiancsd sepfvlyrlq nlpqnasggn lmreiggklq iiyanpglat hr
//
LOCUS       WP_176055019             793 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Paraburkholderia caribensis].
ACCESSION   WP_176055019
VERSION     WP_176055019.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 793)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..793
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86490
     Region          68..775
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mrivyaalsa rtrlslacaa vfavqpawad esttdraiig rpasdtsvsh psvtnnsans
       61 ltepvstlqa vsvtaaraap afapgtpgvv etvtreqida rnivntedsl kyapnvmvrk
      121 rftgdrnavf agrdfnelqs arglvyadgl llsnllgssy aypprwslia pddiaqvevl
      181 ygpfsalypg nsigstvqit trkpekleas ldtqlftqhy ddaygfsknf ggnhqtahia
      241 drvgrfwysl tldrlennsq pmqyaspsst ynaklgapva vtgaatdigp ngqprvivga
      301 qtmerteqin esvrmgyait dhvdatltlg hwenhykdrs dtfltdaagn pvyggnvtig
      361 gknytispta fspangdqen wlyalglngr ldsgwklsgi vsaydvsrdt lrssttappa
      421 aygggpgtif ygdgtgwrtf dlkaesplya ghaltvgyhf dnyflrnety ntpdwlngsp
      481 stlastyrgd trtqalygqd awrfapgwla tlglryerwd aydgalgngs stfgyadrsa
      541 nalspkasvq wqatqdwlfr lsfatgtrfp svaelfqgti snnaivnnnp glkpekaidw
      601 dftaerdvgv gvvrasvfqs dlrdsiysqt tvsgsttvtn isnvdrvrvr gvelafsgqn
      661 vllhgldlda nvtathskil adaanpsyvg krfpripvvr anllanyhft qqwqgsvglr
      721 ysgrqyntld nsdinpdvyg gtssffvidl karyqvgkhw lasvgidnvt drryyvfhpy
      781 pgrtfygelk wml
//
LOCUS       WP_176055059             327 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176055059
VERSION     WP_176055059.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746949
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..327
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35105
     Region          6..119
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          99..322
                     /region_name="PRK10572"
                     /note="arabinose operon transcriptional regulator AraC"
                     /db_xref="CDD:236717"
     Region          232..314
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mslsqdwlsr llgmmtvhgq lelrcsygap weviygdsdp gempyhiils gsailetpgs
       61 gkpqqlcagd ivmlahggah mlhdgsgarp krgheraaln ltisenkgtg prldmlcgri
      121 ilapphdrfi raylparlvt htsptksgvk hgtdgaayeh lnglvalmra eagadnlggy
      181 ammnalsaal faltmrvase sdeapvglla lagnprlspa ltaifsdpar awtlpelanl
      241 csmsratlir hfqdklgrsp ndlltdirma laanelkrpg istevvaetv gyqsvaafrr
      301 afsqrlgmtp adwrrsqrek qhaelat
//
LOCUS       WP_176055072             283 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176055072
VERSION     WP_176055072.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..283
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29968
     Region          4..>172
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
     Region          91..260
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(106..107,109..110,113,117,119..125,210..215,
                     221..222,224..225)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mkvldldavr afvlvadlrs ftraadaldt tqsavslklk rleahlgkpl lertprvvrl
       61 sehgqafldg ardllgahdr algalsadrr rlslglsehv agtdlaalla rvnahdpglv
      121 lelhmglssa llrqfderrl davivrsepd dapredgqll fteplswlat pewqpragep
      181 lplallaapc nvrsvalrtl dgagiawrea fvgggvqavg aaaaaglavs plarrvapgg
      241 lvdsgtrlgl palpesrvtl hsrvrdarsv eslrlvtngl iaq
//
LOCUS       WP_176055128             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia caribensis].
ACCESSION   WP_176055128
VERSION     WP_176055128.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46970
     Region          25..431
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(38..39,42..43,46,86,144..145,147..149,152,172,
                     175..176,179,261,264..265,268..270,273,300,304,357..358,
                     362,366,382,385..386,389..390,393)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 masietthat grvdavrple drtlrkivia svagnamewy dffvygtaaa lvfgqlffpa
       61 gadpligtlg afaafamgfv arplggvvfg higdrygrka slvwtllimg iatfaigllp
      121 tyaqigiwsp valvvlrllq gvasggewgg gvlmisesap pekrgyyaaw sqlgvgggfv
      181 lssaaflaaq slphdafinw gwrlpflasi aifaigvyir hslpesrdfe qtekrgekth
      241 mpvvevikrh pkeilmamgl rvaenggayi flafslvygk fvgiassvml tgvmlamvve
      301 mgamlawgrl sdrigrkpvy migaaglivm afpffwmldt hqapwiylal vlgtavchga
      361 migtlpalvg elfstevrys gvalghevas ifagglspli atallasyha ywpvsvflmv
      421 lgsitvvtlr ftretrvvg
//
LOCUS       WP_176055208             780 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Paraburkholderia caribensis].
ACCESSION   WP_176055208
VERSION     WP_176055208.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..780
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=84327
     Region          65..738
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mkpsrrksrr arlhprkral qlvcgsalas lcaaawsqep apppadtppa dvqqtaqntt
       61 qeaempsilv igttpligig taielvpanv qtirgreidq qhpntltdyf atnlqsvdin
      121 daqgnpsqmd isyrgftasp llgtpqglsv fmdgvrinep fgdvvnwdli pqaaidtiql
      181 ipgsnptfgl ntlggaiait tkngsnspgg eaeisggsfg rksaqiqqgg vigsnvdyyf
      241 tanaanddgw adhngsrlrq afgklryhda dttlsisggg adntldgsqt iprsfldnrk
      301 qaytfpdqnn ntvgyltiag ehyftpnvql sgtlyyrhyr nknvssnvnd dfdpddpdda
      361 ppatnvqstv ftqsyggslq lallqnlfgk rneltlgvaa dlanthftqs sqdatftdtr
      421 atigtgpflp ttdaktrnet ygvyftdtfs ftdqwaltfa grynwsrtti gdesgvqpll
      481 dgrhvfsrfn pavgitynpt dtltayftyn egmrsptsie lacadpdapc slpndfiadp
      541 slkpvisktf eigargrigs nttwsaalyr ttldddiqfi ssngaasslg ffqnvgktrr
      601 qgfelagrtk ygpvgvsasy syidatyqst wtessasnss adangnitvk pgdkipgipq
      661 ntvklridyt pfaawnigtn ltyrgsifar gdennqdvng tvagyflidl dttynvtkql
      721 qvfatvknll nkhyanfail genffngpnh tfdpggvtne qflgigaprg vwvglryawk
//
LOCUS       WP_176055216             137 aa            linear   BCT 11-JAN-2025
DEFINITION  SMI1/KNR4 family protein [Paraburkholderia caribensis].
ACCESSION   WP_176055216
VERSION     WP_176055216.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10558574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..137
                     /product="SMI1/KNR4 family protein"
                     /GO_process="GO:0042546 - cell wall biogenesis [Evidence
                     IEA]"
                     /calculated_mol_wt=15476
     Region          10..133
                     /region_name="SMI1_KNR4"
                     /note="SMI1 / KNR4 family (SUKH-1); pfam09346"
                     /db_xref="CDD:430545"
ORIGIN      
        1 mqyedteqtl shndlcefek naqfrlpeaf krhylahngg fpvdveevag rdhvfpfhgf
       61 fpmkygalki eavrkdlaed fglsnaipfa ydqgsnifyi stspsdcgav fqvtadtkdk
      121 ffvcetfdqf ldglrtv
//
LOCUS       WP_176055223             557 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Paraburkholderia caribensis].
ACCESSION   WP_176055223
VERSION     WP_176055223.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..557
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60675
     Region          25..383
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          453..555
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mtpaslieqy gpresmdydv vivgggpagl saairlkqra aekgveigvc vlekgseiga
       61 hilsgavmdp ralnelipdw kekgapldve vtedrflfls etgakavpnw alpdnfknhg
      121 nyvislanvt rwlgqqaeal gveifpgfpa aevlynddgs vkgvatgnlg igkdgepten
      181 fqlgmelhak ytlfcegarg hlgrqlsdkf klrdgadpqv ygigikelwe idpakhkpgl
      241 vihtagwpld tqtyggsfly hidnnqvmvg fvvglgysnp ylspfeefqr ykthpsiraf
      301 leggkrvsyg araitaggll slpklafpgg alvgddagfl nasrikgsha aiktgmlaad
      361 aafdavqagr qsdeltaype sfktswlhte lyrarnfkqw mskglylgtl mvgieqkllg
      421 gnvpwtlhhq hwdhemlkpa sqckpieypk pdgkltfdrl ssvfisntnh eenqpahltl
      481 kdpsvpvkvn lqtyagpesr ycpaavyefv knddgserlv inaqncvhck tcdikdptqn
      541 ivwvtpeggg gpnypnm
//
LOCUS       WP_176055254             765 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Paraburkholderia
            caribensis].
ACCESSION   WP_176055254
VERSION     WP_176055254.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 765)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 765)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 765)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   4  (residues 1 to 765)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   5  (residues 1 to 765)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   6  (residues 1 to 765)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457627
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..765
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80974
     Region          73..134
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          171..764
                     /region_name="Haloacid Dehalogenase-like Hydrolases"
                     /note="The haloacid dehalogenase (HAD) superfamily
                     includes carbon and phosphorus hydrolases such as
                     2-haloalkonoate dehalogenase, epoxide hydrolase,
                     phosphoserine phosphatase, phosphomannomutase,
                     phosphoglycolate phosphatase, P-type ATPase, among others.
                     These...; cl21460"
                     /db_xref="CDD:473868"
     Site            order(462..466,614..615,642,660..661,664..665)
                     /site_type="active"
                     /db_xref="CDD:319763"
ORIGIN      
        1 msasslsrsk shdapglahd hprdhghahd dhdhdhaddr nhahgdgcct paaarfemme
       61 astvvadgvr tpirilqmdc pteealirkk lagmksvtsm efnlmqrvlt vvhapdalda
      121 vlaavrslgf tpevtesgak aqpvpevpqk pwwplalsai aaiaseaasw lgqpqwvtaa
      181 lailavvacg lttyrkgwva irngnlnina lmsiavtgal ilrqwpeaam vmvlftiael
      241 ieaksldrar naiqglmrla pdkatvqqad gswvevdaqa vvvgatvrvr pgerigldge
      301 ivsgrstinq apitgeslpv ekaegdqvfa gtindsgsfe yrvtatasnt tlariihave
      361 eaqgakaptq rfvdqfarvy tpvvfaisla iavvpplvvg ggwqewiyka lvllviacpc
      421 alvistpvsi vsglaaaarh gilikggtyl eqgrkltwla ldktgtithg kpvqtdfelr
      481 aevdsqrcrt lavslagrsd hpvsqaiaqt pdarslvqla vedfaaipgr gvrgvidgvq
      541 yslgnhrlie elgrcspdle arldvlerqg ktvvmlvdan rvlalfavad tvkdssraai
      601 aalhglgvrt amltgdnpht adaiakqvsi draegdqlpe dklrvieals adgavvgmvg
      661 dgindapala radigfamga mgtdtaieta dvalmdddlr kipvfirlsr atrtilvqni
      721 tvalgikavf lgltlaglgt mwmavfadvg asllvvgngl rllrk
//
LOCUS       WP_176055271             369 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paraburkholderia caribensis].
ACCESSION   WP_176055271
VERSION     WP_176055271.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..369
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40154
     Region          1..355
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masvtlrnir kayddnevmr ninldiqdge fvvfvgpsgc gkstlmrmia gledisggdl
       61 nidgvrmndv ppakrgiamv fqsyalyphm tlydnmafgl klagtkkpei daavrnaaki
      121 lhidhllerk pkqlsggqrq rvaigraitr kpkvflfdep lsnldaalrv kmrlefarlh
      181 delkttmiyv thdqveamtl adkivvlsag nleqvgspnm lyhapanrfv agfigspkmn
      241 flegvvqsis aggvlvryet getqlvlvep grakegdkvt vgirpehlhl dlpdngvsas
      301 vmaieslgda aylyaessva pdgliaripp lerhekggti rvgatpdhch lfdsdgqafh
      361 rkivevlaa
//
LOCUS       WP_176055274             471 aa            linear   BCT 11-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Paraburkholderia
            caribensis].
ACCESSION   WP_176055274
VERSION     WP_176055274.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..471
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49179
     Region          22..430
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mhsntvhpcd erlpfgqllt lgiqhvlvmy agavavplii gsalklpkeq iaflisadlf
       61 scgiatliqt lglwifgirl pvimgctfaa vgpmvaigtn pslgildifg stiaagvigi
      121 iaapmigkml rffppvvvgv visviglslm evginwaagg vgnpdygnpv ylglsfvvlm
      181 lillinkfgk gfvsnisvll givagfviaa llgrvnmegv tsapwvgfvm pfhfglphfd
      241 plsiatmvtv mfvtfiestg mflavgdmve rpvnqktlvr glrvdglgtl iggvfnsfph
      301 tsfsqnvgli gvtgvksrfv camggvilvl lglfpkmaqv vasvpsfvlg gagivmfgmv
      361 aangikvlsk vdfvknhhnl fivavsiglg lvpvvsphff aklppalspl lhsgillasv
      421 savvlnlifn gakgeraatr dirraghdfd grggkddaip gdemlraadm h
//
LOCUS       WP_176055279             362 aa            linear   BCT 11-JAN-2025
DEFINITION  GGDEF domain-containing protein [Paraburkholderia caribensis].
ACCESSION   WP_176055279
VERSION     WP_176055279.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..362
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=38834
     Region          21..>354
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mkrtvtpirp psprwrpqpi avgaialacl vvgllyvavq vkalfsdhfr qqyatlvlea
       61 vgradnalnv atllkrsaps taadatyrqa ldelgarvte ldaligsspv paprlpqana
      121 taksldelkq slaatadywr arrdavsndv rrrtlrvasv lavltvvvtg alfaalvvfa
      181 rrhrrlaglt hqfrhaaqhd amtglpnrqq llarldriaa erapgkcavl yvdldgfkqv
      241 ndtlghaigd eflialaqrf rqslrpgdmv armggdefaa lvsgfgndte lagiaarlmn
      301 cvgetdtqmg lglvrasvgi atypdrivdh rllvaaadga myevkrhgkn gyafavspip
      361 pg
//
LOCUS       WP_176055283             527 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Paraburkholderia caribensis].
ACCESSION   WP_176055283
VERSION     WP_176055283.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..527
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=57731
     Region          17..525
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mdnnnkvhfs hndaravvii gsgagggtla nelaqkgidv ivleagkmht qgdfttdewg
       61 sfsmlswldk rttsgswria tdfpnlpawi cktvggttth wagaslrfqp hefkaktnyg
      121 tikdanlldw pvtseemapw ydraekkmgv trtnglpglp gnnnfkvmyn gatkvgykec
      181 ntghmatnsi vrddrahcfq rgfcfqgcrt gakwstlyte ipraqatghm elrtqaqvvk
      241 ietdakgkas avvyydaagk lqrqkariva vagnaietpr lllnshssrf pdglanssgq
      301 vgrnymrhtt gsvyavfndk vdmykgttma giiedearfd tsrgfaggyh metvslglpf
      361 yaafldpgaw gadftqamea ypytagmwiv gedmpretnr itlnndvkdq yglpvpnvhf
      421 ddhpndeamr ehgfkqgsav yqaagaktvy rvppypsthn lgtarmsakp qdgvcnrfgq
      481 thdvpnlfis dgsqfttgaa enptltivtl airqadyiag qmnrrti
//
LOCUS       WP_176055286             213 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Paraburkholderia
            caribensis].
ACCESSION   WP_176055286
VERSION     WP_176055286.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..213
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23027
     Region          10..212
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mpaakpaqpi rlyttllsgh ghrvklfltl ldlpfeviel dmragdnrkp eylalnpfgq
       61 vptiqdgdvt lfdsnailvy lakrygdasw lpedplgaaa vqrwlslaag qiaygpcsar
      121 lvtvfgapld hetakgiavk lfdvierela tkpfaagehv tiadiaahty iahapeggvs
      181 ldpypniraw lrrvealprf iampptkagl lae
//
LOCUS       WP_176055345             366 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paraburkholderia caribensis].
ACCESSION   WP_176055345
VERSION     WP_176055345.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 366)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..366
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39973
     Region          7..366
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mktedvivsf rgvrktydge tlvvkqldld iyqgefltll gpsgsgkttc lmmlagfefp
       61 tggeiwldgq llnnvpphkr nigmvfqnya lfphltveqn vaypltvrkl paderahkvn
      121 nalkmvrmeg fakrypaqls ggqqqriala ralvfepklv lmdeplgald kqlrehmqye
      181 lkslheklgv tfvyvthdqg ealtmsdrva vfdkgivqql dtvdslyeap cnefvanfig
      241 dsnrlrgtia nvdgdycefh lidgtrlvgr niggaqagaq giacirperm klaagaagga
      301 rpganavage argliyfgdh vrmrcglpqq decfvkvplg tealegfapg apvalefape
      361 hlrvfa
//
LOCUS       WP_176055351             241 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176055351
VERSION     WP_176055351.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..241
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25768
     Region          5..227
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mgnegvvave kalslldcfk pgaesqslam lsqasgmhkt tvyrlmnsle rmgyvvraqs
       61 gnyslghrvl ylgklyeqsf hlstvvepal halaaltkes asyyvhdkgq rlclfrveps
      121 eglretrlag ttlplddtai sqvirfwglg epiydkppal pvftagardl htaafavpvf
      181 gagdkfmaal tlsgpasrls aahasgeldr pqldaaadls rklgasagfc envyrarspl
      241 p
//
LOCUS       WP_176055354             459 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia caribensis].
ACCESSION   WP_176055354
VERSION     WP_176055354.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..459
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48403
     Region          41..440
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(54..55,58..59,62,94,144..145,147..149,152,172,
                     175..176,179,276,279..280,283..285,288,315,319,369..370,
                     374,378,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtishtlsae gaarpadaap vqgiahedya asertlakaf rrilpfific yvisyldrtn
       61 vgfaaltmnk dlgltaeqfg fgaglffvgy flfeipsnli mqkvgarvwi arimitwglf
      121 smatafvvgp ksfaaarfll glaeagftpg iylyfthwfp gkwrakvtaa flvgipvanm
      181 igspvsgall elgglhglrs wqwllliegv pavvlgiacl fvladrpeka kwlsdaekss
      241 lakrlaleqg digarhgstl rdamtnwrvf vlafvnfcgi vgslgvglwm pqiikqfgve
      301 havvgwltai pyaigavgmv wwarvanraa nripyvagal vvaavalcas tfvdtpvlkl
      361 ialcftvsgi lafqatywai psgfltgraa agglalivsv gnlggfvgps migalkqvsg
      421 gftvpllavs gvlllgalti awlgdpgada geaplankv
//
LOCUS       WP_176055357             440 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia caribensis].
ACCESSION   WP_176055357
VERSION     WP_176055357.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..440
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47747
     Region          21..424
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,152,
                     155..156,159,256,259..260,263..265,268,295,299,349..350,
                     354,358,374,377..378,381..382,386)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mqtgfmdrsa ierrtirkvv wrlipflmvc yllafidrgn vgmaslqmnh dlgmsakvfg
       61 fgsslffisy ffcevpsnla lqkygariwi arimitwgiv saatalvhna ttfyilrfll
      121 gaaeagffpg vllylsywip asyrarivat fmvaipaasf igspisalll qmdgfgglrg
      181 whwlfilegi ptvllgiacl fmltnkpena rwldddertw lvnalvsehk apkkvpslpl
      241 tqlfrnryvl clalvdtcas aagstlsvwq pqllksfgls vmqtgllnsv pyavasvlmv
      301 ywgrrsdrlg errwhtvvpm lligaglfat slsgsllpti cmlcgvlvga ysfkgpfwal
      361 atdmlsnsav aaglatvnai anllggglmv nvygwvkdat gsyalalmpl ailtlvsvat
      421 lllltrngsa srlagktgti
//
LOCUS       WP_176055420             386 aa            linear   BCT 11-JAN-2025
DEFINITION  metallophosphoesterase [Paraburkholderia caribensis].
ACCESSION   WP_176055420
VERSION     WP_176055420.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Matange,N., Podobnik,M. and Visweswariah,S.S.
  TITLE     Metallophosphoesterases: structural fidelity with functional
            promiscuity
  JOURNAL   Biochem J 467 (2), 201-216 (2015)
   PUBMED   25837850
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Koonin,E.V.
  TITLE     Conserved sequence pattern in a wide variety of phosphoesterases
  JOURNAL   Protein Sci 3 (2), 356-358 (1994)
   PUBMED   8003970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003658
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..386
                     /product="metallophosphoesterase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0042578 - phosphoric ester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=41518
     Region          117..384
                     /region_name="YaeI"
                     /note="Predicted phosphohydrolase, MPP superfamily
                     [General function prediction only]; COG1408"
                     /db_xref="CDD:441018"
ORIGIN      
        1 mrrlsffiri iaigillhvy vgiriipelp vdaavkglca lwlvlsvlli pvgmvarslq
       61 rqplgdwlaw aglialglfs sllvltfare llllvvmivh aispeavnpa rwevnsasav
      121 pllallstai gffnarrrar vvsidvpikd lphaldgfti vqisdihvgp tikrgyvdai
      181 vdavnrlepd liavtgdvvd gsvehladht rplsrlsarh gaylvtgnhe yysgahawia
      241 efqrlglhvl lnehvvvehd gaqaviagvt dfsaghfdpa hesdpaaale gapgdvlikv
      301 llahqprsae aaadagftlq lsghthggqf fpwnfavrlq qpfvaglsrl ddlwvytsrg
      361 tgywgppkrl gapseitrlr lvggga
//
LOCUS       WP_176055457             290 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfurtransferase [Paraburkholderia caribensis].
ACCESSION   WP_176055457
VERSION     WP_176055457.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..290
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30879
     Region          15..285
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mphthyttli sasnlaerla aapgsvfivd crfdladtds gekayaaghl pqahylhldr
       61 dlsgpktgsn grhplpdrqk lvdrlaalgl kqsqqvvayd aqggmyaarl wwllrwlghd
      121 saalldgglq aweaaghplt qdappqtsgd fkagaplavt vdaqaverni gtkervvida
      181 raadryrgen etldrvgghi pgarnrffkd nltadgrfks ahtlrddfna vipagvsaeh
      241 vvlqcgsgvt achnalamei aglhgaalyp gswsewssdt srpvatgpnp
//
LOCUS       WP_176055458             290 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Paraburkholderia
            caribensis].
ACCESSION   WP_176055458
VERSION     WP_176055458.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..290
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31689
     Region          48..285
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mlqpevdslv phvpfdrrtf ikaalgtgfa acvlpvsaqt ihtdseglea gevsiksgdt
       61 mvpayraqpk gkthlpviiv vheifgvheh iadvcrrfak qgylaiapdl ykrqgdptqy
      121 psmqqlneql vskvpdsqvl adldatfkwa gehggdvnkv gingfcwggr iawlyaehnp
      181 rlkagvawyg rvagnqtpmt panpidrvsd lqvpvlglyg rqdqsipqes ldkmkqaiaq
      241 gpqagrgsef vvyddaghaf fadyrpsykq adaedgwrrt lawfkahgvg
//
LOCUS       WP_176055468             148 aa            linear   BCT 11-JAN-2025
DEFINITION  ester cyclase [Paraburkholderia caribensis].
ACCESSION   WP_176055468
VERSION     WP_176055468.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Sultana,A., Kallio,P., Jansson,A., Wang,J.S., Niemi,J., Mantsala,P.
            and Schneider,G.
  TITLE     Structure of the polyketide cyclase SnoaL reveals a novel mechanism
            for enzymatic aldol condensation
  JOURNAL   EMBO J 23 (9), 1911-1921 (2004)
   PUBMED   15071504
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..148
                     /product="ester cyclase"
                     /EC_number="5.5.1.-"
                     /GO_process="GO:0030638 - polyketide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16344
     Region          13..140
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
ORIGIN      
        1 msqnisediv rttieafyra faakdvallr qvvtpdwqyi pespgakpga dqmadafarm
       61 aialpdmeit ildllthgdr vgvraevtgt qsgellgiap savqikfaih sfhelrgpli
      121 aktwhledwf svfrqigqlp rnlelhpi
//
LOCUS       WP_176055472             108 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF190 domain-containing protein [Paraburkholderia caribensis].
ACCESSION   WP_176055472
VERSION     WP_176055472.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..108
                     /product="DUF190 domain-containing protein"
                     /calculated_mol_wt=11682
     Region          5..104
                     /region_name="COG1993"
                     /note="PII-like signaling protein [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:441596"
ORIGIN      
        1 mqgsqltvfa attgrrkhhq ttvgwildea rqagiqgatv fevsecvdlh gkyhaarfve
       61 laeqpvaitl agecarvdal lerlrqgdvp lfytrcavdy evlgsavp
//
LOCUS       WP_176055493             303 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paraburkholderia caribensis].
ACCESSION   WP_176055493
VERSION     WP_176055493.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 303)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 303)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 303)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..303
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33178
     Region          64..302
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mmttakhvlq eqtvmhatti dpsvrhqqre dramlllmap allvvvvllv lplawlswqs
       61 iyhdgaftlv nyrriftgty ldtflmtfkl siivtgitll lgypvayfaa svppkwsali
      121 lgmvilpfwt svlvrtyawl vllqrtglvn kallstglid rplqlsynqf gtivamvhil
      181 lpfmvlplys amqkipgnls qagaslggsp lhvfwrvflp lsmsgvvagv tlvfvlclgf
      241 yitpelmggg ksimvsmvvs rnveiynswg aasavsvvll vcvfaifyaa srviplektl
      301 gak
//
LOCUS       WP_176055502             300 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Paraburkholderia caribensis].
ACCESSION   WP_176055502
VERSION     WP_176055502.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15202679
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..300
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31720
     Region          21..151
                     /region_name="yhbS"
                     /note="Predicted N-acetyltransferase YhbS [General
                     function prediction only]; COG3153"
                     /db_xref="CDD:442387"
     Region          174..283
                     /region_name="Acetyltransf_18"
                     /note="Acetyltransferase (GNAT) domain; pfam18014"
                     /db_xref="CDD:436212"
ORIGIN      
        1 mstpeplsah strstlatvt lrpfapddia aahalslevk wphraddwrl vadagsgfva
       61 lsegrivgta lcwkfgehga slgmvivspd qqgrgigrel merllemlgg rttvlhatpa
      121 gqplyeklgf raigtinqhq atdfripqiv lkpgeqlrpl raadtprlid lasrasgldr
      181 sallpalldv aqgvalerdg evsgfallrp fgrghaigpv vvehaadest rraqaliahc
      241 laanagaftr idtpgdggmt pwleelglkr vdtvikmsrn gapagdpsvv qfaivnqalg
//
LOCUS       WP_176055510             309 aa            linear   BCT 11-JAN-2025
DEFINITION  3-hydroxyacyl-CoA dehydrogenase family protein [Paraburkholderia
            caribensis].
ACCESSION   WP_176055510
VERSION     WP_176055510.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..309
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=32726
     Region          8..287
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mglskpvvgv vgtglmgvgi atqsalhghr tivhdvdaar ldsvapkaga vldelidagr
       61 idgqakddal sriatsatld amadahivie aipevldlkh rlyaqlngvl rddailasnt
      121 sgfppdqlta plraperfli ahfwnpphmi plvevvpgrd taqhaidttv almhaigmep
      181 vvlskaipgf vgnrlqfavl realnivrsg aatpdvvdrv mkaslgkrwg ivgpfegadm
      241 ggldtfvdis thlmpalakd edvldllreh vqagrvgvrs gegfydwdda qtakvkagrk
      301 rviqgngqn
//
LOCUS       WP_176055515             359 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Paraburkholderia
            caribensis].
ACCESSION   WP_176055515
VERSION     WP_176055515.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..359
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=39136
     Region          17..359
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhhaidepld tpapqvrhiv favapelvll dacgpleafh raeltvrdar rvapasgerl
       61 epvayrttva sidggvldtf pglpvvtqrl dalddepidt livpgipvdd prtlqpalid
      121 wiarraphvr rvcsvctgaf ylaaagvldg rratthwrda hrlaerfprv hvdaepifir
      181 eplhgveadd sravwtsagv tagidlalal iqedyghpva mqvarrlvvf vkrpggqsqf
      241 saalaaqasa ggafdslhgw masnlncdls verlaeeasm sprtfarryv devgrtpakt
      301 vsamrleaas ralaesrrpl krialdcgfg seqnlrrafm rsfgvlpldy rerfasalr
//
LOCUS       WP_176055607             263 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Paraburkholderia caribensis].
ACCESSION   WP_176055607
VERSION     WP_176055607.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869930
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..263
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28093
     Region          6..220
                     /region_name="yflN-like_MBL-fold"
                     /note="uncharacterized subgroup which includes Bacillus
                     subtilis yflN; MBL-fold metallo hydrolase domain; cd07721"
                     /db_xref="CDD:293807"
     Site            order(63,65,67..68,153..154,171,219)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293807"
ORIGIN      
        1 mnkptiitvp ilpfgmvhsh lvigatgcvl vdtgtpgsed kiervlkkhg rcfrdvtliv
       61 vthahtdhag saarlreltg apilahagdl dyyvrrkemt ycvthwwgpl flrsgvpgep
      121 ylpftpdill qddatidlsg ygiegvarht pghtagsvsv elgsgdalvg dliasgvflg
      181 glirkgramr ppfeddpqav svelmgmvea gmqrfhmghg gplaakevrr halslrnlkp
      241 grkygsqaig cacsepklae pvk
//
LOCUS       WP_176055663             174 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase, partial [Paraburkholderia
            caribensis].
ACCESSION   WP_176055663
VERSION     WP_176055663.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         <1..174
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
     Region          <1..156
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 ggshpadimv wsagvkaptf lgqlagievn rsnqvaigpt lqsvddehif algdcasytp
       61 agrerplppt aqvatqqarf larhlpawld gkplpefhfq dlgalvsisd ynafgtlgqf
      121 gffrggfikg rfaqlshaml yrqhqyalhg lrksallwsa erlngcvrpt irmt
//
LOCUS       WP_176055751             120 aa            linear   BCT 11-JAN-2025
DEFINITION  porin, partial [Paraburkholderia caribensis].
ACCESSION   WP_176055751
VERSION     WP_176055751.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..>120
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
     Region          7..>120
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkkrimvaaa tltgltagva yaqssvtlyg ivdtgigwqs sqtslgstag gksvvkming
       61 iwagsrfglk gaedlggglk aifqleegfn satgaqavsg lmfnrqayvg lqdarlgtft
//
LOCUS       WP_176055769             103 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator, partial
            [Paraburkholderia caribensis].
ACCESSION   WP_176055769
VERSION     WP_176055769.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         <1..103
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          <1..91
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 qagqlrslre gevllavsfa pyaqetqkiv edalqrgakl iaitdsrlna lasgadvall
       61 lqesdtfgfr sltstmglaq slfialayrl elayepapai qkd
//
LOCUS       WP_176055943             185 aa            linear   BCT 11-JAN-2025
DEFINITION  HdeD family acid-resistance protein [Brucella intermedia].
ACCESSION   WP_176055943
VERSION     WP_176055943.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..185
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=20041
     Region          16..185
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mdiqqlqlle rktveqrkwk gflglgvllm aggilclflp vfsefaastm fglvlvaigv
       61 vkiiqslwvk swagfvwqel sgavelvggi miylnplkga laitlliaiv vfvhgflqla
      121 lswkikpasg wwwftlsgli awtasamlvm kwpwtrdlps gsiagialli agvayigial
      181 strna
//
LOCUS       WP_176055966             305 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Brucella intermedia].
ACCESSION   WP_176055966
VERSION     WP_176055966.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..305
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32887
     Region          4..293
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(28..29,32,87,100,102,132,166,253,256,292)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(224,229,244,253..255,258,280,284)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mggfasigec mielsgnegd qwrmgfagdt lntawymral meksypveyv tafgedsfsq
       61 kqrvfltsng igiahspiid glhpglyait lngaersfty wrsdaaarrl asdrealeks
      121 ltgrdiiyfs gisvaiilpe hrdtffdvlr qcraagsria fdpnfrhqlw pdrkaaqdii
      181 seamriadia lptfpdeqal fgdkdasaca drlaglgvke ivvkdgtepa lvvtgeervl
      241 vpsvvaqavd ttgagdsfng aylaarlngl tpveaarkah lvaarvveir galapmetar
      301 aafad
//
LOCUS       WP_176055995             450 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Brucella intermedia].
ACCESSION   WP_176055995
VERSION     WP_176055995.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..450
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=48157
     Region          <290..442
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mtgnqaktst kkvfgerkep pvliiargek ishftlrpwm tvlggavfla lsagylgata
       61 ylvlrddlms agiarharnq qlyedrisal rtevdritsr qmldqqvmen kvaelmqrqq
      121 tlsardgkla pllerasqlq pmpempaeta pdieqhsqyi pnealagrdf pgidpiitgp
      181 vpgklpagkp drradagsvg lrlsggisge stletsdkil atithnlhri eseqngkvrv
      241 ladaayekad sildtlnaag lrietpgdts vamggplipv sspgavvndf dmqlrnldsa
      301 ldrldqvrkr vsalplanpa pgkpltslfg vrrdpflgta afhsgidfra aygqtvksta
      361 agkvvkagrf ggygnmveid hgngfstrfa hlsrvlvrdg qqvaagvvvg eagssgrstg
      421 shlhyevren gravnpvnfl kagkqiepll
//
LOCUS       WP_176056003             183 aa            linear   BCT 11-JAN-2025
DEFINITION  ImmA/IrrE family metallo-endopeptidase [Brucella intermedia].
ACCESSION   WP_176056003
VERSION     WP_176056003.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Bose,B., Auchtung,J.M., Lee,C.A. and Grossman,A.D.
  TITLE     A conserved anti-repressor controls horizontal gene transfer by
            proteolysis
  JOURNAL   Mol Microbiol 70 (3), 570-582 (2008)
   PUBMED   18761623
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006736
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..183
                     /product="ImmA/IrrE family metallo-endopeptidase"
                     /calculated_mol_wt=20378
     Region          79..177
                     /region_name="ImmA"
                     /note="Zn-dependent peptidase ImmA, M78 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG2856"
                     /db_xref="CDD:442104"
ORIGIN      
        1 maiirrkknp eavlrrahlg nvdnplelvs lakknglqtq pldvdgllkv lglaveyssd
       61 lpsdvsgklq kkdegwiciv nknhhptrqr ftlahelghy vlhrnqntdf vdhtyfrkad
      121 ninsmefean qfageilmpk etfsyflkfv ssdinkvaea fgvsplaasv rakqlrlvgg
      181 gvk
//
LOCUS       WP_176056059             194 aa            linear   BCT 11-JAN-2025
DEFINITION  peptidylprolyl isomerase [Brucella intermedia].
ACCESSION   WP_176056059
VERSION     WP_176056059.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..194
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=20459
     Region          26..191
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 msfvrsalaa aaffalsqga vhtafaaent vvlklkdgdv aielrpdlap khvaqieklv
       61 gegayngvaf hrvipgfmaq tgdvkfgnmd knfdasrvgt ggsdypdipa efskepfvrg
      121 tvgmarsqnp nsansqffim fadgsflngq ytvvgkvvsg mdvvdkikkg seadngavkn
      181 pdkiikatlq atkk
//
LOCUS       WP_176056120             365 aa            linear   BCT 11-JAN-2025
DEFINITION  microcin C ABC transporter permease YejB [Brucella intermedia].
ACCESSION   WP_176056120
VERSION     WP_176056120.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 365)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..365
                     /product="microcin C ABC transporter permease YejB"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042884 - microcin transport [Evidence
                     IEA]"
                     /calculated_mol_wt=40504
     Region          1..365
                     /region_name="YejB"
                     /note="ABC-type microcin C transport system, permease
                     component YejB [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4174"
                     /db_xref="CDD:443333"
ORIGIN      
        1 mgayilrrll lmiptifgim aisfavvqfa pggpvervia qlsgqggdal drlsggggdf
       61 gqsavdsgsv nskyrgaqgl dpqfiadlek qfgfdkpple rfgqmlwnyl rfdfgrsyfr
      121 disvidlike kmpvsislgl wltflsymis iplgirkaik dgsrfdtwts aviivgyaip
      181 sflfaillim lfaggsffdw fplrgltspd faqmsfwgki gdylwhmvlp vtalvlsafa
      241 tttlltknsf leeirkqyvt tarakglten qvlyrhvfrn amliviagfp gafisafftg
      301 sllietifsl dglgllgyqs vinrdypvvf anlfifslig llvgllsdlt ytwidpridf
      361 drrdv
//
LOCUS       WP_176056122             355 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella intermedia].
ACCESSION   WP_176056122
VERSION     WP_176056122.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..355
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38649
     Region          1..354
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masvelrsih ktygnvevip sidlsiadae fvalvgpsgc gkstllrmia gleqitsgdl
       61 higgrnvnra npserdvamv fqnyalyphm tvfdniafnl qlagrpkaei rdrvgeaarm
      121 ldltalldrk phqlsggqrq rvamgraivr kpsvflfdep lsnldaklrv lmraeikelh
      181 qkvkitsiyv thdqieamtl adrvvvlnkg rieqqgtpme lytrpanifv agfigspamn
      241 fleatvehss agaairlasg skleipdsdt grsgkvvlgl rpehlevrrd ggipakvrli
      301 eptgaqahvm fevgseklma vvdsemslvv gdvvelgisf ermhlfdptt garin
//
LOCUS       WP_176056128             261 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Brucella intermedia].
ACCESSION   WP_176056128
VERSION     WP_176056128.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..261
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27795
     Region          8..259
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mvdddekdgg nlqsvvltmq vleevvrtsk gvgvtslaka lgtsksrihr hlqtlvrqgy
       61 vfqhedsery evghrlvslv qsvsdnagmv haaydpllel rdalghsava sqltpegmlv
      121 iatvpgrspi eigvrvgsll sfhssaqgkv aaafssagfq srvlagqlea ftpstiiepa
      181 vlekefaeir rrgwaiaphe talglntlas pvfdasgmvc gatgivdmvq svsavpteeq
      241 imrtveaark iserlgyqaq h
//
LOCUS       WP_176056134             433 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Brucella intermedia].
ACCESSION   WP_176056134
VERSION     WP_176056134.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..433
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47203
     Region          18..418
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,150,
                     153..154,157,251,254..255,258..260,263,290,294,344..345,
                     349,353,369,372..373,376..377,380)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtqaiytade kklfqritwr ivplvvfiyl iaiidranvg faklqmvsal dmteqlygla
       61 sslffigyla leipsayavn rfgarlwlar illtwgllti atawvtsgsl faafrfligc
      121 aeagaypgii yyftlwfpke yrarvlgflt lgsafgnlfg slvsgflldl dgflgfagwq
      181 wvflatglpa vlltplvlvf lpngpddakf istlerkwlr erlgqetpdg qhgnplaviw
      241 drrvlllaii ymlilaslyg viywlptvvr gfgvsgteng llsaipwvig acalvvvprh
      301 lrkektvlta miaisclglv cfylstalpe nwmrmvamsi gtpcisllfp clwflpslff
      361 sgqrvamaia aistignlgg fiaqnlmpwv anaagtpvaa mlvpasalal vgllasliki
      421 agftnrqpvl ane
//
LOCUS       WP_176056135             218 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: TetR/AcrR family transcriptional regulator
            [Brucella].
ACCESSION   WP_176056135
VERSION     WP_176056135.1
KEYWORDS    RefSeq.
SOURCE      Brucella
  ORGANISM  Brucella
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Brucella"
                     /db_xref="taxon:234"
     Protein         1..218
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24737
     Region          22..156
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mieksaemdg ragkkgkrqt qaerssntqa kicnatleal aevgyhcitt afiakkakvs
       61 rgalthqyas rndllvaalq rlhndwsqvr pftanpttee ytvaqlitel wenlfsdkry
      121 iaslelmvaa rldndlgirl rdemsrwvnv rdeflrslnf tdrkmglnvq hlhlmmstmr
      181 gvalyqlfdr dvqagqklie lysslvesrv dpadtkee
//
LOCUS       WP_176056161             414 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar ABC transporter permease [Brucella intermedia].
ACCESSION   WP_176056161
VERSION     WP_176056161.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 414)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..414
                     /product="sugar ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=43232
     Region          20..410
                     /region_name="XylH"
                     /note="ABC-type xylose transport system, permease
                     component [Carbohydrate transport and metabolism];
                     COG4214"
                     /db_xref="CDD:443360"
ORIGIN      
        1 mnqatgntsl drqdtrvrhd egvsgalrnf fdrvrsgdlg slpvivglvi iwtvfqtlnp
       61 vflssnnlvn llfdcstigv islgivcilm lgeidlsvgs vsglasaivg vlwvnhgwpv
      121 giamlaalct galigllyaf lynrfsmpsf vstlagllaa lglqlyllgn tgsinlpygs
      181 wlvsfgqllv mprplsyalv liaglaifft gfrsaqrrre aglsapssag ialkaivitv
      241 ivggavfyln qsrgvpwmfg lfvalviamn yaltrtkwgr amqavggnre aarraginvk
      301 fiymsafmtc svlaaaggil aaarlasssq qagtgdvnln aiaaaviggt slfggrgsaw
      361 sallgiiviq siasgltlld lssslrymit gavlaiaviv dslarrsrqs hgra
//
LOCUS       WP_176056175             551 aa            linear   BCT 11-JAN-2025
DEFINITION  N,N-dimethylformamidase beta subunit family domain-containing
            protein [Brucella intermedia].
ACCESSION   WP_176056175
VERSION     WP_176056175.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20801894
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..551
                     /product="N,N-dimethylformamidase beta subunit family
                     domain-containing protein"
                     /calculated_mol_wt=60979
     Region          103..530
                     /region_name="DUF6605"
                     /note="Domain of unknown function (DUF6605); pfam20254"
                     /db_xref="CDD:466405"
ORIGIN      
        1 msernnefan fgefpdfglt paqrreavlg hyyeypgmdg prgeiwcytd aysylpgatv
       61 hlqvsataqr fdieivrdga vetpvfskrg idckwqdtpa qcsvvgcgwe ttfavrtdet
      121 wpsgayritl kahgndgqpi hchhlfilrp aagrkpgril qvaatgtwta yntwggsnhy
      181 qgitgpngdq yattvsierp fcrgfallpp daprvpleiv tppaappryp hmewayangy
      241 skkyassgwa sydslffrwa eregyavdla tqhelhfape ildgydcvvf vghdeywtwe
      301 mrdavdnyvd gggraarfag nfmwqtrled ngkrqtcyky raraedpvyr sadprrtsgc
      361 weatetgrpa aetfglnalr glyvgwggca prgvrgfpvy rpehwafagt giyygdllgs
      421 eghafgyevd gldyvirggl pepeegsgap dglqilalgm sslkeesadi paddqflsda
      481 dakfvadtli gndgdaaver ikrgcgmivn fprgkgevfh agscewvaal krgdrmverv
      541 tanvlnhylk r
//
LOCUS       WP_176056187             283 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Brucella intermedia].
ACCESSION   WP_176056187
VERSION     WP_176056187.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..283
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30124
     Region          46..243
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mcekfsvetl qvpgrlhgqa qgqagdctck ariyrgtkll spppvvlhlh ggafsasclg
       61 acervaetla eagavvvspe yssaclnpfp aaleivysil tsmrarcpef ahkksmlfva
      121 geeaggnlaa gvalmardqy ltdlkgqill spmldpclat asfrkycpes avktmsdgwq
      181 hylgecagft hpyaapalct rlaglaptll vtsaqcpmrd etqayaerlr qagvkvqshv
      241 lpgkagwipe nkvagtdwsp qehklvdlfs dffrqagakp iaa
//
LOCUS       WP_176056205             346 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella intermedia].
ACCESSION   WP_176056205
VERSION     WP_176056205.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..346
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35808
     Region          16..346
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msvtstnket aapngakrkt slvhlllegr affsliaiiv vfsflspnyf tvnnfltmss
       61 hvaifgllai gmllvilngg idlsvgstlg lagvvagflm qgvtlqhfgv ilyfpvwavv
      121 iitcalgafv gaingvliay lrvpafvatl gvlycargva llmtngltyn nlggrpelgn
      181 tgfdwlgfnk lfgvqigvlv lvvlaivcai vlnrtafgrw lyasggnera aelsgvpvkr
      241 vkvsvyvisg icaaiaglil asqltsagpt agttyeltai aavviggaal tggrgtiqgt
      301 llgafvigfl sdglviigvs sywqtvftga vivlavllns iqysrr
//
LOCUS       WP_176056190             437 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatase PAP2/dual specificity phosphatase family protein
            [Brucella intermedia].
ACCESSION   WP_176056190
VERSION     WP_176056190.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Pulido,R. and Lang,R.
  TITLE     Dual Specificity Phosphatases: From Molecular Mechanisms to
            Biological Function
  JOURNAL   Int J Mol Sci 20 (18), 4372 (2019)
   PUBMED   31489884
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Patterson,K.I., Brummer,T., O'Brien,P.M. and Daly,R.J.
  TITLE     Dual-specificity phosphatases: critical regulators with diverse
            cellular targets
  JOURNAL   Biochem J 418 (3), 475-489 (2009)
   PUBMED   19228121
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   5  (residues 1 to 437)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12932297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..437
                     /product="phosphatase PAP2/dual specificity phosphatase
                     family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0004721 - phosphoprotein phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006470 - protein dephosphorylation
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=47944
     Region          39..207
                     /region_name="PAP2_Aur1_like"
                     /note="PAP2_like proteins, Aur1_like subfamily. Yeast
                     Aur1p or Ipc1p is necessary for the addition of inositol
                     phosphate to ceramide, an essential step in yeast
                     sphingolipid synthesis, and is the target of several
                     antifungal compounds such as aureobasidin; cd03386"
                     /db_xref="CDD:239481"
     Site            order(110,118,144..146,180,186,190)
                     /site_type="active"
                     /db_xref="CDD:239481"
     Region          310..423
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
ORIGIN      
        1 mtvhltereg ysrrpvvrra ilwllflapf fyltygtanw lasqqshvpn lafawenrvp
       61 fiawsivpyw svnlfyaval fvndspeqvd rlakryltaq iiavlcfvaf pltatfvkpa
      121 tagipgfmfd vlggfdkpfn qapslhiall iiiwdqmrrv mggavrvvwh vwclliglsv
      181 lttyqhhavd ipagallglf alwlfprsgs safagfqlta npkarrlgly ylagavlfla
      241 lgihglsvtg yaifwlwpat alaivalgyf gagagifqkq tdgsvsltsr wllwpyrlfa
      301 glnvrfwtrk lpphveladg vflgrfpkaa elssfatvid laaemvppph daewksfaai
      361 dlvappsekv qlaadaveaa rhhgpvlicc algfqrsatv avawlvstgr vanareaetl
      421 irakgwpvhl hlageaa
//
LOCUS       WP_176056215             339 aa            linear   BCT 11-JAN-2025
DEFINITION  TerC family protein [Brucella intermedia].
ACCESSION   WP_176056215
VERSION     WP_176056215.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023492
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..339
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=37911
     Region          16..321
                     /region_name="R_switched_Alx"
                     /note="integral membrane protein, TerC family; TIGR03718"
                     /db_xref="CDD:274743"
ORIGIN      
        1 mdslivalsg dflgtpvyfw aafivvvvgl lvfdlgilhr deheieakes lllygfyvli
       61 alafggwvww qrgaeaglef ytgylieqsl amdnmfviat ifgflgiprl yqhrvlfwgi
      121 lgviafrail iglgaalvhe fnwilflfga flvftgfkmf ghkdetpdie qnavfkflrr
      181 rfnitselhg rnftvkqphp ktgkmvtwlt plavalimve tvdlifavds vpavfavtqd
      241 tfivytsnif avlglralyf alaaamnrfr ylqvslaiil vligikiflv plgvhintll
      301 sliatlaila sgvlyslykt rnepdvsved lakqhhten
//
LOCUS       WP_176056265             329 aa            linear   BCT 11-JAN-2025
DEFINITION  SPFH domain-containing protein [Brucella intermedia].
ACCESSION   WP_176056265
VERSION     WP_176056265.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Gehl,B. and Sweetlove,L.J.
  TITLE     Mitochondrial Band-7 family proteins: scaffolds for respiratory
            chain assembly?
  JOURNAL   Front Plant Sci 5, 141 (2014)
   PUBMED   24782879
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Lapatsina,L., Brand,J., Poole,K., Daumke,O. and Lewin,G.R.
  TITLE     Stomatin-domain proteins
  JOURNAL   Eur J Cell Biol 91 (4), 240-245 (2012)
   PUBMED   21501885
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417211
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..329
                     /product="SPFH domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=35827
     Region          22..292
                     /region_name="HflC"
                     /note="Regulator of protease activity HflC,
                     stomatin/prohibitin superfamily [Posttranslational
                     modification, protein turnover, chaperones]; COG0330"
                     /db_xref="CDD:440099"
ORIGIN      
        1 mtgfditlli laalvlatlf agiktvpqgf nytverfgry trtlnpglnl ivpffdriga
       61 rlnmmeqvld vptqevitrd naivgvdgva fyqvlnaaqa ayqvanlqya ilnltmtnir
      121 tvmgsmdlde llsnrdaind rllrvvdeaa hpwgikmtrv eikdinppad ivtsmarqmk
      181 aerdkraqvl eaegdrnaqi lraegqkqsq ileaegklea akreaearer laeaeakatt
      241 mvsdavsngn vqalnyfvaq kytealsnia saknqkvvlm pleassligs lggigaiare
      301 vfsdgnrpvd ptpqppapsr prnvppatr
//
LOCUS       WP_176056293             246 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Brucella
            intermedia].
ACCESSION   WP_176056293
VERSION     WP_176056293.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..246
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27489
     Region          6..243
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 msdkaitmng vnkwygqlhv lkdinlevdr gehivlcgps gsgkstlirc inyleeiqdg
       61 iidinrtrlg htganvdhir rdvgmvfqqf nlfphmtvle ncmlaprrvh knslpearek
      121 amhflkrvhi aeqaekypaq lsggqqqrva iaralcmgpk imlfdeptsa ldpemvkevl
      181 dtmisladdg itmicvthem gfaravahrv ifmdrgeiie sappaeffgn pkherakafl
      241 gqilnh
//
LOCUS       WP_176056303             734 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Brucella intermedia].
ACCESSION   WP_176056303
VERSION     WP_176056303.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 734)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..734
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=80486
     Region          22..734
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mntsgaarkq gtknprrtsv kslletvilg gaasiaiasp saaqetgilk ldtieiqtsd
       61 gkgprapveg yiaehsraat ksdvpirevp qsisvvtrdn mndravqsvs eamlysanvn
      121 aqrygadvrs dyftvrgfpa dlyldglrip qiasqsggys gfvvepysle sveilrgpss
      181 alfgqsnvgg ivnmvskqpq aeasheiylr ggsferkefg aditgpinnd prftyrlngi
      241 frdsntsydl gkndriainp sfawrpdadt slvvsggylk ddmgqagvii paygsvlpnp
      301 tgqtisrdfs dgdprnaiyk keigyagydf ehrfndtftl rqnfryshmk tdyrnlftgv
      361 iptkgwdght iprtnylaqp eldaiafdtq lesrfdtgpv ahtllvgfdq qwqrldnyta
      421 sasgptqdlf nptygqplae lspttrllqk qyqtgiyvqd qieagklrvt lggrkdfvsi
      481 rseqtalasg kttdyeqdpd kftgrvgvay lfdsglvpya lystsflptl tladtplkpt
      541 tgtlkevgvk yapegedytv tlsafeaeqq nvvnrisgvy yqtdevrvrg ielegtarlw
      601 drlnltaals fqdpevsesq npdqigklpy tvpknqqsvf lsydmplpgn iegnlvvggg
      661 vrrigktagd tlntfyvpsy tlvdaflryd igsyrlqvna fnlgdkkyva gcnstsqcyy
      721 gqgrsivatt svrw
//
LOCUS       WP_176056282             276 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Brucella intermedia].
ACCESSION   WP_176056282
VERSION     WP_176056282.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..276
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30036
     Region          16..260
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mgdisenpks gaalnsslvk aihilkglaa stddgvrlid lardlelsqp sthrllktli
       61 aenlveqlpd kkayrlslef famaaqarqr dgilsiarps llrlsttfnd tvfllvrsnf
      121 davcldrveg pfpirsftgd iggkvplgig qgslailafl peeereaiir fnmprildks
      181 avdevdlrim iaevretgas tfnfnmidgm aglgvpilnr dgeavaalsi gtlaarltek
      241 rqetvtellr keaaiisqrl npfdptlrhp nqallk
//
LOCUS       WP_176056318             327 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella intermedia].
ACCESSION   WP_176056318
VERSION     WP_176056318.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..327
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35158
     Region          8..321
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mgdtqepvid vrnlrvdfpg rrgtvtalsd vslsirpgei lgvvgesgag ksmtglaiqg
       61 llerpghiag gevwlgkrri dtlddramek irgreigaif qdpltslnpl ftvgaqlvet
      121 irrhlglgka eararavqll rdvgipspee rvnqyphqfs ggmrqrvvia lalaaspklv
      181 iadepttald vsiqaqiisl lrklckekqt avmlvthdmg viaeaadria vmyagrliei
      241 gpveqvlhqp rhpytqglma sipslgarve klnqidgsmp rldaipdgca fnprckvagp
      301 rclrerpdli fsdqtasacw lnaggta
//
LOCUS       WP_176056307             587 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease subunit [Brucella intermedia].
ACCESSION   WP_176056307
VERSION     WP_176056307.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 587)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 587)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 587)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 587)
  AUTHORS   Biemans-Oldehinkel,E., Doeven,M.K. and Poolman,B.
  TITLE     ABC transporter architecture and regulatory roles of accessory
            domains
  JOURNAL   FEBS Lett 580 (4), 1023-1035 (2006)
   PUBMED   16375896
REFERENCE   6  (residues 1 to 587)
  AUTHORS   Higgins,C.F., Gallagher,M.P., Hyde,S.C., Mimmack,M.L. and
            Pearce,S.R.
  TITLE     Periplasmic binding protein-dependent transport systems: the
            membrane-associated components
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 326 (1236), 353-64 (1990)
   PUBMED   1970642
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439527
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..587
                     /product="ABC transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63486
     Region          11..290
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
     Region          333..587
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 msvaavspag ttrarfrfgp lwlvapglvf liifflvpva rlmglsfena dagaitgahy
       61 trifdtdvyf rvllitfria amttmfsllf gyplaywlsr lperkrgmmi llvmvpfwts
      121 ylvksfawvi llgrtgvinq lslgsgvigs plemlhnefg vmigmvhaml plavltmlpv
      181 msgidrrltq asgtlgadsa ksfwlvyfpl slpgaaaagl ltfisslgff ivpallggrq
      241 qtmlaqliiv qvqeilnwaf agalaammlv aalvtcwvyd rvfglsslsg dtgaahkgkn
      301 gilrniglri leisalassr iamavrtllg qaitkrllgi ycflscaflm lptlivipia
      361 ftssqflefp ppgfsldwfr ayftsdlwls atvrsfgvaf atailatvig gfaalalars
      421 rsrwaglifa fflapmivpr iviavglfyl faqiglvatn tglvightvl alpfafvaia
      481 ailknydwrl dqaaatlgan kiqalrfvtv plirsgltaa flfafitsfd eltvaifvsg
      541 gikttlpkqm wddmilqlnp tlaavsvvvf livttlllaa eklrrss
//
LOCUS       WP_176056348             494 aa            linear   BCT 11-JAN-2025
DEFINITION  MATE family efflux transporter [Brucella intermedia].
ACCESSION   WP_176056348
VERSION     WP_176056348.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Putman,M., van Veen,H.W. and Konings,W.N.
  TITLE     Molecular properties of bacterial multidrug transporters
  JOURNAL   Microbiol Mol Biol Rev 64 (4), 672-693 (2000)
   PUBMED   11104814
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192102
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..494
                     /product="MATE family efflux transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52344
     Region          12..448
                     /region_name="MATE_yoeA_like"
                     /note="Subfamily of the multidrug and toxic compound
                     extrusion (MATE)-like proteins similar to Bacillus
                     subtilis yoeA; cd13138"
                     /db_xref="CDD:240543"
ORIGIN      
        1 mkqsidltta pinqalllfa lptlgssilq sangsidtiw igqllgeyal aattngnlvm
       61 flltafvfgf gmastiligq afgrrdieta rtiagttvgt fvplsivvav igwllapkvl
      121 allgtpetie plaraflqvt flampailmq tilmlalrgs gdavtplifm gmavlldivl
      181 npffilgwgp lpalgiagsa latavanyis laamlyyiyh rdlplrlrgr ellllvpdrk
      241 llklifvkgl pmgiqmivvs ssmltmmrlv nregvdttaa fgatqqlwty vqmpamalga
      301 avsamaaqni gagkwdrvss itrigtiyav lmtgalvgll lvadrqalqi flgaespaia
      361 igqhigqiat wgfiafgvtm vlfgtvrang qviwpliilf vsmypvrlgv aiglreqlgs
      421 dalwlsfpaa mlstllmsti lyfhggwrkn ssmrvdahel qgeaacvsqs teaapssnal
      481 apnaplvaev kags
//
LOCUS       WP_176056353             397 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Brucella intermedia].
ACCESSION   WP_176056353
VERSION     WP_176056353.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..397
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41141
     Region          22..368
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,149,
                     152..153,156,225,228..229,232..234,237,265,269,318..319,
                     323,327,343,346..347,350..351,354)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 meqvsgreda aptrapivtr eriavallfl mngyvfggwa pkipefaarl gldsagmglm
       61 ilvfglgsla mmpvagalsa hrgsgivvrm falafipall iiavvpnvvt avivmfyfgg
      121 tmaamdvsmn anavavekkm rraimsscha fwslggliga asggfliaqf gstvhalvtt
      181 vvaailiava wpsiiadtvh hrsgaekqkl tlprnplpwl vgvmalfsmv pegaiidwga
      241 yhmrqdlgas vtvagfgfaa fsgamaimrf agdlvrdrfg avktlractt iaiigmlivg
      301 lgnssttaii gfaicgigis nmvpiafsma gnmpgvnpsv glsiattlgy sgmlvapsli
      361 gfvakhsgfg vvflalpvll lvvlafssla ryadqkh
//
LOCUS       WP_176056434             811 aa            linear   BCT 11-JAN-2025
DEFINITION  PIG-L family deacetylase [Brucella intermedia].
ACCESSION   WP_176056434
VERSION     WP_176056434.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 811)
  AUTHORS   Viars,S., Valentine,J. and Hernick,M.
  TITLE     Structure and function of the LmbE-like superfamily
  JOURNAL   Biomolecules 4 (2), 527-545 (2014)
   PUBMED   24970229
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..811
                     /product="PIG-L family deacetylase"
                     /EC_number="3.5.1.-"
                     /GO_function="GO:0000225 -
                     N-acetylglucosaminylphosphatidylinositol deacetylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006506 - GPI anchor biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89146
     Region          37..173
                     /region_name="PIG-L"
                     /note="GlcNAc-PI de-N-acetylase; pfam02585"
                     /db_xref="CDD:426852"
ORIGIN      
        1 mltarqrier qksspalvrl hralgrlrst vtlmhtgahp ddeqsglmay lrfglgvrvv
       61 iacstrgegg qnalgpergg algiirsrem eeaarildcd vhwlghgpdd cvhdfgfskd
      121 gdgtfahwge eqiierlvra yraerpdivl ptfldvpgqh ghhramtrva eqairlaadp
      181 dafpehfadg ltpwqvakfy lpawsgggdt yddelpppda tltlhasgre eatgadfdri
      241 gewsrachat qgmgqwpekp kvewplhlkl pdsrsektlf dglpetlavl adglafenrk
      301 qlvhvpesve qaiaafpdre aiiknladaa knlktvltsa pdgflllhgh rlerkrqeid
      361 aalmeaaslf erayleqpil asgdetrlvi ehgsgaaeia itaepvlpet csiaceqqts
      421 erkvftvslm edaapsplfe pawrslggng qafvrlraqf ddhlaecgfd leepfaivpp
      481 aslkfdppav iisggeehlp vrlvvdgkad riaftsqngw nislngqsav lhgpsvpkpg
      541 ltnlqaainq npawqmqftn yphigrtvwr epavlpvlvl dvklpnaria yigggadnvd
      601 lwlkrmgfdv tdleahhlag dlsqfttivv gifafglrdd laaatarlhr fvedgghlvt
      661 fyhrpsdgwy pdqtpprklt igspslrwrv tnpdavvtvl kpehpllvgp nviseadwdg
      721 whkerglyfa sawddayqtl lsmhddgeqp lygalvsari gkgrhthtsl vlhhqldklv
      781 pgafrlianl mqpaeqlayd apheilmtlt p
//
LOCUS       WP_176056452             135 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Brucella intermedia].
ACCESSION   WP_176056452
VERSION     WP_176056452.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 135)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 135)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..135
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=15851
     Region          47..125
                     /region_name="Acetyltransf_7"
                     /note="Acetyltransferase (GNAT) domain; pfam13508"
                     /db_xref="CDD:463905"
ORIGIN      
        1 mtefqwieel paeryqefht fycnewwtre rsledvthml ahcdlllfcl dgndriagfa
       61 rvlsdftfka mifdvivaee yrgqglgqal verildhekl krvksfelyc pdrlvpfyek
      121 lgfvkgtssl lfsqp
//
LOCUS       WP_176056453             397 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter permease [Brucella intermedia].
ACCESSION   WP_176056453
VERSION     WP_176056453.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468467
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..397
                     /product="amino acid ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=42919
     Region          1..397
                     /region_name="BatB"
                     /note="ABC-type amino acid transport system, permease
                     component [Amino acid transport and metabolism]; COG4597"
                     /db_xref="CDD:443651"
ORIGIN      
        1 masysaterr qdsggtslly dprvrgifyq vivfgvviga iywivgntvt nlqraniasg
       61 fgflsgragf disqtliqys sdsnygrafl vglmntlyva algvvtasii gflvgigrls
      121 rnwlirkict vyvevfrnip pllviffwyf gvlsvlpqar dsialplgty mnnrgffmpa
      181 pvwgdgawll pvalligiva siviarwakr rqmatgqpfh tirvaaalii glpilaliat
      241 gfpisfdlpk lgtfnltgga qvkpeflalf lalsfytasf iaetvragvl gvnkgqteaa
      301 yavglrpgqt mrliivpqal riiipplssq ylnliknssl aiaigypdlv avggtilnqt
      361 gqsvevvaiw mviylgisli tsglmnwfna kmalver
//
LOCUS       WP_176056467             627 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Brucella intermedia].
ACCESSION   WP_176056467
VERSION     WP_176056467.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 627)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..627
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=69574
     Region          4..516
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          555..618
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 mlilddisvr iagrllidht svtlpagskt gfvgrngtgk stlfrvitgd lapetgsisl
       61 pkntrigqva qeapgtdeal ieivmkadke raalleeaat atdphriaei htrladinah
      121 saearagail sglgfsaeaq rqpasafsgg wrmrvalaav lfaepdllll deptnyldle
      181 gvlwlvdyvk rypytviiis hdrdllnsat ssimhldqkk isfwrgnydq ferqrhemle
      241 lqqkahakqe ahrkhmesfv erfrakaska rqaqsrmkal eklkpielyv esnvqpfrfp
      301 daekkaaspi ialdnadvgy vpgkpvlrnv tlridnddri allgsngngk stlakliagr
      361 ltpekgtltv spnlkvaffa qhqlddlvpe dnaiehvrkl mptepeakvr arvaqmglst
      421 ekmltpardl sggekarllm glatfhgpnl lildeptnhl didsreelvh alnafngavi
      481 liahdrhlie atmerlwlvr eggvktfegd ldeyrqivla dakgepvsdr ddnarvnkae
      541 qrklaaqkre amaplqkkik etealiqklq kqiqvfssql edpalyekep qkairinkem
      601 sdarsalada edkwlelste yeeamad
//
LOCUS       WP_176056482             217 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein, partial [Brucella intermedia].
ACCESSION   WP_176056482
VERSION     WP_176056482.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         <1..217
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          <1..168
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 apdgitvadl vargryphqs ffrqwskgde eaviaameat rvtdlsgrqv delsggqrqr
       61 vwiamvlaqe tpillldept tfldiahqie lmdlladlnr qgrtivavlh dlnhacryas
      121 hliamkdgmi vaegkppsiv teklvedvfg lpsviipdpv sntplivpkg revltgyqam
      181 ersksesgdf rydqgarstt rirldsrasn grwnhrd
//
LOCUS       WP_176056498             297 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Brucella intermedia].
ACCESSION   WP_176056498
VERSION     WP_176056498.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32459
     Region          11..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..285
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(110..111,113..114,117,121,123..129,221..226,
                     232..233,235..236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrvgeivefn tflavaeagr fasaavrlgv tpsavsqsir rledrlglrl fvrttrsval
       61 teageallhq vkpaldqlag vdsiladghs stvgrgrvsv sgaamellia pilpafraah
      121 pgftleivve dritdpvagr ydavirrgsl lekdmiarrl sdddrlvlva sgrflaqegp
      181 fahprdlgrh rilirrprsg aalpwtlsrn vdtvrvdaea slivdsaiaa rqfamaglgi
      241 allahefvvr elktgllhlv mpdwqqpveg fhlmyvhrgh lphplwefer avrqnak
//
LOCUS       WP_176056506             625 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator [Brucella
            intermedia].
ACCESSION   WP_176056506
VERSION     WP_176056506.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..625
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=68084
     Region          3..623
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mvstlshike iervamggat drdqpviqsw lrclneyrln partqqayiv pdtllkehre
       61 qseelirigr sglealfrqv vdqgyvllls dargvtvefm gdptvdnqlr kaglylgsew
      121 sedragtcav gacmvsgqpv iihqddhfda shisltctaa pifdtfgdls avldisqlrs
      181 ptakasqqla lhlvtstarr ielanlmtra redwvlrlar lpdfldvdpd aaitidgsgt
      241 itgmthggfg avargmnlst istrdfigkp issifdidid qlpalmrgrp ngerllrarn
      301 glalfasaia pvssfrapat sisvrlpaal rqlsfgdram ealqaraakl adrhipilik
      361 getgsgkeyl araihdsnak pgpfiavnca aipeqliese lfgyvpgaft gamqkgktgl
      421 ieaanggtlf ldeigdmpla lqsrllrvls eseiqpvgal kpkpvkfrll sashrdlaal
      481 aaegrfredl lyrlnaatlt lptlrqrqdf dnlvdhllrr igeeegetit ldraarkvla
      541 gygwpgnlre ldntlrvaaa iatdatitid clpehfqaei amgngrtdrq alrreldacg
      601 nnisalarkl gvnrstihrr lkqth
//
LOCUS       WP_176056553             600 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella intermedia].
ACCESSION   WP_176056553
VERSION     WP_176056553.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 600)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..600
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=65623
     Region          3..554
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mntsspllqv rdlvtqvatp dgartvvdrl sfdlqsgetl ciagesgsgk smtvlslmql
       61 lpkslarvtg gtavmngrdi lklnenqmrs vrgrqigmif qepmtslnpv ltvgrqlaea
      121 vaneagpngg lsdaalkqrc kdlldqvqis dssrrllqyp yelsggmrqr vmiamalaqk
      181 peilladept taldvtvqsq ilalirklqa engisvilit hdmgvvaema dhvlvmnkgr
      241 eveqgplrdv fhhprdeytq rllaalprlg emtgtdkpkr apaepktepa rapsspilev
      301 enlvvrfdik ggilqrpvrr vhavegvsft vnrgetlslv gesgcgkstt gkallnlvpw
      361 sgdiridgks tkglsrtamr pvlrdiqmif qdpyasldpr mrvgdlvgep ltihglvsgs
      421 elkdrveylf rrvgmsadqm kryphefsgg qrqriciara lslspkliva desvaaldvs
      481 iqaqvldllq diqnetgvsy lfishdmavv eqishrvavm yagrfvetgt raqvfenpqh
      541 aytrrlmsav pvadpdrerr lfvanegelp spvksldyva phlehvelgg ghsvwreada
//
LOCUS       WP_176056614             334 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella intermedia].
ACCESSION   WP_176056614
VERSION     WP_176056614.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..334
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34277
     Region          8..334
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msttennspt swfgserrrl vvqeygifia flllatilsf sneyfltagn isnvllqtsi
       61 ngilaigmtf viltrgidls vgsvvalagi vsaslattst tagiagapys pfiaipvgll
      121 vgigcgalvg tivsrfavpa fvatlgmlsa argltliygg gkpvpalvpd frwigtgnil
      181 gvpvpvilla ivflvswwil nrsrfgryiy avggnphaan tsginisrvr fsvyvisggl
      241 aglagmvlsa rtgsalpqag isyeldaiaa vviggtslsg gvgritgtli galiigvmnn
      301 gldlmgiqsy yqqvlkgali vgavmldqkr nqga
//
LOCUS       WP_176056701             108 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF736 domain-containing protein [Brucella intermedia].
ACCESSION   WP_176056701
VERSION     WP_176056701.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..108
                     /product="DUF736 domain-containing protein"
                     /calculated_mol_wt=12197
     Region          1..105
                     /region_name="COG5489"
                     /note="Uncharacterized conserved protein, DUF736 family
                     [Function unknown]"
                     /db_xref="CDD:444240"
ORIGIN      
        1 makigtftrn ndgffgrirt ltldaevtil pidetdaena pnhrifadgl evgmawdrtg
       61 eragaylsva iddpsfvepi rarmfesdtk kdvwnlhwtr ktrrdeqa
//
LOCUS       WP_176056619             314 aa            linear   BCT 11-JAN-2025
DEFINITION  carbohydrate kinase family protein [Brucella intermedia].
ACCESSION   WP_176056619
VERSION     WP_176056619.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..314
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_function="GO:0016773 - phosphotransferase activity,
                     alcohol group as acceptor [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=32831
     Region          4..302
                     /region_name="RbsK"
                     /note="Sugar or nucleoside kinase, ribokinase family
                     [Carbohydrate transport and metabolism]; COG0524"
                     /db_xref="CDD:440290"
ORIGIN      
        1 mshdvsvvgl yildvlgrpv daippggnve fideirltva gtaggtvvdl aklglnclav
       61 gavgddekad fviatlqrfg vdtarmqrle gvptsasiln irhngdrpal hargasdhfe
      121 iadsaldavl appiihlggt gllakldgep srkllaeaka rgrtttfdll gandgtldli
      181 aplfphidyf mpsieeakqi sgaedvegag afflergvkh cvftlggdgv cfmdasgqiv
      241 rqpafqievv dttgcgdafd agfitalhhr melktalnfa qasaalvatg lgsdagirsf
      301 detlafmntv pvrq
//
LOCUS       WP_176056712             180 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Brucella intermedia].
ACCESSION   WP_176056712
VERSION     WP_176056712.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..180
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20093
     Region          12..152
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 merldridwv yaglsalseg giaavrvell akrlgitkgs fywhfarred llgamieewe
       61 rsqtasvite veslggdpyq rlqhlsdals eldlrleaai rgwggsdpdv rktieridta
      121 rlvylqsvie sagvptlpaq ararlvyfal igelisgrad wledhqeaml lnrtmlltwa
//
LOCUS       WP_176056721             245 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Brucella intermedia].
ACCESSION   WP_176056721
VERSION     WP_176056721.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..245
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=26876
     Region          14..219
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mpfpprkamp nkllallpta dyeaiigeta hvelprgtll aeqggpikkv yfltegigsv
       61 vvttaegkqa eagifgfdgy vptsaiagie nssydvvvqv aakgyemsyg dfrrwmeenr
      121 nfsgimirsi eafsvqlayt avsnaihevp qrlarwilmc ddrisgneia ithkflsiml
      181 gvrrpsvtts lhvleglgli ksergvvfic nrpgleryar daygwperey srlmqgfasa
      241 ananl
//
LOCUS       WP_176056796             256 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Clostridioides difficile].
ACCESSION   WP_176056796
VERSION     WP_176056796.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10578810
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..256
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28367
     Region          7..178
                     /region_name="ABC2_membrane_4"
                     /note="ABC-2 family transporter protein; pfam12730"
                     /db_xref="CDD:403819"
ORIGIN      
        1 mkelldiisc efsklkrlkf ilisilgacl fpipatiliv kdnlpfeqlf klvvnfgyfl
       61 llpivlsiva sqlffierdn dvlknlatvp vqkgklalak lavllfislf ysvaglgati
      121 iggfivgive gvavklgmsi afgimffvtv lpvvvlivyf nrsyifsiil sfvyaifnfs
      181 islniinfep nnpilsvlpa pvimrwwmaf wgdptgeyta lrqpyllstp acvgilclit
      241 iiavllicmi ykkqen
//
LOCUS       WP_176056838             124 aa            linear   BCT 11-JAN-2025
DEFINITION  siderophore-interacting protein, partial [Escherichia coli].
ACCESSION   WP_176056838
VERSION     WP_176056838.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>124
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
     Region          6..>124
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 agvgqivlgg eelegctsrg iddhsnlslp qpdaqfvapt vtedgivwpe gprrtwrdet
       61 plydgvrhgl aidffiredg vascwamqaq pggnltvagp sgslvvpedy adqlyvcdgs
      121 gmpa
//
LOCUS       WP_176056592             599 aa            linear   BCT 11-JAN-2025
DEFINITION  dipeptide/oligopeptide/nickel ABC transporter permease/ATP-binding
            protein [Brucella intermedia].
ACCESSION   WP_176056592
VERSION     WP_176056592.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 599)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 599)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 599)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 599)
  AUTHORS   Monnet,V.
  TITLE     Bacterial oligopeptide-binding proteins
  JOURNAL   Cell Mol Life Sci 60 (10), 2100-2114 (2003)
   PUBMED   14618258
REFERENCE   6  (residues 1 to 599)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439450
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..599
                     /product="dipeptide/oligopeptide/nickel ABC transporter
                     permease/ATP-binding protein"
                     /EC_number="7.5.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63468
     Region          11..286
                     /region_name="DppC"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, permease component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG1173"
                     /db_xref="CDD:440786"
     Region          319..588
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 msalpeisva ptavrmsswr llmsnrlaaf gffmlvlfcl villapvlpl pnpdatspam
       61 rlkpvfseeh llgtdqlgrd ilsrviwgtr vsvavgfaat liaaivgsai glvagyaggr
      121 tdnlmmrgid mlmafpyill alaivavlgp glmnalyaia vvnipffarn vcgvtlglah
      181 refidaarls gkspvsills evlpnvlpvi vitmsttsgw miletaglsf lglgaqppqa
      241 dlgsmlgegr aqlfnaphvs ivpglmifll vislnvlgdg vrdvldprll sgalgrpgai
      301 tdiakdrssp mikdsqkals iagletgfvn gghftpavrs vslelergec lgligesgsg
      361 ksvtalsvmg lvasppgrir ngaiylgdrd vlsmsetelt aargarvayv fqdplttlhp
      421 mypvgrqvee aiaahrriga serreqaivl ldkvgipdaa eranhyphql sggqrqrvgi
      481 amalandpdi iiadepttal dvtvqahile llrdlqrerg mallfithdf gvvseicdrv
      541 avmkdgeiie tgttsavlsn pqhsytkrli acvpqlgqga dflervaglf krengkavg
//
LOCUS       WP_176056934             452 aa            linear   BCT 11-JAN-2025
DEFINITION  TldD/PmbA family protein [Paraburkholderia caribensis].
ACCESSION   WP_176056934
VERSION     WP_176056934.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         1..452
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=49601
     Region          39..451
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 mmrdnrssvs psvsrpyfmt laneieqrlt aneialtsfs aeqsdfirfn egrvrqsghv
       61 sqasvtlrli dgqrqaystf tlcgdmaadt dtiaqaltal rdglrdapdd phllfdttvw
      121 settqragtl pspdtlpllv arcalgldfv gfyaggtmar gfasslgsrg wyevenfnis
      181 wslydasgra irshyagdtw sdavfagkve eaaarlpvls raprmltpgr yrtyfapaal
      241 relveaasls afsartqata rnefyrlnvg evaldprvtl tedlalditp rfnddgyerq
      301 svplieagra vaqltnarta reyglvpnga tageapsals mqggdlaqad elraldtgly
      361 ignlwyvnfs drmncrmtgm trfatfwveq grivapvdam rfddslyrll gselerigaq
      421 pelllndwtw geratggmkl pgllvrsfdl tl
//
LOCUS       WP_176056968             121 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator, partial [Paraburkholderia caribensis].
ACCESSION   WP_176056968
VERSION     WP_176056968.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia caribensis
  ORGANISM  Paraburkholderia caribensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Paraburkholderia caribensis"
                     /db_xref="taxon:75105"
     Protein         <1..>121
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
     Region          34..>120
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 vgrgsvfwfe lppalvepri lhvtsgaaii tgyegprrkv lviddvqinr avivelltri
       61 gfdtvesasg adgialaqte spdliltdiv mpgidgltvt rrframpafa rtpiiaisas
      121 p
//
LOCUS       WP_176057012             445 aa            linear   BCT 11-JAN-2025
DEFINITION  aminotransferase class I/II-fold pyridoxal phosphate-dependent
            enzyme [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057012
VERSION     WP_176057012.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..445
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=47658
     Region          77..443
                     /region_name="BioF"
                     /note="7-keto-8-aminopelargonate synthetase or related
                     enzyme [Coenzyme transport and metabolism]; COG0156"
                     /db_xref="CDD:439926"
ORIGIN      
        1 mglgdnirqq laakalmrql ervseeaqtp gaplaavgpr aaqaasraam csfetmpgyq
       61 qveilrqmge klqvqspffr vhdgiagatt riggaeylny anynylglag dpqvsarake
      121 aidrygtsas asrmvagerp vqreletala sfyevddcvv fvsghatnvt vigslfgpgd
      181 livhdslahn sivqgaqlsg akrlsfahnd wqaldallar vrhdyrrvli aieglysmdg
      241 dipdlaqfvd ikrrhaaflm vdeahslgvl gerglgvreq csvasadvdi wmgtlsktla
      301 gcggfiagsq alidilrhla pgflysvgla pslaaaslaa lerlvaeper vaqlrargrq
      361 fldearaagl dtgksagyav vpiitgstlk aaqwanamfa dginvqpify paveekaarl
      421 rfficsthep eqisrtiaal krlpr
//
LOCUS       WP_176057026             524 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Paraburkholderia
            sp. BCC1876].
ACCESSION   WP_176057026
VERSION     WP_176057026.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..524
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=56844
     Region          15..513
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mtwldallde pfvcitdmlr rfagergdha alicdgevls yaaldarvdr faaalqrdgi
       61 qprdaialca gasvdyvvaf lgglragaav aplapsssaa slvsmignag arllfldadv
      121 krllepvaeq isatpialds hagslpldtw lapqgavpaa vtidpawpfn iiyssgttgt
      181 pkgivqshgm rwayaartiq rgygpdattl istplysntt lvsfmptltf ggtvvlmpkf
      241 eatrylelaq qhrvthtmlv pvqyqrlmah pefdrydlss fqakfctsap faasikadvv
      301 rrwpgrltey ygmtegggsc qleadvypsk lhtvgqpveg hdvrlidelg hevavgevge
      361 ivghspammt gyyrqpekta eaewydpsgk rfirtgdmgr fdvdgfltll drkkdmiisg
      421 gfnvypsdle aevrehpdva dvavvgaqse qwgetpvafv vrrplaeina dtllawvnar
      481 vgkmqrlsal tfvdslprsp igkvlkrelr erfypaaheg ntsa
//
LOCUS       WP_176057107             352 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057107
VERSION     WP_176057107.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..352
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38205
     Region          13..352
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 miqpvskvld thaadielvh vskqygdala vdaidlriag gqyccllgps gcgktstlrm
       61 iaghesvteg diliagrnvt raepaargta mvfqnyalfp hlsaldnvaf slkmrgiakd
      121 errkragell elvamsayae rkpaqlsggq qqrvalaral lnqpgcllld eplsaldpfl
      181 rvqmraelkr wqkelaitfv hvthsqeeam aladlvvvms hgrieqsgtp hevfnrprte
      241 fvarflgghn vfksnghlft vradhlrivp hgvtpvqnag gdsgltrigg vpctvreaey
      301 qgthlrmtld pldgspelis lvsdgdydpa rlgpdarvvv wwneqdahpl aa
//
LOCUS       WP_176057095             261 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176057095
VERSION     WP_176057095.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..261
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29106
     Region          38..244
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mnddptnlle trsvttaqdp paapaapaaa sspgaanpla eqvyqqlknd ifsfrlfpgd
       61 rfsengiaqh ygvsrtpmrd glfrlqregy levgfrrgwk vspinfdqld qlydlrivle
      121 vaaverigag gdtahavlda lkavwcvepa qresdpvkmf gmdenfhrql vaatgnaeml
      181 rvhnevteri rivrrldflk phrtsatyde hstmlnlier grmteaiill rahitqskle
      241 vrkitlsmla aardsklpfv s
//
LOCUS       WP_176057108             304 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057108
VERSION     WP_176057108.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 304)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..304
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33789
     Region          17..304
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 matidlssra qdepvkhrra pawlqatplt ltfllffivp lvitlivsfw dfneyqiipa
       61 ftlknyaaif ngcssmtdic vtlktywstl kfcaivwavt lllgfaiayf lafhvrttsm
      121 qtvlflvcti pfwtsnvirm iswmpllgrn glvnqaliga hlidqplewl lysnfsvvla
      181 fvhlytffmi vpifnammri drslleaard agasgwqvvr dvvvplsktg ivigsifvit
      241 ivmgdfltvg vmggqqiasv gkiiqvqtgy lqfpaaaana iillavvlmi vwaltrvvdi
      301 rkel
//
LOCUS       WP_176057123             341 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057123
VERSION     WP_176057123.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..341
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36436
     Region          107..312
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mtlgdtikgm vgldptghad pdmkavldal kslnpkpiek ctvaearkqp tpadavkklm
       61 tqpafsarps leleavrted ivipgagghg nparvytpqg egpfplmlyf hgggwviadl
      121 dtydatprai aaqshaivvs ahyrqapehr lpaahddafs awhwlvenaa slggdpekla
      181 vmgesaganl ainvsirard agmhtpmhqt liypvasnni vsvsyeenrn arplnkpmml
      241 wfmqnvinse sdltsllidv vsadlsrlpp tvvvtagidp lrsdgetlvq klhtagvave
      301 hrnyrgathe ffgmapvvea ardaqafvsl aqrqafgaap l
//
LOCUS       WP_176057147             634 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057147
VERSION     WP_176057147.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..634
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=67398
     Region          143..610
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mcafdrrtll kgalaapwfg anwrvlaqpq pqplaqgpan aqadktieas easeaagptl
       61 rrvrpgdpaw pstdawqqln aavngrlsvv rsplavcaes pasqacadef krlknpfyig
      121 dtpaltqtcg wldawtsvps eyvvaageaq diasavdfar rhrlrlvvkg gghsyqgtsn
      181 aadslmvwth amrgitshda fvpdgcagrv kpetavtiga galwghvyaa vsaqsgryvq
      241 gggcltvgva glvqsggfgs fskrfgsaaa gllqaeivta dgvvrtvnac thpdlfwalk
      301 gggggsfgvv tqltlrthel pdlvgvvnat vkassetafr alvgefiafs aaslinphwg
      361 etvafrsdnt lrismvfqgl drdtamrvwq pffdwvange hgctttppqv ltasarhfwd
      421 paflaqhvpd altvddrpga dpgnvfwtdn lvdagqylyg ytstwlpaal laparrgdla
      481 dtlvqssrrw svtlhfnkgl agapadalna trqtatnpav ldafalaila dlgapafpgi
      541 aghepdtrng rrsatsiaqa tqilrtivpd pgtylsesdf fesdwqrayw gnhharlaav
      601 krqydpdglf fvhhgvgsee wsadgmtrvd aart
//
LOCUS       WP_176057148             215 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176057148
VERSION     WP_176057148.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..215
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23858
     Region          3..200
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mpyvlyyspg aasmavhwil ielgvafear lvdidigkqr epdylrlnps grvptlvvdg
       61 vprhesaall mllaerhpea gfapapgsad raewfetmif lantvlpamr dwfyaevdgd
      121 aagadavral aerrlveawd rldaqladkp gyliggklst vdlmalmlmr wtrnqprpat
      181 gwphlagyih qlralpsfie lntregltew lnpnd
//
LOCUS       WP_176057191             651 aa            linear   BCT 11-JAN-2025
DEFINITION  AI-2E family transporter [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057191
VERSION     WP_176057191.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..651
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=69665
     Region          38..373
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mkislpppqg rpnrvyppgt pslhglasvv tgvvvvcgly farevlipit lsvllsflla
       61 plvqmlrrlh mghlpsifia vlfalatlla vgglitaqlv qlagdlpqyq vaieqkietv
      121 qektvgrads lmsraaatlq rvapskpspp rltgraarna ppvptpvevh epsptpmqla
      181 qralspaiap iettfivlvv tifillqred lrdrlislfg srdlhrttta indaagrlsr
      241 yfvaqlgvnl saggtiaigl aiigvpgall fgviaallrf vpyigiwiaa ilavflaaai
      301 qpqwtmavyt lilfivvdvv agqiaeplly ghrsglspla vvvaaifwsw lwgpiglvls
      361 tpltlcvvtl gryadrlnfl tvllgdqpal tpaqnfyqrl laddpheaiv qaerllrems
      421 lidyydkval eglklarnda mrgvlmpdql qrindalvdi venleiadgl pdrmsrpdpa
      481 naagallasv sadlserhds hiaahpqlra naqktsvlcv pgrgafdevt tavavqllgr
      541 yglapmmath sgyrsarade psfqdapiic ivsldapesp pylrnmlrrt rewrpratlv
      601 vgvggaaegt petgatgash saptframie ecqaassvqh trqashvgga d
//
LOCUS       WP_176057200             232 aa            linear   BCT 11-JAN-2025
DEFINITION  O-methyltransferase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057200
VERSION     WP_176057200.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467877
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..232
                     /product="O-methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008171 - O-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24883
     Region          72..232
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
ORIGIN      
        1 mnslstgrva qtlqrmfaea eqadgalmaa fsesdqpeql ladsiaehfa eerrdlrgfy
       61 hgyvnnflnv tpaygqflyq caraskatri vefgtsmgvs tvylaaalrd mggghligse
      121 lepgkaarag anleaaglad lvdirvgdar etlaevpgei dlvlldgafs lylpilklle
      181 prlrsgalil aenafdygna yleyvrdpan gylsqpipia pgrgnelslv tr
//
LOCUS       WP_176057217             175 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176057217
VERSION     WP_176057217.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..175
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19099
     Region          26..164
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 msttkvrrts aavdpaavqt dplqaldrid railrqlqtd asisnvalaa kvklsapacl
       61 rrverlresg lirgvvalid pkaagagmlv iigvvldrst pesfaefeka aqkvagcmec
      121 hvvtgefdyf mtirtrdsds fnrlhaeqll ylpgvrqirs fmvlkeilst tkfpl
//
LOCUS       WP_176057269             275 aa            linear   BCT 11-JAN-2025
DEFINITION  siderophore-interacting protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057269
VERSION     WP_176057269.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Merrick,C.E., Gulati,N.M. and Wencewicz,T.A.
  TITLE     Siderophore-dependent ferrichelatases
  JOURNAL   Methods Enzymol 702, 281-315 (2024)
   PUBMED   39155116
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457194
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..275
                     /product="siderophore-interacting protein"
                     /EC_number="1.16.1.-"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /calculated_mol_wt=30449
     Region          8..266
                     /region_name="ViuB"
                     /note="NADPH-dependent ferric siderophore reductase,
                     contains FAD-binding and SIP domains [Inorganic ion
                     transport and metabolism]; COG2375"
                     /db_xref="CDD:441942"
ORIGIN      
        1 mltndhradl tvqrvrhplk frllqvkqvn altphlirvt ftgddlhdfv sasfddhikv
       61 ffpepgadrp alpeagpdgp vfpagqprpt ardftprrfd reareldief amheagpaat
      121 waaqakvgqy lgvggprgsl viptgfdwhl ligddtalpa iarrleelpa gtraaaviev
      181 adpsarieft traelhlvwc yrnetgyrge pllqavreiy lpedgegyvw aagesatmra
      241 vryhlcterg vdksriraas ywkqgavavh enldd
//
LOCUS       WP_176057261             141 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057261
VERSION     WP_176057261.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10022664
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..141
                     /product="OsmC family protein"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /GO_process="GO:0006972 - hyperosmotic response [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /GO_process="GO:0033194 - response to hydroperoxide
                     [Evidence IEA]"
                     /calculated_mol_wt=14211
     Region          3..136
                     /region_name="osmo_induc_OsmC"
                     /note="peroxiredoxin, OsmC subfamily; TIGR03562"
                     /db_xref="CDD:274650"
ORIGIN      
        1 mkrkasavwq gglqdgkgsi stdsgvlket qysfatrfad gigtnpeeli aaahagcfsm
       61 alsaelgkag itperigtta tvtldkdggg fsitavhldv avkipggdka afdkatadak
      121 agcpvskvln atitldakle t
//
LOCUS       WP_176057277             433 aa            linear   BCT 11-JAN-2025
DEFINITION  NCS2 family permease [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057277
VERSION     WP_176057277.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..433
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45416
     Region          1..431
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mdainryfgf daagtnlrte vlaglttflt mayiifvnpa ilgdagmpkd avfvatciva
       61 alaslimgly anypialapg mglnayfayt vvkgmgftwq aalgavfisg clfmivtlfr
      121 vrevivngip hsiriaitgg iglflaiisl ktagvvvgnp atlvtlgdlh sphvilavvg
      181 ffaivtldyl rvrgailigi vgvtvlsfff ggnqfhgivs appsitptlf qldirgalst
      241 gvlnvilvff lvelfdatgt lmgvanragl lvegkmhrln ralladstai lagsmlgtss
      301 ttayiesasg vqaggrtgvt aitvavlfla alffaplagv vpgyatapal lyvsclmlre
      361 mldlpwddat evvpaaltal lmpftysian gvafgfisya glklltgqar kvklvvwiia
      421 aiflfryfyl gse
//
LOCUS       WP_176057278             665 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator
            [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057278
VERSION     WP_176057278.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 665)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 665)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..665
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=72151
     Region          12..662
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mtqrpaspas igrpdviaqa harsveiglr asetpdfhpl rqpvlrelve rnqslythal
       61 pvmetlhaqi vdtqsmvllt dshgvilhsl gdsdfvekan rvalcpgvsw aeadrgtnai
      121 gtalvdgqpt vvhggehflh anriltcsca piadpfgrti galdvsgdtr gfhkhtlalv
      181 rmsaqmienh lfsnqfadai rvhfharaef igtlfeglaa fapdgrflsa nrsalfqfgq
      241 pltdlqrqpi dalfgiafak llqqitrapg esieltlpsg vrvvargeya tpryvapaes
      301 ragssrefgs gsaqatftaa qqrgepvpla tletldtgda hmatvlrrva klrgrdipll
      361 vlgktgtgke wlaraihhds prrsapfval ncaslpdtli eaelfgyedg aftgakkrgs
      421 igkivqadgg tlfldeigdm plaqqvrlmr vlqertvvpl ggtraipvdl rvicathrnl
      481 remieagtfr edlyyringl vvtlpalrer sdlaalvtri lalqpdgerl prrvsaavle
      541 rfaqcrwpgn lrqmanvlrt asimaegaeq ielddlpedf lqdcvdlvgg evvrplaavv
      601 arcddgdarg arvatqspar meewqatlit qtlarlggnv saaarelgla rntvyrylrr
      661 tgtth
//
LOCUS       WP_176057049             424 aa            linear   BCT 11-JAN-2025
DEFINITION  serine hydroxymethyltransferase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057049
VERSION     WP_176057049.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Appaji Rao,N., Ambili,M., Jala,V.R., Subramanya,H.S. and
            Savithri,H.S.
  TITLE     Structure-function relationship in serine hydroxymethyltransferase
  JOURNAL   Biochim Biophys Acta 1647 (1-2), 24-29 (2003)
   PUBMED   12686103
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Chan,V.L. and Bingham,H.L.
  TITLE     Complete sequence of the Campylobacter jejuni glyA gene encoding
            serine hydroxymethyltransferase
  JOURNAL   Gene 101 (1), 51-58 (1991)
   PUBMED   2060796
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10793727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..424
                     /product="serine hydroxymethyltransferase"
                     /EC_number="2.1.2.1"
                     /GO_function="GO:0004372 - glycine
                     hydroxymethyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019264 - glycine biosynthetic process
                     from serine [Evidence IEA]"
                     /calculated_mol_wt=45583
     Region          4..424
                     /region_name="PRK13034"
                     /note="serine hydroxymethyltransferase; Reviewed"
                     /db_xref="CDD:237280"
     Site            order(16,18,25..26,35,40,58,76..77,85,100,107,142..143,
                     268,286)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:99733"
     Site            order(39,59,69,102..103,130,180,205,208,233..234,240,366)
                     /site_type="other"
                     /note="glycine-pyridoxal phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99733"
     Site            order(39,130,234,366)
                     /site_type="active"
                     /db_xref="CDD:99733"
     Site            order(61,68,125,129,131,260,350)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:99733"
ORIGIN      
        1 msnpnpffee platrdaavr gailkelerq qsqveliase nivsravlea qgsvltnkya
       61 egypgkryyg gceyadviet laldrikqlf nakfanvqph sgaqangavm lalvkpgdti
      121 lgmsldaggh lthgarpals gkwfnavqyg vkrdtmlidy eqieelaqqh kpalliggfs
      181 aypreldfar lrkiadgvga klmvdmahia gviaagrhqn pvehahvvts tthktlrgpr
      241 ggfvltnded iakkinsavf pglqggplmh viagkavafg ealqpgfkty idnvlanaka
      301 lgevlkeggv dlvtggtdnh lllvdlrpkg lkgnqveqal eragitcnkn gipfdaekpt
      361 vtsgvrlgtp agttrgfgvs efrevgrliv dvfdalrdhp dghaateqrv rreifalcer
      421 fpiy
//
LOCUS       WP_176057306             373 aa            linear   BCT 11-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176057306
VERSION     WP_176057306.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..373
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=39741
     Region          35..186
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
     Region          161..345
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 msaqplsvna pmsaaalava faaiakqrsl grpvtdldlt radlrgvdws glvfkdvcla
       61 aadlsganls aarfldcdls garlgtatlm rtaligcdca alemvgasaq yltlmqchas
      121 gsdwrgatlq qstlsattlt garfdgtmll rsvlfdckvg ganfsgarld qaalaktdlr
      181 avtlsglsae tsvlmdcdfs glalpaislv rctlqgcnft dadlreatlt eancrqaifa
      241 rtrvdglrae rallldaqls dvdlshttlt gamlakaqlt rvrlngaqle qtvwhnsrli
      301 dvsfddarls yaqfdharga rvsferawle haslhdacfe qasfagahty rmkstdtall
      361 daerptlqle tlr
//
LOCUS       WP_176057289             338 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057289
VERSION     WP_176057289.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..338
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34904
     Region          20..319
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 makpdsallt rkretplqwe vllvivlias lilgralspv flsganlsnv ladlteialm
       61 alpmtliiva aeidlsvasv lgassalmgv lwhmglpmpv vivlvviaga lagllnglvi
      121 vklnlpslav tigtlalfrg layvllgdqa vadfpagyta fgmdtlgasf iplpfviviv
      181 gavlftvllq stafgrslya iganptaaaf sgievaklrl rlfvlsgams alagvvytlr
      241 ftsargdnge gfelsviaav lfggvsifgg rgsmigvlls lliigvlkna ltlddvsset
      301 ltivtgvlll asvlipnlva rwraardrrf iaksassv
//
LOCUS       WP_176057315             523 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057315
VERSION     WP_176057315.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..523
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53427
     Region          20..450
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(27..28,31..32,35,67,117..118,120..122,125,145,
                     148..149,152,276,279..280,283..285,288,316,320,372..373,
                     377,381,397,400..401,404..405,408)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mktvtshgea sakplilaav clsalvlpla fsggavatpa igrdlggsag altwitnafm
       61 lsfgsllmaa galadqfgrk rlfvaglggf ivasvalsla psvawldalr alqgvaaaas
      121 lasgsaalaq eftghartra fsllgtsfgl glafgplmag alithfgwra ifvaiaaiga
      181 lafvfgvprm retrdpaatg ldwpgtlsft gtlglftvav iqapqagwss alvvgllgas
      241 avmlavfvtv elhvarpmld lslfryprfv gvqilpvgtc ycyivlivml plrfigaegl
      301 semeagllmi alsapllavp llvaaltrwi sagvlsglgf liaaaglywl scvdigasrg
      361 saivpmlivg igagmpwglm dglsvsvvpk eragmatgif sttrvagegi alaivtaila
      421 glaqhsltri tadgspamte riaeaaqrlt tgdlasaaas lpqisrhela lsytqaftsl
      481 lhvlivitll sacasfafls rtgaqqneqd neplqeaees avv
//
LOCUS       WP_176057320             224 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057320
VERSION     WP_176057320.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..224
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23573
     Region          12..176
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 mtsfdhqrrp lvigiggttr aassteralg falrgaeaag aqtrlfggtf lhslphyape
       61 npartdeqle lieavrhada liiatpgyhg gvsglvknal dtleelrade rpyldgravg
      121 civtaygwqa agsvltslrs ivhalrgwpt pfgagintle trfdsvdtcs dpkvvdqlat
      181 vgqqaaqfal afashrtpsa apvsgaqnea arnetqparl lhav
//
LOCUS       WP_176057349             416 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057349
VERSION     WP_176057349.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..416
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43505
     Region          18..399
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(27..28,31..32,35,70,117..118,120..122,125,150,
                     153..154,157,229,232..233,236..238,241,271,275,325..326,
                     330,334,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mstthskrya pvfnpttlvi lagalvlsaa mgirqtfglf igpfsfdrgl pvtqiafaia
       61 lhnlvwgfaq pfagaaadry gstpvvafga ttfaaglafa avapsgamli igmgllvgig
      121 vscttfgvvl pavsriatpe krsmamglvs aggsagqvlm vplaqgvrls wgiaaslfvl
      181 aflmllvapl gmvldrrqrt gmpvretaae plrkvlglav rhrgyrlltl gfftcgfqla
      241 fiathlpeyl tlchmpvglg atalaliglf nmagswacgw lggryrqhhv lgwlylirsa
      301 tigtffalpk tstsvivfaa vmgltwlgtv pltsglvakv fgtrhlgslf gvcflshqmg
      361 sflgawlggl vfdltgsysl lweatvaagl faailhfpid datvnaptlr aepasa
//
LOCUS       WP_176057411             395 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176057411
VERSION     WP_176057411.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..395
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42615
     Region          30..385
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mgwkswksla ietpvwlagr fypprfdprr ampreilvlr pndfgelltt tplfealrkr
       61 fpttrliagi gawgrpilen npfvdeivei dapwnnklvd drshrnvlrf lwrspqvaal
      121 rarggvdvgi dvlgsymgav llmragaryr igvrgyrggw sgcqahiefa arqcgraala
      181 qaellgatel pearpqlflt dderahatri wsacadasgr rvvrivagvg agvsskawda
      241 rqagaalaqi araigkggdv cdvvivgsva dqaraaeait tagmgvsirs vagqapmrit
      301 falteqadvv ltnssmlmhv aaafhrptva viggsitrpe rhdaiwgypp pyrsvspeqv
      361 vadeparnwp gvervvqavl esigrqrtpa adaaa
//
LOCUS       WP_176057456             938 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176057456
VERSION     WP_176057456.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..938
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=100738
     Region          37..827
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mstnqtlksf atgavdwnnr pvglnfgraq rtvghllalq hatlheslmg gisghltcvs
       61 ahdnlsptlf iglpvsvriv tdrgqlhtin tiikqvqtgq sdgdltvyql tvcdalslme
      121 krtnsrlfrg ktvidilsil lsewrqrspt larafefdls kldanrypar eitrqanepd
      181 aafirrllrr egitvfakag takesriadd apvhtlvfcd nplrlkqapa gavrlhprda
      241 gteqrdtvtl falhqrlipg rtsrpswdyk karidesiai anidqgesgn dlaelltdva
      301 ieiphvgdsw kdhdritrdr mlahefeaeq ydgvsgirdl avghwitltg dpvldmqpae
      361 krqfvitslt hdvwnnlpkg lteraqslfq ashhlvlpts tpvltisreq dtrykntftc
      421 vrrgvpltpa ydptvdlppt hlltgvvvaq egdevtcdel grvfvqiqgl dpvdhahaqg
      481 vgtkgypgds aplrvasgla gesfgqtfip ragmevllgs iggdpdrlvi lgvvsngknt
      541 ptrfshtgal pgnrylsgvk treikgnryg gqlrfddtpq qisvqlasqh gdsqlnlgyl
      601 thprdngygq hrgegaelrt daaaalraaq gillttyart qasggqldrd ellqllgecs
      661 dlfkslgdya gqhggqspda sgqhavastf eawtpgvgeg tsegmsrsqg lmalgaqags
      721 vnltpkthvt yagenidqva qqnlqllsgq rllasagqgv hvfgrgegvh aiagdgpvvv
      781 qaqqdtvtvt gqksvhvssv gdevivsgkt irlvaedgsy lqvgggvrlg ssgsfvahaa
      841 shdfldpdtd hvnppafsda gadqkfrlry sgtdggssgs rdgengraaa hpvpnrpyei
      901 tlrdgqkitg tsdsegltdl lardamhiah iqvfdakg
//
LOCUS       WP_176057447             180 aa            linear   BCT 11-JAN-2025
DEFINITION  DinB family protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057447
VERSION     WP_176057447.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Cooper,D.R., Grelewska,K., Kim,C.Y., Joachimiak,A. and
            Derewenda,Z.S.
  TITLE     The structure of DinB from Geobacillus stearothermophilus: a
            representative of a unique four-helix-bundle superfamily
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 3), 219-224
            (2010)
   PUBMED   20208147
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..180
                     /product="DinB family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20002
     Region          10..151
                     /region_name="DinB"
                     /note="Bacillithiol/mycothiol S-transferase BstA/DinB,
                     DinB/YfiT family (unrelated to E. coli DinB) [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2318"
                     /db_xref="CDD:441892"
ORIGIN      
        1 msaanlllkm fryqawanqe lldsmqglda ahhaeerhia lrlmnhclvv ekifaghlag
       61 nshgfasdnt pdtpslealr aelsaidnwy leyastvtpd mlshsipfsf tdgdsgtmtr
      121 eemlthvvih ggyhrgevgr vmkqvsassp qslqlpwdty avhlhrseps rrlhdvvaee
//
LOCUS       WP_176057438             303 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057438
VERSION     WP_176057438.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..303
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35087
     Region          86..242
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mdvlltilky svavvlvasl aeavvltvrr grhgydwraa avsvtdflvr eyplrwllpl
       61 afygdamnwv whhrlwtvpm nhwsgwvacf igqefcyywf hraahrtrwf wcnhavhhsp
      121 nqltlsaayr fgwagrlags qlffllapwl gmpprvvlif lslnllyqfw ihatwiprlg
      181 plewllntps ahrvhhasnl eyldgnyggv livfdrlfgt yiaerrdtpc ryglvqpvtt
      241 ynmltiefdh wralwrdlkt arslgevcgy lfkppgwrpd gdgattedlr rragppgiar
      301 eip
//
LOCUS       WP_176057473             442 aa            linear   BCT 11-JAN-2025
DEFINITION  uracil-xanthine permease family protein [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176057473
VERSION     WP_176057473.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..442
                     /product="uracil-xanthine permease family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45545
     Region          2..428
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
ORIGIN      
        1 mnsdpathsv dtrlpawqla lfglqhvlsm aaspvtavfl vsrmlslpgd mtvhligatf
       61 fvcgagtllq slgagsigar lpfvmvpgga pamlfaviat qtdlrtaaga ailtslfywl
      121 vlpvfarclr ffprvvvgtm lvlvsvslik iyagivvgqp gtpgfarpls lglavvtiva
      181 tiavarlfkg tvgrlavllg lvvgtlagwa vglmpaaglw dgplftlpal lpfgmprfdi
      241 laalpmlifs vismaeataq tvavgeitgk pidmrrdvpr tirgdalasl vgsllgtsli
      301 itsaenigvv qttgvrsryv tatagamlmv valfaplgrl ayaipapvvg gtalivfami
      361 gvmginllgk vdlhargnqy tlaaalvvgl ipilvpnvya sfpgpvqivl gngmaagtlt
      421 ailvnlvfga wrlvptekiq pt
//
LOCUS       WP_176057487             459 aa            linear   BCT 11-JAN-2025
DEFINITION  CpaF family protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057487
VERSION     WP_176057487.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008984
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..459
                     /product="CpaF family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50824
     Region          59..443
                     /region_name="CpaF"
                     /note="Pilus assembly protein, ATPase of CpaF family
                     [Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG4962"
                     /db_xref="CDD:443988"
ORIGIN      
        1 mslreqlmmq ngnmpfdaag gaaaagvaae slaarrayqe lkmnihqaii drveldklqr
       61 lspeqikrel aqlverivde dkipmneler rrlaqdvhde mvglgplepl lndptisdil
      121 vntsqhvyve rrgrlehtdv tfyddahlmk iierivsrvg rridestpmv darlpdgsrv
      181 naiippsaid gplvsirrfa vnpltvadmv nnqsftpama qllealikak lnvlisggtg
      241 sgkttllnll sgfipederv vtiedaaelq mrqqhvlrle trppniegkg eisqrslvrn
      301 alrmrpdriv lgevrgaeal dmlhamntgh egsmatlhan tprdaltrle nmvgmagltm
      361 pikairqqia saitvvvqas rltdgrrklm siqeitgmeg dvinmqeift fkrtgvdeng
      421 mikgyfgatg vrpifyerla sfgislpdql fdparrlev
//
LOCUS       WP_176057497             401 aa            linear   BCT 11-JAN-2025
DEFINITION  aminotransferase class V-fold PLP-dependent enzyme
            [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057497
VERSION     WP_176057497.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 401)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424849
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..401
                     /product="aminotransferase class V-fold PLP-dependent
                     enzyme"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0031071 - cysteine desulfurase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006534 - cysteine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=42097
     Region          10..397
                     /region_name="CsdA"
                     /note="Selenocysteine lyase/Cysteine desulfurase [Amino
                     acid transport and metabolism]; COG0520"
                     /db_xref="CDD:440286"
ORIGIN      
        1 msallstaav ealrartpgt qhtthfnhag aslpssatle aihahlwrea ttgpmeagiv
       61 greqterarg laarlfnaqp aeialttgns pgwgaafaal gpwrageril vgrhewggnl
      121 gmmrglaqrv gvsidvipcd adgaadplal eamldervrl ialtwlpang glinpaaaig
      181 qvarrhgipy fidaaqaagq lpidvaelgc dvlstagrkg lrgprgtgll yvrqaflprl
      241 tppytdthsa pldargepvl rddagrfess eaalalhcgl analeealei gietirsqid
      301 svaqrlrvql aelpgvtvld lgaersglva fnlagldavt vqrslaaqgi vigsngvsyt
      361 pfdmtsrglq qiarasisyl ttdaeierll sqihtlvvqs n
//
LOCUS       WP_176057505             215 aa            linear   BCT 11-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176057505
VERSION     WP_176057505.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..215
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23173
     Region          6..198
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mqdwtnilaa vrvggwviyp ltilavlava ivldrayvfl rfgrlpktir nageigmpgs
       61 qidwedslke agrqnafrrm napwtpdpsa plwlrearae alasqierdm skgfwvleti
      121 vtaapllgll gtivgmmhsf qlfggsglvd pggvtggvaq slvataiglv valfalfafn
      181 yfsrrlerlm delesfanar lsevrlaata agaqp
//
LOCUS       WP_176057534             491 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057534
VERSION     WP_176057534.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..491
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49836
     Region          19..466
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(26..27,30..31,34,66,116..117,119..121,124,146,
                     149..150,153,290,293..294,297..299,302,330,334,386..387,
                     391,395,411,414..415,418..419,422)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mnspkpslsp algrilatvs vgfvvtqldv tivnialpki gadlhanvag lqwvvdaytl
       61 afavlmlsag vlgdrlgtrr myaagivlfa laslacglal datllvaara vqgigaaaml
      121 pnslallnra yghdpklrar avglwtaaga isiaagpvvg glliaafgwr siflvnlpic
      181 aagllatllw vprtettprd sqqttgihpa aprgidlsgq claivaltaf vaaviewrpl
      241 glshplvagg fvlalvaaga fiaveartes pmlplslfgk rsfsvavlfg icvnltyygm
      301 vfvlslylqr grgytplqag laflpltggf lisnvasgwv vgrfgvrvpm iagaitaglg
      361 ygllhfvdas tpliglllpf llipsgmgla vpamttavla saeakraata savlntarqa
      421 ggavgvaafg alasgaaapq ivagmqaata isvgllalgg mlscfihpqp htsssssrgv
      481 ddtrvgesrs r
//
LOCUS       WP_176057540             386 aa            linear   BCT 11-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Paraburkholderia
            sp. BCC1876].
ACCESSION   WP_176057540
VERSION     WP_176057540.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..386
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=41504
     Region          34..384
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mahifdapqf iedspslapn rdapqtpehi avvfdnvskq ftnargvstt alanvtlkia
       61 rgevfgiigr sgagkstllr lvngleqqgs gavrvngvsv gelnerelva lrrrigmvfq
      121 hfnllsaktv renialplki agvpkaeidr kvaallelvg lsakrdaypa slsggqkqrv
      181 giaralvtdp dillcdeats aldpettqai lallrdinrr lnltivlith emqvirevcd
      241 tvaviergav vengpvwrvf gdphhdatra llrtlvhdlp adlaervkpl hdlaqtdari
      301 lldvrftgad ahepdigglt salsseggsv sfvhggidri qghaqgrlvv saqvresads
      361 tvqkqiatll erarryanhv evlgyv
//
LOCUS       WP_176057562             536 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057562
VERSION     WP_176057562.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..536
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54242
     Region          107..510
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrrfnapfal ailataglag catssldmap dspdrpwqpr tdasgaivpg pagasgasga
       61 snaagasnal gasgvsatsa ggytlpanpa laavppppal eqahdynlpe lidlaesanp
      121 ltriawndar naalaagiak aaylpqlsaa amglyadahg sstsalgdss atasghgets
      181 vlalnwllfd fggraarvea asqgsviani gftavhqqvi fdvsvafysy qaararidtt
      241 rqgldnaeai laaaqsrykh gvgtvievaq anqnraqakl alvqaqgaes nsylmlisam
      301 gisplskpri atlpthalpa tmndsieqiv ssaiarrpdv lsayaaervn larvkaaese
      361 fmpkvfvsas gayhtgsssi savpaigqql ptvnlsgghy ggsvivgvti piydgglrsa
      421 vlaqarndad sattrlarsr eeavrqivaa qntlqtslsa qaaakellaa aqttydaafd
      481 ayrhgvgsvt dallaqnqll aaknadadsy sgalsaaaal alatgsvdsi ptqgsw
//
LOCUS       WP_176057602             285 aa            linear   BCT 11-JAN-2025
DEFINITION  carbon-nitrogen hydrolase family protein [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176057602
VERSION     WP_176057602.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163270
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..285
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30908
     Region          15..268
                     /region_name="nitrilase"
                     /note="Nitrilase superfamily, including nitrile- or
                     amide-hydrolyzing enzymes and amide-condensing enzymes;
                     cd07197"
                     /db_xref="CDD:143587"
     Site            order(53,125,129,132,157..158,160..161,182)
                     /site_type="active"
                     /db_xref="CDD:143587"
     Site            order(53,125,157)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143587"
     Site            order(126..129,138..140,158,160..164,167..168,194..195,
                     197..199,201..202,223..224,266..268)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143587"
ORIGIN      
        1 mnrnqaslpq tslriavaqa qpvsgdvaan iartveltgl aadrgaklvv fpekflsgye
       61 pdliagdpak yafeahdarl epirevcrrr eiavivgaat rharalhiss lifnrsgeqi
      121 epyhkqylys setsiyqpga qgcmleldgw rlalgvcyds gfpeharlaa vngahaylvs
      181 alfsvksgyh qsriwfpara fdntmyvlls nhvgttggws tcgasaiwsp ygdvvaeasr
      241 drddvitall dpavladvre retvladfna rdeaptgsyt thald
//
LOCUS       WP_176057634             354 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176057634
VERSION     WP_176057634.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 354)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..354
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38380
     Region          15..80
                     /region_name="HTH_MlrA-CarA"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     transcription regulators MlrA and CarA; cd01104"
                     /db_xref="CDD:133379"
     Site            order(16..18,32,49..51)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133379"
ORIGIN      
        1 mvtthdeqsp iqqgyksgea arlakmpvtt lriwerrygv igpaktasgq rlyteddvrr
       61 ltlikmlvsr ghaigaiarl dreqlqflas rnaregdgpp dfgvadtvdi klglvggnla
      121 qrlqgsgvdv rrygvntlst fadladaaaq sagksesida llvnvdslqe diaaqiialg
      181 dahqakamav vygfgtgpaa ellrvagvrl yreadgrtef rqmlgdlcer vriqertgdd
      241 avwsrvrrry ddpeleaiaa rsstiacecp rhlaelvmkl saferysdtc ssrsaqdaal
      301 hrylgdvsnr acamieaale rvareegwfa apalqaqaqs pspqqsplpq aate
//
LOCUS       WP_176057667             172 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057667
VERSION     WP_176057667.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..172
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=18135
     Region          6..158
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mnrqapltln vngathlvaa aadtpllyll rndlalngpk fgcglgecga ctvlldgvpt
       61 racvttakva lgreittleg lgtrtalhpv qqafieeqaa qcgyclngmi mtakalldrd
      121 phpsvetirr elsrnlcrcg thveivravq raaellaaqp aaqsavhesv rt
//
LOCUS       WP_176057670             647 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057670
VERSION     WP_176057670.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 647)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 647)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12379621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..647
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=68752
     Region          2..304
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
     Region          344..622
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mlsnllvqlv ngladastlf lvaaglslif gvtrivnfah gsfymfgiyv aysiasrfgq
       61 ttggfwlsvl aaalvvavlg alvemivlrr iyqapelfhl latfalvlif rdaalwlwgp
      121 edlfgpraph lagaveflgh plptydiali vigpvvllll wyaltrtrwg tlvraatqdr
      181 emlgalginq awlftgvffv gaflaglgga lqgprmsanl sldletigna fvvvvvggmg
      241 sipgafvaal iiaeikalci gighvtifgi gvslsrftlv aefvvmavvl vvrpwgllgr
      301 ataavrgmaa petplrpagk rlkwlaalal lvlvlaplaa nafpympvll veiliavlfa
      361 tslhfimgpg gmhsfghaay fglgaygaal flkvlnlpme aalllgplla vggalvfgwf
      421 cvrlsgvyla mltlafaqiv wsvvfqwddv tggsngvlgl wpsnwlsspv afyyltlvca
      481 vigvwllrkm lfsplgyamr aardsvlrae aigidvkrvq waafviaslf cglagslyaf
      541 skgtispevi svsrsvdglv mvllgglqtl tgpivgaavf twlqdtvarq tdywqallgl
      601 tilllviafp qgivgfirer fgddtvdnad sraaepsqrt aaikegl
//
LOCUS       WP_176057728             443 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057728
VERSION     WP_176057728.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..443
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47845
     Region          23..423
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,152,
                     155..156,159,257,260..261,264..266,269,297,301,350..351,
                     355,359,375,378..379,382..383,386)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mtsalapaad plesavskvk rhvlplflim fianyidrvn igfvnshmqt dlgigaaayg
       61 lgsglffigy alfevpsnvl mqkygarawl trimgtwglv aaamafvwnd tsfyvlrfll
      121 gvaeagffpg vvfyftqwlp qkdrgkavav flagsalasv lsgpitgsll sirgfglhgw
      181 qwmflveggf sivlcgvswm llksrirdas wltaeertvl etsiakeqae reahggahlp
      241 amkllkdpqi llfcflyfai qltiyaatfw lptiirkmgg ltdfqvgmln aipwliamva
      301 mycfavlssk wrfqqawlav alviaacglf astsgnpvls fvaicfsaig fkaaaslfwp
      361 ipqgyldarv aaavialins vgnlggffap atfgylqqht gsitgglygl gvasliaaaa
      421 gfltrdrrvn rdalpepvhr nah
//
LOCUS       WP_176057711             299 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176057711
VERSION     WP_176057711.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..299
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32615
     Region          3..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..287
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,219..224,
                     230..231,233..234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 melrhlryfv avaetgsltv aaerrlhtsq pslsrqirdl edevgaalfs rsargvelta
       61 agkafldhar laltqvdaai eaarrasrpa kqvfalgflt gqemtwlpra mqvlrdelpn
      121 vdvtvsshys pdladalarg kldlaflrae pgfdldykvv yreklivlmp sdhrltgraa
      181 iraedlvget fimasnkakv lhdvieqylq esgvtltpeh gvdnlamams lvastrglal
      241 mpeyannllp wsvvsrpleg dapgvdlvig ysrantspvl klflsraeel vmsaipasr
//
LOCUS       WP_176057736             551 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057736
VERSION     WP_176057736.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..551
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57557
     Region          42..526
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(49..50,53..54,57,89,139..140,142..144,147,168,
                     171..172,175,299,302..303,306..308,311,339,343,397..398,
                     402,406,422,425..426,429..430,433)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msthsnappr pdqptlesde paavrllgff sirkntlalg avclaslmfg leissvpvil
       61 ptlervlhgd fkgmqwimna ytlavttvlm atgtladrfg rrrifvigia lfgvtslicg
      121 laesvptliv arllqgasgg amlicqvavl shqfsdgper arafsawgii fgiglgfgpi
      181 iggmivavss wqwvfwvhav laivtlmllf ggvqesrdph ahsldiagmv tlslavfglv
      241 yfitqvsefg lassraifvl vatalafvaf lcaerftarp mfdfsvfrip pfsgalmgsa
      301 gmnfsfwpfm iylpiyfqig lgydsvsagl allaytlptl lfpplgerla lrygsgvaip
      361 aglltigvgf mlmklgsgva hpgvwsmlpg cvlagaglgl tntpvtnttt aavpperagm
      421 asgidmsarm itlainialm gailvggilf elkarlpgtl dmaslgrvae kiaagnvdai
      481 rtgipglaqi dpaggivhda lmqgfgwvml yggvgvaila vlsfvisgsa srklggkans
      541 vsqpavrcds c
//
LOCUS       WP_176057792             718 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057792
VERSION     WP_176057792.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 718)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..718
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78043
     Region          53..689
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mknrtrvsha alllfaiaah ahaatdespa tdavtdqaak pagnlaksdt ldvqvnarrl
       61 drarngllpe tgssvyrfsq adidalpagq dtplnqvllq apgvasdsyg qlhvrgdhan
      121 lqyringiii pepisgfgqa ldtriidqvn lltgalpaqy gyrtagvvdi rtksgdagdg
      181 gsvsvfggsh qtlktsadvf gtqgpfsyyf sgslgvnnlg ienptssana ihdhtrqgda
      241 fgymsyiinp ltrvslmfgt tsnqfeipnt pglatnftln gnntfnssql netqselnnf
      301 avvalqgtng galdyqvalf trytrtqfnp dpvgdllfng vasqdfhsns angaqvdttw
      361 rlndkhtira gvffqqehav fddnvnvfat dstgaqasdq pfnipdsssk tgylysayvq
      421 dewkitsklt lnyglrydkm deyvsasqls priglvyalt ptttfhagya ryftppafel
      481 vsgstisrfn gttnqspssq ndpvqpersh yfdlgvtqrl gsnvtiglda yykkstnlld
      541 egqfgsaliy tpfnyrlgrv ygleftanyk qdnmsaylnl aysraqgtqi dsaqfnfdpa
      601 elayinshwv yldhdqrita sfggtydlgr ttftfdglvg tglrsgfant drlpvyaqvn
      661 lgviqhfnqp lvgkfdarlm linafnrvye lrdgsgigvg apqygphfav yagitkhf
//
LOCUS       WP_176057808             143 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057808
VERSION     WP_176057808.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..143
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=15778
     Region          20..140
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 msrtpstcqr wsareirvlh emprvlvvdd nagaaealat ylsyegvear sangcaealr
       61 cvkdwvpdvv vldimmpehd gyetasalrs ylpthslgiv aftsldedhv ketgkarhnf
      121 dgycqkgtap tallalmrkl wre
//
LOCUS       WP_176057822              80 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy-metal-associated domain-containing protein [Paraburkholderia
            sp. BCC1876].
ACCESSION   WP_176057822
VERSION     WP_176057822.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 80)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 80)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..80
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7990
     Region          1..70
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mtiefqvegm scqhcvaavt nairehdeaa qvqvdlasgr vvvesaqsaq sadalkgaid
       61 eagytvksvt sgaagggalr
//
LOCUS       WP_176057853             199 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057853
VERSION     WP_176057853.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 199)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..199
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=22512
     Region          6..142
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(8,10,72..73,76)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            10
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(71,123..124,126..127,131)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(77,82..83,119,122..123,126..127,130,133)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(100..102,119..120,123..124,127,131,134,138)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(100,124,127,131,134,138)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(132,138..139)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
ORIGIN      
        1 mrklyygris ttdgqssasq yedarahgvq ekdvfidegv sgyhiapdar eqwrraehdl
       61 rhggvlivrw ldrisrryde lhrtmrrlmd lgvrvectln gmafdgkakd piekatrdav
      121 lafmaaqgea dyrnraemqr rgvaiakaeg kykgrvrshd ysaitawree hgasiratad
      181 efgigtatvk racaeerrl
//
LOCUS       WP_176057873             360 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057873
VERSION     WP_176057873.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..360
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=38749
     Region          17..360
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mlmkctriat lrrinhiaat valmvigvha qaqssvqlyg ivdtwiglqk tpgkasswqe
       61 gggglstsfw gfggqedlgg gyrtifaieg ffrpqngayg sfngdpffsr nayvgltmpa
      121 gtftlgrqss llylqacqfn pfyasftfsp tilqmyaglg typsyrtdqg ivggtawsna
      181 iqyatpdlhg ltghamyafg nsgsgngskq ysvqasyrng pfaagavyqy anfnstagdl
      241 nsllagfhsq satqlaasye fsfaklygey tytnddvinr gfhvnmfegg lsipigtsri
      301 lasyaysrds gglnqnrqta tlgydyplsk rtdlyavyly dhfaglssge tagvgirtrf
//
LOCUS       WP_176057938             451 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: APC family permease [Paraburkholderia].
ACCESSION   WP_176057938
VERSION     WP_176057938.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..451
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47664
     Region          15..440
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mtsssaaepa aahsthlkrt lglpsvllfg laymaplivy gtygvlasas ndtaalayli
       61 aliaiaftal sygklarlfp vagsaytytr ksfnphlgfm igwatlldyf flpmviwlig
      121 aaylsaafph ipswiwivaf ivltsalnil gielanrfni vlmvvqlaiv alfvvlcchy
      181 vtaaagpggl lsaepffkph vpfsatmaga aiaaysylgf davstlteet iapektmpra
      241 ivlialigga ifviaaytvq lahpgavfkd pdsaafevar kvggdlfvtv flaglilaqf
      301 asgisaqasv grllyamgrd evlpkrifgf vhpkfktpal niaiagaigl valkldvats
      361 tsfinfgafl aftavnlcvi rqffnakgta namgiiggll fplagaiadv wllvslekta
      421 lvlgavwfll glcylgwitr wfrqappeva v
//
LOCUS       WP_176057953             261 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176057953
VERSION     WP_176057953.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..261
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27845
     Region          2..246
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mslknglril dfltsqgega glvaiadals lprstchrvl telveggyvr qlvehsryil
       61 tmrmtsngle flsltgiadi aqpiiervaa qtgelarlsl adgeaiiwvg kadgqrigfr
      121 ydpdmgqaar lsctstghaw lmtmtdeqai alvlkqgfgq pnefgpnapt tikallgflh
      181 aarvrgyami devfaprmsa vatpvvsgsr cvgvislagp rmrltaekih eysvllreaa
      241 nelaqlsnma gfpgrpplgk g
//
LOCUS       WP_176057956             407 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057956
VERSION     WP_176057956.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..407
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43533
     Region          17..392
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(24..25,28..29,32,64,114..115,117..119,122,142,
                     145..146,149,222,225..226,229..231,234,262,266,318..319,
                     323,327,343,346..347,350..351,354)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mdttfsrkqk taaltslfia waagyadril istaiipira efnldarqag ivlsafyfsy
       61 aitqliggwl sdkigsrivv vacvaswsff tgatgvawsf aslvairllf gigegafspa
      121 ssvtiaevfp rkeraraksl listtflgna vgsgligltv arfgwrssft mlavmglvva
      181 ailwaslrgg mkaqrernan rhrtlwgpll rmpaawkiaa iwffasvlyv gvtswmpsyl
      241 mhtyhidlah tgmavaipnl lafigtnavg ylldrrakgh erafmiggal vsalsialmi
      301 nttsmtllmv yltvcllafn fvyasvfamp lryfpehlig satglmnfgg qmgatlapia
      361 mgalinasgg ayisafwlli gsavggvlva atwkpieprm gesvqps
//
LOCUS       WP_176057983             486 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176057983
VERSION     WP_176057983.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..486
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=53144
     Region          53..314
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mssirialsl iaslllgaca trpvnppmvq yesrqamqfq klernrgdpq dlvvlafsgg
       61 gtraaafsyg vlealrrtei vsksgertrl ldsvdvitgv sggsftalay glygeklfdi
      121 yessflkrnv qrelvsriln plnwpalssk gwgrsdlaae lydeilfkga tfddlnrang
      181 ptiavsatel stgsrlvflq qtfdvmcael gpfrlsraaa assavpvvls pitinnyggt
      241 cgyhepdwvr qftdtykppr pagrvlkrlq elrefgdaek dpyfhlvdgg vsdnlglrgv
      301 ldfietfeal raagkptpid nvrrfiifvv nsvsspsnqw ntsedppgsl diltkaagvp
      361 idrysgesve llkdinarwt alrelrdsaa fanskdpmpt yvahapnadm yvidvsfgal
      421 kdraeydyln qlptsfhlpd eavdrlraaa grliidspef qqmlkdagar vanepvsptp
      481 veraak
//
LOCUS       WP_176057978             395 aa            linear   BCT 11-JAN-2025
DEFINITION  ammonium transporter [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176057978
VERSION     WP_176057978.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..395
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41535
     Region          1..395
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 meslktgtdt lflllgaamv lamhagfafl elgtvrkknq vnalvkilvd fsvstiayff
       61 igytiaygvq ffgsaetlaa hngyalvrff flltfaaaip aivsggiaer skfnpqlfat
      121 fvlvgfvypf fegiawnghf giqdwlthvf glpfhdfags vvvhafggwv alpavlllgp
      181 rhgryhrdgg iaahppsnip flalgawvla vgwfgfnvms aqtvdkisgl vavnslmamv
      241 ggtltawlag rndpgftyng plaglvavca gsdlmhplga lvtggiagvl fvymftcvqn
      301 rwriddvlgv wplhglcgaw gglaagifgl ralggmggvs fgaqlvgtlg giavatlggt
      361 lvygairltv glrldqeeey ngadlsihri satse
//
LOCUS       WP_176058073             336 aa            linear   BCT 11-JAN-2025
DEFINITION  inorganic phosphate transporter [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176058073
VERSION     WP_176058073.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Forster,I.C., Hernando,N., Biber,J. and Murer,H.
  TITLE     Phosphate transporters of the SLC20 and SLC34 families
  JOURNAL   Mol Aspects Med 34 (2-3), 386-395 (2013)
   PUBMED   23506879
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Biber,J., Hernando,N. and Forster,I.
  TITLE     Phosphate transporters and their function
  JOURNAL   Annu Rev Physiol 75, 535-550 (2013)
   PUBMED   23398154
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Bottger,P. and Pedersen,L.
  TITLE     Evolutionary and experimental analyses of inorganic phosphate
            transporter PiT family reveals two related signature sequences
            harboring highly conserved aspartic acids critical for
            sodium-dependent phosphate transport function of human PiT2
  JOURNAL   FEBS J 272 (12), 3060-3074 (2005)
   PUBMED   15955065
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416760
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..336
                     /product="inorganic phosphate transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005315 - phosphate transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0035435 - phosphate ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=35396
     Region          6..319
                     /region_name="PitA"
                     /note="Phosphate/sulfate permease [Inorganic ion transport
                     and metabolism]; COG0306"
                     /db_xref="CDD:440075"
ORIGIN      
        1 mqsiqlaiwv vaglvavali fdfmngfhda ansiatvvst gvlkpqqava faaafnviay
       61 fvfhlkvaat vgkgtidphi vdhyvifgal vgaigwniit whygipssss haligglvga
      121 alaksgwgsl nfdgliktva fifispllgf vlgsffmlav swiyfrtpps kvdrrfrrlq
      181 lvsaglyslg hggndaqkti giiwmlliat gyassiadap plwviggcyl smgigtlfgg
      241 wrivrtmgqk itklkpvggf caesggaitl ftaswlgipv stthtitgai vgvgatrkls
      301 avrwgvagni vwawiltipa saalsaaaww lghrll
//
LOCUS       WP_176058083             180 aa            linear   BCT 11-JAN-2025
DEFINITION  group III truncated hemoglobin [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176058083
VERSION     WP_176058083.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Keppner,A., Maric,D., Correia,M., Koay,T.W., Orlando,I.M.C.,
            Vinogradov,S.N. and Hoogewijs,D.
  TITLE     Lessons from the post-genomic era: Globin diversity beyond oxygen
            binding and transport
  JOURNAL   Redox Biol 37, 101687 (2020)
   PUBMED   32863222
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Bustamante,J.P., Radusky,L., Boechi,L., Estrin,D.A., Ten Have,A.
            and Marti,M.A.
  TITLE     Evolutionary and Functional Relationships in the Truncated
            Hemoglobin Family
  JOURNAL   PLoS Comput Biol 12 (1), e1004701 (2016)
   PUBMED   26788940
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Wajcman,H., Kiger,L. and Marden,M.C.
  TITLE     Structure and function evolution in the superfamily of globins
  JOURNAL   C R Biol 332 (2-3), 273-282 (2009)
   PUBMED   19281958
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Vinogradov,S.N., Hoogewijs,D., Bailly,X., Arredondo-Peter,R.,
            Guertin,M., Gough,J., Dewilde,S., Moens,L. and Vanfleteren,J.R.
  TITLE     Three globin lineages belonging to two structural classes in
            genomes from the three kingdoms of life
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11385-11389 (2005)
   PUBMED   16061809
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Wittenberg,J.B., Bolognesi,M., Wittenberg,B.A. and Guertin,M.
  TITLE     Truncated hemoglobins: a new family of hemoglobins widely
            distributed in bacteria, unicellular eukaryotes, and plants
  JOURNAL   J Biol Chem 277 (2), 871-874 (2002)
   PUBMED   11696555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10172365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..180
                     /product="group III truncated hemoglobin"
                     /GO_function="GO:0005344 - oxygen carrier activity
                     [Evidence IEA]"
                     /GO_function="GO:0019825 - oxygen binding [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20430
     Region          18..127
                     /region_name="TrHb3_P"
                     /note="Truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins);
                     group 3 (P); cd08916"
                     /db_xref="CDD:381257"
     Site            order(30,43,46..47,54,57..58,61..62,72,74..76,79..80,83,
                     86,90..91,94,118,121..122,125)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381257"
ORIGIN      
        1 mnpsfpaapa veraaeptea nvrelvyafy drvradallg pvfdaslagr wdehlpkmcl
       61 fwgslvlgak qyrgnvqqah qplegvepqh fsrwlylfld tvesryepva airfmepalr
      121 iaqslqlsrf gwdyripaeq qallervapk rardeedahe aarrpgepfp triigramde
//
LOCUS       WP_176058089             158 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MerR family transcriptional regulator
            [Paraburkholderia].
ACCESSION   WP_176058089
VERSION     WP_176058089.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140959
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..158
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=18036
     Region          9..103
                     /region_name="HTH_YfmP"
                     /note="Helix-Turn-Helix DNA binding domain of the YfmP
                     transcription regulator; cd04774"
                     /db_xref="CDD:133401"
     Site            order(10..12,26,42..44)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133401"
     Site            order(56,59,63..64,73,85,89,95,99,102..103)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133401"
ORIGIN      
        1 mptdsptllt vrdaaerlgv tprtlkyyee rglvsptrse gryrlydeed lkrfgrilrl
       61 rslgfslhsv temlkrplep vdgglryste slqqihdaia qqvealdari esmrrelkea
      121 qklraelspd vdylkrrlag enaeallaqr rnaraksk
//
LOCUS       WP_176058180             414 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176058180
VERSION     WP_176058180.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..414
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45116
     Region          65..344
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mptlddfari aeaplhtwlg alivsvvaal lalgiqrvga rivtriarpy pltsvvlryi
       61 dkpsrlflvi laleavwwea pdtltfitpl rdaagiamig aitwlsvrsa aaigeaiiqa
      121 hpldtadnlq arrihtqarv larsvmlviv iigvggalmt fpnvrqigas llasagvagl
      181 vagiaarpvl gnliaglqia lsqpirlddv vviqgewgri eeitgtyvsv rlwdqrrliv
      241 plqwfienpf anwtrsssqi igtvflyvdy rmplaplree lariveaape wdrrvqvlqv
      301 tdgtersmql ralvssldsg lnwdlrcrvr egllefiqqh ypqylprara dvsaelengk
      361 gepldwvprg lhtpagstva hteadpvasr sgrlpvtdad aaaqaaqvka qekv
//
LOCUS       WP_176058181             388 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176058181
VERSION     WP_176058181.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 388)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Ammelburg,M., Frickey,T. and Lupas,A.N.
  TITLE     Classification of AAA+ proteins
  JOURNAL   J Struct Biol 156 (1), 2-11 (2006)
   PUBMED   16828312
REFERENCE   5  (residues 1 to 388)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   6  (residues 1 to 388)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   7  (residues 1 to 388)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   8  (residues 1 to 388)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..388
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42233
     Region          1..383
                     /region_name="COG4637"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443675"
ORIGIN      
        1 mlttlaiagy rslrelvvpl grlnvitgan gsgkssvyrs lrllaetarg gvitslareg
       61 glpstlwagp erfsrgmlag elpieplrrk dpvslrlgfa gdqfgyaidl glpplnrdtl
      121 fpldptikre ciwsgpvlrp sallvdrqgp alrtrdeqgd wqtipqpvas fdsmmtefsd
      181 prtapemitv reqirswrfy dhfrtdaaaa arlpqigtht pvlsndgadl aaalqtirei
      241 gdptalaaai ddafpgsqld istqdgrfev mmrqhgllrp lkgaelsdgt lrylllvaal
      301 ltprppallv lnepetslhp dllpalarli aqaalhsqvl vvshaarlia alereeesqs
      361 ivlekhfgat riadaddrdl pawkwpar
//
LOCUS       WP_176058289             466 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176058289
VERSION     WP_176058289.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..466
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50920
     Region          26..451
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(36..37,40..41,44,90,140..141,143..145,148,168,
                     171..172,175,287,290..291,294..296,299,326,330,379..380,
                     384,388,404,407..408,411..412,415)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 msnqqaaeia arldrlppsr tvwamvilis lggvfefydl fftgyvapgm vqsglfkpes
       61 lgpfaalapl avagfgtfvf atfaglwvga ltlgyvadrf grrviftwsl vwymvctiim
      121 afqttgyaln iwrfvagigi gvelvtidty iselipsrer graysvnqfi tfsvvpvvaf
      181 layalngtkp lgldywrvvi ligsvgavav wflrrnipes prwlarhnrf deaerivaei
      241 errvalekgi tlpppqavep ekegrgafre ifapgyrrrt iilsifnmaq vigfygfaaw
      301 vptllihrgi hvtaslgyaf viaianpfgp ligtlfadkl erktqicggl itmavviavf
      361 sqvstpwilt vlgvvftlaa nimsyayhgy qaelfptrir araigfvysw srisaafagl
      421 aigillhgyg vpgvaafigv smlvaicmil lgpatkglsl etinqh
//
LOCUS       WP_176058307             349 aa            linear   BCT 11-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176058307
VERSION     WP_176058307.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..349
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=37573
     Region          <15..341
                     /region_name="FAD_binding_2"
                     /note="FAD binding domain; cl46878"
                     /db_xref="CDD:481218"
     Region          49..73
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(66..67,70,73,97..98,101,104..105,108,159..160,163,
                     166..167,170,191..192,195,198..199,224..225,228,231..232)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          83..108
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          141..171
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          174..199
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          208..233
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          256..284
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          317..343
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mtdstllthd pdtlapeaaa llprladtdp vvrriallel adleepdtlp liahalahdv
       61 saevrreaar vlgsweeawi adalchalld adhdvrtaaa qslsalkdda cgpvlhrwtd
      121 haepfvqaav lrglrelrya dalepalral dhtddsvrte avvllgwlkd tralapladt
      181 vtgdtnadir raavgalgfa pathtatlta llqalsdpvw qvreetattl gklranaahd
      241 vhdvhdvhkv hkvhkvhdal iaaladdywq vrlravralg hmgeraaalp iaallsnpis
      301 nlrkeaalal gelrepatlp alrdalndad pdvrkavria lqqiedasr
//
LOCUS       WP_176058368             385 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176058368
VERSION     WP_176058368.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..385
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42080
     Region          1..378
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mfhdwtpeql tlrerfaavg eqlakardqq pegfdyagwn rlrdeqlwhl vvprdygghg
       61 edwwgftaal dglsstirtp elllsviaqa gmvramvrhg splqkeryla aimrgkvsat
      121 giaepstgtd vrsiettlse apdgyrlngs kyniahapim dfilvvsrle rressnialv
      181 lldrdtpglv igaqddklgn rnlptgelrf ddihvdasqi lgqagrglgh lidiislgrl
      241 yyglvaanlp lpfvdeamhy aaqrtsfkst idshqyiqkr lvdmkigmer srwaaygalg
      301 rllnahpeal lacsvaklvg asdlidnats lvklygsigy hnggiatllk damgfasvgg
      361 teemhrknif nqmqrlagsa sssqg
//
LOCUS       WP_176058375             219 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent F420 reductase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176058375
VERSION     WP_176058375.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..219
                     /product="NADPH-dependent F420 reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016651 - oxidoreductase activity, acting
                     on NAD(P)H [Evidence IEA]"
                     /GO_function="GO:0052851 - ferric-chelate reductase
                     (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22827
     Region          3..203
                     /region_name="COG2085"
                     /note="Predicted dinucleotide-binding enzyme [General
                     function prediction only]"
                     /db_xref="CDD:441688"
ORIGIN      
        1 mkigilgagf igramatlak qsghdvmisn srdpstlmst aaalgcalgt aqqaasfgdv
       61 vvmavpfsqi galpvaaldg kividtcnyy perdgpiaal derttttsqm laallpgskv
      121 vkafnailaa dlhtdgrpvg apqrralpfa gddaaakqvv sglmdqfgfd pvdvgalrds
      181 wrferakpvy cvpfdrdgmv aglaaaqrdv elphgswrk
//
LOCUS       WP_176058476             312 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176058476
VERSION     WP_176058476.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..312
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33800
     Region          12..71
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..298
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(110,114,153,167,170,233,250,277)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(111..112,116..117,119..120,123,127,129..135,197,
                     227..231,238..239,242)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mkqnftvrqg aldgvevfls vaqhrsfrra aaelgvtpsa vsqtvrvlea rigaalfirt
       61 trsvglteag erflahakpa feelvaasev argfgqrptg llrlsvprav lpilleplia
      121 sfcqaypeve veisaskelv dlaaegfdag irmgqfvdad mvavpltppl rlivvgspdy
      181 faahsppeht ddlrqhaclr wrrssgalal wsfndngqti eiavsgplia ndfstmlgga
      241 iegmglaqvp epmaaqrlra gqlvhvleqf apvipgvfly ypnrrqimpk lrafidhvkr
      301 rpaaqskvpg kr
//
LOCUS       WP_176058492             127 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF427 domain-containing protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176058492
VERSION     WP_176058492.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Lupas,A.N., Zhu,H. and Korycinski,M.
  TITLE     The thalidomide-binding domain of cereblon defines the CULT domain
            family and is a new member of the beta-tent fold
  JOURNAL   PLoS Comput Biol 11 (1), e1004023 (2015)
   PUBMED   25569776
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..127
                     /product="DUF427 domain-containing protein"
                     /calculated_mol_wt=13922
     Region          1..123
                     /region_name="COG2343"
                     /note="Uncharacterized conserved protein, DUF427 family
                     [Function unknown]"
                     /db_xref="CDD:441912"
ORIGIN      
        1 mtertikvpg pdhpitiepa nahvvvtvag qqiassdnal vlreaayppa yyiprtdvem
       61 allertehat ycpykgecay ysiplggert vnsvwtyeap yaavkeiaqh lafypdrvds
      121 ievqaka
//
LOCUS       WP_176058480             433 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176058480
VERSION     WP_176058480.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..433
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46059
     Region          40..422
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mlsiigtpaf rrasarswav lvafgllagr aahaqntglt ldealqiats rsssiqaaqa
       61 svrgssdvvv kagqlpnptl nlgvqelpvs gpnaytlgqd nftmlgvgvq qewvsparrr
      121 lqttlasrav erdqstylek vaevrrqtam awlgaiyakq avalnlalvd hlsqelgarq
      181 asyrgakgta advaqasltl gnardelina rqdektalia lsrwtaagnv ldvsgsppap
      241 esqvsslsde qlaqvqpali aaraaialad adtdvarsnr npnwtwglty fksggrfpdy
      301 vsvgvsiplp ihrgnvedrd vgqksemgtq arltyedter qvvadiqslt aklasgrerl
      361 anakqavlpa aeqkvqlana ayrsgagtla daldarhtql eadlqvlnle rdvslvwaql
      421 eyqvlppdlt sgq
//
LOCUS       WP_176058551             538 aa            linear   BCT 11-JAN-2025
DEFINITION  Fic family protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176058551
VERSION     WP_176058551.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..538
                     /product="Fic family protein"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0042803 - protein homodimerization
                     activity [Evidence IEA]"
                     /calculated_mol_wt=58880
     Region          281..>520
                     /region_name="COG3177"
                     /note="Fic family protein [Transcription]"
                     /db_xref="CDD:442410"
ORIGIN      
        1 mpttneklaa sllvlkqiqd rgvsvfqasa lpeltrvhre rlvranflka vipgwymann
       61 paddagdstl wyasmeafvs ayanarfgse wevnpefsll rhsgytsigt qivihaanan
      121 nqllqlphgc svflyqvkrr astarripsa sglllipvse alvrvgasff ekqplaaqia
      181 mrqvdltdli sallagghsv iggrmagalr avgrdddasq lvatlkaady vvsesnpfeq
      241 slvaisgrrn espyvqriqa mwaamrnavv drfadipqqa prdvdalidd isaryvaday
      301 hslsiegyrv nalliekvrn gnwsplthpe dketqeamaa kgyadthkri relirqvvta
      361 sdnpaealrr dffqwyvtlf spsvaagilk padlagyrss qvfirnalhv plgpeavrdc
      421 mpalfdllva eehpgvravl ghfifvfihp ymdgngrlsr flmncmlttg gypwtivtvq
      481 srrlylaale qastygnivp fadligglva sqaaqpleri tqrpesgewt appgatgl
//
LOCUS       WP_176058552             410 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: tyrosine-type recombinase/integrase
            [Paraburkholderia].
ACCESSION   WP_176058552
VERSION     WP_176058552.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..410
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=46651
     Region          55..386
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 maadeflsar mievadfpkt isimsqeasl dltvagsrgp fycivdsqga ivitlskwlk
       61 slvdaagisn tlssaiqygr tgtylcrwie nselfphltv deiilrlsrp nltewlnhmr
      121 neeglesntv hsrevairtf mewlttidag qlrhpenspy grdgmlpyit rvpkalspky
      181 ipaeyvvqil snmynecerc mfhtqfdtgl risevvklkr sdipdlvlfn saheylpfvv
      241 rrskarggnn lekttlisra vlnrikryha smeyklapdw dindpnkptf ltcnqlkwgl
      301 rnaskqfkea vrrsgvhhdv sthwfrhgta fsvlksdigk tyeekmlliq qmlghaslkt
      361 teiytqvpaa lltkltlkgk ainrlheaef irektflgsl qhtekrghnv
//
LOCUS       WP_176058610             419 aa            linear   BCT 11-JAN-2025
DEFINITION  M48 family metallopeptidase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176058610
VERSION     WP_176058610.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Bode,W., Grams,F., Reinemer,P., Gomis-Ruth,F.X., Baumann,U.,
            McKay,D.B. and Stocker,W.
  TITLE     The metzincin-superfamily of zinc-peptidases
  JOURNAL   Adv Exp Med Biol 389, 1-11 (1996)
   PUBMED   8860988
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Stocker,W. and Bode,W.
  TITLE     Structural features of a superfamily of zinc-endopeptidases: the
            metzincins
  JOURNAL   Curr Opin Struct Biol 5 (3), 383-390 (1995)
   PUBMED   7583637
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..419
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46613
     Region          9..415
                     /region_name="M48A_Zmpste24p_like"
                     /note="Peptidase M48 subfamily A, a type 1 CaaX
                     endopeptidase; cd07343"
                     /db_xref="CDD:320702"
     Site            order(279..280,283,361,365,405)
                     /site_type="active"
                     /db_xref="CDD:320702"
     Site            order(279,283,361,405)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320702"
ORIGIN      
        1 mptlyftvlf vvavvamvgt klwlasrqir fvaghreqvp sqfagtialt ahqraadytv
       61 ertrltmiei vvsaavlvgl tllggvqald laisdwlgrs ytgqialvaa viaitsvidl
      121 pfdyyrqfvv eqrfgfnrms kgiffvdrlk gvllgaafgl pllfvvlwlm nqagslwwlw
      181 twvvwvafqm lvlvlypsfi aplfnkfepl kdealksrie almqrcgfaa kglfvmdgsr
      241 rsahgnayft gfgaakrivf fdtllarlsg neieavlahe lghfkrrhvi krmlvtfvis
      301 lamlallgwl sqcvwfyegl gvrpsliggn sglalvlffl alpvflffvt plgslssrkh
      361 efeadafaat qtdaqdlvna lvklyednas tltpdplyta fyyshppasq ridrllrha
//
LOCUS       WP_176058620             265 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176058620
VERSION     WP_176058620.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 265)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..265
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28210
     Region          30..265
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mqrrlvlkla allgaaslfa asaaraedsi kvgvtggpha qimevvktva aknglnikii
       61 efadyvqpna alaagdldan syqhdpylqa qvkdrgykli riadtvtypm giyskkvktl
      121 aelqpgakia vpndptnggr allllqkqgl vklradaglk atpldivdnp rklkivelda
      181 aqiprslndv daaaintnfa meaglnpkkd aiaaedpkgp yvniiairae dkdkpwvakl
      241 vaayhspevk qfvatkfggs vitaw
//
LOCUS       WP_176058651             414 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176058651
VERSION     WP_176058651.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..414
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=45599
     Region          28..347
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mtthtserts vdvaiigagp agavaaallr kagrsvlvle rqhfprfsig esllpqsmay
       61 leeagmlqav veagfqykng ahfihrdkss afdfrdkhsp gwgttyqver avfddilirc
      121 aaqqgadvrf ghavravhtg arplvdvide adrayqiear fvldasgfgr vlprllnlea
      181 ptrmptraai fthvqdgipa gvtdrnkicv athperrdvw fwmiplaggr ssvgcvaeas
      241 flevpeaerd aklreliqqe ptfnrligna pflmpvrhig gyaanverlh gpgyallgna
      301 gefldpvfss gvtialrsah lavetlnrql dgeeidwsaa ydvplrkgid tfrafverwy
      361 tgalqdiify peqapsirrm iaavlagyaw desnpyvadp vrrlnalhei ctmr
//
LOCUS       WP_176058744             520 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Paraburkholderia
            sp. BCC1876].
ACCESSION   WP_176058744
VERSION     WP_176058744.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..520
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=55349
     Region          24..518
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mslessprst idipallaal pariaeipal aaardpqhva liedarrlts aqllaaveaa
       61 aallresgvr ggdrvmivae nsiaqivllf atakldawal vsnarlsaae ldsirahaqp
      121 rvvayavess kdaeqhavrh qaiaapaftp digawsytve anvqaepvea anhrqcaali
      181 yttgttgapk gvmlshrnlm fiasvssrlr nvgpddvvya vlpishvygf asvclgslha
      241 gatlrlaprf apeavrrala dervsifqgv pamhaklleh lqthghawsa prlrfaysgg
      301 spldaalksq veavyglplh ngygmtessp tvshtmldrp rsdcsvgevi pgvevrfvgl
      361 dgvdaapgei gelwvrgpnv mlgyyrnpeq trvavtedgw lktgdlarqd adgalhivgr
      421 skeliirsgf nvypaeveha lnahpqvvqs avigravegn eevvafveli agakvtaael
      481 iawcgerlap ykrpaevkvl aalpaastgk ilkhrlreyl
//
LOCUS       WP_176058756             514 aa            linear   BCT 11-JAN-2025
DEFINITION  FGGY-family carbohydrate kinase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176058756
VERSION     WP_176058756.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..514
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=55473
     Region          3..448
                     /region_name="ASKHA_NBD_FGGY_RrXK-like"
                     /note="nucleotide-binding domain (NBD) of Rhodospirillum
                     rubrum xylulose kinase (RrXK) and similar proteins;
                     cd07804"
                     /db_xref="CDD:466806"
ORIGIN      
        1 mdyvigvdig tqstkallvd rhgaivaqha ssyqpdtpkp lwaeqwpavw fkavveciaa
       61 cvakakeagg aaksikavcv sslyggsgip vdsemrplyp cliwmdrrat aqvewvrsnv
      121 dldrlrtitg ngvdsyygyt kmlwlrdnep evwahtryfl ppnayviyml tgevavdhss
      181 agniggiydm akrdwsdeal dmlgipatmm perlvessdv vgglltqwte tlgldagtai
      241 vaggvdaama tfaagvthag qhvamigtsm cwgyinqsvd arhglismph vfngqhdiyv
      301 fggaitagas vtwyreqfch aeieaaratp hgdphrllee taanvpagsd gvmflpylmg
      361 erspvwdaka sgafvglslf htrghlyrav legvsfalkh nieagrqgal slddklivvg
      421 gaahsdlwmq iiadvtgypv ytieqdveaa mgaallagvg vglvsreeaq ggwvtlvera
      481 qpdavrmaly eqrfgiytdl ypalkpvmhr lqts
//
LOCUS       WP_176058780             312 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176058780
VERSION     WP_176058780.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..312
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35956
     Region          85..242
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mqfdaellll amapvflaci gweawhlrrt rpgaqlyswr dtfcnaalal mqqaadklaw
       61 laiipvyaff ydhyrvttwq anwvsfvvlf iaqdllyyvf hrcshrvrwl waahvvhhss
      121 ermnfstafr qslmypiagm wlfwiplavl gfppkqivai vlinlgfqff vhtqaigklg
      181 wleyvfntps ihrvhharnd ryidrnyagv lviwdrlfgs yveedshdap vygiveplht
      241 ynplkatfhe wtsmaadfas vrgwrnkwra lfappawaaq yhahraassa asgsmaevee
      301 nhtaafetpr gp
//
LOCUS       WP_176058803             207 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176058803
VERSION     WP_176058803.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..207
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22662
     Region          14..162
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpktlsaddi qqfreamrrv aenafatrga qgvtmrelak elgcsamtpy ryfrdkddil
       61 amvraaafnr falhleaaag nasgdnrlav sdayvafald ephayrlmfd vnqpeggypd
      121 laaaalraqe mltthfeqlv dagllegdpq ligyaywasl hgftmlalan qlplpeaqqp
      181 aghtaptrea vlaqlrrmlw rgaqpqp
//
LOCUS       WP_176058758             335 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176058758
VERSION     WP_176058758.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..335
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34241
     Region          37..335
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mntpnpsssp ktstvssdtp gapvrftwaa lkrstvfypf igllvvcivm vfasdsflsa
       61 anienvlrqv sinaiiavgm tcviltggid lsvgsvmala gtlaaglmva gmnavaalai
      121 giavglgfga angffvafag mppiivtlat mgiarglali ytggypidgl pdwvaffgsg
      181 kilgvqapvv imvviyaiaw vllermpfgr yvyaiggneq atrlsgvrva rvklivysia
      241 gltsafaaiv ltarlmsgqp nagvgfelda iaavvmggts isggrgsiig tligalllgv
      301 lnnglnmvgv npyvqnvikg giillaiyis rdrrk
//
LOCUS       WP_176058825             141 aa            linear   BCT 11-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176058825
VERSION     WP_176058825.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10629346
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..141
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=15290
     Region          31..132
                     /region_name="DUF4440"
                     /note="Domain of unknown function (DUF4440); pfam14534"
                     /db_xref="CDD:434023"
ORIGIN      
        1 mkplirlaav atltlstvfp ahaadhdedr lksleqtwit assntdrvtl dkllddsfid
       61 ttptgtrrsk sdvllapppp psstqtlvnl evrvngdtai vtgtnhfnpg anaqpsdysf
      121 tdvfvrretg wravsaqmtr k
//
LOCUS       WP_176058850             312 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: carbohydrate kinase family protein
            [Paraburkholderia].
ACCESSION   WP_176058850
VERSION     WP_176058850.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Bork,P., Sander,C. and Valencia,A.
  TITLE     Convergent evolution of similar enzymatic function on different
            protein folds: the hexokinase, ribokinase, and galactokinase
            families of sugar kinases
  JOURNAL   Protein Sci 2 (1), 31-40 (1993)
   PUBMED   8382990
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..312
                     /product="carbohydrate kinase family protein"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=33453
     Region          4..290
                     /region_name="ribokinase_group_A"
                     /note="Ribokinase-like subgroup A. Found in bacteria and
                     archaea, this subgroup is part of the ribokinase/pfkB
                     superfamily. Its oligomerization state is unknown at this
                     time; cd01942"
                     /db_xref="CDD:238917"
     Site            order(52,250,253)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238917"
     Site            order(192,220,248,251..252,255,277,280)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238917"
ORIGIN      
        1 matlicgsla ydnimtfegr frehilpeqv hilnvsflvp tmrrefggca gnmayalhll
       61 ggdarimgtl gavdaqlymd rfkalglste nvlvvpdths aqamittdle nnqiaafhpg
      121 ammqshlnra deakgitlai vgpdgfdgmv qhsehlaaag vpfvfdpgqg lplfdgatlr
      181 rmielatyva vndyeaklvs nktgwsieei agkvealivt lgeqgsqihh aggvedippv
      241 kaqqvldptg cgdafrggll ygienklgwa ttgrlaslmg alkiecqgpq nyaptraein
      301 erfkqafgyd lp
//
LOCUS       WP_176058876             165 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176058876
VERSION     WP_176058876.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..165
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18489
     Region          5..153
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 madlemdaid rrilailqen grlsnqeiae cvnlspspcl rrirrleecg virgyvalld
       61 aqrlgldlla yvnvrlekrg gpaprprgdv thadqfraav qtwpevvach amtgdmdyll
      121 rvqvedmahf srfmqdqllh hpsvidvkts fsldtikett alpil
//
LOCUS       WP_176058901             334 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176058901
VERSION     WP_176058901.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..334
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35588
     Region          4..318
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtnlltirnl avnfnglpav drisldvapg evvgvvgesg sgksvtmmal mglidapgkv
       61 tadevtfngr dllkasaker rkiigkdiam vfqdaltsln psytvgyqik evlklheglr
      121 gsaldkrale lldqvgipdp rgrigsfphq msggmnqrvm iamaiacnpk lliadeptta
      181 ldvtiqaqim elliklqker gmalvlishd lavvsevaqr vavmyagevi etnqvpdifa
      241 aphhpyteal laaipehnvg avrlaalpgm vpgrddrpkg clfaprckyv addctkarpa
      301 laplqghaev arvrcikpln lsgdanvhth ggar
//
LOCUS       WP_176058964             237 aa            linear   BCT 11-JAN-2025
DEFINITION  chemotaxis protein CheW [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176058964
VERSION     WP_176058964.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..237
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=26145
     Region          72..230
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 madtqtigfd dcwnrigvrg dsscerlddy vrclncpvfe aaaarllerp iprvdlalhe
       61 arvpaqthqk hegqnasesf lvfrigdewl alptpifkri vqtrpihtlp hrqhravlgv
      121 vnvqgellvc lslahllgfd aggaaqdkrd krndrddrar helprllvvt rgeehavlpv
      181 dqvdgvhrfa ldsfcpppat lsqaaaahtr avapwrgmsv glldadalfd tlnrslg
//
LOCUS       WP_176059055            1060 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: efflux RND transporter permease subunit
            [Paraburkholderia].
ACCESSION   WP_176059055
VERSION     WP_176059055.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 1060)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1060)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1060
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..1060
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115245
     Region          1..1042
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mwivrlalrr pytfvvlall llivgpltil rtptdifpni dipvlsviws ynglpademe
       61 krivlnyerg lsvavndieh testslngia vikiffqpha nidealaevt alsqtqlrsl
      121 ppgitppnil rynastvpil rlalssaslt eqelydfgnn flktqlatvp gasaplpygg
      181 kqrqimvdid srklqernls pmdvvnavta qnlilpsgta kigsteysve mngspdslag
      241 lnnipiksta ngtvyirdva hvrdgfqpqt nivrvngqra alltinksgn tstleivdri
      301 ktmmptlrnl vpaslnidpv adqslfvras vqgvlreali aacltglmil lflgnwratl
      361 iiavsiplsm itsiialsml getinimtlg glalavgilv ddatvaieni shqleqgktl
      421 eqaildgahq iaiptlvstl sicivfvpmf lltgvahylf iplaeavvfa mlasyffsrt
      481 lvptlakyll rhhhkavdah hapaqtrnpf mrvhyafegg ferlreryrv flearvarpg
      541 lfvtlflvcc gvsmflmpfl grdffpavda gtialhlrak tgmrveetav vtdrvdtrir
      601 qlipkeelhs iidniglpvs ginlsysntg tigtsdadvl itlnpdhhps adyvrtlrrt
      661 ltdefpgvqf aflpadivsq tlnfgmpspi diqivgrdva gnrvfaanll nrlrkvpgla
      721 dariqqpadl prifidvdrt raqqagftqr diasnllitl sgsqqttptf wlnprngvsy
      781 nviteapqyt idslqslani plnangrsni lgsfatmtre agnatlnhyn aqttidiygt
      841 adgrdlggvs ddirkiidda kaelpktssi evrgqvqtmn dsfsglfagl vfaillvyll
      901 ivvnfqswld pfiiitalpg alagivwmlf lthttlsipa ltgaimcigi atansilvis
      961 farerllehg datraaieag ftrfrpvlmt alamvigmvp maiglgegge qnaplgravi
     1021 ggltigtlat lifvpvvfsm iyrrlaarrl raaehvvqkp
//
LOCUS       WP_176059062             183 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059062
VERSION     WP_176059062.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..183
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=18321
     Region          2..155
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mtisisltvn gaaisasidp gtllvqflre qlrltgthvg cdtaqcgact vhlngraiks
       61 cnilavqadg atvttiegla qngalhpmqa afkhchglqc gfctpgmvms avslverqpd
      121 ltgdevraql dgnlcrctgy hnivkavleg avgmksagsa naaassagns atansaatap
      181 ata
//
LOCUS       WP_176059066             345 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059066
VERSION     WP_176059066.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..345
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35596
     Region          47..345
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 malklhtesl hteprhgesa aqisaaprvk aastvqkwrr lamqrevivl lamvlfnlif
       61 tphflslqtf nvnmtqvvti vivgigmtlv vatggidlsv gasmaisgal apmlflniag
      121 pagialafvl pvlaaalcgv fngwlvtrla vqpivatlvl fiagrgiaqv vtdgslqafn
      181 tpafqwialg kvagvpfqvl lmlalvavfv wvvrktlfgq yllitggnek aaylcgvpta
      241 tvkliaytlc aalaglagli sisvnsssda nvvglgveld aiaavavggt altggkayig
      301 gtligaliiq llrytllahg ipdaaalvvk agiivaavyv qrrsr
//
LOCUS       WP_176059068             368 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059068
VERSION     WP_176059068.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..368
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38788
     Region          1..364
                     /region_name="LhgO"
                     /note="L-2-hydroxyglutarate oxidase LhgO [Carbohydrate
                     transport and metabolism]; COG0579"
                     /db_xref="CDD:440344"
ORIGIN      
        1 mdqiecvvig agvvglavar alaargrevi vleaaeaigv gtssrnsevi hagiyyprgs
       61 qkaalcvrgr emlydfcaeh nvphsrcgkl lvatsrnqip qlesimakgr engvldllrm
      121 dgdqaqalep alecveavfs pqtgivdshq lmlaiqgdae rdgavcafha pveaieasng
      181 rfiikvggsa pttisaacvi nsaglqanal arqirgldar hvpplylarg nyfsisgrap
      241 fsrliypmpn eaglgvhlti dlggqarfgp dvewvdainy dvdphraesf yaairaywpa
      301 lpddalqpay agirpklsgp gepaadfliq gpaahgvrgl vnlfgiespg ltaslaiaqr
      361 vcelsgra
//
LOCUS       WP_176059073             405 aa            linear   BCT 11-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Paraburkholderia
            sp. BCC1876].
ACCESSION   WP_176059073
VERSION     WP_176059073.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..405
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42983
     Region          16..298
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mpslaagqsa ekhrvarkst fvsialntgl mtlqivvgiv ahsqalvadg fhsladlisd
       61 fvvlianrhs gvkpdadhny ghsryetvas lflgalliav gvgmlwragt rladlqsipa
      121 vhmsalavav fvliskeglf rymlreaqrv rsamlianaw harsdaassl vvaigiigsl
      181 agvrlldpia aaivgfmvar mgwtfgwdal qdlsdraldd aatadmrtll lstpgvrdvh
      241 elrtrkmgdf alvdahilvd plisvseghy iaesarmrvl sdsrvldali hvdpendala
      301 rppvdlpnre qvtseidaal agaglkaaav dihylstgld vdlvlpsrtl sgsapdlasv
      361 dlaalksrlg arklnvlqew dvrldengpa raagadpsad lvknh
//
LOCUS       WP_176059128             292 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059128
VERSION     WP_176059128.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 292)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..292
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31361
     Region          18..258
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 miaplsqavr gqpapsiaep vieviditkr ygrnivhqhl nldvkrgeim sivggsgsgk
       61 ttlvrqilgl ekpssgtikl fgenlatisp etallmrsrs gmlfqrgalf sslsvfdnia
      121 qpvrelgkvp edllrdivml klemvglpck haskmpsals ggmikrvgia raialepell
      181 fldeptagld pqasdefvel isalhralgl tvvmvthdld tmialstrva vladrtvlva
      241 apveeaagvd hpfireyflg lrgrralqal pperraklpr aalepassel pl
//
LOCUS       WP_176059090             256 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176059090
VERSION     WP_176059090.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..256
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27384
     Region          3..247
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mnyivdsvds alkllshvae hpglgvtela nqlginksra yrmlctlelh rfvvqdtras
       61 tyslgpqafv igvaaaqqnt lvrsaqkhml vlnqainenv vlrvreglet vcvarcetth
      121 emrtigavgn rrslnsgasg rillafapda vkteylarlk klpqppdlmk lvdeldaiar
      181 kgyavsvgev tagavaisvp vrdisgeava aisvsgpemr isrieipdyl erlqacsrti
      241 saelgytapq aaaqpa
//
LOCUS       WP_176059130             214 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059130
VERSION     WP_176059130.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789896
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..214
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23574
     Region          9..214
                     /region_name="COG2945"
                     /note="Alpha/beta superfamily hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:442188"
ORIGIN      
        1 mnvhtkkyli dgpvgkieva ldlpdemren gaaprgialv ahphplfggt mdnkvaqtla
       61 rtlvqlkyvt yrsnfrgvge tqgehdagig erddlravld hmraeagqad lplvlagfsf
      121 gtfvlshvaa klreeeqaie rmvfvgtaas rwevapvpen tlvihgetdd tvpiqsvydw
      181 arpqelpvvv ipgaehflhr klhvlkriiv dawr
//
LOCUS       WP_176059139             256 aa            linear   BCT 11-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator
            [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059139
VERSION     WP_176059139.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..256
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27557
     Region          1..236
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mwqedrhqri rallstlqrv sterimadlg vsretvrrdl ldlealgelr rvhggaikpa
       61 deapiaerah mrvksktaia kaatsliasg qtlfidagtt taalaeelak lanltivtns
      121 idvalkmrgg veqtdaanev illggsisdr amattgattv ldiqryradl allspvgvdh
      181 rhgatnydha etevaramva nadrvvilad yskigqrsri sycpveridv lvtnkkaaea
      241 adfaalkkkl eeivla
//
LOCUS       WP_176059159             232 aa            linear   BCT 11-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176059159
VERSION     WP_176059159.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..232
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24693
     Region          25..232
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 msyvfapapq vavpvvgsse qfavrriycv grnyeahare mghdpdrepp fffskpadav
       61 lyvapgttge fpypslsknv hfemelvaai gqggknipad saldhvygya lgldmtrrdl
      121 qaeakklgrp wdtakgfdqs aplgpihpvt tvghvgkgai wlsvngeekq ssdvsqliws
      181 vaetiaylst lfalqtgdli ftgtpegvga vvqgdlmkgg vdglgefsvr vv
//
LOCUS       WP_176059166             395 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderiaceae].
ACCESSION   WP_176059166
VERSION     WP_176059166.1
KEYWORDS    RefSeq.
SOURCE      Burkholderiaceae
  ORGANISM  Burkholderiaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Burkholderiaceae"
                     /db_xref="taxon:119060"
     Protein         1..395
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41406
     Region          22..389
                     /region_name="MFS_YajR_like"
                     /note="Escherichia coli inner membrane transport protein
                     YajR and similar multidrug-efflux transporters of the
                     Major Facilitator Superfamily; cd17472"
                     /db_xref="CDD:341025"
     Site            order(29..30,33..34,37,71,121..122,124..126,129,151,
                     154..155,158,221,224..225,228..230,233,260,264,308..309,
                     313,317,340,343..344,347..348,351)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341025"
ORIGIN      
        1 msnpsatssr msapelratv slaaifalrm lglfmimpvf siyaktipgg dnvllvgial
       61 gaygvtqsml yifygwvsdk igrkpviaig llifalgsfv aagahdmtwi ivgrviqgmg
      121 avssaviafi adltseehrt kamamvgasi gvsfavaiig apivfqwvgm sglftlvgif
      181 silaiglvlw vvpdapkpvh vrapfaevlh nvellrlnfg vlvlhatqta lflvvprile
      241 agglpvashw kvylpvmgls fvmmvpaiia aekrgkmkiv llsaiglili gqlllgvaph
      301 tilsvagilf vyflgfnile asqpslvskl apgtrkgaaa gvynttqsig lalggvvggw
      361 llkvdgasav fftcsglvfc wliiaanmkq pprka
//
LOCUS       WP_176059183             423 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059183
VERSION     WP_176059183.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..423
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=44678
     Region          208..415
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(215,255,293,396,399)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(215,396,399)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(215,255,293)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 mtfrtlaaac gaallaqfav sptvfaadap ahwvaawata lqpipqredl pplyrapeva
       61 grtvrqivyp tlsgraarih lsneygktpl viddlriars aggaaavand garvtfggks
      121 avsipaggel dsdpvtidia dgapyaisaf mgpeqrivaw hrvssqvnyv sepgnhaada
      181 saeafrgrft qyvwvtgvsv eatpssgava aigdsitdgm rsslnqnhrw pdalarrlag
      241 sndrttaivn lgisgnrlls dspcygdala rrferdvlgr pgvktailli gindinfasm
      301 parsgldcdf phtsvtapdl iagyqrvita arhagvkvfg atltpaslpa qresirlavn
      361 qwirtshafd gvvdfdaalr dpgqpdrlrr nfdsgdhihp sdagyaamad avpldtvvns
      421 mrk
//
LOCUS       WP_176059283             455 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059283
VERSION     WP_176059283.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..455
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=49129
     Region          1..434
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfaslglid pllrnlqdln yqtptpvqak aipavlsgkd vmaaaqtgtg ktagfalpll
       61 qrlvqhgpav ssnrarvlvl vptrelaeql lqsfidygkg ldlrflaayg gvsinpqmmk
      121 lrkgvdvlva tpgrlldlhr qnavqfdqvq tlvldeadrm ldlgfereln avfaalpaqr
      181 qtllfsatft ddiramaagi lrgpvdisvs ppnatasrik qwvvlvdkkn kpdlfmhlva
      241 ennwthalvf vktrngvdyl aamldeagya vdtihgdkpq parlralerf ktgevsmlva
      301 tdvaargldi ddlplvinvd lpivaqdyvh rigrtgraga sgvavslvca deapqlaaie
      361 alirqtlrre eepgfeaehr vpqtsatgei ikkpkkpkkp kmpqaapram papskkprpq
      421 ggenkrkpaa prskpvagsh kpaskpasgr gkrqp
//
LOCUS       WP_176059232             668 aa            linear   BCT 11-JAN-2025
DEFINITION  bifunctional DedA family/phosphatase PAP2 family protein
            [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059232
VERSION     WP_176059232.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
REFERENCE   3  (residues 1 to 668)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   4  (residues 1 to 668)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   5  (residues 1 to 668)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..668
                     /product="bifunctional DedA family/phosphatase PAP2 family
                     protein"
                     /EC_number="3.1.3.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=71917
     Region          17..196
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
     Region          264..440
                     /region_name="PAP2_like_2"
                     /note="PAP2_like_2 proteins. PAP2 is a super-family of
                     phosphatases and haloperoxidases. This subgroup, which is
                     specific to bacteria, lacks functional characterization
                     and may act as a membrane-associated lipid phosphatase;
                     cd03392"
                     /db_xref="CDD:239486"
     Site            order(344,351,364..366,408,414,418)
                     /site_type="active"
                     /db_xref="CDD:239486"
     Region          497..>615
                     /region_name="LssY_C"
                     /note="LssY C-terminus; pfam14067"
                     /db_xref="CDD:433691"
ORIGIN      
        1 mehaylhflh slaghpqwml avvflaafle avavigtfip gstamflaga ltgtgslslv
       61 wvfvwaiaga vagdgmsfwl ggrykdrivq lwpfckhpev leaghrffrk hgaksvvlar
      121 figplraivp vvagmlgmpp lrfyamnvls allwapahil pgvvfgasvl lagavsfrlv
      181 vilallvaiv wlsfrvagfl lshanawssa ggryigswac rhpgpigrfa rkmldpetpd
      241 assilltsli vlvsgalffg vlddvisgdp ltqvdlsvyh flqsvrtpwg dtvlaslaml
      301 gsgltlaalv vtvvvwmlle rrwrtigywl aavvfsqlli yalqfamrra ppnelmsnay
      361 afpsnhvaat vivygflafl larrvgkleg vfvatvstvv vivvalagly fgrywvsdai
      421 ggaalayvwv aivaltamwr hpeappartl mpvvvlavvl vsvgvqlgva mpaprpdttl
      481 rrppvlvtqs qwtlsawkrl pcyrsdmggd hkepltlqwl snadsirgql raqgwiegtd
      541 lsahsllsla spnvaavslp vlpklnngvp sslvfmragd trderdvlrf wpsgyaveng
      601 isatplwvgs faherlsrds wpinilrvdr sestldshar agaalgasvv akvicdgvqv
      661 allaspve
//
LOCUS       WP_176059306             199 aa            linear   BCT 11-JAN-2025
DEFINITION  YceI family protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059306
VERSION     WP_176059306.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..199
                     /product="YceI family protein"
                     /calculated_mol_wt=20849
     Region          23..199
                     /region_name="YceI"
                     /note="Polyisoprenoid-binding periplasmic protein YceI
                     [General function prediction only]; COG2353"
                     /db_xref="CDD:441920"
ORIGIN      
        1 mksnlyhsav raairpairp iltgiaalsl fgaglahadv daskstviat tkqmnvpvdg
       61 kfrkfsaqln fdparptags anvsidtgsy dlgaddynkq aqgkewfdsa typaatfvss
      121 aiapaggnqy kitgkltikg ksqtvvvpvt vtaqgatqtf dgslpikrsq fdvgtgewkd
      181 tsvvadevvi kfhlvaskk
//
LOCUS       WP_176059332             237 aa            linear   BCT 11-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176059332
VERSION     WP_176059332.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 237)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 237)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 237)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..237
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25565
     Region          6..216
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mksgiwkeif qltlpvgmgy lptgfafgvl aiqsglspmi tvamsvfifa galqfsavpm
       61 laaatglgtv vlttllinlr hvlyaiplld dlplnrasrs yvvavltden ysllttipea
      121 errrvalrvc linhgywilg tvlgvafgaq aarwipnlgf alpalftila ieqylarrrw
      181 apamigiagy liarsvlpgy alisalafgl ivllaiavgd rhvssrnrld wssdenr
//
LOCUS       WP_176059365             268 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059365
VERSION     WP_176059365.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 268)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..268
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29035
     Region          3..268
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mqrrtiiqnl laiaaislta tfahaadkel rigtmsgpda qiwsvvtkva areglnvkvi
       61 efndyvqpna aldsgdldan gfqhqpflds qirqrgykiv nvgltyvspm gfyskklksl
      121 kdlpegakvg iqndpsngnr allllqkygv iklkpgvgtn gvnatpldva gnpkkirlve
      181 ldaaqlpral ddldaasint dyavkaglqp tkdaiaiedl kgpyanliav rvqdrnqpwv
      241 kklvaayesd evrkyidtqf kgaiipaf
//
LOCUS       WP_176059386             740 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059386
VERSION     WP_176059386.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..740
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=78535
     Region          1..739
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mnligqpvdr idgllkvtge aryaaefpea rlahavlvts tiargtiasi dasraqalpg
       61 vllvmtyqna prlpnggkpa lappagrrls llqdnevhys nepvavvvad tlehatdaah
      121 qlrityqasa atvdftqakp nahapdrpqg rqtdtqrgsf ddgmrsgavh vdatyttpie
      181 hhnpmephat larwdgpqlt lydatqgvss aaqaiaktfg mspadvrvis pfvgggfgck
      241 gsswshvslc amaarqtgrp vrlalerpqm fgpvgarpht eqrfilaarh dgtltamrhd
      301 stsntsvied wtetccmvtr mlyavpnqvt thrivplnlg tptfmrapge ttgsfalesa
      361 mdelavalkm dplalrlkny adadpqenkp wsgkslrecy qigaqkfgws rrnaaprsmr
      421 dgntliglgm atatypanrs eaaaiarilp dgtamvasgt qdlgtgtytv mtqvaadslg
      481 faptqihfal gdsslprapv sggsqsaasv spavrdaasq arsqlitlal adeaspvygi
      541 aldditvidg wvtsrsqpgk rdpaaaiiar sggkpieata tvkpgdekqk ysfhsfgavf
      601 vevhvdaelg tirvprvvaa ydvgrvlnlk tarsqlmggi vwgigaalqe etlldtrygr
      661 ftnanlaeyh vpvnadigsl ditfidrpdp yinslgvrgi geigitgvpa aianavyhat
      721 gvrvrdlpvt ldkvmgpmpv
//
LOCUS       WP_176059438             172 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059438
VERSION     WP_176059438.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10483007
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..172
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18489
     Region          17..164
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; pfam01613"
                     /db_xref="CDD:460266"
ORIGIN      
        1 mtelnahplr admllamrrl arsvaviscs dgerrysmsa tavdslstep psllicinrn
       61 ssifppldqg aafcvnvlsa qhqhiaidcs grlkgeerfs tgdwqrsang vpflldaqas
      121 lictqdgrfd ygthaifigr veqvlisgev dplvyvdgvy ttattparca ta
//
LOCUS       WP_176059424             437 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176059424
VERSION     WP_176059424.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..437
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=45782
     Region          1..413
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnlalseeqi mirdaaaevl tecsasaavr haieqgagrd ealwrtvage lgwcaltvpe
       61 daggaglgat elvlmmeqlg rrlacvpyfg tvclaatala vvsdgvddgv gdaeaarehl
      121 ariasgelsa tlalplsagf dfdtralpvs sgfgfgfgfn fdartvplha eetgggyrls
      181 gtldqvidga saglllvpar vaneaqtlal felrgadiag ltrtplvtld atrplarlel
      241 hdvdvprpav largreaerv lshtawfaal alaaeqvgga qqcldltlay tadrvqfgra
      301 iasfqavkhr caqmlveiea srsvvlgaaq awdqasvaas pgadvfadia aakatandaf
      361 rfcaqeaiql hggvgftwey dpqlyfkraq assalfgtss qmlswiaqrl vdrrdpqsea
      421 padahtdhaq nvlagvl
//
LOCUS       WP_176059442             267 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176059442
VERSION     WP_176059442.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..267
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28331
     Region          5..259
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mtalirlaae dgiatltfdr pdalnalnea maielnakla rlahhddira ivltgaghaf
       61 maggdlhsmr taldekpavr draigtlvrl aqsaveaiaa srkpviasvn gavagfglsl
      121 vaacdlaiaa qratftsayg rigtspdgga tytlpralgv rqaaqwlyld erhsadealr
      181 aglvnwvvpd dqlaeqtrsl lermgalapd afaqtkelll qapqrsfadh lyaeqssflh
      241 caasddfreg idaffdrrpp vfgsgar
//
LOCUS       WP_176059452             264 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176059452
VERSION     WP_176059452.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..264
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27177
     Region          27..243
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; pfam01925"
                     /db_xref="CDD:460386"
ORIGIN      
        1 mfhfnfadgv lgpslqaldf ytllgivval llggmvkgvv sigvplvamp ilshflpiks
       61 avlllsmpii lgnipqaleg gnllptvrri aaplvgtvig nivgvtvlis laphraqaaa
      121 gaflmiaall llatprltls prwakpagfv lgfgaalmes iasvpgplla myliatgatg
      181 rvftkqiaii lvvsiitlvl alsggahasw tdllisacas vpvivgmllv rplrdrlppt
      241 afralvlvfv vaaaaqmiwk sgvl
//
LOCUS       WP_176059461             181 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059461
VERSION     WP_176059461.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..181
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=17659
     Region          27..181
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mkitrsgvla aaiaaaaavp avshaadgti tftgqitsqt ctisgngggk nftvtlptvs
       61 tsalatagtt agrtpfnial snctpnsgnv styfepgatv dtttgqlina sgtatnveig
      121 llngdssvit lgaaqasqns kavalasgaa tlkyfaqyva tngastagtv nttvlysivy
      181 q
//
LOCUS       WP_176059462             138 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059462
VERSION     WP_176059462.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..138
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15417
     Region          3..137
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mirmlipvld nggaveaary aaflflergv tevellevle pidqgraaaf hsrsslvree
       61 kramlkalid vrtileeagv pyhwkrifgh rtkaiadyaa ltqpdvmvid ashmsffrrm
      121 vtlaslarrt vtpvtmvh
//
LOCUS       WP_176059468             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176059468
VERSION     WP_176059468.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33155
     Region          7..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdrfasiavf vaavdegslv aagrrfglsa smagkhlsgl eaelkvrllq rstrslsltd
       61 agrayyarck rildefddan reasdaqrva sgmlrvaapv tfgamhmgdv vtrylsdhph
      121 vdidialddr yvdlqndgid vairigrlpd sqlvarrlap crmvicaspa flaregvpht
      181 pgdlaraprl afseavsage wtlldeqdry hviggplrmq annmqmlvag alagigiayg
      241 ptfvfgehik agnlvvllpg frapeltiha vypsaryvps kvrrfidclv dafgdeppwd
      301 sfravp
//
LOCUS       WP_176059538             204 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176059538
VERSION     WP_176059538.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..204
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22549
     Region          11..170
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdvkprkspr qarakatvda iiegtiqvll degyesftta rvaeragvsv gtlyqyypnk
       61 aalavavvdr cceefliafe nalderrctt lddciralvd fafvshhvtp erhrcvlela
      121 prlgvadrte vvrktavkvl estlrrhade iapeidmtva atmiettmea lahravmtdp
      181 aqtqndslak eatrlitlyl ftgk
//
LOCUS       WP_176059542             357 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176059542
VERSION     WP_176059542.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10088910
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..357
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38096
     Region          11..109
                     /region_name="HTH_MerR-like"
                     /note="Helix-Turn-Helix DNA binding domain of MerR-like
                     transcription regulators; cd00592"
                     /db_xref="CDD:133378"
     Site            order(55,58,62..63,72,91,95,101,105,108..109)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133378"
     Region          148..>219
                     /region_name="COG1373"
                     /note="Predicted ATPase, AAA+ superfamily [General
                     function prediction only]"
                     /db_xref="CDD:440984"
ORIGIN      
        1 msssapclna seaasqlgvs ikalrlyeqq glvtpgrtaa gyrvygpkem drageivalr
       61 alglslaqva rvldgdpqsl aialathata lneelqdlvq kldrirrvrs dlargqmpvg
      121 geltqlidrp gisvafalpw pwggerfelr dirplnyiig slgsgktrla lrlaetlpda
      181 vflgldrlqd kgaaaldllk adtalksrvd ravewlideg atesealtil lvgwetdgpa
      241 alvvdmveqd ldgltqeali tflrlrasas mrslflmtrs saildlaavg pyeaiilcpa
      301 nhsapvrvap ypgapgceav atclatpevr ariarrpets ageatiykpq thaprnp
//
LOCUS       WP_176059559             554 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059559
VERSION     WP_176059559.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..554
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60512
     Region          4..538
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 misvrnltlr rgvnvvldna satftpgeki glvgrngagk ssffgllngt lhedsgefsi
       61 paayrmgqva qdmpetdqna tdfvvegdtv llaaqaevaa aeasddgmrm ahaymelhda
      121 gahdaparaq aliqglgfta eqlsqpvnsf sggwrmrlql aralmcpsdl llldeptnhl
      181 dldalvwlea wlkryqgtlv vishdrefld gvtqvtvhvd naklvryggn yskfeemrae
      241 qlvlqqasva kqadkiahlq kfidrfkata skakqaqsrv kalermekia pvladaeftf
      301 efkeplnvpn pllsmldasf gypapadapp dtpptvivrg inrsvlagqr igilgangqg
      361 kstlvktvah slapiageis egkglnigyf aqqeldvlrp fdtpmehmir lakdtppqmr
      421 apgqssteqs lrtflgtfnf sgdmvhqavh tmsggekarl vlcmivwqrp nlllldeptn
      481 hldlatreal amalnefegt vmlvshdral lravcdefwl vtkggvepfd gdlddyqqfl
      541 rdearrlree avag
//
LOCUS       WP_176059580             455 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: MFS transporter [Burkholderiaceae].
ACCESSION   WP_176059580
VERSION     WP_176059580.1
KEYWORDS    RefSeq.
SOURCE      Burkholderiaceae
  ORGANISM  Burkholderiaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderiaceae"
                     /db_xref="taxon:119060"
     Protein         1..455
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46215
     Region          12..439
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(19..20,23..24,27,59,109..110,112..114,117,137,
                     140..141,144,266,269..270,273..275,278,306,310,362..363,
                     367,371,387,390..391,394..395,398)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msaanrrama aimlavalat ldtaiantal paiaadlhaa paasvwiina yqlamvatll
       61 plaalgdivg hrriyiggia lftlaslacs lattlpmlaa arvlqglgas aimsvntali
      121 rylypphrlg rglgtnaliv gvsfavgptv aslilsvaaw pwlfavnvpl gllafafawp
      181 alphtergth qfdpvaalln vitfaalifa lgeaaqrast llvlsaaaia ivfgallirr
      241 eaghpapmlp vdlfkrpvfa lsavtavcsf aaqglafvsl pfyfedvlhr sqvetgflmt
      301 pwpvvvalaa plagslsdry ppgllgaigl avmsagmasl allpvhphvl digirmavcg
      361 agfgffqspn lkalmasapp ersggasgiv atarllgqtt gaalvalsfg iagrhgptla
      421 lsagaffaga aslasglrll apshrsgaha kaaak
//
LOCUS       WP_176059577             183 aa            linear   BCT 11-JAN-2025
DEFINITION  PadR family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176059577
VERSION     WP_176059577.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Shao,X. and Grishin,N.V.
  TITLE     Common fold in helix-hairpin-helix proteins
  JOURNAL   Nucleic Acids Res 28 (14), 2643-2650 (2000)
   PUBMED   10908318
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Gajiwala,K.S. and Burley,S.K.
  TITLE     Winged helix proteins
  JOURNAL   Curr Opin Struct Biol 10 (1), 110-116 (2000)
   PUBMED   10679470
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   5  (residues 1 to 183)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447868
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..183
                     /product="PadR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=20540
     Region          1..86
                     /region_name="PadR"
                     /note="DNA-binding transcriptional regulator, PadR family
                     [Transcription]; COG1695"
                     /db_xref="CDD:441301"
     Region          96..175
                     /region_name="Vir_act_alpha_C"
                     /note="Virulence activator alpha C-term; pfam10400"
                     /db_xref="CDD:463075"
ORIGIN      
        1 msiqhallts llekpssgyd larrfdksig yfwhashqqi yrelgrmaea gwivasdded
       61 ggkrrrrlyq vlapgqdela rwvsepttdg dasrallikl raesvigphg verelrrlia
      121 ehrakldtyl eieqrdfaas dmpiaqklqh avlrggimte qgwlewasev lpiletagrg
      181 apq
//
LOCUS       WP_176059611             576 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059611
VERSION     WP_176059611.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..576
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63839
     Region          15..491
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mttlisalsv qlesghgplf hdlsftvklg drigllghng cgkssllgvl agsrepsags
       61 vqyagqcrlq hveqhlpprl anltareall eaidkqpeqh wrvdsllnel glpeaadtsv
      121 aslsggqhtr lllgravlqe pnlllldeps nhldlpsllw ledflgrwqg gfilvshdpr
      181 lldtlsdksw ilrdqqlysf dlpcsralia laeadaaaql rhageqkeid rltasskrva
      241 iwgrehdnek lvrqarniqr radklkddqt fvsrgspwrl tlqgkslaad nlqafeglqv
      301 caqsdqpvlf eldalwlrpg dkvallgsng agkssllrqc wsdvqagear agwryhpaas
      361 iayydqslrq ladeatlada lykfapvgdr errqalisag faysrhgqkv atlsggerar
      421 llflalsmas yhllwldept nhldldgkre lavalaafag gfllvshdre lienscnrfw
      481 viskgrvqew pdaasayqsl fatggkvrse tapaalpdlv aqstfasdea evqwqrwcql
      541 eawletdrar kpkhqkshlq qewqqemrrl eeslgl
//
LOCUS       WP_176059617             394 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059617
VERSION     WP_176059617.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..394
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42234
     Region          51..392
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mgvanifhph prkqpptdpq dptgqasttt aasadervrr eswfkhllnr pefaalagta
       61 mvfivfglaa gnsgmfnldg vmnwsqvaay lgliavgacv lmiagefdls igsmigfagm
      121 mvalptmyfh wpiwlaiifa fagsmllgal ngylvmrtrl psfivtlafl filrgltlal
      181 svmfadrtii sgvgdvarqd wlahtlfqgv afkglfvwlg hlglvkmldn gvplvpgipk
      241 vllwwlglai vcafvlartr fgnwifavgg danaaknvgv pvrrvkislf vltafcscly
      301 avlqvcdigs aaadrglqae feaiiaavig gtlltggygs vigacfgali fgvvqigity
      361 tnvdsdwfrv flgvmllfav lfnhyvrsrv aasr
//
LOCUS       WP_176059630             246 aa            linear   BCT 11-JAN-2025
DEFINITION  SOS response-associated peptidase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059630
VERSION     WP_176059630.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Paulin,K.A., Cortez,D. and Eichman,B.F.
  TITLE     The SOS response-associated peptidase (SRAP) domain of YedK
            catalyzes ring opening of abasic sites and reversal of its
            DNA-protein cross-link
  JOURNAL   J Biol Chem 298 (9), 102307 (2022)
   PUBMED   35934051
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Amidon,K.M. and Eichman,B.F.
  TITLE     Structural biology of DNA abasic site protection by SRAP proteins
  JOURNAL   DNA Repair (Amst) 94, 102903 (2020)
   PUBMED   32663791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005396
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..246
                     /product="SOS response-associated peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0009432 - SOS response [Evidence IEA]"
                     /calculated_mol_wt=27092
     Region          1..245
                     /region_name="SRAP"
                     /note="ssDNA abasic site-binding protein YedK/HMCES, SRAP
                     family [Replication, recombination and repair]; COG2135"
                     /db_xref="CDD:441738"
ORIGIN      
        1 mcgrisqyrd prlytqhlgl adplmlfdaa drrpgynlap gthplaifad qtlrpvhwgy
       61 cpdwareqhl pqtinarada aptaryfkel wktgrvlvpa dgwfewrraa apstesaesa
      121 pdvaptgass datprqpyfv hlksaapmyl aalssvrgte pqtegmglvi vtasadaglv
      181 dlydrrplvf gpeaarrwle pdlpadeleq lartgglaag rfrwhrvshd vdrtlndepg
      241 lieald
//
LOCUS       WP_176059646             386 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176059646
VERSION     WP_176059646.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..386
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41286
     Region          1..379
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnfqhtedrr mladslnrfv seqygfdtrd qiarsaqgfs selwgrfael gvigalfdea
       61 nggfggggfd msvvfeclgr glvvepfldt lmvgqalvrs gnetqralle glidgsriva
      121 lahgepdghy elarvatral rdgqadtdgd adgrswqlng skavvqhgeh aglflvsart
      181 hgaddaeegi slflvprdta gvsvrgyrki dggraaevtf dhvtldagal lgtagvgfat
      241 leyaigcgvl alcaeavgam dvakdhtley lrtrkqfgvp igsfqalqhr madllleieq
      301 arsavinaaa algaprttre ralsaakysi grigamvaee ciqlhggigm twelplahya
      361 krlvmidhql gdedhhlerf ialggr
//
LOCUS       WP_176059664             552 aa            linear   BCT 11-JAN-2025
DEFINITION  amidohydrolase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059664
VERSION     WP_176059664.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446324
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..552
                     /product="amidohydrolase"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016810 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59167
     Region          23..548
                     /region_name="YtcJ"
                     /note="Predicted amidohydrolase YtcJ [General function
                     prediction only]; COG1574"
                     /db_xref="CDD:441182"
ORIGIN      
        1 mshfshdshd aarenlryrn ctfvngtiyt ggttptvvpc lavrdgviay agsyadlpae
       61 lhaaeqvdlr grmivpgftd shahpvegfq ltcdadlgda hsldaiahqv recaalhpqr
      121 swvmagnval ealgaqlnrs aldmmvgdrp lllighdvhs gclntaalrv lgvsattpdp
      181 eggiyerdah gaptgvvhea alyglfrhlp qmgadesara lqkaqrqahe ngitgwfeam
      241 vgqrlvdayv rardsgnlka nvslgllvsp nlalapqigk lidwrrqydg grvrlhtaki
      301 fidgvlesht galldnyadv dhngaahwtp aqlheavfaa daagfdlhfh tigdravrma
      361 ldtlealnre rgrrdrraql ahvqlidpld vprfaetgai asvqavwgsv apglkalytq
      421 llgerrmsrq yafgdlqrgg amlsggsdwp vstqnplvai etalrraapg dvadvpflpe
      481 qsvgveamlk aythnsafsl rfdgeagvla vgrpaslavl sgdvrdvaph rvaevqvgmt
      541 lfegervfgg ve
//
LOCUS       WP_176059665             234 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176059665
VERSION     WP_176059665.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..234
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25768
     Region          13..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtvsaasrrv pvqarseqrl raileaarlv fsevgyasat mteiarrvgv seatiftyfa
       61 skrdlcvrvl gnwydeiiaq vegelplidg trskfaylvr thlyrltvdg tglcalilse
      121 grekddkfgd vivelqrryt apmmqvlaeg vaggdvrddm plgllrsavy gpmehvlwda
      181 vrkqravdie ataaslsdll wqglvppdar qaalkqlrnd ivgavkrfea aesk
//
LOCUS       WP_176059673             298 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176059673
VERSION     WP_176059673.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..298
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31585
     Region          41..291
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 martsrpsaa vtaaarpsaa saaepvaaqa danpaadtta prtrtsaldr avqildalqq
       61 anrpatayev arivgaplst vysiindlvd knllarrmdg tiwlgsrlyg ygltyassld
      121 ylavaneemq rlsaeveetv qvcgledgmm vvqqmaegpg hfrvtsrvgs rvplnwtasg
      181 rllvghlpda ervaffvqha qssptgraet rpevlariar ealdarlsiq igesdasvac
      241 laapvldntg acvftisivm peakaelgte rfaqavqava ariearlgwr hrdpepaa
//
LOCUS       WP_176059716             307 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059716
VERSION     WP_176059716.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..307
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32867
     Region          23..276
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mntlpapflp aakprsrfkl ptsrswlaag qwlvtlllca flivpvvmsi magltvnyfk
       61 gvssgltlrw lvevwtqyhd svflslevaa atlfitlltg vpagyvlars ktrlsriiee
      121 flvlpialpg lasalallvv yggftmfrms vafivvghvv ftlpfmvrav aavcassdlr
      181 tleegaaslg asfwqrfvtv vlpnarpgiv agalavvtls igefnltwml htpdtktlpv
      241 gladtyaslr ieigsaytil ffimtmpllv amqwlgvdat gqrsaakkrs aasasksiik
      301 stptstp
//
LOCUS       WP_176059758             222 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FMN-dependent NADH-azoreductase [Paraburkholderia].
ACCESSION   WP_176059758
VERSION     WP_176059758.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Ryan,A., Kaplan,E., Nebel,J.C., Polycarpou,E., Crescente,V.,
            Lowe,E., Preston,G.M. and Sim,E.
  TITLE     Identification of NAD(P)H quinone oxidoreductase activity in
            azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone
            oxidoreductases belong to the same FMN-dependent superfamily of
            enzymes
  JOURNAL   PLoS One 9 (6), e98551 (2014)
   PUBMED   24915188
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003095
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..222
                     /product="FMN-dependent NADH-azoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0050446 - azobenzene reductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24360
     Region          1..206
                     /region_name="AzoR"
                     /note="FMN-dependent NADH-azoreductase [Energy production
                     and conversion]; COG1182"
                     /db_xref="CDD:440795"
ORIGIN      
        1 mkvlhvdasa krersnsral sryfierlrs egvefdidyl dvtvdtpahv teafaiatyt
       61 pehertpamk atlaasdalc qrlldadali fampmynwsm psafkayidn vtrtgltyvn
      121 tadgriegql qrqktifits rgadlraapf ssmdaltpal kaafgfigva nptfvdaqpl
      181 qfsdqqarie alerahreld avaaqwanel spveadeasl ta
//
LOCUS       WP_176059842             545 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059842
VERSION     WP_176059842.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 545)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..545
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59168
     Region          14..544
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msatpatqng aqaatpplle lehlhvtfgd tvavndvtla iargervalv gesgsgksvt
       61 alsilrllnd aqvsgairfd gedllakser emrglrgsdi amifqepmta lnplytvgdq
      121 iaetivvhdg vtanearkra vallgrtgia epgkrvnsyp hqlsggqrqr amiamalacr
      181 prllladept taldvtiraq ivelllelqr deaekrgmav llithdlnlv rhfaqriavm
      241 eqgvlvecgp veqvfaspqh pytqrllasr pertvvpvlp ispvlleard vsvdfkaklp
      301 gfsgwfrtgr fravaqasvs vrqgetlgiv gesgsgkstl amallglqrt ahgeiefqgr
      361 algsyrgaeq ttlrsnmqvv fqdpfsslsp rqtierivge glalhrptmt pearrdkvva
      421 vlrevgldrt vlyryphefs ggqrqriaia ralvlepril ildeptsald vsiqqqvlkl
      481 laglqqkynl gfvfishdla vigamahrva vmqngsives gdveqifatp shpytrkllk
      541 aaldh
//
LOCUS       WP_176059877             383 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176059877
VERSION     WP_176059877.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..383
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=40515
     Region          4..277
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 maqrrlrlgm vgggqgafig avhriaarld drfelvagal ssdpqraqas aaeagiarsy
       61 adwremacae aarddgidav aivtpnhlha pvatafleag ihvvcdkpla islaegeala
      121 klareknklf althtysgyp mvryarelid sgglgelrvv qveyaqdwla epietsgtnk
      181 qagwrtdpal agpagclgdi gthayhlaaf vtgmtpssla aevhtfvpgr riddhvqaml
      241 ryangargml wasqvasgae nalrlrvygt kanlafdqeq pndlwftplg gsaerltrgr
      301 vksaiaahat rvpaghpegy leafaqlykd aalqiealda gralpaesll lttvedgvag
      361 lrfidamlas saadgqwrei gga
//
LOCUS       WP_176060047             188 aa            linear   BCT 11-JAN-2025
DEFINITION  YceI family protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176060047
VERSION     WP_176060047.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..188
                     /product="YceI family protein"
                     /calculated_mol_wt=20261
     Region          1..188
                     /region_name="YceI"
                     /note="Polyisoprenoid-binding periplasmic protein YceI
                     [General function prediction only]; COG2353"
                     /db_xref="CDD:441920"
ORIGIN      
        1 mliavgalas afsvgafaad tyqldpthty psfeadhfgg lsvwrgkftk ssgtvtldra
       61 aktgtvdvtv dpasvetgnt kldehlktda ffdvakypav tykgtdikfd gdkpvqvigs
      121 ltmhgvtkpl nltidsfkcm qhpvlkrevc gveasahfnr adygmdfgtk ygfnmdtklh
      181 iqsegikq
//
LOCUS       WP_176060086             239 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176060086
VERSION     WP_176060086.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..239
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=26455
     Region          13..218
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 midghdprgn hllaalpeae warvsahlvl vdmplgrvvy esgqqlsray fpttsivsll
       61 yvmedgasae isivgneglv gialfmgget tpsravvqsa gwayrldarv lkdefgragp
      121 vqrlflrytq alitqmaqta vcnrhhsidq qlcrwlllsm drlpsnelkm tqelianmlg
      181 vrragvteaa mklqdaglir yshghievld rpaleqrvce cygvvkrefd rllpdlmal
//
LOCUS       WP_176060126             239 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176060126
VERSION     WP_176060126.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..239
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=26611
     Region          13..218
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 msqdhrqhen hllavlpdle wgrvrphlea vdmplgkvvy esgdrlnyvy fpttcivsll
       61 yvmedgasae iaivgnegli gialfmgget tpsravvqsa gnayrldaqi lkaefhragp
      121 vqrlllrytq alitqmaqta vcnrhhsidq qlcrwlllsi drlssnelkm tqelianmlg
      181 vrrsgvteaa lklqdaglir yshghievld rpgletrvce cygvvkrefd rllpalkal
//
LOCUS       WP_176060171             299 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176060171
VERSION     WP_176060171.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..299
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32224
     Region          7..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          91..287
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,222,239,266)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     216..220,227..228,231)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mkdifslrly trvarlgsfs aaarefglsq sqasrviadl egelgarlln rttravvltd
       61 agaqflsrid pilvaldeae qsvreggdlr gmlrmsmpss iatrtvipal asfmaahpel
      121 rvevmlgdqp qdlirdavdv airlgrmlds tatarliati prvvvaspay ldlhgapdkp
      181 ealrahrivg gpasmvptaw rfernrqevt veldahftat endgavaaak aglgvtstse
      241 wscrheladg alirllpewk laaipvhayf plgratraag ravvehlvav irrdegadw
//
LOCUS       WP_176060176             379 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176060176
VERSION     WP_176060176.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..379
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40674
     Region          3..344
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,58,100,227,298,318,320..322)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,58,100,102,109,175,178,180,227,234,298,318,
                     320..321)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,102,175,178,180,321)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            180
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 maklftsakv gaynlthrvv lapmtrvrti qpgdipspim adfygqrask ggllvieaas
       61 isiqarsylg aasiyhdgqh egwkaiadav hakgghaflq lihggrqshv evtggahpva
      121 psevpfdgva ltkdgfvpas phraleidei agivedfrra aerakkagfd gvelhaangy
      181 lvdqfiqdgt nkrtdayggp venrvrflre slealisvyg adrvgvrisp sgewggisds
      241 dpqatfsyva kvldsykiay lhvieprikg ddtlhegqav vaasylrphf sgpiiaaggf
      301 drdgaiatve kgdanliafg rhfssnpdlp yrlehdlplt pyvraafwgg deknysdfpa
      361 ysgqnkddsl qdvvdaeav
//
LOCUS       WP_176060184             367 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176060184
VERSION     WP_176060184.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..367
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39361
     Region          3..344
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,58,100,227,298,318,320..322)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,58,100,102,109,175,178,180,227,234,298,318,
                     320..321)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,102,175,178,180,321)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            180
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 mdklfspitv gpfvlshrvv lapmtrlrti qpcdipspmm aefygqrasn gglvliegts
       61 isltarsylg aasffhdgqt dgwkavadav hakggrvfmq lihggrqshv emtggedpva
      121 psvvpfdgva ltkdgfvpas phralelaei pgiiedfria aqramdagfd gvelhgangy
      181 lvdqfiqdgt nkrddayggp vearvrflre avealisvwg anrvgvrisp sgewggisds
      241 dpeatfshva kvlhgygiay lhvieprvkg ddtlhdghpp vassylrphf sgpiiaaggf
      301 dgesahaivn sgnadlvafg rhftsnpdlp yriqnrlpla pyvragfwgg deklytdfpt
      361 ydgkhgr
//
LOCUS       WP_176060210             297 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176060210
VERSION     WP_176060210.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..297
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33418
     Region          8..67
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 msdatqlpan raivlrnatc aycgrlfgad rketkehvig rrfvpkgtla gqwnvilnac
       61 ndcngdksdl eddisvismm pdqfgqyaid dqrlkdevlr katksqsrrt gkkvadsreq
      121 itiggafrga tlalnftapv qveearlyrl ahyhfrgffy wlsyqreanv ggfirggffp
      181 lgacrrtdwg sprfrwfmal arewdirlca igadtffkal vrrdpggtev wlwafewnhs
      241 irvvgfagne davrsllata pghatavlse tekelirfrp evslledqdd lfavlvd
//
LOCUS       WP_176060201             107 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF190 domain-containing protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176060201
VERSION     WP_176060201.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..107
                     /product="DUF190 domain-containing protein"
                     /calculated_mol_wt=11580
     Region          4..103
                     /region_name="COG1993"
                     /note="PII-like signaling protein [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:441596"
ORIGIN      
        1 mqgyqltfft eqnrkhghqs icdwllkfae qhgasggtlm tgaegfdrag kfhsagffel
       61 adqplaitvs vdeqacqglm nalaeedvdl syvkipvefg rvgrsva
//
LOCUS       WP_176060242             245 aa            linear   BCT 11-JAN-2025
DEFINITION  CPBP family intramembrane glutamic endopeptidase [Paraburkholderia
            sp. BCC1876].
ACCESSION   WP_176060242
VERSION     WP_176060242.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Manolaridis,I., Kulkarni,K., Dodd,R.B., Ogasawara,S., Zhang,Z.,
            Bineva,G., Reilly,N.O., Hanrahan,S.J., Thompson,A.J., Cronin,N.,
            Iwata,S. and Barford,D.
  TITLE     Mechanism of farnesylated CAAX protein processing by the
            intramembrane protease Rce1
  JOURNAL   Nature 504 (7479), 301-305 (2013)
   PUBMED   24291792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10494850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..245
                     /product="CPBP family intramembrane glutamic
                     endopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070007 - glutamic-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0071586 - CAAX-box protein processing
                     [Evidence IEA]"
                     /calculated_mol_wt=27149
     Region          142..227
                     /region_name="Rce1-like"
                     /note="Type II CAAX prenyl endopeptidase Rce1-like;
                     pfam02517"
                     /db_xref="CDD:460578"
ORIGIN      
        1 mdsnqaesva alvqskrprg lfakeftraa wfgpcvylly rffilpggai llarspvgny
       61 tilvnygpaa vflgamfllh rryfansinf vgsfrakdvi vgvaaisaly vatnciavwi
      121 hqprepimeg mfrsltptqt sfligsllcl ppiveelafr hflasffpfr ksivwafvav
      181 iltalwfthm hsyvyltsdv tiflmgiilg larvrtlgmv lpmclhaysi gfalladfvr
      241 tsyag
//
LOCUS       WP_176060385             435 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176060385
VERSION     WP_176060385.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024289
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45665
     Region          21..425
                     /region_name="MFS_ShiA_like"
                     /note="Shikimate transporter and similar proteins of the
                     Major Facilitator Superfamily; cd17369"
                     /db_xref="CDD:340927"
     Site            order(33..34,37..38,41,80,138..139,141..143,146,166,
                     169..170,173,256,259..260,263..265,268,296,300,352..353,
                     357,361,377,380..381,384..385,388)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340927"
ORIGIN      
        1 mstspisaaq pnvagqnssa riifasfigt aiefydfyvy ataaalvigp vffphgsata
       61 qalsafvtfg iafvarpigs flfghfgdri grkstlvasl lvmgvsttli gfvpgydsig
      121 slapillcvl rfgqgiglgg ewggaallat enapagkrgw fgmfpqlgps vgflasnglf
      181 falalslsde qfrswgwrvp flvsavlval glyvrlkiae tpafkaaier kervkvpiat
      241 llsqhwlptl lgalamvvcy tlfynattfs lsygvsvlhi prptflgmlc iavvfmalat
      301 plsawaadry grkpvllvgi vaailsgftm apllgsgqtp lvllflviel flmgvtfapm
      361 gallpelfpt nvrytgagvs ynlggilgas vapyiasvla ahgglpwvga yvsiaaavsm
      421 igvlcmretr dtqlm
//
LOCUS       WP_176060344             174 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176060344
VERSION     WP_176060344.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..174
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18909
     Region          1..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mykrilvaid gsetsehafd salqlahdnd aqlqplyvvd nplmaydasg ydptilrdaf
       61 veegqrllad alarmkhenv agvprivdvt pigediseri risanefnad llvlgthgrr
      121 gfkrlflgsv aervvrsasl pvllvpsrqa qtsvvdaarh ghadvaaavy elpr
//
LOCUS       WP_176060388             270 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176060388
VERSION     WP_176060388.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..270
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=29990
     Region          20..99
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(45,70)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(52..53,64,67,71..72)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          127..268
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mttpptadhp ppleatpara lgdfirahre rlspqavglp pgprrrtpgl rreevaqlcg
       61 vsptwytwie qgrpvsasae alariavalq lsraeraylf elaaqrdpae pdpaaadapa
      121 tlletvrlvn apayvldrqw talawneraa dlfvgwldga hdrnllrytf tepaaseliv
      181 dwetrarrla aefradsirh lndaptrali dslsaasdaf trfwasqdvg greggrrefn
      241 hprdgrivyd qitfkpahre dlklvvlvre
//
LOCUS       WP_176060405             147 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176060405
VERSION     WP_176060405.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..147
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=15616
     Region          1..146
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mqfelngrpf sfdgdaqtpl lwvirdhaml cgtkygcgig acgactvhle gdavrscvlp
       61 vsavagksir tiealspdgt hpvqrawvak dvpqcgycqs gmvmaaaall vhtpkptdaq
      121 idqaitnlcr catyqrirea ihvaaey
//
LOCUS       WP_176060420             127 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176060420
VERSION     WP_176060420.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 127)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..127
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13305
     Region          <44..119
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mnkpqqalht vfkaacasaa viglvaanva haadagngkv ladahncaac hgvnlnkpvs
       61 peypklagqh adyvywalrq yqmgngnphl grnnaimqaq vqslsqgdmk diaayvesln
      121 gdlvqkk
//
LOCUS       WP_176060440             394 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176060440
VERSION     WP_176060440.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..394
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41205
     Region          12..394
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtaaqqengv apvvivgtgm agytvarelr kldiavpivm isrdagsfys kpmlsnalam
       61 kkepqalasf dalamasqlg awirvhqnve rimpaehtll vdnalvgyrq lvlatgadpr
      121 rllvggdgad dvlsindldd yarfrlaltr crsvailgag ligcefandl aaagyavdli
      181 dpattplarl lpqqvgeifa ralegggirf hpgrsvsrid rlsdgyrlsf adgeridadl
      241 vvsaiglapr talaaaagle ieqgirtdaw crtsapdiya lgdcaaidgk vqpyvlpimh
      301 aaralartla geptrvafpv mpitvktpas pavvvtpege gawsietggd tavhaaravc
      361 tqvdgertlg fallgksveg kaalikamap ppnp
//
LOCUS       WP_176060497             314 aa            linear   BCT 11-JAN-2025
DEFINITION  AEC family transporter [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176060497
VERSION     WP_176060497.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..314
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=33134
     Region          1..312
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mlatleillp vfglifagfa crrrgvlgpn saselnrfvv wlalpallfd tmaratwqql
       61 yqpafvatfs iacvavflli lalrlmngrh ladasvdaia asypntgyig fplaliafgp
      121 asltpttiat ilvacvlfaf aivlievglq teraphklgl kvlralarnp livspiagml
      181 lasfhvampa saetflklls gaaspcalvs lglflaekrp sesgargval lltgvklvaq
      241 paltwwlaar vfglsptlve mavvlaalpt gtgpfmlaef yereahitsr tilmstagsv
      301 itlsallllm ghrt
//
LOCUS       WP_176060580             360 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176060580
VERSION     WP_176060580.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 360)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..360
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38958
     Region          1..359
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 maavqlsgif krygdtqvvh gidldiddge fvvlvgpsgc gkstlmrmva gleeisggdl
       61 miggtrantl apqqrnismv fqsyalyphl svyeniafgp rirkessasf kprieaaakm
      121 lnlsgyldrl pralsggqrq rvamgravvr epslflfdep lsnldaklrv qmrteikalh
      181 qrlkntviyv thdqieamtm adrivvmnag rieqmgrple lydrpanlfv asflgspsmn
      241 faegvvasga qgqgltlklt gggqivlega sasaavgakv tlgvrpehie tmaqtpdatm
      301 evevveptga ethlygkigg stwcvttrqr skiepgqria lrlpaehihl fdtesgrrlv
//
LOCUS       WP_176060608             887 aa            linear   BCT 11-JAN-2025
DEFINITION  FHA domain-containing protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176060608
VERSION     WP_176060608.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 887)
  AUTHORS   Li,J., Lee,G.I., Van Doren,S.R. and Walker,J.C.
  TITLE     The FHA domain mediates phosphoprotein interactions
  JOURNAL   J Cell Sci 113 Pt 23, 4143-4149 (2000)
   PUBMED   11069759
REFERENCE   2  (residues 1 to 887)
  AUTHORS   Durocher,D., Henckel,J., Fersht,A.R. and Jackson,S.P.
  TITLE     The FHA domain is a modular phosphopeptide recognition motif
  JOURNAL   Mol Cell 4 (3), 387-394 (1999)
   PUBMED   10518219
REFERENCE   3  (residues 1 to 887)
  AUTHORS   Hofmann,K. and Bucher,P.
  TITLE     The FHA domain: a putative nuclear signalling domain found in
            protein kinases and transcription factors
  JOURNAL   Trends Biochem Sci 20 (9), 347-349 (1995)
   PUBMED   7482699
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..887
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..887
                     /product="FHA domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=96253
     Region          21..120
                     /region_name="FHA"
                     /note="Forkhead associated (FHA) domain, binds pSer, pThr,
                     pTyr [Signal transduction mechanisms]; COG1716"
                     /db_xref="CDD:441322"
     Region          <182..239
                     /region_name="FHA"
                     /note="Forkhead associated (FHA) domain, binds pSer, pThr,
                     pTyr [Signal transduction mechanisms]; COG1716"
                     /db_xref="CDD:441322"
ORIGIN      
        1 matgeapiae mrvtagtafd vvlspvasaq rpaldairiv dnlfaigrse apftdypaer
       61 iarlsrrhar vfteqgalyv adleskngtt vngvavrqtp arvragdelc fggelcyrvs
      121 ieprarivag agsspvsall lvpqrddlgl qpievqafpf liskadevfs rykeryphqv
      181 nyisrrhahi flkggefyve dlgstngtfv ggkrldesal pladgnlvaf ggdhfvyrvt
      241 lqkppevept vtqlvfhpta deaadtdktt fvgaansfld ifcvdparqr edevnqaaqp
      301 wsgpskrdat gsaaragngl sdariaehvn ganatngang angathaada rgsngannks
      361 atqgrthrwr lvagelsktf aggdrtsvrr iamwggaglv vlialvstly lrgsserelk
      421 dllasgdyns avtaakgyla dhpadtkvsa laseallkar lpdwlntlqk vqfdqadtll
      481 nemrslsann adamsligel qwvgdlerfv avrggveapi rmyadettin gllqrwddda
      541 kshqraldri asyvpvfaep yaqalshlrk lesddsvyva aidrlngtir telardkpda
      601 lpavlddyaq ryprlagldr vrddlrqyta llnaalsrql apllamlktt rfstppfqaq
      661 fqqlaasrlp sqdviqqqsa vtaawqrgda qqalaglaam pagpwsdvla aeqthkkall
      721 dqfsdlqktr ggkdyderll sfyasldpvt dvwfaqsiqk dvaalhdkal araqdlllra
      781 qslwkqyras gpiggtqrle agispgfrse arllsdaqta aqqgmriftq lkadhpadfd
      841 rlladidaea dlqrrsltel rmvldpgllk aklaligdeq setrpsp
//
LOCUS       WP_176060708             189 aa            linear   BCT 11-JAN-2025
DEFINITION  Fur family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176060708
VERSION     WP_176060708.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..189
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=19939
     Region          34..172
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mktakpaala akapsaatah ahepghthga sqeaaltlad eycrergekl tpirrkvlel
       61 llnsgratka ysllddmrqi hpgsapptvy raldflltag lvhriesina ftvchdltqc
      121 qhgilvvcqq cgnvtelhqp klrqalvaqi edagyrlasd eielkglcsa cqaaeaeaaa
      181 ssaaavaak
//
LOCUS       WP_176060746             251 aa            linear   BCT 11-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator
            [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176060746
VERSION     WP_176060746.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..251
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26367
     Region          1..251
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mltsqrkqli lealkrngqv iaktlsvefe vsedtirrdl relaaegqlq rvhggalpas
       61 paavdfagre riesaskaai graaagmiap gqivfvdggt tavqlarhlp rdlqativth
      121 spsiavelae htqlevvmig grlfrhsmvn lgaaaietls hiradlffmg atgvhpqagl
      181 stgdreeayv krafaehaae tvvlasaekl haasaykiad vtaasaivve rgtaealtap
      241 fealgitivr a
//
LOCUS       WP_176060785             318 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176060785
VERSION     WP_176060785.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..318
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35022
     Region          5..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..294
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(103,107,146,160,162,226,243,270)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(104..105,109..110,112..113,116,120,122..128,189,
                     220..224,231..232,235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 midritamrt firivdtnsf traaeslnip ratatttvqn leallgtall arttrrlsvt
       61 pegaayyerc tqiladiddm easirhatdn ltgrlriemp gavasaivlp alenfhtryp
      121 nldlaisisn rtvdliseai dcsiqlgelp dsnlvarnlg tlehvtcasp aylarygtpt
      181 dlddlrghva vncmsphngr evdfdfevdg eaqqvkvkgf vkvsdeqayl icglqglgli
      241 qpariaaqpy ldsgllrevl pqwqpvpmpv avayvknrrv sprvrafvdw laelfekaeh
      301 vdqdltrvrq llrglhpa
//
LOCUS       WP_176060793             203 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: response regulator transcription factor
            [Paraburkholderia].
ACCESSION   WP_176060793
VERSION     WP_176060793.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..203
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21722
     Region          8..200
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mrhhaeavih vvdddtavrt almrllhqag fqvkgypsag dflvavpdal pgcllldlel
       61 pgpsgldlqh alhrmgnpmp vvfisahhdi pktvtaikag asdfllkpie tqallaaidn
      121 alasvtveps tdrqhtdtda valnereqvv lrgivagrln kqiaaelals ertvkscrad
      181 lmrkfhahsl adlvrladpa vra
//
LOCUS       WP_176060796             253 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176060796
VERSION     WP_176060796.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..253
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28133
     Region          15..241
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 mstlvinppa lggtrykevk sailaalsag ewkggecips ekrlaerfgv sigtlrkaid
       61 elcaenilir hqglgtfvsm hqrdrhffrf frivrrdgdk aypvvtlidf rkarasreva
      121 atlgietgar vfqftnglal hgatvliehi tvpearfagl teaklrnrpn tlynfyqdvf
      181 ainvvetder vtvaladdle srelsldaga plleirrvay synrcavelr vsrlntenyq
      241 yigahpgree qag
//
LOCUS       WP_176060829             200 aa            linear   BCT 11-JAN-2025
DEFINITION  2'-5' RNA ligase family protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176060829
VERSION     WP_176060829.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Remus,B.S., Jacewicz,A. and Shuman,S.
  TITLE     Structure and mechanism of E. coli RNA 2',3'-cyclic
            phosphodiesterase
  JOURNAL   RNA 20 (11), 1697-1705 (2014)
   PUBMED   25239919
  REMARK    Erratum:[RNA. 2014 Dec;20(12):2011]
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Arn,E.A. and Abelson,J.N.
  TITLE     The 2'-5' RNA ligase of Escherichia coli. Purification, cloning,
            and genomic disruption
  JOURNAL   J Biol Chem 271 (49), 31145-31153 (1996)
   PUBMED   8940112
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..200
                     /product="2'-5' RNA ligase family protein"
                     /EC_number="3.1.4.58"
                     /GO_function="GO:0004113 - 2',3'-cyclic-nucleotide
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0008664 - RNA 2',3'-cyclic
                     3'-phosphodiesterase activity [Evidence IEA]"
                     /calculated_mol_wt=21205
     Region          20..198
                     /region_name="ThpR"
                     /note="RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA
                     ligase) [Translation, ribosomal structure and biogenesis];
                     COG1514"
                     /db_xref="CDD:441123"
ORIGIN      
        1 mpeqfwlpgl eapptptdgl ffavfpdpnt atgiakfaqq lcvearvrsk plaagrlhvt
       61 lqhlgnfagg lpqahvdaam qaaasvrmep ftvefdsvvs fatrprpgpl vlgggegvag
      121 lhalhdalva alpnarvgda tvspampytp hvtlaygmpw aatrpiepvs wnvrefalmh
      181 sllgrtrhvv larwrlagvv
//
LOCUS       WP_176060830             250 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176060830
VERSION     WP_176060830.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..250
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26917
     Region          3..222
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 msdtdpaavn sskpeaiaer iraailehrl apgaklteaq lcevfnvkrg pirqalaqla
       61 tdhlvdlepn rgafvaspsl qevhevfemr riielavvek icnghgmrrl knigsmigre
      121 rkafetrdfp awirlsgefh telagltgna vlcdclnglv arstlisaly eslgrspcsf
      181 edheailaal dagdakeaaa lmsrhlqsve lkmlerparg aadlhevfga ldsaskessn
      241 gksrsksapg
//
LOCUS       WP_176060858             350 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176060858
VERSION     WP_176060858.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..350
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38080
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mnqlqsmrvf vkvadlgsfv gaagaldlst avvtrhvadl earlgtrlln rttrrlslte
       61 sgstylervr hilddlegve qmvvarnhep vgtlrivapv vfglhslapv vqsyaarypd
      121 vmpdvtladr qvdlveegyd vgimvtrhmr sasivtrrlt tgymtvcatp aylaqhgtpt
      181 rpehllehpc lsrpseqggd ervftgpdge vrvrpsnaia anntemlrqf allgmgvail
      241 psyligrdla sgrlvpllgd yrlpqieiti aypsrlhlpa kvrtfidhlv eyfqpgqpss
      301 rdrsasafav taldpahdlp eadlhsdtvr pvrsavrtrs aasvsasspi
//
LOCUS       WP_176060847             467 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176060847
VERSION     WP_176060847.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..467
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=49944
     Region          <13..290
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mmrfkfrrrt qsqgvvgdia aqagklgiei cdvsghveev aarvqrqaqv cralresaaq
       61 tlagnhriat aaremrnvsa eaatgvqasq etllasladi hglvegvtvi esqigalrsa
      121 lahvsrvsee isliarqthl lalnaaieaa ragesgksfa vvaaevknls aktaqatgqi
      181 ettlaqltqq teqlisegsv ntarahrvre gtrkigdvvh atgdaiaqln neageiaalt
      241 geietqcdgl eaqvlemasg vedssenfaq akdrlgnllg vsetlielta atgvetadtl
      301 fidavqraaa avskvfegav argevsiedl fdqryvpvag snppqfvtrf tsftdrvlpa
      361 iqepllklds rvafcaavdl rgylpthnlk fslaqredvv wnmancrnrr mfddrtgiaa
      421 ashtkrfllq tyrrdmggge fvlmkdasap vfvggrhwgg vrvgyrv
//
LOCUS       WP_176060883             359 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176060883
VERSION     WP_176060883.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Lairson,L.L., Henrissat,B., Davies,G.J. and Withers,S.G.
  TITLE     Glycosyltransferases: structures, functions, and mechanisms
  JOURNAL   Annu Rev Biochem 77, 521-555 (2008)
   PUBMED   18518825
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11421525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..359
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39223
     Region          11..199
                     /region_name="WcaA"
                     /note="Glycosyltransferase involved in cell wall
                     bisynthesis [Cell wall/membrane/envelope biogenesis];
                     COG0463"
                     /db_xref="CDD:440231"
ORIGIN      
        1 msissgslls tvsvclptch rpelvvqcid sclaqsygnl eivigddsnd trtqqliear
       61 yrdeprvryt lnrpplgqar nvaslferat gdkillihdd dllttdgvek lvslwkqhpq
      121 ldaafgdqye adhagaigfd gsrqlnidfr rtrdaeglqp lpgrtgliqm fpnngwmada
      181 qlvkrigyse qygmccdfvf gaelclaare vfylhdyvsv yrktatsish strgtaiaat
      241 vsayafvkal slppslepsr rlalrrlapi vvsvharnrq vraglkilfg hlfayrygls
      301 krfyyhlaml aragfsvrpq avaaaavaav aaapavaaep vaavkelvse lvadrsepv
//
LOCUS       WP_176060888             448 aa            linear   BCT 11-JAN-2025
DEFINITION  NCS2 family permease [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176060888
VERSION     WP_176060888.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Koukaki,M., Vlanti,A., Goudela,S., Pantazopoulou,A., Gioule,H.,
            Tournaviti,S. and Diallinas,G.
  TITLE     The nucleobase-ascorbate transporter (NAT) signature motif in UapA
            defines the function of the purine translocation pathway
  JOURNAL   J Mol Biol 350 (3), 499-513 (2005)
   PUBMED   15953615
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789293
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..448
                     /product="NCS2 family permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46045
     Region          15..441
                     /region_name="NCS2"
                     /note="Xanthine/guanine/uracil/vitamin C permease
                     GhxP/GhxQ, nucleobase:cation symporter 2 (NCS2) family
                     [Nucleotide transport and metabolism]; COG2252"
                     /db_xref="CDD:441853"
ORIGIN      
        1 mpkaasaaap assswlerrf alserktsvr ietiagitsf laaayllvvi psllaaggmd
       61 rgaattatil vfvlstvlma lyanlpflvg pgiggsvilg vtlagehvaw qtglgiacvs
      121 gvlflmltlv garslvmrli paqiklglga siglfiavlg frnagmvian aktnalalgd
      181 fsrpgtlval iglgaavvlq grrvpgailw ailiaagagv plgvthlpas flawphsiap
      241 iafkvdlvsa lsvasipylf vffaaeffst lgttlavgak anlldenanl pninrpflvd
      301 siaatlgpvf gipaltalve saagveaggr sglsslaaaa mfalmllfvp valaipkeat
      361 apaliligls mfstirhahf ddftdslpvl smvlltlmsn sfgtgiaggl lcyvlvklla
      421 grfrevpwgl yvlavplgyy fytvvkph
//
LOCUS       WP_176060945             171 aa            linear   BCT 11-JAN-2025
DEFINITION  arsenate reductase ArsC [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176060945
VERSION     WP_176060945.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Messens,J. and Silver,S.
  TITLE     Arsenate reduction: thiol cascade chemistry with convergent
            evolution
  JOURNAL   J Mol Biol 362 (1), 1-17 (2006)
   PUBMED   16905151
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Mukhopadhyay,R. and Rosen,B.P.
  TITLE     Arsenate reductases in prokaryotes and eukaryotes
  JOURNAL   Environ Health Perspect 110 Suppl 5 (Suppl 5), 745-748 (2002)
   PUBMED   12426124
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Messens,J., Martins,J.C., Van Belle,K., Brosens,E., Desmyter,A., De
            Gieter,M., Wieruszeski,J.M., Willem,R., Wyns,L. and Zegers,I.
  TITLE     All intermediates of the arsenate reductase mechanism, including an
            intramolecular dynamic disulfide cascade
  JOURNAL   Proc Natl Acad Sci U S A 99 (13), 8506-8511 (2002)
   PUBMED   12072565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11611440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..171
                     /product="arsenate reductase ArsC"
                     /EC_number="1.20.4.4"
                     /GO_function="GO:0004725 - protein tyrosine phosphatase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030612 - arsenate reductase
                     (thioredoxin) activity [Evidence IEA]"
                     /GO_process="GO:0046685 - response to arsenic-containing
                     substance [Evidence IEA]"
                     /calculated_mol_wt=18835
     Region          8..142
                     /region_name="LMWP_ArsC"
                     /note="Arsenate reductase of the LMWP family; cd16345"
                     /db_xref="CDD:319973"
     Site            order(13,15..20,113,115)
                     /site_type="active"
                     /db_xref="CDD:319973"
ORIGIN      
        1 mtehrkynvl flcthnsars ilaeaalnel asdrfvgysa gshpgtapnp faldllrsqg
       61 isteglrsks wdefaedgap qidfiftvcd naagevcpiw pghpakahwg vadpstaegs
      121 dddkrkaflq ayvqmrkrie lftnlpfekl driaiqqemq sigtllrekg e
//
LOCUS       WP_176060997             303 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: 3-hydroxyacyl-CoA dehydrogenase family protein
            [Burkholderiaceae].
ACCESSION   WP_176060997
VERSION     WP_176060997.1
KEYWORDS    RefSeq.
SOURCE      Burkholderiaceae
  ORGANISM  Burkholderiaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Burkholderiaceae"
                     /db_xref="taxon:119060"
     Protein         1..303
                     /product="3-hydroxyacyl-CoA dehydrogenase family protein"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006635 - fatty acid beta-oxidation
                     [Evidence IEA]"
                     /calculated_mol_wt=31993
     Region          5..284
                     /region_name="FadB"
                     /note="3-hydroxyacyl-CoA dehydrogenase [Lipid transport
                     and metabolism]; COG1250"
                     /db_xref="CDD:440862"
ORIGIN      
        1 mkavigvvgt glmgvgiatq salhghrtiv hdvdparlas vapkaeavld elidagrids
       61 aakqaalari ethaqldvma saqfvieaip evlelkhrly aalapllasd ailasntsgf
      121 ppdqlvaplr akerfliahf wnpphmiplv evvpgtatap dvtqqtaalm saigmepvvl
      181 akaipgfvgn rlqfavlrea lnivrsgaat advvdrvmka slgrrwgivg plegadmggl
      241 dtfldiashl mpelakdedv ldllrqqvda grvgvrsgag fyewdeahla hvkagrkrli
      301 srg
//
LOCUS       WP_176061087             244 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176061087
VERSION     WP_176061087.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..244
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25555
     Region          14..178
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mhtgtknekr srgrprsydp eqalsdarda fwdggysgts ldalsestgm nrpslygafg
       61 dkhalylstl dryvetglqg meaalggdrp ladalmsvyd galaiylpvg vaprgcflig
      121 talaesrvdq evrdklaagl ntfdasferr lerakaagel dsaanpavla kvasailhsl
      181 alrsragdsh aslratakag valicgmqae pprktvrkpr ggggggvpat saldeapvrr
      241 ksnr
//
LOCUS       WP_176061117             657 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176061117
VERSION     WP_176061117.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..657
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=69385
     Region          311..508
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 miaaafsrva drllaadpgl vrlhnalrva laclltgvag iawtvsyhqp itlaapgilf
       61 amvaplfvrd arrsawcgtl fylylcscac faaasvlsrf plagdagflv vmfvgmlcqa
      121 cgpralgcam lgvvcfylgl ylhpsmqhlv mslllsalgp vmvtlvgrvl vptrvtanfr
      181 lavhtvtlra arllhapgaa nlsslneaal sleeqlalln ppdaetvrer ivevevaagq
      241 hafaagpasg gmqasaevlr haigrlrema qrgragraag lpsrvdvdvr faasaaqrfa
      301 dlraklcwlp atrattaafl amlighslsp erwfwavitt fvvflgtrsr adtvyrgaqr
      361 lvgtlagalv svllvaplhg spgllvaamv vcvfgwayfi lnayapgvff itvlvglvyg
      421 elgfamgpla elrieevlvg clvsfavaml mmplaatrhv earlgavlaa lrevvrvagy
      481 srahghgaad gaaeatsdat ldatsamrkl drswhdlria fkplqtqrvv vwnpdvelat
      541 gsllcclhwa rvlsdssrrg davsegaaln aaevgaahma sivarldsli arysgagsal
      601 gglekpeasv aaldvapdaa palaqldgav aqlfdrltqp vqqtrrmfnw afrsrsv
//
LOCUS       WP_176061203             440 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176061203
VERSION     WP_176061203.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..440
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47222
     Region          16..419
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(28..29,32..33,36,68,118..119,121..123,126,146,
                     149..150,153,251,254..255,258..260,263,291,295,345..346,
                     350,354,370,373..374,377..378,381)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mpsideaatm rkvygrlmpl lfammffnyl drinigfaal dmnkqlgfsp avfgfagsif
       61 ffgymllevp snlllhrvga rrwiarillt wgavavataf vfndssfyvl rfllgvmeag
      121 flpgvavylt kwfpvryrar avggyiiags fsavlggpis talmtyangv lglqgwqwmf
      181 ilegvpamll glvtlrimte rpadanwlsa dekrwleatl aterealggn thfpllrvag
      241 dirvwslacl fgcalvgiyg lflwlpqivk slghlsnlev gflsaappll gvlgtvlisr
      301 ssdrtgdrkk hlafvygmsa laiagsayap spviayallc vtglfiyagn plfwslassf
      361 rtgaagaati alintiaqfg glvgpwsigl vrnatgnfkl alltiaafli vatiialvmr
      421 vtpaedesas lahgdaaprt
//
LOCUS       WP_176061151             489 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176061151
VERSION     WP_176061151.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..489
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=52828
     Region          38..466
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(48..49,52..53,56,90,140..141,143..145,148,168,
                     171..172,175,296,299..300,303..305,308,332,336,390..391,
                     395,399,415,418..419,422..423,426)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 msapptaavh ektaavvetd lpsrldrlpw grfhslivva lgvtwlldgl evtlagavas
       61 alksspslrf snadvglags ayiagavlga lgfgwltdrl grrklffitl alylaataat
      121 alswnlasfl lfrfltgagi ggeytainst iqeftparvr gwtdlgingt fwvgaglgaa
      181 gslvlldphl lpadwgwrac ffigavlala ilpmriwvpe sprwllthgd epdarsiveg
      241 iearfrregh eladhdltrl klrardhtpl revfhtlfnv hrrralvgls lmtaqaffyn
      301 aifftyalvl tdfyqvpgdh igwyllpfal gnflgplllg rlfdvigrrk miaatyglsa
      361 illtisgylf eqhlltvvtq tiawmvifff asaaassayl tvsesfplei ralaiavfya
      421 fgtalggiag paffgrlidt hqrsevfsgy lvgsglmlaa aviaaiwgvd aerkslesva
      481 aplssvvdq
//
LOCUS       WP_176061206             284 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176061206
VERSION     WP_176061206.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12033774
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..284
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31136
     Region          23..155
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          196..277
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mqtsdksepe vvcwrdgald gaclataryg dhkfdrhlhd elvivmtesg agqchtrags
       61 dvagpgsvlv fgpgeyhsge vwegrewiyr aiyldmeglg alsavfspes radspllipp
      121 glyqdrhlag llvkahasld eqravsller qanwwgamgm lvgrygesaq tygearreah
      181 kmaqvreyle anyerdisvd elaelvglsr yyltrafcke fglpphayat qvrllaakrl
      241 latghnaasa aaavgfydqs hlnrlfkray gitpgkyaal kpgh
//
LOCUS       WP_176061220             294 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176061220
VERSION     WP_176061220.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..294
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32072
     Region          31..285
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          203..285
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mtetrdllla lkrlakvdtr ppsllrvaar psmfafvare keriadvflp rpslivvleg
       61 skelvtmgrq lrfaagraiv lpggwrgdvv nvpdqvtgfy ralfldfsea lvlgahrahp
      121 ewqaqtgaqn iearldplli gailhsaegi atqslppvlv dhrimeilli lgtrgvlplr
      181 phasaqstad avralvrwrp dhpwtadlls aelgmsnatl rrklagegqs lrallaeerm
      241 aaassllkea gvsvrdaala sgyqssrrfi erfreiegad pralrdsqpi ddgk
//
LOCUS       WP_176061226             725 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176061226
VERSION     WP_176061226.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..725
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78169
     Region          30..657
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mtpsadadga asprlrdewk aywsddaprl lhivkvamaa tlamglcmrl elrtpgtamv
       61 scvivmmhqq sgmviargfy rglgmvcgsl aglvlialfp qqpllfflal aawigacvfg
      121 asyyrnfqsy gfvlagygta itampawsnp ygvfdnvvft vsevvigvvc asvisaavfp
      181 qrvtpalyas sqrnfthlln alhavlerta avagfdlfld lireragvet lrsgavfedp
      241 sirlhnhlfl dldrsfldtv awihalhqlk arvaaeagpr vlavvdellg dllaivpdlr
      301 qtepvaldqv qtmlarldaf eqalpaqler llrsldgqap qqrqfaattg aalffsiadl
      361 rllcrayvda rvedrqpwsl svfqtlsrig rtratanrta alvagaraai avlavgaawl
      421 asgwvngssa ivavaitsal falvpnpavv swqifggcls gwlagfgfnf fllprfdnfp
      481 llaatiaifv mvgsyvnsfa ktavlglgfs iyfcfivsis nptvynpsay ldtgfallvg
      541 iaaaavafst ivpragdwis aqylkqiral vaesarddel ddllysfels lrdfiiqiaa
      601 apvdprvdrn rligwafaal eigramiqmr ldterlggal psgwpaaqda wlaalaelfc
      661 naapqaaqaa laatrraldv lpithsntvd aamlthcrmr allhfteltl qddtvwlwqt
      721 pgapa
//
LOCUS       WP_176061237             217 aa            linear   BCT 11-JAN-2025
DEFINITION  DsbA family oxidoreductase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176061237
VERSION     WP_176061237.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..217
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=23632
     Region          6..206
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(14,17)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 mqaiqvevhy dficpwcwig qrnlsaalad agigeavsir yvpfelnpsm pvegmerray
       61 rtlkfgswar sqamdaqvta aglsagaafd yervlrtpnt rlahrlmqfa qcrneprtta
      121 alyqaiyaay faegrdigsl dtlvaiaaeh tfdadevray lastagdlkv daareradrr
      181 gvqavptivi ddhaisgaqp pvvftqalra aarrdaa
//
LOCUS       WP_176061280             297 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176061280
VERSION     WP_176061280.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444117
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..297
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32623
     Region          7..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..289
                     /region_name="PBP2_CrgA_like_7"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08476"
                     /db_xref="CDD:176165"
     Site            order(101,105,144,158,160,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176165"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176165"
ORIGIN      
        1 mdnlsgivaf vqtaeassfv aasqrlgvsp savgksvarl eqhlgvrllq rstrrvsltd
       61 dgerfyercr qildalseae smmleanavp rgrlrvslpt igyrfllpil pafaerypei
      121 dleldfndri vdvieggfda airsgnlads qlmakrlgpf rfvlcaspgy lqrrgvplap
      181 adladhaclr frfptsgklq pwafrgqpee taarfptalt cnnmealraa aevglgigym
      241 pdflardalr agrlqsvldd hlsdpgqfsv lwpssrqlsp klrafvdfls ehvfsda
//
LOCUS       WP_176061289             421 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176061289
VERSION     WP_176061289.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Smith,M.M. and Moran,G.R.
  TITLE     Building on a theme: The redox hierarchy of pyridine
            nucleotide-disulfide oxidoreductases
  JOURNAL   Arch Biochem Biophys 755, 109966 (2024)
   PUBMED   38537870
  REMARK    Erratum:[Arch Biochem Biophys. 2024 Sep;759:110081. doi:
            10.1016/j.abb.2024.110081. PMID: 38997848]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..421
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45217
     Region          19..421
                     /region_name="NirB"
                     /note="NAD(P)H-nitrite reductase, large subunit [Energy
                     production and conversion]; COG1251"
                     /db_xref="CDD:440863"
ORIGIN      
        1 mtdaavakaq aahegleapr ttvvigggqa agwvvktlrk egfdgrlvmi adevhlpyer
       61 pplskavlag eadidtvrlv kpddfdalnv eawqpdcass idreqrmvrt qsgrevqydr
      121 lviatggaar rlpdalvkts hiaylrtlde avalgerlra srrvlvvggg wiglevaata
      181 rklgveasvv egaprlcars lppmvsgfll dlhrangvdv rlnaslvkle dhpndanrir
      241 atfadgstld adfavagigl tphtalaeaa gvkvedgivv dhfgatddpr ifacgdvanh
      301 psawlkrrvr leswanaqnq aistakallg hfepyadipw fwsdqydvnl qilgdipada
      361 qlavrgdlpg kratlfhled gairgviain tprelklsrk wmnqgrtidl atltdastal
      421 a
//
LOCUS       WP_176061330             450 aa            linear   BCT 11-JAN-2025
DEFINITION  epoxide hydrolase family protein [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176061330
VERSION     WP_176061330.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Bauer,T.L., Buchholz,P.C.F. and Pleiss,J.
  TITLE     The modular structure of alpha/beta-hydrolases
  JOURNAL   FEBS J 287 (5), 1035-1053 (2020)
   PUBMED   31545554
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Reetz,M.T., Bocola,M., Wang,L.W., Sanchis,J., Cronin,A., Arand,M.,
            Zou,J., Archelas,A., Bottalla,A.L., Naworyta,A. and Mowbray,S.L.
  TITLE     Directed evolution of an enantioselective epoxide hydrolase:
            uncovering the source of enantioselectivity at each evolutionary
            stage
  JOURNAL   J Am Chem Soc 131 (21), 7334-7343 (2009)
   PUBMED   19469578
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12070441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..450
                     /product="epoxide hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48830
     Region          55..158
                     /region_name="EHN"
                     /note="Epoxide hydrolase N terminus; pfam06441"
                     /db_xref="CDD:461913"
     Region          125..>242
                     /region_name="MenH"
                     /note="2-succinyl-6-hydroxy-2,
                     4-cyclohexadiene-1-carboxylate synthase MenH and related
                     esterases, alpha/beta hydrolase fold [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG0596"
                     /db_xref="CDD:440361"
ORIGIN      
        1 mpnttlpesp srrrfvgvaa aavaagslsq lafadgnqsi tdiatppggd ktalrplrih
       61 vpesqlsdlr rrikatrwpd reivnddsqg vplatiqtla qhwatdydwr kceaklnalp
      121 nfvteidgld ihfihvrskh enamplivth gwpgsvieql kiidpltnpt ahgasasdaf
      181 hlvipslpgy gfsgkpttig wgpertaraw vllmkrlgya kfaaqggdlg givanvmakq
      241 appelmgihv nfpatippdi akalqvndpp paslsaderl aydqlsalsr rrayaleqgt
      301 rpqtlyglad spialaswll dhpdgngqpa aaltsavlgr tinghassdv tlndvlddit
      361 lywltntgvs aarfyweshf nfyaaadvsi paavsafpge nyqapkswse rayhnliyyn
      421 rpekgghfaa weqpqifaee vraglrplrt
//
LOCUS       WP_176061337             165 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176061337
VERSION     WP_176061337.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..165
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18509
     Region          6..145
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 msirqkldri dikilaelqk ngnitnanla navglspspc lqrvkrleas gvisgygahi
       61 nlskltstvt vftevmlkdh rredfirfea nvheideite chlvsggydy llkflvgnig
      121 hyqevvekll dlnlgiekyf syivirspfv khaaplerll tddet
//
LOCUS       WP_176061341             292 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176061341
VERSION     WP_176061341.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..292
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=30978
     Region          1..284
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 mdlgfigigv mgqpmalnli ragtpltvwn rsldsveplr algatvaasp advfrrtsvv
       61 ilmlahgdai dsvlgrgtpe feanvarhti lhmgttspey sraldadira aggfyveapv
      121 sgsrkpaeag elvamlagda dvieavrall kpvcretfvc gpvpnallmk lavniflits
      181 mtglveaahf adhhgldmqq fravvdagqm assisrvksl klvdrdftvq asitdvlknn
      241 rliaeaarea kvasplldac yalfgethal gydkddmiav vraleartrs ls
//
LOCUS       WP_176061442             470 aa            linear   BCT 11-JAN-2025
DEFINITION  arylsulfatase [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176061442
VERSION     WP_176061442.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10888284
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..470
                     /product="arylsulfatase"
                     /EC_number="3.1.6.-"
                     /GO_function="GO:0004065 - arylsulfatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008081 - phosphoric diester hydrolase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=53204
     Region          7..444
                     /region_name="ARS_like"
                     /note="uncharacterized arylsulfatase subfamily; cd16142"
                     /db_xref="CDD:293761"
     Site            order(15..16,56,109,111,223,277..278)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293761"
     Site            order(15..16,56,109,111,223,278)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293761"
ORIGIN      
        1 makkkqpnil ilwgddigqs nlsifskgmm gyrtpnidri aeegvlftdy ygeqsctagr
       61 asfitgqcgl rtgltkvglp gaplgmsaed pnipellkpl gyvtgqfgkn hfgdrdehlp
      121 tmhgfdeffg nlyhlnaeee pelpdypdpk efpdfhkkyg prgvlhcwsd gkggqkient
      181 gpltkermkt idteflksak efigkahkdd kpfflwfnts hmhfrthied rirgqagrwq
      241 seyhdcmieh dkhigemlav ldelgiadnt lvmystdngp hmnswpdagm tpfrneknsm
      301 wegayrvpam arwpgvikpg ticneivshl dwlptiveaa gdpdikekll kgheangkkf
      361 knhldgfslv pylsgkaphh arkgffyftd dgdlaclrfd nwkvafmeqr cpgtlriwae
      421 pmvtlrvpki fnlrtdpyer aditsntyyd wmldhvsmvl girsnlasqg
//
LOCUS       WP_176061403             476 aa            linear   BCT 11-JAN-2025
DEFINITION  UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
            [Paraburkholderia sp. BCC1876].
ACCESSION   WP_176061403
VERSION     WP_176061403.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Smith,C.A.
  TITLE     Structure, function and dynamics in the mur family of bacterial
            cell wall ligases
  JOURNAL   J Mol Biol 362 (4), 640-655 (2006)
   PUBMED   16934839
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433680
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         1..476
                     /product="UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-
                     alanine ligase"
                     /EC_number="6.3.2.10"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0047480 -
                     UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0071555 - cell wall organization [Evidence
                     IEA]"
                     /calculated_mol_wt=49524
     Region          8..466
                     /region_name="MurF"
                     /note="UDP-N-acetylmuramyl pentapeptide synthase [Cell
                     wall/membrane/envelope biogenesis]; COG0770"
                     /db_xref="CDD:440533"
ORIGIN      
        1 msqsgnamfs lreaaalipg atvlgddsvt fervstdsrs agpgdlfiai kgerfdahdf
       61 lpqvaarnvt aalvtrtpad wsvpsllvpt dtrvalgala rgwrrrfslp lvavtgsngk
      121 ttvkemiasi faaavgeqnr latagnfnnd iglpltlfrl haghrlavve lgmnhpgets
      181 llaklaeptv avvnnaqreh qefmatveav alehasviht lspegvavfp addayasiwr
      241 vaatgsrimd falnsaervs eaavkgtfdg nvlridtpag hvevtlqvlg nhnahnalaa
      301 tsaalaagvs ldaikrgles fgavkgrlqv kraavgaltg atviddtyna npdsmraaid
      361 vlascasprv lvmgdmgevg dngpafhrei gayakergid alyamgdasr dactaygada
      421 hhvpdvgtlv vqlqqagfgs aatllvkgsr fmqmervvda vtspqpnaag tmpaah
//
LOCUS       WP_176061485             174 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)-dependent oxidoreductase, partial [Paraburkholderia sp.
            BCC1876].
ACCESSION   WP_176061485
VERSION     WP_176061485.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia sp. BCC1876
  ORGANISM  Paraburkholderia sp. BCC1876
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449905
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Paraburkholderia sp. BCC1876"
                     /db_xref="taxon:2676303"
     Protein         <1..>174
                     /product="NAD(P)-dependent oxidoreductase"
                     /EC_number="1.1.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
     Region          1..>174
                     /region_name="MmsB"
                     /note="3-hydroxyisobutyrate dehydrogenase or related
                     beta-hydroxyacid dehydrogenase [Lipid transport and
                     metabolism]; COG2084"
                     /db_xref="CDD:441687"
ORIGIN      
        1 evlaaegasv adtpremagr vetvmlcvld aaavgevvfg ahgllsgepe rrrlsrivdh
       61 ssippaatrd yaaraaqagv awidapvsgg vpgaqagtla vmaggpadev eavrpliaay
      121 asrlthlgea gagqtaklcn qpivtatvap iaeavglaqa sgidaarlse alag
//
LOCUS       WP_176061552             501 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Burkholderia multivorans].
ACCESSION   WP_176061552
VERSION     WP_176061552.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..501
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54206
     Region          72..450
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mtkryvstrm gagiavmvfl agcttfskdg gfntvsstak erlgkdaviv ktdadrdava
       61 krtqdlvgkp lsmddavqva llnnrglqas yaelglsead lvqagrlpnp gftfsrtrag
      121 ngdlsigrmf sanvlsiltl pfaahiegrr feqtkletad amlkvaadar rayinavaae
      181 qaaryaeqvk dsadagaela srmrqagnfs kldyareqaf yadsvaqsak thqqavvare
      241 kltrimglwg astqytlpdr lpdlpkqrpd lkdlesyamq nrldiqaakl qtqsvasslg
      301 lskatrfina ldvgylnnye tdkghehgye isveipifdf gsakvaraea tymrsanqla
      361 qtaidarsev resysayvts ydvakhyrde vvpirktisd elllryngml asvfellads
      421 reqvgavnsy idalkdywla etdlqqavgg hlpqagdkqt skesapqrpa vtsapnstqp
      481 aaqstsapaa qsapamdseg k
//
LOCUS       WP_176061614             885 aa            linear   BCT 11-JAN-2025
DEFINITION  phage tail tape measure protein [Burkholderia multivorans].
ACCESSION   WP_176061614
VERSION     WP_176061614.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11474873
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..885
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..885
                     /product="phage tail tape measure protein"
                     /GO_process="GO:0098003 - viral tail assembly [Evidence
                     IEA]"
                     /calculated_mol_wt=94640
     Region          68..812
                     /region_name="COG5283"
                     /note="Phage-related tail protein [Mobilome: prophages,
                     transposons]"
                     /db_xref="CDD:444094"
ORIGIN      
        1 mdnalklrvv fdmidnmtkp lknalagskg lasslketrr elaemgktqk aiasfrelhg
       61 glastttqld aararvkela gslrtfgpps qqmiaelaka rqvasqlrae qkqqsntlqe
      121 lrtrlagagi dtrnlsqher elraniaatn stmndqmrrl dafnererrv atarksmeri
      181 qgvganmamt gyaakatgmh lfgdlretid eskkaeseem riralglgdh atedakkyar
      241 amnvygvstt dnltmmrdal tifadehhaq mvmptlakmk faneamfgae dahaneekfm
      301 nmlkvielrg gtkdeatfkd eanmvqkvlt atggrvggde wrnfiqtggv aakqlrkdaf
      361 yyqmepliqe mgghavgtgl msaysnvyqg kttvraakqm malglldpkk veynkigmik
      421 qikpgalkgg dmlkasplew lekvllpkma akgitdpdkv kdmistiftn rtaanlfstm
      481 ymqreqihkn erlnagadgi eegnrkgqqm tqgreieala klhdlklaig ekvspiynag
      541 lqataaatsk vialmqkhst aakiiltala alaailvvcg tltialagvl gplavlrfsm
      601 ttlgmqgsil arvlgigasa frmlgsaimf vgramlmnpi glaitaiavg ayliyqywep
      661 ikgffgglwd qvrgafaggi gsvaalivnw splglfyqal agvlswfgid ipakfsefga
      721 nivsglvngi tsglggvrda ivnvasstvg wfkeklgihs psrvfgelgg fisqgaalgm
      781 egeqgriaka avglatvavt afggqgaaat plyvrptlpi dnrpplaatt apapanqsag
      841 gfasiviniy paagadpaai aqavraeldr rerskqarig arlsd
//
LOCUS       WP_176061753             423 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Burkholderia multivorans].
ACCESSION   WP_176061753
VERSION     WP_176061753.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..423
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=45008
     Region          68..299
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mafskvvvgw maacalsaaq agtlpnanad agaagkslah aerfdygdsg lpqvaadlne
       61 rilripadas gtvtleatlf kpdgpgpfpl vvfnhgkntg dlrqqprsrp lafarefvrr
      121 gyaviapnrq gfagsggtyr qegcnveqng laqaadvaat irymsqqsyv dasrivvagt
      181 shgglvsvay gteaapgvrg iinfsgglrq dlcdgwqknl vdafdqygah tavrslwlyg
      241 dndsvwtpal vsqmhdayva hgtqaqfidf grykddahrl ivdrdgvpvw wpavhaflae
      301 lnlptavrya vasphepkat gyasidavda vpyvdeagre gyrrflnqhp srafavsseg
      361 awswaeggdd pmalaldnca kqgagpcrly avndrvvwna ntqtadnddt gahgadtral
      421 asr
//
LOCUS       WP_176061785             161 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia multivorans].
ACCESSION   WP_176061785
VERSION     WP_176061785.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 161)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..161
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17213
     Region          18..148
                     /region_name="NUDIX_ADPRase"
                     /note="ADP-ribose pyrophosphatase; cd04673"
                     /db_xref="CDD:467557"
ORIGIN      
        1 mptssssaad atnnvrvvpa vigvvlrdrd vllvrranpp dagrwgfpgg kieagepiad
       61 avvrelaeet aveveavdvf taldafgrdd dgtlrqhfvm vavlcrwlrg apaagddald
      121 arwfgvdele rrddlpmsag vvdvarrave rasaladrpr r
//
LOCUS       WP_176061802              52 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl carrier protein [Burkholderia multivorans].
ACCESSION   WP_176061802
VERSION     WP_176061802.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 52)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 52)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 52)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..52
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..52
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=5692
     Region          1..>50
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 msrneiyasl keifcdvlgr pnielndatt aqdvdgwdsl khidlimaie as
//
LOCUS       WP_176061830             562 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia multivorans].
ACCESSION   WP_176061830
VERSION     WP_176061830.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..562
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=61345
     Region          10..539
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mstertlege fdyvivgagt agcvlanrlt edpdvrvlll eaggkddyhw ihipvgylyc
       61 ignprtdwly ktqpeaglng ralsyprgrv lggcssingm iymrgqrddy drwaretgda
      121 gwswdsvlpv fkrsedhhav asdahgaggy wrvekqrlrw eilesfaqaa qqtgipatdd
      181 fnrgdntgvg yfevnqkrgv rwntskaflr pamaranltv itgahaqrvi fegrravgve
      241 yrgggteyva rarievllts gavnspqlle lsgigdgrrl qalgievvqd lpgvgenlqd
      301 hlqlrmafrv qgvrtlntls arwwgklmig aeyallqrgp msmapsqlga faksdpddpt
      361 laspdleyhv qplsldrfge plhsfnafta svchlrptsr gsvhvasadp haapviapny
      421 lstdydrhva analrltrri asapalaryr peeilpgpry qteaelqeaa gavgttifhp
      481 vgtcrmgrad dpravvdsrl rvrgiaglri vdasvmpfit sgntnsptlm iaerasdmir
      541 adrraardaa asvhtdavvt pa
//
LOCUS       WP_176061971             279 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein, partial
            [Paraburkholderia phymatum].
ACCESSION   WP_176061971
VERSION     WP_176061971.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia phymatum
  ORGANISM  Paraburkholderia phymatum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Paraburkholderia phymatum"
                     /db_xref="taxon:148447"
     Protein         1..>279
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
     Region          1..>278
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mswldqprtl eivsaglpkw qdeclftvsr ltgteklgrl ydytveiatk ddigltvhea
       61 ramvkvdelv gkqvtvkiat egsgtyetgt igvspsinig agvreitgli vsaqcvgsdt
      121 rrafyrlrir pwlflatlnq dsrifqdltv keisetilkk ypfhyelrla gpgfgrqypk
      181 rdyqrmywes dwgylnrlwq ewgitffydg ptlvlcdsta aykkhgpaya tlqyqdrdgq
      241 rideehvyqf eiaralttgk vsvtdydytq sranlaakd
//
LOCUS       WP_176062006             193 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Clostridioides
            difficile].
ACCESSION   WP_176062006
VERSION     WP_176062006.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..193
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22164
     Region          15..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mprfmeqeke iinskllieg eklfalhglk kvtiddlvaa vniskgsfya fypskehlyv
       61 einfrlqkel ftsiettikk kkyknhrdla kdvimlsltg vitspilsqi dlslmdylqr
      121 kissdifenh mysdirilei ledlgvvflv phtviiksly svlscleqfk edeelnmiqn
      181 llvngiiqqv vae
//
LOCUS       WP_176061941             289 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paraburkholderia phymatum].
ACCESSION   WP_176061941
VERSION     WP_176061941.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia phymatum
  ORGANISM  Paraburkholderia phymatum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 289)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 289)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 289)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Paraburkholderia phymatum"
                     /db_xref="taxon:148447"
     Protein         1..289
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31556
     Region          50..288
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mqtatidpsv rqqqredram lllmapallv vvvllvlpla wlswqsiyhd gaftlvnyrr
       61 iftgtyldtf lmtfklsfiv tgitlllgyp vayfaasvpp kwsalilgmv ilpfwtsvlv
      121 rtyawlvllq rtglvnkall smglidrplq lsynqfgtiv amvhillpfm vlplysamqk
      181 ipanlsqaga slggsplhvf crvflplsms gvvagvtlvf vlclgfyitp elmgggksim
      241 vsmvvsrnve iynswgaasa vsvvllvcvf aifyaasrvi plektlgak
//
LOCUS       WP_176062025            1059 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Clostridioides difficile].
ACCESSION   WP_176062025
VERSION     WP_176062025.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425670
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..1059
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=123489
     Region          1..>178
                     /region_name="SWIM"
                     /note="Uncharacterized protein, contains SWIM-type Zn
                     finger domain [Function unknown]; COG4715"
                     /db_xref="CDD:443750"
     Region          245..601
                     /region_name="SNF2_assoc"
                     /note="Bacterial SNF2 helicase associated; pfam08455"
                     /db_xref="CDD:462483"
     Region          <599..1036
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
ORIGIN      
        1 mkidmiykli rrntepsrws rgvkyytnql vdyidididd lqnnlltfrg gvnsednysf
       61 yfnsitidik hfkiiendcs cadcqskgks ifickhivai vikslkqikn kkdvppilid
      121 ilgadkdkls ntnsktsldl skqllslldn tkrervnldv linvdsnkai aefkigidkm
      181 yilknitefa ysklngyeld fgkkftynpn thyfadedek lvdiieeygt nlsynfsssh
      241 skkfmeinas slkqflnaik ykdftlifsk eeyhpkilnd tlpvrfdfkn iedkivlysk
      301 dslpvpltkk ndvllydgni yllshkkahd yskiyqilsk tkelkfdked skdvlgllvp
      361 rlksisqevh lddniknnit kdfksefyfd midgniccdv kyiyddedkk fvlpniqkea
      421 tienkltssq ftkennhyvf kgtdhdlftf ldlqleslke fgdiyysekf klkkiynass
      481 iqasinqtnq nylefnfnis dinpkeykdi lkafqekrtf yklkdgnfid lseretkdff
      541 elvenldimd ksknnkihkn kalyindvir sknlkfidgk keldsicekf rnfdsinlei
      601 panlnanlrd yqinglnwfk vldyykfggi lademglgkt iqtiafllsl snkkslivtp
      661 tslihnwkne fekfapdikv llihgnkrdr ekcfmklenf dvilttygtl rndldkysei
      721 kfdycildea qniknpvalv tesvksinae nkfaltgtpm ennllelwsi fdfimpgyly
      781 skakfqelfi nkednvknlk klikpfilrr skkqvmkelp dkieknffve lnkeqkkiys
      841 vyskdiqdkm kdknlkkdki vifsyltklr qlcldpsivv kdynkksski etcleilrds
      901 inenhkillf sqftsvlkni skeldkykik yhyidgktna kerlelvdef nnsmdkkvfl
      961 islkaggtgl nltsadmvih fdpwwnpsve nqasdrahrf gqknsvqvik liakgtieek
     1021 iiklqeskke linqfingel snegvlksls deeiinlfn
//
LOCUS       WP_176061543             220 aa            linear   BCT 11-JAN-2025
DEFINITION  LemA family protein [Burkholderia multivorans].
ACCESSION   WP_176061543
VERSION     WP_176061543.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia multivorans
  ORGANISM  Burkholderia multivorans
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Schubbe,S., Kube,M., Scheffel,A., Wawer,C., Heyen,U.,
            Meyerdierks,A., Madkour,M.H., Mayer,F., Reinhardt,R. and Schuler,D.
  TITLE     Characterization of a spontaneous nonmagnetic mutant of
            Magnetospirillum gryphiswaldense reveals a large deletion
            comprising a putative magnetosome island
  JOURNAL   J Bacteriol 185 (19), 5779-5790 (2003)
   PUBMED   13129949
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Lenz,L.L., Dere,B. and Bevan,M.J.
  TITLE     Identification of an H2-M3-restricted Listeria epitope:
            implications for antigen presentation by M3
  JOURNAL   Immunity 5 (1), 63-72 (1996)
   PUBMED   8758895
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004309
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia multivorans"
                     /db_xref="taxon:87883"
     Protein         1..220
                     /product="LemA family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24190
     Region          19..209
                     /region_name="LemA"
                     /note="Magnetosome formation protein MamQ, lipoprotein
                     antigen LemA family [Cell wall/membrane/envelope
                     biogenesis]; COG1704"
                     /db_xref="CDD:441310"
ORIGIN      
        1 msenatiasp rysrvratwa avltsvllnl agcgynviqt edeqvkasws evlnqyqrra
       61 dlvpnlvntv kgyanqerdv ltsvtqaraq vgsiratpel isdpqafakf eaaqgqltst
      121 lsrllvvten ypqlksdanf rdlqvqlegt enritvarnr yirsvqaynt tvrsfpnnlm
      181 akafgyqerp nfsvsneaei skppqvdfgs apasagrvtn
//
LOCUS       WP_176062123             341 aa            linear   BCT 11-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176062123
VERSION     WP_176062123.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..341
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=35751
     Region          2..281
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mrfpgkgmgw kefavafkde ltrdmitdwa gavtysgvma lfpfllflva laslvitpdq
       61 aeqivqqlgq iapanvtqil gdriravasd sktglltvga vvalwsassg vaevqralni
      121 iygvqegrpf wkarglallm tlvagaialv agvvavaagp igdaiggplg taltwlrfpv
      181 agvlmmflwa llyyvlpdve qdfkfitpgs vmgvvlwvia swgfsqyvah fgsydatygs
      241 vggaivmllw mwlsslvlla gaeanavieh kseegkraga krladsgasg tkteveeple
      301 pagafsrgea agraaasarg ralaglaalv gaalwlrrre v
//
LOCUS       WP_176062126             391 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176062126
VERSION     WP_176062126.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..391
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=42803
     Region          1..285
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mpelalvltg ggaraayqvg alravgdlwr gsrspfsiya gvsagainat slasgadefp
       61 vaveqlagvw rtltpdrvyr tdtrrllgis trwfkdlsag gllgsprmny lldteplral
      121 lartlpfsrl sqhfrsgalr gvavsatsyt sglgvtffdg vrelqpwyrs triavrqrlr
      181 lphvlastai piffppvkvr glfygdgcvr mpaplspaih lgadrilaig vqfprpvelp
      241 persraprre flpmseiagv lldaifldal esdlerlerv nrtvafippe qrgtaaqplr
      301 avtclvlrps qdlgtlaadq ytrfprmlry llkgigatge tgaellsyla fepeyvnrlm
      361 elgyadtmrr rvevqaflep ererlasggg p
//
LOCUS       WP_176062128             333 aa            linear   BCT 11-JAN-2025
DEFINITION  HDOD domain-containing protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176062128
VERSION     WP_176062128.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Galperin,M.Y., Natale,D.A., Aravind,L. and Koonin,E.V.
  TITLE     A specialized version of the HD hydrolase domain implicated in
            signal transduction
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 303-305 (1999)
   PUBMED   10943560
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..333
                     /product="HDOD domain-containing protein"
                     /calculated_mol_wt=34801
     Region          67..290
                     /region_name="HDOD"
                     /note="HD-like signal output (HDOD) domain, no enzymatic
                     activity [Signal transduction mechanisms]; COG1639"
                     /db_xref="CDD:441246"
ORIGIN      
        1 mappdagpha eaaageeagg fapfaralgm pepaepapla deeeleeerl aslvrerfae
       61 arpepasfpa ialqilnlaa speaevaela rlvardpals agvlsvansa ayrgvqelet
      121 vrdavarlgl tevgrvaaav sartlfspra raeqvahgar wnalfahava vgsaaaaqal
      181 ghrgansdra ylggllhdvg kslalravag llaegriagl gptrlerlld rvhvelgaea
      241 hqvwslpqyl tvlcvrhhdq avpaeeefvd lhlvrltsal advreplfaa raarevvqsa
      301 galgldpyav ralagevrra eeravltfga par
//
LOCUS       WP_176062129             138 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176062129
VERSION     WP_176062129.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..138
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=14270
     Region          5..125
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mavstilvve ddpdirsalc siledegylv acaadgqeal galraglrpa villdlmmpv
       61 mdgrdfraaq lrdprlaaip vvvltadgrl qqaaqalgaa dafakpfelk vllralervt
      121 aasapacetp apqvaahg
//
LOCUS       WP_176062145             301 aa            linear   BCT 11-JAN-2025
DEFINITION  S1C family serine protease [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176062145
VERSION     WP_176062145.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Liu,X. and Fuentes,E.J.
  TITLE     Emerging Themes in PDZ Domain Signaling: Structure, Function, and
            Inhibition
  JOURNAL   Int Rev Cell Mol Biol 343, 129-218 (2019)
   PUBMED   30712672
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Clausen,T., Southan,C. and Ehrmann,M.
  TITLE     The HtrA family of proteases: implications for protein composition
            and cell fate
  JOURNAL   Mol Cell 10 (3), 443-455 (2002)
   PUBMED   12408815
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Bezprozvanny,I. and Maximov,A.
  TITLE     PDZ domains: More than just a glue
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 787-789 (2001)
   PUBMED   11158544
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Sheng,M. and Sala,C.
  TITLE     PDZ domains and the organization of supramolecular complexes
  JOURNAL   Annu Rev Neurosci 24, 1-29 (2001)
   PUBMED   11283303
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Pallen,M.J. and Wren,B.W.
  TITLE     The HtrA family of serine proteases
  JOURNAL   Mol Microbiol 26 (2), 209-221 (1997)
   PUBMED   9383148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..301
                     /product="S1C family serine protease"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=30554
     Region          30..295
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
ORIGIN      
        1 mtalgalsrd lealvaraap svvgveqrrg hgsgfvlapd gylltnahva rgaeplhvrr
       61 sgseplpaer vgldartdla vlrvpasgla plaladrrpl apgalviaig nplgfersvt
      121 mgvvsalyrt lpapdggald gllqtdaavn pgnsggplls aegevvgvtt amlpwahgma
      181 faipartasw vaavlirdge vrrpylgiaa rgedlapaaa salrrtrgvr vlrveggsaa
      241 eaggvrpgdl laaangddva alddlqrvlv ltpapelald vlrdgaplrl alrpgparra
      301 a
//
LOCUS       WP_176062166             135 aa            linear   BCT 11-JAN-2025
DEFINITION  PilZ domain-containing protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176062166
VERSION     WP_176062166.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Cheang,Q.W., Xin,L., Chea,R.Y.F. and Liang,Z.X.
  TITLE     Emerging paradigms for PilZ domain-mediated C-di-GMP signaling
  JOURNAL   Biochem Soc Trans 47 (1), 381-388 (2019)
   PUBMED   30710060
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Yan,X.F., Xin,L., Yen,J.T., Zeng,Y., Jin,S., Cheang,Q.W.,
            Fong,R.A.C.Y., Chiam,K.H., Liang,Z.X. and Gao,Y.G.
  TITLE     Structural analyses unravel the molecular mechanism of cyclic
            di-GMP regulation of bacterial chemotaxis via a PilZ adaptor
            protein
  JOURNAL   J Biol Chem 293 (1), 100-111 (2018)
   PUBMED   29146598
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10537801
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..135
                     /product="PilZ domain-containing protein"
                     /GO_function="GO:0035438 - cyclic-di-GMP binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14264
     Region          9..106
                     /region_name="PilZ"
                     /note="PilZ domain; pfam07238"
                     /db_xref="CDD:399904"
ORIGIN      
        1 mttvashaer rdfsrialsr paaleigaar tacelvdisl rgalvrtrap lvavggqacr
       61 llvqldqgpa tilmrgeiah argreigvsc reldldsaah lrrlvevnlg sekllerela
      121 alvaragarp aagkr
//
LOCUS       WP_176062219             356 aa            linear   BCT 11-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176062219
VERSION     WP_176062219.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..356
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=36551
     Region          38..308
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 msaltkplal aaallsaaal papasawnrg parvfatlpa gasgpeglev grdgqvyvtt
       61 fgftssgpaa gpgqlyvfdr ngglvrqvsv sgssphllgl rlhpstgall vvdfgagqvl
      121 evdprtgass vfltlpsslp hpggsglndl tfdhagnvyv sdssqgivwt tgpqgglasa
      181 wvdsallrts gvppfgangl rfnhaetklf vantgndtvv qipatsggag pvagapavft
      241 ngingadgli vdeddnlwvv anqadevvvv dptgkaiakl gdfsgiergg apvhllfpas
      301 lrflgddllv tnlsldlrlf dpsfqsvdsq wcaqvsryti vrmhprlrrs agewid
//
LOCUS       WP_176062282             225 aa            linear   BCT 11-JAN-2025
DEFINITION  trimeric intracellular cation channel family protein
            [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176062282
VERSION     WP_176062282.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Su,M., Gao,F., Yuan,Q., Mao,Y., Li,D.L., Guo,Y., Yang,C.,
            Wang,X.H., Bruni,R., Kloss,B., Zhao,H., Zeng,Y., Zhang,F.B.,
            Marks,A.R., Hendrickson,W.A. and Chen,Y.H.
  TITLE     Structural basis for conductance through TRIC cation channels
  JOURNAL   Nat Commun 8, 15103 (2017)
   PUBMED   28524849
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Kasuya,G., Hiraizumi,M., Maturana,A.D., Kumazaki,K., Fujiwara,Y.,
            Liu,K., Nakada-Nakura,Y., Iwata,S., Tsukada,K., Komori,T.,
            Uemura,S., Goto,Y., Nakane,T., Takemoto,M., Kato,H.E.,
            Yamashita,K., Wada,M., Ito,K., Ishitani,R., Hattori,M. and
            Nureki,O.
  TITLE     Crystal structures of the TRIC trimeric intracellular cation
            channel orthologues
  JOURNAL   Cell Res 26 (12), 1288-1301 (2016)
   PUBMED   27909292
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Silverio,A.L. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the trimeric intracellular
            cation-specific channel protein family
  JOURNAL   J Membr Biol 241 (2), 77-101 (2011)
   PUBMED   21519847
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458271
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..225
                     /product="trimeric intracellular cation channel family
                     protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22865
     Region          13..207
                     /region_name="YadS"
                     /note="Uncharacterized membrane protein YeiH [Function
                     unknown]; COG2860"
                     /db_xref="CDD:442107"
ORIGIN      
        1 mtvtrfavdl gvlpvaldlg gtfvfalsga aaavkhrldv fgalvlslva assggivrdv
       61 ligavppaal ddwryvaisl laglvvllrh saverlrnpv qlfdaaglal favagahkal
      121 vfhlgplsaa llgmvsgigg givrdllvte vpavlhaeiy avaalagatv vvvgsrlgip
      181 spvattvgal lcfglrflal rrrwrlpiag eaalpageak rrrga
//
LOCUS       WP_176062300             288 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176062300
VERSION     WP_176062300.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..288
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31324
     Region          35..271
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
ORIGIN      
        1 mpvpaypsss earreegflh ardnlrlywq rytppsprat vavapgggdh agrypgltaa
       61 laragfeval ldfrghgqsd grrwhvdafs dyvgdldvfm ahvragaagr kvflvghsqg
      121 glvatlwala grrevagvvl sspyfklald pprlkvmgar lagalvpwlp vatglrmedl
      181 tsdedmrrwt eadplygrat tprwfaesqr aqrsvlprap tfahpllvlv geadrvadag
      241 aaraffdaag sadkafqryp gfrhelfner eagrpigdav awlrqrag
//
LOCUS       WP_176062424              71 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176062424
VERSION     WP_176062424.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 71)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   2  (residues 1 to 71)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787697
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..71
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=7879
     Region          1..56
                     /region_name="XRE"
                     /note="DNA-binding transcriptional regulator, XRE-family
                     HTH domain [Transcription]; COG1476"
                     /db_xref="CDD:441085"
ORIGIN      
        1 mnnvrvmree qlltkaelar kagisaltla rieggsdcrv dtkrkiilal glrpedkerv
       61 fgarftvrkg r
//
LOCUS       WP_176062440             318 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176062440
VERSION     WP_176062440.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 318)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..318
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34780
     Region          3..226
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 milrteglak tfevgfrrrr vqavrdltls vqegeifgfv gpngagkttt ikmlmglifp
       61 sggrafifda pipstaskar igylpenpay yefltgreal rffarlarvp gadakrrcde
      121 llelvgltpa adrqirkysk gmqqrlgiaq alvadpafvi ldepmsgldp igrkevrdli
      181 lelkrrgktv ffsthilpdv eslcdrvgii mrgqlrdvgr lgellsprvk tvelsamvpe
      241 gargalargr vlaeegervs vafddeasad gavravlaag grlvaltphr etledffmrr
      301 lqegearpea tprrlaap
//
LOCUS       WP_176062443             252 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176062443
VERSION     WP_176062443.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 252)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 252)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..252
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26559
     Region          7..176
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mnairclagl tfresmrqkl avnllifall ligasvvisq vtfgeqyrii adlaltaaql
       61 fgtliavfvg aglvagdvar rtlypviakp isrtqyvvgr ylglvlvltl nlavmagttv
      121 avlavylrgf gflagpllpa laalaaqlav vgaiavffst ftnatlaaif slclafsghf
      181 srdvlaywrg npvlravgfa lphlsaldfk vqvvyqeais gaqlgyally allyatvala
      241 lssaifasrd lr
//
LOCUS       WP_176062636             539 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Serratia marcescens].
ACCESSION   WP_176062636
VERSION     WP_176062636.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..539
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59244
     Region          12..521
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mahsaqspyf vlhqltcqfa dgetlfgpld lafdrqrcgl vgrngvgktq llrliagldq
       61 pgnghvesha alayvaqqpe iaphttlaql lgygevfaal arleqgrpla ddidrlegrw
      121 dlndrlqnaf aaaglpafdp lrsasslsgg ermraslcga llgeadflll deptnhldsa
      181 grawlyqqld qwrggllias hdrqllgrme riveltpgal rsyggnyedy rrqrdteqqa
      241 aradlehare errrtrarqq kehdmsqrrs aqtlrvvdtl niasfervay ksaakeslgt
      301 lrkqhqdrrd sldaavreay qrveeeppvl lalpgsevna nkqvlvlerl qlpfvsappl
      361 dlridgpmrv altgpngcgk stllktllgq ltalsghchc plstayldqt lsqldpglsv
      421 mehlglqdsp laegalrtrl aqlqlgadri alplgslsgg erlkaalaca lwrrqpaqll
      481 lldeptnhld lasslaieta ladfpgamlv vshdedflqa lrpthrlnrq adgwrlqaw
//
LOCUS       WP_176062678              91 aa            linear   BCT 11-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin [Serratia
            marcescens].
ACCESSION   WP_176062678
VERSION     WP_176062678.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 91)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 91)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..91
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=10313
     Region          4..91
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mltvkwtdea ktglytllaf iaernpfaae allqrieesv iplaehpylf rpgrvngtre
       61 mvvhpnyivv yrvlaahiei vsvlharqey p
//
LOCUS       WP_176062742              92 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Serratia marcescens].
ACCESSION   WP_176062742
VERSION     WP_176062742.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 92)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 92)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006425
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..92
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=10397
     Region          8..90
                     /region_name="YidJ"
                     /note="Predicted acetyltransferase, GNAT superfamily
                     [General function prediction only]; COG2388"
                     /db_xref="CDD:441953"
ORIGIN      
        1 mehkiladek rfyindehgk liaeisfvps gdrltiidht wvdeslkgqg vgkklvalvv
       61 ekmraeqrki iplcpfakhe fdttpayqdi ha
//
LOCUS       WP_176062876             287 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176062876
VERSION     WP_176062876.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..287
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30329
     Region          89..282
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 milalalagl atlsaaaepa palellpara rpgdaflvhv rgelaappag avagrdlaff
       61 pgrhgqvava glpvetpagp levtvwaeae rggerqalpl raaldvaape fpsralavqr
      121 efveppppel qrridadraa farafaqpee pplfagafaw prrarvtagy geqrtlngvk
      181 psqhygldla gpagapvgaa ndgrvvlvrd cwasgktvil whgaglytty fhlaraavae
      241 gqrvrrgqkl gevgatgrvs gphlhwgvrv gdlyvdprsv lrlrwpw
//
LOCUS       WP_176062882             672 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent helicase [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176062882
VERSION     WP_176062882.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Dillingham,M.S.
  TITLE     Superfamily I helicases as modular components of DNA-processing
            machines
  JOURNAL   Biochem Soc Trans 39 (2), 413-423 (2011)
   PUBMED   21428912
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415199
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..672
                     /product="ATP-dependent helicase"
                     /EC_number="3.6.4.-"
                     /EC_number="5.6.2.4"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003678 - DNA helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016853 - isomerase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=74387
     Region          4..672
                     /region_name="UvrD"
                     /note="Superfamily I DNA or RNA helicase [Replication,
                     recombination and repair]; COG0210"
                     /db_xref="CDD:439980"
ORIGIN      
        1 mvdlstlnpp qreavttteg pllvlagags gktrviahrv awllvqgvqp ervlavtftn
       61 kaaeemkerv salagppgra vfvstfhsfg lwllqeehra aglprrfgic dagdqaalvk
      121 rcmrevnvdd rafdarrvlf llsaaknalq kgvkvrpegq gddydlvaae vypryqaalr
      181 aqravdfddl ialpvellra haalrakyqe rfryllvdey qdtnccqlel lkllagerkn
      241 vcavgdddqa iygwrgaevk nilrferhfp gakevrleqn yrstgrilac angviaknpq
      301 rkakrlwtsa gegapvkvaa lageeeearh vtdrivrgra egrpwahfav lyrlnaqsrp
      361 ieealreasv pyrvaggpaf fdraevrdll aylkvcvere ddvslarivn vparglgdat
      421 lervhahala hrlplfealr rsaevpdlpr gaaermlafv dlidryafaf drqpigevar
      481 rlvaevdlha haragvksae aaqrkveaie svlrsiegwa srtgkkptlp nylaklalds
      541 redededaed gvalmslhaa kglefpvvfl igmeedllpc sgiqgeardl eeerrlayvg
      601 itrareelhl traqartkrg kleprtpsrf lqdlpeaafv lydpakdvqp pevvaarsae
      661 vlaalkarfa rg
//
LOCUS       WP_176062951             339 aa            linear   BCT 11-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Serratia
            marcescens].
ACCESSION   WP_176062951
VERSION     WP_176062951.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..339
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=35983
     Region          1..329
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mieieglhkv yrapdgrrie vlkgvslqvp agsitavvgp sgagkstlak cisllerpss
       61 gsirvngqdl srlagealrr erraigtvfq ssallqrkta wqnvalplty lgvvprdidk
      121 rvksllaavg ladkaafypa qlsggqrqrv giaralalnp svlladeats gldpdatgai
      181 lsllkqlrdr yglsiilith emdavrdaad avaeirdgvi vqqgpvrell aapdsslgrr
      241 lfplktlasd aalrlqvtyc arqpaatdwi srisrqldlq idllgghvev vggslagrle
      301 iavrfgggsr svaelqdelr rlgilaevle qpaalkeav
//
LOCUS       WP_176063023             484 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176063023
VERSION     WP_176063023.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..484
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50413
     Region          28..474
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(28..29,32..33,36,68,122..123,125..127,130,150,
                     153..154,157,282,285..286,289..291,294,321,325,379..380,
                     384,388,404,407..408,411..412,415)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msapgtssvs fqgndrlllg iilgvltfwl faqttlniap dmsrelgtda svmniavait
       61 alfsgifivv mggladrvgr lkivklgfal smvgsllvgl apsgrlavps llagralqgl
      121 sgacimpasl alvkaywdga arqraislws igswggsgvc slfgglvtqh lgwryiffas
      181 vaaaavglvl lrgtpesrae trgeyrfdws gvlafmvamv avqvvvtqgn rlgwsspasl
      241 almatavvfg wlffrieaka pnafidfglf rnstytgatl snfllnavag tlivslqlvq
      301 iggnmsaqqa gvltlgyaia iiafirvgek llrrfgarrp mlwgclitga sillltpanv
      361 mladyevmav igytlfgvgl afyatpstda alsnlpaaqs gsgsgiykma sslgaafgva
      421 isaaiftalg anprsvhwle gvitfqgrqd nlavrgaaii algfnilmvv vaivsvmltv
      481 pkgr
//
LOCUS       WP_176063047             430 aa            linear   BCT 11-JAN-2025
DEFINITION  dicarboxylate/amino acid:cation symporter [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176063047
VERSION     WP_176063047.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Grewer,C., Gameiro,A. and Rauen,T.
  TITLE     SLC1 glutamate transporters
  JOURNAL   Pflugers Arch 466 (1), 3-24 (2014)
   PUBMED   24240778
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Kanai,Y., Clemencon,B., Simonin,A., Leuenberger,M., Lochner,M.,
            Weisstanner,M. and Hediger,M.A.
  TITLE     The SLC1 high-affinity glutamate and neutral amino acid transporter
            family
  JOURNAL   Mol Aspects Med 34 (2-3), 108-120 (2013)
   PUBMED   23506861
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Gesemann,M., Lesslauer,A., Maurer,C.M., Schonthaler,H.B. and
            Neuhauss,S.C.
  TITLE     Phylogenetic analysis of the vertebrate excitatory/neutral amino
            acid transporter (SLC1/EAAT) family reveals lineage specific
            subfamilies
  JOURNAL   BMC Evol Biol 10, 117 (2010)
   PUBMED   20429920
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Kanai,Y. and Hediger,M.A.
  TITLE     The glutamate/neutral amino acid transporter family SLC1:
            molecular, physiological and pharmacological aspects
  JOURNAL   Pflugers Arch 447 (5), 469-479 (2004)
   PUBMED   14530974
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003465
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..430
                     /product="dicarboxylate/amino acid:cation symporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /calculated_mol_wt=44044
     Region          12..404
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
ORIGIN      
        1 mappqaaarr gfrisptqqi mlglvagvlv gwlfpsagva lkpvgqlflr likmivgplv
       61 lttliagiag aggkmvgrvg lkailwfeaa ttlalvvglt ganlvqpgvg vglatdagaa
      121 gklakakgav dfvleafpvs ifdalarndi lqivvfalfv glaigaagek aaavkglaes
      181 gaevmfkvvg fvmrfaplgv gaamaatlga kgirvlipll kvvgtlygcl avffallfla
      241 mwlltrlhlr tflaairepa viaftttsse aamprameam erigvprsiv afvmpagysf
      301 nldgstlyls lavmfvaqaa glhlplgeql aimgvlmltt kgvagvprss lvvlagalta
      361 fhlplegvai llaidelmdm grscvnvvgn cvatavvahw ekaiapgali lgpgrlavae
      421 vperrsavge
//
LOCUS       WP_176063074             144 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176063074
VERSION     WP_176063074.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..144
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15755
     Region          7..142
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mtdwemilcg vdfspasqha lelamdltrr hrcqltiahv yepptasatd vlvappelfd
       61 qavreaerel erlraqaaaa tdrpvrseil mgrpaetlvq warehpcdli vvathgrsgl
      121 krlvlgsvae kvvraapcsv lvar
//
LOCUS       WP_176063100             316 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Serratia
            marcescens].
ACCESSION   WP_176063100
VERSION     WP_176063100.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..316
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=32779
     Region          1..316
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mdtlvqqtvn glmlgsiyal ialgytmvyg ilriinfahg dvlmvgalsa lsainvlqhh
       61 fpalspyatl llaalfamav caitsmaier layrrlrnap rlaplisgig vslllqtlam
      121 liwsrnplmf pqllpmapia ltagsaehap avitgtaivt lavavavmag lwllvehsrf
      181 gramrataen pqvaglmgis pdriivltfa lggalaavag immasnygna gfsmgflpgi
      241 kaftaavlgg ignlrgamlg glllglfesl gtgylgeltg gvfgsnyqdv faflvliavl
      301 vfrpsgllge riatra
//
LOCUS       WP_176063108             498 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Serratia marcescens].
ACCESSION   WP_176063108
VERSION     WP_176063108.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 498)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10411583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..498
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53830
     Region          106..>331
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
     Region          405..493
                     /region_name="Abhydrolase_4"
                     /note="TAP-like protein; pfam08386"
                     /db_xref="CDD:429964"
ORIGIN      
        1 msvlrilall aataaalpaq akpalhgaaa gngirwqscl nsgfqrwfde apppglrcgy
       61 levplayatp paqtvpageq tvrlaltllp atgpkkgsvv tisggpglpg inpylgndah
      121 varlrksydi igydprgvgq stpkiscqva egdelpepdd ndvagaenqt raliaacikq
      181 tgadvlqhig tdeavddlna irhalgepgl tavaysygtk vaalyaerfp kktralvldg
      241 vvdlaeddft qrmnqergfq qsflrfaayc gktdscqlgg ganqalqryh allrklhdqp
      301 fvtaagyeis addvltvtrs lllwperwhe latvlrqlda giagqqvsdl idesyspdad
      361 dalnvitcad vanptadpqq lrrqrqeint aalyahylpl heyplemcdl wpyrgkdrph
      421 tpvasaalpp llfvaqrydp ttpyrnaqam aaafksplit rerdghtlal ngidscvdes
      481 vvdyllapkk prrdkicr
//
LOCUS       WP_176063124             686 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Serratia marcescens].
ACCESSION   WP_176063124
VERSION     WP_176063124.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..686
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=75181
     Region          6..686
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mfpvlaiaaa pgakteesit vtataqpigs ysadtastag ktaapiaevp qsvsvvtsqv
       61 iddfqvksvn damkfvsgvt qgntlggted gfvkrgfgvn sdgsvfidgv rsnqglsmda
      121 ttdrvevlkg sasllygils pggvinlisk kpqydwntri sgatnsvggg sgsvdvtgpl
      181 gggfafrlia erqhadywrn fgsdehtlva pslswfgdqa sfniayseyk ydipydrgta
      241 fidgkpvdvp ynrrlddyan hawgkskrln ahyeyaldpi wttrfnyawl qrrydsnevr
      301 atavdtttgi vsrradanrg fnhqthyysw dltgspqlfg mqhdlllgvd yeknqtykay
      361 syrgkvsktf nmydpvyget pvtdsttysd assnlratlf srslyakdsi hltdqwiavl
      421 garyqsyyqn nsngfqkpkn tlndkddqfl pqaglvyklt pslslygnys rsftpstaid
      481 dngdvatpet gttyevggkw qitpafdatl alyridesnm sifingvtrs ipkarstgve
      541 lelngevarn wdltanysyd kteivednln ldnvgnrlvn aptnmgglyl shrmtlpvvp
      601 gevrigggar yvgrragdpe nsftmpaytv adafvawdsk llgkhtqlkl nvknlfnrey
      661 yassagnlrv iegeprslsl qatvdf
//
LOCUS       WP_176063160             136 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176063160
VERSION     WP_176063160.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004485
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..136
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=14406
     Region          9..133
                     /region_name="YhfA"
                     /note="Uncharacterized OsmC-related protein [General
                     function prediction only]; COG1765"
                     /db_xref="CDD:441371"
ORIGIN      
        1 magaseivvt lpggrrvdaq vgahvvhtdq pvsnggedaa ptpfqlflas lgtcagifvq
       61 gfcasrklsp egiriverpe ldpetgvlrs velrievpas fpekyrealv rvadqcsvkr
      121 aiqaqptfrv etvvap
//
LOCUS       WP_176063170             137 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176063170
VERSION     WP_176063170.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..137
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=14960
     Region          4..122
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mgeprhrvli iddeellirs farilgrdhd italssaaea lrraasgetw dvilcdlqmp
       61 vvdgveffer lnrsrpdlia rvafvtggaf tprarsfler ntrptaqkpv epeglrslvr
      121 qiaagyaaaa gcafars
//
LOCUS       WP_176063189             591 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54-dependent Fis family transcriptional regulator [Serratia
            marcescens].
ACCESSION   WP_176063189
VERSION     WP_176063189.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Peng,Q., Zhao,X., Wen,J., Huang,M., Zhang,J. and Song,F.
  TITLE     Transcription in the acetoin catabolic pathway is regulated by AcoR
            and CcpA in Bacillus thuringiensis
  JOURNAL   Microbiol Res 235, 126438 (2020)
   PUBMED   32088504
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Ali,N.O., Bignon,J., Rapoport,G. and Debarbouille,M.
  TITLE     Regulation of the acetoin catabolic pathway is controlled by sigma
            L in Bacillus subtilis
  JOURNAL   J Bacteriol 183 (8), 2497-2504 (2001)
   PUBMED   11274109
REFERENCE   3  (residues 1 to 591)
  AUTHORS   Shingler,V.
  TITLE     Signal sensing by sigma 54-dependent regulators: derepression as a
            control mechanism
  JOURNAL   Mol Microbiol 19 (3), 409-416 (1996)
   PUBMED   8830233
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461735
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..591
                     /product="sigma-54-dependent Fis family transcriptional
                     regulator"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=65157
     Region          2..585
                     /region_name="AcoR"
                     /note="Transcriptional regulator DhaR of acetoin/glycerol
                     metabolism [Transcription]; COG3284"
                     /db_xref="CDD:442514"
ORIGIN      
        1 mlsddrlpae gasvltqpla eswqrsqgyg ltrtdqhipf ikaglleelr srndwvpqrv
       61 qplieqlgaq itrqpaivvi adagglvlet rgntdflhka srfalapgnq wgeaergtna
      121 igtalalgaf cevrggqhfl nqnaglncta apiyrpdgri agildlsapa qrpyrdaqrl
      181 imqavrhieh rwvrsaiadr hwtlrlhada rclgsaqell lvfhdevlia anrlammefr
      241 lssasfgsve ftqlfpdllr qpsgaphqtl agnqqhyysl leapqrrvsa lrsappaerh
      301 deqhqkalri lnaglslcvt getgcgkehf srslfqesrw rngnfvainc aalpeplies
      361 elfgyapgaf tganpkgyig kireadggvl fldeigdmpa glqtrllrvl qektvtplgs
      421 rsaypvefal vcathhdlhr qveagafred llyriqeysl ripplreraq leafilqlwr
      481 elggerrdir llpealamla rypwpgnvrq llstlkvlla laddhavltl ddlpqsiavl
      541 aprqenadtd qgalqaaidr aggnlsraak algvsrstly rklgrqktaa e
//
LOCUS       WP_176063195             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Serratia marcescens].
ACCESSION   WP_176063195
VERSION     WP_176063195.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34489
     Region          12..71
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          100..297
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(110,114,153,167,169,232,249,276)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(111..112,116..117,119..120,123,127,129..135,196,
                     226..230,237..238,241)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mnkinlpngd ritllhtlvr ivesgslsaa aqqlgtsqpt isrrlqaleq llgakliqrt
       61 thalkltedg ercyrqargl ieqwqsleeg lggardepvg vlrvraphaf gqdqligplg
      121 eylrrypqty vewtlndhsp dfipegvdca ihvgavtdps vvavllaevp rstvaspall
      181 aerpaivdld dlaslpwlav nsfyrnevvl thatsgeqrr fdiaprlstd slyaarkaal
      241 eglgvaivss wvvkeelaqg alqtllplwr aeplpiylly pyasyyparl rkfmemmket
      301 mprilgaqpp tgr
//
LOCUS       WP_176063205             356 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176063205
VERSION     WP_176063205.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..356
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=37411
     Region          <86..355
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mfsrryavfg aifgilfpvl gtlieavthf qnepfgsall laqgepllwv idfaplvlcv
       61 maaitgrrqd dvialeaarr erfektagel fgsaqtllsa vssfssmtvq taasvretta
      121 tmgqlghtat qaaltaetvv glaqkskras degltavers taelakisee vrglsqriqa
      181 ldkrmrdvfe iasvvgsiad rsqqmveave reakrlgseg dslaavvkqm rnhsddvkra
      241 agqvktilie mhkavmtava aadvgvrrae qgaevasstg aairklagal eessgaakai
      301 asvaqqqdhg ieevlkamne iyaateaaia stqsvavqar slndlasglk savgra
//
LOCUS       WP_176063289             233 aa            linear   BCT 11-JAN-2025
DEFINITION  rhomboid family intramembrane serine protease [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176063289
VERSION     WP_176063289.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Brooks,C.L. and Lemieux,M.J.
  TITLE     Untangling structure-function relationships in the rhomboid family
            of intramembrane proteases
  JOURNAL   Biochim Biophys Acta 1828 (12), 2862-2872 (2013)
   PUBMED   24099005
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Urban,S. and Dickey,S.W.
  TITLE     The rhomboid protease family: a decade of progress on function and
            mechanism
  JOURNAL   Genome Biol 12 (10), 231 (2011)
   PUBMED   22035660
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Urban,S., Lee,J.R. and Freeman,M.
  TITLE     Drosophila rhomboid-1 defines a family of putative intramembrane
            serine proteases
  JOURNAL   Cell 107 (2), 173-182 (2001)
   PUBMED   11672525
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002186
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..233
                     /product="rhomboid family intramembrane serine protease"
                     /EC_number="3.4.21.-"
                     /EC_number="3.4.21.105"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=24677
     Region          12..223
                     /region_name="GlpG"
                     /note="Membrane-associated serine protease, rhomboid
                     family [Posttranslational modification, protein turnover,
                     chaperones]; COG0705"
                     /db_xref="CDD:440469"
ORIGIN      
        1 miplkddvpv rrppvvtial iggnvaaflw qiavvglpls vqvggaipye ilslrdvppa
       61 dlvpppftvl tsmflhggfm hiagnmlflw ifgnnvedvl grfrfllfyl acgvaaalaq
      121 vgvaaaagde asllvpmvga sgaiagvlaa ymilfprarv ltlvpififi rliyvpavff
      181 iglwfvlqll safmgdqgsg vafaahvggf vtgfvlvktl aprtgwtvsr rgw
//
LOCUS       WP_176063303             426 aa            linear   BCT 11-JAN-2025
DEFINITION  HdeD family acid-resistance protein [Serratia marcescens].
ACCESSION   WP_176063303
VERSION     WP_176063303.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..426
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=47547
     Region          10..181
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mirliilllg aqalhgqrrl lvlfgwlwia agalmlfdil qdgrsmlald alaiilaleg
       61 lvaisaalvi gssasrpvll kglgfvfmaf ltldvpaddn ivatvvfgsa llldgavria
      121 sstviqhsrw kgvalaggge illslmifvg wpaphrmtvp fclgvmmvls gwallriarr
      181 ltsfslnqhp vrqppppede tapltvyvwt pigaakdprr ryivdryiaa vdgggnistg
      241 haalvlapdv yishyplndi shsvqdfrql lhageqnnvd grflpdlpge iaawcppdkk
      301 iqfyrynpaa lrafwlryrq datynltrrn csttvigald salegvlgdk hlwrrflllv
      361 ldpnlwmlav lrsrgesmtw tpglvldyar mlqqvterqh qrwwlklrem wtilrfgksh
      421 trrqrf
//
LOCUS       WP_176063309             111 aa            linear   BCT 11-JAN-2025
DEFINITION  STAS domain-containing protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176063309
VERSION     WP_176063309.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10604251
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..111
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=12240
     Region          18..91
                     /region_name="STAS_2"
                     /note="STAS domain; pfam13466"
                     /db_xref="CDD:433231"
ORIGIN      
        1 madcnisrer dgervlyrms gvfdrigawa lrekleveta advlldfslv rdfsdlgvav
       61 vahalhetpr rvrfrglrqh qlrifrycgl siddgarasp ataaapaael s
//
LOCUS       WP_176063318             806 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Serratia marcescens].
ACCESSION   WP_176063318
VERSION     WP_176063318.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 806)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 806)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 806)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 806)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..806
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=87252
     Region          17..806
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mlsmaaggwl pfalgddlpp ppsaismpdt tlylepvvng rqtgnvvpvn yrgghyymtp
       61 qqlldaglpv adkqakeiav drlekvdvsy sgesqqllin vpndwlpqqt igarsplqrl
      121 paqsslgllf nydiyasqsn gngrpgylsa wseqrlfdgf gvvantgiyr sgfnggpndd
      181 ggryirydsy wrfnddqrml sviagdlttg slpwssavri gglqlarnfa vrpdlitypl
      241 pqfsgqaalp ssvdlyinsy knsttninpg pftlnsvpyi ngagqatvvt tdalgrqvst
      301 tvpfyvasnl lqtgmsdfsi stgllrrnyg lnsadygqwv gsaslrygvt dwltlegrae
      361 gaaelavggg gadirigqwg vfnasysvsq agdeafnggr piqsptyydp ltgrplqqpd
      421 pqpvyrytgn hgdqssfgyt ysnsrfslna qrilrsadfg disvyksdyr lsrrtdqltg
      481 svslgrlgsl gagyfdvrda iaqrtrlvnl sysvslwrns slyaslnrei gssgysaqlq
      541 lsipfdswgt asfsaardnn nrwservshs raaptdggfg wnlayannps ggdyrqadlt
      601 wrtrrleara gvygtrdetn hwgeisgslv amnggvyatn tindafalvs tqgyadipvs
      661 yenqpigktd aqgyllvptv tsyyhakfqi dplslpadva lptvektvai rdhsgflvef
      721 piqpisaadv elvdeqgkpl angsqvavvg grqqsyvgwd gmtyidpvqq hnrlsvipad
      781 ggppcqaefs lakpqgiqrv gpvvcr
//
LOCUS       WP_176063363             131 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Serratia marcescens].
ACCESSION   WP_176063363
VERSION     WP_176063363.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..131
                     /product="RidA family protein"
                     /calculated_mol_wt=14335
     Region          21..130
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mkngithyhh gviweeengv sqgvrvkdtl yisgqfshdm qgeffgagdi erqtqqtldn
       61 ldrvlagfga ersnlayvei yltdvqahve pcialfkryv gdhrpagsli gvtglaspeq
      121 lveisaiahl n
//
LOCUS       WP_176063367             133 aa            linear   BCT 11-JAN-2025
DEFINITION  Fur family transcriptional regulator [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176063367
VERSION     WP_176063367.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Troxell,B. and Hassan,H.M.
  TITLE     Transcriptional regulation by Ferric Uptake Regulator (Fur) in
            pathogenic bacteria
  JOURNAL   Front Cell Infect Microbiol 3, 59 (2013)
   PUBMED   24106689
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Lee,J.W. and Helmann,J.D.
  TITLE     Functional specialization within the Fur family of
            metalloregulators
  JOURNAL   Biometals 20 (3-4), 485-499 (2007)
   PUBMED   17216355
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002362
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..133
                     /product="Fur family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15155
     Region          1..130
                     /region_name="Fur"
                     /note="Fe2+ or Zn2+ uptake regulation protein Fur/Zur
                     [Inorganic ion transport and metabolism]; COG0735"
                     /db_xref="CDD:440498"
ORIGIN      
        1 mdreaivrtl tergiqpspq rlavaeyvlg akdhpsadrv fevvrgrtpv isratvyntl
       61 nllvreqllq qlvlaegrvv fdphlerhhh fvddatgeih dvpwdalevr hvealrgvdv
      121 reyqvvlrgr wgr
//
LOCUS       WP_176063390             517 aa            linear   BCT 11-JAN-2025
DEFINITION  peptide MFS transporter [Serratia marcescens].
ACCESSION   WP_176063390
VERSION     WP_176063390.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..517
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55807
     Region          6..504
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mqssvnkses rtffghpypl gslfftemwe rfsfygirpl lilfmaatvy dgglglaren
       61 asaivgifag smylaalpgg wladnwlgqr kavwygsili alghlsials avmgtnlffi
      121 glmfivlgsg lfktcisvmv gtlykkgdar rdggfslfym ginigsfiap lisgwliksh
      181 gwhwgfgigg igmlvalvif rvfavpamkr ydrevgldst wnspvakkeg vgvwllalaa
      241 ilvavivlia qgtivinpve vasvlvyvia asvtlyfiyl fafaglsrke rarllvcfil
      301 lisaaffwsa feqkptsfnl fandytnrmi gdfeipavwf qsinalfiil lapvfswawp
      361 alarnnvrps sitkfvigil caaggfglmm laaqnvlsng gagvspmwlv gsilmltlge
      421 lclspiglat mtllapermr gqmmglwfca salgnlaagl igghvkadql dmlpnlfarc
      481 svallicaav livlivpirr mlentqsksa qkpatna
//
LOCUS       WP_176063404             169 aa            linear   BCT 11-JAN-2025
DEFINITION  DedA family protein [Serratia marcescens].
ACCESSION   WP_176063404
VERSION     WP_176063404.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..169
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=18006
     Region          38..>164
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mdelthiiak yspepgmlll liflfalgks vivvssalpp asvtllmgiv agkhalpfga
       61 vwaaialgaa lgsilsfhcg arlhgrdlgr rlparfhapl rkaqrslqkr glpllfasrf
      121 lavmrytvpl magmlqlpar cvyataalsa gvwalllmsa ahlfprflt
//
LOCUS       WP_176063412             830 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Serratia marcescens].
ACCESSION   WP_176063412
VERSION     WP_176063412.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 830)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 830)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 830)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 830)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..830
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..830
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=91030
     Region          8..815
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mklnkkvlsl ltassfllpd tawavtfdts llagesrdsd lsrfylnndm pagrqeidvy
       61 vnhdwkgrya llfgtqrddi qigyqdaqrl gidlsqlptp qapqttlsia slvqggrfdm
      121 dvgalslrlt vpqarinrse agyvdpafws rgisaltlay natyyhaear gegnrsnndd
      181 fytglesgin lagwqfrdss sfrhgsgrgs hwqnntrylq rgfadiksnl tagdfyspge
      241 lfdsvrirgv alasdismrp nsqqgfspiv rgvaqsnalv kvvqngnviy qenvppgaft
      301 ldsiqptgsa gdlwvtvkea dgreqsfsvp fsavpnmlkq gvsqysvlag kvnenntdyd
      361 pgfvqgtlqy gfnnlvtgya gsilsddyqa wllgsgwnlp igavsidlth adtrlknrre
      421 sgqsfriays kfldvtatnf tlaayrystr gyysftdaiy sndgyrqler qvdrwrdeeg
      481 vseldmntwd alrsarpknt ftlnlnqrln egwgtlffsg sqrdywtana ksreyqlgys
      541 nnlgrvsysv sasrvrnsqr eeetryylsf slplsvfdnn aylstglsat dshyqqstvs
      601 lsgnalesnr lsyslsgsnr sggdnmasvn aayrarastl gvsysegddy rqsglsargs
      661 lvaipwhlla sneigntmtv veapqaeglm vngdesivtn aqglalvpya tpyrqnsvtl
      721 sdtghssgae isgnvanhvp yygavsylkf etdqrrpfql ralradgapl pfgaevmden
      781 arpvgfvgqa svlylraeqp ptaltvqlrd gscriakptl aldaspgvcr
//
LOCUS       WP_176063423             694 aa            linear   BCT 11-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176063423
VERSION     WP_176063423.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..694
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=69207
     Region          35..86
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(52..53,56,59,83,86,114..115,118,121..122,125,
                     145..146,149,152..153,176..177,180,183..184)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          83..209
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          96..126
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          131..153
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          158..185
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          317..>405
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
ORIGIN      
        1 msgpadgssd pgaerveeer ryravleldv eapetlarlf ealadpswrv raavverlgg
       61 veparklpgl vvaltadlav gsrnsaaaal eqlgaaavpa llpelerpaa elrtavleil
      121 grigdrrtta alarcladpd pnaraaaaea lgkvggadav aalhgtlggg dlplrraald
      181 alvqlrappa apvlaelmsd rgsrraalrl agasaepaal allaaglddp sravreaalt
      241 giglqrlrpe tpveltaala aavqaaavra pelaaaaaeh leaaeplvra gaiavlqwta
      301 aaehaaalaa agedeqlrpl avealaelgp raaaglagal galtpgarvl alsalarqgd
      361 aralpelipa lgshdaalrg aalealgqlg dpraagpmaa llaedplvaa aavaglsela
      421 ergeaaraav leacraagpr paayrllgrl geardvvtlr eglrgrhrgt rvaaagalaa
      481 lgartalvga evpelldald dadaavraaa aqaigalagg pgaapagpea pawgeatral
      541 aaalrdeegv vramaalalg rcraaeyaph laalaidpqa paeaaaaalh alaemgaadp
      601 gvlanalahp daevvkeavr aaaavpgaav tgmllaaash rrwdvrraaa aalgaraepg
      661 laepvrrlaq aeqdplvaeg lraalrrlea raar
//
LOCUS       WP_176063444             353 aa            linear   BCT 11-JAN-2025
DEFINITION  PhoH family protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176063444
VERSION     WP_176063444.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Kazakov,A.E., Vassieva,O., Gelfand,M.S., Osterman,A. and
            Overbeek,R.
  TITLE     Bioinformatics classification and functional analysis of PhoH
            homologs
  JOURNAL   In Silico Biol 3 (1-2), 3-15 (2003)
   PUBMED   12762842
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..353
                     /product="PhoH family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=38504
     Region          7..330
                     /region_name="PhoH"
                     /note="Phosphate starvation-inducible protein PhoH,
                     predicted ATPase [Signal transduction mechanisms];
                     COG1702"
                     /db_xref="CDD:441308"
ORIGIN      
        1 msqpataqqk ttriefddnd rvralcgahn ehlklierrl gvqvgsrggq lvvsgaseer
       61 vaqaeallre lyeliasgyp lyledvdqat klsgqgvalk eifgdtvyvs arhrvitpkg
      121 lgqkryiqai rdndivfgig pagtgktyla mamavsalie rkvkrivlcr paveageklg
      181 flpgdiaekv npylrplhda lfdmvdyeka safiergtve vaplafmrgr tlndafvild
      241 eaqnttseqm kmfltrlgyg skavvtgdvt qvdlpsgras gllevqkvlr giegiafcaf
      301 sevdvvrhpl vqevvraydl fdaerkaqke qreqeraara alragaeasd dgg
//
LOCUS       WP_176063506             474 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Serratia marcescens].
ACCESSION   WP_176063506
VERSION     WP_176063506.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..474
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49570
     Region          23..461
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(25..26,29..30,33,65,115..116,118..120,123,143,
                     146..147,150,280,283..284,287..289,292,320,324,379..380,
                     384,388,404,407..408,411..412,415)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mehslsgerr glpglpvlll ggfvtvfdlf vvnvaapviq qqfaadfagi glivagyela
       61 fgvlliaggr lgdrfgrrrl fslgmlgftl ssllcglags lslliaaril qgaaaallfp
      121 qiyalmrvly apqqrrrafa wlgmtlglaa ifgqilggfi ieanlfgsgw rmiflinlpi
      181 galalwaarr ipesrvaqaq rldgvglwla aaglsllllp llegpargwp wwiapmlala
      241 lltlwgflrw errlaqrgdd avldpalfrq agfapgmavv laiyatassf flcfalllqa
      301 gagltpfqag slfapasaaf mlasmlaprl tlrwgngvls agvaiyaagl allmaqalwg
      361 galahplrll pglvvlgfgq alsmtpllnl vlglaperqa gmaaglvatv qqvggalgiv
      421 vsgvgfvpll asggaaerya qafagamlcn lvamgvalll lnritrntqk adlk
//
LOCUS       WP_176063519             259 aa            linear   BCT 11-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein
            [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176063519
VERSION     WP_176063519.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..259
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27846
     Region          1..236
                     /region_name="ElsH"
                     /note="Metal-dependent hydrolase,
                     endonuclease/exonuclease/phosphatase family [General
                     function prediction only]; COG3568"
                     /db_xref="CDD:442789"
ORIGIN      
        1 mrvlswnihg mrgrdgradp ervalvieet radvaglqev galggpgell dpagtlarlt
       61 glaqafglte lrggypygnc ilsrhpiaat rsydlsvprr ekrgclradv dlgagalhvf
      121 nvhlgldrre rrrqaaqlls adilrdtala yplvllgdfn awssrsavpr wirrqladaa
      181 laagspratf psafplvrld rayvgsavrv lgcsvhdtrl arlasdhlpv vvdlelapaa
      241 rrppparpva tqgvttevr
//
LOCUS       WP_176063541             310 aa            linear   BCT 11-JAN-2025
DEFINITION  AEC family transporter [Serratia marcescens].
ACCESSION   WP_176063541
VERSION     WP_176063541.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..310
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32284
     Region          1..304
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mtttlfslip vifliamgft lrhknlidra fwlpceklny fylfpalmfi qvgkadlsqf
       61 pvrpialsvl gavligalsl ylwriwlkqp gpvfssviqg alrpntyigv aaaaatfght
      121 gltvtsisia vaipllnvas iailmhygqg trpggkqiak algknpvils vlaglafnas
      181 gwslgaalen iltilggasl plgllavgag ldiqaartaq gpvlqssfvk lllvplltlg
      241 igitlgisgp vlativlfna lpctpsayim arllggdhrl sagiitiqtl laavtipvil
      301 lltqfsahpa
//
LOCUS       WP_176063592             188 aa            linear   BCT 11-JAN-2025
DEFINITION  polysaccharide biosynthesis/export family protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176063592
VERSION     WP_176063592.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..188
                     /product="polysaccharide biosynthesis/export family
                     protein"
                     /GO_function="GO:0015159 - polysaccharide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0015774 - polysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=20062
     Region          25..188
                     /region_name="Wza"
                     /note="Periplasmic protein Wza involved in polysaccharide
                     export, contains SLBB domain of the beta-grasp fold [Cell
                     wall/membrane/envelope biogenesis]; COG1596"
                     /db_xref="CDD:441204"
ORIGIN      
        1 mrrmtlllsl aaaacasttk gervatqpps eyrigredvl eivvwhepel trvmpvrpdg
       61 fialplagev qaagktpael rtalttaltp yvkdaavavl vreingprfs vmgevthagt
      121 fplrgaisvt qalataggtn efagdevvwl rqkpdgkqek vrlslkelvh gdvegalwls
      181 pgdvlyvp
//
LOCUS       WP_176063606             454 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Serratia marcescens].
ACCESSION   WP_176063606
VERSION     WP_176063606.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024624
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..454
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48325
     Region          17..389
                     /region_name="MFS_YajR_like"
                     /note="Escherichia coli inner membrane transport protein
                     YajR and similar multidrug-efflux transporters of the
                     Major Facilitator Superfamily; cd17472"
                     /db_xref="CDD:341025"
     Site            order(24..25,28..29,32,65,115..116,118..120,123,145,
                     148..149,152,221,224..225,228..230,233,260,264,308..309,
                     313,317,340,343..344,347..348,351)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341025"
ORIGIN      
        1 mndnsmtpqe rratwglgtv fslrmlgmfm vlpvlttygm alngaseali giaigiygla
       61 qavfqipfgl vsdrigrkpl ivggllifal gsviaavtds iwgvilgral qgsgaiaaav
      121 mallsdltre qnrtkamafi gvsfgitfai amvlgpiith afglhalfwm iavlalagiv
      181 itlavvpsad thllnresci vrgsfrkvls nsrllklnfg imclhillms sfvalplame
      241 kaglaasehw ivylvtmlvs faavvpfiiy aekyrrmkqv fmgcvavlfc aevllwlsga
      301 hlwgiiagvq lffmafnvme ailpsliske spagykgtam gvystsqfig vaiggslggw
      361 lyglqgaglv fiagavlaav wflvsstmke ppyvsslrit lselavkdsa lesrlkaqpg
      421 vaeaivvpee rsayvkvdtk qtnrgqleal vnsl
//
LOCUS       WP_176063655             841 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176063655
VERSION     WP_176063655.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 841)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 841)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 841)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 841)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 841)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17596983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..841
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..841
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86834
     Region          20..62
                     /region_name="YHS"
                     /note="Heavy metal-bindng TRASH/YHS domain, predicted
                     Cu/Ag metallochaperone [Inorganic ion transport and
                     metabolism]; COG3350"
                     /db_xref="CDD:442578"
     Region          67..115
                     /region_name="YHS"
                     /note="Heavy metal-bindng TRASH/YHS domain, predicted
                     Cu/Ag metallochaperone [Inorganic ion transport and
                     metabolism]; COG3350"
                     /db_xref="CDD:442578"
     Region          133..159
                     /region_name="HMBD"
                     /note="Heavy metal binding domain; pfam19335"
                     /db_xref="CDD:437167"
     Region          180..837
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     human copper-transporting ATPases, ATP7A and ATP7B;
                     cd02094"
                     /db_xref="CDD:319783"
     Site            order(485,487,792)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Site            order(529..531,594,610..612,641,681..683,703,706,709,728,
                     731)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319783"
     Site            order(793,821,825)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
ORIGIN      
        1 mtdpspqpaa paagqpvppr dpvcgmlvdp ehpqggtver gryryhfcsa rcrqafeaep
       61 erwfaldpvc gmevnpkapk ggslehggrt fhfcsmkcla kfqaeperyl lhgpggmpkd
      121 apppapppgg qvvwvcpmdp evrepepvpc picgmalepl vvggmpslge knpelermsr
      181 rfwlglapaa lvlalamshw lpagwsadhl lgprvnawlq lalsapvvlw ggwpfferaw
      241 lslrtrhfnm ftliglgtaa afgesalatl lpasafpeaf rgahgavpiy fesaavivel
      301 vllgqvlelr argrvsgalq allglapkta rrvapgggea dvaieevtpg dllrvrpgek
      361 vpvdgtvvsg gsavdesmvt gesvpvekgp gdrvtgatin gtgsfvfrae rvgkdtllaq
      421 ivrmvaeaqr srapiqrlad tvaawfvpav vasaaltfaa wallgpeprl ahalmnavav
      481 liiacpcalg latpmaimvg ttrgaqagvl vknaealerl arvdtllvdk tgtltlgkpr
      541 larveatgav peaellrlaa alerasehpl aaavlaasre rglppaeara frsvpgkgva
      601 gevdgraval gnaallaelg ipagdlaara dalaaggatv vlaavdgaaa gllavadpvk
      661 pgapaavkal qaggvrvvmv tgdrratala vakelgidev eaevlpgdka avvarhqgag
      721 qrvamagdgv ndapalaaad vgiamgtgad vaiesagltl lhgdlagivr arrlsratlr
      781 nirqnlfwaf aynmvgvpva agalypfsgi llspmiasaa msfssvtvia nalrlkrarl
      841 g
//
LOCUS       WP_176063694             326 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176063694
VERSION     WP_176063694.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..326
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34026
     Region          1..324
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mrvlvlqpgy lgdtvflgpa vralkarwpe grvglcvtpr gapaarllpg cdevlvfdkr
       61 gadrgpaglw ragrrlrafg aelalvphvs artgllawls gaprrigyap lctervrldr
      121 grpfvdralv laeragapge palaldapaa haayaegvla garrpvvglv pgaewatkrw
      181 aaerfaalaa elvrdgatpv llggpseral asriqalsgg alrdttgnai deavavlarc
      241 dlvvggdtgl vhcaralqrp alvlfgptap erhrfthrer altvgiacqp chdhgpptcp
      301 lghhgclaql evaqvagaar allqlp
//
LOCUS       WP_176063721             305 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: LysR family transcriptional regulator [Serratia].
ACCESSION   WP_176063721
VERSION     WP_176063721.1
KEYWORDS    RefSeq.
SOURCE      Serratia
  ORGANISM  Serratia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Serratia"
                     /db_xref="taxon:613"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33319
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..290
                     /region_name="PBP2_LTTR_like_4"
                     /note="TThe C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08440"
                     /db_xref="CDD:176131"
     Site            order(109..110,112..113,116,120,122..128,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176131"
ORIGIN      
        1 mkmsikqlra flavahtlnf aqaserlnis qpalslairg ledalggpll lrttrrvtlt
       61 pegetffpma rqlladwdna eeamrqrftl qmgkvaiaam psfagnplpp ilkafrdrya
      121 ginvavhdvi neqvfemire grvemgiafe pepsdtlhft plcrdrflav vpkdsalark
      181 aqvswkellt ldfitlqrps avrllleqel arsgrtleva feshqlvtvg rmvanglgas
      241 avpalceqqm delgavcvpl igpiierrvg lirlaqhqls saaqalatvi eremagsgae
      301 palkp
//
LOCUS       WP_176063754             530 aa            linear   BCT 11-JAN-2025
DEFINITION  serine/threonine-protein kinase [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176063754
VERSION     WP_176063754.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..530
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=55633
     Region          6..278
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(6,30,34,63,68,73..76,88)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(13..14,16..19,21,37,39,71,87..90,94,96,144,146,
                     148..149,151,161..162,165,182..185)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(13..14,16..19,21,37,39,71,87..90,94,146,148..149,
                     151,161..162)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(17,94,96,144,146,148,165,182..185)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(161..169,178..185)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
ORIGIN      
        1 mrtfgkyrlv epvasggmae vwraeapgae gfvkevalkl irgdhdargd fvrmfvqear
       61 lasrlshani vqvfdfdqvd gryyiamelv rgrtlrevvd rcreqgarlg laravhvcae
      121 varalayahr leeggapagl vhrdvspqnv lvsfegevkl tdfgiaralg asevtapgtv
      181 kgklaymape qargepvdgr advfalgvvl welcagrrlf ardtdaatla allspeplsp
      241 psawneavpp rldevalaal erdparrtas adafaealag lrlelaeghe dldlralmrr
      301 lwpegitpaa rapaaptlvr eaagtavraa ppaqvaledl strtalppap rrrlgvllta
      361 aalavaavgg aavwrgarga tahatateav tanataspsa tpmstatatp tptatatamp
      421 tatptatpta tptatptatp tagrpeappp apprpkvara tpavlevhvs pwamlsvdgg
      481 paeevvvrrd lkllpgqhtl rverpgagta elelslgage rrrwaprlkr
//
LOCUS       WP_176063822             431 aa            linear   BCT 11-JAN-2025
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176063822
VERSION     WP_176063822.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..431
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=45389
     Region          28..431
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mapqarelrs rravaaalaa iedlgegrpl rlalshalar agklgprerr haavaargva
       61 rwlrscdval aaarapqslp adrallryla wrlavlgede aaalrdlalp gprrpraisd
      121 pklaevaral prpgprgpat vrpgggelap ardpavalal rysvpdllaa kllgqlgpde
      181 aaaclaamne eprlalrvha aratrdevla alaaagvaas pgeeplaiqv edraglfdap
      241 pfraglvevq degsqavvva craargerwl dlcagsggka lalaalgarv tahdasarrl
      301 aelprrarra rlevevapep pagtfdgvlv dapcsgsgal qrepdarwri deaalrwlaa
      361 aqdevlraga arvrpggalv yatcsllree gedrvaalla rggfaleeeg rrwphrdpgg
      421 gfywarlrra r
//
LOCUS       WP_176063794             299 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176063794
VERSION     WP_176063794.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Blankenfeldt,W., Kerr,I.D., Giraud,M.F., McMiken,H.J., Leonard,G.,
            Whitfield,C., Messner,P., Graninger,M. and Naismith,J.H.
  TITLE     Variation on a theme of SDR. dTDP-6-deoxy-L- lyxo-4-hexulose
            reductase (RmlD) shows a new Mg2+-dependent dimerization mode
  JOURNAL   Structure 10 (6), 773-786 (2002)
   PUBMED   12057193
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437758
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..299
                     /product="SDR family oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009226 - nucleotide-sugar biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0019305 - dTDP-rhamnose biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31369
     Region          2..294
                     /region_name="RfbD"
                     /note="dTDP-4-dehydrorhamnose reductase [Cell
                     wall/membrane/envelope biogenesis]; COG1091"
                     /db_xref="CDD:440708"
ORIGIN      
        1 mrvavtgang llggaavaql agahevlaig rgacrlpagr fswadadlgd gqtveaalra
       61 fradavlhag altdvdgcer dpdaawrvnv ggseqvarac ralgarlvav stdyvfdgea
      121 gpygeedtpn prgayartkr cgeeaallla pdravarvav vysgrpgakn tfatqvvekl
      181 trgepvtafc dqvvsptlae saaamtlell lehdyqgvlh tagatsldrv dfaqrvaarf
      241 glrgeivpvr tadvkllapr plrsalridr aaallrsrpl aieaaldtfh aqwrsrraa
//
LOCUS       WP_176063856             505 aa            linear   BCT 11-JAN-2025
DEFINITION  tripartite tricarboxylate transporter permease [Serratia
            marcescens].
ACCESSION   WP_176063856
VERSION     WP_176063856.1
KEYWORDS    RefSeq.
SOURCE      Serratia marcescens
  ORGANISM  Serratia marcescens
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Yersiniaceae; Serratia.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Serratia marcescens"
                     /db_xref="taxon:615"
     Protein         1..505
                     /product="tripartite tricarboxylate transporter permease"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=52820
     Region          1..495
                     /region_name="COG3333"
                     /note="TctA family transporter [General function
                     prediction only]"
                     /db_xref="CDD:442562"
ORIGIN      
        1 mdtwmyltqg fevalvpqnl iialigcfvg tivgllpglg pingvaillp lafalklpae
       61 salillatvy igceyggris sillnvpgda aaimtaldgy pmaqqgragv alsisavssf
      121 vgsmiaiggi ilfapllarw slafgpaeyf almvfaiacl gsmmsqnplk sllaaliglg
      181 latvgvdant gvyrftfdsv hlsdgvqfiv vviglfsvse illmlestsa gqklvrktgr
      241 llfnrkeaaq cagptlrssv igffvgilpg agatiasalt ymtekkisgn sdtfgkgdir
      301 gvaapeaann asacgsfipm ltlgvpgsgt tavmmgaltl ynitpgpamf teqpdivwgl
      361 iaallianvi llimnlplvg lftrmltipl wflvpaiaav savgvyavhs ttfdlllmvg
      421 lgvfgyilrk mhfpmsplil gfvlgemleq nlrralsisn gefgilwsss iaqtllvlav
      481 avlalppllr lmrkrrqpaa eakve
//
LOCUS       WP_176063883             206 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176063883
VERSION     WP_176063883.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..206
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=22560
     Region          23..194
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mpgsplrppr paapdalava alveravagd paalralydr hrpavhrlar gfaeldpdea
       61 edvvqetfvr afrslarlad rarfgawlla iarnraltrl arhrasrqla eelaqepeaa
      121 apeaepleeg vaaevevvrr viaelpegae ketvrlfyle grlsareiae rmgvgksait
      181 mrlerfrakv krrvlaevar argegs
//
LOCUS       WP_176063975             590 aa            linear   BCT 11-JAN-2025
DEFINITION  serine/threonine-protein kinase [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176063975
VERSION     WP_176063975.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Canova,M.J. and Molle,V.
  TITLE     Bacterial serine/threonine protein kinases in host-pathogen
            interactions
  JOURNAL   J Biol Chem 289 (14), 9473-9479 (2014)
   PUBMED   24554701
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10195858
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..590
                     /product="serine/threonine-protein kinase"
                     /EC_number="2.7.11.-"
                     /GO_function="GO:0004674 - protein serine/threonine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=63676
     Region          21..287
                     /region_name="STKc_PknB_like"
                     /note="Catalytic domain of bacterial Serine/Threonine
                     kinases, PknB and similar proteins; cd14014"
                     /db_xref="CDD:270916"
     Site            order(21,45..46,75,80,85..88,101)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270916"
     Site            order(28..29,31..34,36,49,51,83,100..103,107,109,146,148,
                     150..151,153,165..166,169,188..191)
                     /site_type="active"
                     /db_xref="CDD:270916"
     Site            order(28..29,31..34,36,49,51,83,100..103,107,148,150..151,
                     153,165..166)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270916"
     Site            order(32,107,109,146,148,150,169,188..191)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270916"
     Site            order(165..173,184..191)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270916"
     Region          <467..558
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
ORIGIN      
        1 mlptpstfrp eslvgttldg ryrlvahias ggmgaifrae hvymrkelai kvlrpdlssl
       61 pdiaerfrre aeiaaslehd nivrvtdfgr spegwlflam ellegeslfd rlrragplsp
      121 qesvsvlvqm crgleaahar gvvhrdlkpe nifltarpag likildfgia kltdpqiasd
      181 tqagmvvgtp eylspeqatg savdgradvy avgligwrml aghhpfradd argllmmqat
      241 qpvpsivear pdltawpvlv taigracakd arerhpsvae lgaelesclg tlelpvparp
      301 sesrsrtraw tppspssgpl paaaaptvqa tmtldagtpi atplpvrvlr fgrahrlalg
      361 lvlaaavllp tsmsfarwme erpaararal laadrpeaar daiapavlrr psdarlrvlh
      421 gqalhrirgq tmaamdayta aldldprald atalsdlgqd lqaerkvaer sakllarvgp
      481 paapyvleav eqtrgnarlr vlelardmgl edrldrvavy gallsdpdcd vrraavrrlg
      541 elgnpaalpr lhelarekrr ikglfglpqe vptcgapeae aaarkltarr
//
LOCUS       WP_176063988             167 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176063988
VERSION     WP_176063988.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..167
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=18475
     Region          16..164
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mpgarasshe ervvllyrey gpavyrrclr llrdreaard atqevfvkll rdmgklaard
       61 talpwiyrva tnhclnlrrd vrrrgeqged aldlapaaaa pypagrlare vlarfdaqtq
      121 avavgvlvdg leheelasal gisrrtvhrk larflegarq llaggep
//
LOCUS       WP_176064020             175 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-binding protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176064020
VERSION     WP_176064020.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Kozak,N.A., Mattoo,S., Foreman-Wykert,A.K., Whitelegge,J.P. and
            Miller,J.F.
  TITLE     Interactions between partner switcher orthologs BtrW and BtrV
            regulate type III secretion in Bordetella
  JOURNAL   J Bacteriol 187 (16), 5665-5676 (2005)
   PUBMED   16077112
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Beaucher,J., Rodrigue,S., Jacques,P.E., Smith,I., Brzezinski,R. and
            Gaudreau,L.
  TITLE     Novel Mycobacterium tuberculosis anti-sigma factor antagonists
            control sigmaF activity by distinct mechanisms
  JOURNAL   Mol Microbiol 45 (6), 1527-1540 (2002)
   PUBMED   12354223
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005496
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..175
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=18423
     Region          28..157
                     /region_name="RsbW"
                     /note="Anti-sigma regulatory factor (Ser/Thr protein
                     kinase) [Signal transduction mechanisms]; COG2172"
                     /db_xref="CDD:441775"
ORIGIN      
        1 mtpsegparg apkpillflr mcpvwvfvde vrhfvesfca cagvsperes qlalathelm
       61 qnaithstsa cielrlaida grdavevslt ndcspgapea lrsrlaalqa epplasylht
      121 maadprargg lglarvryea qleldvttea grltvkafgq lnppplaaat gashg
//
LOCUS       WP_176064002              67 aa            linear   BCT 11-JAN-2025
DEFINITION  cold-shock protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176064002
VERSION     WP_176064002.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..67
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=7109
     Region          1..67
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 matgtvkwfn dakgfgfitq dnggedvfch htaiqaegfr tlaegqkvef dvtkgpkglq
       61 aanvrpv
//
LOCUS       WP_176064023             388 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176064023
VERSION     WP_176064023.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Marreiros,B.C., Sena,F.V., Sousa,F.M., Oliveira,A.S., Soares,C.M.,
            Batista,A.P. and Pereira,M.M.
  TITLE     Structural and Functional insights into the catalytic mechanism of
            the Type II NADH:quinone oxidoreductase family
  JOURNAL   Sci Rep 7, 42303 (2017)
   PUBMED   28181562
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Melo,A.M., Bandeiras,T.M. and Teixeira,M.
  TITLE     New insights into type II NAD(P)H:quinone oxidoreductases
  JOURNAL   Microbiol Mol Biol Rev 68 (4), 603-616 (2004)
   PUBMED   15590775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441299
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..388
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.6.-.-"
                     /GO_function="GO:0003954 - NADH dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006116 - NADH oxidation [Evidence IEA]"
                     /calculated_mol_wt=40977
     Region          3..382
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
ORIGIN      
        1 mskhalvagg gfagleaaiq lrragldvtl vsnrpalciy pisiwvatge rqlddvcldl
       61 adaarrhgfr fvvgeveals garrsatvng lelqadhlvv avggeklrpr gvehtfslgg
      121 dpagaqrlaa alsalmakgr grvamgfggn pkdpsaargg pafelmfnvd allrrrglrd
      181 rfeltffapm aspgermgqk avaaiqrmfg rvgvamrfgk kiagfepgav lfedgarlas
      241 dlvvflpage gapvvkasdl prseagfvet dpgcavpgfp gvwaigdaaa lqgpewrakq
      301 ghlaevmarv aarniaaaee graeresylp hvgitclldm ghgaayvhrd grgermiplp
      361 vvghwlkkgw ggyyklskkk lvprlpgl
//
LOCUS       WP_176064175             441 aa            linear   BCT 11-JAN-2025
DEFINITION  TldD/PmbA family protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176064175
VERSION     WP_176064175.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..441
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=47098
     Region          5..440
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 masdllkvae etvalalrkg areaaggayr vrsvevqwrd gqlekvteat trglglelyv
       61 dgrysavsta dlrpeaveqf vadaialtrt ltpdpyralp dprlyegrst laldledpry
      121 geldaarrvd laraleesar avkgaeails vttgfgdtlg esarvhsngf sgarrvtdfg
      181 lsaqvsvkdp dgrrpedwda aggrhfralp apervgraaa eralarigsr kgesgrftva
      241 venrsaarll gfllgpmtaa alqqkrsfld gklgaqigsa rleladdplv prglgsrlwd
      301 segiaarrfp lfeagalrsy fvdnyygrkl gmaptsrgms nlawklgehg qdrllaelge
      361 gllvtgflgg nsnsttgdfs lgaqgfrvrg gqlaepvgem nlsgnhlelw phlagvgndp
      421 ypwsaartpt lvfegvqvag t
//
LOCUS       WP_176064302             372 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176064302
VERSION     WP_176064302.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..372
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39789
     Region          267..331
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mtdakdlsrl ladllrreqh aladflvals afdrerrwle lgytscfyfl hrelglskga
       61 afyrktaael lqsypeliep lrdgrlclsn vaelakvitp enraevvprf fhaskqeake
      121 vaaelrpaev aprrevvtav rcsaaraape lvsaavaapa sapaapqaka vdfaqavhpe
      181 nqpervaaps pdeiepltae lrrlhftvsk rflaklaaar dalshshpga steavleagl
      241 dlllaakakr kglvakpret aprlssrprh tpaavkravw ardggccqwp vasggvcgst
      301 trleldhvlp varggestve nlrvvcrvhn qlaareffgv armarfaaka pphasapaca
      361 gggggreagd sa
//
LOCUS       WP_176064309             114 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF485 domain-containing protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176064309
VERSION     WP_176064309.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006997
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..114
                     /product="DUF485 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=12595
     Region          21..114
                     /region_name="YjcH"
                     /note="Uncharacterized membrane protein, DUF485 family
                     [Function unknown]; COG3162"
                     /db_xref="CDD:442396"
ORIGIN      
        1 maytasnisr aepkinqsat qviesadfkr lvslrwtvsm vllallfvty ygyillipya
       61 pefmttkige vttaaipigv gvivvafvlt afyvgwanks ydpeverlkn tlrk
//
LOCUS       WP_176064213             235 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176064213
VERSION     WP_176064213.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..235
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25550
     Region          10..235
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mitvrrader ghaehgwlds rhtfsfadyh dpahmgfsdl rvinedrvep gqgfgthghr
       61 dmeiisyvle gelshrdsmg tgsvirpgev qrmsagtgvr hseqnpsrer pvhflqiwil
      121 pdraghtpsy eqkafpeaer rgrlrlvasp dgaegsltih qdarmyagll aegeqarlpl
      181 aegrqawvql argelsvngq alragdgaal tgeaavelag rgaapaevlv fdlap
//
LOCUS       WP_176064334             246 aa            linear   BCT 11-JAN-2025
DEFINITION  NRDE family protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176064334
VERSION     WP_176064334.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Bard,F., Casano,L., Mallabiabarrena,A., Wallace,E., Saito,K.,
            Kitayama,H., Guizzunti,G., Hu,Y., Wendler,F., Dasgupta,R.,
            Perrimon,N. and Malhotra,V.
  TITLE     Functional genomics reveals genes involved in protein secretion and
            Golgi organization
  JOURNAL   Nature 439 (7076), 604-607 (2006)
   PUBMED   16452979
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007231
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..246
                     /product="NRDE family protein"
                     /GO_process="GO:0007030 - Golgi organization [Evidence
                     IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=26698
     Region          1..231
                     /region_name="Tango2"
                     /note="Uncharacterized stress-responsive protein, TANGO2
                     (Transport and Golgi organisation 2) family, contains NRDE
                     motif [General function prediction only]; COG3332"
                     /db_xref="CDD:442561"
ORIGIN      
        1 mctlavawrt drrwpvvvaa nrderlkraa epwglrepgl gpryaapldr vgggtwigvs
       61 argvfaaltn hharqggfpd prrrsrgelv vqalaqesag aaralfaged aarynpfhll
      121 vadaaqaflw lydgaeaall elgpglhvvt esdaegrgpr gelvrsrwpl epdparlrel
      181 lvqhapsple atcvhlddhd ygtrsssvlr lapsleasel wvaegrpctt pfddrsrlla
      241 elarsa
//
LOCUS       WP_176064378             159 aa            linear   BCT 11-JAN-2025
DEFINITION  roadblock/LC7 domain-containing protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176064378
VERSION     WP_176064378.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     Dynein light chains of the Roadblock/LC7 group belong to an ancient
            protein superfamily implicated in NTPase regulation
  JOURNAL   Curr Biol 10 (21), R774-R776 (2000)
   PUBMED   11084347
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005177
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..159
                     /product="roadblock/LC7 domain-containing protein"
                     /calculated_mol_wt=17018
     Region          22..131
                     /region_name="COG2018"
                     /note="Predicted regulator of Ras-like GTPase activity,
                     Roadblock/LC7/MglB family [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:441621"
ORIGIN      
        1 mnsglvmyee efrliagicd rltrdanakv vflidkngql iassgqaqnl dttslaslta
       61 gnvaamggla kllgekefpn qfhegeresl hmsivggrvv lvvifdakss lglvrlrvkk
      121 ageelakvfe alaqkqatpg tqspfaeitd ddidhlfse
//
LOCUS       WP_176064421             388 aa            linear   BCT 11-JAN-2025
DEFINITION  M23 family metallopeptidase [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176064421
VERSION     WP_176064421.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Razew,A., Schwarz,J.N., Mitkowski,P., Sabala,I. and Kaus-Drobek,M.
  TITLE     One fold, many functions-M23 family of peptidoglycan hydrolases
  JOURNAL   Front Microbiol 13, 1036964 (2022)
   PUBMED   36386627
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11432770
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..388
                     /product="M23 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39954
     Region          183..379
                     /region_name="NlpD"
                     /note="Murein DD-endopeptidase MepM and murein hydrolase
                     activator NlpD, contains LysM domain [Cell
                     wall/membrane/envelope biogenesis]; COG0739"
                     /db_xref="CDD:440502"
ORIGIN      
        1 mrralptlll laacatapak lawdategge pygptarlka irgasliatg qaianptsts
       61 tststatata sfaatassta tatagptatl aaapsltaag pgfsdeqlla vdpdepplpp
      121 vanpaperta aeppagppid aallrfaada rarrselpra aafppavaaa wddlalever
      181 ylarpmpqtp laelvrarva leaeldfdrr rfgapspels ahlraqlarl gqraeaaral
      241 gqslfavtrp pvlrwpiada glssgfgprl hpidhirrmh wgidlasatg rvvssaargf
      301 vvragftpgy glavevrhdg eltsryghls rllcgagdrl dagqpiglvg atgratgphl
      361 hfevwrggra edplallgar msgsaggl
//
LOCUS       WP_176064522             161 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176064522
VERSION     WP_176064522.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10483007
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..161
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17069
     Region          12..148
                     /region_name="Flavin_Reduct"
                     /note="Flavin reductase like domain; pfam01613"
                     /db_xref="CDD:460266"
ORIGIN      
        1 mdknaftqvl qkfplpvtvv tvgrggaena ltvswvapas fdppqvvfaa drhhysvdfl
       61 rstknfavnv lregqqrlaa hfsrqamaee dkldavatre gdsgaailkd alsyldceva
      121 aiyesgdhvl vvgnvvdagi lgdgqpltta aglryvkasa r
//
LOCUS       WP_176064528             849 aa            linear   BCT 11-JAN-2025
DEFINITION  M1 family metallopeptidase [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176064528
VERSION     WP_176064528.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 849)
  AUTHORS   Evnouchidou,I., Koumantou,D., Nugue,M. and Saveanu,L.
  TITLE     M1-aminopeptidase family - beyond antigen-trimming activities
  JOURNAL   Curr Opin Immunol 83, 102337 (2023)
   PUBMED   37216842
REFERENCE   2  (residues 1 to 849)
  AUTHORS   Peer,W.A.
  TITLE     The role of multifunctional M1 metallopeptidases in cell cycle
            progression
  JOURNAL   Ann Bot 107 (7), 1171-1181 (2011)
   PUBMED   21258033
REFERENCE   3  (residues 1 to 849)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   4  (residues 1 to 849)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10176184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..849
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..849
                     /product="M1 family metallopeptidase"
                     /EC_number="3.4.11.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=92214
     Region          20..441
                     /region_name="M1_APN-Q_like"
                     /note="Peptidase M1 aminopeptidase N catalytic domain
                     family which includes aminopeptidase N (APN),
                     aminopeptidase Q (APQ), tricorn interacting factor F3, and
                     endoplasmic reticulum aminopeptidase 1 (ERAP1); cd09601"
                     /db_xref="CDD:341064"
     Site            order(125,127,260..263,296..297,300,319,323,376,381)
                     /site_type="active"
                     /db_xref="CDD:341064"
     Region          516..829
                     /region_name="ERAP1_C"
                     /note="ERAP1-like C-terminal domain; pfam11838"
                     /db_xref="CDD:463368"
ORIGIN      
        1 mphatddrny rlptsvrpar yqltlsldpg rrvfagegqv glelaaptge lvlhaaaldl
       61 traelrtadg pravrvvpap asetvrlvle rpapagaatl elawnghvsd glrglyqaag
      121 vavtqfeaad arrvfpcfde pgfkapwalt veapaglall sngapertte aagrqrvafr
      181 etpplptylv alacgalear pagaargvpv rtwavpekla ltafaqeval evlprledyf
      241 glpyafgkld qvgvpefeag amenaglvty reaallldpa taalpvkkrv aevithelah
      301 qwfgnwvtmq wwddlwlnes fatwmaakiv dgwrpewrvw ldfdagkaaa lhldalrsth
      361 pvraevknpe dmtesfdvit yekggavlrm iegylgegpf rdgirlymrr hakanavagq
      421 lwaalaeasg qpvpeladaw iggpgypvve vrregrrval gqrrfysepg vaeagerwpv
      481 plvlryedag gvkearhllr gaageltlpg egevrwlvan ggstgfyrva ydaasaaala
      541 rhlprlapse rigliadqwa lvragarepa dfldllaafg geedyavlde lvgrlaglea
      601 rladepvrqr fqrfvanlvg pafaragwdp apgepdalrm rraallrala lvarepaava
      661 egarrldrfl ggdaaalepn lhdaavamaa ragderrfea lrarfkvepd palkrryltg
      721 lalfedpala araealafgd eiplqdaasy mgallanrta regfwgalrq rwdavqqrvg
      781 gapmllrrvv eavgqlperr hleeataffa ahpvpaarqa iaqtlermrq dvalwerlgp
      841 avarwlaar
//
LOCUS       WP_176064557             441 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176064557
VERSION     WP_176064557.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..441
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=44649
     Region          3..436
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mstlglaaat ffivsggpyg leeivlgygy pgalallavv plvwslpval lvgelaaalp
       61 atggyyawvr ralgpfwglq eawlsmavgi vdiaiyptll vtylgrlwpa lggdqpgapg
      121 wwlgvamial ctawnaagir sigrgsavfg aalfapfall valaawragt aglgparaaf
      181 aapaaagegg laaglmlamw nlmgfdnast fagevrrper sypramatat aaiaisylvt
      241 vaaaavsglt ppawsagswv eigaglggpa lalaialgga isaagmynal llswsrlpva
      301 laedgwlpgr laersartga plaavllgga lsaacvglgm rrlveidvll ygaalllelv
      361 alvalrvrep elprpfkipg glpgvvalsv cpaallalaa wqgrrepgaf glsslalgav
      421 vaavgpawwl aarvrrrgpr s
//
LOCUS       WP_176064570             467 aa            linear   BCT 11-JAN-2025
DEFINITION  YncE family protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176064570
VERSION     WP_176064570.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Kagawa,W., Sagawa,T., Niki,H. and Kurumizaka,H.
  TITLE     Structural basis for the DNA-binding activity of the bacterial
            beta-propeller protein YncE
  JOURNAL   Acta Crystallogr D Biol Crystallogr 67 (Pt 12), 1045-1053 (2011)
   PUBMED   22120742
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Fulop,V. and Jones,D.T.
  TITLE     Beta propellers: structural rigidity and functional diversity
  JOURNAL   Curr Opin Struct Biol 9 (6), 715-721 (1999)
   PUBMED   10607670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465355
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..467
                     /product="YncE family protein"
                     /calculated_mol_wt=49932
     Region          181..390
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          323..>462
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
ORIGIN      
        1 mrsattwlal amcafacaap arsqrtlppl gdegevyvyl epfpaeaehl aftvsaaqva
       61 radgpaaple lllpnlgglg tsrqrllawg rlppgdytsl lltvkratlg spegrsdllv
      121 ppepdrvpva fqvergratl valtlqyars vdrsfafspa ftaeqartpv eqligycsst
      181 alasltafdr hrhralavtp vgrapegvvl drrahrayva lpgedqvevl dlatgadlqr
      241 lplrggdrpr elaltpdgqa lvvlnqgsys vsfldlstas elaraptgee pyslrldrsg
      301 rrayvfnrrs ntvtvvdlps rqvaatvpvd aeplrgqvdr tggrlyvvhg gssyltvltl
      361 pdltvasrly vglgasavev dvrtdrvyva vgrtlevfdp lsivpidsfe lpgaastlav
      421 deventllav lpdlravafi dltsrhltgl vdvgespyat aiegelr
//
LOCUS       WP_176064624              77 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176064624
VERSION     WP_176064624.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 77)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
REFERENCE   5  (residues 1 to 77)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 77)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10590097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..77
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=8037
     Region          6..76
                     /region_name="Thioredoxin_3"
                     /note="Thioredoxin domain; pfam13192"
                     /db_xref="CDD:433026"
ORIGIN      
        1 mliqvlgtgc akckaltana eaaaraagvd arvekvedlr eimkfkvmst palvldgqvr
       61 stgkvltvea irqlltp
//
LOCUS       WP_176064661             405 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176064661
VERSION     WP_176064661.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..405
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=43817
     Region          299..359
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mpdaapasld tvallhrlae lagherhtqv efllhldvfd qrrawaeagy pslwewcvra
       61 lhlsegaagr riaamrvlrr fpglaeplrd grlslstaav lspvltegnw eelvgraayk
      121 tkveteqlva slqprpapre glrrlprpek apatlakpie agcvevdgag erapalrpea
      181 tsvepltleg saaqacprel haaqsaparr atlepvdadt yslrvtvdae lkkdldqlks
      241 llahkvrngd lgallreavk calekhgkrr gavepsrkrn itapaenapp ptpgerepip
      301 aavrrevwkr dggrcawcsp dgrrcgstwm leldhiepva lggrstvdnl rlccrshnsl
      361 haehvfgrer mdrfrkgadr sapptaasgs tsgacgtraq aagst
//
LOCUS       WP_176064686             396 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphoglycerate kinase [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176064686
VERSION     WP_176064686.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Chiarelli,L.R., Morera,S.M., Bianchi,P., Fermo,E., Zanella,A.,
            Galizzi,A. and Valentini,G.
  TITLE     Molecular insights on pathogenic effects of mutations causing
            phosphoglycerate kinase deficiency
  JOURNAL   PLoS One 7 (2), e32065 (2012)
   PUBMED   22348148
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Yon,J.M., Desmadril,M., Betton,J.M., Minard,P., Ballery,N.,
            Missiakas,D., Gaillard-Miran,S., Perahia,D. and Mouawad,L.
  TITLE     Flexibility and folding of phosphoglycerate kinase
  JOURNAL   Biochimie 72 (6-7), 417-429 (1990)
   PUBMED   2124145
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Yoshida,A. and Tani,K.
  TITLE     Phosphoglycerate kinase abnormalities: functional, structural and
            genomic aspects
  JOURNAL   Biomed Biochim Acta 42 (11-12), S263-S267 (1983)
   PUBMED   6689547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..396
                     /product="phosphoglycerate kinase"
                     /EC_number="2.7.2.3"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004618 - phosphoglycerate kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=42602
     Region          5..395
                     /region_name="Pgk"
                     /note="3-phosphoglycerate kinase [Carbohydrate transport
                     and metabolism]; COG0126"
                     /db_xref="CDD:439896"
ORIGIN      
        1 malrtldalq lagkrvfirv dfnvpldeag kvsddrrira alptirrave qrakvilash
       61 lgrpkgkped kkkytllpva erlqelldqe ivfaddcigd gvkklvkelk dgqvlllenl
      121 rfhpeeeand egfakelasl advwvndafg tahrahasta gmakfvkeka agyliqkeve
      181 ylgkallrpe kpfvailgga kvsdkikvle nllakadavc iggamaytfl kaegvpvgks
      241 kveedkldla railekakar gvdfmlpvdh vcgaeatata krevvndrai pdgligldig
      301 pktldryrqr vlsaktvfwn gpmglfeqkp waegtfgvar amaespavtv vgggdsaaav
      361 eeaglvpkmk hvstgggasl efvegrvlpg iqvles
//
LOCUS       WP_176064731             193 aa            linear   BCT 11-JAN-2025
DEFINITION  roadblock/LC7 domain-containing protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176064731
VERSION     WP_176064731.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Koonin,E.V. and Aravind,L.
  TITLE     Dynein light chains of the Roadblock/LC7 group belong to an ancient
            protein superfamily implicated in NTPase regulation
  JOURNAL   Curr Biol 10 (21), R774-R776 (2000)
   PUBMED   11084347
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Bowman,A.B., Patel-King,R.S., Benashski,S.E., McCaffery,J.M.,
            Goldstein,L.S. and King,S.M.
  TITLE     Drosophila roadblock and Chlamydomonas LC7: a conserved family of
            dynein-associated proteins involved in axonal transport, flagellar
            motility, and mitosis
  JOURNAL   J Cell Biol 146 (1), 165-180 (1999)
   PUBMED   10402468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10659021
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..193
                     /product="roadblock/LC7 domain-containing protein"
                     /calculated_mol_wt=19852
     Region          3..>39
                     /region_name="Robl_LC7"
                     /note="Roadblock/LC7 domain; smart00960"
                     /db_xref="CDD:214939"
ORIGIN      
        1 mhellaqlna vpgvvgsllc dgegqllaqa fppavdpaqa eraaavlaar apgleaavgk
       61 aaladfrfag arvvvkgleg ggqllflcap sinlpfltms assvvkkler avrerpgrpg
      121 agalhravqr vdelilrsgg drfklrgqia lkagfaldlv dpdspddpdk lkkleaaata
      181 vlgqpfragd ptp
//
LOCUS       WP_176064768             433 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydroorotase [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176064768
VERSION     WP_176064768.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Gojkovic,Z., Rislund,L., Andersen,B., Sandrini,M.P., Cook,P.F.,
            Schnackerz,K.D. and Piskur,J.
  TITLE     Dihydropyrimidine amidohydrolases and dihydroorotases share the
            same origin and several enzymatic properties
  JOURNAL   Nucleic Acids Res 31 (6), 1683-1692 (2003)
   PUBMED   12626710
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Holm,L. and Sander,C.
  TITLE     An evolutionary treasure: unification of a broad set of
            amidohydrolases related to urease
  JOURNAL   Proteins 28 (1), 72-82 (1997)
   PUBMED   9144792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10793206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..433
                     /product="dihydroorotase"
                     /EC_number="3.5.2.3"
                     /GO_function="GO:0004151 - dihydroorotase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006221 - pyrimidine nucleotide
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=45548
     Region          4..427
                     /region_name="pyrC"
                     /note="dihydroorotase; Validated; PRK09357"
                     /db_xref="CDD:236479"
     Site            order(63,65,182,235,310)
                     /site_type="active"
                     /db_xref="CDD:238642"
ORIGIN      
        1 mtdtvfiegg rvidpasgvd gvrtvvvrdg kvaevaerle rprdvravda rgrwvtpgfl
       61 dlhvhlrepg qeyketvatg araaaaggft avcampntvp pndntsvtel ilararaagl
      121 arvypvgcis kgmkgeelae ygelqaagcv alsddgrpva ssalmrrale yarafdlplt
      181 vheedlalvg kgvmhegpaa trlglkgipa aseevmvard lalleltggr lhiahlstag
      241 svravreakr rglsvtaevt phhlaltded varsryataf kmapplrsaa draavreala
      301 dgtidciatd haphspvekd lefdaaangv vgletafpvg lalvregvls errlvealta
      361 gparafrlpg gslargapad lavldparew rcepalfhsk sknspwmgat lvgrctltlv
      421 ggrivhelae ggr
//
LOCUS       WP_176064787             264 aa            linear   BCT 11-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176064787
VERSION     WP_176064787.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..264
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=26916
     Region          120..252
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          132..156
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          162..192
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mvsgseaaql lesagvapdr laeaarrgla aapgfavgpa rdgdrrllvq ltveraeafg
       61 ggpgagavaq vavsleltsa dgepsrreag aaaeplsdgp aalrvalera ataavdkava
      121 gvalqlgaer ksspelvrdl tspdapvrdr avrtladrga reavpalier lhdsdpavve
      181 raigalaqlh dpraaaplia larhrdgayv aqlarllgdv ggpdarawll tmssghpdda
      241 vrgaaraala elsererqar adpr
//
LOCUS       WP_176064839             246 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176064839
VERSION     WP_176064839.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 246)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..246
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27212
     Region          1..239
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 miairdlhks fgdhkvldgi tidvergttf vvlggsgsgk tvlmkhvigl lkpdsgtvlv
       61 dgieipkleg reltearrmf gmvfqgaalf dsmtvydnva fplherqrgi kpselrervi
      121 eklkvvdlde dvltkfpael sggmrkrval aravvhepkv vlydepttgl dpittayvdd
      181 milsakqrlg vtsmvishdi asafkvadrm avlydghlaa qgtpeevrrs dhpyvqhyls
      241 mwfekq
//
LOCUS       WP_176064842             432 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176064842
VERSION     WP_176064842.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..432
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45126
     Region          113..431
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mtlalllsaa lgaaaaaplp asapgtltle ealararshp rsaqalavaa qaeararevf
       61 gsflpdvnat asysratsnf apspgtqsgg gfrvalpetd atspyyaaal svqaplwdfg
      121 rtlgqvrsar aseaaarsdl aaarqdvelq vrtswfaala aqalvqvadd tigqmqkhld
      181 faqaslevgr rtrfdvtraq vdltnaritk lqadngvasa raaleaavge plgpvrlvap
      241 edpggpdprp adeveralrq rpelraldlr vgaaeqslaa arsawfpvls asgqygwrga
      301 dfplvhnwqv gaalswnlfn gfsdaaavde qrgaveqara arelealqvr seveqaalav
      361 geararrdaa gvlvtqaqen lelaegryqa gvgsivdlad aeaaltsars qqvragydla
      421 taraklvrav ge
//
LOCUS       WP_176064858             293 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Piscinibacter koreensis].
ACCESSION   WP_176064858
VERSION     WP_176064858.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..293
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=29852
     Region          22..293
                     /region_name="COG4798"
                     /note="Predicted methyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:443826"
ORIGIN      
        1 margrgvlga aalaallvva gcassgaase ppldrariea llaspdrsaa drsndvrrkp
       61 aemlafigvr pgmvaldvsa gggyttella ravgpggrvy gqsaprnpar tppaapeggg
      121 apaptaasag asmpgsagvp aaaaprtspt llaeraqrsg lanivpvvrp feeaappeia
      181 nagadlvtlm fnyhdlghlg vdrarmnaal faalkpggvy viadhagrsg tgisesgtlh
      241 rveeafvrre veaagfrlva sgdflrnpnd prdrntpepp qpkdefvlkf vkp
//
LOCUS       WP_176064876             198 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176064876
VERSION     WP_176064876.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..198
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=21402
     Region          6..178
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 masdpdaalm vafqggdera frslfekyar pmvsfchhfv rdqaraeela qdvflkvhrn
       61 aaryqptarf ktflyriasn hclnelrrge yagrravqdg gegalepvdp dalpgvaatp
      121 eedaagralg ravdlllarl pekqraafvl grlegmpyee vaavlettvp avkslvhrat
      181 vaaaaalapy tsaeevap
//
LOCUS       WP_176064888             331 aa            linear   BCT 11-JAN-2025
DEFINITION  AEC family transporter [Piscinibacter koreensis].
ACCESSION   WP_176064888
VERSION     WP_176064888.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..331
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=34300
     Region          1..327
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mqatlavtvp ffalvllgyv aarrellpda avpglnayvl yfalpcmlfr fgsslpirql
       61 idplliaiwa vsalcvialt ivltlrragr pggvgmtdaa fgalvaafpn sgfmgvplll
      121 ellgayaagp vistllidlv ltstvclala qarvhgghme tsllhsaara lrgaaanplp
      181 yaialgavaa atgqrlvgpv ervvfmlads atpvalftig avlwragrha htrtpprhyl
      241 pvaliklfvh plvvfvvghi avatgapvsr sgmtalvlaa alpsasnvsl laerygadng
      301 rvariimast vlafgsfsll awllgsgvlr r
//
LOCUS       WP_176064892             127 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176064892
VERSION     WP_176064892.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002505
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..127
                     /product="response regulator"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /calculated_mol_wt=13494
     Region          3..115
                     /region_name="CheY"
                     /note="CheY-like REC (receiver) domain, includes
                     chemotaxis protein CheY and sporulation regulator Spo0F
                     [Signal transduction mechanisms]; COG0784"
                     /db_xref="CDD:440547"
ORIGIN      
        1 mqrvlvvddd aaireciael lstegfdvre ardgreglra ldaaqpgvvv ldlmmpvmsg
       61 wefleakkqr rpavanipvi vvtasdrpgv etervlrkpf dleallaave eltgrapppp
      121 pggaaaa
//
LOCUS       WP_176064926             528 aa            linear   BCT 11-JAN-2025
DEFINITION  ammonium transporter [Piscinibacter koreensis].
ACCESSION   WP_176064926
VERSION     WP_176064926.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..528
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53676
     Region          90..527
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mkklilagaf laaalgfdga alaqpaasep astasavatd vgsaassaas avaaaasaas
       61 aalagpgtsg atagatgaqp aasaaaptpn kgdvawiiva tllvimmsip glalfygglv
      121 rsknmlsvlm qvfvtfsliv vvwcvygysl aftegnaffg gfdrlfmkgl fnpadgtyam
      181 gatfskgvvl pellfmafqa tfaaitccli vgafaermkf savllfmvlw ftfsyapiah
      241 mvwywmgpda yttaavadem nskagfiwqm galdfaggtv vhinaavagl vgaymvgkri
      301 gygreaftph sltltmvgaa llwvgwfgfn agsaleassg avlafintls ataaavlawc
      361 lgeamlkgka smlgaasgav aglvaitpac gnvgfmgaiv igfiagfacl wgvrglkrll
      421 gaddsldvfg ihgvggivga lltgvfnnqa lggpglvgdw vtgtvsstpi laqvwiqlka
      481 vlltvvwsav vsliaykivd vviglrvsee deregldiss hgetayhn
//
LOCUS       WP_176064970             121 aa            linear   BCT 11-JAN-2025
DEFINITION  nuclear transport factor 2 family protein [Piscinibacter
            koreensis].
ACCESSION   WP_176064970
VERSION     WP_176064970.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Eberhardt,R.Y., Chang,Y., Bateman,A., Murzin,A.G., Axelrod,H.L.,
            Hwang,W.C. and Aravind,L.
  TITLE     Filling out the structural map of the NTF2-like superfamily
  JOURNAL   BMC Bioinformatics 14, 327 (2013)
   PUBMED   24246060
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Izaurralde,E.
  TITLE     Friedrich Miescher Prize awardee lecture review. A conserved family
            of nuclear export receptors mediates the exit of messenger RNA to
            the cytoplasm
  JOURNAL   Cell Mol Life Sci 58 (8), 1105-1112 (2001)
   PUBMED   11529502
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10577308
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..121
                     /product="nuclear transport factor 2 family protein"
                     /calculated_mol_wt=12816
     Region          11..108
                     /region_name="SnoaL_2"
                     /note="SnoaL-like domain; pfam12680"
                     /db_xref="CDD:432716"
ORIGIN      
        1 mtdpnaiast ylrtwnettp daraallrda wsddasyvdp laaargaaqi daliggvqar
       61 fpgfrftlrg tpdghgdhvr fgwslgpdgv eapiegsdvl elkdgrirrv vgfldkvpaa
      121 a
//
LOCUS       WP_176065048             324 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Piscinibacter koreensis].
ACCESSION   WP_176065048
VERSION     WP_176065048.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..324
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35702
     Region          85..321
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mspidlnrra idaagtasar tpdsaarrrr arlwrrsiat glaagsllag ctgletqqrk
       61 wifqprpata emsleeiasf assqgmesvw iehrsaisrr pirlhalwap hegnadapvl
      121 lylhgarrdv gsntwairnm qalgfsvlav dyrgfgnstn elpselgaie daraawdwla
      181 aryperpryv fgyslggava vqlaaelaeq paarqprgvi leatftsird mfqtlrwgwl
      241 pisaliterf dsldaiqrvt apllvvhgsd ddfvparfgq alyeraraar kqfvlveggt
      301 hystnwrgae qyrvalkqmf gvgg
//
LOCUS       WP_176064680             594 aa            linear   BCT 11-JAN-2025
DEFINITION  arginine--tRNA ligase [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176064680
VERSION     WP_176064680.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   O'Donoghue,P. and Luthey-Schulten,Z.
  TITLE     On the evolution of structure in aminoacyl-tRNA synthetases
  JOURNAL   Microbiol Mol Biol Rev 67 (4), 550-573 (2003)
   PUBMED   14665676
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Francklyn,C., Perona,J.J., Puetz,J. and Hou,Y.M.
  TITLE     Aminoacyl-tRNA synthetases: versatile players in the changing
            theater of translation
  JOURNAL   RNA 8 (11), 1363-1372 (2002)
   PUBMED   12458790
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Woese,C.R., Olsen,G.J., Ibba,M. and Soll,D.
  TITLE     Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary
            process
  JOURNAL   Microbiol Mol Biol Rev 64 (1), 202-236 (2000)
   PUBMED   10704480
REFERENCE   4  (residues 1 to 594)
  AUTHORS   Wolf,Y.I., Aravind,L., Grishin,N.V. and Koonin,E.V.
  TITLE     Evolution of aminoacyl-tRNA synthetases--analysis of unique domain
            architectures and phylogenetic trees reveals a complex history of
            horizontal gene transfer events
  JOURNAL   Genome Res 9 (8), 689-710 (1999)
   PUBMED   10447505
REFERENCE   5  (residues 1 to 594)
  AUTHORS   Delarue,M. and Moras,D.
  TITLE     The aminoacyl-tRNA synthetase family: modules at work
  JOURNAL   Bioessays 15 (10), 675-687 (1993)
   PUBMED   8274143
REFERENCE   6  (residues 1 to 594)
  AUTHORS   Cusack,S., Hartlein,M. and Leberman,R.
  TITLE     Sequence, structural and evolutionary relationships between class 2
            aminoacyl-tRNA synthetases
  JOURNAL   Nucleic Acids Res 19 (13), 3489-3498 (1991)
   PUBMED   1852601
REFERENCE   7  (residues 1 to 594)
  AUTHORS   Schimmel,P.
  TITLE     Classes of aminoacyl-tRNA synthetases and the establishment of the
            genetic code
  JOURNAL   Trends Biochem Sci 16 (1), 1-3 (1991)
   PUBMED   2053131
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414312
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..594
                     /product="arginine--tRNA ligase"
                     /EC_number="6.1.1.19"
                     /GO_function="GO:0004814 - arginine-tRNA ligase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006420 - arginyl-tRNA aminoacylation
                     [Evidence IEA]"
                     /calculated_mol_wt=64725
     Region          2..586
                     /region_name="ArgS"
                     /note="Arginyl-tRNA synthetase [Translation, ribosomal
                     structure and biogenesis]; COG0018"
                     /db_xref="CDD:439789"
ORIGIN      
        1 mirdhvialf ekalargaae grwpalaggf tvepprdpkh gdfavnaamv lakpaqkppr
       61 elaqalvevv reidaagdva smevagpgfv nvrlapdlwy ralgeverqg aafgrtsvgk
      121 gkkviveyvs anptgpmhvg hgrnavtgdg varllqwsgh evtreyyvnd ygaqvqtlar
      181 svhlryqqll gravemppks ypgeyvidva ralkeehgar fldapeadwl alfrdravah
      241 vlelirgdla vlditfdvws sekalyasgd verflaqlea kglvyvgklp ppkskkgapp
      301 pppqpdeegv svsddltlfr ssqfgdevdr pvkksdgtpt yfcadiayhw qkrqraealv
      361 dvlgadhggy vprlqaalqa lgydrkdlhv vliqmvnltr ggeavkmskr agtvvslrev
      421 veevgadatr flfftrrada qldfdlelak qqtldnpvfy vqygharlas ilrkaaeagl
      481 pppafdlaaa ralvlpeeqd llrrivsfpd vlagaavaye phrvaywlhe tiaafhayyt
      541 ggkksgervi gpdpvktaar lylcsalkqa langlsalgv sapermesrd laee
//
LOCUS       WP_176065074             364 aa            linear   BCT 11-JAN-2025
DEFINITION  HD-GYP domain-containing protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176065074
VERSION     WP_176065074.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..364
                     /product="HD-GYP domain-containing protein"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39524
     Region          44..342
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 magsdapaap trillvdeda aardavaavl vqegyvcaca rtseqalala qagefhlvlc
       61 dvdtprqegl qlldrlradq pstavilltg rgdteavveg lrrgasdcla kppqlldlvr
      121 aieralakrr lelarhryrt slerrvrekt aelskalrei esayastlya lvaaldareh
      181 etsdhsqrvv rytlaiaerm glpaadlpdi argallhdig kigvpdaill kpgkllpqew
      241 eemrrhpeig htilrsipfl evpsrivlah qerwdgrgyp hglageaipl garifaiadt
      301 ldaitsdrpy rrggplekar eevrryagtq fdprcaeafl sldggvleal rrpdalaaaa
      361 ggsp
//
LOCUS       WP_176065141             510 aa            linear   BCT 11-JAN-2025
DEFINITION  carotenoid oxygenase family protein [Piscinibacter koreensis].
ACCESSION   WP_176065141
VERSION     WP_176065141.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Poliakov,E., Uppal,S., Rogozin,I.B., Gentleman,S. and Redmond,T.M.
  TITLE     Evolutionary aspects and enzymology of metazoan carotenoid cleavage
            oxygenases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1865 (11), 158665 (2020)
   PUBMED   32061750
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Sui,X., Kiser,P.D., Lintig,Jv. and Palczewski,K.
  TITLE     Structural basis of carotenoid cleavage: from bacteria to mammals
  JOURNAL   Arch Biochem Biophys 539 (2), 203-213 (2013)
   PUBMED   23827316
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Kloer,D.P. and Schulz,G.E.
  TITLE     Structural and biological aspects of carotenoid cleavage
  JOURNAL   Cell Mol Life Sci 63 (19-20), 2291-2303 (2006)
   PUBMED   16909205
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Wyss,A.
  TITLE     Carotene oxygenases: a new family of double bond cleavage enzymes
  JOURNAL   J Nutr 134 (1), 246S-250S (2004)
   PUBMED   14704328
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..510
                     /product="carotenoid oxygenase family protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006720 - isoprenoid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55012
     Region          64..507
                     /region_name="COG3670"
                     /note="Carotenoid cleavage dioxygenase or a related enzyme
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]"
                     /db_xref="CDD:442887"
ORIGIN      
        1 mnrrdliral aalgagsalp afaldaapag sgaaaaafdr avaemrwlga lkgvsagtdt
       61 lrcdrlavsg rwpaglrgrf yrngpalfer ggqryrhwfd gdgmvqrfef gpngvshlgr
      121 mvrtpklane reagrflvna lgtriddeap vqgpdsfnta ntnaiehagr vlamweggsa
      181 faldpadlst rgavtwqpgl eqapfsahpk ldpqgnlwni gttqdkvvvw hvdpagklar
      241 vqigespypg gmahdvaite ryivlplppv rlnfgragrg repeqamdfa pdqplrilvm
      301 rkddvaerrv felpaqfvfh vgnahersdg tivlsfvgap datfltrdai almrgeggms
      361 thtrtqvatl dmasgrarvd alagavefpr idprriglpa rhlvtavnwk sfpgrgrtlf
      421 hgiqvqdlas grvdrfdyga davveehivv pkpgstreld awlvgttfda rrqatqvnvl
      481 darrvadgpi aqatlpyalp lgfhgnfsaa
//
LOCUS       WP_176065165             186 aa            linear   BCT 11-JAN-2025
DEFINITION  MOSC domain-containing protein [Piscinibacter koreensis].
ACCESSION   WP_176065165
VERSION     WP_176065165.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..186
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19791
     Region          4..167
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
ORIGIN      
        1 mtrtlvslnt arsdvprtgv artavdgaqg ltlygldgee radaaayglr ralyaypseh
       61 ygfwqtvraq alvadwgatl pwgalgenlt laglvesqvw igdvlrfpdc alavsepgmp
      121 spglnealgf phaaklmass gwcgfflsvr vpgsigpgqr felepgprdv gilelfrerm
      181 eraaat
//
LOCUS       WP_176065270            1035 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Piscinibacter koreensis].
ACCESSION   WP_176065270
VERSION     WP_176065270.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..1035
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=110558
     Region          1..1013
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mnvsawsiry pvpsmllfvm ltvlglfsfr amkiqnfpdi dlpmvtvsal lpgaapaqle
       61 tevarkiens iatlqgvkhi ytkvqdgaat ittefvlekp vqealddvrd avqrvrsdlp
      121 gdlrdpvitk kelagspilt ytvassrmdd ealswfvdnq vtkamlsvrg vgavarvgga
      181 trevrveldp akllalnata adisrqlrsv qqeasggrad vggseqsvrt iatvqtadel
      241 grmevalsdg rrvrldqvat vtdtvaeqrs aallngrpvv gfeivrsrga getevaagvr
      301 arletlkaeh pdisvteafn fvdpvqenyd gsmtllyega vlavlvvwlf lrdwratlva
      361 atalplsiip afwvmdlmgf svnvvtllsl slvvgilvdd aiveienimr hlgmgkspld
      421 aareaadeig laviatsftl iavflptafm sgipgrffvq fgwtaaiavf fslvvarmlt
      481 pmmaayilkp pkkahadpsw mprymalarw clthravtll vtlafsvlal lpvilgkvpa
      541 afippddlsq tqvslslppg stfrqtlaaa eqarailekn phvkliytav gggntgadpf
      601 sgaglpevrq atltlnlthr kerhgvskqa ieadlrqala dlpgvrvkvg fggsnekyvl
      661 vlagedgnvl ashatrvere lrtipgignv tstaslvrpe livrpdsara adlgvtaaai
      721 adtlriatag dydqalakln lsqrqvpvvv rlpadartdl dllsrlpvpg argpvplgnv
      781 aslaiesgpa qidrydrlrn vnfeielngq plgdvskaak avpslqqlpp gvirqevgda
      841 eafrelaesf glailtgvac iyivlvllfh awvqpvtilg alllavpgav lalfltgesl
      901 smpsmiglim lmgiatknsi llveyaimar rdhglarfda lldachkrar piimttiamg
      961 agmlpialgi gvdpsfrapm aivvigglvt stflsllvip viftfvddav qwlrrvvlrr
     1021 kpapptgpaa egahp
//
LOCUS       WP_176065204             287 aa            linear   BCT 11-JAN-2025
DEFINITION  ankyrin repeat domain-containing protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176065204
VERSION     WP_176065204.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Li,J., Mahajan,A. and Tsai,M.D.
  TITLE     Ankyrin repeat: a unique motif mediating protein-protein
            interactions
  JOURNAL   Biochemistry 45 (51), 15168-15178 (2006)
   PUBMED   17176038
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..287
                     /product="ankyrin repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=28459
     Region          41..287
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          90..117
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          120..150
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(121,125..126,129..131,133..134,138,141,150,152,154,
                     158..159,162..164,166..167,171,174,183,185,187,191..192,
                     195..197,199..200,204,207,216)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          152..183
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          185..216
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          251..276
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
ORIGIN      
        1 mradpaggvp psplrllaga lvlvatgsga falgtawmre aalanglpar apraavrppp
       61 pphkdllgpa apaaggaaps pdpaaevlpp llaaarrgel aeltrlldag aevraateqg
      121 rsavveaass gcgacvrlll arggdpdatd pragsaltva askghedaaa alleqdadad
      181 qpdlggrapl hwaveasslp ivkllveaga eldardrega tplhraaeag qvplvealae
      241 agaaldapdg agrtaaerar drghpevvea lrrrgarapg etvagar
//
LOCUS       WP_176065336             270 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Piscinibacter
            koreensis].
ACCESSION   WP_176065336
VERSION     WP_176065336.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..270
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27971
     Region          52..267
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 madwqlwael lvlgcavgfl agllgigggm vlvpfmtfll gqrgfpadll vkvaiatsla
       61 ticftslasv rahhrrgavd wsivkplapg ivigtllgaq larlmpgatl aivfagfvaf
      121 safqmfldrk pkpsrtlpaw pgmlgagsgi gvlsalvgag ggfisvpfmt wcnvpihrav
      181 gtsaalgfpi avsgtigyii agwnleglpp gtlgflyvpa llliattsvl lapvgaaaah
      241 rmnvrqlkrv facllfllag ymlykglttr
//
LOCUS       WP_176065330             309 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease
            [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176065330
VERSION     WP_176065330.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 309)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..309
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=32677
     Region          1..309
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mteflqhlvn glsvgtiyal ialgytmvyg vlklinfahg dvymvgafsg fylanamgvg
       61 gspslakalv vfvgsmiicg ilgvlierfa yrplrhrarl tslitaigvs flleygfqlp
      121 sipglgipfp pgptprffpe pftrvawepf gvyvsnydvi sfftavglml llqyivyrtr
      181 fgtsmravsf dsqvaglmgi nvnrviagtf algsalaaaa allfagsrpk vdplmgltlg
      241 ikafvaavfg gignvpgamv gglalglaee yvsgyalssy rdgiafafli ivllvrpagl
      301 fgsfrpekv
//
LOCUS       WP_176065338             120 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Piscinibacter koreensis].
ACCESSION   WP_176065338
VERSION     WP_176065338.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..120
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=12800
     Region          3..71
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(17,20)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mpeacpplva clcaawcgsc reyqplfarl easfpevvfa wvdiedhadv vgdidvedfp
       61 tlliaigaev vflgpvtphl ataerllrsa ldgalnrvrd agavelagrv rrlradegge
//
LOCUS       WP_176065350             214 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176065350
VERSION     WP_176065350.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..214
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=23381
     Region          3..193
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 meaddltlvs raktgdpeaf ralvvryqrk vyavalgivk drdlawdvaq eafvrvhahl
       61 adfkgdstfs twvlrigshl aidavrkert aakeeldevr gqdvarggeg ilatalgndp
      121 qenalrrela gkmtealaql pekhrailvl releglsyee lseqlgipkg tvmsrlfhar
      181 skmqallrey aglpadegaq tvgrglaprr gges
//
LOCUS       WP_176065420             466 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176065420
VERSION     WP_176065420.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..466
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=48575
     Region          <27..463
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 marsvreerp astrpsarwt daaphlvalr graaeggera appaagltvs lqvkillsyl
       61 vvgavllfav plvfehvpnr llggtiival tlaigfgltt alarvtrlar lkesaveisr
      121 gdlskplasd asphvrdeid dltlsistmq enlrdlvsri qrtaqsvaes anelsssaed
      181 vnastdevar smekiasgae eqsslvelas kvigdiaasi ertarsaeea arasaetssg
      241 aasggeaarl agekvkrvfa rieaaseqvf afgertkais kiveaitsva qqtnllalna
      301 tieaaragey grgfavvade vrklaesagr saeqisslaa disgratavv stmkesvsvl
      361 gegredlnai irgledisqi aasgadkvgv isqaardqlk gsadmvqamd hisdvatsnq
      421 ksteqvrkvt aeqtaavaqm asaaqelsnl slelqsvvsr frlgka
//
LOCUS       WP_176065489             296 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176065489
VERSION     WP_176065489.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..296
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31809
     Region          44..232
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 msladkrrpa lgrgmaalls napapaptsa aaaaagkall alpveaiers peqprkrfee
       61 drleelaasi rehgvvepil vrrhgaryri vagerrwraa qraglkeipa ivreatpaqa
      121 fqialvenvq radlnaieea eayqalvdeh gltqeqvadk vgkerstvan alrllrlpgd
      181 vrdavregrl emgharallg leaaeairra aqrvlreqls vratealvre lagggkkrpt
      241 agatgdsaav raviarlqrr lgcrcrvvpk sdstgrleld ytsldeldgi lgkiga
//
LOCUS       WP_176065524             803 aa            linear   BCT 11-JAN-2025
DEFINITION  LPS-assembly protein LptD [Piscinibacter koreensis].
ACCESSION   WP_176065524
VERSION     WP_176065524.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444609
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..803
                     /product="LPS-assembly protein LptD"
                     /GO_process="GO:0015920 - lipopolysaccharide transport
                     [Evidence IEA]"
                     /calculated_mol_wt=88057
     Region          63..774
                     /region_name="LptD"
                     /note="LPS assembly outer membrane protein LptD (organic
                     solvent tolerance protein OstA) [Cell
                     wall/membrane/envelope biogenesis]; COG1452"
                     /db_xref="CDD:441061"
ORIGIN      
        1 mrpalttlaa algaagalaq tapdaagtap aaaapglaas gpaaaasaas apavaasgie
       61 lrtapslqap prgaagrqlp iivrarelsg rpdidavaeg dvefrrgttv ihadrltydr
      121 kddlaratgn vrisqdgnlf qgpelqlhve rfegffqspt yrfgatgagg tagridfleq
      181 travatdaty tscpadgsgd ppwllsaeri aidtdknegv arnavlrfyg vpilgapvls
      241 fplnderksg wlppnlgids rsgvqasipy ywniapnrda tftpslsskr gfgldtefry
      301 lepshageta lklmpydrlt gdsryalrtr heslfagdtl lqlrvrrvsd ddywkdfpde
      361 idsltrrllg sslslskpfg dwstyarvqr wqvlqtedpt triespyerr pqigaryqhn
      421 wnggfdvsfe teynrfanpd drylvnrhtg ervhalgsia rpfgsqgwvv tpklsfnaas
      481 ysldstptgg rrsasrfipt lsvdsswtle reatlfgrtl tqtleprlly vntpyrrqdd
      541 lpnfdaypkd fnvesiften vfsgvdrvsd ehqltagvts rfldpatgae tlrvgiaqry
      601 lfrdqritpd gepltrrfsn lllfgsgait srwnvdalvt ydpengrier svagvryspg
      661 pyrtigatyr ltrglleqve lgwqwpvyga drrqpngtla gaagscqgal ysvgrvnyst
      721 rdsriidslv gleydagcwi grvvaerrst grseantrlm mqlelvglsr igsnplgtlk
      781 dnipgyrmlr dekrtpspft pyd
//
LOCUS       WP_176065563             336 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Piscinibacter koreensis].
ACCESSION   WP_176065563
VERSION     WP_176065563.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..336
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=35628
     Region          28..336
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mirstrgaal alfaltaata aeaqtapsiy glldvsvarq rpaggrtayr ldsgnmtesf
       61 igirgsddlg gglraryqle sfvrvdqgsa grypgdgfws rdsfvglqga fgttllgrnt
      121 tpffmattsf npfgespgfs psvrqyygra llddrswsns lsytnnatdk dlkvnlayna
      181 aegspgstgs nvgasafyim gpvvlsgavq rvrnsplplp pgfdrqdawq igatwelqvv
      241 rlyaqggqvr teadtdvrtr llqvgasvpl grgsvlaafg haktraagar stdrsasvay
      301 dynlskstdl yaaylnerlt glstghglaa gmrirf
//
LOCUS       WP_176065564             214 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176065564
VERSION     WP_176065564.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..214
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23424
     Region          19..173
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdvkgsphrg rrsrreqgae etraalvsta rslfaargya dvsidditeg trvtrgalyh
       61 hfedkrelfr avveaverel tdevrrqgeg pggpweqlra aceayldacl rpevqriivl
      121 dappfltwrg wceidkrygl gvfegllgka rdaglletrs vetaaqlllg alntgarvva
      181 daadkaaarr svletierll agfwvgrpaa gqrg
//
LOCUS       WP_176065660             273 aa            linear   BCT 11-JAN-2025
DEFINITION  carbon-nitrogen hydrolase family protein [Piscinibacter koreensis].
ACCESSION   WP_176065660
VERSION     WP_176065660.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10166075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..273
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29563
     Region          2..264
                     /region_name="nit"
                     /note="Nit1, Nit 2, and related proteins, and the
                     Nit1-like domain of NitFhit (class 10 nitrilases);
                     cd07572"
                     /db_xref="CDD:143596"
     Site            order(40,96,113,117,128,153..154,156..157,178)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143596"
     Site            order(40,113,153)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143596"
     Site            order(114..115,134..136,154,157..161,163..164,186..187,
                     190..191,193..195,197..198,228,258..259,262..263)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143596"
ORIGIN      
        1 mkiaavqmvs tpdvdrnlea agrliaeaar agarlvalpe yfcliarsdg vkveiaeepg
       61 dgpiqrmlat aarehaiwli ggtlpirsad pervlnascv yapdgqlaar ydkmhlfrfd
      121 ngrerydegr vlcaggqpia fdadglrvgl svcydlrfpe lyrslmqppc dlitvpaaft
      181 httgaahwht llraraienq cyviapaqgg lhengrrtyg hsliydpwge llaevpegeg
      241 vavaeldpar iasvreqlpa lthrfpaalf aag
//
LOCUS       WP_176065663             433 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176065663
VERSION     WP_176065663.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 433)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468417
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..433
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45044
     Region          143..431
                     /region_name="LolE"
                     /note="ABC-type transport system involved in lipoprotein
                     release, permease component LolC [Cell
                     wall/membrane/envelope biogenesis]; COG4591"
                     /db_xref="CDD:443648"
ORIGIN      
        1 mwatlliaar nlvqhrrrsl llggalaavt alllllgaia tgaraamlqs attlltghvn
       61 vggfykprag aaspvlgrap evlaevrrlv peltfaaerg rgfgkaisdr aaldvvlagv
      121 dvsaetsfgr rlqmvtgdaa glahpgtlll fedqarrlgv gvgdavtlsa qtprgvrntv
      181 dlrvvavars agalssfvaf lpgedlrrlq qlgpgttgal hlflrdpaea pavaarlrag
      241 larvgwplvd adpqpywqkl egleaepwtg qrldvstwed elsflgwvfs alrgltgvlg
      301 vvlmgivvvg itntlwiair ertreigtlr aigmgrgqvl rlflaeaall alagaaagal
      361 aaaglaagld rlqlplpdal qillverhla laveplaalr gaavvvavtt laalypalra
      421 arlspvsamq hlg
//
LOCUS       WP_176065687             545 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176065687
VERSION     WP_176065687.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Ousalem,F., Singh,S., Chesneau,O., Hunt,J.F. and Boel,G.
  TITLE     ABC-F proteins in mRNA translation and antibiotic resistance
  JOURNAL   Res Microbiol 170 (8), 435-447 (2019)
   PUBMED   31563533
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Dean,M. and Annilo,T.
  TITLE     Evolution of the ATP-binding cassette (ABC) transporter superfamily
            in vertebrates
  JOURNAL   Annu Rev Genomics Hum Genet 6, 123-142 (2005)
   PUBMED   16124856
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422672
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..545
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59575
     Region          4..529
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
ORIGIN      
        1 mirldaiakq hgqqilflea satlqrgekv glvgpngagk stlfrlitre eqpdegqvsi
       61 drgvtighfs qdvgemagrt avaetmdgag pvsqvakelh dlelaladpe radelealve
      121 rfghvqarfd elggyalear areilaglgf spemmdgdvg alsggwkmrv alarillmrp
      181 dvmlldepsn hldlesiiwl eeflkafqga ilmtshdref mnrvvsrive idageltsyq
      241 gdydfyerer aiaerhqqaq fdrqqamlkk elafierfka rashaaqvqs rvkkldkiek
      301 veppktrktt vfefrpaprs gddvvkiagv skqygsrkvh dgldllvrrg erwcvlgang
      361 agkstllklv agavepdaga vavgasvkmg yfaqhamell spdqtvwdsl qeafprasvg
      421 slrslagcfg fsgdeiekrc rvlsggekar lvlahllydp pnflvldept nhldvgtkem
      481 lvqalagyqg tmlfvshdrr flaalsnrvl elgpegaraw gggyseyvas tgreapglra
      541 aavar
//
LOCUS       WP_176065676             383 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Piscinibacter koreensis].
ACCESSION   WP_176065676
VERSION     WP_176065676.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 383)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..383
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40390
     Region          30..344
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 msdvpasasp alsrrafgvd lgpprtptpl levrglhvaf gspaalpavd gvdlsidage
       61 vvgvvgesgs gksvsalavm glvddpgrva aerlafdgrd llglaptarr allgrdlami
      121 fqdpqgslnp aftveyqlve alrlheggsr ralrtralel lraveipdae rrlaayphql
      181 sggmaqrvml amaiacdprl liadepttal dvtiqaqmla llkrlqrerg malllithdl
      241 gviaevaqrv vvmyagqvve tapvdalfar phhpytaall aalpernagr rrlrtlggvv
      301 papherpagc llaprcayvr prcvaerpal fevedgraar cffplhtpha vppsrpeafd
      361 ghdagdpaap asrsdapaae aap
//
LOCUS       WP_176065709             267 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176065709
VERSION     WP_176065709.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..267
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28710
     Region          4..266
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 malkilvtak rvedpeskir vrpdgagivt egvnykvnpf deiaveealr lkekhggevv
       61 vasiggdkam teiraalamg aergllvrhd gpldpvivsa mlaklverek pdlvilgkqs
      121 idddqnqtgq ylaerlgwpq atfaskhdsl eseaeqkkqp glalaadgka lavvrevdgg
      181 vetlevvlpa vvttdlrlnk prfaslpgim kakkkevkel psaelgvdla pkvvirklse
      241 ppkrqggvkv advnelwakl hdeakvl
//
LOCUS       WP_176065711             318 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176065711
VERSION     WP_176065711.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..318
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=32105
     Region          3..318
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 manvlivaeq rggtlkkaty aalgagqala rrtggkltal vlgqgvgaaa kelqaygdvl
       61 vadgpalehg vadacapvia eaakqvqatf vgaaatafgk dvlpraaarl gaatatevlg
      121 fggdgaqvtf rrpmwagnvl aevelatpvk aftvratefp aaeraaapgq vtavgagaet
      181 grtrfvsfee vksarpelte arvvvsggrg tkgdfkevea ladelgaavg asraavdagw
      241 vpndwqvgqt gkvvapelyv aagisgaiqh lagmkgskvi vavnkdpeap ifqladyglv
      301 adlfkalpel rakvkaak
//
LOCUS       WP_176065724             851 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176065724
VERSION     WP_176065724.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 851)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 851)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..851
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..851
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=93163
     Region          60..849
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mippkapapr eqplgapapp ppppapparr rsllgrllag flvlvllaag aaalvglvay
       61 rrfasglpdi pslaeyrppv vtelvsadgq lagelfderr kvvpyeripk rlveallase
      121 dknffehggv dwlgtlraav ntyvlrhkvq ggstitqqta ksllvsaegf eegtkrnlrr
      181 klrelilarr leaafdkrei lwlylngvfl ghhsygvqaa aenyfrknve dltlaeaall
      241 aglpqapsky spfmhpdaak arrryvlrrm yeermisaee rvaaeetevr vypvddvfre
      301 tapfyaeqar rlivgrygdq rvlhdglrve lamdlerqrg aqaamlaglm evdhrqgfqg
      361 pvahvegqer dalrarlakv wpagalepgd yavgvvgevd draalarvsv gatqgllpia
      421 gmrwarrpnp eqsypdalis rpstalhagd vvlvrrvtre elvkrepper qklvpdaevl
      481 faleqepklq galvsiepft gyvsamvggy dfdasefnra fqacrqpgsa fkpivysgai
      541 eklnytpatl ltdapvvyrd esagvswkpe nyggsfkgev tlrdalvhsm nlpavkvaaa
      601 lgvdqlvswa aalgletpvk relgsaigss cttlwslanv yalldrygek rpstfvkrvl
      661 drdgrlledh saptdpwvpl strlaaaaaq vttpvervmd prsayitvsl lhevatvgtg
      721 aqaaklgkpa agktgttnds fdtwfmgmth dlfagvwlgy dhnemplgrf etggraalpi
      781 wlsymesslr drpqpdfpqp dgielvridp ttgklapegg rgvlepfkle akpvenppdq
      841 prvevqdlfg q
//
LOCUS       WP_176065725             196 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Piscinibacter koreensis].
ACCESSION   WP_176065725
VERSION     WP_176065725.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..196
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=21135
     Region          4..163
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 madrilvfyg syrsdragir ladylvagla argadvelid akaiglpmld rmykeypsge
       61 apaaletlaq kirgadafvf vtgeynwgpq pglknltdhf leeffwrpaa iasysagrfs
      121 gvrsgtawhs ilsemgmvvv sstlavgtis qsldadarpi gaggaaldra fprfaddlaw
      181 wteaareqka rkappy
//
LOCUS       WP_176065749             326 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Piscinibacter koreensis].
ACCESSION   WP_176065749
VERSION     WP_176065749.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455169
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..326
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35586
     Region          5..311
                     /region_name="PldB"
                     /note="Lysophospholipase, alpha-beta hydrolase superfamily
                     [Lipid transport and metabolism]; COG2267"
                     /db_xref="CDD:441868"
ORIGIN      
        1 mgqtaqlyvr eirpenssat ppavvfvhgs gtpaevsfds rmddyswmre varagfdvfs
       61 vsmtgyggst rpapmsnpcn iaraqqagyv papceptyrs plttmtsdwn dvgavvdyvr
      121 rlrgvdrvsl vawsqggprv tgyanlqptk vnrivvlapa ysrtgataep nplptlndgv
      181 msvqsrkdfi anwdrqvgcp nqydpaaatk ifdemlesdp vgakwgegar rapnvptwgf
      241 nqvtvsafkv pylmitgehd vqvpparvre lfqdlgsenk vlvdlacssh namweknray
      301 vydatiqflr dgkvngvsng vvrlay
//
LOCUS       WP_176065765             390 aa            linear   BCT 11-JAN-2025
DEFINITION  zinc-dependent alcohol dehydrogenase [Piscinibacter koreensis].
ACCESSION   WP_176065765
VERSION     WP_176065765.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Persson,B., Hedlund,J. and Jornvall,H.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the MDR superfamily
  JOURNAL   Cell Mol Life Sci 65 (24), 3879-3894 (2008)
   PUBMED   19011751
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Auld,D.S. and Bergman,T.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : The role of zinc for alcohol dehydrogenase structure and
            function
  JOURNAL   Cell Mol Life Sci 65 (24), 3961-3970 (2008)
   PUBMED   19011745
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Nordling,E., Jornvall,H. and Persson,B.
  TITLE     Medium-chain dehydrogenases/reductases (MDR). Family
            characterizations including genome comparisons and active site
            modeling
  JOURNAL   Eur J Biochem 269 (17), 4267-4276 (2002)
   PUBMED   12199705
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Lesk,A.M.
  TITLE     NAD-binding domains of dehydrogenases
  JOURNAL   Curr Opin Struct Biol 5 (6), 775-783 (1995)
   PUBMED   8749365
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Persson,B., Zigler,J.S. Jr. and Jornvall,H.
  TITLE     A super-family of medium-chain dehydrogenases/reductases (MDR).
            Sub-lines including zeta-crystallin, alcohol and polyol
            dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and
            other proteins
  JOURNAL   Eur J Biochem 226 (1), 15-22 (1994)
   PUBMED   7957243
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10169674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..390
                     /product="zinc-dependent alcohol dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0030554 - adenyl nucleotide binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42550
     Region          1..390
                     /region_name="FDH_like_1"
                     /note="Glutathione-dependent formaldehyde dehydrogenase
                     related proteins, child 1; cd08283"
                     /db_xref="CDD:176243"
     Site            order(38..40,43,86,170,174,193..194,196..198,217..219,223,
                     238,263..265,293,310..312,334..336,376)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:176243"
     Site            order(38,40,60,170)
                     /site_type="other"
                     /note="catalytic Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
     Site            order(90..91,93,96,104)
                     /site_type="other"
                     /note="structural Zn binding site [ion binding]"
                     /db_xref="CDD:176243"
ORIGIN      
        1 mralywngvn dlrvgtvrdp eivnphdail rvslsttcgs dlhfidgyip tmkagdvigh
       61 efmgviedvg srvtrirkgd rvvvpsfivc gqcwycrhnm yslcdnthpk pelqepllgg
      121 yhtagiygyt hafggyagah aqyvripfad ndcfkvpegv adetalflsd aaptgymgad
      181 fcdiqpgdtv avwgcggvgl maqqsarlmg aerviaidrf perlqmareh agsetidytq
      241 vdsvletlke mtggrgpdsc idavgmeahg tgpqyaydrv kqalrletdr gqalreaima
      301 crkggtlsvl gvyglidkfp mgaimnkgmt vrtaqqhgqa ymdrllahaq kgelnpayla
      361 thrfsledgp rgyemfkhkt dgcvravfap
//
LOCUS       WP_176065780             294 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease, partial [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176065780
VERSION     WP_176065780.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         <1..294
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
     Region          191..250
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 pdiaapdvrf yetataqevd grlrelaalr aewedlvgyc alavrksqly rllgfasfrq
       61 yceerlglaa rsieerakve errwaspalq eakreglpfe klrllsklpe peiarwaara
      121 kgltcvalrr elegeaerrm raqgrlavpl alrmaavlaa avqavrdrtg rplplgtcla
      181 vlaqhfldtw kggkrartrs rkvrerdegh cqvpgcsrra thahhvlfrs qgggdeldnq
      241 lglcafhhlr cihaghlrvv grapealrwf lggkawsgpe parrsgegve isaa
//
LOCUS       WP_176065803             651 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176065803
VERSION     WP_176065803.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..651
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=70238
     Region          1..649
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 maraveralg errylvaeag tgtgktlayl vpaalsgrkv iistatktlq eqiwqrdlpl
       61 laeragleve aaylkgrany yclergakfa erptfesrge aalwpriqew aratltgdrs
      121 eidlpdqyga wrelsasget clgkecqrhd ecfvtlarar aaqadvvlvn hhlffadlvl
      181 rtsragvevl ppydavifde ahalsevatd yfglsvssyr vddlardavr avadrpdlmr
      241 lvkdrtgele kagerffagv aarmgsspss kmrgrapsys plapgqpppa apalapwrga
      301 rgagpaargd lkvalsddll gplepdqarl dgaledvrev fadaeatala aigrraaelr
      361 velravttla epsrvhfaea rgrgvflrav pvdvaeelve rlyrrvdtav ftsatlaagg
      421 rldyfrrevg lapefdvdea ifpgpfdyar qaalvvpdgl pepaspafta aaaaavrelv
      481 avtggrafvl stsmrgmnal realadlpyq lllqgerpka klldafreep svlfatqsfw
      541 egvdvpgeal slvvidklpf apptdpvlaa rgqalaaegr dafselsvpa aalalkqgfg
      601 rlirtrrdrg lvavldrrlt tkgygrafla tlppapllrs veaarrwwag a
//
LOCUS       WP_176065831             521 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA carboxylase subunit beta [Piscinibacter koreensis].
ACCESSION   WP_176065831
VERSION     WP_176065831.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..521
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=55973
     Region          13..505
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mtsadtappp svhdaaldey rrreaaalam ggaaklarrk ekgvlnarer iaylcdagsf
       61 iesglfgtss snwsdqdktp adgkiagfgr idardvglvv ndftvmgass sttngrkigh
      121 mkevatrrgl plvflgessg arlpdtmgsr gmgallgnda tqyqrtretp wasatlgysy
      181 gssswygvls dfcvirkgav lavssallts latkeevdpe tlggwrvhae itgfadlvvd
      241 tdeqaldair tflsylpshh nelppvrpvp egsgadmati vrhlperrtq vydvrhivrt
      301 vvdagsffel karfgkvavt glarldgrtv givannpivk ggaldtdace kitsflvlcd
      361 sfnipvvtfv dtpgfvigad aerrrapgki mnmmnalqlm tvpkisvilr ksygqaylnm
      421 gggknsdeva awptaevsfm eprfavkvvh glepgdagfd ealeamnrgn tiwdaasmya
      481 vqsviepaat rdylirmldv hrsrrsggig ahrlanwpts f
//
LOCUS       WP_176065879             689 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176065879
VERSION     WP_176065879.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 689)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 689)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..689
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..689
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=72193
     Region          164..667
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mlsslkiahk vlasfgaala ltalaggvay tamsrvsqkl drsagvtvps lvalgecada
       61 hdramrglgc qlvtgtsqet rlacrqlaqe sfraideama rwleiphsqe vlqlqgawkp
      121 lyagwrahtd klserleard rlarddryde ardaelqasr efqlatealv saeaplreiv
      181 hitrrhased rsaggaasaa agvmllagfl ataglmallg wllarslght vaaldaeaqt
      241 vrdaveagal dvrgdeakvt pefrpivrgv navaqtftrr friisdymdk lshgelpell
      301 taevrgeyvv trdainrcvt avqrlvadme altnaslegr latradpgrh egdyrrvvag
      361 vnatleavla piqeasrvla rlaerdltar vtgkyageha aiqeainasa aaleaalaqv
      421 arsaqdlssa teqiasasqa vasgaseqas sieetssqle smtamirtag dgaaaaqgla
      481 qsakglsegg qqsmqrmgda mgkirasaes tsqiikdine iafqtnllal naaveaarag
      541 eagrgfavva eevrslalrs keaaskteal iqesvghaae gdrtarevae nlgritaevt
      601 kvagivaels easgeharav gqvtaameqm nkvtqqnaas seesssasse laaqaqelsg
      661 lvatfrlaag eepaasfapr paarpaara
//
LOCUS       WP_176065900             184 aa            linear   BCT 11-JAN-2025
DEFINITION  J domain-containing protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176065900
VERSION     WP_176065900.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422315
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..184
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=21078
     Region          20..163
                     /region_name="DnaJ"
                     /note="DnaJ-class molecular chaperone with C-terminal Zn
                     finger domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0484"
                     /db_xref="CDD:440252"
ORIGIN      
        1 mdiqlimeie qraaaldgld yfevlrlpre agaaevkaay yresrafhpd rfaalpspel
       61 relvgrvyrr vneaytvlrd dakrrkylad vsgperaakl rfteaeeaal qdeqkrklee
      121 qlgqtpngrk lyaqaladve aqrwdaaera lrsalmyepa narfkellar vekskpkvdp
      181 ykir
//
LOCUS       WP_176065930             149 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Piscinibacter koreensis].
ACCESSION   WP_176065930
VERSION     WP_176065930.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..149
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=15785
     Region          18..146
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 madtrsstsy patasgfrpe rwapeaqall rivsaylflq hgtakllhvp hvamfdnvql
       61 msltgiagli eivfgvllli glftrfsafi lsgemavayf mahaskgsvl vpmlnggela
      121 alycfvflff aaagpgawsv dgargrtla
//
LOCUS       WP_176065896             281 aa            linear   BCT 11-JAN-2025
DEFINITION  class II glutamine amidotransferase [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176065896
VERSION     WP_176065896.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Zalkin,H. and Smith,J.L.
  TITLE     Enzymes utilizing glutamine as an amide donor
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 72, 87-144 (1998)
   PUBMED   9559052
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Zalkin,H.
  TITLE     The amidotransferases
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 66, 203-309 (1993)
   PUBMED   8430515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000620
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..281
                     /product="class II glutamine amidotransferase"
                     /EC_number="2.4.2.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006541 - glutamine metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=30586
     Region          4..275
                     /region_name="YafJ"
                     /note="Predicted glutamine amidotransferase YafJ [General
                     function prediction only]; COG0121"
                     /db_xref="CDD:439891"
ORIGIN      
        1 mgallavlqt dpnllrcqvr rleahvalre pdrlpdaygf gyykgndvll gkrpsgapat
       61 ftltqlagai dseallahar yatvgaqkde nthpfrfrrw lfahdgtvea ftevkprlve
      121 alpdflrrnv egetdselaf slflkhlrda ghlddldvea rvvghalalt ardletwsre
      181 agggrpgaln fvatngrvla atrrgrplhy allegifpcp rcglelgape sdprtrphrq
      241 vkavcfathl lqpngfievp easvvsvsrs lqvsvsslas a
//
LOCUS       WP_176065967             250 aa            linear   BCT 11-JAN-2025
DEFINITION  (Fe-S)-binding protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176065967
VERSION     WP_176065967.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..250
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=27798
     Region          <3..246
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mltvglfipc yieqlypevg latvrvlerh gvrveypedq tccgqpmsnt gcteearpla
       61 ekflrlfrgy ehvvapsgsc vsmvrnhydg flagqpgfdh lkrstwelce flvdvlklpr
      121 legafphkvg lhqschglre lrlgsgserr vapfnkvqll lselrglqlv elarqdeccg
      181 fggtfavqee avscmmgrdr ladheragae ivtgvdmscl mhldglirre rrplqvlhva
      241 qlldraeaaa
//
LOCUS       WP_176066004             239 aa            linear   BCT 11-JAN-2025
DEFINITION  STAS domain-containing protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176066004
VERSION     WP_176066004.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Sharma,A.K., Rigby,A.C. and Alper,S.L.
  TITLE     STAS domain structure and function
  JOURNAL   Cell Physiol Biochem 28 (3), 407-422 (2011)
   PUBMED   22116355
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The STAS domain - a link between anion transporters and
            antisigma-factor antagonists
  JOURNAL   Curr Biol 10 (2), R53-R55 (2000)
   PUBMED   10662676
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..239
                     /product="STAS domain-containing protein"
                     /GO_function="GO:0043856 - anti-sigma factor antagonist
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=25482
     Region          10..92
                     /region_name="STAS_anti-anti-sigma_factors"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist) domain of anti-anti-sigma factors, key
                     regulators of anti-sigma factors by phosphorylation;
                     cd07043"
                     /db_xref="CDD:132914"
     Site            order(22,24..26,32,55,57..59,61..63,66..67,86,90..91)
                     /site_type="active"
                     /note="anti sigma factor interaction site [active]"
                     /db_xref="CDD:132914"
     Site            58
                     /site_type="other"
                     /note="regulatory phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:132914"
     Region          127..>183
                     /region_name="MlaE"
                     /note="Permease MlaE; cl00510"
                     /db_xref="CDD:469798"
ORIGIN      
        1 mgrgeverwe gdggvvlrpp eeldrshlel lwtaasralr rsprrivldl egvtplgagg
       61 valvrelehr cqrrgvvaga spaasaflef vrgrspdrpr apharrtpga vplarkaara
      121 rdalrafvef vgrftasagh laarpgelrv hdalyqlqra gadgmwligg lsvllgvima
      181 fqgpqattde aaafaramsg vvsrlstrvr hdlcavagda araergarre dpsdaaegr
//
LOCUS       WP_176066006             467 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Piscinibacter koreensis].
ACCESSION   WP_176066006
VERSION     WP_176066006.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..467
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48737
     Region          25..462
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mrdritdsat aarpldtlap ppsaslglah avaiivgivi gagifkapsl vagnvpstgw
       61 lfavwalggl fslagalcya elsatypsrg gdyhflsraf gkstaltyaw arfsvvttgs
      121 lallgfvfgd ymsqllplgp hgsalyaava vvvltavnlr girngataqa wltavevggl
      181 vlivvaglwl wlgapaaapa pvvappgsas assiglamvf vlltyggwnd aayisadlrq
      241 rrsimralvl svgvitvlyl lvnwaywhal glagmarsea iatdvltaaf gpaagkavav
      301 mvavsaltsm natlivgart agalaqdwpq lrilaawdda rgvprnsfla qagfalvlia
      361 igaayqsgfr amveytapvf wlffllvgls lfklrvqepd qprpfkvply pltpavfclt
      421 saymlwssls yvrsqqlggi naawvgvavl vsglvllivf rrgtrtt
//
LOCUS       WP_176066060             388 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Piscinibacter koreensis].
ACCESSION   WP_176066060
VERSION     WP_176066060.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475854
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..388
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=43530
     Region          9..372
                     /region_name="BcsL"
                     /note="Acetyltransferase involved in cellulose
                     biosynthesis, CelD/BcsL family [Cell motility]; COG5653"
                     /db_xref="CDD:444374"
ORIGIN      
        1 mkttrpsdaa lrirvvdddi gfrgleagwn alaargggsv fmrhewhaaa wawrrldadl
       61 liicahgadd dlvgvlpllr praasrtlef lavpdaqwcd vqtdptrafa vceaiahall
      121 diastwdvlr fdrlapdsll qrallpalka reatwrlaad dcnlyvdlrg twdayhaers
      181 rklkkafnla snrlarigtv eiecidtaah dvrraqaafd eavgisrrsw khttstgleq
      241 pgplafmrql tdvafangwl slwllrvgge piameyqlvy rrcvhalrad fdethqhasp
      301 gtylnrevir rlfdgrhdry ylgpgrnayk rywsvtgdav ysaavfapta rgralalwsg
      361 lkptlrmlrn ritagkpefd peydlpml
//
LOCUS       WP_176066086             262 aa            linear   BCT 11-JAN-2025
DEFINITION  uroporphyrinogen-III synthase [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176066086
VERSION     WP_176066086.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Schubert,H.L., Raux,E., Matthews,M.A., Phillips,J.D., Wilson,K.S.,
            Hill,C.P. and Warren,M.J.
  TITLE     Structural diversity in metal ion chelation and the structure of
            uroporphyrinogen III synthase
  JOURNAL   Biochem Soc Trans 30 (4), 595-600 (2002)
   PUBMED   12196144
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..262
                     /product="uroporphyrinogen-III synthase"
                     /EC_number="4.2.1.75"
                     /GO_function="GO:0004852 - uroporphyrinogen-III synthase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006780 - uroporphyrinogen III
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0006782 - protoporphyrinogen IX
                     biosynthetic process [Evidence IEA]"
                     /GO_process="GO:0033014 - tetrapyrrole biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=26112
     Region          5..237
                     /region_name="HemD"
                     /note="Uroporphyrinogen-III synthase [Coenzyme transport
                     and metabolism]; COG1587"
                     /db_xref="CDD:441195"
ORIGIN      
        1 mapslagrrv avtrgaggdd plarrlrqlg aevleapaia lappgsfael daalrdlgat
       61 dwiafasanc vertlaraae lgvaaaalar prlaavgrat aaqlarlvrp pdlvpgearg
      121 ealaaalapq vrglrvlvpr aeegrpelve glvaagatvv appayrtvpa ppealaelaa
      181 alaqgavdav afaspsavrs vaaalgagrd llgraalaai gpttaaelql lgftrvvqpl
      241 rasaealaea iaeqlgpgrq qp
//
LOCUS       WP_176066124             498 aa            linear   BCT 11-JAN-2025
DEFINITION  SpoVR family protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176066124
VERSION     WP_176066124.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006558
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..498
                     /product="SpoVR family protein"
                     /calculated_mol_wt=59393
     Region          1..496
                     /region_name="SpoVR"
                     /note="Stage V sporulation protein SpoVR/YcgB, involved in
                     spore cortex formation (function unknown) [Cell cycle
                     control, cell division, chromosome partitioning]; COG2719"
                     /db_xref="CDD:442032"
ORIGIN      
        1 msqknthlpa hlhdirqqve gyargygldf ydtvfevlgf deinmvaayg gfpnryphwr
       61 fgmdyerlsk gyeyglskiy emvinndpsy ayllesnmdv dqklvmahvf ghvdffknnf
      121 mfrhtnrkmm dqmanhatrv rryqdelgve kvedfidrcl sienlidyqs pyvrrhadkk
      181 leaeqqphva kgfktgreym reyinppefm raqqerieqd lqrqkkvper perdvlqfll
      241 ewaplerweh dvlsiireea yyfapqgqtk imnegwatyw hstimtqkal taaelidyad
      301 hhsgtlathp gqlnpyklgv elwrdiedrw nkgrfgkeyd dcdsfeerrr wdrklgagrq
      361 kifevrkhyn dvtfideflt lefcvdqqlf tfgynekhqr weiverefrk vkdkllhmlt
      421 nfgqpiiave dgnyenrgel llihkhdgvd lkvdyardtl rnlqslwrrp anliskldgr
      481 gvifrfdgrd hsdkkidl
//
LOCUS       WP_176066133             235 aa            linear   BCT 11-JAN-2025
DEFINITION  histidine phosphatase family protein [Piscinibacter koreensis].
ACCESSION   WP_176066133
VERSION     WP_176066133.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Rigden,D.J.
  TITLE     The histidine phosphatase superfamily: structure and function
  JOURNAL   Biochem J 409 (2), 333-348 (2008)
   PUBMED   18092946
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10447784
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..235
                     /product="histidine phosphatase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25069
     Region          12..205
                     /region_name="His_Phos_1"
                     /note="Histidine phosphatase superfamily (branch 1);
                     pfam00300"
                     /db_xref="CDD:459751"
ORIGIN      
        1 massdeptlt rviairhget awnadarmqg hldiplnetg rwqarrlaav ladagidviy
       61 tsdlsraret aeivaaaagc plrvdaalre rcfgvfegha freiearwpd daarwlrrdt
      121 dfapsgaetl vdfcarttga atriaaahag qtiaivahgg vldclyraat rvdlqaarsw
      181 qlgnaainrl lhtaqgftlv gwgdvqhlda paldesndgs alarpgqqvr aaggr
//
LOCUS       WP_176066144             294 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Piscinibacter
            koreensis].
ACCESSION   WP_176066144
VERSION     WP_176066144.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 294)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..294
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30959
     Region          9..294
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mnpfdipiqa flgqlllglv ngsfyamlsl glavifgllg ivnfahgaly migayvgfvl
       61 lenfgvnywl alviapllvg vlgvvierll lrhlyhvdpi ygllltfgla liaegvfrsq
      121 fgvsgqsypv pellqgatdl gfmilpnyra wvvvaslavc lgtwyliert plgatlragt
      181 enpklvqafg invprmvmlt yaagaglaal agvlaapviq vnplmgsnli iivfavvvig
      241 gmgsilgsii tglalglveg ltkvfypeas sivvfvimai vlmirptglf gkea
//
LOCUS       WP_176066156             337 aa            linear   BCT 11-JAN-2025
DEFINITION  PhoH family protein [Piscinibacter koreensis].
ACCESSION   WP_176066156
VERSION     WP_176066156.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Kazakov,A.E., Vassieva,O., Gelfand,M.S., Osterman,A. and
            Overbeek,R.
  TITLE     Bioinformatics classification and functional analysis of PhoH
            homologs
  JOURNAL   In Silico Biol 3 (1-2), 3-15 (2003)
   PUBMED   12762842
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..337
                     /product="PhoH family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=36574
     Region          2..335
                     /region_name="PhoH"
                     /note="Phosphate starvation-inducible protein PhoH,
                     predicted ATPase [Signal transduction mechanisms];
                     COG1702"
                     /db_xref="CDD:441308"
ORIGIN      
        1 milrhafipp dnqrlahlcg sldehlrtie aaldvrivrr nesfrvegtk ahaeravall
       61 qdlygraqrp isaeevelgl mealadeaap rrekkprlal agnggdaraa egapaesriv
      121 lqtrrsgltg rtpnqhdylr niiehdvtfg igpagtgkty lavacavdal erstvqriil
      181 trpaveager lgflpgdlsq kvdpylrply dalyelmgie rvgkafekgt ievaplafmr
      241 grtlnhafvi ldeaqnttpe qmkmfltrig fgakavvtgd isqidlprga vsglvdaerv
      301 lrnvkgiatt hftaadvvrh plvakivday aaasrgd
//
LOCUS       WP_176066168             212 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Piscinibacter koreensis].
ACCESSION   WP_176066168
VERSION     WP_176066168.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789896
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..212
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21967
     Region          10..206
                     /region_name="COG2945"
                     /note="Alpha/beta superfamily hydrolase [General function
                     prediction only]"
                     /db_xref="CDD:442188"
ORIGIN      
        1 mnprtvrqai agpagaieca idvpggaprg iavlchphpq qggtldnkvv qtlarafvql
       61 gwrsvrfnfr gvggsagswd agvgevddaf avlqafrnda agapqpyalg gfsfggfvaa
      121 avtermgedr pqrlvlvgps tqkqqvppvp adtvvihges deivplgatl dwarpqalpv
      181 vvipgvghff hgslpllksv vlrelhelgp aa
//
LOCUS       WP_176066338            1028 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176066338
VERSION     WP_176066338.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..1028
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=109136
     Region          1..1005
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mspiktfisr pvftgmltlv vlvfgvvayp rigvdqlpev efpvvtvttv lpgadpeaie
       61 rtvtkpleea lntlsgldtl rsvnvenvsq ivvrfdlern vdvaaqdvrd rvqatlsklp
      121 keidtpvvek fdigaapvat lalsaplpve rltqltddvv kpalqqvpgv gavevvggrk
      181 reitvvpdpr llrgyglsps dvvqalraqs idvpggrtle pgversvkla aearsvealr
      241 alviaspggt plrlgqvaqv ldgpaearsv arlgdrsalg lvvrkqsgsn tvevterlee
      301 slsrlqgqlp pgsevkvvvd gakfirssid avkedmilgg vlavvvvllf lrnwrstlva
      361 avalptsiig tfavmhalhf tfnvitmlal tlsigllidd aivvienivr hleegqspwe
      421 aarrgtgeia lavlavtlav vavfvpvafm egimgrffyq fgvtvavavl isyavsmtlt
      481 pmlsarllre hahpgrasra iegvlraiea fyrralgaml shraltlava savlvltvll
      541 agrlkftfmp sqdmsqvkvt lelpsggtld etrrqlddls rqiravpgvt etfavagaga
      601 qeevhkgeit vnlvpvarra ygqeafkqhl rrtlrvspaa klsvqdfalv agggsrpqqv
      661 qlnlrstdfd alltavektr qamlsnpgfv dvdttwrsgk pqlevvvdre raaalgvpaa
      721 lvgqnvralm ggdkvadfhe ggdsydvkvk lpadvladpa algavpvrap ggqlvelrsl
      781 asivpavgps qiehqaqmrq vtlladlrgy slgegmsylt afaqkelpkg vqfdfegqgr
      841 elgragkafl qalllgivli yiilaaqfes lvhpftimms lpfaviggia glllanqyls
      901 mmamigfiml mglvtkngil lveftnqlra agrstreall eagpirlrpi lmtsvamiag
      961 mipvalaqgd gaetrvpmav aiigglvtst altlgvvpvv yasldalrar larrggraap
     1021 aapadlaa
//
LOCUS       WP_176066396             194 aa            linear   BCT 11-JAN-2025
DEFINITION  superoxide dismutase [Piscinibacter koreensis].
ACCESSION   WP_176066396
VERSION     WP_176066396.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..194
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=21461
     Region          4..191
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mehtlpplpy shdalaphls retleyhhdk hhnayvvnln nlqkgtefen mdleaivkks
       61 sggiynnaaq vwnhtffwnc mkpggggapt gpladainak wgsydafkea ftksavgnfg
      121 sgwtwlvrkd dgavdivnmg aagtplttgd kalltidvwe hayyidyrnl rpkfvetfla
      181 slvnwdfatk nyaa
//
LOCUS       WP_176066406              67 aa            linear   BCT 11-JAN-2025
DEFINITION  Trm112 family protein [Piscinibacter koreensis].
ACCESSION   WP_176066406
VERSION     WP_176066406.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   van Tran,N., Muller,L., Ross,R.L., Lestini,R., Letoquart,J.,
            Ulryck,N., Limbach,P.A., de Crecy-Lagard,V., Cianferani,S. and
            Graille,M.
  TITLE     Evolutionary insights into Trm112-methyltransferase holoenzymes
            involved in translation between archaea and eukaryotes
  JOURNAL   Nucleic Acids Res 46 (16), 8483-8499 (2018)
   PUBMED   30010922
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Bourgeois,G., Letoquart,J., van Tran,N. and Graille,M.
  TITLE     Trm112, a Protein Activator of Methyltransferases Modifying Actors
            of the Eukaryotic Translational Apparatus
  JOURNAL   Biomolecules 7 (1), 7 (2017)
   PUBMED   28134793
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006712
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..67
                     /product="Trm112 family protein"
                     /calculated_mol_wt=7269
     Region          1..59
                     /region_name="Trm112"
                     /note="RNA methyltransferase activator Trm112/YbaR
                     [Translation, ribosomal structure and biogenesis];
                     COG2835"
                     /db_xref="CDD:442083"
ORIGIN      
        1 meprlldllv cpickgplrh arpplhdree licnadrlay pvrdgipvml esearstdep
       61 atsapgp
//
LOCUS       WP_176066420             320 aa            linear   BCT 11-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Piscinibacter
            koreensis].
ACCESSION   WP_176066420
VERSION     WP_176066420.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..320
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=32224
     Region          87..291
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mpprapfrar lvplvllaat agvlaappai aqpavagsda aasapaapss aasaasaava
       61 apasavvaar pasaaaprre tvenpyglga lirhgdaial gtlvilllms igswtiivtk
      121 lvqsvrlare arvaprqffr artlgeatqa lgagsafrai adagitaseh hegaltenid
      181 rntwvgmnvq rslddvqsrl qdglaflatv gstapfiglf gtvwgiynal taigvagqas
      241 idkvagpvge alimtalglf vavpavlgyn wlvrrnkvtm esvrrfgadl hgvlmgapia
      301 atttaasaga apapasttpr
//
LOCUS       WP_176066438             247 aa            linear   BCT 11-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176066438
VERSION     WP_176066438.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 247)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 247)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 247)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..247
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25665
     Region          14..242
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mlpeaprftr gneflsgcrd elpillgvap fgmiygllal saglpvavaq gmssivfags
       61 aqfiaaqlih drapggvivl tvlvvnlrha lysaslapyv rplgrgwkag laylltdeay
      121 avavtrylrd egrsdvspyr hwyflgaglt lwlawqwsta vgifvgarvp aswsldftla
      181 ltfialvvpa lkdragvaaa laagalaiag aalpyklglp laalggvlag lgaealrrep
      241 stagraa
//
LOCUS       WP_176066449             225 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Piscinibacter
            koreensis].
ACCESSION   WP_176066449
VERSION     WP_176066449.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..225
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=24207
     Region          13..164
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mprgrapgya mqreqilana aklfarqgft atsmnqvada cgvskpalyh yvddkhqllv
       61 eiaanhvdrl lgliaeveaa glapepmlra lierflalya dtqaehqvlt gdvrfleppe
      121 rervldgqrr vvaafaaalv rvvpelrdar letpvamllf gmmnwtftwl qphgrlthad
      181 vapliadlll ggvgsiealg appatpstap rakarsrtpp aakaa
//
LOCUS       WP_176066488             293 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Piscinibacter
            koreensis].
ACCESSION   WP_176066488
VERSION     WP_176066488.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..293
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30483
     Region          4..293
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mleqqlvnal slgcvyalfa lgftlvfgvl gvinlahgav fmvgayaale avtrlalplp
       61 lamlvallvs gvigllidvl vlrplrnrna phlipmiati giaiflnsaa qgmfgaenqr
      121 fapevlptes fqigavhvsv ielliiglsf almaalfvlm nrtqtgralr aiaespkaaa
      181 llginveglf rltsfaaaal ggvggvlial ysnavfpmmg qpmlhkgiav iilggmgdir
      241 galvgglflg faevlavayi gstmrdaiaf gllfivlllr pqglfgkvle rka
//
LOCUS       WP_176066489             254 aa            linear   BCT 11-JAN-2025
DEFINITION  YdcF family protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176066489
VERSION     WP_176066489.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003674
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..254
                     /product="YdcF family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=26751
     Region          46..253
                     /region_name="ElyC"
                     /note="Lipid carrier protein ElyC involved in cell wall
                     biogenesis, DUF218 family [Cell wall/membrane/envelope
                     biogenesis]; COG1434"
                     /db_xref="CDD:441043"
ORIGIN      
        1 mfltlsklld llvapltwal alalgaalar arpararala aagaavlylf siepvatllm
       61 aaveaparst yrpevvydav vvlsgevdaa aarrsgrlel tegadrlvaa yellrggrar
      121 aallsggsaf pvpgerseae lvaatlrgwg iapdrlvveg asrntrenav eaarvagarg
      181 wrslllvtsa fhlpralgcf rrvglspdal pvdaragdgr rrswlprasa lgqstealre
      241 wtgrlvywam gyta
//
LOCUS       WP_176066502             327 aa            linear   BCT 11-JAN-2025
DEFINITION  inositol monophosphatase family protein [Piscinibacter koreensis].
ACCESSION   WP_176066502
VERSION     WP_176066502.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Atack,J.R., Broughton,H.B. and Pollack,S.J.
  TITLE     Structure and mechanism of inositol monophosphatase
  JOURNAL   FEBS Lett 361 (1), 1-7 (1995)
   PUBMED   7890024
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10108155
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..327
                     /product="inositol monophosphatase family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0008934 - inositol monophosphate
                     1-phosphatase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006020 - inositol metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34964
     Region          8..251
                     /region_name="IMPase"
                     /note="inositol monophosphatase and related domains. A
                     family of Mg++ dependent phosphatases, inhibited by
                     lithium, many of which may act on inositol monophosphate
                     substrate. They dephosphorylate inositol phosphate to
                     generate inositol, which may be recycled...; cd01639"
                     /db_xref="CDD:238817"
     Site            order(38,42,48,71..72,89..94,216..217)
                     /site_type="active"
                     /db_xref="CDD:238817"
     Site            order(41,43,95..96,98..103,155..157,159,161..162,170..171,
                     174,177..178,180,185..191,199,203..206)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238817"
ORIGIN      
        1 msqalhpmln taikaarsag tiinrasldl drlqinrkap ndfvtevdha aeaaiietll
       61 gaypghgina eesgrthgts sseyvwiidp ldgttnflhg fpvyavsial afrgqvqqav
      121 vydparndlf yaskgrgafl ndkrirvskr trladcllgt gfpfrrgdnf qrylkmmevm
      181 mplcaglrrp gaaaldlcyv aagwydgffe tglkpwdmaa gslmiteagg lvgnftgnad
      241 flergevlaa spriygqlvq llspftsvvn eeaaappeaa raaeltpeaa lgavlddtar
      301 papaaaeapa apklkppvri rkvpape
//
LOCUS       WP_176066518             420 aa            linear   BCT 11-JAN-2025
DEFINITION  RsmB/NOP family class I SAM-dependent RNA methyltransferase
            [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176066518
VERSION     WP_176066518.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414805
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..420
                     /product="RsmB/NOP family class I SAM-dependent RNA
                     methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /calculated_mol_wt=44490
     Region          <129..419
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
ORIGIN      
        1 mtfasearla avpwralqgl apaldaplaa vlasepaerv vdrflrahre lpaearaaak
       61 eaiygvavwr rrlgwhagae vpeasqplcp tggkgrergp srlllaalvr dlggvagaee
      121 llelrpgtlp pprpppddpa irfsfpdwlw aamerelgpe aprladaldl pgpvclrpng
      181 lrttpaalaa rlaaegvata pgrlapsall vtsprpnvyg laawreglle vqdeasqlag
      241 alvearpgee lldlcagagg ktlllaaava pggavdacdl dperlrrlse rarragagel
      301 vrvagaappa gatydaalvd apcselgalr rgpdqrfrld paafaplpgl qlgllaraav
      361 rvrpggrlvy atctfrreen eevaeafera hpafareawr rtwphrdgad affvarwrrg
//
LOCUS       WP_176066634             128 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176066634
VERSION     WP_176066634.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..128
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14500
     Region          5..126
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mrlafhhlav qcadlaacer fyrevlelev vrrwpredgq dravwlgvgd gflalerade
       61 ppppsgfrsg rgglhllalr iapaerarwe arlaelrvpv vhrtrwtlyl rdpegnrigl
      121 shhpddap
//
LOCUS       WP_176066576             298 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176066576
VERSION     WP_176066576.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32682
     Region          7..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..297
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(110..111,113..114,117,121,123..129,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mewlnyhhll yfwtvarngs iarageelrl sqptlstqik kleetlgvkl ferqgrrlvl
       61 tdvgrtvqry adeifrtgre lqlavkglpt gqrprlaagv advipkimae lllrpaleav
      121 pdltlacreg plpqlmaals lheldvvlsd tpaaetqvka fshplgesgv sflaepqlaa
      181 glrrrfprsl dgapallpar gtalrrdlea wfegegvrpl avaefddtal ltafgrrglg
      241 ffaaptviaa evcaqlrvap vgraeevrer yfavsverrl rhpavvalad aarsrtfr
//
LOCUS       WP_176066712             370 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Piscinibacter koreensis].
ACCESSION   WP_176066712
VERSION     WP_176066712.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..370
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38114
     Region          1..368
                     /region_name="LhgO"
                     /note="L-2-hydroxyglutarate oxidase LhgO [Carbohydrate
                     transport and metabolism]; COG0579"
                     /db_xref="CDD:440344"
ORIGIN      
        1 mdrvdalvag agvvglaiar alaergleti vverealigs gvssrnsevi haglynppdw
       61 lktrlcvagr eqlyayceag gvgharcgkl vvatlpeqvg alreiaaraa angveglawv
      121 daaglarlep alhavaalhs pvtgivdsha lmlallgdle raggslalqt pveavarsad
      181 gfvvrtggaq gfelatrvfv naaglgatel atrieprsas iprlflakgn yfglagrapf
      241 grlvypipep gglgvhltld lagqarfgpd vewltgdpaa ldyavdpara apfyrairaf
      301 wpdlpdgalq psysgvrpkl sgpgqpardf mlqgpgehgv aglvnlfgie spgltaclai
      361 adavverlgi
//
LOCUS       WP_176066690             361 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Piscinibacter koreensis].
ACCESSION   WP_176066690
VERSION     WP_176066690.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..361
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38276
     Region          10..313
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 msephapiet dalivgagpv glfqvfqlgl levrahvvdt lpfvggqcie lyadkpiydv
       61 pglpvatgre lierlvtqia pftaplhlgq qvdrvavrgd grfdvetsag trfvataviv
      121 aggagsfqpr tlklegldrh rgsqvfyrrp daahlagqrv liagggvdav elatslasds
      181 gnrpaeivlm hrrddfsagp eplarlaelr qarrirvvvg qpnglveagd rlvaleallp
      241 dggdawiafd tlvialgvsp klgpiadwgl giqrkqvtvd terfqsttpg ifavgdinty
      301 pgkrklivsg fheatlaafa aaaivhpdra lplqytttsp rlhrllgvdg adgerprdpp
      361 a
//
LOCUS       WP_176066728             178 aa            linear   BCT 11-JAN-2025
DEFINITION  methylated-DNA--[protein]-cysteine S-methyltransferase
            [Piscinibacter koreensis].
ACCESSION   WP_176066728
VERSION     WP_176066728.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Margison,G.P., Butt,A., Pearson,S.J., Wharton,S., Watson,A.J.,
            Marriott,A., Caetano,C.M., Hollins,J.J., Rukazenkova,N., Begum,G.
            and Santibanez-Koref,M.F.
  TITLE     Alkyltransferase-like proteins
  JOURNAL   DNA Repair (Amst) 6 (8), 1222-1228 (2007)
   PUBMED   17500045
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Tubbs,J.L., Pegg,A.E. and Tainer,J.A.
  TITLE     DNA binding, nucleotide flipping, and the helix-turn-helix motif in
            base repair by O6-alkylguanine-DNA alkyltransferase and its
            implications for cancer chemotherapy
  JOURNAL   DNA Repair (Amst) 6 (8), 1100-1115 (2007)
   PUBMED   17485252
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11417447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..178
                     /product="methylated-DNA--[protein]-cysteine
                     S-methyltransferase"
                     /EC_number="2.1.1.63"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003908 -
                     methylated-DNA-[protein]-cysteine S-methyltransferase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=18705
     Region          16..172
                     /region_name="AdaB"
                     /note="DNA repair enzyme Ada
                     (O6-methylguanine-DNA--protein-cysteine methyltransferase)
                     [Replication, recombination and repair]; COG0350"
                     /db_xref="CDD:440119"
ORIGIN      
        1 msfaidfvrg gcsaqarhas plgsillart prglagawfe gqkhhpptfd aptnpddpll
       61 rtaiqqlaey fagsrsrfdv aldaagtpfq ravwavladv epgrtcsyae varrvgrpsa
      121 vravaaaigr nplsiivpch rvvgsdgalt gyaggidrkt allalerqrf gedggras
//
LOCUS       WP_176066809             250 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Piscinibacter koreensis].
ACCESSION   WP_176066809
VERSION     WP_176066809.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..250
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=28076
     Region          13..128
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
     Region          <78..117
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mgamehvgei adttieltdr ererlartae mlpadaatcl eigfkdqrvs silarydlvs
       61 idlpgeapas ithplafati aalpfrdqsf dlavctevle hleddvledg vaelarvsrr
      121 hvlvsvpnrq rvwnelskcp scgyvvnamg hlhhfdearl eqlfpafrpv ryamagsteg
      181 yapdwlywlr trvgnawhpc twgcfrcgst tpspppnlig klaqrivwrw earaprrpaf
      241 lfvllerkdv
//
LOCUS       WP_176066822             251 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Piscinibacter koreensis].
ACCESSION   WP_176066822
VERSION     WP_176066822.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..251
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28570
     Region          11..185
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(11,13,98)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(44,97..98)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            96..98
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 msdlsvslff paykdertir tvveeglrll rgyasefeil vvddgspdrs gaiadelaae
       61 hpgivraihh pqnrgygaal rtgvaaarye wicmvdgdne yavsdlrkml evrhfyrlii
      121 afrykklyst nrifisfvyn lvlrrlfrtp frdvstgirt fhrsilddie ltsnspfiga
      181 elaiktmlrg ypvgelgiqt fprtfgrgsa tsmknirrti ddmlrvrrem fsdhyhlpsg
      241 rsrqprslsg g
//
LOCUS       WP_176066835             742 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176066835
VERSION     WP_176066835.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..742
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=80604
     Region          32..506
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mavpaalvse tlstlpgddv rsvmwrlegr ydlqmliqsv rqvargpvar lvaegarssh
       61 dwteqknall ehydacgatg vfmephqggf legpknlama lvafelawvd agaatgalag
      121 hlglspiher gtqeqqdrym slsapaapge drkpwrgafa ltepipyvgv dtgmlggkvs
      181 varwepgqep vlkvekrgrf itnmgfanfv taavdsader ikgtcmvile egdpgtfdrg
      241 tptkklvhql sstsdpifsl evpasrivgg ysvkdgvivp rwshdeiiaa vfkhtrvpvg
      301 vmtaakllsa vepviryqrg rfrgaqqarp gsprydlglq vredvlhrlv dvwatgeaaa
      361 slgfstsrlf deldplekvk fqtlqekgit graelryfkd vnaravelvk lrakpeaerd
      421 aarvaelead plvryailds agavlcpatk lwntghgatv mreavalmgg ygitedcpgf
      481 lghkwmdaql eatyegpeav qrrqlsvcmq nevflaqlda wtkelrhias erpdtgacnl
      541 asafvlwryt ydhlqvatda tgqklyqgpr qgvtfalsda lawlmaarsl vldvveleqk
      601 gaenavlaeg lpglvrfyqd lshvqcaras gevgricael vygynkhpew nadaqqacwe
      661 areldeledl ipgigscakd vieaggghpd kagpcahcss vadfaalrmk ldqcltgarl
      721 akdraaeals kvmipealdy pv
//
LOCUS       WP_176066841             230 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Piscinibacter koreensis].
ACCESSION   WP_176066841
VERSION     WP_176066841.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465536
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..230
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.-.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25715
     Region          118..195
                     /region_name="COG3393"
                     /note="Predicted acetyltransferase, GNAT family [General
                     function prediction only]"
                     /db_xref="CDD:442620"
ORIGIN      
        1 mlsklralfg elgvgagsvy lldrvlrkis hrcgvylyel vvqpigdkpl lpprlsknir
       61 fheiaehdad mqrllarpei kvsrfaqgav clgvyrldvl ighvwfcfgr yeedevrcdf
      121 rlpapgdawd fdlyvfpehr mgigfmavwd aafaylrerg varsfsrvnr fnlasrraha
      181 rlgsrpvgsa lfvklghtel tlssaapfvg ltrrrrlalq vpnpgpaaaa
//
LOCUS       WP_176066840             344 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176066840
VERSION     WP_176066840.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..344
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35663
     Region          3..343
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 metilflsht epdgalpraa lealtaaral aqgtkgqlvl gvfgaetaga aaqlagagaq
       61 ralavtspel aaaryasdaa aaealaraag atvvvapsts rlarvlagvs hrlggkidth
      121 atgvaaqdga ptvtrwfyrq rmeatlrraa rpwfvtvdag tqpafraega apaleavpla
      181 ladaqrrtrv tgfrapeaqa qtirpdakll fvagagwtkk qadgkphldq aeqlilgflg
      241 kakaslgssk smtdlategh gvmgfmthln qvgqtgstpr hakglatcch geephvvgwr
      301 finerravnl dpncgwargk advvyvadaf avmekvnall asrg
//
LOCUS       WP_176066888             260 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176066888
VERSION     WP_176066888.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..260
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27262
     Region          4..240
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mlaietrglt rlfdgkpavq elalavpaga fygflgpnga gksttmrllt gllaptsgea
       61 rvlgldvaas plavkaqlgv vpdglslfer ltgeeqlrih gqlyglprre aarraaelle
      121 alelagdagk vvqayshgmk kklalgcali hgprllflde pfegidavav sgirrllqdl
      181 vsrraltifl tshvlevver lvthvgiihr grlvvqgtle evratgtlee tfiravgear
      241 pappplswla gpggagdgga
//
LOCUS       WP_176066900             565 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176066900
VERSION     WP_176066900.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..565
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=59437
     Region          11..503
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mngfrnmgvr arllvafgav mlltgglgaf avvqlskvna atediatnwl psikylgqid
       61 drintirrye lghvlatdpa vfdryeqkie slgrelaeae kayepllssa eekaayrtfr
      121 dewdhylteq rqvlalshag kqvearnlts stslklhnda iatlagliaq nvagaqrahe
      181 aaaeayrvsr lwvigiiaaa valsvfiava isgalvrqlg gepdyaagia kkvaegdltv
      241 rvalrpgdes sllhamkgmv eklteiiaev rggaaalssa aeqvsstsqs vsqgtseqaa
      301 sveettssle qmsasitqna ensrqteqma vagaknaees gkavgetvta mkeiaekisi
      361 ieeiayqtnl lalnaaieaa ragehgkgfa vvatevrkla ersqkaagei gglasqsvkv
      421 aersgqllle lvpaikktad lvqevaaasq eqstgvaqin kamanvdqvt qrnasaseel
      481 astaeemnaq aeslqqlmgf frvdgaeaqa eraapraaar aaarpalalq paaaaadpgl
      541 hpaalrngka ngvngahpdr eykrf
//
LOCUS       WP_176066902             185 aa            linear   BCT 11-JAN-2025
DEFINITION  chemotaxis protein CheW [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176066902
VERSION     WP_176066902.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Stock,J.B., Levit,M.N. and Wolanin,P.M.
  TITLE     Information processing in bacterial chemotaxis
  JOURNAL   Sci STKE 2002 (132), pe25 (2002)
   PUBMED   12011495
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Djordjevic,S. and Stock,A.M.
  TITLE     Structural analysis of bacterial chemotaxis proteins: components of
            a dynamic signaling system
  JOURNAL   J Struct Biol 124 (2-3), 189-200 (1998)
   PUBMED   10049806
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002856
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..185
                     /product="chemotaxis protein CheW"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=18756
     Region          3..157
                     /region_name="CheW"
                     /note="Chemotaxis signal transduction protein CheW [Signal
                     transduction mechanisms]; COG0835"
                     /db_xref="CDD:440597"
ORIGIN      
        1 msasdatqrn qylsftlags dyavgilqvr eilqyetvtr vpsvppsirg vinlrgavvp
       61 vldlalkfgl eatpvtkrtc vlivdasvgg estvvgvmad avrevlelgg devepppsfg
      121 tqvrvdylvg mgkagkgfvl lldldrvisa gerelaaqlg geggapagal aaggsapaag
      181 ealvp
//
LOCUS       WP_176066920             570 aa            linear   BCT 11-JAN-2025
DEFINITION  cation:proton antiporter [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176066920
VERSION     WP_176066920.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Malo,M.E. and Fliegel,L.
  TITLE     Physiological role and regulation of the Na+/H+ exchanger
  JOURNAL   Can J Physiol Pharmacol 84 (11), 1081-1095 (2006)
   PUBMED   17218973
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Alexander,R.T. and Grinstein,S.
  TITLE     Na+/H+ exchangers and the regulation of volume
  JOURNAL   Acta Physiol (Oxf) 187 (1-2), 159-167 (2006)
   PUBMED   16734752
REFERENCE   3  (residues 1 to 570)
  AUTHORS   Hayashi,H., Szaszi,K. and Grinstein,S.
  TITLE     Multiple modes of regulation of Na+/H+ exchangers
  JOURNAL   Ann N Y Acad Sci 976, 248-258 (2002)
   PUBMED   12502567
REFERENCE   4  (residues 1 to 570)
  AUTHORS   Burckhardt,G., Di Sole,F. and Helmle-Kolb,C.
  TITLE     The Na+/H+ exchanger gene family
  JOURNAL   J Nephrol 15 Suppl 5, S3-S21 (2002)
   PUBMED   12027219
REFERENCE   5  (residues 1 to 570)
  AUTHORS   Dibrov,P. and Fliegel,L.
  TITLE     Comparative molecular analysis of Na+/H+ exchangers: a unified
            model for Na+/H+ antiport?
  JOURNAL   FEBS Lett 424 (1-2), 1-5 (1998)
   PUBMED   9537504
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008671
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..570
                     /product="cation:proton antiporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015078 - proton transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0015297 - antiporter activity [Evidence
                     IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:1902600 - proton transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=58774
     Region          1..558
                     /region_name="RosB"
                     /note="Predicted Kef-type K+ transport protein, K+/H+
                     antiporter domain [Inorganic ion transport and
                     metabolism]; COG4651"
                     /db_xref="CDD:443689"
ORIGIN      
        1 mhdggilltf agglagalvl gylahrlkls pivgyllagv lvgpftpgfv anravaeqfa
       61 eigvilllfg vglrfhlrel vavwrvalpg avvqctastf llavlvrplg wswtsglilg
      121 mgvsvastvv malvladrhd lhatighiai gwtvvedllt valllllpil fgpggaehdp
      181 gpalalaglk vlalvavvvv lgkwvipwal eriakthvre lftlgvlvla vgiavgsael
      241 fgvsialgaf laglavgrse faaraagdav pmrdafavlf fvsvgmlfdp rslvqapllt
      301 aavlavvvvg kpliavgtvr llgvplatav pvgaafsqvg efsfilgtva rqlgllddag
      361 wnalvatslv sislnpalyr wargltpsap alapvstger rplepnrsil vgygpvgrvv
      421 hrllvdrgaa vtvvelnldv vralkadgvn alygdvlrpg tleeagiata gnlvlsadve
      481 daaeiirqar alnpelrvfa rcthlrdapg lkraganvva ageaeigval veamtagela
      541 dgaaladqrd avrarlygpg aperpargrv
//
LOCUS       WP_176066921             404 aa            linear   BCT 11-JAN-2025
DEFINITION  CDP-alcohol phosphatidyltransferase family protein [Piscinibacter
            koreensis].
ACCESSION   WP_176066921
VERSION     WP_176066921.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Nogly,P., Gushchin,I., Remeeva,A., Esteves,A.M., Borges,N., Ma,P.,
            Ishchenko,A., Grudinin,S., Round,E., Moraes,I., Borshchevskiy,V.,
            Santos,H., Gordeliy,V. and Archer,M.
  TITLE     X-ray structure of a CDP-alcohol phosphatidyltransferase membrane
            enzyme and insights into its catalytic mechanism
  JOURNAL   Nat Commun 5, 4169 (2014)
   PUBMED   24942835
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Sciara,G., Clarke,O.B., Tomasek,D., Kloss,B., Tabuso,S.,
            Byfield,R., Cohn,R., Banerjee,S., Rajashankar,K.R., Slavkovic,V.,
            Graziano,J.H., Shapiro,L. and Mancia,F.
  TITLE     Structural basis for catalysis in a CDP-alcohol phosphotransferase
  JOURNAL   Nat Commun 5, 4068 (2014)
   PUBMED   24923293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Koga,Y.
  TITLE     From promiscuity to the lipid divide: on the evolution of distinct
            membranes in Archaea and Bacteria
  JOURNAL   J Mol Evol 78 (3-4), 234-242 (2014)
   PUBMED   24573438
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Koga,Y.
  TITLE     Early evolution of membrane lipids: how did the lipid divide occur?
  JOURNAL   J Mol Evol 72 (3), 274-282 (2011)
   PUBMED   21259003
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..404
                     /product="CDP-alcohol phosphatidyltransferase family
                     protein"
                     /EC_number="2.7.8.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=43649
     Region          219..388
                     /region_name="PgsA"
                     /note="Phosphatidylglycerophosphate synthase [Lipid
                     transport and metabolism]; COG0558"
                     /db_xref="CDD:440324"
ORIGIN      
        1 mnlwidtasa asaeclfgva plerlrltag kvkgidavtl sgpdagaarw lgargdssga
       61 plgtrlraal vtspggivav dganavdprl vgylagraap cvaargegaq ravvlrldpp
      121 ladaippdar dlrevadall aagriaplae adfpayvdkl rrslpywiya vdgaatrrrl
      181 erqmfwdnyk gstdlltryv ypplvwplvr lcirlgihpn avtllsvvlt faavplfarg
      241 dfllgfvcay gmsvldsvdg klarvtltds kignvldhgl dqvhppfwyf awawglgara
      301 wadplyqaav wlivfyfadr ivlaiakrri gfalhaatkl dgrvrsfiar rnitmtimaf
      361 allvgagpag fylitawqgl tfawhsarti wlgflargra rpef
//
LOCUS       WP_176066948             108 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176066948
VERSION     WP_176066948.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..108
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=12010
     Region          2..100
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mfrqifdava aalatgeiap geqlptihal areldvnpnt ivrayreleh aalvvsergr
       61 gtfpveragp lvhkdgvlrk algrmfrece regfsqaevm lflrreir
//
LOCUS       WP_176066958             324 aa            linear   BCT 11-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176066958
VERSION     WP_176066958.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     A novel family of ubiquitous heavy metal ion transport proteins
  JOURNAL   J Membr Biol 156 (2), 99-103 (1997)
   PUBMED   9075641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11440813
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..324
                     /product="cation diffusion facilitator family transporter"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=34392
     Region          32..317
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
ORIGIN      
        1 maeashhhaa hghdhahvah ahahhhaahg pseagsarrl avslgvasvi maaealggwl
       61 sgslalisda ghmltdvaal alallavqfg arpadqkrtf gfrrlevlaa qinvatllgl
      121 tawigweald rlrhphppig falmagtatv gvlgnsvilv wlrgdhnlnt rsaflhvlgd
      181 avaslavlvg agamwlrpdl awidpvlsla iallilwgav rlvveisdil meavprhldv
      241 eeitevmsta eegvvavhdl hvwtissgly alsahlvihv davgrndail tsvkavlrrr
      301 fgidhttlqi esvdyahvdd vhqh
//
LOCUS       WP_176067034             489 aa            linear   BCT 11-JAN-2025
DEFINITION  NADH-quinone oxidoreductase subunit N [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176067034
VERSION     WP_176067034.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436843
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..489
                     /product="NADH-quinone oxidoreductase subunit N"
                     /EC_number="7.1.1.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008137 - NADH dehydrogenase (ubiquinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=49568
     Region          8..484
                     /region_name="NuoN"
                     /note="NADH:ubiquinone oxidoreductase subunit 2 (chain N)
                     [Energy production and conversion]; COG1007"
                     /db_xref="CDD:440631"
ORIGIN      
        1 mtglsptdla amlpiailva galvllmsev fltsgrrgfm agitvaaaal aglaallapp
       61 agrvfggqav vdgfsvfvtv tvcgglalsa lvgaqwlhar daergefyal alfaaagmsl
      121 lgsaadllmt fiaievmsla tyalaaymrr grkpaeaafk yfvlgafssa lllygtalvy
      181 gvtgstlfsd fargsgallv iglglvgagl afkiaavpfh lwtpdvyega ptpvtafmaa
      241 gvktagfavl vrvlmavwgg avmgsarfga vaaalavltm lfgnllavpq rsvkrmlays
      301 siahagyllv gvvsagaaga resalssvlf ylaaytatvi gafavvgave rtdvraepad
      361 awdlsrlagl arrrpglafv mavfmlslag ipptagfvgk flifkaaina qayglaiigv
      421 ltsalgayyy lrvvvymymr apeageegal algpalsval aasavavvvl gigpgpiadl
      481 araasmltq
//
LOCUS       WP_176067102              87 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl carrier protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176067102
VERSION     WP_176067102.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 87)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 87)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..87
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=9180
     Region          4..77
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mtpreaavaa eirrlareel gleqavedge elagrldsla llslvvaved hfrvrvgeed
       61 aaglrtladl arfvaaraeg rsaeasp
//
LOCUS       WP_176067162             499 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176067162
VERSION     WP_176067162.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..499
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=51916
     Region          5..482
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(62,64,68,71,75,108,111..112,121..128,133,136,139,
                     232,236,239,242,244,418,420..421,423..424,427,430..431,
                     433,435..438,447,451,453,467,474..479,481..482)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(148..151,159,174,177,207,224..227,230,248..250,282,
                     383,385,411)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(151,248,279,282)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mtptlklwig geevasaggr lgdvfdpalg qvvrrvhfag redvaravaa aeaalpgwrd
       61 tpplrraril mrfrelleah rdelarlvte ehgktlpdaa gsvqrglevv efatgiphll
      121 kgelsedvak gvschslrqp vgvcagitpf nfpamvpmwm fpvalacgnt fvlkpsekvp
      181 stslrlasll geaglppgvl nvvpgdaeav gallahpgvs avsfvgstpv arhvyetaak
      241 agkrvqalgg aknhavvlpd adldlaadal igagygsage rcmaisavva vgaaaeplva
      301 rlrdraaalr vgagtragve mgplitaahr ervrgliaag iaegavpvld gralrveept
      361 agfflgptll drvttsmsvy reeifgpvli vlrvgsldea ialvnanpyg ngtavftgsg
      421 yaaqrferev qvgmvgvnva ipvpmaffsf ggwkqslfgd lhvhgaegvk fytrtktvtt
      481 rwpepsaata aslamptlg
//
LOCUS       WP_176067181             235 aa            linear   BCT 11-JAN-2025
DEFINITION  spermidine synthase [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176067181
VERSION     WP_176067181.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..235
                     /product="spermidine synthase"
                     /EC_number="2.5.1.16"
                     /GO_function="GO:0004766 - spermidine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=24591
     Region          46..193
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
ORIGIN      
        1 mkpwetidra lapdgtelvl arrgaewvvr agghvlvssr ahgseeglaa lgleraarrd
       61 tvlvgglglg ytvravldrv pagarvivae lsralvdwnr gpvsalagrp lddprvrlqv
      121 sdvadriaea trafdailld vdngpsalvh grnerlygea gvhlafealk pggalavwsa
      181 gpddrylaal rragfaaeav paparagsag arhvvflgvk sprpaprrrt sagrp
//
LOCUS       WP_176067188             126 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Piscinibacter koreensis].
ACCESSION   WP_176067188
VERSION     WP_176067188.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16058428
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..126
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14103
     Region          8..111
                     /region_name="Glyoxalase_6"
                     /note="Glyoxalase-like domain; pfam18029"
                     /db_xref="CDD:436220"
ORIGIN      
        1 mhrsrlaavv idcqtsdvda aagfwsralg wrvdphddpd gsryrrldtp asqpdvlvqa
       61 vehpsrvhvd ietddveaev rrlealgarr vaqvktwwvm eaptgqrfcv vkpqrddfad
      121 ganvwe
//
LOCUS       WP_176067200             257 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Piscinibacter koreensis].
ACCESSION   WP_176067200
VERSION     WP_176067200.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 257)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..257
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26977
     Region          33..256
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mserraavaq aratervptg egagasaavp agpvidargv hkrftegtgs srldvhvlrg
       61 vdlqvqpget laivgasgsg kstllhvlgg ldapsagqvl lagrdfarmg aaaqgewrnr
      121 qlgfvyqfhh llpeftaldn vamplrirrv draeaearaa atlqqvglge rtrhrpsqls
      181 ggerqrvaia ralvgepacv ladeptgnld retaagvfal llelaasrrm aivvvthdes
      241 laercgrarr lvsgqlg
//
LOCUS       WP_176067223             292 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfurtransferase [Piscinibacter koreensis].
ACCESSION   WP_176067223
VERSION     WP_176067223.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..292
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=30663
     Region          24..290
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mssyttlira delqalrasg aprvvvdasf dladtawgar ewrsahlpgs ihldldrdls
       61 gvktgtngrh plperaafra llgrigvapg vqvvaldrng dvyaarvwwl lrwaghceva
      121 vldgglraws eaggevvaad agaatpasta vptqasaagg deraippvid aerlaaglgr
      181 lrvidaraae rfrgdvepld avaghipgal nrfwkdnlda sgrwktsaql raefepllgg
      241 qgpeavvhqc gsgvtachnl lamehaglag smlypgswse wssdpqrpva rg
//
LOCUS       WP_176067253             169 aa            linear   BCT 11-JAN-2025
DEFINITION  RDD family protein [Piscinibacter koreensis].
ACCESSION   WP_176067253
VERSION     WP_176067253.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..169
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17716
     Region          27..169
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 masidegnrf apptvhvedv aastsalasr ggrlaaviid aviqgiavav lsfvtplspf
       61 rppadgalvg fmltnlvlgl vlflllhgyl latqgqtigk kllgirivrs dgsaatfgrl
      121 vglrilpvnl ivlvpyigml ivlidsllif resrkclhdn iadtivvka
//
LOCUS       WP_176067254             229 aa            linear   BCT 11-JAN-2025
DEFINITION  RDD family protein [Piscinibacter koreensis].
ACCESSION   WP_176067254
VERSION     WP_176067254.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..229
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24199
     Region          11..151
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 mtlldtryva etpegiglsl rpagvmprly afvidfgirl vlfaplarll atlgefgwgl
       61 alllyfaidw fyavlfellp gaatpgkrav glrvvmdsgl pitpaasltr nllraadflp
      121 ffyaagalsm llrpdfkrlg dlaagtlvvh rhvvslhgap paaaplapaa dlapraqaai
      181 vawagrvprl tparadelae lasaalpaga rrdpgkellg vahwliger
//
LOCUS       WP_176067329             269 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Piscinibacter koreensis].
ACCESSION   WP_176067329
VERSION     WP_176067329.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..269
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29437
     Region          9..190
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(12,14,95)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(39,94..95)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            93..95
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mtpspthlvi ipsyntgatv yatvraaraa wapvwvvvdg stdgtaeglq qmalddpalh
       61 vmvlptncgk gaavlhalra ahasgfthal tmdsdgqhpa dligpfmaes qrlphamvlg
      121 rpvfdasapl lrvrgrrisn awtnletlga giddslygfr vypiapliav megqrwmrrf
      181 dfdteavvrl awrgvsplni aapvkylrhd eggvshfryg rdnallswmh lrlmggflvr
      241 lpllllrras grppfdlrrr sgrrrpggr
//
LOCUS       WP_176067279             425 aa            linear   BCT 11-JAN-2025
DEFINITION  phenylacetate--CoA ligase family protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176067279
VERSION     WP_176067279.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Luengo,J.M., Garcia,J.L. and Olivera,E.R.
  TITLE     The phenylacetyl-CoA catabolon: a complex catabolic unit with broad
            biotechnological applications
  JOURNAL   Mol Microbiol 39 (6), 1434-1442 (2001)
   PUBMED   11260461
REFERENCE   2  (residues 1 to 425)
  AUTHORS   El-Said Mohamed,M.
  TITLE     Biochemical and molecular characterization of
            phenylacetate-coenzyme A ligase, an enzyme catalyzing the first
            step in aerobic metabolism of phenylacetic acid in Azoarcus evansii
  JOURNAL   J Bacteriol 182 (2), 286-294 (2000)
   PUBMED   10629172
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Ferrandez,A., Minambres,B., Garcia,B., Olivera,E.R., Luengo,J.M.,
            Garcia,J.L. and Diaz,E.
  TITLE     Catabolism of phenylacetic acid in Escherichia coli.
            Characterization of a new aerobic hybrid pathway
  JOURNAL   J Biol Chem 273 (40), 25974-25986 (1998)
   PUBMED   9748275
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..425
                     /product="phenylacetate--CoA ligase family protein"
                     /EC_number="6.2.1.30"
                     /GO_function="GO:0047475 - phenylacetate-CoA ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0010124 - phenylacetate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=44677
     Region          15..421
                     /region_name="PaaK"
                     /note="Phenylacetate-coenzyme A ligase PaaK,
                     adenylate-forming domain family [Coenzyme transport and
                     metabolism]; COG1541"
                     /db_xref="CDD:441150"
ORIGIN      
        1 msaprlrpsr ildpaleqqs paareaylae rlratvahaa aaspafqrrl aaanlaagdl
       61 rgpadlarlp plrkdalpgl qagdppfggl lavapgalar vfmspgpiyd pegdgadfwr
      121 frhalaaagf rageiahnaa syhltplgfm ldaaaralgc avipagvgqt elqvkvaahl
      181 gataylgtps flyallgkar elgtplrfet afvlaemlpe slraelegef gvrvlqgygt
      241 adlgclayec pekggwhlhp eclvevldle tgqpaapgqp gevvatlfdp vyplvrlgtg
      301 dlaalapeap cpcgrtapkl agllgrlgda vkvkgmfvrg gelaaalqkf pevkrfqavv
      361 treqhqdhla ydvelsapag depalaarig ealreavkvr gevrfvppga ipegakrvdd
      421 rrvwk
//
LOCUS       WP_176067331             445 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Piscinibacter koreensis].
ACCESSION   WP_176067331
VERSION     WP_176067331.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428914
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..445
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49977
     Region          26..338
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
ORIGIN      
        1 mqsrptqtdl ppatavktcd vlvigggpag stiaallaer grdvvvmeka qhprfhiges
       61 llpanvtlfe rlgvreqvea igmrkwgaef vspthdhesa iefaeahdks mpyawqvrrs
      121 qldellfrna aakgartleg trvrqvefdd agatvqvdaa dgtretwrvr yvvdasgrdt
      181 llanqfrcke knprhnssal yahftgvers lgkregniqi ywfehgwfwf ipladgvtsv
      241 gavcwphylk trkkpltdff mdtialcpkl aarmrgatlv sevhatgnys ysssrssger
      301 yvmlgdayaf vdpvfssgvl iamqtafeav qvvettlerp aeaaaarrrf nrlarhgpre
      361 fswfifrvtn ptmreffmsp qnpfrvkeal isllagdiyg ktpiwlsifv lkvlyylvsi
      421 gnprrtwdaw qrrrfnirdv gapas
//
LOCUS       WP_176067377             408 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Piscinibacter koreensis].
ACCESSION   WP_176067377
VERSION     WP_176067377.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..408
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42394
     Region          10..391
                     /region_name="MFS_YcxA_like"
                     /note="MFS-type transporter YcxA and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd17355"
                     /db_xref="CDD:340913"
     Site            order(21..22,25..26,29,64,111..112,114..116,119,143,
                     146..147,150,224,227..228,231..233,236,266,270,319..320,
                     324,328,344,347..348,351..352,355)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340913"
ORIGIN      
        1 mqhaadsrya wtrlgvslal mtigsgamyv mavvlppvqa efgvarssaa lpytllmigf
       61 gfggvlmgrl adrfgvmlpa ligsaglaag fvgagfstsl gtfavlhgvl lglfgasatf
      121 gplvadtslw flkrrgtava icasgnylag aiwppivqrs ieafgwrhty iglgvfcalt
      181 mpllamllrp rpplardaap gsidsaarqr pfgmspraaq allcvagtac cvamampqvh
      241 ivaycgdlgy gaargaqmls lmlaagivsr lvsgaicdri gglrtlllgs vlqgialllf
      301 lpfdglaslf visalfglfq ggivpsyaii vrehfapaea gqrvgtvlmf tlfgmalggw
      361 vsgkvfdltg syhaafvngi gwnlvnlaia llllwrtgrg rrfaplpv
//
LOCUS       WP_176067395            1017 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176067395
VERSION     WP_176067395.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 1017)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 1017)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..1017
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=103944
     Region          1..123
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
     Region          <25..616
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          <549..>1000
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
ORIGIN      
        1 mstfyaphga adllsrysfi epilggrrvl eigaaratdg asalalaerg aaavlsvedd
       61 glglgraaev sahpfvqfra aaleelpqha fdlvlvadga alaasperla alaellsprg
      121 hlvtalaaag arglaalage ppildvpsye sfagalaaqf dvvevatqsp avgwviapaa
      181 rgddapdlgv dgslsgapea ayyvalcgar ptglasmvlv tlppgplada alagaeaaha
      241 hagcaealag rdealsrasa agaeaearag aleeviaslr aeleaaaarq advaarlete
      301 ragrnelada varaeaelaa rsgelaaaqe evaareadlr garvearlre ervaaleeea
      361 raraeerdqa rseagaaeqa raeaarsaae areaaeaawr etdaaraaad eelasvraga
      421 daelataraa adadlasara aaeaaagere ealarlaaae gelavardgr aaaeagaaeq
      481 aalaeaarre aeaaraeaaa lreaqrsaee araaeaaaae areaeltgav aaaeaalaaa
      541 ragaeelere laargaqaee agrreaalsa qasglaaeve vlrgrgeeha geaaeletra
      601 laaeaklasl eaeradggar leaeraraee laaaltaara elegtraela aaqaesgaag
      661 prlaealrra edaeaavtrg haeadlladr lkevegrvae ataraeeaer raaavgsqrs
      721 eesaaaarlr gelssareal aarfaeveee rqalrdrvgr leeelatqka daaaaraaag
      781 qaeaaraeae aarraaetsy aealtpaqae aaglrtevet araaaetaea eaatleaelq
      841 avrwekeeie grlqaaqasg gaasagevar lreelaeraa eaaelraeae rraaeltaaq
      901 gelaeraaqa aaagapevra reaesklada lrrlsdaeav aeaartspda pgagvaerlq
      961 rmaherdllq sqvserdtri srlqreiadk tdrlgrlake mgelklkskg glgklfr
//
LOCUS       WP_176067560             162 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Piscinibacter
            koreensis].
ACCESSION   WP_176067560
VERSION     WP_176067560.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 162)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..162
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17513
     Region          8..147
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mkssaalppl datdwailda lqrdasitnh alasvvhtsp atclrrvrrl vdagvierrv
       61 allspeklgf gvtafvevsl drqgadalaa fetraiaepa vrqchrvspg pdfvlcvqlr
      121 dmadyhalvq rlftedanvr nvkayfsvhr akdetalplg eg
//
LOCUS       WP_176067562             382 aa            linear   BCT 11-JAN-2025
DEFINITION  GGDEF domain-containing protein [Piscinibacter koreensis].
ACCESSION   WP_176067562
VERSION     WP_176067562.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 382)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..382
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39374
     Region          108..349
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mdpatvilvl athltcsggl flvvgrqlpe rcgiqlwglc gllfgaafvg rlaagldapp
       61 awgqlsdiam igamllltag lrqffgsepl spraglalll gfaalqtlav lgagavgrfa
      121 vinlglgiah lwvaaiaata rrgaepglqr pllvltilag sqglasatrg lhiaaagvdv
      181 iyrgipaqly yaysslgtvl lamillwllf arlngqlsel atrdaltrll nrtglddalr
      241 rhfgargaqp lrllaldidh fkrindtlgh asgdqvlrav agvlargvrp ndivarlgge
      301 efvvccaaad aatalslaer lrsavaalst vaadgrttar ctisigvsea csaladwsra
      361 aaaadralya akaagrdrvm aa
//
LOCUS       WP_176067696             294 aa            linear   BCT 11-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176067696
VERSION     WP_176067696.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..294
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31339
     Region          68..294
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mklatfrqdg pprvgvvdps ggriwpadel agepvgdmlq lirawprlre rlaprgpgld
       61 larvaleapi prpprnvlcv gknyrahahe ftrsgydssa kgaadavpta pviftkapet
      121 vigpgrpipy pegvseqvdy eaelavvvga ggrglrreda lghvfgytiv ddvtardlqa
      181 rhkqwflgks ldgfcpmgpw ivtadeldpa agvevrcwvn gelrqegntr dlvfdvptll
      241 atisagltlq pgdvlatgtp agvgvgfdpp rflrrgdrvr iaiagigvle nevg
//
LOCUS       WP_176067719             358 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176067719
VERSION     WP_176067719.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..358
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=38782
     Region          60..346
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mtrslplala aalataacrt apapaapaaw elesplqpla ppppgvpfdl arargvrvtp
       61 ekvrlgrwlf fdprlsrggt vacatchdpr hafselrphs tgvegrqgtr kapplvnvaf
      121 plyeawfwdg raaslaeqak gplvnpvemd ntleavvatv aavpgyrraf reaygdgrld
      181 idriadalaa yqatrrsggs aydryqagdd galseearrg mevffgrgrc nachagpnlt
      241 dgkfhnvgig fdpgpdavrl gfqdagryav tgdprdvgaf ktptlrevar hppymhdgss
      301 pdlrdavlry feiadnpwld pamrevrifp fdvrplvafl ealdgtgfed epprsfpr
//
LOCUS       WP_176067261             189 aa            linear   BCT 11-JAN-2025
DEFINITION  shikimate kinase [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176067261
VERSION     WP_176067261.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Herrmann,K.M.
  TITLE     The shikimate pathway as an entry to aromatic secondary metabolism
  JOURNAL   Plant Physiol 107 (1), 7-12 (1995)
   PUBMED   7870841
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Bentley,R.
  TITLE     The shikimate pathway--a metabolic tree with many branches
  JOURNAL   Crit Rev Biochem Mol Biol 25 (5), 307-384 (1990)
   PUBMED   2279393
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431165
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..189
                     /product="shikimate kinase"
                     /EC_number="2.7.1.71"
                     /GO_function="GO:0000287 - magnesium ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0004765 - shikimate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009073 - aromatic amino acid family
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=19505
     Region          11..164
                     /region_name="AroK"
                     /note="Shikimate kinase [Amino acid transport and
                     metabolism]; COG0703"
                     /db_xref="CDD:440467"
ORIGIN      
        1 mprasadarp valtgmmaag kstvaahlgr llrrpvvstd aeverragkp iarifaeege
       61 pafralerev laglagpavv dlgggafcda etqarlleta tvvfldvsaa eaarrlggge
      121 grplakrwee llaarlplyr rahhtlrvdg laaeavarri aellaaapsa gssasevere
      181 aggagedsp
//
LOCUS       WP_176067757             365 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Piscinibacter koreensis].
ACCESSION   WP_176067757
VERSION     WP_176067757.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..365
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=38329
     Region          4..365
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkksllalav lgafsgvasa qssvtlygti dlagryvkne gsnrrfslas dglnssqlgf
       61 rgvedlgggl kasfvllagv nadsgtangk fwnrrstvsl ssnageirlg rdytptfwnl
      121 tlfdafgtng lgnslntaqr hpgtrqdnti qyflpsnlgg wygqfmagts egatsgdrpa
      181 rylggrvgfa agpfdvavag aqiryrgasf ngwtagapgg aitnddqksi nvgaswnfgf
      241 aklmgyvdye rldnaaddre lrgsisavip fgqsevhvgy drsrlrrdga gtstaqqlka
      301 syvynlskrt avygtvsyld nnrnaamsia pasgtnastg sqsatalpst ggdsrgvefg
      361 vrhff
//
LOCUS       WP_176067787             261 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176067787
VERSION     WP_176067787.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..261
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=27744
     Region          23..255
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mhgtkwviaa flalagatar aevktkvidy rqgdtalegf lawddaaqgs rpgvlvihea
       61 wgenqhardq avrlaragyv gfaldmygkg kvtkhledak afmaeaskdp avvrarfeaa
      121 rkllqaqpqv dpkkigavgy cfggnvalnm aragedlaav atfhaaipsa dqpvpgkvkp
      181 rilintggdd plvpksqida fvkelkdaga disvitypha khsftnpeaa qagmdalgyd
      241 adadrkswea smkmfqaafk g
//
LOCUS       WP_176067810             100 aa            linear   BCT 11-JAN-2025
DEFINITION  putative quinol monooxygenase [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176067810
VERSION     WP_176067810.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Lemieux,M.J., Ference,C., Cherney,M.M., Wang,M., Garen,C. and
            James,M.N.
  TITLE     The crystal structure of Rv0793, a hypothetical monooxygenase from
            M. tuberculosis
  JOURNAL   J Struct Funct Genomics 6 (4), 245-257 (2005)
   PUBMED   16496224
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003583
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..100
                     /product="putative quinol monooxygenase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0004497 - monooxygenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0017000 - antibiotic biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=10574
     Region          5..92
                     /region_name="YgiN"
                     /note="Quinol monooxygenase YgiN [Energy production and
                     conversion]; COG1359"
                     /db_xref="CDD:440970"
ORIGIN      
        1 mvtealyvrl eakagkeeav tkflkdalpv veserdtqaw falrlgptsf gifdafpnea
       61 grqahlagqv aaalkskgge lfaapptidr advlaaklph
//
LOCUS       WP_176067900             496 aa            linear   BCT 11-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176067900
VERSION     WP_176067900.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..496
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=53535
     Region          41..323
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mrranapsap gqpwrerlrd ffaeeiwavr vadlkrgqal lyrasrvgys tvrgffvsrl
       61 tvraaaltyy svlsvvpfla fafallkgfg ayasfiettv rpylhqtfgg npallgsler
      121 ilqfvdhtnv stlgalglvi lvytcvslls svedtlneiw gattrrsflr qvtdyvtllv
      181 ttpllvvaag avataaqssr fvlflrdald lggvidfllq ftslavvava ffviyiilpn
      241 vrirplsaal gaavaavlwq lalvlyvrlq vgvssynaly svlsaipifl vwtyvswvvv
      301 lvgaqvaash qnerlvrqrf rarhadqelr etlavvvaah vardflsgap asepaalael
      361 vhvpaltvqe ildalvragl laqaasgrgv rylptrdldr irvsdvrdal rreaqaervr
      421 aeverhlepg lrqvldaaee errgsplnvt lrelagrvgg agvpepaaaa rpgaappaaa
      481 amaaapprsp pvldak
//
LOCUS       WP_176067828             270 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176067828
VERSION     WP_176067828.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..270
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=29261
     Region          148..268
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 malkellvhv dsgartterr dlafllarrf gaqvsgwfae nealgaslvg rrgrsdmdra
       61 aeaarlafea saraagleag wwrlepgepr hlidhttirc rytdlaifgq hddreswvpe
      121 elveevvvgc grpalvvpaf grfpdvgkrv vvawdgsrea aralhdglpl mreaqsvtll
      181 afqrpsagpp gplphldvaa hlaahgvtar yervfvgelg ptdtllnrca evgadlivmg
      241 arpqrglplq dggslrellr qmtapvllsh
//
LOCUS       WP_176067962             292 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176067962
VERSION     WP_176067962.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426520
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..292
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31404
     Region          29..>177
                     /region_name="LysR"
                     /note="DNA-binding transcriptional regulator, LysR family
                     [Transcription]; COG0583"
                     /db_xref="CDD:440348"
     Region          92..281
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,221..226,
                     232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mttwddlrvf lavaragsas aaaralglsq ptvsrrvaal arglgvellh kgprglalta
       61 agqrlrldae kvdrevlaal rgvdrldarp ggavrvtape glglaviapq leafarehpg
      121 idlllvaeta vvnlsrread lalrfvrprq relvmrrlas vpfapyasar ylrarprepg
      181 aalvtgdelv amheslegsp egawlranap qqrvrvrvrs tlalqaalla gagvgllpdy
      241 lgdhpelrpl gagpvlhrdl flvypramrs aervrtvarf ltacldrrga rr
//
LOCUS       WP_176067966             266 aa            linear   BCT 11-JAN-2025
DEFINITION  prohibitin family protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176067966
VERSION     WP_176067966.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Yoshinaka,T., Kosako,H., Yoshizumi,T., Furukawa,R., Hirano,Y.,
            Kuge,O., Tamada,T. and Koshiba,T.
  TITLE     Structural Basis of Mitochondrial Scaffolds by Prohibitin
            Complexes: Insight into a Role of the Coiled-Coil Region
  JOURNAL   iScience 19, 1065-1078 (2019)
   PUBMED   31522117
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Browman,D.T., Hoegg,M.B. and Robbins,S.M.
  TITLE     The SPFH domain-containing proteins: more than lipid raft markers
  JOURNAL   Trends Cell Biol 17 (8), 394-402 (2007)
   PUBMED   17766116
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Morrow,I.C. and Parton,R.G.
  TITLE     Flotillins and the PHB domain protein family: rafts, worms and
            anaesthetics
  JOURNAL   Traffic 6 (9), 725-740 (2005)
   PUBMED   16101677
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Tavernarakis,N., Driscoll,M. and Kyrpides,N.C.
  TITLE     The SPFH domain: implicated in regulating targeted protein turnover
            in stomatins and other membrane-associated proteins
  JOURNAL   Trends Biochem Sci 24 (11), 425-427 (1999)
   PUBMED   10542406
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..266
                     /product="prohibitin family protein"
                     /GO_component="GO:0005743 - mitochondrial inner membrane
                     [Evidence IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0035632 - mitochondrial prohibitin
                     complex [Evidence IEA]"
                     /calculated_mol_wt=29639
     Region          24..217
                     /region_name="SPFH_prohibitin"
                     /note="Prohibitin family; SPFH (stomatin, prohibitin,
                     flotillin, and HflK/C) superfamily; cd03401"
                     /db_xref="CDD:259799"
ORIGIN      
        1 mrlrtlfyag llatpfldgc hcpvvdsghs givfeslgkg tsrtvlgegm hvmplwnsvi
       61 aydlrvhefk eslsvlsnng lalrvdasvr frpkadelfe lqtqigqaya eiliapvvrs
      121 earkvfgrys peeiystkre eierqifeev qkalagkhvi veailirdve lpeaikvaia
      181 dklaeeqrsq kmrftldker qeaqrkqiea egiakyqniv rqgltadfla ykgieaterl
      241 assqnakivv vgsaksglpl ifqpek
//
LOCUS       WP_176068031             301 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease
            [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176068031
VERSION     WP_176068031.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 301)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..301
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=31351
     Region          1..301
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 meqflqqlin glavggiyal ialgytmvyg vlklinfahg dlftyggylg ltlltslalq
       61 grvgtaaava llvlmvmglv gvmgvvlera ayrplrespr lsavvsalga siflqnalml
      121 lygarvqvyp egllpqvavs lfglqvpllr ilvvlasvvm maalylfvqk tkigtavraa
      181 aidqgaarlm gidvnkvvsl vfligpalgg vagllvglyy gqvnftmgwi ygmkaftaai
      241 lggignipga mvgglllgvi ealgaaylsi awkdaiafcv lililivrpt gllgervaek
      301 v
//
LOCUS       WP_176068081             347 aa            linear   BCT 11-JAN-2025
DEFINITION  methionine ABC transporter ATP-binding protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176068081
VERSION     WP_176068081.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Johnson,E., Nguyen,P.T., Yeates,T.O. and Rees,D.C.
  TITLE     Inward facing conformations of the MetNI methionine ABC
            transporter: Implications for the mechanism of transinhibition
  JOURNAL   Protein Sci 21 (1), 84-96 (2012)
   PUBMED   22095702
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Rees,D.C., Johnson,E. and Lewinson,O.
  TITLE     ABC transporters: the power to change
  JOURNAL   Nat Rev Mol Cell Biol 10 (3), 218-227 (2009)
   PUBMED   19234479
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Davidson,A.L. and Chen,J.
  TITLE     ATP-binding cassette transporters in bacteria
  JOURNAL   Annu Rev Biochem 73, 241-268 (2004)
   PUBMED   15189142
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Koonin,E.V.
  TITLE     A superfamily of ATPases with diverse functions containing either
            classical or deviant ATP-binding motif
  JOURNAL   J Mol Biol 229 (4), 1165-1174 (1993)
   PUBMED   8445645
  REMARK    Erratum:[J Mol Biol 1993 Aug 5;232(3):1013]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..347
                     /product="methionine ABC transporter ATP-binding protein"
                     /EC_number="7.4.2.11"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0033232 - ABC-type D-methionine
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0048473 - D-methionine transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37135
     Region          1..341
                     /region_name="AbcC"
                     /note="ABC-type methionine transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1135"
                     /db_xref="CDD:440750"
ORIGIN      
        1 mievdgltkv frrdgeevpv lrgvslqvar geifgvigrs gagkstlvrc vnllerptsg
       61 rvrvagrdmt aldgaglrea rrdigmifqh fnllssrtvl gnvalplela grsreesrre
      121 aaplvelvgl salagrypae lsggqkqrvg iaralasrpe vllcdeatsa ldpettqsil
      181 allkdiqqkl gltvvlithe mqviqavcer vavldrgevv eqgpvfqvft aprsevtrgl
      241 vrdvvdrelp pwlrarlaag apagtspivr iiftgpsatt pviaqavrrf dvllnivqgh
      301 vdyiqgqpyg niiveaegap aaveaalawi rgqdlqaeil ghvardg
//
LOCUS       WP_176068118             167 aa            linear   BCT 11-JAN-2025
DEFINITION  Hsp20/alpha crystallin family protein [Piscinibacter koreensis].
ACCESSION   WP_176068118
VERSION     WP_176068118.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Basha,E., O'Neill,H. and Vierling,E.
  TITLE     Small heat shock proteins and alpha-crystallins: dynamic proteins
            with flexible functions
  JOURNAL   Trends Biochem Sci 37 (3), 106-117 (2012)
   PUBMED   22177323
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Caspers,G.J., Leunissen,J.A. and de Jong,W.W.
  TITLE     The expanding small heat-shock protein family, and structure
            predictions of the conserved 'alpha-crystallin domain'
  JOURNAL   J Mol Evol 40 (3), 238-248 (1995)
   PUBMED   7723051
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Jaenicke,R. and Creighton,T.E.
  TITLE     Protein folding: junior chaperones
  JOURNAL   Curr Biol 3 (4), 234-235 (1993)
   PUBMED   15335775
REFERENCE   4  (residues 1 to 167)
  AUTHORS   Lindquist,S. and Craig,E.A.
  TITLE     The heat-shock proteins
  JOURNAL   Annu Rev Genet 22, 631-677 (1988)
   PUBMED   2853609
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414641
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..167
                     /product="Hsp20/alpha crystallin family protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /GO_process="GO:0009408 - response to heat [Evidence IEA]"
                     /calculated_mol_wt=18396
     Region          64..164
                     /region_name="IbpA"
                     /note="Small heat shock protein IbpA, HSP20 family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0071"
                     /db_xref="CDD:439841"
ORIGIN      
        1 mttltrqlke gaeqafetla egwrelrara ggaltrfrsn dddalrgggv egiprlgrwa
       61 fmaadvierd drivvrleap gmrredfqve vrgqtlrihg ekrvdhests ggyrlvqcay
      121 gafdreirlp gdveveraaa tyrdgvlrve lpkapggaas rfsvpvs
//
LOCUS       WP_176068139             253 aa            linear   BCT 11-JAN-2025
DEFINITION  ParA family protein [Piscinibacter koreensis].
ACCESSION   WP_176068139
VERSION     WP_176068139.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..253
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28479
     Region          1..253
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mryvvfnqkg gvgkstitcn laaisaqqgl rtlvvdldvq gnstryllge redanegvag
       61 ffdqslkftm rpkgaaefvv espwddlhvm pssplldelh gklesrhkiy klreafdeld
      121 gsydriyvdt ppalnfytrs aliacercli pfdcddfsrr alytllenvq eiqadhnkal
      181 kvggivvnqf qpranlpqrl vqelvdeglp vlqpylgssv rikesheqsw pmifmdprhk
      241 ltqefvalhd ala
//
LOCUS       WP_176068158             117 aa            linear   BCT 11-JAN-2025
DEFINITION  YidH family protein [Piscinibacter koreensis].
ACCESSION   WP_176068158
VERSION     WP_176068158.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..117
                     /product="YidH family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=12905
     Region          1..115
                     /region_name="YidH"
                     /note="Uncharacterized membrane protein YidH, DUF202
                     family [Function unknown]; COG2149"
                     /db_xref="CDD:441752"
ORIGIN      
        1 mreprwrreg eepdyrfsla nertflawir talsllaggv lleqfatrls praalvtlat
       61 slavlaalls liayvrwran eiamrhkrpl pssvalplla lavfvvagai amlllrq
//
LOCUS       WP_176068234             154 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176068234
VERSION     WP_176068234.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..154
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16513
     Region          6..145
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mafpwmkvlc pidfsdpara amraavevcr ltggeltlfh ayelpgytlp egsvvaspkm
       61 lqdlsdqaev hlaewkklae gmgaakvrve kgigepalsv velaqergfd livvgthgrt
      121 glrhallgsv aervvrragc pvltihpegy arra
//
LOCUS       WP_176068197              97 aa            linear   BCT 11-JAN-2025
DEFINITION  circadian clock KaiB family protein [Piscinibacter koreensis].
ACCESSION   WP_176068197
VERSION     WP_176068197.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 97)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   3  (residues 1 to 97)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..97
                     /product="circadian clock KaiB family protein"
                     /GO_process="GO:0048511 - rhythmic process [Evidence IEA]"
                     /calculated_mol_wt=10404
     Region          11..79
                     /region_name="KaiB_like"
                     /note="KaiB-like family; composed of the circadian clock
                     proteins, KaiB and the N-terminal KaiB-like sensory domain
                     of SasA. KaiB is an essential protein in maintaining
                     circadian rhythm. It was originally discovered from the
                     cyanobacterium Synechococcus as part...; cd02978"
                     /db_xref="CDD:239276"
     Site            order(28,31..32,56,59,61,65,68..69,72..73)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:239276"
     Site            order(49,52..55,58..60,62,65)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239276"
ORIGIN      
        1 mepaappdfa frlyvsgatp asaralvntr ricethlagr yrldilelae hvelatrdqi
       61 vaaptlikls ppplrrfigd lsenegllrc lpaatag
//
LOCUS       WP_176068350             242 aa            linear   BCT 11-JAN-2025
DEFINITION  energy-coupling factor ABC transporter ATP-binding protein
            [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176068350
VERSION     WP_176068350.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..242
                     /product="energy-coupling factor ABC transporter
                     ATP-binding protein"
                     /EC_number="3.6.3.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=25246
     Region          2..218
                     /region_name="EcfA2"
                     /note="Energy-coupling factor transporter ATP-binding
                     protein EcfA2 [Inorganic ion transport and metabolism,
                     General function prediction only]; COG1122"
                     /db_xref="CDD:440739"
ORIGIN      
        1 mirardlsfa ypggppvlea vsfevaaggl cgvvgangcg kstllalmag lfeptagtlt
       61 vrgepspgrg ggvrdgvalv lqdpdqqiig atveedlllg lpprdarrad eacalaarlg
      121 lselaapvqt lslgqrrklc iatalrdgpe vlvldepfag ldypsalemr allaanrqag
      181 rtqviashdv epfadladaw lvlargrlal ggpteavfpe lrrhgvrpps awrpglevpr
      241 we
//
LOCUS       WP_176068408             378 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176068408
VERSION     WP_176068408.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 378)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 378)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..378
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41411
     Region          36..378
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 meetlfdelk ryvgwsevde ralralhasa aphfpavaev fyatilgheg akrsltgges
       61 qvghlkitlq rwldtllrgp wdeayyqnrs rigryhvrie lpqhymfgam nvvrrelnai
      121 vddtyrtspd alktvrealg rildlelavm lhtfredlva qsaraerlat fgqlvgsigh
      181 dlrnplgvie tslfilrgrv gadervkkhl drigdqlgva ngiitnlldm irnrplvker
      241 vrleqvvaga vdavmrpeam rfraeglagl evegdpgqlr qvfvnllsna veaaspagav
      301 siaasredgr itvavedsgp gvdpavarrl feplittker giglglalvk riverhggsv
      361 ayeppaggga rflvhlpa
//
LOCUS       WP_176068423             510 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Piscinibacter
            koreensis].
ACCESSION   WP_176068423
VERSION     WP_176068423.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..510
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54254
     Region          10..510
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mtaaprfrsl adrvrehara rpsapallqd derldyaafd alldrvaaal qrdgigpgdv
       61 vaicahstpr yaavflgalr agaavaplap svspesfaam lgdagpgrlf adaaaaalld
      121 rvpegvpiva ldraargtpl dgwlmppgst ptpvevqpew pcniiyssgt tgtpkgivqs
      181 hgmrdahier gaaygygphg vtilatplys nttlvvffpt layggsvvlm akfdaaryva
      241 laerhratht mlvpvqyqri maladfdahd ltsfhmkfct sapfsaalka dvlarwpggl
      301 vefygmtegg gtcildaheh pdklhtvgpp apghdirlid ergievapge vgevvghsrg
      361 mmtgyhgrpd ltaeaewfdp sgkrfirtgd vgrfdadgfl tlldrkkdlv isggfniyps
      421 dleaalrehp avveaavvgv psatwgetpv afvvargdan vdagtlkdwl narvgktqrv
      481 adlrlvdelp rsaigkvmkr elreaygrap
//
LOCUS       WP_176068298             208 aa            linear   BCT 11-JAN-2025
DEFINITION  Crp/Fnr family transcriptional regulator [Piscinibacter koreensis].
ACCESSION   WP_176068298
VERSION     WP_176068298.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Korner,H., Sofia,H.J. and Zumft,W.G.
  TITLE     Phylogeny of the bacterial superfamily of Crp-Fnr transcription
            regulators: exploiting the metabolic spectrum by controlling
            alternative gene programs
  JOURNAL   FEMS Microbiol Rev 27 (5), 559-592 (2003)
   PUBMED   14638413
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Green,J., Scott,C. and Guest,J.R.
  TITLE     Functional versatility in the CRP-FNR superfamily of transcription
            factors: FNR and FLP
  JOURNAL   Adv Microb Physiol 44, 1-34 (2001)
   PUBMED   11407111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429533
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..208
                     /product="Crp/Fnr family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=22907
     Region          6..203
                     /region_name="Crp"
                     /note="cAMP-binding domain of CRP or a regulatory subunit
                     of cAMP-dependent protein kinases [Signal transduction
                     mechanisms]; COG0664"
                     /db_xref="CDD:440428"
ORIGIN      
        1 mnedripedl leslgahghs rsyragaili negdpgdaiy ivlsgrlqty lssedgrdvv
       61 ladhdpgeyv gelaldgspr sasvravsps tclivrgael raflvdhpef gfhlsqkltr
      121 mvrrltkqva nlalkdvygr vvylfmetse aigseriire kltqqniaer igssremvsr
      181 vlkdltaggy vslrdgcyvi hrrlpsar
//
LOCUS       WP_176068540             140 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176068540
VERSION     WP_176068540.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..140
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15448
     Region          5..132
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mpewknicca vdfsdssrva mdyaaeiarr yeasltlvhv hdatrasgad mtlrhrqqll
       61 eawrreaefl agrpvagrml eghpaetilr fasegsseli vigthgrggl krlvlgsvae
      121 hvvhradcpv lvsrhfhrpt
//
LOCUS       WP_176068584             256 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176068584
VERSION     WP_176068584.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..256
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27311
     Region          4..244
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mtgapapila ledaaigygr evllrdltlg vsagdflaiv gpngggkttl lrtllgvqpp
       61 lggarrqprp lrvgyvpqrd hvdaywplta aevavmgryr llapgrrpga adreavraal
      121 arvgieelag vpfrtlsggq rqrtliaral asepellald eptngmdpaa eldamdvlra
      181 lhrggglavv mvshrleava nyaqrlcfvd kdkrlfrvga leamltpeal galygrrvav
      241 reeggrrfvy peaear
//
LOCUS       WP_176068614             149 aa            linear   BCT 11-JAN-2025
DEFINITION  cyclic nucleotide-binding domain-containing protein
            [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176068614
VERSION     WP_176068614.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Wang,Z., Jiang,Y., Lu,L., Huang,R., Hou,Q. and Shi,F.
  TITLE     Molecular mechanisms of cyclic nucleotide-gated ion channel gating
  JOURNAL   J Genet Genomics 34 (6), 477-485 (2007)
   PUBMED   17601606
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Kaupp,U.B. and Seifert,R.
  TITLE     Cyclic nucleotide-gated ion channels
  JOURNAL   Physiol Rev 82 (3), 769-824 (2002)
   PUBMED   12087135
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Canaves,J.M. and Taylor,S.S.
  TITLE     Classification and phylogenetic analysis of the cAMP-dependent
            protein kinase regulatory subunit family
  JOURNAL   J Mol Evol 54 (1), 17-29 (2002)
   PUBMED   11734894
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Aiba,H., Fujimoto,S. and Ozaki,N.
  TITLE     Molecular cloning and nucleotide sequencing of the gene for E. coli
            cAMP receptor protein
  JOURNAL   Nucleic Acids Res 10 (4), 1345-1361 (1982)
   PUBMED   6280140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10034975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..149
                     /product="cyclic nucleotide-binding domain-containing
                     protein"
                     /GO_function="GO:0030551 - cyclic nucleotide binding
                     [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=15865
     Region          12..118
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(80..81,90..92)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
ORIGIN      
        1 mnvvdalqra plfkdfsptg lealaeiaqe rklaagevlf qedapgdslf virsgtvrlt
       61 qrleggerev gtlgpgehlg dlgllartvr lvtasaatdc elleltrraf fkkaqdkpvt
      121 clklaavvag eiarrveasr aalrdlagr
//
LOCUS       WP_176068626             423 aa            linear   BCT 11-JAN-2025
DEFINITION  M48 family metallopeptidase [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176068626
VERSION     WP_176068626.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Bode,W., Grams,F., Reinemer,P., Gomis-Ruth,F.X., Baumann,U.,
            McKay,D.B. and Stocker,W.
  TITLE     The metzincin-superfamily of zinc-peptidases
  JOURNAL   Adv Exp Med Biol 389, 1-11 (1996)
   PUBMED   8860988
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Stocker,W. and Bode,W.
  TITLE     Structural features of a superfamily of zinc-endopeptidases: the
            metzincins
  JOURNAL   Curr Opin Struct Biol 5 (3), 383-390 (1995)
   PUBMED   7583637
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..423
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=45768
     Region          8..406
                     /region_name="M48A_Zmpste24p_like"
                     /note="Peptidase M48 subfamily A, a type 1 CaaX
                     endopeptidase; cd07343"
                     /db_xref="CDD:320702"
     Site            order(277..278,281,355,359,400)
                     /site_type="active"
                     /db_xref="CDD:320702"
     Site            order(277,281,355,400)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320702"
ORIGIN      
        1 mtqlvtglfl afflaqlave sglalanlrh varagdavpp plagrldpdt arrsraytla
       61 rgrfglaqaa wgtavtlall fsgvlpalda wlagrglgga hrfaaflaal aaatalldlp
      121 fslystfale qrfgfnratp alwlkdrlkg lllaaalglp llyatygffa ltgrawwlwl
      181 faflaavqia lvwlyptlia plfnrfaplp egplrarlee marqagfatr glyvmdasrr
      241 sghsnayftg ffrprivlfd tlvaqmtvde taavlaheig hyqarhvhrr lalglgvqla
      301 slaalawlvr wpplfqafgf aapsleaava laslgggaft fflaplssfv srrheyeadr
      361 rsvalarapa alasalvkln renlsnlhph pwysawhysh ptllerlaal ealpapaqer
      421 aga
//
LOCUS       WP_176068638             393 aa            linear   BCT 11-JAN-2025
DEFINITION  thiolase family protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176068638
VERSION     WP_176068638.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Haapalainen,A.M., Merilainen,G. and Wierenga,R.K.
  TITLE     The thiolase superfamily: condensing enzymes with diverse reaction
            specificities
  JOURNAL   Trends Biochem Sci 31 (1), 64-71 (2006)
   PUBMED   16356722
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   4  (residues 1 to 393)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..393
                     /product="thiolase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016747 - acyltransferase activity,
                     transferring groups other than amino-acyl groups [Evidence
                     IEA]"
                     /calculated_mol_wt=40635
     Region          4..393
                     /region_name="PaaJ"
                     /note="Acetyl-CoA acetyltransferase [Lipid transport and
                     metabolism]; COG0183"
                     /db_xref="CDD:439953"
ORIGIN      
        1 magrevvvvg avrtpigsfl gslagvqatq lgavvireal rragvepsav devimgnvlq
       61 agegqaparq aaryagcpdt tpawtlnkvc gsglkavvag aqaialgdae vvvaggmesm
      121 snvpyydraa rtgarmgnve lvdgmihdgl wdpydrvhmg mcaeacatsq gisrsqqdey
      181 amestrrave aakaglfkpe ivavevpgrk gektlvdede gpklarpeki pslkpvfkkd
      241 gtvtaanass indgaaalvl msaerakaeg rpvlgrltaw agaarapvef tiapadavkk
      301 llekarlgpk dvdlweinea favvsvannr ligldgknvn vrggavvlgh pigasgaril
      361 vtllhamkdl gkrrglatlc igggeavaal ver
//
LOCUS       WP_176068641             214 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrofolate reductase family protein [Piscinibacter koreensis].
ACCESSION   WP_176068641
VERSION     WP_176068641.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Slansky,J.E. and Farnham,P.J.
  TITLE     Transcriptional regulation of the dihydrofolate reductase gene
  JOURNAL   Bioessays 18 (1), 55-62 (1996)
   PUBMED   8593164
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..214
                     /product="dihydrofolate reductase family protein"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=22838
     Region          6..211
                     /region_name="FolA"
                     /note="Dihydrofolate reductase [Coenzyme transport and
                     metabolism]; COG0262"
                     /db_xref="CDD:440032"
ORIGIN      
        1 mtsvrvagfg vsldgfaagp eqsltqplgr ngpelfqwff ptrtframvg qdggstgvdd
       61 qyaqqamagf gafilgrnmf gpvrgpwpde twkgwwgdnp pyhaptfilt hhprpsieme
      121 ggttfyfvsd giesalrqar aaagdkdvki gggvetvrqy lraglvdtmh lalapvalge
      181 gealfagidl ralgfrvver aasdaathvv lars
//
LOCUS       WP_176068663             141 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Piscinibacter koreensis].
ACCESSION   WP_176068663
VERSION     WP_176068663.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..141
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14574
     Region          2..130
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mtspsqthql giavlrvslg tmwiahallk llvftlpgta qyfasigfpg wlaypvfaae
       61 laggialvlg lyarqaalal lpvmavaawv hapngwvhts tgggweypvf liaasvalwl
      121 lgdgagalrr ssalvprlgt a
//
LOCUS       WP_176068683             291 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Piscinibacter koreensis].
ACCESSION   WP_176068683
VERSION     WP_176068683.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..291
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31538
     Region          6..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          89..282
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(104..105,107..108,111,115,117..123,213..218,
                     224..225,227..228)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176118"
ORIGIN      
        1 mklvflatld ailrrgsfaa aaeeigltps avslqvkrle ehlgqplfvr tgrvaqptav
       61 arelaqslrd alaameslrv rstpvvegri avgtirtvqs stlpgalmev hrrypklsvr
      121 avlgesgalm eqlkmgglda avvirpstgg asrfrwhpla hepfvliapl dseetnlael
      181 arrydwiqfd talvsgrlaa nhlrrvlprv rgsvevdsid aivalvsagm gisvvpkprh
      241 pissvhpvre itlkdgpvre iafvcrelda dnrrvialre sfehayaasg h
//
LOCUS       WP_176068760             350 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Piscinibacter koreensis].
ACCESSION   WP_176068760
VERSION     WP_176068760.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465798
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..350
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=38528
     Region          35..346
                     /region_name="COG3435"
                     /note="Gentisate 1,2-dioxygenase [Secondary metabolites
                     biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442661"
ORIGIN      
        1 madtssltda darralkadl arfncrvaqp ddpplftrep kpdvqslhwr grdlmpller
       61 lgrevdlgag gprrtlrlhn pglpygttnt fwasiqvilp gevatahrhs anafrfvmqg
      121 dgawttvdge cypmhegdlv ltpagtwhdh vhkgsepmiw ldvldislmr mlqatffegy
      181 agsvqpvdai pdrtlrqfgs glmrppnvdv ppgsnpllay trqmaeaaln aaaglvpdpf
      241 ddvvleyrnp adggpamrtl smllqrlrpg fegrarrhtg sklyyvvrge gnttvgeqrf
      301 dwstgdfftv apwawhahrn agsgeatlfq vndtpvlkal gyyreetaaa
//
LOCUS       WP_176068716             310 aa            linear   BCT 11-JAN-2025
DEFINITION  GGDEF domain-containing protein [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176068716
VERSION     WP_176068716.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 310)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 310)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 310)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..310
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33732
     Region          28..305
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mpekrpalve qtfttpvrpe apaeqrpyll vlsgpqfgev faipagrelv lgrsadadvq
       61 lfddgvsrrh asltarerea rladlgsang twiggervke avlqdggrfq vgahttlkfv
      121 lsdhveaeyq hklaqgalhe pltglynrrh fmerlsaels saqrharpla lllvdidhfk
      181 rvndahghaa gdevlkavan vlqgavrked vlarfggeef vvlsretpls gaktlaerir
      241 raverarlrl egkekdvavt vsvgvtvsfg ltkfepgrte qqllaavera lhrakqngrn
      301 tvvaapavgp
//
LOCUS       WP_176068717             394 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Piscinibacter koreensis].
ACCESSION   WP_176068717
VERSION     WP_176068717.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Marger,M.D. and Saier,M.H. Jr.
  TITLE     A major superfamily of transmembrane facilitators that catalyse
            uniport, symport and antiport
  JOURNAL   Trends Biochem Sci 18 (1), 13-20 (1993)
   PUBMED   8438231
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455192
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..394
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41414
     Region          6..384
                     /region_name="UhpC"
                     /note="Sugar phosphate permease [Carbohydrate transport
                     and metabolism]; COG2271"
                     /db_xref="CDD:441872"
ORIGIN      
        1 mhsksvvtll nvahavdhmf llifaaavgt iardfgfsrw edlmpygvga filfgvgsmp
       61 agrlgdlwgr rsmmvvfffg igaaailaal stgpwqlaga ltligafasi yhpvgipmll
      121 qqaarpgati glnglvgnlg iavsavltgf lvqwlgwraa falpgavaiv lgfvfmrvvp
      181 heseapakrk rgqvvpltra qlarvlgvmt vaaatgsmlf nlttngnaql lnerfhgvme
      241 dpatlglllg avyaiaslaq ivvgglidrv alkplylgit laqvpmllla shaqgwwlya
      301 allgtmvfvf gaipftetvi aryvddhmrs rvagmrlavs lglsslalwl lgplvkgvgf
      361 dtlllvlagi alctsatvlw lpsedapmvp vpsr
//
LOCUS       WP_176068702             283 aa            linear   BCT 11-JAN-2025
DEFINITION  lysophospholipid acyltransferase family protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176068702
VERSION     WP_176068702.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Valentine,W.J., Shimizu,T. and Shindou,H.
  TITLE     Lysophospholipid acyltransferases orchestrate the compositional
            diversity of phospholipids
  JOURNAL   Biochimie 215, 24-33 (2023)
   PUBMED   37611890
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T.
  TITLE     Recent progress on acyl CoA: lysophospholipid acyltransferase
            research
  JOURNAL   J Lipid Res 50 Suppl (Suppl), S46-S51 (2009)
   PUBMED   18931347
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Shindou,H. and Shimizu,T.
  TITLE     Acyl-CoA:lysophospholipid acyltransferases
  JOURNAL   J Biol Chem 284 (1), 1-5 (2009)
   PUBMED   18718904
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10168420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..283
                     /product="lysophospholipid acyltransferase family protein"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006644 - phospholipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31132
     Region          61..276
                     /region_name="LPLAT_MGAT-like"
                     /note="Lysophospholipid Acyltransferases (LPLATs) of
                     Glycerophospholipid Biosynthesis: MGAT-like; cd07987"
                     /db_xref="CDD:153249"
     Site            order(87,91,94,111..114,159..161)
                     /site_type="active"
                     /note="putative acyl-acceptor binding pocket [active]"
                     /db_xref="CDD:153249"
ORIGIN      
        1 msdlgaalrq rlraltlelg gpgarerlek ltpprneygv dpygldldfa vsalapflwl
       61 yrkyfrvevh gvervptegr vlvvanhsgq lpfdaamlgv amlveldppr maralvekwv
      121 ptlpfvssfy arlgqvvgtp encrrllaad eallvfpegv rglnkpysrr yqlqdfgvgf
      181 mrlaleadap ilpvgivgae eqapalanlk svarllamps lplsptlglp lparyrlhfg
      241 eplrfhgspd dedgvleekv rtvksaierl laeglaarkh vfw
//
LOCUS       WP_176068780             217 aa            linear   BCT 11-JAN-2025
DEFINITION  class II aldolase/adducin family protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176068780
VERSION     WP_176068780.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..217
                     /product="class II aldolase/adducin family protein"
                     /calculated_mol_wt=22370
     Region          6..213
                     /region_name="AraD"
                     /note="5-methylthioribulose/5-deoxyribulose/Fuculose
                     1-phosphate aldolase (methionine salvage, sugar
                     degradation) [Amino acid transport and metabolism,
                     Carbohydrate transport and metabolism]; COG0235"
                     /db_xref="CDD:440005"
ORIGIN      
        1 mgrsapseaa lrralvdvcr alhardliga gegnvscrlg pdrllvtpag askallrpad
       61 lvvvdlagak vrgrgrpsse lrmhlaayaa rpdaqaavha hpltavaltv aglpppndvm
      121 peasvvlgev svapfatpgt devpralapl larhdvvlle rhgalalgrt laealdriet
      181 lervarvafl arlagrcepl paeavakvla aagvtrr
//
LOCUS       WP_176068849             285 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease, partial [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176068849
VERSION     WP_176068849.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         <1..285
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
     Region          179..239
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 ktkveteqlv aslqprpapr eglrrlprpe qapaalakpi eagcvevdgg ggrapalqpg
       61 atsvealtle aaaaqefrps dpprlpaprr atleplgads ysmrvtvdae lkkdldqlks
      121 llahkvqngd lgallreavk calekhgkrr gavepsrklk spapaekapp lapgqrepip
      181 aavrrevwkr dggrcawcsp dghrcgstwm leldhiqpva lggrstadnl rlccrshnsl
      241 haehvfgrer mnqfrkgadr sapptaasgs tsgacgtrae aagst
//
LOCUS       WP_176068897             368 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176068897
VERSION     WP_176068897.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..368
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39645
     Region          259..322
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mtdaralsrr iasllaeern rladflvala dfdrqrgwgt lgyaplfqyl erelrltssa
       61 aarrmtaaal vqrfpavvep lrdgrvcmsv vyelskaltp enaeevlprf yglskrgaea
      121 lvaelspvan pprrevvtav vraappcapa aaealvpert spakservqp dadlfsapar
      181 prdevvplda dlrryhvtls kaflakldaa kdalshaipd gdteavltaa ldlllektar
      241 rrglvkrprp apqkpsadpr hvpaavarea wkrdggrcsf rlpdgsvcgs tkrleldhih
      301 pvalggrsta dnlrvacwdh nslhaehvfg rkhmdqyrkd adrsapstaa ggstsgacge
      361 gaqtagat
//
LOCUS       WP_176068854             401 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Piscinibacter koreensis].
ACCESSION   WP_176068854
VERSION     WP_176068854.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006969
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..401
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45334
     Region          18..398
                     /region_name="COG3146"
                     /note="Predicted N-acyltransferase [General function
                     prediction only]"
                     /db_xref="CDD:442380"
ORIGIN      
        1 mknasqrrpa aasadegvtv eveddltaid aaewdalver qpsanpfvrh ayllaldrsr
       61 saiedtgwap hyllvrragr lvgacpvylk ghsygeyvfd wawadayrrh gltyypkllg
      121 avpftpvpgp rllaaddavr ralvlaleql aagnelssah llfvdaadqa vlrergwlmr
      181 rtvqfhwhnr spepyadfae flahlqrdkr kkiqqerrrv adagiefeqr qgsaitpadw
      241 dffyrcytlt yrahhsapyl trdffaraaa alpenwlmfi arrdgeaiaa slvvidpvrk
      301 tafgrywgtl apvnclhfea cyyrplawci angferfegg aqgehkmarg llpvetwsah
      361 wlahpqfada ignylarega giddyldeln errpfraets s
//
LOCUS       WP_176069028             369 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Piscinibacter koreensis].
ACCESSION   WP_176069028
VERSION     WP_176069028.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 369)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..369
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40119
     Region          3..369
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtaatflqir nlvkdfsghr avdnvsidia kgeifallgs sgcgkttllr mlagfetpts
       61 gsitldgqdl vplapyarpl nmmfqsyalf phltvadnia fglrrdrlps aevnarvdam
      121 lklvqlekfa grkphqlsgg qqqrvalars lakkpqllll deplgaldkk lreetqiela
      181 niiddigvtc vmvthdqeea mtmasriavm segrflqvgt paeiyetpat rfvadfignv
      241 nlmdgtlved eadhvvvdcg dcrhyvghgi tgtkgmavtv alrpekiris rsaaaeaagd
      301 patrfnraqg rikdmayfgs ytvyhlalas grvikisqsn terhddaplt wgdeawatws
      361 plaqvvltr
//
LOCUS       WP_176069038             560 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase
            [Piscinibacter koreensis].
ACCESSION   WP_176069038
VERSION     WP_176069038.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..560
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
                     /calculated_mol_wt=60502
     Region          <1..>34
                     /region_name="PRK15317"
                     /note="alkyl hydroperoxide reductase subunit F;
                     Provisional"
                     /db_xref="CDD:237942"
     Region          25..384
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          457..558
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 mnteellaqy gpreameydv vivgagpagl atairlkqra aeagseisvv vlekgsepga
       61 hilsgaimdp kaltellpdw kengaplnqp vtsddflfls etgakstpha llpdcfkndg
      121 nyvislgnvv rwlatqaeal gveifpgfaa aevlyaddgs vrgvatgnlg igkdgeptds
      181 fqlgmelvgk ytifaegsrg hlgrtliaky kldagkdpqs ygiglkelwe vtpeqarpgh
      241 vlhtagwple sdtyggafly hldnnlvelg fvvgldyanp wlspfeefqr wklhpsirqt
      301 lesgkrlgyg araitaggil slpktvfpgg afvgceagyl nasrikgsha aiktgmlaad
      361 aafdaitagh qhdelvaypa afesswlhte lqqaknfkqw fkkgrsvatl mtgieqwllp
      421 rlgikvppwt ihrkqadhly lkpasecaqi vypkpdgklt fdrlssvfvs ntnhsedqpa
      481 hltlkdptvp vrinlpkyag pesrycpaav yefvgepgae rlqinaqncv hcktcdikdp
      541 tqnivwvtpe ggggpnysgm
//
LOCUS       WP_176068981             434 aa            linear   BCT 11-JAN-2025
DEFINITION  inositol-3-phosphate synthase [Anaeromyxobacter diazotrophicus].
ACCESSION   WP_176068981
VERSION     WP_176068981.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Jin,X. and Geiger,J.H.
  TITLE     Structures of NAD(+)- and NADH-bound 1-l-myo-inositol 1-phosphate
            synthase
  JOURNAL   Acta Crystallogr D Biol Crystallogr 59 (Pt 7), 1154-1164 (2003)
   PUBMED   12832758
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Stein,A.J. and Geiger,J.H.
  TITLE     The crystal structure and mechanism of 1-L-myo-inositol-
            1-phosphate synthase
  JOURNAL   J Biol Chem 277 (11), 9484-9491 (2002)
   PUBMED   11779862
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Stein,A.J. and Geiger,J.H.
  TITLE     Structural studies of MIP synthase
  JOURNAL   Acta Crystallogr D Biol Crystallogr 56 (Pt 3), 348-350 (2000)
   PUBMED   10713523
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10547093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..434
                     /product="inositol-3-phosphate synthase"
                     /EC_number="5.5.1.4"
                     /GO_function="GO:0004512 - inositol-3-phosphate synthase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006021 - inositol biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0008654 - phospholipid biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=47215
     Region          15..409
                     /region_name="NAD_binding_5"
                     /note="Myo-inositol-1-phosphate synthase; pfam07994"
                     /db_xref="CDD:462335"
ORIGIN      
        1 msklsirpqr pgdrlavlmp glgavattai agveavkrkl gqpigsltql gylleedgsf
       61 gpsiqkvvpm pqldelvfgg wdpiadnvyq aarrakvldh hlvdqleepl savkpmkavf
      121 dkswvrrldg pnvktgskka maealcedir gflqkngcar gvmvwtgste vyaevgpahq
      181 slkafeaale ksdptiapsm iyayaalkcg laylngapnl sadipalrel aereglptgg
      241 kdfktgqtlm kttlapmlha rllglegwfs tnilgnrdge vlddkdsfkt kevsklgvld
      301 aildaekype lyqdidhkvt ihyypprgdn kegwdaidik gwlgygmaik vnfqcrdsil
      361 aaplvldlal lgdlahrage kgpqewlsff fkspvtvpgr ravmdlfrqq rnvhqqlrry
      421 aeaiaasaag akvg
//
LOCUS       WP_176069143             528 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Anaeromyxobacter
            diazotrophicus].
ACCESSION   WP_176069143
VERSION     WP_176069143.1
KEYWORDS    RefSeq.
SOURCE      Anaeromyxobacter diazotrophicus
  ORGANISM  Anaeromyxobacter diazotrophicus
            Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
            Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Anaeromyxobacter diazotrophicus"
                     /db_xref="taxon:2590199"
     Protein         1..528
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=56000
     Region          1..528
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mtglgfkqkv lllpavatat llvmgatdla lgaraitllq eletervpiv tssrdlqeql
       61 erlqralqda vaaedleaia etaklrdafl araaeaasgd drsppravsa efrayyahar
      121 aaaeqlvarr tapqvleetv aryralrdel aartaadrrr laegfqevrr lqrlrafvmg
      181 gltlaavafl awlaawvgrs varpvlelar aaqrvaagdl shglgvhpqd elgelarsfe
      241 vmveklrvvp asllgsveel saavgavasa sgtqgallek qqaglarsrt taerihrese
      301 etsrraeavl kmagqveafg daaqlaardt ltglsdigee vramtdgigr ltahtqlvre
      361 lvlamkrlga eatelalsvs veaaragase gplsgsarql hevaarlvqa sgrvtkalge
      421 vdavvasvga lsdghkrrme kgleqirtsg eslreitavv qksgraarai vasvteqgqa
      481 iaeitkdvve idramgealr skrsaeraae slkratnsia gvvqsfrv
//
LOCUS       WP_176069180             285 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Betaproteobacteria].
ACCESSION   WP_176069180
VERSION     WP_176069180.1
KEYWORDS    RefSeq.
SOURCE      Betaproteobacteria (b-proteobacteria)
  ORGANISM  Betaproteobacteria
            Bacteria; Pseudomonadati; Pseudomonadota.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 285)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Betaproteobacteria"
                     /db_xref="taxon:28216"
     Protein         1..285
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=29641
     Region          15..283
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 maltliglsi glllflvaag ltlifgllgv infahgafym lgayigyqav astgsfwlal
       61 altplivlpa gallervllr plyakphaqq lvmtfglilv meeaarmvwg lgylrvsppa
      121 alagtteifg syigdyrifa cvvaavvaag lllglertsl gatiraaaan prmlsclgad
      181 vnrlrmwtfg ggtalaafag vlvsplvpid sgmaitvitd cfvvivvggl gnargaiaas
      241 llvgllrafg qqfaaewvdv atyglliftl lirpaglfnq rtrta
//
LOCUS       WP_176069181             337 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: branched-chain amino acid ABC transporter permease
            [Betaproteobacteria].
ACCESSION   WP_176069181
VERSION     WP_176069181.1
KEYWORDS    RefSeq.
SOURCE      Betaproteobacteria (b-proteobacteria)
  ORGANISM  Betaproteobacteria
            Bacteria; Pseudomonadati; Pseudomonadota.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Betaproteobacteria"
                     /db_xref="taxon:28216"
     Protein         1..337
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=34585
     Region          48..333
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mkpaspsvgn csaepqapss lghsfgkrat ltaaallama alsaaiappa vhyfltsaai
       61 waifalgfdl afgvagllsf ghsvffaagg ylaalltmla gipmsgaipl aglsagilaa
      121 lvgmlalrms gvylglttla vsqlfetlva vrlraytggm eglvgvarpa ifghvldddr
      181 syflfvfaif mmvlgasall rqshwgrglv amrinevraq qlgfntlrlk isafaasgai
      241 sgvagallas lmrfvnpeil swtisgdvli atliggagtl lgpalgallm sclrevlggm
      301 tthwhgllgv vlivftlwvp nglapavqgl vrklrng
//
LOCUS       WP_176069294             391 aa            linear   BCT 11-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Piscinibacter
            koreensis].
ACCESSION   WP_176069294
VERSION     WP_176069294.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447265
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..391
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=42683
     Region          <36..112
                     /region_name="XkdP"
                     /note="Cytoplasmic potassium-binding protein
                     Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion
                     transport and metabolism]; COG1652"
                     /db_xref="CDD:441258"
ORIGIN      
        1 msrrirfalt tggavaaaql alalaapaah aanypvtpeq rsiaartaet gipvselvpn
       61 apdtytvrpr dtlwdisamf ikspwrwpel wgmnleqvrn phliypgqvl vldtsdgrar
      121 lrlgrrvdgg gplgdarlsp rvrseavald gissipfnli epflneavif etnelsaapr
      181 ivaaqegrvm lsrgdiayvr gelggqreyr ifrtpralkd pttnevlgye atyvgsseyv
      241 rqgetrtgad gkpeivpatf tvtsirqeag igdrlapvpp rdysnyapha paapmdgriv
      301 siygdaltag qnqivalnkg ardgierghv lalwrsgssv ldrtdggrer irlpderhgv
      361 lfvfrvfdrm syalimqvqe pvkpgdrftq p
//
LOCUS       WP_176069328             260 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter permease [Piscinibacter koreensis].
ACCESSION   WP_176069328
VERSION     WP_176069328.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..260
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26864
     Region          9..233
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mngsaidpai llpafaagll vlathvplga evlrkgivfi dlaiaqiaal gvilaglmev
       61 dphgwqvqaa aavaalagaa llvwterrwp evqeaqigvv fvlaatagil llaknphgge
      121 hlrdlltgqi lwvgypqlvv paiatllvga flwriaalpr safyllfaia vtvsvqlvgv
      181 ylvfatlivp algvrgyrae rrlplayaig aagygsglvl saavdlpsga livwclaila
      241 alahamapkr gaerpvnaar
//
LOCUS       WP_176069322             227 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Piscinibacter koreensis].
ACCESSION   WP_176069322
VERSION     WP_176069322.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..227
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23734
     Region          6..221
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mspsnetvsl qasdghrfsa yvarpasapr gaivvlqeif gvnshirsvt dgfaadgwla
       61 iapalfdrte rdvqlgytad dvargrtlkg avddeqvlld iaaaqahvad agpvatigyc
      121 wggtmswlaa arlpglaaav ayygsgiagl ldeaprcpvl ahfgdkdssi ppsaidalrk
      181 ahpqvevhvy padhgfncdq rasfdaasar tarertlafl gahaskr
//
LOCUS       WP_176069329             213 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Piscinibacter koreensis].
ACCESSION   WP_176069329
VERSION     WP_176069329.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..213
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=22491
     Region          20..209
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mlslpelawf alaalllvlt pgpnmiycvs rtlcqgraag vlslagvlvg fvfhvlaaal
       61 gltallaavp yafdavrlvg aayllwlawq avkpdgqapf aarslphdpp arlfrmgflt
      121 nvlnpkvamf ylsffpqflh pdrgsvflqs aalgavqiti sglvnlmlvl gaasvtavls
      181 rsegwlraqr yvmgsvlali avkiatdtrk tag
//
LOCUS       WP_176069331             365 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Piscinibacter
            koreensis].
ACCESSION   WP_176069331
VERSION     WP_176069331.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..365
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=39759
     Region          81..335
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 mewtdnwvla pwgrlallav vaivgatvah rvlrpiamrv grystvlaav frridqpvqf
       61 ilpllallvl wqgvpgdvag isavehttav ltilavtwla sasvhgvaea vitshpldla
      121 dnlearriqt qtrvlariah ttvivaglaf vlmtfpkarq vgtsllasag vaglvlgiaa
      181 rpvfgnlvag lqialaqpir iddvliiege wgrveeitat yvvlkiwder rliiplqwfi
      241 ehpfqnwtrr gaellgtvfl wvdytlpvep irtearrlce gasewdgrvc vvqvtdtsek
      301 smqlrilvsa assslafdlr ckvreglidf iqrehpaalp rartdvesar gatpgalsaw
      361 aaaer
//
LOCUS       WP_176069335             259 aa            linear   BCT 11-JAN-2025
DEFINITION  TlyA family RNA methyltransferase [Piscinibacter koreensis].
ACCESSION   WP_176069335
VERSION     WP_176069335.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439687
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..259
                     /product="TlyA family RNA methyltransferase"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=27201
     Region          1..257
                     /region_name="YqxC"
                     /note="Predicted rRNA methylase YqxC, contains S4 and FtsJ
                     domains [Translation, ribosomal structure and biogenesis];
                     COG1189"
                     /db_xref="CDD:440802"
ORIGIN      
        1 mrldqllvsr glaptrsaaq rliaaravrw ngpkgwavpk kagedvtedc elevtddael
       61 rfvsrgglkl agalercgih psgldcldig qgtggftdvl lqrgarhvvg idvgrgqins
      121 tlaadprvtt yeginardia gsafeaalpp dgfaivvadv sfitlthvlp tvarclasgg
      181 nalllvkpqf elqpvdigkg givkgpnayi rvqqrirdac aalaldvrdy fqspidggdg
      241 nheffvwatp aagateakp
//
LOCUS       WP_176069376             356 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Piscinibacter
            koreensis].
ACCESSION   WP_176069376
VERSION     WP_176069376.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..356
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38115
     Region          40..346
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mltrllshdl prnrllsvvl lvvlvalaaa pflfastral nvaakvmvfi vlaasfdlll
       61 gytgivsfah tmffgigayg vaiasthwgp gwaavavgal aalllaalls fviglfslrv
      121 raiffamitl avasafltla sqlsaftgge dgltfrvpea lqpgtqyvdd pvlgasvdgr
      181 fvtyyllfvv slglvlamlr ivnspfgrvl qairendfra eaigyrtvvy rtlsnvlaal
      241 faalagvlla lwlryngpdt tlsfeimldv llivviggmg tiygavvgsv llvlaqnylq
      301 dlmkvgagav egvpvlsqli spdrwllwlg ilfvlsvyyf psgvvgrlra wrarrr
//
LOCUS       WP_176069382             308 aa            linear   BCT 11-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Piscinibacter
            koreensis].
ACCESSION   WP_176069382
VERSION     WP_176069382.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..308
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33292
     Region          43..298
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mfllqppkvc elalftslpq rfrkrvdsvw aaanrggqpt dsflegpvfd rhgnlyvadi
       61 pfgrvfrida agdwtlvaey dgepnglkfl ddatlliady knglmqldla sgnvrgyldr
      121 rnterfrgln dlvfdgagal yftdqgqtgl hdptgrlyrl rpdgkldlll anvpspngvc
      181 lspdgrvlyl avtrangvwr vpllpdgsva kvgqfftsyg psgpdglaid eqgrlivanp
      241 glgyvwvlna raepewilrg pagasttnia fggegrrtlf vtdsthgnvl carldtagpp
      301 lhqgrsap
//
LOCUS       WP_176069523             186 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF3299 domain-containing protein [Piscinibacter koreensis].
ACCESSION   WP_176069523
VERSION     WP_176069523.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..186
                     /product="DUF3299 domain-containing protein"
                     /calculated_mol_wt=20663
     Region          33..184
                     /region_name="COG3495"
                     /note="Uncharacterized conserved protein, DUF3299 family
                     [Function unknown]"
                     /db_xref="CDD:442718"
ORIGIN      
        1 mnelrlsrrd mallmlaggl gcvgdkaraa ekaasirrls wdelipkdwd pqkffrdkqv
       61 gavregdvge ralmremrqi wdnaptrlel nglvvklpgy vvpvemlvgd ikefllvpyf
      121 gacvhtpppp anqlvyvtle apkplktmdv vwvtgtmrte rngspfgnsg yrleasavep
      181 yrapar
//
LOCUS       WP_176069527             251 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Piscinibacter
            koreensis].
ACCESSION   WP_176069527
VERSION     WP_176069527.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..251
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26615
     Region          7..240
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mpsshcpgep airthdltis yrgrpavwrv saeipagalt alvgpngagk stllaalaga
       61 vprfegavdr aavrriaylp qastldlgfp irvqevvssg lwfrigsfga vgsaeraqia
      121 galdavglgg lerrwmrels agqvqrvlfa ralvqdaglv lldepfaamd erttadllgv
      181 lrvwtregka vvlvthdlaq artrcdharl latelvafgp vsevltsehl saarrvaeqw
      241 riadgpyraa a
//
LOCUS       WP_176069730             853 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Piscinibacter koreensis].
ACCESSION   WP_176069730
VERSION     WP_176069730.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 853)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 853)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 853)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 853)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 853)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 853)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 853)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459725
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..853
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..853
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=90459
     Region          13..851
                     /region_name="YbbP"
                     /note="Predicted ABC-type transport system involved in
                     lysophospholipase L1 biosynthesis, permease component
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG3127"
                     /db_xref="CDD:442361"
ORIGIN      
        1 mteasrppap lvpsawrlgw rqlmrdfrag elrllvvavm lavaalsavg ffadringgl
       61 ardarqllgg daivasdqpa ppafaerara lglavattas fpsmgrapde kggatrlvsv
      121 kavsdayplr gelrlnsgpd tpetgarrap vrgkawvdpa lldalglkvg dplllgdasl
      181 aiekviaiep drgtgfssfa prvlineadl patgliqpas rvgyrlavaa pdpnrdravr
      241 qfvdwaeahv kgnqlrgvrv esletgrpem rqtldraekf lnlvallaal laavavgias
      301 rdfatrhldd camlrvlglp qrtialqylt efgligvlas vaglvvgfav hhvfvlllag
      361 lvkaslppps lwpalfgvgv gftlllgfgl ppvlqlarvp plrvirrdvg amkpaslavl
      421 aagalgfaal llgvssdlkl gaiavggfaa avavfallsw lalallrrav pearaprwlv
      481 latrqlaarp afavlqvsal avgllalvll allrtdligs wrsatpkdap nrfvinvqpa
      541 qadafqqrlr eagvtrydwy pmirgrlvai ngravdpday adtraqrlld refnlshspa
      601 lpghntvegg rwvpdepnal svesglaetl glklgdrlrf dmagetaegr itslrkvdws
      661 smrvnffvlf pttemadapv tyiaayqapk vagfdnalar dfpnitsidv satiaqvqgv
      721 idqvvravef lfgftlaagl vvlfaaitat reararefav mralgasarl laqvqrgell
      781 gvgalagvla slaaiavswa larwvfefsw npapwvpiag gaagallals agwwglrevl
      841 rrpvvqtlrq aad
//
LOCUS       WP_176069769             349 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Piscinibacter
            koreensis].
ACCESSION   WP_176069769
VERSION     WP_176069769.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 349)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..349
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37249
     Region          32..277
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mtrkqpsrrl fvatlsglal aaaslpataq etpirfqldw rfegpaalfl mpitkgyfka
       61 eklnvtvdag ngsggtvtrv asgsydmgfa dmaalmefqa nnptapnkpv avmmvynntp
      121 aavlalkksg iakpadlngk klgapvfdag rkawpifaka nnigsvawta mdptlretml
      181 vrgdvdaitg fsftsllnie argvktgeiv vlpypeygvk lygnaiivse dflkknpeav
      241 kaflraftkg ardviadpqa giatvkardg iineqlelrr lklaldasvl tpdaradgfg
      301 avngprlslm asqvsdafgt kervnvanvw rdgflpsaae rdvfkvark
//
LOCUS       WP_176069826             237 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Piscinibacter koreensis].
ACCESSION   WP_176069826
VERSION     WP_176069826.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..237
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=25676
     Region          63..155
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mstapepdea aevraryarr haadrrysll epaallasqe rqralqrafr tagiddvarv
       61 tllevgsggg gnllemlwlg faaenlagve llaerhatar arlpeavrlt lgdattaplg
      121 asdvvyvstv fssllddafq qrlaaaiwaa vkpggavlwy dftvdnprnp dvrgvpltrv
      181 ralfphgrvg arrttlappi arrvcrlhpa lytwlnalpf lrthvvawia kpplpsp
//
LOCUS       WP_176069944             424 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Piscinibacter koreensis].
ACCESSION   WP_176069944
VERSION     WP_176069944.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..424
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=44777
     Region          223..415
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(230,271,307,395,398)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(230,395,398)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(230,271,307)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 mkskvlptqp tdragikldr rafvvgvpav aaglgwsnea aaisrqdlns saswstapvs
       61 aapaaanqin nqtirqqvhl svggdslrvk lsnrygttpl lisgasvalt gsadqiaags
      121 arqllfngrp tfnipafgel ysdwiswnvp negdltidvy iasntssgts pvtlhnarpa
      181 tqvlsylgeg nqlgagsfta ttsrtawyfl tgvdvsnars pgsvvcfgds itdgsqstpn
      241 tntrypdyla rrllaatasa pmgvvnlgig gnrvltggtg dpalarfdrd vlsqtgayti
      301 ivlegindis ggatadriie ghrqlitrah akrkrilgat ltpygaapea reaqrvvvnd
      361 wirnsgmyda vidfdlatrd panprvmrae fdsgdtlhpn slgyqamana vdlaqlirpr
      421 prlf
//
LOCUS       WP_176069974             424 aa            linear   BCT 11-JAN-2025
DEFINITION  M48 family metallopeptidase [Piscinibacter koreensis].
ACCESSION   WP_176069974
VERSION     WP_176069974.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Bode,W., Grams,F., Reinemer,P., Gomis-Ruth,F.X., Baumann,U.,
            McKay,D.B. and Stocker,W.
  TITLE     The metzincin-superfamily of zinc-peptidases
  JOURNAL   Adv Exp Med Biol 389, 1-11 (1996)
   PUBMED   8860988
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Stocker,W. and Bode,W.
  TITLE     Structural features of a superfamily of zinc-endopeptidases: the
            metzincins
  JOURNAL   Curr Opin Struct Biol 5 (3), 383-390 (1995)
   PUBMED   7583637
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11574938
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..424
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.24.-"
                     /GO_function="GO:0004222 - metalloendopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=45978
     Region          8..410
                     /region_name="M48A_Zmpste24p_like"
                     /note="Peptidase M48 subfamily A, a type 1 CaaX
                     endopeptidase; cd07343"
                     /db_xref="CDD:320702"
     Site            order(282..283,286,364,368,408)
                     /site_type="active"
                     /db_xref="CDD:320702"
     Site            order(282,286,364,408)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320702"
ORIGIN      
        1 mtadtftlvf avslvlslal rfwlsarqir hvarhrdtvp aafagsvsie ahrkaadyti
       61 akarfsqlsm afgavvllgw tlfggldald rwlrgvvvpl agsrayeval vmavvaigal
      121 vdlpfemwst frleqrfgfn rmtwrlylsd lvkgaviall igtpiaaail gimaaagslw
      181 wlwawiawtv fmvlalvvvp tfiaplfnrf epladaslre rvealmarag faakglfvmd
      241 gsrrsahana yftglgrakr vvfydtllar lvpaeveavl ahelghfrlr higkriastl
      301 aisflgfall gwlasrswfy aglgvapsls gvnnalalvl fmlvvpvygv flspllsgls
      361 rrhefeaday asrladggql asallklhad nattltpdpl varfyyshpp aaerlaalaa
      421 atah
//
LOCUS       WP_176070016             187 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Piscinibacter koreensis].
ACCESSION   WP_176070016
VERSION     WP_176070016.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..187
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20453
     Region          5..166
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 maenirvavf vgslraesyn rrlalalarl apetftfehv aigdiplynq drdvnppeam
       61 trlkhevesa qallfvtpey nrgipgvlkn aldtasrpwg knsfagkpag vvgisvgaig
      121 talaqhqlrn vlayldvptl gqpevylqfs egllddagni ykddtrrflq gwvdayvawv
      181 rrfvaas
//
LOCUS       WP_176070060             271 aa            linear   BCT 11-JAN-2025
DEFINITION  TatD family hydrolase [Piscinibacter koreensis].
ACCESSION   WP_176070060
VERSION     WP_176070060.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..271
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29054
     Region          2..264
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mwidthchld aaefepdrea vvaramaagv rqivlpavdv gnfdavrela hrhglayalg
       61 ihpllvdraa dadldrlrga laehradprl vavgeigldh fvpgldharq drflaaqlrl
      121 arefglpvll hvrrsvdavl khlralsvpg giahafngse qqaevfgalg fklgfggnvt
      181 fdrarrirhv aaqvapeliv letdapdiap qwlyqtaaer aagatmrnep aelariagvl
      241 aelrgvtpda laaatnenay avlprlrala g
//
LOCUS       WP_176070113             332 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Piscinibacter
            koreensis].
ACCESSION   WP_176070113
VERSION     WP_176070113.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 332)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..332
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35053
     Region          13..318
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mnrhsnglsr rhllalacal pvaaraqgap lekitvagws kpivevtpll vdadkgfyra
       61 qgidleyvpg tgggdairnl lsgradvaft dpgsffaald kgeklvavyd vypqnvfnvv
      121 alkksgirtp adlrgkrigv yslasgtrqn lqvllhqagl seadvtvvvt gilnfapllq
      181 gqvdataatd tgllvgrrrg lgevevidva rhlnvssdlf vvteaayrsr kaalarflra
      241 yrdaaawmia apeeaaglat traidgsdpa lnleivrlrn aasvsdltrq kglgaldvas
      301 lqaaadvyrk lglvrqplai arhaavdllp gr
//
LOCUS       WP_176070148             511 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Piscinibacter
            koreensis].
ACCESSION   WP_176070148
VERSION     WP_176070148.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..511
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54784
     Region          3..511
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mkfgsflash alrmgekdav vsggerigfa eleastnria hglraagvev gdrvalylpn
       61 giafvqafig iikagalvvp vnlplsvpei ahlltdcepk aafigsstaa ayaraaegrp
      121 rivrigadaa caadltlaal margqdepld lpyaaddcmv aytsgttgra kgvvltqsnf
      181 vfvngylngy hwrlgaddvq lcttplahrt amarlmnmil hgstlvvmar fdaaeatrlv
      241 rdekvtvfgm vptvgrmmlp eieahpehfa svrvmtvtge afpldvkrrl adalpqvrfy
      301 sflaqtecga itgldsseaf shptsvgrpw pgvdvrvvda dgrtlptgea geiwvrsgtp
      361 glystmrcyf rrpeetaati rdgwlatgdv grfdadgyly lmdrkkdmvl sggyniyske
      421 vemalmshpa vadaavigvp dpafgeavca yvelergasv daealiahcr eqiasykkpk
      481 hllfvealpr tstgkvqkav lreqyaarta a
//
LOCUS       WP_176070152             249 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Piscinibacter
            koreensis].
ACCESSION   WP_176070152
VERSION     WP_176070152.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..249
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27512
     Region          59..243
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mpnaavtrrk pararadaaa ppdapveiga rprrvaiega andgatprrk tlrqgealtr
       61 khvlgtvyel isrdgienls mrkvavaagl stgtinyhfg nkqrlliaal esayelpddw
      121 eryqgspvaq lerlltgyvc rlptdrfwrf winylassvr daellthqtd rlqrqqrfwt
      181 rlihdgiaag elasgvdaar kaeellilah glvlrqladp geasrdlare lllgqvrqmr
      241 aparrasta
//
LOCUS       WP_176070175             160 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA thioesterase [Piscinibacter koreensis].
ACCESSION   WP_176070175
VERSION     WP_176070175.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..160
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17726
     Region          2..146
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 melpahqlam tvlmtpdtan fagkvhggtl lklldqvaya casryagryv vtlsvdqvtf
       61 rqpvhvgelv tllasvnhtg tssmevgikv iaedirtqrs rhvnscfftm vavddegkpv
      121 pvpalrpfsp derrrhaaai vrkemriese rrfaelrder
//
LOCUS       WP_176070176             148 aa            linear   BCT 11-JAN-2025
DEFINITION  potassium channel family protein [Piscinibacter koreensis].
ACCESSION   WP_176070176
VERSION     WP_176070176.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Bezanilla,F.
  TITLE     Voltage-gated ion channels
  JOURNAL   IEEE Trans Nanobioscience 4 (1), 34-48 (2005)
   PUBMED   15816170
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Choe,S.
  TITLE     Potassium channel structures
  JOURNAL   Nat Rev Neurosci 3 (2), 115-121 (2002)
   PUBMED   11836519
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Miller,C.
  TITLE     An overview of the potassium channel family
  JOURNAL   Genome Biol 1 (4), REVIEWS0004 (2000)
   PUBMED   11178249
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Doyle,D.A., Morais Cabral,J., Pfuetzner,R.A., Kuo,A., Gulbis,J.M.,
            Cohen,S.L., Chait,B.T. and MacKinnon,R.
  TITLE     The structure of the potassium channel: molecular basis of K+
            conduction and selectivity
  JOURNAL   Science 280 (5360), 69-77 (1998)
   PUBMED   9525859
REFERENCE   5  (residues 1 to 148)
  AUTHORS   Perney,T.M. and Kaczmarek,L.K.
  TITLE     The molecular biology of K+ channels
  JOURNAL   Curr Opin Cell Biol 3 (4), 663-670 (1991)
   PUBMED   1772658
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10545436
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..148
                     /product="potassium channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005216 - monoatomic ion channel activity
                     [Evidence IEA]"
                     /GO_function="GO:0005267 - potassium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0034220 - monoatomic ion transmembrane
                     transport [Evidence IEA]"
                     /GO_process="GO:0071805 - potassium ion transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=16297
     Region          <89..134
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
ORIGIN      
        1 myedwianla vaattglava lcilthyegl lglsrrlavr vrdqrmkvfy aivsllflhv
       61 aeiwifgiaf wgllewpacg altgrahpll davyfsaitf stvgygdmvp sgpvrllagt
      121 eslvglvlit wsasftylem erfwkprg
//
LOCUS       WP_176070209             359 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Piscinibacter koreensis].
ACCESSION   WP_176070209
VERSION     WP_176070209.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..359
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=38868
     Region          120..356
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mnatmtgssd wiltqfarqa slsrhqalgi vvamilsial adylseirls laifyfvpil
       61 lavgwlgtra avavsvasia fkligdvfel sggplpfwiw wnaastlvvl llvvwvcghl
      121 itlyreleqr vaertreilm lsqerrrler ellnasaner nlmgqelhde icqhlvgttl
      181 aaqvlcqrla qqqnplaqda qaiialietg igktrqlarg lllseiapeq lperindlvd
      241 essssglacr fshagdvava dpataaqlyr iaqealrnav rhagatrvdv tlagdrqnvs
      301 lvveddghgl sqersgsgmg lpimshraay igaslsiert erqgtrvvcv lpragaaea
//
LOCUS       WP_176070251             207 aa            linear   BCT 11-JAN-2025
DEFINITION  SCO family protein [Piscinibacter koreensis].
ACCESSION   WP_176070251
VERSION     WP_176070251.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Chinenov,Y.V.
  TITLE     Cytochrome c oxidase assembly factors with a thioredoxin fold are
            conserved among prokaryotes and eukaryotes
  JOURNAL   J Mol Med (Berl) 78 (5), 239-242 (2000)
   PUBMED   10954195
  REMARK    Erratum:[J Mol Med 2000;78(5):243-4]
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005092
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..207
                     /product="SCO family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22519
     Region          54..205
                     /region_name="Sco1"
                     /note="Cytochrome oxidase Cu insertion factor,
                     SCO1/SenC/PrrC family [Posttranslational modification,
                     protein turnover, chaperones]; COG1999"
                     /db_xref="CDD:441602"
ORIGIN      
        1 macalgrhrf tsvsrrgala laaafalaac drqpddrafq siditgadwg rdfrlldadg
       61 rsvqlvdfrg rcvllffgfk qcpdvcptal dratdamrhl gpqaarlqvi vvtvdperdt
      121 pavlreypra lhpsfiglha dlattaataq afkvfyrkvs tggsytmdht vtsylfdpkg
      181 rlrlavkheq saasvaadia rlskenp
//
LOCUS       WP_176070269             357 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Piscinibacter
            koreensis].
ACCESSION   WP_176070269
VERSION     WP_176070269.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..357
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=38581
     Region          47..344
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mffrqagihh styrgdrqlf pipfdrwqia vllvlavaap vllsplymks ymlpwliwta
       61 aalglnlvlg wagqfhfgya aimgigayta vhatlkgipf eialllagsv stligsafai
      121 talrvrglyl alstlalqfv mdwvinkvpa vsggtqatiq applrllgie vssdaglyyv
      181 alvwcvlvti fmlnlrrsgl gralvavrek dfaaavigvn sfyyklvafa mssfiggvtg
      241 ailiftfyra vtpeqfavnv siqvlamviv gglgsvigcy fgvafilllp givanlifaa
      301 aqaadlkigi ellahipafl ygvliigfll feplglakiy snlrnyfifw pfgyarr
//
LOCUS       WP_176070274             385 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Piscinibacter koreensis].
ACCESSION   WP_176070274
VERSION     WP_176070274.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..385
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41711
     Region          1..384
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfdpspeqr aiaettrrfv ekemprhkvl qwardkvepp qelfmklgal gyygfllpea
       61 ysglekpdpm gmlafveqfa rassaittaw graavilapl varfgtqaqk dlvlprvmrg
      121 evfmalglte pgsgsdaasl rttavrrddg hwvingekly csqvksagfl ilaartdpqa
      181 vkqegittfl ipdpgsdpai kltrietmgl gpvptfaahf delvlppdav igqvnkgwqc
      241 vlggldnerl yhgaigvgas qaiidevsay lkqrvqfgkp lsklqsvrhk ivdmqlrvea
      301 arllvyrggs vlektgachn easfakvaga ecymhcattg lhllggygyt vdsgmpmhfq
      361 daklfeiggg amevqrdiia rglgl
//
LOCUS       WP_176070293             385 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Piscinibacter koreensis].
ACCESSION   WP_176070293
VERSION     WP_176070293.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..385
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42506
     Region          4..381
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mpidfsfsee qnllrdsvra mldriatpey irrcdqepry pselydayve mgllrmpfpe
       61 svgglggsvi dfaviaeelg rksydflgay gtcvfnglni lhngteaqrq hwlprlldgr
      121 ikmsismtep gagsdagamr tsarrdgehw vingqkvfst gagaernvin lyarskpegp
      181 hqealslflv dkdtpgitlr kldtlgrrsl gtyevfldkv rvpadrlvge phkawgymla
      241 glqlerlmta agyaggaqaa mdlalayake rqqfgkpigs fqaiahmlad mqtavdasrm
      301 llwraawqle rgedalmais qaklfgseay anianqgmqi mggygyimef dmqrhyrdar
      361 attitagtsq mqrnliaglm glktk
//
LOCUS       WP_176070258             345 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Piscinibacter koreensis].
ACCESSION   WP_176070258
VERSION     WP_176070258.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..345
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=36141
     Region          1..345
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mataslaaqa qssvtlygli diapamvsrt ntaddrqfrl nsdtgsssrf gvrgtedlgg
       61 glaaffnles pldakngsva ggaasgacnv aaacasattp afwrrnayvg lrggfgevtf
      121 grnytaavik qaatvsatps gintgmatnl aaqgisndfw nsnqirydsp kfgpidfsah
      181 valgegvtgr nvggnvgynd gplaislsyq rdenlagdav kwmilsgsyn fgsfkvhvaf
      241 ddvnndervv gfrdskfwtv gasfkatpll tvaaqywnlk dsassnsskq vvlnadylls
      301 rrtalfamlg hvnnkdiavl plwnsgvtva ndkvyglaag vrhsf
//
LOCUS       WP_176070301             260 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Piscinibacter
            koreensis].
ACCESSION   WP_176070301
VERSION     WP_176070301.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..260
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=27915
     Region          6..253
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mteaavlvar rdaiceitln rpeqrnamap ellqafqqvi dqvkadrdir cvvitgsgtn
       61 fcsgadfrst ildrgnelph easyaiyrpf ltildvqvpv iaamnghaig ggfglglvcd
      121 lrvanreary ganfarlglh sgmaisyllp rvcgvpraae llftgrvfsg aeaaemgian
      181 havepaqvla rarelaaeia anapvavrmm krslyrgldw dpksageiea llqsrtldma
      241 dakegvaall ekrtpqfrga
//
LOCUS       WP_176070303             363 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Piscinibacter koreensis].
ACCESSION   WP_176070303
VERSION     WP_176070303.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..363
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37518
     Region          8..325
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mselslplae aadrllsqrc dsrlvaaada gqwpqalwqa veelgpgqll apeaeggagg
       61 dwldacalle raaarcaplp iaqtllagwl rsrvglapaa gpaavaftta plealraagr
      121 adlteadgpv vawaeqashv allgaddagt aqllwlprac vhvravagsa wpaarvgsag
      181 iplhaaagas ptqawcialp glslaevrar aallsaaqia galgrllemt vaytgervqf
      241 grsigqfqgv qhqlaqlaee aaaarvavqa aaatedprrf vaaaaaakvr vgeaaglgtr
      301 iahqlhgaig vtaehtlhly trrlrewrde hgsetfwara lvqairqdge rsawqavvac
      361 tsr
//
LOCUS       WP_176070333             295 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Piscinibacter
            koreensis].
ACCESSION   WP_176070333
VERSION     WP_176070333.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..295
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=31200
     Region          22..295
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 miieflnyal ngallgllya lvamgfvviy raskvfnmat gemlvlgafl vwwavasrgl
       61 hpalgiaaal aiavllglai erlffrrlig esvfsmimvt iglliltrgl vlviwgpqer
      121 afpaliplap livgemiipr plaaagvvav vfafalhrff nrsrtglams avaedhqial
      181 smgisvrrsi afawalggvl svissivyls gksltflsse igfaalpval laglesirgl
      241 llagvivgvv qgltsayvdp liggnaasvv pylfmlvvla vrpngmfgwk rierv
//
LOCUS       WP_176070352             146 aa            linear   BCT 11-JAN-2025
DEFINITION  PaaI family thioesterase [Piscinibacter koreensis].
ACCESSION   WP_176070352
VERSION     WP_176070352.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Song,F., Zhuang,Z., Finci,L., Dunaway-Mariano,D., Kniewel,R.,
            Buglino,J.A., Solorzano,V., Wu,J. and Lima,C.D.
  TITLE     Structure, function, and mechanism of the phenylacetate pathway hot
            dog-fold thioesterase PaaI
  JOURNAL   J Biol Chem 281 (16), 11028-11038 (2006)
   PUBMED   16464851
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130874
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..146
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15495
     Region          27..137
                     /region_name="PaaI_thioesterase"
                     /note="PaaI_thioesterase is a tetrameric acyl-CoA
                     thioesterase with a hot dog fold and one of several
                     proteins responsible for phenylacetic acid (PA)
                     degradation in bacteria. Although orthologs of PaaI exist
                     in archaea and eukaryotes, their function has not...;
                     cd03443"
                     /db_xref="CDD:239527"
     Site            order(48,82,89..92)
                     /site_type="other"
                     /note="CoenzymeA binding site [chemical binding]"
                     /db_xref="CDD:239527"
     Site            order(49,51,54,83..87,89)
                     /site_type="other"
                     /note="subunit interaction site [polypeptide binding]"
                     /db_xref="CDD:239527"
     Site            order(50,58..59,62..63,82)
                     /site_type="active"
                     /note="PHB binding site [active]"
                     /db_xref="CDD:239527"
ORIGIN      
        1 msdkpvsvpt hahgpfqelv gyetltegdr pylrlpvrrd llnphgvlhg gvsltlldai
       61 ggrslvgqlv patgqrilss vtvtlttdfm lgvrdgvlfa tgspdhigkt vayvsvelrh
      121 namdgplvar glgtyrvytr slvspv
//
LOCUS       WP_176070355             345 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Piscinibacter
            koreensis].
ACCESSION   WP_176070355
VERSION     WP_176070355.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..345
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=36249
     Region          43..337
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mrsgnfkedy rqllaltdsv pvivwslvlv aaialaplli gkyfvsllll lmvtavgvlg
       61 lniltgttgl islghagfla vgayaagiva grygwpmpaa llaggtaaaa aglvvgvpsl
      121 rlkglylait tmafaviinh lilnggeltg gseglkvpqp allgqplaae ggyyyvvlav
      181 lllavfatln lqrsrvgral mairehdiaa ramgvnlvrw rllaftvsaf ytgvagalla
      241 fytrylnvds fsllvsieal smlivgglgt vsgallgavf ifvlneglgl lfsalgsgal
      301 staafeikgi vyglaivlfl rfepdglvgr wrdlkhywth wpfry
//
LOCUS       WP_176070382             398 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Piscinibacter koreensis].
ACCESSION   WP_176070382
VERSION     WP_176070382.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..398
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42937
     Region          22..396
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnapttptgr ttassiiqsr irdiqeaarg vtkqyprsyi lqcikedrfp delwrelgkf
       61 gllglsipee hggsgggvle italnealal agvptlflvv tglgrvpivr hgtkeqiaky
      121 vtptctgekk lcfaitepna gtnsfamttl atsnadggwt lngqkvfisg ardadfmlvv
      181 arttkagevk yrtdgmslfv ldmktpgikl qqlniqveta erqymvffdn vqlpadavig
      241 epgkgaklmf eglnserlla agaalglgdy alskavaysk drkpfgkpig syqslqhrma
      301 lakaeleaar lmtydaadrf dngedagaha nmakllasra avaaieatlq vhggygfdrd
      361 ydvvtlwpmt rlleiapinn emlmnyigeh vlglpksy
//
LOCUS       WP_176070391             539 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA carboxylase subunit beta [Piscinibacter koreensis].
ACCESSION   WP_176070391
VERSION     WP_176070391.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..539
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58207
     Region          21..536
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mstiesaihr qseafqaqrq qmlalidnfr dlegrvrdts namesrfrer rqllprervs
       61 llldrgspwl elstlaglrl hdddgeknvl ggalitgigi vsgircmvia sdsaikggti
      121 tpmgmrkslr aeaialenrl pvvrlvesgg anlmhvgevf ieggrgfanq arlsaagipq
      181 vtvmhghsta ggaylpgmsd yvimvrgrak aflagppllk aatgeiagde elggaemhtr
      241 vsgvaeylae ddadgiriar dvlarmpwnd kpgqgtgrgw kppryaaeei aglvppdyrq
      301 pydvrellar liddsdfldf kpefgaatvc ghgaiegqpc gfignngpid pqgankatqf
      361 mqlceqsgtp liylqnttgf mvgkeveqvg mikhgakmiq avtnckvpri tlmigasfga
      421 gnygmcgray dpqfvfawpn arvavmggeq aamvmrivte ekmaragkap peamlegmra
      481 eilkrfdmes hslfatarlw ddgiidprdt ravlslalaa cregrartvr pnsfgvarm
//
LOCUS       WP_176070456             792 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Piscinibacter koreensis].
ACCESSION   WP_176070456
VERSION     WP_176070456.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 792)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..792
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..792
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=84226
     Region          14..790
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msdlsnppvd tlqspigqpv rrredqrylt gaaqytddvm lhgqtygvfl rspfaharig
       61 airldaaraa pgvlaiftga dlaeakvggl pcgwlihskd gtpmkepahp vlaqgkvrhv
      121 gdqvalvvae sylqardaae lievdyedlp avvdlasaad aeasvhddvp gnvcydwghg
      181 daaavdaafa rathvttldi vnnrlipnam epraanavys rhddsytlyv anqnphverl
      241 lmcafvlgls eskvrviapd vgggfgskif lypeetalvw askrvgrpik wtsdrseafl
      301 tdahgrdhvt kaelatdadg nflalrvrtv anmgaylstf assvptilya tllagqyrtp
      361 aiyaevkavf tntapvdayr gagrpeatfv veriveqaar elkidpaelr rrnfitefph
      421 vtpvgltydv gnyaahldka iaradvagfa arraesearg rkrglgyscy ieacglapsn
      481 vagalgarag lfeagevrvh ptgtvtvftg shshgqghet tfaqvvagrl gipvenveiv
      541 hgdtgrvpfg mgtygsrsla vggsaivkav dkviakgkki aahlleaadt diefengefk
      601 vagtdkkvaw gnvsltayvp hnypldklep glnenafydp gnftypsgty icevevdpet
      661 gkttverfta vddfgnvvnp mivegqvqgg iaqglgqamf eactydassg qlltgsymdy
      721 ampramdlps fdvsttvtpc shnplgvkgc geagaigspp afinaltdal gvdsiampat
      781 pervwraanr va
//
LOCUS       WP_176070499             241 aa            linear   BCT 11-JAN-2025
DEFINITION  M48 family metallopeptidase [Piscinibacter koreensis].
ACCESSION   WP_176070499
VERSION     WP_176070499.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Makarova,K.S. and Grishin,N.V.
  TITLE     The Zn-peptidase superfamily: functional convergence after
            evolutionary divergence
  JOURNAL   J Mol Biol 292 (1), 11-17 (1999)
   PUBMED   10493853
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of metallopeptidases
  JOURNAL   Methods Enzymol 248, 183-228 (1995)
   PUBMED   7674922
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..241
                     /product="M48 family metallopeptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=27923
     Region          1..241
                     /region_name="YgjP"
                     /note="UTP pyrophosphatase, metal-dependent hydrolase
                     family [General function prediction only]; COG1451"
                     /db_xref="CDD:441060"
ORIGIN      
        1 msadvrstvr kvkdieyrll pgtarqttdi vierdgcvtv rpparmtpeq vddtvlsrrr
       61 wiyrnlaewr dlnstrvvre wvngesflyl ggayrlllvg eqnepvklrd grfcllrsvv
      121 dqggkaaahe afrdfyitrg rvrlkqrveh faprvgvqpg plqvkelgyr wasslsgggl
      181 hfhwkclmap pkiidyivvh elchlhhrdh telfwnevdk vlpdyrerke wlrargagmd
      241 l
//
LOCUS       WP_176070542             390 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Piscinibacter koreensis].
ACCESSION   WP_176070542
VERSION     WP_176070542.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..390
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=42108
     Region          8..>236
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 madrtehrlr vgvvglgiag glmvpcllrh pratlagvad rdaelrarfa rdyalpvede
       61 aealiaradv davyiatphq fhrshtllaa ehgkhvvvek pmaltladcd amteaaarae
      121 valvvghths fdpaiaeiar rseagewgsl amlalwnytd flyrprrpee ldtaqgggil
      181 fnqlphhvdi arllarspvr svrastavld ptrptegccm afidfvngaa asavysgydh
      241 fdsdelhgwv sstgrrktpr hgesrralss ltggdaearl rathygyggg snqqrgvaqh
      301 qphfgtliat feradvrttp dgvavydddg vheislpsss dgrtrvvdel caavldgtpp
      361 shdgafartt vetclaiqes arlrrevvlh
//
LOCUS       WP_176070552             157 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter small permease [Piscinibacter koreensis].
ACCESSION   WP_176070552
VERSION     WP_176070552.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..157
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=16559
     Region          22..155
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mrvlegaaal lllllmlvvl vdvvgrnvan rplpwgtefl eivlgamifl lypvlawsgg
       61 hitvdlistr pqirraqrtl asvigatlfa liawclgrqa mraigygeat pilgiplgvv
      121 ltgmsilgaa aglafvaama rtwrgktdap shhieai
//
LOCUS       WP_176070570             293 aa            linear   BCT 11-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Piscinibacter
            koreensis].
ACCESSION   WP_176070570
VERSION     WP_176070570.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..293
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32157
     Region          5..282
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mtvelvvdar arlgecplwc ertqslfwtd iqnsqlsrwr sadgsttrwa mrerlgsfal
       61 ceesshlllg lasgialfdv dqaatgdlva vdaeqpstri ndgrcdaqgr fvfgmfnhap
      121 epighfyrvd adlnverlal prvsvansla fspdgmtlyf tdsptrtiwr adyhadgrig
      181 tperfvevpd geghpdgaav dadgglwsar wdgacivrhd adghetdria lpvtrptcva
      241 fggpnldrlf itsargglsd ealarepwag gvlavdvrrr grpehrfrta rrv
//
LOCUS       WP_176070605             469 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Piscinibacter koreensis].
ACCESSION   WP_176070605
VERSION     WP_176070605.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10656590
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..469
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=50816
     Region          63..>151
                     /region_name="Lactamase_B"
                     /note="Metallo-beta-lactamase superfamily; smart00849"
                     /db_xref="CDD:214854"
ORIGIN      
        1 mrlkeviqal vpfallagat sawsaadptl lkarqkffgi dnvdvntgav kkdkviaswa
       61 tnttyvvsvm grvilldsyi tkpelpttpi drryspllpq dlidvrpeai flghghgdha
      121 dnaayiakwt natiyatpet cdvmqqdvar mwadpnpqng gakvvpnpnp vncvgavprg
      181 srpgqynqgp naglskssvs klstpldaqv cvlafkfihs ggspvdpsfp httlndlgdp
      241 rypgrtittp pppvtypamf pnltpytppa tgavagqldt rttgfggpag ayevvyqfil
      301 rngynfnffy lnsagpakeg igsdidlvtl aqyndptfpq erkdlaraig nslydlmdtl
      361 prtdvllgsi vslgaaanqq rdiilatqrl rpkvyipghh tdvaqkgsgi yhmiswketa
      421 vnmgwpqsew pefrllmdpn dflvpqvwsp gdarwfdatk agrvaqlcg
//
LOCUS       WP_176070625             692 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Piscinibacter koreensis].
ACCESSION   WP_176070625
VERSION     WP_176070625.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..692
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=74695
     Region          4..529
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          621..681
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 mlvlqqlslr rgvklvldra svtlqpgekv glvgrngagk sslfsllagr lqpdagdvsi
       61 pprwrvaeva qdmpeteaga tdfvlegdta lmeahaqlaa aeaaddgham aeahhaisea
      121 ggfdarpraq amlmglgfrs dqldapvnsf sggwrmrlql aralmcpadl mlldeptnhl
      181 dldalvwlea wlqrfegtmi vishdrefld avtrvivhld dakltryggn ytafeemrae
      241 rmlqqqanfe kqqermahlq kfidrfkaka skakqaqsrv kalarmekia pvltsadfqf
      301 efreplslpn pmlafagvdc gyrsaaddgg dkvivrgvnr svlagqrigi lgangqgkst
      361 lvktivgdla plsgqitagk gltigyfaqq eldvlslgdg plmhmvrlar dvgppgreqe
      421 lrdflgsfrf vgdmvtqpvg tlsggekarl vlamlvwqrp nlllmdeptn hldlstreal
      481 smalnefegt vmlvshdral lrevcdefwl vsqgsigpfd gdlddyqrwl leqakaaare
      541 pkresagkra gaaddsaaag sareakrsan atavpgrgsg aspsttgngn atpavapvdk
      601 raerqaaaaa rqqqanalkp lrqelnrvdn klgvlfaerd gleasfatga gtpadiaerg
      661 krlkalgeqi deleqrwlel stqldeases aa
//
LOCUS       WP_176070661             252 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Piscinibacter koreensis].
ACCESSION   WP_176070661
VERSION     WP_176070661.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..252
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26883
     Region          2..245
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 mdpapiirve glaagfgdri lmkdvtfdva rgeifmilgg sgsgkstllk niiglyepla
       61 grvlidgddl vgttgaarer ilrkfgvsfq sgalfgsmtl lenivlplea ftalppdaid
      121 lvarmklsqv glggaearmp aelsggmkkr aaiaramald pkilfldeps agldpitsae
      181 ldqlllrlsr elgvsfvivt helesifgig drvvmldgas kgivaagdpr elrdhsehaw
      241 vrrffhrevv np
//
LOCUS       WP_176070680             117 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydroneopterin aldolase [Piscinibacter koreensis].
ACCESSION   WP_176070680
VERSION     WP_176070680.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Illarionova,V., Eisenreich,W., Fischer,M., Haussmann,C.,
            Romisch,W., Richter,G. and Bacher,A.
  TITLE     Biosynthesis of tetrahydrofolate. Stereochemistry of
            dihydroneopterin aldolase
  JOURNAL   J Biol Chem 277 (32), 28841-28847 (2002)
   PUBMED   12039964
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..117
                     /product="dihydroneopterin aldolase"
                     /EC_number="4.1.2.25"
                     /GO_function="GO:0004150 - dihydroneopterin aldolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0046656 - folic acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=12669
     Region          1..116
                     /region_name="FolB"
                     /note="Dihydroneopterin aldolase [Coenzyme transport and
                     metabolism]; COG1539"
                     /db_xref="CDD:441148"
ORIGIN      
        1 mdvlflegle vpcrvgcsap eratpqslrv gvrlfcgslq kagladdlea tvdyrlagdm
       61 idavqdgeyl liervaevla evalrhplvq svevtvrkrp pvqglewagv qitrdrg
//
LOCUS       WP_176070764             713 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Piscinibacter koreensis].
ACCESSION   WP_176070764
VERSION     WP_176070764.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 713)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 713)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..713
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=76338
     Region          20..>199
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mkfskaevda iieasprtfv pfnklvlsed hqarsatapv mslpelaasi kdsgvlqnlv
       61 vvqaargrye vcaggrrlaa ltllvqqgdi adnypvpvlv vpadkalias laencfhvpm
      121 hpadefaafa rllaqgksvd dvaaafgvtp lvvkrrmkla tvsprlmaly reggigldcl
      181 mvlasvddhq rqeqawaglp swnqrpehlr qlltrgeies dadplarfvt vkayekaggp
      241 lrrdlfsddd rkayllapal lerlaadklg krakqllseg wkwvdirprf aydeyvkhge
      301 lrkprraptp eeaetlkald triaalheqm ealvdrdgdg dagegvsgas eandaadedd
      361 asrdraflal eseaegleee rkarlealte wpaawmalag cvlhvgadgr aaikaglirp
      421 edradlaqai tkaaeqksag gggseddadp argsglpalq slpsaagatt rpvhseklmr
      481 rltahrvaai qaelldrpev alaaltthlt lklladplhg ayrlpnllai satgnqhelr
      541 gaaedieasp aaqrieadri awiehlpkep davfdwmlrq ppqtvqrllt flvastvngi
      601 tgtdagrpvn dglalalgld mtrwwsatgk aylqhvskar vvevvhtvag akaagplaal
      661 kkdaavaqae qllagrgwlp dclraqphad apatggeegd andparteap aca
//
LOCUS       WP_176070803             419 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter large permease [Piscinibacter koreensis].
ACCESSION   WP_176070803
VERSION     WP_176070803.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..419
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=43877
     Region          1..418
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mtiliiglfi vaalasipia halvlasvgg llalgrvpvd lavqqmisqm qsfpliaipf
       61 fmltgalmvs grlgqslvnl lsmmigrvhg gpaqvgvlss tifggvsgsa vadasaigsm
      121 lipwlkklgy papfaagtla aaatidilip psipmivyal vsgasigalf vagilpgllm
      181 cggfmlvcyv qgrrrgfprd ttpfrwnafg rqlvlagpal ampvliivfl rfgiatptev
      241 svmstlyalv vsglvyrdlt iaklrhaave agistgvvll iimassivgw ivtyeqlpaa
      301 ftrfatetlq spwliilamn limlatgmfi dlpaavlllt pmfvplaaav gmdtvqlgim
      361 mivnlsigly hppigttlfi tssiakvrig dvvvelipfy vvavglllgf aylpwltlh
//
LOCUS       WP_176070838             349 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Piscinibacter koreensis].
ACCESSION   WP_176070838
VERSION     WP_176070838.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 349)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..349
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35792
     Region          33..349
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mppaptdaal aaderaatpq aaaarraara shwrqraqsl gpliglvvlc iagallnpgf
       61 atwdnamnvl trtafigiia igmcfviigg gidlsvgsma aliagsvila mnalapvvas
      121 pvlvvvlgaa falglgaafg lahgllitkg riepfivtlg tlgifraylt ylanggaitl
      181 gdkvtevysp vyygswlavp vpiwvfaava ligglvlnrt rygryvkaig sneqvaryaa
      241 vdvdrvkils yvllgvcvgv atllyiprlg saspttgllw eleaiaaviv ggtalkggdg
      301 riagtvvgai llsvisniln ltsiisvyln aavqgvviii vaflqrgrr
//
LOCUS       WP_176070874             263 aa            linear   BCT 11-JAN-2025
DEFINITION  TatD family hydrolase [Piscinibacter koreensis].
ACCESSION   WP_176070874
VERSION     WP_176070874.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..263
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28732
     Region          2..256
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 myvdshchls ypgladrida vradmaaadv dralcicttl eefeavhala laydnfwcsv
       61 gvhpdnedvq eptvddlvsr aarprvvaig etgldyyrld grgvdemawq rerfrvhira
      121 slatglplvi htrsasadtl dvlreeggsr atgvfhcfte taevaraald lgfyisfsgi
      181 ltfknaaelr evarfvpldr clietdspyl apvpfrgkpn spawvpyvar qiaelkgssp
      241 eaigettsrn fetlfgrvaa nag
//
LOCUS       WP_176070888             426 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter large permease [Piscinibacter koreensis].
ACCESSION   WP_176070888
VERSION     WP_176070888.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..426
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44548
     Region          1..426
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mtiaifigsl llamaigipi afallvsgva lmahldifda qilaqnvvgg adnypllaip
       61 ffllageimn vgglskrive famalvghir gglgyvaiva svllgalsgs avadaaalsa
      121 illpmmiaag hkperaagli sassviapvl ppsigliifg vtanvsiskl flagifpgll
      181 vglalwitwa ivarhenivp pprkslgelw gtfrrcvwal ilpviilvgl rmgvftptea
      241 gviaavyalf vsavvyrelr lsqlwgifni aarttsivmf liaaamvssw litvadlpgk
      301 vvgllepmlg sptllmfaim ilvmivgtam dmtptililt pvlmpvikaa gidpvyfgvl
      361 fimnnaigli tppvgvvlnv vagvgrmsmd svtrgvmpfm vsqfaimfam vlfpwlvtgp
      421 arllhg
//
LOCUS       WP_176070920             106 aa            linear   BCT 11-JAN-2025
DEFINITION  type II toxin-antitoxin system RelE/ParE family toxin
            [Piscinibacter koreensis].
ACCESSION   WP_176070920
VERSION     WP_176070920.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Hall,A.M., Gollan,B. and Helaine,S.
  TITLE     Toxin-antitoxin systems: reversible toxicity
  JOURNAL   Curr Opin Microbiol 36, 102-110 (2017)
   PUBMED   28279904
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Fiebig,A., Castro Rojas,C.M., Siegal-Gaskins,D. and Crosson,S.
  TITLE     Interaction specificity, toxicity and regulation of a paralogous
            set of ParE/RelE-family toxin-antitoxin systems
  JOURNAL   Mol Microbiol 77 (1), 236-251 (2010)
   PUBMED   20487277
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Dalton,K.M. and Crosson,S.
  TITLE     A conserved mode of protein recognition and binding in a ParD-ParE
            toxin-antitoxin complex
  JOURNAL   Biochemistry 49 (10), 2205-2215 (2010)
   PUBMED   20143871
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Pandey,D.P. and Gerdes,K.
  TITLE     Toxin-antitoxin loci are highly abundant in free-living but lost
            from host-associated prokaryotes
  JOURNAL   Nucleic Acids Res 33 (3), 966-976 (2005)
   PUBMED   15718296
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..106
                     /product="type II toxin-antitoxin system RelE/ParE family
                     toxin"
                     /GO_component="GO:0110001 - toxin-antitoxin complex
                     [Evidence IEA]"
                     /GO_function="GO:0090729 - toxin activity [Evidence IEA]"
                     /calculated_mol_wt=11887
     Region          3..103
                     /region_name="ParE"
                     /note="Plasmid stabilization system protein ParE
                     [Mobilome: prophages, transposons]; COG3668"
                     /db_xref="CDD:442885"
ORIGIN      
        1 mtyavrftas aeadllrlfe fllaransle nlehaqdvid rlresilshl grspwsyrka
       61 ghgrsstrre livpsaaagy vvlyeidsas svlilavrhq reddyq
//
LOCUS       WP_176071009             179 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrofolate reductase [Piscinibacter koreensis].
ACCESSION   WP_176071009
VERSION     WP_176071009.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Francis,K. and Kohen,A.
  TITLE     Protein motions and the activation of the CH bond catalyzed by
            dihydrofolate reductase
  JOURNAL   Curr Opin Chem Biol 21, 19-24 (2014)
   PUBMED   24742825
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Schnell,J.R., Dyson,H.J. and Wright,P.E.
  TITLE     Structure, dynamics, and catalytic function of dihydrofolate
            reductase
  JOURNAL   Annu Rev Biophys Biomol Struct 33, 119-140 (2004)
   PUBMED   15139807
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Gready,J.E.
  TITLE     Dihydrofolate reductase: binding of substrates and inhibitors and
            catalytic mechanism
  JOURNAL   Adv Pharmacol Chemother 17, 37-102 (1980)
   PUBMED   7004143
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11087044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..179
                     /product="dihydrofolate reductase"
                     /EC_number="1.5.1.3"
                     /GO_function="GO:0004146 - dihydrofolate reductase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_process="GO:0046654 - tetrahydrofolate biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=19618
     Region          11..166
                     /region_name="DHFR_1"
                     /note="Dihydrofolate reductase; pfam00186"
                     /db_xref="CDD:425512"
     Site            order(14,31,36,66,104,110,123)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:238127"
     Site            order(16,23,53..55,73,105..108)
                     /site_type="other"
                     /note="NADP+ binding site [chemical binding]"
                     /db_xref="CDD:238127"
ORIGIN      
        1 mdrrapsrpl vslvaavard ggigrdngll vhlpedlkhf krttlgapiv mgrrtwdaig
       61 rplpgrrniv itrdpkwhad gaeraaslda avtlaapapk vyviggaqiy alalpdadel
      121 vlteldaefd adtwfpawpr eaflqqpges hvapqgftyr fvtysrkraq dshttmetr
//
LOCUS       WP_176071015             163 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Piscinibacter koreensis].
ACCESSION   WP_176071015
VERSION     WP_176071015.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10615366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..163
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17328
     Region          21..131
                     /region_name="Glyoxalase_4"
                     /note="Glyoxalase/Bleomycin resistance protein/Dioxygenase
                     superfamily; pfam13669"
                     /db_xref="CDD:463951"
ORIGIN      
        1 msdvapaapg glrpfrilgi qqiaiggadk lrlrtlwvdl fglavestfr serenvdedv
       61 csigsgahkv evdlmqpldi dkkpavhttp lnhvglwvdd lsravewlsa ngvrfapggi
      121 rpgasghdic fvhpksndaf pisgegvlie lvqapaevia ahr
//
LOCUS       WP_176071025              78 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl carrier protein [Piscinibacter koreensis].
ACCESSION   WP_176071025
VERSION     WP_176071025.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Arya,R., Sharma,B., Dhembla,C., Pal,R.K., Patel,A.K., Sundd,M.,
            Ghosh,B., Makde,R.D. and Kundu,S.
  TITLE     A conformational switch from a closed apo- to an open holo-form
            equips the acyl carrier protein for acyl chain accommodation
  JOURNAL   Biochim Biophys Acta Proteins Proteom 1867 (3), 163-174 (2019)
   PUBMED   30543875
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Chan,D.I. and Vogel,H.J.
  TITLE     Current understanding of fatty acid biosynthesis and the acyl
            carrier protein
  JOURNAL   Biochem J 430 (1), 1-19 (2010)
   PUBMED   20662770
  REMARK    Erratum:[Biochem J. 2010 Aug 27;430(3):559]
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Byers,D.M. and Gong,H.
  TITLE     Acyl carrier protein: structure-function relationships in a
            conserved multifunctional protein family
  JOURNAL   Biochem Cell Biol 85 (6), 649-662 (2007)
   PUBMED   18059524
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000754
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..78
                     /product="acyl carrier protein"
                     /GO_function="GO:0000035 - acyl binding [Evidence IEA]"
                     /GO_function="GO:0000036 - acyl carrier activity [Evidence
                     IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0009245 - lipid A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=8661
     Region          4..64
                     /region_name="AcpP"
                     /note="Acyl carrier protein [Lipid transport and
                     metabolism]; COG0236"
                     /db_xref="CDD:440006"
ORIGIN      
        1 mvneqtlrqv matvlripve sinentsmdd veswdslkhm nlvlaledef kvsipdedaa
       61 nitsyqlikv vldelvsg
//
LOCUS       WP_176071062             200 aa            linear   BCT 11-JAN-2025
DEFINITION  HD domain-containing protein [Piscinibacter koreensis].
ACCESSION   WP_176071062
VERSION     WP_176071062.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008511
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..200
                     /product="HD domain-containing protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22723
     Region          31..181
                     /region_name="COG4341"
                     /note="Predicted HD phosphohydrolase [General function
                     prediction only]"
                     /db_xref="CDD:443482"
ORIGIN      
        1 mndrasftrm eastaadwqk igaefmpfar qlpdrlmahl kvlegdyggf pidrythslq
       61 tatralkdgr deeyvvtalf hdigdtlgtf nhfdiaaail kpfvsdanlw mvqnhgifqg
      121 yyffhhigld rnlrdrfqgh ehyertaefc elydnpafda naetlpmsef epmvrrvfaq
      181 pensiykast ampateatas
//
LOCUS       WP_176071156             235 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Piscinibacter koreensis].
ACCESSION   WP_176071156
VERSION     WP_176071156.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 235)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..235
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25899
     Region          1..226
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mhpvvlknva rtyqldavdv paltdinlvi lpnrftvlsg psgsgkttll nligcidrpd
       61 sgtimvggka vqtmdddtls dfrakqlgfi fqnfnllpvl safenveypl lmakmpkerr
      121 hrrvrkllda vgladkgahr pgqlsggqrq rvaiaralar kpqlvladep tanldsktgv
      181 eilelmrkmq rryqvsfvfs shdpklldaa ddaihiqdgr itgierrtlq relga
//
LOCUS       WP_176071196             356 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Piscinibacter koreensis].
ACCESSION   WP_176071196
VERSION     WP_176071196.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..356
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38675
     Region          1..354
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 masvtirgvr knfgatpilh gvdidiadgs ftvlvgpsgc gkstllrmia gleeitagei
       61 riderrinel ppkerdiamv fqnyalyphm tvgrnmgfsl mlakedaati nrkvaraaei
      121 laltplldry prqlsggqrq rvamgraivr dpqvflfdep lsnldaklrv amrseikelh
      181 qrlattsvyv thdqieamtm gdkivvmkdg rieqtgsple lydypantfv agfigspamn
      241 flpgtlrhea gaarvelgdg trldapahvg gvdgqavimg mrpehltlgd rgipskvvvv
      301 eptgadtfva crhegaelsv vfrerhdfap dstiflqpdv rrahlfdags gvrlaa
//
LOCUS       WP_176071222             490 aa            linear   BCT 11-JAN-2025
DEFINITION  tripartite tricarboxylate transporter permease [Piscinibacter
            koreensis].
ACCESSION   WP_176071222
VERSION     WP_176071222.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..490
                     /product="tripartite tricarboxylate transporter permease"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=51029
     Region          1..474
                     /region_name="COG3333"
                     /note="TctA family transporter [General function
                     prediction only]"
                     /db_xref="CDD:442562"
ORIGIN      
        1 mwallgctlg tavgvlpgig patavamllp itakvdptas miffagiyyg amyggsttsi
       61 llntpgesgs lvtamegnkm aksgragaal ataaigsfva gtiatilvtl fapvvaafai
      121 rlgppeyfll mvlafttvsa vlgqstlrgm valaiglffg ligldqisgq prytggvpel
      181 mdgievvlia vglfavgeal ymvlyegrtv etqnplskvh mtalewrrsw pawlrataig
      241 fpfgtipagg seiptflsya aekklskhpe efgtkgaieg vagpeaanna aitatlipll
      301 tlgiptsntt aillgafqny giqpgpqlfd tnaalvwali aslyignvml lvlnlplvgm
      361 wvkllkipkp qlyagilifa tvgvygmrqs afdlvllygi gllgvlmrrf dfptapvvvg
      421 milgplaeaq mrnalsigeg hwgvfvqrpg slvllviiaa vvllprlirv argrgraaap
      481 ldvpkagpet
//
LOCUS       WP_176071265              84 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy-metal-associated domain-containing protein [Piscinibacter
            koreensis].
ACCESSION   WP_176071265
VERSION     WP_176071265.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 84)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 84)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 84)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..84
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=8604
     Region          1..66
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 misfqvsdmt cghcvstitk aieaadknat vnidlasqrv aiepteadaq qlreaiedag
       61 ytpvavptda vapaskprrg ccgg
//
LOCUS       WP_176071291            1056 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Piscinibacter koreensis].
ACCESSION   WP_176071291
VERSION     WP_176071291.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Nikaido,H.
  TITLE     RND transporters in the living world
  JOURNAL   Res Microbiol 169 (7-8), 363-371 (2018)
   PUBMED   29577985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..1056
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=115455
     Region          1..1042
                     /region_name="CusA"
                     /note="Cu/Ag efflux pump CusA [Inorganic ion transport and
                     metabolism]; COG3696"
                     /db_xref="CDD:442911"
ORIGIN      
        1 miarlirwsi anrflvllgt lmigtwgvis llrtpldalp dlsdvqviir tsypgqapqi
       61 venqityplt ttmlsvpgak tvrgysffgd sfvyvlfedg tdlywarsrv leymnqvqsr
      121 lppsakaslg pdatgvgwiy qyalidrsgs qdasqlralq dwflkyelkt vpnvaevasi
      181 ggmvrqyqvv ldpdklaayn iphtkvvdai qkanqetggs vlelgeaeym vrasgylqsl
      241 ddfrkiplss tdagvsvrlg dvariqlgpe mrrgigeldg egeapggviv mrsgknalet
      301 iaavkskles lqaslprgve ivptydrssl ieravdnlty klieefvvva vvcfiflfhl
      361 rsafvaiisl plgilaafiv mryqgvnani mslggiaiai gamvdaavvm ienahkhiee
      421 wrhehdgrap eggahwrvig dsaaevgpal ffslliitls fvpvftleaq egrlfsplaf
      481 tktyamaaaa glavtlipvl mgylirgrip dektnplnrf liaayrpile avlrwpkati
      541 alavlvlats lwplakigge fmprldegdl lympsalpgl gvgkaaellq qtdrliktvp
      601 evlsvygkag raetatdpap lemfettiqf kprdqwrpgm tqdrlieeld rtvqvpglsn
      661 iwvppirnri dmlatgiksp vgvkvagtdl atldritgei ervlknvpgv ssalaerltg
      721 gryvdvtikr deaarfgmni advqsviasa vggenvgetv eglqrfpinm ryprevrdsl
      781 dklrnlpivs grgarlvlsd ladiritdgp pmlrsenarl sgwvyvdirg rdlrgavqdm
      841 qravmkevkl ppgysiswsg qfeflerata klkvvvpftl liifvllylt fqrfgealll
      901 maslpfalvg giwllyvlgy nlsvaaavgf ialagvaaef gvimllylkt awsvrlekgt
      961 tsmadllgai regavlrvrp kamtvavila glfpimwgsg tgsevmqria apmvggmita
     1021 pllsmfvipa ayllmrrprk ervmpwarwr iareda
//
LOCUS       WP_176071447             386 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Piscinibacter koreensis].
ACCESSION   WP_176071447
VERSION     WP_176071447.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..386
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42817
     Region          6..384
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mtataerhpe lraalrdlsk rfpdeyfrkv deargypeef vdalteagwl avmipeeygg
       61 aglglaeasv vmeevnrcgg nagachgqmy nmgtllrhgs leqkrrylpg iasgklrlqs
      121 mgvtepttgt dttqlkttal rkgdryvvng qkvwisrvqh sdlmillart tpladvkrks
      181 egmsifivdl hqaigkgltv rpirnmvnhe tnelffenle iptenligee gkgfkyildg
      241 lnaertliaa ecigdarwfv arsaayarer rvfdrpigqn qgvqfpiagn hieteaadlm
      301 rwracelfda kqpcgaeanm akylaakasf eaanvaiqth ggfgfaceyd verkfretrl
      361 yqvapistnl ilsyvaehvl glprsf
//
LOCUS       WP_176071456             539 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA carboxylase subunit beta [Piscinibacter koreensis].
ACCESSION   WP_176071456
VERSION     WP_176071456.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..539
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58108
     Region          21..536
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mpsiesgidr qseafqaqrq qmlalidnfr glegrvrdts nalesrfrer rqllprervs
       61 llldrgspwl elstlaglrm hdddgeknvl ggalitgigi vsgvrcmvia sdsaikggti
      121 tpmgmrkslr aeaialenrl pvvrlvesgg anlmhvgevf ieggrgfanq arlsaagipq
      181 vtvmhghsta ggaylpgmsd yvimvrgrak aflagppllk aatgeiagde elggaemhtr
      241 vsgvaeylae ddadgiriar dllarmpwnd kpgqgtgrac kpprypaedi vglvppdyrq
      301 pydvrellar liddsdfldf kpefgaatvc ghgaiegqpc gfignngpid pqgankatqf
      361 mqlceqsgtp lvylqnttgf mvgkeveqvg mikhgskmiq avtnckvpri tlmigasfga
      421 gnygmcgray dpqfvfawpn arvavmggeq aamvmrivte ekmaragkap peamlesmra
      481 eilkrfdmes hslfatarlw ddgiidprdt ravlalalav cregrvrgvr pnsfgvarm
//
LOCUS       WP_176071462             548 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Piscinibacter koreensis].
ACCESSION   WP_176071462
VERSION     WP_176071462.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 19108972
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..548
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=59023
     Region          19..206
                     /region_name="NUDIX_AcylCoAdiphos_Nudt19"
                     /note="Nucleoside diphosphate-linked moiety X)) motif 19;
                     cd18870"
                     /db_xref="CDD:467582"
     Region          280..478
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="uncharacterized subgroup of the
                     MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo
                     hydrolase domain; cd16278"
                     /db_xref="CDD:293836"
     Site            order(340,342,344..345,412..413,431,474)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293836"
     Region          511..548
                     /region_name="BLACT_WH"
                     /note="Beta-lactamase associated winged helix domain;
                     pfam17778"
                     /db_xref="CDD:407650"
ORIGIN      
        1 marpvtqlhp prtpvaprpa atllwlrdap agpevlltrr spnasflpgv fvfpggridd
       61 adasaadlvg eaaaalphla aavaalresf eelgvlhahd aagspvaase laglkrhepl
      121 hpqlrarglr laagalrvav rwttdrdvqp rrfdtlflig rmpegqtpva deaeqfepvw
      181 lraadalarh eagtlpmifp tlrtlrwlag fdsvdaalaa cagnrphwes cprgalvggk
      241 pqrfmetdvp fgelelvcpd gqmlhaldwq serpvqllrh lwrftapnpg vmtgpgtnay
      301 llgsaaagwi vidpgppdev hvkrllevtg grvrtiicth shpdhspaaq plaqaceaat
      361 gqrppilglp saptarahse ftpdrtladg ecivlddpah pltlravhtp ghaanhlclv
      421 leedgllfsg dhvlsgsttv idppdgnmaa yidsldrllr ecerhdirfi lpahghvigs
      481 apqaiawlks hrlareakvl aamrecpqgn addwvpiaya dtpkqlwpva rrsllahler
      541 iealgrar
//
LOCUS       WP_176071494             402 aa            linear   BCT 11-JAN-2025
DEFINITION  ParA family protein [Piscinibacter koreensis].
ACCESSION   WP_176071494
VERSION     WP_176071494.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..402
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=44314
     Region          113..393
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mdpttqgpsa thpislkait eqaeratsiv aqargvmlap darklpptfs atqlierlki
       61 ersqydyrvr npgglptgrl tstgarreft lsemrqwarh yrsahlrpeg geaitistah
      121 fkggsskttt attlaqglsm rghkvlvvdv dpqgsmttlf gflpdaevdv tqtllpllsg
      181 depdvnyair ptywdgvdlv psssplfsae filptrqlke asfqfwrtld ygldpirsky
      241 dviicdtpps lsfltvnalm asdgiimplp psnldfassa qfwdlfkdla ddfagrgagk
      301 dfafinills kvkyaapkdn tgqstaiire wiqaayaerv lpveipdvea vrtaskefgt
      361 vydasrdnas trtfksafea ydrfvdlieq qmetfwqrqv gg
//
LOCUS       WP_176071579             295 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Piscinibacter
            koreensis].
ACCESSION   WP_176071579
VERSION     WP_176071579.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..295
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30933
     Region          3..295
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mdwpfffela ingalsglmy slvalgivli yksssvpnla qgalamlgay vvlalfetmk
       61 lpiwaalaag mvvmfgigmg iervalrrla grplimilmm tlaldifvra salvawggtn
      121 rvlplpisad plfigpvlvn rsyvaggvia lslfgffvlf frtrmgivlr aisddytasw
      181 svgisvergv alswamsavv atlagalwgs iqgvdqslsl lllmgitvav lggldsigga
      241 ilaglllgmf qsvasgyldp ivgggsrelv vagtlvftil vrphglfgre diqri
//
LOCUS       WP_176071591             262 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Piscinibacter
            koreensis].
ACCESSION   WP_176071591
VERSION     WP_176071591.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..262
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28412
     Region          7..257
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mstdkpvris reggvgviel arpdkfncls lavhaaiaea ldefeapgsg vravlvraqg
       61 khfctgadld evkhlrsrpa diehfirygh vvlqrleass lpvvaacqgl alaggselmm
      121 acdvvfassd frfgdqhaqy glvpgwggsq rlprivgvrr aldlfysarw idastafawg
      181 lvnyvvepdk laevsmayca qlasrsrigl atmkhlarqg ldqplnegle leqvrisrel
      241 lnddvsegla afearrppvf ks
//
LOCUS       WP_176071600             163 aa            linear   BCT 11-JAN-2025
DEFINITION  PaaI family thioesterase [Piscinibacter koreensis].
ACCESSION   WP_176071600
VERSION     WP_176071600.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..163
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=17717
     Region          22..147
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mpevesnqad kvrkwqqitv ispysrelgl rlhevepdwc vikvlpderm vgnpasgvvh
       61 ggvitallds cyglaiyvkl nnlrpmatld lridylkpat pgreilggav cyklghelaf
      121 vrgaayhdsp ddpiatssgi fmftdgpvip leaaltmleg fkp
//
LOCUS       WP_176071604             385 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Piscinibacter koreensis].
ACCESSION   WP_176071604
VERSION     WP_176071604.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..385
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42668
     Region          4..381
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mpidfsftee qnllrdsvra mldriatpey irrcdqepry pselydafve lgllrmpfpe
       61 pvgglggsvi dfaiiaeelg rksydflgay gtcvfnglni lhngteaqrr ywlpqlmdgr
      121 ikmsismtep gagsdagamr tsarrdgehw vingqkvfst gagaernvin lyarskpegp
      181 hqeslslflv dkdtpgitlr kldtlgrral gtyevffddv rvpadrlvge phkgwaymls
      241 glqlerlmta agysgcaqaa vdlalayake rrqfgrpigs fqsiahllad mqtaveasrm
      301 lmwraafqle rgedalmais qaklfgseay anianqgmqi mggygyimef dmqrhyrdar
      361 attitagtsq mqrnliaglm glktk
//
LOCUS       WP_176071616             363 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Piscinibacter koreensis].
ACCESSION   WP_176071616
VERSION     WP_176071616.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..363
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37748
     Region          2..329
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mselaqplae aadrlfsqrc dsrlvasada gqwpqalwsa vdelgpglll apesaggagg
       61 dwldactlle raaahcvplp igqtllagwl rsraglrpvs gpaalaftaa plaamreagr
      121 adaaesdvap vlwaehahqi afvgadpagt aqllwlpkgc mqtrpltrsf ppsarvtctg
      181 valhapasae parawcvplp glsltevrar aalltaaqma galgrlldmt laytgervqf
      241 grsigqfqav qhqlaqlaee aaasrvavha aaatedphcf vaaaaaakvr ageaaslaar
      301 iahqlhgaig vtaehalhls trrlcwwrde hgseafwara lvqalrdggm rsawqaavac
      361 tsr
//
LOCUS       WP_176071614             302 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Piscinibacter
            koreensis].
ACCESSION   WP_176071614
VERSION     WP_176071614.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..302
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=32540
     Region          48..296
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 msifiappln gfsshgasrr lrrtahaarr aytchvpiqr nsmtasavlv drrgsvceit
       61 lnrpeqrnam apellqafqq videvkgdra ircvvitgse anfcsgadfr sallergsel
      121 pheasyaiyr pflsildvpv pviaamngha igggfglglv cdirvanrea ryganfarlg
      181 lhsgmaisyl lprvcgvpra aellftgrvf sgaeaaelgi anhavepgqv lararelade
      241 iaanapvavr mmkrslyrgl ewdprsagei eallqsrtle madakegvaa llekraprfr
      301 gv
//
LOCUS       WP_176071625             499 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA carboxylase subunit beta [Piscinibacter koreensis].
ACCESSION   WP_176071625
VERSION     WP_176071625.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Toh,H., Kondo,H. and Tanabe,T.
  TITLE     Molecular evolution of biotin-dependent carboxylases
  JOURNAL   Eur J Biochem 215 (3), 687-696 (1993)
   PUBMED   8102604
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469175
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..499
                     /product="acyl-CoA carboxylase subunit beta"
                     /GO_component="GO:0009317 - acetyl-CoA carboxylase complex
                     [Evidence IEA]"
                     /GO_function="GO:0003989 - acetyl-CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /GO_process="GO:0006633 - fatty acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=53091
     Region          21..497
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
ORIGIN      
        1 mtthaastrt rdsrvdqrqd ayqgllatlr arhdealagg sekarklhls rgqllprerv
       61 ralldpgspf feigqlagad lydgvppgat mitgvgkvcg rwcmllvnda tvkggtmfgm
      121 ttkrhtraql fawhhrlpci tmvqsgggfl pdlanifpde gqagsimynq vkmsaegiaq
      181 ialvhgpsta ggayipalcd evviirnqga mflgspqlvf aatgevidve plggaemhsr
      241 vsgvtdhmae ndedalaitr rivdhlgepp rlrwtraepk pplhdpqelt glagvgvieg
      301 agchdilarl vdgsqfqefk qlhgetlvcg fahiegyevg ivaghgelta qacakaahfv
      361 qlcgqrdipl vflvdspgfa dsgqagqatv grhgakllna vanaevpkft vitgrahgaa
      421 yhalggralk pnallmwpga rasaqldapd deagamnwar hlwcdaivep eqtravlaql
      481 ldiagrlpar pttygafrm
//
LOCUS       WP_176071645             382 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Piscinibacter koreensis].
ACCESSION   WP_176071645
VERSION     WP_176071645.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..382
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41893
     Region          1..377
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfgftpdqd tlrasvrrfm rervapriav cererefawd llpqlqpfgy lggllpeeag
       61 gfgmshvawa ilmeeagygw lslrvmmnsl nilaqllhrh gtveqkgrwl qpllagqlrh
      121 wmaitepnhg snvagietra edkgdhwlvn gnklwitngv hgnfgvvvar tysarcdggi
      181 slfivdreet ayeaqradvm firatgtsql afrdaivpka nllgqegegl kailtglnfg
      241 rlnvamgavg aaraaldlsi dyarqrkqfg rsiagfqlvq klivdmmvrc eaaralgyra
      301 awtldqggsa rtecsiakly aaeaahevas malqvhggcg yseelpieri frdtrgglip
      361 egtteiqtli igrevlgvsa fh
//
LOCUS       WP_176071649             295 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Piscinibacter
            koreensis].
ACCESSION   WP_176071649
VERSION     WP_176071649.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..295
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=31326
     Region          4..295
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mileffnytl ngallgllya lvamgfvviy raskvfnmat gemlvlgafl vwwavasrgm
       61 hpavgiaaal aiavlvglai erlffrrlig esvfsmimvt iglliltrgl vlviwgpqer
      121 afpaliplep liigemivpr slavagavav vfalglhwff nrsrtglams avaedhqial
      181 smgisvrrsi afawalggil svissivyls gksltflsse igfaalpval laglesirgl
      241 llaglivgvv qgltsayidp liggnaasvv pyifmlvvla vrpngmfgwk rierv
//
LOCUS       WP_176071663             267 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Piscinibacter
            koreensis].
ACCESSION   WP_176071663
VERSION     WP_176071663.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..267
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=28716
     Region          18..261
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 matyetlrie papgtapdeg vrclmlnrpe vmnamntqmf velraglhel afedglrvlv
       61 vtgagerafs tggdlkqrdg mtdhqwrrqh qlaeevllav kdfpapviaa veghahgggc
      121 elalmcdwiv aarsavfslp evrrgimpgg ggiqnlvraa garrakqlll tarrfsaeqa
      181 aqwnivttlv epgqalaaav aearevalaa pmavhyakva asrggevdfh sgytldiaay
      241 nvlvssqdrl egvrafnekr pprwsgr
//
LOCUS       WP_176071693             133 aa            linear   BCT 11-JAN-2025
DEFINITION  Zn-ribbon domain-containing OB-fold protein [Piscinibacter
            koreensis].
ACCESSION   WP_176071693
VERSION     WP_176071693.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Agrawal,V. and Kishan,K.V.
  TITLE     OB-fold: growing bigger with functional consistency
  JOURNAL   Curr Protein Pept Sci 4 (3), 195-206 (2003)
   PUBMED   12769718
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Arcus,V.
  TITLE     OB-fold domains: a snapshot of the evolution of sequence, structure
            and function
  JOURNAL   Curr Opin Struct Biol 12 (6), 794-801 (2002)
   PUBMED   12504685
REFERENCE   4  (residues 1 to 133)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446204
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..133
                     /product="Zn-ribbon domain-containing OB-fold protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14763
     Region          16..131
                     /region_name="COG1545"
                     /note="Uncharacterized OB-fold protein, contains Zn-ribbon
                     domain [General function prediction only]"
                     /db_xref="CDD:441154"
ORIGIN      
        1 mydkplpvvd pesapywaal kerrlilkrc rdcgrhhfyp ralcphchsd alewsdargt
       61 gsiysytvar rpagpafkad apyvvavvel degarmmtni vtddvesiri gqrvavtfda
      121 vtdeitlpkf kaa
//
LOCUS       WP_176071700             386 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Piscinibacter koreensis].
ACCESSION   WP_176071700
VERSION     WP_176071700.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..386
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=42600
     Region          1..384
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mnfdytetqa qiraavkdlc grfgpeywrq laqdgkypet fvdemakagw laalipeeyg
       61 gaglplldac lilqeinqng asavhchaqm ytmasimrhg seaqkrrtlp riadgslrlq
      121 afgvtepdag sntlaiktfa rrvpggyvln gqkiwtsrys hshlylliar ttpieevkkk
      181 tdglslflid iakagkslqa rpirtminhh tfqvfidnle lsdddrigee gkgfhyllds
      241 lhserllvas eaigdghwfv gkaaaygger ivfdrpigsn qgvqfpiara hmnveaaelm
      301 rnkaatlfda gqscgreatm vkylaseaaw eaaeaamttf ggygvacdfd ierkwkesrl
      361 frtapisnnl vlaqvaehll gmprsy
//
LOCUS       WP_176071719             140 aa            linear   BCT 11-JAN-2025
DEFINITION  single-stranded DNA-binding protein [Piscinibacter koreensis].
ACCESSION   WP_176071719
VERSION     WP_176071719.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Bianco,P.R.
  TITLE     The tale of SSB
  JOURNAL   Prog Biophys Mol Biol 127, 111-118 (2017)
   PUBMED   27838363
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..140
                     /product="single-stranded DNA-binding protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=15109
     Region          30..114
                     /region_name="Ssb"
                     /note="Single-stranded DNA-binding protein [Replication,
                     recombination and repair]; COG0629"
                     /db_xref="CDD:440394"
ORIGIN      
        1 mafvrveqrn arlasairle qvngrdglia rgtvtvisnv rrgsepeeat aipwtlwgkq
       61 aenaaeylgk gsrvnvigrl rnnnytdasg itvygygftc eeidyldska eaearrtrqa
      121 sappkapagp atptddnvpf
//
LOCUS       WP_176071815             159 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Piscinibacter koreensis].
ACCESSION   WP_176071815
VERSION     WP_176071815.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..159
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=18226
     Region          11..148
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 mvknwqgvfs rvrsalmrrg rteheaddlv qeawirlecy rreqpvdepe aflmraalnl
       61 sidahrarit rgeevmledv vlvdtqpsae avllsrerlq rlsvclgrln drtraiflah
      121 rvdgmsyqqi arehglsvss vekhiakatm lvtswmegw
//
LOCUS       WP_176071861             222 aa            linear   BCT 11-JAN-2025
DEFINITION  ParA family protein [Piscinibacter koreensis].
ACCESSION   WP_176071861
VERSION     WP_176071861.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..222
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=23156
     Region          3..201
                     /region_name="ParA_partition"
                     /note="ParA family partition ATPase; NF041546"
                     /db_xref="CDD:469431"
ORIGIN      
        1 mktivianqk ggsgkstltv hlaaaaeaag dgpvvitdtd pqgtagdwfn qrkkaglatp
       61 ryaplalsel atklkaldaa gaaylfidta psvgavnael faaadlilvp lnptpadlra
      121 lvkglplikk satpfsfvla rvrpnlrnnd gtamaldalg lvlptrmher viyaetfahg
      181 ktavdidpsg vaatelaslw qsvkhrlnen ekmvilesek aa
//
LOCUS       WP_176071949             276 aa            linear   BCT 11-JAN-2025
DEFINITION  ParA family protein [Piscinibacter koreensis].
ACCESSION   WP_176071949
VERSION     WP_176071949.1
KEYWORDS    RefSeq.
SOURCE      Piscinibacter koreensis
  ORGANISM  Piscinibacter koreensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Sphaerotilaceae; Piscinibacter.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Schumacher,M.A., Tonthat,N.K., Lee,J., Rodriguez-Castaneda,F.A.,
            Chinnam,N.B., Kalliomaa-Sanford,A.K., Ng,I.W., Barge,M.T.,
            Shaw,P.L. and Barilla,D.
  TITLE     Structures of archaeal DNA segregation machinery reveal bacterial
            and eukaryotic linkages
  JOURNAL   Science 349 (6252), 1120-1124 (2015)
   PUBMED   26339031
  REMARK    Erratum:[Science. 2016 Aug 26;353(6302):aai8230. doi:
            10.1126/science.aai8230. PMID: 27563100]
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Motallebi-Veshareh,M., Rouch,D.A. and Thomas,C.M.
  TITLE     A family of ATPases involved in active partitioning of diverse
            bacterial plasmids
  JOURNAL   Mol Microbiol 4 (9), 1455-1463 (1990)
   PUBMED   2149583
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439703
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Piscinibacter koreensis"
                     /db_xref="taxon:2742824"
     Protein         1..276
                     /product="ParA family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29543
     Region          1..245
                     /region_name="ParA"
                     /note="ParA-like ATPase involved in chromosome/plasmid
                     partitioning or cellulose biosynthesis protein BcsQ [Cell
                     cycle control, cell division, chromosome partitioning,
                     Cell motility]; COG1192"
                     /db_xref="CDD:440805"
ORIGIN      
        1 mktlvvcnqk ggvgksavst llthylahkg hrvlaidldh qgnlttplvq sgrlavagit
       61 sdalmtgpla alpdrpqvlv psgrallgle rqpaqhtpla rqfrdflakv drsfdvcivd
      121 tnpnpdirvi salasadfal spiqlnqeam dgvagllnhe rvglrkikav lnpkltligl
      181 lptlveptpy qranfvqvvq ryhallirlg agpgafasip rrsciaeaqs egavlwemkk
      241 taardtwhei epslariaaf vngtktvlea nhatap
//
LOCUS       WP_176072041             240 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Agrobacterium sp.
            CGMCC 11546].
ACCESSION   WP_176072041
VERSION     WP_176072041.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. CGMCC 11546
  ORGANISM  Agrobacterium sp. CGMCC 11546
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Agrobacterium sp. CGMCC 11546"
                     /db_xref="taxon:2579248"
     Protein         1..240
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26153
     Region          1..239
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mieienvrks fgplevlkgi nltvnkgevv tiiggsgsgk stlltcingl epidsgkiai
       61 dgtevhakst dlnklrrkvg ivfqqwnafp hltvlenvml aprkvlgisk ekaeeiavkq
      121 lthvglaekl kvypnrmsgg qqqrmaiara lamspeymlf devtsaldpm lvgevldtlk
      181 mladegmtmi cvthemafar dvsnrvaffh qgvmaeigtp dqlfgapqhp etqkflanvr
//
LOCUS       WP_176072085             468 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter large permease [Agrobacterium sp. CGMCC 11546].
ACCESSION   WP_176072085
VERSION     WP_176072085.1
KEYWORDS    RefSeq.
SOURCE      Agrobacterium sp. CGMCC 11546
  ORGANISM  Agrobacterium sp. CGMCC 11546
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group;
            Agrobacterium.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Agrobacterium sp. CGMCC 11546"
                     /db_xref="taxon:2579248"
     Protein         1..468
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=49900
     Region          12..466
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mllligsfll lmliglpvai smasasllyi vfynvapdii aaqrliagve sfpllavpff
       61 ilagnlmnta gvtgriysfa valvgwmkgg laqvniigsv ifsgmsgtal adaagigtie
      121 ikamkdhgyp veaavgvtaa satlgpifpp slpfviydmm anvsigalfm agivpgvvmt
      181 llmmitvavf ayikgwgsdt pfnlrtifga slevlvvmmv plgiyiltaf glslnlsili
      241 vlvillacdw yfdfsavmal mtpviliggm tmgwftptea avaavlwslf lglvryrtmt
      301 fktlakstfd tiettasvlf ivaaasvfaw lltvsqaaql lsaailtitd skwiflvlvn
      361 llmlfvgcfl dtiaaitilv pillplvlqf nidpvhfgli itlnlmigll hpplgmvlfv
      421 lsrvaklsve rttvailpwl vplfvallli tfipaitlwl ptemglir
//
LOCUS       WP_176072122             141 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Paraburkholderia phenazinium].
ACCESSION   WP_176072122
VERSION     WP_176072122.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia phenazinium
  ORGANISM  Paraburkholderia phenazinium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Paraburkholderia phenazinium"
                     /db_xref="taxon:60549"
     Protein         1..141
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=15444
     Region          <1..130
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mglipalerl tanftrhtgm rcnlqvpqse vemtdeqavv ifrivqeslt naarhsnakr
       61 vdavfrcepe afaleikdng igfdvqnmrk pntfglvgtr ertlraggem dvvskrgrga
      121 lvrvripipg gmqppedvds a
//
LOCUS       WP_176072158              79 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein, partial [Paraburkholderia phenazinium].
ACCESSION   WP_176072158
VERSION     WP_176072158.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia phenazinium
  ORGANISM  Paraburkholderia phenazinium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 79)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Paraburkholderia phenazinium"
                     /db_xref="taxon:60549"
     Protein         1..>79
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
     Region          8..>79
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mngskayleh vaiwvkdihw hirffedvlg mtmrevdgtl daprqywtlg glqfmhdpnh
       61 dapegrlghl gvmcedmea
//
LOCUS       WP_176072162             187 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator, partial
            [Paraburkholderia phenazinium].
ACCESSION   WP_176072162
VERSION     WP_176072162.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia phenazinium
  ORGANISM  Paraburkholderia phenazinium
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Paraburkholderia phenazinium"
                     /db_xref="taxon:60549"
     Protein         <1..>187
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
     Region          <5..187
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 npsvqsyqqr irsliddkga agalsvpama hqfidasrag ldelaagldd aqfdaavsml
       61 eradniyvig vrrsfpvasy ivyalqhtak rvhlvsglgg myreqirsvr kgdvvvaisf
      121 apygketqyc lraarhnhas tlvitdsrls plvreasahl lvkegsafaf rsltsticlc
      181 qalfial
//
LOCUS       WP_176072231             393 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: acetyl-CoA C-acetyltransferase [Paraburkholderia].
ACCESSION   WP_176072231
VERSION     WP_176072231.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 393)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..393
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40106
     Region          1..392
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mtdivivsaa rtavgkfggs lakvaapdlg aivikaaler agvspgqvsd vimgqvltag
       61 sgqnaarqas ikaglptavp amtinkvcgs glkavmlaan aviagdseiv vaggqenmsa
      121 aphvlpgsrd gfrmgdakli dsmivdglwd vynqyhmgvt aenvakeygi treeqdafaa
      181 lsqnkaeaaq kagrfdaeiv pvaipqrkge plqfatdefv rhgvtadsla glkpafskeg
      241 tvtaanasgi ndgaaavvvm sakkaealgl tplarikaya sggvdpkvmg mgpvpastrc
      301 leragwtvnd ldlmeineaf aaqalavnkq mgwdtskinv nggaiaighp igasgcrilv
      361 tllhemqrrd akrglaslci gggmgvalal era
//
LOCUS       WP_176072336             231 aa            linear   BCT 11-JAN-2025
DEFINITION  GGDEF domain-containing protein, partial [Paraburkholderia
            mimosarum].
ACCESSION   WP_176072336
VERSION     WP_176072336.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia mimosarum
  ORGANISM  Paraburkholderia mimosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Paraburkholderia mimosarum"
                     /db_xref="taxon:312026"
     Protein         <1..231
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
     Region          53..214
                     /region_name="GGDEF"
                     /note="Diguanylate-cyclase (DGC) or GGDEF domain; cd01949"
                     /db_xref="CDD:143635"
     Site            order(89,132)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:143635"
     Site            order(94,97..98,102,106,128,130..133)
                     /site_type="active"
                     /db_xref="CDD:143635"
     Site            order(124,154)
                     /site_type="active"
                     /note="I-site [active]"
                     /db_xref="CDD:143635"
ORIGIN      
        1 gdlaveipss hrheeigelf eathvlrqys ieraqleter gqlirelatm adtdpltrll
       61 nrraferrar allddtggas prvallmfdv dhfkrindsy ghgtgdealr viaelcrttv
      121 rqsdvvarvg geefavlmal dnaqfpvaaa laerlrqrig eavviadsge tcritasfgi
      181 afaapgdghd lmrlfrradh mlykaklagr dcviadvypa eggtstpamt e
//
LOCUS       WP_176072410              48 aa            linear   BCT 11-JAN-2025
DEFINITION  cold-shock protein, partial [Paraburkholderia mimosarum].
ACCESSION   WP_176072410
VERSION     WP_176072410.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia mimosarum
  ORGANISM  Paraburkholderia mimosarum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 48)
  AUTHORS   Ermolenko,D.N. and Makhatadze,G.I.
  TITLE     Bacterial cold-shock proteins
  JOURNAL   Cell Mol Life Sci 59 (11), 1902-1913 (2002)
   PUBMED   12530521
REFERENCE   2  (residues 1 to 48)
  AUTHORS   Bae,W., Jones,P.G. and Inouye,M.
  TITLE     CspA, the major cold shock protein of Escherichia coli, negatively
            regulates its own gene expression
  JOURNAL   J Bacteriol 179 (22), 7081-7088 (1997)
   PUBMED   9371456
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003418
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..48
                     /organism="Paraburkholderia mimosarum"
                     /db_xref="taxon:312026"
     Protein         1..>48
                     /product="cold-shock protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
     Region          1..>48
                     /region_name="CspC"
                     /note="Cold shock protein, CspA family [Transcription];
                     COG1278"
                     /db_xref="CDD:440889"
ORIGIN      
        1 matgtvkwfn dakgfgfitp ddggedlfah fseiktegfk slqenqkv
//
LOCUS       WP_176072446             394 aa            linear   BCT 11-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Clostridioides
            difficile].
ACCESSION   WP_176072446
VERSION     WP_176072446.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..394
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=43983
     Region          6..387
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mknalkkiis lamilvfiip nysyaddksv dkysktsili dqetgrvlys kepdmkvpla
       61 slskmmtfll aieaienkev ketdkvkidk siasvkgssy klkdgeevpl ielmrglmiv
      121 sgndaaiaia khicktkeaf vdrmnkkake igmsnthfln pnglpiydls npkkpakeni
      181 stakdiailg kymfdhyekq vtaitdmety tnsdrsfeks ntnallriip evdgiktgyt
      241 gnagyclsfs mvvnkndkne kkrrvigvvl gtnhknkrts aslallkygk enfnmkkvid
      301 kdsfigkkyi kgmkelevtl kakdelyail kddesiksev kiknieypvk kgdtmgiiky
      361 ytssgdllgs vdivsnnsid nvslktklkm kfan
//
LOCUS       WP_176072434             459 aa            linear   BCT 11-JAN-2025
DEFINITION  GspE/PulE family protein [Clostridioides difficile].
ACCESSION   WP_176072434
VERSION     WP_176072434.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..459
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=51636
     Region          14..457
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mikiileess lpmlipekla kkynvfpvef qddnlvveie dediyalqdl rlatgkeiil
       61 kkekkelise kikkyynsfe ldedyakklf enllekaike nasdihiepf kehlivrmrv
      121 dgelkevskf lvdvypslst viklkasmdi tekrlpqdgr vdiklggnli dirvssiptv
      181 ygekivlril nrdtflkdkl elgfseeaik sinriinkra gillvtgptg sgktttvysl
      241 lndlkginkn imtienpvey kmdgisqiqv nskvglsfdv glrailrqdp diimvgeird
      301 aetakiavra aitghlvist lhtndavssi arllemqipp yllnasligv isqklvrkvc
      361 nhcsheimik dnfsgdvntk vavgcekcnd kgyfgrtaiy eileinddik tcirnmedss
      421 tikdvaqnng mitfedsckr linekittle eclvvnemi
//
LOCUS       WP_176072523             654 aa            linear   BCT 11-JAN-2025
DEFINITION  BglG family transcription antiterminator [Clostridioides
            difficile].
ACCESSION   WP_176072523
VERSION     WP_176072523.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 654)
  AUTHORS   Amster-Choder,O.
  TITLE     The bgl sensory system: a transmembrane signaling pathway
            controlling transcriptional antitermination
  JOURNAL   Curr Opin Microbiol 8 (2), 127-134 (2005)
   PUBMED   15802242
REFERENCE   2  (residues 1 to 654)
  AUTHORS   Manival,X., Yang,Y., Strub,M.P., Kochoyan,M., Steinmetz,M. and
            Aymerich,S.
  TITLE     From genetic to structural characterization of a new class of
            RNA-binding domain within the SacY/BglG family of antiterminator
            proteins
  JOURNAL   EMBO J 16 (16), 5019-5029 (1997)
   PUBMED   9305643
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..654
                     /product="BglG family transcription antiterminator"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /GO_process="GO:0009401 - phosphoenolpyruvate-dependent
                     sugar phosphotransferase system [Evidence IEA]"
                     /calculated_mol_wt=75303
     Region          13..654
                     /region_name="BglG"
                     /note="Transcriptional antiterminator [Transcription];
                     COG3711"
                     /db_xref="CDD:442925"
ORIGIN      
        1 mltdmiqnre ikiikfllke ghttvkaiaa dldvsektvs kslkeveavl kkiglslirk
       61 pkigvyidgd lkkilpyldn kgsqipttre erviyiysvl lksndyitiq qlsdelyisr
      121 gtierdlaev ekllknegis iykkpskgik lniserdkrq ltakfihkfw srnwyikqeq
      181 esfyqafeki qadvngifse ddlsiiidil rnfsrerkfe fsdyefqslv ihlaiaveri
      241 rkgeyieesl yigniennqm sntnylakql eekfsillpk seigyinlhl vaadqhrdtn
      301 elkntstnpc etntnnisnl reiikntlye taydkdlidg ltshvhssin rlkyglsikn
      361 pyvntikqnf slsfeqaldl kkviefiydi rinddecayi alhfeafrer mkelpqnirv
      421 ilvcstglgs srllsarikk yfpmikiekv lsvqelvssk idadlvisti yleletipti
      481 vvspilnesd irtlerniqn vscftskkyk sfgnlifeen illnieasny edaikyitdn
      541 likkgfakeg iaksaieren lsytsfqsia tphanpsyik ksnisvatlk npitwgnekv
      601 eviffislen dknleldeiy evfydfidnk knindilsat stkevydllv eesi
//
LOCUS       WP_176072624             234 aa            linear   BCT 11-JAN-2025
DEFINITION  GspE/PulE family protein, partial [Trinickia caryophylli].
ACCESSION   WP_176072624
VERSION     WP_176072624.1
KEYWORDS    RefSeq.
SOURCE      Trinickia caryophylli
  ORGANISM  Trinickia caryophylli
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Trinickia.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Trinickia caryophylli"
                     /db_xref="taxon:28094"
     Protein         <1..234
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
     Region          <1..232
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 givlvtgptg sgktttlyas lsrletattn imtvedpiey dlsgigqtqv nerigmtfar
       61 alrsilrqdp diimigeird letaqiavqa sltghlvlat lhtndaasav trltdmgvep
      121 yllassllgv laqrlvrrlc pvckeervee grvhwhpvgc dkcarsgyag rrgiyellvi
      181 ddairtmihh naadaeilvt araqgmrtlr edgerwlasg mtsleelirv tgga
//
LOCUS       WP_176072642             298 aa            linear   BCT 11-JAN-2025
DEFINITION  GspE/PulE family protein, partial [Trinickia caryophylli].
ACCESSION   WP_176072642
VERSION     WP_176072642.1
KEYWORDS    RefSeq.
SOURCE      Trinickia caryophylli
  ORGANISM  Trinickia caryophylli
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Trinickia.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Trinickia caryophylli"
                     /db_xref="taxon:28094"
     Protein         1..>298
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
     Region          15..>298
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 msdvsgtshe gaagerqaps plaarllpyg farngqilva hqrpegievw isertngaal
       61 aevarnfgal tavrlpadel aqainqayer ndgsaaqvvg evegevdlsr lmqdipeved
      121 lleseddapi irminalltq aarehasdih iepfenasvv rfrvdgtlrd vvrpkkalhg
      181 alisrikima qldiaekrlp qdgritlrvg graldvrvst lptghgerav lrllekdaqh
      241 lnlealgmgp dtlaqfdkli srphgivlvt gptgsgkttt lyaslsrlet attnimtv
//
LOCUS       WP_176072673             315 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella intermedia].
ACCESSION   WP_176072673
VERSION     WP_176072673.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..315
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32675
     Region          11..315
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mnglamltsr pwiwsfiatv avwiitilft ggagahglsh aaftfasfsv ivglgqmfvi
       61 tlgpgnidls vpanmtlaat lalklmdsqe gmilaglava lliglaigic nyalikllri
      121 ppiiatlsms fliqstaiws nrglrvkppe slaqfttast fgvpnvaiva lvlsiigwvl
      181 lkksiygrwi saigqnpfaa rmagipvdgt rfvtyllcav laslcgflla cfsggaalnm
      241 gaeyllmsia vviiggtava ggdsnipgiw gaalfmfliv smlntygfga gvrlvltglt
      301 iiaviilasg rraar
//
LOCUS       WP_176072685             350 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella intermedia].
ACCESSION   WP_176072685
VERSION     WP_176072685.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 350)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..350
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38094
     Region          1..348
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mkevslrgit ktfgqltvld rvdldiqsge flvlvgpsgc gkstllrmva glepisggdl
       61 liggdranel ppqkrniamv fqsyalfphm tarenigfgp rirgekseet aakvdkaasi
      121 lnlhsyldry prqlsggqrq rvamgraivr epsvflfdep lsnldaqlrv qmrteikalh
      181 qrlkstviyv thdqieamtm adrivvmnqg kiqqigaple lydrpankfv asfigspsms
      241 fipgtvsggi frtgegeeia vlagspenrq aeagirpenf tvapggtglt ltvevieptg
      301 pethiygria gqpiravfre rlhlapgeqv hvtaksehih lfdkdsglpl
//
LOCUS       WP_176072723             301 aa            linear   BCT 11-JAN-2025
DEFINITION  hydrogen peroxide-inducible genes activator [Brucella intermedia].
ACCESSION   WP_176072723
VERSION     WP_176072723.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Jo,I., Chung,I.Y., Bae,H.W., Kim,J.S., Song,S., Cho,Y.H. and
            Ha,N.C.
  TITLE     Structural details of the OxyR peroxide-sensing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 112 (20), 6443-6448 (2015)
   PUBMED   25931525
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444038
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..301
                     /product="hydrogen peroxide-inducible genes activator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33137
     Region          7..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..293
                     /region_name="PBP2_OxyR"
                     /note="The C-terminal substrate-binding domain of the
                     LysR-type transcriptional regulator OxyR, a member of the
                     type 2 periplasmic binding fold protein superfamily;
                     cd08411"
                     /db_xref="CDD:176103"
     Site            order(106,109..110,113,117,125..129,222,225..226,229,
                     232..233,235..236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176103"
ORIGIN      
        1 mlnisvrqlh yfmalvkags fsraaevvgv tqstlsaaiq aleaelgvtl idrsgrrmql
       61 lpagddfler artivaliee lpeharqaer plttrlrmgv ipsiapfllp kilpatsraf
      121 pelqltireg ltrslldslr sgsldvalva hpydldefev selghdifyl avrrdhalan
      181 rdrvdaddlq dqpfllletg hclrehvmaa igstpaqasg dvhatsittl vqlvdfgmgv
      241 tllpevavka gvtrgtelsv vpyegknnyr slvlvwcpna arrnefelfa ehlrrkcmkl
      301 i
//
LOCUS       WP_176072742             611 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella intermedia].
ACCESSION   WP_176072742
VERSION     WP_176072742.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 611)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..611
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67119
     Region          11..568
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msgtelsepi skplltvdgl svefgasrvv ddlsfavhpg rtlavvgesg sgksitslsi
       61 mrladmsgak fpsgrimlge rdllkadqkt mrsirgkeia mifqepmtsl npvftignqi
      121 sevlmlhegm tqqaalaegk rllemvrlpd aegllkryph qlsggmrqrv miamalacrp
      181 klliadeptt aldvtiqaqi lhiirelqqe lemavifith dmgvvaemad dvvvmwkgkk
      241 veegpvgqif skpqhaytkt llsavpklgs mtgeafpkrm pvmtmrdgvp vvsgeeriqd
      301 tarydskpll svddlyvrfp ikknlfgkit hvcnavsnva fdiypgetla lvgesgsgks
      361 tigrtiqqlq tplsgdirfn gkaysamsaa eryamrrevq yifqdpfasl dprktigfsi
      421 aepirthgll dndkainarv aellervglg peharryphe fsggqrqrvc iaralaskpk
      481 liiadealsa ldvsiqaqvi nlfmdlqkeh dlaylfishd mavvekmshr vgvlylgqim
      541 elgsrqqvfe tpshsytkrl lsavpiadpt artkrpaleg eipsttrlid dkpaiykhre
      601 vaaghfvaet a
//
LOCUS       WP_176072766             174 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter small permease [Brucella intermedia].
ACCESSION   WP_176072766
VERSION     WP_176072766.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..174
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=19186
     Region          1..159
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mtkaidffyk ilgailvfll agmaimvfvn vilryaansg ltvseelary ffvwvsflga
       61 vltfrenshl gieslvarfg rqgrvtcmav sylivllcsg iffwgtwkqf dinasmvapv
      121 tglsmiwvyg vglftggamf iiaaerflra vtgrltdeei atfagehsld hlme
//
LOCUS       WP_176072797             355 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella intermedia].
ACCESSION   WP_176072797
VERSION     WP_176072797.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 355)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..355
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39060
     Region          1..353
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtdcrirfen isksygdfkv idglnldigk sefvsllgps gsgkttllmm lagfespssg
       61 tiyidgkpin avpsykrnmg vvfqnyalfp hmtvgenvaf plqmrgvgkg eigklvdkvl
      121 dmvqlstmre rkpsqlsggq qqrvalaral vfepgvvlmd eplgaldkql reqmqldira
      181 lhsrlgltiv fvthdqgeal tmsdriavfn kgkieqigtp raiydepqtr fvaefigetn
      241 laegiierme darafirlkd ggtltaaske tlaagqkvll sirperielg sednsdnllr
      301 trvvdsvyqg dhlriqldgs ahdfivrldr ksrewtpgtd vvakfsaadc wtiva
//
LOCUS       WP_176072799             262 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella intermedia].
ACCESSION   WP_176072799
VERSION     WP_176072799.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..262
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27536
     Region          1..258
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mgrlakivfg atavifliap lfailplaft ssvfltypvp gwsgrwfeel atadvwrrai
       61 vnsliigsgt milatvlgtm aalglrsrii flsdpiktlf llpmvvpavv lgvgmqllfv
      121 rlgiansylg vivahtvisi pfvlvsvtga lggidrrvel aaeslgaspl tvfrkitlpl
      181 ampgiasgav lafatsldev vltlfvagpn qrtlarqmfs tirenispai aaaaflfiag
      241 tvllglaaml frrkrssgiv st
//
LOCUS       WP_176072804             270 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella intermedia].
ACCESSION   WP_176072804
VERSION     WP_176072804.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 270)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..270
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29113
     Region          7..261
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 msnildwrwl prgillglla faifgplanl llwavaerwy fphtlplqyg fsfwanvfsp
       61 rgnalsslgt svliaaltvi vslglaipag yalsrlklpf rglilltlli pqafpnlpvy
      121 vniaqmfysf glngtitgvv lvhvthglvy avwiataafs aidreieeaa rsmgasalkt
      181 ffditlpiaa pgllasaifv flesldeftg tyfvgapdis tlplllytas sggnyqiasi
      241 salillvpsi afmfvverfl radvlskvgr
//
LOCUS       WP_176072779             346 aa            linear   BCT 11-JAN-2025
DEFINITION  dipeptidase [Brucella intermedia].
ACCESSION   WP_176072779
VERSION     WP_176072779.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Yamada,R. and Kera,Y.
  TITLE     D-amino acid hydrolysing enzymes
  JOURNAL   EXS 85, 145-155 (1998)
   PUBMED   9949873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..346
                     /product="dipeptidase"
                     /EC_number="3.4.13.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0070573 - metallodipeptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=37550
     Region          5..346
                     /region_name="COG2355"
                     /note="Zn-dependent dipeptidase, microsomal dipeptidase
                     homolog [Posttranslational modification, protein turnover,
                     chaperones, Amino acid transport and metabolism]"
                     /db_xref="CDD:441922"
ORIGIN      
        1 mateqkipvf dghndvllrl wsseaaapek rfldgenvgh idlpraqkgg lggglcavyv
       61 pspsreldan gnlatpsqtd amkatlamsa illkierese grvrvcrtaa dirdafakgi
      121 fasvyhiegv eafsedldal yvlheaglrt lgpvwsrpni fahgipfrfp aspdigpglt
      181 dhgkalirac nelkvmidls hmnekgfwdi aaisdaplva shsnahalcq qsrnltdrql
      241 dairdtgglv glnfgvsflr edgkrdpdtd lseivrhady ivdrigidhl algsdfdgtt
      301 isstlrdvsd lqlvieafrk hgyddasivn lahgnwinvl ertwga
//
LOCUS       WP_176072688             288 aa            linear   BCT 11-JAN-2025
DEFINITION  glycine betaine ABC transporter substrate-binding protein [Brucella
            intermedia].
ACCESSION   WP_176072688
VERSION     WP_176072688.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Wolters,J.C., Berntsson,R.P., Gul,N., Karasawa,A., Thunnissen,A.M.,
            Slotboom,D.J. and Poolman,B.
  TITLE     Ligand binding and crystal structures of the substrate-binding
            domain of the ABC transporter OpuA
  JOURNAL   PLoS One 5 (4), e10361 (2010)
   PUBMED   20454456
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Gu,Z.J., Wang,L., Le Rudulier,D., Zhang,B. and Yang,S.S.
  TITLE     Characterization of the glycine betaine biosynthetic genes in the
            moderately halophilic bacterium Halobacillus dabanensis D-8(T)
  JOURNAL   Curr Microbiol 57 (4), 306-311 (2008)
   PUBMED   18661182
  REMARK    Erratum:[Curr Microbiol. 2009 Dec;59(6):65]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10194542
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..288
                     /product="glycine betaine ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31787
     Region          30..287
                     /region_name="PBP2_OpuAC_like"
                     /note="Substrate binding domain of Lactococcus lactis
                     ABC-type transporter OpuA and related proteins; the type 2
                     periplasmic binding protein fold; cd13639"
                     /db_xref="CDD:270357"
     Site            order(38,40,86,114,149,153..154,199)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:270357"
ORIGIN      
        1 mlgkltkfgl aavvagtmtm gaafaqdskp vkigwapwsd aefvtklakk liednlgqkv
       61 elvqtdvapl yqgvsrgdid ammmawlpet hadyykrieg kvenlgplye gaklgwiipa
      121 yipeseissi edlkkpevre klkgeiqgid pgagltrlsq eaikkygldy klnisseaam
      181 lttvdratrs dgwfvatsws phwmfgkykl ryiadpegal ggaehidaia rkgfkeenpk
      241 vaslltkmsl piseleaamf daqetsyeka vdkyiadhpd rikewlae
//
LOCUS       WP_176072809             286 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter permease [Brucella intermedia].
ACCESSION   WP_176072809
VERSION     WP_176072809.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 286)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437853
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..286
                     /product="metal ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=30576
     Region          10..268
                     /region_name="ZnuB"
                     /note="ABC-type Mn2+/Zn2+ transport system, permease
                     component [Inorganic ion transport and metabolism];
                     COG1108"
                     /db_xref="CDD:440725"
ORIGIN      
        1 mtlllepfsy nymlnamwvs alvggvcafl saylmlkgws ligdalshsi vpgvagayml
       61 glpfsigaff sgglaaaaml flnqrtklke daiiglifss ffglglfvis lkptavsvqt
      121 ivlgnilait pedtlqlaii gfvslsllll kwkdlmvvff denharsigl rpaqlkimff
      181 tllsastvaa mqtvgaflvi cmvvtpgata ylltdrfsrl lwiavaigsv tsfvgayvsy
      241 fldgatggii vvlqtlvfls vfllapkhgl laarrkasla lrefqq
//
LOCUS       WP_176072883             434 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrolipoamide acetyltransferase family protein [Brucella
            intermedia].
ACCESSION   WP_176072883
VERSION     WP_176072883.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..434
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=46464
     Region          4..433
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mahftiklpd vgegvaeael vewhvkvgdv vreddllaav mtdkatveip ssragkviai
       61 ngevgekiav gselvrleie ggsqeekaee kpvpvaaeaa kpqpaqapet pvllqtpvpp
      121 kpaapkreaa gsafsgagpv rqegekplat psvrlrardg gvdlrrvrgs gpagrithdd
      181 ldlyfqqeig aapvlsgyat dtsvneikvi glrrkiaerm aeakrhiphi tiveevdvtq
      241 leelrnglnn ekkegrprlt llpfiiraiv kavkeqpgln ahfddeadii rqfggvhvgi
      301 atqtpngliv pvvrhaesms vfaaaselar vtdaarngta kreeltgsti titslgplga
      361 iattpiinrp evaivginkm avrpmwdgvq fvprkmmnls csfdhrvidg wdaavfvqkl
      421 kslleapami fveg
//
LOCUS       WP_176072906             283 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella intermedia].
ACCESSION   WP_176072906
VERSION     WP_176072906.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..283
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=30991
     Region          19..272
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mlmeapstia retdgnsvpa ialnnvtrrf vtpdgkmmta lrdftmnvaq gefacvvgpt
       61 gcgksttlnl vtglakpsag evrlmgkpie gispdigfvf qadalfpwls vidnvsagpr
      121 yrgmgmeeay ekarswiarv glarfenhyp hqlsggmrkr valaqtfine pkillmdepf
      181 saldvqtrtl mqgelldlwq qsgasvifvt hdleeaiala dkvyvltagp atvksvydid
      241 iprprvmedi rydsqfvdia kviwddlree vqigqkrala sgn
//
LOCUS       WP_176072926             217 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Brucella intermedia].
ACCESSION   WP_176072926
VERSION     WP_176072926.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..217
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24852
     Region          3..203
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mslklylhpf ssycqkaita fyekdiafea rmldgtepva sefaalwpfg kfpiltdngk
       61 lvfeatgiie yleaayphsr rlipsdplas advrmwdrff dnyvnypqqr lvyialgreh
      121 ddggdrwram ldtayafldr hmagrewasg defnladcaa apsllyadwt yaiaeeftnv
      181 wvyrkrllar psyaraldea rpfrhlfplg apeegrd
//
LOCUS       WP_176072958             251 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Brucella intermedia].
ACCESSION   WP_176072958
VERSION     WP_176072958.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..251
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26352
     Region          12..240
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; pfam01925"
                     /db_xref="CDD:460386"
ORIGIN      
        1 mtysfslilt iaitflcagf vkgvtgmglp tvamgilgal isplaaasll iipsfvtnlw
       61 qlvagpsfga lmlrlwsmml aivvgtitgt avlvggniai ttsmlgfslv vyaaytllar
      121 qlqvpekler llspvigllt gliagatgif vipavpylss lglrkddlvq slglsftvst
      181 aalgvglssr qaysgdllli svlaivpala gmflgqffrr kirpesfrrw fliglmvlgl
      241 emalrplfsl s
//
LOCUS       WP_176073004             201 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Brucella intermedia].
ACCESSION   WP_176073004
VERSION     WP_176073004.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..201
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=21852
     Region          13..200
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 mttqtyehrl kagakgaplf ivfhgtggde nqffglaeql lpdativspr gdvseygaar
       61 ffrrtgegvy dmedlaratd kmagfiaala aehkpsevig lgysneanim anlliekgrv
      121 fdkaallhpl vpfrpkdnpa legakilmta grmdpicppd ltealaqyfe rqkadvelvw
      181 hpgghelrqt elaavqslla y
//
LOCUS       WP_176073012             544 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella intermedia].
ACCESSION   WP_176073012
VERSION     WP_176073012.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 544)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..544
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=59311
     Region          1..532
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtaapvleik nlqialpkga drpfalqdls ltinpgeivc lvgesgsgks lsagaimrll
       61 pephvrvtrg tirlegtdly slseadmkkl rgnrigmifq epmtalnpqk tvgwqidevl
      121 rlhtklgrke rraavldmla evkipdpesa ynayphqisg gqrqrvmiam alilkprlii
      181 adepttaldv ttqaqilkli rdlqrehntg ilfithdfgv vaeiadrvav lrlgelveeg
      241 panevlnhpq hpytralias vpaltpppak psleqpvilr asalrktfka rgglltgkrs
      301 avsavkdlsf elrqgetlgv vgesgsgktt vsrivtrlle adsgkvdvng kdflsaspre
      361 vramrkdiqm vfqdpmasln prrrvvdlia qgpivhgvpk eqahakarel lelvelspaa
      421 adrfphefsg gqrqrigiar alalepriiv adepvsaldv svqaqvlrll adlrerlnls
      481 llfvthdlrv aaqlcdriiv mskgeiaeag ptaqvfanpq heytqrllas ipgkgwtppr
      541 leha
//
LOCUS       WP_176073017             347 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella intermedia].
ACCESSION   WP_176073017
VERSION     WP_176073017.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..347
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35993
     Region          1..347
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 mrierretrp valvatapvi avlaafvlag lliaaagapv lesfrqiaig afgnklsite
       61 tltratplml tglaaavafr sklwnigaeg qfymgalavv acgtqlqlpa vilipllliv
      121 gaiagmifll iplglrlrfg vdevvttlll nfvavlivsm miegpmkdpl afgwpqsepv
      181 pdaavlpkim sgmrlhigia iaialaliia yvqkrtvfgl etkaaglnpr aarfagvpla
      241 rtlvkvacis gglaglagai qvmgvkgyvt tdlspgfgys giivamlanl npvgaifsal
      301 faaamfvgad gmsraigips fiadvtvals lltmlvalff tqyriar
//
LOCUS       WP_176073028             269 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella intermedia].
ACCESSION   WP_176073028
VERSION     WP_176073028.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..269
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29804
     Region          41..265
                     /region_name="ArtM"
                     /note="ABC-type arginine/histidine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4160"
                     /db_xref="CDD:443325"
ORIGIN      
        1 mstssavlen rtsarnwlep hrlvltviai alfasavvfg rwdwlpqylp rlgsgivvtl
       61 fmlfgsailg fmlalplgll qvtgpwwlsw pakafctvir gtplllqlwl lyyglgslfp
      121 sipgirgsfi wpylreawpy glaaltisfa ayegevmrga fagvpsgelq agrafgmspw
      181 kvfrriwlpr aihralptln getvlqlkat plvatitvvd vygvvsrvrq etyltyepll
      241 llaliymilt aglvlvfrrl enriptrga
//
LOCUS       WP_176073054             447 aa            linear   BCT 11-JAN-2025
DEFINITION  TldD/PmbA family protein [Brucella intermedia].
ACCESSION   WP_176073054
VERSION     WP_176073054.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..447
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46810
     Region          25..446
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 misgnsaekl vdraavlvaa arragadhad avvmrarsvs vsvrlgkveg tessesddfs
       61 lrvfvgrria svsanasadp drlaeravam arvapedpye qladpsllvv sprdldlfds
      121 teidtdrltq dalateeaal avkgvsnsgg agasrslggl vlvtstgfsg hyaatrfgrs
      181 vsaiagegtk merdydfssr lhfsdldtpg eigrragera vrrlgarqak tgpvtvvydp
      241 rlargiaghl asaingasva rktsflrdsl gkqvlksgin vtdnplrvrg sssrpfdgeg
      301 iegqpltmve dgvlnhwlls gssarelglq gngrgvrsgs gvspastnfa iepgsqspee
      361 lirsvgtgfy vtevfgqgvd mitgqysrga sgfwiengel aypvsevtia snlkdmflnm
      421 tpasdidrnf gmtaptlvie gmtlagn
//
LOCUS       WP_176073064             186 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Brucella intermedia].
ACCESSION   WP_176073064
VERSION     WP_176073064.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..186
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20375
     Region          4..141
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 msklkvavii gstreqrfap vpaqwiarlv aerpeldvev ldvadypmgf ygdtttttaq
       61 aetadkwktk lrefdayilt aaeynhapta vlknaidygd wiqkpmgfvg yggvggarav
      121 eqlrmiavem ssmsvktgvh ilfpdylavv kgenklddfp hlaeaaknml dqliwwgkal
      181 kagrga
//
LOCUS       WP_176073078             249 aa            linear   BCT 11-JAN-2025
DEFINITION  L,D-transpeptidase [Brucella intermedia].
ACCESSION   WP_176073078
VERSION     WP_176073078.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Mainardi,J.L., Villet,R., Bugg,T.D., Mayer,C. and Arthur,M.
  TITLE     Evolution of peptidoglycan biosynthesis under the selective
            pressure of antibiotics in Gram-positive bacteria
  JOURNAL   FEMS Microbiol Rev 32 (2), 386-408 (2008)
   PUBMED   18266857
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..249
                     /product="L,D-transpeptidase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=27227
     Region          101..237
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mprkksqddl tngfakaafs rrgfligasa valsgcvstv pepsqpvkkl pqpapsrpvp
       61 lmyqalpdeq fpipavdtsk vdpkfwrqev dyptdevkgt vivdtpnkyl yhvlgngram
      121 rygigvgrdg fawagrakia ykrqwprwtp pdemvarqpa lepysiangg mppgiknplg
      181 aramyihkdg rdtlyrihgs peawsigkav ssgcirmlnq dvidlynnvr dgstivvipd
      241 pskgqqvvs
//
LOCUS       WP_176073084             255 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella intermedia].
ACCESSION   WP_176073084
VERSION     WP_176073084.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..255
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27296
     Region          2..255
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mpemsgikle nltrsfsgrg tnvialsdvs lecpagsfta ligpsgcgks tmlrlalgld
       61 rpdsgavsvm dkspveaaka gltgvafqda almpwrsved nialpldvlg lsrsakshri
      121 aelialvglk gfekalpgel sggmrqrvai arslvtdprv lfldepfgal dqilrrqmni
      181 elqriwlesk attllvthgi deavfladri vvmhsrpgri aqiidipler prspeifsts
      241 qfhaledava ealhg
//
LOCUS       WP_176073104             333 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella intermedia].
ACCESSION   WP_176073104
VERSION     WP_176073104.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..333
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36658
     Region          1..333
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 maelqlrdvr ksfgnfevir gvdmdirpge fmvfvgpsgc gkstllrlia gleeissgsl
       61 sidgtvvnsf apskrgiamv fqsyalyphm tvyenmafgm qlagkdkqec kariqaaaem
      121 lqltpylerl prqlsggqrq rvaigraivr dpkvflfdep lsnldaalrv atrleiaklh
      181 esmedttmiy vthdqveamt ladricvlrd grveqigtpl elyekpnslf vagfigspkm
      241 nfltgrysep fgahtvglrp ehlaivaegg hwtgrvihse ilgsdtyvyi dlgleeplvv
      301 resgvaarrs getlsvspmg dnihrfdekg rav
//
LOCUS       WP_176073119             346 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella intermedia].
ACCESSION   WP_176073119
VERSION     WP_176073119.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..346
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36961
     Region          28..346
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msasqyqqdm gqkklgrvqs fklgefirrr pesitffllv aictivsvin paflqastli
       61 digrasvvmg lfalgvfiil aaggidvsft aiaattvysl tllvqaympe lpiifiilma
      121 iaggiflgvl ngllvhylnv pslivtigtq ylfrgfllaf vgtvwimslp ptmgafgrlp
      181 lfqfesttga titmpfyflv lpaaailtww ilnrtlmgra ifamggnsqi aarlgynlrt
      241 ihiflfgyag glaglagiih vcanrqsspf dfvgteisvi aavvlggari tggtgtvvgt
      301 llgvllitvi nsvlvlvgip stwqrlvvgc fillaaaffv trqrkk
//
LOCUS       WP_176073247             260 aa            linear   BCT 11-JAN-2025
DEFINITION  tRNA1(Val) (adenine(37)-N6)-methyltransferase [Brucella
            intermedia].
ACCESSION   WP_176073247
VERSION     WP_176073247.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467886
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..260
                     /product="tRNA1(Val) (adenine(37)-N6)-methyltransferase"
                     /EC_number="2.1.1.223"
                     /GO_function="GO:0008170 - N-methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0016430 - tRNA
                     (adenine-N6)-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=26713
     Region          11..255
                     /region_name="TrmN6"
                     /note="tRNA1(Val) A37 N6-methylase TrmN6 [Translation,
                     ribosomal structure and biogenesis]; COG4123"
                     /db_xref="CDD:443299"
ORIGIN      
        1 mnpetendag etldvfhrga fhlvqpalkg hrsgvdamil asavpngfag rvadlgsgag
       61 aaglavasrc agatvtlver safmagfark sidhplnaal adrvnviead valrgkaria
      121 agladnsfdf aimnppfnea rdrstpdplk aeahvmpegm feqwvrtaaa ivkpgggiai
      181 iarpgsispi lealsgrfgg lrivpvqprp daaairivvt girgsrasls lmpalvlhgs
      241 eghgftprad ginngldalv
//
LOCUS       WP_176073287             200 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Brucella intermedia].
ACCESSION   WP_176073287
VERSION     WP_176073287.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22391
     Region          12..169
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpptatkpkp rtkpaeirrd elmaaaealf lekgfaatsv deivrladva kgtfylhfrs
       61 kddilialre rfidgfcegl erqlaqypvd dwhgklvawa etgiagyldn yrihdmvfhd
      121 fhpplrrmkq enpaivrlda lltdgnsaga wkisnprlta vllfnalhga vdeiisnpdm
      181 mdrtemvagv kafflqtvra
//
LOCUS       WP_176073296             233 aa            linear   BCT 11-JAN-2025
DEFINITION  polysaccharide deacetylase family protein [Brucella intermedia].
ACCESSION   WP_176073296
VERSION     WP_176073296.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Caufrier,F., Martinou,A., Dupont,C. and Bouriotis,V.
  TITLE     Carbohydrate esterase family 4 enzymes: substrate specificity
  JOURNAL   Carbohydr Res 338 (7), 687-692 (2003)
   PUBMED   12644381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10180925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..233
                     /product="polysaccharide deacetylase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26381
     Region          65..220
                     /region_name="CE4_NodB_like_5s_6s"
                     /note="Putative catalytic NodB homology domain of PgaB,
                     IcaB, and similar proteins which consist of a deformed
                     (beta/alpha)8 barrel fold with 5- or 6-strands; cd10918"
                     /db_xref="CDD:213023"
     Site            order(69..70,135,139,175..177)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:213023"
ORIGIN      
        1 mpvpillyhq idvppthrap yrsmivhpdr frqqmawlkr lgyrglsvrd alpyiygkkq
       61 gkiavitfdd gfenvfrnal pvlqefgfta tnyfvanqig gfnlwdqkig varatcmsva
      121 elrewatlgh evgshtldhi llpdasekda iaqihqsrtr iedvlgsevt sfaypyggen
      181 aatrkiveaa gytnatttek rrarptddpf giprltirrn dmlmqflrkt ftr
//
LOCUS       WP_176073333             273 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella intermedia].
ACCESSION   WP_176073333
VERSION     WP_176073333.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..273
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=30272
     Region          16..267
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mslndsmapk ggeayaqtvi dikdlslvfe tndgpvhals nidlavrrge fvsfigpsgc
       61 gkttlmrvva dlerptsgsv tvngktpeqa rlarsygyvf qaaalfpwrt iednislple
      121 imgfsraerr erieknlalv nlsgfgkkyp wqlsggmqqr asiaralsfd pdmllmdepf
      181 galdeivrdh lneqllklwa atrktvifvt hsipeavfls tkivvisprp griheiidcd
      241 lgpdrpleir eseaflkiah rvreglrlgh ihe
//
LOCUS       WP_176073344             267 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Brucella intermedia].
ACCESSION   WP_176073344
VERSION     WP_176073344.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..267
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29488
     Region          13..261
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 miftrgvhle tedryrapal dkgldilell asvdggltqa eiakhldrsp nefyrmldrl
       61 vkrgyvtkle gdrysltlkl fglahlhapv rrlasfatpf mreladrsrq anqlavfdrg
      121 svvviaqqea pdywgisirv gshislfdtg sghvllafrs peerkmmiae yakdvesvkl
      181 dqdfyerldq irergyemmp saqvagvynl sapilgpdgt ciasltcpyv tlvnsasapd
      241 itqtigllqk tvqdlsklvg sdigaae
//
LOCUS       WP_176073350             251 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella intermedia].
ACCESSION   WP_176073350
VERSION     WP_176073350.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 251)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 251)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003065
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..251
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26386
     Region          45..246
                     /region_name="OpuBB"
                     /note="ABC-type proline/glycine betaine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG1174"
                     /db_xref="CDD:440787"
ORIGIN      
        1 mrllvsivpr lvllgilllf larprlfepl frplvdegvp aiydraslvt ltlqhlglva
       61 latlaatlva vsmaifvtrk hgaeflplsr slvnigqtfp pvavlalavp ifgfgdkptl
      121 ialflygllp ifentltglt tlpspvveaa rgmgmtsaqr lvkievplam pvilagirls
      181 avislatati gstvaartlg eviiaglisn nlafvlqggl vvaalailif dgfqaiehyl
      241 lkrsgrtgna l
//
LOCUS       WP_176073396             203 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Brucella intermedia].
ACCESSION   WP_176073396
VERSION     WP_176073396.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..203
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21551
     Region          3..203
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msieflltsf iivaspgtgv lvtlaaglsr garasviaal gctlgivphm laavtglaal
       61 lhasalafel ikyagvayll ymawmtlkeh gtlkietdda prsdgevirs ailvnllnpk
      121 lsifffaflp qfvntqqgat varmvelslv fmamtfvvfa iygvfaaavr nqiisrpavl
      181 awmrrsfaaa fvalgaklal ter
//
LOCUS       WP_176073420             249 aa            linear   BCT 11-JAN-2025
DEFINITION  L,D-transpeptidase [Brucella intermedia].
ACCESSION   WP_176073420
VERSION     WP_176073420.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Mainardi,J.L., Villet,R., Bugg,T.D., Mayer,C. and Arthur,M.
  TITLE     Evolution of peptidoglycan biosynthesis under the selective
            pressure of antibiotics in Gram-positive bacteria
  JOURNAL   FEMS Microbiol Rev 32 (2), 386-408 (2008)
   PUBMED   18266857
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11443278
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..249
                     /product="L,D-transpeptidase"
                     /EC_number="2.-.-.-"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /GO_function="GO:0071972 - peptidoglycan
                     L,D-transpeptidase activity [Evidence IEA]"
                     /GO_process="GO:0018104 - peptidoglycan-protein
                     cross-linking [Evidence IEA]"
                     /calculated_mol_wt=26771
     Region          99..233
                     /region_name="ErfK"
                     /note="Lipoprotein-anchoring transpeptidase ErfK/SrfK
                     [Cell wall/membrane/envelope biogenesis]; COG1376"
                     /db_xref="CDD:440986"
ORIGIN      
        1 mavvaclpfv aaacttasae rpiagtmpqp vafkpepvaa epvsqpapem qtakseyetm
       61 ygavndrgnl ipaldvskia nrnlrrevdy atnepvgtiv vdpyarylyl vqpggkairy
      121 svgvgraglt fsgdakvayk sqwprwtpta nmikrnpehy akyanglegg irnplgaral
      181 ylyrdgkdtl yrihgtnepw svgkaassgc irlynqdild lykrasagar vvvldksqse
      241 aksgkgass
//
LOCUS       WP_176073437             347 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella intermedia].
ACCESSION   WP_176073437
VERSION     WP_176073437.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..347
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35564
     Region          26..300
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 miarmtrklk rlapqlaalv lilaantiia pgfldisfqn grlygslidi lvraapvail
       61 svgmtlviat rgidlsvgav maisgafaas livagyplai vipaalgvgl lcglwngflv
      121 avfdlqpiia tlilmvagrg iaqlitegai ltfnndsfaa lgsgsflgvp vpvliwilag
      181 lavglavrts algflieatg inrraamlag vkahfllfsv yavsgvgaal agliaaadir
      241 gadannaglw leldailavv iggtslnggr fsimasllga liiqsintgi lmagfppefn
      301 liikaiiivi vltfqspaiv qlitflrser kgdgakpvrq sqqgaqq
//
LOCUS       WP_176073440             311 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Brucella intermedia].
ACCESSION   WP_176073440
VERSION     WP_176073440.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..311
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34075
     Region          9..248
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 maaesniava ivglgkiard qhlpsieavd gielkaiasr nagldglpsf hdidallgsd
       61 laidavslct ppqgrfqqay aalkarkhvm lekppgatis evqalerlaq aagvtlyatw
      121 hsreaaavep areflkdaei rsvaviwked vrhwhpgqqw iwepgglgvf dpginalsiv
      181 thilperffl tqsdlyfpen raapiaadlk fqtesgipvs feldwrqtgp qtwdirvetd
      241 kgtvllshgg srlaiagtek maepdreyqr lykrfvqlir agrsdvdlap lthvadafll
      301 gkrhvveafe n
//
LOCUS       WP_176073497             512 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-binding protein [Brucella intermedia].
ACCESSION   WP_176073497
VERSION     WP_176073497.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 512)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 512)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 512)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 512)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418077
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..512
                     /product="ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55194
     Region          25..>158
                     /region_name="ExeA"
                     /note="Type II secretory pathway ATPase component
                     GspA/ExeA/MshM [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG3267"
                     /db_xref="CDD:442498"
     Region          <94..278
                     /region_name="HerA"
                     /note="Archaeal DNA helicase HerA or a related bacterial
                     ATPase, contains HAS-barrel and ATPase domains
                     [Replication, recombination and repair]; COG0433"
                     /db_xref="CDD:440202"
ORIGIN      
        1 mqvgidmgsv agsgsasaaa lgggkqamld leellatrll vqgnsgsgks hllrrlleqs
       61 aqwvqqcivd pegdfvtlad lyghvvvdaa rteaeltria grirqhrvsv vlnlegldve
      121 qqmrsaaafl gglfdaerdy wypmlvvvde aqlfapaaag evsdearkls lgamtnlmcr
      181 grkrglagvi atqrlaklak nvaaeasnfl mgrtfldidm araadllgme rkqaemfrdl
      241 qrghfvalgp alsrrplpik igkvetsars sspklmplpd apedaldlif tpapqeirta
      301 vrrappppps taeilaqvak pkpeaepvea plfpgiveae reellekvmr eivddpeasf
      361 rsvavlyqdf lvrcrihrvp geplalpafr rrlavaqasi esdvangetw qqalilsesl
      421 tddvqgvfli vaqaavtgap cpsdaalara ygthsfsrar rlltyfeerg llvvrndfkg
      481 mrivnfpdla cetapgdpna pddlaeegaa ae
//
LOCUS       WP_176073506             190 aa            linear   BCT 11-JAN-2025
DEFINITION  SH3 domain-containing protein [Brucella intermedia].
ACCESSION   WP_176073506
VERSION     WP_176073506.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Kurochkina,N. and Guha,U.
  TITLE     SH3 domains: modules of protein-protein interactions
  JOURNAL   Biophys Rev 5 (1), 29-39 (2013)
   PUBMED   28510178
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Mayer,B.J.
  TITLE     SH3 domains: complexity in moderation
  JOURNAL   J Cell Sci 114 (Pt 7), 1253-1263 (2001)
   PUBMED   11256992
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Musacchio,A., Gibson,T., Lehto,V.P. and Saraste,M.
  TITLE     SH3--an abundant protein domain in search of a function
  JOURNAL   FEBS Lett 307 (1), 55-61 (1992)
   PUBMED   1639195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..190
                     /product="SH3 domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0070064 - proline-rich region binding
                     [Evidence IEA]"
                     /calculated_mol_wt=19504
     Region          1..91
                     /region_name="YraI"
                     /note="Uncharacterized conserved protein YraI [Function
                     unknown]; COG4991"
                     /db_xref="CDD:444015"
ORIGIN      
        1 mylsvkasif tlaflvsana yassaivtst vnlrtgpgtq ygtigaipng vgvtvggcts
       61 gygwcqvsyg gmtgwaassy iaiqtgngyt tndnfgstaa avgipliagi aigsalsann
      121 drywgtgpyr gwggggnvyn gcigrncqsn wgpprphwtd rpgwndhpgy hpgfgrgfgp
      181 gprirmggrl
//
LOCUS       WP_176073552             240 aa            linear   BCT 11-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Brucella intermedia].
ACCESSION   WP_176073552
VERSION     WP_176073552.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 240)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 240)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 240)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..240
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=26083
     Region          18..240
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mnqtfrpgra sahadivdgv rrglplvvag apfgllfgal avdnglslae avfmsaiiya
       61 gasqmvgldl fsqniapwmi vmsifavnfr hvlysattgr rirhfrlwqk alaffvlvdi
      121 qyaeveqrae agkpvtfawy malgltfylt wvlealiggl fgnlitnpya fgidfllpiy
      181 flgmvmsfrh rqnwlpvviv saisavaayk fvgspwhvsl galggialaa iiakpregea
//
LOCUS       WP_176073572             213 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Brucella intermedia].
ACCESSION   WP_176073572
VERSION     WP_176073572.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..213
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=23421
     Region          19..175
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtdtsdelqa qkqqalsprq ndvleqalrl lveggdralt tasiaraanc skeslykwfg
       61 drdglltamv rwqaskvrvv pltrekldae slfsslehfa rdwllvlsgk tsialnrlav
      121 shaasaksal gdivlangpv amaqrlkpil hmgqeaglla fddideafrt ffglvvrdmq
      181 irlllgdhle ltddvvirda rratkqffal yga
//
LOCUS       WP_176073580             279 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Brucella intermedia].
ACCESSION   WP_176073580
VERSION     WP_176073580.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427633
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..279
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30037
     Region          34..264
                     /region_name="FepB"
                     /note="ABC-type Fe3+-hydroxamate transport system,
                     periplasmic component [Inorganic ion transport and
                     metabolism]; COG0614"
                     /db_xref="CDD:440379"
ORIGIN      
        1 mkrasanwii sfclaaglal fvrnpadaad spkrvvsinv ctdqlailla regqlqsvsy
       61 lsqdpelsvm aakarqlpan haqaeevflm kpdlvlagtf ssratvgllr rlgvrveefa
      121 parsfsdied hlrrmsellg rqaeasreid kmkaalaaiq qpvrrktval yyansytsgr
      181 gtlvdeavrl agldnladka gvsgsaalsl eklvlekpdi lvrssrerap alafenfehp
      241 alralerqar avtiadnltv cggpfsveav aelaeaard
//
LOCUS       WP_176073621             293 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Brucella intermedia].
ACCESSION   WP_176073621
VERSION     WP_176073621.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785415
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..293
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32058
     Region          105..291
                     /region_name="YpfH"
                     /note="Predicted esterase [General function prediction
                     only]; COG0400"
                     /db_xref="CDD:440169"
ORIGIN      
        1 msrratrsll gmlfllsaat asgasslppy kddyfaypgv issadngdyk vvdynemrdi
       61 ngrdavpekr vkdayvslka rayqkdvtfq tkagpvkamt agkregasfi viylhgrggn
      121 rlqgmndftf ggnfnrvknl aalngglyvt pdfkdfadag eaqiagliea vkasspsapl
      181 ilscgsqggt lcwriagnen agsqlaglil lgslwdegff kspafrkrvp vffghgsrdp
      241 vfaidkqesf yreirkrapg ypvqfrrfes gnhgtpirms dwremlnwil akq
//
LOCUS       WP_176073643             523 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Brucella intermedia].
ACCESSION   WP_176073643
VERSION     WP_176073643.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..523
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=57371
     Region          27..521
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 maapydlknd kvvviigsga gggtlgnela qkgidvvile agkrhefedf indewdsfdq
       61 lawldkrtts gswrvshdfp nlpawivkav ggttthwaga slrfqdyefq tlthygkveg
      121 anlldwpitl aelepyyvka edkmgvtrtn gieglpgnnn fkvlkagadk lgykechtgr
      181 mainsaprdd rmgcqqtgfc fqgckwgakw stlyteipkg eetgrlevrp ectalkiehn
      241 aagkvtgvly adkdgkqhfq karvvcvagn siesprllln sasskfpdgl anssgqvgrn
      301 ymrhttgsvy asfekpvhmy rgttmagiir deaahnpkrg fvggyemeti slglpfmaaf
      361 lnpggwgrgf tsalddyvnm aglwivgedm pqeknritls kdvkdehglp vpdvyyedhp
      421 ndiamrnhay aqgkalyeav gairtfptpp ypsthnlgtn rmsekpqdgv vnkhgqthdi
      481 knlfvsdgsq fttggaenpt ltivalairq adyiaeqmkk rai
//
LOCUS       WP_176073653             655 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Brucella intermedia].
ACCESSION   WP_176073653
VERSION     WP_176073653.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..655
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=70116
     Region          1..461
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          585..650
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(607,616..618,625)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            617
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mfskilianr geiacrvirt arklgiatva iysdadkdal hvemadeavr vgpaisaqsy
       61 lnveaiikaa rqtgaeaihp gygflsenag fvdaveaagl afigpsarai ramglkdaak
      121 almekagvpv vpgyhgdnqd gaflkseadr itypvlikar aggggkgmrr vdqpddfaaa
      181 ldsarreaea sfgdgavlve kymakprhie vqvfgdshgn avhlferdcs lqrrhqkvie
      241 eapapgmtpd mrtamgeaav kaalaigycg agtvefiadv seglrpdrff fmemntrlqv
      301 ehpvteaitg ldlvewqlrv asgealpkcq delsingwaf earlyaedpa rdflpatgkl
      361 alfaqpenar vdsgvrtgdt itpfydpmia kiiahgatrd ealnrldaal nktriaglvt
      421 nrqflsalcn leafrtgdvd tgligreaaa lftaeppsdi afalaalgal dllgapqegd
      481 pwvslrgfrl wgeasrsvll dhhgerrmvs ftarggghfg fafgeleira henglvrfav
      541 dgrmreasvs rirhdvtvqf egrdtifhhv qsigaeedas sesrilspmp grvalvsvve
      601 gasvakgdpl vtmeamkmel sltaprdgki asvtvvagdq vsegallvel eeqhg
//
LOCUS       WP_176073660             419 aa            linear   BCT 11-JAN-2025
DEFINITION  lytic murein transglycosylase [Brucella intermedia].
ACCESSION   WP_176073660
VERSION     WP_176073660.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR02283.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..419
                     /product="lytic murein transglycosylase"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0009253 - peptidoglycan catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=45842
     Region          14..345
                     /region_name="MltB"
                     /note="Membrane-bound lytic murein transglycosylase B
                     [Cell wall/membrane/envelope biogenesis]; COG2951"
                     /db_xref="CDD:442193"
     Region          363..418
                     /region_name="PG_binding_1"
                     /note="Putative peptidoglycan binding domain; pfam01471"
                     /db_xref="CDD:460223"
ORIGIN      
        1 maagnwkhsl kiglalvasl aispaiaaps kaqvenqyrs wlekdlwpea kaagvsravf
       61 dqaftgvsin wklpdlvipg ekpstpkeqk qaefgapgky fnartmsavt sggqarygqy
      121 asllkrieqk ygvpgpilla vwgresgfgt vkipynayev lgtkafmatr kdmfrkelia
      181 aleiasrgyi desamksswa galgqpqfmp tsylkhavdf dgdgkrdiwn svpdtlasia
      241 nylklhgwqk grdwgfevnv pqnvscsleg pdqgktiaew aklgitrvng kpfpanemkg
      301 egfllmpagr ygpafvvspn fyvlkdynms dlyalfighv gdriaygagd fsrawgdvgs
      361 myrsdigamq krmqalgydv gkpdglpgfk trrsiglwqa kngmastcfp qpellrqir
//
LOCUS       WP_176073666             553 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella intermedia].
ACCESSION   WP_176073666
VERSION     WP_176073666.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 553)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..553
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=60814
     Region          14..545
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msepmsgpmn dsenktllsv rdlsvafrqn geerisvdrv sfdiaegetv alvgesgsgk
       61 svsalsilkl lpypsashps geilfngrdl mkasepelrr vrgnditmif qepmtslnpl
      121 hsverqigei lkmhqgmgve aarartlell hevgirepek rlsafphqls ggqrqrvmia
      181 malankpkll iadepttald vtvqaqilkl laelkaaqgm smlfithdlg ivrkiadrvc
      241 vmskgkivet gptrdifenp qhpytrhlla aepkgeppaa dpaartvmeg kdirvwfpik
      301 kgflrktvdh vkavdgidvn lragqtlgvv gesgsgkttl glalsrmiss rgeinfdgrd
      361 iakfsfkdmr plrremqivf qdpfgslspr mtiadiiaeg llvhepklsa ddrdarviaa
      421 lnevnldpet rfryphefsg gqrqriaiar amvlnpkfvm ldeptsaldm svqaqvvdll
      481 ralqkkhdla ylfishdlkv vralandvlv mrngkaveyg aakdvfanpq teytktlmaa
      541 afhmeategg vrq
//
LOCUS       WP_176073684             344 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Brucella intermedia].
ACCESSION   WP_176073684
VERSION     WP_176073684.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10524380
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..344
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=38055
     Region          173..340
                     /region_name="MTS"
                     /note="Methyltransferase small domain; pfam05175"
                     /db_xref="CDD:428349"
     Site            order(207..213,232..233,256..258,276)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
ORIGIN      
        1 mitpaqqtlf lpfdqgildm paegqsflgc glsadrrled ewkhaltflq pwrpdwlale
       61 kegikavprl garldeerrf aggllllgkh rgrneawfae llarvepggw iavsgdkklg
      121 idsfrkwvgn iaeisdrmsk nhavvfwlrr padltddfia alkplaanid dmfqtepgmf
      181 shgvidkgsa llvphmekiv fgnvadlgag wgylaaqclk fadrikaidl yeadfealea
      241 argnlerlgp svpisfnwfd vtsekltgiy dtvvmnppfh egrvtdvslg qafiaaaasr
      301 lktggrllmv anrqlpyett lkglfknvtl leeangfkif dakk
//
LOCUS       WP_176073703             291 aa            linear   BCT 11-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Brucella intermedia].
ACCESSION   WP_176073703
VERSION     WP_176073703.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..291
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31697
     Region          8..284
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mtvvrttlfa dhvaelgegp gydplsgnvw wfdilgqkli eknwdsgeth vhalgmkasa
       61 lavidrdrql ivsehglfir erangrltlh hpleadnevt rsndarvhps gsfwigtmgk
      121 kaepdagsiw wyregqvkkl fsgititnsi cfspdgkiay fadtdrniiw rvdtdpetgl
      181 pvsdksvfhh rtqeggvdgs vvdaegtlwn acwggrslna yspqgrlirs vplpvgqpsc
      241 pafvgpdata livtsahegl ddearqsdph agkvllldlt vagrhdppvr l
//
LOCUS       WP_176073708             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Brucella intermedia].
ACCESSION   WP_176073708
VERSION     WP_176073708.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32699
     Region          18..65
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..291
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(104,108,147,161,164,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(105..106,110..111,113..114,117,121,123..129,191,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mnrsqlsqla vlaavaahgs frsaarelai apsavshava tledslgvrl larttrsvap
       61 teagrrller lapalaeidq algaaletkd rpagilrisa plvatqlmla prlgefarly
      121 pditldlrid naftdivaag fdagvrlgen leadmiavrl ggpqrgavvg spayfearpa
      181 pshprdlarh rclrqrfpgg rlyrwefekn gqiveigveg pliandngil leaalagagl
      241 vwlfedytrd flaegrlvrv lqdwcapfeg fhlyypsrrq mrpalrafid fyrhgtgtdr
//
LOCUS       WP_176073740             293 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Brucella intermedia].
ACCESSION   WP_176073740
VERSION     WP_176073740.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..293
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32500
     Region          36..292
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mnddpskkrl grglaalige idrpveerka hvpiernvpi efvtrnprnp rrmfsegele
       61 dlaqsikehg vvqpivvrpa pgqpdrfeli agerrwrasq ragvdtipvi vrdvddrval
      121 eiaiienvqr adlnaveeal gyqqlidnhd ytqndlaqvi gksrshvant lrllklpqpv
      181 qdfivdgals agharslitm enptamaeri vkdglsvrqv ealaqaearg eanarpakpg
      241 pvekdadtka lekllsdvtg mkveinhrdr ggevkiryss leqldeicrr lqs
//
LOCUS       WP_176073750             544 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Brucella intermedia].
ACCESSION   WP_176073750
VERSION     WP_176073750.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..544
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58914
     Region          1..528
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 meydyiivgg gpagcvlanr lsedasvevl lleaggsdwn plfhmpagfa kmtkgvaswg
       61 fetvpqkhlk nrvlrytqak vigggssina qiytrgnaad ydlwagedgc tgwdyrhvlp
      121 yfkraednqr fnddyhsygg plgvsmpsap lpicdayira gqelgipynp dfngreqagv
      181 gfyqltqrdr rrssaslayl apirdrknlt vrmnaqvani elektlvtgv tlmsgetlra
      241 grevivasga igspklllqs gigpadhlkk tgvavkhdlp gvgenmqdhl dlfviaectg
      301 dhtydgvakl hrtlgaglqy illrsgpvas slfetggfwy adpdarspdi qfhlglgsgi
      361 eagveklkna gvtlnsaylh prsrgtvrla ssdpaaapli dpnywsdphd rkmsleglki
      421 areimqqdal kpyvmaerlp gpkvvsdddl fdyacanakt dhhpvgtckm gtdamavvdl
      481 dlkvrglegl rvcdssimpr vpscntnapt imigekgadi irgldplppv vfswernark
      541 vigr
//
LOCUS       WP_176073759             838 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Brucella intermedia].
ACCESSION   WP_176073759
VERSION     WP_176073759.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 838)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 838)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   4  (residues 1 to 838)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   5  (residues 1 to 838)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   6  (residues 1 to 838)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15200922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..838
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=86560
     Region          7..74
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          132..197
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          240..834
                     /region_name="P-type_ATPase_Pb_Zn_Cd2-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     Escherichia coli ZntA which is selective for Pb(2+),
                     Zn(2+), and Cd(2+); cd07546"
                     /db_xref="CDD:319846"
     Site            order(491,493,796..797,818,822)
                     /site_type="other"
                     /note="putative HM ion binding site [ion binding]"
                     /db_xref="CDD:319846"
     Site            order(535..537,599,615..617,647,686..688,707,710,713,732,
                     735)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319846"
ORIGIN      
        1 msetlnqirf ridgmdcasc aakietavrr vrgikdvsvs vaggtmtvsh dgtgdldkia
       61 akvhslgyga epvasekapa kgehshdhsq hdhdhdhgac ggshdhhdhv hdhghehdqd
      121 ghseiaatpd slrfridgmd cascaakidt avrrlpgvtd vsvsvtngam nvnhdgtaks
      181 deiaakvtal gyrttladta paasggraap kasapakplp wwrskkgqmm lacgggliga
      241 yiaghlypai elwaftaaml iglvpiakra ymaaingtpf siemlmtiaa igamfigate
      301 eaaavvflfl vgellegvaa gkarasiqsl talvpktafl ekngttseva adslavgdvi
      361 svrpgdrmpa dgeiltgesa vdeapvtges tpvgkaegdt vfagtingdg vlrvrvtaaa
      421 qdntiarvvr lveeaqeaka pterfinrfs tyytpgvvvv aalvailppl laggdwnewi
      481 ykglaillig cpcalvistp aaiaaalssg arrgllmkgg avletigkit aacfdktgtl
      541 tegkpkvtdv lagdlpedev lrlaasldag sshplalaiv gaaeqrglkl apvtggrahg
      601 gkgvsgmvge kdlflgsrra addiaaipda lanriaacnd egktvsvlva ngriagaiam
      661 rdepradaia glqelkaani rtvmltgdnr rtaeaigrdl gievraellp edkqrivgel
      721 rkeglivaki gdgindapal aaadvgiamg ggtdvaleta daavlhgrvg dveemvdlsk
      781 rtmrnihqni aialglkavf lvttvlgitg lwpailadtg atvlvtinal rllrqpvr
//
LOCUS       WP_176073779             329 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-dependent glycerol-3-phosphate dehydrogenase [Brucella
            intermedia].
ACCESSION   WP_176073779
VERSION     WP_176073779.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..329
                     /product="NAD(P)H-dependent glycerol-3-phosphate
                     dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0047952 - glycerol-3-phosphate
                     dehydrogenase [NAD(P)+] activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0046167 - glycerol-3-phosphate
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=33475
     Region          7..326
                     /region_name="GpsA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0240"
                     /db_xref="CDD:440010"
ORIGIN      
        1 msgktskiai lgggawgtal aamasssghd twlyarddet veaidrtqrn prylgeialp
       61 vaikastdva avvdnadavl avipaqamrt glsqlsslip qtapvvlcak gieratgrlm
      121 sevvaevlpn hriaalsgps fatdvarglp tavtvaceda atadqlaall sgpafrcyst
      181 tdlkgveigg alknvlaiaa gaavgrgfga saqaalvtrg faelrrigqa mgakpetimg
      241 lsglgdlmlt csssqsrnys yglalgrged ltnrplaegv atapiaaelc rkhaisapii
      301 datgalldgt itideavtal lnrplkted
//
LOCUS       WP_176073919             659 aa            linear   BCT 11-JAN-2025
DEFINITION  iron ABC transporter permease [Brucella intermedia].
ACCESSION   WP_176073919
VERSION     WP_176073919.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 659)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 659)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
REFERENCE   5  (residues 1 to 659)
  AUTHORS   Koster,W.
  TITLE     Cytoplasmic membrane iron permease systems in the bacterial cell
            envelope
  JOURNAL   Front Biosci 10, 462-477 (2005)
   PUBMED   15574383
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11484808
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..659
                     /product="iron ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006826 - iron ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=67258
     Region          36..659
                     /region_name="PRK10577"
                     /note="Fe(3+)-hydroxamate ABC transporter permease FhuB"
                     /db_xref="CDD:236720"
     Site            order(418..420,538..539,541..543,545..546,548..553,
                     555..557,598,605)
                     /site_type="active"
                     /note="ABC-ATPase subunit interface [active]"
                     /db_xref="CDD:119348"
     Site            order(419,421,426,478,480..481,484..485,488..489,492,
                     495..496,498,509..510,513,588,640,643..644,647,650..651,
                     654)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:119348"
     Site            order(498,523,580,584,628,637)
                     /site_type="active"
                     /note="putative PBP binding regions [active]"
                     /db_xref="CDD:119348"
ORIGIN      
        1 mrsrdavaea tkprthmfgl fllasvlllg liiaellvgg gnvtlsdvlq apsrpqslaq
       61 iiietirlpr alaavlvgaa laaagvimqt vlrnplaapd ilavtsgaql aliiaslllp
      121 fafpgflati lggaiggglc llvggglraq pvrlalagva islafsalss aivlmaddra
      181 sgillwssgl leqsgwtrva slapailagi lllallgrqf dvmalgndma sglglgkapa
      241 iigllatvvl sgaavsiagp igfiglavpn flraigfhkh glllpaaall gavallaadv
      301 aaqllsshgt iipagvfaac faapvlilvl rrlkgetrtr anvvsqkvlf qrktalypvl
      361 vglmvaafll glifgdgvag wqtdwntvya lrmprvliam gagallacag lllqlvtrnp
      421 lsgpetlgls qgaalaglag lligvvpgsp lfallallga glvvlcisll sirmsperta
      481 ltgiavaasl aavstiivie aklqvaeals wlagsthgrn wedvtalapw lvviplmmil
      541 arrfdilamg rdeaesigln tmsariwtml laslavagav atvgaigfvg liaphaarlc
      601 sgaryrqlvp vtaligailt afadmfgrtl iapqeipagi vtafigaplf illmrrqsr
//
LOCUS       WP_176073939             309 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Brucella intermedia].
ACCESSION   WP_176073939
VERSION     WP_176073939.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..309
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31546
     Region          3..305
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mailliaehd natlsdqtak altaaaqigg dvdvlvagkg akpaadaaak lsgvrkvlla
       61 esdalenrla eptaalivel aanydtiiap attsaknilp rvaalldvmq lseimevvsa
      121 dtfkrpiyag naiqtvqstd akkvitvrta sfsatgeggs aavesvnaaa dpalssfvgn
      181 alsesdrpel tsakiiisgg ralgsaekfq evilpvadkl gaavgasraa vdagyapndw
      241 qvgqtgkvva pdlyiavgis gaiqhlagmk dsrvivaink deeapifqva dyglvgdlft
      301 vlpelqktf
//
LOCUS       WP_176073963             277 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella intermedia].
ACCESSION   WP_176073963
VERSION     WP_176073963.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 277)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467922
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..277
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31395
     Region          51..277
                     /region_name="ArtM"
                     /note="ABC-type arginine/histidine transport system,
                     permease component [Amino acid transport and metabolism];
                     COG4160"
                     /db_xref="CDD:443325"
ORIGIN      
        1 msqtvsnttv pvmapppvvk qwtrmrvagh vivalwfllf aglaiylyna wrvdlfetyg
       61 prywsgllit lklvavsiii gallslpita armsnnrwlr glafgyvyff rgtpllaqtf
      121 liyygfgtfr pflesiglwv ffrdawncai lafslntaay qaeilrgaiq svalgqwegs
      181 aalgiskrvt fwkvilpqal ivalrpygne iilmikgsai vaiitvldlm getrraysrt
      241 fdfqtylwaa viylvivecl rhvwdflerr ltrhlvr
//
LOCUS       WP_176073964             240 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Brucella intermedia].
ACCESSION   WP_176073964
VERSION     WP_176073964.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467993
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..240
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25818
     Region          4..239
                     /region_name="ArtQ"
                     /note="ABC-type arginine transport system, permease
                     component [Amino acid transport and metabolism]; COG4215"
                     /db_xref="CDD:443361"
ORIGIN      
        1 mehyatllsf gpdgwgasia wgllvtvsla latlpvglvl gflvavgkqs sepsirlaan
       61 iyttifrglp elltlflvyf gaslglqrll slfgveanve inafgagmva lgfvfssyss
      121 evflsafrai prgqyeggya vglshwqtmr kvilpqliri alpglanlwl vllkdtslvs
      181 vitlsdilrq tsiaarvtke pflffgiacl lylvlaiiss yfidriarwa daganrsrga
//
LOCUS       WP_176074110             315 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Brucella intermedia].
ACCESSION   WP_176074110
VERSION     WP_176074110.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..315
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=34498
     Region          30..306
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mmlawgqkrk aanndlalpa eesaekpeik rdprrialal gggaargwah igvlraldea
       61 nidiemiagt sigalvggcy lagkldelea farsltrrrm fnllditfrg sglfggmkld
      121 grlrehldgl rieeldrpfv aictelrtgh eiwlssgplv eamrasyalp gvfepvrwqe
      181 rvlvdgalvn pvpvsvcray eqrlvlavnl hydqygraav ikhaqtrqds ltdaihgeke
      241 arlgitgvmm eafniiqdri srarmagdpp dvtlmpivgq igladfhras eaidagytet
      301 lkrledikrl qgiag
//
LOCUS       WP_176074104             330 aa            linear   BCT 11-JAN-2025
DEFINITION  elongation factor Tu, partial [Brucella intermedia].
ACCESSION   WP_176074104
VERSION     WP_176074104.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     gene            <1..330
                     /gene="tuf"
     Protein         <1..330
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
     Region          1..330
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 hveyetanrh yahvdcpgha dyvknmitga aqmdgailvv saadgpmpqt rehillarqv
       61 gvpaivvfln kcdqvddael lelvelevre llskyefpgd eipiikgsal aaledsskel
      121 gedavrslma avddyiptpe rpidqpflmp iedvfsisgr gtvvtgrver givkvgeeve
      181 ivgikatakt tvtgvemfrk lldqgqagdn igalirgvgr edvergqvlc kpgsvkphtk
      241 fkaeayiltk deggrhtpff tnyrpqfyfr ttdvtgvvtl pagtemvmpg dnvamdvqli
      301 vpiameeklr faireggrtv gagivssiie
//
LOCUS       WP_176074114             263 aa            linear   BCT 11-JAN-2025
DEFINITION  TatD family hydrolase [Brucella intermedia].
ACCESSION   WP_176074114
VERSION     WP_176074114.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..263
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=29145
     Region          2..255
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mlvdshchld fadfeperda vvqraldagi krmvtistrv rkfdtiraia eayesvycsv
       61 gthpnnahee lditaddlvr laehpkvvai geagldyhyd yappaaqrqg flvhieaarr
      121 tqlplvihar sadddmaeil eqetekgafp filhcfssgr alaekgielg gyisfsgilt
      181 fknspeirei asivprnrll vetdapflap lphrgkrnep sfvqhtaaml aetigvsnde
      241 varitsdnvf rlfskmprps een
//
LOCUS       WP_176074189             435 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Brucella intermedia].
ACCESSION   WP_176074189
VERSION     WP_176074189.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024287
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..435
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47377
     Region          21..427
                     /region_name="MFS_KgtP"
                     /note="Alpha-ketoglutarate permease of the Major
                     Facilitator Superfamily of transporters; cd17367"
                     /db_xref="CDD:340925"
     Site            order(31..32,35..36,39,77,135..136,138..140,143,163,
                     166..167,170,252,255..256,259..261,264,292,296,349..350,
                     354,358,374,377..378,381..382,385)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340925"
ORIGIN      
        1 mvtitnerse vqstnsrlks iiggstgnlv ewfdwyvyaa falyfaphff psdnqtaqlm
       61 saaavfavgf vmrpigawim giyadrkgrk aglalsvtlm cagsliialt pdyqtiglaa
      121 pallvlarlm qglsvggeyg asatylsema gkdrrgffss fqyvtlisgq llailllivl
      181 qstmetpale swgwripffi gallavvvfw lrrglaetes fkiaktkdap ksgfwtlikh
      241 hpketalvml ltaggtlafy aysiymqkfl vntsgfsrev asqinavtlf vfmclqpiag
      301 alsdkigrkp lmiafgaagv lftypifttl eqtrdpitag vlvmgaliiv tgytsinavv
      361 kaelfpahir algvalpyal antlfggtae yvalsfkngg wergfywyvt imigislivy
      421 lrmrdtskds miked
//
LOCUS       WP_176074248             301 aa            linear   BCT 11-JAN-2025
DEFINITION  peptidylprolyl isomerase [Brucella intermedia].
ACCESSION   WP_176074248
VERSION     WP_176074248.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Galat,A.
  TITLE     Peptidylprolyl cis/trans isomerases (immunophilins): biological
            diversity--targets--functions
  JOURNAL   Curr Top Med Chem 3 (12), 1315-1347 (2003)
   PUBMED   12871165
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433571
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..301
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=32544
     Region          140..288
                     /region_name="SurA"
                     /note="Peptidyl-prolyl isomerase, parvulin family
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0760"
                     /db_xref="CDD:440523"
ORIGIN      
        1 mvtlfdrkqp aagqhnhptg yttyqepdtr vppkprpvfd vvsvngvain etdilteaqn
       61 hpsdnpgaal laaaralavr elllqrarea givperekda egrsetdeda lvrmvierev
      121 evpsatreea lrfyennrhr ftsapileas hiliaadpad sqarekarat aarlasavia
      181 epatfasvah eysscpsgaq ggnlgqltrg stvpefekal ermaageita npiesrfgfh
      241 ivrldrrieg eelpfdyvad riagwleast wskavsqyia ilaadaditg idllsnegae
      301 a
//
LOCUS       WP_176074299             241 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Brucella
            intermedia].
ACCESSION   WP_176074299
VERSION     WP_176074299.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..241
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26428
     Region          3..239
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mvmialnqvk ksfgavpvlk gvsfsvekgq vaaligasgs gkstalrcvd rlevidsgei
       61 ivadhkvhdp kldlhklrld vgivfqsynl fphltieenv mlaprsvkki pkdearemar
      121 aalervglde kanhypeqls ggqqqrgaia rslamepkvm lfdevtsald pkltgevlrv
      181 ieklaesgmt mimvthemnf arkvadrvif mhrglvheeg dasilnapmt lelqdflshd
      241 l
//
LOCUS       WP_176074331             319 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Brucella intermedia].
ACCESSION   WP_176074331
VERSION     WP_176074331.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10549394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..319
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=35985
     Region          134..209
                     /region_name="Methyltransf_11"
                     /note="Methyltransferase domain; pfam08241"
                     /db_xref="CDD:462406"
ORIGIN      
        1 mtenffgipt tddalfenfs eagyleanpd vavavrekri esgrwhfdai ghtegrklir
       61 qdkiaaskqa kiakisgfia wdyappllpt gainclpdyl aemagvehtd aisqhdytpd
      121 vkeliennpg klfldagagf rpiyypnvvn leivpysttd vlgvlekipf rdgtfdyvvs
      181 navlehvrdp ftsakeitrv lkrggkmfiq vpflqpyhgy phhyynmtks glanlfkddi
      241 sidshtvpfy fhpvwvaswf fnswanglsa qtrhqleslt vkelmnfrvq dmrlpfvael
      301 denkqfelas gtyligtkn
//
LOCUS       WP_176074400             605 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC-F family ATP-binding cassette domain-containing protein
            [Brucella intermedia].
ACCESSION   WP_176074400
VERSION     WP_176074400.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   2  (residues 1 to 605)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422934
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..605
                     /product="ABC-F family ATP-binding cassette
                     domain-containing protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=67610
     Region          8..493
                     /region_name="Uup"
                     /note="ATPase components of ABC transporters with
                     duplicated ATPase domains [General function prediction
                     only]; COG0488"
                     /db_xref="CDD:440254"
     Region          529..>585
                     /region_name="ABC_tran_CTD"
                     /note="ABC transporter C-terminal domain; pfam16326"
                     /db_xref="CDD:465095"
ORIGIN      
        1 mappllrldq ikltfggtpl ledaslsvse gdrialvgrn gsgkstllki aagmveatsg
       61 evfkhpgatv rylpqvpdmd gfanvrayve aglgptddph rvtyllehlg ltgeekpdhl
      121 sggearraal arviapqpdv llldeptnhl dlttiewleg elrqirsaiv lishdrrfle
      181 nvsratvwld rgitrrleqg fghfeewrdk vleeeerdhh klgrqiaree hwlrygvtar
      241 rkrnmrrlge lhsmradfrn hrkaqgtavl aasdakesgk lvieakglsk aygervlvkd
      301 fsirvqrgdr iglvgpngag kttllslltg klepdsgtlr lgvnlemvel dqkreslnld
      361 etlahyltdg rgeslvvnge qrhvvsymkd flfqpeqart pirelsgger arlmlarvla
      421 rpanllvlde ptndldmetl dllqelvagf pgtvilvshd rdfldrtvts viapegdgrw
      481 leyaggyadm maqrkeqaln rrsvkasggr tdekpeedap qpkreekrkl sykqkfaler
      541 lpgkmdalak eiavlegkla dpqlyakdpt lfaktadlle kkrsenaame eewlelemlr
      601 eeieg
//
LOCUS       WP_176074490             118 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Brucella intermedia].
ACCESSION   WP_176074490
VERSION     WP_176074490.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..118
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12976
     Region          7..116
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 msllitidpn pdfapkealp tedrlisgtp sfktwaqdas kndkvltgvw eatpgethsi
       61 kgttlefchi lsglvqieek ggetktyrag dsfvmkpgfv gvwrtietvr kiylcvye
//
LOCUS       WP_176074569             152 aa            linear   BCT 11-JAN-2025
DEFINITION  ester cyclase [Brucella intermedia].
ACCESSION   WP_176074569
VERSION     WP_176074569.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Sultana,A., Kallio,P., Jansson,A., Wang,J.S., Niemi,J., Mantsala,P.
            and Schneider,G.
  TITLE     Structure of the polyketide cyclase SnoaL reveals a novel mechanism
            for enzymatic aldol condensation
  JOURNAL   EMBO J 23 (9), 1911-1921 (2004)
   PUBMED   15071504
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Stewart,M.
  TITLE     Insights into the molecular mechanism of nuclear trafficking using
            nuclear transport factor 2 (NTF2)
  JOURNAL   Cell Struct Funct 25 (4), 217-225 (2000)
   PUBMED   11129791
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..152
                     /product="ester cyclase"
                     /EC_number="5.5.1.-"
                     /GO_process="GO:0030638 - polyketide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=16607
     Region          19..146
                     /region_name="COG5485"
                     /note="Predicted ester cyclase [General function
                     prediction only]"
                     /db_xref="CDD:444236"
ORIGIN      
        1 mlseqgttvs gltaeertav etfysafegq pdllneaite dwqdiplapg qqsgregmkp
       61 lirgfkiafp dtkvklheii gvggrvavra tvsgthlgdw fgvsatgkpf eisihefhhi
      121 sngklthtwh ledwlgwlfq vgawpagkqe tv
//
LOCUS       WP_176074595             251 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Brucella intermedia].
ACCESSION   WP_176074595
VERSION     WP_176074595.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..251
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26529
     Region          4..248
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mstlvrlekl svsygsepal edidldigqg etlaiigesg sgkstlalal asllpgnahi
       61 sgqldwadgk pragrdigfv fqdpassfdp lmtvgaqlve tirahakidr laakaratgl
      121 lqrvhipqad asfaryphqf sggqkqriai alaiaasprl liadeptsal dtivqkeivs
      181 llrelvrtdg mtlifithdi alasgladri avfrqgklve fgparnivsn pqtdytrali
      241 aavpvleaah g
//
LOCUS       WP_176074604             227 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Brucella intermedia].
ACCESSION   WP_176074604
VERSION     WP_176074604.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..227
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=25113
     Region          35..221
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mtktpasgds pprpvitafe nspdrgrgma rdmpvrwale etgrdydvrl vsfeamkarp
       61 hldlqpfgqi ptyeegdlal fesgaivlhi aeqnpgllpd dangrarait wmfaahntie
      121 pviveremag fverqeswye qrmpiveari rkrldalsac lgdndwlaga fsagdllmvs
      181 vlrrlkssgi lndypnlaay vargearpaf kraydaqhav flaaskd
//
LOCUS       WP_176074662             581 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Brucella intermedia].
ACCESSION   WP_176074662
VERSION     WP_176074662.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Jankowsky,E. and Putnam,A.
  TITLE     Duplex unwinding with DEAD-box proteins
  JOURNAL   Methods Mol Biol 587, 245-264 (2010)
   PUBMED   20225155
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437332
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..581
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63014
     Region          1..>358
                     /region_name="SSL2"
                     /note="Superfamily II DNA or RNA helicase [Transcription,
                     Replication, recombination, and repair]; COG1061"
                     /db_xref="CDD:440681"
ORIGIN      
        1 mlhlrdyqra avdglydywr eqpgsplivl ptgggkslvl gtickelieg wpdmrvlvct
       61 hvrelilsny qellniwpfa pagifsagvg rrdakaqivf ggvqtianka elighidvvl
      121 vdeahlmprn setqygklie glrainpdlk lvgltatpyr lgeglltegd galfdgicfe
      181 kpigdmieeg ylcrpiskgm atafdlsgvg kqggdykqna lqaaidkddi tasvvdeivt
      241 ygtasgaerk awlcfcsgve harhmrdeir srgfscetvt gdtptgerdr iladfkagki
      301 raltnnsvlt tgtnlpiidl vafcrptlsa glyvqmagrg lrlypgkenc lfldfagvvr
      361 khgpidavtp pgmkkgdgea pvkqcpqepd drglvgcgsl ihaslhtcpd cgyefpvdet
      421 pkisaqaedv pmlskdnast rqverrtfay hegkggkqds vkvsywvgms pinewlgpah
      481 tgffksksdr wwrkhggqap fpktvlefme rqnellptge ivvkpngkyw evldavpgea
      541 ggqdavandn vpvagndnip adtygrvsag laevldddip f
//
LOCUS       WP_176074694             120 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Brucella intermedia].
ACCESSION   WP_176074694
VERSION     WP_176074694.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10611814
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..120
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=12508
     Region          15..98
                     /region_name="DoxX_2"
                     /note="DoxX-like family; pfam13564"
                     /db_xref="CDD:433313"
ORIGIN      
        1 mnkslptist slawllaaff lfgaygntfi seenaaayva wgypgwfhyi tailelaagl
       61 lliraatrpy gaglgalvma aaslttlvna dydhavapsi vllvslvvlg lslavrraah
//
LOCUS       WP_176074698             111 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF736 domain-containing protein [Brucella intermedia].
ACCESSION   WP_176074698
VERSION     WP_176074698.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009347
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..111
                     /product="DUF736 domain-containing protein"
                     /calculated_mol_wt=12500
     Region          1..106
                     /region_name="COG5489"
                     /note="Uncharacterized conserved protein, DUF736 family
                     [Function unknown]"
                     /db_xref="CDD:444240"
ORIGIN      
        1 maeigtftrt etgyagelhs fglherlfiv pakpndlkna pdyrvrlyse dgpdagpawk
       61 dssenagefl svrlegpifp fpiraklfqs ngdpsiwtlr wkhprkiede e
//
LOCUS       WP_176074750             342 aa            linear   BCT 11-JAN-2025
DEFINITION  LLM class flavin-dependent oxidoreductase [Brucella intermedia].
ACCESSION   WP_176074750
VERSION     WP_176074750.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..342
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=37297
     Region          37..328
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 mplshiehfa flipgshhen dpargledtl qlfehgeglg ydsawvrqrh lergissaat
       61 flaaasqrtk higlgtaviq lgyenpfrla edlatvdlls tgrlnvgvsv gappfahlia
      121 dfvdtapvad yshtraekla qalrseplsg eteagnaaga qiprlrpfae gltdrlwygg
      181 gsqnsahwag qagfnlltgn ivsgentddf ltaqkalier frqewrhera prvalgrvil
      241 ptdsaspdar rryaefaser dkrtgfahgp rrtlflpdiv gtteqilerl aadpvlplvs
      301 efrlelpyef haedyaqilt dfarilpasg askpelsvvr ag
//
LOCUS       WP_176074765             271 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Brucella intermedia].
ACCESSION   WP_176074765
VERSION     WP_176074765.1
KEYWORDS    RefSeq.
SOURCE      Brucella intermedia (Ochrobactrum intermedium)
  ORGANISM  Brucella intermedia
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group;
            Brucella.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Brucella intermedia"
                     /db_xref="taxon:94625"
     Protein         1..271
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=28666
     Region          11..268
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mtktasdees sqklvpavmr aaqildqvak saqeggkgsa dglklsdlar rtglpkssvh
       61 glcqtlvhlk llklngdgsf tmgsqsvrwa nvfmagsdiv dafheavaea eglgahtltl
      121 shlegpeviy lscrnstapl gitfrigmrv pavftatgka mlaamspqel arhlpsewpe
      181 litpasapsl kvleaemaev kargysldng qlregmfcig aaicdrpfhp tagialsmma
      241 aearpdiied mgkrvralan dvadrmgwls a
//
LOCUS       WP_176074866             302 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Clostridioides
            difficile].
ACCESSION   WP_176074866
VERSION     WP_176074866.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..302
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35610
     Region          6..>80
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mkegnkvtek qrliitiaqk ifdqkgfqnt sisdivkeck mskatfykhf etkesficei
       61 inyydekfle iihsinennd ipsseklnrk iiavwenifs rttintyire nfsevqrktt
      121 sklqtksran llneyklslf dnygdkieni ifdlvfllda lihqfiyiih vqkrelnvyf
      181 vakftiqild lvvenmdnln plieksmflh kqedeayfsl ynkslffkti qdieeliktd
      241 tsllenskll eatkklyveg knqqydslim dsmiayleke dtlrpkvlll nsiknqlkke
      301 tl
//
LOCUS       WP_176074930             307 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176074930
VERSION     WP_176074930.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..307
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33565
     Region          34..186
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <174..293
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mdmtdivasr esgrrelasl isrfapadgs hatavpalml hrhtrpvdlg cavsraalvi
       61 aaqgakrviv agnayeygah nclitsidlp ilsrvtqasp depylclslt ldlqrivela
      121 aemrlpepda gpegegialt eltpplldaa lrllrlldtp adipviapli ekevlyrlmt
      181 sgqgsrlrhm avagsqthri araiewirnh yaepmrvetl aqavnmsvss lhhhfkhvtt
      241 lsplqyqkql rlhearrlll qqggdvgsva atvgyespsq fsreysrlfg appmrdvvhl
      301 rkkellg
//
LOCUS       WP_176074940             323 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176074940
VERSION     WP_176074940.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 323)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401161
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..323
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36004
     Region          15..97
                     /region_name="cupin_MtlR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to MtlR, N-terminal cupin domain; cd06976"
                     /db_xref="CDD:380381"
     Region          59..283
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mmhpdlevvd vrrdesfkvw shgypyrtir whfhpefelh livatrgkyf vgdhigsfgp
       61 ghlvllgpnl phnwvsdmad getverrnlv iqfdqtfvrr cidafpecrd aqallddarr
      121 gvgfddatsa aiaplfdell gargmrrial fmtilerlcg arertllasp aydhahvtpt
      181 rlshalsyig knlasdlres dlaqltgqsv safsrafhrh tgmpfvqyvn rlriesacqm
      241 lladdasitd icfqagfnnv snfnrqfrav kgmapsefra lqrlnarsre lalhaaptgn
      301 pmpprvvaag tharahalal qpg
//
LOCUS       WP_176074945             515 aa            linear   BCT 11-JAN-2025
DEFINITION  FGGY-family carbohydrate kinase [Burkholderia dolosa].
ACCESSION   WP_176074945
VERSION     WP_176074945.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..515
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=55230
     Region          3..448
                     /region_name="ASKHA_NBD_FGGY_RrXK-like"
                     /note="nucleotide-binding domain (NBD) of Rhodospirillum
                     rubrum xylulose kinase (RrXK) and similar proteins;
                     cd07804"
                     /db_xref="CDD:466806"
ORIGIN      
        1 meyvigvdig tqstkallvd rhgtivarrs agyqpdtprp lwaeqwpqvw fdavlecvgg
       61 cvadardagv padairavcv sslyggsgip vdsdmrplhp cliwmdrrat aqvdwvnahv
      121 nvarlrtitg ngvdsyygft kmlwlrdrrp dvwanvryfl ppnayviyll tgevavdhss
      181 agniggvydv arrewsddal dmlgipatmm perlvdstdv vggllsqwte rlglpagtpi
      241 vaggvdaava tfaagatrtg qhvamigtsm cwgyvtqhvd arhglvsmph vfdgqrdlyv
      301 fggaitagas vawfrdqfch aeidaaralp hgdphvllee aaarvpagad gvlflpylmg
      361 erspvwdaka sgafvglsva htrahlyrav legvafalrh nidagrrgaa alddrlivvg
      421 gaahsalwmq ivadvtgfpv wtieqdveaa mgaallagvg aklvsradaq rgwvslvera
      481 rpdparaaay aarfelytal ypalkpimhg lhsrs
//
LOCUS       WP_176075010             184 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Burkholderia
            dolosa].
ACCESSION   WP_176075010
VERSION     WP_176075010.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..184
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20865
     Region          1..>147
                     /region_name="HugZ"
                     /note="Putative heme iron utilization protein, contains
                     PNPOx domain [Inorganic ion transport and metabolism];
                     COG0748"
                     /db_xref="CDD:440511"
ORIGIN      
        1 msdtenafrr aafllgsarf mtlatvspag epwastvnyv pmedasirvv wysmrdarhs
       61 rniesnarat asifrtdlth esplgldglq legtcraipa delavfhehy yarnfvddva
      121 rhewmlpldd frgdgkrrfy eltverlwll didrwlidkh dqrvavpsla svadalrrtg
      181 gqvk
//
LOCUS       WP_176075035             466 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia dolosa].
ACCESSION   WP_176075035
VERSION     WP_176075035.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..466
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49456
     Region          42..449
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(51..52,55..56,59,91,141..142,144..146,149,169,
                     172..173,176,284,287..288,291..293,296,324,328,379..380,
                     384,388,404,407..408,411..412,415)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mstfdnvvag ratieaaast pgaiiarler lpansmqira rvligtatff dgfdvitiaa
       61 tlpllihkwg lsptqigmli asgaigqlig aflfpalaek hgrvkaiaws savigitsla
      121 cgfaptfevf vllrilqglg lggelpvaat yineitrahg rgrfvllyei vfpigllvsm
      181 algawlvprf gweimyfvgg lplilalvlt hlvpesprwl asrgrladaa haigafessv
      241 rgalppvtqt aafdemvrqh pkrrmvdlfs aayrkrtlav atlwatcgfi qyglstwlpt
      301 iyknfyhapl qlalnlavig svmgvlgsla sallvdrlgr kpvivwsfvl calslalagi
      361 yhassvyvva lfcslslglm asgfitayvy tpeqyptsir asgcglgsaw lkiasfvapm
      421 vvphaivggd lspafyllga vpliaavtvh fvgietkgkv lealea
//
LOCUS       WP_176075036             428 aa            linear   BCT 11-JAN-2025
DEFINITION  NRAMP family divalent metal transporter [Burkholderia dolosa].
ACCESSION   WP_176075036
VERSION     WP_176075036.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Ehrnstorfer,I.A., Geertsma,E.R., Pardon,E., Steyaert,J. and
            Dutzler,R.
  TITLE     Crystal structure of a SLC11 (NRAMP) transporter reveals the basis
            for transition-metal ion transport
  JOURNAL   Nat Struct Mol Biol 21 (11), 990-996 (2014)
   PUBMED   25326704
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Shin,J.H., Wakeman,C.A., Goodson,J.R., Rodionov,D.A.,
            Freedman,B.G., Senger,R.S. and Winkler,W.C.
  TITLE     Transport of magnesium by a bacterial Nramp-related gene
  JOURNAL   PLoS Genet 10 (6), e1004429 (2014)
   PUBMED   24968120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Cellier,M., Belouchi,A. and Gros,P.
  TITLE     Resistance to intracellular infections: comparative genomic
            analysis of Nramp
  JOURNAL   Trends Genet 12 (6), 201-204 (1996)
   PUBMED   8928221
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Cellier,M., Prive,G., Belouchi,A., Kwan,T., Rodrigues,V., Chia,W.
            and Gros,P.
  TITLE     Nramp defines a family of membrane proteins
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10089-10093 (1995)
   PUBMED   7479731
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..428
                     /product="NRAMP family divalent metal transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0046873 - metal ion transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0030001 - metal ion transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45751
     Region          10..412
                     /region_name="MntH"
                     /note="Mn2+ or Fe2+ transporter, NRAMP family [Inorganic
                     ion transport and metabolism]; COG1914"
                     /db_xref="CDD:441518"
ORIGIN      
        1 mndnellept ghkptattwl rrlgpglvtg aadddpsgig tysqagaqfg fqllwvlllt
       61 yplmtaiqlv sarigrvtgk glasnmrkhy prwllyatvv lllaanvini aadlsamgaa
      121 vnlllpgpqq lyvvclggvs aalqifvpye ryanllkwta lvllayvava lilpipwaev
      181 gravvrphia ltsaylttit avlgttispy lffwqasqev eelraepadq plrrvprqap
      241 aqlrrisfdt wvgmgvsnai gffivltaaa tlhlhhidvk tsadaarale plaghfayvl
      301 falgivgtgl lalpvlagsa ayaaagtfrw rnslalqpsv arefyaviaf aivggvaitf
      361 mhfdpiraly wsavingvta apimivmmlm arnrrimgef tikgplawgg wlatlamvaa
      421 aagvfvpg
//
LOCUS       WP_176075064             302 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia dolosa].
ACCESSION   WP_176075064
VERSION     WP_176075064.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..302
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32378
     Region          12..300
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mqmnsavapl ceidglkigf rghdgvvtda vrdlsltlap gerlgivges gsgksltgra
       61 llgllpdaar csartmrfag hdllamspre rrrlcgsqmg milqdpkysl npvmtvakqm
      121 geafrrhepg lggralreri vdalaavqir dparvadayp helsggmgqr vmiammvstg
      181 prlliadept saldvavsmq vlavldtmia rhgtglmfis hdlplvmsfc drvavmyagr
      241 vvetcaardl rdathpytrg llaanpplan ppdelpvlqr dpawldaapp fsmpadrqep
      301 sr
//
LOCUS       WP_176075084             139 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Burkholderia dolosa].
ACCESSION   WP_176075084
VERSION     WP_176075084.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..139
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14762
     Region          27..138
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 mtpnqpflas qrdvllllsr illvilfvmf gwkkivdfsg tiafmgsega papivsaaia
       61 vvmelfagia ilvgfqtrpl alllalytig talighhywt mtggeqinnm ihfykniais
      121 ggllalcaag pgrfsvdrg
//
LOCUS       WP_176075089             322 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176075089
VERSION     WP_176075089.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..322
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35537
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,220,
                     222..225,232..233,236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdmlenmrlf vrvveagsft avakeidatt aqvsravsnl eahvqtrllh rttrhlglte
       61 sgeryferak silaeidyan aearnallrp sgkmrihamt glgqshvvss ivryqednpd
      121 vsieltlaqr mpnlveegyd vsivtasqlp dsgyvaqtcg tscsvlvasr eylarhgtpq
      181 tpgdlpnhvc lrldtpaspa gewrlersdg eetvyelqpa pfqvnvpdal cvavragrgi
      241 acvalytvld dlregrlirv lpeyrlqtvs vyavyatrry ldakirtfld hlrttltpal
      301 endlreldrl aaaqpaasrk ha
//
LOCUS       WP_176075125             153 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176075125
VERSION     WP_176075125.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..153
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16397
     Region          1..132
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mdepdwkila llqangrisy telarqvhls vpavtervkr leaagviegy tarvnpaaag
       61 ypvtaligit vpqpakakfl afldtipevv echhvtgads yvmrfvavgm ahleqligri
      121 nlygetrtsi vmstplaprg larppskteg prg
//
LOCUS       WP_176075126             217 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia dolosa].
ACCESSION   WP_176075126
VERSION     WP_176075126.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..217
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21732
     Region          2..210
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mlfiksvvmg lsiavpvgpi gmlciqrsls rgfragfatg lgaacadaly gllgalgvag
       61 vvaafpmlai gmkiaggafl awlawciarq ppavstsqre tprttvgrdf vttfgltlsn
      121 pmtilsfvgi faalgpasvv agaggrggam gatvalmvag vfvgsaiwwl clsgataalr
      181 tkmsnalmng lsrvsaivia afgavqlvag vrdlvwa
//
LOCUS       WP_176075132             480 aa            linear   BCT 11-JAN-2025
DEFINITION  sialidase family protein [Burkholderia dolosa].
ACCESSION   WP_176075132
VERSION     WP_176075132.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Taylor,G.
  TITLE     Sialidases: structures, biological significance and therapeutic
            potential
  JOURNAL   Curr Opin Struct Biol 6 (6), 830-837 (1996)
   PUBMED   8994884
REFERENCE   5  (residues 1 to 480)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 480)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
REFERENCE   7  (residues 1 to 480)
  AUTHORS   Roggentin,P., Schauer,R., Hoyer,L.L. and Vimr,E.R.
  TITLE     The sialidase superfamily and its spread by horizontal gene
            transfer
  JOURNAL   Mol Microbiol 9 (5), 915-921 (1993)
   PUBMED   7934919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10202570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..480
                     /product="sialidase family protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004308 - exo-alpha-sialidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=51170
     Region          143..427
                     /region_name="Sialidase_non-viral"
                     /note="Non-viral sialidases; cd15482"
                     /db_xref="CDD:271234"
     Region          176..237
                     /region_name="Sialidase propeller 2"
                     /note="Sialidase propeller 2 [structural motif]"
                     /db_xref="CDD:271234"
     Region          242..295
                     /region_name="Sialidase propeller 3"
                     /note="Sialidase propeller 3 [structural motif]"
                     /db_xref="CDD:271234"
     Region          310..363
                     /region_name="Sialidase propeller 4"
                     /note="Sialidase propeller 4 [structural motif]"
                     /db_xref="CDD:271234"
     Region          374..427
                     /region_name="Sialidase propeller 5"
                     /note="Sialidase propeller 5 [structural motif]"
                     /db_xref="CDD:271234"
ORIGIN      
        1 mrriimshsl virlsaamam taaaahaepv lvsgpspfaa ctiggpgtny vnaevepwla
       61 vnpanpnnmi gvwqqdrwsn ggahglvagy tfdagatwar tpqpfsacap gglkyerasd
      121 pwvsfgpdgt aysvsisfnq snnsnavaas vstdggqtws spsvliande pttqffndke
      181 svtanpvkag tayavwdrle lpngnpyanl htqafrgptf fsktvdggkt wstpkvivnv
      241 asrqqtignq ivvdpktgtl ydffdliqpp fskaagkvay vkstddgatw tkpqviaglq
      301 tvgvtdpntg epvrtgdiip epaidpasgq lyvvwqdsrf nggnydeial stskdggasw
      361 saplqvntpt grpafnpsvr vdktgavmvt yydfrdlqpg ntttlptgfw rkishdagst
      421 fgderrvagp fdmklapyae gffigdyqgl dvlpsssfhp ffvqtnagnl tnrtdvffap
//
LOCUS       WP_176075145             193 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia dolosa].
ACCESSION   WP_176075145
VERSION     WP_176075145.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..193
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=19102
     Region          1..193
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mkktirliai aglplaaanl ahasdgtinf tgsvvsstck vsggsnlsva lpkastsqft
       61 gvgstagrtp fkltvsgcat dkageggtvs apvkkvsiaf epgpnvdigt grlnltgtda
      121 akgiqiavln dkyediklga essaqnvqtv aidtavggtg satlqfaaqy vatsdtvtag
      181 sansfvtysl vyp
//
LOCUS       WP_176075146             880 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbria/pilus outer membrane usher protein [Burkholderia dolosa].
ACCESSION   WP_176075146
VERSION     WP_176075146.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 880)
  AUTHORS   Huang,Y., Smith,B.S., Chen,L.X., Baxter,R.H. and Deisenhofer,J.
  TITLE     Insights into pilus assembly and secretion from the structure and
            functional characterization of usher PapC
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7403-7407 (2009)
   PUBMED   19380723
REFERENCE   2  (residues 1 to 880)
  AUTHORS   Remaut,H., Tang,C., Henderson,N.S., Pinkner,J.S., Wang,T.,
            Hultgren,S.J., Thanassi,D.G., Waksman,G. and Li,H.
  TITLE     Fiber formation across the bacterial outer membrane by the
            chaperone/usher pathway
  JOURNAL   Cell 133 (4), 640-652 (2008)
   PUBMED   18485872
REFERENCE   3  (residues 1 to 880)
  AUTHORS   Jacob-Dubuisson,F., Striker,R. and Hultgren,S.J.
  TITLE     Chaperone-assisted self-assembly of pili independent of cellular
            energy
  JOURNAL   J Biol Chem 269 (17), 12447-12455 (1994)
   PUBMED   7909802
REFERENCE   4  (residues 1 to 880)
  AUTHORS   Van Rosmalen,M. and Saier,M.H. Jr.
  TITLE     Structural and evolutionary relationships between two families of
            bacterial extracytoplasmic chaperone proteins which function
            cooperatively in fimbrial assembly
  JOURNAL   Res Microbiol 144 (7), 507-527 (1993)
   PUBMED   7906046
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459850
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..880
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..880
                     /product="fimbria/pilus outer membrane usher protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015473 - fimbrial usher porin activity
                     [Evidence IEA]"
                     /GO_process="GO:0009297 - pilus assembly [Evidence IEA]"
                     /calculated_mol_wt=94068
     Region          53..859
                     /region_name="FimD"
                     /note="Outer membrane usher protein FimD/PapC [Cell
                     motility, Extracellular structures]; COG3188"
                     /db_xref="CDD:442421"
ORIGIN      
        1 mekkhnslrp qsgptlkpic alvlsivagw qmdaraasqd raqtqhvaqa rfaqvefegg
       61 flnngggaid vsrysrgnvv rpgtystdiy vdgdwigrvd vpfkaapdtp daqpcfdnal
      121 ldrigidvar lpldvrtvle adracmrigq aipdasvsfd fndlrldlsi pqismrrhar
      181 gyvspdqwtq gvpvamvgyn anvynsrtsg angstqgyvg vdggfnyerw hfrhsgsfnw
      241 ddrgrrryen vatylqrnlp swssqlvvgd sytsgelfds tsfrgirvys ddrmlpesqr
      301 gyapvvrgva ntnaivtisq ngvklyettv apggfviddl yptgyggdlk vvvteadgst
      361 hsfsvpyaav pmslrpgqsr ysltagvvrn lpsttpaftq atwqrgitna ltgysgmtaa
      421 qgylammaga vlntgwgafg vdvthaatkv pnektysgqs frisyaktva atgtnvaiaa
      481 yrystngyfg lndamaardr sksrvtsgml yrqrnraslt tsqqlgrkgg slsvtastat
      541 ywnrsgsdfd ftigysnsfr nvsynvsatr qrdawgqast layvglsipl grarpatlst
      601 svnrdtrgmt qvatsvsgal gvdnnvsygv nlnrssgsgt qtsaganamy rgsiaelags
      661 vgasrdyrqf afaargaiva hpggitlsrp lsetfaivea khaegarvtn esgvridgrg
      721 yaivpfltpf amndvsldpk glstdvelke tsqrvaplag avpllvfkte ygrsaiirvr
      781 qadgslapfg aivtdaagkd vgvigqggkl largladrge lnvqwekgee ksvcsvsysl
      841 pvrkrasgyr plqsfelpcv vggaaaevda iparraepgv
//
LOCUS       WP_176075147             320 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia dolosa].
ACCESSION   WP_176075147
VERSION     WP_176075147.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..320
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=34471
     Region          175..320
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mnrilaalfs licvifpfda ralscyigkd kgpvtmvekl pddlyvlasm qqggviwesa
       61 airqrfycws rvnepvsfwv nprklpvgeg vevairyngk lyrqsdgsip tgfsvtewyl
      121 twyekyfdlt yslvllrkgm apatgqtqis nysvfqldgq qgingnpnqn fnqlingsia
      181 fsrgtcdfrv gddrkvvalp ptatnslsav gktsgrtrfs igmqkcdvgv srvtfsftgd
      241 adsdlpvafr ntgtatgvgv rlakadddta lgangvgnta tepvndgsvr lnltaeyvgt
      301 ngrpsagsvs alatvsisye
//
LOCUS       WP_176075250             592 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia dolosa].
ACCESSION   WP_176075250
VERSION     WP_176075250.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..592
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=65190
     Region          7..585
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 maadkkphvd avivgfgwtg ailakeltea glkvvalerg eyrdtypdga ypntidelty
       61 nvrkklfvdl skttvsirhg iddtalpyrq laaflpgegv ggaglhwsgv hfritpeelr
      121 lrshyeeryg kkfipegmti qdtgvsydel ephfdfaekv fgtsgqaykv ggkvvgdgnv
      181 feanrsdhfp lppqlntysa qrffdaaksi glhpyrlpsa ntsgpytnpy gvqmgpcnfc
      241 gycsgyacym yskaspnlni lpalrqtpnf elrskchvlr vdlddtkkra tgvtyvdpag
      301 revhqpadlv ivaafqyhnv hllllsgigk pydpisgegv vgrnfayqnl stikaffdkd
      361 tftnpfvgag gngvavddfn adnfdhgplg fvggsplwvn qagvkpvsgi atppgtpqwg
      421 aawkksvkdy yahtismdah gtnmsyrdvy ldldptyrds ygqpllrmtf dwkdndirma
      481 ryvtgqmrri aeamgpkais vwtrefgkhf dtrayqtthl vggaimgtdp ktsvlnrylq
      541 cwdvhnvfvm gasalpqgig ynptgivaal aywsaraire qylknpaplv tv
//
LOCUS       WP_176075262             455 aa            linear   BCT 11-JAN-2025
DEFINITION  sigma-54 dependent transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176075262
VERSION     WP_176075262.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20236632
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..455
                     /product="sigma-54 dependent transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=50647
     Region          <36..130
                     /region_name="VpsR"
                     /note="VpsR domain; pfam20161"
                     /db_xref="CDD:437993"
     Region          <151..446
                     /region_name="RocR"
                     /note="RocR-type transcriptional regulator, contains PAS,
                     AAA-type ATPase, and DNA-binding Fis domains
                     [Transcription, Signal transduction mechanisms]; COG3829"
                     /db_xref="CDD:443041"
ORIGIN      
        1 mnmpitrdkr aggergngqr pliywtqsps vmlrkeltrr dwkvsivaha selrdtsgei
       61 tcgildlsgg hadaigsias tcasmrdvvw valveagqta spnvrallrd ycfdyitlpa
      121 shqriadtvg haygmeclfa rdrerlesde hgivgtcsam lrlfdtvrrf artdapvfvf
      181 getgtgkelt avaihrhser rngpfvavnc gaipphllqs elfgyergaf tganarkigy
      241 veaanggtll ldeigdlphe sqasllrflq ersihrlggs npvpvdvriv sathvdlrea
      301 meegrfradl fhrlcvmrid qpplrargkd iellahhmle rfradarhrv rgfstdaita
      361 lykhdwpgnv relinrvrra vvmtegrlit ardleleycl daaspsvadi rksiereaie
      421 tallrtrelg vsratlyrwm eaygierprg tgssd
//
LOCUS       WP_176075360             402 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176075360
VERSION     WP_176075360.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..402
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=44725
     Region          27..84
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          116..318
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(131..132,134..135,138,142,144..150,244..249,
                     255..256,258..259)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mrdvldrrar phdtadaada pdmldarlmr illvlltert vsraavrlnm sqpatsaalk
       61 rlrtllgdpl lvrsrygmvp telgarliep lrnalqvidf iriqqptfda rtsvrtyrvg
      121 cpdylnvlfv pklvtlfrer apnaqlvfhp lgdgfddera laegeldvvi dnrcthrpri
      181 rhddlfddri vcmmrathpl aargamtvhd fahapqlcpt pswldasgai drqlervglr
      241 rriavtlphf elaahalvrs dliltttyrl arhyarllpl rvvalpaepp nivyrimwne
      301 agscvdgvrw lraliaeatr rwldaeaaqp avaaiaasas asaaahaesn tetrtaaaia
      361 aavsdpprra rrpqrtrcra sqrpgvarta riprhrfaak ph
//
LOCUS       WP_176075380             325 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176075380
VERSION     WP_176075380.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..325
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34785
     Region          6..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..301
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(111..112,114..115,118,122,124..130,221..226,
                     232..233,235..236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 medidlnlvt aldvlltess vtgaarrlgl stsamsrtla rlraatgdpl lvragralvp
       61 tphaaalrdr vhaiaadara vlrpaadvdv atlastftir aaesfmdmla gpvvaalael
      121 aprvrlrfva klardpgplr dgavdleigk rgddapelha rvlfydrhia varadhplfa
      181 saritrarya acrhviatpl gdfdgptddv lgkldpdatv svvvpsypda mrvaagtdli
      241 alvprsslgn afssgladtl rlrsfdvpvh mpdieisalw hprmhgdpvh rrlrdavidv
      301 crraypdaqt ppraatrsmk rresg
//
LOCUS       WP_176075381             461 aa            linear   BCT 11-JAN-2025
DEFINITION  nucleobase:cation symporter-2 family protein [Burkholderia dolosa].
ACCESSION   WP_176075381
VERSION     WP_176075381.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Chaliotis,A., Vlastaridis,P., Ntountoumi,C., Botou,M., Yalelis,V.,
            Lazou,P., Tatsaki,E., Mossialos,D., Frillingos,S. and
            Amoutzias,G.D.
  TITLE     NAT/NCS2-hound: a webserver for the detection and evolutionary
            classification of prokaryotic and eukaryotic nucleobase-cation
            symporters of the NAT/NCS2 family
  JOURNAL   Gigascience 7 (12), 5168872 (2018)
   PUBMED   30418564
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Frillingos,S.
  TITLE     Insights to the evolution of Nucleobase-Ascorbate Transporters
            (NAT/NCS2 family) from the Cys-scanning analysis of xanthine
            permease XanQ
  JOURNAL   Int J Biochem Mol Biol 3 (3), 250-272 (2012)
   PUBMED   23097742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10799042
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..461
                     /product="nucleobase:cation symporter-2 family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015205 - nucleobase transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015851 - nucleobase transport [Evidence
                     IEA]"
                     /calculated_mol_wt=47368
     Region          39..458
                     /region_name="pbuX"
                     /note="xanthine permease; TIGR03173"
                     /db_xref="CDD:274468"
ORIGIN      
        1 mqpassarsa asaddadsar dlvygpndrp apmvafvaal qhllaiivpi vtpgllicqa
       61 lgvssrdttl ivsmslvisg iatfvqcrrf gplgaglliv qgtsfnfvgp liaggsvmvk
      121 qgtpvetvma aifgvviags fvemsvsril pfvkrlitpl vtgivvllig ltlikvglvs
      181 mgggygaian gtfasaenlt lsglvlgtiv llnrvpvvwv rstalviala igylaaallg
      241 rldftgvhqa alfqvptplh fgigfswslf vpmliiylvt sleaigdvta tskiskepve
      301 gpvwmqrikg gvlvngansl lagvfntfps svfaqnngvi qitgvasrhv giwiaamlvv
      361 lglfptvagv lqavpepvlg gaamvmfgav aasginilag vhldrralli iavslalglg
      421 vsqvpdilns lphalknvle sgvatggisa lvmnwflpek k
//
LOCUS       WP_176075386             220 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia dolosa].
ACCESSION   WP_176075386
VERSION     WP_176075386.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..220
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22980
     Region          117..218
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(120..121,154..155,158,162..163,166,208,212)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mkklhlalla svaflaacss asgptfnaye lqprngvrtf qvdchgilss ektcmkvatr
       61 mcdkepvrvv dsaapfrdga dprslvfqcg aapapaaapv paapaavekv sltgdayfat
      121 dsatltpaar aaldkllnrq gdrhfsriev tgytdavgsd aynvalsrrr adavaaylre
      181 rglnadsfva agkgkanpva snataegras nrrveislqk
//
LOCUS       WP_176075447             282 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia dolosa].
ACCESSION   WP_176075447
VERSION     WP_176075447.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..282
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29772
     Region          7..260
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mtrrtaalaa rgltvgyrdh vvidgldlsi aagrvtalcg pngcgkstll rtlaglqpar
       61 agevtvngrp lasfrrrala reltmlaqfn qipsgltvre lvaygryayg gflrglsrad
      121 haaidealat sgladdaerd vgalsggerq rawiamalaq qapivlldep ttyldihhql
      181 dildalrtln rtrgltivwv lhdlnqaaay sdeivlmrag rlvaqgspda mldpaqlraa
      241 fgvdmlklah pqtgapmcvp aygpsdasaa qaagafdrdl av
//
LOCUS       WP_176075473             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia dolosa].
ACCESSION   WP_176075473
VERSION     WP_176075473.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..359
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39336
     Region          8..355
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mkhsferlrl dgvcrsftnt egaqvaaldg ldleirrgef iallgpsgcg kstalnciag
       61 lqpltrggiw lddtridvlp perrgfgmvf qnyalfphms vldnvgfglk mrgvskqetr
      121 rraqqalelv qlvghegklp gqlsggqqqr vaiaraivie pplvlmdepl snldtklrie
      181 mraeirriht qleratiyvt hdqdealsma drivvmkegv vqqvaspkdv ytrphnlhva
      241 rfmgyrnvlp ftlegtagdy vrvaaggvql tgvpmagfdg kdvvvalrpd dveraddggd
      301 nafdatvdtv eyggrdslir attpfgaiwa rvagefaqhe rlrlrvapsr tlvyagdar
//
LOCUS       WP_176075482             308 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176075482
VERSION     WP_176075482.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..308
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33179
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..294
                     /region_name="PBP2_CrgA_like_2"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08471"
                     /db_xref="CDD:176160"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176160"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176160"
ORIGIN      
        1 mdridamkvf vatldegsla gagrrlgrsp aavsraiafl eahtgtally rttrtirlse
       61 ageryaaacr riladleead mlvadersap rglltitapv aagedllral ldefidrhpa
      121 vsirlqlldr pvslidegid valriahlad stlvavpvgt vrrvvvaspg ylaahppiet
      181 padlaqhrii smthfgldsw sfppsgqsal pqvvqfaprf ivntiraaia savaghgvtr
      241 lfsyhvadav kdgalrivlr dsehaplpvh lltpygrlsv pkvrafvdfa aprlrehfar
      301 lsqitddd
//
LOCUS       WP_176075503            1050 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Burkholderia dolosa].
ACCESSION   WP_176075503
VERSION     WP_176075503.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..1050
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114777
     Region          11..1032
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msasreesrf nlsawalrhq alvvyliala tlagilaytr laqsedppft frvmvirtlw
       61 pgatarqvqe qvtdrigrkl qetpaidflr sysrpgesli fftmkdsapv kdvpetwyqi
      121 rkkvgdigyt lppgvqgpff ndefgdvytn iwtlegdgft paqlhdyadq lrtvllrvpg
      181 vgkvdyfgdp gqrifieadn aqltrlgisp qqlaqainaq ndvssggvlt taddrvyvrp
      241 sgqfdnvaai adtliringr tfrlgdlatv krgyddpqvt qmraigadgr gkavlgigvt
      301 mqpggdvirl gkaldaeske lqaqlpaglk ltevssmpha vshsvddfle avaeavaivl
      361 ivslvslglr tgmvvvisip vvlavtalfm ylfdiglhkv slgtlvlalg llvddaiiav
      421 emmavkleqg ysraraaafa ytstafpmlt gtlvtvsgfl pialaksstg eytrsifevs
      481 aialiaswfa avvlipllgy hllperkkha heahlpddhe hdiydtrfyr rlrgwidwci
      541 errfvvllit vvlfvvammg fslvpqqffp ssdrpellvd lrlpegasfa atlreterve
      601 kaldkrpeid hvvsfvgsga prfylpldqq lqlpnfaqfv itaksvkdre qlatwlettl
      661 rdrfpavrwr lsrlengppv gypvqfrvsg ddiatvrsia ekvaatmrgd artvnvqfdw
      721 depaersvrf eidqkkarel nvtsqdvsgf lamtlsgttv tqyrerdkli avdlrapqad
      781 rvdpaklagl amptpngpvp lgslgrftpa leygvvwerd rqptitvqsd vragaqgidv
      841 thaidgklda lraqlpvgyq iniggsvees akaqtsinaq mplmaiavft llmiqlqsfs
      901 rvlmvvltap lgligvvgtl llfgqpfgfv amlgviamfg iimrnsvilv dqieqdiaag
      961 hgrfdaivga tvrrfrpitl taaaavlali pllrsnffgp matalmggit satvltlfyl
     1021 palyatwfrv krderdphdg dtppaapsga
//
LOCUS       WP_176075494             366 aa            linear   BCT 11-JAN-2025
DEFINITION  saccharopine dehydrogenase family protein [Burkholderia dolosa].
ACCESSION   WP_176075494
VERSION     WP_176075494.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..366
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39964
     Region          1..>47
                     /region_name="PRK09599"
                     /note="NADP-dependent phosphogluconate dehydrogenase"
                     /db_xref="CDD:236582"
     Region          25..349
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mkiaivgagl ightiahmlr etgdyevvaf drdadalakl sregiatqrv dsadataire
       61 avkgcdalvn alpyylavnv aaaakaagvh yfdltedvra thairelaeg sdrafmpqcg
      121 lapgfigiaa helvngfsev rdvkmrvgal peyptnalky nltwsvdgli neycqpceai
      181 rdgrkqwvqp leglehfsld gteyeafnts gglgtlcetl sgkvetldyk svrypghrel
      241 vrflledlrl ssdrdtlksi mrravpstkq dvvlvfvtvt gvkdgqlvqd vftrkifakd
      301 vcgmhmsaiq ittagamcav ldlfrekklp qsgfipqekv slkaflanrf gklydggtme
      361 rmhala
//
LOCUS       WP_176075525             308 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Burkholderia dolosa].
ACCESSION   WP_176075525
VERSION     WP_176075525.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..308
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32456
     Region          7..272
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(34..35,38,90,103,105,134,167,253,256)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mraafpdila lgeamiefnq sqpgrpeflq gfggdtsnfc iaaarqgaat gfvsaigddp
       61 fgrllidmwt aervdttyvr idrcaptgvy fvthgpqghq fdylragsaa srystadlpl
      121 dalaaakavh lsgisvaist aacdaafaai dharrhgakv tfdtnlrlkl wplpraravm
      181 realrqtdic lpswddvtal tgandrdaiv damleygpqi valklgkega yvatpnerrv
      241 vpgfaveavd atgagdcfgg afvarivagd dpftaaryan aaaalsttgy gavapiphrd
      301 averllrg
//
LOCUS       WP_176075532             748 aa            linear   BCT 11-JAN-2025
DEFINITION  ATP-dependent DNA helicase [Burkholderia dolosa].
ACCESSION   WP_176075532
VERSION     WP_176075532.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 748)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439892
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..748
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..748
                     /product="ATP-dependent DNA helicase"
                     /EC_number="3.6.4.12"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0004386 - helicase activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=81220
     Region          43..743
                     /region_name="DinG"
                     /note="Rad3-related DNA helicase DinG [Replication,
                     recombination and repair]; COG1199"
                     /db_xref="CDD:440812"
ORIGIN      
        1 mnsplednla arrdassags arapertfel srkrvdeldt ifgeggllar aldgyrpras
       61 qiemaravas ameasarrmp dpeifetrkr parrlgdgdk aaetgadaaa sadadpdagd
      121 ntliveagtg tgktyaylvp amlwggkviv stgtkhlqdq lflrdiptvr nalavpvtva
      181 mlkgranylc hyylqrtadn grlpsrqdta ylqeivrfak itksgdkael asvpetapvw
      241 smvtstrdnc lgqecphyke cfvmqarrea qqadivvvnh hlffadimlr dtgmaellpn
      301 antvifdeah qlpetatlff getlsttqil elardtvaeg lshardavew vklggalera
      361 ardvrlafad dqivrmslaq lgddhplfga ldalegalda lasalasqae raeslgaclr
      421 rarelqdlla gwvapgaaea arqadaaasg dqpasddane kvrwvevfah tvqlhetpls
      481 vapifakqra gvprawvfts atlsvrgdft hyaaqmglss rrsmtlaspf dyqtqgllyv
      541 prnlpqpssp aftdavfeaa lpaieasggg vfmlcttlra vdriasklrd viesrgwntp
      601 llvqgdasrt elldrfrayg nailvgsqsf wegvdvrgda lslvvidklp fappddpvla
      661 arldalakkg lspfavhqlp qavitlkqga grliraetdr gvlmicdtrl vdkpygrriw
      721 qslppfkrtr eiavvqdffd ehraakra
//
LOCUS       WP_176075557             153 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176075557
VERSION     WP_176075557.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..153
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=16815
     Region          14..125
                     /region_name="HTH_YyaN"
                     /note="Helix-Turn-Helix DNA binding domain of the
                     MerR-like transcription regulators YyaN and YraB; cd01109"
                     /db_xref="CDD:133384"
     Site            order(15..17,31,48..50)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133384"
     Site            order(62,65,69..70,79,97,101,107,111,114..115)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:133384"
ORIGIN      
        1 msitvsapsa agpltigqva elmgvsthtl ryyeqagllr aisrtaaghr lyapadldwl
       61 efvmrlkstg mpiaqmqqfa alraqgestl rarrqllvah rdavrthiaq lqasldaige
      121 kiayyerrer dterrastsh ssteqdtphg ttr
//
LOCUS       WP_176075581             259 aa            linear   BCT 11-JAN-2025
DEFINITION  TatD family hydrolase [Burkholderia dolosa].
ACCESSION   WP_176075581
VERSION     WP_176075581.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..259
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28892
     Region          2..257
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mfvdshchin fkgladrlpa vlenmrehdv thalcvsvdf etlpdvlaia qahdnvyasv
       61 gvhpdhedar eptlaelvel aahpkvvaig etgldyyrle grsiadmewq rerfrthira
      121 atatmkpliv htrassedtl rimaeerahv pggvmhcfte swpvaeqala qnfhislsgi
      181 vtfknatdvq dvarrvpldr llietdspyl apvpyrgkpn epayvshvgr fiasergipv
      241 etladattrn ffrlfkiar
//
LOCUS       WP_176075585             319 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia dolosa].
ACCESSION   WP_176075585
VERSION     WP_176075585.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..319
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34368
     Region          83..292
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mplnpkiaqv ldmierakrp syhhqtpqqa raayeksapi ldvapapmha idecvvptrd
       61 grtigarlyl pvapslaepl palvyyhggg ftvgsvdthd alcrmfarda qcavlsvgyr
      121 lapehkfpta vndaddalrw lhrnaasfgi dasrlavggd ssggtlatvc avlardagir
      181 lalqmliypg vtgyqdtesh arlangylls rdtiqwffsq yvrdradrdd wrfapldgtr
      241 gapsfagvap awiaiaeydp lsdegvayan klcaagntvt lvrypgmihe ffkmggyvpe
      301 vraahadava alkaafddv
//
LOCUS       WP_176075587             407 aa            linear   BCT 11-JAN-2025
DEFINITION  leucine-rich repeat domain-containing protein [Burkholderia
            dolosa].
ACCESSION   WP_176075587
VERSION     WP_176075587.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Enkhbayar,P., Kamiya,M., Osaki,M., Matsumoto,T. and Matsushima,N.
  TITLE     Structural principles of leucine-rich repeat (LRR) proteins
  JOURNAL   Proteins 54 (3), 394-403 (2004)
   PUBMED   14747988
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Kobe,B. and Kajava,A.V.
  TITLE     The leucine-rich repeat as a protein recognition motif
  JOURNAL   Curr Opin Struct Biol 11 (6), 725-732 (2001)
   PUBMED   11751054
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Kobe,B. and Deisenhofer,J.
  TITLE     Proteins with leucine-rich repeats
  JOURNAL   Curr Opin Struct Biol 5 (3), 409-416 (1995)
   PUBMED   7583641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..407
                     /product="leucine-rich repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=43368
     Region          89..111
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <90..285
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          112..133
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          134..157
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          158..180
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          181..200
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          202..223
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          224..245
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          246..267
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
ORIGIN      
        1 mkalafclpa vtaltllcgp vrsdaqpser akqavssapv cptytqdgvv yadirdrhll
       61 naldtfivpd kalgtpltpd elahnlpfal dlsenggwli sdlsgiqcas slgildignn
      121 rvsdftplsg mtslhellad nnrvtnasld slahlpnlrl lslarnkisd vrplvanlpq
      181 lasldlssna itdisalaal plselflssn aisdlsplsk istlenlsld gvgmwdlsil
      241 kplaqlqnls lagnriqdls pladlqqlis lnldgnritd lsplialvqr dhtleqlqla
      301 nqtptlqcat tvyeraemrl sdlwkqfklg sgqknlhitg pnpahggptr mydtdkivwk
      361 iasgqtvvpv nveastnian fpalysaytt iplaplgcpg tatgarq
//
LOCUS       WP_176075636             333 aa            linear   BCT 11-JAN-2025
DEFINITION  HEAT repeat domain-containing protein [Burkholderia dolosa].
ACCESSION   WP_176075636
VERSION     WP_176075636.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Friedrich,D., Marintchev,A. and Arthanari,H.
  TITLE     The metaphorical swiss army knife: The multitude and diverse roles
            of HEAT domains in eukaryotic translation initiation
  JOURNAL   Nucleic Acids Res 50 (10), 5424-5442 (2022)
   PUBMED   35552740
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Kobe,B., Gleichmann,T., Horne,J., Jennings,I.G., Scotney,P.D. and
            Teh,T.
  TITLE     Turn up the HEAT
  JOURNAL   Structure 7 (5), R91-R97 (1999)
   PUBMED   10378263
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444215
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..333
                     /product="HEAT repeat domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=35340
     Region          <9..327
                     /region_name="FAD_binding_2"
                     /note="FAD binding domain; cl46878"
                     /db_xref="CDD:481218"
     Region          52..77
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          83..111
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          116..149
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          177..202
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(194..195,198,201..202,227..228,231,234..235,
                     258..259,262,265..266,269,289..290,293,296..297,320..321)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          210..237
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          240..270
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
ORIGIN      
        1 mtlsssvfpl sdahdahdre haalaarvta pdasvrrval leladledpa lvpafvavlr
       61 ddpsadvrse aarvlgaweq pdvvdalcra lldpddgvra taaqslselk dpasgavlcr
      121 waerpeasvr raalrglrel raadayapal raldtddaav raeavavlgw lkdaralpal
      181 ariatddada dvrriaigav gfaaaddasv vrallaalrd rawqvreeaa atlgklrvta
      241 ardalvtald ddywqvrlra aralgqlrda aatpavaall shsisnlrke aalalgelrd
      301 raslqalqaa fddrdpevrk avriairqie dtp
//
LOCUS       WP_176075638             160 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia dolosa].
ACCESSION   WP_176075638
VERSION     WP_176075638.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 160)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140365
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..160
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17483
     Region          18..147
                     /region_name="NUDIX_ADPRase"
                     /note="ADP-ribose pyrophosphatase; cd04673"
                     /db_xref="CDD:467557"
ORIGIN      
        1 mskpssrtag atrnvravpa vigvvvrdrd vllvrranpp dagrwgfpgg kiepgepiad
       61 avvreiveet avevdaldvf taldafdrdh dgtlrqhfvm vavlcrwlrg spaagddald
      121 arwfdldela rddlpmsagv rdvarraler vsftaerlrr
//
LOCUS       WP_176075648              77 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF2274 domain-containing protein [Burkholderia dolosa].
ACCESSION   WP_176075648
VERSION     WP_176075648.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009506
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..77
                     /product="DUF2274 domain-containing protein"
                     /calculated_mol_wt=8238
     Region          6..70
                     /region_name="COG5639"
                     /note="Uncharacterized conserved protein, DUF2274 domain
                     [Function unknown]"
                     /db_xref="CDD:444364"
ORIGIN      
        1 mstikklrlg plpktenikl tfvcpaslka dldryaalha qaygeavdat tliphmleaf
       61 iagdrgfkrg gqmapkl
//
LOCUS       WP_176075658             192 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176075658
VERSION     WP_176075658.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..192
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20683
     Region          1..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtnptntsee ilhcarsliv akgyngfsya disevvgirk asihhhfpsk vdlvrtlvar
       61 yredaeaafa qlalqepvdq lrayvgywaa cigdgtrpfc vcallatemp alppeivlev
      121 rayfrvlsaw ltsvmeqgam lgaltlsgta rseaeafiat vhgamlsara ygdptvfaav
      181 tqpliervia ar
//
LOCUS       WP_176075695             406 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Burkholderia dolosa].
ACCESSION   WP_176075695
VERSION     WP_176075695.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10648119
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..406
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=42870
     Region          <23..406
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
ORIGIN      
        1 mdslitaaar alaagdalga lnrvalrdda palalrgial aqlgdferar slvrsaaraf
       61 gakeavarar civadaeial asrdlgwpsr aldaacatld ahgdranaah arylgirrll
      121 lighldeaer rlagldpapl paasraahel iaagiamrri rahaarsale raraaardag
      181 iaaltaevdt afdvldtpaa rliargasrl vlldeiealq asntlvvdac rhtvrdartt
      241 vslarrpvlf mlaralgeaw padvsrnalv aaafrarhad eshrarlrve igrlravlrp
      301 lanisatprg faleplgvre tvvlarpvdd rhaavlalla dgeawsssal alalgasqrt
      361 vqraldalre agkvhalrrg rarrwmmppl pgfattlllp aplpad
//
LOCUS       WP_176075750             262 aa            linear   BCT 11-JAN-2025
DEFINITION  TatD family hydrolase [Burkholderia dolosa].
ACCESSION   WP_176075750
VERSION     WP_176075750.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Wexler,M., Sargent,F., Jack,R.L., Stanley,N.R., Bogsch,E.G.,
            Robinson,C., Berks,B.C. and Palmer,T.
  TITLE     TatD is a cytoplasmic protein with DNase activity. No requirement
            for TatD family proteins in sec-independent protein export
  JOURNAL   J Biol Chem 275 (22), 16717-16722 (2000)
   PUBMED   10747959
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000566
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..262
                     /product="TatD family hydrolase"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0004536 - DNA nuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=28672
     Region          2..242
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
ORIGIN      
        1 mwidthchld aaefdadrda vaqsaraagv srivipsvgr dnfatvrela qrtpgavyal
       61 gihplftpha rdddldrlrm eieasvddpr fvaigeigld yfvpgldear qqffyqgqlk
      121 larefdlpvl chvrksqdrv laglrrfgvr rgiahafngs fqqanaylaq glhlgfggnv
      181 tferarqirr latqlpldai vvetdapdia pewayksrnt pdqvprigdv laelrgidah
      241 alslstsana laalprlals sa
//
LOCUS       WP_176075781             455 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia dolosa].
ACCESSION   WP_176075781
VERSION     WP_176075781.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..455
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49217
     Region          23..410
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(36..37,40..41,44,76,126..127,129..131,134,154,
                     157..158,161,259,262..263,266..268,271,299,303,352..353,
                     357,361,377,380..381,384..385,388)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mnppssalpg rdplasavsk vkwhvlplvl imfianyidr vnvgfvdrhl easigigaaa
       61 yglgaglffv gyalfevpsn llmqrygarv wlarimatwg ivaaamafvw ndtsfyvlrf
      121 llgaaeagff pgvvlylsqw lppqergkam aiflggsafa svlsgpvtga llsirgfgld
      181 gwqwmfvieg lfsvalcgas wlllkshird atwlsanera alenaldeer atrdlrstvh
      241 vpavvllrdp qivlfcflyf siqltiyaat fwlptiirkm ggltdfqvgl yntipwmiai
      301 gamygfavls akwkhpqrwl afslvlaacg lfastsddpv wsfasicfaa lgfkaaaslf
      361 wpipqgyldt rvaaaviali nsvgnlggfv aptafgylkq htgsitggly alaiasvvaa
      421 vaalfarthr rsdpprglpa dptiqhntml rhaeh
//
LOCUS       WP_176075855             311 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Burkholderia dolosa].
ACCESSION   WP_176075855
VERSION     WP_176075855.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..311
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31510
     Region          2..310
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mtilviaehd nasikaatln tvaaaqkigg dihvlvaghn aqaaadaaak iagvskvlla
       61 dapqlaegla enveatvlnv akdyshilap ataygkniap riaakldvaq isditavdsa
      121 dtferpiyag naiatvqssd pikvitvrat gfdavaaegg saaidkieaa adagvsqfvs
      181 revtkldrpe ltsaniivsg grglgsgeny tkvlepladk lsaalgasra avdagyvpnd
      241 yqvgqtgkiv apqlyiavgi sgaiqhlagm kdskvivain kdpeapifsv adyglvgdlf
      301 tlvpelvael g
//
LOCUS       WP_176075920             224 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia dolosa].
ACCESSION   WP_176075920
VERSION     WP_176075920.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..224
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=23307
     Region          12..215
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msfppasmls dgfflslslc ldiglvnvam lsltlshgfr pgfwlgigsc vgdlvyaala
       61 lagmavllqf epvrwivwig ggavllfltw kmarealapt qapnggdgae dppqprasar
      121 rsfvrgmlla msspsailwf aavggaliak agattpatas vflsgfflgg lawtlfmctl
      181 asqgrkraga glmrachvas allfayfsys vivggyrdli ahav
//
LOCUS       WP_176075927             323 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176075927
VERSION     WP_176075927.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..323
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34685
     Region          12..71
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          98..298
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(110,114,153,167,170,233,250,277)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(111..112,116..117,119..120,123,127,129..135,197,
                     227..231,238..239,242)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mkqnftvrqg aldgveafls varhrsfrra aaelgvtpsa vsqvvrales rigtalfirt
       61 trsvglteag erflsrakpa feelvaasda arelgrrpag llrlsvprav vpilleplia
      121 sfcnaypeie veidaseklv dlaaegfdag mrlgqfvaad miavpltppf rfvvvgspay
      181 fadhdrperi ddlrghacvr wrrsngalap wsfddggrti eaavsgplia rdfptvlgaa
      241 legvglaqlp epmvaeglka gklvqvlepf apmmagvfly ypsrrqiapk lrafidhvkh
      301 daaarndera pgraadarsg kng
//
LOCUS       WP_176075955             648 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Burkholderia dolosa].
ACCESSION   WP_176075955
VERSION     WP_176075955.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..648
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=71091
     Region          <450..618
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mmaggretla nvrifnklkr vvrrvapgla drlkailvkp arplavdlda ieselataga
       61 efdrnhaida kavaavakqs avivasvapf dnvalmidai qreglefgel vivdataeep
      121 rlvairdhia awsrrlpmtr fkvvsyerqe lrfadaiecg wqataqpyaw ivgrnnvpid
      181 rcftylikll lvsersaiav shsvgpdgql rggtinpdal tgnvrqaiqt tagfdvridq
      241 avsgrlserp liemlatfcd gifggeraal addtgrlldg rfisdvavsd fslrkqahga
      301 llvrtraaas rslrggetda vapwealhdw rwlldkraga dvhderielv cpfhrgdvvl
      361 aaqvaahvaq tggrirlhva aslvswaref apmldiesip vgvvsaeety ptllrsyqyv
      421 vqrddaspri archptrgls etgvnlleym leevglprnt rlenrrpevs enarriardh
      481 laslggnvvf vhpmggwglk sipdhiltdl adeiraagfr lvpiggasdr kmpqcdgail
      541 enympsqwre ilehgcallg vdswtshfga ildipqigmy gsthpkhvnt kkwfveqrne
      601 clilgpivnc spcnsltcvs ypdrkycsgy vvdrpalraf lsrlgcek
//
LOCUS       WP_176075997             136 aa            linear   BCT 11-JAN-2025
DEFINITION  GFA family protein [Burkholderia dolosa].
ACCESSION   WP_176075997
VERSION     WP_176075997.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..136
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14735
     Region          5..130
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 msntetmdgg cacgairyri avvptdagfc hcrlcqrttg aavvasasvp idafeylqge
       61 ptvyasstwg errfcgrcga qleyrradap ktveinsatl ddpsrlrpaw hvwyadrfpg
      121 ieiaddlpky rdggpa
//
LOCUS       WP_176076027             469 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia dolosa].
ACCESSION   WP_176076027
VERSION     WP_176076027.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..469
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50353
     Region          14..467
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mnhpaqpaat rrplppamld alrarfgerv stadavrahh grdespfdpq lpdavvfars
       61 addvrevvsl calysvplip ygagsslegh llavrggvsl dlsemnrvls inaedltvtv
      121 epgitrkaln dalrdtglff pidpgadasi ggmtatrasg tnavrygtmr envlgltavl
      181 adgrvvktgs rarkssagyd ltrlfvgseg tlgviteitl rlhplpeavs aaictfptms
      241 davrtvieti qigvpiarve fvdslavrsi nrhsnltlae aptlffefhg teagvkeqae
      301 lvqalagqnr gqgfewatrp edrsrlwaar hnayfamlql kpgcravttd vcvpisqlaa
      361 cveeteadlr asslpcpivg hvgdgnfhva ilidpdkpde ideaerindr iveralrlgg
      421 tctgehgvgl hkmrflpkeh gdnaidtmra iklaldprnl mnpgkiftc
//
LOCUS       WP_176076156             401 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphotransferase enzyme family protein [Burkholderia dolosa].
ACCESSION   WP_176076156
VERSION     WP_176076156.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Scheeff,E.D. and Bourne,P.E.
  TITLE     Structural evolution of the protein kinase-like superfamily
  JOURNAL   PLoS Comput Biol 1 (5), e49 (2005)
   PUBMED   16244704
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457111
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..401
                     /product="phosphotransferase enzyme family protein"
                     /EC_number="2.7.-.-"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016301 - kinase activity [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=43350
     Region          73..328
                     /region_name="SrkA"
                     /note="Ser/Thr protein kinase RdoA involved in Cpx stress
                     response, MazF antagonist [Signal transduction
                     mechanisms]; COG2334"
                     /db_xref="CDD:441905"
ORIGIN      
        1 msfplepdgp gsrdaaardv appqfgvdge qaerdwplia rdevaavler idgageparl
       61 twhsprpfsa avlvcttdgr alfvkrhhas lrdvaalhee hgfiahlrah gvpvpdvlag
      121 rdgatafafg dwtyevhvva pgvdayrgvm swkpfahssh ayaagralaa lhrasagyda
      181 parpvrtlls sfrvlssadl ggalerwvaa qpllmralga rdwrgdvada igpyharfap
      241 llpalpplwt hgdwhasnll wtdtapgaqv qtvldfglad rtcavmdial aiernaidwl
      301 apadarrvey eqidallagy eslaplsdaa yaaliallpi vhtefalsev ayfgcivdap
      361 eivdiaydgy llgharwfge rdgrrlldwl aqrrrakneg g
//
LOCUS       WP_176076173             285 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176076173
VERSION     WP_176076173.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..285
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=31344
     Region          30..86
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Region          105..270
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 madasdnllg aylrarrkkl dpaalglpva rrrtpglrre evaqrahisv awytwleqgr
       61 ggapsadvld rlaralllde aerehlflig lghppdvryh vtgsvpprlq hvldsfdasp
      121 ailrtstwdv vawndaaaat ltdyatlppp arnilrlifa darvrdaqsn wervarfavg
      181 afradlarsg atqvvqafvd emraasaefd amwrdhdirs ndegtkeirh pragrialey
      241 safavkgrpd lslvvftpat aadrariral iaarekdpae rlpaa
//
LOCUS       WP_176076176             332 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia dolosa].
ACCESSION   WP_176076176
VERSION     WP_176076176.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 332)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..332
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35388
     Region          47..325
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mrepsrplps daapaavara pvadaghppg rasaraaarn rapranwrah aplwlmcapa
       61 falfaalvlv plamtlvltf yrfdpatgpi aafqfgnyae vlgssyfhai fartfgiaal
      121 ttaicvaigt peayilskmr dpwrslflla ilapllvsvv vrafgwsmll ntnglvngal
      181 aligvgpykl eyttfaivia lvhvmlpfmv ipvwtalqrl dpqtehaals lgaspfttlr
      241 rivlpqlvpg vlsgslmvfg lsasafaipg llggrrlkva atavydeflg slnwplgati
      301 avlllianlv vmltyyrvle rryarslgga sr
//
LOCUS       WP_176076191             304 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia dolosa].
ACCESSION   WP_176076191
VERSION     WP_176076191.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Hammerstad,M. and Hersleth,H.P.
  TITLE     Overview of structurally homologous flavoprotein oxidoreductases
            containing the low Mr thioredoxin reductase-like fold - A
            functionally diverse group
  JOURNAL   Arch Biochem Biophys 702, 108826 (2021)
   PUBMED   33684359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..304
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=31650
     Region          5..272
                     /region_name="TrxB"
                     /note="Thioredoxin reductase [Posttranslational
                     modification, protein turnover, chaperones]; COG0492"
                     /db_xref="CDD:440258"
ORIGIN      
        1 mhtdhevivi ggsfaglsaa mqlararrrv lvidgglprn rfaphahgff gqdgkppaqi
       61 vdeaaaqlaa yptvqridge arsaardang rfsvtladgr rasadrlila tgvrdvlpal
      121 pglesrwgvs vlhcpychgy evadrrlgvl athplsvhqa mlipdwgptt wftqgvveps
      181 deeaaqlaar gvcierspvv ailgdaphid aleladgkvv pidalfvgar temasdlaaq
      241 lgcefdegpl gpairvdawk htsvpgvfaa gdasslmtna tfaaasgvaa gvgahrslif
      301 glgv
//
LOCUS       WP_176076198             344 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176076198
VERSION     WP_176076198.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..344
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36262
     Region          14..209
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          241..324
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mseplqtpvs dahdlvsell lgmrlsgvqy rriqiarpfg lsfghapgra qfhfvgrgpv
       61 llrdaggatv qleagdaill phghrhalms dadascreig afeaaricdt vasvaavpag
      121 aacasaepag gdalifsacm eldlggmqpl vgtmpsvmhv gtllarypei rpildamere
      181 scaeragfag ilarladvva afivrgwvec gcgdatgwvq alrepklgra ivalhrdpgr
      241 nwsvaelaae agvsrsvfae rflaatgmtp vryltelrmr laaqwiardr esieavayrl
      301 gygslaafsr afkrvvgrpp gavraegdpr adaradassv ttpa
//
LOCUS       WP_176076226             130 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia dolosa].
ACCESSION   WP_176076226
VERSION     WP_176076226.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..130
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14394
     Region          10..108
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mrrqgvtytl hhigipteqr lageryarav gmyttddptg plpiqwhrfe pdsplhplvr
       61 sqphvaykvs dlaaaidght vilgpyepid gyrvamidna gvpvefiett lsdaeiwrra
      121 ttgesaslyr
//
LOCUS       WP_176076248             336 aa            linear   BCT 11-JAN-2025
DEFINITION  sodium:calcium antiporter [Burkholderia dolosa].
ACCESSION   WP_176076248
VERSION     WP_176076248.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schnetkamp,P.P.
  TITLE     The SLC24 gene family of Na/Ca(2)-K exchangers: from sight and
            smell to memory consolidation and skin pigmentation
  JOURNAL   Mol Aspects Med 34 (2-3), 455-464 (2013)
   PUBMED   23506883
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Besserer,G.M., Nicoll,D.A., Abramson,J. and Philipson,K.D.
  TITLE     Characterization and purification of a Na+/Ca2+ exchanger from an
            archaebacterium
  JOURNAL   J Biol Chem 287 (11), 8652-8659 (2012)
   PUBMED   22287543
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424992
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..336
                     /product="sodium:calcium antiporter"
                     /GO_function="GO:0008273 - calcium, potassium:sodium
                     antiporter activity [Evidence IEA]"
                     /GO_process="GO:0006874 - intracellular calcium ion
                     homeostasis [Evidence IEA]"
                     /calculated_mol_wt=35405
     Region          19..332
                     /region_name="ECM27"
                     /note="Ca2+/Na+ antiporter [Inorganic ion transport and
                     metabolism]; COG0530"
                     /db_xref="CDD:440296"
ORIGIN      
        1 mtvmlvelaf mlivilvaae lftnalehlg erlkisegvt gslfaavgta lpetmvplla
       61 liggtsnqav neeigvgail gaplmlatlt tflmsvavig srglrgtiap ersgfvrdln
      121 yflaafvlaa gamfvphhns airallaaam vgiyvlyvfm tfrassrlvd aghgteapha
      181 mflsrigmpt nlatialqll lgvallvgga kgfihgverv sqligvsall lsliivpiat
      241 elpekinsvl wirrrkdtla fgnitgamvf qgtllpaigi mltpweprpe vltgviitia
      301 aalwlrihar thglaiwall angagyagyl fvtlar
//
LOCUS       WP_176076262             108 aa            linear   BCT 11-JAN-2025
DEFINITION  thioredoxin family protein [Burkholderia dolosa].
ACCESSION   WP_176076262
VERSION     WP_176076262.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and
            Ramos,M.J.
  TITLE     Structural and mechanistic aspects of S-S bonds in the
            thioredoxin-like family of proteins
  JOURNAL   Biol Chem 400 (5), 575-587 (2019)
   PUBMED   30367780
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J.
  TITLE     Thioredoxin superfamily and thioredoxin-inducing agents
  JOURNAL   Ann N Y Acad Sci 957, 189-199 (2002)
   PUBMED   12074972
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Powis,G. and Montfort,W.R.
  TITLE     Properties and biological activities of thioredoxins
  JOURNAL   Annu Rev Biophys Biomol Struct 30, 421-455 (2001)
   PUBMED   11441809
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..108
                     /product="thioredoxin family protein"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=11298
     Region          15..101
                     /region_name="TRX_family"
                     /note="TRX family; composed of two groups: Group I, which
                     includes proteins that exclusively encode a TRX domain;
                     and Group II, which are composed of fusion proteins of TRX
                     and additional domains. Group I TRX is a small ancient
                     protein that alter the redox...; cd02947"
                     /db_xref="CDD:239245"
     Site            order(33,36)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239245"
ORIGIN      
        1 mvtpqrytan aptraevdsl vgttviefga nwcgicagaq paivaslaah ptvrhlkied
       61 gpgrplgrsf gvklwptlvf irdgvevarv vrpanahqie aegfaala
//
LOCUS       WP_176076322             311 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176076322
VERSION     WP_176076322.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 311)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 311)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14401161
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..311
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35470
     Region          14..95
                     /region_name="cupin_MtlR-like_N"
                     /note="AraC/XylS family transcriptional regulators similar
                     to MtlR, N-terminal cupin domain; cd06976"
                     /db_xref="CDD:380381"
     Region          31..284
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
ORIGIN      
        1 mnpdleivpt hrdesfrawv hdyphsvakw hfhpeyeihl iqashgkmfv gdhigdfgpg
       61 nlivtgpnlp hnwvseladg ervpsrdvvl qfsrdaiekm vgafselqpv ieliddasrg
      121 vqfpdrvgle vaplmlelan ahgcrrveil mslfdrlssc rerrvlagpg yridaqhyms
      181 stinqvlsyl qqnlpgmlre advaafagms vstftrffrr htgssfvryl nrlrineace
      241 llmfsdltvt dicyrvgfnn lsnfnrqfla mkqvppskfr alhrlnephr rddtpplrrt
      301 psrapdrtlh s
//
LOCUS       WP_176076357             185 aa            linear   BCT 11-JAN-2025
DEFINITION  NADPH-dependent FMN reductase [Burkholderia dolosa].
ACCESSION   WP_176076357
VERSION     WP_176076357.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Grandori,R., Khalifah,P., Boice,J.A., Fairman,R., Giovanielli,K.
            and Carey,J.
  TITLE     Biochemical characterization of WrbA, founding member of a new
            family of multimeric flavodoxin-like proteins
  JOURNAL   J Biol Chem 273 (33), 20960-20966 (1998)
   PUBMED   9694845
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..185
                     /product="NADPH-dependent FMN reductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008752 - FMN reductase (NAD(P)H)
                     activity [Evidence IEA]"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /GO_function="GO:0052873 - FMN reductase (NADPH) activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20466
     Region          4..165
                     /region_name="SsuE"
                     /note="NAD(P)H-dependent FMN reductase [Energy production
                     and conversion]; COG0431"
                     /db_xref="CDD:440200"
ORIGIN      
        1 msyrvavvvg slrrgsfnra lahavislap adfsfefvei gdlplysqdy dadfpevakr
       61 fkqsieaada llfvtpeynr sipgvlknai dwgsrpwgsn swagkpgavl gtsvgamgta
      121 laqqhlrnvl syldvkmlgq pemfikhdpt riddegrivs ddtrkflqgf vdryadwvrf
      181 lkkpa
//
LOCUS       WP_176076358             312 aa            linear   BCT 11-JAN-2025
DEFINITION  GGDEF domain-containing protein [Burkholderia dolosa].
ACCESSION   WP_176076358
VERSION     WP_176076358.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 312)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..312
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34615
     Region          44..311
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mttgspslsd lviervgfgl fvldrsmtvl mwnrfmqdhs gipaadvigr nlfdrfpelp
       61 rawlarkves vfqlgsfafs sweqrpylfr fehdrpitgg vdymqqdctf mpltrgrdve
      121 avcvtisdvt hvsvmqrere eavaklreha nrdgltgian rrffearlgd efarwqrygg
      181 dlsvllfdld hfktindrfg havgdavlre tarrvasivr aqdtfgrfgg eefalllpct
      241 nldeamlvad kvrdaignap vhaeganvpv tasvgaacak pgaptcdvlv neadaalyra
      301 krlgrdrsva ya
//
LOCUS       WP_176076385             260 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176076385
VERSION     WP_176076385.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..260
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27667
     Region          13..245
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mahldappad trtdartaas psqtvrtllg lrelivggel apgeriselw vverlgvsrt
       61 pvraalirlq eegliepiat ggfavrafsa reigdaielr gtleglaarf aaergvspam
      121 lgdlhacade idallagplt ddtfsryvda narfhrllaa aagsdvvarq idkvatlpfa
      181 sasafvvvqs ldpraretlv vaqaqhravl daiarrqgar aealmrehaq iahdnlrrvl
      241 dnqramtkla ggnlirrdag
//
LOCUS       WP_176076391             666 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 28 protein [Burkholderia dolosa].
ACCESSION   WP_176076391
VERSION     WP_176076391.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 666)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 666)
  AUTHORS   Abbott,D.W. and Boraston,A.B.
  TITLE     The structural basis for exopolygalacturonase activity in a family
            28 glycoside hydrolase
  JOURNAL   J Mol Biol 368 (5), 1215-1222 (2007)
   PUBMED   17397864
REFERENCE   5  (residues 1 to 666)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 666)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..666
                     /product="glycoside hydrolase family 28 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=69274
     Region          83..622
                     /region_name="Pgu1"
                     /note="Polygalacturonase [Carbohydrate transport and
                     metabolism]; COG5434"
                     /db_xref="CDD:444185"
ORIGIN      
        1 maansrrpss sarsrsskrv srrtfigwtg afaggavlga plsatrafag sampgvpavd
       61 piwgehgaaa riaaslahvs rlafrgrefd vthygartca tvaqtspytn aakspvspga
      121 elttapgafd srpaflaaid achregggrv vvppgnwyca gpivlqsnvn fhlsanctiy
      181 fspnpadyak dgpvdcgang rlyysrwqan dclnygapvy arnavnialt gegptsvlng
      241 qamtpfagtg ngsvcwwtyk gssgaygaga svpsqasanp nnvdlrivap aisdalyall
      301 tspvtpwqqd qnylpalsea gvpvdkrifg lghylrpcmv efigctnvlm adyqtqntpf
      361 wqhhptacrn vvirgvttns igpnndgfdp dactdvlcee ctfntgddci aiksgknldt
      421 eygpakrhli rnctmnsghg gitlgsemgg gveqiyatnl smlnanwqtn plniairvkt
      481 nmnrggyvkd fhvkgvslpn gvnlkgggyg sallagspvn atvplgvvtp aagnpsaaqg
      541 givtfdcdyq pandavrtrp pvvqnvtisd vkasnvtlgg vtascfqaiv aqgpvafdyn
      601 gapptpavqp isgvtirncd fgtpvasgtp tvtspgpvya fnvsgmtltn vaiagqtidt
      661 titdrr
//
LOCUS       WP_176076403             334 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176076403
VERSION     WP_176076403.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13300132
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..334
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=37612
     Region          29..>163
                     /region_name="PRK11242"
                     /note="DNA-binding transcriptional regulator CynR;
                     Provisional"
                     /db_xref="CDD:183051"
     Region          112..309
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(122,126,165,179,181,244,261,288)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(123..124,128..129,131..132,135,139,141..147,208,
                     238..242,249..250,253)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 msdmptrrtd tddpyarsfs tcyagvvtfl avvtegsfar aadrlgvgrs svsrhvqkle
       61 drldarlfqr ttrsmsltre gelfyencrp giehlaqale dmrelrsgpp sghlrigsrp
      121 gfgrkiiapl lrdfhaqypd itlelllndr padfsadrid vafrdgrmed svivarrlip
      181 mqmivcasps yarryglprh vdelaqhrci nlrtasgrvt ewefkidgla qqrqlaahht
      241 fndmdlvvra vldglgiaql payqvcdlla dgklvsclgq yapddgghyl cylsrkhlpt
      301 rirvfidymi eqtrardlqc ltamtmmppl eavd
//
LOCUS       WP_176076410             505 aa            linear   BCT 11-JAN-2025
DEFINITION  peptide MFS transporter [Burkholderia dolosa].
ACCESSION   WP_176076410
VERSION     WP_176076410.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Steiner,H.Y., Naider,F. and Becker,J.M.
  TITLE     The PTR family: a new group of peptide transporters
  JOURNAL   Mol Microbiol 16 (5), 825-834 (1995)
   PUBMED   7476181
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Paulsen,I.T. and Skurray,R.A.
  TITLE     The POT family of transport proteins
  JOURNAL   Trends Biochem Sci 19 (10), 404 (1994)
   PUBMED   7817396
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459681
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..505
                     /product="peptide MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:1904680 - peptide transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0015833 - peptide transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55172
     Region          7..485
                     /region_name="PTR2"
                     /note="Dipeptide/tripeptide permease [Amino acid transport
                     and metabolism]; COG3104"
                     /db_xref="CDD:442338"
ORIGIN      
        1 mmhapvsqtr sfttvfliel werfgyygma allvlfmvdr lgftdshanl twgaftalvy
       61 aspsvggwig dkvlgarrtm iigaavlsag ylmlavpnda laymyaslgv ivvgnglfka
      121 naanlvrriy egddaridsa ftiyymavni gstvsmlatp wikdhwgwht afavccggml
      181 lailnfmlmh rtlahigsqp ddepirwkrl gavaaggval alitlyvlqh kqlavasvwg
      241 aafailaifa ymivkserse ragliaalvl tgqvilffif yvqmstsltl falrnvdprf
      301 ivfgrtlftw saaqfqalnp iwimllspvl vwiynafskg grdlpvaaky algfgavaag
      361 ylvftisgry avdgrvsswf mvwgyglysl gellvsglgl amvaryvpar msgfmmgayf
      421 vatgvsqylg svvanfaqmp shelpatesl plylslfekl gwlaaigmll allllptmnr
      481 lsrrhqrcvd errdeapdaq avatr
//
LOCUS       WP_176076441             139 aa            linear   BCT 11-JAN-2025
DEFINITION  HIT family protein [Burkholderia dolosa].
ACCESSION   WP_176076441
VERSION     WP_176076441.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Lima,C.D., Klein,M.G. and Hendrickson,W.A.
  TITLE     Structure-based analysis of catalysis and substrate definition in
            the HIT protein family
  JOURNAL   Science 278 (5336), 286-290 (1997)
   PUBMED   9323207
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Seraphin,B.
  TITLE     The HIT protein family: a new family of proteins present in
            prokaryotes, yeast and mammals
  JOURNAL   DNA Seq 3 (3), 177-179 (1992)
   PUBMED   1472710
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001677
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..139
                     /product="HIT family protein"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=14862
     Region          5..136
                     /region_name="HinT"
                     /note="Purine nucleoside phosphoramidase/Ap4A hydrolase,
                     histidine triade (HIT) family [Nucleotide transport and
                     metabolism, General function prediction only]; COG0537"
                     /db_xref="CDD:440303"
ORIGIN      
        1 mpyddnnpfa kilrgelpcv kvaeddatia imdlmpqadg hvlvipkepa aqifelsgda
       61 aaaairmtqr vaaavraale pdglfigqfn gaaagqtvah vhfhviprwe gvelrmhard
      121 vadaatlesv aqrirarfv
//
LOCUS       WP_176076482             454 aa            linear   BCT 11-JAN-2025
DEFINITION  2-hydroxycarboxylate transporter family protein [Burkholderia
            dolosa].
ACCESSION   WP_176076482
VERSION     WP_176076482.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007470
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..454
                     /product="2-hydroxycarboxylate transporter family protein"
                     /calculated_mol_wt=47742
     Region          28..453
                     /region_name="CitS"
                     /note="Na+/citrate or Na+/malate symporter [Energy
                     production and conversion]; COG3493"
                     /db_xref="CDD:442716"
ORIGIN      
        1 mqtsihtpsh peplaeagpa trerfwpagw wklmeirigi iplpvyvill glivgfavtg
       61 kvpgeismai avlaffgftc aelgkrlpil rnigaaaifa tfvpsaltyy hvlpkpvlnl
      121 tveftkstnf lylfiasiiv gsilsmdrrv liqgflkifv plavgtiaaa ivgtavgtal
      181 glgarhtlly ivvpimaggv gegaiplsig ysellhlpqg emfamvlpsv mlgsltaiil
      241 sgaldmlgkr lphltgngrl qvgeagdmtp esdelrghvd vthiagagit aitlylvglm
      301 ahklfglpap vamlflavlv klaravsppl qegafvvykf fstavtypll faigvamtpw
      361 dkltaaftlv nvvtivatva tlmgtgfvvg rlmkmypidt aivnachsgq ggtgdvailt
      421 aanrmqlmpf aqiatrigga ivvtvtlilv ahfg
//
LOCUS       WP_176076483             287 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Burkholderia dolosa].
ACCESSION   WP_176076483
VERSION     WP_176076483.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 287)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..287
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30926
     Region          41..287
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mphavltsrf ssrvssrrva afvrvlaval aallvefalp gsahadtapl kvgistspqi
       61 ealkiaakea kaqgldvriv eftdwntpna alankdidvn yfqhvpflen akkqggydfv
      121 aiapgtimki glyskkvksf selkdgakva iandpvnggr gllllqragl itlkpgvdyr
      181 attrdivanp khlkiiplea sqlarslddv dlaqgypsfi klagtadpns allfdgtenk
      241 nfaiqwvvrp dsvndprirk fiaiyqhspa vrkaldnafg slyaiaw
//
LOCUS       WP_176076503             204 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Burkholderia dolosa].
ACCESSION   WP_176076503
VERSION     WP_176076503.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..204
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=20859
     Region          19..204
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msttahillp lagvlllsva spgpnfvivt stavasrrag imtglglaaa sgtwaaiaia
       61 glsllvthvg wvhtalriag aayliwlgvk mivtarqpls aitpgtmsdw taarkgygvs
      121 mtnpkavafy gsifalmvpa dapawldlsv vgmsiaisgv wyctmallas hpavrrllvl
      181 rkalldtaag mllvglggrm lagr
//
LOCUS       WP_176076534             260 aa            linear   BCT 11-JAN-2025
DEFINITION  gamma-glutamyl-gamma-aminobutyrate hydrolase family protein
            [Burkholderia dolosa].
ACCESSION   WP_176076534
VERSION     WP_176076534.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Kurihara,S., Oda,S., Kato,K., Kim,H.G., Koyanagi,T., Kumagai,H. and
            Suzuki,H.
  TITLE     A novel putrescine utilization pathway involves gamma-glutamylated
            intermediates of Escherichia coli K-12
  JOURNAL   J Biol Chem 280 (6), 4602-4608 (2005)
   PUBMED   15590624
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449689
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..260
                     /product="gamma-glutamyl-gamma-aminobutyrate hydrolase
                     family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016811 - hydrolase activity, acting on
                     carbon-nitrogen (but not peptide) bonds, in linear amides
                     [Evidence IEA]"
                     /calculated_mol_wt=27299
     Region          9..244
                     /region_name="PuuD"
                     /note="Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
                     (putrescine degradation), contains GATase1-like domain
                     [Amino acid transport and metabolism]; COG2071"
                     /db_xref="CDD:441674"
ORIGIN      
        1 merkplvgit adtnqigaha shtvgdkyva aiadgarala mvlpalgerq svddvldavd
       61 gllftgsysn vephryggep sapgtkhdpa rdattlpllr aaiaagvpvl avcrgfqeln
      121 vvcggtlhqr vhevrgfadh reddaapmdv qygpahvvhl mpggmlhala dgrdevhvns
      181 lhqqgiaqlg aglaveavap dglieavrvv dapafalavq whpewrhahd plssaifraf
      241 gdacrarrqr rpnaaaaala
//
LOCUS       WP_176076541             221 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF799 domain-containing protein [Burkholderia dolosa].
ACCESSION   WP_176076541
VERSION     WP_176076541.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..221
                     /product="DUF799 domain-containing protein"
                     /calculated_mol_wt=23144
     Region          7..221
                     /region_name="COG4380"
                     /note="Uncharacterized conserved protein, DUF799 domain
                     [Function unknown]"
                     /db_xref="CDD:443506"
ORIGIN      
        1 mfktlsfklm svlsivalls acaqpvkrpd ytafkksqpr silvlppine tsdvaatygm
       61 lsqmtlplae sgyyvvpvav mdetfkqngl tnpteiqqts paklreifga daalyskvsq
      121 ygtvyrvlas atvvsasakl vdlrtgdvlw qgrasassde ggnnggggli gmlvtaavkq
      181 iantlmdqsh nvagvtsgrl lsagppngll ygphspkygt d
//
LOCUS       WP_176076563             369 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)/FAD-dependent oxidoreductase [Burkholderia dolosa].
ACCESSION   WP_176076563
VERSION     WP_176076563.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426424
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..369
                     /product="NAD(P)/FAD-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38755
     Region          1..367
                     /region_name="LhgO"
                     /note="L-2-hydroxyglutarate oxidase LhgO [Carbohydrate
                     transport and metabolism]; COG0579"
                     /db_xref="CDD:440344"
ORIGIN      
        1 meqmdcvvig agvvglaiar elaargretl vleaadaigt gtssrnsevi haglyyprgs
       61 lkatscvrgr dllyefcdth hvphrrigkl lvatsaaqvk qlkaiaaraa engvldllpl
      121 trseaqtlep alecvealfs patgivdshq lmlallgdaq rdgavcalks pvesidvlrg
      181 grfvvrtggd apteidaacv vnsaglgaqa larrtrgldp rwvpplylar gnyfglsgra
      241 pfshlvypmp draglgvhlt ldlagqarfg pdvewidtvr ydvdparana fyasirafwp
      301 alpdgalqpa yagirpkvag pgeppadfvv qgaaqhgvrg lvnlfgiesp gltaalalaq
      361 rvadmaayg
//
LOCUS       WP_176076610             279 aa            linear   BCT 11-JAN-2025
DEFINITION  polyphosphate kinase 2 family protein [Burkholderia dolosa].
ACCESSION   WP_176076610
VERSION     WP_176076610.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Motomura,K., Hirota,R., Okada,M., Ikeda,T., Ishida,T. and Kuroda,A.
  TITLE     A new subfamily of polyphosphate kinase 2 (class III PPK2)
            catalyzes both nucleoside monophosphate phosphorylation and
            nucleoside diphosphate phosphorylation
  JOURNAL   Appl Environ Microbiol 80 (8), 2602-2608 (2014)
   PUBMED   24532069
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Sureka,K., Sanyal,S., Basu,J. and Kundu,M.
  TITLE     Polyphosphate kinase 2: a modulator of nucleoside diphosphate
            kinase activity in mycobacteria
  JOURNAL   Mol Microbiol 74 (5), 1187-1197 (2009)
   PUBMED   19843229
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Nocek,B., Kochinyan,S., Proudfoot,M., Brown,G., Evdokimova,E.,
            Osipiuk,J., Edwards,A.M., Savchenko,A., Joachimiak,A. and
            Yakunin,A.F.
  TITLE     Polyphosphate-dependent synthesis of ATP and ADP by the family-2
            polyphosphate kinases in bacteria
  JOURNAL   Proc Natl Acad Sci U S A 105 (46), 17730-17735 (2008)
   PUBMED   19001261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..279
                     /product="polyphosphate kinase 2 family protein"
                     /EC_number="2.7.4.-"
                     /GO_function="GO:0008976 - polyphosphate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016776 - phosphotransferase activity,
                     phosphate group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006797 - polyphosphate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=31527
     Region          7..277
                     /region_name="PPK2_rel_1"
                     /note="polyphosphate:nucleotide phosphotransferase, PPK2
                     family; TIGR03709"
                     /db_xref="CDD:274737"
ORIGIN      
        1 mpkrpslddf rvpygthgke aaaftldafd paakpfssgs keadrerlsa vsaeldvqqe
       61 rlhtqqkkrv llvlqgmdts gkdgtvravf rdvdplgvri vsfkaptpie aahdflwrvh
      121 aqvpaagela ifnrshyedv lvprvlgtlg dkecerryrq irdfetmlae ngttivkcfl
      181 hiskdeqrar lqarvddptk hwkfdiadld arkhwdayqs ayrdalaats aehapwyvvp
      241 adskthrnvm iaelllrtmt dmkleypppk pelegvkir
//
LOCUS       WP_176076628             288 aa            linear   BCT 11-JAN-2025
DEFINITION  patatin-like phospholipase family protein [Burkholderia dolosa].
ACCESSION   WP_176076628
VERSION     WP_176076628.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Six,D.A. and Dennis,E.A.
  TITLE     The expanding superfamily of phospholipase A(2) enzymes:
            classification and characterization
  JOURNAL   Biochim Biophys Acta 1488 (1-2), 1-19 (2000)
   PUBMED   11080672
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448329
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..288
                     /product="patatin-like phospholipase family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=31925
     Region          5..277
                     /region_name="RssA"
                     /note="Predicted acylesterase/phospholipase RssA, containd
                     patatin domain [General function prediction only];
                     COG1752"
                     /db_xref="CDD:441358"
ORIGIN      
        1 mfdqivfagg gnrcwwqagf wdvaqpalal rprviagisa gaatacmlyt rdaawvmryy
       61 eqalrdnrkn aywanlfrre pvfphyqiyr qalldiygep fpklaaapei rigvshvprw
      121 lgarsavaag lvayniekyv rktlhptlgr tlgfrpefvr aqacanvdel adlilqssct
      181 ppftpvlrrg grpvldggmv dnvpvgalda apgdvlvlvt rryprpqmft vahgdqrrly
      241 vqpsskvpis swdytspsqm qhaydlgrrd gehflarvge ltggraaa
//
LOCUS       WP_176076630             204 aa            linear   BCT 11-JAN-2025
DEFINITION  CGNR zinc finger domain-containing protein [Burkholderia dolosa].
ACCESSION   WP_176076630
VERSION     WP_176076630.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Bakolitsa,C., Bateman,A., Jin,K.K., McMullan,D., Krishna,S.S.,
            Miller,M.D., Abdubek,P., Acosta,C., Astakhova,T., Axelrod,H.L.,
            Burra,P., Carlton,D., Chiu,H.J., Clayton,T., Das,D., Deller,M.C.,
            Duan,L., Elias,Y., Feuerhelm,J., Grant,J.C., Grzechnik,A.,
            Grzechnik,S.K., Han,G.W., Jaroszewski,L., Klock,H.E., Knuth,M.W.,
            Kozbial,P., Kumar,A., Marciano,D., Morse,A.T., Murphy,K.D.,
            Nigoghossian,E., Okach,L., Oommachen,S., Paulsen,J., Reyes,R.,
            Rife,C.L., Sefcovic,N., Tien,H., Trame,C.B., Trout,C.V., van den
            Bedem,H., Weekes,D., White,A., Xu,Q., Hodgson,K.O., Wooley,J.,
            Elsliger,M.A., Deacon,A.M., Godzik,A., Lesley,S. and Wilson,I.A.
  TITLE     The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 A
            resolution reveals a new fold (the ABATE domain) and suggests its
            possible role as a transcription regulator
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 10),
            1198-1204 (2010)
   PUBMED   20944211
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475615
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..204
                     /product="CGNR zinc finger domain-containing protein"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22595
     Region          13..204
                     /region_name="COG5516"
                     /note="Uncharacterized conserved protein containing a
                     Zn-ribbon-like motif, possibly RNA-binding [General
                     function prediction only]"
                     /db_xref="CDD:444267"
ORIGIN      
        1 mvtrfeaslh grewtdadfv gghpaldfln tvadtgktrd ddklvdwtav rawaeksgll
       61 apsdlarfar harrdgadel talrgfreda yaaiayltsd arggagaraa drlavairda
      121 igrstfeaad grfawrpdah aasrwidaaa lgfeqllrsd dfarvrqcar ctwffvdrgr
      181 gvgrrwcdmr tcgnrakvea frer
//
LOCUS       WP_176076683             561 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Burkholderia dolosa].
ACCESSION   WP_176076683
VERSION     WP_176076683.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..561
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=61198
     Region          10..539
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mttgrtlege fdyvivgagt agcvlanrlt edpdirvlll eaggkddyhw ihipvgylyc
       61 ignprtdwly ktqpeaalng ralsyprgrv lggcssingm iymrgqredy dgwaqetgda
      121 gwswdsvlpi fkrsedhhag asdahgaggy wrvekqrlrw qilesfaqaa qqtgipatdd
      181 fnrgdnsgvg yfevnqkrgv rwnaskaflr pamtranltv itgahvqrvv fdgrravgve
      241 yrgdgtdyva raraevllts gavnspqlle lsgigdgrrl qalgidvvhd lpgvgenlqd
      301 hlqlrmafrv dgvrtlntls arwwgklmig aqyallqrgp msmapsqlga faksdpddpa
      361 ltrpdleyhv qplslerfge plhrfnafta svchlrptsr gsvhiasadp gaaptiapny
      421 lstdydrhva analrvtrri asapalaryr pqeilpgpry qteaelieaa givgttifhp
      481 vgtcrmgrad daravvdsrl rvrgidglrv vdasvmptit sgntnsptlm iaerasdmir
      541 adrraareat hvrteaaaap v
//
LOCUS       WP_176076684             294 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            dolosa].
ACCESSION   WP_176076684
VERSION     WP_176076684.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 294)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..294
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=31315
     Region          11..293
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 meifgiplpa mlsqlllglv ngsfyailsl glavifglln vinfahgalf mlgamlawmg
       61 lsyfglpywa mlvlaplivg afgiaiersm lrwlykldhl ygllltfglt lvvegvfrsv
      121 ygssgqpydv psqlsgatnl gfmflpnyra wvvvaslavc latwfviekt rlgaylragt
      181 enpklveafg vnvpmmitlt ygfgvalaaf agvlaapviq vsplmgqpmi itvfavvvig
      241 gmgsilgsiv tglmlgvieg ftrvfypeas atvvfvimai vllirpaglf gkek
//
LOCUS       WP_176076704             476 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Burkholderia dolosa].
ACCESSION   WP_176076704
VERSION     WP_176076704.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..476
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=49641
     Region          36..476
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mqngdgnaah gapraaapad dvledalaaa lgdalvtrsa aiepryftay nepagvrpra
       61 lvrptsvvdv srtlalctrf gqpvvpqggl tglaraaval ggevvlsmer fagiealdra
      121 agtitvragt plqavqdaad aagftfgvdl gargscqigg mlatnaggtr airygmmreq
      181 vlgleavlad gtivssmnrm lknnagydlk qlfigsegtl gvitravlrl hpklaapata
      241 lcrvrdydav aalwnrmral peivsfeamw psfyeyvarh tpdvvapfag dggfavliec
      301 atsapggdar haletalaaa fdagvvddaa latserqare lwtlreglai dalphlinyd
      361 vslptgelga faerceaalr aswpdivcvf fghvgdgnvh igvslagmrd tegdaidrcv
      421 yatvrdmggs vsaehgigal kraylahtrs eaeidlmrrv kaaldpagil npgkvl
//
LOCUS       WP_176076730             216 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia dolosa].
ACCESSION   WP_176076730
VERSION     WP_176076730.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..216
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24082
     Region          61..147
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mhdsrhsnll advaayysar laehgqtarg vdwngedgqr lrfaqltkiv apgadgfsvn
       61 dvgcgygalv dfldehaggr hhtyagndis aemidaarqr yrdranvsfd vgdtpraisd
      121 ytiasgifnv hrghdadawl dyihatldvl hdtsragfaf ncltsysdpp hmrperlyya
      181 dpcalfdrck rrysrhvall hdyglyefti lvrkdg
//
LOCUS       WP_176076764             443 aa            linear   BCT 11-JAN-2025
DEFINITION  carotenoid oxygenase family protein [Burkholderia dolosa].
ACCESSION   WP_176076764
VERSION     WP_176076764.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Poliakov,E., Uppal,S., Rogozin,I.B., Gentleman,S. and Redmond,T.M.
  TITLE     Evolutionary aspects and enzymology of metazoan carotenoid cleavage
            oxygenases
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1865 (11), 158665 (2020)
   PUBMED   32061750
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Sui,X., Kiser,P.D., Lintig,Jv. and Palczewski,K.
  TITLE     Structural basis of carotenoid cleavage: from bacteria to mammals
  JOURNAL   Arch Biochem Biophys 539 (2), 203-213 (2013)
   PUBMED   23827316
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Kloer,D.P. and Schulz,G.E.
  TITLE     Structural and biological aspects of carotenoid cleavage
  JOURNAL   Cell Mol Life Sci 63 (19-20), 2291-2303 (2006)
   PUBMED   16909205
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Wyss,A.
  TITLE     Carotene oxygenases: a new family of double bond cleavage enzymes
  JOURNAL   J Nutr 134 (1), 246S-250S (2004)
   PUBMED   14704328
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007818
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..443
                     /product="carotenoid oxygenase family protein"
                     /EC_number="1.13.11.-"
                     /GO_function="GO:0016702 - oxidoreductase activity, acting
                     on single donors with incorporation of molecular oxygen,
                     incorporation of two atoms of oxygen [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006720 - isoprenoid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=48870
     Region          10..439
                     /region_name="COG3670"
                     /note="Carotenoid cleavage dioxygenase or a related enzyme
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]"
                     /db_xref="CDD:442887"
ORIGIN      
        1 mttfdlnsga lapvadevel vdlrvsgtip pelhgtllrn gpnppggrfd gndvlswwpe
       61 aamlhaiafe rgratayrnr wirtrrwaav hapehasrlp dtnpnvsvlr hagellalae
      121 ggapiaitta ldslgaparh aalggamtah pkldpatgel mlfradwrep wlrygvadaq
      181 gvqrvdveva vrapsmmhdl aitetrslll dlnvgydfam lkhghrmplr whdergarig
      241 viarhggavr wfdiepcfiq hvvnaydcde scivldavry pwflrldprt grfddnplge
      301 lwryvidtah glvdegplad ggielprine srtgrryryl yaveqpngve mrgvmrfdhv
      361 rgtttryavp hgdqngepvf vprpggvded dgwllvvvyr aatdtsdvvi ldahaidarp
      421 vatvhlprrv pagfhgawvp gep
//
LOCUS       WP_176076906             439 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia dolosa].
ACCESSION   WP_176076906
VERSION     WP_176076906.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..439
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=45961
     Region          22..420
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(32..33,36..37,40,72,122..123,125..127,130,150,
                     153..154,157,245,248..249,252..254,257,285,289,347..348,
                     352,356,372,375..376,379..380,383)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 msenhsvpna pprirrgqri alallmvsgi vnyldrgtla vassairgdl glslgqmgll
       61 lsafswsyal cqfpvgglvd rigprrllgi glivwslaqa agglvstfgw fivarivlgi
      121 geapqfpsaa rvvsnwfplr argtptgifn aasplgtala plllsvlvat ldwrwafiat
      181 gaagvvvaav wfalyrdpvr aqltateray ldadadnvva apkltfadwr glfshgttwg
      241 mligffgsvy lnwvyltwlp gyltmerhms lirtgfaasv pflcgfvgsl lagwlsdlvt
      301 rrsrspvvsr rnavvvamlg mvaftvpaal vqsntlalac isvviflana asacswalat
      361 aaappsrvas lgaiqnfggf iggalapvlt gviaqrwsfv palltaaaia fagamaylll
      421 vrkpipeqsa saapgalpa
//
LOCUS       WP_176076937             311 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Burkholderia
            dolosa].
ACCESSION   WP_176076937
VERSION     WP_176076937.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..311
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=31913
     Region          1..309
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mhtfaldafn glsyglllfm lsagltlifs vqgvlnfaha sfymlgayvg ygiaaqagfw
       61 calvfaplav gligagcerw llrrvqargh tsellltfgl ayligeaakl vwglaplpap
      121 vpawfdgapv vafgvalpry rlfmmtmsat mlialgvllr vsrvglvvra althraavea
      181 lgydvprvmt glfgagtala alagvigapl aviepalaem vgsvvfavvv igglgslgga
      241 fvaslavgfa qtfaassdts lrelaqwagv alpdgvgavs vaqlaplvpy lllvavlvar
      301 prglfgerad a
//
LOCUS       WP_176076946             157 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Burkholderia dolosa].
ACCESSION   WP_176076946
VERSION     WP_176076946.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 157)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001596
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..157
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=17257
     Region          1..135
                     /region_name="MutT"
                     /note="8-oxo-dGTP pyrophosphatase MutT and related
                     house-cleaning NTP pyrophosphohydrolases, NUDIX family
                     [Defense mechanisms]; COG0494"
                     /db_xref="CDD:440260"
ORIGIN      
        1 mkkrggaprt vscgvvilda agrvflahat dtthwdipkg qgepgetpad aalrelreet
       61 gielaatrlv dlgrfayrhd kdlhlfavrv aqdeidparc tctslfpsrr dgspipemda
      121 yrwtepdeid ayasrslarl fhttlplael hrrlpga
//
LOCUS       WP_176076997             539 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA synthetase [Burkholderia dolosa].
ACCESSION   WP_176076997
VERSION     WP_176076997.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..539
                     /product="acyl-CoA synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016405 - CoA-ligase activity [Evidence
                     IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=57722
     Region          48..538
                     /region_name="MACS_like_3"
                     /note="Uncharacterized subfamily of medium-chain acyl-CoA
                     synthetase (MACS); cd05971"
                     /db_xref="CDD:341275"
     Site            order(111,241..243,267,287,289,293,314..317,336..341,
                     344..345,361,421,433,436,442,444..447,476,505,510..511,
                     513,515)
                     /site_type="active"
                     /db_xref="CDD:341275"
     Site            order(192,195..200,202..203)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341275"
     Site            order(237,289..290,293,314,444..446,505,511)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341275"
     Site            order(314..317,336..341,361,421,433,436,442,447)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341275"
ORIGIN      
        1 mlpaadryed llsrfawdvp arynigvdvc dkwadgsgrv alihetaqgd vsrftfddlr
       61 nasnrlansf sraglrrgdr igiflaqgpe tavahlaayk lgaiavplft lfgvdaleyr
      121 lanseaaalv tdaagyakia plrarlpalh tcycigddap dapgvlryda alaaeapdft
      181 padtaaddpa liiytsgttg kpkgalhahr vllghlpgve msqqcfprda rlfwtpadwa
      241 wigglldvll pswhhgvpvl arrfekfdgd aafalmarhg vthaflppta lklmravpkp
      301 reryalslks vasggeslgt eltawgrdal gvtinefygq tecnmvlssc aalfdaqpga
      361 igkavpghtv aivddngtpl ppgvegriai rrpdpvmfie ywrnpaatrd kfagdylltg
      421 dtgivdadgf vrfvgrdddv itsagyrigp gpiedcllth pavrmaavvg vpdatrteiv
      481 kafvvlnpgh vgddalvral qahvrtrlaa heypraiafv dslpmtatgk ivrralrda
//
LOCUS       WP_176077057             397 aa            linear   BCT 11-JAN-2025
DEFINITION  ammonium transporter [Burkholderia dolosa].
ACCESSION   WP_176077057
VERSION     WP_176077057.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Williamson,G., Tamburrino,G., Bizior,A., Boeckstaens,M., Dias
            Mirandela,G., Bage,M.G., Pisliakov,A., Ives,C.M., Terras,E.,
            Hoskisson,P.A., Marini,A.M., Zachariae,U. and Javelle,A.
  TITLE     A two-lane mechanism for selective biological ammonium transport
  JOURNAL   Elife 9, e57183 (2020)
   PUBMED   32662768
  REMARK    Erratum:[Elife. 2022 Jan 27;11:e77377. doi: 10.7554/eLife.77377.
            PMID: 35084334]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Mirandela,G.D., Tamburrino,G., Hoskisson,P.A., Zachariae,U. and
            Javelle,A.
  TITLE     The lipid environment determines the activity of the Escherichia
            coli ammonium transporter AmtB
  JOURNAL   FASEB J 33 (2), 1989-1999 (2019)
   PUBMED   30211659
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..397
                     /product="ammonium transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008519 - ammonium channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0072488 - ammonium transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41285
     Region          1..395
                     /region_name="AmtB"
                     /note="Ammonia channel protein AmtB [Inorganic ion
                     transport and metabolism]; COG0004"
                     /db_xref="CDD:439775"
ORIGIN      
        1 mdglksgvdt lflligavmv lamhagfafl elgtvrkknq vnalvkilvd fsvstlayfl
       61 vgytiaygve ffddigtlsq hsgyalvrff flltfaaaip aivsggiaer akfnpqlvat
      121 liivgfiypf fegiawnerf gvqawlahaf gapfhdfags vvvhafggwv alpavlllga
      181 rhgryakdgr iaahppsnip flalgawvla vgwfgfnvms aqtldkisgl vavnslmamv
      241 ggtlaawlag rndpgftyng plaglvavca gsdvmhpiga lvtgaaagal fvamftcvqn
      301 rwriddvlgv wplhgmcgal gglaagvfgl palgglggvs flsqlvgtlg giaiataggt
      361 lvygalkatv glrldreaef dgadlsihri satperd
//
LOCUS       WP_176077064             182 aa            linear   BCT 11-JAN-2025
DEFINITION  peroxiredoxin [Burkholderia dolosa].
ACCESSION   WP_176077064
VERSION     WP_176077064.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Jeong,W., Cha,M.K. and Kim,I.H.
  TITLE     Thioredoxin-dependent hydroperoxide peroxidase activity of
            bacterioferritin comigratory protein (BCP) as a new member of the
            thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide
            peroxidase C (AhpC) family
  JOURNAL   J Biol Chem 275 (4), 2924-2930 (2000)
   PUBMED   10644761
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..182
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.24"
                     /GO_function="GO:0008379 - thioredoxin peroxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=19520
     Region          29..170
                     /region_name="PRX_BCP"
                     /note="Peroxiredoxin (PRX) family, Bacterioferritin
                     comigratory protein (BCP) subfamily; composed of
                     thioredoxin-dependent thiol peroxidases, widely expressed
                     in pathogenic bacteria, that protect cells against
                     toxicity from reactive oxygen species by reducing...;
                     cd03017"
                     /db_xref="CDD:239315"
     Site            order(68,71,141)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239315"
ORIGIN      
        1 mkrklwmtga ammlaghali ahaqlkpgaa apdfttqasl ggktytysla dalkhgpvvl
       61 yfypaaftkg ctieahafad avdrykayga tvigvsadni dtltkfsvse crskfpvaad
      121 pgakiireyd aklpaldran rvsyvispeg kilyeytsls pdkhventla avkawadahp
      181 rq
//
LOCUS       WP_176077097             293 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Burkholderia dolosa].
ACCESSION   WP_176077097
VERSION     WP_176077097.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..293
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31529
     Region          13..270
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mnepikallk phvrdignlq vrrtlpalaa rlvgpfiffd hmgpaalppg tgldvrphph
       61 iglatvtylf dgailhrdsl gsrqeivpgd vnwmtagrgi vhsertpdaq rasghtvhgi
      121 qtwvalprah etvepsfehh aadtlpkrne ngvsltviag dafglrspvt tfsrtlyvaa
      181 efaaggrvel dasheeravy vvdgdlaidg tpvpaermav lapgatvtla sgsgaramll
      241 ggdridgerf iewnfvassr daierakhaw trqemgtvpg etewiplpes rpr
//
LOCUS       WP_176077127             304 aa            linear   BCT 11-JAN-2025
DEFINITION  sterol desaturase family protein [Burkholderia dolosa].
ACCESSION   WP_176077127
VERSION     WP_176077127.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459499
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..304
                     /product="sterol desaturase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006629 - lipid metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=35029
     Region          85..242
                     /region_name="ERG3"
                     /note="Sterol desaturase/sphingolipid hydroxylase, fatty
                     acid hydroxylase superfamily [Lipid transport and
                     metabolism]; COG3000"
                     /db_xref="CDD:442238"
ORIGIN      
        1 mrfdvellll alapvfllci gweawhlhrt raqdrvyawr dtlcnatlal mhqgadklaw
       61 vfvipvyayc yrhyrvftwd dgwlsfavlf vcqdllyyvf hrashrvrwl waahvvhhss
      121 ermnfstafr qslmypvagm wvfwlplavl gfppqqivgi vlinlafqff vhtqaigklg
      181 wleyvfntps ihrahharnp ryidrnyagv lviwdrlfgs yvdespddpp qygiveplgs
      241 nnplvatfhe wvsmaadalr vegtrnklra ifgppewasa yhaqiaeaan hdprtaplaa
      301 vrdq
//
LOCUS       WP_176077138             234 aa            linear   BCT 11-JAN-2025
DEFINITION  TerC family protein [Burkholderia dolosa].
ACCESSION   WP_176077138
VERSION     WP_176077138.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023488
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..234
                     /product="TerC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=24582
     Region          12..191
                     /region_name="R_switched_YjbE"
                     /note="integral membrane protein, YjbE family; TIGR03717"
                     /db_xref="CDD:163429"
ORIGIN      
        1 mlefltslhw gavlqiviid illggdnavv ialacrnlpa nqrlrgvvwg tagaillrvv
       61 liafavvlld vpflkfgggl lllwigvklm apaadahdnv kpadrlweav ktiviadavm
      121 sldnviaiag aaeqadpshr lalvifglvv svpiivwgst lvlklldrfp ivvtlgagll
      181 gwiagglmvr dpvgdrwpvl dtpaaiygas iagallvvvv gyllrnrraa psth
//
LOCUS       WP_176077176             131 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA thioesterase [Burkholderia dolosa].
ACCESSION   WP_176077176
VERSION     WP_176077176.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..131
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=14064
     Region          7..131
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mtestlelpq kqpalrvvpq phdanvhgdv fggwimsqvd iagsipasqr angrvatvav
       61 nsfvfkqpvf vgdllsfyat itrtgntsvt vdvevyaqrm rlmgevvkvt eatltyvatg
      121 adrkprplpp l
//
LOCUS       WP_176077187             109 aa            linear   BCT 11-JAN-2025
DEFINITION  FmdB family zinc ribbon protein [Burkholderia dolosa].
ACCESSION   WP_176077187
VERSION     WP_176077187.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Isernia,C., Malgieri,G., Russo,L., D'Abrosca,G., Baglivo,I.,
            Pedone,P.V. and Fattorusso,R.
  TITLE     Zinc Fingers
  JOURNAL   Met Ions Life Sci 20 (2020)
   PUBMED   32851833
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006375
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..109
                     /product="FmdB family zinc ribbon protein"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=10505
     Region          1..74
                     /region_name="COG2331"
                     /note="Predicted nucleic acid-binding protein, contains
                     Zn-ribbon domain [General function prediction only]"
                     /db_xref="CDD:441902"
ORIGIN      
        1 mpiyayrcea cgfakdvlqk msdaplsqcp ecgkdafrkq vtaagfqlkg sgwyvtdfrg
       61 gsggssapat assgdaapaa tpaaptasgs estttsaapa paaapaagg
//
LOCUS       WP_176077244             259 aa            linear   BCT 11-JAN-2025
DEFINITION  ComF family protein [Burkholderia dolosa].
ACCESSION   WP_176077244
VERSION     WP_176077244.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Solomon,J.M. and Grossman,A.D.
  TITLE     Who's competent and when: regulation of natural genetic competence
            in bacteria
  JOURNAL   Trends Genet 12 (4), 150-155 (1996)
   PUBMED   8901420
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Londono-Vallejo,J.A. and Dubnau,D.
  TITLE     comF, a Bacillus subtilis late competence locus, encodes a protein
            similar to ATP-dependent RNA/DNA helicases
  JOURNAL   Mol Microbiol 9 (1), 119-131 (1993)
   PUBMED   8412657
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437133
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..259
                     /product="ComF family protein"
                     /GO_process="GO:0030420 - establishment of competence for
                     transformation [Evidence IEA]"
                     /calculated_mol_wt=27161
     Region          84..229
                     /region_name="ComFC"
                     /note="DNA utilization protein ComFC/GntX, contains
                     phosphoribosyltransferase domain [General function
                     prediction only]; COG1040"
                     /db_xref="CDD:440662"
ORIGIN      
        1 mnrrsvprtm rvvlsharml aaravtialp nrcamcgnls haaicaacda aywnearlrc
       61 dacavplgsn rrrspaagaa ayrcdacrat appfdatlal adyrapldgl arglkfharl
      121 algaefaarl arliddtpga ggfdvvapvp lshkrlvarg ynqawaiarp larrlgvrae
      181 aallarviet apqsrldrra rrdnvtaafa vagdvagrhv alvddvmtsg atlaaaaqal
      241 kaagaarvtn lvalrtard
//
LOCUS       WP_176077254             378 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia dolosa].
ACCESSION   WP_176077254
VERSION     WP_176077254.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..378
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=40172
     Region          1..373
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mdfqhtedrr mladtlnrfi aeqypfavrd riaqsadgfd ramwrrfael gaigalfdea
       61 dggfggagfd iavvfecigr glvvepflga llagralsla ggdahrakla alidgsasaa
      121 fahdepgshy elthvrtrae ragdgwvltg akgvvdqaaq aaffvasarv sgdaddaagi
      181 glfvvpadap gvslrdyrki dggraaevrf ervalpadaa lgdrdgdaga allervlgyg
      241 llalsaealg amdvakdatl eylrtrrqfg apigsfqalq hrmadlliei eqarsavina
      301 aaqldadrvv reralaaaky sigrigtlva edsiqlhggi gmtwelplsh yakrlvmidh
      361 qlgdedhhla ryialskp
//
LOCUS       WP_176077339             259 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Burkholderia dolosa].
ACCESSION   WP_176077339
VERSION     WP_176077339.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..259
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=28895
     Region          2..219
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mnvlivyahp eprslngalr dfavahlqaa ghtvqvsdly amswkpalda hdmierspda
       61 rfdpaldskr ayengtqred iaceqdklkw adtvilqfpl wwfsmpaimk gwvervyayg
      121 faygvgehsd rhwgdrygeg slagkramvi vttggweshy sargingpid dvlfpihhgi
      181 lyypgfdvlp pfvvyraqrm dearfaetra algkrldeld ttppipfrrq nagdyeipal
      241 tlkpdiapgk vgfaahlaa
//
LOCUS       WP_176077348             558 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Burkholderia dolosa].
ACCESSION   WP_176077348
VERSION     WP_176077348.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..558
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=60557
     Region          22..556
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 matvtpratn esvhptigag rltlgnrill sfgvlfvlml vtagvsyerl raingeavsi
       61 erdslpgvyl aaslrgavne sftllqqatf vdtdpesaqr dlakipdalk eieslstdyq
      121 namfrdddrq rfltfrsayd ryvpqlneam qkhrvsrdda vaayakvvpl wtevvrdant
      181 lvqenrkfad qsakliresv qatevvlata laivllsalv lgyalyravt vpmarlvevh
      241 damrtgnlth rldlrrrdef gtletgfnrm adeltelvsr aqqsslqvtt svaeiaatsr
      301 eqqataneta attteigats reifatsrdl lrtmnevasv aeqsatlagv sqsgltrmge
      361 tmrsvmdaag svnaklailn ekalninqvv atitkvadqt nllslnaaie aekageygrg
      421 favvateirr ladqtavatf dieqtvkeiq savsagvmgm dkfseevrrg mldvqqvggq
      481 lsqiiaevqt laprfqmvne gmqtqangae qitqalsqls eaaqqtaesl rqssqaiddl
      541 tlvanqlrts vsrfkvda
//
LOCUS       WP_176077389             232 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatase PAP2 family protein [Burkholderia dolosa].
ACCESSION   WP_176077389
VERSION     WP_176077389.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Hemrika,W., Renirie,R., Dekker,H.L., Barnett,P. and Wever,R.
  TITLE     From phosphatases to vanadium peroxidases: a similar architecture
            of the active site
  JOURNAL   Proc Natl Acad Sci U S A 94 (6), 2145-2149 (1997)
   PUBMED   9122162
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 17575897
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..232
                     /product="phosphatase PAP2 family protein"
                     /EC_number="3.1.3.-"
                     /GO_function="GO:0016791 - phosphatase activity [Evidence
                     IEA]"
                     /GO_process="GO:0008610 - lipid biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=24364
     Region          1..149
                     /region_name="PgpB"
                     /note="Membrane-associated phospholipid phosphatase [Lipid
                     transport and metabolism]; COG0671"
                     /db_xref="CDD:440435"
     Region          <78..148
                     /region_name="PAP2_like"
                     /note="PAP2_like proteins, a super-family of histidine
                     phosphatases and vanadium haloperoxidases, includes type 2
                     phosphatidic acid phosphatase or lipid phosphate
                     phosphatase (LPP), Glucose-6-phosphatase,
                     Phosphatidylglycerophosphatase B and bacterial acid...;
                     cd01610"
                     /db_xref="CDD:238813"
ORIGIN      
        1 mfdlpphlwi titafggagl tlplavtiav wlalgyswqr aaawlgvlaa aigvvaltki
       61 aflgwgigir awdftgfsgh amlstsvypv aiflmlirtr tpirvagial glaagvavgv
      121 srvaldahsp sesitgcivg alaalafiag swravphrws apavvaslal vtvglhgitv
      181 pshrwvtkva lhlsgherpf vrarwkanpn yrpasqpssl qrtdstphtl ha
//
LOCUS       WP_176077411             138 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Burkholderia dolosa].
ACCESSION   WP_176077411
VERSION     WP_176077411.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..138
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=13797
     Region          <4..138
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mpgtcdirag ddrkvvvlpa vadvslstvg atsgrtalsv avqncvgvkq vkfsfsgapd
       61 dnmpvafrnt gtakgvavrl aeagddgtia adgtassive pvtndaasvr lhaeyigttg
      121 rptagsvssl atmnidyq
//
LOCUS       WP_176077448             488 aa            linear   BCT 11-JAN-2025
DEFINITION  flippase [Burkholderia dolosa].
ACCESSION   WP_176077448
VERSION     WP_176077448.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Samuel,G. and Reeves,P.
  TITLE     Biosynthesis of O-antigens: genes and pathways involved in
            nucleotide sugar precursor synthesis and O-antigen assembly
  JOURNAL   Carbohydr Res 338 (23), 2503-2519 (2003)
   PUBMED   14670712
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Liu,D., Cole,R.A. and Reeves,P.R.
  TITLE     An O-antigen processing function for Wzx (RfbX): a promising
            candidate for O-unit flippase
  JOURNAL   J Bacteriol 178 (7), 2102-2107 (1996)
   PUBMED   8606190
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10192054
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..488
                     /product="flippase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0140327 - flippase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52195
     Region          5..395
                     /region_name="MATE_Wzx_like"
                     /note="Wzx, a subfamily of the multidrug and toxic
                     compound extrusion (MATE)-like proteins; cd13128"
                     /db_xref="CDD:240533"
ORIGIN      
        1 mdkrilknvs infiglilpt fvslvtvpay ihalgveryg vvslvwtlig yfgildlgms
       61 maaqnhiska laggdaaesa rvfwsafwln lgtgivggll iyfgafvyta yftkvsaamq
      121 hevylalpwl alaiplanvs wvfagainga erfgvfntnq tigtflfqll plgaawwiap
      181 nlqtvlaaav varliaaaml ghasikvlgi tridppqwrt akglfnfggw mliasttsmi
      241 adtldrvmlg agmgakfvty ytvpqnlvtr lnmlpnalvr tlfprlsavg rdhadtlarq
      301 sleflngvft pvgivaifal apfltlwvga dlaahsapvg rllvigvwlv gqagvtrili
      361 qsqvnparaa laglvqmpff vgglwlgihh fgligaaavv avralvdygv llylsairmr
      421 aivldmlahl afllaslfla hawpglgesi alcavvlvln vawsltmtpg lralvrglfv
      481 rlnarktv
//
LOCUS       WP_176077579             277 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia dolosa].
ACCESSION   WP_176077579
VERSION     WP_176077579.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..277
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30264
     Region          3..135
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          156..275
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 msyktllvhl ddsdrcatrv alaldlagrw nahliglyvv cqdlleplrr pdeplklavy
       61 erlcdqrrke aeekflaaae ragrtvewqa psgvaidaal qharhadlll lgqedpndrm
      121 thvarhfved vvmgsgrpai vvpyagdlrt fgenaliawd ggreaarams dalpllarar
      181 fvnvetivhg hpdpdrtpag vdvaaylerh giraafsstp hdpaagvgvt llnritdlha
      241 dllvmglysh armhervlgg atrtilesmt vpvllsh
//
LOCUS       WP_176077659             476 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome ubiquinol oxidase subunit I [Burkholderia dolosa].
ACCESSION   WP_176077659
VERSION     WP_176077659.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Borisov,V.B.
  TITLE     Generation of Membrane Potential by Cytochrome bd
  JOURNAL   Biochemistry (Mosc) 88 (10), 1504-1512 (2023)
   PUBMED   38105020
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003361
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..476
                     /product="cytochrome ubiquinol oxidase subunit I"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0070069 - cytochrome complex [Evidence
                     IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=51920
     Region          4..443
                     /region_name="AppC"
                     /note="Cytochrome bd-type quinol oxidase, subunit 1
                     [Energy production and conversion]; COG1271"
                     /db_xref="CDD:440882"
ORIGIN      
        1 meidalllsr lqfawvialh illpaftvgl scyiatlevl hwatgrdvyq rlsafwlrif
       61 avsfgmgvvs givmpfqfgt nwsrfvaats nvvggfmaye vltafflesa flgvllfgrn
      121 rvprwahals avmvalgtll ssfwilavns wmqtptgyrl vdgrfypdsm lsillspsfp
      181 yrlthtvtaf lvttafvvlg vgahyllqrr aedesrvmvk mgllfltiav pvqialgdah
      241 glntlahqpa klaameglwe tgrgvratlf alpdernetn rfevsipklg slylthdwng
      301 lvhglkdwpr derpsvpivf fafhlmvglg vvmlaivvrg ltlwrgrrly arrgwlatcr
      361 aaipigfvav lagwttteag rqpwtvyglm rtadsvtpsl ttadvalsla lyvvsyvaif
      421 gsgfvllrrl vrigpaapar phgvapgada sarsarplsa vsgsgaaqpe anddrt
//
LOCUS       WP_176077681             351 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Burkholderia dolosa].
ACCESSION   WP_176077681
VERSION     WP_176077681.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..351
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37681
     Region          22..334
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mpfsfltapr rtrararral vasltaalaf agvglpqaah aegririaeq fgvvylmlnv
       61 ardqqlieke grkagvdikv dwvrlsggaa vndallsgai dvagagvgpl ltvwdrtrgr
      121 qnvkgvaslg nfpyylvstn pnvktiadls akdriavpav gvsvqsrvlq yaaakqwgdk
      181 qfdkldaltq aiphpdataa ilanssvitg hfgnppfqdq elagnpnahv vlssydvlgg
      241 pssatvlyat ekfrddnpkt yrafvaalad aarqiaadpe raadtyirvn gskidralll
      301 kilrnpqvqf ktapqntlrl aqfmyrtgai rnepkswrdy ffddpatagg s
//
LOCUS       WP_176077682             321 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia dolosa].
ACCESSION   WP_176077682
VERSION     WP_176077682.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..321
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=34890
     Region          44..293
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mnatsprtwl ppfsarerap agadaapdar givrpatdrp hsdatserll aidrvsleyr
       61 sgarivrath qvsfdvygsd rfvllgpsgc gkstllkaia gfiepvsgsi aldgrpvrgp
      121 gpdrivvfqe fdqlppwktv venvafplra aaklpraear eralhyldkv glrafadayp
      181 htlsggmkqr vaiaralamq prvllmdepf aaldaltrrk mqeellrlwd darftllfvt
      241 hsieealvvg nrilllsahp grvraelnsh qhsladagss gfrdsvarih rllfdtdadr
      301 dtataadada agarqaeera s
//
LOCUS       WP_176077690             239 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176077690
VERSION     WP_176077690.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..239
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27556
     Region          30..171
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mtetkhntap rkrsttadds agtsgrrltp earerqivek avehfathgf sgstrelarq
       61 igvtqpllyr yfpskealid rvydevytwn pdwekliadr amplqqrlva fyrsyaqtil
      121 rrewirtfif aglsregint rylsrlrerv flpvlrelrh eydiatpase aqrnaeieli
      181 wslhasifyl gvrkwvyglp vpddldaeie rlvdaflngt pavlkrvaad tpakprrrg
//
LOCUS       WP_176077685             731 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Burkholderia dolosa].
ACCESSION   WP_176077685
VERSION     WP_176077685.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..731
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79343
     Region          13..731
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mgkgtnavrh viaiaaggal caasggahaq ttpsageaat padaraatlp kidvtagagk
       61 asvglvgrrt aigtktdtpv adipqtvniv taqqiemtga tdlnqalryv pgfatfgads
      121 rtdwyaalrg ftptlyvdgv papntavian wrvdpymidg igvlrgpssv lygagepgat
      181 vdvqtkradg ervreagvqi gnyarkqtml dvgdtldpdg ryayrfvgva rdgnawtgph
      241 adrrvalaps frwrpsadts ltfsatflqd hgdissnflp asgtvlpnpn gglsqdiymg
      301 dptfndyrkk qwslgytleh rvnaiwslrq elrwsrllld datvfgnglv prsttnmmrf
      361 aglfqldysr ldvdhraqar fgmgplehtl llgvqydrqt ttnsvwlala psldlyrpvy
      421 rpvtaaifsg ptslghieqf tamntfgaya qdqirwhrwt ltfggredfv nahfddrtag
      481 mhtqqdvsaf ssrvgftyea dggwtpyvgy stsfdpvigv rmfggglpqp trgkqieagl
      541 rwqppgknlm lsaavyridq thvvtpapsn ldptgtssvq tgevrsrgie lnavgkvtre
      601 lsvvasyvyq dvknvkanda slnhwpvavp lprqmaslwa dwtwrdgtfa gfgigagvry
      661 qsalagapdn slkvpgytly dlamhydtrh wrfalnvanl fdrrevsgcq sytvcvfgne
      721 rtvtasakyn w
//
LOCUS       WP_176077708             302 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176077708
VERSION     WP_176077708.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33107
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..289
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,219..224,
                     230..231,233..234)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mklsfealea ldaidrtgtf aeaaellhrv psaltylvqk lesdlgvvlf drsgrraklt
       61 hagrvvveeg rrllraaeql emkaqraqqg wetevricid eilpfdalwp yvhqfyalem
      121 dtrlrlstev lggtwdalis rradlvvgaa geppelpniv arpigslkhv faiapthpla
      181 alpeplsmas vveyrgavis dtsrelqpqs vaidahqpyl avptlaakld aqceglavgt
      241 lpeciaarai aegklvarev tgmrdtthcy lawrgdeagr alnwwveqld rpdlvdcfta
      301 ld
//
LOCUS       WP_176077713             158 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia dolosa].
ACCESSION   WP_176077713
VERSION     WP_176077713.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..158
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=17521
     Region          1..141
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mstsivvgis enstmsifsk aldiarsrda riiavhvfdc pipcrarldy cnwesmiaae
       61 rargwmtler alarfdngvp avegrmlmrg ttgstvgrdi asiceasdag lvilgsrrqg
      121 wwrfldedva rnvrrhtstp vqivdvafdd arprehrs
//
LOCUS       WP_176077719             927 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia dolosa].
ACCESSION   WP_176077719
VERSION     WP_176077719.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 927)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 927)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..927
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..927
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=101293
     Region          24..834
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mvvkppalge lkfrelydai hrgllqrnrl lkldtplgqn aliplrargt arigrdynwt
       61 ldvaslrddt allslmhqpv tlwiqqatap ftdsiyrpih gfvhrvgylg gdgglstyql
      121 efssalvflg gtrndegwle qtaqdivsdl lnrypqlqgr frfnlnrepa vrswcrqset
      181 dlhffhrlle degwycywth epvrngetpk ttlvivdqva alpdakpvdf argagngeav
      241 ngfthwaamq tmqslryess sfdykrpksr fqadsalvat symlddgrrq aqhpiptvpm
      301 tvyeptaygy pdsdsgaara rrrvqgwdar arryfggggl rwldagsrfv lndhprhper
      361 ddadrtflvv earwfiennv pigqplaefp lslratlaqq qavhgarfat pshaedgtag
      421 ffmleveaqd arveyrsple hpkpamsieh aivvtqegie awsnernqvr vhfawdrknp
      481 dgafssspll ssmqadtgng ygavhvprag ewvlvgywgn dcdkpfilgr vnggttpapw
      541 htnvllsgfr srgfgntgay nafvhddath qggtrlisyt gksyaalaqg yliqqdgntr
      601 grylgqgfvl hadeygavra skglsisthp kayddeqlsv dearaqlqka gmlveslssa
      661 sttaqaeslq aaqdalkdlt tamqhavsgq tsggvtaggg igsangfakp aiviatpadf
      721 aavadrsahv vaegevnmis ggntqlasgk sliaaaaeki slfvqkagmk lfaakgpiev
      781 sahtdeikln sakdtslfsk krivleatde lilkcggsyl rltkegiedg trgartiksa
      841 sfsrqgpssv aeymnslpsa kfndpyvlrd ritgevlknh pyelirgdgt rltgvtdelg
      901 hvaeqksedi eklavralrp sptgpai
//
LOCUS       WP_176077776             107 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Burkholderia dolosa].
ACCESSION   WP_176077776
VERSION     WP_176077776.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 107)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 107)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 107)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008682
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..107
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=11067
     Region          23..107
                     /region_name="CytC552"
                     /note="Cytochrome c551/c552 [Energy production and
                     conversion]; COG4654"
                     /db_xref="CDD:443692"
ORIGIN      
        1 mkqtilrall atllagvmaa ahaqadglal aqrkncmach avgkplmgps fhdiagryas
       61 rpdaadylaq sivkgsvgvw gsvpmpantq ltgaeartla qwvlslr
//
LOCUS       WP_176077817             455 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia dolosa].
ACCESSION   WP_176077817
VERSION     WP_176077817.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..455
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46914
     Region          19..447
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(26..27,30..31,34,66,116..117,119..121,124,144,
                     147..148,151,273,276..277,280..282,285,313,317,369..370,
                     374,378,394,397..398,401..402,405)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mnadtglplp qrywaivcva lgitlavldg aianvalpti ardlhasdaa siwivnayql
       61 avtitllpla slgervgyrr iyiaglvlft aaslgcalag slpmlalmrv iqgfgaagim
      121 svnaalvrmi ypssmlgrgl sinamvvals saigptvasa ilsfaswpwl favnvpigia
      181 avlgsiralp anplhdapyd ftsalmnacv fgllitavdg lghgesrayv aaelfvavvv
      241 gyffvkrqlt qpapllpvdl mripmfalsi ctsiasftsq mlafvalpfw lqnslgfsqv
      301 dtglymtpwp lvivfaapla gvlsdrysag ilggiglalf aagllslati gahpgtvdiv
      361 wrmalcgagf glfqspnnra mlssaprers ggaggmlsta rltgqtlgaa lvalifglap
      421 drgptialyv atafaavaal vsmlriaspr pdaaa
//
LOCUS       WP_176077942             226 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia dolosa].
ACCESSION   WP_176077942
VERSION     WP_176077942.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10163224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..226
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22697
     Region          123..224
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(126..127,160..161,164,168..169,172,214,218)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mnklalalal satalaacst asgptysase lqprdgvrtf qvdchgllsg pqtcmkaark
       61 icgdqpvrva dsaralrdga dpatlvfqcg aapaepasaa epapaaaaap aavehvnlag
      121 dalfatgaat ltpaarasld kllsarddrt ysnvaitgyt dsvgsdasnv alskrraqav
      181 aaylnahgln artltvtgrg sadpvasnat adgrasnrrv eislqr
//
LOCUS       WP_176077989             416 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia dolosa].
ACCESSION   WP_176077989
VERSION     WP_176077989.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12947616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..416
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43353
     Region          24..402
                     /region_name="MFS_MefA_like"
                     /note="Macrolide efflux protein A and similar proteins of
                     the Major Facilitator Superfamily of transporters;
                     cd06173"
                     /db_xref="CDD:340863"
     Site            order(34..35,38..39,42,74,129..130,132..134,137,157,
                     160..161,164,236,239..240,243..245,248,272,276,329..330,
                     334,338,354,357..358,361..362,365)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340863"
ORIGIN      
        1 mtaplpesls ssplpanlfr hapfrrfwgt rvmsslafqi lsvaigwyvy althsafalg
       61 lvglaqfvpm faltlvvgqv adrydrrria ticqsveala aavfllgvaq gwlgapgvya
      121 laaivgtara fespsvssll pavvprtdlp ratalstsan qaaqilgpaf ggllyglgap
      181 vafgtsviaf alaatlsgti plrsappare pvtlrsvfsg iafirrepai lgalsldlfa
      241 vlfggatall piyardilqv gpwglgalra apavgalagt lwltrfplkv rpgramfggv
      301 iafgiativf gmsrhfalsl valaalgasd vvsvvvrlsl vqlrtpddml grvsavnslf
      361 igtsnqlgef esgvtaawwg aptaivvggv atiavalawm rlfpqltymk slerdr
//
LOCUS       WP_176077999             310 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Burkholderia dolosa].
ACCESSION   WP_176077999
VERSION     WP_176077999.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..310
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33541
     Region          30..285
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(45,131,133,135..136,165,219,240,243,254,256,285)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 msetirnvqp vvvnlgkega gelvpsryav rigdvdvvli sdgvlplpts tmstnvsead
       61 rnawfdgrfl qrdmfdwaln valvrsgdrl ilidsgvgdg feyftragqs mmrlesagid
      121 laaitdivit hmhmdhvggl nvdgvqgklr pdvrihvsaa evefwknpdf sktvmpeavp
      181 palrdaaarf akryaenivp fdrtvqvapg vsarvtgght pghcvvdvas ngekltfvgd
      241 aifevnfdhp dwqngfehdp qasvdvrial leeaadtgal laaahvafps ighiarngdg
      301 frfvpvlwdy
//
LOCUS       WP_176078018             304 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176078018
VERSION     WP_176078018.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..304
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33670
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..295
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,190,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdrfdamraf irvveagsft kaaetlhmsk ttvthlvqql earlrvrlln rttrrlnvtp
       61 dgiayyervv rlladmddae tslssasavp rgrlrvdvps pfarlilipa lpaflarypd
      121 iqldmgvsdr tvdiirenvd cvvrggepad rsmvarrvaa lslgvfaspg ylalagtpsh
      181 paelenshhr ivgfswgsag nlyplvmhrr detinvqgry alavddgnay laagvaglgi
      241 mwlphymaka aveqrelval fddwqldpmp lyvcyppnrh vspklrvfid wvvelmngpg
      301 rmqp
//
LOCUS       WP_176078040             509 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Burkholderia dolosa].
ACCESSION   WP_176078040
VERSION     WP_176078040.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..509
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53834
     Region          16..492
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(73,75,79,82,86,119,122..123,132..139,144,147,150,
                     243,247,250,253,255,428,430..431,433..434,437,440..441,
                     443,445..448,457,461,463,477,484..489,491..492)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(159..162,170,185,188,218,235..238,241,259..261,293,
                     393,395,421)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(162,259,290,293)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnanptprtg qhvptvklli dgafvdsatd ewrdvvnpat qqvlarvpfs tvaevdaavr
       61 aahaayatwk ntpiaarmri mlkfqdlvrt nlqriaktlt aeqgktipda egdifrglev
      121 vehacsvgtl qlgefaenva ggvdtytlrq plgvcagitp fnfpamiplw mfpmaivcgn
      181 tfvlkpseqd pmttmelvel aleagvpkgv lnvvhggkev vdaicthplv kaisfvgsta
      241 vgthvynlgs qhgkrvqsmm gaknhaivlp danreqavna lvgaafgaag qrcmatsvav
      301 lvgaardwlp divekakalk vnagseagtd vgpvvsrgak arilslidag vkegaklvld
      361 grdvkvpgye dgnfigptif advktgmsiy theifgpvlv vmevdtldda ialvnanpfg
      421 ngvglftqsg aaarkfqsei dvgqvginip ipvpvpffsf tgsrgsklgd lgpygkqvvq
      481 fytqtktvta rwfdddttag pvnttirlh
//
LOCUS       WP_176078043             379 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Burkholderia dolosa].
ACCESSION   WP_176078043
VERSION     WP_176078043.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..379
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41474
     Region          26..362
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 mstpvtthda gaapasdvlf rvvnrvalit lnrpaalnal syamigelaa lfarcrdddr
       61 ivavvlrgag gkgfcaggdv relhrmvaqr etwlpffvde yrldyaihtf pkpvvalmdg
      121 vtmgggmgla qgaalrvate rsriampetr iglvpdvgat hflarmpvel elyvgltgat
      181 lsgadalsak ladlcvpstw ldtfetrier anwdgdvlaa lrkvfeppcn vvphaaldsq
      241 lpwivrhfdk rsgverivat lkqdlardel preqrqwlqa tldalaahsp tmlsvtreal
      301 lrgrqmtlae sfrmelgiva raieegdfre gvrahlidkd rkprwapasl velraervrh
      361 fltspwklca hpladlgag
//
LOCUS       WP_176078085             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176078085
VERSION     WP_176078085.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33240
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          90..292
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(100,104,143,157,159,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(101..102,106..107,109..110,113,117,119..125,187,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdhfnairlf lriverrsft latedlgmpr stgteaikel erhvgvrlle rttrqvtptl
       61 egqayyerca allseldete mslregtarg lvrvgapgrf arhflapalp almeqnphlq
      121 vrvaqtgqti dlirdgvdcv vqmgppkdst ligrqvatld vvtcaspsyv arfglpsspd
      181 elegrhemvg yfssatacff plsfggvggs vrtlflparv svtdddthva maklgfgliq
      241 apryqiaeei gsgqlvpvlp dfpvpplpaf llypqnkqls prvrvviewv vatlatsvtt
      301 easana
//
LOCUS       WP_176078092             251 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia dolosa].
ACCESSION   WP_176078092
VERSION     WP_176078092.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..251
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=26828
     Region          1..232
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 msaplleirv rrkryggrtv lndtrlavra geivsllgps gcgkstllri vagldrdfdg
       61 svklhgvpld gpspelgvif qeprllpwld vannvcfplr argeaadrva allaevglpg
      121 idarwpkels ggmaqrvaia rglfsrpsvl lldepfsavd aitrmrlqdl llqvtsshrm
      181 aalvvthdvd ealllsdrvl vmqsgqndag ggivhelrvd vprprsrqaa gdgapraall
      241 erlaalfaqp v
//
LOCUS       WP_176078097             367 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Burkholderia dolosa].
ACCESSION   WP_176078097
VERSION     WP_176078097.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..367
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37844
     Region          22..>250
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mssvvsaiah gepasaelga wldahadald tdasraadvl pqlakagvtr vgvpgsmggs
       61 ggtiadaiva vadvarhslt aafvlwghrt fieylvqsdn valrsrwlpa llaghvagat
      121 glsnamkyls sieplqmras csgtgwslag alpwitnlrp qgfvaaaafe hddgtppsif
      181 aiahdapgve rsadldlvam rasntaalkv ngtilddasr iandaraflv rvrpaflglq
      241 cgmsvglarr alaevaaana gsraaladea advdarltaq tkqlldgvps gtfrdepaal
      301 felrialakt vehavalevq asggrgylra tggtarrvre asfvpivtps lvqlkaqlaa
      361 yyrtaar
//
LOCUS       WP_176078098             253 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Burkholderia dolosa].
ACCESSION   WP_176078098
VERSION     WP_176078098.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..253
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=27225
     Region          1..253
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 msgariavng vslayaahrv lhgveltver gelvavlgps gcgkssllrv laglvrptag
       61 avriddvpvt gprpdvalaf qqssllpwls vernvafgla fkrqphlsra srrarvlgal
      121 revglehvrs whpsqlsggm aqraalarsl areprvllld epfgaldevt radmqrllla
      181 vvrrigastv lvthdideal lvadrivllg ergtpaaqwa vdvpqprevq ldrldplriq
      241 irtalqrvia raa
//
LOCUS       WP_176078106             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176078106
VERSION     WP_176078106.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33624
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..288
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mfdltslalf vraaelgsls raaqqshmsl stasrriall ehhfhvvlln rtvagveltp
       61 ageallrhat dlllrtdaiy selsdytkgs igrvrvfani saisqdlpdq lrafsqryrd
      121 iklqiselrs adilqalreg radvgivtsr tategihlap ycmdrasvvv pedypltdes
      181 idfsallehd lvalddrsel trslvkeaal lgksvrfrvq vqsfeamcrl iaagqgigil
      241 peravalfre pmrlrfirln dpwanrvmsv girtgavpqp trklfeflas fapaslaagd
      301 tepsnd
//
LOCUS       WP_176078227             143 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Burkholderia dolosa].
ACCESSION   WP_176078227
VERSION     WP_176078227.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..143
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=15008
     Region          1..116
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mllvydgtde adaalahcat lsralsaevd vvaivdsvta narsagllsd lahhrlaefa
       61 hhelqravgk lasggiaarg cvrfgraada iaahatttrp dmvvvghcar tgfarwwrer
      121 pvhfdlaerl rgaalivvti ppa
//
LOCUS       WP_176078224             462 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Burkholderia dolosa].
ACCESSION   WP_176078224
VERSION     WP_176078224.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 462)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..462
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=49484
     Region          105..459
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mnnelddscs avaarsarkt ppdasgpdvt pvfdgrasas lfgvdlhalr hvsraiandv
       61 apaarvgall dvamqrtsat wgvmailrdg gweaaadaga adssridaer ppierlpvpi
      121 laaaahlrdg lvlhdartad qwrtddyvrr rkpravicmp ircngaltga lylehgsapg
      181 vfspaqtavv eivalqagfa lenmrlrdel aalharlsrt eaqmrdaqce meranrlkty
      241 gelaasivhe vaqpvtaidt saraglkwln rsapnidaar emlahicaca vrartivsal
      301 rakarqeapv favfdladal reaseivest ldmmkvslrv eglslptpmh gdrvqlqqav
      361 igllmngaes mlgipdrerv lvlscerasn llririddrg dgfdpalaer ifeplfttkp
      421 hgmgmglsic ksivdahhgg laltpradgg tratmtlpll pm
//
LOCUS       WP_176078232             127 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator transcription factor [Burkholderia dolosa].
ACCESSION   WP_176078232
VERSION     WP_176078232.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..127
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=13398
     Region          10..>126
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mplslsatdl vsivdddpfv raaarsfvrs lggqarefas gaafvasdav srtgclicdv
       61 empgmdgiel larleaaglr iptvfvtaya tarvrervra gtalcllekp ldareletwv
      121 arafgrg
//
LOCUS       WP_176078236             399 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia dolosa].
ACCESSION   WP_176078236
VERSION     WP_176078236.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Yan,N.
  TITLE     Structural advances for the major facilitator superfamily (MFS)
            transporters
  JOURNAL   Trends Biochem Sci 38 (3), 151-159 (2013)
   PUBMED   23403214
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Pao,S.S., Paulsen,I.T. and Saier,M.H. Jr.
  TITLE     Major facilitator superfamily
  JOURNAL   Microbiol Mol Biol Rev 62 (1), 1-34 (1998)
   PUBMED   9529885
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..399
                     /product="MFS transporter"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=41747
     Region          1..349
                     /region_name="AraJ"
                     /note="Predicted arabinose efflux permease AraJ, MFS
                     family [Carbohydrate transport and metabolism]; COG2814"
                     /db_xref="CDD:442063"
ORIGIN      
        1 mmvhprsmsp rvasfvllga lltacgygat fllsmhfrsa gggdvdtgaa lgeamvgtli
       61 glplvawlay rigaarttal aalvvgagvv gfaligrtgs lsavpgllvg igwggfylaa
      121 pmmlaerttd tererwflrf gsfqmagvgg gpavaalair nwhwttgtvf wavgalcama
      181 almleyfgrl spasrpvapp trqrwvgeig aiarthaiyp iaiialgssv fsglmtfqms
      241 maqetgvkag tffglysatv vvirwllgai viqirvdatt qillgfmils vavtfavphs
      301 allhsasavl lgtgygliyp ivqaravngi darhrhavlt wfvasyfigv fgfpalgslv
      361 lvsmgrtmll mliaacglaa lllsivehrk rvspapraa
//
LOCUS       WP_176078309             246 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase [Burkholderia dolosa].
ACCESSION   WP_176078309
VERSION     WP_176078309.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 246)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..246
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25913
     Region          5..243
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 mantsneskt ilitgassgi gegaarllaa qghrvvigar rtdrlarlae sieasggivr
       61 yreldvtsad dvaafarfal dafgridvli nnagvmplsp lnalkldewn rmidvnirgv
      121 lhgiaavlpt meaqgrgqiv nissigglsv sptaavycat kfavraisdg lrqetdkirv
      181 tvicpgvves eladsisddt artamqtfrr iaitpdaiar aiayaveqpd dvdvseivvr
      241 ptaspf
//
LOCUS       WP_176078317             357 aa            linear   BCT 11-JAN-2025
DEFINITION  porin [Burkholderia dolosa].
ACCESSION   WP_176078317
VERSION     WP_176078317.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Vergalli,J., Bodrenko,I.V., Masi,M., Moynie,L.,
            Acosta-Gutierrez,S., Naismith,J.H., Davin-Regli,A., Ceccarelli,M.,
            van den Berg,B., Winterhalter,M. and Pages,J.M.
  TITLE     Porins and small-molecule translocation across the outer membrane
            of Gram-negative bacteria
  JOURNAL   Nat Rev Microbiol 18 (3), 164-176 (2020)
   PUBMED   31792365
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Masi,M., Winterhalter,M. and Pages,J.M.
  TITLE     Outer Membrane Porins
  JOURNAL   Subcell Biochem 92, 79-123 (2019)
   PUBMED   31214985
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007050
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..357
                     /product="porin"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /calculated_mol_wt=37736
     Region          25..357
                     /region_name="OmpC"
                     /note="Outer membrane porin OmpC/OmpF/PhoE [Cell
                     wall/membrane/envelope biogenesis]; COG3203"
                     /db_xref="CDD:442436"
ORIGIN      
        1 mkqtqriaar armrnvvrtl gvtatlgagl astfvdaraa ggaevqlygi vgtyvgsvkr
       61 sdtpqaaalm gsgglttsfw girgkedlgg gvsaifales ffqpqngalg rnatdpfwsr
      121 naylgfqgdf grltfgrhrn ptytaeslvn pfgsstvfsp lvlqtfvtny ggtmigdtvw
      181 nntaqyttpn vrgfgatviy glggvagspg ignlgvhfsy qghgltavls gqrvrytaag
      241 pvgaqyayla gaaydfkvat lygawamtsd vstptgshty eaglsipfsp adfllaewar
      301 tkrsgprpan nslrntvslg ydhflskrtd iyaiysydkl taratgntfa vgvrhtf
//
LOCUS       WP_176078318             480 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Burkholderia dolosa].
ACCESSION   WP_176078318
VERSION     WP_176078318.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..480
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51833
     Region          49..465
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(58..59,62..63,66,98,148..149,151..153,156,176,
                     179..180,183,299,302..303,306..308,311,339,343,394..395,
                     399,403,419,422..423,426..427,430)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mntpltaysv dvgrsdgatr taseqlraan llfrvenvpf crwhtkariv mgsatlfdaf
       61 dalslafvlp vlvglwhlsp gqigvliaag ylgqvvgala fgwlaerfgr vpsatvtvgv
      121 msvmsivcaf tgsfhmlflm rflqgigvgg evpvaatyin elsqahgrgr ffilyelifp
      181 lgllaaaqlg afivprfgwe ymflvggipg iavafliarl pesprwlist grfdkaervi
      241 erleastpkr nldsrtqkae idervaslln glqskqkgsw kelfspfyrg rtiavwllwa
      301 tsyfvangin nwlpslyktv yhlplqeslr masisnvlst cgvlacalli drvgrrrwam
      361 gcfvvsatll aalgihgags assvmflgss ayavmatttv llylytpeiy ptrmraigtg
      421 latswlraas aaapaivgvv ltdkgiaavf ilfavvsavg fivatrmvet tnrsleeisp
//
LOCUS       WP_176078353             130 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Burkholderia dolosa].
ACCESSION   WP_176078353
VERSION     WP_176078353.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..130
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14270
     Region          7..125
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 miefkwdhlq lcsadaeata awfarclnae ivrrpgrvdl rigdinlfit alphahsait
       61 pdgarvqrid hfgvlvddld aayahlvdng adivqpiaqv ragvrccfvr apgdilvevl
      121 errpaemtfn
//
LOCUS       WP_176078369             242 aa            linear   BCT 11-JAN-2025
DEFINITION  DsbC family protein [Burkholderia dolosa].
ACCESSION   WP_176078369
VERSION     WP_176078369.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Shao,F., Bader,M.W., Jakob,U. and Bardwell,J.C.
  TITLE     DsbG, a protein disulfide isomerase with chaperone activity
  JOURNAL   J Biol Chem 275 (18), 13349-13352 (2000)
   PUBMED   10788443
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Chen,J., Song,J.L., Zhang,S., Wang,Y., Cui,D.F. and Wang,C.C.
  TITLE     Chaperone activity of DsbC
  JOURNAL   J Biol Chem 274 (28), 19601-19605 (1999)
   PUBMED   10391895
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122483
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..242
                     /product="DsbC family protein"
                     /GO_function="GO:0003756 - protein disulfide isomerase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=25710
     Region          44..238
                     /region_name="DsbA_DsbC_DsbG"
                     /note="DsbA family, DsbC and DsbG subfamily; V-shaped
                     homodimeric proteins containing a redox active CXXC motif
                     imbedded in a TRX fold. They function as protein disulfide
                     isomerases and chaperones in the bacterial periplasm to
                     correct non-native disulfide bonds...; cd03020"
                     /db_xref="CDD:239318"
     Site            order(44..52,55..82)
                     /site_type="other"
                     /note="dimerization domain [polypeptide binding]"
                     /db_xref="CDD:239318"
     Site            75..82
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239318"
     Site            order(131,134)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239318"
ORIGIN      
        1 mkktiriasl tlavamaalg ctaqadqatd klkatlqerl gsdapiksvs kspvaglyev
       61 nlgsqiiysd atgdhvllgd lvdtkthknl tdarlselnk idfaslpfan aikvvkgsga
      121 rkiavfsdpn cpyckrlett lqsidnvtvy tflypvlspd stakskaiwc atdraktwqs
      181 wmldhrvptg agncdtsald knlalgrgmn vtgtptiflp dgrrlpgavs adqlnqalas
      241 sk
//
LOCUS       WP_176078392             318 aa            linear   BCT 11-JAN-2025
DEFINITION  OmpA family protein [Burkholderia dolosa].
ACCESSION   WP_176078392
VERSION     WP_176078392.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Confer,A.W. and Ayalew,S.
  TITLE     The OmpA family of proteins: roles in bacterial pathogenesis and
            immunity
  JOURNAL   Vet Microbiol 163 (3-4), 207-222 (2013)
   PUBMED   22986056
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Smith,S.G., Mahon,V., Lambert,M.A. and Fagan,R.P.
  TITLE     A molecular Swiss army knife: OmpA structure, function and
            expression
  JOURNAL   FEMS Microbiol Lett 273 (1), 1-11 (2007)
   PUBMED   17559395
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..318
                     /product="OmpA family protein"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_function="GO:0042834 - peptidoglycan binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32915
     Region          28..316
                     /region_name="OmpA"
                     /note="Outer membrane protein OmpA and related
                     peptidoglycan-associated (lipo)proteins [Cell
                     wall/membrane/envelope biogenesis]; COG2885"
                     /db_xref="CDD:442131"
     Region          213..316
                     /region_name="OmpA_C-like"
                     /note="Peptidoglycan binding domains similar to the
                     C-terminal domain of outer-membrane protein OmpA; cd07185"
                     /db_xref="CDD:143586"
     Site            order(218..219,252..253,256,260..261,264,306,310)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:143586"
ORIGIN      
        1 mprtihvrrm rlsrlssfva allaaglvgn gaayaqntgg atvtpvgngt vataalpapn
       61 aggapgtasg tvvrgtagti tpppanavpg qvvvggkvpd eatkaavlqk lrdtygaanv
      121 vdqievgdva tppnwsanvq kllgaqlkqi skgqlkingt qiemkgevhn eaqrqqiasd
      181 mantlnptyt iknalrvsas eqglldqtla nrtiefetgs atltpqgrqi ldqmaaalsk
      241 lqnrtvdiig htdnsgnrts nialsqarad avkgylitkg ippqqmtttg vgpdqpiapn
      301 dtaegrarnr riefrvgq
//
LOCUS       WP_176078394             930 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia dolosa].
ACCESSION   WP_176078394
VERSION     WP_176078394.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 930)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 930)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..930
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..930
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=101351
     Region          14..821
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnvtelaqai rggliqqgrl lktdipalpn nalvprravt rselgrdfsv vldlvstasd
       61 velktliaqp itlwiqqtnk sylpingyih tarrlgtdgs latyqlsfas wmhflrfrsd
      121 mrywqeqpid ailadvfdmh pqargqyrfa lskplpsrsy crqsetdwnf vhrlmedegl
      181 fgfwrhgedg kshtfvitdd lhaidalspn tvsfdrfgsg tetggftqwa asrtlqstlh
      241 ttrtfdyksp ssagnpngts lptkadqgdl paqaeiyeyt gaytypgqdr geqlskirle
      301 ewesrakrff gvggvrgida grrftltdhp ehdrdaaser qfaaigvtry iennlpvseh
      361 easfphslqd qlaqvkagrg kaaafevghd dgsagfylve veaqrasvpy rspfehrkpa
      421 mqletaivvg pkgeevytde lnrikvmfmw drqsegreta scwmrvvqsd tgggyggvhi
      481 prvgeevlig yiggdcdrpi vmhrvyngaa kpqwhsdgil sgfrtkeyag aghnemvldd
      541 atgqnrarlf sssansllhl gylieqngnt rgaylgsgfd lrtdaygamr agqglyvtth
      601 lkqansqpld vgdakqqlan aeglvesmsq vsemhqaesl gtgrdalkql adatqhsvag
      661 atagggrtgg ggtgnanafk epvmlfaspa gigvasqqsv hlaseqqtni vsgqstfits
      721 gksliagird rislfaqnag mklfagkgkv evqahadnve ltaqktvkil satekteiaa
      781 areilltsgg ayirigngni eihapgrvdv kgsqhsfagp arlsyplpdl pqsspatfsq
      841 kvlfrsiddg esvsqvkysm fsvspeaarr vvmgvssdeg serrvnpaet ehltvlygqg
      901 ewsaiydfni drendgsmtd frqesdtgvs
//
LOCUS       WP_176078456             190 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter small permease [Burkholderia dolosa].
ACCESSION   WP_176078456
VERSION     WP_176078456.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..190
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=19799
     Region          35..187
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mtrhtsldsa aaagssagaa adgtaagrpp avpflrgvnd vlfrtlavia slclaaltvl
       61 vfyavvmryv fenapdfvep ialllvivia mfgaamkvrd gghigldsfv rrlsprardv
      121 vvaiqhlsli afavailigc gsmaaetmgd ripiiglpeg vrylitipaa vaiilfsleh
      181 llalrrasth
//
LOCUS       WP_176078474             282 aa            linear   BCT 11-JAN-2025
DEFINITION  DedA family protein [Burkholderia dolosa].
ACCESSION   WP_176078474
VERSION     WP_176078474.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..282
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=29503
     Region          5..>152
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 mlsheliary galivflnvf asslglpvpa aptlvmvgag mslaagdvas tlaqlgttvg
       61 aaaiggvlgd lvwfqggkry geralhgvfa llmlrptcvr ymerfftrwg vrvlvvsrfv
      121 pglalvsvpl cgamavrlra fmlhdcagig lwasaavaag amfapqidrt avlatrfgwh
      181 alaaaafala lyvpyrhfrr aigesgperi gagadaadep afagaaprts gapeagaaya
      241 pafrrtttra pcgacsalay aarppaafhv lptrrrrrwr ra
//
LOCUS       WP_176078482             296 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176078482
VERSION     WP_176078482.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..296
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31769
     Region          1..>128
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          91..286
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(101,105,144,158,160,221,238,265)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(102..103,107..108,110..111,114,118,120..126,187,
                     215..219,226..227,230)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 melndlrifv atvdagsfta aaeqlmlskq fvsrrtmale aslgvrllhr ntrnlavtes
       61 ghefyaraqr ilaevadaeq amsvrstelh gslkisapls fgithvspli aeflsahpav
      121 rlnldltdrr vdvigegfdl vlrigaleds tliarplgaw kmiacaspay lkrrgtpatp
      181 adlaghtcll ygrerrvgwe frvdgaartf gvqgplvann gevvrdaaia glgiallphf
      241 ivgaaierga lvpvldayap spitlnavyp qhregfvtlr tfigflaqrl aqadaa
//
LOCUS       WP_176078487             342 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Burkholderia dolosa].
ACCESSION   WP_176078487
VERSION     WP_176078487.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..342
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=36260
     Region          107..314
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mkivkpllia aavaalsstv saasaaepvr pdaktsafla alnaqkgpgl etlspakarq
       61 vlvdaqngvk vdvsgidvsn rtieqdglsv pitivrpqqv sgtppvfmff hgggwilgdf
      121 ptherlvrdl vvqsgavavf vnytpspeah ypvainqaya atkwvaahga digvdgsrla
      181 vvgnsvggnm aavvslmakd kggpairfqg llwpvtdhdf ntgsynayrq dhfltrpmmk
      241 wfwdaytkne aqrndiyasp lrastaqlkg lppaliqvaq fdvlrdegea ygrkldaagv
      301 datttrydgt ihdfgllnal addaptkaal kamaneiatr lk
//
LOCUS       WP_176078489             188 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176078489
VERSION     WP_176078489.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..188
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20475
     Region          1..163
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 metkstvreq ildhaitlmm lrgyngfsyr dlselvgvkt ssihyyfpsk dhlvmeavaa
       61 ysdevlaavr aidpalpadv klslytklfg rtlgdgnqic lcgmlaadie slpdnvrqav
      121 qaffnanekw lagvleqgan egslafsgkp daaartlyaa fqgsvlasrl fhtrarledv
      181 eavwkars
//
LOCUS       WP_176078512             342 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Burkholderia dolosa].
ACCESSION   WP_176078512
VERSION     WP_176078512.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..342
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37495
     Region          69..269
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 makdtskdkk stgnlhlaag llrglaqena aletrlpeps asavaaptva apmqstaasa
       61 dsqdlgapqk vavkdcipnp fnprvfyses slhelaltlk regqiepikv trlpefpgkl
      121 vvidgqrrlr atsingdeti natfrtdhtp eqlytiayra nhdherqtif ddavawkrll
      181 dekvfpdqnt laekigkdka sisktlslna lpntllerma sasdvvglqa ayflklifer
      241 lgeatadrll tavierkksv rdlenflraq sdgnkktgrt rysvrhdfav esraigqlkt
      301 ypdgrldlql kgvdashqea ladklksvid ayvaelatnv qr
//
LOCUS       WP_176078516             313 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176078516
VERSION     WP_176078516.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..313
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34380
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,161,163,227,244,271)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,190,
                     221..225,232..233,236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mdtlqmmrif vrvaeegsft saaqrlditt ayasrsvaql eahlrtrlln rstrrialtd
       61 agqryldrcq rilgyideae aeaadaqakp sgrlhvhatt sfgqayvvpa vvryrqryps
      121 vaveltlsqh vpdiidegyd vslqlsttel pdsglvsqrl gevhsvlcas paylkergtp
      181 rtvrdlegha clqivtpifp rdrwhldgpd gretfelplp dfqvnlaeal gaalragvgi
      241 gavpmstalp alasgalvrv lpeyrlqklt vytlyasrqy ldakirtfvd flrecvpeml
      301 aadeaalrgs cna
//
LOCUS       WP_176078561             581 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Burkholderia dolosa].
ACCESSION   WP_176078561
VERSION     WP_176078561.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..581
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=61385
     Region          13..581
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 milrrklptp iglaililaa payaqslpna gsllneqqia pqprapqatt peevipseaa
       61 pgaaepeagp tvtlksitfn gdksvadaed lqsvtasmvg kklthaglqk iadtitqylr
      121 grgyalayay lapqdltagn lvitivegrl esgndrvtih gntrssnari aaianaalpt
      181 drplkkedle ralllindrp gvsakavlqk gaqpgtsrll vettptpivn gqlsidnygn
      241 rstgiergta tffvndpfgm gdqvtlglsk sqgtevanlg ysvpltptgl tlllggsylh
      301 yrvvqdaysa ldlrgsavtg svglnypivr trtqnlnatv mydhkylkds aldvslskrk
      361 ldnltfslag nrydgllqgg vtearaavtf ghvdlsgnpv dqladsmtar thgtftklaa
      421 nlsrlqtldq nwsvyggwag qlsntnldss ekfllggptg vrgypvgegs gdegwmgtve
      481 lrrfvnigvp svkvqalgfv dvgqirlhht ayagsqineg htnkvtltsa glgvnvwsgr
      541 wnahaavart igrndgasla gnnadglnts wrawlqlgma f
//
LOCUS       WP_176078551             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia dolosa].
ACCESSION   WP_176078551
VERSION     WP_176078551.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444078
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33048
     Region          7..66
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          96..292
                     /region_name="PBP2_LTTR_like_4"
                     /note="TThe C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator,
                     contains the type 2 periplasmic binding fold; cd08440"
                     /db_xref="CDD:176131"
     Site            order(111..112,114..115,118,122,124..130,222..227,
                     233..234,236..237)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176131"
ORIGIN      
        1 mginfdltdl qafravvelg sfrkaadais isqpalsrri dkleealgvr lferttrsvt
       61 lttvgrvfap saeqllddld aallgirdvs ssrlghvtia cvpsvayyfl pnvianyhrr
      121 fprirvklld asanevlgav isgeadfgvs fmgsqeaeie fkmllqerfv aacrrdhpla
      181 rkkrvtwsel yeheyvsvdk tsgnrllldq alsavappap svcetrhvtt mlglieaglg
      241 vaavpsmamp ghdhpiltsv plvepvvkrr vgivkrrgra ltpaadafhr miveakrggt
      301 agaat
//
LOCUS       WP_176078602             458 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Burkholderia dolosa].
ACCESSION   WP_176078602
VERSION     WP_176078602.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..458
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=48827
     Region          157..426
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 mtenrllshr lasvirdfnq pvmiwqaail vgalglawla arfvhgrida rrraagrapg
       61 agahslkral fplfggsfvl aaqlaldpfm stsllslalv plfgigliyv lfffarrvfa
      121 rdghthawls ivekivsvvv waamvltvlg iqrdvlawld svqfrvanah ltllsvisga
      181 lwvcvtlmva mwagsvleer larsstldan lkvvlsrigr allvfaavli glslvgidvt
      241 vlgvfggalg vglgfglqki asnyvsgfii lldrslrlgd aisvgglqgv vtqirtrytv
      301 vrgldgnetl ipneklitdv vqnqssyqtr ghakvavqva ytsdveqala lladaakgvp
      361 rvlddppptp ylvgfgadgi dlelgfwied aakgtsgvrs avnrniwrlf cehgvsipfp
      421 qrdvrvvglp dgfvaadaaa drdsapwsga ddlrasaa
//
LOCUS       WP_176078609             238 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Burkholderia dolosa].
ACCESSION   WP_176078609
VERSION     WP_176078609.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..238
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=25658
     Region          1..224
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mdlesilytq gfgsrrqcrg lieagrvavg gatatdpdaa fdtdglvftv dgtawpfhar
       61 aylalnkpag yecsrdpqhh asvfsllpap lvargvqcvg rldqdttgll llsddgqfvh
      121 aytspkrkvp ktyvatvrhp lddtqlhtlr tgvqlhgepk piaavaadar dahtlvltvv
      181 egkyhqvkrm vaavsnrvda lhresigglt lpddlapgtw rwldeaelaa lrnpvktl
//
LOCUS       WP_176078713             155 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein, partial [Burkholderia dolosa].
ACCESSION   WP_176078713
VERSION     WP_176078713.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         <1..>155
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
     Region          <2..137
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 laaidligld gfenayprel sggmrqrvgf aralvvdpti llmdepfsal dvltaetlrt
       61 dlldlwtqgr mpiksvlivt hnieeavfmc drilvlssnp grviaeikvp fkhprnrldp
      121 tfrklvddiy akmtarqige ttkkglelgs wlprv
//
LOCUS       WP_176078736             362 aa            linear   BCT 11-JAN-2025
DEFINITION  elongation factor Tu, partial [Burkholderia vietnamiensis].
ACCESSION   WP_176078736
VERSION     WP_176078736.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     gene            1..>362
                     /gene="tuf"
     Protein         1..>362
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
     Region          1..362
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makekfertk phvnvgtigh vdhgkttlta aittvltkkf ggeakaydqi daapeekarg
       61 itintahvey etanrhyahv dcpghadyvk nmitgaaqmd gailvcsaad gpmpqtrehi
      121 llarqvgvpy iivflnkcdm vddaellelv emevrellsk ydfpgddtpi vkgsaklale
      181 gdtgelgeva imnladaldt yiptperavd gaflmpvedv fsisgrgtvv tgrvergivk
      241 vgeeieivgi kptvkttctg vemfrklldq gqagdnvgil lrgtkredve rgqvlakpgs
      301 itphthftae vyvlskdegg rhtpffnnyr pqfyfrttdv tgsielpkdk emvmpgdnvs
      361 it
//
LOCUS       WP_176078785             540 aa            linear   BCT 11-JAN-2025
DEFINITION  RHS repeat domain-containing protein, partial [Escherichia coli].
ACCESSION   WP_176078785
VERSION     WP_176078785.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Koskiniemi,S., Lamoureux,J.G., Nikolakakis,K.C., t'Kint de
            Roodenbeke,C., Kaplan,M.D., Low,D.A. and Hayes,C.S.
  TITLE     Rhs proteins from diverse bacteria mediate intercellular
            competition
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), 7032-7037 (2013)
   PUBMED   23572593
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459983
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         <1..>540
                     /product="RHS repeat domain-containing protein"
                     /GO_function="GO:0030246 - carbohydrate binding [Evidence
                     IEA]"
     Region          <1..540
                     /region_name="RHS_core"
                     /note="RHS element core protein; NF041261"
                     /db_xref="CDD:469161"
ORIGIN      
        1 qsedeglitl whydasdrit hrtvngdpae qwqydehgwl ttlshtsegh rvsvhygydd
       61 kgrltgerqt venpetgell wqhetkhayn eqglanrvtp dslppvewlt ygsgylagmk
      121 lggtplveyt rdrlhretvr sfgsragsna ayeltstytp agqlqsqhln slvydrdygw
      181 ndngdlvris gprqtreygy satgrlesvr tlapdldiri pyatdpagnr lpdpelhpds
      241 tltawpdnri aedahyvyhy deygrltekt driptgvirt dderthhyhy dsqhrlvfht
      301 riqhgeplve srylydplgr rmakrvwrre rdltgwmsls rkpeetwygw dgdrlttvqt
      361 dttriqtvyq pgsftplirv etengereka qrrslaeklq qegsedghgv vfpaelvgll
      421 drlegeiran cvssesrqwl aqcgltverl aaqiepvylp erkihlyhcd hrglplalis
      481 edgntawsae ydewgnqlne enphhlhqpy rlpgqqydke sglyynrhry ydplqgryit
//
LOCUS       WP_176078674             346 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Burkholderia dolosa].
ACCESSION   WP_176078674
VERSION     WP_176078674.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia dolosa
  ORGANISM  Burkholderia dolosa
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Burkholderia dolosa"
                     /db_xref="taxon:152500"
     Protein         1..346
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34867
     Region          11..301
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtrlrtllrh plvwpvltlv llfaldvahr pgflsislld ghlfgapidi lnraaplviv
       61 slgmtlviat ggidisvgai vaiagaaaai vldadpsrvg talaaalavg llagawngvl
      121 vafvgmqpii atlilmvagr giaqlltggq iipigspgyl tlgggylatv pnavwiaiaa
      181 ivaiallvnr talglfirai gvnpvatrlv glrsgavvfg vylccgvmaa vagilassnv
      241 rsadgnnagl lleldailav tlggtsllgg rfslagsvlg aliiqtltyt tysigvppea
      301 tlvvkaivvi vvtliqsdaa ralvvrhasr lvsfarartt tgatsr
//
LOCUS       WP_176078876             482 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Paraburkholderia tuberum].
ACCESSION   WP_176078876
VERSION     WP_176078876.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tuberum
  ORGANISM  Paraburkholderia tuberum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Paraburkholderia tuberum"
                     /db_xref="taxon:157910"
     Protein         1..482
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=51105
     Region          30..482
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mtepsitddk ttqtatptat ataplattle alraalgvda vrvgeqiger altdwtrhep
       61 trpaallmpr ttdevsrala ichaahqpvv pqggmtglag gaiarandia lslerlsgve
      121 eldaasatlt vragttlqaa qeaaeaagfe laldlgargs cqiggnlatn aggnrviqsg
      181 tardqvlgle vvlangdvls slgkmvknnt gydlkhwfig segtlgvitr avlrlhprra
      241 arhtalvald dydaavsllr rlatrfgndi gafeimwpdf ydfgvkltga rspfdaahpl
      301 yaliehagfd addagerfaq altdalqaga lrdaviaqsv adaralwair ectaefplkl
      361 dpinfdvslp igeigtfvdr craaldqrwp gnrsyffghi gdsnlhltvd ghsipgvdhh
      421 avyafvyeml rplrgsvsae hgigslkref lpisrspael aamvaikral dphgilnpgk
      481 lf
//
LOCUS       WP_176078895             374 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: FUSC family protein [Paraburkholderia].
ACCESSION   WP_176078895
VERSION     WP_176078895.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..374
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40699
     Region          27..267
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 maaadtptli srraalsrmv ravtspyyry rhakvlhslr vglamlvsil attgidiphg
       61 iwssvtllvv igglqhhgni rkkaaeraag tllgasigll livqqhfigs lpltyvleai
      121 iasicawfai gssgyigllt aitmcivagh gdnlidvglw rtlnvligiv ialafsfafp
      181 lhatyswryg laanlrecag iyarlldget iteeeqikrf lrinkrlvql rslmpsvake
      241 idvpqsrlee iqrlhrsvls slellatgpl mnadaaarta yaahcgaevr avraillsta
      301 rglrfgrpsr fgipaaaplg kghgdvatal ppdwqgpywl gqrlaeqvdr lrallletep
      361 nwnierhera trgr
//
LOCUS       WP_176078937             237 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: J domain-containing protein [Paraburkholderia].
ACCESSION   WP_176078937
VERSION     WP_176078937.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia
  ORGANISM  Paraburkholderia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Zhang,R., Malinverni,D., Cyr,D.M., Rios,P.L. and Nillegoda,N.B.
  TITLE     J-domain protein chaperone circuits in proteostasis and disease
  JOURNAL   Trends Cell Biol 33 (1), 30-47 (2023)
   PUBMED   35729039
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Walsh,P., Bursac,D., Law,Y.C., Cyr,D. and Lithgow,T.
  TITLE     The J-protein family: modulating protein assembly, disassembly and
            translocation
  JOURNAL   EMBO Rep 5 (6), 567-571 (2004)
   PUBMED   15170475
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Kelley,W.L.
  TITLE     The J-domain family and the recruitment of chaperone power
  JOURNAL   Trends Biochem Sci 23 (6), 222-227 (1998)
   PUBMED   9644977
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Cyr,D.M., Langer,T. and Douglas,M.G.
  TITLE     DnaJ-like proteins: molecular chaperones and specific regulators of
            Hsp70
  JOURNAL   Trends Biochem Sci 19 (4), 176-181 (1994)
   PUBMED   8016869
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10446266
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Paraburkholderia"
                     /db_xref="taxon:1822464"
     Protein         1..237
                     /product="J domain-containing protein"
                     /GO_process="GO:0006457 - protein folding [Evidence IEA]"
                     /calculated_mol_wt=26067
     Region          3..66
                     /region_name="DnaJ"
                     /note="DnaJ domain; pfam00226"
                     /db_xref="CDD:395170"
     Site            order(31..33,43,46..47,50..51)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
ORIGIN      
        1 matlyetlgv pahatddeik rayrkaamkw hpdrnhgaed varaafqeik dayailsdae
       61 qrnvydavyt eqmreweaqh trrqraqakr eaaaraadea ayaemvsiai rfadqghnrd
      121 vlfgvllgrq cepqraaqia dsvaalqaar rdeadaaqna qragktaksa qaaqaeasep
      181 eladraqdtg aasqtaphdt qpsrrenhak rdetvsdmhp agalgnlwfq flnslkf
//
LOCUS       WP_176079002             322 aa            linear   BCT 11-JAN-2025
DEFINITION  PDR/VanB family oxidoreductase [Paraburkholderia tuberum].
ACCESSION   WP_176079002
VERSION     WP_176079002.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tuberum
  ORGANISM  Paraburkholderia tuberum
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Mathews,F.S., Cunane,L. and Durley,R.C.
  TITLE     Flavin electron transfer proteins
  JOURNAL   Subcell Biochem 35, 29-72 (2000)
   PUBMED   11192725
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 18977663
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Paraburkholderia tuberum"
                     /db_xref="taxon:157910"
     Protein         1..322
                     /product="PDR/VanB family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=35481
     Region          15..227
                     /region_name="PDR_like"
                     /note="Phthalate dioxygenase reductase (PDR) is an
                     FMN-dependent reductase that mediates electron transfer
                     from NADH to FMN to an iron sulfur cluster. PDR has an an
                     N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding
                     domain and a C-terminal iron-sulfur...; cd06185"
                     /db_xref="CDD:99782"
     Site            order(56..57,59,73..75,81,83..84,125,226)
                     /site_type="other"
                     /note="FMN-binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Site            order(56,58..59)
                     /site_type="active"
                     /note="flavin binding motif [active]"
                     /db_xref="CDD:99782"
     Site            order(81,84,87,94)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99782"
     Site            order(117,121..124,126)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99782"
     Site            order(122..123,147..149,201..202)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99782"
     Region          240..322
                     /region_name="Fdx"
                     /note="Ferredoxin [Energy production and conversion];
                     COG0633"
                     /db_xref="CDD:440398"
ORIGIN      
        1 mtppledafl rlkiagkeki ardiwrfelt dpqgaplppf eaganltvvv pngsrrsysl
       61 cndsqernry viavkrdgng rggsisfidd taegdavdvs lprnefplde raksfvlvag
      121 gigitpmlsm arqlraeglr sfklhyltrd pegtaffdel tsdewrsdvk ihhdhgepsk
      181 afdfwpvfer sksaqhvycc gpqalmdtvr dmtghwpsgt vhfesfgasn adarestpft
      241 vrlsrsgtsf dipanrsile vlrdanvrvp sscesgtcgs cktalcsgev dhrdlvlrdd
      301 eketqimvcv sraksaelvl dl
//
LOCUS       WP_176079081              80 aa            linear   BCT 11-JAN-2025
DEFINITION  BlaI/MecI/CopY family transcriptional regulator, partial
            [Clostridioides difficile].
ACCESSION   WP_176079081
VERSION     WP_176079081.1
KEYWORDS    RefSeq.
SOURCE      Clostridioides difficile (Clostridium difficile)
  ORGANISM  Clostridioides difficile
            Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
            Peptostreptococcaceae; Clostridioides.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Wittman,V., Lin,H.C. and Wong,H.C.
  TITLE     Functional domains of the penicillinase repressor of Bacillus
            licheniformis
  JOURNAL   J Bacteriol 175 (22), 7383-7390 (1993)
   PUBMED   8226686
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Clostridioides difficile"
                     /db_xref="taxon:1496"
     Protein         1..>80
                     /product="BlaI/MecI/CopY family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0045892 - negative regulation of
                     DNA-templated transcription [Evidence IEA]"
     Region          3..>80
                     /region_name="CopY"
                     /note="Transcriptional regulator, CopY/TcrY family
                     [Transcription]; COG3682"
                     /db_xref="CDD:442898"
ORIGIN      
        1 mmirkipqae lkvikfiwrv dntvtskdvi evmeqkygwk qtttltllsr lvkrgfldaq
       61 kidkytnyai ivkhkdylsf
//
LOCUS       WP_176079184             193 aa            linear   BCT 11-JAN-2025
DEFINITION  peptidylprolyl isomerase [Paraburkholderia tropica].
ACCESSION   WP_176079184
VERSION     WP_176079184.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..193
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=20606
     Region          26..193
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 mkwlmlalgs aalianapaf aqngpqaahp qvlfktsdgd irvelypeka pktvdnflqy
       61 vksgqyngti fhrvirgfmi qgggyttsfv ekptrapipl esknglkntt gmlamartsd
      121 pnsataqffi ntvdnanldy pnpdangyav fgkvtqgldv vkkieatptt srgpmsdvpq
      181 tnvviqsatv vgk
//
LOCUS       WP_176079200             269 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphatidate cytidylyltransferase [Paraburkholderia tropica].
ACCESSION   WP_176079200
VERSION     WP_176079200.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Sparrow,C.P. and Raetz,C.R.
  TITLE     Purification and properties of the membrane-bound CDP-diglyceride
            synthetase from Escherichia coli
  JOURNAL   J Biol Chem 260 (22), 12084-12091 (1985)
   PUBMED   2995359
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001733
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..269
                     /product="phosphatidate cytidylyltransferase"
                     /EC_number="2.7.7.41"
                     /GO_function="GO:0004605 - phosphatidate
                     cytidylyltransferase activity [Evidence IEA]"
                     /GO_process="GO:0016024 - CDP-diacylglycerol biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=27873
     Region          2..268
                     /region_name="CdsA"
                     /note="CDP-diglyceride synthetase [Lipid transport and
                     metabolism]; COG0575"
                     /db_xref="CDD:440340"
ORIGIN      
        1 mlktrvitai vllavllpvt lfapvaafgv lihvvvafaa wewarllkag kvgsivyali
       61 aalavlaser lasprplfqa agifwivagp yvlvrkpvla agawraflla aglvifcacw
      121 halvlartsg vafvlslllv vwladigayf agkafgkhkl apaispgktw egavggwaav
      181 mivaaaalal haseptlysa lagqlglgra ffvltvlvaf svvgdlfesm lkrqagvkds
      241 sgllpghggv ldridallpv lplamlllg
//
LOCUS       WP_176079240             480 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia tropica].
ACCESSION   WP_176079240
VERSION     WP_176079240.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..480
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51898
     Region          42..465
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(52..53,56..57,60,100,150..151,153..155,158,178,
                     181..182,185,301,304..305,308..310,313,340,344,393..394,
                     398,402,418,421..422,425..426,429)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 msslpvgath eslresvppa saaqinarid rlpaaravwt lvlliatggw fefydlffta
       61 yvgpglvksg lystttasff gfsglgafva asfaglfigt fcftgladry grrtmftasl
      121 lwysaatcvm alqtsapain lwrliagigv gielvtidty vselvpkhmr grafafvhlv
      181 qytavptval lawwfvprap lgfdgwrwvv mfgaagalia wairrnvpes arwlaqrgrh
      241 deaarvlatl eakieaqtgr llpapplate sataaplrka rfseiwqppy rrrtitllvf
      301 nlfqaigfyg faswvptllv skgvtithsl lyafviaasn pfgpligmai adrierktlv
      361 vlsalaiavf gslfamqtsp vmlmvlgvli tlgatllsvg yhayqvelfp trmratavgf
      421 vysmsrlsam fsgfmiafal rhfgvpgvfa litgamvavm aaiglfgprt nnrslddish
//
LOCUS       WP_176079257             384 aa            linear   BCT 11-JAN-2025
DEFINITION  glycerate kinase [Paraburkholderia tropica].
ACCESSION   WP_176079257
VERSION     WP_176079257.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004951
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..384
                     /product="glycerate kinase"
                     /EC_number="2.7.1.31"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0008887 - glycerate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38557
     Region          11..362
                     /region_name="GlxK"
                     /note="Glycerate kinase [Carbohydrate transport and
                     metabolism]; COG1929"
                     /db_xref="CDD:441532"
ORIGIN      
        1 msnpsfeapv vviapdsfkg slsadgvaaa iaegirrara daeiricpma dggegtldam
       61 lsvggerril nvegaalarr datvgllhdg caivetaeiv gitdpvgmgv pvaarstrgm
      121 geaisallde gvrrfyvalg gsstndggag llaglglqlf daadnalapt pealtrvarv
      181 disgldarls easfvamsdv dnpltgdhga tavfgpqkgv tpgevapida algrfadlle
      241 aalgrtarde agagaagglg falrmlgasf epgaevvart igldqalaga qwlitgegrs
      301 dvqtlhgkap fiacrhaqaa gvpatllsga vdsaalprla ehfsgcfspa pgpitletai
      361 rdaaallane aeqltrlkyg aarp
//
LOCUS       WP_176079268             394 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Paraburkholderia tropica].
ACCESSION   WP_176079268
VERSION     WP_176079268.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..394
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44031
     Region          50..379
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mqeelveped hataaaflpl palppaldgr dganrarggi aqtsarndie avrlwlaeyv
       61 asphtlrsyr keavrlmlws tntlgkplss ltredfvlye qflaapsadw adperprrgr
      121 errlfdgpla prsrrqalgi lgglfnylva agylagnpla lrrsrmpqaa rsrrveryld
      181 qalwqqvldg idafpqdtpr erqhyercrw lirflyrtal raseaaqara gdferrrgrw
      241 wlrvvgkggv egdvpasdel madfaryraf hglpgtpapg etrpvvlgva gkderpltst
      301 avylivktvf rrvadrlead dpagadtlrr asthwlrhta athqadagtd lryiqknlrh
      361 asiettglyl hadddarher ttaapttppg diar
//
LOCUS       WP_176079397             583 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Paraburkholderia tropica].
ACCESSION   WP_176079397
VERSION     WP_176079397.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 583)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..583
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=62565
     Region          59..583
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mkitkrlavl pltamvftth aqqsptpaee aaaarantaq qqqlqqqrea qqreaavlae
       61 avrstvprea ayptlphesp cfrierftle vpdtlpapah aagasalpld sfafarewle
      121 hyrgecvgka gldvltkglq qailsrgyvt trvlvspqdl aggtlvfslv pgvvrsivfa
      181 dpdtrgvlrt afpvtggdll nlrdleqgle qmkraasqda smqieptsep gqsdvvvtvr
      241 rtkpwsfvas vdnagtkatg kwqgnvslgi dnplglndif avganqdlsf gnhslgshgf
      301 ngsysvpwgy wtatltgstn tyytplatet gplvssgnaq nvalrlagvl mrgqvdvtga
      361 yvqlgkrfgd sfiedmtipv qhrnntflel gvtnrhyfgv sqfdgtlayr qgigglgatv
      421 dpwpngptyr fhmavldanl svpfaaggqa fryvttvhgq ftndalfyid dltigsrytv
      481 rgfdgetmla aergfywrne lqwpigstgq alyagidygh vygpgtavla gtqlagavig
      541 lrggiparda gfsydmfvgt plykpkafpt arftvgvqas vqf
//
LOCUS       WP_176079412             329 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Paraburkholderia
            tropica].
ACCESSION   WP_176079412
VERSION     WP_176079412.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..329
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34780
     Region          11..316
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 mnsaaepgrf divariaqcv pdlrpaerdv aalilddlas aarasigela rragvsiatv
       61 trfakavgch dvrelklrla qaaavgerfl rgaagqesla kakrgkvakg akgarrdask
      121 anatpdadap latrvygeih aaleqnhell rqapfaeaaa alaqarmiyv fgmgggssal
      181 ademrfrlvr lgrpvasyqd sllqrmvast lapdcvvval sltgrvpell dacriardyg
      241 akliavtapa splaaladwl vpivasetdf iykpsssrya mlmaldvlvt elalaqpess
      301 rellrrmkht ldahrgtagr ggerqplgd
//
LOCUS       WP_176079416             232 aa            linear   BCT 11-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Paraburkholderia
            tropica].
ACCESSION   WP_176079416
VERSION     WP_176079416.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..232
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24927
     Region          22..232
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 msyvfepapq ayvpvagssa hfpvrriycv grnyeahare mghdpnrepp fffakpadav
       61 lfvppgaaad fpypaqsknv hfemelvaai gkagknipve saldhvygya lgldmtrrdl
      121 qaeakklgrp wdtakgfdhs apigpihpva qvgqlakgsi wlsvndeekq rsdisqmiwp
      181 vadtiaylst lfelkagdli ftgtpegvga vvkgdlmkgg vdglgeiavr vv
//
LOCUS       WP_176079468             401 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent rRNA methyltransferase [Paraburkholderia
            tropica].
ACCESSION   WP_176079468
VERSION     WP_176079468.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..401
                     /product="class I SAM-dependent rRNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0006364 - rRNA processing [Evidence IEA]"
                     /calculated_mol_wt=43956
     Region          4..400
                     /region_name="RlmK"
                     /note="23S rRNA G2069 N7-methylase RlmK or C1962
                     C5-methylase RlmI [Translation, ribosomal structure and
                     biogenesis]; COG1092"
                     /db_xref="CDD:440709"
ORIGIN      
        1 mnivtlkpsk eksllrrhpw vyanaidrve gkpasgatvi vrahdgrfla raaysphsqi
       61 rarvwsfden epidhaffkr rvqralahrq amvrdtgavr lifgeadglp glivdwyted
      121 vaqnprgqlv cqfmaagvea wkeaivnalt satgcpnvye rsdvsirdke gleqitglla
      181 gdeppetiia nengvryhvd vrnghktgfy vdqrdnralv qtcaqdrdvl ncfcytggfs
      241 laamkggakr vvsidssgea lntaqknvqa ngfdagratw ldadafktlr rlheegerfd
      301 lvvldppkfa asrehvdraa raykdinltg fkllrpggll ftyscsgaid aelfqkivag
      361 aaadakvdar iikrlgagvd hplltafpeg eylkglllqi a
//
LOCUS       WP_176079505             129 aa            linear   BCT 11-JAN-2025
DEFINITION  single-stranded DNA-binding protein [Paraburkholderia tropica].
ACCESSION   WP_176079505
VERSION     WP_176079505.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Bianco,P.R.
  TITLE     The tale of SSB
  JOURNAL   Prog Biophys Mol Biol 127, 111-118 (2017)
   PUBMED   27838363
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Theobald,D.L., Mitton-Fry,R.M. and Wuttke,D.S.
  TITLE     Nucleic acid recognition by OB-fold proteins
  JOURNAL   Annu Rev Biophys Biomol Struct 32, 115-133 (2003)
   PUBMED   12598368
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Murzin,A.G.
  TITLE     OB(oligonucleotide/oligosaccharide binding)-fold: common structural
            and functional solution for non-homologous sequences
  JOURNAL   EMBO J 12 (3), 861-867 (1993)
   PUBMED   8458342
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..129
                     /product="single-stranded DNA-binding protein"
                     /GO_function="GO:0003697 - single-stranded DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=13305
     Region          1..93
                     /region_name="Ssb"
                     /note="Single-stranded DNA-binding protein [Replication,
                     recombination and repair]; COG0629"
                     /db_xref="CDD:440394"
ORIGIN      
        1 midalvagkl wktpeerrsn agkafvianv raadgegegl fvnvvafsds akaallaled
       61 gdsvslagtl kigtyegrdg svkpsvsmva skvltayhva rkrkavadaq aadgrlgrep
      121 amaddaldf
//
LOCUS       WP_176079545             473 aa            linear   BCT 11-JAN-2025
DEFINITION  TniQ family protein [Paraburkholderia tropica].
ACCESSION   WP_176079545
VERSION     WP_176079545.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Li,Z., Zhang,H., Xiao,R. and Chang,L.
  TITLE     Cryo-EM structure of a type I-F CRISPR RNA guided surveillance
            complex bound to transposition protein TniQ
  JOURNAL   Cell Res 30 (2), 179-181 (2020)
   PUBMED   31900425
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Kholodii,G.Y., Mindlin,S.Z., Bass,I.A., Yurieva,O.V.,
            Minakhina,S.V. and Nikiforov,V.G.
  TITLE     Four genes, two ends, and a res region are involved in
            transposition of Tn5053: a paradigm for a novel family of
            transposons carrying either a mer operon or an integron
  JOURNAL   Mol Microbiol 17 (6), 1189-1200 (1995)
   PUBMED   8594337
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10534787
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..473
                     /product="TniQ family protein"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=52489
     Region          35..173
                     /region_name="TniQ"
                     /note="pfam06527"
                     /db_xref="CDD:461938"
ORIGIN      
        1 mtfpfrsrlp ggwpedapsr silyslaphg csgedreslg syltrlceay emtrwtltnt
       61 iigpaaeell hvsgdrmsrd vgraayrlnv sglteqvshw aytlnhltgr dnlqlctllp
      121 lrnlvsdfvl qaererfcpv cfeedvrrkr dcygrllwti davkacplhq lqlvgqpqak
      181 qrrgvsrset gctaqrsttq hkigespiqq pasdfdvets rliaelldda vifsqagysa
      241 saqtvfltha inhlfegspa rfaahlgvnk sqthgwvkgt vqmsftrlvq tafccgcaia
      301 dillgnrvvl slrpmpdgqr rrltnrrvsg arranevvra eldelirsgd atnatgaata
      361 vgislkflra nfpeqherlv rlgreraesv rreateafne mylseanalr aagvypsrrr
      421 vlgrlegkvm vgrfrriqna hrnalaatgm snsgglgwrt atrcdlepkt rgi
//
LOCUS       WP_176079576             543 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Paraburkholderia tropica].
ACCESSION   WP_176079576
VERSION     WP_176079576.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..543
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58620
     Region          1..531
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 mqydyvivgg gsggaslagr laercpdasi alieagphte rnlfvnmpmg vaalvpfrnk
       61 nnyayqtvpq pglngrrgyq prgrgfggss ainamiytrg hpldydewar lgctgwawdd
      121 vlpyflraed narganawhg aggplgvsdl rernavaerf vqaaleagfp anddfngahq
      181 egvgfyqvtq rggerctvar aylygkprpn lhliadatvl rvsfdgvrat gvdvvragrs
      241 eriearaevi laagafntpq llmcsgigpa ahlrehgiav qhdapdvgrn lidhidftyn
      301 krvhssetvg yslrgaarmv pglvrylrgr rgmfttnvae aggflksrpe lerpdlqlhf
      361 ctalvddhsr rlhwghgysl hvcvlrpasr gtvtlasada reapvidprf lsdardldll
      421 vegtriarri ldapallrmg greiytqagq sdaelratia thadtiyhpv atcrmgsdaq
      481 svvdpqlrvr gathlriada svmptliggn tnaptvmige raadlivaar resasthsaq
      541 mta
//
LOCUS       WP_176079620             224 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein,
            partial [Paraburkholderia tropica].
ACCESSION   WP_176079620
VERSION     WP_176079620.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         <1..224
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
     Region          <1..219
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 lapatasgkn vtpriaakld vaqisditav enadtferpi yagnaiatvq sadpvkvitv
       61 rttafdavaa eggnvsveki eaaadngkaq fvnrevtkld rpeltsakii vsggrglgsg
      121 enytkvlepl adklnaalga sraavdagyv pndyqvgqtg kivapqlyva igisgaiqhl
      181 agmkdskviv ainkdeeapi ftvadyglvg dlftavpelv ntla
//
LOCUS       WP_176079595             204 aa            linear   BCT 11-JAN-2025
DEFINITION  YbhB/YbcL family Raf kinase inhibitor-like protein
            [Paraburkholderia tropica].
ACCESSION   WP_176079595
VERSION     WP_176079595.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Corbit,K.C., Trakul,N., Eves,E.M., Diaz,B., Marshall,M. and
            Rosner,M.R.
  TITLE     Activation of Raf-1 signaling by protein kinase C through a
            mechanism involving Raf kinase inhibitory protein
  JOURNAL   J Biol Chem 278 (15), 13061-13068 (2003)
   PUBMED   12551925
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Serre,L., Pereira de Jesus,K., Zelwer,C., Bureaud,N., Schoentgen,F.
            and Benedetti,H.
  TITLE     Crystal structures of YBHB and YBCL from Escherichia coli, two
            bacterial homologues to a Raf kinase inhibitor protein
  JOURNAL   J Mol Biol 310 (3), 617-634 (2001)
   PUBMED   11439028
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004829
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..204
                     /product="YbhB/YbcL family Raf kinase inhibitor-like
                     protein"
                     /calculated_mol_wt=21199
     Region          47..203
                     /region_name="PEBP"
                     /note="Uncharacterized conserved protein,
                     phosphatidylethanolamine-binding protein (PEBP) family
                     [General function prediction only]; COG1881"
                     /db_xref="CDD:441485"
ORIGIN      
        1 mrnrrvtaap altaiarasv iavkaarvgv alllicagar vqaaehfavs sanwhdgaqv
       61 asaqifnesg cegrnhspql swrnapagtr sfavtvfdpd apgrgwwhwa vaniparvas
      121 lpenasasga lkklgaiear ndfggdgygg pcpppgkphr yvvtvyalrv dklalapgrp
      181 gtmfeheieg aalgsatitv tygr
//
LOCUS       WP_176079624             393 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Paraburkholderia
            tropica].
ACCESSION   WP_176079624
VERSION     WP_176079624.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Hamed,R.B., Batchelar,E.T., Clifton,I.J. and Schofield,C.J.
  TITLE     Mechanisms and structures of crotonase superfamily enzymes--how
            nature controls enolate and oxyanion reactivity
  JOURNAL   Cell Mol Life Sci 65 (16), 2507-2527 (2008)
   PUBMED   18470480
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Holden,H.M., Benning,M.M., Haller,T. and Gerlt,J.A.
  TITLE     The crotonase superfamily: divergently related enzymes that
            catalyze different reactions involving acyl coenzyme a thioesters
  JOURNAL   Acc Chem Res 34 (2), 145-157 (2001)
   PUBMED   11263873
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11240944
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..393
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42476
     Region          37..377
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
ORIGIN      
        1 mnarpeavrh aavgtsaqte alspeqsevl vrvvnrvaiv tlnrpaalna lshamvrela
       61 vllermrhdp evvalvlega gpkgfcaggd vraidrlara gerlgeqgwq qffvdeyrld
      121 yalhtfdkpv valldgvtmg ggmglgqaas lrvattrtki ampetrigll pdvgathfla
      181 rmpahmelyv gltgallnga dalhlhladv cvpgdwldgy earlaqvsfd ggvydglrqv
      241 fetsghdaia splaarepli arhfdrqarv geivaslrad legappgdar awleatldal
      301 thysptmlev treallrgrh atlaesfrme lgivvraiee gdfcegvrah lvdkdrtphw
      361 spatladlre prvqhflasp wraedhplad lga
//
LOCUS       WP_176079635             669 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha
            [Paraburkholderia tropica].
ACCESSION   WP_176079635
VERSION     WP_176079635.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Lee,C.K., Cheong,H.K., Ryu,K.S., Lee,J.I., Lee,W., Jeon,Y.H. and
            Cheong,C.
  TITLE     Biotinoyl domain of human acetyl-CoA carboxylase: Structural
            insights into the carboxyl transfer mechanism
  JOURNAL   Proteins 72 (2), 613-624 (2008)
   PUBMED   18247344
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Jitrapakdee,S. and Wallace,J.C.
  TITLE     The biotin enzyme family: conserved structural motifs and domain
            rearrangements
  JOURNAL   Curr Protein Pept Sci 4 (3), 217-229 (2003)
   PUBMED   12769720
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469140
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..669
                     /product="acetyl/propionyl/methylcrotonyl-CoA carboxylase
                     subunit alpha"
                     /EC_number="6.4.-.-"
                     /GO_function="GO:0004075 - biotin carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016421 - CoA carboxylase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=71424
     Region          1..465
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          601..665
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(623,632..634,641)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            633
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
ORIGIN      
        1 mfnkilianr geiacrvaat crrlgvksva vysdadanak hvaacdeavh igeasaaqsy
       61 lrieriiaaa katgaqaihp gygflsenee fgraceeagi vfigppvaai aamgskaaak
      121 almhaaavpl vpgyhgddqd aallqreada mgypvllkas aggggkgmrv versedfaaa
      181 lasckreaas sfgndrvlie kylqrprhve vqvfadshgg avylfdrdcs vqrrhqkvle
      241 eapapgladd vrramgeaav aaaravdyvg agtvefimtg anfyfmemnt rlqvehpvte
      301 mitgldlvew qlrvaagepl plaqsqlavt ghaleariya enpvrgflps tgtlkhlhmp
      361 agvefrlgda gqrasvrids gvregdtitp fydpmiakli vhgatradal armqraleec
      421 evvgpstnve flhrlvtcep fanadldtgl ierhhdalfa prdrplreal alasaaligr
      481 egggvntasp wqtlahwrln sgftqtfkwr dverdtpiev afahdggvqt lacaasderf
      541 twwrgasane ygvtigdtrv tgrvfidgdv fhvfclgaal sfewqnllah aadaehgegr
      601 ltapmpgkvi avlvepgavv ekgaplivme amkmehtiga paagkvtevl ygvgdqvadg
      661 aqllmlete
//
LOCUS       WP_176079646            1061 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Paraburkholderia tropica].
ACCESSION   WP_176079646
VERSION     WP_176079646.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..1061
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=113985
     Region          1..1043
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mniskffidr pifagvlsvl illagvialf qlpiseypev vppsvvvhaq ypganpkvia
       61 eavaapleeq ingvenmlym qsqansdgnl tltvtfrlgt dpdkatqlvq nrvnqalprl
      121 pedvqrlgit tikssptltm vvhlispnnq ydmtylrnya llnvkdrlsn iqgvgevqlw
      181 gagdyamrvw ldpqkvaqrn ltaqdvvnai reqnvqvaag vigaspsvpg tplqlnvnar
      241 grlrtesefg diivktnpdg gvtylrdiar ielaaseygl rslldnkpav alainqapga
      301 nslaiseqvr aamkdlkqdm pagvdykivy dptqfvrssi eavihtllea ialvvivviv
      361 flqtwrasii pliavpvsiv gtfslllafg fsinalslfg mvlaigivvd daivvvenve
      421 rnianglsar datykamqev sgpiiaialt lvavfvplaf msgltgqfyk qfamtiaist
      481 visafnsltl spalsalllr ghdakedwlt rgmnrvlggf ftrfnkvfhr gsesygrgvn
      541 gvlrrkgaml vvyvvllgat vlmsrvvpgg fvpaqdkeyl iafaqlpnga sldrtesvir
      601 emsaialkqp gvesavafpg lsvngftnss sagivfvtlk pfkerkgkal aagaiagaln
      661 qqyasikdsf iavfppppvl glgtlggfkm qledhgalgy ealnratqdf vkraaqtpel
      721 gptftnyqin vpqlnvdldr tkakqlgvpv tdvfdtmqiy lgslyvndfn rfgrvyqvrv
      781 qadapfrqka ddilqlktrn aagdmvplss lvtvsptygp emvvryngyt aadinggpap
      841 gyssgqaqaa aeriaaevlp rgvkfewtdl tyqqvlagna giwvfpisvl lvflvlaaly
      901 esltlplavi livpmsvlca ltgvwltqgd nniftqiglm vlvglaskna ilivefarel
      961 ehdghtplsa aieasrlrlr pilmtsiafi mgvvplvlss gagsemrham giavffgmlg
     1021 vtafgllltp vfyvvlrtla ggkihvaqkd nahapkhtvd a
//
LOCUS       WP_176079691             161 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA thioesterase [Paraburkholderia tropica].
ACCESSION   WP_176079691
VERSION     WP_176079691.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..161
                     /product="acyl-CoA thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18171
     Region          3..125
                     /region_name="YciA"
                     /note="Acyl-CoA hydrolase [Lipid transport and
                     metabolism]; COG1607"
                     /db_xref="CDD:441215"
ORIGIN      
        1 mnfhtrkwvk pedlnpngtl fggsllrwid eeaaiyaicq ldnqrvvtkf isevnfvssa
       61 rqgdiielgm tatdfgrtsi tlrcevrnkv trksiltier mvfvnmdaeg kpaphgrdri
      121 ryaeeayery rqtvhtavda taaaaekeae realnedeav h
//
LOCUS       WP_176079748             579 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein
            [Paraburkholderia tropica].
ACCESSION   WP_176079748
VERSION     WP_176079748.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 579)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..579
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=62892
     Region          8..579
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 mknknrffav plgvlvplav haqtspdvaa aranaqqdqq vqqqrdaqqr aatvaapavr
       61 sdvpakgewp dlpvetpcfr idtfaldvpa tlpddmrakg asalpqdrfa farewlehyr
      121 gqcvgkrgld tlvkgvqqti lsrgyvttrv mlpaqdlsgg alklalipgv irklgfkdat
      181 trgtwktafp ardgdvlnlr dleqgmeqmk rvssqdatme lvaasvpges dveiavarak
      241 pwtfvasvdd sgtretgsii gtvtlgidnl lglndiltag fnqdlqfgdh gvgthgwngs
      301 ysipwgywta tlfgytntyy envagvnqty vvsgnsqtag vklqrvlrrs qsdvfgaefq
      361 likrfgasfi edteiaaqhr dntfielglt drhyfgasqf dgtlayrqgi gwlgaspdta
      421 dgpsyrfhma tldanlsvpf avagqrlayv gtihgqytnd elnyiddlsi gsrytvrgfd
      481 getmlaaerg fywrnelqyp igstgqafya gldyghvwgp saqylvgtql agavvglkga
      541 vrtrfailsy dvfagtpvyk padfpasrvt lgfqvtgqf
//
LOCUS       WP_176079760             455 aa            linear   BCT 11-JAN-2025
DEFINITION  TniQ family protein [Paraburkholderia tropica].
ACCESSION   WP_176079760
VERSION     WP_176079760.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Li,Z., Zhang,H., Xiao,R. and Chang,L.
  TITLE     Cryo-EM structure of a type I-F CRISPR RNA guided surveillance
            complex bound to transposition protein TniQ
  JOURNAL   Cell Res 30 (2), 179-181 (2020)
   PUBMED   31900425
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Kholodii,G.Y., Mindlin,S.Z., Bass,I.A., Yurieva,O.V.,
            Minakhina,S.V. and Nikiforov,V.G.
  TITLE     Four genes, two ends, and a res region are involved in
            transposition of Tn5053: a paradigm for a novel family of
            transposons carrying either a mer operon or an integron
  JOURNAL   Mol Microbiol 17 (6), 1189-1200 (1995)
   PUBMED   8594337
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10534787
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..455
                     /product="TniQ family protein"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /GO_process="GO:0032196 - transposition [Evidence IEA]"
                     /calculated_mol_wt=49206
     Region          32..161
                     /region_name="TniQ"
                     /note="pfam06527"
                     /db_xref="CDD:461938"
ORIGIN      
        1 mdsrrvitrg elfdasahar ievqgegtgr ieqlssvaar laeklclpfi evyrfainqs
       61 psaegavgrl pmisrkllie aigetalkwt tslarftgaa dlrnctllpf qgaiaakrlv
      121 spgrrwcpvc leemadsgiv yeplvwrvse tldcarhrrp lvdicpdcgk gtqsslvana
      181 rvgccrycgs wlgrkavste apsqslfaly caqacedlla lpqcvkdges ilpssvsvsg
      241 lrdcffegng samarrlgel psqlnaycng efpaplhvfl ragyvtgasm hqilvsqdfs
      301 vlgagnaeaq fdlrraepra ydqshvdesl raaildgggm svlqlasqln vevvtlwrrs
      361 pklakelaia haayiakrsa kgqsefvesv rttvadlrsq gvnptasevk rllgdagigl
      421 npwkrtvvhe ltgdvgpler inrcehhsge ddgeq
//
LOCUS       WP_176079780             232 aa            linear   BCT 11-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Paraburkholderia
            tropica].
ACCESSION   WP_176079780
VERSION     WP_176079780.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..232
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24318
     Region          23..228
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 msefavpapv qpsvaiatsn arfpvrrvfc vgrnyashar emgndpdrep pfffmkpsda
       61 vvpangtipy psltsnlhhe vemvvaigrp gfnvsveaap dhvwgygvgi dltrrdvqdq
      121 akkmsrpwdw akgfdssgpc galvpvseig hpstgsiwln vngtprqsgd lnemiwsvae
      181 iiaaisssva iapgdlifsg tpagvaalnp gdtvtagvdg igeisfhisg vs
//
LOCUS       WP_176079774             885 aa            linear   BCT 11-JAN-2025
DEFINITION  AAA family ATPase [Paraburkholderia tropica].
ACCESSION   WP_176079774
VERSION     WP_176079774.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 885)
  AUTHORS   Snider,J., Thibault,G. and Houry,W.A.
  TITLE     The AAA+ superfamily of functionally diverse proteins
  JOURNAL   Genome Biol 9 (4), 216 (2008)
   PUBMED   18466635
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 885)
  AUTHORS   Snider,J. and Houry,W.A.
  TITLE     AAA+ proteins: diversity in function, similarity in structure
  JOURNAL   Biochem Soc Trans 36 (Pt 1), 72-77 (2008)
   PUBMED   18208389
REFERENCE   3  (residues 1 to 885)
  AUTHORS   White,S.R. and Lauring,B.
  TITLE     AAA+ ATPases: achieving diversity of function with conserved
            machinery
  JOURNAL   Traffic 8 (12), 1657-1667 (2007)
   PUBMED   17897320
REFERENCE   4  (residues 1 to 885)
  AUTHORS   Hanson,P.I. and Whiteheart,S.W.
  TITLE     AAA+ proteins: have engine, will work
  JOURNAL   Nat Rev Mol Cell Biol 6 (7), 519-529 (2005)
   PUBMED   16072036
REFERENCE   5  (residues 1 to 885)
  AUTHORS   Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L.
  TITLE     Evolutionary history and higher order classification of AAA+
            ATPases
  JOURNAL   J Struct Biol 146 (1-2), 11-31 (2004)
   PUBMED   15037234
REFERENCE   6  (residues 1 to 885)
  AUTHORS   Frickey,T. and Lupas,A.N.
  TITLE     Phylogenetic analysis of AAA proteins
  JOURNAL   J Struct Biol 146 (1-2), 2-10 (2004)
   PUBMED   15037233
REFERENCE   7  (residues 1 to 885)
  AUTHORS   Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L.
  TITLE     Classification and evolution of P-loop GTPases and related ATPases
  JOURNAL   J Mol Biol 317 (1), 41-72 (2002)
   PUBMED   11916378
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..885
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..885
                     /product="AAA family ATPase"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=96152
     Region          76..715
                     /region_name="RloC"
                     /note="Wobble nucleotide-excising tRNase [Translation,
                     ribosomal structure and biogenesis]; COG4694"
                     /db_xref="CDD:443729"
ORIGIN      
        1 miftriaewi etqqlwlsda arrilvngri rdeefgeila lakahagied paarapqplt
       61 rdmipagaea essitlvelr nlrgvnaias dqsisfsqtg lsviygnnga gksgysrvlr
      121 kacraratgg ailgnvfsdg aadspsaeil irrynaaape llvwnqgspa padlasvavf
      181 dtqcarafnd aegevaytpr gldvlaqlaa lcgkvrerld veingihast tsfadllgdh
      241 aagrllavfd krshlpqyrd elttlaklga edfaeierlt telaeanpaa ratdlrgrka
      301 ridglavrwe lcesklsdek akiavelgea vtaaeasvrl aaeafaaggd llsgtgsdpw
      361 rvllaaardf svqiaypehq fphvdggkcv lcqqdlsaaa aermlrfeqf vqqeaqktaa
      421 aaklkaggaf saialadpsa lmadeallne ieqarpglre alktgdqglv drqrslnemw
      481 aaqrfegaip pfvsqvavlr dlsrtieeda vrfdklaaae grkkseqalk dlksrealag
      541 rlvqiikiad dlalkkklqa ahraadstav srkmsalhse alsadaetaf vrecdalgva
      601 hvpirsttrm ergkakqqvk latagaekvg dvlsegeqra lalasfmaev slvqghgaii
      661 fddpmssldh shrervarrl vqeaairqvi vfthdlafan hladeaaaqr vetsamsvrr
      721 vkqraglvfp elpfagvkvs erlerikkma teadetlrng hierseniir agygrlretw
      781 ergveesiln etvvrfrpgi stqrlravvl edpdyvkihe amarcsyfaa hdtsadanta
      841 tpsvdelrtd ieaarvffad rkkvneetdr rrrellerpa afkqa
//
LOCUS       WP_176079929             563 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paraburkholderia tropica].
ACCESSION   WP_176079929
VERSION     WP_176079929.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 563)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 563)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..563
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=61368
     Region          1..547
                     /region_name="GsiA"
                     /note="ABC-type glutathione transport system ATPase
                     component, contains duplicated ATPase domain
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1123"
                     /db_xref="CDD:440740"
ORIGIN      
        1 mgaaihvrdl timagesvlv drlafdiapg qvlaligesg sgktttalal mgyardgcai
       61 apdsvvnvge rnvtaldaaa qralrgrvvt yiaqsasasf npsrtimdqv veparihktm
      121 praeaekrav elfrelalpn petigaryph qvsggqlqrl maamalitdp dlvildeptt
      181 aldvttqvev lrafrrvvqq rktsavyvsh dlavvaqvad hilvlrhgkm reygesdqil
      241 hapaddytrs llaaarpker hadapddavh aradapllrt dpegtrrapq pllqidalca
      301 gygpldaqgr pqnrildkvd lklyrgqaig vigesgsgkt tlaravagli apfegriafd
      361 gktmspqldq rsrgelrriq ivfqiadtal npahtieril arplqfyhgl qgkalrtria
      421 qlldmvrlpr tlmerppaal sggqkqrvnl aralaaepdl llcdevtsal dtvvgaavld
      481 lmadlrkdlg vsylfishdl htvraicdei vvmqhgrkvt qvaredydrg phhpyyells
      541 rsvpelrrgw idevqlpkte tva
//
LOCUS       WP_176079935             269 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paraburkholderia tropica].
ACCESSION   WP_176079935
VERSION     WP_176079935.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..269
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29035
     Region          8..241
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mrpnpfvrga livlvvlila flmipvlivv pisfsdtrfm tfpppalslr wyasffgnpe
       61 wlsaarvtli aslaaaciat pvgvaaayai ehgehplirp lktvlmlpmi vpiiivavgv
      121 ffvyskfgyv ntlggliiad smlglpyvli svgadlrsfd haqemaarsl gmnrlrsflt
      181 vtlpqirssv isgavfvfiq aldetvvalf vsggdnqtlt rrmfvtlrde idptiaaist
      241 mltaltlalv llvvvsrrsg qrqlqpara
//
LOCUS       WP_176079957             472 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Paraburkholderia tropica].
ACCESSION   WP_176079957
VERSION     WP_176079957.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..472
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=50651
     Region          1..390
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 msfatlglid plqrtlrdln yqtptpvqvk aipavlsgkd vvaaaqtgtg ktagfalpll
       61 qrlvqngpav ssnrarvlvl vptrelaeql vqsfieygkg ldlrflaayg gvsinpqmmk
      121 lrkgvdvlva tpgrlldlhr qnavqfdqvq tlvldeadrm ldlgfareln avfeavparr
      181 qtllfsatfs eevrtmaagi lrnpvdisvs ppnataskik qwvvtvdkrn kpelfmhlva
      241 rnkwqnalvf vktrngvdyl atllekagys vdtihgdkpq parlralerf karevqmlva
      301 tdvaargldi ddlplvinvd lpivaqdyvh rigrtgraga sgvavslvca deapqlaaie
      361 alirqtlrre eepgfladhr vpetsasgei lkkpkkpkka kvpqvvagvl pgkqaqpgdg
      421 pgpgwvnpfs tqkprakpaa rksaagsgga rkpvgktggk psgkpaggrg kr
//
LOCUS       WP_176079967             154 aa            linear   BCT 11-JAN-2025
DEFINITION  pyridoxamine 5'-phosphate oxidase family protein [Paraburkholderia
            tropica].
ACCESSION   WP_176079967
VERSION     WP_176079967.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Ahmed,F.H., Carr,P.D., Lee,B.M., Afriat-Jurnou,L., Mohamed,A.E.,
            Hong,N.S., Flanagan,J., Taylor,M.C., Greening,C. and Jackson,C.J.
  TITLE     Sequence-Structure-Function Classification of a Catalytically
            Diverse Oxidoreductase Superfamily in Mycobacteria
  JOURNAL   J Mol Biol 427 (22), 3554-3571 (2015)
   PUBMED   26434506
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10472314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..154
                     /product="pyridoxamine 5'-phosphate oxidase family
                     protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16470
     Region          2..89
                     /region_name="Putative_PNPOx"
                     /note="Pyridoxamine 5'-phosphate oxidase; pfam01243"
                     /db_xref="CDD:426149"
ORIGIN      
        1 mlndavlasm kksvlcwlat adangapnvs pkeifcahgp nvvlmanlas pgsaeniahn
       61 pnvcvsfvdp fvqkgfklkg qarllhesde afatlalplt qlagprfpfr slfaieidgv
      121 epiiapsyrl ypetsearqv esamksygvr pdtd
//
LOCUS       WP_176079973             537 aa            linear   BCT 11-JAN-2025
DEFINITION  MDR family MFS transporter [Paraburkholderia tropica].
ACCESSION   WP_176079973
VERSION     WP_176079973.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Kumar,S., He,G., Kakarla,P., Shrestha,U., Ranjana,K.C.,
            Ranaweera,I., Willmon,T.M., Barr,S.R., Hernandez,A.J. and
            Varela,M.F.
  TITLE     Bacterial Multidrug Efflux Pumps of the Major Facilitator
            Superfamily as Targets for Modulation
  JOURNAL   Infect Disord Drug Targets 16 (1), 28-43 (2016)
   PUBMED   27052334
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   4  (residues 1 to 537)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13025406
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..537
                     /product="MDR family MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56548
     Region          37..533
                     /region_name="MFS_LmrB_MDR_like"
                     /note="Bacillus subtilis lincomycin resistance protein
                     (LmrB) and similar multidrug resistance (MDR) transporters
                     of the Major Facilitator Superfamily; cd17503"
                     /db_xref="CDD:341046"
     Site            order(43..44,47..48,51,83,133..134,136..138,141,161,
                     164..165,168,295,298..299,302..304,307,335,339,391..392,
                     396,400,416,419..420,423..424,427)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341046"
ORIGIN      
        1 msaksaqsvq saqsaqstpa aeetvslraw vavlggvfgc fmagmnvhvt naslpdirga
       61 lgasfeegsw ittaylvaei vvipltgwlv qvfsarrvll vgasgflafs lacslaptig
      121 smiaaralqg afggvlipls fqliatelpa srralgmalf avannvaqaa gpslggwltd
      181 ayswrwifyl qippalalia aiawsikpvp vdlarfknad wfgiltmvvg lsalqvvlee
      241 ggrkdwfash divllssvaa lglvafvaie lkraqpfinl rllgrynfgv aslmqfmfga
      301 vvfgvvflvp nyfaqtqgys ardigmtmip yglvqfamsf atpplmrvvg prmaivagfa
      361 lvavgclmni hlgadsaanv ivpslivrgv gqslvvials vmavdgieka qlgsasgvfn
      421 mvrnvggaig ialasqivve reklhamrig esitpyasaf qermaalsrl vaqrhlahad
      481 alprarldgv hetalaiieq rvlheallma ysdafliagv amlacmtaaf slrgasr
//
LOCUS       WP_176079979             294 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Paraburkholderia tropica].
ACCESSION   WP_176079979
VERSION     WP_176079979.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..294
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31922
     Region          12..256
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(24,105,107,109..110,138,188,209,212,225,227,256)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mstqsfpshq agdftihais dgylnasldf lsnidateas tmqrdageqt ptavhincyl
       61 lrgarriilv dggaggikqw ggrlqdnlll agiepsaidt illthahpdh vgglvnadgr
      121 mafpnaelvv ntreirfwqd danlaraser argnfeiarr vfdaygdira fdagevlpgi
      181 ramplpghte ghtgyivear erslliwgdv vhfphiqiqr pdvsiafdqd aslaastrsr
      241 lldvvssegl lvagmhlgel gfariarkkg gydlryerea mppqavrqda pnal
//
LOCUS       WP_176079999             383 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Paraburkholderia tropica].
ACCESSION   WP_176079999
VERSION     WP_176079999.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Laub,M.T. and Goulian,M.
  TITLE     Specificity in two-component signal transduction pathways
  JOURNAL   Annu Rev Genet 41, 121-145 (2007)
   PUBMED   18076326
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Hoch,J.A. and Varughese,K.I.
  TITLE     Keeping signals straight in phosphorelay signal transduction
  JOURNAL   J Bacteriol 183 (17), 4941-4949 (2001)
   PUBMED   11489844
REFERENCE   3  (residues 1 to 383)
  AUTHORS   West,A.H. and Stock,A.M.
  TITLE     Histidine kinases and response regulator proteins in two-component
            signaling systems
  JOURNAL   Trends Biochem Sci 26 (6), 369-376 (2001)
   PUBMED   11406410
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
REFERENCE   5  (residues 1 to 383)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   6  (residues 1 to 383)
  AUTHORS   Alex,L.A. and Simon,M.I.
  TITLE     Protein histidine kinases and signal transduction in prokaryotes
            and eukaryotes
  JOURNAL   Trends Genet 10 (4), 133-138 (1994)
   PUBMED   8029829
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467953
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..383
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=40740
     Region          14..370
                     /region_name="COG4191"
                     /note="Signal transduction histidine kinase regulating
                     C4-dicarboxylate transport system [Signal transduction
                     mechanisms]"
                     /db_xref="CDD:443345"
ORIGIN      
        1 mlrgmidvmp saalavdeqg tivvanaraa llfgysaael svlpldmlvl psqdtdiaep
       61 vgtswvmrga pgsttrpavv rkrdgsqraa qvtssvsfai errpyavlvi dalcgegdeg
      121 dagdvaraqe pgvrragqal mhhdqasdvg dmaaalahev dqpltailsn aqaarrflas
      181 tppnigemle lldeivsdst rahaiirkmr qfgkreqsel saidmgclvc dvmqllhrra
      241 rerhvalssh ienglpmlrg davqlqqvlv nlilnafdam qgmapaerav fvsvgaapgg
      301 rgvriairdc gdgvsdeqma tlfkpfstsk pnglglglsi sriivmghgg hmwaernrer
      361 gmtfqfelpa egattnsgah epl
//
LOCUS       WP_176080051             212 aa            linear   BCT 11-JAN-2025
DEFINITION  RNA polymerase sigma factor [Paraburkholderia tropica].
ACCESSION   WP_176080051
VERSION     WP_176080051.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Sineva,E., Savkina,M. and Ades,S.E.
  TITLE     Themes and variations in gene regulation by extracytoplasmic
            function (ECF) sigma factors
  JOURNAL   Curr Opin Microbiol 36, 128-137 (2017)
   PUBMED   28575802
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446377
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..212
                     /product="RNA polymerase sigma factor"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016987 - sigma factor activity [Evidence
                     IEA]"
                     /GO_process="GO:0006352 - DNA-templated transcription
                     initiation [Evidence IEA]"
                     /calculated_mol_wt=23634
     Region          30..208
                     /region_name="RpoE"
                     /note="DNA-directed RNA polymerase specialized sigma
                     subunit, sigma24 family [Transcription]; COG1595"
                     /db_xref="CDD:441203"
ORIGIN      
        1 meppltpnpl phpdlpdlpd lpdrdiadtv arerprlrsf irrrvidqde aedilqdvfe
       61 elveawrlpe pieqvgawlf rvarnrivdr frkrkevpla dlgggigqsa qsgaepgddh
      121 sdyrldlalp sadggpeaay araalldtlr daldelpasq revfvaheld ghsfkelaaa
      181 tgvgvntlla rkryavlhlr erlraswdgy di
//
LOCUS       WP_176080052             541 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paraburkholderia tropica].
ACCESSION   WP_176080052
VERSION     WP_176080052.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 541)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..541
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=57315
     Region          1..531
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mttpvlevdg ldirigsrri vrgidltiar gervalvges gsgksltala llgladaaqv
       61 sgsvrlagqe llgkseaqwr avrggdiamv fqepmtalnp lwsigrqige slrlhanlrg
      121 aaareraial lrrtgiaepe rkvdcyphql sggqrqrami amalacnprl liadepttal
      181 dvtvrrqivd llielqeada dgrglavlli thdlhlvrrf ahrvavmqhg aiveqgatea
      241 lfaaqrhpyt rklfdsaprr tlapvpddas rvlavdglra gyrarapgwr gvlragtsav
      301 ldgidlhlra getlgvlges gcgkstlaaa ivglvqpvag tirfaglngl dgapqspprr
      361 vlaahvqmvf qdpfgslapr ltvgeiveeg lalhhpdlpa darrarvaal laetglpada
      421 asrlpaafsg gqrqriaiar alavnprmlv ldeptsaldv siqqqilall ttlqrrhgls
      481 yvfishdidv lravshrlvv mhggkivetg dtlavldapa haytrklvsa aqlapaslaa
      541 a
//
LOCUS       WP_176080058             402 aa            linear   BCT 11-JAN-2025
DEFINITION  aminotransferase class V-fold PLP-dependent enzyme
            [Paraburkholderia tropica].
ACCESSION   WP_176080058
VERSION     WP_176080058.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 402)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424849
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..402
                     /product="aminotransferase class V-fold PLP-dependent
                     enzyme"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0031071 - cysteine desulfurase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006534 - cysteine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=41936
     Region          12..399
                     /region_name="CsdA"
                     /note="Selenocysteine lyase/Cysteine desulfurase [Amino
                     acid transport and metabolism]; COG0520"
                     /db_xref="CDD:440286"
ORIGIN      
        1 mttntiltda vvdalraqtp gtrttthfnh agaslpssat lsaihaqler eatrgpmeag
       61 vaasaitdda ralaatlfna qpdeialtgg nsqgwgaafa alggwkpger mlvgrhewgg
      121 nlaamqfaaq ragatidvip sradgtidta alasmiderv rllaltwlpa ngglinpada
      181 vgaiarrfdi pyfvdaaqaa gqlpidvrai gcdvlcaapr kalraprgtg llyvrrafld
      241 rltpayvdry sapldargep ylrndagrfe saetsmalra glakalseal aigvpairrr
      301 idqmatrlrq rlagieavel ldegversgl vafnlagrdp qavqaalaar gisiglsgva
      361 ytpldmrarg ltnvarasvs ylttdaeiar lvaaiaeias va
//
LOCUS       WP_176080088             322 aa            linear   BCT 11-JAN-2025
DEFINITION  type II secretion system F family protein [Paraburkholderia
            tropica].
ACCESSION   WP_176080088
VERSION     WP_176080088.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Clock,S.A., Planet,P.J., Perez,B.A. and Figurski,D.H.
  TITLE     Outer membrane components of the Tad (tight adherence) secreton of
            Aggregatibacter actinomycetemcomitans
  JOURNAL   J Bacteriol 190 (3), 980-990 (2008)
   PUBMED   18055598
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Peabody,C.R., Chung,Y.J., Yen,M.R., Vidal-Ingigliardi,D.,
            Pugsley,A.P. and Saier,M.H.
  TITLE     Type II protein secretion and its relationship to bacterial type IV
            pili and archaeal flagella
  JOURNAL   Microbiology (Reading) 149 (Pt 11), 3051-3072 (2003)
   PUBMED   14600218
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009000
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..322
                     /product="type II secretion system F family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=35031
     Region          147..319
                     /region_name="TadB"
                     /note="Flp pilus assembly protein TadB [Intracellular
                     trafficking, secretion, and vesicular transport,
                     Extracellular structures]; COG4965"
                     /db_xref="CDD:443991"
ORIGIN      
        1 mnttfltaav llfvavvmsc qsawvwwngr hgaaakrlaa rlealtagst srrealsilk
       61 arrlgaatpl aralpflrsl dawlmqsglp wslgrlgatc tafaliamlg aslarvplag
      121 afgaalagal lpllyvrrhr arrlrhferq lpdicdmlar alraghafss aidmagtefa
      181 epaggefrit fdeinygvsl ndalaglatr mpvrdlrylv iavliqretg gnlaelfdsi
      241 awlirerfkl fdkvrvlsae grlsawvlgm lpigsaalis ivnptfldvf wndpvgvrll
      301 dgivismicg avwirrivri rv
//
LOCUS       WP_176080138             290 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Paraburkholderia tropica].
ACCESSION   WP_176080138
VERSION     WP_176080138.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..290
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31494
     Region          48..285
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mlkpevdslv phvpfdrrtf lkaalgsgfa aavlpvsaqt ihtdseglda gevafqsngt
       61 lipayraqpr gkthlpviiv iheifgvheh iadvcrrfak lgylaiapdf fvregdasvy
      121 ptiqqineni vskvpdaqvl ddidaaiawa gqhggdvkrv gvngfcwggr yawlyaehnp
      181 riktavawyg rvvgdhtant pqnpldlagt lqvpvlglyg rqdtsipqdt leqmkaaiaq
      241 gpqgargsqf vvyddaghaf fadyrpsyrk adaedgwkra iawfkehgvg
//
LOCUS       WP_176080157             330 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Paraburkholderia tropica].
ACCESSION   WP_176080157
VERSION     WP_176080157.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..330
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=36557
     Region          20..328
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mtsalastav qaaiestfeh fgfltlpnfs miafssavev lrmanyvgrg dhyrwsvytl
       61 dgeparasng iavrpaqrld lnklpdvliv cggiriqeav dervravlae vaargiplgg
      121 ictgayalit sglldgyrca vhwenlstfy esfpdvqfad elfvidrdrl tctggtapld
      181 lmlelvgarl grqtaakvse qfilerirgs tdlqpipvda rvgfsraelv evvrlmeani
      241 keplsleela rlvrlsqrhl qrmfkeylnv spthyylslr lkrarellrt tdtsiarvts
      301 icgfnspchf skayrvqfgh apsherrapg
//
LOCUS       WP_176080178             290 aa            linear   BCT 11-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Paraburkholderia
            tropica].
ACCESSION   WP_176080178
VERSION     WP_176080178.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..290
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30799
     Region          71..279
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mklvrwgnkg sekpgaldrd grvrdlssvl pdlagaalss aslaglgsld lhslplapad
       61 arlgpcvgqv gkiicvglny sdhaaesnmp vpsepvlffk atssivgpnd dvvippgaqk
      121 vdwevelgvv igeearyvsr eraldyvagy cvvndvsera wqierggqwd kgksadtfap
      181 lgpwlvtrdd ipdpqaldmw ldvdgkryqq gntrtmifdv atvvsyishf mslqpgdvis
      241 tgtppgvgmg qkpapvylra gqvmrlgvag lgeqqqrtva staqasaftr
//
LOCUS       WP_176080179             451 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia tropica].
ACCESSION   WP_176080179
VERSION     WP_176080179.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..451
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=47465
     Region          21..431
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,152,
                     155..156,159,256,259..260,263..265,268,297,301,357..358,
                     362,366,382,385..386,389..390,393)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 msseasqasl haqsavgkam rrllpflllm yvlafldran igfaqkalqh dtglsdaafa
       61 fgagvffagy alfevpsnll lhrmgariwm crimvtwglv saamawvqsp asfyalrfll
      121 gvaeagffpg iifyltqwfp qssraraigl fyfgaplafi fggplsgfli dlhgvgwlag
      181 wkwlflvega lasvvgvwaf wyltdrpdda hwldiderra lvaalrvdag eamahgprda
      241 laalvdrrvl ayaaiyaliq msvygvvffl pqqvaslaga kvglkvglla avpwlcaval
      301 twivprradr fgshrawtvr llvlsglgia vsgaaggvgs aagavvamaa lccaasgfia
      361 aqplfwtfpa relagtasas gialinslgg lggfiaplmr aaadkhfssh aaglvllgfa
      421 slaaavlvli vvpragarta aaferaagha r
//
LOCUS       WP_176080205             390 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Paraburkholderia
            tropica].
ACCESSION   WP_176080205
VERSION     WP_176080205.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Ogasawara,H., Yamada,K., Kori,A., Yamamoto,K. and Ishihama,A.
  TITLE     Regulation of the Escherichia coli csgD promoter: interplay between
            five transcription factors
  JOURNAL   Microbiology (Reading) 156 (Pt 8), 2470-2483 (2010)
   PUBMED   20466769
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..390
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=42107
     Region          203..386
                     /region_name="CsgD"
                     /note="DNA-binding transcriptional regulator, CsgD family
                     [Transcription]; COG2771"
                     /db_xref="CDD:442052"
ORIGIN      
        1 mpaddaadsl gslidaiyda gldarrwpal larlarriga tyvnlsvlap dealsladws
       61 giesgfarry aqhygaldpl vpqvrrwpag tlvtdtmirp qtahassefv qdwvrpqrih
      121 tvafasvmre dgvtavlgal rhtprfyadd eldvlrallp hlrnavrvqr rvtqslqsts
      181 hppadplaal dafdaldsla qcvliadrda hvvfanraas allaqarglr eerqglcapt
      241 ldatqrlram iarasssesg traggamlie raahdaplqv lvaplgthrv iegatavsrr
      301 gtamlvitdp qaarrgveqr lialfgltpa earvagevgk gheprdiaat lqimpstvrt
      361 hlhhvfakta trrqgdlmrl leqialtrgd
//
LOCUS       WP_176080247             169 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paraburkholderia
            tropica].
ACCESSION   WP_176080247
VERSION     WP_176080247.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..169
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17645
     Region          1..139
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mfhehgydav glaalteelg ikapsfyaaf gskaafferv meryaqtalp aadllapgrp
       61 padaladlle raarayakdp rrrgclvlea argagdtesa vlarrvaqer rdeirayvaa
      121 trpeaadavt dyvasvmsgl sgsaregmse arlaavaraa asglhallg
//
LOCUS       WP_176080278             563 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Paraburkholderia tropica].
ACCESSION   WP_176080278
VERSION     WP_176080278.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..563
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=60185
     Region          4..543
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 makatthydf ivigagaagc ltagrlvrdh garvllveag apdrnplihm pagfvkllsn
       61 hdymtfhrsa khphlndrqp sipqgkvlgg gssvnamvyi rgqardyddw vsltgdeswr
      121 yqallphfir legnstfnna ahgvngplkv sdganlsdvs rafvlaaqqn glpynpdfns
      181 gtqrgtgfyq tttfqgrrcs gvdaflapvm ndarltirtg aqvtrilieq nvakgieiqs
      241 gtqreqlfad qivltagalv tpkllmlsgi gpanalarln ipviadlpgv genlqdhhev
      301 pvvafcngrq gyfgqdrgwn qirnglqyla frsgpvasna veagaffnpd dtsgapsiqm
      361 fclptvyldp dvtstkaayg ftlnscvmrp ksrgrvtlqt sdpsatpivy pnylehpddl
      421 rlsiaglrra aqimregpla amvdrivlpd eqavthacaa sdaalaehcr rtvktvyhpa
      481 gtarmgadnd pmavlrndmt vrgiaglrvf dtsswptiis gntvattyav adrgvalmmg
      541 etlpgaspac rstpadaalm pal
//
LOCUS       WP_176080298             176 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Paraburkholderia tropica].
ACCESSION   WP_176080298
VERSION     WP_176080298.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..176
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=18686
     Region          10..162
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mlhsasfagp ltlsvngttr tiegatpdtp llyilrndce lngpkygcgl gqcgactvlv
       61 dgqptrscvv pvaaarnrev ttleglgtld alhpvqrafi deqaaqcgyc lngmimstaa
      121 llarnpspde dairdalrfn lcrcgthlei vravkraaly lqqadkvene qgsear
//
LOCUS       WP_176080296             455 aa            linear   BCT 11-JAN-2025
DEFINITION  dienelactone hydrolase family protein [Paraburkholderia tropica].
ACCESSION   WP_176080296
VERSION     WP_176080296.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10785456
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..455
                     /product="dienelactone hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47957
     Region          33..264
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
ORIGIN      
        1 mafvclatla haalptydpd vepaaplnek ilrvpvqasp rvnlevtvym paqggpfpla
       61 lvnhgasddp pnaprvadqf ipwyflsrgy avampmmrgf aqsgghmtph gcnvlaigad
      121 aasdirkvld vvktlpgvda trivvagksm ggwntlvfga anppdvkgll nfaggvkesd
      181 csqpdaslia saaelgartr lpsiwfygdn dqifssatwh gmfsrytaag ahaelvdyga
      241 fqkdahamta sgaglplwve kadaflagig lpgrevapey lpraaprpsg yaslddlaav
      301 pflsaqqkak iyagflaapl pralaigstd aiwasggfdp artalarcwq tsqycqiyai
      361 dktvvwprqp dapprtqfaa lqnvnavpfl qppgrrayqq ylatgrpraf aiapdgawga
      421 asgvdaisea lvrcgngheg criysvdgdv vwagk
//
LOCUS       WP_176080327             295 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Paraburkholderia tropica].
ACCESSION   WP_176080327
VERSION     WP_176080327.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..295
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32115
     Region          4..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..286
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(108..109,111..112,115,119,121..127,215..220,
                     226..227,229..230)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdrlrsievf vsavdsgsfs aaaraldlsp vmvgkhvrql ethlgaqllq rntraqsltd
       61 agrrfyeesr kvleqlalae asverlraep rgtlrisaat tlgacvvapl aaayqnahpq
      121 vridldlsng vvdlvdegfd vavrigaldp dldliarplg qyrmticaap aylarhgtpr
      181 tladladhrc lshavwdrrn gwrllgdnrw peqtdfvcnd ghglrqaalh gaglllqpai
      241 lvaddlasgr lvsvldafap egrpvyalyr qdrqplpkir sfvdflaeha vaqlg
//
LOCUS       WP_176080381             471 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Paraburkholderia tropica].
ACCESSION   WP_176080381
VERSION     WP_176080381.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..471
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=50729
     Region          15..467
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mnhpappala rrpfpaelld alrsafgerv staeavrahh grdesrfdpq lpdavvfaqs
       61 tedvqtivkl carhqvpiip ygngsslegh llavqggvsi dlsqmnrvls inaedltvtv
      121 epgisrkqln ealrdtglff pidpgadasi ggmsatrasg tnavrygtmr envlgltavl
      181 adgrviktgt rarkssagyd ltrlfvgseg tlgviteitv rlypqpeavs aavcafpsma
      241 eavravieti qmgvpiarve fidalavrai nkhsnlglre khtlffefhg teagvaeqaq
      301 tvqelaaqng gegfewatrp edrsrlwnar hsayfamlql kpgcravttd vcvpisrlae
      361 cvaeteadlk gsalpcpivg hvgdgnfhva ilidpdkpde ideaerlnhr ivqrairmdg
      421 tctgehgvgl hkmdflveeh gadtvdtmra ikhaldphnl mnpgkifswa a
//
LOCUS       WP_176080416             296 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Paraburkholderia tropica].
ACCESSION   WP_176080416
VERSION     WP_176080416.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..296
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=31983
     Region          62..285
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mrepnllips spsplasadv qtnaqpaapl tppasaldar slvstlstrs pnplnatssp
       61 tplraargga sradrvyesl redifelrll pgvwlteaav aarfevsrtp arealqrlqg
      121 dglmrgyvrg gwevapidfs rfddlyemre lietfairrl cerhgrgdra avqaldalga
      181 iwlvpeaarl tdaprvaald eafhlalvda vgnaelsaal rrvtdrihvv hrlgfvyger
      241 vgetyaehae ligairaggv gvaielaerh vrrcraeicr lgaqrlelar gepagv
//
LOCUS       WP_176080463             138 aa            linear   BCT 11-JAN-2025
DEFINITION  sirohydrochlorin chelatase [Paraburkholderia tropica].
ACCESSION   WP_176080463
VERSION     WP_176080463.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Al-Karadaghi,S., Franco,R., Hansson,M., Shelnutt,J.A., Isaya,G. and
            Ferreira,G.C.
  TITLE     Chelatases: distort to select?
  JOURNAL   Trends Biochem Sci 31 (3), 135-142 (2006)
   PUBMED   16469498
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Scott,A.I. and Roessner,C.A.
  TITLE     Biosynthesis of cobalamin (vitamin B(12))
  JOURNAL   Biochem Soc Trans 30 (4), 613-620 (2002)
   PUBMED   12196148
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450325
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..138
                     /product="sirohydrochlorin chelatase"
                     /EC_number="4.99.1.-"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=14184
     Region          1..>122
                     /region_name="SirB"
                     /note="Sirohydrochlorin ferrochelatase [Coenzyme transport
                     and metabolism]; COG2138"
                     /db_xref="CDD:441741"
ORIGIN      
        1 msthgmilfg hgardarwke pftrlaakla aarttdtadn aggpvalafl elmepslpda
       61 iaaqaaqgct vitvvpvffg qgghirrdlp aliaqcqadh pdvqircata vgeddavlda
      121 ivgyclthas ahaspgda
//
LOCUS       WP_176080538             354 aa            linear   BCT 11-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Paraburkholderia
            tropica].
ACCESSION   WP_176080538
VERSION     WP_176080538.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..354
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=38508
     Region          130..351
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 mdksrrnwlk agatitatat gvfsgrifaa qeqqagtkie sippltgqpg vrlvtysvga
       61 qpsigvvldd grlldlkaea harhlklafd pssmlslikv gdpalqqvrt lsehprstll
      121 sletvrllsp iprpdrniyc vgwnyldhfe egqavrtdnk tstlpahpvf ftkgthtmng
      181 pfdpipydaa nststdweae laviigrtgi niseadamny vfgysafndt terdiqqkrh
      241 ggqwfkgksl dghgpmgpwi vtaagvkldd vrvicrvngv ekqnasyqqm yfkipriiae
      301 lsrgmtleag diiatgtpsg vgfarqppef lkpgdimetd ivgvgvirne iqpv
//
LOCUS       WP_176080542             280 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Paraburkholderia tropica].
ACCESSION   WP_176080542
VERSION     WP_176080542.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Luo,D., Wu,Z., Bai,Q., Zhang,Y., Huang,M., Huang,Y. and Li,X.
  TITLE     Universal Stress Proteins: From Gene to Function
  JOURNAL   Int J Mol Sci 24 (5), 4725 (2023)
   PUBMED   36902153
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10084616
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..280
                     /product="universal stress protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0050896 - response to stimulus [Evidence
                     IEA]"
                     /calculated_mol_wt=30488
     Region          3..142
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          155..278
                     /region_name="USP-like"
                     /note="universal stress protein (USP) and similar
                     proteins; cd00293"
                     /db_xref="CDD:467483"
ORIGIN      
        1 mqyktvlayl dpddratarl dfaltlagrf dahliglysp fapdvracft vagsapyyse
       61 ycdalrgqqs aseaafhhal rrvgmdgewi afdfhaeqpi vrrsrhadll vagqttpddd
      121 naslrrrfle qvvmtsgrpv lvlpyagalr atcetiviaw dgsreaarav hdamplleta
      181 krvtvlhiat pnssrtakpg paiadidlml arhavnvdfa qdfsdsdeta getliswvak
      241 ndcdfivaga yghpqwrerl lggvtlalle satvpvllsh
//
LOCUS       WP_176080551             234 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Paraburkholderia tropica].
ACCESSION   WP_176080551
VERSION     WP_176080551.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..234
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25803
     Region          37..233
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 miehrpfhsl gvlrrdwlha rlhfrvgdig raehaplgpl hvwnedefap hsgfglhahr
       61 dveivtwvrs gaitheddag nrarlvadsv qvmsagstif haerndedkp arlfqiwlrp
      121 rtpggtprwa tracareyre grfvtlasgd pgdvrtgalp inadarvmva tlragasvkr
      181 tmsgtrtayl vsdhgdidvg slrvgardgv airrereisl tahqdtdvvi vell
//
LOCUS       WP_176080557             256 aa            linear   BCT 11-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator
            [Paraburkholderia tropica].
ACCESSION   WP_176080557
VERSION     WP_176080557.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..256
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26747
     Region          1..249
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mlveeryrri rallkahgtv svdhmtealg vsretirrdl veldtageir rvhggamfve
       61 selpisvrag irvkekrala rgalahigsg qtlfidagtt tailaealas lsglhivtns
      121 vavanelage raaksgghav hllggafnas vgatyggaai aevhrfhadi allspvgvda
      181 vhgatsfvqe eaemadamsr nakqtlilad yskigvrsrv vscpverisa ivtnsraaks
      241 adaqalaeav raieyv
//
LOCUS       WP_176080640             199 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Paraburkholderia
            tropica].
ACCESSION   WP_176080640
VERSION     WP_176080640.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Eulberg,D., Lakner,S., Golovleva,L.A. and Schlomann,M.
  TITLE     Characterization of a protocatechuate catabolic gene cluster from
            Rhodococcus opacus 1CP: evidence for a merged enzyme with
            4-carboxymuconolactone-decarboxylating and 3-oxoadipate
            enol-lactone-hydrolyzing activity
  JOURNAL   J Bacteriol 180 (5), 1072-1081 (1998)
   PUBMED   9495744
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450212
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..199
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20497
     Region          40..178
                     /region_name="YciW"
                     /note="Alkylhydroperoxidase family enzyme, contains CxxC
                     motif [Inorganic ion transport and metabolism]; COG2128"
                     /db_xref="CDD:441731"
ORIGIN      
        1 msrlplhtve sapeasrpfl erslaangfl pnlvaslana pvaletyltv geingrsglt
       61 laereavqit aaaihgcgfc vaghtavalk kaqlaapvvd alrtgspsgd arldavavft
      121 rdviatrgav pdaaraafaa agfsdanale vilgvslatl cnfannfaqn elnpqlagyr
      181 wnaddylhha tqpatehsa
//
LOCUS       WP_176080641             320 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Paraburkholderia tropica].
ACCESSION   WP_176080641
VERSION     WP_176080641.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12123318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..320
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34349
     Region          6..192
                     /region_name="Cupin_6"
                     /note="pfam12852"
                     /db_xref="CDD:432833"
     Region          225..307
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mpsqvdafsa wlieglevts tlfhvgqycg awqastsghr rasfhlilhg rcwlhlpera
       61 grparsvala agdavflldd vahclsphal ppaagaehar hgamtpldav slaapdslgl
      121 acgffefksg ldglmldllp dhviarhdqp alhgarqife liraeahldp htpspliarl
      181 tsllflytlr aldsndeltp cfwallrrpa faplvaaiva epgrrwttas madfahmsra
      241 rfcklfaelc gqppaqfltl vrmklaasml stgtsmpdaa eqvgyqsesa faqafkrvtg
      301 vqpgawrraa sgdaalaalh
//
LOCUS       WP_176080647             262 aa            linear   BCT 11-JAN-2025
DEFINITION  thioesterase II family protein [Paraburkholderia tropica].
ACCESSION   WP_176080647
VERSION     WP_176080647.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Smith,S., Mikkelsen,J., Witkowski,A. and Libertini,L.J.
  TITLE     Thioesterase II: structure-function relationships
  JOURNAL   Biochem Soc Trans 14 (3), 583-584 (1986)
   PUBMED   3732600
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..262
                     /product="thioesterase II family protein"
                     /EC_number="3.1.2.-"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=28599
     Region          6..240
                     /region_name="GrsT"
                     /note="Surfactin synthase thioesterase subunit [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG3208"
                     /db_xref="CDD:442441"
ORIGIN      
        1 mparhadval tlyclpyagg naatyrgwga llgpriecva ldlpghgrlr atpaladwpa
       61 lidallanld plptrpfaff ghsmgalval elahairerh greplwlgas acvaprerel
      121 ddehpshwla cstaemvael rrlggtpdel ladaefldla lpalradfhl canqarrard
      181 rsirlgcpiw sfggtddsvs eryenlsawr hettggfhqr mlegghffve tareqvirdi
      241 aaalhalafa tathadepay py
//
LOCUS       WP_176080658             313 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Paraburkholderia tropica].
ACCESSION   WP_176080658
VERSION     WP_176080658.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..313
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33458
     Region          75..287
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 malhpqvaqf iaslpppppg pldpaamraa deshvapieq rlpvhavter ilptrtgdvp
       61 vrvyqptaad thpvlvyfhg gafflgslnt hdhvaralan atqcavvavd yrlapehafp
      121 aglndcyaal ewiaqhgrep engigwnget lvvagdssgg nftaavaama ldaglncith
      181 qvlyypsldl dfdveryasl ktnavgngle taslkpfnaf yidsgadpan plvspikrnd
      241 laglpaaliv taecdplrde gelyghalkq agvpvkvhry esaahgfvqy fawlpefqgv
      301 faetadfirn pqr
//
LOCUS       WP_176080668             721 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Paraburkholderia tropica].
ACCESSION   WP_176080668
VERSION     WP_176080668.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 721)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..721
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79622
     Region          63..721
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mkigdlsnpl klsviaallg ssvlrahaad stdaasaaaa asapsastng nvlpmvnvks
       61 aavedpqgpg vgyvakrskt gsktdsavid npqsistvtr qqmddqgvqt vdqalryttg
      121 vytqdgtdvr fdqlrargfd mdsymdglal yqsprfatpr idtylmdrid vlfgpssvly
      181 gqgnpggmvn yvsklptdtp yheveaiign hnnyqlgfdf sgpldkdgtv lyritgigrd
      241 setqvsdikd qriaiapsit fkpdhqtslt lqagyqrdpn gglfnpitas gtiwdnpngk
      301 lgpdqyfgdp ntdgmqrtqy wfgyqfqhaf ndtwsvsqnl rylhideryy qtsvtsgltn
      361 ndtaymwgnv dnehwsqfqv dthaqakfat gpvdhtvlfg ldyrrvlggd dtggglagtl
      421 nlfnpdyasl stitpderld yslaqvgvya qdemryrhwv ftvgiredya stnqqddsav
      481 thatdhaftw raglayefdn givpyvsyar sfepvlgste ngapfvpttg kqlevgvryq
      541 pkgyagyfrl saydlrqnnv astdptnanf qvqtgqvrsq gieaeahani teelkliasy
      601 tylnqrvtqd styegkrpti aprnsaalwa dytfhrgplr nfglggglry mgssegdsan
      661 tfqvpartlv dlafhydwqn wrlglninnl fnheyisyct ntfycywgat rsivgsaryt
      721 w
//
LOCUS       WP_176080664             267 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paraburkholderia tropica].
ACCESSION   WP_176080664
VERSION     WP_176080664.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..267
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=29104
     Region          4..256
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 msipllavqr vdkrypngtv alddvrldie pgefvsllgp sgcgkstllk mfagietpth
       61 ghlrwwggpf atvgapgrrl sfvfqeatlm pwatvaenvr lpldlagvpr reaqaracea
      121 legvglgkfc aarprelsgg mqmraslara lvtepdllll depfgaldef trnrldsdlr
      181 alwlrramtv vfvthsiqea vflssrvvvm qarpgrviad vpidgpaard ddwristpfi
      241 ehtcalskri adahaalqid edsevqs
//
LOCUS       WP_176080681             175 aa            linear   BCT 11-JAN-2025
DEFINITION  DsbA family protein [Paraburkholderia tropica].
ACCESSION   WP_176080681
VERSION     WP_176080681.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Collet,J.F. and Bardwell,J.C.
  TITLE     Oxidative protein folding in bacteria
  JOURNAL   Mol Microbiol 44 (1), 1-8 (2002)
   PUBMED   11967064
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447254
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..175
                     /product="DsbA family protein"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=18683
     Region          21..161
                     /region_name="DsbG"
                     /note="Protein thiol-disulfide isomerase DsbC
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG1651"
                     /db_xref="CDD:441257"
ORIGIN      
        1 msnltppvha adhiqgtads pvtlveygdf ecpycgamyp vvkavqqamg nrlrfvfrqf
       61 pltsmhphal haaqmseaaa avgrfweahd llyenqgaln daalanyaah vgvsasdlks
      121 afegayderi qrdfdgglrs gvngtpslfi ngrrydgdrd arsllealda aaaga
//
LOCUS       WP_176080689             378 aa            linear   BCT 11-JAN-2025
DEFINITION  alkene reductase [Paraburkholderia tropica].
ACCESSION   WP_176080689
VERSION     WP_176080689.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Odat,O., Matta,S., Khalil,H., Kampranis,S.C., Pfau,R.,
            Tsichlis,P.N. and Makris,A.M.
  TITLE     Old yellow enzymes, highly homologous FMN oxidoreductases with
            modulating roles in oxidative stress and programmed cell death in
            yeast
  JOURNAL   J Biol Chem 282 (49), 36010-36023 (2007)
   PUBMED   17897954
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10121216
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..378
                     /product="alkene reductase"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40179
     Region          4..346
                     /region_name="OYE_like_FMN"
                     /note="Old yellow enzyme (OYE)-like FMN binding domain.
                     OYE was the first flavin-dependent enzyme identified,
                     however its true physiological role remains elusive to
                     this day. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a...;
                     cd02933"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,233,300,320,322..324)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            order(23,25,56,98,100,107,181,184,186,233,240,300,320,
                     322..323)
                     /site_type="active"
                     /db_xref="CDD:239243"
     Site            order(25,100,181,184,186,323)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239243"
     Site            186
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239243"
ORIGIN      
        1 msslltpydl sglalpnria mapmtrarap hqgeatarma qyyaqrasag lliseatnvs
       61 shsaafelap glvtdaqvqs wkpvteavha khgrlfvqlw hsgrvsslal ldgnqplsps
      121 glnddleqlq vwgqlqngfy tkihatpsra mttdeivqai aeyrraaina laagfdgvei
      181 haangyllhq flssttntre dqfggslanr trflaevika vgeviplakv gvrvspyaay
      241 nnvrdadpdg tyayvarmld eagiaylhaa dtngwsgqpd lprmietlrp afkgtlmlng
      301 sitpsaadrl iaagdadlvs fgrayianpd lveriagnle laaprpvgwy ggddvgyvdy
      361 pphgapsgep saadalss
//
LOCUS       WP_176080694             294 aa            linear   BCT 11-JAN-2025
DEFINITION  SMP-30/gluconolactonase/LRE family protein [Paraburkholderia
            tropica].
ACCESSION   WP_176080694
VERSION     WP_176080694.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Slack,F.J. and Ruvkun,G.
  TITLE     A novel repeat domain that is often associated with RING finger and
            B-box motifs
  JOURNAL   Trends Biochem Sci 23 (12), 474-475 (1998)
   PUBMED   9868369
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465288
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..294
                     /product="SMP-30/gluconolactonase/LRE family protein"
                     /EC_number="3.1.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32227
     Region          10..283
                     /region_name="YvrE"
                     /note="Sugar lactone lactonase YvrE [Carbohydrate
                     transport and metabolism]; COG3386"
                     /db_xref="CDD:442613"
ORIGIN      
        1 mntltpevew nvgallgegp vwvereraly fvdikrrrvh ryvpesgers sweapaqtgf
       61 vlphadggfv cglqgglhrf tpenarfvlr vpvesglpgn rlndahvdte grlwfgsmdd
      121 aereptgslw rvegdqaprv hdsgyiitng pamspdfrtl yhvdslrrai ytfdvgndge
      181 lssrrlfsth appgdpdglv vdaegyvwva tfggariery apnglsvghv afpcsnvtkl
      241 afcgddlrta yvttarkgld eaalarepfa galfsfrapa agqkqslcri vwpd
//
LOCUS       WP_176080761             461 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Paraburkholderia
            tropica].
ACCESSION   WP_176080761
VERSION     WP_176080761.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Cox,C.D., Nakayama,Y., Nomura,T. and Martinac,B.
  TITLE     The evolutionary 'tinkering' of MscS-like channels: generation of
            structural and functional diversity
  JOURNAL   Pflugers Arch 467 (1), 3-13 (2015)
   PUBMED   24819593
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461657
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..461
                     /product="mechanosensitive ion channel family protein"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /calculated_mol_wt=49803
     Region          157..434
                     /region_name="MscK"
                     /note="Small-conductance mechanosensitive channel MscK
                     [Cell wall/membrane/envelope biogenesis]; COG3264"
                     /db_xref="CDD:442495"
ORIGIN      
        1 mmenrifshm lggvirdfgq pvmlwqagvl igalvlawll arllrrvlea rrqdryeglr
       61 fgaeslsraf fpligagcvw iareiasnfi htsllnlalv plfgigliyi afffarrvfg
      121 rngqthawlg iveklvsliv wlgmlftvlg iqddvlawme svrfrigtah vsllslsngv
      181 lwvcvtmiva vwagaaledr lmrattidan lrvvlarvgr allvfaailf slsivgidit
      241 vlgvfggalg vglgfglqki asnyvsgfii lidrslrlgd tinvsglagk vtqirtrytv
      301 vrgldgvetl ipneklitdv vqnqssyltr gyakaavqva ydtdldqama llaragegve
      361 rvltdpaptp ylasfggdgi nlelgfwiad aangtssvrs avnmniwrly neagisipfa
      421 qrevriigga mpvagpparg qneapageqp qdqpqaaade r
//
LOCUS       WP_176080876             504 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Paraburkholderia tropica].
ACCESSION   WP_176080876
VERSION     WP_176080876.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..504
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=53386
     Region          4..466
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 msvsladlsa vdarrligng elspvellda clariesiep avnalaataf erardearra
       61 eqavvrgeal gvlhglpigv kdleetggll ttygsplyrd hvpvsdnafv arlraagaiv
      121 aaktnvpemg agantrnavw gatgnpfdtr lnaggssggs avalatgmlp latgsdlggs
      181 lripaalcgv vgyraspglv pserrvlgwa pnwvsgpmgr nvadvrlqla avaghasadp
      241 lsypatldaf areprldlsa lrigytedfg acavdasira tfrakierls rivaqcepid
      301 idlreahrvf dvvraqefva slretyerdp sllgantran yemggaltla dvaraetqrt
      361 alyrqfqahf srydvivspv spvtpfawtt shcesidgtp lenyyrwval tyvvtvltnp
      421 smslpcgidh agmpfglqli gpmrgdarll daaqalevaf arepalarpv pdlaalrgtp
      481 hqaraalrsi vtdpprlrda slsl
//
LOCUS       WP_176080878             441 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Paraburkholderia tropica].
ACCESSION   WP_176080878
VERSION     WP_176080878.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..441
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=46615
     Region          22..428
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mneanpsfvt aliaqrgnpa asrarldeav araealeslh vfthrpdayv epdayaplag
       61 lpvgvkdlid tvdmptcygs piwrghrpqa dapivtqlre lgalvfgktv ttefawrqpg
      121 ptvnpwrrdh tpggsssgsa aavgagivpl algtqtvgsv irpaaycgvv gykpsygtis
      181 regvhalaas ldhigffard vevaalahal fvaqrveaid svdawqawfa plaapprlgv
      241 vrtpfdarlq dmqkvnfdaa laqlraagae iaeiefeadf eqivdalqvi lrveawhavg
      301 pearahreql sahmralvde gaampearyq aalalqaqwr arsaqllagc dalvsvpatg
      361 vapqglddtg dptfcapwsl lgmpavtvps gwtdaglplg fqtigafged letlrvaawi
      421 eqvigarrel elaaasteai a
//
LOCUS       WP_176080896             393 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase [Paraburkholderia tropica].
ACCESSION   WP_176080896
VERSION     WP_176080896.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 393)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..393
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40408
     Region          1..392
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mteivivsaa rtavgkfggs lakvaapdlg aivikaaler vglkpeqvsd vilgqvltag
       61 sgqnvarqas ikaglpaavp amtinkvcgs glkavmlaan aiiagdaeiv vaggqenmsa
      121 aphvlpgsrd gfrmgdakli dsmivdglwd vynqyhmgvt aenvakeygi treeqdafaa
      181 asqnkaeaaq kagrfddeiv pveipqrkgd plvfktdefv rhgvtaesla slkpafakeg
      241 tvtaanasgi ndgaaavvvm sakkaeelgl kplarikaya nagvdpkvmg igpvpasqrc
      301 leragwsasd ldlmeineaf aaqalavnkq mgwdtskinv nggaiaighp igasgcrilv
      361 tllhemqrrd akrglaslci gggmgvalal erg
//
LOCUS       WP_176080905             241 aa            linear   BCT 11-JAN-2025
DEFINITION  copper homeostasis protein CutC [Paraburkholderia tropica].
ACCESSION   WP_176080905
VERSION     WP_176080905.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Latorre,M., Olivares,F., Reyes-Jara,A., Lopez,G. and Gonzalez,M.
  TITLE     CutC is induced late during copper exposure and can modify
            intracellular copper content in Enterococcus faecalis
  JOURNAL   Biochem Biophys Res Commun 406 (4), 633-637 (2011)
   PUBMED   21362400
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Li,Y., Du,J., Zhang,P. and Ding,J.
  TITLE     Crystal structure of human copper homeostasis protein CutC reveals
            a potential copper-binding site
  JOURNAL   J Struct Biol 169 (3), 399-405 (2010)
   PUBMED   19878721
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..241
                     /product="copper homeostasis protein CutC"
                     /GO_function="GO:0005507 - copper ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=24505
     Region          3..240
                     /region_name="CutC"
                     /note="Copper homeostasis protein CutC [Inorganic ion
                     transport and metabolism]; COG3142"
                     /db_xref="CDD:442376"
ORIGIN      
        1 mpitleicvd svdgldaava ggadrielcs aldlggltpt pgliaaaaha pipvyamirp
       61 harsfawspa dteamladid amraaglagv vlgaaradrq ldvqmlavlc erarglgttl
      121 hrvfdlvpdp araleeaval gferiltsgg aaraadgiva lnalvrhaan rigimpgsgv
      181 dalnvagivr asgatqvhas cravfahgeh kgvelgffpe rgsmtsarav mglkhamaal
      241 a
//
LOCUS       WP_176080906             330 aa            linear   BCT 11-JAN-2025
DEFINITION  ROK family protein [Paraburkholderia tropica].
ACCESSION   WP_176080906
VERSION     WP_176080906.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Conejo,M.S., Thompson,S.M. and Miller,B.G.
  TITLE     Evolutionary bases of carbohydrate recognition and substrate
            discrimination in the ROK protein family
  JOURNAL   J Mol Evol 70 (6), 545-556 (2010)
   PUBMED   20512568
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Larion,M., Moore,L.B., Thompson,S.M. and Miller,B.G.
  TITLE     Divergent evolution of function in the ROK sugar kinase
            superfamily: role of enzyme loops in substrate specificity
  JOURNAL   Biochemistry 46 (47), 13564-13572 (2007)
   PUBMED   17979299
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..330
                     /product="ROK family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=33264
     Region          15..323
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
ORIGIN      
        1 mpdhalpala gartfytadi ggsfirlaac thagelvala kqptpahdwt qfvdtlsaml
       61 aahvdgaada alalsiaglv dpadstafsa nipcitgrkl aselgarlgr pvfaandadc
      121 lalaeavaga gaghrvvfsa vlgtgvgggl vangqliqga ggvtgewghg pivntqcqpe
      181 gepeplyvpr facgcgqrgc vdtiggargi erlhvflnaa sttdsptpal dshaildawt
      241 hadraavrti gvwlelvadp laavvnvtga srvtvgggla gspaligrld qavrsrvlhr
      301 rdeplvvpgr fsadggliga allarqasnr
//
LOCUS       WP_176080914             246 aa            linear   BCT 11-JAN-2025
DEFINITION  GGDEF domain-containing protein [Paraburkholderia tropica].
ACCESSION   WP_176080914
VERSION     WP_176080914.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 246)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 246)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 246)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..246
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26853
     Region          7..239
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mdatayrrev shdhapdlfr nesealerar aigadphada dayrqaldel irhyerlmre
       61 trrligrsdr aeremqaltq qlhyrathda ltgvfnrsav iertvkalra dravmilldi
      121 ddfktvnddf ghpagdavil givnclrgil gehgligrvg geeftvvlpg feirdaldla
      181 ermraaiaah afpdpvsrsi tasfgvsdna agtdfdtayg ladaalyaak rggrdrvsfd
      241 gplasa
//
LOCUS       WP_176080999             447 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Paraburkholderia tropica].
ACCESSION   WP_176080999
VERSION     WP_176080999.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..447
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=48387
     Region          57..422
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mtvfharqaa rravatalva gatalaalaa sgigaahaqs sspgspaqsq palsdvaslg
       61 klifndpsls asgrmscasc hspahaygpp nglaaqpgga dlhaqgtrav ptlgyvlnrt
      121 pvwthvqaas vferltdads ppaggfawdg ryntlhdqal fplfnpnema nrdsaqvaak
      181 lerapyaarf kqlfgetifv skdaavhqam qaverfelee psfhsytskf davldrkaef
      241 tasemrgkkl fddpnggnca schidqggan gahplftdyq fealgvprnp elranrdpky
      301 ydkglcgpvr tdvssnknyc glfktptlrn vatrevffhn grfhtlrdal rfyverdtnp
      361 ekwypkdrhg hvvkfddlpa aervnvdtvd epltrkpggk pawnardidd viaflktldd
      421 gylptnppta gvrfvkistt sapikrq
//
LOCUS       WP_176081046             718 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent receptor [Paraburkholderia tropica].
ACCESSION   WP_176081046
VERSION     WP_176081046.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Silale,A. and van den Berg,B.
  TITLE     TonB-Dependent Transport Across the Bacterial Outer Membrane
  JOURNAL   Annu Rev Microbiol 77, 67-88 (2023)
   PUBMED   36944260
REFERENCE   2  (residues 1 to 718)
  AUTHORS   Ratliff,A.C., Buchanan,S.K. and Celia,H.
  TITLE     The Ton Motor
  JOURNAL   Front Microbiol 13, 852955 (2022)
   PUBMED   35464957
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446927
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..718
                     /product="TonB-dependent receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78518
     Region          53..689
                     /region_name="CirA"
                     /note="Outer membrane receptor protein, Fe transport
                     [Inorganic ion transport and metabolism]; COG1629"
                     /db_xref="CDD:441236"
ORIGIN      
        1 mnhhrtllar aalvafaiva anparsaetd tatdgttnna ataspansnt ldvevnakrl
       61 dearngllpe tgssiyritq sdiqsmpqga ntplnqvllq apgvandsyg qlhvrgdhad
      121 lqyringimi pepisgfgqs ldtriidqvn lltgalpaey gyrtagivdi rtksgdfgng
      181 gsvdvyggsh qtlqtsadvy gsngdfsyff sgslgennlg ieaptaspnp ihdhtrqrna
      241 fgymsyiinp ltrvsvmfgt aanqfeipnt pgltpnfmla gtptfnsanl netqselnnf
      301 avvalqgtng galdyqvalf trytrtqfnp dpvgdlifng vasqdfhsdt anglqadtty
      361 rlnehhtlra gvlfqqehan fwdnvsvfpa dadgnqtsdv pytlsdsssk tgylysayvq
      421 dewkitdrlt lnyglrydgm deyvqasqls prigaifklt pttsfhagya ryftppsfel
      481 vsnstisryn gttnqsevtq ndpvqperdd yfdlgvtqql gsdltlglda yykkahnlld
      541 lgqfgtaliy tpfnyqygrv ygveftanyk hdnvsaylnl afsraqgknv dsaqfnfgad
      601 elafisnhwv fldhdqrvta sfggaynwhr ttftmdgtvg sglrngfant gklplyaqfn
      661 laviqhfnlp migkvdgrfv venafgrtye lrdgsgigvf apqygpyraf yagltkyf
//
LOCUS       WP_176081052             501 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia tropica].
ACCESSION   WP_176081052
VERSION     WP_176081052.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..501
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=54245
     Region          50..478
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(60..61,64..65,68,102,152..153,155..157,160,180,
                     183..184,187,308,311..312,315..317,320,344,348,402..403,
                     407,411,427,430..431,434..435,439)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mpsetetrqs tqssestiga dineraaive tdlparldrl pwgrfhvliv valgvtwlld
       61 glevtlagav asalktspvl hvdnaqvgla gsayiagavl galgfgwltd rlgrrklffi
      121 tlavyllata atacswsfas fmvfraltga giggeyaain stiqeftpar vrgwtdlsin
      181 gtfwvgagig algsyalldp rwlppdwgwr acfligavla liilpmrrwi pesprwllth
      241 gehdearsiv erietrfrea ghtlndnats slrlrarrht plsevmhaif vrhrrrafvg
      301 lslmtaqaff ynaifftyal vltefyrvpg gdvglyllpf avgnflgplv lgrlfdvlgr
      361 rkmiaatyal sgvllsasgy lfahgwltvv qqtvawmvif ffasaaassa yltvsesfpl
      421 eiralaiavf yafgtglggm igpalfgrli dthqrsevft gylvgsalml gaaliaaiwg
      481 vdaerksleh vatplsaidd a
//
LOCUS       WP_176081077             528 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia tropica].
ACCESSION   WP_176081077
VERSION     WP_176081077.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..528
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=55426
     Region          33..461
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(40..41,44..45,48,80,130..131,133..135,138,159,
                     162..163,166,290,293..294,297..299,302,330,334,388..389,
                     393,397,413,416..417,420..421,424)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mqlselgqdl arenhdplrp tqmrrnalal iavclaammf sleissvpmi lptlevvlhg
       61 dfkqmqwimn aytlacttvl matgtladrf grkrvfvvti vlfgaaswlc glassttali
      121 asrfvqgasg gamliclvav lshqfpqgaa rarafsawgi vlgiglgfgp lvggaivals
      181 swkwvfwvhv aiavatlgla lagvresrdp qarkldiagm vtlsaavfgf vwtitqgadi
      241 gffsvpalsv laastasfaa fvaielraah pmfdfsvfri rsfsgallgs vgmnfsfwpf
      301 iiylpiyfqs vlregplasg lsllaytlpt lvfppigerl alrlqparai paglftiglg
      361 fllmragsaf ghghalavlp gclvagaglg itntpvtntt tgsvsadrag masgidmsar
      421 mvtlainial mgsllvasva rhlqdalgga aqtvswqala arvaagnltp gdgsighadf
      481 ethfepyfet taraaleagf ntlmlyggla vctlavlsyl ifsrrptr
//
LOCUS       WP_176081116             319 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paraburkholderia tropica].
ACCESSION   WP_176081116
VERSION     WP_176081116.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..319
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32402
     Region          2..315
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mtdwfarvqr fslpgalvav svffavcspg fartanladv llnnfallai aslgmtlals
       61 igavdlslgt avdvgslvfv lltahhvgvp laaiaglgaa llvgafngvl vaglgiapfl
      121 atlgtlfigq tlqqlatdgg qpvyllgmsl pplfsalahg sfagvplplw ivaalalvvh
      181 valahsvfgr ysaalgsqpg varysglpva avvvatfvag aliygvvgll lasmvkayvp
      241 qagngyllna igatfigttl srtrrpnvpg tllgvlllsl vangllligw nfywqqvatg
      301 vlifavlals fasrraefa
//
LOCUS       WP_176081145             371 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Paraburkholderia tropica].
ACCESSION   WP_176081145
VERSION     WP_176081145.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..371
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38620
     Region          4..369
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msylevlepl vstliapeaa qtdqlarfpr aavdalgeaa llglisaeev ggmglgaaqa
       61 crvveriard cpstamvvtm hyagasliek ygpveirrai argehlttla wsetgsrshf
      121 wapvgtarad gddfvlsgsk smvtsasead syvwssrpvs aegastlwlv dsraqglqsp
      181 hafdglglrg nasapiraeg lrvpasamlg adgsggdimn gdalpvfanl vastsiglad
      241 galqratqhi tasrfaesge alcelptira ylaraqlrad qartlrddtl aamsagrada
      301 mlrvlevkaa aaeaaldvtd tamricggaa frkevgierl frdaraasim gptsdvlydf
      361 lgrvlcgmpl a
//
LOCUS       WP_176081173             200 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Paraburkholderia
            tropica].
ACCESSION   WP_176081173
VERSION     WP_176081173.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..200
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21609
     Region          3..147
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mnaapavevr qhildtampi llgkgfsavg lneilaaagv pkgsfyhyfg skeafgeall
       61 tfyfteyaer leaqlvrapg tarerlmryf eewramqcad gpdgkclavk lgaevsdlse
      121 pmrvvlrrgt deiigriaac ieegladgsl egvrnasgta gtlyelwlga tlmekirrdr
      181 spldsamvtt rallnlppat
//
LOCUS       WP_176081166             494 aa            linear   BCT 11-JAN-2025
DEFINITION  catalase [Paraburkholderia tropica].
ACCESSION   WP_176081166
VERSION     WP_176081166.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433537
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..494
                     /product="catalase"
                     /EC_number="1.11.1.6"
                     /GO_function="GO:0004096 - catalase activity [Evidence
                     IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=55449
     Region          2..493
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:440516"
ORIGIN      
        1 maessgkplg ksttsagapa vsdrnsltvg pdgpillhdv hfleqmahfn rekvperqph
       61 akgsgafgef kttedvsqyt kaalfqkgaa temlarfstv agemgspdtw rdvrgfslkf
      121 yttegnydlv gnntpvffvr dpmkfphfir sqkrlpdsgl rdsemqwdfw tnnpesahqv
      181 tylmgerglp ktwrnmngyg shtymwvnak gekfwvkyhf htqqgmasft naeaeatagr
      241 dadfhrrdlf eaikrgefps wtlfvqvmpy aeaknyrfnp fdltktwshk dyplikvgtm
      301 tlnrnpenff aqieqaafsp gntvpgigls pdkmllgraf ayndahrari gtnfnqlpvn
      361 rpkvpvqtyq fdghmayeht gnapvyvpns fgrpwadetg paedgwetdg dmvrsaytlh
      421 aedddfgqpg dlvrkvfndk qrellveqvv aslngvgspv renvftywkn idadvgrrie
      481 ekagaatkva epak
//
LOCUS       WP_176081204             483 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia tropica].
ACCESSION   WP_176081204
VERSION     WP_176081204.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..483
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=51679
     Region          54..463
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(64..65,68..69,72,106,156..157,159..161,164,184,
                     187..188,191,303,306..307,310..312,315,342,346,395..396,
                     400,404,420,423..424,427..428,431)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mnsqpmelgg raareadpgl paaardgsar aaqgvtlggf mdempvgalh rfvvwvvgig
       61 lffdmyeifl vssigsalqn eygldghstg fklllasafi gmffgslclg sladrigrrr
      121 aflltlvwys afsllaafsv nagmlvvcrf ltgvgvgaiy pvadsylsei lpkdrrgrla
      181 awayttsyia vplvgflavw lnplhlggva gwrvilaigg lgavfvlaik hrlpesprwl
      241 laqgradear atlgrfadsa gvalpaafeq tgerkhaltl gerigllrra pygkryfmlt
      301 vfhlfqafgy ygfgtlagvv vksrgfdvtg stlfvalsfl gypigsllsv pllnwierrt
      361 lviaslisva lfglgfaysn sialivcfgf lttcasnvfs nayhvyqaei fpasvrstai
      421 gstyslsriv ssalpfillp vlnqhgplam fgvislalai vaitlrtlgp lttrrsqdei
      481 npv
//
LOCUS       WP_176081269             561 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia tropica].
ACCESSION   WP_176081269
VERSION     WP_176081269.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..561
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=56710
     Region          60..469
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(65..66,69..70,73,105,155..156,158..160,163,183,
                     186..187,190,315,318..319,322..324,327,355,359,413..414,
                     418,422,438,441..442,445..446,449)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 manpdlvere stsaaksvpk sthavaaqas pcdelviraq ptavdrpcrr krlalaatil
       61 gssmafidgs vvnvalpsiq aelgasvaam qwvvnayllf lgslvlvggs mgdklgrrti
      121 fiagialftl asaacgfasn aaaliaarav qgigaallvp sslaiigavf ddaargraig
      181 twagvgaits avgpvaggwl vdalswraif flnvplavlt talalasvpn shkadaperl
      241 dwpgalaaaa glaaltfglt lastlgfaqa rvlgsigagv lllgvfvwie ahsenpmmpl
      301 dvfrsrdfsg anlvtlllyf glggalfflp ftlirahgyh atqagaallp vpviigllsr
      361 ftggltsrfg aralltvgpg iagigfalla apwargggyw sgffpalvvl gigltitvap
      421 lttvvmgava adrtgvasgi nnavarvasl laiavlgivf vwahdaalaa rldtlqvpre
      481 awqtglslep aahadanpnp asvplatpva raqaeaiada lravalvsaa cafaaaglal
      541 ttirplkpsa lppqiahhgd q
//
LOCUS       WP_176081287             483 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Paraburkholderia
            tropica].
ACCESSION   WP_176081287
VERSION     WP_176081287.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454547
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..483
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=53899
     Region          228..479
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          394..481
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mfsmlyfplv sslatpepvv sgnqaerfgf alregkllaa shltsrwide tnaagmgeha
       61 lhglqlhadl qlllgvevea eeayrrslkl irsskrdira sscrnaawqa lfrhrigtal
      121 scfarvvdep gieparaaea rfgivcalhe lgrtgealqa ldefahrlde diddphghwh
      181 dlattvrfdl evqtalrcas elsdhvywqs gaagvtartq edvlravrvp llrarieylr
      241 hlqlaaladr naigglqhhl nwareqgvgd yqrtlrleia laalagaqph yahamleplh
      301 plvragaigh rhieylycaa ktrqaqgraq esltlysrya lvamqclred aslqmplasr
      361 mskpgpqldd vgarlparyr raysyvldnl drpdlsvrei aaeigvtera lqsafknflg
      421 lspselirrq rmeriraelt erayaadrgv lvaankwgvq nrstlvngyr kqfheapset
      481 ler
//
LOCUS       WP_176081301             742 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Paraburkholderia tropica].
ACCESSION   WP_176081301
VERSION     WP_176081301.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..742
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=78694
     Region          32..671
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mnvtpagatp trlrdrlrde wpaywqddap rllhiakvgl avviamglcm rlelrspata
       61 mlscvivmmh qqsgiviarg fyrglgmvag slaglvlial faqqplpffi alaawiglca
      121 fgsayfrnfq syglvlagfa taitampals npygvfdnvi ytisevvigv lsasvvstvv
      181 lprkvapaly aagrasfthl lgtlratlar eaaptqaraq tgaqtdtqts tllgligera
      241 nvellrtgal fedpsmrllh svfldldrsf ldtvmwlhal qrvkahaaad ahpraqaaia
      301 tltdaalall pdtatppgia ddaaaallpq ldafeaalpa riaaqlhald dlplaqrriv
      361 estgaallfm sadlrllcrs yldarqadrq pwtvsvlqai triarqravg nrtaalvaga
      421 ravvavllvg avwiasgwtg gstaivavai tstlfalvpd pptaawqift gclagwlagf
      481 afsffvlpsl gtfallaavv ailvmiggyv ntfpktavlg lgfniyfcfi vgianpavyn
      541 psayldtgfa llcgiaaaav afsvlaprag ewiarrylae vcalvasdar dgdldddlly
      601 aferklrdci lqiagapadp cvdrahmiaw afavleagra milmrldtqq iaptlppawp
      661 dhqtawltal adlfdtptpe radralaatr aaldalppgi epaadapvgp dslvrcrmha
      721 llqftelalr ddplairter aa
//
LOCUS       WP_176081308             238 aa            linear   BCT 11-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Paraburkholderia tropica].
ACCESSION   WP_176081308
VERSION     WP_176081308.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..238
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=26070
     Region          48..210
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mrnhandpaa gngvvfsdth fdrddlaral resgdeptfe rcqfdgedls nidfhaarfa
       61 qctigqtrfe hsdlsrtrwi gcrgaaasfr yanagdarfi rsdlnntdwt gaklastift
      121 evkltgarfi dtralglsfh dsllvgatlr glsfrkqtle qlnfsdadla dcdfrdavfe
      181 ggslgnvrll ntrfdgadlr svdlsglrls dvlqhlkgti lsvdqavmli gdcgvrvm
//
LOCUS       WP_176081352             488 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia tropica].
ACCESSION   WP_176081352
VERSION     WP_176081352.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..488
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50824
     Region          32..476
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(39..40,43..44,47,79,129..130,132..134,137,157,
                     160..161,164,294,297..298,301..303,306,334,338,391..392,
                     396,400,416,419..420,423..424,427)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mtddslaaap plaaptsaat arshhgwalv vllvgailpp idyfivnlal paihsglsas
       61 aaqlqmvvsa yacanavaqi tggrlgdlyg rkrmfmigma gfvlastlcg latsgamlva
      121 grilqglfaa vlapqvlati rsvftpheqv rvmgfygfvf gvaavigqlg ggalislhpf
      181 glgwraiflv nlpigvlall gswrfipesr pprgaridmp gtvllslfll mlvypltrgr
      241 eegwptwmli claasvpmlg allrvearsl arghdplldv rlfrnpvial glvlaflfyt
      301 lsafflsygi ylqgalhwtp lasgvailpf glgflsspll mprlvfrlgs yrvltlgfvl
      361 ialglaaaas lasvsapgag fyfglgamgm gqglvlpsvv rivlaevdpa ragvasgmvt
      421 atlqigaavg aatlggvffs hlgahpvald yvqgfrvsmf alvgilcvcv lsslalgpmh
      481 rrlhpqpa
//
LOCUS       WP_176081355             400 aa            linear   BCT 11-JAN-2025
DEFINITION  tyrosine-type recombinase/integrase [Paraburkholderia tropica].
ACCESSION   WP_176081355
VERSION     WP_176081355.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Gopaul,D.N. and Duyne,G.D.
  TITLE     Structure and mechanism in site-specific recombination
  JOURNAL   Curr Opin Struct Biol 9 (1), 14-20 (1999)
   PUBMED   10047575
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Esposito,D. and Scocca,J.J.
  TITLE     The integrase family of tyrosine recombinases: evolution of a
            conserved active site domain
  JOURNAL   Nucleic Acids Res 25 (18), 3605-3614 (1997)
   PUBMED   9278480
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471964
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..400
                     /product="tyrosine-type recombinase/integrase"
                     /GO_function="GO:0009009 - site-specific recombinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /calculated_mol_wt=44427
     Region          42..396
                     /region_name="XerD"
                     /note="Site-specific recombinase XerD [Replication,
                     recombination and repair]; COG4974"
                     /db_xref="CDD:443999"
ORIGIN      
        1 mhtallaprp ldalelpadl dgrdgvnran grmqiaaand ldairawlar vadskatfet
       61 yrkeaerlll waivqlgkpl sslthedlla yqrfladpqp aarwcagggr kharddprwr
      121 pfygplsaas qrqamvilna lfswlvsagy lagnplslsr qrarraqpri trylerglwd
      181 evkayvdalp rasarererh grarwlltll ylgglrisev gintmgdffa rrdasgeerw
      241 wldvlgkger rrlvpatael mtelaryreq rglsalpaph eatplvlpig qstkpltraa
      301 lhtivkgifa gaaqrlrdaa aqeadparaa ggtaraalle sasahwlrhs agshmadgdv
      361 dlrmvrdnlg hasisttsly lhsdddrrhr eteakhridw
//
LOCUS       WP_176081381             306 aa            linear   BCT 11-JAN-2025
DEFINITION  MotA/TolQ/ExbB proton channel family protein [Paraburkholderia
            tropica].
ACCESSION   WP_176081381
VERSION     WP_176081381.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Deme,J.C., Johnson,S., Vickery,O., Aron,A., Monkhouse,H.,
            Griffiths,T., James,R.H., Berks,B.C., Coulton,J.W., Stansfeld,P.J.
            and Lea,S.M.
  TITLE     Structures of the stator complex that drives rotation of the
            bacterial flagellum
  JOURNAL   Nat Microbiol 5 (12), 1553-1564 (2020)
   PUBMED   32929189
  REMARK    Erratum:[Nat Microbiol. 2020 Dec;5(12):1616. doi:
            10.1038/s41564-020-00825-4. PMID: 33168990]
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Kitao,A. and Nishihara,Y.
  TITLE     Structure of the MotA/B Proton Channel
  JOURNAL   Methods Mol Biol 1593, 133-145 (2017)
   PUBMED   28389950
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Celia,H., Noinaj,N., Zakharov,S.D., Bordignon,E., Botos,I.,
            Santamaria,M., Barnard,T.J., Cramer,W.A., Lloubes,R. and
            Buchanan,S.K.
  TITLE     Structural insight into the role of the Ton complex in energy
            transduction
  JOURNAL   Nature 538 (7623), 60-65 (2016)
   PUBMED   27654919
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Cascales,E., Lloubes,R. and Sturgis,J.N.
  TITLE     The TolQ-TolR proteins energize TolA and share homologies with the
            flagellar motor proteins MotA-MotB
  JOURNAL   Mol Microbiol 42 (3), 795-807 (2001)
   PUBMED   11722743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002771
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..306
                     /product="MotA/TolQ/ExbB proton channel family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015252 - proton channel activity
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
                     /calculated_mol_wt=31784
     Region          80..286
                     /region_name="TolQ"
                     /note="Biopolymer transport protein ExbB/TolQ
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG0811"
                     /db_xref="CDD:440573"
ORIGIN      
        1 mkkrsfaala asmlfavatv dtfvaptlan aqasdtsata sagatasapa taatapapvp
       61 aadqpppppa tsetvsnpyg lgalwkngdf varfvllllv imsmgswyim itkfieqara
      121 nrrakvaddq lwnaptladg akqleetspf rfiaetaiea gehhdealle avdrntwidv
      181 sveraitnvs nrlqdglafl gtvgstapfv glfgtvwgiy haltaigiag qasidkvagp
      241 vgealimtai glavavpavl gynflvrrnk avmervrafg aqlhavllag gkrgaratsr
      301 avamae
//
LOCUS       WP_176081385             478 aa            linear   BCT 11-JAN-2025
DEFINITION  TldD/PmbA family protein [Paraburkholderia tropica].
ACCESSION   WP_176081385
VERSION     WP_176081385.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..478
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=51809
     Region          11..476
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 mideswtlav rglrssadfw svrfvderkd dhvvrndval plriarerga mvtawagaga
       61 gyaatadlta sglqraleia taraqasaah alidhrevar paqsgeyvsp naqaalpsrr
      121 ewldrlahec aaakldariv erqagmevtq cdqlyltsdg vrieqrfrfl mpalsvvahd
      181 dgdtqertlg ghygllaqgg meilarygfd gagarvanea lqllaapncp tgkrdlllmp
      241 dqmmlqihes ighpleldri lgdernfagw sfvkpemfgs yqygsellnv tfdpdtreea
      301 aayafdddgs aaskeylira gmlerplgga lsqqraglpg vansraanwn rppidrmanl
      361 niepgdqpld aliagvehgi lmstntswsi ddhrnkfqfg cefgqlieng klteivkrps
      421 yrgisasfwr slaavgdast ravygtpmcg kgepaqvirv ghaspacvfs nvevfgaa
//
LOCUS       WP_176081519             480 aa            linear   BCT 11-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Paraburkholderia
            tropica].
ACCESSION   WP_176081519
VERSION     WP_176081519.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..480
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=48808
     Region          25..290
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 matisserle taarkeaswa vgacrqfiad rcpslaasia fysafslapt lvmviavagw
       61 ffgadaargq lfrevhnvlg ndaaaaitti vqnahragda ggvaalisla mlaigasatf
      121 sslnsalniv wplegprass vialvrvrli sfglvlgvaf llivslvlda gitfvgqwlm
      181 gestyliign ivqlvvgllv lavafagllr flpdapvlwr dalvgglvaa vlfsvgkklf
      241 alylahagma tafgaagsla vllmwlyfsa avlllgaefs aargrlhdpr gawgmleetp
      301 pgsraklasv laastiapmr eaaaglqtar avaaegangv kgvngavgag svgsvdgatl
      361 daavgaappy aaavaasvqp gktprpadap lhaigkarat ggafarlhgg slqirrsvvr
      421 medsatyaaa ltlvqagrtv aaadryvkrh pwssvllvas aavamtaaag rrhagvhrkd
//
LOCUS       WP_176081361             158 aa            linear   BCT 11-JAN-2025
DEFINITION  OsmC family protein [Paraburkholderia tropica].
ACCESSION   WP_176081361
VERSION     WP_176081361.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Meireles,D.A., Domingos,R.M., Gaiarsa,J.W., Ragnoni,E.G.,
            Bannitz-Fernandes,R., da Silva Neto,J.F., de Souza,R.F. and
            Netto,L.E.S.
  TITLE     Functional and evolutionary characterization of Ohr proteins in
            eukaryotes reveals many active homologs among pathogenic fungi
  JOURNAL   Redox Biol 12, 600-609 (2017)
   PUBMED   28391181
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Atichartpongkul,S., Loprasert,S., Vattanaviboon,P., Whangsuk,W.,
            Helmann,J.D. and Mongkolsuk,S.
  TITLE     Bacterial Ohr and OsmC paralogues define two protein families with
            distinct functions and patterns of expression
  JOURNAL   Microbiology (Reading) 147 (Pt 7), 1775-1782 (2001)
   PUBMED   11429455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004484
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..158
                     /product="OsmC family protein"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0004601 - peroxidase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006979 - response to oxidative stress
                     [Evidence IEA]"
                     /calculated_mol_wt=17320
     Region          5..153
                     /region_name="OsmC"
                     /note="Organic hydroperoxide reductase OsmC/OhrA [Defense
                     mechanisms]; COG1764"
                     /db_xref="CDD:441370"
ORIGIN      
        1 mahgehmytv kvqwtgnrgs gtsgyrdydr dhliestgkp aipgsadpaf rgdaarwnpe
       61 dllvasasac hklwylhlca dagiavldyv deaqgtmidt aeegrfkeiv lhprvtirag
      121 ddraraehlh htahekcyva nsvnfpirce pvivqada
//
LOCUS       WP_176081378             315 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Paraburkholderia tropica].
ACCESSION   WP_176081378
VERSION     WP_176081378.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444115
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..315
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34433
     Region          18..77
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          105..304
                     /region_name="PBP2_CrgA_like_5"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08474"
                     /db_xref="CDD:176163"
     Site            order(116,120,159,173,176,239,256,283)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176163"
     Site            order(117..118,122..123,125..126,129,133,135..141,203,
                     233..237,244..245,248)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176163"
ORIGIN      
        1 mrkstskats kppgkptlad lqafmtvaar rsfvqaagel gvsrsalsha mrglentlsv
       61 rllhrttrsv slteagerll grlrpvlsel dhalddvard dealrgslri ngsdgairhl
      121 lqtvlprfla qypqmeldlv segrfvdiva egfdagvrlg eavhkdmiav risddlrfla
      181 vasprylrkh grpalpgdlq ahrcirqrlp ggrryrwefa rhgeavaidp pgaltldsnt
      241 lmveaaldgl giayvpepya rdalarkrlv avledwcpai pglflyfpgn rhipaglral
      301 ievvraeree sgaap
//
LOCUS       WP_176081553             243 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Paraburkholderia
            tropica].
ACCESSION   WP_176081553
VERSION     WP_176081553.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10487553
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..243
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=24831
     Region          16..229
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE; pfam01925"
                     /db_xref="CDD:460386"
ORIGIN      
        1 mtlagtpatl awlasislla gvakgltgfg galvmaplfg lllgpadtaa vivfvhcvts
       61 lqgirqwgrv arwrsilpla avalvsaala shwmagadar rlrhataiav laitvlhmrg
      121 wrwrhhgsgm plvaagvvsg mltalaglgg ppavyyfagi dqgpalranl lgyfaalfcg
      181 tallfaishr itvshaitgv glapafalgv llgersgarm srvafdrivs gllllsgcla
      241 lvs
//
LOCUS       WP_176081548             359 aa            linear   BCT 11-JAN-2025
DEFINITION  LLM class flavin-dependent oxidoreductase [Paraburkholderia
            tropica].
ACCESSION   WP_176081548
VERSION     WP_176081548.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Mascotti,M.L., Juri Ayub,M. and Fraaije,M.W.
  TITLE     On the diversity of F420 -dependent oxidoreductases: A sequence-
            and structure-based classification
  JOURNAL   Proteins 89 (11), 1497-1507 (2021)
   PUBMED   34216160
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Reis,R.A.G., Li,H., Johnson,M. and Sobrado,P.
  TITLE     New frontiers in flavin-dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 699, 108765 (2021)
   PUBMED   33460580
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Huijbers,M.M., Montersino,S., Westphal,A.H., Tischler,D. and van
            Berkel,W.J.
  TITLE     Flavin dependent monooxygenases
  JOURNAL   Arch Biochem Biophys 544, 2-17 (2014)
   PUBMED   24361254
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005401
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..359
                     /product="LLM class flavin-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070967 - coenzyme F420 binding [Evidence
                     IEA]"
                     /calculated_mol_wt=39265
     Region          37..335
                     /region_name="SsuD"
                     /note="Flavin-dependent oxidoreductase, luciferase family
                     (includes alkanesulfonate monooxygenase SsuD and methylene
                     tetrahydromethanopterin reductase) [Coenzyme transport and
                     metabolism, General function prediction only]; COG2141"
                     /db_xref="CDD:441744"
ORIGIN      
        1 maairidhla fltpgnyrde spfegieqsl dlfavgetlg ydsawvrqrh leravssaat
       61 flaaasqrtt riglgaaviq mgyenpfrla edlasvdvls rgrlnvglsa gapghgallg
      121 erlfdadpqq idfsyariar lrqnlagdwl gdadtfvesa agrvrprvtp yaaglterlw
      181 ygggslrsve waarngfnll ignitagegt dhfreaqlrq iaayrgnwhd arpprialgr
      241 vivpldsast atrefyraya agrhartlmp hgerrtlfap dlvgsaeeiv aalqadpvla
      301 evselrlelp ydlpfehyrq iledvatrva prlgwrarda laaanvampd vardrreva
//
LOCUS       WP_176081586             296 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfurtransferase [Paraburkholderia tropica].
ACCESSION   WP_176081586
VERSION     WP_176081586.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..296
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=31413
     Region          21..292
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 msieqthdtr radvlveaaa larelgepdl vvldahvelp sprfdgdyrv asgydgwlaq
       61 rvpgarhadl savlsaphet lsfmrpapsa lahgletlgv snasrvviyd radgfwaarl
      121 wwmlrwigid arvldggwra wraadlpves gsgravargh ievreragmw adradveaiv
      181 agavrstlvc alsaevfsgv sasryarrgh ipgsvnvpar glfdesgrya avpalhaamg
      241 aldraqpvcv ycgggisaav dalaltltgr ddvsiydgsl qewaadpala mvaiar
//
LOCUS       WP_176081640             467 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia tropica].
ACCESSION   WP_176081640
VERSION     WP_176081640.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022776
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..467
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=50137
     Region          43..450
                     /region_name="MFS_SV2_like"
                     /note="Metazoan Synaptic vesicle glycoprotein 2 (SV2) and
                     related small molecule transporters of the Major
                     Facilitator Superfamily; cd17316"
                     /db_xref="CDD:340874"
     Site            order(52..53,56..57,60,92,142..143,145..147,150,170,
                     173..174,177,285,288..289,292..294,297,325,329,380..381,
                     385,389,405,408..409,412..413,416)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340874"
ORIGIN      
        1 mrtldttlgh rggtavgesi trgsiiarle rmpangmqvr ariliglatf fdgfdviaia
       61 atlpiliqkw hltpweigfl iasgsvgqlf gaflfpwlae rhgrvraiaw ssgiigvtsi
      121 acgfapsfav faalrviqgf glggelpvaa tyinevsrah grgrfvllye ivfpigllas
      181 nalgawivpr fgwqamyfig gmplilffvl rklvpesprw laererlqda dqavsafert
      241 vkgplepvtn aaefdalakr hpkrsvkdlf gpayrnrtia vamlwmtcgf iqyglstwlp
      301 tiyrtvyhap lqlalnlava asvlgvlgsl tcallvdkvg rkpiinvsfv lcgislalag
      361 ichamsvyvv atfcalalgl lasgfitayv ytpelyptsi ralgcgvgga wlkiaaifap
      421 tivsktmigg nldvafyila avpflaaiav hflgietkgk vleqlea
//
LOCUS       WP_176081661             217 aa            linear   BCT 11-JAN-2025
DEFINITION  DsbA family oxidoreductase [Paraburkholderia tropica].
ACCESSION   WP_176081661
VERSION     WP_176081661.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Chivers,P.T., Prehoda,K.E. and Raines,R.T.
  TITLE     The CXXC motif: a rheostat in the active site
  JOURNAL   Biochemistry 36 (14), 4061-4066 (1997)
   PUBMED   9099998
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122494
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..217
                     /product="DsbA family oxidoreductase"
                     /EC_number="1.8.-.-"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=23686
     Region          7..207
                     /region_name="DsbA_FrnE"
                     /note="DsbA family, FrnE subfamily; FrnE is a DsbA-like
                     protein containing a CXXC motif. It is presumed to be a
                     thiol oxidoreductase involved in polyketide biosynthesis,
                     specifically in the production of the aromatic antibiotics
                     frenolicin and nanaomycins; cd03024"
                     /db_xref="CDD:239322"
     Site            order(15,18)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239322"
ORIGIN      
        1 mtqalqidfi sdiacpwcai glsslqrala nlgdsvearm tvhpfelnpd mgpdgesive
       61 ylgkkygrtp eqiaetqeai rergesvgft fgprtriynt fdahrllywa rlegrqvslk
      121 mallrayhge gqdmsdhavl vavaqsvgld agkarevlet gayadevrge eqqaqamgiq
      181 svpaivfneq ylisggqpve tfenairqil aeaakda
//
LOCUS       WP_176081663             428 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia tropica].
ACCESSION   WP_176081663
VERSION     WP_176081663.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022908
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..428
                     /product="MFS transporter"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=46451
     Region          8..406
                     /region_name="MFS_ExuT_GudP_like"
                     /note="Hexuronate transporter, Glucarate transporter, and
                     similar transporters of the Major Facilitator Superfamily;
                     cd17319"
                     /db_xref="CDD:340877"
     Site            order(20..21,24..25,28,60,110..111,113..115,118,138,
                     141..142,145,229,232..233,236..238,241,269,273,333..334,
                     338,342,357,360..361,364..365,368)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340877"
ORIGIN      
        1 mfrrattrvl lllcamylit yvdrvnvsta asqfaaelhl shtevgivfs afaypyllfq
       61 iiggwvgdrf gprrtlavca liwagatvlt glaggfasmi varlllglge gatfptatra
      121 msnwmpadrr gfaqgtthaa srignavapp livwlmlmsg wrgafivtgv vsflwallwi
      181 wyfrddprah priteaecag lerytgaker epvpwrrlaa rmspvtavyf cygwvlwlfl
      241 gwipqyflhn yhmqlgksal fasgvffagv lgdwlggsvt drilkksqnl rlarnvmvgv
      301 cmfltllsla pilfvqnvtv tlaalclsgg fffnemtigp mwavpmdiap khagtasgim
      361 ntgsaaaaiv spvvggwlid rtgnwnlpft vsmaimaagi vlsftmrpdr aldsasrsad
      421 gahahtaa
//
LOCUS       WP_176081666             247 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Paraburkholderia tropica].
ACCESSION   WP_176081666
VERSION     WP_176081666.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..247
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27013
     Region          24..234
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mqnadipdaq lasaqpeahe lalpklarqr lhdtvvdhlr efivegqlap gvklnerklc
       61 evlgisrtpl realkvlaae glieispnrg atvaqlseae irdmfelmsg lesfagelac
      121 arisegelaq ikvlhaamlv craqndlsgy yarnhaihdl inaaarnval rqtyvtlnrr
      181 lqalrfrsnf qtakwdsair dheamiaale arngaalsai lrshllakrd avlaehtlsv
      241 agmrapr
//
LOCUS       WP_176081677             333 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Paraburkholderia tropica].
ACCESSION   WP_176081677
VERSION     WP_176081677.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..333
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36073
     Region          5..225
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 mqtilsienl skvyatgfra lsninldigr geifallgpn gagkttlisi vcgivnpseg
       61 rvrvaghdiv tdyraarsli glvpqelttd afetvwatvs fsrglfgkpp npayvervlr
      121 dlslwekrnn kiltlsggmk rrvliakala hepqilflde ptagvdvelr rdmwelvrgl
      181 kangvtiilt thyieeaeem adrigvinag eimlverkdv lmrklgrkql tlqldtplta
      241 ippalaawrl elgndgaelt ytydaenern diiallkslg dagigftdlk tsqssledif
      301 vslvgkdaaa aargtattsa tsaesgqdqe tsr
//
LOCUS       WP_176081686             389 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Paraburkholderia tropica].
ACCESSION   WP_176081686
VERSION     WP_176081686.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11441727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..389
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40738
     Region          207..>382
                     /region_name="YccC"
                     /note="Uncharacterized membrane protein YccC [Function
                     unknown]; COG1289"
                     /db_xref="CDD:440900"
ORIGIN      
        1 miaaacsrav nrallhdpef arlrgaarst laslltaslg vpwalqhhqt atlavpaalf
       61 amiaplflre arlsgwlvsl lilcgcacaa faaaatvaaq pmwrdagsll vvfvgmlcqs
      121 lgaravgaal ltlvafylgl ylhpvdarla emltgmalap fvvafvgrvl ipverveaas
      181 srsraafvrg vpasvaaaka rialalrlaa dvlvtgrpsr rplsellahr lhrlawrpal
      241 vatvaallam lagsalsadr amwavistfv vflgttshqg trarvmkria gtltgaaasv
      301 lliglcghep wllvaatals vfgwayyilh ayargvffit mlvglvygql gfaivplarl
      361 rieevlagcv islvvamllm psasapera
//
LOCUS       WP_176081689             607 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA-binding protein [Paraburkholderia tropica].
ACCESSION   WP_176081689
VERSION     WP_176081689.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13774834
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..607
                     /product="DNA-binding protein"
                     /calculated_mol_wt=63920
     Region          9..127
                     /region_name="KfrA_N"
                     /note="Plasmid replication region DNA-binding N-term;
                     pfam11740"
                     /db_xref="CDD:432038"
     Region          <151..>587
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
ORIGIN      
        1 mssssiaitd elvaeiadrm aedgqtvspv aiwsevhtgs vvsvaaslrk wrearaprvp
       61 qvserpalpd avtetmrdal drlwtsaqde aeravtrrla smrervedac nerddalael
      121 qntvqeldsl qvqldrmtsa yeakvdagsg ldedialavq rtdaaekrvq eltervnlle
      181 aeleqaasef aaeraareaa eaevvrqtei aaaataaaqq ivaeqaaaae raaaeqaaaq
      241 aaaeqaaaek aaadqiaaeq aaaeqaaaeq aaaqhaaeqa aaeqaaaela teqaaaeqaa
      301 aeqaaaeqaa aqaaeqaaep avdneaeraa leaahaetvs rlegelesir aalqaeqeah
      361 aarrdevssa qaerdaaase lqnvqtqvas lteerdagat eiarlsatvt eaqeraaels
      421 qlaenaaaea aanaeaiaka eqavkdaqea healqaqaqa qaeeaqaaas apqeaqqaaq
      481 qdtaaieale tlkaqftqea qthaaainea rdnlkkwady anglkqqliq sneqmmliha
      541 rgvgeaslsr rlagelsqlk pdhellrkef qqrviveais aqleaqgyry dastgavtkl
      601 naenasa
//
LOCUS       WP_176081699             332 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease
            [Paraburkholderia tropica].
ACCESSION   WP_176081699
VERSION     WP_176081699.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..332
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=35806
     Region          25..310
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mmptrnlgwl alfviglalp flvrsdyslt vmstafifal atiglnlltg ytgqfnlahg
       61 gfmavgaytv giltvdyqvp fwiafalagv vsvvlgffvg lvslrlkgny faiftlcvgy
      121 iiflaiekwd slthgvvgii giaappsigs isfenpraly yltfaflaag mwimhrivns
      181 lvghtfvair nsehlaqalg idlmrnkmla flistfyagi agglyagfvr flgpdlanig
      241 htfdmtmyvv vggigtlagp llgaialpwl tqslqfmqdy rflvfgplli vlliflprgl
      301 vglyqsvrsr latrdvapar trratssgdg ha
//
LOCUS       WP_176081708             741 aa            linear   BCT 11-JAN-2025
DEFINITION  TonB-dependent siderophore receptor [Paraburkholderia tropica].
ACCESSION   WP_176081708
VERSION     WP_176081708.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Brillet,K., Journet,L., Celia,H., Paulus,L., Stahl,A., Pattus,F.
            and Cobessi,D.
  TITLE     A beta strand lock exchange for signal transduction in
            TonB-dependent transducers on the basis of a common structural
            motif
  JOURNAL   Structure 15 (11), 1383-1391 (2007)
   PUBMED   17997964
REFERENCE   2  (residues 1 to 741)
  AUTHORS   Ferguson,A.D. and Deisenhofer,J.
  TITLE     TonB-dependent receptors-structural perspectives
  JOURNAL   Biochim Biophys Acta 1565 (2), 318-332 (2002)
   PUBMED   12409204
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11469152
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..741
                     /product="TonB-dependent siderophore receptor"
                     /GO_component="GO:0009279 - cell outer membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015267 - channel activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0015891 - siderophore transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=79522
     Region          86..741
                     /region_name="FhuE"
                     /note="Outer membrane receptor for ferric coprogen and
                     ferric-rhodotorulic acid [Inorganic ion transport and
                     metabolism]; COG4773"
                     /db_xref="CDD:443805"
ORIGIN      
        1 mnnhetarrr gqklprplqi avwltfaaaa psafaqtatt andsaaapag asaaasaaaa
       61 atgaekalpa vnvnaaavvd splhlatpvs sgalgtrsql dtpfsttvvt gedladrqan
      121 klgdvfagda svtdnssays awatyitvrg lpidwqngfk idgnpfisyg itmpyenler
      181 vellkgaggf mygfaqpggv vnyvtkkpgk npvtsfdigy rmdgvlsqha dlsrrfgpdg
      241 mfgarinyth eqgktynagd inrnsvalal dgqltrdldi yfnaiyqtsr ssgqtpaiyi
      301 pssyvgtslp atisggsnll nsagqhlntn lqlytagvky qitpdwtfnt sasysksard
      361 rnestltlls qsgdysdyrw ngdeghqdiy wqgafegkvk tgpfthqiva gasiqhqtnd
      421 ystaagtagg tlgagnlyvq npyafysgsg ldkyrasein qkalflsdtm qitsrwslla
      481 glrytnydqe sfseaggtts sygkngvvtp tfalmyklep ettlyasyve sleagqvvsd
      541 iyanggsvln plrsrqyevg ikseharwsa naalfrierg asyandqnvl mqdgnsiyeg
      601 leagasvrlg rswqvagdim lldtwyakgq tyngkrvaga pqftaatrvt ydvpyvpglq
      661 lgvdakytgn tevrpagdle tggyllvnvg anyvtriggh dvtlraaldn itnrrywmfq
      721 ydsyiapgdp rtislnakid f
//
LOCUS       WP_176081719             271 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Paraburkholderia
            tropica].
ACCESSION   WP_176081719
VERSION     WP_176081719.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..271
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=29160
     Region          20..263
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 mndeatheav ngrirvdrde rddaiaivti drpaklnalt rtlwrtlggt fetlsadasl
       61 rcivlrgage kafspgndig efatdrsnve qareygalmh rtlnlidacp vpvvamihgi
      121 cvggglelaa lcdlricges srfgapiknl glvmahaeln allrlageav aleillegri
      181 ldarealakg lvtrvvpdae vsahaldtar riaggaplva rwhkqfvrra rnpaplseae
      241 rdegfacfgt edfrigyqaf lakstpqfkg r
//
LOCUS       WP_176081789             380 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia tropica].
ACCESSION   WP_176081789
VERSION     WP_176081789.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..380
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=38379
     Region          10..374
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(20..21,24..25,28,60,110..111,113..115,118,137,
                     140..141,144,209,212..213,216..218,221,249,253,302..303,
                     307,311,327,330..331,334..335,338)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 mdfadrpatr latrlaflva gfgiacwapl vpfakhrldv ddgllgmlll ciglgsvaam
       61 mltgalsary gskpiivasg iglaivlpll tiaatplalg itllafgaal gsldvamnvh
      121 aveveraaqr plmsgfhalf svggfagstf mtfllsmqvg alestllcsv lmlaamlvar
      181 prllrakqag ggplfvtprg ivlliaaltg itflaegall dwsallitgk glvsaaqggl
      241 gymlfaiamt agrltgdavt arigdratli wggavavagf avvllspltt lalagfllig
      301 lgaanivpvl frragsqqam paamaiaait ttgyagilvg pagvgfvaka vgletafwvl
      361 lgllcivpcc atlvtanakq
//
LOCUS       WP_176081798             477 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Paraburkholderia tropica].
ACCESSION   WP_176081798
VERSION     WP_176081798.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..477
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=52317
     Region          86..475
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 mnsssnvvpp stalssqnag aprryrlvlw salavlllmm tcavyafayp ermpkavgem
       61 lenefgvnph pvhlmrpqna plsllaqigk qifydpslsa sgtqscasch spqhaygppn
      121 alavqlggeh ltlegyrppp sltylyrqan fsigpdpvdm dttpvslndt aqqaqgvara
      181 qknagvapaa pamvpqgglf wdgradtlqa qamgplfnpv emantseaev aqkllrggya
      241 eklkklfgpa mlhspvmlvd eamsavsryq iedasfhefn skydewlegk arlspaelrg
      301 lrlfnnqdka ncagchlsqp grdglpplft dtqyealgvp rnpalaqnkd akffdmgvcg
      361 pyrhdlatqt qycgmfltpt lrnvstrqtf fhngvyrdlk qvmdfynlre tspekiyprd
      421 aagkvekynd ippkyaanid vadapfdrkf gdrpamseqd iddiiaflkt ltdgykn
//
LOCUS       WP_176081799             533 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Paraburkholderia tropica].
ACCESSION   WP_176081799
VERSION     WP_176081799.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..533
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=59264
     Region          3..533
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 matnqsadvv ivgagiasgq iaqklakagi dvlmleagpr ierwriveny rnspfksdfq
       61 spypptehap hpqyspsndy lvqrgpeqyk agylrmvggt twhwsaqswr llpndmklkt
      121 lygvgrdwpi syddlepyyy eaevemgvgg pedlgsprsk pyphpplpls dfdqkfkdvv
      181 ekagykhvte paarntapfd grpaccgnsn cmpicpieaq ytgetairka eaakarllpn
      241 avvyriehde narivavhyk dpdgntqrvt gkifvlasna ietpklmlis ksdkfqdgig
      301 nssdqvgrnl mdhpgttvtf lsaepmwpgr gpmrlscinn lrdgafrsey samklnvgny
      361 spmravsdyl iskgvygael dekirdyasr wvvvnsffdi lpdpenrita stefkdklgi
      421 arpevhyrid dyinraakva rghyahiadl fggtevrfdd syfnnnhimg tlimgddprd
      481 svvdkdqrsh dhenlfiass gtmasagtvn ctltlcalsm rladklidem kha
//
LOCUS       WP_176081817             338 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Paraburkholderia
            tropica].
ACCESSION   WP_176081817
VERSION     WP_176081817.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 338)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..338
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36227
     Region          19..318
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mtptfnrrrf lrgvgllgas vaasglaapy largasapir ivsnpglena tlnalmdelg
       61 yfkrfgvnaq iveipgvhgp ldamaagagd vcmvsgynlv lsriaqgarv kivgagmkrc
      121 altvfarpdg attladlkhk tvavgpergl lhslmvqllk argidysqvr fvdkgsnddc
      181 haavvkgevd ascssishln drdglvvind gnmwqalphc ifqtayasdd airnkhddmv
      241 avmaaygaly eflmspdsrd affaarkhaq krfdaasaqa iwqfnetqrp yskdlsltea
      301 diaylqdmyi glgsldrkqd faevadmsaa reaakllg
//
LOCUS       WP_176081865             524 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Paraburkholderia tropica].
ACCESSION   WP_176081865
VERSION     WP_176081865.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..524
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=53419
     Region          42..519
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(43..44,47..48,51,83,133..134,136..138,141,162,
                     165..166,169,293,296..297,300..302,305,333,337,389..390,
                     394,398,414,417..418,421..422,425)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msdssvssva ldsaaptdph pdsfssrhpn vtlavasatc alivldtnvv avslpaiaha
       61 fhasfadiew vvsaymtafa acllpagaia drfgrrrvlq cglalfalas lgcgvaptaa
      121 lliaaravkg lgaallltsa laviahrfaq gpsrerawai wgmcmgiata iapwvggait
      181 qwvgwrwifl mnlpvcavla lgarraides rdphakrldl pggmlfaaal acavstligi
      241 pahgwqsgat lgrgaasial falficsqrw qtrpmidlrl frrarfvgal lgmfgyaaca
      301 qvmmtflply lqiafgltal qaglgmlpfa aamiagpslg aalarrvttg gvlsaglali
      361 gagnlamaac aagghylava famlvtgtga gvmngdtqka imacvprert gmasgisttt
      421 rftaivtavg vlgavlavrt hsalvqsiag vpaalhavda rfmasllagd pgealrtlda
      481 ptahllaqaa plafahgfar allvsgvval vsaiavklma dard
//
LOCUS       WP_176081917             441 aa            linear   BCT 11-JAN-2025
DEFINITION  GspE/PulE family protein [Paraburkholderia tropica].
ACCESSION   WP_176081917
VERSION     WP_176081917.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Planet,P.J., Kachlany,S.C., DeSalle,R. and Figurski,D.H.
  TITLE     Phylogeny of genes for secretion NTPases: identification of the
            widespread tadA subfamily and development of a diagnostic key for
            gene classification
  JOURNAL   Proc Natl Acad Sci U S A 98 (5), 2503-2508 (2001)
   PUBMED   11226268
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457962
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..441
                     /product="GspE/PulE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0009306 - protein secretion [Evidence
                     IEA]"
                     /calculated_mol_wt=46740
     Region          <42..438
                     /region_name="PulE"
                     /note="Type II secretory pathway ATPase GspE/PulE or T4P
                     pilus assembly pathway ATPase PilB [Cell motility,
                     Intracellular trafficking, secretion, and vesicular
                     transport, Extracellular structures]; COG2804"
                     /db_xref="CDD:442055"
ORIGIN      
        1 mfsiphrsrs sngshalaae glsngggggg naraslntps paaslddapa vrlladtlre
       61 aarrnasdlh vepleqgwri rvridgvlhe iarppvhlrd afvtrvkvla rmdiaerrip
      121 qdgrlrlapl aqhasaedyr vnslptlhge klvlrrleal padlslaalg lddtqqhtlg
      181 aaiaaphglv lvtgptgsgk tlslycflqr lndasrnlcs vedpaeiqla ginqvnvrek
      241 agltfalalr allrqdpdvi migeirdeet asvavkaaqt ghlvlstlht ndapaavarl
      301 idigvepynl aaalrlvtaq rlvrrlcpqc rvpsneseav lraaglevda rasslsspss
      361 vfaargceac hgigyrgrvg ihevmpvsas mremivgkrs aheiahqara esvatlrdaa
      421 larvrdgtts laealaatdt p
//
LOCUS       WP_176081933             870 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Paraburkholderia tropica].
ACCESSION   WP_176081933
VERSION     WP_176081933.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 870)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 870)
  AUTHORS   Palmgren,M.G. and Nissen,P.
  TITLE     P-type ATPases
  JOURNAL   Annu Rev Biophys 40, 243-266 (2011)
   PUBMED   21351879
REFERENCE   3  (residues 1 to 870)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   4  (residues 1 to 870)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   5  (residues 1 to 870)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   6  (residues 1 to 870)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457580
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..870
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..870
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015662 - P-type ion transporter activity
                     [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=89295
     Region          16..90
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          108..869
                     /region_name="ZntA"
                     /note="Cation-transporting P-type ATPase [Inorganic ion
                     transport and metabolism]; COG2217"
                     /db_xref="CDD:441819"
ORIGIN      
        1 mneplvadsa aasrvaelei hgmtcascam rvekalakvp gvtrasvnla tekatveana
       61 daegaqvaas afvdrlvaav ekagyeaapi vdenpasadn dadspaiahf aiggmtcaac
      121 snrvekvlak vpgvasvsvn lateeaavtl ngplsgemsd qlvavvkkag yeatpivkda
      181 pagsaahaat dsaahggaps raaaaedaar relravliaa vltaplvvpm fghwlglhwm
      241 lpaaaqlvla sivqfgfgar fyraawkavr agagnmdllv algtsaawgv svyamlahpg
      301 dtahlyfeas avvitlvrfg kwlearakrq ttdairalna lrperarlre ngaerdvpla
      361 qvrvgaivvv rpgerlptdg vvlegrshvd eslitgeslp vpkepgepvt agsingegli
      421 avrttkigae ttlariirlv esaqaekapi qrlvdrvsav fvpailviaa itlggwllag
      481 asaetailna vavlviacpc alglatpaai magtgvaarh gvlikdaeal etahnvgvva
      541 fdktgtltlg qpsltafepa ggfvrnetla laaavqqhsd hplakavvka yddasqgapl
      601 paaadaravp grgvqaqveg wqlaigsarw vaelaldvps alaaratale aegntiswli
      661 gtqsgaqsna qseanpdakp dtvlallafg dtvkptarda iarlksmgir svlvtgdnag
      721 sahavaaelg idevhaqvlp ddkartirdl kirsgaivam vgdgindapa laaadigiam
      781 atgtdvamna agitlmrgdp alvaaaidis rrtwrkiqqn lfwafvynli giplaafgll
      841 npmlagaama fssvsvvtna lllrtwrdkr
//
LOCUS       WP_176081961             391 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Paraburkholderia tropica].
ACCESSION   WP_176081961
VERSION     WP_176081961.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..391
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41406
     Region          49..390
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mgvagkhfps hapddaqdpr apqpaqasas hgdervrres wfghllgrpe faaisgtvlv
       61 favfaigagg sgmfdldgvm nwsqvaaylg ilsvgacllm iagefdlsig smigfagmmv
      121 aiptmyfhwp ialsivfafv gctalgalng ylvmrtrlps fivtlaflfi lrgltlalsi
      181 mfadrtivsg vgdvakadyv tnllfhgtaf kglfvalahi gigkmldngq plvpgvpkvi
      241 lwwfalvivg afvlaktryg nwilavggds naaknvgvpv krvkislfml tafcsclfav
      301 lqvcdigsaa adrglqkefe aiiaaviggt lltggygsvi gaafgalifg vvqigitytn
      361 idsdwfrvfl gmmlliavlf nhyvrrrvaq s
//
LOCUS       WP_176081999             238 aa            linear   BCT 11-JAN-2025
DEFINITION  (2Fe-2S)-binding protein [Paraburkholderia tropica].
ACCESSION   WP_176081999
VERSION     WP_176081999.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Meyer,J.
  TITLE     Ferredoxins of the third kind
  JOURNAL   FEBS Lett 509 (1), 1-5 (2001)
   PUBMED   11734195
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449880
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..238
                     /product="(2Fe-2S)-binding protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0051537 - 2 iron, 2 sulfur cluster
                     binding [Evidence IEA]"
                     /calculated_mol_wt=24462
     Region          71..233
                     /region_name="CutS"
                     /note="Aldehyde, CO, or xanthine dehydrogenase, Fe-S
                     subunit, CoxS/CutS family [Energy production and
                     conversion]; COG2080"
                     /db_xref="CDD:441683"
ORIGIN      
        1 mshdrshdap aaadapastp padtsrrrfl qsaaaaaalg atphlhaqpn apasdaandt
       61 asappvvpaq pvqlningre yalhieprvt lldalrdyag ltgtkkgcdr gqcgactvlv
      121 egrrinaclt lavmhegqri ttveglasat qpsplqrafv erdalqcgfc tpgqlcsata
      181 clsefaagta saatadvrtr paqlsdaeir ermsgnlcrc gayvnivaav rdahsaga
//
LOCUS       WP_176082008             266 aa            linear   BCT 11-JAN-2025
DEFINITION  (Fe-S)-binding protein [Paraburkholderia tropica].
ACCESSION   WP_176082008
VERSION     WP_176082008.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Wang,S.A., Ko,Y., Zeng,J., Geng,Y., Ren,D., Ogasawara,Y., Irani,S.,
            Zhang,Y. and Liu,H.W.
  TITLE     Identification of the Formycin A Biosynthetic Gene Cluster from
            Streptomyces kaniharaensis Illustrates the Interplay between
            Biological Pyrazolopyrimidine Formation and de Novo Purine
            Biosynthesis
  JOURNAL   J Am Chem Soc 141 (15), 6127-6131 (2019)
   PUBMED   30942582
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..266
                     /product="(Fe-S)-binding protein"
                     /EC_number="1.5.3.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /calculated_mol_wt=28396
     Region          <1..262
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 mkprlyptgp rptdvylfat clvdlfvpqa gldavkller egltvhfprg qsccgqpays
       61 sgnprqarev araqlglfeq pwpvivpsgs cagmmrhhwp alfadeaade araldlssrv
      121 yelteflvrv ldvdlgaaga yadaartqpd ervvlhtscg arremgtrvh gveavdalpg
      181 vtrveheres eccgfggtfs lkhpdisgam vadkiasaca tgcdrlvsad cgcllnigha
      241 aarkgaplev ehlasflwrr tggdaa
//
LOCUS       WP_176082049             145 aa            linear   BCT 11-JAN-2025
DEFINITION  PaaI family thioesterase [Paraburkholderia tropica].
ACCESSION   WP_176082049
VERSION     WP_176082049.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..145
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=15348
     Region          1..135
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mtdlvdrarg alhaqpfsvl lgtelmhvga deltlrllvr delkqqhgfv hggvisylad
       61 naltfagala lgprvvtgey kinylrpalg gtlmararvv hagrqqatcq csvfvmedgg
      121 erlvalaqgt inrmgdngdn nghaa
//
LOCUS       WP_176082067             686 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 28 protein [Paraburkholderia tropica].
ACCESSION   WP_176082067
VERSION     WP_176082067.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 686)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 686)
  AUTHORS   Abbott,D.W. and Boraston,A.B.
  TITLE     The structural basis for exopolygalacturonase activity in a family
            28 glycoside hydrolase
  JOURNAL   J Mol Biol 368 (5), 1215-1222 (2007)
   PUBMED   17397864
REFERENCE   5  (residues 1 to 686)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   6  (residues 1 to 686)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11475089
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..686
                     /product="glycoside hydrolase family 28 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=70310
     Region          146..644
                     /region_name="Pgu1"
                     /note="Polygalacturonase [Carbohydrate transport and
                     metabolism]; COG5434"
                     /db_xref="CDD:444185"
ORIGIN      
        1 mptqnnengl aparasgapa sparrsfmaf agatagasll gtlpgcggst taastadtgt
       61 aasvdpiwgt ggaaqqiida vqhvalslfp stdylvtnyg aqplttqvva atawspaipw
      121 lgqtasptsp gadqmvsssi tgtaydsrta fnqaivaana agggrvvvpa gnwycggpiv
      181 llsnvnfhls anctiyfspn padyavdgph atanghlywt rwqandclnf gspiyayqqq
      241 nigltgegds silngqsmtp aqangvtpsf cwwtfkgtng aygcassstp sqayvnpnna
      301 alttlsssam tnpeaatllp lldtgtswaq dqnylpalae lgvtvaqrvf gnghylrpcm
      361 vefigctnvl mqnyhtqntp fwqhhptdck nvviqgvfad sigpnndgfd pdacsyvlad
      421 gvtfntgddc iaiksgkald ieygpaqyhv iqnctmnsgh ggltlgsems agvqniyarn
      481 lnmlnenwat nplniairik tnmnrggavq dvwidgvtlp ngvtlvgkgy gasnmiagsp
      541 itasvpvgtt ssagsnpaas qgglitfdcd yspagdavri sppvvknini snvtagnvts
      601 sgttascfqa ivaqgpvaad yngpapaptv lpisgvtitn cnlgtpvcsg ttsatnpgvi
      661 yvnnvnaitl nnvviggtty ntslvg
//
LOCUS       WP_176082094             223 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF1028 domain-containing protein [Paraburkholderia tropica].
ACCESSION   WP_176082094
VERSION     WP_176082094.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465224
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         1..223
                     /product="DUF1028 domain-containing protein"
                     /calculated_mol_wt=23209
     Region          2..210
                     /region_name="COG3342"
                     /note="Uncharacterized conserved protein, Ntn-hydrolase
                     superfamily [General function prediction only]"
                     /db_xref="CDD:442571"
ORIGIN      
        1 mtfsiagrca rtgavggivt sssiavpsrc lwasrdgvvl sqnvtdprlg qiglgelaqg
       61 ygaqavleri agarpytewr qlavldaagf sawrtgergl glhagasgtd cvavgnllan
      121 dsvpaamiea faehaaralp drllraleag laaggeagpv hsaglcvfdg aswpvaelrv
      181 dwsdrpiaal ralweryepq mkdyvlratd ptrapsygvp gde
//
LOCUS       WP_176082146             342 aa            linear   BCT 11-JAN-2025
DEFINITION  ShlB/FhaC/HecB family hemolysin secretion/activation protein,
            partial [Paraburkholderia tropica].
ACCESSION   WP_176082146
VERSION     WP_176082146.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Aoki,S.K., Diner,E.J., de Roodenbeke,C.T., Burgess,B.R.,
            Poole,S.J., Braaten,B.A., Jones,A.M., Webb,J.S., Hayes,C.S.,
            Cotter,P.A. and Low,D.A.
  TITLE     A widespread family of polymorphic contact-dependent toxin delivery
            systems in bacteria
  JOURNAL   Nature 468 (7322), 439-442 (2010)
   PUBMED   21085179
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Zeth,K.
  TITLE     Structure and evolution of mitochondrial outer membrane proteins of
            beta-barrel topology
  JOURNAL   Biochim Biophys Acta 1797 (6-7), 1292-1299 (2010)
   PUBMED   20450883
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Hertle,R.
  TITLE     The family of Serratia type pore forming toxins
  JOURNAL   Curr Protein Pept Sci 6 (4), 313-325 (2005)
   PUBMED   16101433
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458196
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         <1..>342
                     /product="ShlB/FhaC/HecB family hemolysin
                     secretion/activation protein"
                     /GO_component="GO:0046930 - pore complex [Evidence IEA]"
                     /GO_function="GO:0015288 - porin activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0015031 - protein transport [Evidence
                     IEA]"
     Region          2..>342
                     /region_name="FhaC"
                     /note="Hemolysin activation/secretion protein
                     [Intracellular trafficking, secretion, and vesicular
                     transport]; COG2831"
                     /db_xref="CDD:442079"
ORIGIN      
        1 rrdaqqreaa vsapavrstv tkieaypalp aetpcfridr faldvpdtlp aaahakgasa
       61 lpldpfafar ewldhytgqc igkqgidils kalqqavlsr gyvttrvlvp qqdlttgtls
      121 falvpglvrq vrladpsmwg twknafpvsg gdllnmrdle qgleqmkrva sqdvdmkiep
      181 tdipgesdvv vsvrrakpwt fvasvdnsgt estgkwqgnv slgidnplgl ndvftvsanq
      241 dlsfgnkalg shgfngsysv pfgywtatls gntstyyqni agvnetfvss gnsqtaalri
      301 arvlsrgqnd vlggyvqlsk rfgdsfiddt tiptqarnnt fl
//
LOCUS       WP_176082379             427 aa            linear   BCT 11-JAN-2025
DEFINITION  adenylate/guanylate cyclase domain-containing protein [Leptospira
            alexanderi].
ACCESSION   WP_176082379
VERSION     WP_176082379.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Linder,J.U.
  TITLE     Substrate selection by class III adenylyl cyclases and guanylyl
            cyclases
  JOURNAL   IUBMB Life 57 (12), 797-803 (2005)
   PUBMED   16393782
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Hurley,J.H.
  TITLE     The adenylyl and guanylyl cyclase superfamily
  JOURNAL   Curr Opin Struct Biol 8 (6), 770-777 (1998)
   PUBMED   9914257
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..427
                     /product="adenylate/guanylate cyclase domain-containing
                     protein"
                     /EC_number="2.7.7.-"
                     /EC_number="4.6.1.-"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0009975 - cyclase activity [Evidence
                     IEA]"
                     /GO_function="GO:0016779 - nucleotidyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /GO_process="GO:0009190 - cyclic nucleotide biosynthetic
                     process [Evidence IEA]"
                     /GO_process="GO:0035556 - intracellular signal
                     transduction [Evidence IEA]"
                     /calculated_mol_wt=48336
     Region          48..426
                     /region_name="AcyC"
                     /note="Adenylate cyclase, class 3 [Signal transduction
                     mechanisms]; COG2114"
                     /db_xref="CDD:441717"
ORIGIN      
        1 mpdsvlevlk keersgiiit nyfrylialf flvqiivnvn ngnhkfnlia fliylsltfv
       61 htivirvspl svvsvfnyit lfteyllilg vllfytfttk nvdlgfalkn pinlfflfpi
      121 iysllqfkir fvfiglflfy liyysilwva vsqgqlmytk dwgsyvsgpn iliedivagk
      181 pglyfcfamm ismgifrtis mvkrigiveg qktelsryfs pkivnemven petfqngnrq
      241 ivsilfldir nftsmsenmd pkelgellse frkimtecvf enngtldkyi gdavmatfgt
      301 pnpspsaevd arnavgcgvi mqkrlaewnl lrkskgktpi sigigihtge vfagnvgsdl
      361 hreysvigda vntasriesl ckvlkkpfli sketmellgg kytlnrmprv kvkgkeeplq
      421 iyevvwg
//
LOCUS       WP_176082408             474 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar phosphate nucleotidyltransferase [Leptospira alexanderi].
ACCESSION   WP_176082408
VERSION     WP_176082408.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135430
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..474
                     /product="sugar phosphate nucleotidyltransferase"
                     /EC_number="2.7.7.-"
                     /GO_function="GO:0003977 - UDP-N-acetylglucosamine
                     diphosphorylase activity [Evidence IEA]"
                     /GO_process="GO:0006048 - UDP-N-acetylglucosamine
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=54654
     Region          1..225
                     /region_name="NTP_transferase"
                     /note="NTP_transferases catalyze the transfer of
                     nucleotides onto phosphosugars; cd04181"
                     /db_xref="CDD:133024"
     Site            order(3..6,20..21,77,103,105..106,170)
                     /site_type="active"
                     /db_xref="CDD:133024"
     Site            order(3..5,50,103,105)
                     /site_type="active"
                     /note="Substrate binding site [active]"
                     /db_xref="CDD:133024"
     Site            order(105,223,225)
                     /site_type="active"
                     /note="Mg++ binding site [active]"
                     /db_xref="CDD:133024"
     Region          249..428
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(252,254,330)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(279,329..330)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            328..330
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 miaaagkgtr ayprttyipk plfefqgkti lernvelmqs tfrvkkiyil vghlkemvls
       61 eiekirknhq nveiipspwt tkglasdias lesqirspfi tilgdefyfh pdhkkfiqtf
      121 rkhpkliasi gvqkttllsr irknysvelk gdrilelvek psdppnnllg lgsylftpay
      181 feyfketpps akngiieitd vidlmakksr kvfateldve yfninsmqdy hhavyeirne
      241 efarfkttli vptknnersi advivdfrgk vdeilvvdfg stdktleiak kekakvlsfk
      301 tegdedhfgk qiregiraas gdiaiiitpd gsyrskdypk lleylkdsdm vigtrttrqm
      361 ieqgsnllpg vrvvnlilgk lievfwwgme prftdamcsy faiwkdsysk iepdlemndr
      421 riipelmmet vrsymrciei pisyyrpies vpknttrefl sivrlmlkkk wfgn
//
LOCUS       WP_176082436             312 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176082436
VERSION     WP_176082436.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..312
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33302
     Region          6..233
                     /region_name="CcmA"
                     /note="ABC-type multidrug transport system, ATPase
                     component [Defense mechanisms]; COG1131"
                     /db_xref="CDD:440746"
ORIGIN      
        1 msnpvieven ltkryknava vdginltigr geifgllgpn gagktttilm llglteptfg
       61 svrilghdpl replevkrrv gylpdavgfy dqlsarenla ftarlggiga edasarieqa
      121 marvrltevt drrvssfsrg mrqrlgiael lvkgsevail deptagldpq stqelleliv
      181 tlsregmtiv lsshllsmvq aictrvalfn kgkvgllgrv pdlasqvlgg ayvieadidd
      241 ldaeatlsgl egvtrvspmq sgltridatg dvrsavarrv veaggtlksl sisrsdlddv
      301 yaryfeevsh aa
//
LOCUS       WP_176082437             337 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176082437
VERSION     WP_176082437.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 337)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..337
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=35761
     Region          33..230
                     /region_name="NosY"
                     /note="ABC-type transport system involved in multi-copper
                     enzyme maturation, permease component [Posttranslational
                     modification, protein turnover, chaperones]; COG1277"
                     /db_xref="CDD:440888"
ORIGIN      
        1 mppdattadq spavlsgtgh kpskgspfqg latvalkeaa dhmtsprmhl vmllmvltai
       61 gaiyaaigqi kntvsedpfl flnlftlakq pfpsfvalls fllslvgitl gfdavngeyn
      121 rrtmsrilsq piyrdgllag kflgallvva inlialfllv tgmgilmlgl ppsgeealrg
      181 laflitclay sgvwlavaml fstvfrtpat salaaltlwl iftlfwsmia pgvasliapi
      241 dpynpmtaih qaeitqvisr fspstlfgea atgllnpatr slglvfmsqm qgaipgaplp
      301 ldqslllawp elagliaamv ivyaiayiaf qrqeira
//
LOCUS       WP_176082439             296 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Martelella sp. HB161492].
ACCESSION   WP_176082439
VERSION     WP_176082439.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13722860
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..296
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32608
     Region          24..173
                     /region_name="AraC_N"
                     /note="AraC-type transcriptional regulator N-terminus;
                     pfam06719"
                     /db_xref="CDD:461994"
     Region          <186..292
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 meqdllrrvd rltrtgtppv mtdvpglvlm rydhqrqpnh limrpalcvt lqgaktslig
       61 dtthfygagd alvvsmempa igtiiaasps epylgiaimf dagimhaalt emdepltspa
      121 rprnafvsrf dgpveacver lvalldrpka ipvlypaimr elsywllsgp ggadlaammf
      181 gseripsvlt alhllrdrfr etvrveelae sarmsasvfh rrfkaltamt pvqyqkrlrl
      241 iegrrliige avnvenaafr vgyesasqfs rdysrmfgvp pradkgapaa erlsea
//
LOCUS       WP_176082447             225 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176082447
VERSION     WP_176082447.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 225)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..225
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24317
     Region          2..221
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mpalelrdia vsfeglatpv laidrleiaa gehvaisgps gsgkstfvni vtglerlrag
       61 raiwgdtdls alsesrrdrw rgdnvglvmq dfhlfaglsa lenvllparl shrlssalqd
      121 raaalladvg ltrptqriet msrgemqrva iarallrepa ilvadeptas ldaeagatva
      181 glllklaarr ettlivvshd erllepmqrr lrfhagriva ddwrp
//
LOCUS       WP_176082444             212 aa            linear   BCT 11-JAN-2025
DEFINITION  DedA family protein [Martelella sp. HB161492].
ACCESSION   WP_176082444
VERSION     WP_176082444.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..212
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=22740
     Region          1..188
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 msdqilalvp lygvpvmala vmlscigipi paalvmligg smvatgemsp gpsyiaslla
       61 atagdqigfw vgrlggrpmi ekftrdrpkr vamvqrahdf tekrgalaif ltrwllamig
      121 pyvnpvagas gmrwrifsia afageilwvg iyiglgytfs hnivavaqia gnasgfiaag
      181 latlflgwri trvlhmslkn gkrrflkprg rr
//
LOCUS       WP_176082471             136 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF805 domain-containing protein [Martelella sp. HB161492].
ACCESSION   WP_176082471
VERSION     WP_176082471.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006974
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..136
                     /product="DUF805 domain-containing protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=15046
     Region          18..133
                     /region_name="yhaH"
                     /note="Uncharacterized membrane protein YhaH, DUF805
                     family [Function unknown]; COG3152"
                     /db_xref="CDD:442386"
ORIGIN      
        1 msdtapsgra hrvvgfqeaf klafsnyanf rdrssrgafw ywvlaswivs vvlsvidyvl
       61 fggadnvgil egiwglatlf paiaigarrl hdinrtgwwq llsisiigvv vliywwcqpg
      121 eaetnrfgpd reagrg
//
LOCUS       WP_176082479             367 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176082479
VERSION     WP_176082479.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 367)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..367
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40147
     Region          1..360
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mtgvtlkqvk ksygkvevlh gvdlditpge fvvfvgpsgc gkstllrmia gledisggei
       61 fidgqvvndi ppskrgiamv fqsyalyphm svydnmafgm riakeskqei dqrvrkaadm
      121 lqitpyldrl pkalsggqrq rvaigraicr dpkvflfdep lsnldaalrv atrieiakln
      181 dsmpdttmiy vthdqveamt ladrivvlsg gfieqvgppl elyerpanlf vaqfigspam
      241 nimpavitra getteielrd gkrvnvpvkt pdgdvgkpvs fgvrpedvre aaededflfe
      301 gtvsilealg evtliyiegk lvdddpiivk lpgihegkpg damrfvaepd klhlfdesgr
      361 sylypkg
//
LOCUS       WP_176082516             204 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Martelella sp. HB161492].
ACCESSION   WP_176082516
VERSION     WP_176082516.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..204
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21608
     Region          5..203
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 msveflital vvvlipgtgv vytlaiglsq grrasiaaal gctigivpai aasilglaal
       61 fhtsaiafqa vkiagvaylv ylawmtlker gamavssagm ktrsmagvvr dgfllnilnp
      121 klsvfflafl pqfidagrgs allqmlelsa tfmvmtfivf viygqlsalm rdrvlsserv
      181 mvwmrrsval afagfglkla larq
//
LOCUS       WP_176082544             448 aa            linear   BCT 11-JAN-2025
DEFINITION  TldD/PmbA family protein [Martelella sp. HB161492].
ACCESSION   WP_176082544
VERSION     WP_176082544.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Hu,Y., Peng,N., Han,W., Mei,Y., Chen,Z., Feng,X., Liang,Y.X. and
            She,Q.
  TITLE     An archaeal protein evolutionarily conserved in prokaryotes is a
            zinc-dependent metalloprotease
  JOURNAL   Biosci Rep 32 (6), 609-618 (2012)
   PUBMED   22950735
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Murayama,N., Shimizu,H., Takiguchi,S., Baba,Y., Amino,H.,
            Horiuchi,T., Sekimizu,K. and Miki,T.
  TITLE     Evidence for involvement of Escherichia coli genes pmbA, csrA and a
            previously unrecognized gene tldD, in the control of DNA gyrase by
            letD (ccdB) of sex factor F
  JOURNAL   J Mol Biol 256 (3), 483-502 (1996)
   PUBMED   8604133
  REMARK    Erratum:[J Mol Biol 1996 May 31;259(1):203]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001052
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..448
                     /product="TldD/PmbA family protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008237 - metallopeptidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=46285
     Region          34..447
                     /region_name="TldD"
                     /note="Zn-dependent protease PmbA/TldA or its inactivated
                     homolog [General function prediction only]; COG0312"
                     /db_xref="CDD:440081"
ORIGIN      
        1 msvndassdl iknasrivda araagadaad vvvsegvsna isvrdgkren aqasenqgls
       61 lrvfigqria svstnsaddv salveraiam akvspedpya claepdrlah asadlelydt
      121 tavppeklae ralaaesaal avtgvskssg asaasgeivf alvtsggfag gyrrsyfsvs
      181 asavagdgta mqrdhdsdtr afdadltape eigrnagrra verlnprqle tqrgigiifd
      241 qrvatslvgh lagaisggai arktsflkds lgkkvmkagv sliddptilr gagsqpfdge
      301 gvaslpltmv gdgvleqwfl stalgrelgl vtngrgarsg nslsatgtnl ilepgtetpe
      361 ammkalgsgf lvtelighgv nmvtgeysrg asgfwfenge iaypvsqmtl agnlkdmyln
      421 mtpasdidrr ysiaapsllv egltlagr
//
LOCUS       WP_176082557             323 aa            linear   BCT 11-JAN-2025
DEFINITION  complex I NDUFA9 subunit family protein [Martelella sp. HB161492].
ACCESSION   WP_176082557
VERSION     WP_176082557.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Parey,K., Wirth,C., Vonck,J. and Zickermann,V.
  TITLE     Respiratory complex I - structure, mechanism and evolution
  JOURNAL   Curr Opin Struct Biol 63, 1-9 (2020)
   PUBMED   32058886
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Babot,M., Birch,A., Labarbuta,P. and Galkin,A.
  TITLE     Characterisation of the active/de-active transition of
            mitochondrial complex I
  JOURNAL   Biochim Biophys Acta 1837 (7), 1083-1092 (2014)
   PUBMED   24569053
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   7  (residues 1 to 323)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10142961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..323
                     /product="complex I NDUFA9 subunit family protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_process="GO:0010257 - NADH dehydrogenase complex
                     assembly [Evidence IEA]"
                     /GO_process="GO:0022904 - respiratory electron transport
                     chain [Evidence IEA]"
                     /calculated_mol_wt=33930
     Region          10..279
                     /region_name="NDUFA9_like_SDR_a"
                     /note="NADH dehydrogenase (ubiquinone) 1 alpha subcomplex,
                     subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs;
                     cd05271"
                     /db_xref="CDD:187579"
     Site            order(14,16..19,38..40,82..84,97,119..121,132,136,
                     155..158)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187579"
     Site            order(132,136)
                     /site_type="active"
                     /db_xref="CDD:187579"
ORIGIN      
        1 mtlsnipplv tvfggsgflg ryvvralakr gyrirvavrr pdlagflqpl gnvgqitfvq
       61 anlrypdsvk navsgashvv ncvgllfesg knkfdsvqak gaalvaeaar aegaalthvs
      121 aigasasaas syartkaage ravqdtlgda vilrpslvfg tedqffnkfa amtlsspflp
      181 ligggrtkfq pvyvgdvaea valsvegklv ngaiyelggr dvvdfrqcle milkitgrkr
      241 rlvsvpfgla slfagiasav plvrppvtpd qirllkhdnv vsaeaiaegr tleaagitpv
      301 vlgsvlpsyl vqyrehgqfg rva
//
LOCUS       WP_176082593             469 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding oxidoreductase [Martelella sp. HB161492].
ACCESSION   WP_176082593
VERSION     WP_176082593.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416043
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..469
                     /product="FAD-binding oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /calculated_mol_wt=51834
     Region          1..446
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
ORIGIN      
        1 mtdyqqikae legiaiednp amvlrksrdf ywyspilkaq lehvtgdliv spenedelik
       61 vlkvafkhda pvtargggtg nygqsmplsg givldmtkmn rikliepgrv iaepgiicae
      121 ldrqtkahsg qelrfhpstt gqatlggfia ggsggvgsvh wgglrdlgnv lrlrivtlea
      181 eprvmeltsl dllkvshayg tngiitevem plapayewvd vivghdsfmd avrfsdhlas
      241 stgiltkeia piaapvpyny ftrlkpflee gesisvvmva phsiepfkal vevhggtiry
      301 rsdtaentkg vprayelgwn httlramkme pdnftylqvq ypspghvakv qemcaifgde
      361 vighleflrf dgaiqcsglp lvryttperl eeiiriheen gcpvfnphry tleeggmkqt
      421 derqlefkke tdpkgllnpg kmiawddpef dfkagknylf kgitavtge
//
LOCUS       WP_176082609             305 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar kinase [Martelella sp. HB161492].
ACCESSION   WP_176082609
VERSION     WP_176082609.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..305
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32447
     Region          8..299
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(32..33,36,91,104,106,136,170,259,262,298)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(228,233,250,259..261,264,286,290)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mkklpenilc igecmvemap redgaynrgf agdtfnsawy lskvlpghft vdyfsgagnd
       61 avsgemlsfm enagvgtasi rriadrtvgl ymialknger sfsywrdvsa akllaedkda
      121 lraavkgrgm ilfsgitmav iyaehrqnll dvlsearaeg tivafdpnmr arlwpskdim
      181 aetimrsaav sdivlpsfde dgvvfgdadp katiaryrsi gvntvivkng petiyaedse
      241 egpvtfsptp sknvvdttaa gdsfnagmis almtghalvd alakgsalsa rvigargalv
      301 edaia
//
LOCUS       WP_176082597             129 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Martelella sp. HB161492].
ACCESSION   WP_176082597
VERSION     WP_176082597.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..129
                     /product="RidA family protein"
                     /calculated_mol_wt=13959
     Region          1..127
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mkksinppgv rqpfgnyshg lyvppgasll vtsgqlgigp ddviprtvkg qaelcfeair
       61 kileeggmsf adviringyv tmredfpaym evrdrytcdp lpvstllvvg gftraeflve
      121 vevtaakvl
//
LOCUS       WP_176082604             370 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176082604
VERSION     WP_176082604.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..370
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40990
     Region          1..366
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 marvelknle kvygkfkavh ginleiqdge fmvlvgpsgc aksttlrmia glerisggei
       61 rigedlvndk apgqrgiamv fqnyalyphm kvknnlsfgl rlkhapkdqi aaatedvshi
      121 leieeylerl pkqlsggqaq rvavgralik kpqvflfdep lsnldaklra smrvritdlh
      181 kqllsegmhs tvcyvthdqt eamtmgnric vmkegrimqv adpytlyqkp anafvagfig
      241 spemnigdat lgndgtikig tqtlklddkt larldkdapt evtyglrpqh fevvepgagn
      301 clngrvshve fmgheiflyl tiedqsftvv vpatgfrqqy lrdqqisiap redamhifhr
      361 rsgenislsa
//
LOCUS       WP_176082681             157 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Martelella sp. HB161492].
ACCESSION   WP_176082681
VERSION     WP_176082681.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 157)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140352
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..157
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016818 - hydrolase activity, acting on
                     acid anhydrides, in phosphorus-containing anhydrides
                     [Evidence IEA]"
                     /calculated_mol_wt=17444
     Region          21..149
                     /region_name="NUDIX_DIPP2_like_Nudt4"
                     /note="diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase
                     type 2 and similar proteins; cd04666"
                     /db_xref="CDD:467551"
ORIGIN      
        1 mfsliwnnyl apllgrparv qiaalcfrle kagpevllit srttrrwiip kgwplygtdg
       61 ggtalqeawe eagvkprgga pvrigsyryk kivdgglpvp tivdvyaiev eklldnfpem
      121 dqrkrqwmkp eaaakavdee qlkailmdls gllekar
//
LOCUS       WP_176082684             284 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Martelella sp. HB161492].
ACCESSION   WP_176082684
VERSION     WP_176082684.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..284
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30120
     Region          8..156
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
     Region          163..282
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 mdkltafidg siyaesvcdh aawmagriga pielvhilek pvanqapvnl agtiglgart
       61 alleeladld arnartaqkr grlllesate rlalggvadv ttklrngdfv eaveetctds
      121 rvivigkrge gadfasghlg snleravrsa kcpvfvaars fkpihkvlia ydggpsaeka
      181 iervatsdil egctctlvsv cedgdalakk akqaihrleh skveasliir sghaekvied
      241 iaaeektdll vmgayghsri rslmigsttt avlrachipv lllr
//
LOCUS       WP_176082698              69 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy-metal-associated domain-containing protein [Martelella sp.
            HB161492].
ACCESSION   WP_176082698
VERSION     WP_176082698.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Rosen,B.P.
  TITLE     Transport and detoxification systems for transition metals, heavy
            metals and metalloids in eukaryotic and prokaryotic microbes
  JOURNAL   Comp Biochem Physiol A Mol Integr Physiol 133 (3), 689-693 (2002)
   PUBMED   12443926
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Gitschier,J., Moffat,B., Reilly,D., Wood,W.I. and Fairbrother,W.J.
  TITLE     Solution structure of the fourth metal-binding domain from the
            Menkes copper-transporting ATPase
  JOURNAL   Nat Struct Biol 5 (1), 47-54 (1998)
   PUBMED   9437429
REFERENCE   3  (residues 1 to 69)
  AUTHORS   Silver,S. and Phung,L.T.
  TITLE     Bacterial heavy metal resistance: new surprises
  JOURNAL   Annu Rev Microbiol 50, 753-789 (1996)
   PUBMED   8905098
REFERENCE   4  (residues 1 to 69)
  AUTHORS   Bull,P.C. and Cox,D.W.
  TITLE     Wilson disease and Menkes disease: new handles on heavy-metal
            transport
  JOURNAL   Trends Genet 10 (7), 246-252 (1994)
   PUBMED   8091505
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006509
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..69
                     /product="heavy-metal-associated domain-containing
                     protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=6995
     Region          2..69
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
ORIGIN      
        1 mtekmtlsid gmgcskcvek vekalnaidg isgvsvnleg ksasfelasp asrdqaveav
       61 edsgydvvg
//
LOCUS       WP_176082712             212 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Martelella sp.
            HB161492].
ACCESSION   WP_176082712
VERSION     WP_176082712.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..212
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22914
     Region          7..192
                     /region_name="YbjK"
                     /note="DNA-binding transcriptional regulator YbjK
                     [Transcription]; COG3226"
                     /db_xref="CDD:442459"
ORIGIN      
        1 mnrkpfrrat daerrddliv atldciaegg lasatvrqva eragvsggli rhyfaskdll
       61 lqaayrrimg rmtaiacdaa dvgetpadrl rafivaslsp pmidarmlgl waafiaqvrv
      121 dpameaihre ayvefrsaie iiladafaaa grpvgaaecr rlatrinavl dglwlegcla
      181 hslfndeelk eagiesveai tgiglkqdhv re
//
LOCUS       WP_176082738             370 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176082738
VERSION     WP_176082738.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..370
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38452
     Region          19..367
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mspasaapvd lvrershsag arvdvsgvak hfgdnavlks inlsvapgev vallgpsgsg
       61 kttllrllag lmapsdgria igdmvvadga tgklvppekr sigmvfqdya lwphmsvagn
      121 vafplevqhv nraerkarva ealdlvalgp fagrspatls ggqqqrvala ravvsqpsli
      181 lfdeplsnld relreqlvvd iaalvrslgm tgvyvthdha eafaiadrva vmadgyilqi
      241 aapemlvrqp asaevasflk lglliparkg aagivvereg tvlqppagfg gadgkghlfv
      301 praalemrga gqaslsgrvv hsmfrgdgya lrlkldcgid adlasaepla dgaavslsfa
      361 wetarwfgdn
//
LOCUS       WP_176082748             315 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Martelella sp.
            HB161492].
ACCESSION   WP_176082748
VERSION     WP_176082748.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..315
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=33908
     Region          1..>28
                     /region_name="DUF945"
                     /note="Bacterial protein of unknown function (DUF945);
                     cl19471"
                     /db_xref="CDD:473173"
     Region          23..306
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mkkslpilav gvvvalapvl gassyilgvg vlvfaylvsa mslniiygll gllslahvaf
       61 wgiggyvavi avvdhgvsfw lavplaglaa gilsilvgyp alrlnrhsfv vvtlsltlla
      121 tlvsrdwmgv trgpmgipgl papnffgisl dgplgfyyls fafaavslgl myifftsrla
      181 gtmraicqse elarsqginp tpykllgffl safftamagg iyafhmrvid plifdfyfmq
      241 afliivivgg rgsftgvlis gaimailpev lrfsvdlrmi lygvillvfv lklpeglagf
      301 vrrrreekmr lelrq
//
LOCUS       WP_176082743             273 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Martelella sp. HB161492].
ACCESSION   WP_176082743
VERSION     WP_176082743.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..273
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29775
     Region          20..265
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mgeqgitdlp ksttdldanq slskalqiik mlsategdig vrelgrrlsi ppsvvhrlla
       61 tlknhdfveq dprtmryrvg fglygagqsy lmqrtladaa leelqqlsik fqmsaylgvl
      121 hdteivyfls lpgapmsvnp qpgrtvpiht talgkvilag mdsdeleacv rrldfrrhtd
      181 ktvtdighfl kevencriag yatcleenld gifavgvpvh dergdvvaai slgnsdgpef
      241 hrllepiiae lhkaagrise klgrpvrvra gkg
//
LOCUS       WP_176082778             220 aa            linear   BCT 11-JAN-2025
DEFINITION  cysteine hydrolase family protein [Martelella sp. HB161492].
ACCESSION   WP_176082778
VERSION     WP_176082778.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..220
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23315
     Region          19..206
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 maiikarpfd fdlksenaal ividmqrdfi epggfgetlg nevallqaii patarliagf
       61 raagltviht rechrpdlsd cppakrargn pklrigdpga mgriliagep gadiiaelyp
      121 vageivldkp gkgafyatpl adilqergit hlvfagvtte vcvqttmrea ndrgyeclla
      181 vdatesyfpa fkaaaiemit aqgaivgwaa etdqiveala
//
LOCUS       WP_176082797             293 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Martelella sp. HB161492].
ACCESSION   WP_176082797
VERSION     WP_176082797.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11171394
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..293
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31087
     Region          76..267
                     /region_name="Abhydrolase_3"
                     /note="alpha/beta hydrolase fold; pfam07859"
                     /db_xref="CDD:400284"
ORIGIN      
        1 mdyraildqd vvafidktls fysadlaadd wqgqraaydr maahfhagrp aglavsdgri
       61 advpvriyge etatvivyvh gggfvlggld shddvcaeia aatqrrvvsv dyrlspehrh
      121 paayddllav vkslvetcdv vlcgdsagas lcaclcgcwh dariigqfli ypalgfapeg
      181 gsferhahap llsrdeveay gavrggerdd pratasagdl arlpptfifp aecdplhdda
      241 lryaeaaakc gtditvetsa glvhgwlrar hestraartf agiagkiaaf cag
//
LOCUS       WP_176082807             118 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Martelella sp. HB161492].
ACCESSION   WP_176082807
VERSION     WP_176082807.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007407
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..118
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12642
     Region          9..115
                     /region_name="COG3450"
                     /note="Predicted enzyme of the cupin superfamily [General
                     function prediction only]"
                     /db_xref="CDD:442673"
ORIGIN      
        1 mtsleafaal ddvalgpfqp kpttltagqe easamlwssp dgstrigvwe ctpgrftadr
       61 tkageychii sgsasvkntd gsgerrlaag dllvlpqgwt geweihehvr klfiiear
//
LOCUS       WP_176082805             297 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176082805
VERSION     WP_176082805.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 297)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 297)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 297)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..297
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32656
     Region          22..295
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 maaslanqtn aaglkhderi eklrlfglsa pallivfvvl vipvgwlfyl sfigadgsfs
       61 lenyarmisr ssyrrifemt fevsvfttal tiligypmay flaqlpnrla sifmiavllp
      121 fwtsllvrty awlvllqkqg linqwaislg lwdepikmvh dmngtligmv himlpflilp
      181 tfgamkaidr dlmkaasnlg asprhafwtv ffpltipglf agalmvfilc lgfyvtpavl
      241 gggkvimvsm kivsniemfv nwgaasalgv vllvmtmiil wiaskflnld qiagggh
//
LOCUS       WP_176082808             538 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Martelella sp. HB161492].
ACCESSION   WP_176082808
VERSION     WP_176082808.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..538
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58306
     Region          1..538
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 maefdfivtg agsagsvlan rlsedgrysv llleaggsdr sfwlmmpigy gkafydkryn
       61 wmymtepdeg lggrpsywpr gkalggssai namifvrghr sdfdgwaamg npgwgfddvl
      121 pyfkklesnd rgandmrggd gpltieskdk dihptcgnfi rasteagfae nddfngssle
      181 gvgiyqittk ggmrmstara ylrpalkrrn lkvethalae kilfdgtrav gvryrqngav
      241 heararrevi vsagainspl llqhsgigpa allqrhgipv vtardgvgrh lqdhlcidym
      301 ftsrvptlnd qlsplsgrlr fglqylltrs gplslginha ggfvrsrpal dapnmqlffs
      361 pmsyskappg erplmkpdpf sgfllgaqpt rptsrghlei rsadpaaapl ihpnylstef
      421 dqqemiaasr lvrrlaeaps laaiisseve pgpdvrsdea lledarrrsg tvfhpvstcr
      481 mgpdpvtdvv daslrvygte alrvvdasif ptltcgntna ptimvaekaa dlvlagqr
//
LOCUS       WP_176083018             169 aa            linear   BCT 11-JAN-2025
DEFINITION  peptidylprolyl isomerase [Martelella sp. HB161492].
ACCESSION   WP_176083018
VERSION     WP_176083018.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Wang,P. and Heitman,J.
  TITLE     The cyclophilins
  JOURNAL   Genome Biol 6 (7), 226 (2005)
   PUBMED   15998457
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Stamnes,M.A., Rutherford,S.L. and Zuker,C.S.
  TITLE     Cyclophilins: a new family of proteins involved in intracellular
            folding
  JOURNAL   Trends Cell Biol 2 (9), 272-276 (1992)
   PUBMED   14731520
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002023
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..169
                     /product="peptidylprolyl isomerase"
                     /EC_number="5.2.1.8"
                     /GO_function="GO:0003755 - peptidyl-prolyl cis-trans
                     isomerase activity [Evidence IEA]"
                     /GO_process="GO:0000413 - protein peptidyl-prolyl
                     isomerization [Evidence IEA]"
                     /calculated_mol_wt=18470
     Region          6..168
                     /region_name="PpiB"
                     /note="Peptidyl-prolyl cis-trans isomerase (rotamase) -
                     cyclophilin family [Posttranslational modification,
                     protein turnover, chaperones]; COG0652"
                     /db_xref="CDD:440417"
ORIGIN      
        1 maetrdpent limetskgki vietlpgvap lhvarvkelt regaydgvvf hrvisdfmaq
       61 ggdvqfgnke sssyhpgrag mggsdkpdla aefsaerhvr gtcsmarsqs pnsansqffi
      121 cftdapwldk qytvwgkvve gmdivdkfer gepvrnpdhi isvkveadl
//
LOCUS       WP_176083024             239 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176083024
VERSION     WP_176083024.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..239
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25773
     Region          4..226
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 mstaaliefr nvyksygmde atvsalngvs fsieagefva imgpsgsgks tamnilgwld
       61 apssgqymfq gvstadlpss kltllrryll gfvfqgfnll prtsalenve lplvyrgigr
      121 rerrqmaeaa lenvglgdrm hhftqqlsgg qqqrvaiara ivtdpavlla deptgnldtr
      181 tsseimdlis dlnrsrgitv imvthdhaia shaarrirfl dghlvsgpgs raeegehvs
//
LOCUS       WP_176083080             202 aa            linear   BCT 11-JAN-2025
DEFINITION  LysE family translocator [Martelella sp. HB161492].
ACCESSION   WP_176083080
VERSION     WP_176083080.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Kutukova,E.A., Livshits,V.A., Altman,I.P., Ptitsyn,L.R.,
            Zyiatdinov,M.H., Tokmakova,I.L. and Zakataeva,N.P.
  TITLE     The yeaS (leuE) gene of Escherichia coli encodes an exporter of
            leucine, and the Lrp protein regulates its expression
  JOURNAL   FEBS Lett 579 (21), 4629-4634 (2005)
   PUBMED   16098526
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Nandineni,M.R. and Gowrishankar,J.
  TITLE     Evidence for an arginine exporter encoded by yggA (argO) that is
            regulated by the LysR-type transcriptional regulator ArgP in
            Escherichia coli
  JOURNAL   J Bacteriol 186 (11), 3539-3546 (2004)
   PUBMED   15150242
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Vrljic,M., Garg,J., Bellmann,A., Wachi,S., Freudl,R., Malecki,M.J.,
            Sahm,H., Kozina,V.J., Eggeling,L., Saier,M.H. Jr., Eggeling,L. and
            Saier,M.H. Jr.
  TITLE     The LysE superfamily: topology of the lysine exporter LysE of
            Corynebacterium glutamicum, a paradyme for a novel superfamily of
            transmembrane solute translocators
  JOURNAL   J Mol Microbiol Biotechnol 1 (2), 327-336 (1999)
   PUBMED   10943564
REFERENCE   4  (residues 1 to 202)
  AUTHORS   Zakataeva,N.P., Aleshin,V.V., Tokmakova,I.L., Troshin,P.V. and
            Livshits,V.A.
  TITLE     The novel transmembrane Escherichia coli proteins involved in the
            amino acid efflux
  JOURNAL   FEBS Lett 452 (3), 228-232 (1999)
   PUBMED   10386596
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003423
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..202
                     /product="LysE family translocator"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /calculated_mol_wt=21696
     Region          1..196
                     /region_name="RhtB"
                     /note="Threonine/homoserine/homoserine lactone efflux
                     protein [Amino acid transport and metabolism]; COG1280"
                     /db_xref="CDD:440891"
ORIGIN      
        1 mlsaflhlal ihllmamlpg pntvavsyfa atrsrsagfr aaagvaaasf iwlalslagv
       61 gtfllqagif yrllriagaa yliyiairmi larrastpae pprggapfrs gfmttlsnpk
      121 savfwtsvfa lvlpatappg fylavivwit lqafawyglv alflstplir rlysraglwl
      181 griaggfmll fglkildear rt
//
LOCUS       WP_176083077             145 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Martelella sp. HB161492].
ACCESSION   WP_176083077
VERSION     WP_176083077.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..145
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=15692
     Region          7..129
                     /region_name="COG3607"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]"
                     /db_xref="CDD:442825"
ORIGIN      
        1 mtkfdrrmtm itlgvadler stafyerlgw arsvasqegv tfialdgivl slfgrkalae
       61 daglkddiag gfpgfslayn vdseaavdea vqfacacgak pvkpprkvfw ggysgyvadp
      121 dgflweiafn pfmplddkgh mileq
//
LOCUS       WP_176083087             251 aa            linear   BCT 11-JAN-2025
DEFINITION  metal ABC transporter ATP-binding protein [Martelella sp.
            HB161492].
ACCESSION   WP_176083087
VERSION     WP_176083087.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 251)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438190
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..251
                     /product="metal ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27265
     Region          1..240
                     /region_name="ZnuC"
                     /note="ABC-type Mn2+/Zn2+ transport system, ATPase
                     component [Inorganic ion transport and metabolism];
                     COG1121"
                     /db_xref="CDD:440738"
ORIGIN      
        1 mkpaaicfdn vtlaydrhpa vhhltgrfep gsltaiagpn gagkstlika lmgeiapaag
       61 ridrgglmvr dlgylpqaae idrhfplsva dtvmlgawrk igafggmtre tarqaeeala
      121 avglegferr pisalsagqf qrvlfarlll qdarvvvlde pftaidartt rdlldivmrw
      181 hgegrtviav lhdfdqvrah fpqtlllare miawgeteta lssrnlfnar alaeafdeaa
      241 elcqrdavna r
//
LOCUS       WP_176083171             276 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176083171
VERSION     WP_176083171.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 276)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 276)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 276)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..276
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29438
     Region          3..245
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mpllilpata lvimllvvpm agllrislnh ysptelmvea vtgenylnai tdpfyqkill
       61 vtvavavsct alslllsiap aywlarmqsr wksaliiltl fpllvgnvvr aagwmailst
      121 dgalnaflgl fgfgpyklly qpaavvfgta avvmpymilt lsavieaipr qteeaatnlg
      181 appltvlrri llpqaapgvv agcvlvfims mnayatpvll ggpnftmlap avydqfvrvg
      241 nwpfgaalaf llllstlvlt vlvnfalvra lkrksl
//
LOCUS       WP_176083196             541 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Martelella sp. HB161492].
ACCESSION   WP_176083196
VERSION     WP_176083196.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..541
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57272
     Region          15..453
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(22..23,26..27,30,62,113..114,116..118,121,141,
                     144..145,148,287,290..291,294..296,299,327,331,384..385,
                     389,393,409,412..413,416..417,420)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mslkstlkwq gliilllaqf gtmadnagvs vsatslalal haqmsqiava namypliags
       61 fmvsigtlgl flgwtrtfqi gvallilael iaattheiai fnfgarslag fgasflipsv
      121 lglvsvlysg rdrvvafgai gavvgianii apmifgfiid afsyrvafls lcgffvllla
      181 aslllpaeth kedlktydrg gavlvslgll lfsgglmqts swglihpina pitlfgispc
      241 lplilagllv ligfwrfevs raangraclv pvsffatpqi ragvymcafm ffvlgaftil
      301 gipylqmvag ysafetslil vffpvgmvls slgtpvlfsh lssqmicrlg mvlsalacli
      361 gafgitrdgi gllyfpstfl iglgtglias qasiivteav dqklasqsga vqaaarnigq
      421 aigvaliawl lmfsltddfk sdarlnqnis asvlndvsev aaiplmsned fgnamtrlkv
      481 pdndrqtffs inrdarydaa hmswlvlall ilisiplltr svpkhslmqd kqtseggtsa
      541 i
//
LOCUS       WP_176083275             276 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176083275
VERSION     WP_176083275.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 276)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438366
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..276
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30248
     Region          16..258
                     /region_name="MlaF"
                     /note="ATPase subunit MlaF of the ABC-type intermembrane
                     phospholipid transporter Mla [Cell wall/membrane/envelope
                     biogenesis]; COG1127"
                     /db_xref="CDD:440744"
ORIGIN      
        1 mraqldqkqd giseetreti ltvrgltvgf gnasnvlenl dldvyrgeil gfvggsgtgk
       61 svlmrtilrl nrrkagsiki fggdfdeigl derlaiemri gvlfqqgalf sgltvleniq
      121 vpmreyldlp kslmddlarl kiemvglrpe aasrypsels ggmikraala ralaldpdlv
      181 fldeptsgld pigaaefdel iarlrdtlgl tvymvthdld sisavcdria vlgkkrvlve
      241 gtldtmlhyd dpwvksyfrg krsraifqna asgqns
//
LOCUS       WP_176083287             151 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Martelella sp.
            HB161492].
ACCESSION   WP_176083287
VERSION     WP_176083287.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..151
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=16737
     Region          1..136
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mdrtdrkiin llgadarrsl adigtavgls qsavnerirr lqatgvirrf tvevshrald
       61 esvlvfiqll laadadeeaf rramarhcdv lechhvsgrw syllklrfav lgdveaflge
      121 lkragyiaas etiitlstvr ersfrddgdp s
//
LOCUS       WP_176083318             203 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Martelella sp. HB161492].
ACCESSION   WP_176083318
VERSION     WP_176083318.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..203
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=22052
     Region          10..183
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mfyqtdtndh glphdpfkai vsprpiawvg trdlqgranl gpysffnava dqpklvmfss
       61 sgmkhshdni aatgvftlsl vgrdlaeamn mtsaplktgm sefdfaglta vdgrlvdapf
      121 vgeayaalec rlteiitpkt lddqptpnri ifgqvvaihi reegltdgll dmakvrplar
      181 mgyldycdgg etfqmrrptv tgd
//
LOCUS       WP_176083338             237 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176083338
VERSION     WP_176083338.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 237)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..237
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=25394
     Region          4..229
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msgetvlsve natrhyrsgd svvkaldgvs lsvrrgelvg ivgpsgsgks tflmiaglla
       61 tpssgavwla gervnapdvd lgrlrdfrrr higfvfqkan lipfltaaen iaialeiddv
      121 pagpaleyah yllealdlgh rsgnkpsrls ggeqqrvaia ralanepsli ladeptaald
      181 gtrgrqamal frdiavkrdt avvvvthdpr afdlfdrilt fedgrivsek qrdtrsa
//
LOCUS       WP_176083332             273 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfite exporter TauE/SafE family protein [Martelella sp.
            HB161492].
ACCESSION   WP_176083332
VERSION     WP_176083332.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Shlykov,M.A., Zheng,W.H., Chen,J.S. and Saier,M.H. Jr.
  TITLE     Bioinformatic characterization of the 4-Toluene Sulfonate Uptake
            Permease (TSUP) family of transmembrane proteins
  JOURNAL   Biochim Biophys Acta 1818 (3), 703-717 (2012)
   PUBMED   22192777
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..273
                     /product="sulfite exporter TauE/SafE family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=28896
     Region          8..273
                     /region_name="TauE"
                     /note="Sulfite exporter TauE/SafE/YfcA and related
                     permeases, UPF0721 family [Inorganic ion transport and
                     metabolism]; COG0730"
                     /db_xref="CDD:440494"
ORIGIN      
        1 mppvsdiiel vvlllvaggv agllaglfgi gggavlvpvf yqafamagvd esvrmqlcvg
       61 tslaiiipts lrsfqahykr gsvdmsllrr wviavpvgal mstlvlayap pavvksafav
      121 itlliaakml frrlaelklg edlprppaly gfgwaigmls gligigggtl nntfmtfynr
      181 pmlqavatss gvgvliavps ffgnvyggwg reglpifstg fvnwiavili ipitmyvapi
      241 gaklahrlsk rqleisfgif lliisarffi tli
//
LOCUS       WP_176083324             162 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Martelella sp.
            HB161492].
ACCESSION   WP_176083324
VERSION     WP_176083324.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 162)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..162
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18442
     Region          1..138
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mdrldrkilr llqedttlav adigkkvgls ttpcwrriqk meeegvikrr valldpekin
       61 anvtvfvsir tnshsvewlk rfaevisgfp evlefyrmsg dvdyllrvvv pdiaaydafy
      121 krliakieir dvsssfameq ikfstelpld ymvlepskgs ge
//
LOCUS       WP_176083358             208 aa            linear   BCT 11-JAN-2025
DEFINITION  DedA family protein [Martelella sp. HB161492].
ACCESSION   WP_176083358
VERSION     WP_176083358.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..208
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=23218
     Region          7..203
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 msitaelsty imstidsagy wavgilmale saclpipsev vmpfagylas ighmnlilaa
       61 tigaigcnvg stlaylagyy ggrpfierwg ryilinhaei ekvvrffdry gaaavfiarl
      121 lpivrsfisl pagiskmpqw kfqlysflgs wpwcfvlafi gfhlgkawqn spwlrdtmhs
      181 fhlaiavmia fsilfylfhk frksqddi
//
LOCUS       WP_176083455             280 aa            linear   BCT 11-JAN-2025
DEFINITION  universal stress protein [Martelella sp. HB161492].
ACCESSION   WP_176083455
VERSION     WP_176083455.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Tkaczuk,K.L., A Shumilin,I., Chruszcz,M., Evdokimova,E.,
            Savchenko,A. and Minor,W.
  TITLE     Structural and functional insight into the universal stress protein
            family
  JOURNAL   Evol Appl 6 (3), 434-449 (2013)
   PUBMED   23745136
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Kvint,K., Nachin,L., Diez,A. and Nystrom,T.
  TITLE     The bacterial universal stress protein: function and regulation
  JOURNAL   Curr Opin Microbiol 6 (2), 140-145 (2003)
   PUBMED   12732303
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Freestone,P., Nystrom,T., Trinei,M. and Norris,V.
  TITLE     The universal stress protein, UspA, of Escherichia coli is
            phosphorylated in response to stasis
  JOURNAL   J Mol Biol 274 (3), 318-324 (1997)
   PUBMED   9405142
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001747
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..280
                     /product="universal stress protein"
                     /GO_function="GO:0042802 - identical protein binding
                     [Evidence IEA]"
                     /calculated_mol_wt=30113
     Region          154..278
                     /region_name="UspA"
                     /note="Nucleotide-binding universal stress protein, UspA
                     family [Signal transduction mechanisms]; COG0589"
                     /db_xref="CDD:440354"
ORIGIN      
        1 msyktilsvm ettsqsagfl dhtmhlahlf eahviglhae svtatpivap meipdpvsiq
       61 alqdaaekrs ealgalfeer arkeaisyew rkiitsvgya gasvidsarc sdliiapqas
      121 pdvsadakad fesflfesgr pvlliphtak sampfkkvlv awngsreaar atfdalpflk
      181 raeeveifsv nppdtttvss emtggeiatt larhginvta vnahadkara atlienrmsd
      241 ssvdllvmga ythsrlwqll fggvtrtlle smtaatlmar
//
LOCUS       WP_176083301             479 aa            linear   BCT 11-JAN-2025
DEFINITION  DEAD/DEAH box helicase [Martelella sp. HB161492].
ACCESSION   WP_176083301
VERSION     WP_176083301.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Gustafson,E.A. and Wessel,G.M.
  TITLE     DEAD-box helicases: posttranslational regulation and function
  JOURNAL   Biochem Biophys Res Commun 395 (1), 1-6 (2010)
   PUBMED   20206133
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11423521
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..479
                     /product="DEAD/DEAH box helicase"
                     /EC_number="3.6.4.-"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /calculated_mol_wt=52482
     Region          1..432
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
ORIGIN      
        1 mtsfselgls pkvlsavada gytdptpiqa gaipvalerr dvcgiaqtgt gktasfvlpm
       61 ltllergrar armprtlile ptrelaaqva enfdkygknh klnvalligg vsfdeqdrkl
      121 ergadvlict pgrlldhaer gkllmtgvei lvideadrml dmgfipdier iakmipftrq
      181 tlffsatmpp eiqgladrfl qnptrievap psstaatveq kvvasgvkdf ekrstlrsli
      241 dtqeelknai ifcnrkksva dllrslqrhg ysagalhgdm dqhsrtailq nfrdgklpll
      301 vasdvaargl dipdvshvfn fdvpihaedy vhrigrtgra grkgsaftiv trkdvkplda
      361 ieklidrkid wldgdlstlg aeedeapkpr trrgknadkp akapvndeak askaepaakk
      421 adaeekvvtr qkssetrnsk araanddrnr srrrdrddep tpvgfgddip afmligska
//
LOCUS       WP_176083496             170 aa            linear   BCT 11-JAN-2025
DEFINITION  DinB family protein [Martelella sp. HB161492].
ACCESSION   WP_176083496
VERSION     WP_176083496.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Cooper,D.R., Grelewska,K., Kim,C.Y., Joachimiak,A. and
            Derewenda,Z.S.
  TITLE     The structure of DinB from Geobacillus stearothermophilus: a
            representative of a unique four-helix-bundle superfamily
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 3), 219-224
            (2010)
   PUBMED   20208147
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006340
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..170
                     /product="DinB family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19393
     Region          8..151
                     /region_name="DinB"
                     /note="Bacillithiol/mycothiol S-transferase BstA/DinB,
                     DinB/YfiT family (unrelated to E. coli DinB) [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG2318"
                     /db_xref="CDD:441892"
ORIGIN      
        1 mlphfrmfaa ynnwanslvy ssashlaydd ytrdlgaffh svhgtlnhll ytdriwmkrf
       61 ageytgsvkl nsiisddfed lrlareaedq aiiayidsls edqlagrfsy lrgnppeqhn
      121 dslskalahl fnhqthhrgq ihmmlttlgr pslemdliyf lrsaagrpfa
//
LOCUS       WP_176083523             385 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176083523
VERSION     WP_176083523.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 385)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..385
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41707
     Region          1..365
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 msnvkladin knygsfhalk ninldiapge fvvmvgpsgc gkstllktia gledvasgli
       61 eiagkdvthe epgdrgiamv fqsyalyphm tvrdnmgfgl rimkrpaaei eaavgkaaki
      121 lrienlldkk paqlsggqrq rvaigraitr qphvflfdep lsnldaalrt qmrvelaslh
      181 kaldatmiyv thdqveamtm adrivvlhag eieqvgaplq lynnpcnrfv asflgsprmn
      241 ffegrvetvt satarvhlag lgsvtfnnis ekhglktgeq itvgvrpehf ilasdmpvma
      301 rgrlrlseel gretvlyvaa galkaigsdt gtsdvtlltn lpvaleddmi dfgfspeday
      361 lfgpdgktit iekplrheha rrakg
//
LOCUS       WP_176083460             436 aa            linear   BCT 11-JAN-2025
DEFINITION  replication-associated recombination protein A [Martelella sp.
            HB161492].
ACCESSION   WP_176083460
VERSION     WP_176083460.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Page,A.N., George,N.P., Marceau,A.H., Cox,M.M. and Keck,J.L.
  TITLE     Structure and biochemical activities of Escherichia coli MgsA
  JOURNAL   J Biol Chem 286 (14), 12075-12085 (2011)
   PUBMED   21297161
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Barre,F.X., Soballe,B., Michel,B., Aroyo,M., Robertson,M. and
            Sherratt,D.
  TITLE     Circles: the replication-recombination-chromosome segregation
            connection
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8189-8195 (2001)
   PUBMED   11459952
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..436
                     /product="replication-associated recombination protein A"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006260 - DNA replication [Evidence IEA]"
                     /calculated_mol_wt=48186
     Region          1..436
                     /region_name="RarA"
                     /note="Replication-associated recombination protein RarA
                     (DNA-dependent ATPase) [Replication, recombination and
                     repair]; COG2256"
                     /db_xref="CDD:441857"
ORIGIN      
        1 msdlfapkip eelekrrpla drlrpqhlne vtgqdhltgp dgaltrmias gslgsmifwg
       61 ppgtgkttva rllsgeadla feqisaifsg vadlkkvfea ararrmngrq tllfvdeihr
      121 fnraqqdsfl pvmedgtivl vgattenpsf elnaallsra rvltfrahdh dslselltra
      181 eaaegralpl dedaretlig madgdgrail tlseeiwraa regevldpkg lagvvqrrap
      241 iydkgqdghy nlisalhksv rgsdpdaaly ylarmidage dplyigrrlv rmatedigla
      301 dpqavliata akdaydflgs pegelalaea ciylatapks nsvevawhaa laaakrhgsl
      361 mppkhilnap trlmkeegyn qgyrydhdep dafsgqnyfp temgrqkfyq ppergferei
      421 nkrlawwdkl rrerns
//
LOCUS       WP_176083625             119 aa            linear   BCT 11-JAN-2025
DEFINITION  GFA family protein [Martelella sp. HB161492].
ACCESSION   WP_176083625
VERSION     WP_176083625.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..119
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=12565
     Region          4..>106
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mstkhyhgsc qcgavdfdvd idlgftavcn csrcrrlgsv laftspsaft lnsgadvltd
       61 ylfnkrtirh qfcsvcgiea fafgkvpgdg semvavnvnc ldgvdarslp skpydgasl
//
LOCUS       WP_176083524             718 aa            linear   BCT 11-JAN-2025
DEFINITION  beta-galactosidase [Martelella sp. HB161492].
ACCESSION   WP_176083524
VERSION     WP_176083524.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Coines,J., Raich,L. and Rovira,C.
  TITLE     Modeling catalytic reaction mechanisms in glycoside hydrolases
  JOURNAL   Curr Opin Chem Biol 53, 183-191 (2019)
   PUBMED   31731209
REFERENCE   2  (residues 1 to 718)
  AUTHORS   Naumoff,D.G.
  TITLE     Hierarchical classification of glycoside hydrolases
  JOURNAL   Biochemistry (Mosc) 76 (6), 622-635 (2011)
   PUBMED   21639842
REFERENCE   3  (residues 1 to 718)
  AUTHORS   Vuong,T.V. and Wilson,D.B.
  TITLE     Glycoside hydrolases: catalytic base/nucleophile diversity
  JOURNAL   Biotechnol Bioeng 107 (2), 195-205 (2010)
   PUBMED   20552664
REFERENCE   4  (residues 1 to 718)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   5  (residues 1 to 718)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449001
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..718
                     /product="beta-galactosidase"
                     /EC_number="3.2.1.23"
                     /GO_component="GO:0009341 - beta-galactosidase complex
                     [Evidence IEA]"
                     /GO_function="GO:0004565 - beta-galactosidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006012 - galactose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=80549
     Region          19..664
                     /region_name="GanA"
                     /note="Beta-galactosidase GanA [Carbohydrate transport and
                     metabolism]; COG1874"
                     /db_xref="CDD:441478"
     Region          657..713
                     /region_name="Glyco_hydro_42C"
                     /note="Beta-galactosidase C-terminal domain; pfam08533"
                     /db_xref="CDD:400716"
ORIGIN      
        1 mkktaksapl svwrpvnidq filgvphype hvsrdlwend akrmaeagfn tvrmgefawh
       61 iwepyqghfd fslfddaiav lgrygiktil ctptatpprw ltvahpevlr adeqgrraih
      121 gsrqhadtts pvlrdhsrri tramaehyqd dpnvigwqtd nelntttsis fsescaiefr
      181 kwchlrygdi aalntawggd fwathydsfe qielplpmap gyvspghrqd yhrflaaata
      241 afqkdqieil rsiktgwfiy hnlghlddid lrgnfgedld flgydvypml hdemqrnggh
      301 aytqalaldw frafggnfiv peqasglgsq ptfatmtpep gemrrmalts vargadglmf
      361 frwrpahfga eiywmglidh dneprrrfae akhfaediea iktellgthv rmdvgiaaad
      421 fdnqesykty pmglpspred gillhkvlye rniaagfihp sddlsklkal yvphfmmwnd
      481 awtenlrrfv enggllivsa mtgtrtvdnh iheklapgng lsellgikve efgrmtgpga
      541 dglfeppgra dgfgpaatgr vpacsagrry nlrfgnkeyq aghlyerlml eddvetlaew
      601 strflagepv ltarklgqgq asylgtylte alaerladti cevadvapil svetpeveis
      661 ersgddgrkm ifvintgsek vkieldgtys drltdrhirg tlelegygaa ilspgnel
//
LOCUS       WP_176083639             333 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Martelella sp.
            HB161492].
ACCESSION   WP_176083639
VERSION     WP_176083639.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 333)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..333
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35891
     Region          6..273
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mkttlisals asvfallagq afaadpvtlq lkwvtqaqfa gyyvaldkgy ytdedldvti
       61 kpggpdiape qviagggadv ivdwmaaala arergvplvn iaqpfknsgl lltclketgi
      121 espadfpgkt lgvwfygney pfyawmaklg lgtdggadgv tvlkqgfnvd pliqkqadci
      181 stmtyneygq vldagitpdq ltvfnyrdeg vgmledglyv medklqdpaf edkmarfvra
      241 smkgwkyaee hpdeaaemvi ehddtgaqtl ehqqymmgev akltagsdgs ldvddynetv
      301 htllsavspd npaitkepeg aytlditnka lgk
//
LOCUS       WP_176083647             470 aa            linear   BCT 11-JAN-2025
DEFINITION  S41 family peptidase [Martelella sp. HB161492].
ACCESSION   WP_176083647
VERSION     WP_176083647.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Rawlings,N.D., Barrett,A.J. and Finn,R.
  TITLE     Twenty years of the MEROPS database of proteolytic enzymes, their
            substrates and inhibitors
  JOURNAL   Nucleic Acids Res 44 (D1), D343-D350 (2016)
   PUBMED   26527717
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..470
                     /product="S41 family peptidase"
                     /EC_number="3.4.21.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=50116
     Region          42..377
                     /region_name="CtpA"
                     /note="C-terminal processing protease CtpA/Prc, contains a
                     PDZ domain [Posttranslational modification, protein
                     turnover, chaperones]; COG0793"
                     /db_xref="CDD:440556"
ORIGIN      
        1 mirratllla gvaigasvtg vifsadipar aagddstyke mslfgdvfer vraqyvtppd
       61 eqkmiedain gmlsgldphs symtakesee mrdeskgefg glgievtmed evvkvvapid
      121 dtpaakagvm agdkiieidh qsvrgmslnd avnlmrgevg qpidvtimrd gvdkpidmti
      181 vrgvipmnsv karvengdvg yiristfmne kldenlkdai ekiqsevped klkgyildlr
      241 lnpggflnqa vavsdtfltg gevvstrgrn pqetrrfdag pgdltngkpl ivlinggsas
      301 aseivagalh dlkratlvgt rsfgkgsvqt ivplgnegsl rlttalyytp sgtsiqgtgi
      361 kpdivvqqkl pddikdlvvp egesslrghi qgadetdags gsvayvpqdp kddvqlqfal
      421 dllegkktdp sfpadpnkav qelqskeqqt qaaaetdskt ddtktddkan
//
LOCUS       WP_176083681             747 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 2 protein [Martelella sp. HB161492].
ACCESSION   WP_176083681
VERSION     WP_176083681.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 747)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 747)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 747)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14312057
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..747
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=83180
     Region          9..>546
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
     Region          654..743
                     /region_name="Glyco_hydro2_C5"
                     /note="Glycoside hydrolase family 2 C-terminal domain 5;
                     pfam18565"
                     /db_xref="CDD:436582"
ORIGIN      
        1 mrhitqfndg wvftegfdst wpdalqpgla vrlphtavel pfnyfdetcy qraftyqkvi
       61 pfdpafagri vslvfdaama dsvvylngvp iaahrdgytp fevdltphlk agdnlltvki
      121 dgsenpeipp fgdmidylty agiyrdvwlk vtgkavirni kietpdvlaa hksltavafl
      181 dgiagcanar lraclcdaag triaitnlsv tgdraliemt dlddirlwdi ddpalysltv
      241 tldadgetde isqrfgfrsv alttdgfsln griiklrgln rhqcwphlgy amgrrgqekd
      301 aeilkyelac nvvrtshypq sryfldrcde igllvfeeip gwqhiggegw kqesianvrr
      361 mierdwnhpa ifiwgvrine sgddhgfyse tnrlahalds trptggvrci ensemledvy
      421 tmndfilgde elpgrnqgrv ftrdqqqvtg lrqqvpymit eycghmyptk rfdqeqrqae
      481 hvtrhlqmln avagdakiag stgwcmfdyn thmdfgsgdr icyhgvldmy repkfaafay
      541 asqgrpedav vlkpvtfwar gerniggilp liiltncdyv elafgdgapk riepdrttyp
      601 hlphppvvvd lrsvtpaefg ewgrvwrdgt itgfvdgkaa ktmhmaadpl ptrleiaada
      661 talkagekdc vrvilraldq cgnilpffdd paavslegpg rivgpdliaf kggtaglyve
      721 agdeagtltl svrcrlfddq tvtftln
//
LOCUS       WP_176083695             290 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Martelella sp.
            HB161492].
ACCESSION   WP_176083695
VERSION     WP_176083695.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..290
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=29753
     Region          1..290
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mdalmqflls gitvgavyal valgftiiyn asdvvnfaqg efvmmggmit aftyaaglpl
       61 plaaviaili taaagvalnk laiepargap vvslviitig asifirgaaq lifdkqlhrf
      121 pafsgddpir ilgatllpqs lwviggalfv figlwafftk tltgkavlaa annrqaaqlv
      181 gininwvmtl sfslsagiaa lggvlitpit lvgydvgval alkgfaaaml ggmgnpkgal
      241 vggialglle altagyissq ykeavafivi lavlfvmpqg lfghksterv
//
LOCUS       WP_176083753             540 aa            linear   BCT 11-JAN-2025
DEFINITION  CocE/NonD family hydrolase [Martelella sp. HB161492].
ACCESSION   WP_176083753
VERSION     WP_176083753.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 540)
  AUTHORS   Turner,J.M., Larsen,N.A., Basran,A., Barbas,C.F. 3rd, Bruce,N.C.,
            Wilson,I.A. and Lerner,R.A.
  TITLE     Biochemical characterization and structural analysis of a highly
            proficient cocaine esterase
  JOURNAL   Biochemistry 41 (41), 12297-12307 (2002)
   PUBMED   12369817
REFERENCE   4  (residues 1 to 540)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
REFERENCE   5  (residues 1 to 540)
  AUTHORS   Bresler,M.M., Rosser,S.J., Basran,A. and Bruce,N.C.
  TITLE     Gene cloning and nucleotide sequencing and properties of a cocaine
            esterase from Rhodococcus sp. strain MB1
  JOURNAL   Appl Environ Microbiol 66 (3), 904-908 (2000)
   PUBMED   10698749
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459260
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..540
                     /product="CocE/NonD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=57400
     Region          1..532
                     /region_name="COG2936"
                     /note="Predicted acyl esterase [General function
                     prediction only]"
                     /db_xref="CDD:442179"
ORIGIN      
        1 mldkprptpi epetasltls dgvrlvadiy rpvepgdypv llmrqpygrk iastvtlahp
       61 awyaahgyiv vvqdvrgmgg sqgdfdclrq evrdgaeava wardikgsng riglygfsyq
      121 avtqylalag garvdamapa masfspehdw ayeggalrfg gmtfwarqma llkaahkgdr
      181 aswdmlaalt dpaaiyrall arpdlshlal waensadywd kasparllkd idlaipvlht
      241 ggfadfmltg tlaadaafrk asaatthlii gpwshipwna sageahlpae aarsidrdqi
      301 affdfylkgi gmappalsly dmgtnawrdf aaipagekrs ldltsgglaa thlgngrlge
      361 aekddgfdli vsdpfrpapl vgghlgdpag pvdraahddr sdvatyttaa aenpftlcgp
      421 lsaeitvkta qpvfdlvasl slvspsgvar vittgttrts vsgrpvqidl rsiyqtvakg
      481 dclrlslqia awpafsypge dpadanpmar qpatlailhg gatasrlhlh vmtedhanga
//
LOCUS       WP_176083726             240 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Martelella sp. HB161492].
ACCESSION   WP_176083726
VERSION     WP_176083726.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..240
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26329
     Region          15..235
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mprgksdskt tarrngaqtd kaksltdqay drlrheiitc klqpgtdlge qelaeklams
       61 ktpvrealar ltleglveaf prrgyritpv tvksvndvft vrkalegvac elaadrltda
      121 eidriealsn atyvpgeept ieafiktnnd fhaaiaegar vprlvtliss yleestrlfy
      181 mgaamrdvnp etstdhaliv aalrrhdsda areaiiqhte ntrrglltal isdsesllvl
//
LOCUS       WP_176083754             271 aa            linear   BCT 11-JAN-2025
DEFINITION  creatininase family protein [Martelella sp. HB161492].
ACCESSION   WP_176083754
VERSION     WP_176083754.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Yoshimoto,T., Tanaka,N., Kanada,N., Inoue,T., Nakajima,Y.,
            Haratake,M., Nakamura,K.T., Xu,Y. and Ito,K.
  TITLE     Crystal structures of creatininase reveal the substrate binding
            site and provide an insight into the catalytic mechanism
  JOURNAL   J Mol Biol 337 (2), 399-416 (2004)
   PUBMED   15003455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..271
                     /product="creatininase family protein"
                     /EC_number="3.5.2.10"
                     /calculated_mol_wt=29740
     Region          7..259
                     /region_name="ArfB"
                     /note="Creatinine amidohydrolase/Fe(II)-dependent FAPy
                     formamide hydrolase (riboflavin and F420 biosynthesis)
                     [Coenzyme transport and metabolism]; COG1402"
                     /db_xref="CDD:441012"
ORIGIN      
        1 mpqkshwwwd hstkdfsemd msefvailpv aaveqhgphl pvrvdsaina giiaraveim
       61 pddlkvlvlp mqavgksveh leypgtltls yetlarlwfe igesvaragc kkiifanshg
      121 gqpqvmeivc relrikcgmf avsswvsaga sqsdlysehe lkhgihgges etstmlhlhp
      181 dlvdmqyadd fqpmsvqmen dnqvltaegr igfgwqtqdl hpsgacgnaa aadaergath
      241 vqrsaeslva lcqevlafpm erltqktmfk g
//
LOCUS       WP_176083771             200 aa            linear   BCT 11-JAN-2025
DEFINITION  superoxide dismutase [Martelella sp. HB161492].
ACCESSION   WP_176083771
VERSION     WP_176083771.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Parker,M.W. and Blake,C.C.
  TITLE     Iron- and manganese-containing superoxide dismutases can be
            distinguished by analysis of their primary structures
  JOURNAL   FEBS Lett 229 (2), 377-382 (1988)
   PUBMED   3345848
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Bannister,J.V., Bannister,W.H. and Rotilio,G.
  TITLE     Aspects of the structure, function, and applications of superoxide
            dismutase
  JOURNAL   CRC Crit Rev Biochem 22 (2), 111-180 (1987)
   PUBMED   3315461
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427369
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..200
                     /product="superoxide dismutase"
                     /EC_number="1.15.1.1"
                     /GO_function="GO:0004784 - superoxide dismutase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22086
     Region          4..191
                     /region_name="SodA"
                     /note="Superoxide dismutase [Inorganic ion transport and
                     metabolism]; COG0605"
                     /db_xref="CDD:440370"
ORIGIN      
        1 mafelpelpy aydalapfms aetlefhhdk hhnayvtagn klaaeaglad lsveeimvka
       61 ygtnqalfnn agqhfnhmhf wkwmkkdggg tklpgalesa iasdlggydk fkadfiaagv
      121 gqfgsgwawl avkdgkveim ktpngenpvv hgakpilgvd vwehsyyidy rnarpkylea
      181 fidslvnwdy vlelyeaatk
//
LOCUS       WP_176083770             495 aa            linear   BCT 11-JAN-2025
DEFINITION  FGGY-family carbohydrate kinase [Martelella sp. HB161492].
ACCESSION   WP_176083770
VERSION     WP_176083770.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Zhang,Y., Zagnitko,O., Rodionova,I., Osterman,A. and Godzik,A.
  TITLE     The FGGY carbohydrate kinase family: insights into the evolution of
            functional specificities
  JOURNAL   PLoS Comput Biol 7 (12), e1002318 (2011)
   PUBMED   22215998
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Hurley,J.H.
  TITLE     The sugar kinase/heat shock protein 70/actin superfamily:
            implications of conserved structure for mechanism
  JOURNAL   Annu Rev Biophys Biomol Struct 25, 137-162 (1996)
   PUBMED   8800467
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Kabsch,W. and Holmes,K.C.
  TITLE     The actin fold
  JOURNAL   FASEB J 9 (2), 167-174 (1995)
   PUBMED   7781919
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10167391
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..495
                     /product="FGGY-family carbohydrate kinase"
                     /EC_number="2.7.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016310 - phosphorylation [Evidence IEA]"
                     /calculated_mol_wt=52518
     Region          3..452
                     /region_name="ASKHA_NBD_FGGY_RrXK-like"
                     /note="nucleotide-binding domain (NBD) of Rhodospirillum
                     rubrum xylulose kinase (RrXK) and similar proteins;
                     cd07804"
                     /db_xref="CDD:466806"
ORIGIN      
        1 mayvigldig ttstigilie lpsrvvgivs rpvtlksphh gwaeedpaew wgnvqaicre
       61 liglehtdpa aigavgvtgm lpavvlldea grvlrpsiqq sdgrsgreva elraerdeaa
      121 fiahagngin qqlvtaklrw iernepdvfs kiatvfgsyd yinwcltgek tveqnwalea
      181 gfvdvaagll dddliswahv apevvprkva sheiigrvta kaaertglap gtpvvggaad
      241 mvasafgagv nqagdvllkf ggavdiltat dlvrpdprlf ldyhlipglf mpngcmstgg
      301 salnwfiatf agreemlake agitvyryld qmaaekpaga egvtilpyll gektpihdan
      361 argvisgltl shdighlwra llesyayalr hhidvlndmg hqttrylvsd ggaqsrvwmq
      421 ivadvlgapv qcltghpgsc lgvawtaamg agladdwsgv tafvgtgdli apeagnravy
      481 dagyatyral yrpsa
//
LOCUS       WP_176083779             648 aa            linear   BCT 11-JAN-2025
DEFINITION  FUSC family protein [Martelella sp. HB161492].
ACCESSION   WP_176083779
VERSION     WP_176083779.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Hu,R.M., Liao,S.T., Huang,C.C., Huang,Y.W. and Yang,T.C.
  TITLE     An inducible fusaric acid tripartite efflux pump contributes to the
            fusaric acid resistance in Stenotrophomonas maltophilia
  JOURNAL   PLoS One 7 (12), e51053 (2012)
   PUBMED   23236431
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12054228
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..648
                     /product="FUSC family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=69548
     Region          47..610
                     /region_name="FUSC"
                     /note="Fusaric acid resistance protein family; pfam04632"
                     /db_xref="CDD:428044"
ORIGIN      
        1 mtsstgetpg hplrflirag fdperfsfaa rtavaavlal faafalgldh pqwaamtvfa
       61 asqptrgqlv eksffrlagt amgafagvcl vafsggnpml lvpglalwig lstltanvlr
      121 gfvsygaila gysasmvall dfahpddvmh lgldrvatia tgivaalvvg limikrqgen
      181 plhgrirlll shvlqdmslr laqevpprtg klpdllaela aiedalgpng agslrshrfa
      241 raarglliae veallwlrsg psriwppava dmlgrasaal krsdgeaear rilaeaaatc
      301 gaetplghvl ggletalray lgpetgspgd lgphrrvilh rdfrgaarag lrslfamllv
      361 ggfwivtgwq sgpfmllgls imltmfstfe nparmmpivf agqflgviga lacrflvwph
      421 avsdfelvam mvpfillgvp isanrrsmpf gfdysmvsll llkpalpltg dfrswlltgl
      481 avvlapafaf ivyrlvfpin narrrtllig amvrelrlia asdtalekrq awrarfyhrq
      541 lrllryseps slavkasvdt glaimglgnl vfrmhewasd dagsprlrra arlglarvar
      601 iesephkaal glrrlsallg nsqpevsrtm aqaadditvw sgtraeag
//
LOCUS       WP_176083816             191 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Martelella sp.
            HB161492].
ACCESSION   WP_176083816
VERSION     WP_176083816.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..191
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21163
     Region          2..151
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mileaaltvf aekgfasari ediaraaglg kgtiylyfsd kqalfmglva elmtplitng
       61 eqllaheeft ardilasvyq tfsvevlatr kadllrlvit emgnfpelaa yyhnnlirpg
      121 ldllgvller akargelrst ivmrapqvif aplvmtvvwn tlfqrfgrfd seaafqffld
      181 slfhpaegae q
//
LOCUS       WP_176083884             202 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Martelella sp.
            HB161492].
ACCESSION   WP_176083884
VERSION     WP_176083884.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11095567
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..202
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22690
     Region          25..71
                     /region_name="TetR_N"
                     /note="Bacterial regulatory proteins, tetR family;
                     pfam00440"
                     /db_xref="CDD:425684"
     Region          82..192
                     /region_name="TetR_C_11"
                     /note="Tetracyclin repressor-like, C-terminal domain;
                     pfam16859"
                     /db_xref="CDD:435608"
ORIGIN      
        1 mpeakkvkkr vsigaarnpd sqdailnaae eillevglsg ftieavarra ragkptiyrw
       61 wpskaallld vyqrqkpedi fadtgntedd lflllrglmd fwhntpggal frsvlaaeqs
      121 dlqsrallre htrnrhqmsa alfhrakarg eledwvdpll aaeiagsfaw grllrdelai
      181 ddetlrrvtr qiieglrrkk pa
//
LOCUS       WP_176083830             185 aa            linear   BCT 11-JAN-2025
DEFINITION  HdeD family acid-resistance protein [Martelella sp. HB161492].
ACCESSION   WP_176083830
VERSION     WP_176083830.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007121
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..185
                     /product="HdeD family acid-resistance protein"
                     /GO_process="GO:0009268 - response to pH [Evidence IEA]"
                     /calculated_mol_wt=20259
     Region          14..182
                     /region_name="HdeD"
                     /note="Acid resistance membrane protein HdeD, DUF308
                     family [General function prediction only]; COG3247"
                     /db_xref="CDD:442478"
ORIGIN      
        1 mvfleeekpe ilpiqkrwgw ilafglillg fsivlianlf vatiasvvff gvmimlagvf
       61 hlvqlmhakv rgqvifwlat gilyilagif viynpimasr lftviigisl avaggfrlyl
      121 gmsfrpikgw gwlvisglvl llsaimiasd fahsslwllg lfvavdflvy gislvvfals
      181 ikptn
//
LOCUS       WP_176083906             271 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176083906
VERSION     WP_176083906.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 271)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..271
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29473
     Region          4..268
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mherrgrefy ilaafftvfv lflygplsai lilsfqgphg gltfplngvs lhwfanlfet
       61 qavgdfggsf rrslmlglmv mvvtvvvslm aglafrrkfv gatvlfyvai aslvvpsiii
      121 slgigvmfqq vgiapawyts afgaqltwal pfgvlimfav fnrfspsyee aardlgataw
      181 qtfryvllpm iapsligval fgftlsydef artlltagty ntlpleimam ttnvttpvly
      241 algtvttvfs fiviglaltl irslnrgrak g
//
LOCUS       WP_176083945             191 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Martelella sp.
            HB161492].
ACCESSION   WP_176083945
VERSION     WP_176083945.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..191
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=20768
     Region          3..153
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 matpstrdli iekadtlfye rgfeatsfad iaasvgisrg nfyhhfktkd eildavidrr
       61 ientsamlda faadastprd giiafihivi tnrtkimafg cpvgtlcael akldhalkpr
      121 aaalftlfgd wltrqfaalg madhagryal hvlawsqgva alaaafhdet firrevddit
      181 awldslpavl a
//
LOCUS       WP_176083949             363 aa            linear   BCT 11-JAN-2025
DEFINITION  COX15/CtaA family protein [Martelella sp. HB161492].
ACCESSION   WP_176083949
VERSION     WP_176083949.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495902
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..363
                     /product="COX15/CtaA family protein"
                     /EC_number="1.17.99.9"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006783 - heme biosynthetic process
                     [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=40119
     Region          22..349
                     /region_name="COX15-CtaA"
                     /note="Cytochrome oxidase assembly protein; pfam02628"
                     /db_xref="CDD:460629"
ORIGIN      
        1 mvaatamkpg dererrnaal vrywlylvvl tlfclvlvgg atrlthsgls itqwkpihgv
       61 ipplslkdwq eefalyqqip eyqllnkgmt lagfkalfww ewahrllars igliffvplv
      121 yfwlsgrlak slrlplfgvf llggfqgfig wwmvssglsv rtdvsqyrla ihlvtaclif
      181 tacvyiaagl kprkvqpspa fgsgsfaall vlavlvqiyl galvagldag fsyntwplmd
      241 galvpdgllv qhpaylnffe npktvqfihr iggytvfila llhmiaewrg avargldlel
      301 sqhargalli filvlvqacl giftllfqvp lplalchqgm alivlaavva hargyrqpmf
      361 vls
//
LOCUS       WP_176083980             154 aa            linear   BCT 11-JAN-2025
DEFINITION  GFA family protein [Martelella sp. HB161492].
ACCESSION   WP_176083980
VERSION     WP_176083980.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007990
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..154
                     /product="GFA family protein"
                     /GO_function="GO:0016846 - carbon-sulfur lyase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=17053
     Region          3..126
                     /region_name="COG3791"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443005"
ORIGIN      
        1 mtetfsggcq cgairfrash lgrpsichcr mcqkafgsff gplvsadiah ltwtrgkprl
       61 frssakilrg fcekcgtplt yqhpggvela igafdepehf apqvqvnydh rlpwietlfd
      121 apkaeqsmde teivsyqhpd hdtdswpptd etga
//
LOCUS       WP_176083984             426 aa            linear   BCT 11-JAN-2025
DEFINITION  LysM peptidoglycan-binding domain-containing protein [Martelella
            sp. HB161492].
ACCESSION   WP_176083984
VERSION     WP_176083984.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Visweswaran,G.R., Leenhouts,K., van Roosmalen,M., Kok,J. and
            Buist,G.
  TITLE     Exploiting the peptidoglycan-binding motif, LysM, for medical and
            industrial applications
  JOURNAL   Appl Microbiol Biotechnol 98 (10), 4331-4345 (2014)
   PUBMED   24652063
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Buist,G., Steen,A., Kok,J. and Kuipers,O.P.
  TITLE     LysM, a widely distributed protein motif for binding to
            (peptido)glycans
  JOURNAL   Mol Microbiol 68 (4), 838-847 (2008)
   PUBMED   18430080
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447265
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..426
                     /product="LysM peptidoglycan-binding domain-containing
                     protein"
                     /GO_function="GO:0097367 - carbohydrate derivative binding
                     [Evidence IEA]"
                     /calculated_mol_wt=44936
     Region          <76..>272
                     /region_name="Ig_like_BLP2"
                     /note="Ig-like repeat protein Blp2; NF040520"
                     /db_xref="CDD:468522"
     Region          239..395
                     /region_name="XkdP"
                     /note="Cytoplasmic potassium-binding protein
                     Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion
                     transport and metabolism]; COG1652"
                     /db_xref="CDD:441258"
ORIGIN      
        1 menkrplvvv aviallliia avifftirsq kddaaatipa papqtetaek papaatqdkt
       61 tsiriptfdv lrvepdgtav iagsaepdgk levkegekvi tasdvdksgd fvaiidkplp
      121 pgnheiylnv smpdgrsars qqtatiaipe gddkkdllav itepdkptqv veapeptkla
      181 enatpdapat tgdadtklns vnvetkaaea paetsaakpa idasvrisav eiegstlyia
      241 gdgtanaavr gyvdnafaaq dtvnakgsfv iqatidipvg rhqirvdmld kdgnviaras
      301 vpfdrpegnq vsavakapan dattdasgtq tfvqpelqas dnsviirkgd nlwtisrrvy
      361 grgvryttiy lanepqiadp nlilpgqvfs vpdqplpige aeelhrrlek glpvgpeykl
      421 pektgn
//
LOCUS       WP_176084085             121 aa            linear   BCT 11-JAN-2025
DEFINITION  NADH-quinone oxidoreductase subunit A [Martelella sp. HB161492].
ACCESSION   WP_176084085
VERSION     WP_176084085.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Steffen,W. and Steuber,J.
  TITLE     Cation transport by the respiratory NADH:quinone oxidoreductase
            (complex I): facts and hypotheses
  JOURNAL   Biochem Soc Trans 41 (5), 1280-1287 (2013)
   PUBMED   24059520
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Baradaran,R., Berrisford,J.M., Minhas,G.S. and Sazanov,L.A.
  TITLE     Crystal structure of the entire respiratory complex I
  JOURNAL   Nature 494 (7438), 443-448 (2013)
   PUBMED   23417064
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10012780
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..121
                     /product="NADH-quinone oxidoreductase subunit A"
                     /EC_number="1.6.5.9"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016655 - oxidoreductase activity, acting
                     on NAD(P)H, quinone or similar compound as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0048038 - quinone binding [Evidence IEA]"
                     /calculated_mol_wt=13772
     Region          1..121
                     /region_name="PRK06602"
                     /note="NADH:ubiquinone oxidoreductase subunit A;
                     Validated"
                     /db_xref="CDD:180638"
ORIGIN      
        1 mtellssyip ivifiaicli iglalmiapf avafkapdpe klsayecgfn afddarmkfd
       61 irfylvailf iifdlevafl fpwavsfgdi gwfgfwsmmi fllvltigfv yewkkgalew
      121 e
//
LOCUS       WP_176084071             226 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176084071
VERSION     WP_176084071.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 226)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..226
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24182
     Region          4..225
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 marpalvlkn irqdygqges llhvlkgasf tmkpgemval vapsgtgkst llqiaglleh
       61 ptageviing rnaadltdde rtalrrndig fvyqfhhllp efsaleniml pqliaglsrn
      121 dakeraeqml dylkiahrge hrpaelsgge qqrvaiarav anapslllad eptgnldpgt
      181 agyvfealea lvrqsglaal iathnldlag rmdrrvtlqd glvvaa
//
LOCUS       WP_176084116             363 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176084116
VERSION     WP_176084116.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 363)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..363
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40097
     Region          3..363
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mttsvsikdl slsfgaievl rdlnleineg eflvllgssg cgkstllnci aglleatqgq
       61 ifikgknvtw eepkdrgigm vfqsyalypq mtveknlsfg lqvakvpkde irsrverasg
      121 ilqiepllkr kpaelsggqr qrvaigralv rdvdvflfde plsnldaklr selrveikrl
      181 hqslgntmiy vthdqiealt ladriaimks gviqqlddpi tiynrpvnrf vagfigspsm
      241 nflngrlvvk ggrrvfathd vdfaldgyda sgelpgerdv algvrpehim vdeeipeghe
      301 thdaivdlee pmgadnllwl khaghlisvr vggnrryktg qkiklgfnmd laslfdakse
      361 lrl
//
LOCUS       WP_176084143             305 aa            linear   BCT 11-JAN-2025
DEFINITION  cell division protein FtsQ/DivIB [Martelella sp. HB161492].
ACCESSION   WP_176084143
VERSION     WP_176084143.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446343
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..305
                     /product="cell division protein FtsQ/DivIB"
                     /GO_process="GO:0043093 - FtsZ-dependent cytokinesis
                     [Evidence IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=33471
     Region          77..283
                     /region_name="FtsQ"
                     /note="Cell division septal protein FtsQ [Cell cycle
                     control, cell division, chromosome partitioning]; COG1589"
                     /db_xref="CDD:441197"
ORIGIN      
        1 mtgkqggydr tersaapdga rslprparrv arslsnlatg rtpiprhlgs vvavvffaac
       61 gvnavmvagn geqlsraaie lsgfsiddiq isgnvetsei avlqsldldt sislhgldid
      121 rargqllnlp wvadadirki ypntlkislk erkpyalwqq edgsllmiee sgnvigalte
      181 akfrrlplvl gqganlaakd ldslltswpe lsnrvraykr idgrrwdiyl dngmivklpe
      241 tgtdaavarl ksleetrqil ereiaaidlr lddriaiqlt pdalerrdae veqlkksfkn
      301 kgvrl
//
LOCUS       WP_176084248             451 aa            linear   BCT 11-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Martelella sp. HB161492].
ACCESSION   WP_176084248
VERSION     WP_176084248.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..451
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=51116
     Region          92..268
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mdedetrklf segksawnrw angllrekpd tsiptsqlpa neqvererlt qdwqqranvv
       61 lrkhifeqki dfsgwlfpgf ltfdrvefaa aisfngcefs aitfhgvafk gqldlsrcqa
      121 telkffharf hdatdfsgsh isqefaiqss emhkpanwkg mrserklnls gstfhegadl
      181 seamlegtva mqgskfhapl vvagkdlhgs nfrsaslhda dftntnleda nftgadltna
      241 nllgahtntk tifekatadg crinryalec lkdygelsdg armkmaiqdd vailrqrfsg
      301 ylrwmhlval vafifpyawf llskwgearf fdnpavehit laealcryiy nggvnwetgf
      361 dfsfsfvifi lgllfnclrg imlwktktle fqeevrgvrv dfslvdpife aqglrrltwg
      421 tlqkiadkav lvyflivasn tvhflmmdip v
//
LOCUS       WP_176084251             440 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter large permease [Martelella sp. HB161492].
ACCESSION   WP_176084251
VERSION     WP_176084251.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..440
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46156
     Region          14..439
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mdfifdyvde tvfaavllfg lffwmlaqgi aisvaiavss iitglfflpp kvaffvatqk
       61 mfsgldsftl laipffilag nimnkggiai rlvnlakllg grlpgalaht nvianmlfgs
      121 isgsaiaaaa avggtmaplq kkegydptfs aavniasaps gilippsgpl ilfslvsggt
      181 sisalfiggy vpgimmglav mivagiiakr rnfpiserpg tgeairvvwq alpsllmvvv
      241 viggivigaf tategaavav lysfilsliy rlatwreyle vlkgsmitsa vilfliaasg
      301 imsyvmtitg ipdaiadgll tfknpivill imniclliig ffmdltpavl iftpiflpia
      361 tqvgmdpvqf glmmifnlgi gsmtppvgsv lfvgcsiagv tiekvakpll pffitlfial
      421 mmvtyipalt lglprllglm
//
LOCUS       WP_176084259             230 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Martelella sp. HB161492].
ACCESSION   WP_176084259
VERSION     WP_176084259.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..230
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26024
     Region          15..217
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mtetdldflg pvdfsqpivp qihrklrnai irnylepgrr vseagvadal kvsrqpvret
       61 firladqgml dirpksgssv pqisiskviq iqaireaiea diargaarlm ttrhiddlfa
      121 qldrqeceea rnpstfmeld dlfhktlaqg adlpfawnvi evqkaqldrv rflalneips
      181 sslkeqhrav veaiadhnpd raememrahl rnvlrdlpii arrnssyfid
//
LOCUS       WP_176083992             295 aa            linear   BCT 11-JAN-2025
DEFINITION  mechanosensitive ion channel family protein [Martelella sp.
            HB161492].
ACCESSION   WP_176083992
VERSION     WP_176083992.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Malcolm,H.R. and Maurer,J.A.
  TITLE     The mechanosensitive channel of small conductance (MscS)
            superfamily: not just mechanosensitive channels anymore
  JOURNAL   Chembiochem 13 (14), 2037-2043 (2012)
   PUBMED   22915507
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Haswell,E.S., Phillips,R. and Rees,D.C.
  TITLE     Mechanosensitive channels: what can they do and how do they do it?
  JOURNAL   Structure 19 (10), 1356-1369 (2011)
   PUBMED   22000509
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Pivetti,C.D., Yen,M.R., Miller,S., Busch,W., Tseng,Y.H., Booth,I.R.
            and Saier,M.H. Jr.
  TITLE     Two families of mechanosensitive channel proteins
  JOURNAL   Microbiol Mol Biol Rev 67 (1), 66-85 (2003)
   PUBMED   12626684
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Martinac,B.
  TITLE     Mechanosensitive channels in prokaryotes
  JOURNAL   Cell Physiol Biochem 11 (2), 61-76 (2001)
   PUBMED   11275684
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430441
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..295
                     /product="mechanosensitive ion channel family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008381 - mechanosensitive monoatomic ion
                     channel activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31798
     Region          9..275
                     /region_name="MscS"
                     /note="Small-conductance mechanosensitive channel [Cell
                     wall/membrane/envelope biogenesis]; COG0668"
                     /db_xref="CDD:440432"
ORIGIN      
        1 meeqakefik asgdaanfvy aliaqytfsv igaiillivg wivagilqrs vkvsmarlkn
       61 vdqtlagffg avtryavlvi vivmvlgqfg vqtasivaal ggmalaigla lqgtlqniaa
      121 gimllvlrpf rvgeyidtgs ingivmeigl fatelktpdg myrlapnstl wnvpitnfsr
      181 mptrrfdlvv giayednidt aitilmdlae khenvmtdpa pdcfvsnlgd saveitlryw
      241 assavwwpts remtknakna fdaagisipf pqmtlstlka edkpaelmsp dglqn
//
LOCUS       WP_176084296             345 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176084296
VERSION     WP_176084296.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..345
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35239
     Region          2..312
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mpqgikrvlp qlvtlaflva lvsvffpafl qvdyssgrfv gpvvdvlkra apvallsigm
       61 tlvvatkgid lsvgtviait gavaaatlta gygipaaifm alvagliagl fngtlvafig
      121 iqpivatlil misgrgiaql itegriltfn apgfawlgsg alfgipvptv iwllaaviai
      181 lvmrrtalgl lveavgvnmk aaslagvnar vlliavymas glcaavagii taadirgada
      241 nnaglwleld avlatviggn sllggrfsis asvigaliiq tidtgillag fpseynlvik
      301 aalvviilvl qspnvvgdlk ffrqdffrrg asattndpav rrgak
//
LOCUS       WP_176084300             308 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Martelella sp. HB161492].
ACCESSION   WP_176084300
VERSION     WP_176084300.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..308
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33423
     Region          1..241
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mtqigiaivg fgkiardqhl paitadhqfr lagvvdptlp ddirpaftsl nalldadrni
       61 dalalcvpph arfplamaal kagchvllek ppatslaema tlkqeadrrg ltlfaswhsr
      121 fapaaeparr lvaqsavraa rlrwhedvrr whprqdwiwq sgafgvfdsg inglallghi
      181 lpmplhlhaa hlvypdgrda piaarlqfeg aaglgieaaf dwrktgpddk mivvetdsgs
      241 ieidrsgmrl rhngvtlcea pereyaglyr hfatligsgq sdvdtsplaq vtdalargir
      301 etgpafce
//
LOCUS       WP_176084340             237 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Martelella sp. HB161492].
ACCESSION   WP_176084340
VERSION     WP_176084340.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..237
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26680
     Region          7..228
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mtaeehpiek vktrgsgtqk vyealrheil smklapsspl devrlsdrfg msrtpvreal
       61 lrlageglvt tlpnrntivs ainfadlppy fdaltlmyrl smrgaatkrd kpamekmrac
      121 qndfiaavea qdafamiean refhvataec agnpyytaff arlldegrri lrlyyqtfdd
      181 rlprqyvdeh eamiavieng eieeadrlai ahadqivrqi qeylardtgq arglklg
//
LOCUS       WP_176084361             343 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176084361
VERSION     WP_176084361.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 343)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..343
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37107
     Region          1..343
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 msdihldnir ksygrtevlh gislelasge fvsllgasgc gkttllrsva glesvtagri
       61 iidgqdvtql ppekrdiamm fqsyallphl svsenvrfpl rmrrignree qaervkaale
      121 tvqlahlser lprqlsggqq qrvalaraiv snpkvlllde plsnldarlr edmqveliei
      181 hrrlglttlf vthdqeeals lsdrvvllna gtveqegapa eiyaepataf vsgflgsani
      241 lparlgadgt akltdgqiva ipptsltgdv qlvlrqedls latkgnglaa tvrtrvflga
      301 rnryvlelag ktirlltgne iilepgasvt lqiaadrirv ldr
//
LOCUS       WP_176084360             267 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176084360
VERSION     WP_176084360.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..267
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28303
     Region          8..260
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mvkavplwlk ivtaifialv vlvmlgplvv vigtsfsanq fiafppkgfs lewyhkvlss
       61 saylaaggls lalalmvtls svtiggaaai aihrrqlpks dligaaflsp lilptiiyai
      121 gllmfwsstf gpvsfvtlwi ghtvitlpyv vrttlavlse adpfveeaar tmgagriqrl
      181 ifvvlpqcgp glaagaffaf nisfdeavls lflrtpdltt lpvqiygqle fspdpsvaav
      241 stimigltvv lilvidrvlg ikkfass
//
LOCUS       WP_176084378             265 aa            linear   BCT 11-JAN-2025
DEFINITION  pseudouridine synthase [Martelella sp. HB161492].
ACCESSION   WP_176084378
VERSION     WP_176084378.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439600
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..265
                     /product="pseudouridine synthase"
                     /EC_number="5.4.99.-"
                     /GO_function="GO:0003723 - RNA binding [Evidence IEA]"
                     /GO_function="GO:0009982 - pseudouridine synthase activity
                     [Evidence IEA]"
                     /GO_function="GO:0140098 - catalytic activity, acting on
                     RNA [Evidence IEA]"
                     /GO_process="GO:0001522 - pseudouridine synthesis
                     [Evidence IEA]"
                     /GO_process="GO:0009451 - RNA modification [Evidence IEA]"
                     /calculated_mol_wt=29034
     Region          27..249
                     /region_name="RsuA"
                     /note="Pseudouridylate synthase RsuA, specific for 16S
                     rRNA U516 and 23S rRNA U2605 [Translation, ribosomal
                     structure and biogenesis]; COG1187"
                     /db_xref="CDD:440800"
ORIGIN      
        1 mkdtrrrpas gkrsqrrsaa egkratlpra lskrgycsrs qaerlvaegr vsvdgkivts
       61 letwvdveta ricvdgmsve aeqpiylmln kprglvttrh dpegretvya clkdhadahi
      121 spvgrldkas eglllftndt afaqalldpe thvakiyhvq idrvadaalv aalengvahd
      181 geylkaakae ilrqgdrhsw lsitleegrn rqirrmleal diaclrlvrv aigaitlgsl
      241 ekgsaralse teiaalrqai aakrr
//
LOCUS       WP_176084405             136 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Martelella sp. HB161492].
ACCESSION   WP_176084405
VERSION     WP_176084405.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..136
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=14421
     Region          5..129
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 midlktapya alllrvvtgl lfithgltkl fvftpagtmg yfsslglpgf lgiivmilei
       61 vggvalilgv ktrefsfvlg lellgaalfg hiqngfsfan pngggweypv mwafvqfala
      121 llgdgvhall psrrlk
//
LOCUS       WP_176084390             338 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176084390
VERSION     WP_176084390.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..338
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36216
     Region          5..329
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mtgpildirn lstvfetrag tatavdrvsi rlqagetlcv vgesgcgksv tamsimglva
       61 ypgkvvggei lldgddltek spdalsrirg nrismifqdp ssslnpvhtv gaqiaevfml
      121 hqnmgkreaa vaaekmladv gipdaarrmk ayphemsggm aqrvmiamal acrpevliad
      181 epttaldvti qaqildlmrd lqrdfgtaii lithdlgvva emadnvavmy agqvveyadv
      241 rslfrapehp ytqallrsvp vigeeteele visgrvpqlt qlppgclfsp rcaarqqene
      301 prceterppi vgtgggrscr cwlvegetdm agskveqa
//
LOCUS       WP_176084410             267 aa            linear   BCT 11-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Martelella
            sp. HB161492].
ACCESSION   WP_176084410
VERSION     WP_176084410.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..267
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29383
     Region          1..256
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mhekerhrii lsavqekpvv tvselvelte sseatirrdi aalhvqkrlr rvrggaeals
       61 ppqfvglagr pfrvnetmhq rqkqaiakaa vqlcadgdsv iinggtttfq mvnylasrrl
      121 qvftnsfpia ehllkhtknt vmvsggtiyr eqniilspfd ndvtrnfwar rmfmgaqglg
      181 plglmetdpl liqaeqklid qadelvvlad sskfgrrssl ilcplkriat vitddrisdk
      241 daamledagv tlivaesage kevsaar
//
LOCUS       WP_176084413             327 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176084413
VERSION     WP_176084413.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..327
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=33913
     Region          9..303
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 matrllksre allvlamvil atliemrfsg flsakstvai fndtailiil algqaavila
       61 rgidlsiaan lalsgtvaal vnasfpgvpv efllvlsvla gallgaingl lvwkldippi
      121 vvtlgtmtvy rgmiflltdg awinahemsd afkavpravi fglpllswia lcviavmilv
      181 fsftrigraf yavggnpnaa vytgisvgrt hffayvvagt laglagylwv aryavayvdi
      241 angfeldvva acviggisia ggvgtaigav lgalflgiik nalpvidisp fwqmaisgtv
      301 iiiavavnar aarpkgrvil kkaehai
//
LOCUS       WP_176084414             335 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176084414
VERSION     WP_176084414.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..335
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35388
     Region          25..329
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 msdiqtrfvp drlhgtfsri trsweallia vtvavfiins faspyfldpw nlsdatynft
       61 ekaiiafama lviisgeidl svaaiialas tamgyalqfg agtgelvaig lvtglicgaf
      121 ngflitglgl psivvtigtm slyrglayvv lgdkaftgyp pafayfgqgy vfwvisfela
      181 lfavlavlfa illhktsfgr mvyavgnnat aarfsgirvg rvkfilfllt glmsgiaavc
      241 ltsrlgstrp sialgfelev vtmvvlggvs ilggsgsifg vviaafvlgl vtfgfglmnv
      301 pgivmsifvg llligviaip ilwrrvgrrl krkpa
//
LOCUS       WP_176084423             196 aa            linear   BCT 11-JAN-2025
DEFINITION  nucleoside 2-deoxyribosyltransferase [Martelella sp. HB161492].
ACCESSION   WP_176084423
VERSION     WP_176084423.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007604
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..196
                     /product="nucleoside 2-deoxyribosyltransferase"
                     /calculated_mol_wt=21510
     Region          9..157
                     /region_name="RCL"
                     /note="Nucleoside 2-deoxyribosyltransferase [Nucleotide
                     transport and metabolism]; COG3613"
                     /db_xref="CDD:442831"
ORIGIN      
        1 msarkkvyia gpdvffrnas evmrikgema leygfdpstl aeddlnpegl tafrfgvaig
       61 lanerkmdea dfivanltpf rgisadigta yevgymraqn kpvfaysnsg rdyftrltgd
      121 fysgipleki dgvtrgpdgl mvedhgmadn lmldtaaves ggaficenve sddflgdlsv
      181 yrkcleqara yfdnrt
//
LOCUS       WP_176084427             305 aa            linear   BCT 11-JAN-2025
DEFINITION  MurR/RpiR family transcriptional regulator [Martelella sp.
            HB161492].
ACCESSION   WP_176084427
VERSION     WP_176084427.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Sorensen,K.I. and Hove-Jensen,B.
  TITLE     Ribose catabolism of Escherichia coli: characterization of the rpiB
            gene encoding ribose phosphate isomerase B and of the rpiR gene,
            which is involved in regulation of rpiB expression
  JOURNAL   J Bacteriol 178 (4), 1003-1011 (1996)
   PUBMED   8576032
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448252
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..305
                     /product="MurR/RpiR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32649
     Region          18..292
                     /region_name="RpiR"
                     /note="DNA-binding transcriptional regulator, MurR/RpiR
                     family, contains HTH and SIS domains [Transcription];
                     COG1737"
                     /db_xref="CDD:441343"
ORIGIN      
        1 merprdqrra rlpadtpvar kiadaypamp aalrkfadlv lseplhvarl svhdavalid
       61 vsvatanrfa ttlgyegype frseliagfe allepftrme rklaakptpa tvfqaslked
      121 ianleetlgm ipeetimraa rlilgaerif iagfdlsahl ggllaiglsn lgtpvrtves
      181 gggtigalrh lvdygakdlv igiafphyfr etlqlieyah drgtpvlgit dglgsplaal
      241 ateslfvsad hdfnppssta iagvveglva avnslkpaia eknrqfvees yaymaakggh
      301 wgkhd
//
LOCUS       WP_176084430             285 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176084430
VERSION     WP_176084430.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 285)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..285
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31842
     Region          4..269
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 msnlvevenl wvrfptrtgi fdavrgisfs lgkerlgivg esgsgksmtg rallrlirkp
       61 gmvsadrmqv lehdlltise kdmralrgrd ismvmqdpkf slnpvmtvgq qiaealltht
      121 rlnrgktrer vlemleavai rdpervhday phelsggmgq rvmiammlia dpkiliadep
      181 tsaldvsvqi qvleimdklv rergmglifi shdlrlvsnf cdrilimygg rivetcaaga
      241 ledaqhpytr gllnsmprld mperrletln rdpewrnaps vsgml
//
LOCUS       WP_176084439             368 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176084439
VERSION     WP_176084439.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 368)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..368
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39169
     Region          1..360
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 msyvtldhia kdfgptrvid dlslsiekge fvvfvgpsgc gkstllrlia gleqvsggsl
       61 qidgtdithv dsanrgiamv fqsyalyphm tvaenitfgm rmnkvdktli aerlaraaam
      121 lhlepllerk paqlsggqrq rvaigraivr dpsvflfdep lsnldaalrh emrveilklh
      181 rdlgatmiyv thdqveamtm adkivvlsgg rieqvgapld lylrpanrfv aeflgspkin
      241 ciettvhala dsvaslllpg etamafpvgd aaiaagdavt lairpehftl geggeaalag
      301 tvelvehlgs etlltvrvda gtvmtvkvdg vsrvrsgdqi rlgltaqacq lfsasgetlv
      361 fstiaaae
//
LOCUS       WP_176084452             227 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176084452
VERSION     WP_176084452.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 227)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Schneider,E. and Hunke,S.
  TITLE     ATP-binding-cassette (ABC) transport systems: functional and
            structural aspects of the ATP-hydrolyzing subunits/domains
  JOURNAL   FEMS Microbiol Rev 22 (1), 1-20 (1998)
   PUBMED   9640644
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438980
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..227
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=24421
     Region          5..224
                     /region_name="LolD"
                     /note="ABC-type lipoprotein export system, ATPase
                     component [Cell wall/membrane/envelope biogenesis];
                     COG1136"
                     /db_xref="CDD:440751"
ORIGIN      
        1 msqllldvra vgktvrsssq aieilkgvdl slrpgerlcv igasgsgkss lleilgtlst
       61 pdtgqvlltg qdvmsiddra rtqlrretig fvfqgfnlie hisavenval plryiglgrr
      121 dalhraadal ervglthrlr vrasrlsgge kqrvaiaral vtkprlilsd eptgnldeet
      181 grlvldllme nvgegcglvm vthnldharh fdtvlriagg rchaagl
//
LOCUS       WP_176084462             358 aa            linear   BCT 11-JAN-2025
DEFINITION  cupin domain-containing protein [Martelella sp. HB161492].
ACCESSION   WP_176084462
VERSION     WP_176084462.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11465798
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..358
                     /product="cupin domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=40021
     Region          34..351
                     /region_name="COG3435"
                     /note="Gentisate 1,2-dioxygenase [Secondary metabolites
                     biosynthesis, transport and catabolism]"
                     /db_xref="CDD:442661"
ORIGIN      
        1 mdmsqpedsa elralyqafr qnhlnplwtq igdlmpvhpk pkavahvwkw adlyplaqqs
       61 gelvpvgrgg erraiglanp glggeayisp tlwcaiqylg aketapehrh aqnafrfvve
      121 gegvwtvvng dpvrmsrgdf lltpgwnfhg hhnetdqpma widgldipfs yqndvgffey
      181 gsdrvtdyat pefsrgerlw chpglrplsg lensvsspig ayrwdytdra lteqllleee
      241 gqpatyaqgh aairyvnptt ggdvmptira efhrlragve tatrrevgst vfqvfeghga
      301 vvmngerktl ekgdifvips wvpwaleaet qfdlfrfsda pimerlnfar tliedtaa
//
LOCUS       WP_176084480             357 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176084480
VERSION     WP_176084480.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 357)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..357
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38612
     Region          1..357
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mqpivhfsnv tksygsgapa vdaldlaiek gkfvtllgps gcgksttlrm lggfetptsg
       61 aitlsgndvt ylpphkrnvn ivfqdyalfp hltvarniaf glelkgmssa dikkrvdell
      121 alvrledyad rmpsalsggq rqrvalvral apdpdvllld eplsaldakl rhqmqielks
      181 iqeqtgktfl fvthdqeeav tmsdvivvmn ngrieqmgdp qtlyarpknr fvatfigesn
      241 fldatmvsae dgiatlnwgg levhacltgp apeagrtvtv slrpeaifav kqqlnrrnvl
      301 pgeivgeifk gshslltvrl sdgreltvdl dpvalgqidg ssvwigwrek davvlad
//
LOCUS       WP_176084501             297 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Martelella sp.
            HB161492].
ACCESSION   WP_176084501
VERSION     WP_176084501.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 297)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..297
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32672
     Region          11..272
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mqnfhisatg hslnylpeyv avwqgffree elevttevps pwdlvldqig sdkanaalgg
       61 iwvpsmfhtr gkryipfaqv aaraplavig rerpenfawg alpgkviamk gsngasvglf
      121 ikmllrehgi dprtvnfvqd ldgkmltdlf vggmadylvi dypsaatlea sgrahvvapl
      181 sisggnipws vfytdgeasa aaldvhcrfv ralgrgmdwi narpaeeyrt flaetfpkfa
      241 pdilvrltdv yrengmwttp ridpdayqrw qngicdghlt sapiayetli dtrptaa
//
LOCUS       WP_176084512             193 aa            linear   BCT 11-JAN-2025
DEFINITION  NAD(P)H-dependent oxidoreductase [Martelella sp. HB161492].
ACCESSION   WP_176084512
VERSION     WP_176084512.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Ullmann,E., Tan,T.C., Gundinger,T., Herwig,C., Divne,C. and
            Spadiut,O.
  TITLE     A novel cytosolic NADH:quinone oxidoreductase from
            Methanothermobacter marburgensis
  JOURNAL   Biosci Rep 34 (6), e00167 (2014)
   PUBMED   25372605
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Li,R., Bianchet,M.A., Talalay,P. and Amzel,L.M.
  TITLE     The three-dimensional structure of NAD(P)H:quinone reductase, a
            flavoprotein involved in cancer chemoprotection and chemotherapy:
            mechanism of the two-electron reduction
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8846-8850 (1995)
   PUBMED   7568029
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1995 Nov 7;92(23):10815]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006206
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..193
                     /product="NAD(P)H-dependent oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0008753 - NADPH dehydrogenase (quinone)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0050136 - NADH:ubiquinone reductase
                     (non-electrogenic) activity [Evidence IEA]"
                     /calculated_mol_wt=21739
     Region          2..193
                     /region_name="MdaB"
                     /note="Putative NADPH-quinone reductase (modulator of drug
                     activity B) [General function prediction only]; COG2249"
                     /db_xref="CDD:441850"
ORIGIN      
        1 mrvhviyahp lhdslaaklh etvvesliaa ghqvddldly aekfdpvlsa edrrgyhdip
       61 enrsridpyv arlqaadalv lchpvwnfgw pailkgyfdr vflpdvsfkl tdgklgpglt
      121 nirklatvtt ygskrwraaf lgdaprknat rflrvvcapg vkveyhalyd mnnvgehkta
      181 ayiekirqam lrf
//
LOCUS       WP_176084539             299 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Martelella sp. HB161492].
ACCESSION   WP_176084539
VERSION     WP_176084539.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..299
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=32295
     Region          <24..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,160,162,224,241,268)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,189,
                     218..222,229..230,233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mkdlndirvf lavaahgafa aaarelsmta psvtravsal egrlgvqlfl rttrsvslts
       61 agavyaarmr plvdamdaaa eavraeaeav aglirlngpl sfgqrilpdv vsgfraenpa
      121 itvsvaltds fvdimtapfd lairisgppd dkssiwrkic pvrrvlvasp gfiatngrpq
      181 tpeeldqmpc lafdadavse twdlasagrk rkvraghfia snngdliaal aengagiall
      241 plfiveealq agrlmqiled wlppelwltl yypsyerlpm rvarfsdffe syvtrirpl
//
LOCUS       WP_176084566             255 aa            linear   BCT 11-JAN-2025
DEFINITION  enoyl-CoA hydratase/isomerase family protein [Martelella sp.
            HB161492].
ACCESSION   WP_176084566
VERSION     WP_176084566.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Linster,C.L., Noel,G., Stroobant,V., Vertommen,D., Vincent,M.F.,
            Bommer,G.T., Veiga-da-Cunha,M. and Van Schaftingen,E.
  TITLE     Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
            proofreading
  JOURNAL   J Biol Chem 286 (50), 42992-43003 (2011)
   PUBMED   22016388
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Agnihotri,G. and Liu,H.W.
  TITLE     Enoyl-CoA hydratase. reaction, mechanism, and inhibition
  JOURNAL   Bioorg Med Chem 11 (1), 9-20 (2003)
   PUBMED   12467702
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10787157
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..255
                     /product="enoyl-CoA hydratase/isomerase family protein"
                     /GO_function="GO:0016829 - lyase activity [Evidence IEA]"
                     /calculated_mol_wt=26919
     Region          4..249
                     /region_name="CaiD"
                     /note="Enoyl-CoA hydratase/carnithine racemase [Lipid
                     transport and metabolism]; COG1024"
                     /db_xref="CDD:440647"
ORIGIN      
        1 msqvhlirdg qvaelrldnq akmnaftvem lgalaahlev ierdatirav mltgageraf
       61 ctgadiegwg glqpaefarf wvrdghrifd rlarlskpsv avingyafgg glelasacdi
      121 rvmatgaala lpeagvgivp gwggtqrllr lmpepmvkem alfgnrikad ralasgyvaa
      181 vaddpraaaq klleravals praqeiaksm ihaaanedrg amvealgsaa iaassdraeg
      241 vaafrekrkp qfsge
//
LOCUS       WP_176084580             362 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176084580
VERSION     WP_176084580.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 362)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..362
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38972
     Region          1..354
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mstieienve ksfgvttvlr gislsipags fvavlgpsgc gkttllrala gfepidhgai
       61 rlgdrlvsgk gqhvapedrg igvvfqnyal wphmsvagnv syglrikgfs radrdrrtar
      121 vletvglsdl adrrpaalsg gqrqrvalar clameagivl ldeplanldv hlrgemeaef
      181 srfhresgat mfyithdqae alaladrvav mdrgqiaqfa tpsqlyrepa nemvagfigd
      241 gqiatieevw pdgngharar ffgqdvllrc rasrahaaka rvafhpadlr lcletggida
      301 virrltyrge mlrvelgagp dldttlfmnv papaslspgq rvavtltdgw vledpqsakv
      361 ll
//
LOCUS       WP_176084594             287 aa            linear   BCT 11-JAN-2025
DEFINITION  aldo/keto reductase [Martelella sp. HB161492].
ACCESSION   WP_176084594
VERSION     WP_176084594.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Hyndman,D., Bauman,D.R., Heredia,V.V. and Penning,T.M.
  TITLE     The aldo-keto reductase superfamily homepage
  JOURNAL   Chem Biol Interact 143-144, 621-631 (2003)
   PUBMED   12604248
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Jez,J.M., Bennett,M.J., Schlegel,B.P., Lewis,M. and Penning,T.M.
  TITLE     Comparative anatomy of the aldo-keto reductase superfamily
  JOURNAL   Biochem J 326 (Pt 3) (Pt 3), 625-636 (1997)
   PUBMED   9307009
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002080
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..287
                     /product="aldo/keto reductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=31233
     Region          11..275
                     /region_name="ARA1"
                     /note="Aldo/keto reductase, related to diketogulonate
                     reductase [Secondary metabolites biosynthesis, transport
                     and catabolism]; COG0656"
                     /db_xref="CDD:440421"
ORIGIN      
        1 milnetytlp ngvkipklgl gtwmiddntv aaavkaaiai gyrhidtaqa yanergvgea
       61 irssglardd lfvttkldaa fkthaesraa idgsldslgl dhidlmiihs pqpwgefage
      121 erffdgnlqa wraleeayna gkiraigvsn feeadlanll nnasikpmln qvlahisntp
      181 fdlieycesk gilveayspv ahgkildhre iaemaakygv svpqlsiryc lelgllplpk
      241 tanpdhmrtn aavdfeisaa dmdvlksmdr ikdygdanmf pvygakl
//
LOCUS       WP_176084582             350 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176084582
VERSION     WP_176084582.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 350)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..350
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38200
     Region          1..346
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtgisaenla mrfdrftavd dvsfsvksge fvtllgpsgc gkttllkiis gfltpsagri
       61 flggedvtri ppeqrdtalc fqsyalfphl svaenlafgl kqkkvplrer karigdmaek
      121 lgltaqlakl pnqlsggqqq rvslgralvm rpgvilfdep lsnldaklrd qvrieirriq
      181 qesqltaiyv thdqaealam sdrifvmnag rveqadtpeg lyhaprtrfv adfigganil
      241 dgqiewksag ravihtpigs lpmplspaeg dkayaicwrp eaarilphac egalsgrvvn
      301 rafqgqftdl mvetagifyr iqtresrige gdmihfdlap eaviplgteq
//
LOCUS       WP_176084678             320 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Martelella sp. HB161492].
ACCESSION   WP_176084678
VERSION     WP_176084678.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..320
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35540
     Region          10..317
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 msisenrtcr igfvvvpdfs litlasgiep frlaniaagr kvfdyrtlav fdrqvlsndg
       61 vqmlaedeis tldfdivfli asldaadfds aklsawlrrl dragamiapv gagtmiaarl
      121 glmdgyqsvt hwrlydrfqe qfprvhlqrg vfcidgrras gaggasttdl alqvvanlve
      181 priavevaev vmvskirsgs dtqrlptrwr fgirddrvar aielmeayie nplpletiae
      241 rlglslrqld rafgralgrt pkqqyvlirl qsaqrlllet sepiyriair sgffdsahfs
      301 ssfksafgip ptemrkrtap
//
LOCUS       WP_176084625             347 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176084625
VERSION     WP_176084625.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..347
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37503
     Region          1..345
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 miaisiqnls kkfgtftals elslevrtge fvtllgpsgc gkttllklis gfleptsgti
       61 sidgkdvtqt ppeardtalc fqsyalfphl tvrdnlefgl rqkrlpaadr rarvgdvaak
      121 lgleaqmdkl pnqlsggqqq rvslgralvm rpsvilfdep lsnldaklrd qvrveirriq
      181 keygltaiyv thdqaealam sdrvvvlksg rveqidtpeh lyaaprtgfv adfigsanvf
      241 sghatgrtid grlqvstpvg tveviapata pgaqvslcwr pervvpgsge ltgtvlnraf
      301 qghftdltid sngcihriql aesdaregde irfsiapehi illgadh
//
LOCUS       WP_176084692             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176084692
VERSION     WP_176084692.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..359
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38865
     Region          1..351
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mtgvslkqir kaygtlevih gvdieiekge fvvfvgpsgc gkstllrmia gleeitggdl
       61 hihgqrvnnv dpshrgvamv fqtyalyphm tvdqnmgfgl rmngtpraev arrvaeaari
      121 lqiedlldrk prqlsggqrq rvaigraivr hpevflfdep lsnldaelrv atrlelaklh
      181 qqlagstmiy vthdqveamt ladkivvlrk grveqigrpm alyenpanlf vagfigspkm
      241 nfldltddna ggfrfadesr lrlegpaadr vavlgaradq mklvaagsgh ftgtvsvver
      301 lgdsefvyvr tgwgqelvvr veggsdipvg letgialsgr thffdsdgqs lpgiavtag
//
LOCUS       WP_176084717             248 aa            linear   BCT 11-JAN-2025
DEFINITION  amino acid ABC transporter ATP-binding protein [Martelella sp.
            HB161492].
ACCESSION   WP_176084717
VERSION     WP_176084717.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Walshaw,D.L. and Poole,P.S.
  TITLE     The general L-amino acid permease of Rhizobium leguminosarum is an
            ABC uptake system that also influences efflux of solutes
  JOURNAL   Mol Microbiol 21 (6), 1239-1252 (1996)
   PUBMED   8898392
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438336
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..248
                     /product="amino acid ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0015424 - ABC-type amino acid transporter
                     activity [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27307
     Region          9..246
                     /region_name="GlnQ"
                     /note="ABC-type polar amino acid transport system, ATPase
                     component [Amino acid transport and metabolism]; COG1126"
                     /db_xref="CDD:440743"
ORIGIN      
        1 mstttaksil eihalyksfn gtevlkninl rvyegelvfl igpsgsgkst llrccnrlee
       61 psdgaivvdg vnitavttdi nqmrqrigmv fqqfnlyphm taeqnvmlal rrvqkkslae
      121 areiahrele rmglgtrlth ypnqlsggqq qrvaiartla lgpkvmllde ptsaldpqlv
      181 gevlqamrel kdegmtmlvv shemrfarea adrvafmeag qivelgtpae liargpesra
      241 sqflahgh
//
LOCUS       WP_176084720             492 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Martelella sp. HB161492].
ACCESSION   WP_176084720
VERSION     WP_176084720.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..492
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=51478
     Region          14..454
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mleeettsdr rdgdlagltv aegsrriatg dispsallda ilaridavdg vihsylrmdr
       61 eaaakaaeaa tgraqagrrl gpldgipfav kdniytsglp ttggsrvpqr hdpathatlv
      121 arlqaagavl igkantweyg tgtgsvefdl dapparnpwn pghftggsst gsaaavaagt
      181 aafaigtdtg gsvrlpaaac glvglkptfg risrhgvmpn cwsfdtpgpl tltvedaami
      241 ydviaghdpl dpesltaave ptlpalkegi agrvvgfvkn ldpggappep sivdalsrsa
      301 aalqahgaiv reielpiaps eyraismpin rsesfsiheq dylehrhlmg rslreklemg
      361 mylraadyia alrqrrilaa rtdavfsdvd ivllpmtyrt apdihdreav isfttgsags
      421 pfsltghpal alpagfdqng lpisvqlaag yrqealllra afaleqaltp epvraepshi
      481 lagapaameq ar
//
LOCUS       WP_176084758             269 aa            linear   BCT 11-JAN-2025
DEFINITION  creatininase family protein [Martelella sp. HB161492].
ACCESSION   WP_176084758
VERSION     WP_176084758.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Yoshimoto,T., Tanaka,N., Kanada,N., Inoue,T., Nakajima,Y.,
            Haratake,M., Nakamura,K.T., Xu,Y. and Ito,K.
  TITLE     Crystal structures of creatininase reveal the substrate binding
            site and provide an insight into the catalytic mechanism
  JOURNAL   J Mol Biol 337 (2), 399-416 (2004)
   PUBMED   15003455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..269
                     /product="creatininase family protein"
                     /EC_number="3.5.2.10"
                     /calculated_mol_wt=28761
     Region          1..259
                     /region_name="ArfB"
                     /note="Creatinine amidohydrolase/Fe(II)-dependent FAPy
                     formamide hydrolase (riboflavin and F420 biosynthesis)
                     [Coenzyme transport and metabolism]; COG1402"
                     /db_xref="CDD:441012"
ORIGIN      
        1 mplmnwmdls trefdhlptn availpiaai eqhgphlpvg tdtlinrgii hragsfldes
       61 vtalvlpeqa vgvstehlkf agtlsqstql lldyltvile rvhaagisrv liynthggnk
      121 sllyplalem rarhdmlvaf ssrgdagips glfnlphlef dihagaiets immalhpelv
      181 sqveirdfvs naigyeerfq hlgagpggsr tagygwmsqd lnpfgacgda raatpeaghm
      241 lvnhaakala gilaeiasan dllkskpkn
//
LOCUS       WP_176084768             258 aa            linear   BCT 11-JAN-2025
DEFINITION  YoaK family protein [Martelella sp. HB161492].
ACCESSION   WP_176084768
VERSION     WP_176084768.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..258
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=27546
     Region          6..222
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 msrssiasvl sfnggyvdtm gfvalnglft ahvtgnfvtl gatlangtgg vlakllalpv
       61 fcitvllara fgdwmqrrri qavpvflalk calfllaall avvlplhdra gdasvplgmv
      121 lvvamaiqna lhrthltdqp pttlltgttt qimldlsdvl fgdrtkglpi yprlmplira
      181 lvlfaagcav aalayrvshr fcffipplti aaalmlswre erpvphkarp aaeaddrvde
      241 alresfpasd ppasgrfd
//
LOCUS       WP_176084783             373 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176084783
VERSION     WP_176084783.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 373)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..373
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39924
     Region          10..371
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 maaimeeerr gaeirltgls rsygdnkvva dvdlvaggge vlallgpsgc gktttlrmia
       61 glvrptsgev aidgvavtal pvhqrnlgml fqnyalfphl nvldnvafgl tmrgmakgea
      121 aararqalaq vrlsgfeerm paalsggqqq rvalaraivy hprallldep faaldkklre
      181 emqievrqla nelglttiiv thdqeealvl adriavmkgg rieqvadara iyerpathfv
      241 adfigssnfl eativelswg rttlrdragv llesaiahda grgeqvtlav rpenvllspa
      301 gdvengpgqe snvfsgkvlr tvfkgqtlsv wlerpdggef iatlsggtgp gpgpgekwtv
      361 rfspersliv rnh
//
LOCUS       WP_176084807             317 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Martelella sp. HB161492].
ACCESSION   WP_176084807
VERSION     WP_176084807.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..317
                     /product="LysR family transcriptional regulator"
                     /GO_component="GO:0032993 - protein-DNA complex [Evidence
                     IEA]"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35576
     Region          20..79
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          108..304
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(118,122,161,175,177,238,255,283)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(119..120,124..125,127..128,131,135,137..143,204,
                     232..236,243..244,247)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 mvdtqkpafi gsnaddsdrl slisafvnva slgsfsaaae ssktnastis rrvsrledll
       61 gvrlfnrttr rvsltepgrl yydscllile qiaeadammg eftsaprgkl ritmpvafgr
      121 lhmvdaitef mirypdveve anstdrfvdl vaegydiair tgslqdsglv vrqiaanrrl
      181 lvgrrsyler hfyprqpedl vhlnclrftn ysaahwqfqn ereirdilis gtmtsdssda
      241 iygailkglg iglvaeymch neiasgeiev llpewavqpe akiyishigs rhispkvraf
      301 sdfvvgyfrr rdfprwn
//
LOCUS       WP_176084818             357 aa            linear   BCT 11-JAN-2025
DEFINITION  saccharopine dehydrogenase family protein [Martelella sp.
            HB161492].
ACCESSION   WP_176084818
VERSION     WP_176084818.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Johansson,E., Steffens,J.J., Lindqvist,Y. and Schneider,G.
  TITLE     Crystal structure of saccharopine reductase from Magnaporthe
            grisea, an enzyme of the alpha-aminoadipate pathway of lysine
            biosynthesis
  JOURNAL   Structure 8 (10), 1037-1047 (2000)
   PUBMED   11080625
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448323
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..357
                     /product="saccharopine dehydrogenase family protein"
                     /EC_number="1.5.1.-"
                     /GO_function="GO:0016646 - oxidoreductase activity, acting
                     on the CH-NH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0009085 - lysine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38795
     Region          3..>51
                     /region_name="PRK06223"
                     /note="malate dehydrogenase; Reviewed"
                     /db_xref="CDD:180477"
     Region          29..>274
                     /region_name="Lys9"
                     /note="Saccharopine dehydrogenase, NADP-dependent [Amino
                     acid transport and metabolism]; COG1748"
                     /db_xref="CDD:441354"
ORIGIN      
        1 mtrfkvaifg agnigsalaa nlshgqdvdv tmiepsedal dsfsalglea etvrpkrsgd
       61 ipaaartadl ivaatpgwav sgiaeiavga kthfldfapl raevknvlgp laqkrvvlng
      121 cgiapglven iacnliaecr rvseltirvg slprfpvnrl gygqiwdida lideytkpce
      181 airdgntvmi spleeleqlr fngtdyecft tsrglsdlsp yraagidrlt fktlrypghl
      241 dhmrfllddl glrekrdmlr sllmnglpiv kddelvlflt awqkagarri eqsqtyrfrp
      301 gpdhpfnami saasayaasl ialvkdgqlg qvgfvdhhqi esltllkgpf lsrliaa
//
LOCUS       WP_176084854             199 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Martelella sp.
            HB161492].
ACCESSION   WP_176084854
VERSION     WP_176084854.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..199
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22460
     Region          2..161
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mrrkaeetre dilntaealf rekgysgvsi adiaaalems panvfkhfqs klvlgqaiay
       61 rygerfrahc deveqdtglp adirltrfvd rltkdhlqkm qndrylfeml pfvfedpank
      121 grmyrglvrd riaailddgm kaqlfregdp vrdaevivdm ltcvlhpnmv kcadlatqsd
      181 kahailrlvd aglkygvak
//
LOCUS       WP_176084962             230 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Martelella sp. HB161492].
ACCESSION   WP_176084962
VERSION     WP_176084962.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..230
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=26278
     Region          1..215
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mstlyhhpms aasrfvrlvm geydfefdli eerpwekrra flaanpagtl pvyvddnmrv
       61 lcgasviaef idethgvlqr drrllaeepf qraeirrlte wflqklehdv typlcrervy
      121 klqmtsgngg gapdsrilra araniqqhlk ylswlggsrp wlagkrlsya dlaaggaisv
      181 ldylgeikwe eapgakewyq rlksrpsfrp llaervrgvv pvshyadldf
//
LOCUS       WP_176084972              65 aa            linear   BCT 11-JAN-2025
DEFINITION  Trm112 family protein [Martelella sp. HB161492].
ACCESSION   WP_176084972
VERSION     WP_176084972.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   van Tran,N., Muller,L., Ross,R.L., Lestini,R., Letoquart,J.,
            Ulryck,N., Limbach,P.A., de Crecy-Lagard,V., Cianferani,S. and
            Graille,M.
  TITLE     Evolutionary insights into Trm112-methyltransferase holoenzymes
            involved in translation between archaea and eukaryotes
  JOURNAL   Nucleic Acids Res 46 (16), 8483-8499 (2018)
   PUBMED   30010922
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Bourgeois,G., Letoquart,J., van Tran,N. and Graille,M.
  TITLE     Trm112, a Protein Activator of Methyltransferases Modifying Actors
            of the Eukaryotic Translational Apparatus
  JOURNAL   Biomolecules 7 (1), 7 (2017)
   PUBMED   28134793
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006712
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..65
                     /product="Trm112 family protein"
                     /calculated_mol_wt=7256
     Region          12..65
                     /region_name="Trm112"
                     /note="RNA methyltransferase activator Trm112/YbaR
                     [Translation, ribosomal structure and biogenesis];
                     COG2835"
                     /db_xref="CDD:442083"
ORIGIN      
        1 mpasqdkydp ridprmlell vcpltkgrlt ydreagelvs ekarlaypir dgvpimlvse
       61 arqlt
//
LOCUS       WP_176084979             434 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter large permease [Martelella sp. HB161492].
ACCESSION   WP_176084979
VERSION     WP_176084979.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..434
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=46577
     Region          8..433
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 maffsdhali imlaimvtit itglpfgiam ivssifylfl ahrdvglaae nvlngvfgnf
       61 valavplfif aanvmnegki sdrlldfsla vvgrlpggla qvniftslif sgmsgsaisd
      121 aagvgkiitd mmmkenrypr gfagaltaas avvgpifpps ipmvfyalis stsvgvlflg
      181 gvvpallmct vmaiavaima kirgfpveea vplrmlpvvi irafpallmp iillggiysg
      241 iftpteaaav salyalllaf fayrvlglas fwrvvvstvk ttavvtmvlc gafifnyvit
      301 iervpqmvfd tvqnyqfepw qflmllnily lllgcildvs timlvvtplf iptaaalgid
      361 lnhlgvvlvf nmmiglitpp ygillfiika lngiplaemi retwffmail ismllaltfi
      421 pglvlwlpra agml
//
LOCUS       WP_176085035             148 aa            linear   BCT 11-JAN-2025
DEFINITION  cyclic nucleotide-binding domain-containing protein [Martelella sp.
            HB161492].
ACCESSION   WP_176085035
VERSION     WP_176085035.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Wang,Z., Jiang,Y., Lu,L., Huang,R., Hou,Q. and Shi,F.
  TITLE     Molecular mechanisms of cyclic nucleotide-gated ion channel gating
  JOURNAL   J Genet Genomics 34 (6), 477-485 (2007)
   PUBMED   17601606
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Kaupp,U.B. and Seifert,R.
  TITLE     Cyclic nucleotide-gated ion channels
  JOURNAL   Physiol Rev 82 (3), 769-824 (2002)
   PUBMED   12087135
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Canaves,J.M. and Taylor,S.S.
  TITLE     Classification and phylogenetic analysis of the cAMP-dependent
            protein kinase regulatory subunit family
  JOURNAL   J Mol Evol 54 (1), 17-29 (2002)
   PUBMED   11734894
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Aiba,H., Fujimoto,S. and Ozaki,N.
  TITLE     Molecular cloning and nucleotide sequencing of the gene for E. coli
            cAMP receptor protein
  JOURNAL   Nucleic Acids Res 10 (4), 1345-1361 (1982)
   PUBMED   6280140
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10034975
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..148
                     /product="cyclic nucleotide-binding domain-containing
                     protein"
                     /GO_function="GO:0030551 - cyclic nucleotide binding
                     [Evidence IEA]"
                     /GO_function="GO:0030552 - cAMP binding [Evidence IEA]"
                     /calculated_mol_wt=16000
     Region          15..123
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(79..80,89..91)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(111..113,117..119)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
ORIGIN      
        1 malsrdievl rrtdlfsgft gdqlllvaft arqirlepge lllrendise gayvvaegkl
       61 sleaggqscg iagpgsvlae valvspiahr ltatadlrse iffisreafi klvgeypdig
      121 eamdrrlrqg faemvsalds vrtrlsdf
//
LOCUS       WP_176085085             230 aa            linear   BCT 11-JAN-2025
DEFINITION  cysteine hydrolase family protein [Martelella sp. HB161492].
ACCESSION   WP_176085085
VERSION     WP_176085085.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003554
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..230
                     /product="cysteine hydrolase family protein"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=25604
     Region          29..219
                     /region_name="PncA"
                     /note="Nicotinamidase-related amidase [Coenzyme transport
                     and metabolism, General function prediction only];
                     COG1335"
                     /db_xref="CDD:440946"
ORIGIN      
        1 mswktkwrsf yyqgapepad palekgkval liidvqntyl krpdpdtltd aelaryhawt
       61 pfhdrmhetv ipnsqkllqa frargldvly ariaalrtdg rdrslsqkkp gwndlllpkd
      121 ewdsqiidal apekdeivvt kttdsaltgt nlrlvlgnlg ithvvcagif tdqcvastvr
      181 sladesfdvi iaedacaags telhereiei mnmiyasvms sdeliaylpe
//
LOCUS       WP_176085086             254 aa            linear   BCT 11-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Martelella
            sp. HB161492].
ACCESSION   WP_176085086
VERSION     WP_176085086.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..254
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=27489
     Region          5..254
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mklskserqa qiltelngta slrvaelarr mdvstetirr dldemteqgl lnrtyggatr
       61 slssepavse rhtlfisere riakatipli rdarilmigs gsttvhvarr iavemrditv
      121 lthafgvatv lsmnptikvl mlpgdyhade gatvgvhtvs flndyfadaa ilgasglaed
      181 gptdalieca svysamvlrs srtivtadhs khgrifpary sswkkldqlv tdmapagsla
      241 raltqhnidv tiad
//
LOCUS       WP_176085093             465 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Martelella sp. HB161492].
ACCESSION   WP_176085093
VERSION     WP_176085093.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..465
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=47156
     Region          12..457
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mtadatalaa aigkgeltar qameqslaaa ktqsalgalc lvdetaglda aaqfdslpvd
       61 ekrrmpfggv plvakdlggp frgfplrags ramapnadld sdlaarfraa gfcmfglats
      121 pefglslaae pligpcarnp ldpglspggs sggsaaavaa givaiahatd aggsirvpaa
      181 acglvglkpg rgampagpgy gnylggiase lavcrsvrda alafetlsgd akgpfpevkp
      241 skaggmlsig vlaetgdqtp ttperaaavl daarrlerkg hrlvalewar vsalaeecaa
      301 lfgdiaainl atnvrrfgld ctklepltqa vvarglamsg tdvwqitnrl afvardcqal
      361 fdgfdvlatp mlsgpprpvg afpadhgdta ahfarmaafa platlanmsg faaltlpvga
      421 dhdglplplq lmapsgaelp llglaqtlen edlwhhpfai agfgr
//
LOCUS       WP_176085107             130 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Martelella sp. HB161492].
ACCESSION   WP_176085107
VERSION     WP_176085107.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10790122
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..130
                     /product="VOC family protein"
                     /calculated_mol_wt=13866
     Region          10..127
                     /region_name="VOC"
                     /note="Lactoylglutathione lyase-related enzyme, vicinal
                     oxygen chelate (VOC) family [General function prediction
                     only]; COG3324"
                     /db_xref="CDD:442553"
ORIGIN      
        1 madgsstgrv tglggifvls anseglsawy rdvlgltvea wggsrfddaa rpsgssslwc
       61 sfnaesgyla psprdfminf ivddmdlmls rldqkgvail grddsddngr fawvldpdgt
      121 kielwqpgka
//
LOCUS       WP_176085108              91 aa            linear   BCT 11-JAN-2025
DEFINITION  HPr family phosphocarrier protein [Martelella sp. HB161492].
ACCESSION   WP_176085108
VERSION     WP_176085108.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Hu,K.Y. and Saier,M.H. Jr.
  TITLE     Phylogeny of phosphoryl transfer proteins of the
            phosphoenolpyruvate-dependent sugar-transporting phosphotransferase
            system
  JOURNAL   Res Microbiol 153 (7), 405-415 (2002)
   PUBMED   12405346
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10788234
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..91
                     /product="HPr family phosphocarrier protein"
                     /GO_function="GO:0008982 -
                     protein-N(PI)-phosphohistidine-sugar phosphotransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=9470
     Region          4..90
                     /region_name="PtsH"
                     /note="HPr or related phosphotransfer protein [Signal
                     transduction mechanisms, Carbohydrate transport and
                     metabolism]; COG1925"
                     /db_xref="CDD:441528"
ORIGIN      
        1 mseasrelti inrrglhara sakfvqtver fdahvtvskd gmsvggtsim glmmlaagie
       61 sqivvsasgp dadealdaia slvecrfgee c
//
LOCUS       WP_176085183             232 aa            linear   BCT 11-JAN-2025
DEFINITION  AzlC family ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176085183
VERSION     WP_176085183.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 232)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 232)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 232)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003447
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..232
                     /product="AzlC family ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:1902495 - transmembrane transporter
                     complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=24427
     Region          6..208
                     /region_name="AzlC"
                     /note="Predicted branched-chain amino acid permease
                     (azaleucine resistance) [Amino acid transport and
                     metabolism]; COG1296"
                     /db_xref="CDD:440907"
ORIGIN      
        1 mhkdgfltgl kdglvpslsa apfgvlfgav avaqgqtvfe talmsitifa gasqlvgvel
       61 fghrvaawii ilsivavnfr hvlysaamtp aithfslpek aiafflmtdp qfaetlkrhe
      121 nghgvsfvwy lgvglclygf wnvmtligat lggfiddpaa lgldillpiy flslvigfrk
      181 rdnflpvvlv salgsviaya tigspwhvsi galagialaa alppktnkea sa
//
LOCUS       WP_176085203             277 aa            linear   BCT 11-JAN-2025
DEFINITION  polyphosphate kinase 2 family protein [Martelella sp. HB161492].
ACCESSION   WP_176085203
VERSION     WP_176085203.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Motomura,K., Hirota,R., Okada,M., Ikeda,T., Ishida,T. and Kuroda,A.
  TITLE     A new subfamily of polyphosphate kinase 2 (class III PPK2)
            catalyzes both nucleoside monophosphate phosphorylation and
            nucleoside diphosphate phosphorylation
  JOURNAL   Appl Environ Microbiol 80 (8), 2602-2608 (2014)
   PUBMED   24532069
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Sureka,K., Sanyal,S., Basu,J. and Kundu,M.
  TITLE     Polyphosphate kinase 2: a modulator of nucleoside diphosphate
            kinase activity in mycobacteria
  JOURNAL   Mol Microbiol 74 (5), 1187-1197 (2009)
   PUBMED   19843229
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Nocek,B., Kochinyan,S., Proudfoot,M., Brown,G., Evdokimova,E.,
            Osipiuk,J., Edwards,A.M., Savchenko,A., Joachimiak,A. and
            Yakunin,A.F.
  TITLE     Polyphosphate-dependent synthesis of ATP and ADP by the family-2
            polyphosphate kinases in bacteria
  JOURNAL   Proc Natl Acad Sci U S A 105 (46), 17730-17735 (2008)
   PUBMED   19001261
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10023124
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..277
                     /product="polyphosphate kinase 2 family protein"
                     /EC_number="2.7.4.-"
                     /GO_function="GO:0008976 - polyphosphate kinase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016776 - phosphotransferase activity,
                     phosphate group as acceptor [Evidence IEA]"
                     /GO_process="GO:0006797 - polyphosphate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32059
     Region          4..266
                     /region_name="PPK2_rel_1"
                     /note="polyphosphate:nucleotide phosphotransferase, PPK2
                     family; TIGR03709"
                     /db_xref="CDD:274737"
ORIGIN      
        1 mdfrkhlvve pgskvqlski dpgyhgeids kkageaelek vldritplqe rlyaekkhal
       61 lvvlqgidaa gkdgvcwhvi ramnpqgtyv asfkqptate qlhdflwrvh artpasgqva
      121 vfnrshyedv liarvhnlvp ekvwskryhq inmfeeylse ngvaivkffl yiskdeqldr
      181 fekrledker qwkisasdya ererwdayie ayeamlgncs tryapwyvlp anhkwfrnla
      241 aaniiletle gmnietptpt vdiddiyrky hhavrss
//
LOCUS       WP_176085218             154 aa            linear   BCT 11-JAN-2025
DEFINITION  RDD family protein [Martelella sp. HB161492].
ACCESSION   WP_176085218
VERSION     WP_176085218.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004363
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..154
                     /product="RDD family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=17123
     Region          14..150
                     /region_name="YckC"
                     /note="Uncharacterized membrane protein YckC, RDD family
                     [Function unknown]; COG1714"
                     /db_xref="CDD:441320"
ORIGIN      
        1 msldrdtsly aptdwraysg vlsrrifafl vdyiviallw ipaavivffv giatfglgfl
       61 lypilyfiva ifyfgmtmgg paqaspgmra mglkivrtdg mpmdfltavv hlalfwifns
      121 lltplvlivg iftsrkrllh dflvgavmvr seqf
//
LOCUS       WP_176085223             296 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Martelella sp. HB161492].
ACCESSION   WP_176085223
VERSION     WP_176085223.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..296
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32420
     Region          8..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..282
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,216..219,
                     225..226,228..229)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mkrgtiplna lrafeatmrh gqmglaadel gvthsavsrq vrqleailgv alfegprnrl
       61 tpsqaaldlq pvlseafesi eravaramqr drqildvsct stlamrwlip rlvdfqtrhp
      121 tieirltadd aavdfsrhrf dvairvlkpp fgdaivdplf pdetgpvlsp rlagdmtlen
      181 aeallhlpal qtrtrphawm dwgrqlglsp padgrifehf yfmleaatag lgvaiapeil
      241 vrddlaagrl iapfgflpsg ltyvalrprr pnraaerfvn wltgasetgs snggdh
//
LOCUS       WP_176085253             398 aa            linear   BCT 11-JAN-2025
DEFINITION  phosphoglycerate kinase [Martelella sp. HB161492].
ACCESSION   WP_176085253
VERSION     WP_176085253.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Chiarelli,L.R., Morera,S.M., Bianchi,P., Fermo,E., Zanella,A.,
            Galizzi,A. and Valentini,G.
  TITLE     Molecular insights on pathogenic effects of mutations causing
            phosphoglycerate kinase deficiency
  JOURNAL   PLoS One 7 (2), e32065 (2012)
   PUBMED   22348148
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Yon,J.M., Desmadril,M., Betton,J.M., Minard,P., Ballery,N.,
            Missiakas,D., Gaillard-Miran,S., Perahia,D. and Mouawad,L.
  TITLE     Flexibility and folding of phosphoglycerate kinase
  JOURNAL   Biochimie 72 (6-7), 417-429 (1990)
   PUBMED   2124145
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Yoshida,A. and Tani,K.
  TITLE     Phosphoglycerate kinase abnormalities: functional, structural and
            genomic aspects
  JOURNAL   Biomed Biochim Acta 42 (11-12), S263-S267 (1983)
   PUBMED   6689547
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000622
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..398
                     /product="phosphoglycerate kinase"
                     /EC_number="2.7.2.3"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004618 - phosphoglycerate kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=41617
     Region          6..398
                     /region_name="Pgk"
                     /note="3-phosphoglycerate kinase [Carbohydrate transport
                     and metabolism]; COG0126"
                     /db_xref="CDD:439896"
ORIGIN      
        1 mpafktlddl tdiagkrvll rvdlnvpvsd gkvtdttrie rvaptilels ekgakvilma
       61 hfgrpkgavv pemslkliip sveevldhsv afatdcigep aekaiaamen gdilllentr
      121 fhkgeeknep dfvaalakng diyvndafsa ahrahasteg lghhmpayag rtmqaeleal
      181 ekglgvpvrp vvaivggakv stkidllqnl iekvdalvig ggmantfiaa kgidvgkslc
      241 ehdladtara imakakttnc aivlpvdgvv arefkanadn etvaidaipa dammldvgpa
      301 sialvnewia kaatlvwngp lgafeiepfd tatvsaakfa aeqtragkli svagggdtvs
      361 alnhagvadd fsyvstagga flewmegkal pgveilkk
//
LOCUS       WP_176085274             356 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176085274
VERSION     WP_176085274.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..356
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38970
     Region          1..356
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 madlvlsqin khygdhqvlh didlmipdge fvvlvgpsgc gkstllrmia gleevtygdl
       61 iigghrsnhv tpqrrniamv fqsyalfphm tvrdniaygp klrgekaeei dvkiahaaei
      121 lnltpylery prqlsggqrq rvamgraivr epslflfdep lsnldaqlrv qmrteikalh
      181 kkvgrtsiyv thdqieamtl adrivvmnag hieqigtple lydtpktlfv akfigspamn
      241 lldatiassd gqmramisds isialpgatg lqpgdtltlg irpehfelap dgeglplavd
      301 lveqtgadty vygkvggqsv valfrhrlvv dsdavlsvrp qlgmehlfnp qtgkri
//
LOCUS       WP_176085292             277 aa            linear   BCT 11-JAN-2025
DEFINITION  carbon-nitrogen hydrolase family protein [Martelella sp. HB161492].
ACCESSION   WP_176085292
VERSION     WP_176085292.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10166075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..277
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=29583
     Region          4..268
                     /region_name="nit"
                     /note="Nit1, Nit 2, and related proteins, and the
                     Nit1-like domain of NitFhit (class 10 nitrilases);
                     cd07572"
                     /db_xref="CDD:143596"
     Site            order(42,97,114,118,130,155..156,158..159,180)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143596"
     Site            order(42,114,155)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143596"
     Site            order(115..116,136..138,156,159..163,165..166,188..189,
                     192..193,195..197,199..200,230,261..262,265..266,268)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143596"
ORIGIN      
        1 mtftaaaiql csttspaknv aametlvrea anrgagyiqt pemtgavqkd raglravlrg
       61 eaddlvvaka aslardlgih lhigstaial ddgmianrgf lfspegtila rydkihmfdv
      121 dldngeswre savyrpgera avidtplari amgicydvrf pdlftaqala gaeilsapaa
      181 ftrqtgeahw hvlqraraie ngafmisaaq agrhedgret yghsiiidpw grimaeadge
      241 geaivmaeid saavraarak ipnlknirpf tletsap
//
LOCUS       WP_176085309             224 aa            linear   BCT 11-JAN-2025
DEFINITION  YoaK family protein [Martelella sp. HB161492].
ACCESSION   WP_176085309
VERSION     WP_176085309.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007619
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..224
                     /product="YoaK family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=23871
     Region          5..216
                     /region_name="YoaK"
                     /note="Uncharacterized membrane protein YoaK, UPF0700
                     family [Function unknown]; COG3619"
                     /db_xref="CDD:442837"
ORIGIN      
        1 mskpvlasll sfnggyvdtm gfvtlnglfv ahvtgnfvtl gasivngtgg efskllaipv
       61 fclsifaari fgqwlkekdy pvvtillvtk filfsiaagm afsitfgkta staeivlgmv
      121 lvvamamqna lhrvhlperp pstlmtgttt qimldladil fgrdidrekv sgrlkmlvpa
      181 lvafgigcat aaliylvagk lcflvppali alsfilhwrs genf
//
LOCUS       WP_176085344             232 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Martelella sp. HB161492].
ACCESSION   WP_176085344
VERSION     WP_176085344.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..232
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25789
     Region          15..229
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 maraatnrld ikdgamrrqp rlslrdqayq vikskivsce lkpgeavtvt dladalgigr
       61 tpviqavdrl midglvevmp rkgvvvspvs ldelveliev rqinearvsr waaeriqdkq
      121 vkelrdnldr mlkatqkrel gqlialdraf hqaialtagn simtellgnl hdravrfwtl
      181 slnvpdqnsr vcdqhaeiie klaahdpdga eqamlshina fkanlfdtlm ks
//
LOCUS       WP_176085352             584 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Martelella sp. HB161492].
ACCESSION   WP_176085352
VERSION     WP_176085352.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008832
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..584
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=63924
     Region          188..513
                     /region_name="COG4782"
                     /note="Esterase/lipase superfamily enzyme [General
                     function prediction only]"
                     /db_xref="CDD:443812"
ORIGIN      
        1 mrlaqivlls flstcafvpf palaqqvspf dpvgfeitls gvtdpterlt lidaaiaqle
       61 adktpdlevy fdlsemrldl lraadqtlla akaaegladf atsrsaeidr nplpyldlaa
      121 alytkaeayr ealrvldkai dyrtnggqsg qpiadliark aeiatlrgdq asaerfrqma
      181 aaalkpveag arsadgeggf savnvfyatd rartgnndpa dfygygrgdl eygvvtvtip
      241 kqhvpgaiet psiwklefgp spakhvmvek vdpldvndyf srmnnelehr erkeivvfvh
      301 gfntrfdaaa kraaqlaydm dyrglpvlys wpsagqtmry vadtavvrls grrlayfled
      361 lrnrsgadti hivahsmgnr altdaleila lrngveegda plfgqvffaa pdvdaglfke
      421 mmktvhpiae rltlytshnd walvasrklh gdapragqgg atvatdqlfd tidmsdlged
      481 mlahtyfadd ssaladivsl iwknpppdvr cgmnrdmtet gqitwkyqkg gcfdkmmigm
      541 ishlwdqnsi tpadvsnlvg rlvvdkaeas alegrldtyi epqp
//
LOCUS       WP_176085461             315 aa            linear   BCT 11-JAN-2025
DEFINITION  endonuclease/exonuclease/phosphatase family protein [Martelella sp.
            HB161492].
ACCESSION   WP_176085461
VERSION     WP_176085461.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Dlakic,M.
  TITLE     Functionally unrelated signalling proteins contain a fold similar
            to Mg2+-dependent endonucleases
  JOURNAL   Trends Biochem Sci 25 (6), 272-273 (2000)
   PUBMED   10838565
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10789901
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..315
                     /product="endonuclease/exonuclease/phosphatase family
                     protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=33852
     Region          37..308
                     /region_name="YafD"
                     /note="Uncharacterized conserved protein YafD,
                     endonuclease/exonuclease/phosphatase (EEP) superfamily
                     [General function prediction only]; COG3021"
                     /db_xref="CDD:442257"
ORIGIN      
        1 mkaistllsa aalsaivlci ipifssswff sfiggmrlhl avfailvsll lvltgqwpys
       61 llplvaslam liylnlisar veqpatiaaa phklkviefn ifnantngae isaflrsaqa
      121 dvafilesda vaaripelae typyrlgcge ktktcdlmil srhpllegkv rsvggirdhr
      181 ymqakidlgg gssvsvvalh ltkpyyddah aeelrdaaql vstiegplil agdfnssila
      241 gdvqtflkql glhtaahepr twpisapslg laidhilvrp pahidsihri ednfgsnhyg
      301 lmadisvesq kpggn
//
LOCUS       WP_176085535             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176085535
VERSION     WP_176085535.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..359
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38334
     Region          1..357
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mstsiqlskv tkrfgsldvi rgidleirpg eftvfvgpsg cgkstllrmi agletisggd
       61 lliagtrmnd vmaskrgiam vfqsyalyph mtvyknlafg letaglkrde idrrvkeaae
      121 tlriseylsr rpkalsggqr qrvaigrsiv rdpniflfde plsnldaelr vqmrveiakl
      181 herlgntmiy vthdqveamt madrivvlks gqvmqvgtpl elyntpanqf vagfigspkm
      241 nflegtlgsd gtltvagttv rlsgaaagls aagetvtfgi rpehivlges agetlgearv
      301 elvehlggtt alhattstge sltvvapgqs kiahgdlipi gfdaenghvf skdgaalrh
//
LOCUS       WP_176085551             236 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Martelella sp. HB161492].
ACCESSION   WP_176085551
VERSION     WP_176085551.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..236
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=24785
     Region          54..148
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
ORIGIN      
        1 mnqtsaakfd adrageyarq srialagyda chalsacmls aalgagraar llvagaggta
       61 geiitaatle phwsfvavdp apamlelaka qiaganlser vtfveglvsd lqqsppfdaa
      121 imigvihhlp gdaakrails diaarlkpqa plvlagnvrp yasqpelmaa wanlwrlhgt
      181 adaeieekla rilqgaeppr seealaalln etgfgtplrf faslfwgawl iprdnd
//
LOCUS       WP_176085536             436 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Martelella sp. HB161492].
ACCESSION   WP_176085536
VERSION     WP_176085536.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..436
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=48633
     Region          1..345
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 mkyaivgtgs rhkmfrgava dtyadkndlv glcdinekrl alsalavdkg gngiatyrae
       61 qfgemideqk pntvivtvpd ylhhdyiida mrrgcdvmte kpmtidlskl kaildvqket
      121 grkvtvtfny rytpartqik dilmsgaigd vtavsfrwyl drvhgadyfr rwhryknqsg
      181 gllvhksthh fdlvnwwlgs sptnvtahgs rafyqpemak qmglsergpr cygcpvaekc
      241 dlrldlmade alrelyldae dedgylrdrc vfdeditied tmqvhatyan gamlnytlca
      301 yspweglevk fygtkgelsh rhvevhgvfg gerakaegse amtttlyvag kpaedlpvwe
      361 gagahggadp vmlgylfdpd mghdrygrgs thidgawsil tgiaanasie rnetvhidsf
      421 lsehgivlpk kewkfg
//
LOCUS       WP_176085555             621 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Martelella sp. HB161492].
ACCESSION   WP_176085555
VERSION     WP_176085555.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 621)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 621)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..621
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=67453
     Region          376..616
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mtithaaatp ireswsafrg svfcallpvi lttlllaalp hiitlplppg atvldhatie
       61 kagalpiavs lprswqlygt ppqasvtyhl efpasavper dpvlfipsfr qgvdarlngt
      121 llepqassff sterngsyyl aaipqqllha gsnsleisqk rvdgwisayl spvylttaga
      181 lqpyqkfydf iieqwraasl alqamimisv iamtllrprd rvfywfslmm lvsflstvag
      241 yllparetea mrlylglaqm tvslltigla lalaerprpa kltiaiialp vlllilgsqk
      301 llpipvvill aalmsigima lsstivlehy vrtrdwisgi iaipfglsil fglndmsmmf
      361 glgqgtrmls pyipavapla imsiltgrlv lslkqvdgan aslqrqmadq enelrrlhek
      421 drersaqail eqertrlmsd lhdglsghlv siiaqseksd adpgaigvsa realddlrlv
      481 vqsldlgddd lrvalasfqe rcgpqlrrig vqldwsteam ppvtgitpss alailrilqe
      541 avtnavkhgp atritiraqa ddkgaaiivv endirravpp sggyglsnmt krarsfgaei
      601 sfergakvar ltlhlpptlr p
//
LOCUS       WP_176085609             295 aa            linear   BCT 11-JAN-2025
DEFINITION  ParB/RepB/Spo0J family partition protein [Martelella sp. HB161492].
ACCESSION   WP_176085609
VERSION     WP_176085609.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..295
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=32481
     Region          38..291
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mndetskrrl grglaaligd iekpqttvse tpvihpdrqv piefvtrnpr nprryfeeee
       61 lrdlaasirq hgivqpvvvr tiaeqryeii agerrwraaq lsglaeipvl irdvddrtal
      121 eiaivenvqr adlnpleean gyealmaehg ytqndlgeii gksrshvans lrllklpegv
      181 rdllssgals agharalist pdplslarii vdkglsvrdt eklaqraieg gegrrssssa
      241 vekdadtlal erslgdilgl tvtidhkang gqikiayrtl dqlddichrl errpg
//
LOCUS       WP_176085621             390 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Martelella sp. HB161492].
ACCESSION   WP_176085621
VERSION     WP_176085621.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13024414
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..390
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=40783
     Region          18..384
                     /region_name="MFS_MosC_like"
                     /note="Membrane protein MosC and similar proteins of the
                     Major Facilitator Superfamily of transporters; cd17393"
                     /db_xref="CDD:340951"
     Site            order(28..29,32..33,36,68,118..119,121..123,126,145,
                     148..149,152,219,222..223,226..228,231,259,263,312..313,
                     317,321,337,340..341,344..345,348)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340951"
ORIGIN      
        1 mtefasiarp trymtkkrsa vsllflmngf ftgswapkip efaerlqlse salglmiltf
       61 gvgsiaampv tgiaiarfgs arvlktvals flpmlllitl vtsvplavii milfgstmam
      121 mdvsmngnav svekvehrsi msschafwsl ggligaalgg mliaaigvfg haiiatligg
      181 glialawknv tpdapeteak reklrlpltp lpwligimal fsmipegaim dwsalylkde
      241 rmvaiawsgf gfaafelamt amrfagdkvr drfgavstlr fcaamsvigl lmiglapsvp
      301 lvilgfaiag igisnmipia fsaagnlpgl apgiglsvtt tlgysgilva psaigfiaeh
      361 tgfapvyagl allhvvvfal aplarhadrg
//
LOCUS       WP_176085623             259 aa            linear   BCT 11-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Martelella
            sp. HB161492].
ACCESSION   WP_176085623
VERSION     WP_176085623.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..259
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26812
     Region          8..254
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mndilmrerq taimqrlsqd grviaadlaa dfavsedtir rdlrelsarg lcervyggal
       61 pvtpssgrlg rrdhensdvk allgraiaae impgmsvfld asstniaaar amadadvtlv
      121 tnapaiaaal dahaavtvim iggvihrsvg gavdakavse lsqfhfdlcv lgacgvdiea
      181 gvtcfhydda lfkraaaara drmiaavtad kiatraphav taltaldgli vdpaldgeaw
      241 aalrsagarl isagketap
//
LOCUS       WP_176085626            1066 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Martelella sp. HB161492].
ACCESSION   WP_176085626
VERSION     WP_176085626.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..1066
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=114211
     Region          38..1065
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 mkpqklgiag gltksfissp ltplfllaal algivalftl preeepqisv pmvdviveap
       61 glkaedavkl vtepletiik gindvehvys qtndnqvmlt arfkvgtpad savlrvhdkv
      121 manmsaipvg ipepsivgrt iddvaivalt ltpsadkgqd vtaadlsrva relqteltki
      181 ddvgltylvg etgdairiap dpeklalygv slqaltakvt aanrafstgt vrnsnmqidv
      241 magetlstpe eignllittn dgrpvyvrdv anvsfitnds daitanvsln adgsvdrvpa
      301 vtlavakrag anavtvadqi lhrvdelksr lipdtmsvav trdygetane kanellfhla
      361 latisiiilv aiaiglreal vvaivipvti lltlfaanim gytlnrvslf alifsigilv
      421 ddaiviieni arhwamkdgr srvgaaidav aevgnptiva tltvvaallp mmfvsgmmgp
      481 ymspipavas aamifsffva vmitpwlmvk iagtaklhne dahgggllgr ayaavarpil
      541 ktkfrawsfi aivviatfgs lslfytkhvt vkllpfdnks elqvtldlpe gssveetdav
      601 aqavaavvlk tpevvsvqth agtadpfnfn glvrhyymre qpqqgdvqin ltpkgersrt
      661 sheialdlrq qiladvsvpd gtslkvvepp pgppvmatll aeiygpdaqt rravaekvre
      721 afnsvpfivd vddsygqqtk rlrvtisgdd leyygvsedd vfdtlqalna tttvgyshrg
      781 ggrqpipiei arpkgdkvld esflatpvps sqsdgttsdv velgdvvkvt eeptsytifr
      841 hnghfadmvt gelagdfeap lygmlavqdv idkmdwgnlp kpviklhgqp edeaepvllw
      901 dgewevtwvt frdmgaafmv allgiyilvv aqfgsfkvpl viltpipltf igimaghwlf
      961 hapftatsmi gfialagiiv rnsillvdfi rhaksedvpl tetlieagai rfkpilltal
     1021 aaiigaavil adpifqglai sllfglisst lltvliipai yrvlrt
//
LOCUS       WP_176085643             323 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176085643
VERSION     WP_176085643.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..323
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34316
     Region          2..313
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 maflrnlnqe rivfaitiai falaslmlpg ffsaenlvai vrsisvlgil algmsiiiig
       61 rgidlsmvai mamtvawylq mlndgtpdgf alllalsgvi aiglingflv ayadvpaifv
      121 tlatasfvfg fvrsqlidtd avpvpdghwi efigslrfad vpievfifaa lafaafiflr
      181 fskwgryvyy agdnpeaarn agmpvrpmmv lryvlsaisa ftagiltags lqsintrvvn
      241 stllydivli aviggiglsg gkggvrnvlv gaaligimln amtildipll yqnliksail
      301 laaiiidgll nprdeqtaqq gdi
//
LOCUS       WP_176085650             339 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176085650
VERSION     WP_176085650.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 339)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..339
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36488
     Region          7..326
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 msdttplldv qglsvsfatd rgrvkaiddv sfsvskgeil sivgesgsgk svtlmsllgl
       61 ndrktsfveg avsfrgkhil empdrelrri rgagiglisq dpmtamtpvy tigwqiaeai
      121 rahenvskka araravella avglpnpdea vdryphqlsg gmrqramiam alacrpallv
      181 adepttaldv tvqaqvldll lrlrdefgsa iilithdmgv vaevadrvhv myagrmvekg
      241 ttedvferpm hpytvgllss ippltgpkla rlsaipgmpp tpenipagcg faprcpharq
      301 ecaarppirr dndhsalcvl ddketdamri awsnrmaea
//
LOCUS       WP_176085685             432 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter large permease [Martelella sp. HB161492].
ACCESSION   WP_176085685
VERSION     WP_176085685.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..432
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44844
     Region          6..431
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 msalavflfm iavlavllsl gfwvglalva tgitglflmg apniggligs tlfsainswp
       61 ltalplfllm geilfrskis edlfrglapl trrlpggllh vnilgsgila aivgssgvcc
      121 atvgrmslpe lkargyderm aigtltgsgt lgllippsim mivygistqt svarlflagv
      181 vpgllmvvlf mgyvaiwsli hrdrapvhpa geetrladla riaapvvlii avigsiyggl
      241 atptesaaig vagafllala qraltlktll esfmaavrss alimlimaga avlstalaya
      301 qipvkvaafv tamqlgpigl llaltvlyvv lgcflegvsm ivltasvvmp mvaavgidpv
      361 wfgifvviiv eiaqitppvg fnlfivqalt grdiatvtra slpflmlmla aivlitavpe
      421 lvlflpqtmi gq
//
LOCUS       WP_176085815              68 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF2065 domain-containing protein [Martelella sp. HB161492].
ACCESSION   WP_176085815
VERSION     WP_176085815.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..68
                     /product="DUF2065 domain-containing protein"
                     /calculated_mol_wt=7169
     Region          5..62
                     /region_name="yjeT"
                     /note="Uncharacterized conserved protein YjeT, DUF2065
                     family [Function unknown]; COG3242"
                     /db_xref="CDD:442474"
ORIGIN      
        1 mplrdivigl afflvieglv yalapslvka varripsvde gylrvvgvva vafgvglvwl
       61 vhirltgi
//
LOCUS       WP_176085456             465 aa            linear   BCT 11-JAN-2025
DEFINITION  SLC13 family permease [Martelella sp. HB161492].
ACCESSION   WP_176085456
VERSION     WP_176085456.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Pajor,A.M.
  TITLE     Sodium-coupled dicarboxylate and citrate transporters from the
            SLC13 family
  JOURNAL   Pflugers Arch 466 (1), 119-130 (2014)
   PUBMED   24114175
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Bergeron,M.J., Clemencon,B., Hediger,M.A. and Markovich,D.
  TITLE     SLC13 family of Na-coupled di- and tri-carboxylate/sulfate
            transporters
  JOURNAL   Mol Aspects Med 34 (2-3), 299-312 (2013)
   PUBMED   23506872
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Markovich,D.
  TITLE     Sodium-sulfate/carboxylate cotransporters (SLC13)
  JOURNAL   Curr Top Membr 70, 239-256 (2012)
   PUBMED   23177988
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11422084
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..465
                     /product="SLC13 family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015293 - symporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006811 - monoatomic ion transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=48900
     Region          91..461
                     /region_name="CitT"
                     /note="Di- and tricarboxylate antiporter [Carbohydrate
                     transport and metabolism]; COG0471"
                     /db_xref="CDD:440239"
ORIGIN      
        1 mlrkyltikh lvvlalflia lylvvsppdm ltkdqtltlg ivlvtlslwa tgivpgfmas
       61 llffavtlil klsppnvvls gftstaiwlv fsgsiiaatv rgsglgerlg ailgrhltgh
      121 yavlvsglfi ataalsfiip sslgrffvml piamalasra gfakgsnght aialtlilsa
      181 nmtgftilps nvpnlvlaga setihgitlt yasylalhfp vlgllkgvit vflvlhffpd
      241 rvgaplpeen qdvpasgpls arqwyaiail latlllwmtd smhginaawv glsaslllmv
      301 pgigairpen fdktvslsvl iftagilslg avinatglgt aiahglenal pltpgrdfln
      361 fmslalmafl tgmvttlpgv pavlaplaae lshltgfsvt avlmtqvvgf stvmlpyqaa
      421 plmvglqvtg qpvsrmirit lplslitiav llpldflwwk ligli
//
LOCUS       WP_176085830             273 aa            linear   BCT 11-JAN-2025
DEFINITION  creatininase family protein [Martelella sp. HB161492].
ACCESSION   WP_176085830
VERSION     WP_176085830.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Yoshimoto,T., Tanaka,N., Kanada,N., Inoue,T., Nakajima,Y.,
            Haratake,M., Nakamura,K.T., Xu,Y. and Ito,K.
  TITLE     Crystal structures of creatininase reveal the substrate binding
            site and provide an insight into the catalytic mechanism
  JOURNAL   J Mol Biol 337 (2), 399-416 (2004)
   PUBMED   15003455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..273
                     /product="creatininase family protein"
                     /EC_number="3.5.2.10"
                     /calculated_mol_wt=28936
     Region          4..256
                     /region_name="ArfB"
                     /note="Creatinine amidohydrolase/Fe(II)-dependent FAPy
                     formamide hydrolase (riboflavin and F420 biosynthesis)
                     [Coenzyme transport and metabolism]; COG1402"
                     /db_xref="CDD:441012"
ORIGIN      
        1 mkrywmelss pehaalpdnt lailpvaave qhgphlpvgt dclinnsiia amlkklgddv
       61 pavvlplqpv gasqehldya gslahpasdl mqswtrildc avrstglkrl lifnshggqs
      121 gllsvvaldq rvrhnilaay atwfdsgype glftddeirt gfhggdiets mmlalhpdlv
      181 amgraedfrs avdeiegkta qlsanpgggr vgglgwkaqd lhpdgvtgda srataekgrv
      241 lldhaatala alvgdltsve mpdgnwppaq yra
//
LOCUS       WP_176085833             367 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176085833
VERSION     WP_176085833.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 367)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..367
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38769
     Region          10..358
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 maekhapdhl viskvmknyg gaepalksvs lsvrkgefla llgpsgcgkt tllkiiagle
       61 katqgtmala gagldaiptf krdigivfqs yalfphmsvd anirfgldmr gikgqeaddr
      121 vaealdlvkl hglsarmpna lsggqqqrva laralvirpk lllldeplsn ldavlrksvr
      181 vdirelheri glttvmvthd qeeamsmadr vavmangyvl qhdspetiye qpasafvatf
      241 vgnppaillp vekaqdgglt lggaafapsa alrravdaap grslllglrs drlsfadaad
      301 dgtvsgevhs seyiggawlv hvalgehrla vpsrekppqf gapahiriad aapllfdakt
      361 gqkleaa
//
LOCUS       WP_176085874             283 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176085874
VERSION     WP_176085874.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 283)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..283
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30882
     Region          11..278
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mqlppyaspi eriwhysylv icgliffflv fpiiviipls fnaenfftft pkmleldpsg
       61 yslkhyvdff tnrdwqsalk nsvliapaat imattfgtla aiglsrahvp frgaimavli
      121 spmivpliis aagmyffysr igiqgtywgv vlahavlgtp fviitvtatl vgfdrslera
      181 aaslganpvi tffkvqmpli lpgvvsgalf afitsfdevv vvlfvgsasq ktlpwqmftg
      241 lreqisptil avasilvals vallcvleli rrrserqrgl tpg
//
LOCUS       WP_176085885             181 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Martelella sp. HB161492].
ACCESSION   WP_176085885
VERSION     WP_176085885.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008083
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..181
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=19908
     Region          10..146
                     /region_name="COG3865"
                     /note="Glyoxalase superfamily enzyme, possible
                     3-demethylubiquinone-9 3-methyltransferase [General
                     function prediction only]"
                     /db_xref="CDD:443074"
ORIGIN      
        1 mtdrpnsrlc iflkdgaeva arfyaatlpd ttvdhvqnir pnmamvfwtc matrymlmdg
       61 ndsfapkhdh sisiatldqs etdrlwdals aggsegrcgw lrdrfgvhwq iiptalahml
      121 sdpdrvaagr aqavmmgmkk iadadlpfag slrmlprrra rerqlplcgd ggtggassnr
      181 w
//
LOCUS       WP_176085889             299 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176085889
VERSION     WP_176085889.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 299)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 299)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..299
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=32899
     Region          12..298
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 mtdttvatye rtrpawlkpn lwwlvlpail fiilfflipv islflssfdk ampgqitfqg
       61 nfsldnyeri ftkslyymai wrsvwigavv savclfigyp lafiiartlk pgtatlltil
      121 vlssmqldmv irlyglmvlm gdkglinsgl malgiisepl plmynafgvi vglvqvtlpf
      181 mvlsligair sinpsleeaa rslgssrwhv mrtitwplsl pgvyagtllv falaissyvv
      241 palmggwkvi tlpihiyqqi aevgrwqfga avaailfits lfamglyila lrrnaggrv
//
LOCUS       WP_176085890             268 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176085890
VERSION     WP_176085890.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..268
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28703
     Region          8..260
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 medvnpipft frviaaiall vllvpvaivv laglnsgdyl tfppqgfslr wiknffvspt
       61 flpafklsfa lalatsiist vlgtlasifl trsvsrsref lraifflpvv lpgvvlgial
      121 yvfyiwsdvg larsltglii ghvlvtmpfv iatvtaslvd ldlsveeaar slgaspvqaf
      181 mkvtlplitp gisagsifaf ivsfgqfelt lflstpnlqt lplaiysslr yafeptaaaa
      241 gifaiclvtv stlistrlsn lkkllsrr
//
LOCUS       WP_176085895             361 aa            linear   BCT 11-JAN-2025
DEFINITION  DUF917 domain-containing protein [Martelella sp. HB161492].
ACCESSION   WP_176085895
VERSION     WP_176085895.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007525
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..361
                     /product="DUF917 domain-containing protein"
                     /calculated_mol_wt=38247
     Region          1..358
                     /region_name="COG3535"
                     /note="Uncharacterized conserved protein, DUF917 family
                     [Function unknown]"
                     /db_xref="CDD:442756"
ORIGIN      
        1 mreihpedle diavgaailg tggggdpyig kllarcaiee hgpvklisld elpddakvvt
       61 ggamgaptil iekipsgdem lmalhhyedv tgekvdalmp feagglnscl pivlaaqtgl
      121 plvdadgmgr afpqlemetf nvygvkaapv amadergnla mvetedaaka eflargicir
      181 mgghvsliny pmsgetakrv svpatislaq digrvlreak rakkpplatl ieflktthyg
      241 haevlgsgkv adiarkveng wsvgivtiap fdgsepysir iqnenlsler ngdviavvpd
      301 licvldidta eaipterlry gqrvnilgir vpeimrtpea lavfgpsafh idatyaplgg
      361 s
//
LOCUS       WP_176085915             325 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Martelella sp. HB161492].
ACCESSION   WP_176085915
VERSION     WP_176085915.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 325)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 325)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13673967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..325
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35805
     Region          36..164
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          <180..285
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mgnsvlselk gkapigrlis lprghqdlha mpvsagyeir tdssydwdgr rrgqspfsvi
       61 qytiaghgnl rfdnrefrlk pgdtmltcvp snhrywvedg gyweffwisl ngeeamriqq
      121 avlatsgpvl klsqttidgl atclgellsp rvetparasi iayetimlly ddvfgaraip
      181 avehramkrv vryidsnlss alpvdvlaev sglsrahfsr lfakaegmpp aefvllrrlr
      241 qatrllssag lsvkevaglt gfadpnyfak vfrryfrvsp tefrniglaa aimpfsgepm
      301 vhdetgleit diaetellpp gdasd
//
LOCUS       WP_176085998             415 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent RNA methyltransferase [Martelella sp.
            HB161492].
ACCESSION   WP_176085998
VERSION     WP_176085998.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455144
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..415
                     /product="class I SAM-dependent RNA methyltransferase"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0001510 - RNA methylation [Evidence IEA]"
                     /calculated_mol_wt=44118
     Region          4..412
                     /region_name="TrmA"
                     /note="tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD
                     family [Translation, ribosomal structure and biogenesis];
                     COG2265"
                     /db_xref="CDD:441866"
ORIGIN      
        1 msaetvtier lgsqgdgiar gpvfvpftlp geevmiarnk dhgtllalkt paperiapvc
       61 rhfgpdgtng tcggcslqhl gpegyrafkt alvtdalafh hidcpveplv eaapgerrra
      121 sfagrktetg ivfgfsspss hhivaieecp vllpslvarf safkllagil assaepfria
      181 vletatgldi afsglkkpse krrqaaikaa ltlkgiarls iddeilvepd kptlaidgva
      241 lvpppaafsq asitaeetma rlvlahlags krvadlfsgf gtfalrlare arvhavessa
      301 palgaldhaa rnqqglkpvs verrdlfrrp lmpqelkifd gvvfdpprag areqaeelar
      361 sivpkivavs cnpatlardl eilvaggyrv dsitpidqfl wsphveavac ltkqv
//
LOCUS       WP_176086045             267 aa            linear   BCT 11-JAN-2025
DEFINITION  DeoR/GlpR family DNA-binding transcription regulator [Martelella
            sp. HB161492].
ACCESSION   WP_176086045
VERSION     WP_176086045.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442564
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..267
                     /product="DeoR/GlpR family DNA-binding transcription
                     regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=29244
     Region          11..264
                     /region_name="GlpR"
                     /note="DNA-binding transcriptional regulator of sugar
                     metabolism, DeoR/GlpR family [Transcription, Carbohydrate
                     transport and metabolism]; COG1349"
                     /db_xref="CDD:440960"
ORIGIN      
        1 mtdennaeel lpaerrqqlv dwfknnkagt sqdlarmfsi svstirrdld llaseglvkr
       61 thggavsirs ratyepstdl arrtaleekq giarealrfi eadqallidt gavtchllad
      121 eianldlplt vitndlyvak vltykqnikl ivpggacrfg sfsllgepgl sfladircdl
      181 ffmsaaavde tcisetmlel vqlkramiea agkvillads srfmeralhk taaidkinii
      241 itdeglrqdd idkfpspgpt fikaams
//
LOCUS       WP_176086046             331 aa            linear   BCT 11-JAN-2025
DEFINITION  Gfo/Idh/MocA family protein [Martelella sp. HB161492].
ACCESSION   WP_176086046
VERSION     WP_176086046.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Taberman,H., Parkkinen,T. and Rouvinen,J.
  TITLE     Structural and functional features of the NAD(P) dependent
            Gfo/Idh/MocA protein family oxidoreductases
  JOURNAL   Protein Sci 25 (4), 778-786 (2016)
   PUBMED   26749496
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430574
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..331
                     /product="Gfo/Idh/MocA family protein"
                     /GO_function="GO:0000166 - nucleotide binding [Evidence
                     IEA]"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=35172
     Region          4..251
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
ORIGIN      
        1 meqklrwgil atggiaasft gdllasglsv taagsrsadk arafadrfgi akahgsykal
       61 vadpevdiiy vatphpqhaa aailaleagk hvlvekaftl nageaktlad larekdlvlm
      121 eamwtrflph miriheiids gligpvrsvq aehrqflptd pshrlnapel gggalldlgi
      181 ypvsfafdil gapeavsama rftgtgvdae iavnmrhagd amsssvsald cagpntaviy
      241 gekgrieids vwytpstfkv vdyagrliet ydgrvehrgm qfqafemerl iasgarsssr
      301 mpiaetvaim etldairaqi glsypgetpa a
//
LOCUS       WP_176086053             130 aa            linear   BCT 11-JAN-2025
DEFINITION  group II truncated hemoglobin [Martelella sp. HB161492].
ACCESSION   WP_176086053
VERSION     WP_176086053.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Keppner,A., Maric,D., Correia,M., Koay,T.W., Orlando,I.M.C.,
            Vinogradov,S.N. and Hoogewijs,D.
  TITLE     Lessons from the post-genomic era: Globin diversity beyond oxygen
            binding and transport
  JOURNAL   Redox Biol 37, 101687 (2020)
   PUBMED   32863222
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Bustamante,J.P., Radusky,L., Boechi,L., Estrin,D.A., Ten Have,A.
            and Marti,M.A.
  TITLE     Evolutionary and Functional Relationships in the Truncated
            Hemoglobin Family
  JOURNAL   PLoS Comput Biol 12 (1), e1004701 (2016)
   PUBMED   26788940
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Wajcman,H., Kiger,L. and Marden,M.C.
  TITLE     Structure and function evolution in the superfamily of globins
  JOURNAL   C R Biol 332 (2-3), 273-282 (2009)
   PUBMED   19281958
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Vinogradov,S.N., Hoogewijs,D., Bailly,X., Arredondo-Peter,R.,
            Guertin,M., Gough,J., Dewilde,S., Moens,L. and Vanfleteren,J.R.
  TITLE     Three globin lineages belonging to two structural classes in
            genomes from the three kingdoms of life
  JOURNAL   Proc Natl Acad Sci U S A 102 (32), 11385-11389 (2005)
   PUBMED   16061809
REFERENCE   5  (residues 1 to 130)
  AUTHORS   Wittenberg,J.B., Bolognesi,M., Wittenberg,B.A. and Guertin,M.
  TITLE     Truncated hemoglobins: a new family of hemoglobins widely
            distributed in bacteria, unicellular eukaryotes, and plants
  JOURNAL   J Biol Chem 277 (2), 871-874 (2002)
   PUBMED   11696555
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10201300
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..130
                     /product="group II truncated hemoglobin"
                     /GO_function="GO:0005344 - oxygen carrier activity
                     [Evidence IEA]"
                     /GO_function="GO:0019825 - oxygen binding [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=14790
     Region          10..128
                     /region_name="TrHb2_PhHbO-like_O"
                     /note="Truncated hemoglobins, group 2 (O);
                     Pseudoalteromonas haloplanktis PhHbO like; cd14773"
                     /db_xref="CDD:381282"
     Site            order(42..44,50,53..54,57,68,77,80..81,84,86,90..91,94,
                     119,122..123,126)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381282"
ORIGIN      
        1 mekletisly daiggeaavr rltkrfyelm dtlpeaqhcr aihpadlags eakfydyltg
       61 ylggpplyte khghprlrmr hmpapigpae rdewllcfrq algevvdnpr lydiilppie
      121 rlahhmqnkv
//
LOCUS       WP_176086058             538 aa            linear   BCT 11-JAN-2025
DEFINITION  APC family permease [Martelella sp. HB161492].
ACCESSION   WP_176086058
VERSION     WP_176086058.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Vastermark,A., Wollwage,S., Houle,M.E., Rio,R. and Saier,M.H. Jr.
  TITLE     Expansion of the APC superfamily of secondary carriers
  JOURNAL   Proteins 82 (10), 2797-2811 (2014)
   PUBMED   25043943
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Vastermark,A. and Saier,M.H. Jr.
  TITLE     Evolutionary relationship between 5+5 and 7+7 inverted repeat folds
            within the amino acid-polyamine-organocation superfamily
  JOURNAL   Proteins 82 (2), 336-346 (2014)
   PUBMED   24038584
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Schweikhard,E.S. and Ziegler,C.M.
  TITLE     Amino acid secondary transporters: toward a common transport
            mechanism
  JOURNAL   Curr Top Membr 70, 1-28 (2012)
   PUBMED   23177982
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Jack,D.L., Paulsen,I.T. and Saier,M.H.
  TITLE     The amino acid/polyamine/organocation (APC) superfamily of
            transporters specific for amino acids, polyamines and organocations
  JOURNAL   Microbiology (Reading) 146 (Pt 8), 1797-1814 (2000)
   PUBMED   10931886
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11425014
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..538
                     /product="APC family permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015171 - amino acid transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0006865 - amino acid transport [Evidence
                     IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=57019
     Region          3..439
                     /region_name="PotE"
                     /note="Serine transporter YbeC, amino acid:H+ symporter
                     family [Amino acid transport and metabolism]; COG0531"
                     /db_xref="CDD:440297"
ORIGIN      
        1 mamrreiglt gltfvavggv lgsgwlfapl dtaqmagpas liswligava mllialtyae
       61 iatlfpiagg laripqfshg rllalamgws awvgycttap ievkaslgya ssylpwltda
      121 sgnltvegml aaaaflavlt vvnlfgvtwf arlntsltwf klivplifiv vliasrfekg
      181 nfadaaaggf apfgtagifs avatggvvfa figfrhaidl agevrnsqrv iplalilsvl
      241 iclfvyiglq iafigaqspa disggwakle aahhlgplga latslgilwm vsllnvaaii
      301 spagsglvst ssnarlalam snngvfprli arlnvfgvpa walllnyvia lamlillpfn
      361 ailalngsav vlsfiagpvs mvafrmlvpe ahrpfrvpav ktlggaafvi atlmiywsgw
      421 stmwlldlll avgaalfflr lafigredle pqsaiwfgiy mvgltvlsyf ggygggigvv
      481 phpldstiag vfglvmffma vkgritqdvf nrfiheqkvy ereeygradv enqivgrr
//
LOCUS       WP_176086086             859 aa            linear   BCT 11-JAN-2025
DEFINITION  DNA translocase FtsK [Martelella sp. HB161492].
ACCESSION   WP_176086086
VERSION     WP_176086086.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Jean,N.L., Rutherford,T.J. and Lowe,J.
  TITLE     FtsK in motion reveals its mechanism for double-stranded DNA
            translocation
  JOURNAL   Proc Natl Acad Sci U S A 117 (25), 14202-14208 (2020)
   PUBMED   32513722
REFERENCE   2  (residues 1 to 859)
  AUTHORS   Crozat,E., Rousseau,P., Fournes,F. and Cornet,F.
  TITLE     The FtsK family of DNA translocases finds the ends of circles
  JOURNAL   J Mol Microbiol Biotechnol 24 (5-6), 396-408 (2014)
   PUBMED   25732341
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447545
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..859
                     /product="DNA translocase FtsK"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_process="GO:0007059 - chromosome segregation [Evidence
                     IEA]"
                     /GO_process="GO:0051301 - cell division [Evidence IEA]"
                     /calculated_mol_wt=92592
     Region          <70..202
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          327..855
                     /region_name="FtsK"
                     /note="DNA segregation ATPase FtsK/SpoIIIE or related
                     protein [Cell cycle control, cell division, chromosome
                     partitioning]; COG1674"
                     /db_xref="CDD:441280"
ORIGIN      
        1 mplsrfpsln snpadsgktd dralaerree eaqnasnavi ldpdklptwq rpfvlapnvr
       61 ftrtpsqtyp apqirpegpa raphtpqmla pnadaaavps irdttagpaa elraapspas
      121 dlqrriaral seepatvsaa pqppapsrra vdflshpldr teithaatet adapepeqvs
      181 katateapsa fgfisdalvw emmglgilde atpvattapa aadaiaaeta aaqsvddvpa
      241 daeddtqadd glespspval yrqitprllp eqspdteaqm adtddvaadp iasddqtemd
      301 aetdgdaeae stmtaahdae tasdtvaeae pidipvpvpa rrlalkhrdr stedylfpsi
      361 dllqsprpnp aaemsqehle qsagllenil edfgvkgeii dvrpgpvvtl yefepapgvk
      421 ssrvinlsdd iarsmsalsa rvavipgrnv igielpneer etvylrelfe srsyvgtdfr
      481 lplclgktig gepvvaelak mphllvagtt gsgksvaint milsliyhlr pdecrlimvd
      541 pkmlelsvyd giphlltpvv tdpkkavlal kwavremeer yrkmsrlgvr nidgfnerva
      601 earakgetim lsvpsgfdks tgeqtfeeqe ldltalpfiv vivdemadlm mvagkeiegt
      661 iqrlaqmara agihlimatq rpsvdvitgt ikanfptris fqvttkidsr tilgeqgaey
      721 llgqgdmlhm kgggrisrvh gpfvsdneve kivahlktqg spsylgsvtt deedsgdaed
      781 dtavfdntdm gsgsddgddl yeraikivqr dkkcstsyiq rrlsigynra aslvermeqd
      841 glvgpanhvg kreilepgn
//
LOCUS       WP_176086096             513 aa            linear   BCT 11-JAN-2025
DEFINITION  tripartite tricarboxylate transporter permease [Martelella sp.
            HB161492].
ACCESSION   WP_176086096
VERSION     WP_176086096.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..513
                     /product="tripartite tricarboxylate transporter permease"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=53388
     Region          3..496
                     /region_name="COG3333"
                     /note="TctA family transporter [General function
                     prediction only]"
                     /db_xref="CDD:442562"
ORIGIN      
        1 msldvigqal dialqpnvli alvlgaiygl figalpglta tmstallvpv tfymapvpai
       61 alivsstama itagdipgal mrvpgtpasa aytdeafrmt lkgkagkvls lgfffsalgg
      121 ltgalvllvt gpllakisln fssfeffwla vlglltcalv sgndaarglt sllfgllist
      181 vgldittgap rftfgsmdlm ggvsyipvmi gmfafseilr gfttnqhgng gempalgkiv
      241 pfkgvlgllk kypfsfirga slgtvvgalp giggdlaawi aygmskrlsk tpekfgtghp
      301 eglieatssn naglssawip alvfgipgda vtaiavgvlf mkgvnpgprl fvenpsmpta
      361 iimtffisnl llfplgfvai klarhvlavp rnvivpiili ccflgsyavn nslfgvwiml
      421 aagvvgyime rngfpiapvi lglvlgpvle rnfimsmqia ngnllaffyr piacglgiai
      481 iailvatavr siltyrrage pvpdkkelad eal
//
LOCUS       WP_176086155             512 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Martelella sp.
            HB161492].
ACCESSION   WP_176086155
VERSION     WP_176086155.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 512)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   5  (residues 1 to 512)
  AUTHORS   Tam,R. and Saier,M.H. Jr.
  TITLE     Structural, functional, and evolutionary relationships among
            extracellular solute-binding receptors of bacteria
  JOURNAL   Microbiol Rev 57 (2), 320-346 (1993)
   PUBMED   8336670
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11433522
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..512
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=55311
     Region          41..505
                     /region_name="DdpA"
                     /note="ABC-type transport system, periplasmic component
                     [Amino acid transport and metabolism]; COG0747"
                     /db_xref="CDD:440510"
ORIGIN      
        1 mkslllsttf avalalgaah gtfaagtdti vigtdvdagt ldprltrdtt aqrtanliys
       61 glvdlsssle pkpelaaswe spdpttiifh lrpdltfsdg spltaddvvy tyqtildpdf
      121 napqrtlytp isaveavdpq tvkftlsapy apllsyldmg ivskaaaegg rdlatnplga
      181 gpmklvawnr gsdieleknd nywgaapkva dakiqiiadn tsraqaleag dldaiqspls
      241 pqdikrlesd drfgnaimpg lgvtylnfnv sdpmlsdpem rqafamlvdq dtivnqiyqg
      301 vdavatsvlm ptswayspdi kqpafnvega vakfnelgwk dtngdgildk dgkplkitls
      361 thsedpnrvq sveylqavfq sagidaevni sdwptfstny vqkgehqial lgwlnivdpd
      421 rllyaqlttn gstnwggysn pevdkllneg rssldqsvrt eayqkaaail akdlpyyiis
      481 dqgyqlfysk diaypvvanp rgtfrgligi gq
//
LOCUS       WP_176086156             346 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Martelella sp. HB161492].
ACCESSION   WP_176086156
VERSION     WP_176086156.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448193
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..346
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=37752
     Region          8..121
                     /region_name="YhcF"
                     /note="DNA-binding transcriptional regulator YhcF, GntR
                     family [Transcription]; COG1725"
                     /db_xref="CDD:441331"
ORIGIN      
        1 mfsieassid kslpvpvgtq lhglmsytla fgniphgtkl psvrqlandl giapmtvaev
       61 ykklrdagqv emrpglgays vlgahhknrd alpidelrhd iahliekaes fglstmslvs
      121 minaqarlpk aeaaldiifv cifegpgrdy veelkpvfap qdhvrlvsld llgksqewre
      181 acekadivlt flhreaevrs htpkanvlgl hfipsqqtrq nlagldprah iaavthfkey
      241 iaimrpsvre faphvsdiav twssapdlke tlarcdavvf asgadevatl aapgafcfey
      301 rhapdpghie svltpqlall rrqhmsteia ephspqekav asalrs
//
LOCUS       WP_176086194             365 aa            linear   BCT 11-JAN-2025
DEFINITION  microcin C ABC transporter permease YejB [Martelella sp. HB161492].
ACCESSION   WP_176086194
VERSION     WP_176086194.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 365)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467933
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..365
                     /product="microcin C ABC transporter permease YejB"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0042884 - microcin transport [Evidence
                     IEA]"
                     /calculated_mol_wt=40065
     Region          1..365
                     /region_name="YejB"
                     /note="ABC-type microcin C transport system, permease
                     component YejB [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4174"
                     /db_xref="CDD:443333"
ORIGIN      
        1 mgsyilrril lmiptligim aisfivvqfa pggpveqvia qlngqaggae erisggsdag
       61 msmdnfdggg ssqyrgaqgl dpelikklek qfgfdkpplt rfllmmrdya tfdfgdsffr
      121 ntsvidliie klpvsislgv wililsygis iplgiakavr dgsrfdvwts avvvvgyavp
      181 sflfgilliv lfaggsffdl fplrglvsdd faslswwqki ldylwhitlp iialsvsafa
      241 tttlltknsf ideikkqyvv tarakglser qvlyghvfrn amliviagfp gafisafftg
      301 sllienifsl dglgrlgyls vvnrdypvvf gtlyifslig livglisdli ytwidpridf
      361 ekrdv
//
LOCUS       WP_176086196             535 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176086196
VERSION     WP_176086196.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 535)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..535
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=58322
     Region          1..530
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 mtdtpllsvr dlsvafgtsl avdhvsfdiq pgevlalvge sgsgksvtan svlkllpypa
       61 ashpsgeilf egedlltvsd rrlrqvrgaa itmvfqepmt slnplqtiek qvgevlalha
      121 gltgpkarer vltlmnevgi rdaekrlsay phelsggqrq rvmiamalan rpklliadep
      181 ttaldvtvqa qilkllkklq reygmsllfi thdlgivrkf adrvcvmtgg kivergpvae
      241 ifdnpqhdyt rhllaaepkg dppphdpqrp vvvaaddvkv wfpvksgflr kvvdhvkavd
      301 gislqlrage tlgivgesgs gkttlglalt rmiasegria figqdidgfs fkamkpyrnr
      361 mqivfqdpyg slsprmsvge iiaeglkihe tslsaaerda rvcaaleevg lsaatrwryp
      421 hefsggqrqr iaiaramvlk prfvmldept saldmsvqaq vvdlladlqk khdlaylfis
      481 hdlkvvrala neivvmrfgk vvergpaaev fqnpkadytk sllaaafdie pvean
//
LOCUS       WP_176086201             256 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176086201
VERSION     WP_176086201.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..256
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27206
     Region          3..242
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 msifsvkdlt valggttilk dvsvdvghne ligligpnga gkstllksml gliphkgsir
       61 llgddvstmg fdqrarsvay lpqeheiawp vtvrhvvalg rqpfesghpf gdfesgrvis
      121 damvrmgish lagrvatsls ggekarvlia ralaqttpll vadepaagld pahqiglmkv
      181 frdltresrs vitsmhdlnl aarwctrlil lskgrivadg rpedvltaar laevygirar
      241 ieagkdglai tildla
//
LOCUS       WP_176086289             365 aa            linear   BCT 11-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Martelella sp.
            HB161492].
ACCESSION   WP_176086289
VERSION     WP_176086289.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..365
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=38981
     Region          8..267
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mtgriarmlr rlpltllalt vmaqlpaaga sanpyivvda ktqrvlfade afkrwypasl
       61 tklmttylvf edlvagrlrl dtpitvsaaa aneapskmyf spgtritlds alkmmlvhsa
      121 ndaakavaen epggeqafva rmnataaslg mnsthfvnan gmpkdgqytt ardmaalama
      181 lqknfpqfay ffdipgisad sgryrntnll lstfdgatgm ktgyicaagy nqvstaqrdg
      241 hsvvsvvlga ssipdrtets arllqsgltv asengpllsa frpgpdvdkt vadisstmct
      301 peaiqarigv idedgnypln spylkplped yttvpakrlp ndtdmaaael dqlktiplpy
      361 arpaq
//
LOCUS       WP_176086305             602 aa            linear   BCT 11-JAN-2025
DEFINITION  glycoside hydrolase family 2 protein [Martelella sp. HB161492].
ACCESSION   WP_176086305
VERSION     WP_176086305.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Sun,J., Wang,W. and Hao,J.
  TITLE     GH2 family beta-galactosidases evolution using degenerate
            oligonucleotide gene shuffling
  JOURNAL   Biotechnol Lett 45 (5-6), 655-665 (2023)
   PUBMED   37071382
REFERENCE   2  (residues 1 to 602)
  AUTHORS   Domingues,M.N., Souza,F.H.M., Vieira,P.S., de Morais,M.A.B.,
            Zanphorlin,L.M., Dos Santos,C.R., Pirolla,R.A.S., Honorato,R.V., de
            Oliveira,P.S.L., Gozzo,F.C. and Murakami,M.T.
  TITLE     Structural basis of exo-beta-mannanase activity in the GH2 family
  JOURNAL   J Biol Chem 293 (35), 13636-13649 (2018)
   PUBMED   29997257
REFERENCE   3  (residues 1 to 602)
  AUTHORS   Davies,G. and Henrissat,B.
  TITLE     Structures and mechanisms of glycosyl hydrolases
  JOURNAL   Structure 3 (9), 853-859 (1995)
   PUBMED   8535779
REFERENCE   4  (residues 1 to 602)
  AUTHORS   Henrissat,B., Callebaut,I., Fabrega,S., Lehn,P., Mornon,J.P. and
            Davies,G.
  TITLE     Conserved catalytic machinery and the prediction of a common fold
            for several families of glycosyl hydrolases
  JOURNAL   Proc Natl Acad Sci U S A 92 (15), 7090-7094 (1995)
   PUBMED   7624375
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674. doi:
            10.1073/pnas.93.11.5674. PMID: 8643635]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461541
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..602
                     /product="glycoside hydrolase family 2 protein"
                     /EC_number="3.2.1.-"
                     /GO_function="GO:0004553 - hydrolase activity, hydrolyzing
                     O-glycosyl compounds [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=68851
     Region          64..>588
                     /region_name="LacZ"
                     /note="Beta-galactosidase/beta-glucuronidase [Carbohydrate
                     transport and metabolism]; COG3250"
                     /db_xref="CDD:442481"
ORIGIN      
        1 mlersaiaen alqalhdedy drpfnlqnln hetmifmggr dvisldgewn fcvdlldtgl
       61 rqkwfamdpa dpcdrqepwd ydpymgetvp vpscwqmlqe kwyffegsaw ytravdftpk
      121 adkrfflrvg aaqydckvfl ngqfignhyg gstpffaelt dqlqqgrnwl mlcvnnvrtt
      181 drvpmrntdw fnyggvyrev slietpktli rdlfvrlnpd plvndidvsi aaegadyarf
      241 eiaelgiavd ipleggkgta sipaapllws pdrpklydvv ltaggdrvcd rigfrrierr
      301 grelflngrp lwlrgisvhe ddavlgkvvt eddlrrryad akqlgcnyvr lahyphhera
      361 valadeigll lwteipvywa idfdnpatlr daenqllemv krdrnrasvv iwsvgnenpd
      421 tdqrlafmrh ladtarandp trliaaaclv nhhklkiedr laahldiigi neyygwyded
      481 fselpkilan sqpdrpvvvs etgadadisd kgpkaglfse tyqaevyrsq iatlkeldfv
      541 rgmspwilyd frterrqgiy qrgfnrkgli aadkatrkea failasfyha maereakewe
      601 tl
//
LOCUS       WP_176086349              80 aa            linear   BCT 11-JAN-2025
DEFINITION  Lrp/AsnC family transcriptional regulator [Martelella sp.
            HB161492].
ACCESSION   WP_176086349
VERSION     WP_176086349.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Unoarumhi,Y., Blumenthal,R.M. and Matson,J.S.
  TITLE     Evolution of a global regulator: Lrp in four orders of
            gamma-Proteobacteria
  JOURNAL   BMC Evol Biol 16 (1), 111 (2016)
   PUBMED   27206730
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Deng,W., Wang,H. and Xie,J.
  TITLE     Regulatory and pathogenesis roles of Mycobacterium Lrp/AsnC family
            transcriptional factors
  JOURNAL   J Cell Biochem 112 (10), 2655-2662 (2011)
   PUBMED   21608015
REFERENCE   3  (residues 1 to 80)
  AUTHORS   Yokoyama,K., Ishijima,S.A., Clowney,L., Koike,H., Aramaki,H.,
            Tanaka,C., Makino,K. and Suzuki,M.
  TITLE     Feast/famine regulatory proteins (FFRPs): Escherichia coli Lrp,
            AsnC and related archaeal transcription factors
  JOURNAL   FEMS Microbiol Rev 30 (1), 89-108 (2006)
   PUBMED   16438681
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445815
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..80
                     /product="Lrp/AsnC family transcriptional regulator"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /calculated_mol_wt=8815
     Region          <3..74
                     /region_name="Lrp"
                     /note="DNA-binding transcriptional regulator, Lrp family
                     [Transcription]; COG1522"
                     /db_xref="CDD:441131"
ORIGIN      
        1 mqtifvqfkc lsgaaydvad livrsleets eiystsghyd llakfylpkd adighfvtsk
       61 lqtiegvkdt ftlvtfkafa
//
LOCUS       WP_176086360             260 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176086360
VERSION     WP_176086360.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 260)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..260
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27604
     Region          20..255
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mraerlatll tlaavllfli gpfvvivmag lssgnnlafp ppglslkwvy kvftidsfra
       61 sfgvsmflai fgtlaalilg vpaayalsry kvpgaeavrl ivsspiivpg iivglallry
      121 fvvplqlkvs lalfcahtal iipyavrvvs aslqnlrsdi eeaavllgas rvgaffrvil
      181 pnirggvlsa filgfvtsfn qvpvslflsg pgihtlpvdm lgymettydp siaalsalla
      241 flsigivmia erflgftryv
//
LOCUS       WP_176086368             170 aa            linear   BCT 11-JAN-2025
DEFINITION  Dps family protein [Martelella sp. HB161492].
ACCESSION   WP_176086368
VERSION     WP_176086368.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Ren,B., Tibbelin,G., Kajino,T., Asami,O. and Ladenstein,R.
  TITLE     The multi-layered structure of Dps with a novel di-nuclear
            ferroxidase center
  JOURNAL   J Mol Biol 329 (3), 467-477 (2003)
   PUBMED   12767829
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: at the crossroads of iron and oxygen metabolism
  JOURNAL   J Nutr 133 (5 Suppl 1), 1549S-1553S (2003)
   PUBMED   12730463
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Grant,R.A., Filman,D.J., Finkel,S.E., Kolter,R. and Hogle,J.M.
  TITLE     The crystal structure of Dps, a ferritin homolog that binds and
            protects DNA
  JOURNAL   Nat Struct Biol 5 (4), 294-303 (1998)
   PUBMED   9546221
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   5  (residues 1 to 170)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002504
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..170
                     /product="Dps family protein"
                     /EC_number="1.16.-.-"
                     /GO_function="GO:0008199 - ferric iron binding [Evidence
                     IEA]"
                     /GO_function="GO:0016722 - oxidoreductase activity, acting
                     on metal ions [Evidence IEA]"
                     /calculated_mol_wt=18613
     Region          16..170
                     /region_name="Dps"
                     /note="DNA-binding ferritin-like protein (oxidative damage
                     protectant) [Inorganic ion transport and metabolism,
                     Defense mechanisms]; COG0783"
                     /db_xref="CDD:440546"
ORIGIN      
        1 manvaavlkp kshestmqtg lseqyrsdma dqlsnilaat yrltikthiy hwnvvgplfr
       61 slhelteehy nalfaatdii aeriraigfl apetvsasng fapdgktiss lsadamvrdl
      121 isehetavrq mreagaaage agdlvtedml tqrltfheka lwmlraiisd
//
LOCUS       WP_176086384             267 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176086384
VERSION     WP_176086384.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..267
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28486
     Region          1..253
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mrrngafatl fnllfaafml apiivvigva ftptgylefp psgisfrwfr aildnpefie
       61 aavnslelgv laaclativa vpaalaldrg rfsgrealla flmsplmvpt vvlgiaflrf
      121 ltliglngtf sglvichavv itpyvlrlvl asltgldrtv ekaaislgas hwtvfyritl
      181 psilpgivgg wvlafitsfd evtvtifivn pstttlpvrl fshiaqttdp lvasvsavav
      241 lftigvmvlv drlygldkll igegkhv
//
LOCUS       WP_176086385             286 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176086385
VERSION     WP_176086385.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 286)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..286
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31051
     Region          10..284
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 msalskqghw flsapalilf avfllaplvm tfilsfhqfd fyggiddsys lknyadvlgd
       61 syfyeifgrt fgialattff civigvpasy flnrmrpaar svmilvvlgp llisvvvrtl
      121 gwaiilgnkg vinnflmnig lierpikmmy tsggivlalv hvmipfmvla vwaalqrqdp
      181 steaaaeslg aspltifwri vlpqavpgvl sgslivfsls asafatpail ggrrvkvvat
      241 avhdefmntl nwplgaaiam llmvailvvm vawnrlvenr fgraya
//
LOCUS       WP_176086389             185 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease [Martelella sp. HB161492].
ACCESSION   WP_176086389
VERSION     WP_176086389.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..185
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21206
     Region          74..133
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mtiavspqal palvlnadyr plsyyplslw swqdaikavf ldrvniiaey dqevsspsfs
       61 mklpsvvclk hyikpsrnpa ftrfnvflrd rfqcqycgsr deltfdhvip rcrggettwd
      121 nvvaacspcn lkkgsklpkq agmiphqrpf qptvqdlhnn grlfppnflh eswidylywd
      181 selep
//
LOCUS       WP_176086392             304 aa            linear   BCT 11-JAN-2025
DEFINITION  YihY/virulence factor BrkB family protein [Martelella sp.
            HB161492].
ACCESSION   WP_176086392
VERSION     WP_176086392.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Callahan,C. and Deutscher,M.P.
  TITLE     Identification and characterization of the Escherichia coli rbn
            gene encoding the tRNA processing enzyme RNase BN
  JOURNAL   J Bacteriol 178 (24), 7329-7332 (1996)
   PUBMED   8955422
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003440
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..304
                     /product="YihY/virulence factor BrkB family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=33769
     Region          3..272
                     /region_name="BrkB"
                     /note="Uncharacterized membrane protein, BrkB/YihY/UPF0761
                     family (not an RNase) [Function unknown]; COG1295"
                     /db_xref="CDD:440906"
ORIGIN      
        1 mkkpvrtalr vaydalyhfs eddgwamash valstllamf pfvifgtala gflgadqfad
       61 aavnliltsw pkeiaqpvae qirqvltvpr gglltvsvla aayfasngve avrlslnray
      121 rveenrswww lrmkslgyvv msviifvfls fmlvavpial hfaerwfpwl egllqtlssn
      181 riagtlivlf lglmiahlnl aagkrrlidv lpgvvltlvf wavfayvfty ylanfaqysa
      241 tyaglatpmi llvflytvgv illlgaeina allkynvikd apwathverr prrsepaktp
      301 dver
//
LOCUS       WP_176086396             249 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit beta/FixA family protein
            [Martelella sp. HB161492].
ACCESSION   WP_176086396
VERSION     WP_176086396.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..249
                     /product="electron transfer flavoprotein subunit beta/FixA
                     family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26429
     Region          1..248
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
ORIGIN      
        1 mkilvpvkrv vdynvkirvk adgtgvelan vkmsmnpfde iaveealrlk eagkadevvv
       61 vsigpakaee tlrtalamga drgiliatdd tveplavakl lkavaldedp glvilgkqai
      121 dddanqtgqm lsaligwaqa tfvskleldg dtatvtreid gglqtikvsl paiitadlrl
      181 nepryaslpn imkakkkpvd kktpedfgvs taarlevlkt eepatrkagi kvanaaelvd
      241 klkneagll
//
LOCUS       WP_176086407             238 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Martelella sp. HB161492].
ACCESSION   WP_176086407
VERSION     WP_176086407.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..238
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=26910
     Region          5..185
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(8,10,93)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(40,92..93)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            91..93
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 mklaiiipsy nesqnipliv srlretigqr sdvevilvdn gstdnsqqvl aaelnekdfi
       61 rsihvpvnqg ygygilsgla asdadvlawt hadmqtdpyd vikafdllsa qadakiivkg
      121 krqnrkklee fftfgmqlva smvlgvhlsd vnaqpkvftr pfyetfvker aphdfsldlf
      181 llyqavtngy kilevpvffa errfgeakgg gnwktrikli rrtfayifef rdslrkqd
//
LOCUS       WP_176086429             173 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter small permease [Martelella sp. HB161492].
ACCESSION   WP_176086429
VERSION     WP_176086429.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 173)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..173
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=19892
     Region          1..156
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 marltavyrw fgrraenlla lllaslfvaf llqivfryll nlpvgwtvew vtiawlwgil
       61 fgyafviret diirldiiys acprgmrraf dvisggiiaa ifiyslvptw dyitfmsier
      121 taylripfsy vfaiympfaf svivrsllmv waglsgsgrr hdtehsaesh dyd
//
LOCUS       WP_176086430             431 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter large permease [Martelella sp. HB161492].
ACCESSION   WP_176086430
VERSION     WP_176086430.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..431
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=45392
     Region          6..429
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mtdpfalcli iivvlslmga svgiamvags ivylgmagfd psiasetllq glfnsytlla
       61 iplfilaadi mnmgsladrl lafsqalvgr frgglghvnv vssvifsgms gsaiadavgm
      121 griiinmmtk dgrypasyaa aitaatatvg pvippsipmv lyalvsdqsi sylfaagllp
      181 gllmalvmav mnftiarrrn fpvdevvpir klpgitwral palmlpvill ggiyggittp
      241 teaaavaafy alfvsvvvyr svrfgdfyya llgsakstas vgvlvagait fnyvitrenl
      301 pdtisafiah yhfsqvgfli ainvlllllg mfleggaill iivpiliptv qamgidlvhf
      361 gvivvvntmi glitppygll lfvtanitke pisaiirdvv pfiialival giitfspdfv
      421 lflprllgyq g
//
LOCUS       WP_176086462             251 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Martelella sp. HB161492].
ACCESSION   WP_176086462
VERSION     WP_176086462.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..251
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27152
     Region          4..251
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mpiiqsvqra lmilnlfdee npemkitdia arldlhkstl hsilktlqme gyieqnheng
       61 ryrlgmklve rgtfvinsld lrkragpala alsqatgetv hlgilegkng vyidkvdgsr
      121 aligysrigr slpihctaig kvllafrpte evwsllggyd ftaftertit aaepfvaals
      181 tvraeglald deehsrgvrc maapvfdhdk kvvaavsist ltsvtdsaaf arliaplkqa
      241 saaislalgd r
//
LOCUS       WP_176086471             337 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Martelella sp. HB161492].
ACCESSION   WP_176086471
VERSION     WP_176086471.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Conserved domains of glycosyltransferases
  JOURNAL   Glycobiology 9 (10), 961-978 (1999)
   PUBMED   10521532
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135621
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..337
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37150
     Region          8..196
                     /region_name="DPM1_like_bac"
                     /note="Bacterial DPM1_like enzymes are related to
                     eukaryotic DPM1; cd04187"
                     /db_xref="CDD:133030"
     Site            order(11,13,102)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133030"
     Site            order(48,101..102)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133030"
     Site            100..102
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133030"
ORIGIN      
        1 msartlsivv pvyneaanla nlvsrlnmla aklaqdhgle vsyifvddgs rddsyqmlag
       61 ldfqgnparm lqfsrnfgke aalsagidas vgadatifmd adlqhppelv vemveiwlrd
      121 dvdsvytyks drlaseglar svfsrmfykt mnrggryqli egagdfrlvn rrfadalrrl
      181 peserfmkgl yawvgftqrg ipltpppreh gvssfntlrl ltmsfdalts fttaplrlma
      241 ltgvfialls gfygvyivle rlffessgig issiltlvsf fggvqmiflg llgeyvgkav
      301 leakrrpcyi iaedrtiavs kpgatpepke ecragqd
//
LOCUS       WP_176086478             516 aa            linear   BCT 11-JAN-2025
DEFINITION  tripartite tricarboxylate transporter permease [Martelella sp.
            HB161492].
ACCESSION   WP_176086478
VERSION     WP_176086478.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Winnen,B., Hvorup,R.N. and Saier,M.H. Jr.
  TITLE     The tripartite tricarboxylate transporter (TTT) family
  JOURNAL   Res Microbiol 154 (7), 457-465 (2003)
   PUBMED   14499931
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007232
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..516
                     /product="tripartite tricarboxylate transporter permease"
                     /GO_component="GO:0042597 - periplasmic space [Evidence
                     IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=53292
     Region          1..501
                     /region_name="COG3333"
                     /note="TctA family transporter [General function
                     prediction only]"
                     /db_xref="CDD:442562"
ORIGIN      
        1 mdtlsavmng fsvaltfenl slallgcflg tiigalpglg psngvailip laftlglpat
       61 palilltsvy fgamyggris sillnipgde pavmttldgy pmamkgqage alaisglasf
      121 vgsfaaicgl avlapqlvkv allfgpaeyf alyvlafatl ggitsrnqak salaaalglg
      181 vamigidqqt gvprltfgqm hlydgidflv aivglfalse vftflehhgs kvdtaghgsk
      241 pvvigrivpr lsmivqtsgs mvrgtvigfl agvlpgagas lgsflaygae knlknrddtf
      301 gkgdprgvaa peagnnaaag galvpmlalg vpgsgttavl lamllalnvt pgpllftknp
      361 dvvwgliaal mlanvmllll nipmvgmfvr illipskylm ptvamvsfvg iygisgsvfd
      421 lsvmvafglv gwllrkldvp lvpvimgvll gnqmevnlrr amtisdgdws alfasplaig
      481 lwivavagfv lpiilnmtkr rnrvlmthne elaegd
//
LOCUS       WP_176086483             371 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176086483
VERSION     WP_176086483.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 371)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..371
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=39329
     Region          19..364
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mlsasptkna gtagivkpet pllqgvavhk eygtvhavrg idfaieansy vtllgpsgcg
       61 ktsllrmigg feeissglie ldgrslagtp aakrpvntvf qnyalfphls vrenvgfgla
      121 yrrlakaeia ervdgalamv qmeamaerrp rqlsggqqqr valaraivnq prillldepl
      181 saldrrmrkd mqielkdlqr rlgmtflhvt hdqeeafals dhiivmndgr ieqqgapaei
      241 yrrpqnayva dfigganlva griadlaagg atiktvaglf fcpsvsglav gdaavltlrp
      301 eqvrlsddga iaatvthtvf rgsewlvetv ladgtalslt tsadeapvag sqvalgfdpa
      361 rgwiaaagrg d
//
LOCUS       WP_176086501             356 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Martelella sp.
            HB161492].
ACCESSION   WP_176086501
VERSION     WP_176086501.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..356
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=37726
     Region          36..356
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mmnritygal gvkiaalliw avllfapflf qdvralevaa rvlifialva sydlligytg
       61 ivsfahtmff gfgaygvaia lkhygpgwae valgalaglv vsaivaaaig llslrvkaif
      121 famitlaags vvlvlasqms qftggedgmt yaapalfkpa tkllidahgk vvslfgvkln
      181 gklaayyfvf vfsglvfaam lrlvlsplgt vlkaireneg raeaigyrvv ayrtfvftis
      241 avaasligsv yavwlkytgp dttlsfaimv dillmvvigg mgtmwgavig aallvvaqfy
      301 lrdimeaaat alapippaaa lmnpdrwllw lgllfillvy ffpkgiagta mekgkr
//
LOCUS       WP_176086502             330 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Martelella sp.
            HB161492].
ACCESSION   WP_176086502
VERSION     WP_176086502.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..330
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=34950
     Region          33..325
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mselmkffer lggvnllpvi laviafalig qpssfatlti aglamgmmvf lmasglslvf
       61 gmmdvlnfgh aafisfgafi aasvlaglng wlgadsvfls glafalafva altfglaagw
      121 ffetvvikpv yrdhlrqili tmgamiveeq iilaiwggtp iavprphfle gawiigdvsi
      181 eiyrvfafll gliafvglym alnhtrigll iragvenrem vetlgfrvdr lfvavfmvgs
      241 alaalggamw ggyqtlitpa lgsqmmiivf ivviigglgs iggtllgait vglvtnyvgf
      301 lapkmalasn milmtaillw rpnglrpavk
//
LOCUS       WP_176086509             391 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase [Martelella sp. HB161492].
ACCESSION   WP_176086509
VERSION     WP_176086509.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 391)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..391
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=40585
     Region          1..390
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 msdiviagac rtavggfmrs lstvpahelg aavirealsr snvsghevde vilgqvltag
       61 qgqnparqaa mkagisesat afginqvcgs glravalgmq qiitgearim vaggqenmsl
      121 sphcqhlrgg tkmgnatmvd tmlndglmda fgdfhmgita eniasryqis raqqdafala
      181 shhkaaeadr enrfvdeivp fsvksrrsev ifdrdeqirp dadettlakl rpafdengtv
      241 tagnasglnd gaaamvlmsa teadlrgiqp mariaafata gvdpaimgig pvnaslkale
      301 ragwsiddid lveaneafaa qacavnselg ldpakvnvng gaialghpig asgarvlvtl
      361 lhemkrrnvr kglatlcigg gmgvamcver g
//
LOCUS       WP_176086517             364 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176086517
VERSION     WP_176086517.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 364)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..364
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38805
     Region          1..358
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mgsvslsnvn ksfgavdvih dvsleiedge fcvligpsgs gkstllriia gleevtsgvv
       61 siagkdvtdl ppkqrdiamv fqtyalypqm tvaenmgfal klagmpkaki aekvqqtarm
      121 lelepllerl pkalsggqrq rvsmgraivr dpsvflfdep lsnldaklrv qvrgeiadlh
      181 krlgttsiyv thdqveamtl gqkivvlrdg rveqagaplk lyddpvntfv asflgtpsin
      241 liaatvegan geaaarlvdg tllplgaghg fapgqqilyg irpehvrvld grqaggvsat
      301 ihaventgsd mvilsdadgf rmtaafkeqr plaagqditi vpdpskvrvf daesgkrirr
      361 seds
//
LOCUS       WP_176086525             170 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter small permease [Martelella sp. HB161492].
ACCESSION   WP_176086525
VERSION     WP_176086525.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..170
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=18070
     Region          1..157
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mriirrildg ivasamaill samvavlawq vfsryvlnap stfseeflrf gviwlsllga
       61 afstgrgthm aidlltemah grtkaalmal vpvsfiifsv lvliiggmrg vniaahqtsp
      121 vlgvpmgliy aslpvsgvlm liysllnlvd lmtgkrslpd tidravtagd
//
LOCUS       WP_176086537             263 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176086537
VERSION     WP_176086537.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11439530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..263
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28416
     Region          2..257
                     /region_name="PotC"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component II [Amino acid transport and
                     metabolism]; COG1177"
                     /db_xref="CDD:440790"
ORIGIN      
        1 mtgrsihpls rlfgwlvilf lagpivivig tsisntpyla fppqgftlkw yanvfnhsgf
       61 ldtfiismev alggtlialv tglaaayalt rykmkipgwy gsvfflpffi peivfgfsll
      121 ktlivqlqlp ilpslilgha ilclpymvrv igaslsgfdf siqeaavslg mhpvkafwti
      181 vlpnirsgvi agmvlafits lndmavalfl tgpgistlpi evftyvqqff dptvsavsvl
      241 lmgvtilvmv lierslglsk tvq
//
LOCUS       WP_176086591             315 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 2 protein [Martelella sp. HB161492].
ACCESSION   WP_176086591
VERSION     WP_176086591.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Oriol,R., Martinez-Duncker,I., Chantret,I., Mollicone,R. and
            Codogno,P.
  TITLE     Common origin and evolution of glycosyltransferases using
            Dol-P-monosaccharides as donor substrate
  JOURNAL   Mol Biol Evol 19 (9), 1451-1463 (2002)
   PUBMED   12200473
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Breton,C. and Imberty,A.
  TITLE     Structure/function studies of glycosyltransferases
  JOURNAL   Curr Opin Struct Biol 9 (5), 563-571 (1999)
   PUBMED   10508766
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Campbell,J.A., Davies,G.J., Bulone,V. V and Henrissat,B.
  TITLE     A classification of nucleotide-diphospho-sugar glycosyltransferases
            based on amino acid sequence similarities
  JOURNAL   Biochem J 329 (Pt 3) (Pt 3), 719 (1998)
   PUBMED   9445404
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10135280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..315
                     /product="glycosyltransferase family 2 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=34784
     Region          10..182
                     /region_name="DPM_DPG-synthase_like"
                     /note="DPM_DPG-synthase_like is a member of the
                     Glycosyltransferase 2 superfamily; cd04179"
                     /db_xref="CDD:133022"
     Site            order(13,15,89)
                     /site_type="active"
                     /note="Ligand binding site [active]"
                     /db_xref="CDD:133022"
     Site            order(42,88..89)
                     /site_type="active"
                     /note="Putative Catalytic site [active]"
                     /db_xref="CDD:133022"
     Site            87..89
                     /site_type="active"
                     /note="DXD motif [active]"
                     /db_xref="CDD:133022"
ORIGIN      
        1 meienlsvav lvpcyneevt iakvvsdfra alpgatvyvy dnnstdatce caaqagavvr
       61 lekrqgkgnv mrrmfadiea dvyvlvdgdd tydaasapkl vevlcsegld mvngrrdggk
      121 veayrpghrf gnrlltglvs mifgnefsdm lsgyrvfsrr fvksfpalam gfeieteltv
      181 halelrmpta evgtpykerp egsasklrtf hdgfrilrti mllvrderpf qffslialfl
      241 flfslvvmvp vfltyfqtgl vprfptvmla tgggilgals lfcglildtv tlsrreakrm
      301 rylaiasihs lirga
//
LOCUS       WP_176086628             353 aa            linear   BCT 11-JAN-2025
DEFINITION  PhoH family protein [Martelella sp. HB161492].
ACCESSION   WP_176086628
VERSION     WP_176086628.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Kazakov,A.E., Vassieva,O., Gelfand,M.S., Osterman,A. and
            Overbeek,R.
  TITLE     Bioinformatics classification and functional analysis of PhoH
            homologs
  JOURNAL   In Silico Biol 3 (1-2), 3-15 (2003)
   PUBMED   12762842
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..353
                     /product="PhoH family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=38285
     Region          21..349
                     /region_name="PhoH"
                     /note="Phosphate starvation-inducible protein PhoH,
                     predicted ATPase [Signal transduction mechanisms];
                     COG1702"
                     /db_xref="CDD:441308"
ORIGIN      
        1 mnvtelvaet aqgarpntkd eashfvltfe nnryaselfg qfdehlklle drlkvkavpr
       61 gnsvalsget vatyqarral dflysqllng ghveksdveg airmavatdd qlslptlerk
      121 aklsmsqist rkksiaartp aqdayirale rnelvfgtgp agtgktylav ayaaqllerg
      181 vvnkiilsrp aveagerlgf lpgdmkekvd pylrplydal ydmmpgdkve raitagviei
      241 aplafmrgrt lanaavilde aqnttsmqmk mfltrlgens rmiitgdpsq idlprgvksg
      301 lvealgilkg vesisiirft dtdvvrhplv arivaaydge srsageasea sda
//
LOCUS       WP_176086702             351 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176086702
VERSION     WP_176086702.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 351)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 351)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008637
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..351
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=36495
     Region          18..346
                     /region_name="NupP"
                     /note="ABC-type guanosine uptake system NupNOPQ, permease
                     component NupP [Nucleotide transport and metabolism];
                     COG4603"
                     /db_xref="CDD:443653"
ORIGIN      
        1 mseqetiltp qprgfglrfr redffvrivi alalsilcaa vlvalagknp lvafgaiisg
       61 afgsphqigv alnracpyll agsglamcfr agvinmgsdg qialggigat atvlfwpgep
      121 giltllaala aaallgagwa alatgihlyr rvhevlatll lnfvavllvq qvlsgpmgqk
      181 gagflqsprm pqpvwltrip efgfhigivv giviaialsf ilwktpfgfa lrvvgrsrra
      241 tayagfsvpa itwsvmliag algglaggme ilglhhrmie gfsegfgfka vtvallgaie
      301 paavipaalf iglletgsls mqrqigvpsa lvvviegitm lfiltatvrr a
//
LOCUS       WP_176086704             477 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Martelella sp. HB161492].
ACCESSION   WP_176086704
VERSION     WP_176086704.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..477
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=49706
     Region          1..447
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mmedisslse alangtltae allerslari aagdpalnaf vamdvagarr aakasdarrq
       61 rgallspidg iplsikdnil vkdmpatwgs rafadfmpat delpvarlra agaiiigktn
      121 vpeltldgft sndlfgttrn pwnnaltpgg ssggaaasva agfvpaamgt dgggstrrpa
      181 chtglvgwkp ssghmprldg fpailtdfev iglltrsvrd aaildqllra pdprdrrsml
      241 ettappipaa prilfvptfg dipvdpevss acrrfvdglr ergatvtesa lffdldsvne
      301 iwrvisrsgv aymmdwhhga lksgaspsvr alaedgaais gadyigalek taalraglag
      361 lfaqydlvit ptagalpwpv ekpypdmidg rpagprdhav ftgwvnvggl paislpiais
      421 retlpigiql vaafgadaal ldfaeglwqh cialpdlpqs aatqqsgral hgssgaf
//
LOCUS       WP_176086733             377 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176086733
VERSION     WP_176086733.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 377)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..377
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41183
     Region          1..353
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mgqlelkkiy knygiydvik gidlnvnege fvvfvgpsgc gkstllrmia gledisggdi
       61 tidgervnnl ppvrrgismv fqsyalyphm svyeniafpl rvqkmaeaqv rdrvegaaki
      121 lqleerlqqk pgmlsggqrq rvaigraivr kpkiflfdep lsnldaalrs emrieltrlh
      181 hdlkatmiyv thdqveamtm adrivvlnag diaqvgaple lyhkprnlfv agfignpkmn
      241 flpvtcisvs degvtvefrg qtitvpvapr qhlegkvltl girpehtvlg pgdmsvtiap
      301 nvierlgint iayaalddet tfcslsagsa pvkvdeeiti ginagdchlf dpagyalerk
      361 veltafdfet vlapeag
//
LOCUS       WP_176086770             386 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176086770
VERSION     WP_176086770.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..386
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=41944
     Region          1..358
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 madvkldrvv krfgeletih gvdldiesgs fvvfvgpsgc gkstllrmia gleevtegdv
       61 yiggkcvtea kasargigmv fqsyalyphm tvrenisfgl evagepkdvi earvgeaaei
      121 lklgelldrk prqlsggqrq rvaigrtivr qpkvflfdep lsnldaelrv qmrieitrlh
      181 erlgntmiyv thdqveamtm adkivvlrdg aveqvgtpla lyhrpenrfv agfigspkmn
      241 flpvrveava gnsvtitlpd sqeitlsasg plpppgamle lgirpehfiv gkggdfevml
      301 hcdvveelgg ttyvygeygg cqvivegdgd mqiargrdsl fsfersrlhl fdgdgkavml
      361 qrgtdhapag krlandaaad himstr
//
LOCUS       WP_176086813             383 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176086813
VERSION     WP_176086813.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 383)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..383
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42159
     Region          1..381
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 manvslrdir kiypngfeav hgidldvrdg efmvfvgpsg cakstilrmv agleqisdge
       61 lkigpsvvnk lppkqrgigm vfqnyalyph mkvydnmalg lkiahvpkde iksrvmhaae
      121 llemvnlldr ypkqlsggqa qrvavgrciv krpevflfde plsnldaklr asmrvrltel
      181 hrelrnsgqp staiyvthdq veamtmgeri cvlkegtiqq vdaptalyer pvnafvagfi
      241 gspemnirpa tlvandgaln lllgektlvs lpgafaekls ghvgrkvrfg irpehigtpe
      301 smalrrheea vaanvtgtvk llehmgneiy vyfdleglpf aaripvddar mldesargkp
      361 fsfsfvmeka hvfddetgan ltl
//
LOCUS       WP_176086827             292 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Martelella sp. HB161492].
ACCESSION   WP_176086827
VERSION     WP_176086827.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..292
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=31133
     Region          54..287
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 malaheqvip lwpgrpkgtp adlepiiter senlfrtsrv itgvvepslt aivpekpngv
       61 sliaapgggy rrisldaagy klaqqlaplg vttfmmtyrl pgeghdnaad vplmdaqrav
      121 rlirrnaadw gldpgrigfl gssaaghmaa svatghgrkv yeplddadav sarpdflglm
      181 vpvitmsdpf vhagsreall gakddaatrr ayspdlqvtp dtpetflvla dddqsvpaen
      241 glgfyaalrr agvpaelhvf rdgghtfsvp gapvrdwsrl figwlrqigm ld
//
LOCUS       WP_176086829             329 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Martelella sp. HB161492].
ACCESSION   WP_176086829
VERSION     WP_176086829.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869928
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..329
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=35348
     Region          51..302
                     /region_name="OPHC2-like_MBL-fold"
                     /note="Pseudomonas pseudoalcaligenes organophosphorus
                     hydrolase C2, and related proteins; MBL-fold metallo
                     hydrolase domain; cd07720"
                     /db_xref="CDD:293806"
     Site            order(66,153,155,157..158,185,234,255,258,271,273,302)
                     /site_type="active"
                     /db_xref="CDD:293806"
ORIGIN      
        1 mkttgklgrr glmkgvgltt laapallagv ahaqedqmte mpkdmpetkr fsmgelkfvv
       61 vrdgirkmdn pgtifgadqp petvaallrq nflpsdvsvn mfsptlidtg sqvmlfdtgm
      121 geagrswgag qllkglaaeg ygpedidvvv ithmhgdhin glmeagapaf pnaryvfgqt
      181 eydfwtdpar igtpaegghn avktmivpla ekasfiadga siapgitamd apghtpghmv
      241 fmvesagrql lltadtanhy vlslqrpdwq vrfdtdpvma satrrrifdm vaadgipflg
      301 yhmpfpavgy aekqgdgyrf vpasyqfel
//
LOCUS       WP_176086839             254 aa            linear   BCT 11-JAN-2025
DEFINITION  creatininase family protein [Martelella sp. HB161492].
ACCESSION   WP_176086839
VERSION     WP_176086839.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Yoshimoto,T., Tanaka,N., Kanada,N., Inoue,T., Nakajima,Y.,
            Haratake,M., Nakamura,K.T., Xu,Y. and Ito,K.
  TITLE     Crystal structures of creatininase reveal the substrate binding
            site and provide an insight into the catalytic mechanism
  JOURNAL   J Mol Biol 337 (2), 399-416 (2004)
   PUBMED   15003455
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003645
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..254
                     /product="creatininase family protein"
                     /EC_number="3.5.2.10"
                     /calculated_mol_wt=27515
     Region          8..248
                     /region_name="ArfB"
                     /note="Creatinine amidohydrolase/Fe(II)-dependent FAPy
                     formamide hydrolase (riboflavin and F420 biosynthesis)
                     [Coenzyme transport and metabolism]; COG1402"
                     /db_xref="CDD:441012"
ORIGIN      
        1 mdydktdiar lndsemeaal aktpvlilpi gaveshgdhl pagtdnilaa rlaeelarvi
       61 ggdtpvlrlp vlpfgqvwsl aeapcsfgis netvsntive ialsaaqkgi rtivvvnahl
      121 gnaiairdaq rrlreegitl anffypgsgs vieevrekke ahpsymhace ietsyvlhla
      181 pdavnmdkai enypefpedf stvayrwtdf skspvlgdar aataekgeki lkvvlanmak
      241 qiavlyarqf nsns
//
LOCUS       WP_176086841             317 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176086841
VERSION     WP_176086841.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 317)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..317
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32522
     Region          42..317
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mavpailsna kpagatwral allvillvvl fvfsgrvsmv qvmdnarqaa plglialgqa
       61 lilmmgrldl svgataglan vvlaasfagt mdnmaaalai tiffgllvgl angvlvvvlr
      121 ipaflatlat slvlsgailv ytggspkgsi pagfrviseg wlfgilpwsv viwiiaslil
      181 lvfvhyslag rkmllsgana rsakrngiaa drmvifsfvl asfmatlggi mlssitgmas
      241 igiadtytvd siaaavigga lftggvflpl gaaagslilf flqsllyvls lptaarfvlq
      301 gsiiilalal snfkkdr
//
LOCUS       WP_176086842             312 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176086842
VERSION     WP_176086842.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..312
                     /product="ABC transporter permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32137
     Region          21..303
                     /region_name="AraH"
                     /note="Ribose/xylose/arabinose/galactoside ABC-type
                     transport system, permease component [Carbohydrate
                     transport and metabolism]; COG1172"
                     /db_xref="CDD:440785"
ORIGIN      
        1 mfegslrsnl llslpalals vlliaitgll spnffsdsnl tnlsvrllpl glvalgealv
       61 lfagridlsv gsimslatai maltsdtlgw lavplalgag lvcgiftasg vnflrinplv
      121 mtlataaivk gitmlilpsp ggevdyafye alfgaerlls apllialavf ivvaivmnws
      181 rlgrsiyafg sdpraafang isalridlvv fglsgvlaaa agvvlsiril sgdpligesy
      241 tldavsaail ggvalqggrg navgvffaal alvlinnmfn lldidtslqn iakglifiva
      301 lvffmrgkae es
//
LOCUS       WP_176086856             355 aa            linear   BCT 11-JAN-2025
DEFINITION  GGDEF domain-containing protein [Martelella sp. HB161492].
ACCESSION   WP_176086856
VERSION     WP_176086856.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 355)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 355)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..355
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37575
     Region          83..343
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 mllisglssf sgttlygitm akglptpaai galaivgsvl lmwvgirrfc glsagwtvag
       61 iilaamatli alsgnssdgr dtalfagqli thcliafdlf rhnrrgfgsg laasgaiani
      121 iansltlgfs llyvfgsvsa stkamvrtds mllvalgail tifgialmai drllleledr
      181 aghdeltglp nrrqfveqld raktqsrlrg tdfsillidi dhfkqwndgf ghltgdmalk
      241 hfariaskal apddllartg gdefcvlmpg ssldkaakla eqlvrsmget plclesgavt
      301 ltisigiaas nrlarkqked plaladialy sakkdgrnrf cvyspdldaa fgrqv
//
LOCUS       WP_176086863             371 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176086863
VERSION     WP_176086863.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 371)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..371
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40577
     Region          20..365
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mtrlsrntgf tkgqasaalp aaieltgitf sydrtrnild rlslairpge ffsligpsgc
       61 gkttilglvs gllepddgti migdrdvtrm pthkrdigvv fqnyalfphm tvdenvgygl
      121 kmrgvdeagr raavrealem vgmdqmmrrf pgelsggqqq riglaravas rprvmlldep
      181 lsnldaklre qmcieisdlq krlgmtmlyv thdqgeamam sdrlaimngg ivqelgtptt
      241 vyenprshfg aqflgnvnlv tgfgeggrfs fgdgryitpa pesyrpgpvt lmirpetili
      301 daseghenrf eariermvyr gayheltlav tgydqpvlav ahgrhglrng qllaiaiped
      361 gihildtesg k
//
LOCUS       WP_176086864             295 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter permease [Martelella sp. HB161492].
ACCESSION   WP_176086864
VERSION     WP_176086864.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 295)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 295)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 295)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003093
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..295
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31085
     Region          7..292
                     /region_name="PotB"
                     /note="ABC-type spermidine/putrescine transport system,
                     permease component I [Amino acid transport and
                     metabolism]; COG1176"
                     /db_xref="CDD:440789"
ORIGIN      
        1 msgirrsgkr srhfaasply aiaglpmgli fgaclvflvv isffkpsvfa lfepgfslan
       61 hikastsply sraivlsvvy aliatpiaal iaypmaffia ryagrlkgff iaivvsvflv
      121 tfvvkifawq illqqsgpva qllfalgltd tpvslvgtta gviiglvyap lpymilamla
      181 sieglprnle hasavcgatp aktfftvtlp lsmpgvvtsl lfgfalniaa fivpamlgag
      241 kismsglviq rvsvgfgsig gnwplaaals iqllvvsmaf ssillallsg rrwrr
//
LOCUS       WP_176086873             280 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176086873
VERSION     WP_176086873.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 280)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438141
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..280
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30789
     Region          6..258
                     /region_name="FepC"
                     /note="ABC-type cobalamin/Fe3+-siderophores transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism, Coenzyme transport and metabolism]; COG1120"
                     /db_xref="CDD:440737"
ORIGIN      
        1 mnrhslraeq ivagygekri lenlsfevpd gkitaivgan acgkstllrt larlltpkhg
       61 evlldgkaih kmptrklaqm lgllpqspla pegitvadlv srgrhphqgm fsrwtrqdde
      121 aiaaaldtta taeladrpvd elsggqrqrv wiamvlaqqt dillldeptt fldishqiev
      181 ldiltdlnrr ngttivmvlh dlnlaarygd hlvamragal hvagapekvl seahirdvfg
      241 lesriitdpv sgrpmmlpig rhrstenpfs seerrqredi
//
LOCUS       WP_176086889             328 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Martelella sp. HB161492].
ACCESSION   WP_176086889
VERSION     WP_176086889.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..328
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35129
     Region          10..326
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 mnnitaaapv ltidhmsaaf ktrrgsveal sdinlqlqag eilalvgesg agksltsscv
       61 ngllprncsi tsgeirlngk ridrlgtram ekirgaeigt vfqdpltsln plftvceqiv
      121 rtlkahrvmt reaaeaealr lleevgipaa rqrlhcyphe fsggmrqrvv iamalalrpg
      181 liiadeptta ldvsiqaqil dllrrlsreh gssvilvthd mgvvaetadr vavlyagriv
      241 etgpvadvll kpahpytkgl laaipslerk verlpqipga mpsmhavpqg cafhprcpva
      301 tdacmaerpa ffsagerlva clhageir
//
LOCUS       WP_176086892             227 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Martelella sp. HB161492].
ACCESSION   WP_176086892
VERSION     WP_176086892.1
KEYWORDS    RefSeq.
SOURCE      Martelella sp. HB161492
  ORGANISM  Martelella sp. HB161492
            Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
            Hyphomicrobiales; Aurantimonadaceae; Martelella.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Martelella sp. HB161492"
                     /db_xref="taxon:2720726"
     Protein         1..227
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25948
     Region          1..220
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 matekvrgkh pvedllydrl vdaiidkhlr pgqhlnevkl aerfdvprsr vrrvlerlrd
       61 edvvvfelnr gafvsrpttk eahnvfetrr hledlvvrla ceratpedia llrenlrder
      121 eafaamrsdv nrvaanfhfa iarisgngvl ekmvaqlirr cvlvqsvyek ksgilclsee
      181 hgslidciek ndpegaahlm ahhfdhiiss ldltearrae idsfefi
//
LOCUS       WP_176087101             136 aa            linear   BCT 11-JAN-2025
DEFINITION  SDR family oxidoreductase, partial [Burkholderia vietnamiensis].
ACCESSION   WP_176087101
VERSION     WP_176087101.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 136)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468002
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         1..>136
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
     Region          6..>122
                     /region_name="YdfG"
                     /note="NADP-dependent 3-hydroxy acid dehydrogenase YdfG
                     [Energy production and conversion]; COG4221"
                     /db_xref="CDD:443365"
ORIGIN      
        1 msenidgkvv vitgassglg laaarhlaar gahvvlgarr ierlqqlvee lsgqgarala
       61 faadvtvreq verlvdgavq gfgridvmin naglmslapl erlkvdewdr midvnlrgvl
      121 ygvaaaavrr ddaasa
//
LOCUS       WP_176087114             144 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein, partial [Burkholderia
            vietnamiensis].
ACCESSION   WP_176087114
VERSION     WP_176087114.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 144)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         <1..>144
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
     Region          1..>144
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 rmiagledvs ggvasiggrr vngvpdaqrg vamvfqgyal fphmtvyeni afglrlaktp
       61 kaeidrkvre asrilqldal lerhpkalsg gqrqrvaigr aivrepgvfl fdeplsnlda
      121 tlrgqtriei grlhrqfgea svvy
//
LOCUS       WP_176087182             352 aa            linear   BCT 11-JAN-2025
DEFINITION  elongation factor Tu, partial [Burkholderia vietnamiensis].
ACCESSION   WP_176087182
VERSION     WP_176087182.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Torres,A.N., Chamorro-Veloso,N., Costa,P., Cadiz,L., Del Canto,F.,
            Venegas,S.A., Lopez Nitsche,M., Coloma-Rivero,R.F., Montero,D.A.
            and Vidal,R.M.
  TITLE     Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and
            OmpT Proteins of Shiga Toxin-Producing Escherichia coli
  JOURNAL   Microorganisms 8 (8), 1184 (2020)
   PUBMED   32759661
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Widjaja,M., Harvey,K.L., Hagemann,L., Berry,I.J., Jarocki,V.M.,
            Raymond,B.B.A., Tacchi,J.L., Grundel,A., Steele,J.R., Padula,M.P.,
            Charles,I.G., Dumke,R. and Djordjevic,S.P.
  TITLE     Elongation factor Tu is a multifunctional and processed
            moonlighting protein
  JOURNAL   Sci Rep 7 (1), 11227 (2017)
   PUBMED   28894125
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Wolff,D.G., Castiblanco-Valencia,M.M., Abe,C.M., Monaris,D.,
            Morais,Z.M., Souza,G.O., Vasconcellos,S.A., Isaac,L., Abreu,P.A.
            and Barbosa,A.S.
  TITLE     Interaction of Leptospira elongation factor Tu with plasminogen and
            complement factor H: a metabolic leptospiral protein with
            moonlighting activities
  JOURNAL   PLoS One 8 (11), e81818 (2013)
   PUBMED   24312361
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR00485.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     gene            1..>352
                     /gene="tuf"
     Protein         1..>352
                     /product="elongation factor Tu"
                     /GO_function="GO:0003746 - translation elongation factor
                     activity [Evidence IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_process="GO:0006414 - translational elongation
                     [Evidence IEA]"
     Region          1..352
                     /region_name="PRK00049"
                     /note="elongation factor Tu; Reviewed"
                     /db_xref="CDD:234596"
ORIGIN      
        1 makekfertk phvnvgtigh vdhgkttlta aittvltkkf ggeakaydqi daapeekarg
       61 itintahvey etanrhyahv dcpghadyvk nmitgaaqmd gailvcsaad gpmpqtrehi
      121 llarqvgvpy iivflnkcdm vddaellelv emevrellsk ydfpgddtpi vkgsaklale
      181 gdtgelgeva imnladaldt yiptperavd gaflmpvedv fsisgrgtvv tgrvergivk
      241 vgeeieivgi kptvkttctg vemfrklldq gqagdnvgil lrgtkredve rgqvlakpgs
      301 itphthftae vyvlskdegg rhtpffnnyr pqfyfrttdv tgsielpkdk em
//
LOCUS       WP_176087208             770 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD-binding and (Fe-S)-binding domain-containing protein, partial
            [Paraburkholderia tropica].
ACCESSION   WP_176087208
VERSION     WP_176087208.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416044
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..770
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         <1..770
                     /product="FAD-binding and (Fe-S)-binding domain-containing
                     protein"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_function="GO:0051536 - iron-sulfur cluster binding
                     [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
     Region          <1..298
                     /region_name="GlcD"
                     /note="FAD/FMN-containing lactate dehydrogenase/glycolate
                     oxidase [Energy production and conversion]; COG0277"
                     /db_xref="CDD:440046"
     Region          251..756
                     /region_name="GlpC"
                     /note="Fe-S cluster-containing oxidoreductase, includes
                     glycolate oxidase subunit GlcF [Energy production and
                     conversion]; COG0247"
                     /db_xref="CDD:440017"
ORIGIN      
        1 krrvsgynld qllpengfni aralvgsegt lattlraqvt lvegrpervl vvlgfdtifd
       61 aadsvphllp lgaiamegld qgivgglkal glklddiael pagdawllve fgastrdaai
      121 aqaramadaa qrfpqqpsvr fvedaalmnr lwtiretgas atslsrdpaa pdpvvgweda
      181 avepallgay lreftalver ygyktnlygh fgdgcihsri tfdlrsargv hdwrafleea
      241 arlvvkyqgs lsgehgdgqa kgeflhlmyt prlmqafref kalwdpqglm npgklidamp
      301 vdenlrmgpq yrqgnvkgmf typmaaqtas ddarvdalee rgygreterc igmgkcrsmd
      361 ggtmcpsfka treernstrg rarlffemln gevidetrna eavkesmdlc lsckgckndc
      421 pthvdipkyr aeflhryykt rrrplmdaav grigawlpva trvsglvnga mrnrlvkkas
      481 qrfglaegaa fpaiasqafr dtpaakklia pwparfgaqd vvvwtdtfnn gfspavldaa
      541 lrvveaaggt prltprhvcc grplydvgll deakknlldi vemmrapvaa gvpvlileps
      601 clsvfrdeml alighdaeag elarklsssc itvaeyaqkn glnlpstlpg egsraesvhv
      661 hthchqracg gagaeknlga kvldtgccgm agafgyhhkt aavakavgek elvpklaalp
      721 ddaivvadgf scrsqigklt grtaqhlaqh laeaiasanp tvrtgtdepa
//
LOCUS       WP_176087244             669 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Virgibacillus dokdonensis].
ACCESSION   WP_176087244
VERSION     WP_176087244.1
KEYWORDS    RefSeq.
SOURCE      Virgibacillus dokdonensis
  ORGANISM  Virgibacillus dokdonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Virgibacillus.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12036995
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Virgibacillus dokdonensis"
                     /db_xref="taxon:302167"
     Protein         1..669
                     /product="methyl-accepting chemotaxis protein"
                     /calculated_mol_wt=74036
     Region          45..274
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          166..668
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mitnknnrhi fkqksiktkl lipftllilf aggtvalisy nftikmmvne ltnssesqmk
       61 smsetfdmff sntdniiqqy tvnsllleyk qenhaelisr lqetkdahas iafiyagdek
      121 tgdmidptgd ldenynpker pwyqqavkad getiwtrpyv degtgktvlt aarayydnqk
      181 lqgvfavdvt intlmdmvkq vsigetgyam vldqaghyiv hpeeekvgqq mdeilfeklt
      241 ntqkqgsley evndeekvis fatnpttgwi iggtvdqaef askaksviip ivvaliivii
      301 igvilsllit nritkpiksv myrmnkiaag dlsdpplish sadetgqlvr asnkmgenmr
      361 hlldemqtas eavrhhsedl tqfanevhag tdqiaatmee laagsetqah sanqlahgmg
      421 efdtkmkdvn ekgeltetns kkvqnltdeg srrmqaskeq mdtiyhivhe avekvrgldq
      481 qskqiselit ivhdiadqtn llalnasiea aragehgqgf avvateirkl aeevatsvtd
      541 iteivgniqq esmnvttslq tgyqevevga sqiqttletf vqintsiakm gehitnisnh
      601 lrdmtassqd mnrsieevas saeqaaagve eisatteets ssmeeivrns ekmekladkl
      661 hqlmtkftf
//
LOCUS       WP_176087226             102 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein,
            partial [Paraburkholderia tropica].
ACCESSION   WP_176087226
VERSION     WP_176087226.1
KEYWORDS    RefSeq.
SOURCE      Paraburkholderia tropica
  ORGANISM  Paraburkholderia tropica
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Paraburkholderia.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Paraburkholderia tropica"
                     /db_xref="taxon:92647"
     Protein         <1..>102
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
     Region          <1..>102
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 vrttafdava aeggnasvek ieaaadngka qfvnrevtkl drpeltsaki ivsggrglgs
       61 genytkvlep ladklnaalg asraavdagy vpndyqvgqt gk
//
LOCUS       WP_176087121              41 aa            linear   BCT 11-JAN-2025
DEFINITION  P-II family nitrogen regulator, partial [Burkholderia
            vietnamiensis].
ACCESSION   WP_176087121
VERSION     WP_176087121.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia vietnamiensis
  ORGANISM  Burkholderia vietnamiensis
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 41)
  AUTHORS   Huergo,L.F., Chandra,G. and Merrick,M.
  TITLE     P(II) signal transduction proteins: nitrogen regulation and beyond
  JOURNAL   FEMS Microbiol Rev 37 (2), 251-283 (2013)
   PUBMED   22861350
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001244
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..41
                     /organism="Burkholderia vietnamiensis"
                     /db_xref="taxon:60552"
     Protein         <1..41
                     /product="P-II family nitrogen regulator"
                     /GO_function="GO:0030234 - enzyme regulator activity
                     [Evidence IEA]"
                     /GO_process="GO:0006808 - regulation of nitrogen
                     utilization [Evidence IEA]"
     Region          <1..41
                     /region_name="GlnK"
                     /note="Nitrogen regulatory protein PII [Signal
                     transduction mechanisms, Amino acid transport and
                     metabolism]; COG0347"
                     /db_xref="CDD:440116"
ORIGIN      
        1 qaveaieraa rtgkigdgki fvtpieqvir irtgetgada l
//
LOCUS       WP_176087340             564 aa            linear   BCT 11-JAN-2025
DEFINITION  methyl-accepting chemotaxis protein [Virgibacillus dokdonensis].
ACCESSION   WP_176087340
VERSION     WP_176087340.1
KEYWORDS    RefSeq.
SOURCE      Virgibacillus dokdonensis
  ORGANISM  Virgibacillus dokdonensis
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Virgibacillus.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Lacal,J., Garcia-Fontana,C., Munoz-Martinez,F., Ramos,J.L. and
            Krell,T.
  TITLE     Sensing of environmental signals: classification of chemoreceptors
            according to the size of their ligand binding regions
  JOURNAL   Environ Microbiol 12 (11), 2873-2884 (2010)
   PUBMED   20738376
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Hazelbauer,G.L., Falke,J.J. and Parkinson,J.S.
  TITLE     Bacterial chemoreceptors: high-performance signaling in networked
            arrays
  JOURNAL   Trends Biochem Sci 33 (1), 9-19 (2008)
   PUBMED   18165013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11435591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Virgibacillus dokdonensis"
                     /db_xref="taxon:302167"
     Protein         1..564
                     /product="methyl-accepting chemotaxis protein"
                     /GO_process="GO:0006935 - chemotaxis [Evidence IEA]"
                     /calculated_mol_wt=62297
     Region          10..564
                     /region_name="Tar"
                     /note="Methyl-accepting chemotaxis protein (MCP) [Signal
                     transduction mechanisms]; COG0840"
                     /db_xref="CDD:440602"
ORIGIN      
        1 mrklftfksi rmklffafsi vimlvillgv invisinrsn qgteemiqqd mqllvteeql
       61 afnmaertgy lrgyllynde rykqsfqnti detlelenyv skhnnseevk llmekklewg
      121 eltdkffqem degnsakakv imaneiqpig nqlidgfkel aqksennitn ksedviqage
      181 ftlsfglivt vsvvvlgvlt alltaysiak plkrvkermt kiangelnne pldikgkdei
      241 aelmattnem neqlkellis iknvssvvdd kskalnqasd emqqgteqva atmeelasga
      301 enqanhaanl asmmndlnni iqevsqnsnr ieksskgvlv ktksghdimg ttndqmvkid
      361 hivknavesv rgldiktkei sklvtvigev aeqtnllaln aaieaarage hgkgfavvad
      421 evrklaeqvs lslnditkvv ndiqtesdqv ttslqdgyke vtagseqmke tkdtfesiyh
      481 svnemanais qvkehfdwvs enskemhgsv geiaaisees aagieqtsas aqqasssmqe
      541 vsanadrlsk ladnlktlmq rfti
//
LOCUS       WP_176087387             227 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: response regulator transcription factor
            [Bacillaceae].
ACCESSION   WP_176087387
VERSION     WP_176087387.1
KEYWORDS    RefSeq.
SOURCE      Bacillaceae
  ORGANISM  Bacillaceae
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 14439489
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Bacillaceae"
                     /db_xref="taxon:186817"
     Protein         1..227
                     /product="response regulator transcription factor"
                     /calculated_mol_wt=26087
     Region          5..117
                     /region_name="REC_OmpR_NsrR-like"
                     /note="phosphoacceptor receiver (REC) domain of
                     Streptococcus agalactiae NsrR-like OmpR family response
                     regulators; cd18159"
                     /db_xref="CDD:381143"
     Site            order(35..36,54..64,83,90)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381143"
     Region          138..223
                     /region_name="trans_reg_C"
                     /note="DNA-binding effector domain of two-component system
                     response regulators; cd00383"
                     /db_xref="CDD:294013"
     Site            order(155,174..175,193,196,204..205,216,221)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:294013"
ORIGIN      
        1 mkinifvved ddalfaalkk gleawsfrvt rpddfegvmr sfleqqpqlv imdvtlpkfd
       61 gfhwcreira vskvpivfls srdhpmdmvm alsmgaddfi qkpfhtdvly akiqailrrt
      121 yaygeeqvni lewngalidl nrgvirnaek evdltkneff ilitlvksnn viisrydlir
      181 klwedeqfvn dntltanitr lrqkletidl adaivtkkgl gymaitl
//
LOCUS       WP_176087486             293 aa            linear   BCT 11-JAN-2025
DEFINITION  PhoH family protein [Leptospira alexanderi].
ACCESSION   WP_176087486
VERSION     WP_176087486.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Kazakov,A.E., Vassieva,O., Gelfand,M.S., Osterman,A. and
            Overbeek,R.
  TITLE     Bioinformatics classification and functional analysis of PhoH
            homologs
  JOURNAL   In Silico Biol 3 (1-2), 3-15 (2003)
   PUBMED   12762842
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447890
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..293
                     /product="PhoH family protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /calculated_mol_wt=33244
     Region          2..292
                     /region_name="PhoH"
                     /note="Phosphate starvation-inducible protein PhoH,
                     predicted ATPase [Signal transduction mechanisms];
                     COG1702"
                     /db_xref="CDD:441308"
ORIGIN      
        1 mdiiprgngf qiegesakve faldffkkle anyrerpdrd fidsfdfayi lkdagkelrk
       61 kkareneser stpwkpsdki lttyrgkhif prtrnqeiyf rsfqenlitf algpagtgkt
      121 flsvatacrf lqagtidkii ltrpaveage nlgflpgdln qkvdpylrpv ydalnecigp
      181 ektqeyislt kieiapvafm rgrtlsnafi ildeaqnctl aqlkmimtrl grnsrmcisg
      241 dstqidldhg rsglekvvtl fkntdqigmv ffgkeditrh plvevivrkf eel
//
LOCUS       WP_176087531             274 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Leptospira alexanderi].
ACCESSION   WP_176087531
VERSION     WP_176087531.1
KEYWORDS    RefSeq.
SOURCE      Leptospira alexanderi
  ORGANISM  Leptospira alexanderi
            Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia;
            Leptospirales; Leptospiraceae; Leptospira.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11437497
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Leptospira alexanderi"
                     /db_xref="taxon:100053"
     Protein         1..274
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=32082
     Region          31..268
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
ORIGIN      
        1 mkrsmnpifi fllsaiflvl flvwwnqdrl iffpeklpkn fvfrfpnefq eiklntpdge
       61 tsyglyfpsk sniskktvlf fhgnagslrt wgricedflp fgwnilitdy rgygknsgsi
      121 seksmnedae lwlnyvlqei kvprneiviy grsigtgvaa dlafknpdld lfletpftdl
      181 ptlarnyypf lqtwmlrfqf rnlskletvr skirifhgte deiipysnse iifkklkern
      241 qdvilftipn gshndlalyp eyrralkksl deir
//
LOCUS       WP_176087572             287 aa            linear   BCT 11-JAN-2025
DEFINITION  MBL fold metallo-hydrolase [Achromobacter anxifer].
ACCESSION   WP_176087572
VERSION     WP_176087572.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Bebrone,C.
  TITLE     Metallo-beta-lactamases (classification, activity, genetic
            organization, structure, zinc coordination) and their superfamily
  JOURNAL   Biochem Pharmacol 74 (12), 1686-1701 (2007)
   PUBMED   17597585
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Callebaut,I., Moshous,D., Mornon,J.P. and de Villartay,J.P.
  TITLE     Metallo-beta-lactamase fold within nucleic acids processing
            enzymes: the beta-CASP family
  JOURNAL   Nucleic Acids Res 30 (16), 3592-3601 (2002)
   PUBMED   12177301
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Daiyasu,H., Osaka,K., Ishino,Y. and Toh,H.
  TITLE     Expansion of the zinc metallo-hydrolase family of the
            beta-lactamase fold
  JOURNAL   FEBS Lett 503 (1), 1-6 (2001)
   PUBMED   11513844
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Aravind,L.
  TITLE     An evolutionary classification of the metallo-beta-lactamase fold
            proteins
  JOURNAL   In Silico Biol 1 (2), 69-91 (1999)
   PUBMED   11471246
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10869981
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..287
                     /product="MBL fold metallo-hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=31330
     Region          <3..287
                     /region_name="bifunc_ST_SDO"
                     /note="bifunctional sulfur transferase/dioxygenase Blh;
                     NF040641"
                     /db_xref="CDD:468609"
ORIGIN      
        1 mspqiqaffd pvtatvtyvv hepapggaca iidsvldydp ksgrsstasa drvadyvrqh
       61 glktewllet hahadhlsaa pylqrqlggv iaigqsirtv qgvfkkifnl epefqldgsq
      121 fghlfadget frigaltaqa ihvpghtpad mayligdaaf vgdtlfmpdv gtarcdfpgg
      181 dahqlyrsiq rllnlpadtr lymchdyppa greaswqttv aeqrranihv rdgidedafv
      241 dmrtrrdatl smptlilpai qvniraghfp paedngvryl kipvdal
//
LOCUS       WP_176087613             395 aa            linear   BCT 11-JAN-2025
DEFINITION  GGDEF domain-containing protein [Achromobacter anxifer].
ACCESSION   WP_176087613
VERSION     WP_176087613.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Cotter,P.A. and Stibitz,S.
  TITLE     c-di-GMP-mediated regulation of virulence and biofilm formation
  JOURNAL   Curr Opin Microbiol 10 (1), 17-23 (2007)
   PUBMED   17208514
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Simm,R., Fetherston,J.D., Kader,A., Romling,U. and Perry,R.D.
  TITLE     Phenotypic convergence mediated by GGDEF-domain-containing proteins
  JOURNAL   J Bacteriol 187 (19), 6816-6823 (2005)
   PUBMED   16166544
  REMARK    Erratum:[J Bacteriol. 2006 Mar;188(5):2024]
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Chan,C., Paul,R., Samoray,D., Amiot,N.C., Giese,B., Jenal,U. and
            Schirmer,T.
  TITLE     Structural basis of activity and allosteric control of diguanylate
            cyclase
  JOURNAL   Proc Natl Acad Sci U S A 101 (49), 17084-17089 (2004)
   PUBMED   15569936
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10112692
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..395
                     /product="GGDEF domain-containing protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=41819
     Region          12..>377
                     /region_name="COG5001"
                     /note="Cyclic di-GMP metabolism protein, combines GGDEF
                     and EAL domains with a 6TM membrane domain [Signal
                     transduction mechanisms]"
                     /db_xref="CDD:444025"
ORIGIN      
        1 mdtalkfslp kwrltrwlth sghdtpadir saliaslfgt lpifaggvin tlmiagvvaw
       61 rrpeplylsw lamevllavv rvlilrsalr aapkggntht diyillallw afsvgygvfv
      121 tfingdwlaa tlagvscgam aggicfrnyg aprlvgamif lslgpmclga aftgeyvtai
      181 vfiqipfylv smsiashrln rilvstmlae rdserrased altglanrag lqaalervca
      241 sargqdssaa llymdmdgfk lindtyghaa gdkvlittaq rmrsmlrvdd vaariggdef
      301 ivlvtgidat aalrlgehll hdasqpitla dgtrvsvgls igisivsgan rspdaalhsa
      361 daalyrakaq ggrccavagm esiekevpdg epava
//
LOCUS       WP_176087617             252 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176087617
VERSION     WP_176087617.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..252
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27499
     Region          7..247
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mtseydvpai rrthdilrll asrnapvkas elaeacqlar stlyllldcl eqrrwierrd
       61 ggyvigielm algyaylrqd glqtafqaaa gafvarhnev vqlatldgfd vvylaredar
      121 rpvrlvsdlg lrlpahacal gkallaslpp edlaarvpda lprvtersla traaldqele
      181 qvrrsglaqd leevatglvc yaayvgvtpl gkrvavstsi ptdrldpehr rdvmegiriv
      241 ardvalrvip ga
//
LOCUS       WP_176087626             178 aa            linear   BCT 11-JAN-2025
DEFINITION  fimbrial protein [Achromobacter anxifer].
ACCESSION   WP_176087626
VERSION     WP_176087626.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Busch,A. and Waksman,G.
  TITLE     Chaperone-usher pathways: diversity and pilus assembly mechanism
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 367 (1592), 1112-1122 (2012)
   PUBMED   22411982
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Allen,B.L., Gerlach,G.F. and Clegg,S.
  TITLE     Nucleotide sequence and functions of mrk determinants necessary for
            expression of type 3 fimbriae in Klebsiella pneumoniae
  JOURNAL   J Bacteriol 173 (2), 916-920 (1991)
   PUBMED   1670938
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Klemm,P. and Christiansen,G.
  TITLE     Three fim genes required for the regulation of length and mediation
            of adhesion of Escherichia coli type 1 fimbriae
  JOURNAL   Mol Gen Genet 208 (3), 439-445 (1987)
   PUBMED   2890081
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10007530
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..178
                     /product="fimbrial protein"
                     /GO_component="GO:0009289 - pilus [Evidence IEA]"
                     /GO_process="GO:0007155 - cell adhesion [Evidence IEA]"
                     /calculated_mol_wt=17604
     Region          1..178
                     /region_name="FimA"
                     /note="Pilin (type 1 fimbrial protein) [Cell motility];
                     COG3539"
                     /db_xref="CDD:442760"
ORIGIN      
        1 mnkntlakfa llataaavsq aalaedgrvq fngeivdapc svspgatnlv vplgkvsras
       61 mdgaagkhst paqfeiqltd csasakgasi tfsgtpdsvs sdvlaiansg gltasasgva
      121 velrdatrak ialgspspky vlgvgtnnlk feaayvstga tvtpgpanat aqftvnyn
//
LOCUS       WP_176087654             434 aa            linear   BCT 11-JAN-2025
DEFINITION  dihydrolipoamide acetyltransferase family protein [Achromobacter
            anxifer].
ACCESSION   WP_176087654
VERSION     WP_176087654.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Kumaran,S., Patel,M.S. and Jordan,F.
  TITLE     Nuclear magnetic resonance approaches in the study of 2-oxo acid
            dehydrogenase multienzyme complexes--a literature review
  JOURNAL   Molecules 18 (10), 11873-11903 (2013)
   PUBMED   24077172
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Perham,R.N., Packman,L.C. and Radford,S.E.
  TITLE     2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning
            and halfway there
  JOURNAL   Biochem Soc Symp 54, 67-81 (1987)
   PUBMED   3332999
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11485570
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..434
                     /product="dihydrolipoamide acetyltransferase family
                     protein"
                     /EC_number="2.3.-.-"
                     /GO_component="GO:0045240 - alpha-ketoacid dehydrogenase
                     complex [Evidence IEA]"
                     /GO_function="GO:0016407 - acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=45438
     Region          1..434
                     /region_name="PRK11856"
                     /note="branched-chain alpha-keto acid dehydrogenase
                     subunit E2; Reviewed"
                     /db_xref="CDD:237001"
ORIGIN      
        1 mdievvmpai gagttqgkil qwlkqsgdtv kvgdilaeie tdkavielea lddgvldrih
       61 vpagdtevpv gdviatllrq ggaaqlpasq psapavanpp aadslaansp aaarpavtaa
      121 pqpearagla eqrlfaspsa rrlaralgvd lhalsgsgpn grivrvdien aaatqpaksa
      181 aefaapvsga eapqhtrsqt qpqvqpqiqp htpmratiar rlvqskqqvp hfyltvdcrm
      241 dallaaraal narsesarep mrhslndlla mavaravgqv pavnaqwtde givqlgevdl
      301 siavalesgl itpivrnadk kslreistei aqlaeqarrg rlrpeqyegg sltlsnlgmh
      361 gvrefaaiin ppqsailaag avvrqpvvdg ddirvghvms ltlsadhrvv dgalgarflg
      421 avkqllenpi elil
//
LOCUS       WP_176087669             505 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Achromobacter
            anxifer].
ACCESSION   WP_176087669
VERSION     WP_176087669.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..505
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=54172
     Region          4..504
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 mypidfffra aeqypdrial dgpegqvtys rlaadtrala aalqeldpap qtrvaicagn
       61 sarhilalla vlasgkvwvp lnyrsterei grildateps ivivdgagaq lapaaqapqg
      121 rrhihledaa aplaldalla rcagrepqrh alprdatqai kftggttglp kgvmqpyhaw
      181 nagiinqias wglthedryv vaapithgtg tyllpvlarg gahllldgvt pasittafre
      241 rggtlsfmpp tliymimaqp gvtradfprl rnliyggapm pvekidrara ffgpvlgtty
      301 gqteapqivt vlrpadleap enrasvgrvt wltdvaimsp dgallprgei gevvvqgdll
      361 msgywrlpek taetvvegwl htgdtglida rgylflkdrl rdviitggfn iypvdvenal
      421 sahpavyecs vfglpddkwg eavhaavqfh pgaavsedel kahvrgllgp vatpkqfhih
      481 dslprssvgk vlknavrdaa lkets
//
LOCUS       WP_176087680             332 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Achromobacter
            anxifer].
ACCESSION   WP_176087680
VERSION     WP_176087680.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10008335
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..332
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=34957
     Region          25..307
                     /region_name="LivM"
                     /note="ABC-type branched-chain amino acid transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG4177"
                     /db_xref="CDD:443336"
ORIGIN      
        1 mskkidhall almavvlail pfaasgyviy vvnllmvfvv lalglhlvig etgqfalsha
       61 afygvgiyta glinnlwhpp ffisivaggl laaalgyvig alalrmrdiy lalstfafge
      121 amqwvflnwq svtngsngfr ispatlfgye lvsdakaypf vvliaalllw atvalsrsql
      181 gsafravres dvaaqamgvn vnaikrtaft lsaayagiag gmyttfasfi hpeslgfqtt
      241 ililtmvvvg gigsvrgaia galafglise llrqalsfqe iiygfilmgf mmfapkglfa
      301 grgergrvap pvapqpsapr qaaakptqrs aa
//
LOCUS       WP_176087708             296 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176087708
VERSION     WP_176087708.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 16009404
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..296
                     /product="helix-turn-helix transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=33469
     Region          40..95
                     /region_name="HTH_31"
                     /note="Helix-turn-helix domain; pfam13560"
                     /db_xref="CDD:433309"
     Site            order(41,66)
                     /site_type="active"
                     /note="salt bridge [active]"
                     /db_xref="CDD:238045"
     Site            order(48..49,60,63,67..68)
                     /site_type="other"
                     /note="sequence-specific DNA binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238045"
     Region          114..268
                     /region_name="MLTR_LBD"
                     /note="MmyB-like transcription regulator ligand binding
                     domain; pfam17765"
                     /db_xref="CDD:465492"
ORIGIN      
        1 mtatvapkrl ertradlsef lrlrrerlsp aelglpaggr rrtpglrree vaalagvgla
       61 wytwfeqgrn isvsadflen larvlkldaa errhlyllah qrppsepgrt wctvpaqvrr
      121 lmddlparpa yvlnlrwdvv vwnaaadrvf nfsaqapgrr nllwmlfadp amrelfvdwp
      181 aqapamlstf rrdfasagra pdvgelvdel ervspdfktw wrehdvhgsc mglrslslpa
      241 lgelafehst lsvdesrhlr lvvyapapde pktkdferwl raaatrraka argtse
//
LOCUS       WP_176087732             192 aa            linear   BCT 11-JAN-2025
DEFINITION  recombinase family protein [Achromobacter anxifer].
ACCESSION   WP_176087732
VERSION     WP_176087732.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Stark,W.M.
  TITLE     The Serine Recombinases
  JOURNAL   Microbiol Spectr 2 (6) (2014)
   PUBMED   26104451
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Keenholtz,R.A., Rowland,S.J., Boocock,M.R., Stark,W.M. and
            Rice,P.A.
  TITLE     Structural basis for catalytic activation of a serine recombinase
  JOURNAL   Structure 19 (6), 799-809 (2011)
   PUBMED   21645851
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Rice,P.A.
  TITLE     Resolving integral questions in site-specific recombination
  JOURNAL   Nat Struct Mol Biol 12 (8), 641-643 (2005)
   PUBMED   16077726
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Smith,M.C. and Thorpe,H.M.
  TITLE     Diversity in the serine recombinases
  JOURNAL   Mol Microbiol 44 (2), 299-307 (2002)
   PUBMED   11972771
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Hallet,B. and Sherratt,D.J.
  TITLE     Transposition and site-specific recombination: adapting DNA
            cut-and-paste mechanisms to a variety of genetic rearrangements
  JOURNAL   FEMS Microbiol Rev 21 (2), 157-178 (1997)
   PUBMED   9348666
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132968
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..192
                     /product="recombinase family protein"
                     /GO_function="GO:0000150 - DNA strand exchange activity
                     [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0006310 - DNA recombination [Evidence
                     IEA]"
                     /GO_process="GO:0015074 - DNA integration [Evidence IEA]"
                     /calculated_mol_wt=20997
     Region          4..135
                     /region_name="SR_ResInv"
                     /note="Serine Recombinase (SR) family, Resolvase and
                     Invertase subfamily, catalytic domain; members contain a
                     C-terminal DNA binding domain. Serine recombinases
                     catalyze site-specific recombination of DNA molecules by a
                     concerted, four-strand cleavage and...; cd03768"
                     /db_xref="CDD:239737"
     Site            order(9,11,72..73,76)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239737"
     Site            11
                     /site_type="active"
                     /note="catalytic nucleophile [active]"
                     /db_xref="CDD:239737"
     Site            order(71,116..117,119..120,124)
                     /site_type="other"
                     /note="Presynaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(77,82..83,112,115..116,119..120,123,126)
                     /site_type="other"
                     /note="Synaptic Antiparallel dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(101..103,112..113,116..117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Flat tetramer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(101,117,120,124,127,131)
                     /site_type="other"
                     /note="Synaptic Site I dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239737"
     Site            order(125,131..132)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:239737"
     Region          147..188
                     /region_name="HTH_Hin_like"
                     /note="Helix-turn-helix domain of Hin and related
                     proteins; cd00569"
                     /db_xref="CDD:259851"
     Site            order(148..150,182..183,185..187)
                     /site_type="DNA binding"
                     /note="DNA-binding interface [nucleotide binding]"
                     /db_xref="CDD:259851"
ORIGIN      
        1 msrvfaycrv stadqttdnq vreieaagfa ltprrtvteh isgsvsamer pkfkalsekl
       61 edgdvlvvtk ldrlgrnamd vrstvealat egvrvhclal ggvdltsaag rmtmqvlaav
      121 aeferdllie rtnagikrak adgktfgrpp altperqqev rqklaegvpv aqlardyktt
      181 rqtimrvrer sa
//
LOCUS       WP_176087779             479 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Achromobacter anxifer].
ACCESSION   WP_176087779
VERSION     WP_176087779.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..479
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49646
     Region          28..471
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(34..35,38..39,42,74,124..125,127..129,132,153,
                     156..157,160,255,258,289,292..294,297,325,329,381..382,
                     386,390,406,409..410,413..414,417)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 msststavip psllrdgvst wvatlvaclc afmvvmdgai vsvalpamrd dldlsavqlq
       61 wvvdiyllll ggfmllaara sdiygrrnvl lwglalftga slmgglaqsg aalliaravq
      121 gfgaaalats plavivaahp rgasqdraig cwaacaamgs afgvviggal tslvdwrwvm
      181 fvnvppglil famvalslsp qhpdtlrakl dmpgaitvtl slasflyavs qsvhagwndq
      241 ivfnamvfal vmflafvfre fcarqpliql gifrlrnvpi gmvmvsglga ilttstffls
      301 lalqridgrn pletgmallp mavalaiaam asrslrdagf trlpliggli aaagliwlyw
      361 lpmhpvhate lllptllaga gnglvmmsat qavlagvprr dsglaaglqn tsrqlggavg
      421 iavlasvahg vttarlagge mpqvaelagy qaafliagli sivsalasll ldvrppeaq
//
LOCUS       WP_176087822             342 aa            linear   BCT 11-JAN-2025
DEFINITION  ketopantoate reductase family protein [Achromobacter anxifer].
ACCESSION   WP_176087822
VERSION     WP_176087822.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Mondal,S., Nagao,C. and Mizuguchi,K.
  TITLE     Detecting subtle functional differences in ketopantoate reductase
            and related enzymes using a rule-based approach with
            sequence-structure homology recognition scores
  JOURNAL   Protein Eng Des Sel 23 (11), 859-869 (2010)
   PUBMED   20876192
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Mondal,S. and Mizuguchi,K.
  TITLE     Structural insights into the enzyme mechanism of a new family of
            d-2-hydroxyacid dehydrogenases, a close homolog of 2-ketopantoate
            reductase
  JOURNAL   Genome Inform 23 (1), 98-105 (2009)
   PUBMED   20180265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449024
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..342
                     /product="ketopantoate reductase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36139
     Region          8..321
                     /region_name="PanE"
                     /note="Ketopantoate reductase [Coenzyme transport and
                     metabolism]; COG1893"
                     /db_xref="CDD:441497"
ORIGIN      
        1 mkdahqcrva vygagaigcl laarlaqagc evtmiargqt laalrqrgvg ltvdgvtrhh
       61 avratddprq vrdveylfla vkqqaldeig ahlapmlapq gtvvpavngi pwwylptlas
      121 plgdaplqsv dgrgilrral plervlgsvv yiaahaaapg vaaqnarnnl ilgepdgsrs
      181 aratrlagll tasglqcevs drihqavwik amgnatfnpl svlahatmea mvrdpylgrl
      241 aramlgeyla lgtalgltlp vtveqrmqaa asagaartsm lqdalqgkpl eidalvgali
      301 eiaaklnldm pyanmvwglv rhrnlntvpl enqaqkitgd yt
//
LOCUS       WP_176087848            1101 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Achromobacter
            anxifer].
ACCESSION   WP_176087848
VERSION     WP_176087848.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 1101)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 1101)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1101
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..1101
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=115071
     Region          11..877
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mdptatpglf ssdarlygle gegalaslqv egwiareals giaqirlval sdsagldlgd
       61 misrpvtlwt tradgsragr sglvreaell sgdaglaryr ltiapwlwla tqqrnsrvfe
      121 arsvldivgh vlggyegyvh rvgadateal arvasrpytt qyretdydfi srllveaglg
      181 wtvvedpevp arhvvlifad srglaedaes asggvrfhra gatesrdtvq amvrqwrrgp
      241 drvtvlgwhd ggkravaaea larpadgsee tglewyevag hggfadeaea rrqanlaiea
      301 vqagaetfvg lggvrtfrsg trftlqnmsa lgpageegfe pvfaldrveh iginnlppet
      361 raslaqrlgg ldahltldae alappgaarp nadlpqadaa vlakarevgy anrfqavrcd
      421 rpwrpalpqa rgarlsgaps vhgvhtaivt gadgavqaqg gdeilrnkrg dvrirfhwqa
      481 dgdeglaksr warvaqrqsg agmgmsfvpr igqevlvrfl dddvdqpivv galyngrgeg
      541 gtpatpggrd ggqsdtqvya aardtapsaq anlaggnapa whgagggedn hrnaaalsgf
      601 kskefggsgy nqivfddsdg qmrlqikssl easelnlghl ihqagnyrgg lrglgaelrt
      661 daygavrgga gvllstyvga ggnagpagea aglqalasqa dqmarsldgv vgahqglrla
      721 salgakgada svlddgkapl aamhravsgt vagdsldgar sdasakhtqa adgkvphltd
      781 pvvlmaarag laqvsgehmq ytagetvhws sgrdqnlavm galrvhtgqg lgivaglqqg
      841 gadsgldlis atgdvqvqaq hdilrvqaqk ditmgsakts veyaapkrir iataagasiv
      901 leggnitvta pgridvktgn kqfagpdqms yalpvfvqsa pepmklalrl qdmpgahgia
      961 pegetwrivk vpagltvvqs ggrinpqvfd ssewsevlse gktpasgelg lteaqqysvh
     1021 sevmanpgrv wlisgltaqa mtparwttts eqatserild alnfarkgse ldtahadwls
     1081 ehaladgsaq gmetlkpktk a
//
LOCUS       WP_176087828             826 aa            linear   BCT 11-JAN-2025
DEFINITION  heavy metal translocating P-type ATPase [Achromobacter anxifer].
ACCESSION   WP_176087828
VERSION     WP_176087828.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 826)
  AUTHORS   Bublitz,M., Morth,J.P. and Nissen,P.
  TITLE     P-type ATPases at a glance
  JOURNAL   J Cell Sci 124 (Pt 15), 2515-2519 (2011)
   PUBMED   21768325
  REMARK    Erratum:[J Cell Sci. 2011 Nov 15;124(Pt 22):3917]
REFERENCE   2  (residues 1 to 826)
  AUTHORS   Chan,H., Babayan,V., Blyumin,E., Gandhi,C., Hak,K., Harake,D.,
            Kumar,K., Lee,P., Li,T.T., Liu,H.Y., Lo,T.C., Meyer,C.J.,
            Stanford,S., Zamora,K.S. and Saier,M.H. Jr.
  TITLE     The p-type ATPase superfamily
  JOURNAL   J Mol Microbiol Biotechnol 19 (1-2), 5-104 (2010)
   PUBMED   20962537
REFERENCE   3  (residues 1 to 826)
  AUTHORS   Arguello,J.M., Eren,E. and Gonzalez-Guerrero,M.
  TITLE     The structure and function of heavy metal transport P1B-ATPases
  JOURNAL   Biometals 20 (3-4), 233-248 (2007)
   PUBMED   17219055
REFERENCE   4  (residues 1 to 826)
  AUTHORS   Apell,H.J.
  TITLE     How do P-type ATPases transport ions?
  JOURNAL   Bioelectrochemistry 63 (1-2), 149-156 (2004)
   PUBMED   15110265
REFERENCE   5  (residues 1 to 826)
  AUTHORS   Axelsen,K.B. and Palmgren,M.G.
  TITLE     Evolution of substrate specificities in the P-type ATPase
            superfamily
  JOURNAL   J Mol Evol 46 (1), 84-101 (1998)
   PUBMED   9419228
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457611
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..826
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..826
                     /product="heavy metal translocating P-type ATPase"
                     /EC_number="7.2.2.-"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0019829 - ATPase-coupled monoatomic
                     cation transmembrane transporter activity [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0140358 - P-type transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /calculated_mol_wt=85042
     Region          11..>56
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          76..144
                     /region_name="CopZ"
                     /note="Copper chaperone CopZ [Inorganic ion transport and
                     metabolism]; COG2608"
                     /db_xref="CDD:442020"
     Region          166..817
                     /region_name="P-type_ATPase_Cu-like"
                     /note="P-type heavy metal-transporting ATPase, similar to
                     human copper-transporting ATPases, ATP7A and ATP7B;
                     cd02094"
                     /db_xref="CDD:319783"
     Site            order(465,467,772)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
     Site            order(509..511,574,590..592,621,661..663,683,686,689,708,
                     711)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319783"
     Site            order(773,801,805)
                     /site_type="other"
                     /note="putative Cu binding site [ion binding]"
                     /db_xref="CDD:319783"
ORIGIN      
        1 msaitadsva vslpiegmtc ascvgrveka lkavpgisqa svnlaterad itfdgtpdva
       61 aavqavqkag ytvaettvel svtgmtcasc vgrvekalka vpgvsnatvn laterasita
      121 aggvssaali qavakagyea raiaaessdt davaerqaae lkslkrslti atifalpvfi
      181 lemgahivpa fhhviaqtig tqnswylqfa lasivlfgpg lrffkkgipa llrgapdmns
      241 lvavgtsaay aysvvatfaa gllpagtvnv yyeaaaviva lillgrymea rakgntseai
      301 krllglqakt arvvrngatq elaidqvvag dlievrpger ipvdgevveg nsfidesmis
      361 gepvpvekqp gsevvggtvn qngaltfrat kvggdtvlaq iirmveqaqg sklpiqalvd
      421 ritmwfvpav maaavatfii wlvfgpdpal tfalvnavav liiacpcamg latptsimvg
      481 tgraaqmgvl frkgealqsl kdakvvavdk tgtltkgrpe ltdlivaagf eraavlgqva
      541 tveaksehpi aqaildaare qgialgaisq fesvtgfgvs alvdgalvqi gadrymrelg
      601 lsvesfgada arlgdegktp lyaaidgkla amiavadpik ettaaairal hdlglkvami
      661 tgdnrrtgea iarqlgidev vaevlpdgkv aavqrlkqqy gpiayvgdgi ndapalaead
      721 vglaigtgtd iaieaadvvl msgdlggvpn aialskatir nikqnlfwaf aynvalipva
      781 agllypvngs llspvfaaga malssvfvls nalrlrrfaa pfpara
//
LOCUS       WP_176087886             302 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176087886
VERSION     WP_176087886.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..302
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33404
     Region          <22..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          99..298
                     /region_name="PBP2_DntR_NahR_LinR_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators that are involved in
                     the catabolism of dinitrotoluene, naphthalene and
                     gamma-hexachlorohexane; contains the type 2 periplasmic
                     binding fold; cd08459"
                     /db_xref="CDD:176148"
     Site            order(105,107..108,112,170,206,273)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176148"
     Site            order(106,109..110,113..114,117..118,120..121,124..125,
                     127..131,133,196,223..227,230..231,234..235,238,252)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 maelrdvdln llllfqhlle drnlsavarr mdlsqpavsn alrrlreafg delfvrtaqg
       61 mqptpraqrl agpvsealtv lsqalkdqdv fdattstrrf rvamtdvgei hfmprlmevc
      121 vqvaplvrid svrvqgadll remeagrvdl aigafdemga gtlqrmlfrq gyatlfrqah
      181 ptahagmglk afraerhliv sraapygqvn qsmeragvdl aehfsvphfs avpyivsatd
      241 llatvpekla asaappfglr ymtppirvpa lqtnmywqrr vdrdsgnqwl ralivntfav
      301 ga
//
LOCUS       WP_176087952             383 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Achromobacter anxifer].
ACCESSION   WP_176087952
VERSION     WP_176087952.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..383
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=41423
     Region          3..381
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 msnidltpeq qelqhsirrf mlaevaplva qhekartfpf elmpklaelg ylggnlpedq
       61 gghgidmptw ammmeelgyh wlslrtivni tngsikrlaa hgspaqkeky lkplmaghlk
      121 actgltepnt gsniagiqtr adlvgdewvl ngrklwitng cdadfamvva rtfsptcegk
      181 lstfiveral anydvrkldt mvlrctgtae lgfadvripk enlvgvegaa lagtlkglda
      241 arlniamgav gaaqaaldls tdyakqreqf grpigsfqlv qkhivdmtvr veaaralgmr
      301 aahaleagkd vrqacsiakl yateaaheva nmalqvhggl gyseeypier ifrdtrggmi
      361 pegtteiqtl iagreilgmn aia
//
LOCUS       WP_176087986             285 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176087986
VERSION     WP_176087986.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..285
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=30869
     Region          10..252
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mnpesstlyv qslatgiavl dafdaehtsm slpdiaaaag itrsaaqrfa ftlealglln
       61 kdpvskrysl ssrtldtgcr yleshplldr anpfllelnr nagetvnlae psgqdmiyig
      121 rfpsplrllv hmpvgrripm ycsstgrvyl agmsdeqaye alaaservky tantltdvde
      181 lmaqihlsre qgyacckeey yrgdlalavp vydlnqrvva glqlsvsaak wtvkravsrf
      241 vpmmletarq istspptpra ltafgggaar dlhaeppgkv ggrka
//
LOCUS       WP_176088046             267 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176088046
VERSION     WP_176088046.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 267)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 267)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13673967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..267
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=27991
     Region          22..146
                     /region_name="AraC_binding"
                     /note="AraC-like ligand binding domain; pfam02311"
                     /db_xref="CDD:396749"
     Region          <145..262
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mspgqflmqr salagvqava ahsrhafsrh theqfgigvm rlgaqvshsg rgqveagpgh
       61 vitvnpgevh dgaplgdgvr awqmlyldpa vvaqaaaeld agnqgyefeh paqdrpalar
      121 dvlalyaqat agaaplacda lllrilaqar dggasrlelp ravpdairya ralidddpaa
      181 slsladlaaa sglsryqvlr afaratgltp hayqvqrrll larslirqgt aladaaaavg
      241 fadqshmtrl fvraygvspr ryalaag
//
LOCUS       WP_176088049             314 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176088049
VERSION     WP_176088049.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..314
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33953
     Region          8..63
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          97..295
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(111..112,114..115,118,122,124..130,223..228,
                     234..235,237..238)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdgglsarrl qyffeavttg svrgaaerlg vepsivsrqi qlletelgva llerkgrgiv
       61 ptdmaaivmd hcrdrqaseq alrarldevn glqrgdiqiv asegfvdllm sgvvdefcrq
      121 hpgvrvslkv agasdavrav vhddahigvv fgapadpgir vvhtrnhplc viawpdhpla
      181 rqrkrpalkd varypvalmg pgfglrqlie maelsenivl spsfiansvv tlkryvesrl
      241 gltftsansv vkevargelv alrttnpife aaqtrlivra nrpltsaarg mleriqaspl
      301 flgakpqram pgka
//
LOCUS       WP_176088180             494 aa            linear   BCT 11-JAN-2025
DEFINITION  aminotransferase class V-fold PLP-dependent enzyme [Achromobacter
            anxifer].
ACCESSION   WP_176088180
VERSION     WP_176088180.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   2  (residues 1 to 494)
  AUTHORS   John,R.A.
  TITLE     Pyridoxal phosphate-dependent enzymes
  JOURNAL   Biochim Biophys Acta 1248 (2), 81-96 (1995)
   PUBMED   7748903
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11424849
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..494
                     /product="aminotransferase class V-fold PLP-dependent
                     enzyme"
                     /EC_number="2.6.1.-"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0031071 - cysteine desulfurase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006534 - cysteine metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0016226 - iron-sulfur cluster assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=52604
     Region          45..466
                     /region_name="CsdA"
                     /note="Selenocysteine lyase/Cysteine desulfurase [Amino
                     acid transport and metabolism]; COG0520"
                     /db_xref="CDD:440286"
ORIGIN      
        1 mntptktapa katplqqfqa slktddvaaa ladgligkda vvdgpygikp lvyadyvasg
       61 ralmqverfv leqvlpyyan shteasycgg fitrlrrear aaiarccgag dkhavifags
      121 gataginrlv hlfgvreaia agrkvrviig pyehhsnilp wrecgaeive laesaaggpe
      181 ltqldaalqa gegalvical saasnvtgiv advaqvtrrv kaagakmlwd yaggapylpm
      241 qmspaadaai daivfsphkf iggpgasgvl ivrrdavldt kptwpgggtv rfvspvghdy
      301 sgsleareea gtpnvvgdir aalvllvkea lgadfmrqrn ehfvrralar wqgaaqlell
      361 gsltasrlpi fsfrvrngrg gyvhqqlvtr mlsdrfgiqa rggcacagpy vhrlldigad
      421 eslqmrqail dgremekpgf irlnfsvllp dekadfilds vlalaadate fedrygfdps
      481 raiffphsae qqaa
//
LOCUS       WP_176088171             213 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176088171
VERSION     WP_176088171.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..213
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=22376
     Region          23..180
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mpatpadpls lpagkdaaak prtkpaavrl delmaaaeal fiekgveaat iseiveragv
       61 akgtfyhyft skndmlaalr akfsqgfldh iaravdacap ddgvarlraw tqagveayfd
      121 gyelhdvvfh daqhpdrgta eksavlrqle aileagarag cwplddaala aivlyhgmhg
      181 avdasiaqgr rdapalsgpl aamflrtlga ras
//
LOCUS       WP_176088201             215 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Achromobacter anxifer].
ACCESSION   WP_176088201
VERSION     WP_176088201.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..215
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23788
     Region          1..210
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mmtiwgrrss fnvqkvlwla gelgldyehv laggqhglld taeframnph gkvpllrdga
       61 tvvweshail rylaardgag rfwaddpaqr agadgwmdwa qtalqpafls gvfwgyyctp
      121 eaqrdaaaig raiaathacl eqldraladq pylggeslgl adipagttly ryfeldiphl
      181 plahvqawye rlqarpayre hvmvpfgelr grlaf
//
LOCUS       WP_176088271             475 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Achromobacter anxifer].
ACCESSION   WP_176088271
VERSION     WP_176088271.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..475
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=50337
     Region          1..474
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 msdslcelsa veaarlirar slspvelvra sleraerlqp vlncfitlcp eqamaearra
       61 eaalmrgdap gllhglpftv kdlvntagvr ttfgalpfrd nvpaedavav arlreqgail
      121 igktttpefg sksmtdsplf gqtrnawnle rtcggssgga aaataagita lavasdgggs
      181 tripaacngv vgfkqslgai phsqaqdaig nqtyvtpttr tvadtrlmma amagphdcdp
      241 wslgvprady anaaagpgtl rgkrirycaa ppgrpvdagv rrafeaalar ladlgaeiep
      301 fdgagfdvep vwrvinhtvw rarflplier epeaysptfr rqiasaaqfs aqqyqeamfa
      361 rtalyrkvqa llgqadllam ptmsrtalpl gadifdtiti dgrayddira hwypwtmlfn
      421 ltghpaisvp cglgddgmpv glqlvarshg dlqllqaaea yelagaplpr ppava
//
LOCUS       WP_176088209             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176088209
VERSION     WP_176088209.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444116
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=33288
     Region          13..>160
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          98..296
                     /region_name="PBP2_CrgA_like_6"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08475"
                     /db_xref="CDD:176164"
     Site            order(108,112,151,166,168,231,248,275)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176164"
     Site            order(109..110,114..115,117..118,121,125,127..133,195,
                     225..229,236..237,240)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176164"
ORIGIN      
        1 mattithdrl sgievfvqav eagsfalaae rlnltrsavg ksiarlearl garlfhrttr
       61 qqsltddgqa yydrcvrala elqtaeaeld sgrrepqgrl rvsaplvfgr hcvapvlrdl
      121 alqypqlqve isfndrvvdl ieegydlgir vgdlpdsssl aarrlgtqtm gigaspayiq
      181 ahgrpsgvde lmqhagiiyt hngverawti kdadgqalql rlsprlrldd lqaiadaais
      241 gaglawlpcw mlshyvrtge ldvlmhgdrl asqevhavwp qarylpsktr aaidalaarv
      301 pamlaa
//
LOCUS       WP_176088231             345 aa            linear   BCT 11-JAN-2025
DEFINITION  FAD:protein FMN transferase [Achromobacter anxifer].
ACCESSION   WP_176088231
VERSION     WP_176088231.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Bertsova,Y.V., Fadeeva,M.S., Kostyrko,V.A., Serebryakova,M.V.,
            Baykov,A.A. and Bogachev,A.V.
  TITLE     Alternative pyrimidine biosynthesis protein ApbE is a flavin
            transferase catalyzing covalent attachment of FMN to a threonine
            residue in bacterial flavoproteins
  JOURNAL   J Biol Chem 288 (20), 14276-14286 (2013)
   PUBMED   23558683
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003878
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..345
                     /product="FAD:protein FMN transferase"
                     /EC_number="2.7.1.180"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0017013 - protein flavinylation [Evidence
                     IEA]"
                     /calculated_mol_wt=36255
     Region          43..338
                     /region_name="ApbE"
                     /note="FAD:protein FMN transferase ApbE [Coenzyme
                     transport and metabolism, Posttranslational modification,
                     protein turnover, chaperones]; COG1477"
                     /db_xref="CDD:441086"
ORIGIN      
        1 masspsyaqr gapaaavsva ygampvrpaa aaalaaalag atmgttwsar malpagltea
       61 aarqaiqaal devvaqmstw esgsdisryn qaaagwqtlp aeffhvlsha ltlaedsgga
      121 ydptvgplvn awgfgphqra yeppspaaie aararcgwrr vqldaerraa lqpggvyldl
      181 ssiakgygvd raaqaldalg itqylvevgg elrargrrpd gqpwrvaiev pdasddhala
      241 lplrdrsiat sgdyrrhags ddqryahtid prtglpvrnt lasvtvlhsg cmeadalatv
      301 ltvlgetdgl ayarrhdlaa lfilrerdaw rvvatpafqa laand
//
LOCUS       WP_176088283             397 aa            linear   BCT 11-JAN-2025
DEFINITION  cytochrome-c peroxidase [Achromobacter anxifer].
ACCESSION   WP_176088283
VERSION     WP_176088283.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448982
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..397
                     /product="cytochrome-c peroxidase"
                     /EC_number="1.11.1.5"
                     /GO_function="GO:0004130 - cytochrome-c peroxidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /calculated_mol_wt=42646
     Region          105..397
                     /region_name="MauG"
                     /note="Cytochrome c peroxidase [Posttranslational
                     modification, protein turnover, chaperones]; COG1858"
                     /db_xref="CDD:441463"
ORIGIN      
        1 maasrlpvli lglalalaap asradtagnt rpaadaaack gpagwdaacl rrhyagpsaa
       61 wpapvidpgv awrewapvps assaplswta anagqqelaa dvarpaivtl gqtlffdtrl
      121 srkgqvscas chlpqraftd glalavgedk lmgrrrstpl yaapfaprlf wdgraaslkq
      181 qvlgpihdpr emnhdaggvv arlldtepyp aeflrafgaa papqppvdad rlaralaayv
      241 atlrpeptrf defldgrpda lddaemvgmh lfrtqarcmn chsgalltdh gfhdiglsfy
      301 grrnqdlgry evtrdaadlg kfrtpslrnv sragpwmhng lfpdlkgllr mynagmgrdp
      361 apadppdpha prksehirpl dlsadeidal lafmrvl
//
LOCUS       WP_176088302             292 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Achromobacter
            anxifer].
ACCESSION   WP_176088302
VERSION     WP_176088302.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 292)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..292
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=30527
     Region          5..291
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mdvlfflevt laglgsggly alaalafviv ykatrvvnia igeflmlgay vfyafatgme
       61 wpiwlaivga vvvsgalgal verltirpml geapisvfmi tvglasilvg vveliwtadq
      121 rrlpefmpra pvmigeafva pkvfygfwva vvlallvlvv frywrggval ratasdqgaa
      181 yamginvprv fslawvaaga laavsgvivg aiggisssmg vfglsvlvvv ivggldsvag
      241 alvggvfigl leawagaymg geykllatfi vlvvvlmvrp yglfgtreie rl
//
LOCUS       WP_176088322             289 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Achromobacter anxifer].
ACCESSION   WP_176088322
VERSION     WP_176088322.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..289
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=31516
     Region          9..261
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mtsifgkeln irgvakrydg pgdgaqalqv lqdihldvpa gqfvsivgas gcgkstllrl
       61 ilgldddyag qilldgkpvr gagldrgivf qdhrlfpwls vernigaalr naplskaekr
      121 elvaehialv glqgfeksyp hqisggmaqr vaiarglvnr prvllldepl galdaltrsr
      181 lqnelqriwq qekitmvlvt hdveeavflg drvvvmqprp grirrivdvd lphprnrsdp
      241 rfirlrddvl sdfldpdgrv adgealppsg gllatvgglp algrlrmaw
//
LOCUS       WP_176088331             240 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176088331
VERSION     WP_176088331.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..240
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26287
     Region          27..237
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mttlsrgsaa aplaapangq rlgervrslg devyetllsq lislkiapgm riavdalvre
       61 lgvsqtpira alirletegl vvkthhvgys aapmptrrrf eqmyelrlql epfgaglaaq
      121 rmtdaslqel aalsaamsap saddarvayg kfavldaqfh swiaeqsgne llaealarly
      181 ahthlfrlrf hsrvteeavt eharivqaln ardaagaqdt mrdhilrsre rmapyfemld
//
LOCUS       WP_176088340             538 aa            linear   BCT 11-JAN-2025
DEFINITION  GMC family oxidoreductase [Achromobacter anxifer].
ACCESSION   WP_176088340
VERSION     WP_176088340.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Wongnate,T. and Chaiyen,P.
  TITLE     The substrate oxidation mechanism of pyranose 2-oxidase and other
            related enzymes in the glucose-methanol-choline superfamily
  JOURNAL   FEBS J 280 (13), 3009-3027 (2013)
   PUBMED   23578136
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Cavener,D.R.
  TITLE     GMC oxidoreductases. A newly defined family of homologous proteins
            with diverse catalytic activities
  JOURNAL   J Mol Biol 223 (3), 811-814 (1992)
   PUBMED   1542121
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..538
                     /product="GMC family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=58232
     Region          1..531
                     /region_name="BetA"
                     /note="Choline dehydrogenase or related flavoprotein
                     [Lipid transport and metabolism, General function
                     prediction only]; COG2303"
                     /db_xref="CDD:441878"
ORIGIN      
        1 metydyiivg agsagcvlan rlsrdpaaqv llleaggrdn yhwihipvgy lhcignprtd
       61 wmyrtvaepg lggrsliypr grvlggcssi ngmiymrgqr qdyedwaals gdpawgwdqv
      121 lpvfkrsedy hrgadefhga ggewrvesqr lrwdileafa gaaeqegipr vqdfnrgdnf
      181 gcgyfevnqr ggwrwntska flrpvqkrpn lhvmtgaqae qlvfegkrcv gvqlrrggqs
      241 vtlrarrevv laagavntph llelsgvgep arlresgial rhalpgvgen lqdhlqlrvi
      301 lqvqgvktln riastwwgka gigleyllkr sgpmsmapsq lgafaksdpg qaranvefhv
      361 qplslgafge plhgfdafta svcnlrptsr gsvhaqgpqg apvispnyls tdadlrvaad
      421 sirlvrriaa apalqryqpq ewlpgpafqt daelreaagk igttifhpvg tcamgrdadg
      481 gavvdarlrv lgleglriad asvmplitsg ntnsptimia eraadmired agggsaar
//
LOCUS       WP_176088375             305 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176088375
VERSION     WP_176088375.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..305
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32840
     Region          10..68
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          99..285
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(113..114,116..117,120,124,126..132,225..230,
                     236..237,239..240)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mensaeavsl rqlralvsva dtasftiaad qlglsqpsis hlirrlenev gqalvirgre
       61 vsltaqgral admarrsimt idsalkecrd qsqlrtgsvs vavghvsaat llpqilhafh
      121 aqhpalemqv vdcmveqikn klvsheadlg igamveggdt qimlenlidg svhlfmrddh
      181 plaarkqvda kvlaelrciq lnpqapawla isrqlaaeei fprieqrvil lstafgmvqa
      241 gmgvamlpsf asaqmppgik avplrnpvld wpvslarlan rplspaaqaf aavartvlrr
      301 qfara
//
LOCUS       WP_176088381             316 aa            linear   BCT 11-JAN-2025
DEFINITION  GlxA family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176088381
VERSION     WP_176088381.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Bandyopadhyay,S. and Cookson,M.R.
  TITLE     Evolutionary and functional relationships within the DJ1
            superfamily
  JOURNAL   BMC Evol Biol 4, 6 (2004)
   PUBMED   15070401
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11471967
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..316
                     /product="GlxA family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=34575
     Region          2..316
                     /region_name="GlxA"
                     /note="Transcriptional regulator GlxA, contains an amidase
                     domain and an AraC-type DNA-binding HTH domain
                     [Transcription]; COG4977"
                     /db_xref="CDD:444002"
ORIGIN      
        1 mhtiavvafa gissfhlsvp cmvfgddlar lgapryrllv cgeavepvat msgfdihvph
       61 dysalaeadt vivpawrdpd erppetmlqa lrdahargar viglclgafv laeaglldgr
      121 pasthwvwsd dfarkypqir ldrkalyvdd gdiltsagta aaidcclhll rcdhgaelan
      181 rvarrmvmap hrdggqaqyi erpltredgg dpisvamewa iehlqeplgl drlaseagls
      241 rrnftrrfkl ktgttvtqwv lnhrlaaaqr lletgglsvd rvaeatgfgs tvslrqhfta
      301 afsvspaayr kqfrqr
//
LOCUS       WP_176088393             223 aa            linear   BCT 11-JAN-2025
DEFINITION  HNH endonuclease [Achromobacter anxifer].
ACCESSION   WP_176088393
VERSION     WP_176088393.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Zhang,L., Xu,D., Huang,Y., Zhu,X., Rui,M., Wan,T., Zheng,X.,
            Shen,Y., Chen,X., Ma,K. and Gong,Y.
  TITLE     Structural and functional characterization of deep-sea thermophilic
            bacteriophage GVE2 HNH endonuclease
  JOURNAL   Sci Rep 7, 42542 (2017)
   PUBMED   28211904
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003646
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..223
                     /product="HNH endonuclease"
                     /GO_function="GO:0003676 - nucleic acid binding [Evidence
                     IEA]"
                     /GO_function="GO:0004519 - endonuclease activity [Evidence
                     IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25204
     Region          122..170
                     /region_name="McrA"
                     /note="5-methylcytosine-specific restriction endonuclease
                     McrA [Defense mechanisms]; COG1403"
                     /db_xref="CDD:441013"
ORIGIN      
        1 mayafdlrqv cggyayfstf thgdlspddr yeirvpsevn vdrfstalee lgqsfqfids
       61 edsyriwiys qgwavvapaf arsrmqnwlk qhkcistalg aftdieiaap svmkrsfrgv
      121 akkkildrdg grclecgsqn altlqhvipf saggetssrn mvtlceecnq syrdeinpel
      181 crlaglhygy epsliklapd rqtalrravy fsnnlmhtrc dlw
//
LOCUS       WP_176088402             335 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Achromobacter anxifer].
ACCESSION   WP_176088402
VERSION     WP_176088402.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..335
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36078
     Region          13..326
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 msadrhtaga ptlevrnlrt hfhtragvlp avddvsftle rgkilglvge sgsgksvtgf
       61 simglvdapg rivggevlfq grdltklapr elrklqgnri amifqdpmmt lnpvlrvdaq
      121 mietvrahnk msaaqarals rdtlgmmgip speerllayp hqlsggmrqr vaiaiamlhr
      181 pdliiadept taldvtiqaq ilsevqklaq qhgtsliwit hdlsvvagla ddvavmyagr
      241 ivehgtvddv ldrpqhpytv glidslpsnn qrgqrlrqip gmtpnllnlp agcafaarcs
      301 rataacgqqp gitqalpehk vrcfhptiqt seama
//
LOCUS       WP_176088412             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176088412
VERSION     WP_176088412.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33397
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          93..285
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,220..225,
                     231..232,234..235)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mefrqlecfi avaeelhfgr aaerlcmtqp plsrqiqlle qdlgvtlfer nsrqvllsaa
       61 grrflrdarh llefsaraaa sarrtsggea ghitlgftav aayrlmpsmi mrarkllggv
      121 eiqlretvst dlgrlllare vdailarsip qqagiearlv ereplvlalp agsplcehat
      181 vplrllhgqp fvlyspregk yfydrivgaf gladvqpdyv qragqthtll alvraglgvg
      241 ivpdsarelr fegvefrpig qrnlyadmyl awhaqhdnpa leaflqrvve vdraassrrr
      301 a
//
LOCUS       WP_176088470             137 aa            linear   BCT 11-JAN-2025
DEFINITION  PaaI family thioesterase [Achromobacter anxifer].
ACCESSION   WP_176088470
VERSION     WP_176088470.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Kunishima,N., Asada,Y., Sugahara,M., Ishijima,J., Nodake,Y.,
            Sugahara,M., Miyano,M., Kuramitsu,S., Yokoyama,S. and Sugahara,M.
  TITLE     A novel induced-fit reaction mechanism of asymmetric hot dog
            thioesterase PAAI
  JOURNAL   J Mol Biol 352 (1), 212-228 (2005)
   PUBMED   16061252
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Dillon,S.C. and Bateman,A.
  TITLE     The Hotdog fold: wrapping up a superfamily of thioesterases and
            dehydratases
  JOURNAL   BMC Bioinformatics 5, 109 (2004)
   PUBMED   15307895
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005230
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..137
                     /product="PaaI family thioesterase"
                     /EC_number="3.1.2.-"
                     /GO_function="GO:0016790 - thiolester hydrolase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016836 - hydro-lyase activity [Evidence
                     IEA]"
                     /GO_function="GO:0047617 - fatty acyl-CoA hydrolase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=14923
     Region          1..136
                     /region_name="PaaI"
                     /note="Acyl-CoA thioesterase PaaI, contains HGG motif
                     [Secondary metabolites biosynthesis, transport and
                     catabolism]; COG2050"
                     /db_xref="CDD:441653"
ORIGIN      
        1 mlratetidn llerqrgtlp dtfgvrpvsi eegrmamemt vapwmmapng ylhaatqvml
       61 adtcagyatl ahlpegakgf ttlelksnfl gtakegvlrv eavaehmgrt tqiwsatvvd
      121 angrklslfr csqiilw
//
LOCUS       WP_176088460             123 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Achromobacter anxifer].
ACCESSION   WP_176088460
VERSION     WP_176088460.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..123
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=13529
     Region          1..123
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mqidhlilrv adaarsisfy qqvlalphas appfevlrlg ngcvidlleq apndpvhlal
       61 evdrkafeav yqrlrtlglp fggdaftrdg gigwqygarg wadalyfhdp dlhsievrty
      121 daa
//
LOCUS       WP_176088525             518 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Achromobacter
            anxifer].
ACCESSION   WP_176088525
VERSION     WP_176088525.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..518
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=56171
     Region          4..517
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 marlidffer glrmsaeapc faepggrvld ygtvadishr ianglhaagi gpgdkvglls
       61 pnhlltfvav lgivrsrgvw lpvnarnsie enlhvlargh caflflhgsf agdldqiraa
      121 lpdlkglvfi dgpqeqapgl eewaaiqsaa pveseasade vvairgtggt tglpkgvlvt
      181 hrmyatllan wfaampvret pvhlvvaplt haagmvafat layggvnivl psarpeaile
      241 aierhrvtql fcpptviyrl lahsdarrrr ydslryfvys aapmsaakle lalevfgpvm
      301 vqcygqaeap ftctsmtaed hiaamqpgag hrlascgraa pfarvevmdp qgrllgader
      361 geivvrgdlv mpgyynnpeg taqalrdgwl htgdvgyrdv dgffyivdrm kdliisggfn
      421 ispgkieqvl wahplvndca vigvpdedwg eavkaivelk pgaawseeqa iaycrsrldg
      481 mktpksvefr delprsqvgk vlkqqlrepy wagrdrrv
//
LOCUS       WP_176088557             259 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176088557
VERSION     WP_176088557.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Jain,D.
  TITLE     Allosteric control of transcription in GntR family of transcription
            regulators: A structural overview
  JOURNAL   IUBMB Life 67 (7), 556-563 (2015)
   PUBMED   26172911
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Haydon,D.J. and Guest,J.R.
  TITLE     A new family of bacterial regulatory proteins
  JOURNAL   FEMS Microbiol Lett 63 (2-3), 291-295 (1991)
   PUBMED   2060763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450764
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..259
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=28961
     Region          22..259
                     /region_name="MngR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG2188"
                     /db_xref="CDD:441791"
ORIGIN      
        1 maeprpetsl riraarpage gaafsplyrq ikdllvqsle rgewkpgeli pseidlaarf
       61 qvsqgtvrka vdelaaehml lrrqgkgtfv athhearvry rflrlaadde geagraesri
      121 lecrrlrapa eiaraldlrv getvimirrl lslghaptvv ddiwlpgsif rgltlellsa
      181 nkaplyglfe sefgvsmvra deklravlap aevcpllnvp pgtpllqvdr vsytygdrpm
      241 eirrglyltd ryhyrnsln
//
LOCUS       WP_176088565             591 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Achromobacter anxifer].
ACCESSION   WP_176088565
VERSION     WP_176088565.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 591)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..591
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64047
     Region          3..533
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msaaqpllsv rdleirfpgk rdaapvvnrv sfdlhagesl sivgesgsgk tligktllgl
       61 lpdsarisgg qalfegqdll rqtprdwlak rgtgigmvfq epmvslnpaf rvgeqlieal
      121 vlrrgmtrra awdeavrmle rvrvrdardc mkryphefsg gmrqrillag vmllkprlli
      181 adepttaldc vvqkevldlm celtreqdta lifishnlal vaaytqrvlv mcrgravetg
      241 pvaevlsrpa dpytlsllda lpkrgparaa vdrppilqvd glaidysvre gwfskravra
      301 vhqatfavap getlaivges gsgkttvmms ilglvpqaqg rieldgqalp aggsgqawqa
      361 arrrvqmvfq dpyssldprm tigdlvgegl rleagmtpei rrqrvaealr dvglgdgyae
      421 ryahelsggq rqrvaiaral vlrpeviiad epvsaldvtv qkqvletlms lqrshgfacl
      481 lishdlgvve qiadrvvvml rghiveegtr devfdrpthp ytrrllqavp elrgnpaegf
      541 rvevrdlpag qgrdeadyfd psaalgapam aavlesgath rvalaaaaag a
//
LOCUS       WP_176088612            1057 aa            linear   BCT 11-JAN-2025
DEFINITION  efflux RND transporter permease subunit [Achromobacter anxifer].
ACCESSION   WP_176088612
VERSION     WP_176088612.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Nikaido,H. and Takatsuka,Y.
  TITLE     Mechanisms of RND multidrug efflux pumps
  JOURNAL   Biochim Biophys Acta 1794 (5), 769-781 (2009)
   PUBMED   19026770
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Tseng,T.T., Gratwick,K.S., Kollman,J., Park,D., Nies,D.H.,
            Goffeau,A. and Saier,M.H. Jr.
  TITLE     The RND permease superfamily: an ancient, ubiquitous and diverse
            family that includes human disease and development proteins
  JOURNAL   J Mol Microbiol Biotechnol 1 (1), 107-125 (1999)
   PUBMED   10941792
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436314
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..1057
                     /product="efflux RND transporter permease subunit"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0042908 - xenobiotic transport [Evidence
                     IEA]"
                     /calculated_mol_wt=115360
     Region          21..1034
                     /region_name="AcrB"
                     /note="Multidrug efflux pump subunit AcrB [Defense
                     mechanisms]; COG0841"
                     /db_xref="CDD:440603"
ORIGIN      
        1 msgahqdapa qaqrheegrf nlsawalrhq plvifiitli tlfgvlsysk laqsedppft
       61 frvmviktlw pgataqqvqe qvtdrvakkl qeapntdfmr sysrpgesli fytmkdsapa
      121 stvaeqwyqv rkkvgdiaat lppgvqgpff ndefgdvytn iytlqgdgfs aaqlrdyadr
      181 lrtvllrvpg vakvdyfgdq pehiyveisn tqltrlgvsp qqivqainsq navasagtlt
      241 taddrifvrp tgqypdsral adtlirvdgk sirlgdiati hrgyddptve qmrlggaavl
      301 gigitmqpgr dvvhlgkalg akfdelqaql pagltlkevs smpkavshsv ddflrsvaea
      361 vaivlavslv slglrtgmvv visipvvlav talfmdmfgi glhkvslgtl vlalgllvdd
      421 aiiavemmav kleqgwsrar aaafaytsta fpmltgtlvt vagflpiala ksstgeytrs
      481 ifqvsaiali tswfaavvli pllgyrmlpe rkreahlpdd hehdiyntrf yqrlrgwvgw
      541 cvdrrylvlg atvlvfvvsm acfrfvpqqf fpssdrsell vdvrlqegas faatlrqver
      601 lekalegrpe idhsvsfvgt gaprfylpld qqlatpnfaq lvitahsved reklaqwlqp
      661 vlreqfpair srlsrlengp pvgfqvqfrv sgdkiaevra vaeqvaaevr adprstnvqf
      721 dwdepsersv rfeidqqkar elgisssdis dflamtlsgy tvtqyrerdk linvslrapr
      781 eeridparls tlamptpngp vplgsighvr ygleygviwe rdrqptitvq advtagaqgi
      841 dvthaidakl aalraglpvg yrvevggpve esakgqssin aqmplmavav ltllmlqlqs
      901 farvlmvvlt aplgligvva alllfgkpfg fvamlgviam fgiimrnsvi lvdqieqdig
      961 aghkrvdaiv gatvrrfrpi tltaaaavla lipllrsnff gpmatalmgg itiatvltlf
     1021 flpalyaawf rvrhderdep egvppganag dtverga
//
LOCUS       WP_176088569             497 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Achromobacter anxifer].
ACCESSION   WP_176088569
VERSION     WP_176088569.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..497
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=52993
     Region          7..483
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(64,66,70,73,77,110,113..114,123..130,135,138,141,
                     234,238,241,244,246,419,421..422,424..425,428,431..432,
                     434,436..439,448,452,454,468,475..480,482..483)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(150..153,161,176,179,209,226..229,232,250..252,284,
                     384,386,412)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(153,250,281,284)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 msevprvpll iggklvqskt tewrdvinpa nqevvakvpf atreeldlav snakeafktw
       61 rnsgqgarmr vmlkfqellr antaklaemi trehgktlpd aegevgrgle vvehacsian
      121 lqlgeyaena asgidvytli qplgvcagit afnfpvmlpc fmfpiavacg ntfvlkpseq
      181 dptsslflaq laleaglppg vlnvvhggpd tanglcehpd ikavsfigst rvgteiynra
      241 saagkrcqsm mgaknhcvil pdadpdvaln qlvgaafgaa gqrcmassva vlvgearnwl
      301 pdfverskkl kvnsgmdrea dlgplvspna kkrvesliqk gvdegaklll dgrslkvagf
      361 eqgnfvgpti fdgvtenmti yteeifgpvl cvvgvetled avafinrnpn gngvalftqd
      421 ggaaryfqnn idvgqvginv pipvpvawfs ftgsrgsklg dlgpngkqav qfwtqtktvt
      481 arwsahaksv nttismr
//
LOCUS       WP_176088632             430 aa            linear   BCT 11-JAN-2025
DEFINITION  aspartate aminotransferase family protein [Achromobacter anxifer].
ACCESSION   WP_176088632
VERSION     WP_176088632.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415008
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..430
                     /product="aspartate aminotransferase family protein"
                     /GO_function="GO:0008483 - transaminase activity [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=45528
     Region          27..423
                     /region_name="ArgD"
                     /note="Acetylornithine aminotransferase/4-aminobutyrate
                     aminotransferase [Amino acid transport and metabolism];
                     COG0160"
                     /db_xref="CDD:439930"
ORIGIN      
        1 msqdlsapts tsgellarrr ralgaayrlf ydepvhpvrg edvwledaqg kryldaynnv
       61 pvvghahpgv vealarqaav lnthtrylhe gvveyaerll alfpagldna mftctgsean
      121 dlalrvaiea tgrtgfivtr nayhgvtrsl admspslrpv ashvrtvppp dsyrgdpala
      181 alrfaeavea aadelaqagt paaalmvdtv fasdgihtes nqalalaaaa irrrgglfia
      241 devqgglart gqswwaferd dvlpdmvslg kpmgnghpig alvlrsdlve efgrkcryfn
      301 tfggntvsaa vglavldalq amdapkrvad vgahleaglr rlaaahpiig dvrgrglywg
      361 velvdarrpa epapavaaal vnglrhagvl igasgpqanv lkirppltfq kahadlllqa
      421 leqqcaaarp
//
LOCUS       WP_176088618             206 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176088618
VERSION     WP_176088618.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..206
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=23032
     Region          13..201
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mpkaataqpg lvdriaqdiq agvygpgawl kqidlqeryd akrldvrral dqlaakrlia
       61 hipnrgyhvy amdpdqhlqi rdirilletg aaadlmpnvt aakvralrtl aerfakllqd
      121 gtlleqyevn lafhagmydm cgnrelvali hetrargpaa pakewvtrsr ielsarehfd
      181 mvdaleardv krlqkiiaqh vgqdis
//
LOCUS       WP_176088641             293 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Achromobacter
            anxifer].
ACCESSION   WP_176088641
VERSION     WP_176088641.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 293)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..293
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=31186
     Region          3..291
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mtttllqall ggiasgavyg lialglslqf gvmkiinfah gaflmmsmyv cfaltshfgl
       61 hplaamplta vvlfaagyac qrwlidgiyr ketsrepigv lifttglwif ldnaflalag
      121 pdsrtidapw anevwmpgdl iftypqiagl vfaclitaal vlflrhtrtg rairatgqdr
      181 eaasvlgids arvyrlsfai glmvlgaaga lllplypvnp fvgdifglra fvivvlggig
      241 svagafwggi lvgvlesvgs qlipityaea lifllflatm yfrpsglfgv ene
//
LOCUS       WP_176088638             309 aa            linear   BCT 11-JAN-2025
DEFINITION  phytanoyl-CoA dioxygenase family protein [Achromobacter anxifer].
ACCESSION   WP_176088638
VERSION     WP_176088638.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009183
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..309
                     /product="phytanoyl-CoA dioxygenase family protein"
                     /EC_number="1.14.-.-"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051213 - dioxygenase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=34699
     Region          7..274
                     /region_name="PhyH"
                     /note="Ectoine hydroxylase-related dioxygenase,
                     phytanoyl-CoA dioxygenase (PhyH) family [Secondary
                     metabolites biosynthesis, transport and catabolism];
                     COG5285"
                     /db_xref="CDD:444095"
ORIGIN      
        1 mkqldlqalq hqlaeegyav ienvldarql eqarervaal maaeradpfp ldderhedde
       61 dilayykrhy tvsdlearrm varvhqyrrd nentrwpvpi nkvsknflhl ptlfdddksq
      121 rvwnllnkap emipliehpv vlpmvrsvmg qdcnlhdfqa tsigpgtggg awhvdaplgq
      181 iaeplpefpl tlqnvwmldd ftadngatrv mprshklrks ppwgsgpldg evtltapags
      241 vaiwlsntwh rsgpnhtere rrailcnynv swlrgfadft stlaegvaag lsndaryllg
      301 ygarapltr
//
LOCUS       WP_176088721             509 aa            linear   BCT 11-JAN-2025
DEFINITION  CoA-acylating methylmalonate-semialdehyde dehydrogenase
            [Achromobacter anxifer].
ACCESSION   WP_176088721
VERSION     WP_176088721.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..509
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=54391
     Region          15..493
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(69,71,75,78,82,115,118..119,128..135,140,143,146,
                     239,243,246,249,251,429,431..432,434..435,438,441..442,
                     444,446..449,458,462,464,478,485..490,492..493)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(155..158,166,181,184,214,231..234,237,255..257,289,
                     394,396,422)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(158,255,286,289)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mnashasags rnaghyiggr pvdgtgsrqp vfnpatgava kqvvlatpde vnravasara
       61 afpqwadtpp irrarvlfrf lelmnkhrde lahlitaehg kvfsdaqgev trgidivefa
      121 cgvpqllkga hteqvstgid nwtlrqplgv vagitpfnfp vmvpmwmfpv aiaagntfvl
      181 kpsptdpsas lriaellsea glpdgvfnvv qgdkvavdal lehpdvkavs fvgstpiany
      241 iyetgarhgk rvqalggakn hmvvmpdadi dqavdaliga gygsagercm avsvavlvgd
      301 vadrllprli ertktlkvld genpaaemgp ivtraaheri sgyialgvqe gaqllvdgrg
      361 fqgaqagdgc gdgfwmggtl fdhvtpdmri ykeeifgpvl gcvrvkdlke avdlinahey
      421 gngvacftrd gnvarefgrr ievgmvginv pipvpmawhg fggwkrslfg dmhaygeegv
      481 rfytrqksim qrwpesigkg aefamptak
//
LOCUS       WP_176088653             220 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176088653
VERSION     WP_176088653.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..220
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=24723
     Region          3..200
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mkvserirla veediragvl lpgdaideqe laarfgvsrt pvrealiqlk vqgmlasqpr
       61 ngmevarmdv qellaiwelm aemegvctrm acqrmspeer qelarihrea aalveaddaq
      121 gwreanhafh evlyrgcrnp ylrqellslr artgaylrha fsavgrvras yeqhgellea
      181 ilandperah lmmmrhisla qgakgladfl inlprsmvkt
//
LOCUS       WP_176088766             300 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176088766
VERSION     WP_176088766.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..300
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32896
     Region          8..67
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          99..298
                     /region_name="PBP2_DntR_NahR_LinR_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators that are involved in
                     the catabolism of dinitrotoluene, naphthalene and
                     gamma-hexachlorohexane; contains the type 2 periplasmic
                     binding fold; cd08459"
                     /db_xref="CDD:176148"
     Site            order(104,106..107,111,169,206,273)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176148"
     Site            order(105,108..109,112..113,116..117,119..120,123..124,
                     126..130,132,195,223..227,230..231,234..235,238,252)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 mnlqdvdlnl lvvfnelrkh grvsavaesl gisqpgvsna lgrlrkllgd elflrtsrgm
       61 vptpyaqdla qpiaaaleal hstlnaraaf dpahsgrafv igvndvgety flprlmrald
      121 raapgvtvrt vrttsidvkd emergridla mgflpdlktg ffqrqlfrqp yvcifrrdhp
      181 lartgvsarq fraaehvaia segtghgvvd qvieqagirr rlrltvphfi avgpvlaatd
      241 miavvpqrfa dcacgpfgla tapcpvkipe svinvfwhar nhrepanqwl rqvvvdefad
//
LOCUS       WP_176088816             479 aa            linear   BCT 11-JAN-2025
DEFINITION  MFS transporter [Achromobacter anxifer].
ACCESSION   WP_176088816
VERSION     WP_176088816.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P.
  TITLE     Understanding transport by the major facilitator superfamily (MFS):
            structures pave the way
  JOURNAL   Nat Rev Mol Cell Biol 17 (2), 123-132 (2016)
   PUBMED   26758938
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Zhang,X.C., Zhao,Y., Heng,J. and Jiang,D.
  TITLE     Energy coupling mechanisms of MFS transporters
  JOURNAL   Protein Sci 24 (10), 1560-1579 (2015)
   PUBMED   26234418
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Yan,N.
  TITLE     Structural Biology of the Major Facilitator Superfamily
            Transporters
  JOURNAL   Annu Rev Biophys 44, 257-283 (2015)
   PUBMED   26098515
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 13022956
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..479
                     /product="MFS transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=49051
     Region          17..409
                     /region_name="MFS_MMR_MDR_like"
                     /note="Methylenomycin A resistance protein (also called
                     MMR peptide) and similar multidrug resistance (MDR)
                     transporters of the Major Facilitator Superfamily;
                     cd17321"
                     /db_xref="CDD:340879"
     Site            order(24..25,28..29,32,64,114..115,117..119,122,143,
                     146..147,150,275,278..279,282..284,287,315,319,373..374,
                     378,382,398,401..402,405..406,409)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340879"
ORIGIN      
        1 mthgihgkqr wwalmvlclg vlmivldtti vnvalpsire dlhftetslv wvvnaymltf
       61 ggflllggrl gdlfghrrmf laglvvftva slacglaqgq tlliaaraaq glggavvsav
      121 slslimnlft etgeraramg vygfvcaggg sigvllggll tsalswhwif lvnlpigvvv
      181 yalclrlipp appaaagarl dvagalsvta slmlavyavv ngneagwtsa qsltllgaaa
      241 vlmilfltie arvdsplmpl glfrlrnvat anivgvlwaa amfawffvsa lymqlvlgys
      301 pmevglaflp anlimaafsl glsaklvmrf girgplaigl fiaalglalf arapadgsfa
      361 vdvlpamlll glgagvafnp mllaamsdve psqsglasgv vntafmmgga lglavlasla
      421 aarsaglaaa gaaptlalng gyqltflaga viataaavls avlvrtrnhd vpvqagaqh
//
LOCUS       WP_176088806             298 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176088806
VERSION     WP_176088806.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20370986
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..298
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=31847
     Region          2..>171
                     /region_name="LysR_Sec_metab"
                     /note="selenium metabolism-associated LysR family
                     transcriptional regulator; NF040786"
                     /db_xref="CDD:468737"
     Region          92..288
                     /region_name="PBP2_CrgA_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulator CrgA and its related
                     homologs, contains the type 2 periplasmic binding domain;
                     cd08422"
                     /db_xref="CDD:176114"
     Site            order(102,106,145,159,161,223,240,267)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176114"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     217..221,228..229,232)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176114"
ORIGIN      
        1 minlnrlamy aavveagsft aaadalgatk avvsfnikql eqelgvallt rstrrlalte
       61 agegfyrhca rllreaeaav dearsgqsal sgslrvtasv dygnrvvapa laafarehpg
      121 lqvsyragsa hadliaerld lairvgaled ssyratrigq fklwlvaspa llaqhgaprs
      181 pqalaalpwl anrpgrsdrw rlidgkgreh elrvapvaqa dtasallafa lagcgvaalp
      241 ewlleeplar galqrvlpsy slprqevyav ypdtrhvsak vrrfidflra rlgpagaa
//
LOCUS       WP_176088819             135 aa            linear   BCT 11-JAN-2025
DEFINITION  carboxymuconolactone decarboxylase family protein [Achromobacter
            anxifer].
ACCESSION   WP_176088819
VERSION     WP_176088819.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10495839
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..135
                     /product="carboxymuconolactone decarboxylase family
                     protein"
                     /calculated_mol_wt=14792
     Region          46..126
                     /region_name="CMD"
                     /note="Carboxymuconolactone decarboxylase family;
                     pfam02627"
                     /db_xref="CDD:460628"
ORIGIN      
        1 mstvkllsde evrqnpqawa vfediratrk sdfvnnfwra landppqler vwgqlkqvmm
       61 adgelsplvr emiyiavsta ngctycihsh taaarakgmt dgqhaellgv igmaaqtnam
      121 vtamqvpvde afivk
//
LOCUS       WP_176088831             427 aa            linear   BCT 11-JAN-2025
DEFINITION  SGNH/GDSL hydrolase family protein [Achromobacter anxifer].
ACCESSION   WP_176088831
VERSION     WP_176088831.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Anderson,A.C., Stangherlin,S., Pimentel,K.N., Weadge,J.T. and
            Clarke,A.J.
  TITLE     The SGNH hydrolase family: a template for carbohydrate diversity
  JOURNAL   Glycobiology 32 (10), 826-848 (2022)
   PUBMED   35871440
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Akoh,C.C., Lee,G.C., Liaw,Y.C., Huang,T.H. and Shaw,J.F.
  TITLE     GDSL family of serine esterases/lipases
  JOURNAL   Prog Lipid Res 43 (6), 534-552 (2004)
   PUBMED   15522763
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10110748
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..427
                     /product="SGNH/GDSL hydrolase family protein"
                     /EC_number="3.1.-.-"
                     /GO_function="GO:0016788 - hydrolase activity, acting on
                     ester bonds [Evidence IEA]"
                     /calculated_mol_wt=44487
     Region          215..422
                     /region_name="XynE_like"
                     /note="SGNH_hydrolase subfamily, similar to the putative
                     arylesterase/acylhydrolase from the rumen anaerobe
                     Prevotella bryantii XynE. The P. bryantii XynE gene is
                     located in a xylanase gene cluster. SGNH hydrolases are a
                     diverse family of lipases and esterases; cd01830"
                     /db_xref="CDD:238868"
     Site            order(222,259,295,403,406)
                     /site_type="active"
                     /db_xref="CDD:238868"
     Site            order(222,403,406)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238868"
     Site            order(222,259,295)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238868"
ORIGIN      
        1 mnrfnpfslv stavlaagla alapsaaaaq pallaeaars nwvsswfasp qplwedafvl
       61 ptempaelrg qtlrqtlmls lggprlrvvl snrygtqple igaasvalaa ggskihpess
      121 rglafggrpg vtvapgaqav sdpvelpvsv laelavslyf pqatpvttfh wgaqqsgala
      181 rgdatvaael pgaqalqgra flagiwvesp srapvvvafg dsltdgngst pganrrwpdy
      241 larrlapqgi gvanagisga rvwgdkmgvn amarfdadvl sqpgvrtvvm mmgindigwp
      301 dsgfapddap mtaarlsegy rqlaeaarlr gvrivggtia pyegslhgtp lsghynpakd
      361 avrlevnrwi resgvfdava dfdavlrdpa hparllpayd sgdnlhpnda gyqamaqald
      421 matlfgd
//
LOCUS       WP_176088853             532 aa            linear   BCT 11-JAN-2025
DEFINITION  glycerol-3-phosphate dehydrogenase/oxidase [Achromobacter anxifer].
ACCESSION   WP_176088853
VERSION     WP_176088853.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Austin,D. and Larson,T.J.
  TITLE     Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol
            3-phosphate dehydrogenase of Escherichia coli K-12
  JOURNAL   J Bacteriol 173 (1), 101-107 (1991)
   PUBMED   1987111
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426419
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..532
                     /product="glycerol-3-phosphate dehydrogenase/oxidase"
                     /EC_number="1.1.-.-"
                     /GO_component="GO:0009331 - glycerol-3-phosphate
                     dehydrogenase (FAD) complex [Evidence IEA]"
                     /GO_function="GO:0004368 - glycerol-3-phosphate
                     dehydrogenase (quinone) activity [Evidence IEA]"
                     /GO_function="GO:0071949 - FAD binding [Evidence IEA]"
                     /GO_process="GO:0006072 - glycerol-3-phosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=57192
     Region          43..529
                     /region_name="GlpA"
                     /note="Glycerol-3-phosphate dehydrogenase [Energy
                     production and conversion]; COG0578"
                     /db_xref="CDD:440343"
ORIGIN      
        1 mnqplasvap pdrnrllntl dnthswdviv igggatglgt avdaasrgyr tlliegadfa
       61 kgtsskatkl vhggvrylaq gnvslvreal hergllnrna phlvwplgfv vpaynlfdqp
      121 fygiglkmyd mlagklnlsp srwlsrrdtl anaptlaenv qgknlkggvl yydgqfddar
      181 lavslmrtlf dlggtavnym ratgltmtgg kvdgvtaeda iggasftlra rcvvnatgvw
      241 vdavrrmedk naqtmvapsq gvhltlpqdf lpgkrailip ktddgrvlfv vpwnghtivg
      301 ttdtprddlp ldpqagaqdv dfilstaary lsrkptrddv tsvwaglrpl vkatgeastk
      361 slsrehtilv skaglvtvtg gkwttyrrma qdvvdtaiqh qlltqascrt eslplhgaag
      421 lapsqehagt pdsyygsdlp alkalpgadr mlvkssglse ahvrfaarye larsaedvla
      481 rrnralflds eaamlaapev arilaeelgh daawqqrtlq dlavvaanyr lk
//
LOCUS       WP_176088881             306 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Achromobacter anxifer].
ACCESSION   WP_176088881
VERSION     WP_176088881.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 306)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 306)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11461647
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..306
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=32527
     Region          46..267
                     /region_name="TsdA"
                     /note="Thiosulfate dehydrogenase TsdA, contains C-terminal
                     cytochrome c domain [Inorganic ion transport and
                     metabolism]; COG3258"
                     /db_xref="CDD:442489"
ORIGIN      
        1 mtaaslrfls aaaclavsaa afaaeprpaf tppsaasipd ndfgkvvreg eqiflhtpqk
       61 askfvgndln caschldagr radsapmwaa yvlypayrak nghvntlaer lqgcfrfsmn
      121 gkapaaddpt ltalqtymfw laskaptgvv legqgyrklp apaqkadyvr ggkvyaqyca
      181 vchgaegqgq kngkhwvfpa lwgadsfnwg agmhqignaa gfikanmplg qagmlsdqea
      241 wdvayfmnah erpqdpryte svaktrakyh dsddslygie vnghllgsda papggkliqa
      301 aaktgg
//
LOCUS       WP_176088882             234 aa            linear   BCT 11-JAN-2025
DEFINITION  c-type cytochrome [Achromobacter anxifer].
ACCESSION   WP_176088882
VERSION     WP_176088882.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Santucci,R., Sinibaldi,F., Cozza,P., Polticelli,F. and Fiorucci,L.
  TITLE     Cytochrome c: An extreme multifunctional protein with a key role in
            cell fate
  JOURNAL   Int J Biol Macromol 136, 1237-1246 (2019)
   PUBMED   31252007
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Sawyer,E.B. and Barker,P.D.
  TITLE     Continued surprises in the cytochrome c biogenesis story
  JOURNAL   Protein Cell 3 (6), 405-409 (2012)
   PUBMED   22723177
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Ow,Y.P., Green,D.R., Hao,Z. and Mak,T.W.
  TITLE     Cytochrome c: functions beyond respiration
  JOURNAL   Nat Rev Mol Cell Biol 9 (7), 532-542 (2008)
   PUBMED   18568041
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Allen,J.W., Daltrop,O., Stevens,J.M. and Ferguson,S.J.
  TITLE     C-type cytochromes: diverse structures and biogenesis systems pose
            evolutionary problems
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 358 (1429), 255-266 (2003)
   PUBMED   12594933
REFERENCE   5  (residues 1 to 234)
  AUTHORS   Barker,P.D. and Ferguson,S.J.
  TITLE     Still a puzzle: why is haem covalently attached in c-type
            cytochromes?
  JOURNAL   Structure 7 (12), R281-R290 (1999)
   PUBMED   10647174
REFERENCE   6  (residues 1 to 234)
  AUTHORS   Kroemer,G.
  TITLE     Cytochrome c
  JOURNAL   Curr Biol 9 (13), R468 (1999)
   PUBMED   10395550
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006741
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..234
                     /product="c-type cytochrome"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0020037 - heme binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=23291
     Region          14..114
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
     Region          116..221
                     /region_name="CytC553"
                     /note="Cytochrome c553 [Energy production and conversion];
                     COG2863"
                     /db_xref="CDD:442110"
ORIGIN      
        1 mtprslssal ilgalyaasa gaqgapdgkq istqgangap acmtchgarg egnpaggfpq
       61 lagmggpyle eqleamangs rvspimaata kaldpaqrka vaeyyaslps tvdtdklaat
      121 amhpvapsdt gawlatrgaw dknvpacnqc hgpggigvga nfpvlagqpa ayiagqlraw
      181 qqgqrppgpl glmpavatrl ssaeidavsa yyaglpkaad qlaaqantta gakq
//
LOCUS       WP_176088900             273 aa            linear   BCT 11-JAN-2025
DEFINITION  MetQ/NlpA family ABC transporter substrate-binding protein
            [Achromobacter anxifer].
ACCESSION   WP_176088900
VERSION     WP_176088900.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 273)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Dawson,R.J., Hollenstein,K. and Locher,K.P.
  TITLE     Uptake or extrusion: crystal structures of full ABC transporters
            suggest a common mechanism
  JOURNAL   Mol Microbiol 65 (2), 250-257 (2007)
   PUBMED   17578454
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003704
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..273
                     /product="MetQ/NlpA family ABC transporter
                     substrate-binding protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=29477
     Region          25..273
                     /region_name="NlpA"
                     /note="ABC-type metal ion transport system, periplasmic
                     component/surface antigen [Inorganic ion transport and
                     metabolism]; COG1464"
                     /db_xref="CDD:441073"
ORIGIN      
        1 mflpqlftkl argaaaagla lacvanasaq dkplrigvip svanaatela iaqakkegle
       61 vklvefndwv lpniavadgs vdanffqhep flelfnqrrg adlkpiaygy sttiglfskk
      121 lkkgdpmpdg atiavpndpv ntgralllle sigliklkpg vahqaslqdv vsnpkklkfv
      181 piegsqsart fddvtasvty ttfakqagln ekdglafdnt dpanvrryai rwvttparaq
      241 dprllkfisi yqnspevkak lrslygdlid fpw
//
LOCUS       WP_176088949             378 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Achromobacter anxifer].
ACCESSION   WP_176088949
VERSION     WP_176088949.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 378)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..378
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=40943
     Region          1..363
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mtdivldqis ksyggttvld rlsltirdge fltllgasgc gkstllklla glempdsgtl
       61 rkggtdilaq spserdcamv fqsyalyphm svgdnictpl ymrslnfaqr lpgarwlspg
      121 irrrmrdaqe qgrhvagvlg idhlwarkpa qlsggqrqrv alaramvrrp slflfdepls
      181 nldanlrqsl rgeirqlhdq lgvtfvyvth dqheamsmsd rvavmrgghi lqlgtpqeiy
      241 haphhadvaa fvgaprinfl tvgrdgagra alqeqaieph fparsarlaf rphaatlvqm
      301 rdalavsgqv qlveftgadc mvtlqtagae kvvvvlpagt rihsgealrv yvplaawhaf
      361 dtaghsladg qralslaa
//
LOCUS       WP_176088962             287 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Achromobacter
            anxifer].
ACCESSION   WP_176088962
VERSION     WP_176088962.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 287)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..287
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=29908
     Region          1..287
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mdllaqilvn gvllgglyav maqglalvwg vlnivnlahg afimlgayas wylyndagvd
       61 pflglpltaa amfvlgyalq rgllnlvvra pmfntllitf glevvltyla qlafsadfrt
      121 inppyagdsy tlgpvtlpma rlaafgvala itlgmwlfll hsrlgraira taqnlvaarl
      181 ygveprhlya vtfglglaqa gaagglygtv sqinpyigat ltakcfaisi iggldnplgv
      241 mvgglflgiv eslttlyvgp tyadvasfgi lvlvllvkps gllgkaa
//
LOCUS       WP_176088981             332 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Achromobacter anxifer].
ACCESSION   WP_176088981
VERSION     WP_176088981.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11418519
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..332
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36002
     Region          8..328
                     /region_name="DppD"
                     /note="ABC-type dipeptide/oligopeptide/nickel transport
                     system, ATPase component [Amino acid transport and
                     metabolism, Inorganic ion transport and metabolism];
                     COG0444"
                     /db_xref="CDD:440213"
ORIGIN      
        1 msahshpllr vrdlhinidt pthvkhvvra vdfslergkt lcivgesgcg ksltalalld
       61 llptaarrrv aqlefagqdl aaltpaalaq lrgariamif qdpmtslnpv fpigtqlvdv
      121 lrrhkrvsrr eaeeraeyll rrvgianpee rmrqypfels gglrqrvmia malmcgpell
      181 iadepttald vtvqaelldl lrdiqaefgl gmvfishdmg lvariadhvi vmyagdiveg
      241 gsvrevlehp shpytamlln cipqpgrtap raelptiaga vpsldtairg cafrercpaa
      301 earcaapfpa rvqgghrclc ikpgalrpgv pa
//
LOCUS       WP_176088984             159 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter small permease [Achromobacter anxifer].
ACCESSION   WP_176088984
VERSION     WP_176088984.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Mulligan,C., Fischer,M. and Thomas,G.H.
  TITLE     Tripartite ATP-independent periplasmic (TRAP) transporters in
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 35 (1), 68-86 (2011)
   PUBMED   20584082
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Forward,J.A., Behrendt,M.C., Wyborn,N.R., Cross,R. and Kelly,D.J.
  TITLE     TRAP transporters: a new family of periplasmic solute transport
            systems encoded by the dctPQM genes of Rhodobacter capsulatus and
            by homologs in diverse gram-negative bacteria
  JOURNAL   J Bacteriol 179 (17), 5482-5493 (1997)
   PUBMED   9287004
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006919
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..159
                     /product="TRAP transporter small permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0015740 - C4-dicarboxylate transport
                     [Evidence IEA]"
                     /calculated_mol_wt=16963
     Region          1..150
                     /region_name="DctM"
                     /note="TRAP-type C4-dicarboxylate transport system, small
                     permease component YiaM [Carbohydrate transport and
                     metabolism]; COG3090"
                     /db_xref="CDD:442324"
ORIGIN      
        1 mlhrlsails giskavaava vallailisy vvfsrfvtht tphwaeelpr lvlvwsafig
       61 gvacsyersh lmagllpfvv rnprilnafe rinqafiivg laalgyagwq laeltmdqtl
      121 paldvsagtv ylalpfacai tivvhlaqlf spapaavke
//
LOCUS       WP_176088985             427 aa            linear   BCT 11-JAN-2025
DEFINITION  TRAP transporter large permease [Achromobacter anxifer].
ACCESSION   WP_176088985
VERSION     WP_176088985.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Kelly,D.J. and Thomas,G.H.
  TITLE     The tripartite ATP-independent periplasmic (TRAP) transporters of
            bacteria and archaea
  JOURNAL   FEMS Microbiol Rev 25 (4), 405-424 (2001)
   PUBMED   11524131
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Rabus,R., Jack,D.L., Kelly,D.J. and Saier,M.H. Jr.
  TITLE     TRAP transporters: an ancient family of extracytoplasmic
            solute-receptor-dependent secondary active transporters
  JOURNAL   Microbiology (Reading) 145 (Pt 12), 3431-3445 (1999)
   PUBMED   10627041
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10003989
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..427
                     /product="TRAP transporter large permease"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0031317 - tripartite ATP-independent
                     periplasmic transporter complex [Evidence IEA]"
                     /GO_function="GO:0022857 - transmembrane transporter
                     activity [Evidence IEA]"
                     /GO_process="GO:0008643 - carbohydrate transport [Evidence
                     IEA]"
                     /calculated_mol_wt=44698
     Region          5..426
                     /region_name="DctQ"
                     /note="TRAP-type C4-dicarboxylate transport system, large
                     permease component [Carbohydrate transport and
                     metabolism]; COG1593"
                     /db_xref="CDD:441201"
ORIGIN      
        1 mstgalflmg vftvtvlidm piafglvlsc laylavydaa pmmvaaqqyv vgldsftlla
       61 iplfilaaql mngagltqri vrlcaaivgd ikgglavvav laclmfgals gsgvadvvai
      121 gslllpamar sgydkgfsca lvgsagatst iippsivliv ygtitdtsvg klfvagiipg
      181 illglsligv aiwqsrkhnw aggqpfswte lraaaidalp almvpvliig girfgiftat
      241 eaassaiiya lligffwyrt lslrslwdnl kstgessasi lliigasglf awvlvaeqvp
      301 qalstllvew tdsktavllv ltvvllllgt fmeaipviii vapvvmpvla hynidpvhfg
      361 illsinmaig antppvgvdl maackiggin mmqtlrplsw mmlamtavml lltfvpelvl
      421 flprhvq
//
LOCUS       WP_176088993             319 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176088993
VERSION     WP_176088993.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..319
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=34396
     Region          3..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..292
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,221..226,
                     232..233,235..236)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mdlrkienli hvadsgsfsk aasvlgiaqs algrqvrkle decgcallyr ngrgvsltpe
       61 gekllerlrp lltqmtrvvt efhdeqksps gqvtlgltpt lshmvgmplv aeiwkrhpri
      121 qlnvitgysg yvhewlanar vdiavlhdar rsqhvvvdpl aeldlalvsp tqnlapaara
      181 qscidfgqig slplalptrs hglrrtleha atqadtplnv afemdalelm keivlaglah
      241 tvlalpavvg elasgrlvar rivnpalstr lmlatassrp ltqavkivqd tlrevlagmv
      301 qaepyraymr magadaatg
//
LOCUS       WP_176089008             161 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Achromobacter anxifer].
ACCESSION   WP_176089008
VERSION     WP_176089008.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11457526
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..161
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=18039
     Region          20..149
                     /region_name="CatE"
                     /note="Catechol-2,3-dioxygenase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG2514"
                     /db_xref="CDD:442004"
ORIGIN      
        1 msttstlapa drrpriarth lalfvrdpfa sapwyesvlg mqetargeqw vflsfgrkhh
       61 dialiraaeg epargpvnmq hygleiegdv delrrlygml lakgvevvki tdhkvgygly
      121 ftdpdghrfe ffcetvhgde egkqvlhdhn apsipmtldp l
//
LOCUS       WP_176089017             301 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176089017
VERSION     WP_176089017.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Felder,C.B., Graul,R.C., Lee,A.Y., Merkle,H.P. and Sadee,W.
  TITLE     The Venus flytrap of periplasmic binding proteins: an ancient
            protein module present in multiple drug receptors
  JOURNAL   AAPS PharmSci 1 (2), E2 (1999)
   PUBMED   11741199
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444097
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..301
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33639
     Region          5..61
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          95..295
                     /region_name="PBP2_DntR_NahR_LinR_like"
                     /note="The C-terminal substrate binding domain of
                     LysR-type transcriptional regulators that are involved in
                     the catabolism of dinitrotoluene, naphthalene and
                     gamma-hexachlorohexane; contains the type 2 periplasmic
                     binding fold; cd08459"
                     /db_xref="CDD:176148"
     Site            order(101,103..104,108,166,203,270)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:176148"
     Site            order(102,105..106,109..110,113..114,116..117,120..121,
                     123..127,129,192,220..224,227..228,231..232,235,249)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176148"
ORIGIN      
        1 mdfdlnlmrv fltvlhersv traaqrlnlt qpavsyalar lrekfddplf artasgmqpt
       61 pvafalaepi ergmnsfaea vnlrqrfdpa ssarrfrlsm sdigemvflp slmervhala
      121 prlqvevlei plerlpqalk egevdlaign laglgsetch aelfserytc mgrrghpvls
      181 agltrsqykr ldhilvasra sahrllddvl seaglprrpy ltlphfsaaa eivrrtdltm
      241 tlplraalwf nhddafqirp lpialpplsv tvhwharfes dpgtswlrrl vvetladpdp
      301 a
//
LOCUS       WP_176089043             229 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176089043
VERSION     WP_176089043.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..229
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=25971
     Region          4..224
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mqstklrldr srhaapqvfe hlreqilsle lapgaslsrv tlaetyglsq tpirdalmrl
       61 aeealveiyp qhttvvsrid vaaareahfl rrsleleivq mlaqrpdpvl fkrlqasidl
      121 qrashasgqy qrfidadqaf hrdmhdaagv irlwelaqry sghldrlrrl hlpesgkaer
      181 ilddhqrlld aivaqdpqaa qrvlrehlsg tlsqvaeick rypdyvlaa
//
LOCUS       WP_176089048             370 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA dehydrogenase family protein [Achromobacter anxifer].
ACCESSION   WP_176089048
VERSION     WP_176089048.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Kim,J.J. and Battaile,K.P.
  TITLE     Burning fat: the structural basis of fatty acid beta-oxidation
  JOURNAL   Curr Opin Struct Biol 12 (6), 721-728 (2002)
   PUBMED   12504675
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Hiltunen,J.K. and Qin,Y.
  TITLE     beta-oxidation - strategies for the metabolism of a wide variety of
            acyl-CoA esters
  JOURNAL   Biochim Biophys Acta 1484 (2-3), 117-128 (2000)
   PUBMED   10760462
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449292
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..370
                     /product="acyl-CoA dehydrogenase family protein"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0003995 - acyl-CoA dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=38504
     Region          14..345
                     /region_name="CaiA"
                     /note="Acyl-CoA dehydrogenase related to the alkylation
                     response protein AidB [Lipid transport and metabolism];
                     COG1960"
                     /db_xref="CDD:441563"
ORIGIN      
        1 mtaasaasal padlrawleq hadalddgsl dgatvlprla aagvfrhgvp aaqgglagtd
       61 igdaieavsq vaelsvasaf vawgqrvfie yllrspntal adawlgplle grqagatals
      121 namkflsgie slqisaragd glwvldgrmp wvtnlrvqgf lvaaavtapd gtpavvalph
      181 diagltrspd lsllalqssn taaldvrgvr igpewlihad arqylpqarp afaglqcgls
      241 iglarralra aeqagqgqas rgilgqplea lraqvetlae hlisgvrser fvaepwrlfe
      301 irialaeaaq eavqlelqas ggaaylkpag agfarrwrea aflpivtpsl vqlktelakr
      361 qsrlaagaaa
//
LOCUS       WP_176089071             204 aa            linear   BCT 11-JAN-2025
DEFINITION  ferritin-like domain-containing protein [Achromobacter anxifer].
ACCESSION   WP_176089071
VERSION     WP_176089071.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10090058
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..204
                     /product="ferritin-like domain-containing protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=22435
     Region          13..122
                     /region_name="Ferritin_like"
                     /note="Ferritin-like superfamily of diiron-containing
                     four-helix-bundle proteins; cd00657"
                     /db_xref="CDD:153097"
     Site            order(22,52,55,116,119)
                     /site_type="other"
                     /note="dinuclear metal binding motif [ion binding]"
                     /db_xref="CDD:153097"
ORIGIN      
        1 mkrtagnapq ikellyqale teiggllvye tavscavnqd lkkewadyle etrthrrvll
       61 tvfeqlgldp aaqppgrevv rhigeslvka mkmaisagdp daaqlvatec vvlaetkdha
      121 nwqligliaq qhsgdeakvl kqaydavasd edhhlyhtqg wsrelwieal gfpavlpppe
      181 evkqvetaig asraeqardk mlnh
//
LOCUS       WP_176089082             199 aa            linear   BCT 11-JAN-2025
DEFINITION  HD-GYP domain-containing protein [Achromobacter anxifer].
ACCESSION   WP_176089082
VERSION     WP_176089082.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Francis,S.H., Turko,I.V. and Corbin,J.D.
  TITLE     Cyclic nucleotide phosphodiesterases: relating structure and
            function
  JOURNAL   Prog Nucleic Acid Res Mol Biol 65, 1-52 (2001)
   PUBMED   11008484
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Aravind,L. and Koonin,E.V.
  TITLE     The HD domain defines a new superfamily of metal-dependent
            phosphohydrolases
  JOURNAL   Trends Biochem Sci 23 (12), 469-472 (1998)
   PUBMED   9868367
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11454351
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..199
                     /product="HD-GYP domain-containing protein"
                     /GO_function="GO:0004112 - cyclic-nucleotide
                     phosphodiesterase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=21504
     Region          <14..198
                     /region_name="HDGYP"
                     /note="HD-GYP domain, c-di-GMP phosphodiesterase class II
                     (or its inactivated variant) [Signal transduction
                     mechanisms]; COG2206"
                     /db_xref="CDD:441808"
ORIGIN      
        1 mppdvpeype gscvaalfaa mrardaatgr hservvalsv alaracglpe seqeavavaa
       61 rlhdigkigt pdrvlyspkr ldkddweimk ahaaagadii mhsdipqrel iaqavrhhhe
      121 hydgsgypag lsgetiplhs riisladsyd algdarpyhp arthaeilri mnqeagakcd
      181 pallrtfeam iqksplrvp
//
LOCUS       WP_176089205             191 aa            linear   BCT 11-JAN-2025
DEFINITION  NUDIX hydrolase [Achromobacter anxifer].
ACCESSION   WP_176089205
VERSION     WP_176089205.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Srouji,J.R., Xu,A., Park,A., Kirsch,J.F. and Brenner,S.E.
  TITLE     The evolution of function within the Nudix homology clan
  JOURNAL   Proteins 85 (5), 775-811 (2017)
   PUBMED   27936487
REFERENCE   2  (residues 1 to 191)
  AUTHORS   McLennan,A.G.
  TITLE     The Nudix hydrolase superfamily
  JOURNAL   Cell Mol Life Sci 63 (2), 123-143 (2006)
   PUBMED   16378245
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Mildvan,A.S., Xia,Z., Azurmendi,H.F., Saraswat,V., Legler,P.M.,
            Massiah,M.A., Gabelli,S.B., Bianchet,M.A., Kang,L.W. and Amzel,L.M.
  TITLE     Structures and mechanisms of Nudix hydrolases
  JOURNAL   Arch Biochem Biophys 433 (1), 129-143 (2005)
   PUBMED   15581572
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10132634
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..191
                     /product="NUDIX hydrolase"
                     /EC_number="3.6.1.-"
                     /GO_function="GO:0016817 - hydrolase activity, acting on
                     acid anhydrides [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009132 - nucleoside diphosphate metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=21607
     Region          52..179
                     /region_name="NUDIX_Hydrolase"
                     /note="uncharacterized NUDIX hydrolase subfamily; cd03674"
                     /db_xref="CDD:467542"
ORIGIN      
        1 mnhlaqilen tkeqvvnyvl ehpwqifalg rlltdlgkdd vsvfdrknma ghittsalvv
       61 nesethallv hhkayglwlp pgghmepdap slwqsaarev leetglvltd rylplldidt
      121 hpiparpskn egphwhhdfm flatapddfv ptaqecevha aewrpisdlt kssnarmrrl
      181 sekfrerqis l
//
LOCUS       WP_176089266             179 aa            linear   BCT 11-JAN-2025
DEFINITION  C40 family peptidase [Achromobacter anxifer].
ACCESSION   WP_176089266
VERSION     WP_176089266.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     Evolutionary history, structural features and biochemical diversity
            of the NlpC/P60 superfamily of enzymes
  JOURNAL   Genome Biol 4 (2), R11 (2003)
   PUBMED   12620121
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Barrett,A.J. and Rawlings,N.D.
  TITLE     Evolutionary lines of cysteine peptidases
  JOURNAL   Biol Chem 382 (5), 727-733 (2001)
   PUBMED   11517925
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11434971
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..179
                     /product="C40 family peptidase"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008233 - peptidase activity [Evidence
                     IEA]"
                     /GO_function="GO:0008234 - cysteine-type peptidase
                     activity [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_process="GO:0000270 - peptidoglycan metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=19651
     Region          <52..175
                     /region_name="NlpC"
                     /note="Cell wall-associated hydrolase, NlpC_P60 family
                     [Cell wall/membrane/envelope biogenesis]; COG0791"
                     /db_xref="CDD:440554"
ORIGIN      
        1 mhqakrlfml lvvlvssgct plhpsrptas ilhdrtaleh setditnfdr etasspgsev
       61 vmhaltllks kyrfggkspe tgldcsglvs hvydnalgls vegsassmal qgrritrkdl
      121 kagdlvffnt lgrprshvgi yvgndkfvha ensrtgirin rlsdryyaar feeartllh
//
LOCUS       WP_176089381             579 aa            linear   BCT 11-JAN-2025
DEFINITION  AI-2E family transporter [Achromobacter anxifer].
ACCESSION   WP_176089381
VERSION     WP_176089381.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Khera,R., Mehdipour,A.R., Bolla,J.R., Kahnt,J., Welsch,S.,
            Ermler,U., Muenke,C., Robinson,C.V., Hummer,G., Xie,H. and
            Michel,H.
  TITLE     Cryo-EM structures of pentameric autoinducer-2 exporter from
            Escherichia coli reveal its transport mechanism
  JOURNAL   EMBO J 41 (18), e109990 (2022)
   PUBMED   35698912
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Rettner,R.E. and Saier,M.H. Jr.
  TITLE     The autoinducer-2 exporter superfamily
  JOURNAL   J Mol Microbiol Biotechnol 18 (4), 195-205 (2010)
   PUBMED   20559013
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001851
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..579
                     /product="AI-2E family transporter"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /GO_process="GO:1905887 - autoinducer AI-2 transmembrane
                     transport [Evidence IEA]"
                     /calculated_mol_wt=61569
     Region          275..570
                     /region_name="PerM"
                     /note="Predicted PurR-regulated permease PerM [General
                     function prediction only]; COG0628"
                     /db_xref="CDD:440393"
ORIGIN      
        1 mktlllmadd glsssvwlhm amhhlnqgkg vltisdpgsg pypdaigtgd alptyasgla
       61 ghprfhsvrl adpavllavl ldqrpdtvlm fdmdvfvkae kdprwlevia fcaqsghdmv
      121 lphynglqwr ygladlmkap dggvaniasi awdrlagrdv vadnieavrt lvpsladqie
      181 rpgiripasa aghqpdhlgd fcwqsisrng svewripkhy gpklhdlspf pelwtdqapg
      241 glstpapssl aspfdlsaag ivlalllmvl lfglmpglla glgafsltrw ltrnrvvqrl
      301 lgrragplsa mlvillpmla igvaglelgr fvasalnnva alydhvmgvl lkwgamlpap
      361 fddllpsdaa glqeklagav qvhglrlagv gktwigalif vvvgvvvgal aaisvptstg
      421 klalamrarg alllagftkv vmaqvwiaav ntlftatllf vafplidvhi pyaawlvllt
      481 fvagllpivg nllcnivlti aglgvgphia iaclvflvav hkleyfinak vmgsqiktaa
      541 wellivmfaf eavfgvvglv aaplyyaymk melsrlgwv
//
LOCUS       WP_176089703             198 aa            linear   BCT 11-JAN-2025
DEFINITION  TetR/AcrR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176089703
VERSION     WP_176089703.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Deng,W., Li,C. and Xie,J.
  TITLE     The underling mechanism of bacterial TetR/AcrR family
            transcriptional repressors
  JOURNAL   Cell Signal 25 (7), 1608-1613 (2013)
   PUBMED   23602932
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442015
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..198
                     /product="TetR/AcrR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=21189
     Region          9..165
                     /region_name="AcrR"
                     /note="DNA-binding protein, AcrR family, includes nucleoid
                     occlusion protein SlmA [Transcription]; COG1309"
                     /db_xref="CDD:440920"
ORIGIN      
        1 mdtptsnttr elllahaekl irtrgcngfs yrdlaehvgv ktssihyyfp gkddllyeav
       61 eaystralaa mrgidaslsa heqldqylsm mesracgsge lclagmlaae vnslpervrg
      121 alqgffrahe awlarvlaeg aaqgtmkfag tpdvaaravf atvqgcilia rlfqqpaalc
      181 eaigalyvec qgkedgap
//
LOCUS       WP_176089721             352 aa            linear   BCT 11-JAN-2025
DEFINITION  pentapeptide repeat-containing protein [Achromobacter anxifer].
ACCESSION   WP_176089721
VERSION     WP_176089721.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Zhang,R. and Kennedy,M.A.
  TITLE     Current Understanding of the Structure and Function of Pentapeptide
            Repeat Proteins
  JOURNAL   Biomolecules 11 (5), 638 (2021)
   PUBMED   33925937
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Bateman,A., Murzin,A.G. and Teichmann,S.A.
  TITLE     Structure and distribution of pentapeptide repeats in bacteria
  JOURNAL   Protein Sci 7 (6), 1477-1480 (1998)
   PUBMED   9655353
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11442852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..352
                     /product="pentapeptide repeat-containing protein"
                     /calculated_mol_wt=37931
     Region          16..174
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
     Region          141..316
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
ORIGIN      
        1 mnldqlldqv rhgepiahls lagrdlrgld lagaffdqvd lsgakmsgcq lqdsqflncv
       61 lagvdaadan ldtarlfrcq argavldrch ahglsftecd ldqasleqae lreaafnsts
      121 leaasfrsar lersvfsrgt ltradlsqar msftlfhqld lrsivlagas aestmfiecd
      181 ltaqdfaaqa yplchftdsq ldgadfrnad lrqagfkgas lrgarftgas alqglfpqad
      241 lsgadlqggr fdgaiwaeat ldgaslrgas lslcvfqrar cantdfrgan ltdadfslad
      301 ldqadlrdat flrtrmhral tqgarwterr giiendapll qaelwsagra ap
//
LOCUS       WP_176089484             145 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Achromobacter anxifer].
ACCESSION   WP_176089484
VERSION     WP_176089484.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 145)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 145)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10607277
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..145
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16187
     Region          46..125
                     /region_name="Acetyltransf_7"
                     /note="Acetyltransferase (GNAT) domain; pfam13508"
                     /db_xref="CDD:463905"
ORIGIN      
        1 mhfertnscv dallalplla gldayypdfq hwyvnrvvpg vvtgqdvlvl akergavvgi
       61 algkrgpdet klrcvrllpe fqqtgagirl idhmlehlec erphctvaee lvhtyarafv
      121 nrygfslssv dkgryragkl eyafn
//
LOCUS       WP_176089579             516 aa            linear   BCT 11-JAN-2025
DEFINITION  sensor histidine kinase [Achromobacter anxifer].
ACCESSION   WP_176089579
VERSION     WP_176089579.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Dutta,R. and Inouye,M.
  TITLE     GHKL, an emergent ATPase/kinase superfamily
  JOURNAL   Trends Biochem Sci 25 (1), 24-28 (2000)
   PUBMED   10637609
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Stock,J.
  TITLE     Signal transduction: Gyrating protein kinases
  JOURNAL   Curr Biol 9 (10), R364-R367 (1999)
   PUBMED   10339418
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Grebe,T.W. and Stock,J.B.
  TITLE     The histidine protein kinase superfamily
  JOURNAL   Adv Microb Physiol 41, 139-227 (1999)
   PUBMED   10500846
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468388
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..516
                     /product="sensor histidine kinase"
                     /EC_number="2.7.13.3"
                     /GO_function="GO:0000155 - phosphorelay sensor kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0004673 - protein histidine kinase
                     activity [Evidence IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_process="GO:0007165 - signal transduction [Evidence
                     IEA]"
                     /calculated_mol_wt=56652
     Region          256..510
                     /region_name="ComP"
                     /note="Signal transduction histidine kinase ComP [Signal
                     transduction mechanisms]; COG4585"
                     /db_xref="CDD:443642"
ORIGIN      
        1 mlgvvsrlgw kfpdqqakvv srspnlelfw sgmtyvphaa ilfcagygvl klnrmahslf
       61 elrskeeitq ifregldssl hlrmmnaarg sgssvtdmpv rvrargldls lsisiealpq
      121 feqegiallf lreiepaqlr rthppvkals rglmqemlnr lshpgwiiqs pytvyfrnpn
      181 ygkmlsrcar sflegngiig pacqgcpgae raahsllkea idqvraihev veyqvdlggc
      241 ghwnvvmvpi dqatdvacla vpasestaaa sltgalvsle npallvsarr aaeklsaiea
      301 lqeardlern tiareihdal gqeltvlrls lrrlwqgvrg hadipthlda estmifgqld
      361 kvvssarria helrsdgvks qgfssaahsl vsnfqerlgl qgqmevygew aepdqtvgwh
      421 lyralqelln niakhayasr fnvrvafvag ryrlevcddg vgipeaiava rtgiglrsiq
      481 eraaiyqgev nirtrpevpg svvevvipap vsleve
//
LOCUS       WP_176089737             277 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Achromobacter anxifer].
ACCESSION   WP_176089737
VERSION     WP_176089737.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..277
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=30305
     Region          15..270
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mglsaatpvd ntekaaplla vdkvsieykt rerrvrathq vsfevhgaer fillgasgcg
       61 kstllkaiag fieptegria idgqpvrgpg pdrivvfqef dqlppwktlr qnvafplvas
      121 rklgrreade ramhyldkvg lsafadayph tlsggmkqrv aiaralamqp rvllmdepfa
      181 aldaltrrrm qeellalwed vrftllfvth sieealvlgs rvlllsphpg rvraelnaht
      241 fglhsqgsaa fqsaarrihd llfdappvea paeraaa
//
LOCUS       WP_176089739             231 aa            linear   BCT 11-JAN-2025
DEFINITION  GntR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176089739
VERSION     WP_176089739.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Liu,G.F., Wang,X.X., Su,H.Z. and Lu,G.T.
  TITLE     Progress on the GntR family transcription regulators in bacteria
  JOURNAL   Yi Chuan 43 (1), 66-73 (2021)
   PUBMED   33509775
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448455
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..231
                     /product="GntR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=26087
     Region          11..224
                     /region_name="GntR"
                     /note="DNA-binding transcriptional regulator, GntR family
                     [Transcription]; COG1802"
                     /db_xref="CDD:441407"
ORIGIN      
        1 mdygetsplg qaladrsitg avvdalrgei ihgqlkpger lrqdavasrf rvsqtvvrea
       61 fkdlirecfl iseprrgvsv atmsadeaee mtilrsvvep qalawaiprl teaqfeaaer
      121 vlkqlddeks vdqiillnar fhqglyaaan rprtltmvet lrlgferylr ytweftshrd
      181 rsqqehwell amckqgeves acrlltqhir atgdllvecl akrpveplsk v
//
LOCUS       WP_176089740             245 aa            linear   BCT 11-JAN-2025
DEFINITION  HAD family hydrolase [Achromobacter anxifer].
ACCESSION   WP_176089740
VERSION     WP_176089740.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Leader,D.P. and Milner-White,E.J.
  TITLE     The conserved crown bridge loop at the catalytic centre of enzymes
            of the haloacid dehalogenase superfamily
  JOURNAL   Curr Res Struct Biol 6, 100105 (2023)
   PUBMED   37786806
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Yang,L., Lu,Y., Tian,W., Feng,Y., Bai,J. and Zhang,H.
  TITLE     Insights into the functional divergence of the haloacid
            dehalogenase superfamily from phosphomonoesterase to inorganic
            pyrophosphatase
  JOURNAL   Arch Biochem Biophys 705, 108896 (2021)
   PUBMED   33940035
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Burroughs,A.M., Allen,K.N., Dunaway-Mariano,D. and Aravind,L.
  TITLE     Evolutionary genomics of the HAD superfamily: understanding the
            structural adaptations and catalytic diversity in a superfamily of
            phosphoesterases and allied enzymes
  JOURNAL   J Mol Biol 361 (5), 1003-1034 (2006)
   PUBMED   16889794
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Allen,K.N. and Dunaway-Mariano,D.
  TITLE     Phosphoryl group transfer: evolution of a catalytic scaffold
  JOURNAL   Trends Biochem Sci 29 (9), 495-503 (2004)
   PUBMED   15337123
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..245
                     /product="HAD family hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=26831
     Region          8..234
                     /region_name="YigB"
                     /note="FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil
                     phosphatase YigB, HAD superfamily (riboflavin
                     biosynthesis) [Coenzyme transport and metabolism];
                     COG1011"
                     /db_xref="CDD:440635"
ORIGIN      
        1 mtlrlsdfda vtfdvygtli dwepsiarfl trwarenrie adaetlimaf dgaraaiqke
       61 rpahlypdvl tkcfericae fkvavdpdlr rqfaaaphtw pafedshagl vrlqqsakvg
      121 afsnidqasl ntscdnldfr fdlvvtaqrv gaykpdwphf dtgigeltrm giprerilhv
      181 gqslraditp anrlgvrcaw vnrpgrllgl sgegaaeakp dltvsslael vaaltgadqp
      241 aatla
//
LOCUS       WP_176089743             127 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Achromobacter anxifer].
ACCESSION   WP_176089743
VERSION     WP_176089743.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..127
                     /product="RidA family protein"
                     /calculated_mol_wt=13420
     Region          1..125
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 mirkaysgel tpppagtysv amqaghflfl sgqtprdrds vrhgdktfav qarmaldnle
       61 aaanaagasl rdavkvgvfl rdlghaqefd aiyasyvgtp ppartliqsg fsafdievda
      121 ilvrgpd
//
LOCUS       WP_176089798             186 aa            linear   BCT 11-JAN-2025
DEFINITION  sugar transferase [Achromobacter anxifer].
ACCESSION   WP_176089798
VERSION     WP_176089798.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Ray,L.C., Das,D., Entova,S., Lukose,V., Lynch,A.J., Imperiali,B.
            and Allen,K.N.
  TITLE     Membrane association of monotopic phosphoglycosyl transferase
            underpins function
  JOURNAL   Nat Chem Biol 14 (6), 538-541 (2018)
   PUBMED   29769739
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005412
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..186
                     /product="sugar transferase"
                     /EC_number="2.-.-.-"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0016780 - phosphotransferase activity,
                     for other substituted phosphate groups [Evidence IEA]"
                     /GO_process="GO:0000271 - polysaccharide biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=20798
     Region          <1..184
                     /region_name="WcaJ"
                     /note="Sugar transferase involved in LPS biosynthesis
                     (colanic, teichoic acid) [Cell wall/membrane/envelope
                     biogenesis]; COG2148"
                     /db_xref="CDD:441751"
ORIGIN      
        1 mkrvfdllls lfaalvllip viivallvrl tspgpvlyws drvgrnnrif kmpkfrsmkv
       61 dtpavathll pdpaacltpv ggflrkssld elpqlwsiiv gdmsfvgprp alfnqddlia
      121 lrteagvdal tpgltgwaqv ngrdelpipd kvrldieymn rrsvwfdiri lwltfvkvlr
      181 rdgvsh
//
LOCUS       WP_176089821             298 aa            linear   BCT 11-JAN-2025
DEFINITION  AEC family transporter [Achromobacter anxifer].
ACCESSION   WP_176089821
VERSION     WP_176089821.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Blakeslee,J.J., Peer,W.A. and Murphy,A.S.
  TITLE     Auxin transport
  JOURNAL   Curr Opin Plant Biol 8 (5), 494-500 (2005)
   PUBMED   16054428
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..298
                     /product="AEC family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=31126
     Region          9..294
                     /region_name="YfdV"
                     /note="Predicted permease, AEC (auxin efflux carrier)
                     family [General function prediction only]; COG0679"
                     /db_xref="CDD:440443"
ORIGIN      
        1 mpavvqfyfs aivlmlpllf cvgigvywgk rdlpfggsfi tmlvtsvttp alvfhtfvtt
       61 hlddraladv aaatllallf calacalllk awklpvrtll ptaflpnagn lglpisqmaf
      121 gdaglsvava ffavssfvmh tiavrllpgv ntkgswkspi llasliaval rllhvpvpaw
      181 liettrmlga vtvplmllsl ghalalipan glrdgakvaa irlavglaag lavvwaldle
      241 pvlagalslq mampcavvsy myvkrytslg dtaagavlvs tvaflllapv ilwfshgg
//
LOCUS       WP_176089823             305 aa            linear   BCT 11-JAN-2025
DEFINITION  alpha/beta hydrolase [Achromobacter anxifer].
ACCESSION   WP_176089823
VERSION     WP_176089823.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Chatonnet,A., Perochon,M., Velluet,E. and Marchot,P.
  TITLE     The ESTHER database on alpha/beta hydrolase fold proteins - An
            overview of recent developments
  JOURNAL   Chem Biol Interact 383, 110671 (2023)
   PUBMED   37582413
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11429202
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..305
                     /product="alpha/beta hydrolase"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=33193
     Region          64..>236
                     /region_name="Aes"
                     /note="Acetyl esterase/lipase [Lipid transport and
                     metabolism]; COG0657"
                     /db_xref="CDD:440422"
ORIGIN      
        1 mhnadidlff ptvaerevqy narqsvpdfd acvrryaess arvrtrrpgi ldlrygmgqd
       61 erldlflpaa snaaapvfvf ihggywraqr kedapvmaea fnaagaavat leytlvpeat
      121 lgevvrevrs avawlywnaa aygvdperiy vggssagghl aamlaapdwp arynlpddvi
      181 kgtlalsglf dlrplcdvlp ntwlqltpeq aahqspifhl peragpmlla vggletqgfk
      241 nqtaafeaaw naaglastri ptpqcnhfdl vneledpdse ltratlemmg lakadgvrra
      301 elqks
//
LOCUS       WP_176089826             304 aa            linear   BCT 11-JAN-2025
DEFINITION  branched-chain amino acid ABC transporter permease [Achromobacter
            anxifer].
ACCESSION   WP_176089826
VERSION     WP_176089826.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001728
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..304
                     /product="branched-chain amino acid ABC transporter
                     permease"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0015803 - branched-chain amino acid
                     transport [Evidence IEA]"
                     /calculated_mol_wt=31592
     Region          1..304
                     /region_name="LivH"
                     /note="Branched-chain amino acid ABC-type transport
                     system, permease component [Amino acid transport and
                     metabolism]; COG0559"
                     /db_xref="CDD:440325"
ORIGIN      
        1 mtllfeqlln glqfgamlfm laagltlifg imgvvnlthg sfymvgayca ayaigttgsf
       61 lagvlaallg aglygiaaev lvirklykrd hlyqvlatfg lllfsneavs lifgrrpplv
      121 giptflegav tlapgfqypl irlsfiaiga lvavglwwlv nrtrigmlir agaddremvd
      181 algvdirkly tlvfglgall cglagvmaap llaveigmge rilittfvvi viggvgsvrg
      241 alagallvgm vdslgraflp qllstmfspa tadplaagla sasiyvlmai vliakpgglf
      301 parg
//
LOCUS       WP_176089842             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176089842
VERSION     WP_176089842.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=32755
     Region          5..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..290
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(107..108,110..111,114,118,120..126,218..223,
                     229..230,232..233)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mhgialkyfl evaqagslsg aserlhvavs aisrqiakle eeagaplfer aargmvlsea
       61 grlllaharr tmleadsvlq eiaaikgtar neirvasveg variflpsvm arfhrdwpni
      121 rfdlhvgspa evsrrvaegs velgmafiae risgvsprys rrapvhavma adhplayras
      181 vslqdlsqyp laltgpgttt rqlfemgcal esvqlepalt cndssplhgf vlgsdaimls
      241 gyisvawslq rdeliavpis naelqsrtlq iqvmpgrvlp paaeafaell cseldralqg
      301 gaakqa
//
LOCUS       WP_176089889             586 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Achromobacter anxifer].
ACCESSION   WP_176089889
VERSION     WP_176089889.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 586)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467929
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..586
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=64181
     Region          1..542
                     /region_name="YejF"
                     /note="ABC-type microcin C transport system, duplicated
                     ATPase component YejF [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG4172"
                     /db_xref="CDD:443332"
ORIGIN      
        1 msetllaveg lsvefgprgq pyravksldf tigrgetval vgesgsgksv talsilrlie
       61 raggriaagv arfmprdgre vdlfkleesa lrrvrgneis mvfqepmtsl npvmtvadql
      121 aevyllhqdi sraqawkqae amlaavkmse perrmtqypg dlsggmrqrv miamalacrp
      181 qlliadeptt aldvtvqaei idlirdlqre vgmavlfith dmgvvaeiad rvvvmrhgdk
      241 ieenetaalf gapsqsytrd llasvpklgd gspgeaalqg rpvvlevagl akrfpvkaga
      301 fgkvvanvha vegvsfalra getlalvges gsgksttgrl lmklvqpteg airlagqdvt
      361 hmkpdqmrem rrhiqmifqd pyaslnprlh awdlvseplk vhgelsreqr reraaqller
      421 vnlprefldr yahqfsggqr qrlciarals vnpkvivade pvsaldvsvq arvielmkel
      481 qaemdlsylf ishdmavvek vshrvavmyl gqiveigptq evlhrprhpy tqrllsavpi
      541 pdparrhqra astardipsp irkvgdnpqv gelvqvaagh yvqlaa
//
LOCUS       WP_176089945             351 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Achromobacter anxifer].
ACCESSION   WP_176089945
VERSION     WP_176089945.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Dassa,E. and Bouige,P.
  TITLE     The ABC of ABCS: a phylogenetic and functional classification of
            ABC systems in living organisms
  JOURNAL   Res Microbiol 152 (3-4), 211-229 (2001)
   PUBMED   11421270
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467400
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..351
                     /product="ABC transporter ATP-binding protein"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=37363
     Region          1..343
                     /region_name="MalK"
                     /note="ABC-type sugar transport system, ATPase component
                     MalK [Carbohydrate transport and metabolism]; COG3839"
                     /db_xref="CDD:443050"
ORIGIN      
        1 mssivldnlt kqygnaaaih gvsftvpags ftvllgpsgc gksttlrmia gldtptsgsi
       61 higdrdvtql ppakrrismv fqsyalfphl svrenilfgl kvrkepardy drrlqrvasl
      121 lglnhlldrk psqlsggqqq rvalgravis eapvclmdep lsnldaqlrh emrreiralq
      181 qdlgitmvyv thdqteamsm adqvvllrgg kieqhdtpdg lyarpatefa arfigtppmn
      241 lislaprqgg fviagtqgpd iagapagaak lgvrpehiri daggiaatve sveyfgadsi
      301 vvcrvgdtsg vavrvgghlr asagetlgls wqdsqqhffa adsavinsag r
//
LOCUS       WP_176089976             135 aa            linear   BCT 11-JAN-2025
DEFINITION  DoxX family protein [Achromobacter anxifer].
ACCESSION   WP_176089976
VERSION     WP_176089976.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Nambi,S., Long,J.E., Mishra,B.B., Baker,R., Murphy,K.C.,
            Olive,A.J., Nguyen,H.P., Shaffer,S.A. and Sassetti,C.M.
  TITLE     The Oxidative Stress Network of Mycobacterium tuberculosis Reveals
            Coordination between Radical Detoxification Systems
  JOURNAL   Cell Host Microbe 17 (6), 829-837 (2015)
   PUBMED   26067605
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Muller,F.H., Bandeiras,T.M., Urich,T., Teixeira,M., Gomes,C.M. and
            Kletzin,A.
  TITLE     Coupling of the pathway of sulphur oxidation to dioxygen reduction:
            characterization of a novel membrane-bound thiosulphate:quinone
            oxidoreductase
  JOURNAL   Mol Microbiol 53 (4), 1147-1160 (2004)
   PUBMED   15306018
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10006227
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..135
                     /product="DoxX family protein"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /calculated_mol_wt=13841
     Region          6..134
                     /region_name="DoxX"
                     /note="Uncharacterized membrane protein YphA, DoxX/SURF4
                     family [Function unknown]; COG2259"
                     /db_xref="CDD:441860"
ORIGIN      
        1 miksddtgkl ilrltlgili llhglfkltg ggvsgiagml sshglpgfla ygayvgeila
       61 pvllivgiyt rlgglliavn mvvaillaht gqlssmtnng gwalelqgmf lftalaiafm
      121 gagrfslagn ggrwn
//
LOCUS       WP_176089992             395 aa            linear   BCT 11-JAN-2025
DEFINITION  GGDEF domain-containing protein [Achromobacter anxifer].
ACCESSION   WP_176089992
VERSION     WP_176089992.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Romling,U. and Amikam,D.
  TITLE     Cyclic di-GMP as a second messenger
  JOURNAL   Curr Opin Microbiol 9 (2), 218-228 (2006)
   PUBMED   16530465
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Romling,U., Gomelsky,M. and Galperin,M.Y.
  TITLE     C-di-GMP: the dawning of a novel bacterial signalling system
  JOURNAL   Mol Microbiol 57 (3), 629-639 (2005)
   PUBMED   16045609
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Simm,R., Morr,M., Kader,A., Nimtz,M. and Romling,U.
  TITLE     GGDEF and EAL domains inversely regulate cyclic di-GMP levels and
            transition from sessility to motility
  JOURNAL   Mol Microbiol 53 (4), 1123-1134 (2004)
   PUBMED   15306016
REFERENCE   4  (residues 1 to 395)
  AUTHORS   D'Argenio,D.A. and Miller,S.I.
  TITLE     Cyclic di-GMP as a bacterial second messenger
  JOURNAL   Microbiology (Reading) 150 (Pt 8), 2497-2502 (2004)
   PUBMED   15289546
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Jenal,U.
  TITLE     Cyclic di-guanosine-monophosphate comes of age: a novel secondary
            messenger involved in modulating cell surface structures in
            bacteria?
  JOURNAL   Curr Opin Microbiol 7 (2), 185-191 (2004)
   PUBMED   15063857
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Pei,J. and Grishin,N.V.
  TITLE     GGDEF domain is homologous to adenylyl cyclase
  JOURNAL   Proteins 42 (2), 210-216 (2001)
   PUBMED   11119645
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10005578
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..395
                     /product="GGDEF domain-containing protein"
                     /EC_number="2.7.7.65"
                     /GO_component="GO:0005886 - plasma membrane [Evidence
                     IEA]"
                     /GO_function="GO:0005525 - GTP binding [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0052621 - diguanylate cyclase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=42397
     Region          118..380
                     /region_name="GGDEF"
                     /note="GGDEF domain, diguanylate cyclase (c-di-GMP
                     synthetase) or its enzymatically inactive variants [Signal
                     transduction mechanisms]; COG2199"
                     /db_xref="CDD:441801"
ORIGIN      
        1 miapvnllli aalagvlalc vlgslarsgm agikeairan lltlaafgly alqitdaplw
       61 lsviasntav alalcayytg lrrlvglpvp rrlmvlasga tllvlagyty iepevgprmv
      121 amsalmaafm vaivvtvgrg mpanrsryay hfvrvvalvs aavcmtragv ylldiatpqa
      181 lllptvwntv fmtlgvltmp cltlgtimii hdrmladreq eastdfltgl msrkawwlqa
      241 erycaqalrt rrpltlllld idhfkrindt hghaagdavl rhfgllatat lrtgdhvgrv
      301 ggeefavlfp dmrsdavmev agrlldsvrr tpcahggsii syafsagvad wvpgeslqaf
      361 feradrklya akaagrnriv gpgqeaerqp lpeaa
//
LOCUS       WP_176090022             106 aa            linear   BCT 11-JAN-2025
DEFINITION  helix-turn-helix domain-containing protein [Achromobacter anxifer].
ACCESSION   WP_176090022
VERSION     WP_176090022.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10009472
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..106
                     /product="helix-turn-helix domain-containing protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=11522
     Region          1..100
                     /region_name="COG5606"
                     /note="Predicted DNA-binding protein, XRE-type HTH domain
                     [General function prediction only]"
                     /db_xref="CDD:444337"
ORIGIN      
        1 mtrnnsspst dnvlldlgfe daeelsakaa lalklndlid qrglsqmeaa altgmtqpkv
       61 sqirryklqn islerlmral vsldqhveiv veparrahar gitvaa
//
LOCUS       WP_176090131             359 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Achromobacter anxifer].
ACCESSION   WP_176090131
VERSION     WP_176090131.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11467437
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..359
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=38639
     Region          10..357
                     /region_name="PotA"
                     /note="ABC-type Fe3+/spermidine/putrescine transport
                     systems, ATPase component [Amino acid transport and
                     metabolism]; COG3842"
                     /db_xref="CDD:443052"
ORIGIN      
        1 mgqgqktagt pilqiqnvsk tfgasaalkg vsldvregef ltllgpsgcg kttliriiag
       61 fetptsgdvr idgqsilsap pyrrplgmvf qnlalfphlt vaenigyglr mrretpaair
      121 gkverslamv glegygaryi gqisggqkqr valaraivme prvllldepl galdmkirrq
      181 mqtelkliqe klgttfifvt hdqeealtms drvavfrngl idqvsdpati yekpqtrfva
      241 efvgdtnffe gvvqagaarv dcaelgcafd lpeprfaags avgvslrpqh lrlasaagar
      301 lqahverrvy agqntrvwlq agarsliadw paqdglslpe qgaavgltwd dsrisvvsl
//
LOCUS       WP_176090150             180 aa            linear   BCT 11-JAN-2025
DEFINITION  MOSC domain-containing protein [Achromobacter anxifer].
ACCESSION   WP_176090150
VERSION     WP_176090150.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     MOSC domains: ancient, predicted sulfur-carrier domains, present in
            diverse metal-sulfur cluster biosynthesis proteins including
            Molybdenum cofactor sulfurases
  JOURNAL   FEMS Microbiol Lett 207 (1), 55-61 (2002)
   PUBMED   11886751
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11455027
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..180
                     /product="MOSC domain-containing protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0030151 - molybdenum ion binding
                     [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /calculated_mol_wt=18791
     Region          5..178
                     /region_name="YiiM"
                     /note="N-hydroxylaminopurine reductase YiiM, contains MOSC
                     domain [Nucleotide transport and metabolism, Defense
                     mechanisms]; COG2258"
                     /db_xref="CDD:441859"
ORIGIN      
        1 mrpivtavac spahgfskav vpaimlrkgl gvegdahmgv tvkhrsrvka dptqpnlrqv
       61 hlihgelhde lqlagfnvae gtmgenittr gldllglprg allhigadav vevtglrnpc
      121 sqldnyqkgl taavlgrhpd gslmrragim givveggavs agdairvvlp alphlplerv
//
LOCUS       WP_176090192             232 aa            linear   BCT 11-JAN-2025
DEFINITION  fumarylacetoacetate hydrolase family protein [Achromobacter
            anxifer].
ACCESSION   WP_176090192
VERSION     WP_176090192.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Weiss,A.K.H., Loeffler,J.R., Liedl,K.R., Gstach,H. and
            Jansen-Durr,P.
  TITLE     The fumarylacetoacetate hydrolase (FAH) superfamily of enzymes:
            multifunctional enzymes from microbes to mitochondria
  JOURNAL   Biochem Soc Trans 46 (2), 295-309 (2018)
   PUBMED   29487229
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11415096
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..232
                     /product="fumarylacetoacetate hydrolase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=24885
     Region          22..232
                     /region_name="YcgM"
                     /note="2-keto-4-pentenoate
                     hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase
                     (catechol pathway) [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG0179"
                     /db_xref="CDD:439949"
ORIGIN      
        1 msyvvdpaap vavpvagsqd sfpvrrvycv grnyaahare mgfdpdrepp fffckpadav
       61 vpvaegstls lpypsetanl hyeielvaai gkgganisvd ealqhvwgya vgldmtrrdl
      121 qmkmreagrp welgkafdqs apigplypas avknidqaai wlqvngadkq rsdigkliws
      181 vaetiaylsk yfrleagdli ytgtpegvgp vvrgdkmlgg vdglgtlsvq mv
//
LOCUS       WP_176090198             173 aa            linear   BCT 11-JAN-2025
DEFINITION  response regulator transcription factor [Achromobacter anxifer].
ACCESSION   WP_176090198
VERSION     WP_176090198.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Galperin,M.Y.
  TITLE     Diversity of structure and function of response regulator output
            domains
  JOURNAL   Curr Opin Microbiol 13 (2), 150-159 (2010)
   PUBMED   20226724
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Stock,A.M., Robinson,V.L. and Goudreau,P.N.
  TITLE     Two-component signal transduction
  JOURNAL   Annu Rev Biochem 69, 183-215 (2000)
   PUBMED   10966457
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11468274
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..173
                     /product="response regulator transcription factor"
                     /GO_function="GO:0000156 - phosphorelay response regulator
                     activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_process="GO:0000160 - phosphorelay signal transduction
                     system [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=17806
     Region          <2..71
                     /region_name="FixJ"
                     /note="DNA-binding response regulator, FixJ family,
                     consists of REC and HTH domains [Signal transduction
                     mechanisms, Transcription]; COG4566"
                     /db_xref="CDD:443623"
ORIGIN      
        1 mqaprpdles vlssltprer eivayvaagr pnkviaidlg islrtveahr arifaklqvr
       61 hamqlacrlc ehgrsgaspv lgasgapgag agregpprqg lsrqqehpgp avheyallpm
      121 prlgsgvpsq vlheasgpey gqyqagpapp qsdpgaglar dagpflpgad agv
//
LOCUS       WP_176090235             334 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Achromobacter anxifer].
ACCESSION   WP_176090235
VERSION     WP_176090235.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 334)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..334
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=36366
     Region          45..315
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 mkslpsprla aaalfalfap laaqaealnp pvkvryeevv rsilyvpkyv alsqgyfkda
       61 gldvsmktsq gtdkgmtall sgsadivlig peasiyvhns espvkpkifa gltatdgffl
      121 larkpvekfd wsmlkgkevi gfrpgsnpiv fletalrkhg vdpqkdvkll nnigiparag
      181 awmagqgeyg iflepeagel vrngkgyiva svghevgqvd ytvftatdky irdnpkviqa
      241 wtdvvaraek yvkdtpaatl tpqimsyfpg mdqaavteai erykkyqiwk atplvtaeam
      301 nqlqdmlias avmkdnarvk yedvvvtdfa kkaq
//
LOCUS       WP_176090284             283 aa            linear   BCT 11-JAN-2025
DEFINITION  sulfurtransferase [Achromobacter anxifer].
ACCESSION   WP_176090284
VERSION     WP_176090284.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Cipollone,R., Ascenzi,P. and Visca,P.
  TITLE     Common themes and variations in the rhodanese superfamily
  JOURNAL   IUBMB Life 59 (2), 51-59 (2007)
   PUBMED   17454295
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Bordo,D. and Bork,P.
  TITLE     The rhodanese/Cdc25 phosphatase superfamily.
            Sequence-structure-function relations
  JOURNAL   EMBO Rep 3 (8), 741-746 (2002)
   PUBMED   12151332
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11458420
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..283
                     /product="sulfurtransferase"
                     /EC_number="2.8.1.-"
                     /GO_function="GO:0016783 - sulfurtransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0000098 - sulfur amino acid catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=29851
     Region          11..280
                     /region_name="SseA"
                     /note="3-mercaptopyruvate sulfurtransferase SseA, contains
                     two rhodanese domains [Inorganic ion transport and
                     metabolism]; COG2897"
                     /db_xref="CDD:442142"
ORIGIN      
        1 mtmtlisaad lakrldapdv rvfdvrhdlt nhaagrqayd aghipgaryl dhetelsaar
       61 tgkngrhplp sraafgalma ahgvtpqtlv vaydgsggmy aahlwwmlrw lghdqvavld
      121 ggwqawtaag lptttvaaaa vragepvepg lslagsvdaq tvldnisrpa ftvidaratn
      181 ryrgevepmd pvaghipgal nrpngenlqa dgrfkpaaql reefaslldg rdpaaivhqc
      241 gsgitachnl lsmeiaglsg srlypgswse wcsdpsrpva kga
//
LOCUS       WP_176090289             284 aa            linear   BCT 11-JAN-2025
DEFINITION  IclR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176090289
VERSION     WP_176090289.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Krell,T., Molina-Henares,A.J. and Ramos,J.L.
  TITLE     The IclR family of transcriptional activators and repressors can be
            defined by a single profile
  JOURNAL   Protein Sci 15 (5), 1207-1213 (2006)
   PUBMED   16597823
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Molina-Henares,A.J., Krell,T., Eugenia Guazzaroni,M., Segura,A. and
            Ramos,J.L.
  TITLE     Members of the IclR family of bacterial transcriptional regulators
            function as activators and/or repressors
  JOURNAL   FEMS Microbiol Rev 30 (2), 157-186 (2006)
   PUBMED   16472303
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11444403
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..284
                     /product="IclR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=29160
     Region          41..282
                     /region_name="IclR"
                     /note="DNA-binding transcriptional regulator, IclR family
                     [Transcription]; COG1414"
                     /db_xref="CDD:441024"
ORIGIN      
        1 mqsfsdpkri ahpaakpdgk velslparrk raagagegas spdfitalar gldvlrcfrh
       61 gvaalgnldl arltglpkpt isritytlte lgylryhpdt gkyspgygvl algfgllagl
      121 evrelakasm telaratgga valgafdgda mtyveaihgs salylrlpvg yrasldsamg
      181 raylaslppq acadalarlg eaapapaaie raraelretg ccyaigewqs ginavavpfs
      241 sitgegvfvm scggpasllp eaglrtrvap llraaiagla gapa
//
LOCUS       WP_176090323             509 aa            linear   BCT 11-JAN-2025
DEFINITION  amidase [Achromobacter anxifer].
ACCESSION   WP_176090323
VERSION     WP_176090323.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000643
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..509
                     /product="amidase"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=52398
     Region          8..506
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
ORIGIN      
        1 mstaerhdss tldatalgad iaqgattala amqqavdrva arnpsinaac gvqaeiglrl
       61 aqsldeelag lsqeqrlaql qqrpflgvpt llkdlgtaal glpssmgsvl ygqvqwnvda
      121 eivkryrrag lipfgrttsa elglspttes pvygpatqnp wkaghsaggs sggagaalas
      181 gmvriahgsd gggsiripss ccgvlglkps rglmplgplk gegwgglate hmmtlsvrdc
      241 aasldisaga dvgapyaapa qpaesyrava arvaadprsa ahrriafvnt tyegeaihpe
      301 vaaavdeaak lfaslghelv pvappvgsee vlspmlplia saaanaidgf vaargrrlaa
      361 delqpttlga reyaraisga qyvacvdtch eitrrvgrfl eregtqgydl flspvlaqpp
      421 aaigryamdn adylayrlgk kgvigyspfa planltgmpa isipfgmssd glpigiqlmg
      481 plgseallle laaqvealrp walvapmar
//
LOCUS       WP_176090346             416 aa            linear   BCT 11-JAN-2025
DEFINITION  TolC family protein [Achromobacter anxifer].
ACCESSION   WP_176090346
VERSION     WP_176090346.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Johnson,J.M. and Church,G.M.
  TITLE     Alignment and structure prediction of divergent protein families:
            periplasmic and outer membrane proteins of bacterial efflux pumps
  JOURNAL   J Mol Biol 287 (3), 695-715 (1999)
   PUBMED   10092468
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446113
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..416
                     /product="TolC family protein"
                     /GO_function="GO:0015562 - efflux transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=43318
     Region          41..416
                     /region_name="TolC"
                     /note="Outer membrane protein TolC [Cell
                     wall/membrane/envelope biogenesis]; COG1538"
                     /db_xref="CDD:441147"
ORIGIN      
        1 mrlsvlpltl aalliaspas gegaggtrtp vpleqggavl tlesalsaal ernpgfsaar
       61 neaeasvgll aqagvlpnps idvsvddtqk atrtttamln vpvetggkra arvkaaelsr
      121 dmarqgveda raglraavia affdvavaqe svrvargtvd iaggalrlae rrvaagkapp
      181 legskaqval anariearaa eaalldarrk lgllwgeaep afasvggdln alpqrapide
      241 lrsalaaspk mqggklsvdl graqleveks krypdvtlsa gvardneagr nkallgvsip
      301 lpifdrnqgn vyaasmqayk aqdlyreles glmaqllqav srfdlavgsa reyrksvlpg
      361 ateayeaark gfeagkfgfl evldaqrtls dgniayltvl asvyqasadi drilgr
//
LOCUS       WP_176090356             318 aa            linear   BCT 11-JAN-2025
DEFINITION  glycosyltransferase family 9 protein [Achromobacter anxifer].
ACCESSION   WP_176090356
VERSION     WP_176090356.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Breton,C., Snajdrova,L., Jeanneau,C., Koca,J. and Imberty,A.
  TITLE     Structures and mechanisms of glycosyltransferases
  JOURNAL   Glycobiology 16 (2), 29R-37R (2006)
   PUBMED   16037492
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Coutinho,P.M., Deleury,E., Davies,G.J. and Henrissat,B.
  TITLE     An evolving hierarchical family classification for
            glycosyltransferases
  JOURNAL   J Mol Biol 328 (2), 307-317 (2003)
   PUBMED   12691742
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11436709
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..318
                     /product="glycosyltransferase family 9 protein"
                     /EC_number="2.4.-.-"
                     /GO_function="GO:0016757 - glycosyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35848
     Region          14..310
                     /region_name="RfaF"
                     /note="ADP-heptose:LPS heptosyltransferase [Cell
                     wall/membrane/envelope biogenesis]; COG0859"
                     /db_xref="CDD:440620"
ORIGIN      
        1 mpevvvyvrs qpqlgdqiva lptlyqlktw waskrirvva rddlggfyrs vpwvdefvra
       61 atfgdylrsl kkntgvcvsl hhsserfgll nllrlpamrf gfrnarlsdl vwthchrkni
      121 geyiglanlr llasyrrfda eaaarrcfqt lahphrhdvl gadvvlipgg gagafkrwsl
      181 lnylrlaerl klllgpdtrf lfvlgaqeaa erqkletmrr pefsiafcrp lrelsaimlr
      241 arlvvsndcg pshiaqgacv pyvgifnean pewfwdrpys aavvpehprd ginsitpddv
      301 lgacrkvleh hahpayag
//
LOCUS       WP_176090369             763 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Achromobacter anxifer].
ACCESSION   WP_176090369
VERSION     WP_176090369.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 763)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..763
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..763
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=82056
     Region          <50..>186
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          195..760
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 mthtaqlsrr gflqgalgal tlavtskglv ttawaaesga qkygadsmpg gtvddplvfv
       61 siaadgtvti vahraemgtg vrtslpmvva demearwdrv kivqaqadea rygnqnvdgs
      121 rsvrhflmpm rrvgaaarqm leaaaaarws vpvaevkavq hevlhqptgr rlaygelaad
      181 aakqpvpagd alklkdraef ryigkdqvrl vdleaigkgq asygmdmhlp gmvyavvarp
      241 pvvggklrrf dsakalavpg vlkvveippm qgapafqplg gvavvarntw aarqgrdale
      301 iewddgpngs ydsntyrqtl esaarkpgka mrnqgdaaqa wakapeaerv taeyyvphla
      361 hasmeppaat vlikdgraev wtsvqnpiaa rdavsarlkl epakvtvnvl llgggfgrks
      421 kpdfvdeaai varampegtp vklvwtredd ihhdylhtvs verleavldk ngqvqswlhr
      481 saaptiaslf segakgqqlf esamsainmp yripnvrvet aeveaharig wfrsvaniph
      541 ayaaqcfiae lahragkdpk dfaldligpa rridpgtmad twnysesper ypydtgrlrg
      601 vieaackgae wgrtlpqghg lglafcysfm sytatvveva vdakgqvrvv avdmamdcgp
      661 qinperiraq meggaimglg lamvseisfe kgrvkqsnfh dyevlrhnas prvirthlvn
      721 ddhalppggv geppvppvap alcnaifaat gkrvrslpvr sga
//
LOCUS       WP_176090379             213 aa            linear   BCT 11-JAN-2025
DEFINITION  glutathione S-transferase family protein [Achromobacter anxifer].
ACCESSION   WP_176090379
VERSION     WP_176090379.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Dulhunty,A., Gage,P., Curtis,S., Chelvanayagam,G. and Board,P.
  TITLE     The glutathione transferase structural family includes a nuclear
            chloride channel and a ryanodine receptor calcium release channel
            modulator
  JOURNAL   J Biol Chem 276 (5), 3319-3323 (2001)
   PUBMED   11035031
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11427749
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..213
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=23503
     Region          20..213
                     /region_name="GstA"
                     /note="Glutathione S-transferase [Posttranslational
                     modification, protein turnover, chaperones]; COG0625"
                     /db_xref="CDD:440390"
ORIGIN      
        1 mnqtphplag kpleladtlr sgnawkirla cgymglpikr rtfdivqgdl eteafarinp
       61 wrqvpalltp egewlaesqa ilwylamgtp wlpagrleqa qvsswlsfeq tqhmhafaqp
      121 rllihlrnta qvddpamraw reigmkaaal mdahlagrdy lvgaaptiad valypytsma
      181 aeggydlsgf thidawlarm ralpgftpli eaa
//
LOCUS       WP_176090418             510 aa            linear   BCT 11-JAN-2025
DEFINITION  class I adenylate-forming enzyme family protein [Achromobacter
            anxifer].
ACCESSION   WP_176090418
VERSION     WP_176090418.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Gulick,A.M.
  TITLE     Conformational dynamics in the Acyl-CoA synthetases, adenylation
            domains of non-ribosomal peptide synthetases, and firefly
            luciferase
  JOURNAL   ACS Chem Biol 4 (10), 811-827 (2009)
   PUBMED   19610673
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11416945
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..510
                     /product="class I adenylate-forming enzyme family protein"
                     /EC_number="6.-.-.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016874 - ligase activity [Evidence IEA]"
                     /calculated_mol_wt=53723
     Region          3..499
                     /region_name="MenE/FadK"
                     /note="O-succinylbenzoic acid-CoA ligase MenE or related
                     acyl-CoA synthetase (AMP-forming) [Lipid transport and
                     metabolism]; COG0318"
                     /db_xref="CDD:440087"
ORIGIN      
        1 myltqglhra grlypgkial regarswtya allawtarka avlrghgvlp gdrvallgan
       61 gadyvswila cwwlgaaamp lntrwsgael sraladcgpr lllvdeamap riagvevpra
      121 tsplsaevla ahaetedaaq dvraggdala ailytggttg spkgamltha nlwsaavarm
      181 atvptppdss tllvaplfhv aglgrligqi vagasivvqr gfnpravlqa lqdegvsevl
      241 lvpsmiqmll depgfaqyrl dgvarviwga spisralldr alaafpraef vhaygmteta
      301 atvainaqvr lggaraesag rpalgvetci lapdgseaap gvigelavrg pmvmqgywnq
      361 pedtrrvfaq gwlltgdaar qdedgylyiv drlkdmivsg genvygaeve gvlahhalva
      421 rcavigvahe rwgeavhavi vpragmapda aaldrhcraq laaykcpkty eflgelpmsa
      481 agkvlksvlr qdhesrraav aapahqekqa
//
LOCUS       WP_176090429             386 aa            linear   BCT 11-JAN-2025
DEFINITION  D-alanyl-D-alanine carboxypeptidase family protein [Achromobacter
            anxifer].
ACCESSION   WP_176090429
VERSION     WP_176090429.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Families of serine peptidases
  JOURNAL   Methods Enzymol 244, 19-61 (1994)
   PUBMED   7845208
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Evolutionary families of peptidases
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 205-218 (1993)
   PUBMED   8439290
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Ghuysen,J.M.
  TITLE     Serine beta-lactamases and penicillin-binding proteins
  JOURNAL   Annu Rev Microbiol 45, 37-67 (1991)
   PUBMED   1741619
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447584
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..386
                     /product="D-alanyl-D-alanine carboxypeptidase family
                     protein"
                     /EC_number="3.4.-.-"
                     /GO_function="GO:0008236 - serine-type peptidase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=41212
     Region          3..372
                     /region_name="DacC"
                     /note="D-alanyl-D-alanine carboxypeptidase [Cell
                     wall/membrane/envelope biogenesis]; COG1686"
                     /db_xref="CDD:441292"
ORIGIN      
        1 mlmkklaasl ivaaacmsga vaqtvpapal sakawlllde tsgqviashe attriepasl
       61 tkimtayvvf ealskkelsa nqlvtvstra wkvpagsskm flepgskvsv ddllrglmiq
      121 sgndaaiala eavsgsveaf varmndtaak lglhathfas phglpdpgty stasdlsvla
      181 arfirdypdl yktydsakqf tfnkitqpnr nrllwldpsv dglktghtes agycivasar
      241 rpngadqrrl itvvvgtasd klrtqesrel lewgfqgfnt iklyargqav atpevwkgeh
      301 dtlkagfard ayvtvpagak vepvwtpqdp lvapiaaqst vgslrvlvdg kpamqfpvva
      361 lepvaeagfa grawdsirlw wrghag
//
LOCUS       WP_176090441             540 aa            linear   BCT 11-JAN-2025
DEFINITION  acyl-CoA synthetase [Achromobacter anxifer].
ACCESSION   WP_176090441
VERSION     WP_176090441.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Schmelz,S. and Naismith,J.H.
  TITLE     Adenylate-forming enzymes
  JOURNAL   Curr Opin Struct Biol 19 (6), 666-671 (2009)
   PUBMED   19836944
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Starai,V.J. and Escalante-Semerena,J.C.
  TITLE     Acetyl-coenzyme A synthetase (AMP forming)
  JOURNAL   Cell Mol Life Sci 61 (16), 2020-2030 (2004)
   PUBMED   15316652
REFERENCE   3  (residues 1 to 540)
  AUTHORS   Karan,D., David,J.R. and Capy,P.
  TITLE     Molecular evolution of the AMP-forming Acetyl-CoA synthetase
  JOURNAL   Gene 265 (1-2), 95-101 (2001)
   PUBMED   11255012
REFERENCE   4  (residues 1 to 540)
  AUTHORS   Watkins,P.A.
  TITLE     Fatty acid activation
  JOURNAL   Prog Lipid Res 36 (1), 55-83 (1997)
   PUBMED   9373621
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10149318
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..540
                     /product="acyl-CoA synthetase"
                     /EC_number="6.2.1.-"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016405 - CoA-ligase activity [Evidence
                     IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58058
     Region          48..536
                     /region_name="MACS_like_3"
                     /note="Uncharacterized subfamily of medium-chain acyl-CoA
                     synthetase (MACS); cd05971"
                     /db_xref="CDD:341275"
     Site            order(111,239..241,265,285,287,291,312..315,334..339,
                     342..343,359,419,431,434,440,442..445,474,503,508..509,
                     511,513)
                     /site_type="active"
                     /db_xref="CDD:341275"
     Site            order(190,193..198,200..201)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341275"
     Site            order(235,287..288,291,312,442..444,503,509)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341275"
     Site            order(312..315,334..339,359,419,431,434,440,445)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341275"
ORIGIN      
        1 mltradsytq lasqfqwqvp aaynigvdac dkwadgsgrl aliyeksdga qsrytfdqik
       61 alsnqlarsl erhgvkrgdr vavylpqape tavthiavyk mgavavplft lfgvdaiqyr
      121 lansgaaalv tdaegcrklr eiraslpdlk vvycidedcp dgalpfhael aaesedytpa
      181 ataaddpavi iytsgttgkp kgalhahrvl lghlpgvems heffpenaal mwtpadwawi
      241 gglldvllps whhgvpvlar rfekfdgasa felmarhgvt htflpptalk mmrgtelpag
      301 agalalrsva sggeslgael idwgrrvlgv tinefygqte cnmlvsscss lfdpcigaig
      361 raapghrvai vddqgaevad gqegnigvlr ldpvmflgyw nnpeataekf agdylltgdq
      421 gvrdaqgfir fvgrnddvit sagyrigpgp iedclighpa vrmaavvgvp daqrteivma
      481 yvvlnegyag sdalvkdlqa hvrkrlaahe yprairfvts lpttatgkii rrelrdgsya
//
LOCUS       WP_176090477             864 aa            linear   BCT 11-JAN-2025
DEFINITION  penicillin-binding protein 1A [Achromobacter anxifer].
ACCESSION   WP_176090477
VERSION     WP_176090477.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 864)
  AUTHORS   Sauvage,E., Kerff,F., Terrak,M., Ayala,J.A. and Charlier,P.
  TITLE     The penicillin-binding proteins: structure and role in
            peptidoglycan biosynthesis
  JOURNAL   FEMS Microbiol Rev 32 (2), 234-258 (2008)
   PUBMED   18266856
  REMARK    Erratum:[FEMS Microbiol Rev. 2008 May;32(3):556]
REFERENCE   2  (residues 1 to 864)
  AUTHORS   Zapun,A., Contreras-Martel,C. and Vernet,T.
  TITLE     Penicillin-binding proteins and beta-lactam resistance
  JOURNAL   FEMS Microbiol Rev 32 (2), 361-385 (2008)
   PUBMED   18248419
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11472030
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..864
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..864
                     /product="penicillin-binding protein 1A"
                     /EC_number="2.4.99.28"
                     /EC_number="3.4.16.4"
                     /GO_function="GO:0008658 - penicillin binding [Evidence
                     IEA]"
                     /GO_function="GO:0008955 - peptidoglycan
                     glycosyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0009002 - serine-type D-Ala-D-Ala
                     carboxypeptidase activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /GO_process="GO:0009252 - peptidoglycan biosynthetic
                     process [Evidence IEA]"
                     /calculated_mol_wt=93079
     Region          49..749
                     /region_name="MrcA"
                     /note="Membrane carboxypeptidase/penicillin-binding
                     protein [Cell wall/membrane/envelope biogenesis]; COG5009"
                     /db_xref="CDD:444033"
ORIGIN      
        1 mstpqqssan pggkpgfpwk rilvkagvaa agaavcgavl lglalalawp slpdlhamtd
       61 yrprvplriy tadkvligey geehrnvlrf deippvmrqa vlaaeddrfy shggvdwmgv
      121 aravltnvvk gsksqggsti tmqvarnfyl ssektysrkf yellltfkie seltkdqile
      181 lymnqiylgh raygfaaasr tylgkpladv tpaeaamlag ipkapsrfnp itnfpraeir
      241 qhyvlgrmkt lgyltpeqad ealkqrltir gadgssargf aihgdypael arqlmygvfq
      301 eetyskgidv yttidskdqe aayravrdgv mdytrravyp gpedqielpd gvekdatald
      361 eildgvqekt pdsedlltav vlaasptevt larsardiit isdkkalavv aralnpkasd
      421 sqrlrrgsvv yihkngdgwe iinmpalqaa lvsmvpqdga iramvggfdy nrggfnrvtq
      481 awrqpgsnik pfvyaaaler gltpatqisd qpfmltaeqt gskawqpknd gnkyepmltl
      541 rqglmrsknm vsirilqais pqyaqdyltr fgfdksrwpa vlplalgagg atplqvvngy
      601 svfanggyrv tpylvdrvtd rsgkvlmqaq pvvagdeqar aidprtawvm ddilrgvtvs
      661 gtaarahqvl krndiggktg ttndavdvwf sgftpslatt vwmgfdqpks lgtnefgsgl
      721 alstwldymq palkgipeak paprpdgliv dngeyyfsef ppgqavasld lssgdaltdf
      781 lnnnrstdgv dtsvkplqqp ggavpqdgsv qppvalpvpv psaggtpaan ppaippipvp
      841 rvegdapara savsgvgala arpl
//
LOCUS       WP_176090461             224 aa            linear   BCT 11-JAN-2025
DEFINITION  flavodoxin family protein [Achromobacter anxifer].
ACCESSION   WP_176090461
VERSION     WP_176090461.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10002025
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..224
                     /product="flavodoxin family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /calculated_mol_wt=24550
     Region          9..188
                     /region_name="WrbA"
                     /note="Multimeric flavodoxin WrbA, includes
                     NAD(P)H:quinone oxidoreductase [Energy production and
                     conversion]; COG0655"
                     /db_xref="CDD:440420"
ORIGIN      
        1 mnsdhpekrl lilvgsprrd gnsaalgaaa qrgaeaagan atllflddyi qsflpdlrhs
       61 pvptdryael flehflpadg vllstpiywy gmsaqskaff drsfshyags gpepervrqr
      121 mtgkrlglav aseetypgaa lgivhqvqey srythsefig hvhgagnlrg eiandprrpl
      181 qaaeelgasf ftrkysdyrv etprsrnvwe paapalrstp gvlp
//
LOCUS       WP_176090498             143 aa            linear   BCT 11-JAN-2025
DEFINITION  MerR family transcriptional regulator [Achromobacter anxifer].
ACCESSION   WP_176090498
VERSION     WP_176090498.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Fang,C. and Zhang,Y.
  TITLE     Bacterial MerR family transcription regulators: activationby
            distortion
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 54 (1), 25-36 (2022)
   PUBMED   35130613
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Hobman,J.L.
  TITLE     MerR family transcription activators: similar designs, different
            specificities
  JOURNAL   Mol Microbiol 63 (5), 1275-1278 (2007)
   PUBMED   17302809
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Brown,N.L., Stoyanov,J.V., Kidd,S.P. and Hobman,J.L.
  TITLE     The MerR family of transcriptional regulators
  JOURNAL   FEMS Microbiol Rev 27 (2-3), 145-163 (2003)
   PUBMED   12829265
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10140925
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..143
                     /product="MerR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=15719
     Region          19..114
                     /region_name="HTH_MlrA-like_sg2"
                     /note="Helix-Turn-Helix DNA binding domain of putative
                     MlrA-like transcription regulators; cd04765"
                     /db_xref="CDD:133393"
     Site            order(20..22,36,53..55)
                     /site_type="DNA binding"
                     /note="DNA binding residues [nucleotide binding]"
                     /db_xref="CDD:133393"
ORIGIN      
        1 mtrtestvtl ppipakryft igevsdlcgv kphvlryweq eftqlkpvkr rgnrryyqhh
       61 evllirrirs llyeqgftis garnrlgdar evphdqdaav rlsgaemqsl rnelgnvstm
      121 laealgtaan tagasagaas psv
//
LOCUS       WP_176090583             179 aa            linear   BCT 11-JAN-2025
DEFINITION  VOC family protein [Achromobacter anxifer].
ACCESSION   WP_176090583
VERSION     WP_176090583.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   He,P. and Moran,G.R.
  TITLE     Structural and mechanistic comparisons of the metal-binding members
            of the vicinal oxygen chelate (VOC) superfamily
  JOURNAL   J Inorg Biochem 105 (10), 1259-1272 (2011)
   PUBMED   21820381
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Armstrong,R.N.
  TITLE     Mechanistic diversity in a metalloenzyme superfamily
  JOURNAL   Biochemistry 39 (45), 13625-13632 (2000)
   PUBMED   11076500
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001243
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..179
                     /product="VOC family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=20000
     Region          11..142
                     /region_name="GloA"
                     /note="Catechol 2,3-dioxygenase or related enzyme, vicinal
                     oxygen chelate (VOC) family [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0346"
                     /db_xref="CDD:440115"
ORIGIN      
        1 mdhtaarpve glhhfawrcr daeetrrfye dllglplvhv ikkdsvpstg efcpyvhiff
       61 rmrdgsciaf fdlgdqtaal pspntpgwvn hialrvpqve dllamkvrle ahgvevvgvt
      121 dhdsyiesiy ffdpnglrle ltvevaapev vegyareara eldrwtadkr vlaaqgsla
//
LOCUS       WP_176090630             169 aa            linear   BCT 11-JAN-2025
DEFINITION  flavin reductase family protein [Achromobacter anxifer].
ACCESSION   WP_176090630
VERSION     WP_176090630.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Pimviriyakul,P. and Chaiyen,P.
  TITLE     Overview of flavin-dependent enzymes
  JOURNAL   Enzymes 47, 1-36 (2020)
   PUBMED   32951820
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004785
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..169
                     /product="flavin reductase family protein"
                     /GO_function="GO:0010181 - FMN binding [Evidence IEA]"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=18449
     Region          9..161
                     /region_name="RutF"
                     /note="FMN reductase RutF, DIM6/NTAB family [Energy
                     production and conversion]; COG1853"
                     /db_xref="CDD:441458"
ORIGIN      
        1 mslsstaiep rrfrealghy asgitvitsh iegepigftc qsfhsvsmsp plvsfsvmts
       61 sasypkirra grftvnilsd eqvrisnqfa qrgadkwhdv ewqksplgnp iiagslhwld
      121 ceihaehpag dhlivigevk alnlqegast qpllyfkgqy rniaahgav
//
LOCUS       WP_176090679             130 aa            linear   BCT 11-JAN-2025
DEFINITION  RidA family protein [Achromobacter anxifer].
ACCESSION   WP_176090679
VERSION     WP_176090679.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Niehaus,T.D., Gerdes,S., Hodge-Hanson,K., Zhukov,A., Cooper,A.J.,
            ElBadawi-Sidhu,M., Fiehn,O., Downs,D.M. and Hanson,A.D.
  TITLE     Genomic and experimental evidence for multiple metabolic functions
            in the RidA/YjgF/YER057c/UK114 (Rid) protein family
  JOURNAL   BMC Genomics 16 (1), 382 (2015)
   PUBMED   25975565
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Lambrecht,J.A., Flynn,J.M. and Downs,D.M.
  TITLE     Conserved YjgF protein family deaminates reactive enamine/imine
            intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme
            reactions
  JOURNAL   J Biol Chem 287 (5), 3454-3461 (2012)
   PUBMED   22094463
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Mistiniene,E., Luksa,V., Sereikaite,J. and Naktinis,V.
  TITLE     Oligomeric assembly and ligand binding of the members of protein
            family YER057c/YIL051c/YJGF
  JOURNAL   Bioconjug Chem 14 (6), 1243-1252 (2003)
   PUBMED   14624641
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10000806
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..130
                     /product="RidA family protein"
                     /calculated_mol_wt=13409
     Region          1..129
                     /region_name="RidA"
                     /note="Enamine deaminase RidA, house cleaning of reactive
                     enamine intermediates, YjgF/YER057c/UK114 family [Defense
                     mechanisms]; COG0251"
                     /db_xref="CDD:440021"
ORIGIN      
        1 maghplnpag vcaplgpysq gvltegagrw lhiagqvgvs segalaqgfe aqahaawrni
       61 qamleaagmd agdlvkvvty itdesqlpll gpvrlaylge arpaatlvvv ralarpewli
      121 eveasaykpa
//
LOCUS       WP_176090700             155 aa            linear   BCT 11-JAN-2025
DEFINITION  molybdenum cofactor biosynthesis protein MoaE [Achromobacter
            anxifer].
ACCESSION   WP_176090700
VERSION     WP_176090700.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10001056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..155
                     /product="molybdenum cofactor biosynthesis protein MoaE"
                     /EC_number="2.8.1.12"
                     /GO_function="GO:0030366 - molybdopterin synthase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006777 - Mo-molybdopterin cofactor
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=16892
     Region          1..143
                     /region_name="MoaE"
                     /note="Molybdopterin synthase catalytic subunit MoaE
                     [Coenzyme transport and metabolism]; COG0314"
                     /db_xref="CDD:440083"
ORIGIN      
        1 misvqeadfd gaaltaalre sagpgvggiv tfvgyvrdya pdtptdtlfl ehypgmcere
       61 leeiaatara rwnldgtviv hrvgalprna qivfvaaasa hrgdafrgce yiidalktra
      121 pfwkretlag gssfwveqrq sdqdrtqswd edtta
//
LOCUS       WP_176090714             291 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter ATP-binding protein [Achromobacter anxifer].
ACCESSION   WP_176090714
VERSION     WP_176090714.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Bouige,P., Laurent,D., Piloyan,L. and Dassa,E.
  TITLE     Phylogenetic and functional classification of ATP-binding cassette
            (ABC) systems
  JOURNAL   Curr Protein Pept Sci 3 (5), 541-559 (2002)
   PUBMED   12370001
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Holland,I.B. and Blight,M.A.
  TITLE     ABC-ATPases, adaptable energy generators fuelling transmembrane
            movement of a variety of molecules in organisms from bacteria to
            humans
  JOURNAL   J Mol Biol 293 (2), 381-399 (1999)
   PUBMED   10529352
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11438110
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..291
                     /product="ABC transporter ATP-binding protein"
                     /EC_number="7.6.2.-"
                     /GO_function="GO:0005215 - transporter activity [Evidence
                     IEA]"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0016887 - ATP hydrolysis activity
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0006810 - transport [Evidence IEA]"
                     /calculated_mol_wt=31410
     Region          1..262
                     /region_name="TauB"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, ATPase component [Inorganic ion transport and
                     metabolism]; COG1116"
                     /db_xref="CDD:440733"
ORIGIN      
        1 mkkhvrierv gqtfntrkga fvalrdidlt veqgefitli ghsgcgkstl lnliagltrp
       61 tsgvllcaer eitgpgpdra vvfqnhsllp wlscfqnvyl avervfgase krpqlaerts
      121 aaldlvgllp aqhklpreis ggmkqrvgia ralaiepdvl lmdepfgald altrahlqde
      181 llkivaktrt ttvmvthdvd eavllsdriv mltngpaati geilavplpr prdrvrland
      241 aiylacraav vdflhrrhgn persqtaiqa naaldaepqp laeagasrav a
//
LOCUS       WP_176090731             335 aa            linear   BCT 11-JAN-2025
DEFINITION  ABC transporter substrate-binding protein [Achromobacter anxifer].
ACCESSION   WP_176090731
VERSION     WP_176090731.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Maqbool,A., Horler,R.S., Muller,A., Wilkinson,A.J., Wilson,K.S. and
            Thomas,G.H.
  TITLE     The substrate-binding protein in bacterial ABC transporters:
            dissecting roles in the evolution of substrate specificity
  JOURNAL   Biochem Soc Trans 43 (5), 1011-1017 (2015)
   PUBMED   26517916
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 335)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11431285
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..335
                     /product="ABC transporter substrate-binding protein"
                     /GO_component="GO:0055052 - ATP-binding cassette (ABC)
                     transporter complex, substrate-binding subunit-containing
                     [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /calculated_mol_wt=35242
     Region          36..326
                     /region_name="TauA"
                     /note="ABC-type nitrate/sulfonate/bicarbonate transport
                     system, periplasmic component [Inorganic ion transport and
                     metabolism]; COG0715"
                     /db_xref="CDD:440479"
ORIGIN      
        1 miyrnaphaf natrrrliqg aalgaatlaa palvraqsgp airigfwpva aglpfyaale
       61 kgyfkeagln veplkfagpq qimeamlagr adgsangtgs anlaigeias pglfkifasn
      121 psnakhvlde fivakdspik siadlkgkkv gsgpgiqnat lakavlerag atgatvvela
      181 isqhvaavaa gqldacytle ptgtvgrlng ttrvleagvi akyvlgdpma pwfggsaslt
      241 taflkkhpee srkfiaayar gielvrskpd earpylkgyt aiegpmteev plaaytlhne
      301 ftpgdiqyfq kffdlftdkg vfaqkvdvsa mlykg
//
LOCUS       WP_176090819             287 aa            linear   BCT 11-JAN-2025
DEFINITION  pirin family protein [Achromobacter anxifer].
ACCESSION   WP_176090819
VERSION     WP_176090819.1
KEYWORDS    RefSeq.
SOURCE      Achromobacter anxifer
  ORGANISM  Achromobacter anxifer
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Alcaligenaceae; Achromobacter.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11448280
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Achromobacter anxifer"
                     /db_xref="taxon:1287737"
     Protein         1..287
                     /product="pirin family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=30731
     Region          12..278
                     /region_name="YhaK"
                     /note="Redox-sensitive bicupin YhaK, pirin superfamily
                     [General function prediction only]; COG1741"
                     /db_xref="CDD:441347"
ORIGIN      
        1 mkkilglhas prphwvgdgf pvrsmfsynd kgkntspfll ldyagpaqfe paeqprgvgq
       61 hphrgfetvt ivysgevehr dstgnggvig pgdvqwmtaa sgilheefhs haftrkggel
      121 emvqlwvnlp akdkmapagy qgildadipa velpdgagtl rviagnyagh agpartftpm
      181 dvwdvrlaag ksatfpvaeg rnsmlvvlrg tvlvngetva rdaqlalfsl egeditvean
      241 ndavflvlsg epidepvvgy gpfvmntqae iveaiqdfna grygkmh
//
LOCUS       WP_176090993             471 aa            linear   BCT 11-JAN-2025
DEFINITION  phenylacetate--CoA ligase family protein [Burkholderia ambifaria].
ACCESSION   WP_176090993
VERSION     WP_176090993.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Luengo,J.M., Garcia,J.L. and Olivera,E.R.
  TITLE     The phenylacetyl-CoA catabolon: a complex catabolic unit with broad
            biotechnological applications
  JOURNAL   Mol Microbiol 39 (6), 1434-1442 (2001)
   PUBMED   11260461
REFERENCE   2  (residues 1 to 471)
  AUTHORS   El-Said Mohamed,M.
  TITLE     Biochemical and molecular characterization of
            phenylacetate-coenzyme A ligase, an enzyme catalyzing the first
            step in aerobic metabolism of phenylacetic acid in Azoarcus evansii
  JOURNAL   J Bacteriol 182 (2), 286-294 (2000)
   PUBMED   10629172
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Ferrandez,A., Minambres,B., Garcia,B., Olivera,E.R., Luengo,J.M.,
            Garcia,J.L. and Diaz,E.
  TITLE     Catabolism of phenylacetic acid in Escherichia coli.
            Characterization of a new aerobic hybrid pathway
  JOURNAL   J Biol Chem 273 (40), 25974-25986 (1998)
   PUBMED   9748275
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11446184
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..471
                     /product="phenylacetate--CoA ligase family protein"
                     /EC_number="6.2.1.30"
                     /GO_function="GO:0047475 - phenylacetate-CoA ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0010124 - phenylacetate catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=52982
     Region          64..>369
                     /region_name="PaaK"
                     /note="Phenylacetate-coenzyme A ligase PaaK,
                     adenylate-forming domain family [Coenzyme transport and
                     metabolism]; COG1541"
                     /db_xref="CDD:441150"
ORIGIN      
        1 mnglseertd ssiydtqshh ggitqimrqa vlneysqadt afmqmaalsh wwqhrdalla
       61 apyapveqir aqqlilirti vdyaftnvef yrnlysasgy tlgalqswnd faalpiiskk
      121 eitdhafgmt lvdgsdhiak fstrssgssg ipmttwldqn dvirdfaeqt rflheatkgs
      181 ltpqdwiytl hhggfwyssv lgkyrvfrlm dlehvdglva hwrklspril ttlpsylpml
      241 aaigplrpyg ieavttnsem screerdrys qlfdvpvlde ysseeiglma tecldgrhhv
      301 vedgvymeia dadhdgvgrv ivtdlgnylm plirydhgdl arlsdkpcsc grsfrgldal
      361 hgrqddalit tddryvptas vmaacdallt dersgmreyr liqcsatqid lhyvmspggt
      421 vdtdavvsal esrlshligh rielkaqche alptlpsykr rillrtwdgr r
//
LOCUS       WP_176090944             739 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia ambifaria].
ACCESSION   WP_176090944
VERSION     WP_176090944.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 20364106
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..739
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=78276
     Region          70..>204
                     /region_name="MoCoBD_2"
                     /note="Molybdopterin cofactor-binding domain; pfam20256"
                     /db_xref="CDD:466407"
     Region          212..732
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msrglieagr agagvsrrsf lkvgmslgaa aggglllgfs mpaagddarr sviggdaden
       61 aragvfapna fvqidrggkv tlvmpkvemg qgvytalpml iaeelevpls nvtldhappn
      121 eklfldpllg gqltggstsv ryaweplrra gatartllva aaakqwnvdp atcraengev
      181 qhppsgrras ygqladaast lpvpkdvalk qpadfkligk pvkrldspek vdgtaqfgld
      241 vrlpgmlyav ivnspvfggt vasvddtaar kipgvrqvvr vdnavavvgd htwaakrgas
      301 alvvkwnega dakvstkdiv adlaqaaang kgavarkegd vgrafanakt rvdavyeqpf
      361 lahatmepvn ctvqvradgc eiwvgtqvpt rardtvqqlt glapekivvh nhllgggfgr
      421 rletdmigqa vkvakqvnap vkvvwtreed iqhdmyrpyy ydrisaglda ngkpvawqhr
      481 ivgssiiarf appafkdgvd pdavevaael pydlpnqlvd yvrqeprhip tafwrgvgpt
      541 rgtfvvesfi delaaqtktd pvqyrralld ktprarnvld vatkaagwgt slpkgqgrgv
      601 svmhafgsff sividvavee gevqvkrvvc avdcgmavnp stieaqvqgg iifgitgaly
      661 geitiedgrv vqsnftdyrm mrinetppie vhlvksaeap ggigepgtaa taaalsnaif
      721 aatgkrlrkl pvgsqlkta
//
LOCUS       WP_176091028             292 aa            linear   BCT 11-JAN-2025
DEFINITION  class I SAM-dependent methyltransferase [Burkholderia ambifaria].
ACCESSION   WP_176091028
VERSION     WP_176091028.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10614797
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..292
                     /product="class I SAM-dependent methyltransferase"
                     /EC_number="2.1.-.-"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008757 - S-adenosylmethionine-dependent
                     methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=32112
     Region          45..225
                     /region_name="PRK11207"
                     /note="tellurite resistance methyltransferase TehB"
                     /db_xref="CDD:183040"
     Region          55..>144
                     /region_name="UbiG"
                     /note="2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,
                     4-benzoquinol methylase [Coenzyme transport and
                     metabolism]; COG2227"
                     /db_xref="CDD:441829"
ORIGIN      
        1 menigrfgsk pddtksitlq apldrivtsg iadlrishyy fdeplfdeye lttvratwdf
       61 aaaesivrdg hcvldlgcgd grlllhlagk falkesfgid ispvaidrfn asighrhiha
      121 lrgdifdlpt titqrrfdvv tfgdatvnfi ldddklegll csakaqlrns esrimvavfg
      181 dgtperlsfm dkrctvvpfr rsngeaaliw waykydsdkl imhrsvfaqs glnedgnieg
      241 vvcdlrdrmw tpsalvpiae asglkveqvi esdvqdgaav gmataivilk sa
//
LOCUS       WP_176091140             323 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_176091140
VERSION     WP_176091140.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444112
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..323
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=35662
     Region          4..62
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          92..293
                     /region_name="PBP2_CrgA_like_3"
                     /note="The C-terminal substrate binding domain of an
                     uncharacterized LysR-type transcriptional regulator
                     CrgA-like, contains the type 2 periplasmic binding fold;
                     cd08472"
                     /db_xref="CDD:176161"
     Site            order(102,106,145,159,161,225,242,269)
                     /site_type="active"
                     /note="putative effector binding pocket [active]"
                     /db_xref="CDD:176161"
     Site            order(103..104,108..109,111..112,115,119,121..127,188,
                     219..223,230..231,234)
                     /site_type="other"
                     /note="putative dimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:176161"
ORIGIN      
        1 mdriqamevf trvvdansft raadtlampr asvttiiqnl eallgvrlmh rttrrlsltp
       61 egaayyehcm kiiseiaead asfqsgnrkp sgvlrvhmps slgrrvvlpa lsifrqrypd
      121 itldlglsdr yvdpveegid cmirggpled ssmvarrigm lkrvtcaspd ylarhgepqe
      181 iadladhhav nfrashgara ipwvfmidgk plevrmngsv tvndsdayvt cglegfgmiq
      241 ptlfmvlpnl rdgslvevlp dcnpkpkpis ivyphnrhls qkvrvfadwl aelfestpal
      301 eggenwrgkv radaveergs vva
//
LOCUS       WP_176091147             350 aa            linear   BCT 11-JAN-2025
DEFINITION  AraC family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_176091147
VERSION     WP_176091147.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Cortes-Avalos,D., Martinez-Perez,N., Ortiz-Moncada,M.A.,
            Juarez-Gonzalez,A., Banos-Vargas,A.A., Estrada-de Los Santos,P.,
            Perez-Rueda,E. and Ibarra,J.A.
  TITLE     An update of the unceasingly growing and diverse AraC/XylS family
            of transcriptional activators
  JOURNAL   FEMS Microbiol Rev 45 (5) (2021)
   PUBMED   33837749
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Agarwal,G., Rajavel,M., Gopal,B. and Srinivasan,N.
  TITLE     Structure-based phylogeny as a diagnostic for functional
            characterization of proteins with a cupin fold
  JOURNAL   PLoS One 4 (5), e5736 (2009)
   PUBMED   19478949
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Dunwell,J.M., Purvis,A. and Khuri,S.
  TITLE     Cupins: the most functionally diverse protein superfamily?
  JOURNAL   Phytochemistry 65 (1), 7-17 (2004)
   PUBMED   14697267
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Egan,S.M.
  TITLE     Growing repertoire of AraC/XylS activators
  JOURNAL   J Bacteriol 184 (20), 5529-5532 (2002)
   PUBMED   12270809
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Martin,R.G. and Rosner,J.L.
  TITLE     The AraC transcriptional activators
  JOURNAL   Curr Opin Microbiol 4 (2), 132-137 (2001)
   PUBMED   11282467
REFERENCE   6  (residues 1 to 350)
  AUTHORS   Dunwell,J.M.
  TITLE     Cupins: a new superfamily of functionally diverse proteins that
            include germins and plant storage proteins
  JOURNAL   Biotechnol Genet Eng Rev 15, 1-32 (1998)
   PUBMED   9573603
REFERENCE   7  (residues 1 to 350)
  AUTHORS   Gallegos,M.T., Schleif,R., Bairoch,A., Hofmann,K. and Ramos,J.L.
  TITLE     Arac/XylS family of transcriptional regulators
  JOURNAL   Microbiol Mol Biol Rev 61 (4), 393-410 (1997)
   PUBMED   9409145
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15746491
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..350
                     /product="AraC family transcriptional regulator"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0043565 - sequence-specific DNA binding
                     [Evidence IEA]"
                     /GO_process="GO:0006355 - regulation of DNA-templated
                     transcription [Evidence IEA]"
                     /calculated_mol_wt=38973
     Region          23..179
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          <130..312
                     /region_name="AraC"
                     /note="AraC-type DNA-binding domain and AraC-containing
                     proteins [Transcription]; COG2207"
                     /db_xref="CDD:441809"
     Region          230..314
                     /region_name="HTH_ARAC"
                     /note="helix_turn_helix, arabinose operon control protein;
                     smart00342"
                     /db_xref="CDD:197666"
ORIGIN      
        1 mdqaafvpvf kfrttdypep drfhvwvkdm lcdyrlddpg ghgpfdaqas gaalgplils
       61 grqwrsrapt ytvhrttrri rldgqdsirf tlllggrlas htggpelikr agdvfvydva
      121 qindcrvdag dvislvvprh llpshaaqah gqtltsgvgr lvgdqmlslf rnlpdlrmhd
      181 vpsvvqslll llaaavapsa qalddargpi dnalvervrr yidvhllepd ltpdricrdi
      241 gvsrarlyql fkeaggvmrq itrrrlrhay hvlgdpqrrh rriaeiawah gfpdekyfhr
      301 lfkaefghtp ketlecaaap vllpcdaadd rwgdggrltg wtlpfgvltn
//
LOCUS       WP_176091152             306 aa            linear   BCT 11-JAN-2025
DEFINITION  LysR family transcriptional regulator [Burkholderia ambifaria].
ACCESSION   WP_176091152
VERSION     WP_176091152.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Maddocks,S.E. and Oyston,P.C.F.
  TITLE     Structure and function of the LysR-type transcriptional regulator
            (LTTR) family proteins
  JOURNAL   Microbiology (Reading) 154 (Pt 12), 3609-3623 (2008)
   PUBMED   19047729
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Schell,M.A.
  TITLE     Molecular biology of the LysR family of transcriptional regulators
  JOURNAL   Annu Rev Microbiol 47, 597-626 (1993)
   PUBMED   8257110
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10444297
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..306
                     /product="LysR family transcriptional regulator"
                     /GO_function="GO:0001216 - DNA-binding transcription
                     activator activity [Evidence IEA]"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /calculated_mol_wt=33311
     Region          5..64
                     /region_name="HTH_1"
                     /note="Bacterial regulatory helix-turn-helix protein, lysR
                     family; pfam00126"
                     /db_xref="CDD:459683"
     Region          94..295
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            order(109..110,112..113,116,120,122..128,224..229,
                     235..236,238..239)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:176102"
ORIGIN      
        1 mtfdlrqlra fttivtcgsl graadalhvt qpalsrilkr ledqvgaplf erhskgvqlt
       61 afgeallpha tllqheaeha reeldamrgf akgtikvgtv gsiaslvlpv avgrvldrwp
      121 nlrveilegv wdrladglhk heidlalsah gpdtdeivai pecrwqdrsh ivaaphhplr
      181 algraptlad tlharwaipp rgtapfdhmr atfdahglal pdiavetrsv ttlkslvaha
      241 gflswmaepm ygaeqragti dtlpvrevva vrtltafrrr hgilpgpagk lldelvaltr
      301 dardah
//
LOCUS       WP_176091191             920 aa            linear   BCT 11-JAN-2025
DEFINITION  type VI secretion system Vgr family protein [Burkholderia
            ambifaria].
ACCESSION   WP_176091191
VERSION     WP_176091191.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Coulthurst,S.
  TITLE     The Type VI secretion system: a versatile bacterial weapon
  JOURNAL   Microbiology (Reading) 165 (5), 503-515 (2019)
   PUBMED   30893029
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Pukatzki,S., Ma,A.T., Revel,A.T., Sturtevant,D. and Mekalanos,J.J.
  TITLE     Type VI secretion system translocates a phage tail spike-like
            protein into target cells where it cross-links actin
  JOURNAL   Proc Natl Acad Sci U S A 104 (39), 15508-15513 (2007)
   PUBMED   17873062
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11466136
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..920
                     /product="type VI secretion system Vgr family protein"
                     /GO_component="GO:0033104 - type VI protein secretion
                     system complex [Evidence IEA]"
                     /GO_process="GO:0033103 - protein secretion by the type VI
                     secretion system [Evidence IEA]"
                     /calculated_mol_wt=100484
     Region          17..825
                     /region_name="VgrG"
                     /note="Uncharacterized conserved protein VgrG, implicated
                     in type VI secretion and phage assembly [Intracellular
                     trafficking, secretion, and vesicular transport, Mobilome:
                     prophages, transposons, General function prediction only];
                     COG3501"
                     /db_xref="CDD:442724"
ORIGIN      
        1 mnvqdlaaal rgglseqdrl lkldtplrpn tlvvqravgr atigrdyift ldvvssdsti
       61 elkkliaqpv tlwiqqasgg yrpihgyvyt arrlgadggl ttyqitlhaw mhvlkfrrdq
      121 riwidrsved ivsdvlnqhp eargrfrftl sqplanrsyt rqsetdwnfv hrllenegly
      181 sywdqaddgk shtlvitdkl dalpalspkt vlfyrsctqs evdaltqwsg trslqsvalt
      241 trtfdyknpa arsnpkgtsv paagnqgalp sqlevyeytg aytyleqqrg drlsrirmee
      301 wesrakrfhg vggvrgldag rrfelgdhpa hdgdsveqre fatiavswwi ennlpvtpas
      361 nfphslhrdl aearasrsds asfevphadg cvgyflveve aqrvtvpyrs pfehekpkmh
      421 letalvvgps geevhtdeln ririqfvwdr vnpgdqgasc wvrvvqadtg ggygsvhipr
      481 igeevlvdhv ggdcdrplvm grvyngaakp qwhsdgilsg yrskeysgag fnqlvmddat
      541 gqsraqlmss agnsilhlgy linqqgntrg aylgtgfdlr tdaygavrat sglyvtthpk
      601 satsqpldvr etqqqlvnae gllesmseva eqhqadslkp ghdamraftd atrssvsgea
      661 sggrtagggt gsanafkepv mlfgspagig lstqqsahli adihvnlvsg qsthiaagks
      721 liasiadkis lfvqnagmkl faakgkveiq ahkddieiva qksvkvlsat dkievaaeke
      781 vlltsggayi rlkggdieih apgkidvkga qhsfsgptsq ayampqfkps yqaqyilksq
      841 vdgspmmqha yelklpsgrt vlghtndmge tipvftpsaq tvnlraleqe kvetepwkfa
      901 gggqpdiysd yvkegdasra
//
LOCUS       WP_176091355             343 aa            linear   BCT 11-JAN-2025
DEFINITION  MULTISPECIES: ParB/RepB/Spo0J family partition protein
            [Burkholderia cepacia complex].
ACCESSION   WP_176091355
VERSION     WP_176091355.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia complex
  ORGANISM  Burkholderia cepacia complex
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Schumacher,M.A.
  TITLE     Structural biology of plasmid segregation proteins
  JOURNAL   Curr Opin Struct Biol 17 (1), 103-109 (2007)
   PUBMED   17161598
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Lee,P.S. and Grossman,A.D.
  TITLE     The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB)
            contribute to accurate chromosome partitioning, separation of
            replicated sister origins, and regulation of replication initiation
            in Bacillus subtilis
  JOURNAL   Mol Microbiol 60 (4), 853-869 (2006)
   PUBMED   16677298
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Bignell,C. and Thomas,C.M.
  TITLE     The bacterial ParA-ParB partitioning proteins
  JOURNAL   J Biotechnol 91 (1), 1-34 (2001)
   PUBMED   11522360
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445026
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Burkholderia cepacia complex"
                     /db_xref="taxon:87882"
     Protein         1..343
                     /product="ParB/RepB/Spo0J family partition protein"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /calculated_mol_wt=37811
     Region          70..301
                     /region_name="Spo0J"
                     /note="Chromosome segregation protein Spo0J, contains
                     ParB-like nuclease domain [Cell cycle control, cell
                     division, chromosome partitioning]; COG1475"
                     /db_xref="CDD:441084"
ORIGIN      
        1 mskkdfsaal nagvkrdqtm retatpsrfd rvdealsgrs slldqpnenv aaptrsaaea
       61 ylasleqagr vqaryitmpi shiddnplns rtiykeelia araasmardg qlvpvlagrh
      121 pdfpdraili dgqfrklgal rnrsetldvk llegldpidf yrlaraanne reqetildva
      181 lgykklldqg haksndelav lveegkskvs kilalldlpq avldvigshp kqfglstsye
      241 ltlffkasde krtlafaeri rdeelpfqkv kairesleng raprkslsrq ykvstldgae
      301 igaikewgdg kvrldlalgs aekaeayvaa fkkllaedgh qlk
//
LOCUS       WP_176091427             765 aa            linear   BCT 11-JAN-2025
DEFINITION  xanthine dehydrogenase family protein molybdopterin-binding subunit
            [Burkholderia ambifaria].
ACCESSION   WP_176091427
VERSION     WP_176091427.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 765)
  AUTHORS   Wang,C.H., Zhang,C. and Xing,X.H.
  TITLE     Xanthine dehydrogenase: An old enzyme with new knowledge and
            prospects
  JOURNAL   Bioengineered 7 (6), 395-405 (2016)
   PUBMED   27537049
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11445946
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..765
                     /product="xanthine dehydrogenase family protein
                     molybdopterin-binding subunit"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /calculated_mol_wt=81166
     Region          <27..>217
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
     Region          226..764
                     /region_name="CoxL"
                     /note="Aldehyde, CO or xanthine dehydrogenase, Mo-binding
                     subunit [Energy production and conversion]; COG1529"
                     /db_xref="CDD:441138"
ORIGIN      
        1 msadtkitrp grrrfllgav glggalvvgw gvmpprsrlg dpavfpetsg qialngwiki
       61 tsegdvilam prvemgqgih tglsmlaaee ldipltrvsi esspieriyg nvvamgdssl
      121 plhpddadki waralhwima ksareiglii tggsssmadg wqpvreaaat aratlveaaa
      181 rewgvrstlv tvregqligp ggkqmpfsav aqkareiapp snvtlkpasq fqlvgkpapr
      241 ndiaaktdgs arfaidvrpp gmlyaavvmc pvfggklktf nskaalvmpg vryvvpfegs
      301 tggapgvavv adhywqarea lgalepewdn gphatldsag irqqlvgald sdnggftyrs
      361 mgeglkafen apgativeae ysapylahat mepinctaqv tkdrvqlwap tqvatlaqlv
      421 aaraagvsrd qvhidiplig ggfgrrlesd fvgqavtiaa rteghpvqvi wsreddikhd
      481 fyrpqaiarl karvengklt aiasrsagqs ilagelerlf gapsldidry taeglfdqpy
      541 eiehehiahl vvdlpvpigf wrsvghsytg fflesflndv aaaakldpla mrrdllkahp
      601 relkvldiaa qaagwdqpla paadgaarar glalhsafgs vvaqvvevsl kdgkprvhrv
      661 vcvadcgtvv npgivaqqme sgiifglsaa lysqiqikdg rviqsnfpdy pvlkmaeapa
      721 ieihvvpita eptgvgeiav ppiapavaha vaqltgksvr qlpmv
//
LOCUS       WP_176091449             353 aa            linear   BCT 11-JAN-2025
DEFINITION  acetyl-CoA C-acetyltransferase, partial [Burkholderia ambifaria].
ACCESSION   WP_176091449
VERSION     WP_176091449.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Merilainen,G., Poikela,V., Kursula,P. and Wierenga,R.K.
  TITLE     The thiolase reaction mechanism: the importance of Asn316 and
            His348 for stabilizing the enolate intermediate of the Claisen
            condensation
  JOURNAL   Biochemistry 48 (46), 11011-11025 (2009)
   PUBMED   19842716
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Igual,J.C., Gonzalez-Bosch,C., Dopazo,J. and Perez-Ortin,J.E.
  TITLE     Phylogenetic analysis of the thiolase family. Implications for the
            evolutionary origin of peroxisomes
  JOURNAL   J Mol Evol 35 (2), 147-155 (1992)
   PUBMED   1354266
REFERENCE   3  (residues 1 to 353)
  AUTHORS   LYNEN,F. and OCHOA,S.
  TITLE     Enzymes of fatty acid metabolism
  JOURNAL   Biochim Biophys Acta 12 (1-2), 299-314 (1953)
   PUBMED   13115439
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11481662
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the carboxy end.
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         1..>353
                     /product="acetyl-CoA C-acetyltransferase"
                     /EC_number="2.3.1.9"
                     /GO_function="GO:0003985 - acetyl-CoA C-acetyltransferase
                     activity [Evidence IEA]"
     Region          1..353
                     /region_name="PRK05790"
                     /note="putative acyltransferase; Provisional"
                     /db_xref="CDD:180261"
ORIGIN      
        1 mtdvvivsaa rtavgkfggs lakiaapelg atviravler sgvkpeqvse vimgqvlaag
       61 sgqnparqsl ikaglpsavp gmtinkvcgs glkavmlaan aiaagdaeiv iaggqenmsa
      121 aphvlpgsrd gfrmgdaklv dtmivdglwd vynqyhmgit aenvakeygi trdeqdafaa
      181 lsqnkaeaaq kagrfddeiv pvsipqrkge plqfatdefv rhgvtaesla glkpafakeg
      241 tvtaanasgl ndgaaavlvm saqkaaalgl tplarikaya nagvdpsvmg mgpvpasrrc
      301 leragwtpgd ldlmeineaf aaqalavhkq mgwdtskvnv nggaiaighp iga
//
LOCUS       WP_176091452             245 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein-ubiquinone oxidoreductase, partial
            [Burkholderia ambifaria].
ACCESSION   WP_176091452
VERSION     WP_176091452.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia ambifaria
  ORGANISM  Burkholderia ambifaria
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11428947
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on the amino end.
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Burkholderia ambifaria"
                     /db_xref="taxon:152480"
     Protein         <1..245
                     /product="electron transfer flavoprotein-ubiquinone
                     oxidoreductase"
                     /EC_number="1.5.5.1"
                     /GO_function="GO:0004174 -
                     electron-transferring-flavoprotein dehydrogenase activity
                     [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0022900 - electron transport chain
                     [Evidence IEA]"
     Region          <2..72
                     /region_name="FixC"
                     /note="Dehydrogenase (flavoprotein) [Energy production and
                     conversion]; COG0644"
                     /db_xref="CDD:440409"
     Region          141..243
                     /region_name="ETF_QO"
                     /note="Electron transfer flavoprotein-ubiquinone
                     oxidoreductase, 4Fe-4S; pfam05187"
                     /db_xref="CDD:461576"
ORIGIN      
        1 aitaggllsl pktvfpggal igddagflna srikgshaai ktgmlaadaa fdavqagrqs
       61 delnaypdaf kqswlytely rarnfkqwma kglylgtlmv gleqkvmggn vpwtlhhkha
      121 dhemlkpasq ctpieypkpd gkltfdrlss vfisntnhee nqpahltlkd anvpvnvnlr
      181 tyagpearfc paavyefvkn ddggdrlvin aqncvhcktc dikdptqniv wvtpeggggp
      241 nypnm
//
LOCUS       WP_176091552             375 aa            linear   BCT 11-JAN-2025
DEFINITION  cation diffusion facilitator family transporter [Clostridium
            felsineum].
ACCESSION   WP_176091552
VERSION     WP_176091552.1
KEYWORDS    RefSeq.
SOURCE      Clostridium felsineum
  ORGANISM  Clostridium felsineum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Kolaj-Robin,O., Russell,D., Hayes,K.A., Pembroke,J.T. and
            Soulimane,T.
  TITLE     Cation Diffusion Facilitator family: Structure and function
  JOURNAL   FEBS Lett 589 (12), 1283-1295 (2015)
   PUBMED   25896018
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Montanini,B., Blaudez,D., Jeandroz,S., Sanders,D. and Chalot,M.
  TITLE     Phylogenetic and functional analysis of the Cation Diffusion
            Facilitator (CDF) family: improved signature and prediction of
            substrate specificity
  JOURNAL   BMC Genomics 8, 107 (2007)
   PUBMED   17448255
  REMARK    Publication Status: Online-Only
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11414568
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Clostridium felsineum"
                     /db_xref="taxon:36839"
     Protein         1..375
                     /product="cation diffusion facilitator family transporter"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0008324 - monoatomic cation transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_process="GO:0006812 - monoatomic cation transport
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=42296
     Region          3..238
                     /region_name="FieF"
                     /note="Divalent metal cation (Fe/Co/Zn/Cd) efflux pump
                     [Inorganic ion transport and metabolism]; COG0053"
                     /db_xref="CDD:439823"
ORIGIN      
        1 mpillniilf lckfiigtis gsmaitadaw nnildagnst iallgikiar ygkgekhpfg
       61 hgrmewmvsl fssmvvmlag yellktswks vrnpknitvs lvvfliliis iviklymyay
      121 yrkvakssds esmkamsvds lcdslatgav lvstianaaf gwkidgwcgm vvsvfiiytg
      181 yssisetgkr ivgktpdkel idkiemlvkq ygvieniqem tihdygvgkf mvameigvye
      241 qedselikgi pedisyalye klgcdsviqi sylledener qiyfgsveei kkideaiqve
      301 nfrivqaqkh kvihvdislp mrlekrenei rkiienkick vgkeykamik fkimpnyqgt
      361 rkininrkmk vssqk
//
LOCUS       WP_176091544             141 aa            linear   BCT 11-JAN-2025
DEFINITION  FHA domain-containing protein [Clostridium felsineum].
ACCESSION   WP_176091544
VERSION     WP_176091544.1
KEYWORDS    RefSeq.
SOURCE      Clostridium felsineum
  ORGANISM  Clostridium felsineum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Li,J., Lee,G.I., Van Doren,S.R. and Walker,J.C.
  TITLE     The FHA domain mediates phosphoprotein interactions
  JOURNAL   J Cell Sci 113 Pt 23, 4143-4149 (2000)
   PUBMED   11069759
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Durocher,D., Henckel,J., Fersht,A.R. and Jackson,S.P.
  TITLE     The FHA domain is a modular phosphopeptide recognition motif
  JOURNAL   Mol Cell 4 (3), 387-394 (1999)
   PUBMED   10518219
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Hofmann,K. and Bucher,P.
  TITLE     The FHA domain: a putative nuclear signalling domain found in
            protein kinases and transcription factors
  JOURNAL   Trends Biochem Sci 20 (9), 347-349 (1995)
   PUBMED   7482699
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11447961
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Clostridium felsineum"
                     /db_xref="taxon:36839"
     Protein         1..141
                     /product="FHA domain-containing protein"
                     /GO_function="GO:0005515 - protein binding [Evidence IEA]"
                     /calculated_mol_wt=15618
     Region          48..139
                     /region_name="FHA"
                     /note="Forkhead associated (FHA) domain, binds pSer, pThr,
                     pTyr [Signal transduction mechanisms]; COG1716"
                     /db_xref="CDD:441322"
ORIGIN      
        1 mstilkfvii aivyliifta fkimykdmkn gdkrptsskk rktfglevvd sgmnesirng
       61 svvpvsreit igrkddnsim lnegyvsghh arvylrnnqy iledlnstng tvlngqkiks
      121 kayikagdei kigssvfkvi g
//
LOCUS       WP_176091585             258 aa            linear   BCT 11-JAN-2025
DEFINITION  GNAT family N-acetyltransferase [Clostridium felsineum].
ACCESSION   WP_176091585
VERSION     WP_176091585.1
KEYWORDS    RefSeq.
SOURCE      Clostridium felsineum
  ORGANISM  Clostridium felsineum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Salah Ud-Din,A.I., Tikhomirova,A. and Roujeinikova,A.
  TITLE     Structure and Functional Diversity of GCN5-Related
            N-Acetyltransferases (GNAT)
  JOURNAL   Int J Mol Sci 17 (7), 1018 (2016)
   PUBMED   27367672
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Favrot,L., Blanchard,J.S. and Vergnolle,O.
  TITLE     Bacterial GCN5-Related N-Acetyltransferases: From Resistance to
            Regulation
  JOURNAL   Biochemistry 55 (7), 989-1002 (2016)
   PUBMED   26818562
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Vetting,M.W., S de Carvalho,L.P., Yu,M., Hegde,S.S., Magnet,S.,
            Roderick,S.L. and Blanchard,J.S.
  TITLE     Structure and functions of the GNAT superfamily of
            acetyltransferases
  JOURNAL   Arch Biochem Biophys 433 (1), 212-226 (2005)
   PUBMED   15581578
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Dyda,F., Klein,D.C. and Hickman,A.B.
  TITLE     GCN5-related N-acetyltransferases: a structural overview
  JOURNAL   Annu Rev Biophys Biomol Struct 29, 81-103 (2000)
   PUBMED   10940244
  REMARK    Erratum:[Annu Rev Biophys Biomol Struct. 2005;34:vi]
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Neuwald,A.F. and Landsman,D.
  TITLE     GCN5-related histone N-acetyltransferases belong to a diverse
            superfamily that includes the yeast SPT10 protein
  JOURNAL   Trends Biochem Sci 22 (5), 154-155 (1997)
   PUBMED   9175471
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 15732852
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Clostridium felsineum"
                     /db_xref="taxon:36839"
     Protein         1..258
                     /product="GNAT family N-acetyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0008080 - N-acetyltransferase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=30361
     Region          10..122
                     /region_name="Acetyltransf_19"
                     /note="Acetyltransferase (GNAT) domain; pfam18015"
                     /db_xref="CDD:465618"
     Region          137..247
                     /region_name="Acetyltransf_1"
                     /note="Acetyltransferase (GNAT) family; pfam00583"
                     /db_xref="CDD:395465"
     Site            order(198,199,209..210)
                     /site_type="other"
                     /note="Coenzyme A binding pocket [chemical binding]"
                     /db_xref="CDD:173926"
ORIGIN      
        1 mtldikkans ieeiynerel yikslhfaqe qyleqivkkc dvyiieiesk ikgyfcvnnd
       61 kviyefyldv ealkfsqyif ktiiengyft saecksydsl fmslcldfhk kascsgylfr
      121 dfydteisls gfeklkfrqa elrdvskidd inydffqrle eqivkgeifv lysnevllga
      181 gviqkvfhst nyydigmivn knyrnrgigt yiitklrqia cnkklepicg cwyynyaskk
      241 alekagfisk hrilnfdf
//
LOCUS       WP_176091594             333 aa            linear   BCT 11-JAN-2025
DEFINITION  electron transfer flavoprotein subunit alpha/FixB family protein
            [Clostridium felsineum].
ACCESSION   WP_176091594
VERSION     WP_176091594.1
KEYWORDS    RefSeq.
SOURCE      Clostridium felsineum
  ORGANISM  Clostridium felsineum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Aravind,L., Anantharaman,V. and Koonin,E.V.
  TITLE     Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP,
            photolyase, and PP-ATPase nucleotide-binding domains: implications
            for protein evolution in the RNA
  JOURNAL   Proteins 48 (1), 1-14 (2002)
   PUBMED   12012333
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Tsai,M.H. and Saier,M.H. Jr.
  TITLE     Phylogenetic characterization of the ubiquitous electron transfer
            flavoprotein families ETF-alpha and ETF-beta
  JOURNAL   Res Microbiol 146 (5), 397-404 (1995)
   PUBMED   8525056
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449614
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Clostridium felsineum"
                     /db_xref="taxon:36839"
     Protein         1..333
                     /product="electron transfer flavoprotein subunit
                     alpha/FixB family protein"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /calculated_mol_wt=37139
     Region          9..314
                     /region_name="FixB"
                     /note="Electron transfer flavoprotein, alpha subunit FixB
                     [Energy production and conversion]; COG2025"
                     /db_xref="CDD:441628"
ORIGIN      
        1 mdksfcsksv lviadiwskq sensvarlvs kanqlsekln tvvnvcmfgv eiddsiqmik
       61 aygvknifyk kfedisqitd ekltnlsyel ikkiepqivl ypitvrmksi sarlaarlet
      121 gltadcidfs idsetnlllq krpafedsvi atitcpdklp qmatanplsf elkektidei
      181 evvniddfsf ktkdkvsvle ikkigeetid eegkskivvg igrgvnkdnl qqikllvkkl
      241 narlvasrav vdsglldyky qiglsgkeit cetyiafgis gmmqhmsglk syknliavnt
      301 dksarimsfa nygicdtten vvkhmlsyle nrn
//
LOCUS       WP_176091599             166 aa            linear   BCT 11-JAN-2025
DEFINITION  DedA family protein [Clostridium felsineum].
ACCESSION   WP_176091599
VERSION     WP_176091599.1
KEYWORDS    RefSeq.
SOURCE      Clostridium felsineum
  ORGANISM  Clostridium felsineum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Okawa,F., Hama,Y., Zhang,S., Morishita,H., Yamamoto,H., Levine,T.P.
            and Mizushima,N.
  TITLE     Evolution and insights into the structure and function of the DedA
            superfamily containing TMEM41B and VMP1
  JOURNAL   J Cell Sci 134 (8) (2021)
   PUBMED   33771928
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Doerrler,W.T., Sikdar,R., Kumar,S. and Boughner,L.A.
  TITLE     New functions for the ancient DedA membrane protein family
  JOURNAL   J Bacteriol 195 (1), 3-11 (2013)
   PUBMED   23086209
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11426582
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Clostridium felsineum"
                     /db_xref="taxon:36839"
     Protein         1..166
                     /product="DedA family protein"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /calculated_mol_wt=18564
     Region          1..162
                     /region_name="DedA"
                     /note="Membrane integrity protein DedA, putative
                     transporter, DedA/Tvp38 family [Cell
                     wall/membrane/envelope biogenesis]; COG0586"
                     /db_xref="CDD:440351"
ORIGIN      
        1 maivlpeesl lfvigslssl gkiniwlviv vviiatfigd sinyligrkl gsnilnkdks
       61 iiikkehiyk tqnyynkrgs vtviigrtlp iirtfipfva gmagmnykkf iifnmigaip
      121 wlmiyivggf flgnhpfvek nftivliiia ifplipsivk yyikia
//
LOCUS       WP_176091603             438 aa            linear   BCT 11-JAN-2025
DEFINITION  nucleotide sugar dehydrogenase [Clostridium felsineum].
ACCESSION   WP_176091603
VERSION     WP_176091603.1
KEYWORDS    RefSeq.
SOURCE      Clostridium felsineum
  ORGANISM  Clostridium felsineum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11430796
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Clostridium felsineum"
                     /db_xref="taxon:36839"
     Protein         1..438
                     /product="nucleotide sugar dehydrogenase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016628 - oxidoreductase activity, acting
                     on the CH-CH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /calculated_mol_wt=49994
     Region          26..427
                     /region_name="WecC"
                     /note="UDP-N-acetyl-D-mannosaminuronate dehydrogenase
                     [Cell wall/membrane/envelope biogenesis]; COG0677"
                     /db_xref="CDD:440441"
ORIGIN      
        1 mlkqeslikk ienktavvgv vglgyvglpl avqsavkgyk vigfevnnkk vnkinngeny
       61 ikdilndvlk dmvlsgrlka tsnfqfiknv divlicvptp ldkyqqpdis yvknsvevig
      121 kylhknmmvi lesttypgtt eelilpilek easlkceedf ylafspervd pgnikykten
      181 vpkvvggiqk kstklaaefy knilevnvhe vsspkvaeme kilentyrni niglinemai
      241 icnkmninvw evieaaktkp ygfqafypgp glgghcipld pyyltwkare ynyhtrfiei
      301 sgeinnymsk yiverigail nrfnkplrds kilvlgiayk kdiddyresp airiienlkl
      361 qgaevsfydp yisvykykgk eyyglditke klgdydlvvi ttehskydyd fiqknsnfif
      421 dvrnatkdlk drdniell
//
LOCUS       WP_176091604             432 aa            linear   BCT 11-JAN-2025
DEFINITION  right-handed parallel beta-helix repeat-containing protein
            [Clostridium felsineum].
ACCESSION   WP_176091604
VERSION     WP_176091604.1
KEYWORDS    RefSeq.
SOURCE      Clostridium felsineum
  ORGANISM  Clostridium felsineum
            Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
            Clostridiaceae; Clostridium.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Burnim,A.A., Dufault-Thompson,K. and Jiang,X.
  TITLE     The three-sided right-handed beta-helix is a versatile fold for
            glycan interactions
  JOURNAL   Glycobiology 34 (7) (2024)
   PUBMED   38767844
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12131601
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Clostridium felsineum"
                     /db_xref="taxon:36839"
     Protein         1..432
                     /product="right-handed parallel beta-helix
                     repeat-containing protein"
                     /calculated_mol_wt=45269
     Region          128..320
                     /regio